LOCUS       WP_090498201            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090498201
VERSION     WP_090498201.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116857
     Region          31..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mektstkhcy vkfltatlfy llipwlafaq ktikgtvvdq tnkplpgvsi iekgtkngta
       61 tnadgkftlt vqkegaiita rivgyrsvek tvsasstvsf sleednntln evvtigyqki
      121 trkkttaais sisgkelanl paasfdqllq grlsgvnvqn ftgqpgvapt vsvrgnstgs
      181 tgydqfnvir splyvvdgvp qssddlvppg tgtgtnymag lnpndiesid vlkdasaaai
      241 ygsraangvi littkkgvgg dtrvsfnsyy gmvqrpnlrq atmgtterrq kmevlqrqls
      301 ydqrvqlpyi ltdslnpafn ghtdwqdlfy qtgkindnnl sisggtdngt tyrfsggyyd
      361 edgivkgtgf kryttrlnlt sramnkklmi npifyyssas rgrgnedpnd pskptkvgsg
      421 nlpsslfnis pekldyfvsk dgenlnrnvs nqfganlnla yefnkhftln sqssytndnt
      481 rrdvsmsnll nngfgnssss fsssaiglrt snylayngai kkhsfsavag qdieyslfqs
      541 tqasgyggas dniqtvtgfk qqniyaysny iahglvayyg rfnydydgky llsgtirtdg
      601 ssgfgennky gvfpsisagw llseenfmkn ltnnpftlik irgsygvtgn edkrnayvqy
      661 ntyqvnngyf sgnsgatsyn gvtaitpnfr ngvaqkdlsw ekstqwnigt dmeidngrya
      721 isfdvynkev kqklfnidlp vtsgydnaft nafavrnsgl eltltanpir kefkwnssfn
      781 isynknqims lpnggrdiil sgdrfdknhv lsvgsplnaf ylyrtkgvfs tsadipqnpy
      841 tgeryrnsng pynagdfyla dldgdyfidv fndginpdka pigdpnprft ggwtnsfsyk
      901 nfslsifvnf tlkrdvlnlf dsdrftnatd anavynfasv sapdlsrlni wrnpgdqaey
      961 akldlgsyry yytaaqsffl ekggyarirs inlgydfspk ivrklgltql klyaiadnvy
     1021 mfqqskklpd aeavsgygey ngtgypiprk ytlgvqvqf
//
LOCUS       WP_090498614            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090498614
VERSION     WP_090498614.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119472
     Region          26..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkmylkcls illlcfitis afaqttitgt vkdssgplpg vsvsvkgtsk vtqtdgngkf
       61 sltvnpgevl vftaigfakq evsinnqtsl nvilkessnq ldevnvvtta lgikrqeksl
      121 gyavstvtak qlteagntnf asalygkaag vkittapgga ssavnvqirg insinynqqp
      181 lyvvdgvmir ndgqngaaga nnnnywddqr vrgngildin padiesltvl kgasasalyg
      241 sdaasgvvvi ttkkgsknrg lgvdfnyqgs idqvaflpnf qntygpgydr etniangate
      301 egwiadaisp sgfrpyfray anfgpkmegq qvrwwdgsir syspqpnnyr dvyqngytsn
      361 anvaisnqte gvnyrfsasr ldykgtqpgn tgakntfnln stiklapkls advivsyvnt
      421 itknrpyqlg qvlgsfagff sraedmglmk erfqtsngyk yatfdqtarp epflfnirat
      481 nlldfywqql knqydenenr llssftlnyd vaknlklrgr vgndytsvkt enhqfteips
      541 alntntstga ytttqgqysv lygdalltys nkigedfgls isggyqgrke tykdlksntr
      601 dglvtenffa lsnsfnvaet tearkeqlky aylglvnlsy kdflfaegta rqeyvstlpp
      661 gnnqysyysv nsgfvfsdlw klpkfwsygk lrasygvvgn appiyeanis ykqtslqsin
      721 gpvpsivsln sygnlglmpe kkheaefgle trflngrlgl dvsyynnkik nqilpldvta
      781 tngaqkqivn vgevgnkgwe ialnatpvsg kfrwdtrlnf stnkskvnsl ydanseinfy
      841 ssdqatakiv aragedlgni yirprktdan gnylinddgy yvmdnsvyvk agnimpkavg
      901 gfsntfsygn faldvtidyr fggkmiapnl kymrgagmle nsmefrdaas gglsytsngk
      961 tyndgvvlqg vnqttglpnt kvlsaadyyi ttynwgegsl teaeifdndy ikmreivlsy
     1021 kipasftkkl kisnlrfsli grnlfyihrt lkdldpeapl gnkwwsqgvd vgstaasrnf
     1081 gfslnanf
//
LOCUS       WP_090500661            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090500661
VERSION     WP_090500661.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114525
     Region          23..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkllillg iltcyvvsya qttvkgkvtd gsnvgipgvs vlvkgsttgs stagdgtysi
       61 tvpsnnatli fksigfvtre vvvgertqvd iqllgdakel sdvvvtalgi krseksigya
      121 aqkidgdalt mtketnvigs lagkvagvqv tgssganlgg tqkikirsvn sltgggspli
      181 vvdgtpitqn nfgggengvd ygntsqdvnp ddiesinvlk gpaasalygi rgqygvllit
      241 tkkggkgakm qidissayti dkignflplq niygvgnsqv fsklangqny vngndeswgp
      301 kmdgtpirki nsfypqdpty gqlspfepqp nnikdffetg qninngiflt ggsdnstfki
      361 gytnaytkgt ipntwlkrnn lslsttfdln kkltvganvn yannsgqrpt qgyqgsftga
      421 vqwfqrnldi ntlrnyryad gtilnwnvnp ntagvitnnk psdwnnpffd ayevlnnddr
      481 nrlfgdvnls yqvlpelkis gfvrsdmfsq hithkeplgg rnldnyaitk adgidnnyef
      541 laqfnknind fsinvnagan lyttkftqts qstvgglssp ntytiaasvd rpnsssylrq
      601 kqvrsmyamg sfgykdtyfl dasirndiss alpsannsyw ypsfsgsflf snliqskvlt
      661 ygklrasyai agsdfdpfqt aityafgspy patsgtissl tvpdilknpd lkpsfansye
      721 agvdlrflnn rlgidftlyq qrnknqvinl svsgasgyet yvvnaglien kgleltltgq
      781 pvksklftwd islnyaknkn tikelypgin vyqldqnvys sqtiflnssl nqsfgnlvgp
      841 gykrdpatge illgadnmpi svngvnfgsv vpnytggitn nfkiwkfdlg aalsfqsggk
      901 ffswsqmlaa ksgqseitaa lndkgvnvre pvangggvkv sgissvtgqp vtayvdarty
      961 yrtnlgtkfy dewiydasyi kirelslgyn fdskilsktp fkaiklsava rnpvmiwqka
     1021 pkgvdpsels sgssaiswie kgelqtvrsf gltlnvkf
//
LOCUS       WP_090500011            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090500011
VERSION     WP_090500011.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118267
     Region          55..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrftyasl vclkkslwvt clfivifnsa fsipktneki vlkpseqkri penariikgh
       61 vtdekklgip gvsvlikgtn tgtvtnqegd fsikandgdv lvfssigyvn keitvdhsdm
      121 yqimitedak alsevvvtal gvkkersklg yvaqtvqgen lvkarepnii ssltgrvagl
      181 nisnstdlfq dpgislrgrk plividgipd qsadlfrvna ddvesvtvlk ganasalygs
      241 igqngaimit tkrgkgnnls idvnsstqiq pgfiripkvq teygagykgk ytyvdgsggg
      301 qegsgwiwgp kldqpdpttp sgffetpqfn sprdpitgkl vplpflsrgk nnvedffqtg
      361 vissnnisit qssekgsfra sashiyqkgi vpntdlnnss fnvsgnykls daftidarln
      421 ynrqftknfp etgygptnyl ynlvlwtgtd vsvqdlkdyw vpgkegiqqr nynisyynnp
      481 yfqayeylrg ydkdntygsl nlnykispaf svqfrngint yglnrtykep msyigygnks
      541 rgqftvatqn yidlvtdlig dynhtfsdkf klhaqiggsn yyrnhkygst ntdgltipgf
      601 ynlsnsanpl qgsnfveerr tssvyaildl eflnaiylta tgrndiistl ptnnnsffyp
      661 sigssvvvsq ltklpewfsy lkargswsrv ssgtlgddty tygylpafdk gtswnsipal
      721 tfgsllkqan ltpqtsdswe igldtkffkn rlsveatyyq tsdfnniasp disitsgygs
      781 qlvngniyqr kgmefvvngt vlknndfqwd mainlskyrr ylkeiyggae tlgnlrvgdr
      841 tdriygsvyq tnsqgqmiyg sngfplndnf srfignespd wtygientfn yksftlkflv
      901 dgrigglmys ttnqkmwwgg thpgtlnqyr idanagkatf vgdgvvvtsg tatydangni
      961 isdtrvfapn tkavnyidym ietsngaynn ynffsqtflk lrevtlgwqv ptkllgksfv
     1021 kgldfsvvgr nlllfskmpn idpdpakdnl qtpsarsfgf nvnlkf
//
LOCUS       WP_090500752             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas borbori].
ACCESSION   WP_090500752
VERSION     WP_090500752.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas borbori
  ORGANISM  Pseudomonas borbori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Pseudomonas borbori"
                     /db_xref="taxon:289003"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38683
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikklvgqg hqvtvqsgag vsasipdsay eavgaaigsa
       61 aaafgadlvl kvlapsdael aqmqtgavlv gmlnpfsnet iarinargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atarrlgavi easdvrpavk eqieslgakf vdvpcetdee recaegvggy arpmpaswma
      241 rqakavhera kqadivitta lipgrkaptl lhestvaemk pgsvvidlaa aqggncpltv
      301 aeqvivsnng vtivghsnla alvpadasal yarnlldflk lvidkdgqfh lnleddivka
      361 clmcrdgqvv rtng
//
LOCUS       WP_090500753            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090500753
VERSION     WP_090500753.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113582
     Region          52..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkllplvf vytvltlfll fepimasagg lstavfsktv tdktlnvayi gitgkvtden
       61 gvglpgvsva ekgtrnavvt nssggytinv vnnnavlvft svgykpveit vnaktvvnvs
      121 mvavtnalne vivtalgikr eakslgyaaq kadvqalqtn rttnlanale gqvagldvsp
      181 paagpggstk irlrgqssft adnsplivin glpmsqgass sngytqnvdq gdnlqginqd
      241 diesmtvlkg staaalygsr avngaiiitt ksgstntgig iefnsnftin qaldftdfqy
      301 eygqgennir pssqgtaqss gawsfgvpfd nvptyqfdgv qrpyapvkdr iktffrlaps
      361 wsntvaisgg ndkgsfrvsl anqdaqgivp nndfhkkifn vginykltek lsaqfyvnyd
      421 hqfnnnpplv gvqgnsipts iyrlansisf dvlkagaida ngnetptsrf atitnpywil
      481 anqfqrqtkd hllgtavvry qffdwlylqg ranmdllqtt yesntptgtl avsaaptgly
      541 ngsygistsn trqnnfdfll ggghkwkdfs fnatvggnnf plitstfnea vtnfyirdly
      601 tigngvtans synltkqtvn slygtaefsy kdllylnvtg rtdwysvlar didhyfypsi
      661 sgsfvfsell pkttwlnfgk lrvaiaetgs aqgvgaynal tfllaqnsfn glplgsingt
      721 aspntqikpf gvnekeigie lrmfnnrvnl dvaaydkktt nqavpislsa atgyattlvn
      781 lgglankgle fnlelipiqn knftwktafn safnsskvls lannqsqlvv gspeffgsiv
      841 hmvglplnqi vgstykrdas gnivlsggkp vasdkpvnfg sglptatggw lntlnykgft
      901 fiahidykag gkvlsstsln llreglskes lpgreggvif pgvnatdglp nttavnaedf
      961 yanyrstnil dpfiysssfv klrnlslgyd lskfinkkyv kslvlsavcr nvliikkytp
     1021 nidpeaiass gdnltgyeqa slpttrtygf nlnikf
//
LOCUS       WP_090500957             940 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090500957
VERSION     WP_090500957.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..940
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103451
     Region          51..939
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtryikcsgv mlciisyllt ctafaqtnnk qdtvrimkan rkdstdklie ipfatrsrae
       61 lnyaqsslry nqltqvpisn lsgllagrls gflfrwtgnq pgggnvsyqi rgkssyaqga
      121 tpaflvdgie rdfedmdise iesvtvlkda aglnwyglng gngailvttk rgkigenlis
      181 fdaqggfqsa snlikplnsf dfatlynrgl tnvgqapayn daalegyknh tnpylypdnn
      241 yldrflskra atqryaltfs ggsnrvryfs svsyfnqqgl lketetpnyd snygykrynf
      301 rinldydvtk tltltllagv rsevrndvgd gtstvlsnly nlppnafpil nadgsyggts
      361 lfqsnplgql qstgfsrttt nillasimad qkmdfitkgl sanlffsydg ygnygdglsq
      421 nyavfnqtvt pvqtyrtpav iayrtaafqt ntknnelwfg ldynrtfatd hqikanvraq
      481 qyvsaavdrl dyrsrmivgr adysfkqryr lgftgsysgs enyapgrrfg ffpavsagwl
      541 iskedfmkga svisylklrg sygrsgnigp tydasgnvvr lpyrtlftrd agpflgstfs
      601 tsttarlvsp agnplttwek idrlnlgtdv dflkgalsfs vdyfdekrtd ilgpanlpgi
      661 vgiaiaqvns gkvsskgfda sgtfhkkige vlistnanft yakniilert envlpnqsti
      721 gryvnggnyy iaegifqsqa einaspkqtl sslvvpgdlk yrdvnndkii dandaissdy
      781 tdipkiyygf gfnirykqfd lgaqfqgvgg rtvdvsdivy agpnglnqls ldtwtpataa
      841 takyprigis dngnntanst fwlysgdflk lrsaeigyst pqsfnqrlrf kgarifvsgn
      901 nifsisklge lgidpetpna grfssypyvk tfaiglnvkf
//
LOCUS       WP_090501591            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090501591
VERSION     WP_090501591.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112915
     Region          36..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meksylkwsp gffaillipf lllfkeaaqa qnkrytisgk vtdagnngai pgvvvkvlst
       61 nlvtstntng gytfavdlap gkyqiqfsyv gykskiqavd lggndqvqls aslsadavgl
      121 devivtgtsq gttrkelgsy vstvkgddln kapsgnvlss lqgktagaqi sqnsgdpagg
      181 lsvrlrgiss vnssseplyi idgvivnnst trvtntssny dggnfvgsig qnrmvdinpa
      241 dierievlng aaaaaiygsr ansgviqift kkgvsgaaqv nfstsltlsh lrkqievnqs
      301 plkfggsvnt ftqdviqtag dpamlltntt pvtrynyqdy ifqsatgtdn tisvsggnen
      361 tkyytsaayf snqgiikntd ftrynfranv dqkitewakl saglnyirss anekpdgnsf
      421 fspmnsvtii gnfhdifard angnllavge rgrvnpvsvi edikqrqetn riiananlkl
      481 ypvknltldf tlgvdnsgqs gstyippfay nvnpdfyggg aaldgtlngy asaatnnafq
      541 fnnefnatyq aklsdlisst tqigysfqye ktryqlvngr glaplietvn aaatqlpsid
      601 grtelsvsgg yvqqnfkykd hffvtgalrv dqssvfgsan rtqeylkgsl syvlssadyw
      661 knlgvsgwwd afkiraayge sgnltgigay drinayatqs flgraslfss atlanenvkp
      721 erqrelelgt dlsffknrlg lqfnwynkkv sdlliasvqa pstgfsslld nigslrnkgi
      781 elvlngtpvs akdfkwntsv ifnrnrntal dvgglrlfst npgapvaiin geaigvfygt
      841 ffarnpdgsl ltnangipqi ekgiqnsatt ftpqrdangm ptgttlrkvi gnpnpdynms
      901 fvndftykrl nlhvqldavq ggdvwnadwr trqgvgsgki aeqeqmgllp rgyvagvyai
      961 eewriddgsf vklreislsy nvgklkflrd ltvtlsgrnl iswdnykgyd pelnsggqst
     1021 ilrnidfgsv piprtfslgl svkl
//
LOCUS       WP_090501604            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090501604
VERSION     WP_090501604.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109418
     Region          24..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkllflfl gvcffagqvf aqqitisgkv tsaddgtplp gvsvkvkgsa agistdtdgr
       61 ytikatsdqi lvfsyigsit eerpigdnkv invqlkqdak tlnevavtaf gvkqevrslg
      121 fstqnvkake ivdsqqpnlv namqgkvagv qitnssgapg ssanimirgg sslsgnnqpl
      181 fvvdgipvdn ttpvsqagla astapasnra idinpedies ltvlkgpaaa alygiraasg
      241 aivittkkgs ggaakvtyqn tfsldnvnrl pelqgkykqg eagnfsatap nswgpefaan
      301 etvydnlnnf fktafaqshd lsvsgssers tfytsaslld qgsivdnadf rrksfrvnad
      361 tkigekltvg gsanyvrtdr tsvpqgsang tmgalywprn ddmtnylnpn gsqrvfpsgn
      421 dnpywtiqnk pitsginrfi gianinynpf sflnltyrlg tdlytenfka vrmpgtletd
      481 alkgavaqnt ntnqittstf iatakktfwd dynfslaign nientriqtl tanainfidp
      541 tfpsinntva tdrsvsenln rrrivgvfgd fnfdwknmiy vnlrarndwt stipvgdnaf
      601 fypaistsvv ltdllkelkl ksddqifsyg kiraaysnvg kdapphvitt slaavtntft
      661 inprgfitna nnpfgnptlv peftrafevg adlrfiknrf gidftyyrsk sdnqilatrv
      721 ppsagafity lnggaiqnkg iefvlnaqai vkkdfrwtid infahnksiv kalpgaldrv
      781 elsdawvaan aaqgaaflng slfgingnvw krnaqgqlll sntgypqvqt alanigdrnp
      841 dftsgitntf nyknfalsfm vdvrvggdvf natenslvrs glstktldrg skvfdgiies
      901 tglpntlsvp lsqnyyqtiy anqgydfved gswyrlryat ltynmpnsfl aktklkglaf
      961 tvtgrnlili tkysgvdpev sgsgagvggs gsfgfdnlgi patrgvdmgl rltf
//
LOCUS       WP_090501996            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090501996
VERSION     WP_090501996.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109247
     Region          26..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtklkttfft mamlcflqiy gqtslisgki tdalgqpipg isvkikgitg gtssdtkgvf
       61 sinspnpatl vfsgigyink efaysgqsni tivlsedqqn lneivvtalg vkrekrnlty
      121 ssqevkgdqi tqskepnlvn alagkvsgvq itsssgtpgs ssrivirgan slygnnealm
      181 vidgipvnnd etgnlnsgpg tnriadldpn iiesinvlkg gaatalygsd gakgviiitt
      241 ktgglnkkps isfsssfsme kpllpeiqdk yslgsngvyf dgvsqktsts wgarmdtlki
      301 ngqpapvynq sdlffktgkt ysntvaitgg saynsyflsy tnfaqngtvp ttsfdrntlf
      361 gkfttqiikd lnvtfslnya ntknrrlpeg yalespvwti fsapvsydlq psvnpdgsqr
      421 lfrfsrnnpy wvldnisnts ivnrflptft adykplswlt iterfgadvy veqgkytesl
      481 lsvsnpngri vnnntnfrqy nndlilnank sfgdfnieal lgnniistys qngyanglgi
      541 tipgfnnigs astvkftets yltrkvgfyl qsnidykkfi ilsltgrydg asvlakdntf
      601 ypygsaamsf ifsnffspgv ssvmnfgklr vsystvgnas igayslltpy esqtirnttf
      661 pyqgqsgfli sqtlnnpnlk nerinevevg letgffksri glevtyfdkk trngiiptva
      721 lapstgfnat svnsasmrnr gievllnakp iatkdfnwdl tinysrirnk vlsiykdlnq
      781 vgngftsifv nqpygviygt ryarnasgql ltdetglpfa adtqgiigdi npdwmggivn
      841 nlkykqftfs fsfdmkkggd iqnnvdgygy fygtpkvted rgprvvegvn attglpntvs
      901 vlgqayyqri nsvlesviqd gtyvklrnvs lgyhlkpgwl qkspfktigf qvtgrnlwiy
      961 aphftggdpe vssfgssngs qgiysfstpt srsvdfsvkl tl
//
LOCUS       WP_090502042            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090502042
VERSION     WP_090502042.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122922
     Region          129..1136
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrilylrrva eyscltmmlc actlfcsaql marnvahang lkaqtindnk islkaavqli
       61 ktrfdikiay kagilenkds dltetqlmaf gdaktaltfa lngsmldfnk isesqyiivn
      121 asainladvi kgnifsasdn lpligatvyi kgtktgastd aqgqfsitip nelvgksiil
      181 siasvgyetl elpvtdfkip vsvklkesas slndvvvtal gikrdskalg yavtevkgse
      241 ftqarennva naltgkiagv natglstgpg gssrviirgn gsfngnnqpl yvvngmpidn
      301 svpggaattn glatnvdrgd gissinpddi esitvlkggt aaalygsras ngvilittkk
      361 gvkqkgigve ynttftiena indndyqyey gqglggvkpm tkndaiatgr lsfgakidgs
      421 dyvaadglth pysavkdnik nfystgtnft ntiafsggtd giiyrlslsd ldskgiisst
      481 rfkrqtanln inakitdkik veglaqynle kgfgrtlagd algnpnwtpy evantvdvrw
      541 lapgydaagn qtpwndagia tngyfvinky qqndvknrfi gqgsitydiv knfqlkgvis
      601 rdfynynyvn ilptgdiyip kgqysgiksd vsetnslitg nyknriadki gisilggans
      661 rrfenkqlnm dgntftipff ysyknlatas tiptyqrirt nsvfgsadmd yksilfltyt
      721 arndwfstls pdnnsilyqs vggsfvvsda fklpssidil rvraswaevg ggaadpyrin
      781 lsytnvpsag qplqnvttnd itnpnlkpyt sttyeagvel kmfkgrlgld ftaysrkttn
      841 dilnaaisst sgynnavlnv gelsnkgvef lltgapvqgn kfgwnisynv aynksevlkl
      901 vdgtttfema rsvgnwgyin qtvgsaygti vgtrmlrnea gqivynsatk rpvatglqel
      961 gngvapltmg ltqdfrfgnf nlsflidgkf gnkvfsikev yatrlgllks tlpgrenglt
     1021 isgvdqagnp ysalipvsdl rayyndmrny selfvhdggf iklrqailsy nipvkkldfl
     1081 kiqsasvsfv arniltfykk tdnfdpessy tngnaqgfes iglprtrtfg lnlmvkf
//
LOCUS       WP_090503473            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090503473
VERSION     WP_090503473.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115884
     Region          28..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnillytl livciicctn aysqekniiv ngtvldkdtk qgvpgvsvvl qstnkgltqt
       61 ngdgkfsvnv pvggtllfkf lgyntasaki tgqtnitvti senrkdlndv iivayqnrpk
      121 etaagsvtvl sgkdvsdvpv snietllqgk vpglniqnnt gapgfrgsvq lrglsslsis
      181 gsgndsflqp tsplyiidgv pldadraaef gfqtqgpgvs plslipqedv eniqilkdaq
      241 atsmygsrga ygviiittkr gnskvpriky vsnffvnapp klretlggns erqlkiqqii
      301 lnaeninqir gisntpflad slnaywnnst dwqdvfyqtt fnqshnlald ggdqkfnyka
      361 nmgyyaekgv ikntgynryn lnmnmefkpn dkfrffgfvn gsvgkqnkgn gagllqsgva
      421 angqastllp ppsfyqasgg vlsalqtlnd nnsrnlrani daryefipgl aasstlsydy
      481 tsdtettftp aaangsfakl ydyngrnfql ynrnaityak tlgdkhnffi ntfneiykig
      541 aqssisrqer ipndqlqgpl gydgyysrgg gvlssyknat iasfagslsy dydkkyvaef
      601 syrldgtsss glenpyskns svglrwnfnk enwlidqkwl dygslrltwg qnivptgnlq
      661 siygiynlng nynntqtigi dydlipnpal kptttsqyni gfdigflnrf sivvdsyfkk
      721 vdnllfdrvl snttgfnkla sndlgianyg tevnlivkav tskdfdlsfs ingaynrdvl
      781 lklpeeyngq yirfdgsgyl qhnvfrvgrn tlsnylrinq gvyrtdadvp vdpvtgkryq
      841 tnntffyggd pilkdvngdy ildgrdyeit gnsqplftgg lsltmrykkw glnvyasyta
      901 drtilnnala driaimrdpy alnavvplgd lniwqrpgdv akypypydfa rygniqplra
      961 dqtlwqesgs ylkinnltls ymfdkklirr yglanlrifg stnnlitfsk ysgpnpenvt
     1021 algrdisngy pvprtynigl nlelntgn
//
LOCUS       WP_090503482            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090503482
VERSION     WP_090503482.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113622
     Region          14..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrylwaclaf faaftlnvlp nyaagkknhk gltinylifq dttrikivsl kdslqkdsle
       61 qirkktlynk lsggiqkdtr dlalfpaisl qqnlkgnfag lyvqepsgep gsmqnmfirg
      121 aampllskkd lydaqplvvl dgiplvrehp fafdiqqfdf nrigpatnll agidmnnias
      181 vevlkdlast svygprgvng vivltsktav gryraisfns yigmvqkpfv ntingkyens
      241 frqrfydvyt tngrysddee ypvylsdsln nvysgksdwt dlyyknalvy ginfslaggt
      301 dranfrfalg ntksegvade tgidrysatf ninmkptkwl lfstminanr lnrdrnktlr
      361 drfaqlnyfp dlsaplppnk dfygsylqqy kkgfddnktn siqgyakleg ifgqfkvvss
      421 fnadysegyr dvfyartllq gnsyasnyyg fsqrlmmdnk vtydlnlnkv hdfhfalgqs
      481 mqwdiykysn ayaykgvndy ikinlldskp knddgtdngg yltpvafpre ltyrfldkte
      541 dnllsfygka dysfsdkyfl sailrldgss naqptsrwfy sptisaawnl kneflksnsl
      601 vddlvlrasv grmgrtfsyd nytqgpqyta svgytgnltv pgynafgvlt rpyqfgwvgy
      661 gvpwsysdqf nigadvamlk nrlhvsvdly sktdknqlig ipayaeygyk qaiesgmsvn
      721 nmgidftvsa qviakskfsw nsavnfnhna nelkalprgl dqlvvsnrfl kvgqpvdqyw
      781 llenngiyts dadvptvngq klkykgivlk agdprwkdqn gdntiddndk vlkghslptl
      841 sggfdnnfky gnwslgtsfy fnlgrklinq emanrfdfvn regntdinsv keitfwekrg
      901 dyskyplynp wstvipyrad qdlflenasf lklrqvslgy elgnllnkkn ikinkffvyg
      961 avsniftitp ytgqdpelvs ydgvdtgygq piprtytlgv kmel
//
LOCUS       WP_090501625            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090501625
VERSION     WP_090501625.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118845
     Region          25..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqnllifia lfcsliafdg ygqsrkitgk vldsknmaip nvsiviqdan mssqtdlygn
       61 fslsvnkgvt vvfkslgfqd qsivigdqtn ytikledavr nldevvvvgy gtlkkeaitg
      121 svssinaddi anrpvanalv alegsapglq innsygepgs apsirirgfg singnsaplv
      181 vldnvvysgs vndinpndie sisvlkdats aslygskgsn gvivittkkg kngisnlnls
      241 vnqglytrgi peydkvtpqe ymgvaflgyr nqlmtanpal tiaqanatvn anlvptilkt
      301 nifnlpdnql fdangnlmpd aqikgtyaed ldwfkpisrd gyrqdynlsg qsgseksnlf
      361 yslgyldeqg yiktsdferf tgrvsgsisp rswikaglsl ngnyqvnnnt tgsgsgfttp
      421 wnfarniapi ypvyahnlst geytldasgn kiydngvnsr tqylnrhviw enelnmdrty
      481 qnslisqayv dinflkdfkf stiasnslrn seqrtynnat igdgagnkgr gsrtvyrrne
      541 ltlqqqltyk ksindhnfdf laghesyyyr ynylygyktt etfagqvdlv nftqitnltd
      601 yeqndrtesl lsrlrynyke kyfvegsfrr dgtsrlhpdn kwgnfwsvgg twlvskedff
      661 ssishyvndl klrgsygkvg nissvdlygy mplytigqnn niaalyktqn enpdlkwegq
      721 raisaalegr ffnrlnltve yfdkgsdgli fdvnlplsag atsttsgvsi itknigkvrn
      781 sgfelsadvd iiknpnftwn fganatflkn kivalppenk angiitapfk ymeghsiydy
      841 flyqyagvdm mtgqalyyad daafsptntt gahyqflvnv ngvnytrnat yakrdwsgna
      901 ipdvmgsfnt sfsyknftls tlfnysiggk gfdysyiglm svtstpsavh kdilnswngv
      961 pegmtltspd rinptatpqi nftnsqynnn sisnrflydn syfviknial gynvpknvir
     1021 kldlsklsft flvdnlstft rmkglspqqt fggysesqfv psrtfslgvn igl
//
LOCUS       WP_090504775            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090504775
VERSION     WP_090504775.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111187
     Region          40..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslqltcl llyastglya atpknhfnna vsvhavyqdv ikgtvkdetg atlpgvtiti
       61 kgaqggtqsn tsgqysiaak tgdvlvfsfi gyqrkevtvg tqntiditlt pdsknletvv
      121 vtalgikrse ksltyttqqv sgeelnkvks pnlvnslngk vagmtispss sgvggsakvi
      181 lrgsrsvsgn nqplyvidgv pisnngnana qqnsvfgggq dggdgisnln pddiesltvl
      241 egasaaalyg sqaqngvili ttkqgkagkt qigfsssltf dkiaykpefq nsygpasatt
      301 rdswgtaisn ttdnldqffq tgtnatnsin fsggseiaqt yfsyantyas giqegnklnr
      361 hninlretak flnnkltvdg nvsyinqrin nspsiglynn plvglylfpr gvditpykdn
      421 yllagnvgta rqnwlggsad vsqnpwfltn lnpntairnr ylfsgnvkye ftpwlnlqvr
      481 gnidrttddf enrrysging nfnsngrgyl sqntqtfiqk yadailnvtv plkgsdfkin
      541 gligssindq ktsglslagd lsavdlftpn ntivanagny tsdvlnttka sdayhsqlqa
      601 vfananlsyk dwafltltgr ndwssnlaft pnisyfypsv glsfivsqmv klpeaityak
      661 irgtyaevgn tvpayltfiq ntlgnggalt intnrafael kpertksfei gtdmrflanr
      721 lnfsftyykt ntknqyipvk papsglvgtg ylnagdvqnq glqftlgadv vkgdglnwnt
      781 aingsmnrnk iidvaasqgl nsidltgggn nayisriatg gsygdiygyt lqrdangrii
      841 lngdgtaanp yfpvksadys liananpkfq lgwnnsfkyk dfslsflvdg kfggkvlslt
      901 ealmdqagas kasgdaraqg gvkidgvdas gkavsatinp qsyysflgdr ngvtgeyvys
      961 atvvrlreas igynlplkgt fksmrlslig rnlfyfykka pydpevtmst gnglsgidvf
     1021 nqpvtrsfgf nlnvlf
//
LOCUS       WP_090505427             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas borbori].
ACCESSION   WP_090505427
VERSION     WP_090505427.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas borbori
  ORGANISM  Pseudomonas borbori
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas borbori"
                     /db_xref="taxon:289003"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38633
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikkligqg hqvtvqsgag vsasipdsaf aaagatigsa
       61 aaafgadlvl kvlapsdael ahmqtgavlv gmlnpfsset iarmnargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atarrlgavi easdvrpavk eqieslgakf vdvpcetdee recaegvggy arpmpaswme
      241 rqakavhera kqadivitta lipgrkaptl lhestvaemk pgsvvidlaa aqggncpltv
      301 aeqvvvqhgv tivgysnlaa mvpadasaly arnlldflkl vidkdaqfhl nleddivaac
      361 lmcrdgqvvr nng
//
LOCUS       WP_090505182            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            terrae].
ACCESSION   WP_090505182
VERSION     WP_090505182.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter terrae
  ORGANISM  Pedobacter terrae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Pedobacter terrae"
                     /db_xref="taxon:405671"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116887
     Region          55..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnihilill igfcpliafg qesfsgkils aadstavlsn ieltgadglm rkmqtdakgl
       61 fllrlpagay rfvatavgfk tyavtitlpl trafvarlpp adnqlnevtv stgyqlldrt
      121 ratgsfdkld karldqqvgk nildrleaig ngltfdrtts asgkfsirgt stirgprdpl
      181 ivvddfpyag dlaninpedv esitvlkdaa aasiwgtrag ngvivittkr gkkntplavn
      241 fsgsigfaqk pnlryeqris sadaldveqf lfgkgyytsq inssqkpalt pfvellilna
      301 agklstadle qakagfaahd vyddfdryiy ktgvnqqyal slsgggekha wlissgynhn
      361 vdnldganar qnmrlsnnfm llrnlnlntl fsytggkvta gqpgiggits ttslypyaaf
      421 adangtplpi tknyraayla spavtqlldw syyplldnqy tdnvtrltdl masfdlgykl
      481 plgfklslky nieeqrtnre ilqglgsyyt rnlinsfaqv saggavsypi pigaimdrne
      541 grlrseqyrg qldfnrvwps hrldalvgve wrkaqstgvs grmygvdtdk lntgsvdytr
      601 tfpnsvtgsa ayipdgngls qtannyfsqf vnlaytfkda ytlsasarad asnlfgvatn
      661 dkwkplwsag lgwditkmpf fkvgfidqlk lrstlgfsgn adpsmsgvnt iryqvnspyt
      721 qtpyaifdky anpelrwetv rmlnmgldfs mfkarlsgsv eyyqkhasdl fgiypidytt
      781 gvgttilrnv aeikgkgldl qlnglilqgs ftwgstlnls vykdkvakyy lpsvqgsnfl
      841 qanatvsgve glpvysifsy rwagldgatg epmgflngqp skaystiisg tkltdlafhg
      901 salpryfgnm vndfgfkgft lsvalsfkfg yyfrrkgidy tnlfangsgh adfgsrwknp
      961 gdeqftqvps mpyplsssre sfyrfseeli dkgdhiriqy inldyavgkt lakkiglktl
     1021 nvfanlanvg iiyrankhql dpeyvtssfn lppgqtlafg lragf
//
LOCUS       WP_090516681             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium neworleansense].
ACCESSION   WP_090516681
VERSION     WP_090516681.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium neworleansense (Mycobacterium neworleansense)
  ORGANISM  Mycolicibacterium neworleansense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Mycolicibacterium neworleansense"
                     /db_xref="taxon:146018"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52193
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl tgetrvaatp qtvgqiiklg yevvvengag aassfsdaay veagaeigtp
       61 wdadvvlkvn apddaevgkl rdgatlvsli spalkpelve klstrpitvl amdavprisr
      121 aqsldvlssm aniagyravv eaahafgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivra tdprpevadq vaslggeyls vanenaevsa tgyakemddd ykareaalya
      241 eqckdvdiiv ttalipgkpa priitaemva smkagsvivd maaanggnve gtvkdqaivt
      301 dngvtiigyt dlagrlpaqa sqlygtnlvn llklltpekd gkvvldwddv vqrsmtvvrd
      361 gettwppppv qvsaapaaqp aaaapvvkee kqpmstgrrl avtfaaaaai faliaispaa
      421 lqvhltvfal aivigyyvig nvhhalhtpl msvtnaisgi ivvgallqvg hgnalvtaia
      481 tcaillasin vfggfavtrr mlamfsrs
//
LOCUS       WP_090519719            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niastella
            yeongjuensis].
ACCESSION   WP_090519719
VERSION     WP_090519719.1
KEYWORDS    RefSeq.
SOURCE      Niastella yeongjuensis
  ORGANISM  Niastella yeongjuensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niastella.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Niastella yeongjuensis"
                     /db_xref="taxon:354355"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117736
     Region          22..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllallll pcmlttayaq tktvsgkitd atgtplqsis itikgtssgt tsgtdgsfrl
       61 tvpenatlvf sgvgyeptem svrnrtafdi qltpevksls eivvtgtgva tekkklsidv
      121 asvgnkdmak sailsidqal igkvaganiq slsgepgqkp niilrginsl gstnpiilvd
      181 gvqvtdingl dvsnvekvev akgpsagmly gaqgangviq iftkkgsrnk plaitlnskv
      241 sidnvilged ktlsaklhhf qqdangnild rngdvlqpds ngmwpepaee dfntdfnlkn
      301 nktypstlpl ydhleqayqt atstinslgi sgggnktdys ftlshidqen vlnnhlrrtn
      361 lsanlgfelf kgftarnstq lilqdenlls gtynvtsrml fnvddlfkgt nnnrfemins
      421 ypwidftaky pgtdlvvvrp rdenqlnvls epdwhsrysk dnrvinnsnl nykfprfvel
      481 dfkygielwn sefqdlyknq esspqvdlgy wgntalgsvr ddhakstyqn alssvyvrld
      541 fnkdfklnvp ittttqfsyd wrkleynsff sqgvnlpqyp panitaagvk tsgdgsleyi
      601 tfgylinqti dfgnlfgatg glrsdynsqf gdqkspftfg ratayfrpse llkinvlndw
      661 kvraaygaag ippnefdgny ysrqttlssq qlgsgvglyl pnipgnprlq vqevkemelg
      721 tdvtllpgtk dwfnrislsf tywkknnnnn iqyvdqpass gfqqtvenli dltvkgadis
      781 ldanmytskk vdwtlavrfg tfktkvdrva ngrdfvnglf ivkegeslgn fytsnpltsi
      841 nqtrqsdksr yipeadasqy eiangvvvnk ttkravltda ndqyitgnay pdftmsftnn
      901 itlfqklsis mqwdwshgnd iynltrqwmy rdrlhkdfdk sltingetgs fvnfynsmyn
      961 svqrtgwfve dgsywrmrdl tliyqlgdli kdkaswvkgi altvsgrnll titdytgldp
     1021 eatsaqdsqg nrsvgagsni gadyfsvpnl rsfqfginlq f
//
LOCUS       WP_090521907             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            isoporae].
ACCESSION   WP_090521907
VERSION     WP_090521907.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus isoporae
  ORGANISM  Paracoccus isoporae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus isoporae"
                     /db_xref="taxon:591205"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55766
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkesh egearvgitp sstaflkklg hevfietgag ekagfsdqdy eaagvtvlps
       61 aqeltdgvdv vvkvrqpqdg eigrmregqt lishfypaqn edllakakdq gitaiamdmv
      121 prisraqkmd alssmaniag yravieaann fprfftgqvt aagkvppakv lvvgagvagl
      181 aaigaatslg aqvfafdvrp evaeqiesmg aefvyldfee etkdgaetgg yaapsspefr
      241 ekqlekfrel apemdivitt alipgrdapv lwtkdmveam ktgsvivdla aekggncelt
      301 epdqrivsen gvviigytdf psrmatqase lygnnirhfv tdltpgkdgv idhnmeddvi
      361 rgatvahage vtypppkpkv aaiaaqkpke kkkdltaeer raaevaafka etksqvtlla
      421 gggillllig lvapasfmsh fivfvlacfv gfkviwnvah slhtplmait naissiiilg
      481 almqigsghw lvvilaslav lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_090523910             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090523910
VERSION     WP_090523910.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107837
     Region          27..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mykklllrls aivlcciftg talaqnrtis gtvtdaadgs plpgvsivvt gmsvgttsna
       61 kgvytlsvpa saktisfsyi gytskqmplt adatlnvals aannslqevv vvsvgygtld
      121 krevssaith vsskdllpva snsplmslqg kvaglsitnt sgadpnssps vqlrgvssrn
      181 aglgplyvvn gvpggnidni nqndiesidv lkggaasaiy gtrgsngvii ittkkgssqa
      241 rtfyegyasf dyltnqlqnl tpeqfiadrv knsqgqdyga ktnwmdavtn spafaqkhtv
      301 qlsggsgktn yfasadyrna dgidlrahkk eygarinvnh tsdngvfvas lniaprymnt
      361 knsdqgnfnn altlnptypi ydnagrynyi ntgffsnnpv enanviksea qikemdlngs
      421 lkvnilknls ttvtiseisk strsfnftps tlssilhagk itqtnfasqr qeendqknve
      481 wtgnyslnlg qhhlkalggy sytlynyntf yaqnydfpfd sylwnnlgsg lynggaagqg
      541 qsavsstqng stlisffgrl nydfnnryil taslrregss kfgiknkwgn fpaasaawrv
      601 seesfmkgal pwvndlklra dygvtgnqdf dsylslllyg gagyfpyngq tyqvygptsn
      661 vnpdlkweks infnagidfs ildnrisgsl dyyirknkdl lgyynvplpp nsqsqtfanv
      721 gtmknyglel alngsvirqp dfsynitaal aynrnkfisf sndvykgapf velaglpapg
      781 spgniqriqe grsigefytl rsagvnkdga lqvykkdgti vqanqassdd kqfvgnglpk
      841 figsigntfr ykrfdlgifl rgtfgykifn taafyigtps sqsdanvlrs aydskskysl
      901 ltnpattaia sdyflengsf vkidnvalgy tqpfktkylk siriyatgrn lhtftsftgg
      961 dpdlvqvngl tpgvntslny ypatlqlilg lqatf
//
LOCUS       WP_090524702            1149 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090524702
VERSION     WP_090524702.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1149
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124342
     Region          70..123
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          139..1145
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkldsfifl rcccflmvll grsaygyaqm altsnnriha ksygytdpqa venkvllkda
       61 lenlkkqfnv qiayqeglld nkfvpanlts nisqltlddn lkqllsafql tyrkindnqi
      121 siftvkdltp nnvsvaavtl tgkvvdagdg qpvvgasvyl kmdnkvgait ditgsfrliv
      181 pdkysgkplt lvvafigynq eevavndpas plqiklapnn kalnevvvta lgiskqkksl
      241 gysvtevkgt eftqarennv analtgkvag vnaaglstgp ggssrvvirg ngglagdnqp
      301 lyvvngmpid nsvpggpatv ngitnnvdrg dgiaainpdd iesisvlkgg taaalygsra
      361 angvilittk kgriqkgvgv efnstatydn vavfpdyqye ygqgdggvkp ttlaaaqasg
      421 rrswgskidg stdyvavdgk thpyvaqknn lknyyqtgst ytnslaflgg neaftyrfsa
      481 adlnskgilp gttydrktfn lalngklsdk lsiealaqyn vetghnrtga gdalgnpnwt
      541 plevantvdv rwlkpgydam gneqiwndas iasngyfvin kykeddvknr figqgsviys
      601 piknltfkat isrdffnyny tnilptgtly ipngqyagik sdvsetnela tvsyktkiis
      661 dlnvnvlggv nsrkyttnql tlngsqftip yfysftnlav sstlpynaki vtnsifgsad
      721 fdykslvfls ftgrkdwfsv lspksnsify psvggsfils davklpdffn lvklrgswaq
      781 vgggdpdaya inltysnvps agqplqnvts nnitnstlkp ytsttfeggf elqmlknrlg
      841 ldvtlydrkt tndivntais stsgynnvil nvgqvsnkgi evllngtpvk tssftwsasy
      901 nvaynnnkvv klapglntiq latsvgnwgi ldniegkpfg mlvgtrmqrd angtvvfnat
      961 tglpvqtplq qlgksvaplt mgltnefryk rislsflvdg kfgnkvfsvm evyatrlglm
     1021 kstlpgreng lvlngvdqtg apytrtvpvs glrsyydnyk tyselflhdg sfvklrqvil
     1081 syalptslln kvkiqsasis fvarnlwtiy kqtdnfdpeq sftnsktqgf esiglprtrs
     1141 lgvnlavkf
//
LOCUS       WP_090525523            1013 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090525523
VERSION     WP_090525523.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1013
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109283
     Region          27..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqikhllnvc ffavflflme pamaqnkiit gkvtdkkdgs pligvsvvta vgaqggaitd
       61 angaykisvp asaasitfty vgylnvtvpi ngrtsidvqm seankalnev vvigygtqkv
      121 kdatgsvasl stkdfnkgvi stpdqllqgr isgvqvtpss gepgagaaia irgagsirtg
      181 dgplyvidgi pidnsagtag sygvgagsss arnplsflnp adienisvlk dassaaiygs
      241 rgangvilit trkgrkgqgi qfssntsvss pakrydvlgr daflkavaav ganaspaadg
      301 gvdyggntdw qkeifrspis qnynlslgga skdntgslra sfgyddqqgi vkksslkrln
      361 grinasqsfl ndrvkldlqs tysnvkdqfa pvtnnagfng sligaaiqln ptapvfdsqg
      421 ryfnlngynd agypngnsfr npvsllnqid drdninrfln nltltlklfa gisykgnfgv
      481 disrgvrktf ydpkivgftd aigirqvnyp sptgngtaii thnevtnytt ehtlnydkkw
      541 kdgssitala gysyqtfknf arndfgfgts tagvlvknyd dfkthlpypv gdsssyklqs
      601 yfarvnysyk dryivtgtir rdgssrfgdn hkygnfpava vkwritneef mpkgglfddl
      661 slrlnygktg nqeipdlgsq nlwqllnfpg tataqlhqnn pdlkwqsnit ygagldfsii
      721 ngrlngsvdy fhksikdllf rqdlpqptaa pqlyknldgd vinqgvevgl nfaaiqgkdf
      781 swdvaynmtf isntlknfkn yivtgnidgq glsgayaqli tngvplytfn mpnyagldkn
      841 gfgiypqgid vpslqgspnp kftasltnnf nyknwsfsff lnaatgfyiy nntanaffyk
      901 gnllsgrnvt kdvaatnesp lnsgevstrf lekgdflrls natlgytfpi ksnaiktlrv
      961 sltgqnllli tnysgldpev ntdkqrndva skgidytsyp kariftlgvn asf
//
LOCUS       WP_090525898             444 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090525898
VERSION     WP_090525898.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..444
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49901
     Region          <14..440
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mitrrntcwk pmprydassr fpannrwaff psvslgwaat kekflqnvnw lnnlklrasl
       61 gnlgnqnign ypyqetynfk syynnktsya ypfvgstvts gvinnsltnp nikwettrvf
      121 digtditvln nklsfsfdwy dkltsgilet attltplyfg lnapiinygk mkntgieasf
      181 eyndrfgnvg fsfggniqan kntlvsygap aistgtntin qegqpygsfy mlkyvgifqs
      241 aaeiaasptq qynpqpgymk yadtngdgkv ddsdrvivpg aypkfnyafn tsvnwnnfdl
      301 tvffygsygq klyvngwgiq pfnqgspppk ewlnawtasn psttmpmvyv lgqgnissna
      361 ntastyylrd asflrlknvq lgynlpkdwv khlfmsglri yfagdnlvtf tkfpgldper
      421 ivsntryvth pqnqvysfgv ratf
//
LOCUS       WP_090525899             708 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090525899
VERSION     WP_090525899.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..708
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=77577
     Region          70..120
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          132..>705
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfisksvag mrpaitkvll vmkliaiimi tvfssvsaks fsqtvtlhek nvsvkkilky
       61 iekqsgyhvi linvnpettl agtininleh atveealnec frnkpityti iqgtiiikkk
      121 eeelaaevke sidihgkvid ekgqplpgvn vkvkgatvgs itgaqgeyti kvpdgqavlv
      181 fsyvsfetqe vvvgdkrain itmkeasnrl sevivvgygt qkkvdltgav vtvtgselnk
      241 rvatdptqll qgklpglsvv qgsgeagneg tslrirgtgt fssagnspfi ivdglpgsit
      301 aldpqniesv tvlkdaasas iygtraangv ilittkqgke gkmqlsydyn lgitrasalp
      361 nnmiynsaqy mtlwnqaatn snypnkysda qialytnptd htlypdynwl daifntvkvq
      421 thhlgitggs ngttynvglg yvdqpdvmlg yyykkyniql nltsklnkwa tfgsaitlns
      481 sergytsrgs qdqflsalsq qpmygpilpd gsgrytnsvf psvqtpnknp iaiaknaink
      541 qndyylqssf ylnihllkgl ewrtnggfnf dynktidfkp vinqynwfak pgdapertld
      601 vngqgidvtd nnsfypvayt qftysrsinn nhnfkllagt qveynksqnl eglrnlpfas
      661 ntlqevdagp iasqltngts niyslhsyyg rlnydyqeky lleanapv
//
LOCUS       WP_090526100            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090526100
VERSION     WP_090526100.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114310
     Region          47..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekeikvsgm mlsiaisvlf tlmiaghvqa esavaartnp evgvqivtgk vtdekggpli
       61 gvsvsekgtk ngvltdangn yklqvsadna vllfsyvgyn pkteplngrt tlnvslepks
      121 taiseiivta lgikreskkl gyaaenvrva eittnrstnf vnslegkvag ldisppasgp
      181 ggstkirlrg qsafqgdnap livlnglpls qspsstngyt qsvdlgdnmq qinpddiesm
      241 tvlkgataaa lygsrasnga liittksgnk nggigiefts nftqnkaldf tdfqyeygqg
      301 ennvrpktqg qaqssgawsf gekfdnapty qfdgvqrpya pernriskff rlanawtnti
      361 afsggnekgs frfsysnqda qgiipnndyh kkifnlglny nftpklsaqi yvnydhennk
      421 nppvigiqgs svtnyiyrys nsvsldvlka aavdangnet ptsrfttltn pywimnkqft
      481 rqtkdhllgt atlryqffdw lylqgrvnme yspsyyeqns ptgtlanaaa pvglyngsyn
      541 sndntyraln adfllggghk wgpfsfdatv ggntfpsssq gytvtatnfy vrdfytlgng
      601 vtntsafavs kstvnslygt aefgyksylf lnvtgrndwf svlspehnhy fypsvsgsfv
      661 fseflknpps wltfgkirat yanvgsangi npysnsltft lsqnafngvp lgsisnvttp
      721 nqaikpysvk ekeiglelrm fnsrvnldia aydkhttnqi lsvaisnasg ytgtivnlge
      781 lqnrgmefll elvpvrkpnf swrsafntai ntskvlalan gqkqltlgag effgsivdqv
      841 glplnqiqgs tyrkdangki ivsggkpvas tspalfgsal pkatggwvnt ftykrftlma
      901 hidykkggki lsssnlnflr eglskeslvg reggvkfdav nadgtpntta vnaedfyany
      961 rsqgildpfv yksdfiklrn lsvsydfskm mktkfikglv lsavchnvli ikkytpnidp
     1021 eaisssgdil tgyeqsslpt trtygfnlnv kf
//
LOCUS       WP_090526715            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090526715
VERSION     WP_090526715.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118121
     Region          24..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllaswc lfmlfisvvh aqnktvtgrv tskddglplp gvsvrvvgtt lgtqtnadgk
       61 fslsvpasak slsfsfigft sqtveitsap ldvkltssan klsevvitga ygtkqssrsa
      121 syaaqvvksd alntirqpnv nnalagkvag vqvrsqsaaa lgrntnirlr gatgfgsgnn
      181 plyvvdgtim pnaddlsndd idnisilngp aasaqfgsqg aygaivistk kgkktkgvgv
      241 elnlganfdk ayilpnyqns ygggasadfi qyhwkdgdpe gwkaldgkyy pdytddsswg
      301 pkmvgqeyip wyawaagtky sfktakwtpq pdnakdffrt gvslnnsvaf tkaaddynir
      361 msynnqhttg ivpetwlnkn nftlnanydl nkhltagasi nfsgtqlhgq isdayasass
      421 gsfnswfhrd ldmgimkelq dlkspdgtyv swnhqnpnsy dasnpssfya gnywynpylw
      481 qkqwqnmntr drlygniylq ykinndlsfk vtyrrnqtnt wnegkissei qasgtqtgqk
      541 agygtstsys nrenyetlln ydkqikdfhi nvnagsdfyn wsykdngant nnglsvpdly
      601 tlansvdpis asntriqeqy ravfakasan ykrivyadat lrndwfstis tinnansvls
      661 ksfggsfvfs evlpefkdwl nygkirgswg qvplalgntt etfgayrnnt lygiapnkwn
      721 gallqggptq fvdpalhgtt ttskeigldl gffndrltfg atywaaddkd lplglavnaa
      781 sgvssiltnv glikrrglei tasgtpirlp nfswtinanf aqlldntvve isnkygvdrv
      841 qvagvwgtdm pylinqkgkw wgqiygngik rnaagipilt ssgayindpn vyfgsalpky
      901 tggiqntftl fkefvlsani dyqfggkfas lsnrwgqysg ltantaalnd kgmsvrdpva
      961 dgggvkvtgv dadnkavtyy vdaksyyqgl tnnktydpyi ydltfiklre vavgynlpik
     1021 rwglgnvfqs aridltgrnl lliyakskdf dpseitateg etaqypgtrg fgfnlkvtf
//
LOCUS       WP_090527429            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090527429
VERSION     WP_090527429.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116200
     Region          29..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkhilfyiv lavctilfca dvhaqaqnit vtgtvvekat nkilpgvniy mgskgliqtd
       61 ykgkftvsvp anstltftfv gfvtekvkle pgqknitvtl tedkkglnev iivayqnrnk
      121 esspgaavtl tqkdiqdvpa snvenllqgk vaglnvqnnt gapgfrgsvq vrglsalsvs
      181 gsgsesflqp tsplyiidgv pldadkaaef gfqtqgpgvs plslipvedi qsiqimkdaq
      241 atsmygsrga ygviiittkr gnskvprvry tgnffvnavp qlratlggns errakiqqil
      301 snatiidelr klgqtgflad slnaywnnst nwqsifygtt hnqshnvald ggndrfnykv
      361 nmglysekgv ikntgfdryn lnmnmefkpn dkfrffgslf gslgsqakgn gvgllqqgva
      421 sngqastllp ppsfylspdg vtsalqtqns nstrnirtni dgryefipgl alsssisydy
      481 tsdaestftp aaanaqfaqv ydyegrnftl ynrnaltyak tfsadhtifi ntfneiykqg
      541 gqsgiirqnr ipndqlqgpv gsdpynsrgg gvlsnfknat iasfagsfny dykkkyvlel
      601 syrldgtssn glenpysknp aagfrwnyyk enwfknwdwl tsgglrltwg qnivptgslq
      661 siyglynlng nfnnnptigi nyefvpnpal kpttttqynl gfdmtilqgk vdltfdtyyk
      721 kvdnllfdrf lpnstgfqkk ssndvsiady gyelmvtvrp ltakdfnwtv sfngainrdy
      781 llrlpaeyng qyikfdynny qhivfrvgkn tlsnyllinq gvystdadvp vdpvtgkkyq
      841 tgglafkggd prfkdvngdy ilddrdyeit gnsqplitgg istninyknf glniyasyta
      901 krtilnnals drlsimkdpy allaavpldd ldiwrkpgdq skypnpysfs rfnqikplrs
      961 dqnlwqeegs ylkintvtls ymfdkkfvrr fgfnnvrvyf stnnlvtfsg yngpnpenvt
     1021 slgrdissgy pvprtynlgl nielntsk
//
LOCUS       WP_090527422            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090527422
VERSION     WP_090527422.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113751
     Region          70..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrylwlcfvv faaittnalt glakgnegkk skvkrsvfyk tyirkdttak dsllkdsini
       61 iikhtlynkl adsvtkkpyd lskfpavslq qllkgqfagl yiqepsgepg tvqnmfmrga
      121 pmpllsprdv yqsqplvvld giplvtehpf aydiqlynyn rmgtatnpfa gidmnniasv
      181 evlkdlsata vygpravngv ivltsktpia aksitfdsyi glaqrphvtt ingryenafr
      241 qrfydlyttn grysddenyp iylsdslnnv ysgksdwsdl yyrnasvygi nfgisggtdr
      301 anfrfslgdl knngvadgtv lnrysamfni nmkpikwllf samvnanrie rqrnrylrdr
      361 faqinyfpdl saplppnkey yadylaqykk gfdnnktniv dgyakigidl gkfkfvttfn
      421 ldynegyrdv fyartllqgn syasnyfgfs qrimadnrat ydltvnkvnd fhfelgqstq
      481 wdiykysnay aykgvndyik idlldsnpkn pdgsdndnyl nptafprelt frfldkikhn
      541 lvsfyaktdy sfkekyflsa tvradgssna qptsrwfysp vlsaawnikk evlsnstiin
      601 dlilrasagr igrlnafdny aqgpqytasv gytgnltvpg ynafgvltrp ystgwigygi
      661 pwsysnqlni gtdagflnnr lhlsvdwylk qeknlligip afaeygykqs iesgmavnnt
      721 gidvsvsani irntkfgwts slnlnhnink lkalprglnq iiidnrllkv gspvdrywll
      781 vndgiykses eipvvngqpl kyngialhag dprwrdingd nvidnndkvl kghalpkisg
      841 gydnnfrygn wnlnvnlyfn lgrdlihqem anrfdfinre gnsdvnsvke itfwekrgdy
      901 nkyplynpws tvipyrvdqd lflenasflk lrtvsigydl tkamrlkkik ltrfyvyata
      961 nnvftitpyt gqdpelvnyd gydtgyglpi prtytlgvkm el
//
LOCUS       WP_090527677            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090527677
VERSION     WP_090527677.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113528
     Region          42..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maycyinkcl tgitllmlll vktsyaamqq dtaavaparp gqvsgivlde ygnplqgvkv
       61 inkgknstlt tgkdgmfain aikgdalvft aanynarqvt vkntakltvr lidtyiqapk
      121 tinvlydtis tsknvgaist iytnqltstp atlytyalpg qlpglytqqy sgfaapqtgv
      181 qtvndfigav vqhnnysand ntefglslrg qgpitiidgv qreiasldpe siesvsvlkd
      241 alsnmmlgin ssrgtllitt krgqvgtphi sftaqtgtqq plglpnplpa yqyaylynea
      301 lqndgkpaly ssadfnayrn htdplrhpdv nwfktilrdn spmtsyklnv nggtqvarys
      361 vslnyldqag mfrtasavpy ntnndlnryi insdlavnvt kkftvdlqlf griqqstqpg
      421 agygnilgal ystpnnaypl ynpnntfggt ttytnnllsq tefsgyqrts sndvlanldl
      481 nynlssitpg lsakakgnla fssqsflnrs lqnnaysfna dssysavgss vaqnnsfstv
      541 ssarysfaqa svnydrtfgk snitgmalyd vrsvvlnydl sqvttnralk agynydgkyf
      601 ieaavnssgy nryppgnqyg lfyaggigwq mgkedfikdn fswinswkwr atygktgnnn
      661 vdnygyynfl qtygpsqgys ystgtskspv qgyfentlan pyirwekark ldigadislf
      721 nnhfnitady yhdryydllq vrgnsiallg tsypyenlgi nlykgaeltl tyqnhiqnfn
      781 yfisgnasiq sskiifsdee pypypwlrht grstnaiygy taigyfkdaq daatsatttg
      841 ytaqagdvky kdlngdhiin qfdvsaiggn rplvyygfsa gfnykgfsls fllqgvanre
      901 lmfnnsqvng fagvgflglt ysgqayntil grwtpetaat ataprlsign anntanstly
      961 lrkgnyirlk naevgynlpy ewahklrlsg lrifvngenl ytlygykdfd pevygtaypi
     1021 qrvinagvni kl
//
LOCUS       WP_090528700            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090528700
VERSION     WP_090528700.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115561
     Region          25..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrlllilc sfvfavtqlf aqnhtvtgtv takedglplp gvsvkikgtt tgtqttvdgk
       61 fslsvpnnav lsfsfigyat qdvpvgasan lkvvleasar glnevivtal gisrqqkslg
      121 yaaqqvkgdd ltvtkqsdln talagkiagv qvlggsgakf gtstirirgv nslsggnpiy
      181 vvngvvtdpn ainnddiesl svlkgpaata lygqrasega vvitlkkgsn kgigvslnqs
      241 ttfekvyqlp eyqneygggt sttwktytyd pangspasfa kfngvkyydy gvdeswgpkf
      301 dgtmyapwyf wdpsnpdfgk lkpfvaqpnn vrdfyrtgvt yntnaafska gddynfrvsy
      361 tnidrtgitp nsdqkrnnvg lngelkltkk ltvsanfnfs qinsnnipae gygtqtagsf
      421 sqwfhrdiei dklknykrad gtytswniis pdnlaphywd npyteayvnt nksnsnrvyg
      481 nitasyqftk dlslsliare dllnrddnsr igsgtinids ysqsqytyke nnyvanlays
      541 hnfkdlsvka glyaetrqdr ylftsgntng glatpdlyil snsidaptaf synalsrvns
      601 yygytsfgyk dflyldfnar ndisstlpvn nnsywyggls gsfvftelle kndwltfgkl
      661 rlsaakigsd tqpyqvytty nlsttpygsh pvqtvpntlt nptlkptlst ayevgtelhf
      721 lkdrvkfdfn yytrtakdqi lplpvngtsg ystaivnage iknhgielsl ggtpikskdf
      781 twnvdfnvsf nrnkvisiyp ginslqvspd glggyglsgg nqaagaksfg fvgspsfgvn
      841 gvvgssygqi igsgftrdtk gnivvdedgl pivnntvnlg smlpsytggf tnsfnyknfv
      901 lafsldfqkg gkfvsvtqqn lngsglgiat vglnakgnpk rnavsagggt lfpgvhedgt
      961 pnttyvstrl lyesalsqiw enytfdatyv klrevslgys fpkkmlgrlp fqtayfgitt
     1021 qnpwmiyskl kgvdpsqlqt sfyeggqlpn trnigfnlkv tf
//
LOCUS       WP_090529365            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090529365
VERSION     WP_090529365.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121176
     Region          29..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkiyqrlkt vitvllfcva psilfgqtki sgtvtddkhl plpgvsvrik eqnkgtvtdi
       61 dgrysitata gqtliysfvg yapvyvvvdn kttinvtmig dskalnevvv talgvkketr
      121 rigystqsvn gadvtmardp npitgltgkv aglsvgpsae llgnpsvlir gnsvtlyvvd
      181 gfpintdtyn ispddietyt vlkgpsaaal ygsraqngai littkkgekn kkgltvdins
      241 stvmntgfla fprtqslfgp gentfytfvd gkggapggvd sdydvwgpyf agqlipqyds
      301 pvvngvrqgt pwvargkdnl knflktgyqt nnnislgsvg dtyvtrfsvs qqhqtsyips
      361 qyldiananf yaqftptkrw kfeanvdfnr qstdnfpdvq ygpnsiiyni avwtgadwni
      421 napdikaiwq pgkegvqsvf aeytryhnpy lltqkwtrgh ykndvygyls gnfkindnln
      481 vtlrsqidty nilrtedlpf sahpygregn qgdyredrrn lfdnntelfv nynytiknfv
      541 nlsglvgsnl rsfnynsswt stdylnvpev yafsnsknav qstnfssaer vlsgyysida
      601 tfgkyatlss tgridkssaf qnvttyyyps vsaatvisdy vklpevisfl karasystvk
      661 adassstigp apfnaisvyg gstttsnpns nplflnplgy gstynspyng psyqlnpfyl
      721 tskpynsqpa asasdflyqp niktstrvny eegfdikflq nrlglsattf qyidgpqila
      781 nsistatgyt tlylnalktr ktgyefsleg tpiknlggfs wnvlvnvatf kdvyeelppg
      841 qdayktffkk gdrtdklygt afartpqgqi indaagkpla lpvpqylgne nakyswsfsn
      901 klryknfnmg fqfdgsvggv iidymhnktm rgganietat galgdarykd wqnfgkkgyn
      961 gsyvgegvtv sngaainydp atgkiinyga lqyapngktv fvqdyvskyy nvdesnlmsk
     1021 tfsklrevtl gydfpkawld ksfikkasvs vygrnllyfy gdkrfkdvdl dqynyatsst
     1081 vlqsptvrsy gfnlnvsf
//
LOCUS       WP_090529581            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090529581
VERSION     WP_090529581.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114632
     Region          23..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklllicsf lillisegya qsrtitgtvl dnsskpidgv tivvvetqks tlsdangkfs
       61 iavkngqsvr fsyvgakpil vtitadtktl dvvfkdaenk lnevvvtgyt serkkdltga
      121 vavvdlapvk nnssgntmqa lqgrvaglyi ekdgsangat srilirgant lgnnnplyii
      181 dgipttrpev fqnlspsnia svqvlkdass esiygsrasn gvvivttkng gntegkvqfq
      241 fnnstsiqse kslrfkmlns vdrgralwqa svndgqdpaa gygeiynfdw nnnfgnpvln
      301 svtpkpfvgg dpntpagdtd wqsvlyktaf vynndftasv gnknssiqin fgnikntglv
      361 rftkygrttg sinaitrpfd gkvtfgvnik itnsnetltt ndlggastpf lavtlaptip
      421 vyqkdgvtya gesgagysdr nnplhmqdla kwnnanrlnt fgnvflevqp iknlyfrsny
      481 gadnadylsk vitptfsega lnrttnslff dqnhylsttl sntlrysydl nskhhfkilv
      541 gteyiktftd fqttlkqgya iqtedyftld agtgntivtg rsignslfsq fgrfdynyag
      601 kylvsatvrr dgssrfgtnn qygifpsasl gwkidqenfm kngtlfselk lragigrvgn
      661 qeigdlsrya lyntrygttq nqltpgfweq ymnvgtaysl sgantgslps gfvqtqaenp
      721 alkwettdel ntgldfailn gkisgsfdyf trkttgilit ppvasalgeg qsktvngask
      781 tnrgweflvt yhgqrsgdfn ynvtlnfshf rdkitdlpen vrpaypgnid ntiighsqfd
      841 ifgyktnglf qsqaevdaap tqigagpgri ryvdinhdgk idandqtwig ttlpaleyga
      901 ridltykkfd lsifgsgvag rkgfdvytlf nnlmhsrenv gpgvfdgwtp qhtntnvpal
      961 tlkdnnnegr tsdyfivnts yfklrnlqlg ytilpkavft rlrvfamaen iftvksskyl
     1021 spdperidln pipiprifsf gvnasf
//
LOCUS       WP_090530861            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090530861
VERSION     WP_090530861.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120209
     Region          30..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqfylnlkr wvvlllplfi sanlfaqtnv tgvvrddagp lpgvtvlvvg tttgvqtnin
       61 gaysikvakg avlkfssvgy takevtvgdn avinvtlaag kgelnevvvt sfgikrqeks
      121 lgyatttita kqlteagntn fasalygkap gvkittapgg sssavnvqir ginslnyntq
      181 plyvvdgvii rnnseagadg annggywsdq rirgngildi npqdietltv lkgasataty
      241 gsdgmsgaiv ittkkgsksr glgvdfnyvg taeqvaftpk fqnvygpgyd ratnlaggft
      301 edgwladpns psgyrprfss yaqfgpkmeg qkirwwdgqi rdytpqpnny kdlfqtgyss
      361 naniaisnqt dnvnyrlsat rldytgiqrg qkqqknsfnl nttvklsnki stdivasyvn
      421 tlthnrpyql grvlanfggf lnrsekadvl ldnyqtsagy kyvtlgnavr npteafkynm
      481 sggdimdffw tqlknsedet enrlitsatl nwdvlknlkf rgrigsdytg rntesmqyne
      541 ypvafnspas tgyygvskaq ysgtygdlll tyspkltkdl smsvsggyts rsetyrdqss
      601 gtngglvten ffslsnsygt qtttatrgfm ktqaffgiln lnyknylfle gtarnesasa
      661 lptknntyfy psvnagfvft dafqmpefis ygklrasygv vgnkppryvp nvlynqspls
      721 vpgstvtqlt ydatygnlel kpemkyeqey glearflkdr vgfdltyytn qvkdvimgln
      781 iapsngagni ianaatlhsn glevalngkp ivgkfnwdvr lnfavnhskv nnlapgfekl
      841 tfyngdqsal mvvaqpnqpi gnilvypiat dangnkivng dglytidksk finvgniqpk
      901 ivggiantfn ykgfsldvlv dyrwggkmvs nplkygtaag myestlqyrd aahgglayyi
      961 dgsgkhlgta pnggktyndg vvlpgvneng eknttivdaa syylntydwg ensvnenavf
     1021 knnyvklrev vlgyrlpasv nkalhlnnlr fslvgrnlly vyrtlknldp eapigdkwyr
     1081 qgidegsspa trsfgfslna nf
//
LOCUS       WP_090531376            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090531376
VERSION     WP_090531376.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114351
     Region          27..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkiykllla iilpfilvqt vagqsvkisg evtaksdglp lpgvsvsvkg kttgaqtnvd
       61 gkfiinanvn dvlrvsyigf ttqeipitqg ittlnvvlie apnslnevvi talniskdkk
      121 slgyavqglk skdiseaket nfvnalagki agvqvtnsqg dmgssrivir getsitkdnq
      181 plfvvdgviv dntqflgsgg srdfanalsd lnsediesls vlkgpnaaal ygsraaagvi
      241 lirtktgkga kglgvtinsn tsfsnvqvlp kyqneygqgs ngkfsyvdgk gggvndgvde
      301 swgpaldgsl ipqfysngqa vpfiahpdnv kdffrtgvtl nngialagsn eksdfrvsyn
      361 nlhqtgivpn tsqgrnsfal nssyrfnpkl tvnttvnyik ddadnlpgay gkratstmlq
      421 ftwfgrqvdi nklknykdan gntfnwnnsy ysnpywlaye ntvgqhknhl igsvelnyki
      481 idglsanfrt gtdyyndrrk ikvaygtngt pfgsyeeday svnenntegr lqytkklnnd
      541 fsldafvggn isvktleqnd qlapklaipg lynmgnsrdp lvstnfyskl ktnsvfgsaq
      601 vgfrnyafvn vtarndwsss lpidnmsyfy psvngslils ealgiksdvl tyaklrggws
      661 kvgkatdpyq lrnvfassil fnanpqqslp atdanntlkp esttsaeagf elgffqdrlh
      721 ldvsayntns tnqilavqvs satgfgqkii nggrlnnkgl eiqlgitpik skeftwditt
      781 nyslnrsmva sldaegrlqs lpigsdrtvq vtaalgqpyg alygtaytrn asgqividan
      841 gtpvfnttkr ylgkftpnwl gsinnsftyk ginlsflvda rfggsiysnt nrtgtytgvl
      901 astlpgrgaa ngglsyyysd nkttnpavqv tgaapagvtv yndgmifkgv kadgspntti
      961 ipaqsyykgf tnideafvyd asyiklrevk lgyslpakwv nkigfqgatf svvgrnlwii
     1021 hknapnidpe tafnagngqg ledltlptvr nigfnvnlkf
//
LOCUS       WP_090531395            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090531395
VERSION     WP_090531395.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110236
     Region          30..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfkqllkrf ilpllsvfvf cystyaqtvt lkgkvtdekg epivgasvki kntsagsvtn
       61 gsgmfslnyt gqgtlmvtai gfatqeiklt gqaqvnvala ednkqlnevv vtalgikrdk
      121 riltyssqev kaesivqske pnlvnalagk vsgvqvtsss gtpgssariv irgatsfyge
      181 ngplmvidgv pvdnaetgnl nsgpgtnrla didpsiiasm nvlkgaaata lygskgangv
      241 viittkngal nqkplitfss dfsfenpllp qiqnkysqgt ngiyydgvnq ktstswgarm
      301 dtlkingqpa kvynqsdlff ktghtynntv niggggnnst ylvsysnfnq qgtvpttkfl
      361 rntffakysa qvlknltttf qlnysnsqnd rlpegyales pvwtiftapv synlqpylnp
      421 dgtqrlyrfs rnnpywvldn iknhsgvnrf lptftadykp fswltiterf gadvysemdr
      481 yhestqsvsn pngrlvdqnl tyrqynndll isankqfgnf nvdvvlgnnl istygestya
      541 ngvgltvpgl ynmasastvn ysegsslqrk vgfylqsnie ykrflllslt grydgnsvls
      601 idhsfypygs aagsfifsef fspefskvmn lgkvrvsygt vgndgnigay glltpynkat
      661 irnlsfpynq qagflindvl gnpnlkneri nefeagfeag ffnnrislea sfynkktngg
      721 iiptvalpps tgysatsvns avmrnrgiev llnvnpiksr dfnwdltlnf trnrnkvlsi
      781 ykdlslisng ftnvivgqpy gviygtryar naagkllidd sglpyaddnq givgninpnw
      841 lgginnnfry kqfnfsfffd ikrggdiqnn vdgygyfygt pkitenrglr vvdgvnattg
      901 qpntvavngq ayyqrangvl esviqdgsyv klrnvslgyt lkpswlsksp fksatfsvtg
      961 rnlwihaphf tggdpevssf gssngsqgiy sfstptsksv dfslkvtl
//
LOCUS       WP_090531639            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090531639
VERSION     WP_090531639.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114987
     Region          23..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklflllsv llclgsalka qdrnitgtvt dekgaplpgv aiqvkgsttg titnadgkys
       61 ikatnlqaiv vgakflgyny qektlkigem nadfkmvpsq naldevvvvg ygtqkkvhlt
      121 gavaavdmkt iqdipttnla aalrgtnaav svtggiarpg qsgtitirnp vflaknggst
      181 tplyiidgvq rseadfnlld qsevenisil kdaaaaiygi lgangvivvt tkrgqaggpk
      241 vsfsssvgia daiqlpkmms gfqmatylnd ieqtrynhti tpegyingdl snkdlkyytp
      301 deleyfknnn qnfleqafkp avtsrnalsi tggndkvtyf aganyvnqns nfkgvntnrf
      361 gfrasvdakv akglklslsl sedlakskiy wyklsstses pdndflslnq appwqkyfid
      421 ghpvylgtsn ndnlnffavq nsnnytgnnn tvfnglanls yeipgisglt anvsynrnln
      481 nafnkqygst fyynqysgeg dnnhipggtv vgvkaikngd rvrltptmad nyqfnanlty
      541 hkrfgaheit alalyeqyes ysegvaaead gvivggkdnq tftigdqssn qatlvkeygr
      601 kavagrvnya yadkylvela mradantnfa pghqwgyfps asagwviske nffksvsfvd
      661 llkfrgsvgl lgsdntpsfl yavnyqfgtg nkggavfggn sdrglgalln iaipnanltw
      721 dhdlktnygl daaflgnrls vsadyfwehr ydmlaslnts vpvtigaaps aenygivntf
      781 gyeisvswkd kigsnfsynf spffswsdnk yikydiaaaq vgtiqdltgk ssdqgtlgyk
      841 slgiirtqad adaiiaeraa aaggaqnvki fgyvpspgmi nyvdkngdgi ikqndlndqf
      901 ylgkkssnhy nlglnfggay ktlslnvvmg mswggnqsie saaikqatan qnrpvfwadh
      961 wtpsnpnaky pdpyysddvs atsdfwfvsp ftwnissanl sytlpasitk rlgmssiray
     1021 vvatnpinfv npfpehyrdi sspfgaypnl rtvsfglnlg f
//
LOCUS       WP_090532623             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sartisoli].
ACCESSION   WP_090532623
VERSION     WP_090532623.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sartisoli
  ORGANISM  Paraburkholderia sartisoli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia sartisoli"
                     /db_xref="taxon:83784"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39525
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr pyetrvaatp etvkkyvsqg hrvtvqsgag tgasftdeaf aaagaelvda
       61 ptafgadlvl kvqsptdtel pmlrrgatlv gmldpfnsen ssklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllgatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmpaswla
      241 rqsvlvhera kqadivista lipgrpaptl isvetvqamk pgsvlidlaa grgpeyegqr
      301 ggncpltead kvvtkfgvqi vgytnlasmv psdasslyar nlldflkliv tkegalnidl
      361 addivaatll ardgavtrka
//
LOCUS       WP_090532933            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. NFR10].
ACCESSION   WP_090532933
VERSION     WP_090532933.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. NFR10
  ORGANISM  Mucilaginibacter sp. NFR10
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Mucilaginibacter sp. NFR10"
                     /db_xref="taxon:1566292"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115416
     Region          24..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkitlifv llitiltrtf aqditvkgiv kdnqglpipg atvknkstga vtvtdlkgsy
       61 sitangnatl vfsfvgsatq eqpvngrtti dvtladankq leevvvigyg travkdvtga
      121 issvkaekle nehpasatdi irgnipgisv alntsakggg tgdlqirgka slsgnvqpvi
      181 vldgviypgq ladinpndid rvdvlrdpsa lavygaqsag gvvaittkkg kkggtqitln
      241 anfgiaqllq nqkyytgdgf lnwradgars sntsnpyyyy snpnklpegv tldqflngat
      301 gdpttiwlqr lglfpneian yqagkmtdws klifrngfrq dytgsfsgss etvkyyvsgn
      361 ytknqnliqg gqytdgrfrv nlegkaakfl tlgvnaqfas rdegaastpl sgqgidgtea
      421 dwtqiinssp ygdvynadgs lrridtddsg lnqrnpflgn rynqnvavqn tlfsvlfarl
      481 dlpfgikytv nyaptiesyr nfffrpvanp nelsggtair tqenryrynl dnilswnktf
      541 gihsfdatfl lnkekyqtwy tnasntqltp tdilgyhnig agnlpvessd driynadaim
      601 grinytllgr yivtatvrrd gfsafglqhp revypsgaia wvfsdesfmk gdafkwldyg
      661 klrfsygang nrtstttadp sislavlggi kyptannsgt vtnnsgiyvs tlqnaqlkwe
      721 rtvgpnigld ftilhnrlsg sidvydrktt dllvkrsild vqgynssgdl vggannsnpy
      781 tnigqvnnkg feisldgkii ksenfnwnas gtfflnrnki vhlygafpvt dangvttnve
      841 kddigngwfi ghdinavwdy rilgvwktad ateaarygak pgdfklqdvn gdfkftnddk
      901 qflgstnprf swslrndfnf lkhfdvsfll vssigqlrqy nqalnnpgsv gfarmnsyvl
      961 pywtpdneid dyarlnsgss gttinvwrka sfvrlqtasi gytfspqlik rlgissaklf
     1021 vnasnaavfs swplwdpqng gptprylsag fnvvf
//
LOCUS       WP_090533621            1009 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Mucilaginibacter].
ACCESSION   WP_090533621
VERSION     WP_090533621.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mucilaginibacter
  ORGANISM  unclassified Mucilaginibacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="unclassified Mucilaginibacter"
                     /db_xref="taxon:2617802"
     Protein         1..1009
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110251
     Region          38..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meknyrsilr lwhrsgktic lfmlmlmass avfaqdgtik gtvtdesnlp lpgvvvtvks
       61 sgrststnan gaytvktsga gdvlkftflg svpkevtvge kntvnvtmvt dtkqlkdvvv
      121 igygtasrkd vtgaitsvka eefnngvltt paellqgkva glnitksgdp nkqpatilrg
      181 pstfregaaq qpfyvidgvp gasidllapa diesidvlkd asstaiygsr asngviivtt
      241 rkaktgqtrl tysgygavek vsknidvlta delrkyladn gvaalskptd ddgsntnwqk
      301 laektsysqn hnlsyggagt nseygasvny lknngilknt slertiykgy inqrffndrl
      361 klsinltnsa tknndiyqsq vlsgilfylp tvspfnpdgt ykenytrtgs gplnplslid
      421 nnfirtennk tlingsaqvd ilkglkftlt gstqkeqnnv niystsqsgi fvnahgvasr
      481 saytntsnvv eayfnydrvf gqhslkllgg ysyqqdrnnd gfgvqtqnfs ndaltynylp
      541 fsnptqlsqi ifnpnyains napaityist lrlisfyara qyqfsdkyll qasiredgss
      601 afglntrhgy fpavsvgwki isedfmksip visdlklrag ygvsgnslgf daftarliyg
      661 vppgggkfls ngnivnpigp vrndnpdlkw estgttnigl dfgilnnrit gsvdyyvkkt
      721 sdliatypvs stlyfypfyt anvgkiknng ievvinaipv ksqsftwrts fnvshnknvv
      781 eslsnsrftl pfiqtaqlgg kgqsgnysqi iqpgyaigtf dlwhymgkna ngvstyqkad
      841 gsvvatqplt sdqfikydaq pklvygwsns ffyknfdlnf lvrgvygnki lnatlaslnn
      901 padarlqnip rftlgesfkd inaylisdrf lesgsylrld natlgytvkp hiqaikslrf
      961 yasgnnifii tkyrgvdpev niggltpgid nrdfypktrt fslgitaqf
//
LOCUS       WP_090539175             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas sp. Nm132].
ACCESSION   WP_090539175
VERSION     WP_090539175.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas sp. Nm132
  ORGANISM  Nitrosomonas sp. Nm132
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas sp. Nm132"
                     /db_xref="taxon:1881053"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39403
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeiy agetrvaatp etvkkytakg fhtvlvqsga gagasipdaa yqeagativd
       61 dvsqlysqsq ivlkvrgpgt delalirkda vligllsphq megievlarh gltafsmekl
      121 prisraqsmd vlssqanigg ykavimaanv yqkffpmlmt aagtvkaarv lvlgagvagl
      181 qaiatakrlg avieafdvrp avkeqveslg akfvevplte eekakaetag gyatemsedy
      241 krrqgelvha raaaadivit talipgrpap vlireetvqa mkpgsvivdm aveaggncpl
      301 selnktvvkh gvhligianl pglvaadasa lyarnlmnfl nlmldsnnge lkinwedeii
      361 agtlvcsgge vikki
//
LOCUS       WP_090544777             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia caballeronis].
ACCESSION   WP_090544777
VERSION     WP_090544777.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caballeronis
  ORGANISM  Paraburkholderia caballeronis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Paraburkholderia caballeronis"
                     /db_xref="taxon:416943"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54076
     Region          3..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mamtiavpre thpgerrvaa tpdtvaqllk lgyaveietg agalasfddn ayraagatvv
       61 sdthalwsna dvvikvrpps leeaqrlkpg atligfvwpa qnpalleafa arnatalamd
      121 cvprisraqk ldalssmanm agyravieaa qhfgrlftgq itaagkmppa kvlvigagva
      181 glaaigaarg lgaivrafdt rpevaqqves mgaeflqvda deegggaggy akqmsakfie
      241 aemalfeaqa rdvdiiitta lipgkpaprl itaqtaalmr agsvivdmaa eqggnceltr
      301 anevvnvggv tvvgytdlps rmatqssqly atnvrhlltd ltpakdgelk ldmddvvqrg
      361 ttvvqrgalc wppaqpapqp tpakpaaeaq ppaiaaagsp ldaaararrr gafslvalav
      421 aavgllalga vappsfvahl tvfvlavfvg yqvvwnvtpa lhtplmsvtn aisgiiviga
      481 llrpgstetl vsvlagvall vatiniaggf lvtqrmlkmf qrt
//
LOCUS       WP_090546231             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia caballeronis].
ACCESSION   WP_090546231
VERSION     WP_090546231.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caballeronis
  ORGANISM  Paraburkholderia caballeronis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia caballeronis"
                     /db_xref="taxon:416943"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39652
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anetrvaatp etvkkyagqg hrvtvqsgag vpasfpdday aaagaelvda
       61 atafgadlvl kvqspsvsel pfmkrgavlv gmldpfnaqn aaqladaglt afaleaaprt
      121 traqsldvls sqaniagyka vlvasnlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atarrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqsalvhera rqadivista lipgrdaptl lpaetvqamk pgsvvidlaa grgpvadeat
      301 grrggncplt eadqvvvrhg vqicgytnla amvaadassl yarnlldflk livtkegtln
      361 idladdivaa tllardgqva rka
//
LOCUS       WP_090554949            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090554949
VERSION     WP_090554949.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112426
     Region          24..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkkvlyllg fvllfavqaf aqtrtitgkv tdagdgtplp gvsvsagrng avtrtsaage
       61 ysltvpnavk nlsfsfvgyt grtleitsqk lntaltssqn qlnevvvsgy sttskkdftg
      121 savkvtaaqi ankpvqsfdq alagqaagvn iiqpngvlnn ppvfrvrgfn sislssypli
      181 vvdgvpvftg ntgntssvss nsasnnplgd inpndiesid ilkdasstai ygsraangvv
      241 vittkkgkqg ktrinydgwv gitkafnlph llnaeqyvtl knearvnanl apafalqkda
      301 sgnnietdwf kvvyqtgisq nhnmnisgat entsyflstg yskqesfikt nsferkifrg
      361 nvdhhlskai tvgtnfsysn tlnigpnsgs llgqayntgg larlplvlfp nvspynadgs
      421 ynisgtgtlg qgantvsnny pnavvlldnd rftskndnii anvygeleii tglklktqys
      481 inklntants fqnpiagdgq snnglalntf eeynrrdwtn tlnyvvalgk nhinalvgqe
      541 eyhttnvgtg tertnladsy fknyqgnfln vrstpatgnf nsengfrsff gtvtydfdkk
      601 yllsgtfrrd gfsglsannk ygnfggasig wniaeedffk sstlstifdd lklkgsygvv
      661 gnigvsdyas lslfnsglyg gsstvyfnqa gnpnlkwets kktdagisfs lfkgkiqadi
      721 dyynnsinnl ilnapqspsr gipgdpanti aanvgsmfnr gfefsftsrn iarsnfswtt
      781 nfnistlnnk vtglaqgnsd iygstsglet anitrvghtl gsifvvptag vnpangqrif
      841 vnrfgqqvqy nqaaaqkwty ldgtvapaid gtldgtiagk siptyfggln ntftyknfdm
      901 ivgitfsggn kiyngtqatl rdqrfwnnht eildrwtapg qqtdiprvvy gdnvsngsai
      961 pnssnvqnga yaklknvalg ykfpaelins agisslriyv qatnlavvtg ykgsdpevss
     1021 ngnsnlspgv drntvpsari ftfglnvgf
//
LOCUS       WP_090555376            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090555376
VERSION     WP_090555376.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114525
     Region          27..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfklyklvig iiislftlqs ataqsvkisg vitdkasgqp vpgvsvsvkg sgngtqsnsd
       61 gkfslnakpg dilsvasigy tsrefpvsse npvlnivlee sqnalsevvv talnipkekk
      121 slgyavqelk skdiseakea nlvnafagki agvqvtnsqg dmgssriiir getsisgnnq
      181 plfvidgvpv dntqtlgnta isatagsrdy anpisdinse diesisvlkg pnaaalygsr
      241 aaagvvlvtt kkgkgskglg isinsntsfs sllvlpdyqn sygqgangqf sykdgagggl
      301 ndgvdeswgp rldgrlipqf nsngvavpfi ahpdnvrsff ntgrtlnngi sfsgtgekfd
      361 yrlsynnfdq tgvipnssqs knsflfnssy kitpkltlnt yanyvnssad nlpgsggkra
      421 tstmlqftwf grqvdveqlk nykdangnni nwnnsyysnp yfiayentvg qvrnrlignv
      481 elnykiidgl sanfrtgndn ytdrrktkia ygtngtpfgs yeedaytfne nntearldyt
      541 kklskdfsld vllggnirts tlenndqlas klavaglytl snsrdplisy nyytkqkvys
      601 afssaqlgfr nyaylnltar ndwsstlpve nrsyfypsln gsfilteafd iksdvltyak
      661 lrggwskvgk daspyqlint ngflapfdgn pqqyanaidl npdlkpettk steagfelgf
      721 lqnrirfdas vyntnsinqi lsldvststg fsqklvnggt innkgvelql gltpiktknf
      781 swdintnfss nksrvkslyg diqsyvlgtd gtvqilaaig qpygsifgta yernaagdii
      841 vnadgtpais askkilgkyt pdwlggitns fiykrinlsv lvdahvggki ysgtnatgty
      901 tgvlastllg rgtengglsy yypgndntgk avqitagsaa pggatvyddg lvfkgvladg
      961 tanstiipam qyykattnad etavysatyv klrevklgyt lpqqwiksig lqsatisvvg
     1021 rnlliihkev pnidpetafn agngqgledl tlpgvrnigf nlnlkf
//
LOCUS       WP_090555662            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090555662
VERSION     WP_090555662.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116457
     Region          23..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkqllicfv fllfaigana qdktvtgtvt skadglplpg vtirvrgvkq gtitnasgkf
       61 slsvpqgsat veisfigylm qavtipasnv inatlsedsq qleqvvvtal gitrkknelp
      121 faaqelkaee itrtrdinlv nslggkvagl dikrsnamgg stnvvirgsk sitqgnqalf
      181 vidgvpvsna santenqgtg ragydygnaa sdinpddvas mtvlkgaaat alygsraang
      241 viiittkkgs knstnitvns gvtfgkidks tfptyqkeyg qgynspatdg vgntvptagf
      301 wyrdvfgtgk vmtpqfssda sygpkfdpnl lvyqwsaldp fspnyqkatp wvaaangpet
      361 fyetavtsnq sisidgggek stfkigytrn dekgvlpnsk itknlfnfgg syemaknltv
      421 sasanyskid glgrygtgys glnpnqgfrq wwnvgadike leeaynrngk nvswnwgdat
      481 gtkpiyadnp yfnryqnvan dtrdhffgnt alnykvndwf nvigrvsydg tsdlqeehia
      541 igstalplya rtngtfsetn fdlllnfnkn itedisfkgl lgsnlrrsrl tnisaktngg
      601 ltvpglysls nsvspieapv eryerkavdg yfasttfgyk dlvfidatvr rdqsttlptn
      661 nnvfwypsva gsfvfsnvlk dltwlsygkv rlnyaevgnd apnlsvydty tkptafgsip
      721 mfsvsdtknn galkpertks ieagvetafl nsrfgfdvtl yktntvdqit pvsvttatgf
      781 lklyvnagev qnkgievsaf lvpvknknfs wtlnvnwskn ksevlslyen vqnielntls
      841 lsgavtynaa igqpygvikg tnyvynngqk vvnangyyaa tassaevigd pnadwmggig
      901 ntfkyknlsl nflvdirkgg dlwsldqwyg qgtglypnta gtndlgnpvr sslatgggii
      961 lpgvladgtp ntkridvsns gasaygypnn pprastiyda gyvklreval gyslpqkfvs
     1021 klrafkgidv slvgrnlwii hknvpfadpe dglgsgnvqg yqsgsypavr tvgfnvkfrl
//
LOCUS       WP_090555985            1138 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090555985
VERSION     WP_090555985.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1138)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1138)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1138)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1138
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1138
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122711
     Region          136..1137
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnkilssrf sfknlasfil tiilfqyals traastvkqg ldtkitlkvt nmpvaevlkk
       61 inhlvkidfa ygsdalgdnk kvslnvkeek lsdvlkmild pfhmefyyak dliliqmiqe
      121 dskhpvknit ankqsqvtgv vtdakglalp gvsvklkdgq aaastnadgk ysislpdgng
      181 nlvfssigfi tqeipvsgrs tinvsmkees qalsevvvta lgiarekkal aysvtevkgd
      241 eltkarennl gnalagrvag vnasstatga ggssrviirg ngslggenqp lyvvngvpmt
      301 nstpstpgty ggvdrgdgln sinpddiesi svlkggtaaa lygsraangv ilittktgkg
      361 qrglgveynt tytmetplsm pdwqyeygsg drglkpasks eaiangrisw gakldgssvv
      421 ntdgisrpyv aqknniqnfy dtgntfsntl altggnetsn frfsasnmdn kgivpnssln
      481 rktfnlsasa nlskkvifeg nvqfnieknk nrsyiadftk npnasvglia tsldvrtlap
      541 gydaqgfevp wndyvfvvnp yfavnkvqne derkrfigsf strynitdyl yargrlgidy
      601 fntngfdinp sgiltdtrgs mttdrnstye tnaeallgfd ktfgkfsvna liggnqmhsq
      661 vragtlssgl fnvpftyfig ngssqtftdt fsesainsff ssadigfnny lylsltgrkd
      721 wfstlsmann slfypsagls filsnawask pswlsyakvr sswaqvggga pnpyslalty
      781 taqsvthlgq pllaitgsni pselkpytst tteagietrm fnnrigvdlt vynrvttndi
      841 vnaavavsss fnsvslnvgk mrnkgvelll tgtplrsskg inwdvsfnma ynnnkvinia
      901 egldklalpg amprtenayv yhyegqsfgm iagnkaktda ngnviynsan giplqseivp
      961 lgkgvppwtm gisntityrn vslgflvdgk fgakmytstn aygtyygldk rtaangvren
     1021 gitltgvdet gapfnktvsa qdyyqgiayt ltdqflydas fiklrqitlg yslpkkllak
     1081 tpvqsatlsl varnlwliys kvpnvdpest ynnsnaqgle nfgvpttrsy glnlsvkf
//
LOCUS       WP_090556101            1091 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090556101
VERSION     WP_090556101.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1091
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121236
     Region          50..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlviagrr ssyackilll lqitilmtcg sarqvyalts ktpqalrini kvrgrivded
       61 gngiagavik ikdgkttvls dlqgyfwlla vddhavltis hlgfqqlemr vkkdlgeirm
      121 kesygqlnev givstgyqsi pkeratgsfv lidsallnrk vstnildrld gvtsglifnr
      181 nktgntpyis vrgrstiasd anpliildnf pydgdisnin pqdvksvtvl kdgaassiwg
      241 sragngvivi ttykgvfnqk pmvtlnsnvt iggrpdlyyr pqltnqqfig ieqflfdkga
      301 yntvinngys slspaveiml qnrkgtiteq rksalldsia mhdnrddlkk yyyrpsvnqq
      361 yqlsvnggga nnkyyvsmgy dknqantvin sndrislnas ntvsmlnnkl evvtgimfta
      421 snanvdgtay tpqfpyenla dqngnalait ktlrlpyvdt vgkgrlldwh ykpldeirnp
      481 sttqrsrltd yrinvglsye ilkslrlsgs ytydkgvdeq vkrntlasyy trdiintysq
      541 inqatgvvty pvplgeiadn ssrlyyshya rgqlnyekli agkhavnaig gievkdyqsk
      601 fnsftlygfd netlsnknnt inptvlypgi ygfnssripl nianastidr yrsyffngsy
      661 tyndryilsa sarkdesnlf gvktnqkgvp lwsaglawni snesfyhfdq ltylklraty
      721 gysgnvnksv sayltaqamg lnnlwnvpyv titnppnpsl rweqvrninl gldfqtranv
      781 lsgsveywik sgfdligtsp iaqqtgvssf tgntasmrgq gvdvtlnsnn lkvggfswsa
      841 qfhfnyntdk itdykvkavd ngsivnnnfm spvigrsyya vfsyrwrgld nqgnpqavln
      901 gvtstnypgi tnstnindle yngtltpkyy gnimnniswk afqlsfnivy klgyvfrras
      961 lssssvyaat vygasryqqe dyeqrwqkpg delltsvpal vypvnssrda vyssssalie
     1021 kgdhirlqdl rlgyspgirn takawlkhlt vfayasnlgi lwkatgrkvd pdyssgiplp
     1081 ktlaigfkgs f
//
LOCUS       WP_090556382            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090556382
VERSION     WP_090556382.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122256
     Region          53..115
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          133..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myktfttigk wrsyalkill imrlttvill atllqvsatt fgqkvtlrqn aislnqvfni
       61 lekqtgytvm ytteslndel kintnfnetp leeaiktiik dlpisytikg kaivlqrvek
      121 nilekivnvf snidvsgrlv dkdgnpisga titvkgtnrt vlsgstgffs lsnvdeknil
      181 tisyvgyval eipvqknlgn ivlnaadskl eeveinagyy tvtdrgrtgn iikitsttie
      241 kqpilnplqa lqnripgiqi tqttgvaggg fnvlirgrss intqvgnnpl yiiddviyps
      301 talggnnqan afgiaridpl stinpndies ieilkdadat aiygsrgang iiliktkrgk
      361 agdikingvf tqgfsqvakk vnllktseyi emrmealknd glspstidyd ingnwdknky
      421 tdwqkeiigg tantsvasln isggndkvny liggnyyneg tvlpgnfgfs riglrsninf
      481 gsfkdrvnln ftstynhttn sqlgfdptan illapnqpdp ynqygqlnwa nntvyanpma
      541 sflnsnkigi dnmivnatls yrlldnlsfk issgynllky edfiknsfas isparnptsa
      601 srrssfsnss inswtaepql nfktkiglgh ldalaglsfq esinqsrgld atnfasdell
      661 dnilsagsit asaatytqyr ysavfsriny sladklfvnl tarrdgstrf gkdkqfanfg
      721 aigaaylfse erfiknalpf islgkirasy gvtgndqigd ykylqlytss giyqntstls
      781 ptlgnadygw etnkkgeial qlnlfkykvn feisyynnrs snqligdplp pstgngtiia
      841 nrpatvqntg lefatnfnli knknwrwtsg inltipknkl lsypgiensa davnfvvgqp
      901 lsivriynsk gvsrqtglye fedknnngtn lfddgdrylq kfigqyfygg fqnslryknl
      961 tldflisftk qngfnylnsi qsvpgnwsan sypasnqpta aldrwrqagd nssaqkfsts
     1021 ldaddafyna iiygglnvsd asyarlknls lsyaipnewl akshisnasi sitgqnvfti
     1081 tnyigldpet mdlrrlpplr tfamsinltf
//
LOCUS       WP_090556585            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090556585
VERSION     WP_090556585.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112393
     Region          25..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiyvrcfc vlllslltms tyaqktvtgt vkdaggdplp avsvmvkgtk lgtntdgtgr
       61 fsisapanav lvfrylgfki qetavgtsgi vnvvlledkn dlsevvvtal giqrekkslg
      121 yavqevkgst lvetrepnlv ntlsgkvagl qvtrssngpa gsskitlrgn nsltgdnqpl
      181 ivvdgiplnn ftgninpssg vlnndyynpa idmgnglsdi npediesisv lkgpsasaly
      241 gsragngvim vttksgklqk glgitvsstl giesvftnpk lqgdfgqgtn gvfdkvsdls
      301 wgpkisgqsv aawngdgplr sydnignyvd qgissnqsvs fqqqvnstsv ytsfnklddk
      361 siipgaelhr tnllaratsk fgkddrwvtd tkiqytnska enrpnnganv nnvfatlynl
      421 prslditqfn pstdrdgkmi wynptstdln pywakqynln qdvrdryvmn gsvkynfnsw
      481 lnaelkggad systtvegkl yggspssatg qyslsketft etnfsalisg rkdnvfgrlg
      541 gafsaggnlm sqensilgss sgqlvvpnlf slnnginspt vsqtyrrkki nsvygtaqln
      601 wdgylfldgt frndwsstls psnrsffyps vslsyvvtem ftkmgktlpt wlsfaklras
      661 yatvgndlga yqlyntynig kdpngnttas rngvlfdenv vneliksfea gaemrflngr
      721 fgfdlsfyks natnqlidlp ldplsgyssk kinagniqnk gvelmvdani lsnpnslnwn
      781 lsanyshndn tvkylsgdvs qyrlggyddi silavaggky geiygskflr vnspgsaldg
      841 qllldanglp qrgeqnvklg nqqadaligi tntfgykgfn lsflvdgrfg gkifsgtlaq
      901 mqengtannt vvnglrdnmv aagavlntas ntyeanthav spqqywsava gvgnlgitea
      961 nlydatnirl rnvnlsynis pkllaktfvq rakigvscnn vwlitshlng idpesvfatg
     1021 gnavgfenss ppttrtfsfn ltlgf
//
LOCUS       WP_090556685            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090556685
VERSION     WP_090556685.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107932
     Region          40..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miknytlisr ftnqlqwkgi fslilvlvls vsafaqqtgr ivkgtvidea krslpgvtvr
       61 vkgssaavst nqdgeysirv sgpqdvlvfi mlgsvtqeip vgtrtdvspv lkenskllnd
      121 vvvigygssn kkdltgavvs issdefnqgv lvspaqllqg kvaglnvtks gdpnkqpstt
      181 lrgpstfrtg aaqepfyvid gvpgasidll apadietidi lkdasstaiy gsrasngvii
      241 vttkkskagq arlsysgyga venvsktydv lsgpelrkyl adngqaplsa ldddgsdtdw
      301 qkliertgys qnhnvsyggs gqssdygasv nyldnqgilk ntslkrtivr gyinqrffnd
      361 rlklgvtvsn sssnsddiys qttalsnmlf flptvgpfna dgtykenylr tgsgtrnpls
      421 vvdnnlvkik nektlingia qvnildglkf taslstqkdq snnntylnsq sglarnangv
      481 airsevlntt kiaegyfnyd ktfgkhsikl lagysfqedk tndgfglqtq gfsndqlgan
      541 npalsnptgl sqlildqtlv gstlrlisfy graqynfnek yllnaslrrd gssafginsr
      601 wgyfpavsag wriisedfmk svpvvsdlkl ragwgksgns lgfnafssll vygagskfyn
      661 nglisnaigp vrnenlnlkw estatsnigv dfglfknrit gsvdyyikkt sdliydqyav
      721 sttqfptnti tanvgkikns gieitlsava vktptfswtt spnishnknv vealsdaiyk
      781 idyiqtaqlg gkgqsgnysq iiqpgealgt fklwnyagkn aagvstyina agqtiasqpl
      841 ttdmkiagna qpkyiygwnn sfsykkwdln flvrgvlgnk ilnataagln tpadaklqni
      901 prssltesfa dvnaylisdr ylesgsylrl dnatlgytik pksptikair lyfsannvfv
      961 itkysgidpe idmggatpgi dnnnfypktr tlsfgvnasf
//
LOCUS       WP_090557357            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090557357
VERSION     WP_090557357.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114173
     Region          5..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maqartisgv vksradgqpv pgvsvkvagg sggvatnsdg aysivlnaea ktlvfsslgy
       61 ttqtisiagl svvnitledd skqlgevvvt algikretka lgyaaqsvqg gdltkadqgd
      121 vlkslsgria gvqvtsssgt pgaatyiqlr gansltgnnq plfvidgnpi nnsqnssgdp
      181 aagsgnvleg atnsnrgsdv dpndiesitv lkgpaaaaiy gieaangaiv ittkrgkagr
      241 aqvdfntgvs fdvvnrlpkl qnqwvkgeng vlapfsstnr yswgpnakdl swtgvpnefd
      301 shgdlvlnsd paakipfvpy dnlnnffrtg stltnsvals ggneqatyrt sisnnysnsi
      361 vplqhfqrts vsfagdlkis drlkmssnvn yitsdgnmpq qgsntsgiml gltrtpisfd
      421 nsnggksadd psaillsngl vrsyrngvyd npywtinknp ystylsrlla naqvdydlgk
      481 gfsamyragl dtyqdnhhqy yeiqsgyapa gkiyddryty rsinndlils yakqltgklr
      541 fdgkvggnly srkidrlyvq gdgltspdyh niynaitiks anlitpyrke glyydlnlsy
      601 asmlylettg rndwtstlpk gnnsffypsa nvsfvfsele glkgssvlsf gkirasiaqv
      661 gkdpssflts sfyvpttfnd gnttgisfps ngipgysqne rlgnpdlkpe kttayelgtq
      721 lqffknrlgf ditgyyskgk dlivqapvag ssgyqyitln sgsirnkgle vqitgtpikt
      781 ndfewtafln ysmtrskvls ladgvqqitl ngftgtviaq lpgkqagaiy gygytrdgsg
      841 nividdrpva ngggyplvnt neqkqignpn pkflmglgnt ltykglslyt lldwkfkgdi
      901 wngtrgslaa igtsdltnnr ntntvfsgvs ghlnasgdlv hysaagaevq gagsantasv
      961 pldqawyqgn gggfgnlnea fiedgsyikl revslsydfk klfarmnnpf iksmtagvya
     1021 rniiiwtpyh gidpetsltg asnaqgidyf nnpgtssygl nlkfkf
//
LOCUS       WP_090557368            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090557368
VERSION     WP_090557368.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119225
     Region          23..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlllslvm vlciagaafs qnrtitgnvt gsedgiplpg vsvkvvgaag gsvtnsagqy
       61 svsippggta ltfsfigfvs qtirvtssnt invalsndak alsevvvtal giqrnrnqva
      121 yaaqtldgsa vsenrspnlg sslsgkvsgl eirqnntlgg stnvvirgvk smtqnnqalf
      181 vidgvpvann nmntsdqqsg iggydygnpa sdinpddven itvlkgaaas alygsrgsng
      241 vilittkkgk sglnitlntg islgiidkst fpkyqtkygg gygpyygtde snylvnnvdi
      301 ngdgindlva pltedasygq kfdpnlmvyq wdafdptspn fgkatpwvaa kndpttffek
      361 plsnnqsimi snsydkgsfk lgytrdnqng ilpnsniqkn tvnfgstyni sskltagadv
      421 nyskvdgrgr ygtgyngagv ynpatnfrqw wqtnvdvkel kaayfrakdr saanpafvgq
      481 enitwnpady tsgrpifwdn pyfsryenye tdnrdrvign vnlnykvtdw lnlmgrysld
      541 tyhqlqeerq aigsldvply skytqdytes nvdflatfnk klsedfnlsg llgvnvrrqr
      601 tqsnyaitng glglsgiysl snsvnpieap ieidakrevq gvfagatiay kntytldgti
      661 rrdasstlpk nnnsyyypsv sagfvfsell keekdwlsyg klranyaqvg sdapiytian
      721 tfniatpfdg raqasvsttr glieavknnp nlkpeqsrsk eigveasffg srlgldatyy
      781 ntktidqilp vrvstatgyd skylnsgtvv nkgielslng splksrdfew kvnvnwtrnr
      841 nkvtelfkdd sgneatnlsi asfqggvsvn asidqpfgti rgsnfvyndk gekvigangr
      901 ylqsatanet ignmnpkwtg ginnsfrykn vnlsflidir kggsvfsldq yyglatggye
      961 etaglndlgn esrlpisegg giinpgvlad gtpntirvtn seygsygyrr lpaaafvyda
     1021 gyiklrevil gyslpqafvs klgplkgvdl sligrnlwii hknlpnadpe dglsfgnvqg
     1081 yqvgsypsvr tfafnlkvrf
//
LOCUS       WP_090557364            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090557364
VERSION     WP_090557364.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115611
     Region          23..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnklilsmfv flflagnaia qnrtvtgtit sqedklpipg vsvkligapg gtvsgsdgtf
       61 sisvpssvkt iqlsflgyvs qtvnvpvsgr lnvalasdsk glnevvvtal glnrqsktlg
      121 ysstqvssee inraaptnlv sglqgkvagv disntsgspg gsskvilrgf tsisgnnqpl
      181 yvvdgvpvnn srpggtapan sigdlsenyd fgnaandinp ndiesisilk gaaasslygs
      241 rasngvilit tkkgkegklk infssaasft qvsivpdlqe kfgqgwgyqn ylaengswgp
      301 rldgqirpwg svvdgvqqek pftavknnfr dafdtgaeyn ntlsfsggnd kstfnlsygn
      361 vysngilpgd ndtykrntfs lggsttykal tvtgsanyig kntrfvqtgq stsgigssfy
      421 edilqipvdy pvqsfkdyna pynnvndyfs pfsqnpyysi nengskfksd rfygnvdvkv
      481 kandwltfqf qqgadlnnis dklwnaknap iagswagggn degynrqasv gnviegsery
      541 fefdsklnal fskklnddwd ingvvgmnyn drgsralytg venlaipgfy qlsntandpt
      601 ttetetqrri fglyasaaig ykgyayltln arndwsstlp vngrsffypg anlsvilsqa
      661 ldlsstpisf lklraaygqt gsdtdpyriy ntlsrtnval gfgnitfpig gvpgytisnt
      721 lnnqdlkpei stesefggei kflnnrigld vsyynkitnd qilpiassps tgytfrvvnf
      781 gkvrnrglev sltgtpvktk diswdlgytf trnrnvvlel pdglsqvtln taydaqflak
      841 vgqplgvfea pvpsydpqgr iivasngypv vsptngnygs sqrdfimglt nsfrykeftf
      901 tftldyrkgg vfysgtadll nfvgndqktl yndrrtliip nsvvavtgan gavtyventv
      961 pitetstsnl yytsqglata yknrildktf lkvrditlty alpksiaski gsdratltaf
     1021 grnlftwlpk enrtidpevs nlgndlssei gefrsgpstk sfglslnvsf
//
LOCUS       WP_090557675            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090557675
VERSION     WP_090557675.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113005
     Region          69..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktnnnpqga lvkkglpkls laanlafasl lflnldasat vnphriplks iaykttttfl
       61 ndnkladiit gtvkestgep lagvtvyikg tktatqtsad gkftisakpg dilvfsyisf
      121 dnkevtvgte rtitvemtss skglnevvvt algvkrseks ltystqsvsg ssltdvksdn
      181 lmnsvngkva gvtispsasg vggsakvllr gnrsaagnnq plyvidgvpi snssnangqp
      241 nstyggtpdg gdgisnmnpe diesltvlkg asaaalygsq aangvivitt kkgkagktii
      301 nysggysink nayepefqnn ygateagstt swgpkisgad dnlskfyqtg nnltnaislt
      361 ggneiaqsyf sysntnargv epgnklnrdn infhetakfl nnklsvdgnm nyitqkinns
      421 ptigfytnpl tglylfprgq sidqyktnye gvigtngvpt qswpfqedlq qnpwwivnrn
      481 insskrnril lnasakyeft nwlniqargs idrtsdvydq ryyagtlapl aagnnngsys
      541 gsdqvlnqky gdvivnlnlp gttdfkldgl igtsindqft sginwgnglg gyglsipnlf
      601 tiqniqvsgp aqgtntgsnv ntlanfhnqi qavfananls ykdwayltvt arndwssnla
      661 ftetnhyfyp saglsfivsq mtklpevisy akvrgsyaev gntviqyspl ptntgtasgv
      721 tlssvapypg lkpektksve lgtdlrflkd klnfsftyyr tntenqsikv tpgpatgyse
      781 gylnagkirn tgfeftlgyt pietssfswn tsingakntn tiidvasgqg inkvelsntn
      841 syrsyvatgg sfgdiygqtl qkdaqgrvli tdqglpllss dfvkianpap kfqlgwsnsf
      901 tykklslnvl vdgkfggqvv svlqsildsy gvsdvtgaar daggvqingv spngtavnti
      961 daqkwytsig grnaalgqyv ysatvvrlre aslgytittk gplkairlsi tgrnliyfyk
     1021 kapydpevts stsnglggvd vfnqpatrmy ganlnvtf
//
LOCUS       WP_090558203            1202 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090558203
VERSION     WP_090558203.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1202)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1202)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1202)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1202
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1202
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129369
     Region          142..1201
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkcketrkv lfiqlmrvsv lqiislfmls gvlfansvsa esvlnkrlsi nlknvtleta
       61 lhniqnkanv kfvysstiip lttkvsvnas qeklgdilng mltaldvdyt vnasqyivlk
      121 knqlafadsl ianglvlpnv qrivtgkvtg kadgkpfpgv svsikgtktg tvtgsdgnyr
      181 isipnnesvl vftyvsfqtq evlveantvi nvqlsessna lsevvvtaag ikrekttlgy
      241 svstlssdkl aqksepdplr altgkvagvn igssggvagg stninirgss slngnnqplf
      301 vvdgvpfdns sfgnvggqss ggssvtnraf dldpnniqsm tvlkgaaaaa lygsraanga
      361 viittkagkk msrkgteity ntsysvenvs glpeyqtkyg qgtnndyrqg vygswgqpfp
      421 gvqsilptra tipaqltrqf ssavfpqlyq adgvtpiqip yrsyaeenak nffrtgsvye
      481 nalsissgse kgnlnagfsr tnntgvvpgn sinrtsfnis gnmkldnkfy vsgsmnyvtt
      541 gqktppigga tgsimsalmy tptsfdltgn pyenpidgsn vydytgldnp ywstvhsvst
      601 snvdryygnl vlgfdplpwl niqntagfna ytdrrlnvrg kgsssysngs iatddiyrqe
      661 ldntflvtat kkltsdlslr wiagnninqr ltdrkafygd giivpdlnti tntssvtpiq
      721 ltnnrnllkq ryyafftdit fdykdyasln lvgrndisst lpannrsyfy ggangsfift
      781 kafkmddkil sfgkvrggyt rvgnestayq taefylvnsp lgattgvgsi gspftnsngt
      841 ynsstlanll tnsnlkpefi televgtelq ffknrigldv tyynkkstsq ifevtaapss
      901 gfttqilnlg eatnkgveia lnlapfrnpn gfswdistvf trnrnlinnl ggyqqfvfgg
      961 aagtssvhmv gkaygliygt ayardsagdi lidpntgkpl qsgslkaign pnpdyilgit
     1021 nnftyknfsl svlfdlkkgg dlysntvgqm lsrgvtrdte nregvlvspg vlgnpatlqp
     1081 ildangntip nnvgisyedl ffnggigpgg vdegsifdat vfrlrevsla fqfpksmlkg
     1141 tpfgsgmisv tgrnlwyyap nfpkytnfdp evsslgagns qgydnlsvpt tkrfgvnlrf
     1201 tf
//
LOCUS       WP_090558996            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090558996
VERSION     WP_090558996.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114941
     Region          23..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkillfllf fafakaeaqt klitgtvkdt ggaipgvsiv legtgtatqt dkdgkfriqa
       61 apgttlivts igystvrmpv ttgsvyninl vneenklnev vvtalgisrq kkslgyasqe
      121 lsgeslnqvp tsnitnslsg kaagvqvqrn nnfggstniv irgntsltgn nqalfvvdgv
      181 pvsnstfnsa dqqgagggyd fgnlasdinp ddvesmnvlk gaaatalygs raangaiiit
      241 mkkgagkgkp vielssgvti gvidkstwpk fqqeygsgye kiygpnrdqf fnsqdvngdg
      301 vldlvpafna ygsfgaaydp sllvyqwnaf dpalatyhva tpwvapkngp daffetpvtn
      361 tnsismagst dnggnyrfsy tnvnqkgllp nsdikrnnfs msntfkindr ltvngsgnfs
      421 kadvvgrnlt gnesgsgggn ysaivrqwwq nnvdlgqlkd ayfstgrnit nfiggtidnp
      481 ywtryenyes dtrtrfygnl glkykltdwl tadgrvsvdt ysylqedrtn tgttgqvgry
      541 trqdidfmes nydlmlnfnk nitkklnisg vvgtnirrnd lrtvfmetng glivpglfsv
      601 snsvsapaap ievaeklgvd giyglvslgy ndtyfldvtg rsdhastlpe nnstffypsv
      661 aasfifsnll ksdfinfgkl rlnyaevgss apanrltdil qkptpfgsvp lyavnttknn
      721 asllpestqs yeaglemsfl krrlgldvsv yktntkdqii pvevssttgy tskyvnagev
      781 qnkgvevvls gtpvtskdfs wdvkvnwakn kntvvslfeg vdnlqlgsfr gtvtlnatvg
      841 eaygtlkgad fiylngkrvi nqttgeyakt stfnnvigdv npdwkggvsn sfryknlsls
      901 flidmqkggd ifssdmaqgy rsglyentvg lndlgnpvrn sladgggiil ggvapdgspn
      961 avrtrmdtyn nalgivkgpq alyiydatyv klrevaityk vnasflkkir vrglsisavg
     1021 snlwiihknl pyadpesgls agniqgyqlg plpttrdfgl nvklqf
//
LOCUS       WP_090559007            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090559007
VERSION     WP_090559007.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118080
     Region          84..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknflhekcn dacvylyeny skekirtiis skpsrvikft glmvlattlq vaaapankls
       61 sfnitkpfne salalnsftn ppvvitgkvt dakraplpgv svklkgstvg tttdangnys
      121 isapdistli fssigfatqe vdvnrrtsin vtlaedskgl sevvvtafgv krarrglvys
      181 ssevagsslt earennvass ltgkiagvda sqissgpggs srvvirgaga inpnannqpl
      241 yvvnglpins gnsgagtntt glnvdrgdgi ssinpddiet itvlksgaaa alygsqaang
      301 vilittksgk aqkgigveys snivygspsa ypnfqeeygs gidgvkpatq aaalsagrls
      361 fgakvdgsnv iqfdgvsrpy satgvknnin nfynlsrdwt ntvafsggse alnfrlsvsd
      421 lsskaqtpns tynrktvnls tranmgknnl inlestiqyn iedaknrpgv gyaernsswg
      481 tyllgntvdv rnlagpngng tdalgneiqw npvpaasnpy fvaystgnsd ktqrliangs
      541 irinllenlf ikgtvardfa ytdlqdyvpi gtaytplgyl ntgqrqndrt nfnammnynt
      601 tflkdfkvna mvganrerls dlntnlggvn fqvpnfihis nlatinpntd lapyrnrgts
      661 gtnsvfgsad fdykgivyls ftgredtfst lqagnnsify psvgssvims divklpevis
      721 flklrgswak vgsntvtpgq inrtysfgts fngvpvqnnt ntlidfgirp lsiytteggf
      781 evrflknrls fdatyysrvt kddqlaptis ptsgfiagft nvgkvtnrgi eillsgtvvq
      841 skdfswnvsl pfaynqskiv elapglttie vgtgisnqvr vlnavglpyg tvrgwgllkd
      901 angnqvynkt sgyevrvekd lgvanppwti glgndfkykk fslnvlfdak fgavaynnmw
      961 lyasrfgltk etlpgrdtgv qltgvdqtga pfsklwgvad vdnyynnlgn tiseistfst
     1021 dfvklrqvil nytipslkln kigiqsatig ivgrnlaily rdkrtkaagl dpemqqsvgn
     1081 atgtagagep rtrtiglnln vkf
//
LOCUS       WP_090560094            1212 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            hartonius].
ACCESSION   WP_090560094
VERSION     WP_090560094.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter hartonius
  ORGANISM  Pedobacter hartonius
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1212)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1212)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1212)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1212
                     /organism="Pedobacter hartonius"
                     /db_xref="taxon:425514"
     Protein         1..1212
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134901
     Region          137..1211
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfytqypar ycsrlskill vmrliflill sglmqvhakt ygqqfslknq sisikevfka
       61 vkvqtgydil wqpgkldasr kinanfnkss lseviqaclt nsltftiedk sivikpvkee
      121 kglinnsyiv qdslvykgtv ndekgkplpg atvkivggtk ttftnssgdf liyatakssi
      181 risylgylsk eislaglnag qaiktsmipg tnnlgevniv stgyqdlake ratgsfevit
      241 keqlqhssdp nllrrlegit tsmnfnnnlt ptnssvlgqs rkspltnlti rgkntldpnn
      301 iqnssgqvlv vidgiaspys idlvnpndve sitvlkdaaa asiwgsraan gviviktkkg
      361 syeqplrisf ntnvnvtekm nlfykkymst sefidaqifq ydasktslgv pssinlpqrl
      421 aspvaeildl qkqgkidaae tnrqldalrg ndirkdydky llrdavtqsy slgldggskr
      481 mayrisgayd nilnntkyss aerivlnfnt sfrplknlel qanlsyneqr nqdqagensl
      541 tasfgngyyp ytrladdngn plavpfvyrp ayldlltsty gsslldlrfk pledvkegyn
      601 rnisrslnfn lgaiykisni lsvnatyndn rgrndneily kqnsfymrnl intftdpstl
      661 tkqvplggmf lpllsttsnq tlrgqlnank nwgekhslna iagidvnqty sysrgeqylg
      721 yndkaltsvd ridyvnylni mfidpdigig adqipvrasg isdqkirtys lyanaaysyl
      781 gryifsgsvr kdassefgvg tnkggtpfys mgaswniake pfyqlnwlpr lqlrstfgyn
      841 gnvnskisar pvilhqlfla pnglpfavtg sdpsnsqlrp ektsitnfgl dfgirnnris
      901 gsieyynkrt tdliadntid pttgfnrptf niaslhgwgt ditlnsinfq nnvfswtssf
      961 lfssnrvkvs klfsasanta ldvvvggisy segydlsrmf afrwagldpn tgeprgfvng
     1021 qpitisatss gsdawnsila apisstkyfg slvpvyfgsl rnsfnysgfm vsvnllykfg
     1081 yyfrrpssei vqygqlfnsn rlqgaeysrr wqkpgdelst nvpslkypas gikdnfyyys
     1141 dinvlkadhi rlqeinlsyt fknhnwfikn priytnisnl gviwrankyg ldpdindypn
     1201 prtyalglsa nf
//
LOCUS       WP_090566241             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Belnapia
            rosea].
ACCESSION   WP_090566241
VERSION     WP_090566241.1
KEYWORDS    RefSeq.
SOURCE      Belnapia rosea
  ORGANISM  Belnapia rosea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Belnapia.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Belnapia rosea"
                     /db_xref="taxon:938405"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39379
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,295,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,285..286,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavlkerr paetrvaatp etvkkfialg ltvaveagag lsagipdaey aaagaelapd
       61 aasalhgagi vlkvraplgt gegavdelsl iargtlllgq lqatpemaat yaqlgleaga
      121 mellpritra qsmdilssqa nlagyravie aaaafdrgfp mlmtaagtip aanvfimgag
      181 vaglqaiata rrlggrvsat dvrpaakeei kslgasfvgy edeeskaaqt aggyakqlsa
      241 nfyakqaevv athiakqdiv ittalvqgrk aptlvtaemv rsmkpgsiiv diasdaggnv
      301 altkpgevvt tengvtilgh snwpgripaa asalyarnll tflttfwdke akapklpesd
      361 eivkgvlltr ggavihpsla paqaa
//
LOCUS       WP_090571970             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas sp. Nm33].
ACCESSION   WP_090571970
VERSION     WP_090571970.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas sp. Nm33
  ORGANISM  Nitrosomonas sp. Nm33
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas sp. Nm33"
                     /db_xref="taxon:133724"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39450
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeih agetrvaatp etvkkytakg fhtvlvqsga gagasipdaa yqdagavivn
       61 dvsqlysqsq iilkvrgpet eelalmrkda vligllsphr megiealarh gltafamekl
      121 prisraqsmd vlssqanigg ykaviiagnv yqkffpmlmt aagtvkaarv lvlgagvagl
      181 qaiatakrlg avieafdvrp avkeqveslg akfvevpltd eekakaetag gyatemsddy
      241 krrqgelvhe raivadivit talipgrpap vlikeetvka mkpgsvivdm aveaggncpl
      301 telnknvvkh gvhlvgianl pglvatdasa lyarnlmnfl nlmldansge fkinqedeiv
      361 agtlicsgge iikka
//
LOCUS       WP_090576223             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. ov407].
ACCESSION   WP_090576223
VERSION     WP_090576223.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. ov407
  ORGANISM  Arthrobacter sp. ov407
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Arthrobacter sp. ov407"
                     /db_xref="taxon:1761748"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38389
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqvgvgreqr tgerrvaatp etvqqltafg lhilvesgag neagfvdaaf keagatvise
       61 lpfealdvll hvrpltpeaa arlrpgtvti glaspaselp tvralaaagi tsfalellpr
      121 israqsmdal ssqalvtgyr avleaaaryp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandiraas adevasmggt finldvdaaa dgtggyaral gedraqrqrs
      241 llaphvaaad vlittaaipg raapllvtta mvasmragsv vvdlaaesgg nvegviagqd
      301 vqvpvdggsv tlvglqdaas ampsdasrlf arnvsnflal mtdggavapd fdddvvagtc
      361 lthggavrha ptaaaletea
//
LOCUS       WP_090587961             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter subterraneus].
ACCESSION   WP_090587961
VERSION     WP_090587961.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter subterraneus
  ORGANISM  Arthrobacter subterraneus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Arthrobacter subterraneus"
                     /db_xref="taxon:335973"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38531
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,288,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,278..279,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mlvgikretr agerrvaatp asvrqlaklg ldiavesgag vhaghddaay raagalvvpt
       61 ldentiapav lchvapltve eacrlrpgti tvgfaspaae lptvralaea gvtsfaleli
      121 prisraqsmd alssqslvag yravleaair fprffplymt aagtvpparv lvlgagvagl
      181 qaigtakrlg arvsaydvrp askdevtslg gtfihldlda iegsggyare msedraarqr
      241 ellaphiaas dvlittaavp gkpapllvtt amvqgmkgga vvvdlaaetg gnvegtragh
      301 svavpgdggt vtlvgmkdaa samaadasrl faanvanlve lmtvdgrvvp dfaddvvaga
      361 cltsegavlh qptaaalega s
//
LOCUS       WP_090588847             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium brumae].
ACCESSION   WP_090588847
VERSION     WP_090588847.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium brumae (Mycobacterium brumae)
  ORGANISM  Mycolicibacterium brumae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Mycolicibacterium brumae"
                     /db_xref="taxon:85968"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52307
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligiphess pgetrvaatp qtvsqlikig ytvavetgag aassftdeay veagadivar
       61 eqalgaevvl kvnapdaaei aafrdgatvi glispglkpe lveqlatrpi tvlamdavpr
      121 israqsmdvl ssmaniagyr avvesahafg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaagslgai vratdprpev adqvrslgge ylsiedenae vsatgyakem gddykareaa
      241 lyaeqcedvd iiittalipg rpapriitge mvasmkagsv ivdmaaangg nvegtvkdea
      301 ivtdngvtii gytdlagrlp aqasqlygtn lvnllklltp ekdgqlvldf ddvvqrsvtv
      361 vrdgdvtwpp ppvqvsaapa aakaapvepa pakepmttgr rlgiafgaaa viflllaisp
      421 aalqmhltvf alaivigyyv ignvhhalht plmsvtnais giivvgallq vgdanpaiaa
      481 latiaillas inifggfavt rrmlamfsrs
//
LOCUS       WP_090579168             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas sp. Nm58].
ACCESSION   WP_090579168
VERSION     WP_090579168.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas sp. Nm58
  ORGANISM  Nitrosomonas sp. Nm58
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas sp. Nm58"
                     /db_xref="taxon:200126"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39303
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeiy agetrvaatp etvkkytakg fhtvlvqsga gagasipdaa yqeagativn
       61 dvsqlysqsq ivlkvrgpgt delalirkda vligllsphq megievlagh gltafsmekl
      121 prisraqsmd vlssqanigg ykavimaanv yqkffpmlmt aagtvkaarv lvlgagvagl
      181 qaiatakrlg avieafdvrp avkeqveslg akfvevplte eekakaetag gyatemsedy
      241 krrqgelvha raaaadivit talipgrpap vlireetvqa mkpgsvivdm aveaggncpl
      301 selnktvvkh gvhligianl pglvaadasa lyarnlmnfl nlmldsnnge lkinwedeii
      361 agtlvcsgge vikki
//
LOCUS       WP_090596987             496 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pelagibacterium luteolum].
ACCESSION   WP_090596987
VERSION     WP_090596987.1
KEYWORDS    RefSeq.
SOURCE      Pelagibacterium luteolum
  ORGANISM  Pelagibacterium luteolum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Pelagibacterium.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Pelagibacterium luteolum"
                     /db_xref="taxon:440168"
     Protein         1..496
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49555
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavvrerv ggetrvaatp etvtrliglg atvsvekgag easrildqhy kdagasveat
       61 aaaaikgadv ilavrrpdaa tlagaakgal vlaiadpygn epalaalaka gvslfamelm
      121 pritraqvmd vlssqanlag yqsvieasmv ydralpmmmt aagtvraakv fvmgagvagl
      181 qaiatakrlg aavsatdvra aaaeqvaslg akfimtdalk dasgtggyar eltkdeqaaq
      241 aelvaghiak qdivittali pgrpapklit ramvesmapg svlvdlaaer ggnieltvpg
      301 qtvvhkdvti igtlnlqgki satasqlysk nlyafletmi dkdakalkid wedelvkatl
      361 ltrdgavvht nfagaaaaap vtkpaagkkp aapkapaktg avsasaaakp vvaetpapkt
      421 aakpkapakt gatgkpaaak vatagavavp aakpaapkaa akpaakaaap kspatkkpaa
      481 kkpatktpaa ktdgda
//
LOCUS       WP_090598455             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium lentiflavum].
ACCESSION   WP_090598455
VERSION     WP_090598455.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium lentiflavum
  ORGANISM  Mycobacterium lentiflavum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            simiae complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Mycobacterium lentiflavum"
                     /db_xref="taxon:141349"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37771
     Region          9..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdaqlelvk vgvvaesgtd errvalvpka vaslvsggva vvvesgagar allpdelyte
       61 sgatigdaws advvvkvapp tpdevgklrs gqtligflap rnaensigal kaagvqafal
      121 eaiprisraq amdalssqgn vsgykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwlslg dkdvaaageg gyarelteee
      241 raqqqqalek aisgfdvvit talvpgrpap rlvtaaavqa mkpgsvvvdl agetggncel
      301 tepgktvvkh dvtiasplnl patmpehase lysknitall dllitdgkla pdfgdeviad
      361 scvtrageds
//
LOCUS       WP_090601884            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090601884
VERSION     WP_090601884.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117442
     Region          38..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekqrqrvtc crhlpqllvs llvalllipv lsaaqgnqvt gtvtdvsggp lagvsirvqg
       61 klagtstdan glfqliaeag dvlsvsmvgy vlqevevtdt ityqivlqed seslsevvvt
      121 algvkkekvk lgyavqevqg sdlnkarepn lvnsltgkva glnirnttdl fqdpgislrg
      181 rtplividgi pdqtadlwri naddvesmnv lkgptasaly gsigqngaim ittkrgkgka
      241 inlevnsstq fqtgfirvpe vqtiygngnf gqyayvdgsg ggtegagwiw gpkldqpdpt
      301 tpsgywetpq fnspvdpntg elvplpflsr gkdnirnffe tglistnnvs ltqasergsf
      361 rasashiyqk gvvpntdlnn tsfnvagnyq lterllmdar isynkeyten fpvvgygptn
      421 ylynlvlwtg pdidvrdlrn ywregqegiq qrhyniswyn npyfqayeyl qgydkdnvfg
      481 svsfdyrftd qfsvslrngi neyglrrnwk epksyvgyss fsrgnytera tsyfdiasdl
      541 ilkynqsfsd nfaihaelgg ynyyrnirql esntdglnva gfynldnsis pilatnsieq
      601 rrttsaygfv dfelynalyl tvtgrqdkvs tlpvqnnsyf ypsvagslal srflplpewt
      661 nflklrgswa rvtsgiilda sdnedpygfi asydrgtiwn grpavnfgnv qinpnikpqt
      721 sdtweaglew rlladrlsid vayfrsndfn qivrlptpis sgylerleng nryrregwef
      781 mvnatpvrgt ftwdmllnls tyrrtlteiy gdepyldrlq vgdradaiyt smfetspage
      841 vvyqsngmpk sdpfsrligy rdpdlvygft nnfrfkdfsl giqvdgrigg smfsetnqkm
      901 wwggshpgtv npfredandg lsnyvgqgvv vtsgeityds ygnvtsdtrq fapntqevsy
      961 idymtttsny ahtnysyfsq tflklrevsl gwqlprkwln eigfvsnvgv nivgrnlllf
     1021 sklpnvdpds grdnlqtpst rnigfninvq f
//
LOCUS       WP_090602093            1140 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090602093
VERSION     WP_090602093.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1140)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1140)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1140)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1140
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1140
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125515
     Region          33..1139
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkallpgwv lapkilllla glslgadlfa qniqisgrvl datdnspltg vsvvvkgtnt
       61 gtntdasgsf tltaasnatl sfsflgylpq eiavngqnll tirlqadqaq lgevvvtalg
      121 itkekkslgy svtdikgsdl aitnevnpin alqgrvagvq idqgagglfg nskilirgns
      181 tlrnnnqpif vidgvimdnd tfngngrdfg ndlknlnmed fesvsilkgs aaaalygsra
      241 ingvvlitsk kgqkraglgv efsqtvnife pyagpdfqnv fgggtngpff tdyrepnyqa
      301 desyytkvfp tdpttgrpyi dpginrelen wgprmegqev lnydgtltry lpqpnnflda
      361 frngagyntn vavsggsdrs tlrfsynrne skgvvynnnl ekhafslrat helndwisld
      421 gsadytsfkg lnpprlggld afasynygkl ftwmmprnyd tnywmqrehy tsafggapnr
      481 gdleetnrap esrfwfnlfe neylqreqmi rgrlavtasl tdwsklileg nfnniytkte
      541 ekelgqgrgf tgglyalgne vkesyflkgm ltvdrsltpd lalsgyigge iqraensytk
      601 gttdgglsyp gnyflansvn qprseggitf rrafnslyas vdlsyknqfy lqgtwrgdwa
      661 saltysngtg nnffnypsas lswiftetfq lpewlsygkl raniaalgsg adpfvlnpgf
      721 afsgytnsng qtlpistfsd rrvraanlkp erkiakeigl earflnsrvg fdfswyrdnt
      781 hnqiidittp fesgvdaili nagniqnqgi eiavdavpvr tdnfswstal nysrnrnliv
      841 elyegrseyn lganiaeiss waivgksygt lrssiqarkf qatdasgnpi dhpnngkdvl
      901 eyrtdaraaf parsntiqdv gdinpkfrgg wdntfryknf slnvlvdaki ggdfvlatyr
      961 ygthtgvlpn tlagrdpeyg gitwvsawdg kqyddgiipd gvfpqgfqvp vagggqanvg
     1021 gmtyqeaydq glvepthaph yyyrygssst gvsdywvfen swvslrqval nysfpqavcq
     1081 klklnalsla vvgrdllyly nslpynynpa snnsnntafy geegflpmmr swaftlkvgf
//
LOCUS       WP_090602229            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090602229
VERSION     WP_090602229.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117653
     Region          23..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkylsflflv iiasnkvygq qtitlrgvvk satdgsplig atiqivdspt stktdddgnf
       61 tittnqqkgq lriqylgfkv tdvnftsfqt apfqidlepe ermieeveis tgyqrlsser
      121 ttgsfvqidn ellnrslstd ilsrldgvtn gllfdktasy aepqlsirgp stihadaspl
      181 iildnfeyng dirninpndi anvtvlkdav atsiwgarag ngvivitsks gqfnqrpnis
      241 lttnisvtqk pnqftrqqls ssdfidletf lfsrghysya ltgpempsvt pvvwmleqrr
      301 lgnissgdss aavdafrqld vrndiskyfd rnsvaqqhal svngggqynr yyasvgwdkn
      361 lnnkvgsgfd rltmnfnntf sfinnklevs tgliytqsqd ddnthgllvn ypyaqladad
      421 gnslpiaryr psfidtvgqg rlldwnyrpl delgfadqtv katdlkfnai aqyalfpflk
      481 anvryqygrg nsnrrnhrsq etfftrdlin qfssiapngq vsrpvplggi ldlsagnyea
      541 hhlrgqldwd kdlglhsing ivgaelsnmv tqsnsnrfyg ynaeretvgn idpinfypsi
      601 itgwntqipt sqnlqyltdr fvsfyanany tfnnkynlyg sfrrdasnlf gvatnqkwtp
      661 lwsagfswkv sdegfynlnw lpslklrsty gksgnvdrsv sayliasaip ifndynqpnl
      721 rigspanpnl kwetietvna aldfsilrsg ritgsieqyw klgsdlmgda emapssgrvt
      781 frgntasmag hgtdvtinsq nlltklkwtt talysytwnk vtqylltpan vnsymlgaya
      841 egrpinaifg ykwggldgtn gnpngyldge issdytaits stdindlvff gstspthfgs
      901 irntfdwkgv sfsfnvlfkl gyyfrrngld ysqlftgnya ygdfemrwrq pgdelhttvp
      961 amvypaisqr etfyryneiq ilngshirlq dvrlayiinr nnfqsirfks lqlfaiasnl
     1021 gllwnsnnkg idpesrdiaa qytvsgglrl ef
//
LOCUS       WP_090602330            1156 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090602330
VERSION     WP_090602330.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1156)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1156)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1156)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1156
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1156
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126481
     Region          106..1155
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maepqfsgld ekisvrltnt naatlirelg kqstysfiys geqlekkqik avnfqsvals
       61 tvlqqleere gfkfavqakt isvkllhpld ggnavggvqq sgrivghvtd angaalsaas
      121 ihvieldrnt qtdqegnfsi dvppgtytve aryvsfktqr eeriaveagq raalrfvlse
      181 eeselsevvv talgikraek algyasqqis gnsitnsmpt nwssalagkv aglsvvtagg
      241 pisttrvklr gdvslnqrgn naliildgvp lsntitnsgs ayaasgmnsv dygngfgdvn
      301 pediesiqvl kgagatalyg traangvimi ttksgnqaek gigitftsst smdrafnhpd
      361 yqydfgqgmt qstggpgspf enqryydynv mkihvasyga pfvpgaryiq ydpvtqapgt
      421 eptdwvaykd srlgifqtgf ttsntaavns kgdrgslras vtydknswil pntgferlta
      481 tvsaaqkvsn yldvnfrasy tnkdipnspl lgyssssvqy flifqnpsin ldwyrpkwyn
      541 gqehlrqlqp fsqypgnpfv tlyestnask rnslisnlsa tlqitpktsl llrsgiqfsn
      601 dereqrrpis dvvkgngyfs qqpvmemetn sdallthres fsngldmnlm aggnllyyry
      661 naqeafiegl vvpgiyklsn gsstplvnsl iqekglnsly gaanfswkdk vfvditarnd
      721 wsstlpkanr sffypsints llvhemvqlp qtvsflkvrg slsqvgndte pyktgkyyli
      781 sqfpgsatvp ttranpgfkp eistnyeagl dlrlfnnrlg mdfsfyynkt rnqiidapmd
      841 pttgytrati nagvvrnrgy elvvngtpir tdrfvwnstl nwsrnenril elaegleenq
      901 vigsvgsvsi igkvggttgd lwgyktvrne hgdrlidpdg rpttattiey igtaypdwka
      961 glhnefsykg vtlgflvdgq lggivysqsh ykmmelgqln eslngrlpgt eyyiagddpr
     1021 laaaglppvg gvymvapgvv rntdgsyspn tnlvsieayn trefrmanie snsysasflk
     1081 lrevrveynv psrflrklpf nslsvalygr nlaiwsdfpm ydpeaaalng gsilpgietg
     1141 qlptprtfgf nlrvsl
//
LOCUS       WP_090602350            1224 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090602350
VERSION     WP_090602350.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1224)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1224)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1224)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1224
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1224
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=135592
     Region          124..1183
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnfllqwqwy mkitailyfv latttsllqa spshgqvlkk rvtvsyqgtt lhdvikdlqr
       61 qanvdfgftk dlkldevtvk nvrfddkslr evlasllepn dlvfnevaga ivlshkqqpg
      121 rlvgritder geplagasir ivelnrsfst dgegnftisl qpgiysvevn yisyqrqtkq
      181 gvkveesstv tadfvlqesl daldevvvta lgisrqeksl gysvgkvagd qlvrvpqenv
      241 lnalsgkvsg vtinqtgptg ssvsmvirgg tslagdnqpl fvidgipvss tlnnvgqfgs
      301 gnpvdygnai sdlnpedies mtilkgpsaa alygsraasg vvvvttksgk nakglrvdvs
      361 tntvfdipyk fyrkqnlfap gtrpitqddv pegtildlpa svttgmgipl dkgifatqwr
      421 rpeytdepll ptevvghpdn frnfvntglt ttnslslsng nermnyrvgv tnmtnqgiip
      481 gtdlnrnnfs aagqfkggrn ftfstninyt qswadnrpag nrgtnvlqya mqmpnnldir
      541 efenywvtgk egqelvrlyd gwdnpyflay evknafrrdr vygnliaeyq ilpklsamar
      601 mtmdsfferr etkipvgysg epnngayglg nitnyernfd flikwddrvg dfaytlsagg
      661 nemytkgtdi snsstpgrgl ispnvftikn iapenllyss awsqkaiqsl yafanlgwkd
      721 rvyldltarn dwsstlpknn rsyfypsasl sllvdqlidl gprvsliklr ggwaqvgndt
      781 spyqllatyn alepwgtttr yaksgtmlvp nlkpelatsi efgtdlaffq nrlrfegtyf
      841 vvdnenqivq nqpipsssgf sttnlnmglv qskgweftlg gtpiqtagwr wdvnvnmtrt
      901 rtvlkelapg itrlpiwnea sagsaswvnv geqigniysp kevrvtdpts eyygypilns
      961 qgrwtsvsre vanyrsgnfn pdfilgansv vsyknfalnf tldwryggef fsdterrirn
     1021 ngasprayer etidaggrtg kalsdwlkan dhlftddgli ryvggptrem ggyhavdgia
     1081 wdgtfapgvl eqrdadgnli gyiehlgegs etiwgvfrqy dtswnfpqas ilpadfiklr
     1141 evsltynipp saleklkikg lavsvfsrni mlwtkakvni dperafvptt egegrrgiqm
     1201 rqgteefnie pwvmpmgvkl nvtf
//
LOCUS       WP_090602630            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090602630
VERSION     WP_090602630.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116691
     Region          25..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 menrilllvg flltmaftyg qqraitgkvi gsadrqaips atvqvegsnv atqtddngsf
       61 rlevpqhati lissvgyevy rltvgsatyy evelnlestg ldevvvtalg isrerkslgy
      121 aaqtiggedv stvntgnvtn alsgkvagvq irrntnmggs tnivirgygs ltgnnqalfv
      181 vdgvpidnss pntgdnsfdy gnmasdinpd diasinvlkg aaatalygsr aangaviitt
      241 kkgataeras irissgvnfg sidrstfpkf qtkygagigp vygangssyf neqdidgdgt
      301 vdlvvpftat asmgapfdpd llvfqwhamd pespkymqkt pwvpaengpi tffenpltyt
      361 nnasleggsa ngtyrlsysn ylhsdlmpns rlkrhnfsln vshklldklt asgsanyina
      421 qskgrteags gasftnplat frnywqtnid vkemgdmyfr tgrnvrpfyg gttdnlyyvi
      481 yesfqsdern rlfgnmslky eindwlnieg rvatdlysyi qedrrnnmtr vparytnyts
      541 nfietnydlm lnfnkdlstk fnlngvlgtn irrskfqsvf nttnnglive klfaisnsln
      601 tpppteevlr rigvngyfgl lsmgynsmfy ldvtgrvdqs stlpesnnty fypsiatsfi
      661 fselmqsdvl sfgkfrlnya kvgsdaqans lvdvltkpvp fgsvqlytin dtkrnpelrp
      721 estesweagi etsflnnrlg ldvslyktnt rdqimpvavt sttsylskfv nagdvenkgi
      781 evflkgtplk rerlqwdvnv nwalnrnkvi slfegveslq lrsfgagvtl nahvgrpygt
      841 wygtdyiyld gqrvvnqtng eylrttttnn lignmnpswn ggvlnkiryk dfnlsflvdv
      901 qkggdifsnd manglrdgvy ddwtvglndl gnpirnslad gggiilpgvd engnpntvrt
      961 pinttnhalg snrapqkyfi fdasyiklre vslsyrlpgg ifrstpiesi dlsligsnlw
     1021 iihknlpyad peagvgsgna ygyqvgvypt trtigfniqv qf
//
LOCUS       WP_090602635            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090602635
VERSION     WP_090602635.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116701
     Region          25..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqfflflnc lvflvlcana qqkaitgivm saedrlpipg atvkvegtgv atqtdengsf
       61 rleaavgatl iassigfgeh rlqvggdnyy eirlindted ldevvvtalg isrqkkslgy
      121 asqeisgdlv nqvptgnitn nlsgraagvq itrnnnfggs tnviirgsts ltgnnqalwv
      181 vdgvpidntt ynsggqttgg ggydygnlas dinpddvesi nvlkgaaata lygsraanga
      241 iiittkrgsq rtrssievss svtfgaidks twpkfqweyg agyekiygpn rdqffneedv
      301 ngdgvpdlvs plavygsfgg pydsdllvyq wnafdpespy ymqatpwvap andpiaffet
      361 pinntnnvsl sgsagdagty rfsytnanqk glqpnsnirr nnffmngsfk lnerltvtgs
      421 gtfskndavg rnetgnesgs nggnfvavvr qwwqnnvdvl qlkdaylttk rnvtnfiggt
      481 ignpywqrye nfqsdtrnrf ygnmglnfkv tdwlnidgrv svdtysylqe grvnngtlne
      541 vgsyqrrdid atefnydlma nfnknfgekf nvsglagini rrntlrsvqm qtngglivdr
      601 lyaisnslnp pnapneqetk igidgiygmv slgyadtyfl dvtgrsdhas tlpeenstff
      661 ypsitgsfif snliqsdils fgklrlnyae vgssapansl vdvlqkptpy gsvpfysvss
      721 rknnarllpe ltksyeggle laflgrrlsa dislyqtnti nqiipvsist vtgfgskyvn
      781 sgevenkgve vvlsgtpvrk enfswditln waknvnkvls lyegvdnlqi gssrgsvsln
      841 asigepygtl rssdfiylng krvinqtnge yertsasnyv vgnvnpdwra glsnnfryrs
      901 isvsflidmq rggdifssdm aygyrsglye ntiglndlgn pmrnsledgg giildgvapd
      961 gsvntvrtrm dtynnalgvv kapgaffvyd asfvklreva vsytlpsrll rdtfirsisv
     1021 saigsnlwii hknlpysdpe agmsagnyqg yqlgpmpttr dfgfnvklqf
//
LOCUS       WP_090602885            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090602885
VERSION     WP_090602885.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118428
     Region          23..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhilflwcg llaanlshaq grltgtvsdg tgnplagasv rylstgrmaa tgadgsfflp
       61 lplradtlli sfvgylsqrl pvaaaesgpl qialeadpna ldevvvstgy yqipkeratg
      121 sfehvdnalf nrsvstnilq rlegvvpgvq fvepqagdas girvrglsti eadtrplivv
      181 dnfpyegdin tinpndvesi tvlkdaaaas iwgaragngv ivintkqgay nqpawisvns
      241 nvtvgerpdl fysqnylpsa tvmeiqqelf ergtyseanq tyipsyvell ikqrdglisd
      301 gefarqeafm qqtdlrrdvm eylyqppvnq qyslgvrggg dsyhyalsag ydrnrshvtg
      361 ndserlnlsl qntfrvrpnl eltgtvwytq qraanngith gdlglfgtmg nrsfiydalv
      421 daegnpgitf sqyrqayreq aeslglldwm yrpldeqril dntngskelr lnagvrysfl
      481 qsfnldasyq ytngdgwgrq yhtpesyyvr nlvnrftqad gstpiphggi lelgappahq
      541 thsgramlnf drdfgadhrv avllggevrq riletlpaar yyaydpalgt gradldyrts
      601 ypvrpqftar ipptttvgvl apsqltdrfl syfgnasytv knryilsgsa rwdgsnllgv
      661 ktnqrgtalw svggswditk epfyrmkwlp ylrlrttygs agnidksqsh yptiyigtdp
      721 atglpqssld hpgnpslrwe qvntfnagvd wrlsgnring sveyynkhar hllgdnlmdp
      781 ttgvggnykm nyaglrtqgw dvtvesrnlt gefgwstmll lsttnnrits ynaplppsas
      841 yylssqirea gesadivysf pwhglspeng mpiifvdgqp stdpaqyasy ylnfppeeli
      901 ragnsvptaf gsirnvfswk nieigalfsw kagyvfrrss igpgqeylas pfyhtdyfdr
      961 wqnpgdesrt dvpawaetaa pnqrwgvyrd sealitngah irlqdisasy slpktllprm
     1021 pvstlrlyay arnlgilwka ndngidpdyv nadyvapktf alglqief
//
LOCUS       WP_090602944             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090602944
VERSION     WP_090602944.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108468
     Region          24..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqifmllil smathwvfaq qtavvsgivq datgeplagv tvrvvnetan idrqtstdkq
       61 glfqfeqlpe ggpyafivss lgyetqrldg yrvvrgerit lavklqestt eldqivvvgy
      121 gntkrenlvg avqsvneedf nsgvfsspgq llqgkvagln itksgdpnnr gaiilrgpst
      181 lrdgaqepfy vidgvpgasi dlvapddivs vdvlkdasst aiygaraang vimittrkat
      241 mgqtrlsysa yaateqvsna iemlsgsqlr qyleangrtl aasdndgsdt dwqkevsrtg
      301 vsqnhnlsfm gtsaktayga sinyldnegi ikgtslerfn lrtniqhrqf ddrlrlnfsl
      361 vnsitntenv helvysnmlk ylptvavkrp dgtysedwsr trnylnpvsl idnntfdgkv
      421 ktllasgqae vdiltglkyt lnisaqdeqi tnnnyynsls giyqnangra vrntvnntkr
      481 iletylnydr lfgahevkll agyswqedkf gdgfqtsnqg ftsddlgynn pglgdppagv
      541 pvdygnmriq tqriisfygr anytfqnkyl lqasirrdgs safgannrwg yfpavsagwl
      601 lhnegfmqgv savdllklra gygvsgnsqg fdaftatlly gsaqrfyyng sfinaigpfq
      661 nanpdlrwer tgmlnigvdf glfsglvsgs vdwydkrtsd liwtypvstt qyfvnqltan
      721 agevkntgve vqlntaplrn gnftwktsln fshntnelis lsndnfelpl iytaylggkg
      781 qsgnssqivq egypigtfyt wryagkneeg vtliydregn pttaptsddf tfagnaqpkl
      841 iygwnnsfry knfdfnfflr gvsgnkimna tladlnspge atfsnipvft ldeaandnna
      901 yllsdryies gsylrldnat lgytfklkna stlrlytsgn nlfvitdyrg idpeinmggl
      961 tpgidngnyy pktrsfifgl nvif
//
LOCUS       WP_090603048            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090603048
VERSION     WP_090603048.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118974
     Region          24..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkriaiaila mcllpvftva qtaikgivqn engegmpdvm iieknrrnvv ytdtlgnfsm
       61 tvadrdaalv vslmgyhtee idigkqpsgf lnivlktsmy lldevqvstg yqslpkerit
      121 gsfniidnkt fneqistdvl srleavangl dvsrtttlgg sdmgirirgl stlstgglrd
      181 pliivdnfpy egdigninpn dvenitvlkd aaassiwgar agngvivitt kngrlgepla
      241 isfntnttvn sipdlgyypl mdsrsyieae rflfsnryrf adtaalsrpa fspayevmfr
      301 rlngqldewq adllledlaq gnirdeyrky myqtginqqy alsvtggter wshylsagyd
      361 rnrdnldgry qrlnfnfrns yspvdklrld adihytqsrt vsgnrpyapt gqlpytmlad
      421 eagnalpamk dfrqplldti gggklldwny yplledsysr stakvssavi saganyapae
      481 winvdlkyqy qaqdtdgetl ydeqsyvard lvnrfsqisa vtgevayhip kgaimdltrt
      541 rltvhnirgq invdknwrrh nitslvgtel rssatvgnrg rtygydvetl nfgnvdyvnr
      601 fphfitgsns fipnnelhtg lmnrfvsvfa navyaydrry lltlsgrrda snlfgvgtnd
      661 kwnvlwsvga gwnisnepfy rsgilpglkl rmthglsgnv dmsrsavttf nylsqqspyi
      721 qraiasisqh anpalrweqv rmtnmgvdfn srgnrltgsi evylkkgidl fgpapmdvtt
      781 gtastitknv aslkgkgmdv dlnsaniaae hfswrsnlsl syyndevlsy yrasapqgsv
      841 fvggstpsmi riegypifam fsykwggldp etgdpvgfvg gnpskeynli tgagtqlsdi
      901 vyhgssvptv fgslgnsfsw knlslsvrli ykmgyyfkne gisysglfnm spygyheefv
      961 drwqkpgdeq vtdvpsmvyp nngyrttfyl nseikvargd hirlqyinia ydfmksshrw
     1021 lpvkqakayl nmnnlgiiwa anddgvdpay gpyglppsfn calgvqisf
//
LOCUS       WP_090603374            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090603374
VERSION     WP_090603374.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112703
     Region          24..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrllcffm lgilligsay aqdrrisgrv taeedgnpia gvsvlavgan iaaqtddlgt
       61 ftidvpssvt slefrylgyi sqtvslgsnt nitvalatda talsevvvtg ygtqrrseit
      121 gstarvsgaa vadrplqsfs qgltgqaagv nivqpnglln nppvirvrgl ssltlssfpl
      181 vvvdgipist ndvspnsatn npladinpsd iesidilkda asaaiygsra aagvllittk
      241 rgkagearvt ydgwfginna vrlpevlnaq qymdhknaai drayeinpsa slpprnafqp
      301 sydangnlid tdwqdlvyrt aysqnhnvtv sgggdktvyy fsagitdqdg flrensfqrk
      361 sarfnvdhkv tnwlkflgnv sytnsmnksp nsgsdpgsaf nssglgriav aqapnvgpyn
      421 edgsynvqna sigwganqts lqfanpevli kedknssenn rlfanlgaev qlaeglsfrt
      481 sytwdfrlte diqfwnping dgyspngsat nrntrannwn wintlqyqks fngihnlnvs
      541 lstdaqkqrt qnwganrqgl idpffnqfqg tyninnasgn gitqlsymay iaiasynyan
      601 kyfisgnfrr dgnsglargn qwgnfggasv awgisqeefy knsslsetvs nlrfkaswgr
      661 vgngnvgayn eystygsgiy ggaptwafnr agnsnlswet sqqtnigvdi glfndkiive
      721 anwfnkdidn mildvpqaps kgipnneira nvgsmynrgw efsvsaspis kenfrwttnl
      781 nlgliknevt slvtgqqlaf stgglelsnv tvtghsaasl ygvrvvgvnp engrqiflng
      841 dgeqvqylhl ggasawtyld gspavapntt pvvlggtipt wsggfnnsfq yknfdlalnf
      901 tfsggnyiyn gsraglldqr vwnnsvevln awtaigqqtd ipmavwgdnv sngsawlids
      961 niekgdflrl qtatvgyrlp ttlfgnsgin sariyasvnn afiltnytgv dpeissnggd
     1021 nlgsgiernt ipqgraftfg vnigf
//
LOCUS       WP_090604183            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090604183
VERSION     WP_090604183.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118239
     Region          24..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mryiliassi amllvhqlca qmavtgkvvr aedneplpea tllllnkrqt vlsghdgtfs
       61 lqvdgadtll vshvgylarr mavaagtpsl iiqmervpne leevqistgy yqvpieratg
      121 sfvhignrll nraiganvlq rlegiapgvq fvnpggtaaa dirvrglsti esdetplivl
      181 dnfpyegsld nidpnsiesi tvlrdgaaas iwgaragngv ivittkkggt dgrvhislna
      241 ntnitdkpdl lysrawlpsa tvmeiekery glghyatdnr tpiplyvewl rdydegrisa
      301 gelaaqeavl rqtdtrqqam dylyrrsgfq qyalnvsgga erygydvsag yhgasgelsg
      361 ddskrvnlsm rnrfslfsgt elvttlayvg qrsgnngigf gslspssigp spylrladgq
      421 gnalavprdl ryryaesaas nglldwlyrp ldeqrrnant tfsnelring dlntriwrgl
      481 sakvsyqyvr anagsqshhr kdsyyvrnlv nqftqpdgtl viphggilqv gnpagrfshf
      541 grallnferg fgdshrmaal ggieirhsqs etfpasvlyn yndeyltgss qlnfnqrypt
      601 lpegsptrli pggsdihrlf tnrdlsyfgn asytyrqryt vsgsirwdgs nlfgvktnqk
      661 gvplwslggs weasrenfyp lagwlpyarl ratygvagnv nktvthyptv nfgrsfinlp
      721 satilsvgnp slrwervstv naafdwrlkr drvsgsieyy tkrgndligd dymdpttgit
      781 gnykinyadt kthgwdiqis srnlegqlrw nssvlaswvf neitgyrtne avrvtnyfss
      841 vappaigkpr dvvyalpwsg lsadglplvf idgretqdyl syfnqyltpd mlaeagvsvp
      901 sfygslrntl mwkgleveal itwrsgyvfr rpsmepdgdy ymryhvdyfn rwqrpgdena
      961 tnvprkisyg emtagnssga snayrnseal itrgdhirlq darisyllpa alitdwpira
     1021 vrvsayarnl gilwrankqd idpdyansly raprqfafgv qvdf
//
LOCUS       WP_090604956            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090604956
VERSION     WP_090604956.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119314
     Region          25..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkvhgfil lccmllcsva ytqerrisgr vsgpdggpma gvtvvatgts sgvttddygr
       61 ytisipagte sltfrfigyt pkviavgtsn vldaalspdp tqlaevvvtg aygikatsrs
      121 ashnaqvvsq eqmntirqtd innalagkvt giqvrsqspa algretevrl rgmsgfsqgm
      181 gaiyvvdgti lpnindinld didnvsvlqg paaaaqfgsq gangaivitl rkgrqtpgvg
      241 vtvnlgaqfd nvyvlpayqn lyagganasl tqytwqeghp eawraldgky yhdmqddasw
      301 gprmegqeyi pwyawygghs rsyqtaslmp qpnnardffe tgvtlnngit fssstekldf
      361 kttfnnqtvn gllpessmsk nnlnvvttyr lndklalsan inyinrelng liqdsygsts
      421 tgsfnqwfhr dldidilrel rglnhngiyg swnkrnpnay dpsspdewyr anywynpytq
      481 ydfnpiseqn drlfgdvsft ykiidglsvk gtyrkqqnty vreartytel ensayqtgvf
      541 gayatqtsyq nrenleflas ydktfndfsv nanlgtdffn avyrsngant nqgltvpngf
      601 fisnsvqspt ientrwneky navfgtavlg ykdmlfanvt lrndwfstlp sdnndvlsks
      661 fggsfvftel lpgiswlsfg kvryswgeip qalgesrgrf gayrypgmay signnqwngn
      721 ilmptpdqlv dpnihgavnm qqemgidlrf lsnrlgasft ywngkdrdfp fsltvngasg
      781 ftslltnige ikkegveiql taqpvvkpgf rwdvnftysh lirndvvevs eeylvtrsns
      841 vanvafgnlp qayhekgmrs gqligrgilr nddgvpilns ngsyqvdpev fygsvlpdft
      901 ggiqnsfnfl ndfylafnid yqfggvfasl sdgfgaysgl sartavtndk gmnvrdaved
      961 gggikvvgvn annepveyyv dvrthyvnif nngtvdeyih pldfiklrev slgydlpvnk
     1021 wnlrrlgvqn anfsivgrnl wlihskangd ydpseissfa getaqlpgtr gwgfnlrvgf
//
LOCUS       WP_090605016            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090605016
VERSION     WP_090605016.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118162
     Region          41..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqklrlgds yaliryisll aititmcaea rsqrpepsgp vlsgivvdta glpiagatit
       61 tkgtsdktis aangrftfys kvpsgtlmvs ylghrtadek fgegnigpfh ivlipnenml
      121 devevstgyq klsperstgs fvhvdnelln rsfssdllsr legvtngllf nrstsgtpva
      181 lsvrgpstih adgqpliild nfeyngdlrn inpndiasvt vlkdagassi wgakagngvi
      241 vitskngryn aaprvtvgtn vsttakpdlf sqmqvssgdf idlelflfnr gyynntltnn
      301 skpavsplvw llaqrragll ssqdsagmid alrgldvrnd isnyldrtav aqqytaaisg
      361 gsqhhsyhas agwdknltnk vgngydrltl nfnntflllr dkleittgvi ytqakdeend
      421 pfvpisypya qladaggrsl piarynqgfl dtvgqgrlld wtyrpldelr lmdntvkttd
      481 lkfnvatqyr ltsflkaslr yqygrgisnr rdhrsqasff trdlinqfss iasngqvars
      541 vplggildlr sneytahhlr gqldvdkawg ihsvsgiigg elsdvvtqsa anrfygynee
      601 retvgivdpv nsytsmvtgr sniripapqn layltdrfvs yyanasysyd nryilsasfr
      661 rdasnlfgva tnqkwtplws aglawkisde rfygvdwlps vklratygks gnidrnvtaf
      721 ltamafpvne ygqptmtitn ppnpdlkwet itmvntaldf allkshrvtg sveyywkigk
      781 dlmgdaeips ssgrstyrgn taamaghgld ltlntqnlmg klrwrtdamy sytwnkvtey
      841 lvkpvnlnsy mggaflegkp irslfayrwa gldpsngnpr gyigedvsad ysalvnstdl
      901 gellfvgsvv pthfgslrnt fdwksfsfsf nivykfgyff rrnsldyasl fsgsyqgnpd
      961 fvtrwqqpgd eattdvpslv ypantmrdnf yrnseilais gshirlqdvr layhianrqn
     1021 gklpfegiqv famasnlgll wrsntygidp dsqnisqsht isggirlef
//
LOCUS       WP_090605230             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Parapedobacter koreensis].
ACCESSION   WP_090605230
VERSION     WP_090605230.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39832
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklaivketk taesrvaitp dvvkslvkag ftcliessag masgfgdhay eqaggaivad
       61 katllqqada llkvnaptfe elealreesv tisflyaytv pdlvnhclrr risafamdav
      121 prisraqkmd alssqanlag yktvilgana lgkifplmmt aagtitpakv lifgagvagl
      181 qavatakrlg avvevtdvrp etkeqveslg grfiqvedgg vqteggyaka vsdeylqkqk
      241 dlvakhvaea dlviatalvi gkkapilvte emvktmkags vivdmavesg gncalseygs
      301 tvvkhgvtii geanlpallp vnaselyarn istlllhlad kegfkwelde eitkgaliih
      361 rgtlvhaftk ellnkss
//
LOCUS       WP_090605486            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090605486
VERSION     WP_090605486.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119178
     Region          50..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqilrlrds yalinpklkk igiqyislla vmitmcaear aqrpepsgpv lsgivadtag
       61 qpipgatiav knsaakaisg rdggfafrap qqsgtlivsy lghqtieekf gdgntgpyrf
      121 tlvpgenqle evevstgyqt ipkeratgsf vqvdnkllnr svganildrl egvssgvlfd
      181 rraglsdirv rgistifsea qplvvldnfp yegdlstinp ndvesisilr daaaasiwgi
      241 ragngvivit sksaakqkqq kievsanati gekpdllytk qiaaadyiei erflyergyy
      301 rgtlsnpyan vspvvealwl neagtvsdsq lsallaefse ydvrddmrry lyrpsinqqy
      361 nlnvsgdngk sayiwsagfd nrqhsvntss drrftlraah dfhffdrklt lrsntsfakl
      421 lsegnangfm pvtpyqmlad etgnplsvqn sstlrasyvd tagngrlldw ryyplkenrp
      481 regndlnftq qvtalfrpve alqvhlhyly qqgvgetqil ndtssfftrd linrytqiqg
      541 dgtvvypvpl gdirdnqtsr ysahsgrlqv sygkrlglkh rvdalagmev nthdaenash
      601 rlygynpetr vnanalmdfv tqfpqyfnqa stvripasas grsnsdrars yfanasynya
      661 grytlsgsvr rdesnifgvk tnlkgvplws vgtawmvhee sffrigwvdl lklratygyn
      721 gnvnksttaf ltaraaltpy npwglyntrv mnppnpslsw ervgnlnfgi dyglfdnrit
      781 gsleyfvkra asligdspia pqtgvsefrg nsanmettgw dlsitslnir gafswtsnvl
      841 vstardkvtr ylgkqssnrn ivasnymspl egyplnaafs fpfygldasg npkampdged
      901 vlgynamlna ndpgliryhg sfsprmygaf rndlswkrfg lsfnilfkln yfmrntalfd
      961 gsssylsmsa vdyqnrwkqp gdenhtnvps lvypsngsra vfytnsdihi yradhirlqd
     1021 irahyelksf tvfcmvnnvg ilwranplgi dpdvgnatyp airsvafgln vrl
//
LOCUS       WP_090605781            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090605781
VERSION     WP_090605781.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120069
     Region          25..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkviksltil tfiliqlaay pqaqrtvtgt vysndtkqai qgasivskst grsivsgqsg
       61 sfifrnltds dtlaisfigh askeipvasi vqspidvyle evvkqidevv vntgyqslpr
      121 eratgsftqi gndlfnrsvs tdlvsrlegv tnglafelpa trgapsstpn lrirglstir
      181 geteplivvd nfpyegdinn inpndvesit vlkdaaaasi wgaragngvi vittksgais
      241 rrptinfntn vsitqrpdly ysrdylspae tvelehtlye rglytrndwt aytpaveilh
      301 alaeeridea tanaqlevlk rydirdeavr hlyrqglnqq yamninggae whqyylsagf
      361 dnnasnlign gyeritlmak ndfqpipkln istslnyvqg rstsngiglm dltpigfnnp
      421 yvyarladen gnalpivrnn rfsytdaale mglldwhyrp ldelrlndnt sntneirvnt
      481 svgyqlyrgl raevryqyqn igeqarqhyp qesyyarhai nrftdengtr rvplggildr
      541 sggdfsshyg rfqldyngdw adrhelngva glelrqersi srgtsrlygy ndevlsyatn
      601 lnfdtsfptr prlsaripyd nspgrhitdr fvsyyanfay tfdgkyilsg strwdasnif
      661 gvdfnqkgvp lwsiggawna sdepffnvdw vnlaklrlty gsngnavrsl sslpfitygg
      721 tnaytglpyg ilrsvgnpdl sweqvntlni gldfslfdrr isgsvdwynk nssnligsdv
      781 fdpttgispl sgtlynldnq rnyadlntkg idievntvnv drglkwqtta lfskvrntvm
      841 nynnlrtpmg vdlltvvaap livgnaidql yslpwhgldg tgaplvmvng elgtdyntyf
      901 ndltqegvir agvtmppyfg airntftwrs lsasvnivwk aghrfrrgsi syanlfgtsk
      961 vmhmdyldrw qqpgdelttd vpsmpestna rrdqaylwse atlergdhir lqdvnlsyql
     1021 pdsysrhigl sqvriyafas nlgllwkhtd ydvdpgvsal yprpiqvsfg lqiql
//
LOCUS       WP_090606078            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090606078
VERSION     WP_090606078.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114547
     Region          21..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlflilfvv lfittafaqq rkitgtvlsr stgealsgvt ikgtsqttat dangkfsina
       61 asgetlvlsy vgmndlrvtv tdettelnla meentatldq vvivgyttqr kkdltgsiav
      121 vnlssdvtst tsgntaqalq grvaglyiek dgspngatsr ilirgsntlg nnnplyvidg
      181 vpttrpevfq nlnpasiesv qilkdasass iygsrasngv iivttknggn tegkvqfqln
      241 snvaaqsers irfnvlnaid rgralwqasi ndrqdpaaay geiynfdwng nyeqpvlngv
      301 slqpfvggds ntpsgdtdwq dvmyktgmvt nnnltasvgn knsslelgfg yikntgmmry
      361 tgydrisgni navtrafndk ltlgvninia nsnelltand lggsastfna vtlaptipvf
      421 qkdgstyage lgagysdrnn plhmqylarw nntnrlntfg nvfievqpvk nlffrssiga
      481 ddsrflrkvi eptftegals rttnslthdq nhflsltlsn tlrynlalgd hsrfnfllgt
      541 eyiktdlnyq ltrkqgfsiq tedyftlnaa tgntsvsgnl tgnrlfsqfa rvdynlldry
      601 liavtirrdg ssrfgsnnqy gvfpaasigw kidqedfmrd srlfselklr lgvgrvgnqe
      661 igdiaryaly earyglsqne ltpgfwepym nigtayslng antgmlpsgf vqtqggnpnl
      721 kwestgelna gldfallenk ifgsfdyfsr kttgilitpp vasalgegqs kpvngatktn
      781 kgwefvvgyr geksgdfsyd vqmnfahfrd eitelpesvr paypgnllht iighsqfdif
      841 gyktdglfqs qqevdeaptq igaapgriry vdlngddrid dldrtwigtt lpkleygvri
      901 gaayrsfdis ifasgvagrs gydvysnfnn lmksrenvgp gvfngwtptn tdtnvpaltl
      961 vdannetrts dyfmvntayf kmrniqlgyn ltpksifsnv rffvmgenlf wiksneyqgp
     1021 dperidlgpv pipktytfgv nlsf
//
LOCUS       WP_090606185            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090606185
VERSION     WP_090606185.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118675
     Region          23..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktilkliii tillpaitea qpvlqgvvkd adgnpltgas irnsanddie htnefgtfql
       61 niatipisif vshvgfhrad idinsydtlh itlfpltnvl qeveistgyq sipkeravgs
      121 fdfidsetln eqvstdvlsr leavanglni erratsgtdm girirglstl sagairdpli
      181 ildgfpyegd inninpndvk ditllkdaaa asiwgsragn gvivittkmg anrqptsfnf
      241 nanttvgkip dltkyplmtg adfieaekfl fenrhrfsdt aarsrpvftp vyellflqrn
      301 niiaaqevdr qlsniaegnl lkqyqqymyd aslnqqyaan iqggsdnnaw yvsagydrnk
      361 salaatydrw nlsfkntytp hralrfdvsm lytlsesvsg ktayspsmgl ppytrimdes
      421 gnplavmrty rqsfldtlgd grlldwnyyp lvedhysktt aslnnavvnt gasytplpwi
      481 alhikyqyqq qktenntlye eqsyiardlv nqftvldasg githnvpkgg vldvgysslr
      541 ihnlrgqlnt dnqwgshnlv sllgaefrsg ttsgknsraf gydptnltyg tidlknrfph
      601 litnsnifip snqdftglvn rfvsgfvnva ytyddryllt lsgrrdasnl fgvnvndkwn
      661 llwsvglgwn ihnesfftsv fldklkvrat hgysgnvdis ksavttlmyn saqspytntp
      721 malitqhanp eltwervnms nvavdfalkd srlhgsveff lkkgldlfgp apmdpttglt
      781 gsitrnvasl kgkgfdvelt tdytfprnik wsgtlnlsyy ndkvlsyyrd sdatgsvfvt
      841 ggspsmirve gkpifsmfsy kwggldpatg dpigylggfp smdynaitgl gttiddivyh
      901 gsaiptyfgs frnaisyrnf sisfsvlykl gyyfrnegid yasvmranpt gyhqefnerw
      961 qnpgdqrftn vpsmvypnhs drddfylnse vkvkkadhir lqyvnfsynf ntdkgflksl
     1021 rnakaylnlt nvgmlwkand vgvdpeygay glppvmtgsl gvqltf
//
LOCUS       WP_090606933            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090606933
VERSION     WP_090606933.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118053
     Region          22..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyvyilala lwacpsfaql ggrvssqsgq plagatlrll nsvhmaqsgn dgrfslpmpa
       61 tsdtllvrfv gyaeqrlpvg psttgplaiv llpddntlee veintgfyrv ppervtgsft
      121 hidgktlnra vggsilqrle giasgvqfte angtsasdir irglatiqsd gtplivvdnf
      181 pyegdintin pndvesitvl kdaaaasiwg aragngvivi ttkrggygqq arislnsnvs
      241 vgekpnlfys qnrlpsnvvl qlekdkyehg gyylesaqqr pfpqyvelli ardsgwisea
      301 dfllkessfr ntevrdealk ylyqpsvyqq yalgvqgggq tnvyylsagy dknrshvigd
      361 gnnrlnlslq ntfrplkgme ltagvwytqq raennglalg dlaaretqlg lspytrlkdn
      421 agnnlpivkd yrlayvirad idglldwqyr pldevaladn rsgsnemrln gglrysflqh
      481 fdvnvsyqyv rarsegssly hedsyyvrdm vnrftqgngs yiiphaaifs mgnpaeavsh
      541 sgraqlnfvr sigdhaisal gggeireyvq hifpgytmyd ydpslltgta yydyvenytv
      601 rptgraripq psstrrrftd rylsyfgnas ytyrdryvls gsarwdgsnl fgvktnqkgt
      661 plwslgaswe agkepfyrid wlpylrmrat ygssgnvnkq vsvfptirhf gsdansglnw
      721 anvisagnps lrweqvntln lavdfatkgr risgtidyya kdakdliged ylppstgiit
      781 ggtasatnli nyanlrtqgl dvqlashnir gafqwtstll lnyvrnrvtg yhtaetsqvy
      841 hytnspsvpv pgrsrdavya fpwnglehdt gmpliyvdgv ksddygtyys vgnlmaagvs
      901 vppfygslrn dvswkglsvs vllawktgyv frrkssvpga ayisslnyhm dylkrwqqpg
      961 deqwtsvpvh happvdsyma svyelsetli tnadhirlqd invgftlpqk ymdrlplrhi
     1021 rlyayarnlg ilwrankngi dpdypnadfa aprtfaigvq mdf
//
LOCUS       WP_090607502            1158 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090607502
VERSION     WP_090607502.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1158
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124867
     Region          28..1155
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnlyinccm vimallgsvl lvyaqpsitg ivrdvdgpia gvsvqiqgts rgtqtdaegr
       61 ytisasaget lqfsalgyvt qniavgstpt invtlelssg eigevvvtaf gikrekralg
      121 yatqtvsggn ltvtqpssva qglagkvagl nisqasggve ggssrlvirg ntsltgdnra
      181 liivdgvain ndpvnnnann ggggavgtql gadvsgyndw gtglnfinpe dieditvlkg
      241 paaaalygar gangvilitr kkgtsrkglg vdysysfrgv nayefldfqn eygsggvaam
      301 wtadndkmfp tnaagqrvqi sldngynfpa gdytssaygk fpydnttdyy nllsfpsgls
      361 wgprfddqpi lwydgvlrpy saqpdnwkaf fpngsvgqhn vaisgggdfg tarfsytrsd
      421 nkanvlnsnf ntntfnlgtt ikvssrvtae itgsytsyer lntppvgagh flagfsyavp
      481 rdyrsdveel nnfapdgsrl dvtnssnfpa gsprypyysy mansfwrqyk nnttfardql
      541 iggakiiadv tdwltltaqg gldnssdnte iknyptnlag tqdgyygqam aksfnrnlna
      601 yarlhkdnlf dqaisgslta gteayhrndy tvsnktngnf vkpfifalnn gvnpptaaee
      661 trygkkinsi ygfldlsynd nlflqvtgrn dwsstladay nsyfypsanl syvfsdgikg
      721 mqtaapwlnf gkltlsyaet gsdtdpytiy diitteayng qaaqtypntl kfpgiepqrs
      781 rayelglslg flknrlnvel taytmkssnq iltnalpiss gfsniqinrg elgnkgfefi
      841 inaraiqtpd fswnisvnga tsttkvlald egiddltlgs ffggsgvsqr vkvgekygti
      901 ygrdfvyang qkevvdvvnp dnglpltytv ngqtyiagtr wkttdtevpi gnalplltgg
      961 isntfsykgl slyamidaki ggdtyfgtya aamgngllqe tvkerngggl plvypdgtta
     1021 ntgvvfdgvy atygsdgeli sttpntnvvn yqwyylntft swnhlghipr sasvfentwv
     1081 klrevaltyq lpvnfvqktg flqnlsvsli grdlfyiyts ipkglnpegv ngignmqgie
     1141 yssvprarsf gfsiktsl
//
LOCUS       WP_090607688            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090607688
VERSION     WP_090607688.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119092
     Region          31..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkistylalp illifgcvpl sfsqqihrih ghvfsssrnt pidgavitdg esggeavtde
       61 dgffelfvrn dstvlfcram gfspwqhkmd lpipdgiriy lqdttqllee vvvttgyesl
      121 pleratgsft kidnerlnra tgmdvlgrle gvtnslmfdr rstqpvmmvr grstiyagqa
      181 plvvldnfpy ygdinninpn dvesvsilkd aaaasiwgvk agngvivitt kqgaagqrpv
      241 fgfsanatii aepdvfyspv issadfieve rflfgqgfyn nqenngnrpp lspvvellir
      301 qrdglatqqq tdaaidllak qdvrqdfrky lyepgvnqqy alnyrggsdl fsyyasagyd
      361 rntgftgdrt drvtlrmdqv fsptrylkir aglvytgnkn vagrpshlsi tpggtknlyp
      421 yarladengn alpivkdyrf pfagqaeesg lldwmyrpls dyrhtdvsqt grhlladfgv
      481 dqiflknftf qlkyryetgn dvdatlsgle syytrnmvnr ftqadseggl tyavpmggif
      541 ntvsgvlnah sgraqlgyqk legnhqvtal ggfeirqirn qsstsqaygy dedvltsvav
      601 dyvtnfpqyh npntraripv gsgstlfser ldrfisayan aaytyadkyt asgsirkdas
      661 nlfgvnsnqk gvplwsagis wnlhkepfyr sdripylklr atygfsgnvd nglsaystvt
      721 yfngnlnngr yaalrsypnp dlrweksrii nlgvdfalkn smvsgsleyy vkrgtdligd
      781 apidptvgiy sglirrniae msgegidiel ngkwidryir wetglifnyn tnrltkyytd
      841 atsgsrylgs gigivpiegk plynlmsyrw rgldgasgdp lgvvdgvvst dysaitrntp
      901 leglvyhgps lspvfgnlln tfswkqlsas vnigyrfghy frrpsisyga lfnnweghad
      961 fadrwqrpgd eqhtdvpsmv yplnnnrdqf yryaetlvdr assirlqdvr isydisdvrq
     1021 rhfssirlfl yaknlgtlwk atdaaidpdy glgipmgksf slglnmef
//
LOCUS       WP_090608486            1168 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090608486
VERSION     WP_090608486.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1168)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1168)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1168)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1168
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1168
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128103
     Region          68..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          130..1163
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnyfkkakai vlalplpflf limklsiafl liaviqvpak sysqdinlnv rdmsletvfa
       61 lieeqsgyvf fyddqlvkdr kitlkveras idnllsnhfk nlpleftvvg dknivvkqki
      121 kttsipiqdr qvrgqvtsaa dgsplvgvsv svrgttqgtq tdnegryiit aangailvfr
      181 svgfaektav vsastvnvsl eeiqsaldev ivvaygtttk atnvgsiaqv ssenfenrpl
      241 tnvtdalvgs apgvqgtigg gapgaeanir vrgfgsisas naplyvvdgi pydagssgns
      301 givnlnpddi esisilkdaa ttalygsrga ngvimittks gksgesnftv saragfisrg
      361 lpeydrvday eyypliweay rnslvhgana vpidvansia sgqttsynga tysdivsqvr
      421 ynpfnvsdee lmgidgrlnp sarllfpedl dwakaiqrgg ksrqsydlsy dggagktnyf
      481 aslgytddrg yllksdmkrv narvnintqa tnwlrtginl tgsyqasnyd aaggggyinp
      541 fgasrimapi ypvyehdlvt geyllnedgs rqysfgdyrp ygggrhaiwe nemdvrkeqr
      601 tvvgarsfle aqilpqlkaa tnfgvdiqdr hnrtyqnpii gdgapggras hnfyritsyt
      661 wnqtleytqs fgqhnvgmlv ghenyaykyn nlsggrqdmv vdgilelpnf atitsvnsre
      721 dnstiesyfa rasydfdeky vlnasarrdg nskfhpnvrw atfwsvggay niskedfftt
      781 pwvdnlkira sygtvgndgg ldyypyqaly gfrnntttpg faqeslqnds ltwetgknfd
      841 lgidfslfkn rlsgsieyfd rvtdglifgv pvplmnggvv ssspyfhein mnigslynrg
      901 iegsltaniv rsenfsystt lnvttfknei tvmpdgqpli qsgnhaysvg hsiydfylre
      961 fygvdpdngd alyrtnrets ntriinndtv ttvlgeanfr ytgdssipdv ngsmlhnlry
     1021 knfslsitlt yqlggkvyds pyatlmssgt ygytlhrdll tqrwqnpgdi tdvprldvaa
     1081 tanlsgqstr fltdasflsv nnvtlgykip qswistagik dcylyatgen lallsarkgm
     1141 nvlnsfngsi gndynfsrvi sfgarikf
//
LOCUS       WP_090608973            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            koreensis].
ACCESSION   WP_090608973
VERSION     WP_090608973.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter koreensis
  ORGANISM  Parapedobacter koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Parapedobacter koreensis"
                     /db_xref="taxon:332977"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113787
     Region          78..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqklrlgds yalihklsay wrnqqsetfr khkrklvkkl cvqthaqafa lpgrgraigv
       61 lallllglct fgiaqqrqti sgkvvsaanr saiegatisn kqtrihaltd rsgeysilag
      121 pddiliisfl gyrtveekvg drmvvevlle tventldetv viaygttsrr lntgsvgrvt
      181 aetiakqpvg npllalagri pgleinqtng lpgsavnvri rgrnsiqqgn eplyiidgvp
      241 wlstsltqfq trgaagdisp fnsinpadie sievlkdada taiygsrgan gvilittkrg
      301 tagktsvdvn mytgfgkvtr tmelmntqqy lemrreafrn dgveptpana pdlllwdttr
      361 yvdwkklmig ntarvndvqv alsggsegtq frlagsyrre ttvfpaddqa dkrgsaqlnv
      421 thrsaddrlq anvsvgyshn andlmmndrt aaiytppnql aftesgelaw eengsaltsp
      481 laqlyrtsss ttsnllgnmn lsyrlvkdls ikvqggftqt amdaekiqpk stfaptyags
      541 gladfsasrs tswilepqla yeaslakasq lsvlfgttwq atdadaslvq asnysneall
      601 gsingaatlv nsasynayry qsffgrinyn hagryllnlt arrdgssrfg sgrqyasfga
      661 igaawifsee swlngnggiw sfgklrasyg itgndnigny qyldtygttn pyqgiaglyp
      721 nrlfnadyaw etnrklegal dlgfmsdril fstawfrnrs gnqllqdalp tqvgfanitr
      781 nlpalvqnig wefelntvpi qrpgftwssd inftlsrnkl leypgletsn nasryamgkp
      841 ldnvrlwsyt gidpetgiyt vdtelgqtlf ydmtpsfygg wnntltykgf easvffqfvk
      901 qeqrnaiasl irppgfqynv pviasnrwqq tgdeasvdmq rytrggdalt aftrfgnstg
      961 vytdasflrl knlsiayrvp rsllgkygle nlrfysqiqn lftftayrgn dpetgnsnvl
     1021 pplrmismgl qitl
//
LOCUS       WP_090612408            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AR20].
ACCESSION   WP_090612408
VERSION     WP_090612408.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AR20
  ORGANISM  Bacteroides sp. AR20
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Bacteroides sp. AR20"
                     /db_xref="taxon:93974"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116982
     Region          41..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnilnkrns rycftcfvmw lllglghlna vaqeaggtan itgkvidqyg npvsgvvitm
       61 kntdfktvtg ddgtfefqyk kgdmlrfshp gflhkeikvn klrnqerifk vtlteefvkf
      121 pdvingpydt kdkasylgsa atvytdqvss lmgttilpsl qgrlpgldiv rtrgarksqi
      181 essssgtifn fnsptlgkea ysdntefnvl srhnapvvvv dgvqrelysi dpdaiesvsi
      241 qkdalssmfl gmrssrgalv ittkdpikqg fqlsftgrfg vqssvkklnp lstsqyayll
      301 neallndgkn pfysyddfik frdhsspyth psvnwcdelm nknsttqsyn lnatggnkya
      361 qylisvgyvg englfknpgg dahdtnttfd rymisskvni nitddltakv tlmgrieegt
      421 qpggtgngyd dilssiystp snaypvtnpd gswggsqsfn nnllsqtins gyitdgardv
      481 lgainlrydf gklvkglsvr mvgsvtsqnr sttkrtktse vfdytidkdg ndvytrygek
      541 ktqsnsfssv styrqmygql avdyerqfgk hkfkasvlgd trntltnwdl peypsniigd
      601 vsydyaeryf aqvalsesyy nryapgrrwg tfyafglgwd iskenfmenc ewlnqlkirg
      661 vygktgngmn nagyytyyqt yssggddyrl gtnlgqssgs ftekdklanl yqtwekgnkl
      721 nigvdialfn nklqvtadyf ndkyydllqa rgksieligq nypdeniake rwyggefsit
      781 yqdhvgdfny yasanwsceq skvlykdeqk vpyeylrttg kpkgaifglv aegfftsqde
      841 itkspviegf nniqpgdiky kdqnndgvin dfdkvmiggd kplsyfgidl gfewrglefs
      901 mfwqgvynkd vlmsdwnlle gfqtqgqvyg qayenmldrw tpetaatatf prlsaggnky
      961 nqgngwgssf wlrsgnyirl knvslgynlp dsfcrnylgg arvkvfvsgq nlftkaanel
     1021 vdpevsfgny plqrcistgi nvkf
//
LOCUS       WP_090611977             977 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_090611977
VERSION     WP_090611977.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109464
     Region          74..976
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mviilpnffl qkpvcrllav mgflgfsgai asqssspani dsvktymkkd sfeknvgsrf
       61 vtnrsidsfg vsdtvdirml qrsqflsiqq llkgnvpgvy vqenngepgt iqsmlvrgls
      121 spvfsnkdvs gvqptvylng vplmlensyv ydikqfdinp igaaanmlag ldissiesie
      181 iikdplqlak lgplaangai wittkdgyyg genvsigvsa gmafapssvr mtngsyekaf
      241 rqrfydtysl tpgkqpdylm dtrdvryfgk pdwaddyyqs sllynvnasi gggskkanyv
      301 ftlattkdag aadntsytky nigfalnmvp ldglnvstii naakidrvrn rnfrdrfaem
      361 eymvdfstpl apagnlyndf lisndltkdd nynnllngll alsytkqrfn atasikldyt
      421 tnvrrafwpm allesvnfvs nysgynqrii getsasyllp ladihklniq wngsitsdly
      481 hynytraydg dddmkpttst gnfkqyryvd rlenrwvsts ialdykyknl lnvgllaryd
      541 gnsaiqsdhr wmftpaasae wnlknqfftg stalsglslr asyariaksf qsdryelgpq
      601 ylatsitwsg epllssangf atitrpyasg wvgydlklpy sdkmelalkg sffdnriiae
      661 islyknyekn lltylpvtqe mgyeyklasg mdisnqglel nlsasilknt plkwdlsfna
      721 synknklekl penqkttvig dhklqvgqsv dafwvyqnkg iytndsevpv mngkplnvng
      781 vpfkagdpvw tdvdgnnqin dndrvltgha ippytggltn qfaykrfdfs fnlffalghs
      841 alnlrdqqry dfatldniqs lqsvkeiffw qntnqrddyp iynpqssvhp yraeqdlfle
      901 klsylklrni tvgytlpikk vgsnipksly fyltgsnlls fsnfsagdpe lvnfngtydg
      961 yslpiprsvs lglrfkf
//
LOCUS       WP_090612731             926 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AR20].
ACCESSION   WP_090612731
VERSION     WP_090612731.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AR20
  ORGANISM  Bacteroides sp. AR20
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 926)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 926)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 926)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..926
                     /organism="Bacteroides sp. AR20"
                     /db_xref="taxon:93974"
     Protein         1..926
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101881
     Region          38..925
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkinyilit lllggsvsln aqtskaasem qladtlsigy qmnvssrtss ysingvnasa
       61 fekspyidis kalygkvagl nvyqgtgssa dnvstlsihg naplvlidgf prdisditsm
      121 eiescyvlkd aaaaalygmr gangvvlitt krgisnglkv nvdynfgvnt qfrspdfada
      181 ytyanalnta lsgdglpary naqeldafrt giypydypnv dwwnetlnnt glthnlkmsf
      241 sggsdkfrfy tvvdyyrdrs mlkkntedtr fdttptdtrl tvrtnldvkv testllkagi
      301 vgrlkefrgt rygrsaifnk iygipsaafp iryengiygg ssvygtgnpv allkdyghir
      361 nvygtlladl sirqdlsalt kglaaeasvs fdniggmnet tnkeyrymns nasitsdgtl
      421 vttpaiygtd setlghtqpf erlmlrsdfq akvdynrtfg khqvggaliy dmqsvvkngr
      481 nnsqknqsvl vnatytydnr yslnavfnrs gsaylpdgdk ysnypavsaa wivsdeafme
      541 kvtpinlfki rasyglsgwd gnlshelwrq sygsggagyn fgvnaggqsg gsegdlpvig
      601 lvaeksqkat fgfdlaafdn rlnatvegfy ekrsdilvsg anstsgiigi tvgqvnegiy
      661 kykgvdasls wndkigdfhy gigasmsyln tevvnvnqay qeydylytkg nrigqmygle
      721 aigffnsqqe innspqqtfs dvapgdvkyk dqngdnride kdvvkmfgss vprfyfgfnl
      781 nfsykrlels adfqgmtgvt vsllnsplys plvsngnisn tflneeiswt penktnatmp
      841 rlttqenlnn yrasslwyrd gsflklrnll vaytfpksqt rfadlkvfvq gtnlfsldni
      901 hfadpeqlgi aypstrsywa giklnf
//
LOCUS       WP_090613738            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_090613738
VERSION     WP_090613738.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121069
     Region          62..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqtnkvfyt lvaiflscsi emagqvqkvi sgtvtelfgk taeplvgvnv nlvnnqnrsl
       61 gggitnlngq ynvkvpdgek dltivysyig mktkrikytg qtllnvtles esmavdevvv
      121 sarrlnrndl gisdkemvsa tqkvdmekli aaapvvsiee alqgqlggvd ivlggdpgsr
      181 sairirgtst lnassdpliv idgvpyptdi sddfnfstat eedlgallni spndiasvev
      241 lkdasataiw gtqgangvlv iktkqgtvgk trfsfsskwt mkedpstipm lngkeytslm
      301 qesiwnsaky iglnnpgnky lnmlsdapai gdnpdwryyd eynqntnwld yvrqkalvsd
      361 nsfsmnggge katyrfslgy msdigttigt smnrlntsmv inyqfsnklk fgadfsysqt
      421 ntdanwvnti rsealskmpn kspftvndlt gtltdeyfty hdpnfegsfn gksnynpvam
      481 aheainrtvq regkitfrad yeilpgffyk gwasinmrai ktrrflpqvv tgveqvnqya
      541 nqsadaysdq lalqtenklm yiknwnnkhn iianvlvrtg qyinsgynse vygnassdls
      601 dpvvgttisd mnssesetrn vsfvgvlnyt lldryvvhgs lnaegnsamg rnermgyfpa
      661 vglawnfqne sfmekardkw ldeakfrfsi gqsgrapsga svylgayvkg tdymnmsatk
      721 qarmqldnlr wetsteynyg ldasvlkgrl rftfdyyykt vkdllqknyk lpsttsfgsi
      781 syfnsgkmen kgwefrtdvv lfenkdwrin gyvnfsrnen kitelpanmv qenyspknga
      841 yaaraevgrp igsfygyryk gvyqnteaty ardaegnvmn dakgrpivmk nltatcqpgd
      901 amyedinhdg vinqydivyl gnanpiltgg agltikykqf svntffhgrf gqsvvntarm
      961 nnesmngnan qstavlrrwk negdvtdipr alygegfnyl gsdrfvedts flrlkqltln
     1021 yafpksicnk mgitsltcfv tgynlftwss ytgqdpevnl psrptdlatd sattpvsrry
     1081 tfgfnlsf
//
LOCUS       WP_090613744            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AR20].
ACCESSION   WP_090613744
VERSION     WP_090613744.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AR20
  ORGANISM  Bacteroides sp. AR20
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Bacteroides sp. AR20"
                     /db_xref="taxon:93974"
     Protein         1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121499
     Region          30..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkltklyfsv villcivgev vaqtqqiiig nvtelfgksa epligvnini mnsqerslgg
       61 tvtnmngqyk laipekekdl tlvfsyigmk tkrikytgqk slnvtmests eaigqveiva
      121 erkdrndlgv glkeqtsatq kinmedlvat spvtsveevl qgqlggvdit lsgdpgakst
      181 ifirgastln assdplivid gvpysdsnts dfdfatanee dlgallnisp ndiesvevlk
      241 dasatavwgt kgangvliit tkkgsvgktr fsfsskwtak vepktipmln gdeyvalmqd
      301 aiwnsanyvg vsqasnylrl lfntpeigdn pdwqyydeyh qntdwldlvr qnalssdnsf
      361 smsgggnrat yrlslgyatd dgttigtsmn rfnstlridy nfskklrfga nvtytqtdkd
      421 anwattvrse afkkmpnksp yviddvthlp ldqyfnrqtt dwegvfkssn dkgdatnynp
      481 vamakesknn tlqretraii danykilpgf tysgyvsikm ntskntkflp qsvtgavwmn
      541 ayanqaydam seslsiqten klqfmknwng khnlitnlrw ntsqstsssy asktsgmass
      601 glsdpvvgts vqsmgsgese grsisgmgmi nytllgryvf qallniesss amgrnqrmgy
      661 fpafgvnwni qdepflaaak ekwldmakir lsygesgtpp kgnsvymgaf kstgdnymnm
      721 ssiapsrmql dqlkweslke ynigadfgfl hnrlrftfdy ywrdrediln knyripsttg
      781 fsniayfnsg strnqgwefr tdlvffenkd wrisgyfnvs rnknkitelq sgategikna
      841 devkngeyay itqvgrpigs ffgyrykgvy qnkdatyard aegnvmndlk gnpivmkngs
      901 ylcypgdamy edinhdgvin kydivylgnt qplvtggggv tvkykqvtls affhgrfgqs
      961 ivnmarmnne smfgsnnqsk avlrrwkneg dntdipraly negrnylgsd rfvekasfvr
     1021 lksmtlsygf prkicnrfnv nslsvfvtgy nlftwtnytg qdpevsvkdn laidtattpv
     1081 akrfsfglnm sf
//
LOCUS       WP_090613747            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_090613747
VERSION     WP_090613747.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115938
     Region          27..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknikrmlav alpllfatcm ygqknykltg kiisatntpi adavvsvqdt lnattkadge
       61 ftfklrdksg visvwapgyl pvrqllngrt evvimmisdn qykhneqvvl pfrgdnteis
      121 dytaatniak kdfllgsaki dralagqvag lqvkrgsgmp gegsyynlrg irsltgdnap
      181 livvngvpyl pdknespiig gltrdifqay nindiqnitv lkgaeaamyg smgsngvili
      241 qtdgassndm etkvsyygqy gvtwsdkrip llggkdylny ltdagmtyys dmdkfysnfp
      301 flkdpnnply lntynnqtdw qdlmyntgya tdhlfrvegg deiakydlsl gyskenglye
      361 ststerfhtq lngnilvskk vdifatigla ylnghfqeqg mniktnpila ayaqspvlsp
      421 ynkdkdgnil styspyyfgk cttmdfaisn plaivntlda hnrqydltlr agvnytplpg
      481 lvftglvgmy ynydnesmfi pgltdktivp isdtygtann mvrsgvgets nmylnlnary
      541 skmfnrihql naiagaqilt tknefdvgeg rntdndfyqt lgntqadgrr fygylnkwnw
      601 msyyghadyt ynnlvqasvn vsvdgasstg tsanrfyvyp sagvtllgkg wkplqnsewi
      661 nklnvraeys ltgntrfasn mgtfyyssaa yqdisaiarv nvpnthlkpe knaslnlgld
      721 lslfrnrlnv sfdyfnnkis dmicmqptss iygsapyyan vgkmdnkgve lsvqaslvrt
      781 rdfewivggn iahyddkits lggeeriing nwitevgksp yqfygyqvvg vfstqaeaea
      841 anlmadngny frggdmhyvd qngdhridsk drvalgsaap dffggfytqf kykgfalgae
      901 fsyskgnmay navrnqlegm ntlgnqsiav lnrwsldgqv tdmprvqhnd pyrstsfser
      961 wledasylrm ksvtlsysfn ktvlnffrsg tlyvsgenll tatkylgldp efsysygems
     1021 qgldyakmvq pksvkfgvnl kf
//
LOCUS       WP_090613995             305 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Paracoccus alcaliphilus].
ACCESSION   WP_090613995
VERSION     WP_090613995.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus alcaliphilus
  ORGANISM  Paracoccus alcaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Paracoccus alcaliphilus"
                     /db_xref="taxon:34002"
     Protein         1..>305
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..>305
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkesf egearvsitp ssslhlqklg hevfiesgag aragfsdedy aaagvtveat
       61 aasllaavdv varvrppses eigqmregqt lisffypaqn selleaarqq gitaiamdmv
      121 prisraqkmd alssmaniag yrsvieaann fgrfftgqvt aagkvpparv lvvgagvagl
      181 aaigasvslg aqvyafdvrp evaeqiesmg aefvfldfee qardgaatgg yaapsspefr
      241 ekqlekfrel apqmdivitt alipgrdapk lwtkdmveam krgsvivdla aekggncdlt
      301 vpder
//
LOCUS       WP_090615446            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AR20].
ACCESSION   WP_090615446
VERSION     WP_090615446.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AR20
  ORGANISM  Bacteroides sp. AR20
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Bacteroides sp. AR20"
                     /db_xref="taxon:93974"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113211
     Region          28..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkilkccm vsallltstv yaqqiqnirg mvadtdgkpl sgvvvqvpgt kkqaltdvdg
       61 yfdlpitegt klsfshpdfy sqetcykkkg rfivqmasra mpgpedkeiv vdrlrgtskk
      121 geltetigfi ngtsvtstpt ynflgaiqgr mpglniyrqg gdmpaaygwk vrnsrtnlfl
      181 vdgierdfyt mdpdqiesvq vlkdglstvm lgqrsaagvi nvitkkgnvg rprfsftaet
      241 gfekalklpd llgavdyitl vneayandlr epgayieayn paiiekyrnk enpylypdvd
      301 wydellnnta pvhrynfnvs gatnsfnyfv dldwyrengf fktndansyn tnaqtnrfsv
      361 rsnlgvkvts ttfmqinlag rqerynqpaa gtrsfysnml ttrpnrypvy npdgsygsyi
      421 dskanqnlkg llydnghqfk dsrhmsfdlt ikqkmdflld glyleatgsy ysatsylttr
      481 skefaaylyk edgsyqqvge dkdqgnsgnk dqryritflk gavgydhsfg khkvaalfva
      541 dlnqiqdqnv qkgylrnytn ysgrmnynyd drylaeavyt rggynwlapg nrwadywgvg
      601 aawnghnesf vkelnifstl kprisyavtg qaicdyaeyk qsygtskvhl yggpfdnkwt
      661 eenktasrln peiakklnvg idlgflndrl aftfdyyqnr fsdvvatsei ktailgnvyp
      721 rsncekysyt gtemvltwqd rirnfnyfin gnlsfeqskf eyspqlpkay pwmsrlgdpv
      781 gmtygyvadg ifqsqeeida ydaflpsavk stimpgdiry kdlngdhiid mhdqtnlgsk
      841 kakgyygisa gfnyrgfdfs vfaqgtlnrq vylngdfmdg sgkngegait syvlgrwtpd
      901 nhtnthtrvw ygsnnnnrqt ssfwiydadf frlknveigy tlptlltrkl gipsvriyaq
      961 gmnlltvsei fdvrkdidpe iwggsfpmtr tinfgisikl
//
LOCUS       WP_090615687            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_090615687
VERSION     WP_090615687.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118148
     Region          7..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvvgknfvi pssartlqis yigmrtqevt ikttllkvvl kpdaevlqev vvtgmqrmdk
       61 rlftgaaskl taesvkldgl adisrglegr aagvsvqnvs gtfgtapkir vrgatsiygs
      121 skplwvvdgv imedavevsa dqlssgdaet lissaiagln addiesfqil kdgsatsiyg
      181 aramagvivv ttkkgragvs kisytgeftt rlipsyndfn imnsqeqmga ykemmekgwl
      241 nfsetsrnae sgvygkmyql lntydpltgr ymldntdaak ngylraaemr ntnwfsqlfs
      301 nslsqnhsvs istgtdkssf yaslsamhdp gwykqssvdr ytanlnttyn ilknlninli
      361 ssasyrkqka pgtlgqdidv vsgqvkrdfd inpysyalnt srtldpneyy tsnyspfnil
      421 nelennymdl niadvkfqge lkwkvipsle lsvlgavkyq gtsqehnikd dsnqagayra
      481 glddktimdr npflytnpdn pyalpvsilp eggiyqrrdy kmlgydfrat aswnhvfket
      541 hitnffagme tnstdrsrsy fqgwgmqysm geipyyvyef fkkgiedgsn yyslnrtrsr
      601 saaffanaty sykgkytlna tgryegtnrm grsrssrwlp twnvsgawna heeaffeslk
      661 palshftlka sysltadrgp advtnsqaii tsyspyrpft diqeaglylk elenseltye
      721 kkhelnigad mgfldnrinf avdwytrnny dligivntqg vggqilkfan iatmkshgie
      781 ftvssrniqn kdfrwntdfi fsytknevtd lqqnsnvmdl isgngfakqg ypvrglfsip
      841 fkgldengvp mvlnekgvvt stdinfqerq ntdyliyegp tdptftgslg nmftykgfrl
      901 nvfvtysfgn virlnpvfsa kysdlssmtr efknrwtlpg denktnipai lnkrdydsnt
      961 nlryaynayn ysteriakgd firmkeisls ydfpkswisn lklsdlslkl qatnlfliya
     1021 dkklngqdpe ffnaggvasp vprqftltlr lgl
//
LOCUS       WP_090617956             305 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Paracoccus alcaliphilus].
ACCESSION   WP_090617956
VERSION     WP_090617956.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus alcaliphilus
  ORGANISM  Paracoccus alcaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Paracoccus alcaliphilus"
                     /db_xref="taxon:34002"
     Protein         1..>305
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..>305
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkesf egearvsitp ssslhlqklg hevfiesgag aragfsdedy aaagvtveat
       61 aasllaavdv varvrppses eigqmregqt lisffypaqn selleaarqq gitaiamdmv
      121 prisraqkmd alssmaniag yrsvieaann fgrfftgqvt aagkvpparv lvvgagvagl
      181 aaigasvslg aqvyafdvrp evaeqiesmg aefvfldfee qaqdgaatgg yaapsspefr
      241 ekqlekfrel apqmdivitt alipgrdapk lwtkdmveam krgsvivdla aekggncdlt
      301 vpder
//
LOCUS       WP_090619118             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azotobacter beijerinckii].
ACCESSION   WP_090619118
VERSION     WP_090619118.1
KEYWORDS    RefSeq.
SOURCE      Azotobacter beijerinckii
  ORGANISM  Azotobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Azotobacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Azotobacter beijerinckii"
                     /db_xref="taxon:170623"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40297
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkllgqg htvtvqsgag leaslpdsaf eavgatigda
       61 aaalgadlvl kvvapspael aqmktgavlv gmlnpfddgn iarmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee rqcaegvggy arpmppswme
      241 rqaravhera kqadivitta lipgrkaptl lheatvqemk pgsvvvdlaa aqggncpltv
      301 pdevvvrhgv tvvghsnlpa lvaadasaly arnlldflkl vvdkdghfhl dleddivkac
      361 lmceggrvvr tnggapspsa avpratkena
//
LOCUS       WP_090618167             301 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Paracoccus alcaliphilus].
ACCESSION   WP_090618167
VERSION     WP_090618167.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus alcaliphilus
  ORGANISM  Paracoccus alcaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Paracoccus alcaliphilus"
                     /db_xref="taxon:34002"
     Protein         <1..301
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          <1..300
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 dgaatggyaa psspefrekq lekfrelapq mdivittali pgrdapklwt kdmveamkrg
       61 svivdlaaek ggncdltvpd erivtnngvt iigytdfpsr mgaqaselyg nnirhfmsdl
      121 tlkkdgvidh nmeddvirga tvtrdhditw pppppkvaai aaqkpkekkk eltveerraa
      181 evaafraetr sqvtllvagg lfllliglva pasflshfiv fvlacfvgfr viwnvahslh
      241 tplmaitnai ssiiilgalm qigsgsawvv vlgalavlma gvnifggflv trrmlamfqk
      301 s
//
LOCUS       WP_090622469            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090622469
VERSION     WP_090622469.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118496
     Region          24..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktaitftlf ilfscgpvaa qellsgnvtd kegdplpqts vqllgngrti rvtasgnfsi
       61 rrpqapdsll fthvgylskt vpidagtktl rivlevdpgm lqevevntgy yavpreratg
      121 sfthidnell nrsvspnild rlegitsgll fdrsnlsged ingkprlrvr glstieadse
      181 plivvdnfpf egdvntidpn dvesvtvlkd aaaasiwgar agngvivitt khgrynqpar
      241 isfnsninvv akpdlfysqq ylpaatvmdi qkelfergay reddrtflpg yvellikqrd
      301 gliadndfna aenamkqtdl rrqslqylyq paitqqygls vrggserysy sfsggynrnr
      361 gvsvgngder invgmqnsyk alegleitga iwytkqsdkn ngrghlkaas iyeglvdeng
      421 nprsiisryr ssyheraees glldwmerpl deirlndsrt saqtvrfnga vnytflrdvk
      481 aalsyqylvs esggseyhdk esyyvrdlvn rftgeagnrv ipyngimdyn atsggqahsg
      541 rlqlnysksf rdkhavsvlg gaevrqtitr ltpgvtlynf dkdvwtgtgq ldhstwfptr
      601 psgsssiaag vglpdkttnr ylsyfgngsy tflerytmst smrwdgsnll gvkanqrgtl
      661 lwsaggswei sqepfyrlsa fpyvrlrtty gsagnidktq shyptislnt ngytsltyan
      721 ltspgnpslr wervntlnvg ldwrtkqqrv ngsieyytkw anhllgsdlv dptlgiptsq
      781 sykvnygslk tvgwdiqlnt rnltgalswn ttamlsysrn eithltrpvl ryayefvtks
      841 ipevgksvdl lyatpwngls adnglpvvyv dgkpttevsa ytnyvlglsy delakvgvtv
      901 ppffgslrnn iqwkgikldf litynfghvf rrtsmspgde ylnllipryh mdyfkrwekp
      961 gderftdvpa aigvsdlgis dyyrysaali dkgdvirlrd igvsytlnkn tfsrlpfrsi
     1021 slslyarnlg ilwranksgv dpefpsadyp aprsfalglq fsi
//
LOCUS       WP_090623145            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090623145
VERSION     WP_090623145.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114792
     Region          128..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlnhyikvsa tglflliavn qvaygrfpkp gashrtvdqi ginspikvvd eygkplpavk
       61 iyslrnellg etdeqgeaal tvtgpdmhis lrhpayyskt laagtattva lvpnylqepa
      121 tvdvlhdkrd rntvigsvav vynsqlkstp tslylnaltg rlpglytqet sgfrsariap
      181 itandlagsl ptsatkysts lsdnaevafq lrgqnpvvli dgvqreiysi dpesiesitv
      241 akdalssill gqrssrgvlq vttkkgrpgp prisftaqtg vqhalkrpep lsshqyayly
      301 neallnsgra pvysqedfda fkngnsplfy pdvnwydavl ktntpitkyn lgvnggtkna
      361 ryalslsyln qqgmfqssdq fdyetnlgqq rylinssidv dvtsdltigl qlfgriqegr
      421 spgagvegil kalqstpnna ypifnddgty ggsseyptnl yqqvtgsgyr ldntrdvlan
      481 ldfnyrfdrw lpglyakgkf nvsstssslv drnrqqpvyd vryneagelv yvrygnisdq
      541 pnsfattsta nfiyyqgnig ydthinedhr igvrifadqq tanyqfdlpa ihtnvaatan
      601 yayqnkyfae vaanysgfnr fqpgskfglf yaaglawdla qesflaeqsd wltelklrat
      661 ygktgntneg algyyswras ygqdgnngyg vgseysfvss lvekglanva gtwekghkfn
      721 vglnlslwns lslsaeyyrd tyydllqqrg stieligigy pnenigknry egqelaityr
      781 nhvgnfnyfi aanasrmrte vvymnevfqk ynwnrrtgmp vgqtfgylad glikdqvead
      841 aapllggsev hpgdvklvdl ngdgminiyd qtaigntkpl lyfgttigfn fvgfdfsvll
      901 qgvanrtyqq tdysfgsdge rqgysyllgr wtpetaetat yprltigsdp tntpylntss
      961 ywtrsgeylr irnidlgytf pfhlsrkirv salrifaneq nlftltpydr ldpeisgdta
     1021 ypiqrvinfg vtikl
//
LOCUS       WP_090624787            1153 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090624787
VERSION     WP_090624787.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1153)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1153)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1153)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1153
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1153
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128948
     Region          48..113
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          129..1152
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknpillfi mrvstlqlff slmlavssfa ndsraqsilk ktasiegknq tvetllerig
       61 qvygvnfiys peliqaeqtg risskehtls svlkelltpl hisyevygkk nivlnkadqp
      121 rnvqsrqtvi rgrvldaggi plvgvsirek gtengattge ngsfsitvad vnailvfsyv
      181 gyfakeipaq sdnltvvlee dqtnldevvv vgygtqkrvn ltgaitsvkt ddignipaan
      241 lsntlagrip gatvvgtsgl agasssirir gsfqeplyvi ngvikgkadf daldvneves
      301 inflkdaasa avygskagng vvlvttkqgi vqkpsfeykg sysfsnptqp iqdfsatqei
      361 eyvnqmavsm gqpkpygqei ydyfkdksyr indyiwqtpt vqqhnlgvrg gseillynls
      421 lgthnekgsy knlnfdrynf rsdvtanisk nfkinlnlsg nqrnyhrwyw pydgaedfnv
      481 gdffratfnw trlypfyvda ngnpststdd fpvvpgawhp velmvnsggy rdlkyrnldg
      541 ilrfdldlsd yvdglstslq ghynaydrnm ksfvihnrsy ifqpasttnr fvpgpidptk
      601 vnihnlsaty pniaedagfy nsyqfnwylr ydknfglhdi salavyeqak dngkylngra
      661 ddllttsidq iynassdntk rwfsgnetqa aresyigrln ytfnskyiae fsfrydgnyk
      721 fapshrwgff psgsaawrls eerflqdvrw lnelklrgsy gttgndtypn gdpipafqws
      781 qtyakstgfi fgntlsdgla pgampnplit wstsamwnvg adfgilnnrl tgaidyfere
      841 erdilgarla stpstlgatl pnvnyakrsw kgvefnadwn nrigelnytv ygnlgyaidq
      901 wdlfdqaqal tdgtykdnwr svigkpanri ygliskgiir tqeqldaipe gftqfgrdpk
      961 lgyllfedir ganytegpdg kiddndftyl sdngapriny gvgfrlqwkg lavnahfqgv
     1021 gaydrmvstr ngggvfqvdr pyfnvwasdy wtpenpnaty prvtgewnta dvggaastfw
     1081 lrngayfrlk nidlgyalpq qwfsrlgvqr vqffvnatnl fsisglaehd peqntldsyp
     1141 lmrtftggln inf
//
LOCUS       WP_090624877            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090624877
VERSION     WP_090624877.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116165
     Region          50..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mckvftttgs ekpgiyslpy lvvittlmll apaftrmava lpvtisqepi agivrdsign
       61 plegvsvlvr gtsrgtatda sgqfqmqasa gevlifrtig ylsqeltlgn qrtvnvvlqm
      121 essdldevvv vgygttkrkd ftgsvgsmnl enspvalapn invleslkgs isglnigatn
      181 saggqpamqi rgqnsingen splivldgvi fmgnlsdinp ndiatidvlk datsaaaygs
      241 rsangviavt tkrgrigkpv isfnssvgfq ewqnrpemlr aeewiemvna rnqytpgstn
      301 wlkngelanr eagretvwld eisrtgvmqn yqaaisgase ninyylstsf ddnksiivgd
      361 qfnrialmgk ikadvtkwle vgvdagfskr dysgvaanin eaqtmspygv mfrddqgnle
      421 kypytqsgvn plwgvnngtr dnedflynyr lnthavvkvp wveglsyrvn ylinqdethy
      481 gnfyyedhyv qegespdrys patlqnlltn angtiekrkg nsyvwdniln fnrtfdrhsl
      541 dvtlvatrdh mkyeryvmtg rdfaangnta lglqglhkat vqridydgtn addlatrnye
      601 rsnigylgrv nysfddtyyf tgsyrrdgas vfgadnkwad ffgagfswrv tneafmepve
      661 ilndlklkvs wgqngnqgln pygtlstven aasggaryef sntpgriyyg lyqgklgnts
      721 lgwektsswn agfesawlgn rifadldlyf akttdqiflr nipvmtgfkq mmtsmgqvnn
      781 tgieatvrti nvqksdltws ttltfwknfn klvslygddl dgdgredddl anglfigksl
      841 gaiygyeqig ivqeddteyi eltgaapgap kyrdldgqpg itaadrkilg yekenfrlnf
      901 ssnlsyknfg lyvmvtgtfg gnnmyvksnp saylvngtgr fndnlhyipy wtsenrsnvy
      961 psalfagdgr fqglqsrgfv riqdislsyt fnqpwlsaah igslkvfata knlatfadwf
     1021 ggdpetgari resesalrlp vastyslgvn lsf
//
LOCUS       WP_090625054            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090625054
VERSION     WP_090625054.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114339
     Region          26..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfvfkiplli vgfsmlgmal ygqspvsglv ineedqpivg vsivvrnssq stvsdesgmf
       61 llndlsegsv licshvgyqt kevtvlnpke kitvvlmats ealdevvvvg ygtqrktdlt
      121 gaihridasq fqrqsstnvl emlsgtvagf ssnqgtsaqg ggsmeirgqt sikasndpll
      181 vvdgviyrgv itdinpsdia tidilkdasa aavygaqsas gvliittkrg ttgtpkvnas
      241 tklgvvsltn mmrpfnaeey lenrgvdtyq tygdkplyyy snpndlptgv sledwknlda
      301 ttsddpvdmw lnrlrltnte kknylagrtv dwfdmifrng lrqdydlsis ggtpqvsyfa
      361 sggytknegv ilgdnfnvfr srinldiraa sflkfsvdan ysnrnhgftp vsisnaigas
      421 pygqvyaddg tmewytheda tapnpliyyt yrerlnpvqs lfatisaeln lpfgitykps
      481 fvsnqrwvkd ytfdpvetpn gynnggsgsr snttynewml dnlfswnkti gtdhqltatf
      541 lynieknqsw ndvqsntrfa pndalsfhal qaginpslnn ndsystgnal mgrlnygyks
      601 rylltltirr dgysafgqdn pyatfpsaal awriseepff klepvdelkl rlswgangnr
      661 svgiydalar lsttqyiygn elvtgvysst manrhlrwes teavnagvdf ellgrrlsgs
      721 ldgyvmkttn llidrslpsi igytnvasnl gelqnrgmel tlnsrninrt nfswstafnf
      781 sfnrnkithl ygdkvpvmda ngavigerea ddvtnqwfig rsidqiwdye rlgiwqldet
      841 deaaiygkkp gdvklkdqng dgvltpmedk ifqgnkkply niglrndirf lrdfelslfl
      901 radlgffgnn plyretqwid rknilyapyw tenkpsneyp kldtevsspd ygvwksrsfv
      961 rlqdvtlsyn vptvllnryq lqglnlfvnm rnyltitkwn hwdpesqatp mpkyitvgln
     1021 anl
//
LOCUS       WP_090625351            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090625351
VERSION     WP_090625351.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122037
     Region          26..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkilymklcv livtctsmvs lsfaqqtltg tvsdaqgpip gvtitvhgtt ratqtnedgr
       61 ysfqatsget iqfsmigyvt qtvvvgssnt initlhedag qleevvvtal giqrapkelg
      121 yamstveaee ltktgspnfa galygkapgv risaapggat sgininirgt nsitgnsqpl
      181 viidgipmrq stfnnsdywg dqrargngle dlnpediesi svlkgasaaa lygseamngv
      241 vlvttksgkg gqgfsidfna tytndqiayl prfqdvrgpg ydpsyadvgq sedmffyydd
      301 gvrgtantsl nfgpkfdgqp irswdgeirp ysaqnaydkf fnnpnntvfn lalghtgdrs
      361 ntrfsltrqd nqmtsldsyn kknianlnts fkfvdrlttd vvinyinqht hnrpfltdrl
      421 innftgmist fdnpewyiek yktslgyrfv tgtdpsltpe enityngyrg dvldymwqvk
      481 aknydeysnr ligsftntwq vtddfsvrar fsadmtalrt edkqpsekpl sidkntgyyg
      541 lgsqnanvyy tdllatynkq vtgavklgvm vgytatksqd tyihrgtngg lsvrdwfdln
      601 asnntatwnd rynyknnmlr dalfgsvnfn lkefwfvegt lrreristmh pdnnvlyyps
      661 vnsslilsda fnfpsffdya klrgswgivg nypdiyrsal sltqtslgiq tdsgqpityt
      721 llptsdfgne kikpetkhei efgletrmln grlgldityy ngqirdqiln ytlpistgas
      781 silanvgtlr nkgwefaltg tplaegnfrw tsalnfamnk niveelpgga gellhrdydg
      841 aaaqlvskvg kpmgdimvhp iatdangnki vqdnglyqld adnwikagna mpkaiggfin
      901 tfsyknftld alidfrwggh vmptgiawmt srglteesln ymdaehggms yyldengkgv
      961 aysgtsgpng ekifhdgvlm dgvlangnpn envitqvlyy aatynwggpq ysdsryelyv
     1021 qknnyikmre lslgyrlpdh iaaklraksl qlsafgrnlf fvyrsvkdld peqmtggsnw
     1081 vnqvsnagts patrtyglml rasf
//
LOCUS       WP_090625880            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090625880
VERSION     WP_090625880.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121282
     Region          40..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrsllnrsrl nrsaprltff faalaigfmg glspgfaqet irgtvldens qpltgvsitv
       61 rpedtqtvtd esgnfqlaas igdtlefafl gyetaihvve nndpiaetlv lagatdleev
      121 vvvgygtqkk snltgavsav nareltkisp snlsntlagr apgvnvtnts glsgatsrir
      181 irggfgeply vidgvvrdka afdaleafev dqmsflkdaa tasiygsrag ngvvlvttrk
      241 gtqqkptfnf qsnytlgqpt mtllsdltta tdeliyqnrv atfngtplpn gdeefeyfrn
      301 rsynvhdfiw rnpishrqsl svnggserit yysllsyrge qgsykslehg kvnlrsnvsa
      361 kinesisidl nlsayqqnge rfywpftgdd dynvsdlyrv tfnwpktypf yteadgtpan
      421 yvtdypvqtp mgswlawsvi dqvigdryik trerqfnpil svnikldkvt pglstkvvgs
      481 ylgedymrkk yltfqtnyqf ipadpdgnrf ipaapdpnrt ntfnfsqnqp fldyeihtnw
      541 ayqfnwflny trtfgdhaid alavyeqaed glfaayarge npitnydqmf ayptdrqfre
      601 adgweeigsr qsfigrvnyn ydnryiaefs frydgntlfp ehqrwgffps isaawrisee
      661 affqntetai ndlklrasyg ttgndlmist ddripafsyt eryvnsggym fgdryygaia
      721 pgptpspnlt watstsynag ldvgvfnskl taaldvflrk etnilgprlv svpdnygqel
      781 apenyaarsw rggeltmqwn dqlaanneir yavnanlgya kdrwdiydes aayapggnrh
      841 fesrigmphe riiglkalgi irtqeqldel laqgltqygr dpylgglyfe dvrgdgfapg
      901 pdgkidgndi qllskkatpl mnygfgldvy yknftlqahf qgvmgydrii snqegpgmrq
      961 hggairpyyp iwasddvwtp enpdgkyprp igqnwyesgt gassfwirng aylrlrtlnv
     1021 aytlpeswms alhinnaqlf fngtnlffls amrefhdpeq enydsypvmk tftfgldvsf
//
LOCUS       WP_090626014            1124 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090626014
VERSION     WP_090626014.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1124
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122618
     Region          35..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          112..1123
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktnrhyivf sfvlllffid gkaftqtdls krlslniknv elisaltile keadvkfays
       61 aeslpghkrl tltysevpls vilddisekn dlkyevtgql ivisrnlakq qrtvsgtvtt
      121 etgeplagvs vnikgtqlst stdenghfsl slaegsgmlv fssvgyitqe idvneqssvr
      181 vvleqeektl neivvvgygt qkksvvtgai ssvksedlqn qqigrveqal qgrtsgltia
      241 sssgapgsaa tvrvrgatsl negasdplyv vdgvvvdigg idylnpsdie sievlkdaas
      301 aaiygarssa gvilvttkkg ssgavrlsyn gylgtqapak klsllnatqy atlmneqain
      361 gggnsifsdp eslgrgtdwq daifnngalv qnhefslsgg gekstfyssv gffdqngiva
      421 teisnfkrin irlnsthkia dwltigenvg ysriknlsgv sgntdfggpl sgalmmdptt
      481 ptlitdpsei devpystqpv vrdelgnpyg iskyvaqqvt nplayirtrd gnyswsddiv
      541 gnayveiipl aglrfrstvg trlsysgges ftplyylnsn qfttqtsfar nrqqalnwnl
      601 entlsygkqv gehdfsillg qgaysdnnss glsvtyfnlp vntfkdasmn ystasdniqa
      661 sgyegithtv sslfgrlsyn faekylftgi lrrdgssrfg snnkfgyfps asvgwvvtqe
      721 dffpmnssvd flkirasygi tgndvlgnfr yistvgggrn yifgddiyhi gyspdapanp
      781 dlrweetsql nvgfdailfk nfdltfdwfk kkttdilqvv qlpnyvgstg ssygnvadme
      841 nkgvelelgy rktlgnlrln irgnisyldn svsflgdgks fldggetiqs tsypitrtav
      901 gyaigsfygf etlgifqnqq einsyvnaeg nliqpaaqpg dfiwadldsd gaitaddrtf
      961 igdptpnwsf gftlnlawkd fdflmfgqgv agneiyqglr rldiptanwq tdawnrwhge
     1021 gtstsyprlt tkdvnknfsn psvfhlqrgd yfriktlqvg ytlpaklvdp iglakirvyv
     1081 ssnnlwtitg ytgydpeigg gsygidravy pqsrsflfga nlsf
//
LOCUS       WP_090626038            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090626038
VERSION     WP_090626038.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117002
     Region          29..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkttctgif iylfsllvpl iafsqqldit gsvvdaksns plagvsisvk gkpvsaqtds
       61 kgtfmlagls ptdvlvfsfv gyfpreiavn qqdpplviql tsstenldev vvtafgvsra
      121 kkalgyavqd vnaqelatrp analgaisgk vaglqvipsg gnlggstrvl lrginsisgn
      181 nqplyiidgt pidntdlnss smingsagkd fgnliqdlnp ddianisvlk gpsaaalygs
      241 raangvilit tkkgegadkf nitfntgiel enivrlpkrq hlygqgytns fatatingqt
      301 ynivnyeade swgpkldgtp vlhwynldpe ypadylnpqp weypehdvsy ffrtgvsntn
      361 nlaisgssgn tayrlsytnr nvrgttpnss lgrntlnfag stqfgrlkvs snlsythnnt
      421 lgrpwagasn rniileafqw ggvqvdykrl aeykrpdgtp rawnrtgyqd tpaaeatrfi
      481 dnpywsayes yleekrdrly gnigltlqat dwldlsgrvh gdvyahqfqd riavysrsqs
      541 qyqeysnhfn eynyefiata nkqwsqfsls gnvggnirdq qrritdgitq gglivpsyyn
      601 lknapsvltn nafyhkrvys lfgsfsagwn dmlyidgtlr ndwsstlpis dnsflypsvt
      661 gsfvfselps lrnsniltfg kirvgwaqvg ndtdpyqlqq vfealpafag npnyalsgtl
      721 nnallkpeit sswetgvnlv ffnnrlslda tyydnvsknq ilpvpisaaf gydakilnag
      781 rvtnkgvevt ltgtpikndr fewnstvnws tnrnrvdkld egvntlelsn alvtlvareg
      841 qpygqllgyd fvytpdrqrv vqedgtylkt sqlvplgsvl pdyligfqnq frfkkltfgf
      901 lidgrvggsf fsqtykvgmy sgildrtaan girengvvvd gvkadvtflp dgtyttanir
      961 pndtrisaqd warneyngpt afsifdatff klrevtlgyq fslanhigis slnvslygrn
     1021 lwniytksky idpeftnsgg nvqgieggsi pvpatyglnv tvnf
//
LOCUS       WP_090626055            1203 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090626055
VERSION     WP_090626055.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1203)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1203)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1203
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132206
     Region          143..1202
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyvpylrea vkitvnamaa vfsmtprcpl amkltplavf llvlntyaet slaqrvsira
       61 nnvplenvlr eirkqsgydf likeeylskf kpvslevsem evgtllplvf anqqfeysvn
      121 gkiitlvpkr tskaslpvet vqqtvqgtvk detgaliaga siyikgtqrg tmtnddgrfv
      181 lpdvpagatl visntgyetr evavgsqtal titlttvsqe idevvvvayg takkkdftgs
      241 itsvssddit qqqvstvsqa legkvagiql tspsgqpgnd skirvrgmgs inasndpliv
      301 vdgavfnlgl salnpddves ivvskdaaan aiygsraang lilvttkkgk sgtpkigvdl
      361 rwgafsqgvp dmevvrdpgt yyeytwqgiy nymrykqgyt dadarqyasd nlftangasn
      421 tgnglgnymn ykipegttli dpatgkirte aallyhdswp dyflktalrq eyntnisgas
      481 ektdyyvslg mlknpsyvmg sefnrysarv nlntqiaswl kgganmsysk nysnaptgyt
      541 ggttntnift fmnlfaptyp iyaydangqi irdadgkpvy dlgtnqtysp ygstarnafn
      601 gyspavyfek dltettndff sgrgyleakf lkdftlkadv avdnsyqnyl eygnnesgsd
      661 ardyegrirs afnkamtlnl tqlltwnrsf gehtldalvg hefnkfqsdn ingtkykmya
      721 ldnpsmgnav rvldltggde ertlegyfsr vnynyaekyy lsaslrtdgs syfrgnrwgt
      781 fwslggayri geenfikdna dwitdlrlrg sygvqgnngv pvstryawtn tyglsavgsi
      841 tdaefalsan twgdpsitwe snhivdggld frlwnrfygt vdyfrrktvd lllsvsypas
      901 agragalrnv gkllntglev dlgvdiirkp dlnwsfnina sryrttllei pdnmkssgld
      961 ggylsgnflr regtdyfnly myryagvdqe tglgmlykkl teadlanypg ksvgdvvttt
     1021 vgseatrfel gtstpdlvgg asttvrykdf dlgvavsyql ggkvvsrtyq yitgqsigrg
     1081 vhvdlldawt pentdsnipm rmlgdtnfgs qpigggegqy sdfslfdady fnlrsinlgy
     1141 rlsssltqrl hlqglrvyva adnlyfvsak kgvdprqvld gvsvnpfnyp qtksisfgln
     1201 isl
//
LOCUS       WP_090626459            1533 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090626459
VERSION     WP_090626459.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1533)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1533)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1533)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1533
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1533
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=171078
     Region          24..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
     Region          1103..1302
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cl21747"
                     /db_xref="CDD:451378"
     Region          <1415..1531
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mkkktllfll lvtasyslra qssvtgrvls eldstavggv sivnsidgnv ltktdndgvf
       61 kinnskgies lilshiayqm dtvrltqttg rivvylqpds hviseivvst gyeslntrkt
      121 tgsytlvnne llnrsvtpdi lsrlegvtns lsftrkdlvg erertpelrv rgkstihgdg
      181 splivldnfp yegqlnsinp ndiqditilk daaaaaiwga ragngvivin tkkgginrrp
      241 vvsfnsnvti gerpnllysp lfmdaadfle vekelyrrgf fdnpddrtvl spvvemlikd
      301 getpstatka amdklaeidf rneasrlfyq qkvnqqyavn fqggadrfgy yisggydanr
      361 vnikrnsdnr vtlltqfnvk ltnklevnlg lnlvasqvaa nglgltsmvs sgkaallpyt
      421 tfldeagvpa vinhnyrqly vdnaeamgll nwqyrpleeq algnsvskat esranaaisy
      481 qivpsirlda kyqyhrilnd hatnfhessf yardlvnrft qqdgtqiipk gavlegsnse
      541 ttdhafrtqa nidktlngmh eitglmgfem rqtktigspg yllygvdndi lvgknrldys
      601 iahstrpqgr alipapqtaq rylidrylsy yanisylygg kygfsasarq dgsnlfgvky
      661 nqkfvplwsa gfawivsees fvdwgidtfl klratygysg nvdksatafp tatysadprs
      721 gllsaiirsp gnpslrwekv qtlnfgtdfs vlsgrlagsv dyyvkrgldl igddvsdptt
      781 glgfpalqgg tlsnrinyan tktkgldvev tsenlrgkfr wstallanyv nnlittyrgt
      841 ddpnilaytv ttgpispmeg rpidplyslp wyglnpddgs plvrvdgtls nqygqfinql
      901 thadlilsgs sipkwfgsir ntfgwgdlsl sfniswksgy yfrpssidyn slfsqwlghr
      961 dfadrwlkpg dekftnvpsm psletydasg rmdlvytrsn ilvekgdhlr lrdinvnytf
     1021 hkstfrrlpf qsmiltlymq nlgilwrans kgidpdvpna sypnptayav glnvnlnqlk
     1081 mttkhififf avaacmcisc edfleikpdk sivvpdrled fqalldnnai mnagtghqlg
     1141 eisgdnyfis rvawenltna fqrnayvwek eifegelstd wnnpslvily snlalegaak
     1201 itrddrnfne wnnlkgsalf frayafyqla qlfcdtykss sasqdlgipl rlesditlps
     1261 vratiertyr qivadvteas tllpvvpvfk trpskpasha flarvflqmg dyenallhan
     1321 lslddfnslm dynsidatdn fpfvpyndev ifhshmsspa ilnqsrlqva dellkayead
     1381 dlrktcffre nngsivyrgs yygsnafftg lssnevfmia aecnarigdv pqaleclnal
     1441 lasryragtl vaieetdpql lldiilaerr kelpfrglrw sdlkrlnlds ryaktleriw
     1501 eneavvlepn spryifpipd avidisgieq nkr
//
LOCUS       WP_090626849            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090626849
VERSION     WP_090626849.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113870
     Region          29..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkmkllnklw tvtliaccfs lygsaqqais grvtangqpv vgasiqvagt stavqtnqdg
       61 tysitaasgs gvlvvsyvgf vtqhvpinnr tvihvelqeg ateigevlvt algierekka
      121 lgysiqevdl stvtearesn ianslkgkva gvhvnattgg agsssfvvir gsssiagenq
      181 plyvvdgvpi dnqtldqagi fggkdygdgi nninpddvae msvlkgpaga alygargang
      241 vilittksgr grkglgvefn snfvmetinv iptmqdrwgv gyggtnsfgs meyegtsypa
      301 qtgngdqfgg pldgqlimft ympewsprpy spqpadnird ffdtgktwtn tiavsgggdk
      361 nsfrlsvsdm rntgiipnnk lqrqtfnlra tsnitdklfv egklnyirqg genrqatgit
      421 tqnpayslyl tprfvdlnwl kdykkedgtm vnwksgtpyn pywlvnefqn ddkrdrvigm
      481 lmgryaftsw lslqaragtd fytdvrfdrk gtysppaalm pgtvdnatwh vkeenfdvll
      541 tangdlsedf kgyfsvganh lnrkqevvgl sgenlnipyv yhisnaqivr prnslsrkqm
      601 nsvyfagqvg ykdylfldvt grndwsstlg lnsnsffyps iatsfvftda lgmrnnpils
      661 fgkirlsvaq agndavpfqt tggyaldmvg ygpglpyatl rsqvplldlk nelttgfeag
      721 telrffknrl gidftyytqs tknqilpvqv smatgyatrv inageiknhg velllngtpv
      781 evggfrwdls lnlsrnrsqv vslapnisth vlienangri earvgeaygn ivgfpylrtd
      841 dgrlllsetg vaqraaeqvv lgniqpdflg gltstfnyrg vslsglldir iggqvfsfsr
      901 yhqhakgtgv ftndrenlin dgvilqedgt ykqsdivltp enyygqrawg nvgeemimda
      961 dylalreltl gyafrpgflk stpfqhikls vvgrnlfylk rdplmkemgi tpetafapta
     1021 aaqgyevaam pttrtfgfnl sfal
//
LOCUS       WP_090627504             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas marina].
ACCESSION   WP_090627504
VERSION     WP_090627504.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas marina
  ORGANISM  Nitrosomonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas marina"
                     /db_xref="taxon:917"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39308
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir ggetrvaatp etikkytaag vhivsvqtga gagasipdse feaagakiva
       61 daatlysqsd mvlkvrgpea eelammrkda vligllapsk senidilaqh gitafamekl
      121 pritraqnmd vlssqaniag ykavimaanv yqrffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avveafdvrp aakeqveslg akfvevplne eekanaetag gyatemsedy
      241 krrqselvhe ravaadivit talipgrpap vlikeetvka mkpgsvivdm aveaggncvl
      301 seldqtvvkh dvhligiani pglvaadsst lyarnlmnfl nlivdaesgq lridrddeiv
      361 agtlvcsdgn vvqas
//
LOCUS       WP_090628170            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090628170
VERSION     WP_090628170.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117051
     Region          23..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkallmtll wcvglsiama qtrsvngvvr davgktpidg atikafgtqr ttssaqdgtf
       61 sievasgnds llvsfigydq avvhieanas tvsvdltvss eslqevvvtg fglqqkkesl
      121 tsaississe disrsvssta sgalvgkvag lnsrqtdgrp gaetalkirn mgtplyvvdg
      181 vqmdagqfnn ldfndiesis vlkdasasiy gvraangvvv vntkrgqrnt kntinvtany
      241 gfqdlstfpk panavtyvek yiqaetvqgv dsyrfsaedl dkwrqgtekg yvpfdwyeyi
      301 wetspqtyln anvsggseni nyyfsvghln qndvivnygg fqrtnvqmni tsqiserfkv
      361 ggsfnaryek tqnpgvpggd dlwlprfatf rnlptvrpfa ndnpayptlt sndpgtnfaw
      421 lnydlsgkfq etwrvgqlnf daeytiidgl kakalvgyyy agqrldnhey tyqlygydea
      481 tdtypvifqn nnpwrerrmg heermnsnvq lnyskvfgnh nvaviggmet mlinepttwv
      541 hsipvsnnlp lidfesmdty ddlgdrpear lgyifkanyd fankyllefm grydgswkfp
      601 pgdrwgffpg gsigwrisee nfwkdgklgt iandfkvras yglvgdddlg tindvpiysa
      661 fdylggynyk qggavidgky vlgtrprglp vrtlswirak mfdvgldaaf lnnrltvtld
      721 yfrrertglp aarydvlips evgfglpnen lnsdmhqgyd gmvrwadrag elnysvggni
      781 tysrfydwdr yrprfsnswd eyrnslvrrf gylnwglead gqfqsweeiq nwpvdndrqg
      841 nrtlrpgdvk yvdqngdkvi nglderpigy rqnetpvlnf glnfsfawkg fnlafdftgg
      901 gmftfyqewe qrnpfhdggn npqsyfddsw rlrdifdpns dlipgkypmp lignsahsny
      961 wnstfwkhnv rylklrnlef gyslptrile plsitgvrvy fsgqnlftla niegvdpegd
     1021 atnglgyptm tiynfginls l
//
LOCUS       WP_090628379            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090628379
VERSION     WP_090628379.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114534
     Region          29..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrlliqrl faimllagip gsnmamqqqt vtgtvadatd gtpiagvtir vrgtsiavss
       61 addgryivtg intddvlvfs ylgyrsreep iegrttisvq lgrledvlee vvvtalgirr
      121 eekslgysvq riggeqvqqv kgvdiatslt gkvaglwiqn stefdespdi rlrggssnpl
      181 lvidgvpygn mglrqiapdd iesidvlkga tasalygvrg gggaiivttk sggngisvns
      241 nnmffagyla lpevqtsysa glggsynsid yvwgdkldvg imeeqwnpet kqfelmelts
      301 rgrdnlknfl epgivtnnni sfarsgdigs vraslnhvyn kgqypnlkln rlnatisgql
      361 klseklelks higynrsmtp qitgagygdq gyiyqllmwt gpeydvtkfr dywvvpneqq
      421 nwhykawydn pyliayekly grennmtnvn ltsdykpfeg akvtarvgyd fysnedtrrn
      481 ppgifstrgw hangmfgqyq srgfslntdl lfnygkkklf ntldidftag gtiyryedqs
      541 lsgatrsgli vpgvyslnns verpdvwtsr ygkqvnsllg lasfgwkdav fldltgrndw
      601 sstldittrs yfypsvsgsi lleeffklpt wvgmwklrgs wavskqdlgv yatnvnydis
      661 qgawdglnta dypsglntsv ikpqtnrtwe agtaiymldn rltidlayyn vfnynrqlss
      721 tipassgfta tlintnetrv rrgvevslnt gvlkkrnftw daavnwatth qyykeldpvy
      781 spdnlwtkvg grvdnytitd wlrdpqgrvi htngglpqqg qyasaigysd pkfiwgftns
      841 ftfrdfdlql sfdgrvggll ynytaykmwd tgshpdsdnq wrydevvngn esfvgngvkv
      901 vsgsvsfdpy gritedtrmy apndvpvsye tyarrfadgr fgatdptfik irelaigytv
      961 prslserwgm srarisltaq nvflwtkdfr fadpdwnads dltspsqrfi glnlnfhlan
     1021 dnqpnn
//
LOCUS       WP_090628623             312 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Nitrosomonas marina].
ACCESSION   WP_090628623
VERSION     WP_090628623.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas marina
  ORGANISM  Nitrosomonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Nitrosomonas marina"
                     /db_xref="taxon:917"
     Protein         1..312
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36103
     Region          5..173
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiinlfskr qkelrgeipd vytyedlprg lrvqichiwe dtlgnhsefr nnnkvrsayq
       61 livdslcrey glfqlpaank yadgmyqnel idsflqesdi ekqldivels fnvintytrn
      121 yeylyrpnfl eiannaieel ncrfkehgig fqfieneivr vdselihvea vkpalrllnd
      181 kkyngpqqef lsayehyrhg rhkealndcl ksfestmrai cdkqnwsysp natakdliqv
      241 cftnnlipkf wqqqfaslrs tlesgiptgr nklsghgqgt tptvvpdylv aymlhmtast
      301 llflilaekk ik
//
LOCUS       WP_090629565            1091 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090629565
VERSION     WP_090629565.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1091
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120579
     Region          27..1090
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miqtfakfif llvglnyaqh awaqqltvkg qvtdaasgep lsgatvsvvg stvsttsden
       61 gryslvvhvt pekisvtflg yqkqeqplgg qteldfrlvk sdasldevvv talgikrerk
      121 slgysvgnvd gealnetpqa nvlnalsgkv agvqisqmdg tagssvnmvi rganslngdn
      181 qplfvidgvp vsnqlnngfs gadmgnaisd inpndienvs vlkgpsaaal ygsragngvv
      241 littksgags krgigvslsa altaevpyry vpvqnkfgng kagahllees enenwgaeld
      301 ageqwvqwns ngqavplvsy pdrfqdffqt gltstnnvav dgsydkgnfr lsvgnmenkg
      361 iipntdlsrv tlalntsyrl tdrlratanf gitesgsdnr pvidgernsp vrslyetgaq
      421 vnildlvnyw ipgmegiqql kykdkqnnpy flayenptsf krnrtvsklq ldytisddfa
      481 flvryardet nenqeakray snfnnlkgsy qlddnyrked nidatlsykk efasiwsina
      541 magfnrmerq vqimnnytse lvipdlysis ngapgtvvyd sfksrkllyg vygtasvgfa
      601 dkiyldltar ndwsstlpsn nrsyfypsas lsfllhelva lpdwltflkl ragsaqvgnd
      661 vepyslraty sndsdwgsak rlymgnelrn atlepeists heaglefqfl gnrlgfeaty
      721 ytvnnknqvl siglpiesga gsklinaglv rsrgiearls gtpiqnrnfr wdmnvtftrn
      781 rtvieelaeg ieyfnftsys glevrtyagg gigdmymrpm ltvkdknspy ygyplltnsg
      841 vyqtdndisn lvkignfnhd fmlsfqpsft yksfslyani dwrqggmfys ntmmflgnng
      901 qleetlsgas ydrsrgieeq vkaspeayfg kwiggrnady gglpwpgaes evrkqdasfn
      961 igvreviden ghssyvenlg gattvwldpf nayrystrpf pdrnlysaty vklreialty
     1021 rlpqsfssrl rlqqtsvsfv annvfqwnaa gididperay rqsaagwiqg veyynvmpwt
     1081 asfglkltvn f
//
LOCUS       WP_090630855            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090630855
VERSION     WP_090630855.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121407
     Region          25..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklfiltvli cctistskvw gqttkltgrv vndadgkplv galvrssngn sptktdesgm
       61 fvltispkdt vlyvsflgye tseinlrtpy akpltvmlqp gvraleeviv stgyeeiple
      121 ratgsfekid nallnrsvgm dvlsrienia sgvyfnnrkv dinsvgppdh dlyvrgistl
      181 rnaqvgatap livldnfpye gsianinpnd iesvtilkda aassiwgaka gngvvvittk
      241 kadfsqptrv sfnhsvnvta kpdlyarkvm easdiidmem flfdkgfyns netkrskpal
      301 spivelliql rdgkmdttna ynaidqyran diredmldyi yrqsvnrqya lsmdggnayh
      361 rfrlfggydk mlnsqrgsen drinvklens fnigtkllld srifwtqtrn tyaslgttga
      421 nygsngypyp yirfadddgq plpvpndyrm gfldtagqgk lldwqyrpld eirnpanhvl
      481 treilmnvgl tykiaqwana elkyqygnen gihqnhgsle nyatrdlinr ytqidangvv
      541 syavplggil rltntaassh rlrgqanink dwtdrhrlrg llgmdvqqrk ttsnaydtyg
      601 yddeyltfvt nidhntrypi yanlaaasfi pntrafagsv nrfvsvygnl aytfldkyti
      661 tgsarkdasn lfgvstnnkw tplwslgvnw nlakesfipd gwfdrlnirf stgysgnvdn
      721 smsalttisy ttvnsvwgid wpaaqianlp nrelrwekvs thnlgldfsi wnrrvsgsid
      781 lykkntfdll spfpvdpstg rsllimnvar tesrgldlql htqntvgklk wstdlvfayn
      841 nnwiretfed elnpvsytnl gslivykgam aygaysyqwa glnpengqpm gylngeasad
      901 yrqiasrent rltdlvlhgs arplyfgslr ntvtfrnvsi sfnltgkfsy yfrregldyg
      961 slielnngha dyyrrwqhpg delhtnvpaf vyptdsrans fyrnsevlve rgdhirlqdi
     1021 riayrldpvr agqtvllkna evflfgnnvg fvwranrlgl dpdvadgipl prsiaaginl
     1081 sf
//
LOCUS       WP_090631714            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090631714
VERSION     WP_090631714.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118370
     Region          36..104
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          117..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklirlstla fllllawslt prnvyaqher sptvtlnvtn itldqlfkql eattgyqfry
       61 tddviharrl ytydftnekl stvlnqiakd sgldykiqgk nitlrkgekk kvegkvtdae
      121 gtplmgvsvm akgtaytast nadgmysitv psgttlqfss vgmetlemey tgqprldavm
      181 tegavgleev vvvgygtqkk rditgtvasl pmerlemapn vnltqaiqga ipgvqvstss
      241 agaapsqsvm mrgrnsikas tsplvvidgi agglgdvnpn dvasvevlkd asaaaiygsr
      301 gsngvilvtt ksgkggdtki ryngyysmqr fanlpdimkg eefyrfkmer npeaftssel
      361 diyesgewvd wldlalrngk stqhnlsfsg gfketqyyis tgitdvtgla vnddylklts
      421 rinvdtkfkn wltvgtrtql aytdaggiap twdgdqgvfw mnpftkayde ngeltiypwp
      481 edtyfrnplm gtlaknides yqvvsnnyav vdfpfvkglq yrvnagirlg fsndatyygr
      541 ntqrglsnsg daatsrglsr nvvienivny nrefgkhsvf atglysfenp rsntnsvdaq
      601 gfpndfltwy sapqaelvvp gfsntetsll ssmlrinyay dsrylltltg rndgysgfga
      661 ktkwgffpsl avgwnisred ffgwndvvne lklrasigls gnqaisayet isrlssediv
      721 agsttlpgyv psklgqddlg wettrtlnlg ldfgilnnri igdvnfyksn tfdllldrti
      781 spiygvssit qnigqtenkg levsftsrnl ttenfqwett gnisfvknki vslygmlden
      841 gneiddvast wfigkpilvn ygykwdgvwq ldeaeeakay gtqpgyikik dvsgpdgvpd
      901 gvlspdydrv iigqrdpkyi wgmnnsfsyk nltlnvfihg vhgvtknntl lndtdvdqav
      961 rmtttkknww rpdnptnewy mntwnanlqd gksaapyeha gfvrikdvsi aydfaksals
     1021 rygigkcqly ltgrnlftlt rfggmdpeln gqrniplqke yviglnlef
//
LOCUS       WP_090631776            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090631776
VERSION     WP_090631776.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114728
     Region          62..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklnlrigeg yalskhklky ayiqyislla vatimclear aqspdhsgav ppgtdttsnv
       61 rdtitieevq vntgyqrlpk eratgsfvli dnellnrsis tnllerldgi tnsmlfdkrg
      121 akpriqvrgl ntltqhmsep livvdnfpye gdigdinpnd venitvlkda aassiwgara
      181 angvivittk rgafnkpgrv hfssnvtime rtnlfdrpep gpkdiiemek flfdngyfda
      241 qiadrtgfpa ltpvveilaa qrdgtlseqa amaelgrlse ddarrdfeky inrpavnqqy
      301 sagisggagn isyylsagvd knieelvgnt ydrvslrstt tyrpykkltv eiglgytehr
      361 dinnslggyg saaykfgsrt mpnyhslmne dgsansidrd yralftdtag ngmlldwkyr
      421 pldemaaqdr ssrsraltgn vavnyeiapf lvadvryqyq qtqrtdrdyy sgenfyarnl
      481 inlfsvpdgg emrygvpndg ildltttgiq shsirgqlnf kntyrlhsin afaggearqa
      541 mnaanmyrty gysdvlttsn vdyvnrlptf agiagnilvp nnawfsditn ryisvyanag
      601 ysfrttyhvt asvrkdasnl fgvkanrrgv plwsagvkwd iakerfyris afpylafrat
      661 ygyggnvntg msayttieyr saneqptnlp yaiisqrpnp nlrwektrti nmaldfreke
      721 gsvsgsieyy fkkstdvlgm epldptvgta slltnsahvn gegldvqlrf smfkrrpvhw
      781 dlstnfnyvt ykvtrylter smlgytssgg lispfvgynp yllvshrwag ldsetgdpmg
      841 yvggeiskdy rellrnpgee qvihgpalpp ffgniintlt ykqlalsfni twrmghytrl
      901 ssvnygnlfa tgdphidylq rwqkpgdeky tdvpslvypn psvnrdsfyg daeinvinss
      961 sirftdirls ydftiprlat nlrlygylsn lnvmlwkand kgidpeypeg llpnksiavg
     1021 lafdf
//
LOCUS       WP_090632566            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            indicus].
ACCESSION   WP_090632566
VERSION     WP_090632566.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter indicus
  ORGANISM  Parapedobacter indicus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Parapedobacter indicus"
                     /db_xref="taxon:1477437"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119462
     Region          22..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrcllvalcv itqcvyvygq vtvrgkvisa ddgvplaeas mhlvstgrsf ssradgaftf
       61 ritgtdtlvv thvgyttqri avngqtaslh iqmsrqdnll dvvevstgyy nvpldratgs
      121 fahvdnalln rsvsmdiisr legvvpglqf drrsvtgeqd ggpelrvrgl vtlesesapl
      181 ivvdgfpyeg dinsispndv esitvlrdaa aasiwgarag ngvivvttkq grfgqrakis
      241 lnsnwnigtk pdlhynqnrl psttvmdiek elfhrdtyee nprtvlpyyv elliqnrdgl
      301 lsdaalaeqe tmlrntdvrr ealdflyqse itrqssvnis ggsdtyryym saghdgyqgl
      361 lkgnggdrla lnmqntfrpv enleitggvw ytnqrrhtng lslndlsqsv gnsvspytrl
      421 adaggtplsi pyalrwayqq daenqglldw gfrpldeinl rdsksygqef rmngglrysf
      481 lksfnlhvsy qfrqgrsgse nyhapqtyyv rdlvnrftgp dgeqvipyng iydmnatqmn
      541 tsqsgrlqln yerllegnhr ivalagaeir gqiqerapgf rlynfdpdfl tgtntfdylt
      601 nypvrpegss ripapddsrl kyidrylsyf gnasytyrdr ytltgslrwd gsnlfgvkan
      661 qkgvplwsvg agwniaderf fpkdifsrlk lratygsagn vnkqvsafpv vsyslesrtq
      721 lqrglirsag npslrweqvn tlntgldfgf arnrisgsle yyvkkasdli gedylapstg
      781 sfyrltspip nrinyanmes rgldvqlsvg ilqqafkwnv ttwgswvvnk ithfnvrete
      841 nvsnylsnpp pvigrsrdvl yaypwigldh gtgmplvevd gvvgtdydaf vqgfgidrll
      901 vggvtvppyh galrntfswk gfevsanvlw kaghvfrrns mapgneyisa qtyhmdyfkr
      961 wqkpgdekht dvpayasvph nnrsfmyqns evlvtkgahi rlqdinvsys igraqwdrlp
     1021 vrnvrlyvyg nnlgilwran ksgidpdyvn aeyppsstya iglqldf
//
LOCUS       WP_090639182            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090639182
VERSION     WP_090639182.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115559
     Region          24..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllaslc flllcltqvh aqnrtvtgtv takddglpip gvsvkikgts sgtqtnaagk
       61 fslsvspgav lsfsfigynt qdvavgtkst ievvllsans qlnevvvtal giqrqaisvg
      121 ystskvtgkd itqakpisvt ngltgkvsgl qvtttnnglf aptrvtlrgn rslignnqpl
      181 yvvdgsifys distlnpedi aettvlkgss asavygsdas ngvivittkh gakgtsaltv
      241 sstyqiekvs yipeyqtrfg anggegevfd fskfvdeidg hynyypyenq sygpefngkl
      301 vpigrplpdg sselvpysav knqkkdffdt gittqhnfnf tsgeengsfy msgqdlhsks
      361 impkdegrrd vfrvggdkky gafstsysva ytyltknqtn tgavyndlie spvnipvkdl
      421 rdptskygnp dtyyndyyis pgqiinesry tlvenhiqan lqanlkvakf ltlsyrtsld
      481 ntsgrseakd agrtysdftk naetmiypnn sggldtvend gaghkyaand llpsygtsdy
      541 tnllfssdfl anynfklpad fkidgtlgva yldnkvtatt vnqgsinflp yntqnlssvp
      601 slseyslqar klgyfgtatl gyksyafihg syrtdldsrl ssknkyigyy didgsvvlse
      661 ifkdianndy lnfvkvryah sktgnasals ggsqyiafga yrtiptvgla ggfpysstgi
      721 sgyslsgtia npdikpetvt edevgldlgf lkdrltltas ayksttkdgi vtaqisrasg
      781 ftsallnaan senkgleldl hgtvissqav kwtlgvnytk qsskvisivs gvnelslggn
      841 tfavknlpya qikgydwnrd patgkvivda ttglpvrasa tqplgnvnpt dllgftssls
      901 ykgftlnlti dyrsgykifn aigstldhsg ngvtttltgr qrfvfpnsvy kdasgkyvdn
      961 tniltqdgny nffpttwlgv danyvisaaa wklreaslny nfpkawlrdv kfiknvnvav
     1021 sgrnllmfrp stnkftdpef nddtsnavgr ttlnqapptr iisgtlavtf
//
LOCUS       WP_090640086            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090640086
VERSION     WP_090640086.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119261
     Region          54..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 memrithtpy skwipgtill clqlvfslav fgqqksslil kghiklpdgl qlqvsvgspk
       61 ngytnsdsag nfsipvrvip dtlkfsavgl ktqyeviktp lsflnitmet atqmlnevvi
      121 ntgyqqvran eingsvsqin etmfnarpgt nilnrllgqs tglllnigks ngnpqnttnl
      181 sirglgting pldplivldg fiyegdisni npldvesvsl lkdaaaasiw gsragngviv
      241 istkkgrynq plaigfnanv ivqqlpnlya lnqmssadyi dverkmfnag yfddqinnsp
      301 yqalspavev mlaqrsgkis gsvanaqlda lskqdsrsay lkefythait qqyglnvrgg
      361 gsnykfllsg aydkvlsety aknnkfnigl tqefragknl tlsgrvyfts letasgrpay
      421 nslsvggril pylsfrdaqg nalplasayr gaytdtagng klldwkyypa ddylhnmvnt
      481 nrwdifastg lkyhltsfln fdlsyqyqrq ydetvslsda qsyqarnlin tytqlnpttg
      541 iltypvplgg iqtlslgnvs sstargqfnl nktlgqhslt aiagaetrsa ktdgksaawy
      601 gyngdpltys nidlvnaype fltgnysqvg sgnnltatqy rfvslyanaa ysfkkrytls
      661 gsarrdgsni fgantndrwk plwstglgwl lsgepfyrld wlpelrikat ygtsgnvdlt
      721 rtalpvasya tnnvtglpit rissinnpdl kweqlsqwni gmdftlkdrr lqgsvsyfvk
      781 hgtnlygpal ydyttwggsq elirniaemk gygvetelha lnlqrssfrw qadiyfnfnm
      841 sktvtynnsy ttglynilas gtsitplvgk plyaiavykw agldaagnpr gylngkpsid
      901 ytamaleass sgdnllyvgs atptyygnli nsffwkgfsl sfnmsyrlgy ytikptinys
      961 rliangtgns dyalrwqkag dealttvpaf vypanqdrdy fytasqpnvi kadnirldyi
     1021 nlgyrldlsk mklpfrsvdl yanmqnvgii wranhlgldp dylntlspvr sltfglrsnf
//
LOCUS       WP_090642530            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090642530
VERSION     WP_090642530.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118121
     Region          24..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllftslc flllcltqvh aqnrtvtgtv takddglpip gvtvivkgtt lgtqtnaagk
       61 fslsvpanat ltfkfigykt vempavdpit vvltsvsnql gevvvtgafn tkqtsrsisy
      121 aaqvvksdal ntirqpnvnn alagkvaglq irsqsvgalg rntqvrlrga tgfgnssgal
      181 yvvdgtilpn sddlnpddve nitvlqgpaa saqfgsagan gaivittkrg gkvkgvgiel
      241 nagvnfdkvy ilpnyqntya ggaaadlmqy hykagdpegw kaldgkfypd ytddsswgpk
      301 mvgqeyipwy awapgtkysf ktaslvaqpn narnyfetgt tlnngiaftk saddynirms
      361 ynnqhvngiv pytalmknvf nlnvnydlgk hftvganvnf vsqkvhgnis dgyanastgn
      421 fnqwmhrdld mgimkelkdl tspdgtlvsw nhqnptsyta ddpgyfyagn ywynmykiae
      481 lntkdnqrdr fygnvylqyk lnkdfnikat yrknsrsewq eefipailqk sgsqtgvkny
      541 yrtynvyenr enyellanyn kqiadfkidv nagsdiynrs ykdnggntvd glsipdlyni
      601 tnsvsapsvf ntrtneqyra lfakatlgyk nflfidgtvr ndwfsslfpq dnsvlaksfg
      661 gsfvfsellp qfnnwlsfgk vrlsygetpq alatatdnyg gyrnntvygv nqykfgtnil
      721 mntpdqsvdp alhgavfkqt evgldlrfln drlglsatyy agtdvdfpas vtvnpasgfs
      781 siltnfgkiq rkgieltlsg tpvrinnfnw dvtingarql qnkvvevskk ygvtrytnps
      841 dqvwgtdmpy mvfqegkewg qiygngikrn aagvpiiaan gmyandpnvy fgsvlpkwtg
      901 giqnsftifk sfvlnanidy qvggkfvsls nrwgqfsglt aataalndkg vpvrdpvadg
      961 ggvkvsgvda dgksvsnyid aktyfqgltn nktydsyiyd ltfvklrevs igykipvakl
     1021 glgkviqsar fditgrnlll iyakskdydp seissqqget gqlpgtrglg fnlkvtf
//
LOCUS       WP_090642553            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090642553
VERSION     WP_090642553.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114171
     Region          27..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlknykflla illpffliqt vaaqsvkisg vvtaksdglp lpgvsvavkg ttngaqtgad
       61 gkfslnanin dvlkvsylgf atqeitvkqa etnlqivlqd apnslnevvi talniskdkk
      121 tlgysvqglk skdiseaket nlvnalagki agvqvtnsqg dmgssriiir getsignnnq
      181 plfvvdgviv dnsqflgtng srdfanaiad lnsediesvs vlkgpnaaal ygyraaagvi
      241 liktktgkga kglgvtinsn tsfstvnilp yyqneygqgs ngkfsyvdgk gggvndgvde
      301 swgpaldgsl ipqfysngqa vpfvahpdnv knffntgvtl nngvalagns dkadyrlsyn
      361 nlhqtgivpn tsqgrnsfll nstfklspkl tvttianyik ddadnlpgag grratstmlq
      421 ftwfgrqvdi sqlknykdan gntfnwnnsy ysnpywlaye ntvgqhknri igsvelnyki
      481 ieglsanfrt gtdyyndrrk ikvaygtngt pfgsyeeday tvnetntear lqytkklnnd
      541 fsldvlgggn istilneqnd qvapklavag lytlsnsrdp lvssnyygkl ktysyfasaq
      601 igfknyafin ltgrndwsst lpaanlsyfy psvngslils ealdiksdil tyaklrggws
      661 kvgkattpyq linyynftap fgsnpqqslg tvdlnsklkp etttsaeagf elgffqdrvh
      721 ldvsayntns inqivtvdvs pstgysqkli nggsinnkgi evqlgltpvk skeftwditt
      781 nyslnrskvv klddegrlqs iilgsdrtvq vlaalgqpyg tlygnaytrd asgqivigan
      841 gtpvinptkq ylgkftpnwl gsinnsftyk rinlgflvda rfggsiysnt nrtgtytgvl
      901 astlpgrgaa nggisyyypg nnasagavqv sgnapagvtv yndgmifkgv kadgtantti
      961 lpaqsyykgf tnvdeafvyd asyiklrevk lgytfpsnwv ksvglqsatl svvgrnlwii
     1021 hknapnidpe tafnngngqg ledltlptvr nigfninlkf
//
LOCUS       WP_090642720            1007 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090642720
VERSION     WP_090642720.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1007
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109562
     Region          30..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkqllkkf ilplvalfvf clnanaqtvt vkgkvsddkg lplpgvtvrl kgtnkgvstn
       61 ingaysisyp gtgtlnfsai gyipkeiklt gqteinvvlp ednqaisevv vtalgikrdk
      121 rvlsyssqev kgaelvqgkd pnivndiagk vsgvqitsss gnpgsstriv vrgassfygd
      181 nnalmvidgi pidnsetgnl nsgpgtsria dldpnivesi nvlkgaaata lygslgangv
      241 iiittktgsa gkkatvsfss dfssenpllp qiqskyaqgt ngqfydgttl ktstswgplm
      301 dtlkingqaa kkynqsdlff ktghtynnvv singggeasn yyisysnfnq qgtvpttsfi
      361 rnslfakyga kilpnltttf qlnysnsqnd rlpegwales pvwtiftapi synllpyena
      421 dgtqrlyrys rnnpywvlnn isnksgvnrf mptftadykp lkwltvterf gadvyveqdk
      481 yhesansvsn pngrivvnna nfrqinndli isgnhqfgdf nidgvlgnni fsqytensya
      541 ngvglsvadl dnissastvs yseshalvrr igfylqtnid ykkflilslt grydgssvls
      601 tsnnfypygs aaasfifsef fskdfqdvmn lgkfrvsyat vggsnvgays lttpyysqti
      661 rnitfpyqgq sgfllsstlg nsflknerin efeagfetgf fnnrisleas yfakktvdgi
      721 ipgvsiapst gysgttvntg vmqnkgiell ltvvpvktrd fnwsvtmnft rtrnkvlnly
      781 gdlqqlgngf tslivgqpyg iiygtryarn aqgkllidag glpyaddtqg iigntnpdwt
      841 ggfssnlryk qfnlsfffdv kkggdiqnnv dgygyfygtp kvtenrgprv vdgisattgq
      901 pntisvngqa yyqringite sviqdgtyik lrnvsvgytv kplwlkstpf ktlnfsvtgr
      961 nlwiyaphft ggdpevssfg asngaqgiys fstptsrsid fslkftl
//
LOCUS       WP_090644100             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Asticcacaulis taihuensis].
ACCESSION   WP_090644100
VERSION     WP_090644100.1
KEYWORDS    RefSeq.
SOURCE      Asticcacaulis taihuensis
  ORGANISM  Asticcacaulis taihuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Asticcacaulis.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Asticcacaulis taihuensis"
                     /db_xref="taxon:260084"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38384
     Region          3..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgltlavtte qtagetrvaa tpdtvkkwtt agltvniqsg aglgasvpdd aftaagativ
       61 ktakealkaa divlkvrgpa kdeiaalkdg aiviatldpy rekdtlnala akgasayame
      121 fvpritraqv mdvlssqanl agyravieaa saygkafpmm mtaagtvapa kafimgvgva
      181 glqaiatarr lgavvtatdv rpatkeqves lgakflaved eefknaqtag gyakemsaey
      241 kakqaaltas hiakqdivit talipgrqap ilvtkemvas mkpgsvlidl aapqggnveg
      301 cvadkvvdvg gvkiigfsni vaaiaadasa lyaknlqafv gllidkdgnl apdaedeilk
      361 aalvtaggav vhpnlkga
//
LOCUS       WP_090646308            1132 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090646308
VERSION     WP_090646308.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1132
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124695
     Region          72..138
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          167..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mykkdltwpf calskrlihk qhsgkaasia lnikralfng rpaqffllav fimlscpava
       61 qssaekiiti afnnvsleng ikllekqsht kfvyndklld kkiilnqsft gqrlsavlnw
      121 irdkyginye iiddqfivlk ssrplplptg ppatgarqps ltgfvqsgvv kdengepmpg
      181 vtihlnnaan gaqtdshgvf nigipndesi liftfigykt aerkatrnqe mvfllepdpa
      241 rldevqvigy gtatrrtstg sqaeisaqnl mntpatnpas aiqgrmagvy vsqgnglpgs
      301 pmtftirgtn slagsnnplf ivdgvpylad aissmdaang atsplnsinp adienitvlk
      361 dadataiygs rgsngvvlit tkkgkqgdtr veglvkhgvs kvnhfvktls tpeylairrk
      421 ayantgidpa tdaafdltrw dqnaytdfqk lligntahtt danvalsggd altnfrisgt
      481 hhlegnvftp dqgykrssln fnlghksfdq kfevnlsaiy sadendisvl dqtsaayylp
      541 pnfplhnpdg slywsgvayg vprnplgqln qvqsnkgsnl isnmtlayhm vkgltfktsl
      601 gfsrsdmdqk rlspkssmdp gisynvsgsm faynvsnnyi iepqltystk ismgelstll
      661 ggtwqyqssr tpyytlatdf psddllenla saqnvstssg ssqykyvsvf grvnynweqk
      721 yilnlnfrrd gssrfgpdsr fgnfgsagaa wvfteekfak afplisfgkl rasygvvgsd
      781 qigdyqflds yvsvpyvyng atglvpsria nptyrweqtr kleaaidlsf lkdklsftaa
      841 fyrnrtgnql vsyplsiqag fssyqanmpa nvenkgweft lssqniksss frwssefnis
      901 fnrnkllsfp niqntsyysr yvvgrplssv ylfkytgfsp qtglptfadl ngngtinfgf
      961 aetgrgdryf agytqpnyyg glsntfiykn itldflfqfv kqkgrsvlsq sfyppgmmyn
     1021 gaakpvlqyi naglpgqpqi tstynnayna ysnyvssdai ltdasfvrlk ninvaydftg
     1081 dwvkrmklqk lrlqlqgqnl ftvtnylgfd pesqglnvpp lrtivgviqf tf
//
LOCUS       WP_090646668            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090646668
VERSION     WP_090646668.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118693
     Region          24..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiiitmmv ligyalpira qyiikgkvid avtkqplqan ikfklakyst vaendgsftl
       61 gtnvendtli vsclsyfpri ipikghkaap llilleehly qvdnvvistg yyqlprerit
      121 gsvtqvneka lntsvstdii srlkgvangi sfderipder klnirgisti ngdtqplivl
      181 nnfpydgdin sinpndvesi tvlkdaaaas iwgvraangv ivintkkgrf nakqeisfns
      241 nisveqkpdv yalhtmssad yigvekflfn ngfyasmevd pahpalspvv eqlianrdgr
      301 lsndqlnasl nalgkldvrd qfnkylyqks inqqyalnln ggtatgnyfy slgydhninn
      361 laarysrfsf radnnftigy lkvnpvisya rtsqqggrps yiditpgsgk glypyaqlad
      421 asgnaipitk dyrvgyadsa eskgllnwry rplqdfkerh tqttgndlla glnldygfgk
      481 yltaqiqyqy ewstndlsdl ydsssyytrd fvnrftqddg sgnlsfpipk ggilytannt
      541 lksqsgrfql kysntwdknd lailagteir dirqagnsht tygynpsglt stpvdyttlf
      601 pqyydpgnfq gipyrnnfig ltnryrsyya naaytydqry tlsasarkde snifggnann
      661 kgvplwsagl swnlsnerfy pggvlnylkm rvtygfngnl pqnltavasl lqdngnlnnq
      721 pfaiistypn pdlrwekvav vnagfdfgsr nnvltgsvey yhkkasdlig rqpidqtvgi
      781 pdgfitrnva dmnangidiq lngkivdrlf kwttgllfny nkdkvtqynn sstigsffin
      841 gglgiapvvg rpvssifsfk wagldsqtgd pmgivngqps kdysaivyqt elkdlqyngp
      901 atppyfgnff ntfsykgfsl yvniayrfgy ffqhpsisyy ylyhngnghs dfaarwqhpg
      961 deskthipsm pgvdnnsyer dyfysyssal vekgdnirlq dlnlsyspkl ngwkrfpirg
     1021 lqlyayarnv gilwkankag ldpdyasgyl ppsltlsfgl kasf
//
LOCUS       WP_090647893            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090647893
VERSION     WP_090647893.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115226
     Region          23..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkffllfsi lliissmlka qtrtvtgkvv ssdkneplig vsvqvkgsta gtttdtsgry
       61 sikvtnlqsv vikvqyigys fqektlnvge mnadfkmvpt ssnldevviv gygtqkrshl
      121 tgavetvdmt kiqdipttnl aaalkgtnaa vgvsggtarp gqnasitirn piflakdggs
      181 tdplyiidga krtlsdfnll dqsevenisi lkdaaaaiyg iegangviiv ktkrghsgqp
      241 kisfsasags adavqlpkmm sglqlatwln dyeqglngfn itpdgyiggd ltkkdlnyyt
      301 pdelayfadn nnnflkqafh palvergavn vsggndkvty faganyvnqn snfsgvntnr
      361 fgfrgsvdak ltqglklsls lsedvsksks ywyklsgtse sldndflsln qappwqqyfi
      421 dghpvylssr tatdninffa vqnsnnytss nnyimnalan lsydipgvkg lsanvsynrn
      481 innnfskqyg tsfvyyqysg tgsnnhipgg tivgtptikn gdrvrltpsi tdnyqfnvsl
      541 nynrifgkhe isfialyeqy etsfegvnae adgvilngkd nqnfttgaqs snqassiseg
      601 gkqayaarln ygyadkylve lslradantn fppgnqwgyf psgsvgwvvs kedffknvsf
      661 vdffklrasv gslgsyntka yqyavnykig tgsgggavfg gnnadkgigl ttniaianpd
      721 ytwdhdtktn ygidlrflnn rlsatadyfw dhhynmlasl nssvpvtvga tpstenygsi
      781 ntfgyevsvs wkdhigknwt ynvspfftws dnkylkydla sglagtfqdl tnksgdqgtl
      841 gykslgiirt qadadaiiae rataaggagn vtimsqavkp gmlnfqdlng dgiidskdlq
      901 flghksnnhy smgfnfggsy kslslnvimg lswggtasie gaatkqatas enrpvfwadh
      961 wtptnteaky papyyyqtya vttdfwfvsp vtwnissanl syalpdnisk klgmasvray
     1021 vvatnpvsfl npypnsyrsq stpftsypnl rtisfglnlg f
//
LOCUS       WP_090649079            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090649079
VERSION     WP_090649079.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113468
     Region          42..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maycylkkcf tgfvilmlml vktgyaamqd ttgrgsthpg wvsgvvldey anplngvkvm
       61 vkgktdasft dkdgrfeina vsgdklvftm lnyytsevni sskspvtikl ldtylktpet
      121 invlygtkka aanlgsvaai ytnqltttpa slytyalpgq lpglytqqys gfaspqtstq
      181 tvadfignvv qhnnysandn teiglslrgq tpitiidgvq reissidpes iesvsvlkda
      241 lsnillgins srgvllittk hgqagapris ftaeagsqhp ldlpkplpay qyaylyneal
      301 qndgkptiys addfnayrnh tdpahhpdvn wfntllrnss pissyklnvn gggsvaqysv
      361 slnymdqqgm fktspaatyn tnnelsryii nsdlsvnvtk kftvdlqlfg riqqatqpgt
      421 gysgilntly ntpnnpypvy npngsfggtt lftnnllsqs qfsgyqrtns ndvmanldln
      481 ydlssvtkgl svklkgnlaf esqglvnrsl qnntyllnkd ssysavgtpi sqsngfatvs
      541 sarysfaqaa lnyerqfgkg tvsgmllydt rsvvlnydls gvttnraakl gynydgkyfi
      601 easanssgyn ryppgnqygm fyavglgwqm gqerfikdis wisswkwrat ygktgnanvd
      661 nfgyynflqt ygtsigypyt lgtarsviqs ynentlanpy irwenakkld igtdislfkd
      721 hfkitadyfh drfydllqtr gnsiallgtt ypaenigvkl ykgteltlty qdhagnlnyf
      781 ltanatrqts tnvfsdeepa pypwlrrtgl sndvifgyta lgffknaqda atsattvgyt
      841 pqagdvkykd lngdhvinqf dqsaiantkp liyyglsfgv nykgfsvsvi mqgvtnhqii
      901 ynnnlvngfa glglfgniyq gqgydaltgr wtpetadiat lprlsstgnv nngllstlyi
      961 rsanymrlkn aevgyslple warklrlsgi rvfangenly tfygykgvdp evyglaypiq
     1021 rvfnaginik l
//
LOCUS       WP_090650885            1149 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090650885
VERSION     WP_090650885.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1149
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124674
     Region          70..123
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          142..1145
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkfdfstfl kcccfllvll gqsvygyaql altsnnrfht kapgyamqqv aenkvllkda
       61 lenikkqfnv qiayqeglld nkfipvslfn nakqfnlden lkqllaafql eyrkindsqi
      121 siysirettv ntapvvaavl igkvvdekdg lpvigasvyl kadpkigtst dvmgnfklvv
      181 pdkftgkplt llvayigynk eevtvtdlts pvqiklkqnn stlnevvvta lgiskqrksl
      241 gysvtevkga eftqarennv analtgkvag vnaaglstgp ggssrivirg ngglagdnqp
      301 lyvvngmpid nsvpggaptv ngitnnvdrg dgiaalnpdd iesisvlkgg taaalygsra
      361 angvilittk kgrvqkgvgi eynstatydn vavfpdyqye ygqgdggvkp ttlataqgtg
      421 rrswgakidg stdyvavdgk thpytaqkdn lknyyqtgst ytnslaflgg neaityrfsa
      481 adlnskgilp gttydrktfn laltskltnk isiealaqyn ietghnrtga gdalgnpnwt
      541 plevantvdi rwlkpgydan gneqvwndaa iasngyfvin kfkeddvkdr figqgsvsyt
      601 pitnlvfkat lsrdffnyny snilptgtly vpngqyqsik sdvsetnelv tvsyktkivs
      661 dfngsvlggv nsrknitnqq tvngsqfvip yfysstnlat tsttpynaki vtnsvfgsad
      721 fdykslvfls ftgrkdwfst lssknnsify psvggsfils davklpqfft laklraswaq
      781 vgggapdpyv inltysnvps agqplqnvts nnitnsalkp ytsttteagl elqmlqnrlg
      841 idvtlydrkt tndivntais stsgynnvil nvgevrnkgi evalngspvk skefswnvny
      901 nvayndnkvv klapglstiq matsvngyal lnntegmsfg tlygthmvkn ssgqvvfnat
      961 tglpvqsaye plgksvaplt mgltnefryk rfslnflldg kfgnkvfslm evyatrlglm
     1021 kstlpgreng lvlngvdqtg aaytrtvpvs glrtyydnyk iysdlfthdg sfvklrqvil
     1081 synlpgldlk kihiqsasis lvsrnlwtly kktknfdpee sftnsntqgf esiglprtrs
     1141 lgvnlavkf
//
LOCUS       WP_090651147            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090651147
VERSION     WP_090651147.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120330
     Region          29..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkfyqrlkt vitvllfcia psillaqski sgtvtdenhl pvpgvsvrik dqnrgtvtdi
       61 egryiisasa gqtltfsfig ytpqnivvad knvinvslng dnkvlnevvv talgikketr
      121 rigyaiqtvq gdalttardp npitgligkv agvsvgpsae llgnpnvlir gsqvslyvvd
      181 gfpintdtyn ispddietyt vlkgpaaaal ygsraqygai littkkgakn kkgltvdins
      241 stvlnsgfla fprtqnsfgp gentfyefvd gkggapggvd gdydvwgpyf ngqlipqyds
      301 pivngvrqgt pwtargkdnl knflkvgsqt nnnvalgvvg dtyttrfsvs qqhqtsyips
      361 qylniananl yasftptpkl tfegnvdfnr qstdnfpdvq ygpnsiiyni siwtgadwdi
      421 napdikaiwq pgkvgvqsqf eeyqryhnpy lltqkwtrgh ykndtygylg gtykfndnln
      481 lrlrsqidty nilrtedlpf sahpygregn qgdyredrrn lfdnntelil nynytvknfl
      541 nlsglvgsnl rtmsynsswv stdylnvpev yafsnsknpi qatsfnaser vlsfyasldm
      601 sfgkyatlsg tyrrdkssaf qnattynyps vsaatvisdy iklpeaisfl kargsyanvr
      661 advssptigp apfssitafg gstgpslfnn plgygstyts pyngpdysln psystskpyn
      721 nttagyatns lyinniktst rvnyeegfdi kflqnrlgls atafqyidgp rvfasqista
      781 tgyttlylna lktkrsgyeg slegtpiknl ggftwnvlvn vsnnkevyke lppgqngtyl
      841 nyysvgdrtd ilrgskflrt kegqiindaa gkplsvggqv lghenanynw siankirykn
      901 fsmgfqfdga vggviidymh nktmrggani etatgtlgda ryqdwknfgv agyngtyvgp
      961 gvnvsngtai nldsktgail nysalqfsqn kqtalvqdyv skyynvdesn lmdktfsklr
     1021 evtfsydfpk awlqksfiqk isaslygrnl lyfykdkrfk dvdldqynga qaqtvlqspt
     1081 vrsygfnlnl sf
//
LOCUS       WP_090651178            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090651178
VERSION     WP_090651178.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109173
     Region          27..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqfkhllkvc ffaviylfsv pvmaqnkiit gkvtdkkdgs pligvsvkts ltspggaitn
       61 tegeyrisvp gnatvlvlty vgyvsqtvni dgrttinvtm dasskalnev vvigygsqrv
      121 kdatgsvasl stkdfnkgvi atpeqllqgr iagvqvtpss gepgagatin irgassirss
      181 nnplyvvdgv pldnggtagg ydsgagsssa rnplafinpa dienisilkd assaaiygsr
      241 gangvilitt rkgrkgagiq fgastsvsna akrydllgre dflkavasvg adatsvdykg
      301 ntnwqdqilr taisqnynia fgganntgny rfsagyddqq givkktdlkr fnarlnasqs
      361 lfsgrikfdl qslysnvkdq fapitnnagf ngsligaalq tnptipvydd kgryfdingy
      421 ddqgfpknns frnpvsmlnq iddrdninrf lnnltltvrl vqgltykgni gvdlsrglrk
      481 tfydptivgf tdqtnirdfn vpsatgngrg ilqhteltsi itehtlnyek kfsdnsslta
      541 lagysysnyk nysrndfgwg tatsgqfvkn yndfknhlay pvgdsssyrl qsffarvnys
      601 ykdkyiltgt lrrdgssrfg nnhkygnfpa laakwrisne sfapkgifdd lslrlnygqt
      661 gnqefpsyas lalrqlnyyg tsstplnaan pdlkwetqta ygagidfsil ngrisgtvdy
      721 fnksqknllf lqdlaqpaas trywvnlpgn vrntgvevgl llqavqgkkf swdinynmtf
      781 vknrienfgn rnvitgnidg qglsgayaqf fgngyplyef nvsqynglda ngfgiypngi
      841 daatphgspl ptflaginnt ftygnwmlsf flnaqtgfyi ynntanaffy kgnlvsgrnv
      901 tkavastnen plnsgevssr flekgdflrm snaslgytfp vkrmaikslr vavtgqnlfl
      961 itgysgldpe intnkerngv psrgidytsy psartftlsl nasf
//
LOCUS       WP_090652019             981 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090652019
VERSION     WP_090652019.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..981
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106927
     Region          29..980
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknyskkyv llcaflmmsv mafaqtgsik gkvldetnap lpgaavtidg ttigattdgn
       61 gnytitgvkt gnvtvtakfl gyvalkkavt vgntavevnf slkpdnqnln evvvvgygtq
      121 kkkdltgsvt sisakdfnqg pvttpeqlit gkvsgvqits nsgapgsgst irirggaslt
      181 gsndplivvd giplsnngis gvsnplslin pddiesynil kdasataifg srasngviii
      241 ttkkgkdgkl hidfdskssl skvtkevsvl sadqfrtavk aqspgqasll gtantdwqsl
      301 iyrpaytydn nlsitggikg lpyrlsvgyl dqdgivktdn lkrttvafni shdflhnslk
      361 vdlnlkgsht lshfaagaig naiafdptqp vysndkskyg gyfewldgsg npntlaprnp
      421 vgllnqqdaq gratrgigtl nvnytfpflk elqfnatvgg dlsdgkgytf ipasaasnfa
      481 qggsyshyfs elytyntdyy lkytkdfkei kshldlqagy syqyfnsyyr tfqgykadkt
      541 tpvgsaasps ygqyyiespf arlnyafnek ylltatirdd rssrfselhr ngyfpsvafa
      601 wrakeesflk gvdflsdlkl kagygitgqq dggdyfpyla vyepsntaaq yqfgstfvnt
      661 lrsdrynanl kwestattnl aldyglfngr vngtiefynk ktkdlliytp ipagtnlsny
      721 ilanignltt kgvdfninvi avatkdinwk lgynlslnkr kitnisltsd pnqtiavtgi
      781 pggvgntigl ykagqspsaf yvyqqvydqn glplegvyvd rnkngsssdd kylykqsepk
      841 afmgfnsdfs ykqwnlgfsa ranlgnylyn aqsaangaya glkfsgylgn lpssvlqtqf
      901 qqyqlysdyy venasfvrmd yatlgytfhi kgthnlrasf nvnnvfvitk ykgldpevng
      961 gvdnnfyprp rvytlglnls l
//
LOCUS       WP_090651841             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090651841
VERSION     WP_090651841.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106697
     Region          30..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvylfkyg ltvlllisai asfaqkgafr gkvvddlnqp lpgatvhvkg asqttvtdan
       61 gmfsltgdtq qaltvqitfv gydvlervik anenptfqlv psskaltevv vmgygtvkks
      121 dltgavatig akdlnpgsvt nplqqlagka agvnitqvgs epgvaptvri rgltslqggn
      181 dplvvvdgiq gnmdllnqvp pseiasidil kdasataiyg srgapgvili ttrktaagks
      241 sveytenssl dviahklqel naaqwtaqae kqgvdvsanh gsntdwfnll tqngvtqnhn
      301 lafgggtngf nyrasvsait qtgivinsny kkyigritat qkalddkltl tmnvnsginn
      361 dvyspigigr aaftsnlisn tyisrptdpv fntdgsyysd pnvfqyinpy avaktvkndv
      421 ntnnlftslr gdldiykgis agwfgswrks dtntgyyapv astiataidn kgianisnnh
      481 vdeklmdisl sykhefglsh fdasaiyewq aqtyngsfaq grgfvndfat ynalqlgdis
      541 kvlqgdissy kndrrlisyi gqihysynnk ylltasirrd gstvfgvnnk wgnfpsaala
      601 wridqedfmk nqtlfssfkl rvgygvtgnq qgitpqnsia lvgqagsvff ggstipnyfy
      661 tqnanpnlkw etrkqanagf dfsmfndrln gtfdvyratt dnllyhytvp vvgqffvnni
      721 lanvgslrsq gvelslsymv iksqdmtltl aangsllqsk vlklggniqg fdvptnyvgw
      781 gpnaylvvgk pvgtflilkh lgkdansaet vvdrdkngti dqgsqskdry eegqslpkyt
      841 yaftpsftyk nfdasmvwrg sggnkiyngl rqdlsllenl gksnvltsav plgiqsspyg
      901 sdlwlesgsy lrwenlslgy rfnlakvkyi salrlsvtgq nlaiitkykg ldpevnvsgd
      961 sssggdygty prtrtfslgl nvilk
//
LOCUS       WP_090651503            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090651503
VERSION     WP_090651503.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116386
     Region          26..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksflknlm gillalfcqy ayaqnrtitg tviskddglp ipgvsvvvkg yktgtqtsat
       61 gkftlstsak attlvftfig yetqevtipe ngivavtlkn dfkllsevvv tgsgvatskt
      121 klgiaveavs gkglaqtpqa sidqglvgkv pgaqisavdg tpgartnill rgintiqggt
      181 spmilvdgve srvtdislld patvdhlevv qgaaastiyg aqgangviqv ftkkgqsgka
      241 rvdisssvta sdyinsgdvh qaklssfltd atgnfittsg skivlnedgi ypgvrwqyqs
      301 dannptamsn plniarqqyg tnlkyydhlk qlfrtayttn ynasisggtd ksdynltisn
      361 nhqqsnirtn gyndrtnltt nlgtelfkgf tirnitqliy nkntlnpamg ngnsgalyav
      421 lnaspfydln qklasgdypl slnsgsvsvn gsnpfyfsey gskidnrvdv lenlqanyki
      481 nkfvelnaky ginysheean ylyksqtenq nsidtkatyg ayggeldknt yttvfqnfng
      541 satirtdfek dfhinvpitt stllqydyrk nnykqfftqg iglpsyaiyn fgqtstqavt
      601 sdytepfvtf gyvvnqkidv geyggvsggf rsdyssafge gskpftfpnv ngylrvssfd
      661 fwknsklgal fpewklraay geagiqpgpf dryptvstgn lgsalvftip angrnpalnv
      721 evskeyeygt dlaikgmdgn wlsdfslsat ywrrkgsnvi ynvsvapstg ssqiltnaid
      781 lsshgvqasl nisvlktrdf nwgfttnfsn etskidning ppiilttaag stqealvagq
      841 kigqiygfka ltsltavnhe garyisdadl gsyevvngrv vnkttkaiqf enevsplgdp
      901 npkfnmsfin sfsykklsfg fqfdwvhgsh lynqtkewmy rdgingdydn avtiggqsga
      961 ytayyrsaya dffgarngar ngtkdyfyed asflrlrnvs laydfsglik gkifrkailt
     1021 ftgrnlftst kytgfdpeis sggsnsafdr gvdhssmpnv ksyqvglslg f
//
LOCUS       WP_090652625            1121 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090652625
VERSION     WP_090652625.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1121)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1121)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1121)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1121
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1121
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120692
     Region          33..102
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          130..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvsitvvvc slvccqllla ktaksqisat lvkisfgkes lqssisklek qtgikfsynp
       61 edlkgysvkp nkfkeeklsn ilnylfsktq ltfkeisdgi viydktatlk tslftdkssg
      121 pdiktesadi tvtgtvsdln gplpgvsvvi egstkgvitn tngayslraa pdaalifssi
      181 gyktqkinin nqtvinvtmv sdlrslsdvi vvgygvqkks ditgsivsvn eqalrdipaa
      241 nigqalqgqa agvdiqksag nshpgatpsi lirgtrsina snsplivvdg lpfngslndi
      301 npddivslev lkdasstaiy gsrgangvll vstrrgkkgg tsitysgyag fnkpmghynv
      361 mngtqfedlk kwglingnpg kysglddpaf ltdgsfapqe vasiksgrst dwqdliyktg
      421 fvtdhqlgvs ggndltqyai sggyynetgi yfgqsfvrya iklsidqqlg knvkiglssl
      481 ntlsytngen anplgqalra splstpydda tgqlvgftag sanqvwnpla nfvpgavaet
      541 rkrfgtftta yaeinlapgl kyrfnggaei rpdiygnyya sattnnlgga stannqstys
      601 ynytlenilt ydktiaqkhh inftglyslq esqsqsnsfs ynnilsdgiq yfnpqyganl
      661 sgsgsyskwd iisymarvny gfankylltl tmrsdgssrl apgnkyhvfp saaaawnitq
      721 epmfkdshvl snlklrvsyg tvgntainpy qtlgaltsvn ynfgstnltg ayptnvpnpn
      781 ltweytstln agvdfgfldg ritgavdayh qytrslllpl slpptsgipn siltnvgqtq
      841 nkgieisvss vniqgngrns fswttsanit fnrgtvtkla sgvtqdiann lfvgqsinai
      901 fdykkvgiwq ntaadtaqak slgltttgtg svigtirved vnkdgkisas drivlgsdqp
      961 kytggftnri aykgfdftvv gvyrvgglit srlfqsggfv ntfqgnynnl nedywtptnh
     1021 qnfypkpnsa stntpyssll syfdgtflki rsatlgyymp esitkrikak slriyataqn
     1081 pfilfspyrn tfhgldpeta gslaidtppt ksfifginmt l
//
LOCUS       WP_090652704            1142 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090652704
VERSION     WP_090652704.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1142)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1142)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1142)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1142
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1142
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126580
     Region          69..118
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          134..1139
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkltflynav cairkvkckf llvlklitim llvgvmhvsa asyaqtvsly gknksletvf
       61 keikqqtgyl ffynekvnik gktanlnvkn vplaealdic lkdnglsfti idktiviqnk
      121 vaeektgnii nkvqvsgqiv dsvskatvpg vnislkgskg iigqsngmge fsvmadpgqt
      181 lvftfigyks aeikvtaaav itvkllpdin nikdvvvtgy qvikkdnytg naitvsgadl
      241 irnnpqnlik siqsfdpsfk vlddnligsd pnklpkinvr gataipsind dilnrnnlss
      301 nynlpafild gfevslqkvv dldinriesv tllkdgaata vygsraangv mvittkapva
      361 grlqlsynyq ltfngpdlsd yhvlnakqki dyeqlvglys astsssgdtk qadldaqlft
      421 rlknvasgvn tywlsqplrn ayqqkhtvya qggdqsfryg idlryqtqpg vmkgsdntry
      481 sggvdftynp nsrliirndl titqvnqans pygnfatyvn anpyfpmrds tgallqelan
      541 wrintgrqgn dqyitenvfn plyeaslssf dksayteile sfsadykitt glrfkalmsv
      601 nktnssadhy vsplsnafyn tptdklnnrg tydyannnnl nldgsttiny nrqigdhffn
      661 lvlganiiaa ksdaksfsae gfsndrfsni gfariykens gpggnviksr tagsffsgny
      721 syknrylldv sarvdgssaf gadkrfapfw svgagwnahq eaflkgsdvi sqlrlkgsia
      781 tlgsisfpay qsrsiyqyqt snwystgiga tilgygnsnl ewqktktyda gidlglfndr
      841 ivispryyyk ltrglitdin lapstgfsty kdnlgdmsnk gyelylvanv frtkdwnvnl
      901 tgnlahnvnr ivhisdalka fnsnidnfqt ntdnnafsip ltryvegksl ntiyavkslg
      961 idpengkeil vkkdgtltyt wdvkdiqdvg nttpkaegff gstvtykrfm lsfsfhyrfg
     1021 gqafnqtlid rvenadprfn vdsrvleqrw kqpgdhtffk niadlsdtyv ssrfvqkdnl
     1081 ielqslylsy dfnpksihrf glqnlrfaat andifrasti everginypf arsltvsiqg
     1141 sf
//
LOCUS       WP_090652882            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. OK283].
ACCESSION   WP_090652882
VERSION     WP_090652882.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. OK283
  ORGANISM  Mucilaginibacter sp. OK283
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Mucilaginibacter sp. OK283"
                     /db_xref="taxon:1881049"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116060
     Region          28..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkyilfyvv livciicsad tyaqtknitv sgkvldkpen kvlvgvnisi dkkgiaqtda
       61 ngrfsitvpv nsvvsfsfig fvtqklkvee nqkdiiitls edkkglneiv ivgyqnrske
      121 tttgasaiit nkdiadipvs sfeqllqgkv aglniqnntg apgfrgsvqv rglstlsvsg
      181 ngnesflqpt splyiidgvp ldadkaaefg fqtqgpgvsp lslipvediq siqimkdaqa
      241 tslygsrgay gviiittkrg nskvprvryt tnffvnappk lretlggnde rrakiqqils
      301 nattvdelrk igmtgflads lnaywnnstn wqsifyatty nqshnlaldg gdqkfnykan
      361 vgyysekgvi kntgfdrynl nmnmefkpnd kfrffgslfg svgsqakgdg lgllqqgvas
      421 ngqastllpp psfylssdgv tsalktlnsn ssrniranvd gryefipgla lsssisydyt
      481 sdaestftpa aansqfaqvy dfegrnytly nrnaityakt iggnhnifvn lfneiykqgg
      541 qsgiirqert pndqlqgpvg ydsynsrggg vlsnyknati asfagavsyd fqrkyvvels
      601 yrldgtssng lenpysknps vglkwnyske nwfkdlswlt yggirltwgq nivptgslqs
      661 iygiynlngn fnnnptigin ydfipnptlk pttttqynlg fdiglfqsrv dlnfdtyykk
      721 vdnllfdrfl snttgfnrrv sndvaiadyg yeltltvrpv iskdfnwsis mngainrdvl
      781 lklpaeyngq yikfdnspyl qhivfrvgqn tlsnylhinq gvystdaevp vnpatgkkys
      841 sngvpfkagd pifkdvngdy ilddrdyeit gnsqplvtgg istniiyknf glniyatfta
      901 krtvlnnala drlaisrnpy dllavvplsn mdiwrqpgdh tvypnpysfs tynqiqplrp
      961 dqtlwaedgs yfkinnvtls ysfdrklirk igfnnlrvyf stnnlttfss ykgpnpenvt
     1021 tlgrdissgy pvprtynigl nlelntsk
//
LOCUS       WP_090653514             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090653514
VERSION     WP_090653514.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104822
     Region          27..979
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrllihvm lcvlcfplll saqdnavslk vqetngqpia gvtisidkkr tmvtdaqgav
       61 tipnanssii vfsatgfksk tikadtltqs tiileqdvan ldevivtgls tnvkrrnlan
      121 avatissrel sstapaqtld galegkipga yinansgapg ggitvklrgv tsvygntqpl
      181 yvvdgvfidn satsaglnav tsaasggaat stqdnpsnri adinpqdiqn ieilkgasaa
      241 aiygskaaag viiittkkgr qgktainvsq dlglitvrkl lgvreftadr aaslssdpat
      301 sealkkqftd aqaaghiydy ekemygntgf arntelsltg ggeqtsfffs asqkdeggiv
      361 kntgyrntgl rlnidhrisd nikigittny inssadrglf gndnvgatig valsstpsfa
      421 elhpdangny pannfaasnp lqtialmknn esvnrfitgl nleatlqnsg ksttkfiarg
      481 gvdfynlqts alfpgtlqwq avnkgtsiqg ftknlstnyi aslvntftps dnvslttsag
      541 ftqetgdynn llnvatqvia gqsnvsqaga lnatqlrtky lnsgvfiqee asiidavtlt
      601 agvrfdrssn ngdaakfyty pkaglswnlt rsgivdegff nniklraayg qannvpaygs
      661 kftgmaisni agnpgvivni qqgdanikpe rqkeleagid fsvlnnrlsf eltyynksis
      721 dflmlqslps ssgfsskwln agdlrnhgve lglnaipvqs ksvtwntsvn fwlnrskvir
      781 liippipqgs fgyvlgsfqv eqgksatqiv gldgdngvgv lgdaeptfqm ntynevtffg
      841 rlslrfllhw knggdninlt slqsdfggts adydkvtnkm gvpdavyrim qigttarifv
      901 edasylrlre aglyytfnef hnsfiksinv gvsfnnyltf tkyrsydpev snfgtgfstg
      961 vdvlpypask raafhisfsf
//
LOCUS       WP_090655002            1125 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090655002
VERSION     WP_090655002.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..1125
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122844
     Region          26..1124
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrfhflff lvfvlltaga naqekktitg tvydslhkgl pdvsvhvkns ktgsvtdaqg
       61 nfriaagagd vlqfssigye aqevavgnss nvsvtlksas nslnevvvtg fgsrtntrkl
      121 syatqeikat elqtapspnv lnslqgklag vridqgtgga gsssririrg ntsltgnqsp
      181 lfvidgvlik pgisgpesws dnnnvdfgni lknineddie sisvlkgsaa salygsgaqn
      241 gvilittkkg tgrglgvsvn itgmwdkayk tpdfqteygg gisptfekda dgnnildpdw
      301 spyynfgpki dpnvmvkdld ghmrpwknyd fldffqtggq qnynvaltga tenssirasf
      361 sknistglip ngskldrntf tvrgtqklgk ifnvdvsaty aqskntnptr evsnynplfr
      421 ftyyranttd wnyylknymd tvnggqvlga adpygvntfl wttfqnnqys yddnlranid
      481 fttyirpwlt lltranlnny dvriekkflg sgagyangyy yvqnsqtrny rfqalltasr
      541 nltddltgsl tlgaeknkdk lgmvltqntn gglstnnpff fnlsnsvnpi sttqsyspsr
      601 ltnaiyaygd ftwrnmltln ysvrqdynst ltyadgtgky tfvypsvgas fifsellkns
      661 saldflsygq lrasygitgk dydpfalnqi gnynlqgade ivgpdgsvtt iphagftnlt
      721 lpnkdfknek tkeieiganl kffnnrlgid vsyynkntyn qilaltipae tggnnaifnv
      781 gqvrnqglei llnatpiqrt nfswnfianf stnkntiisl apgiaqynll tafgadvrai
      841 aepgkqygav ysgysfayyq atdgdgkpid dpnngkkvig napngsnglt flraqdygpg
      901 lvhdkylgti mekfiagtyq tftykdftlg fqvdakvggl masgthqygg sngsftyslp
      961 grdaahggie ytddqgvvqd dgiipdgvfg qgvtanvngq tidlagltwq eayesgyvkp
     1021 kpawqyyedl tqwssgirey svfdnswval revaigynlp kkissklkmn nlrvnligrn
     1081 ltyiwknakg ginpeglssn naaafaeygg lpyvrslgfs lnanf
//
LOCUS       WP_090655056            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090655056
VERSION     WP_090655056.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114587
     Region          32..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknepscrna gvgrkllvfs lffllafsvr sqtvtgkvtd edgkplqavs vlvkntktgt
       61 atdssgnysi kagpnvtlvf ssvgfvsiel nvgnrsvvda vlpantqnlg dvvvtalgik
      121 rserglgyst tivkpdeltv nrtsnpmnal qgkvagvnis slgtgpggts kirirgqsai
      181 tgggsplivi ngvpidnssf ngntvgvsgg gvyadggdgl gsinpddies mtvlkgapaa
      241 alygnraang vimittktkg knrgigvtln snytfetpld ftdyqnqygq gengvrpttp
      301 nptsgewsfg ekiepgmtqi lfdnltvpyv aqgsrikefy rtgqnfantv tlesmgekgg
      361 vhlslnnten lgitpnnkfg ryivnlgfny dlsdkfsfag nvnysnerik nppnianqdn
      421 sipttlmala ntmplkvlee nkynadgney vfsrftnrtn pywvlaeqfh nikrdrvfgn
      481 islkynilpw wwvqgrvgmd yysrdedvnn fptgiasrap aqagfvngvy tqearrnret
      541 nldfltvank sfgdfditlt aggnnrrnrl dinnvqvtdf vvrglytvqn graknpvytl
      601 sqfgvnslyg sgeigwkktl ylngtirkdw fstlskenmg iiypsvsgsy vfseslgkaa
      661 pwltfgklrv gyaevgsdgd vgpyadqlfy tvnsntilnp sgtavtvgts gstlpnpnlr
      721 pmrvkefeag melrmfnnrv gldvavykkt tidqifsvqi sdasgflntr insgesynkg
      781 fegllnitpv ltnnfrwdft antsynitkv isistntpge ratigshpfn gevrvvvgee
      841 mgqiagygya rndngqmifq snglplrtdd fvlfgsglpk wtggffnsfn ykgvyltvli
      901 dyklgntmls gtnfnavrhg lhkmtlegre tgyvvgdgvs qdgqkntaqa avqtywehlr
      961 tqqivepvvy nagfwkirqv slgydftkkl panwpikglk ldfvannvli lkkwvdnidp
     1021 etvgygvdnm iglespgvps trsmgvnlni kf
//
LOCUS       WP_090655881            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090655881
VERSION     WP_090655881.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117967
     Region          38..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknvllatsl ffsaiisgvn aqsgnssdtl pkaasgvrti tgvvsddagk plpdvtvrik
       61 gtgqtvvtdk agkfylvttd tsstlqithi smayeevrtk pgvlnitmhp ndnslndviv
      121 vgygtqqrsk algaintika dklnempvtn lgsslrgrip alsvsggnar pgadatltir
      181 npvilskdgg tlsplyiidd virteddfnl ldpsevedis flkdaaaaiy gvrsaqgaiv
      241 vrtkrgkvgr tqvnvnssyt tndatslpsm mtgyelanyl nastqasknf vadgssgyle
      301 sssyytddel eyfknhnynw ldhawkpsnt yrttvsvsgg sdkatffasa syvkqdgnld
      361 rinydkwtfr antdvnlgag fkvglslsgn lnhnnqyllk qggenpendv kgllytpgyt
      421 ppyingypvr lsqssnqnti dafhyfevqr ldnfndsrnn sfnvvgslqy dapwlkglta
      481 kvqysrlldn tfpkqygtqy ylynfemtge hshiysdnvi lsntspvkvs ngnriyikps
      541 yrdayqldas vgynnhfgkh nisalaiveq tefkyddvqt vvesptpgap pdgrfafgee
      601 dvyetesegg llgyigriny dyagkylaef qvrydastnf arenrwkpfg svsagwvisq
      661 enflknsnai nflklrlsag klgsdntkay gylqrytplq nygavfggng dlilgvrnea
      721 ipnpdvrwdd dlklnggida rflnnrlsat idvfhdhryn mltaltasvp iligsaiase
      781 nyatinaygy eisagwndni gkdfsyhana fftwsdaksi kvdvaagkig tyedptgkst
      841 dmgvqgyeyi gmfrsqaevd swlaknpdyt ifgktpmpgm lyykdirgpk dpetnqyapp
      901 dgkidendqa fitprssnhy gfgltlggay kglqlemvis gsfggqgvve saarklgtat
      961 strpefwnnv wtpdntnaay pnpyynsdyd vtssfwfrss tqirmtninl sytlparwtd
     1021 kigmqsikvy anainafnfy npysykdnyl gsfdaypvlr sfsfglnlgf
//
LOCUS       WP_090656327             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Parafilimonas terrae].
ACCESSION   WP_090656327
VERSION     WP_090656327.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40582
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtiailkepi netrvsllpe aadtltkqni vvnieknaga layapdelyq skniriaert
       61 eilnasdiil tiqplsqeei talktnaili giyqplfnyq fikqlaekni tafsldmmpr
      121 ttraqsmdvl ssqaniagyk avleaaniyp ryfpmfmtaa gsikparvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgak fievegaada skaggyaveq teeykqrqqq
      241 kiaasvakad iiittaqipg rkapvlitne mldsmkpgsi iidlaaatgg ntlqtknnet
      301 vkyknitivg nsnlaatmpg dasklygknv lnflqliitk egninlnfed divagccith
      361 ggkvvnervg glidklig
//
LOCUS       WP_090657702            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090657702
VERSION     WP_090657702.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116923
     Region          23..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilftlfv miacslaafs qsrtvrgkvv dqngeavpfa tinikgskma vsadanadft
       61 itantgdvlv itavgidkte itvgdadlss ivvnrnsqnl nevvvtalgi krsekavgya
      121 iskvdpdaiv qksepdvlks lqgkvpgvdi rvgqgapgaa triqirgiss iglntqpliv
      181 vdgvpysnde igsgsvfsgg gasgtgfanl dandiasinv lkgaaaaaly gsrasngvvl
      241 ittksgsagk gpkplnvsyr gsysiekigr lpefqniyga ganfkeqgsn gswgarfgqg
      301 viydgngnvi gtsssgidsi paatwgamya aypelfpngr aaykaypdnv kdlfetghmv
      361 ensvnfnggt entsfnatls nitqngyimn ssytknnvav ggqtklgnlt lggnvsyahs
      421 kqlggyfgqv qsfltqwgrt ftmarnwdia gfpstdksgn qigfnsgqyt npvwaayhnt
      481 itttddrtvg tfrasyrvnn fltvnytfgi nnytlyrdai vdessygstd navgnitetv
      541 yrnqelqsti vavitpkisn dftldiklgn dfnqrtsryq qvygsdfivs glynltntnt
      601 ktfnsdsrnk rrlvgffgda tigyknfayl nisgradlts tlpyknaqyi ypgisgsfiw
      661 tdafnlqsnw ldygklrigy akvgndanpq ngqdvfglys tsflgqpraa rsgttydpdl
      721 tpefthelea gmdfqlfknr igaeitwydk kttdliysvd vpsttgytsf ytnigeient
      781 gweiglnvkp vvtknfswei rgaythnknt inelvegler ipiggytdfa geyleagfpy
      841 gyfrgtaaar yegkllvdpn tgwavedpnn vylgnpnpky klgitnnfsf kgitlgvlfd
      901 mtvggsfyse ainsmlgrgv tldtkdretn rvidgyyanm tqqlgddgkn hfvpllidgk
      961 pvqnqtkitt ndlyfqagva nvtsfatnsa gefniygatv yhlreitlgy dlpsklisrl
     1021 klsnvnisvs grnlwfvapn vpkythydpe vssfgtgttq gfdisgapsp kryginlsva
     1081 f
//
LOCUS       WP_090657710            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090657710
VERSION     WP_090657710.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116646
     Region          26..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msyinkaagl llclllcvcs hagqltvkvt dasnnqpvag aevhvagssy ysltdtsgfa
       61 sipagdkggr itvkalgyat ataafsqadt diqvrlvpag asletvtvst gyqllpkera
      121 tgsfatidsa algrqvttgi tdrlkgaasg llfdgrlkss sglnvrgiss ingpsaplii
      181 ldnfpyegdi nninpnnies itllkdaaaa siwgakagng vivmttkkga ynqplrleln
      241 asltytakpd vykaqdfmns agyieveqml fdndfysyye sspfrpalsp vvetliqqrd
      301 glitpaqaaa rldtlghndv rrdfdryiyk sslqqqyals lsgggdkary llsagynana
      361 dalsagynry sfsgqndlqp fkaltlhigf mytrskatsg kpgwdniipt agrllypytr
      421 laddegrpla itkdyplpyv dtagggllkd whyyplddyr hntttsgved llldvntqlr
      481 llpwlkagis yryekqhttg lalqdaesyy arnmvnsytq agsdgslfya vppggiavns
      541 yaaveghalr aqadidkrwn nmeltalaga evrqtasgag sytlygydda tlsytpadvv
      601 nsyplyvsgy sdyinpgtgl sshtdrflsg yinaalsyrs rytisasark dasnlfgaat
      661 nnrgtplwsa ggawqlnrep wwqagwlpll rlrasygftg dvdqqrsavt tlsivpgasy
      721 tnysfanisq fanpglrwek tgmlnagvdf amkdnllags ieyyhkhgtd llgyapldyt
      781 sglrqqaiik ntaamkgdgv datlnstllk aplswqvtly ygynlskttr yyrgesalgs
      841 dyvsdgniis aapgkplyav asykwagldp qtgdprgwld gkpstdyaal lqqtmaddlv
      901 ytgsglpvhf gyfnnsfsyr qwsltisisy klgywfrkas vdygqlynyg ymnrdfekrw
      961 qqpgdekhts vpslvypyss frdqfynnse alvvrgdhir lqyiylvynm apgqkhrmfs
     1021 naqlylnvln agilwranke gldpdryypn qlpvpfslag gikitf
//
LOCUS       WP_090659359             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas marina].
ACCESSION   WP_090659359
VERSION     WP_090659359.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas marina
  ORGANISM  Nitrosomonas marina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas marina"
                     /db_xref="taxon:917"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39575
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir geetrvaatp etikkytakg vhvvsvqtga garasipdse feaagakiva
       61 daatlysqsd ivlkvrgpea eelammrkda vligllapsk senidilarh gitafamekl
      121 pritraqnmd vlssqaniag ykavlmaanv yqrffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avveafdvrp aakeqveslg akfievplne eekanaetag gyatemsedy
      241 krrqselvhe ravaadivit talipgrpap vlikeetvra mkpgsvivdm aveaggncvl
      301 seldqtvvkh dvhligiani pglvaadsst lyarnlmnfl nlivdaesgq lridrddeiv
      361 agtlvcsdgn vvqas
//
LOCUS       WP_090661181             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090661181
VERSION     WP_090661181.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110277
     Region          21..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilllpll ftalfasaqt rplegkvvsa tdqhavskas itikngksfi addsgsfrie
       61 vpsgalsltv ssigfasqnv avnaadnnii iqlietdknl nevivvgysd kkrgeltssv
      121 avvdagklkd vttndvgsml qgkvaglqvv nssgvpgana eirlrgvssi nasqsplyvv
      181 dgiiggnfdp ndvesitvlk daaatamygs qanagvivvt tkraktnkta fefkattgfr
      241 tpdfgkldmm ngeqlynyqk efyrdyiptd tgnsykidll kfyaerprel qdqnhnwmtt
      301 ifnpafmqny yisisgrtek sdyylgasyy nedgtfkntk fqranlrass tlhfnpkisl
      361 tntinisgit gtsydyndiy yaflnlpwdn pydsagkpvy vdgnssfkww srdkvnplht
      421 idhsdhpykg fdvnydlnfn yqitnwlafs stnrigasys kstnyysgdv agqyhgtgyl
      481 dessilsysg isndllkfnf kfgdhqlngl agvafeggkt etigasgrgl pfnlrvlnvv
      541 ssnlsvngyy dqsalisyis qvnysyknky fltgsyrvdg stafqknnry gsfpaisagw
      601 lvsnedflkn nhiidllkir ggygvtgtqd igasrylgly sltsqynnes aatpsqlpsp
      661 nltweskyqt nigvdidffk rislsvdvyk nqtknlllqv sqplsvgfet rwensgeien
      721 kgleialsti niqsknfswt tdfnisfntn tlqklpagfv ktgswaisqt yrnggnlyef
      781 ympvwkgvdp qtgaplweki tkdadgnvta kettssyaea tlqevgsalp kyqggftntf
      841 tyknfslsan lyflygnkvy sndlrfvmnd gnepyynqiv lpsgysiwak pgdiatnpsp
      901 qnaanstets trylqdgsyl sirnislgyn lpqsfatrlg lqniavtvta dnvytftkfl
      961 gqdpqttiqs diyttpgvsd fkypnnhqyl lninikf
//
LOCUS       WP_090662152            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090662152
VERSION     WP_090662152.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115595
     Region          24..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrstiitgf flllfyglna qpgqtitgtv tasdtkqple kvavqekgtr nsvltdntgr
       61 ysitlskgna tlvfsyvgyd tresgvgssa ildvaldpsg naltdvvvta lgikrevktl
      121 gyasqqvdat qiaqakqpnl inalqgkvag vtiqssgggp gqgasilirg vnsispsndn
      181 qplfvidglp vdnstfttgt tgdrgasmpn rlsdlnpddv esinvlrgga atalyglrga
      241 ngvivvttks gqagkmrvsf nasynidnvn kipdiqlkys qgwmgvydst dfwpawgptv
      301 eeakkidpsh pdklfnnwkh ayntghqfrs gvnfsggsek itysssfsyl kqegvipntf
      361 yqgingrlng qlkfsekfkm gtsiyytntn gnfydanryn edlvywtprw dvrdyltpqg
      421 tmksygndnp iyqtatnkfg sqvnhiissv nfayspvkwl tatylvgvdq ygdartatap
      481 gavgfpgefi aadnqdydgk ygtgfvhdyq lnyrqinsnl lltfdhtwan kfqttfrvgn
      541 dildrnikri saegsgldvy nwfslanakh tqidqtrtky riiglygdlt lgynnylylt
      601 ltgrndwtss lemdnrsffy psaslsyifs qhltmpswft ygkfraslag igkdappyrt
      661 sityapsgsp isnngvdiir wtrnsnagsv dlkpektttf eigtdlsffk srlglnltly
      721 ksnskdqiid vttttttgfg sitlnageie nkgievtvtg npvksknfnw disanfsanr
      781 nkvlslyegl rsiyigsvfg ygrstissyy vpgepvgniw gtpvmrygdd paiaddavha
      841 nkdlpvligd ngfpvyadgt nqkilgnsyp kwltglsntl tyknwslyfm wdaqlgvhky
      901 dqftnflaaf gestvtlnrn etivfdgvta dgkqntkpvw lgqgvgpdnv dygagyyrni
      961 yrgvsenfve daswvrlrta tlsyslpenl iknsfinnvs lsftgtnlil itkykgydpe
     1021 trsdaapgsn lnvssgfsyp alrsyifsln vgf
//
LOCUS       WP_090662543             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090662543
VERSION     WP_090662543.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110744
     Region          35..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlhnqnrka ifraltllll llsafnpkqa aaqtqeikgv vrdsaaaaia gatvsvngtk
       61 rnvitandgs ftinaapgdq lritaigfse qiipvsgkgl ltvtmltevk alsdvvvigy
      121 gsqrradvts avasvkqenf ikgpvqdagq liqgkvaglt vsapsgdpts gtqillrgnt
      181 tlfgantnpl vlvdgvpgsl ttvapedies idvlkdgsaa aiygvrgtng vilittkras
      241 gnnintveyn gyvstetiar kldmltaady reqikegird aswdlgsntd wldeitrtpv
      301 sqvhnitfrg gnsktnylls lnyralqgif lrsnnntftg radinhnmfd dklklnlqll
      361 nqnidyiqtt dggsfngyty rqaliynpts pvknedgtwf qqvgnfnyen plsriyetsg
      421 kyqgvntrin anltytpvig lklnalfsys rlnnesgyse tkqhvstlrd glngyaavgs
      481 tqsidrltel taeytksfkd hrfsllggyg yqeneyfnfy ernydfptdi fdysniqlgn
      541 alkegkatly sykgetnlis ffgrlqysfa dkylllasir reaasqlyga kkpwgtfpsv
      601 svgwhitkeg fmlhqtlfdd lklragygvt gnppaslflg vaqigygsyn ysngqwiqtl
      661 aptqnanpyl kweekqetni gldfsmlkgr isgsadyyir rikgllynyq vpsppnlyst
      721 teanvgtmen kgfevivnfi pvqtksfqwt tsvnfstnsn klislsndly katsdyfttg
      781 ytgepiqtft hivyigkgig dfygfkvtgl ddngkwiyeg qdgkpvnydd fahsfedkkv
      841 ignglpkyya gwnnnfkyka fdlsitmrga fkyqvlnyqr myyenptlqn ynrlksaydk
      901 pygkalltap lefnsyyien gdfwkvdniv lgytfslhsk yikglrlyas tintltitgy
      961 kgidpevnrl glnpgdddrd kyptsrtytf gvnvtf
//
LOCUS       WP_090662555            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090662555
VERSION     WP_090662555.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117492
     Region          23..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktvsmlim vlltsvaaws qgkisgtvkd qngdpvpfat vnvkgtkvtv aadvnanfti
       61 paksgdvlvi tavgvdplei tvgnnpvvta tvnrtsgtit dvvvttalgi rrnrnelpya
      121 aqtvtseemt ktnnsnfans msgkvsglqi ktnnslggst niilrgarsi tgdnqalivi
      181 dgvpvnnsty nssstqqgfa gydygnqgsd inpediasvn vlkgaaasal ygsraangvi
      241 littkkgksg lgitlnlgas tgnmdkstwi kyqrqygsgy ydpdyytysd appspdshfw
      301 yldangdgve dlvvptteda sfgakfdpnl kvyqwtafdp tsptylqatp wvaakhdpta
      361 ffqnpvsava slivqggddk ftyklgyshn ddkgilpnsk lkkdivnfqa dykitdklti
      421 tgatnfskis glgrygsgyd afnlatnfre wwqmnvdvmd qkaayerthk nitwnmtdpp
      481 ndigpiywdn pyyvryesfe tdsryryisy itlnyavnnw lnlmgrvsld tyenlqeern
      541 gyesinigay skynnsykey nydflasvnk nisdnlnfka vvgtnlrrny fkstfaitng
      601 gliipgiydl ansanpieap teedqqreig rvfggitlay kemlildlta srdqsstlpk
      661 gnnayfypsa sggfvfskll pdatwlnfgk lrlnyaevga dapfdylvdn ytqptpfgtv
      721 plfsvnstkk nadlkpektr syeagieasf lknrigfdvt yyhtntidqi ipvtisgatg
      781 yttqiinagv venkgieasl nlipvktkdf swnmalnwtn pknkvvsltg gtenilmgsf
      841 qggvtlnavv gqpmgvlkgs dyiytdgqkt vdgdgyyevs sttnniigni qpkwygginn
      901 tftykgisls flidmkqggd lysvdqwygq gtgltantag lndkgnpird avedgggikf
      961 pgvtedgkpn gtyalitglr gygynsfpna gyiydasyvk lreasisysl psklisklnp
     1021 ikgidisvyg rnlwiihknm pdsdpeegps agniqgfqvg syptyrmigl nlnfkf
//
LOCUS       WP_090666851             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas nitrosa].
ACCESSION   WP_090666851
VERSION     WP_090666851.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas nitrosa
  ORGANISM  Nitrosomonas nitrosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Nitrosomonas nitrosa"
                     /db_xref="taxon:52442"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39054
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeiy agetrvaatp etvkkytakg fhtvlvqsga gagasipdaa yqeagavivd
       61 dvsqlysqsq vvlkvrgpaa nelvmlrkda vligllsphq aegiealakq gvtafamekl
      121 prisraqsmd vlssqanigg ykavimaahv yqkffpmlmt aagtvkaarv lvlgagvagl
      181 qaiatakrlg avieafdvrp avkeqveslg akfvevplte eekakaetag gyaaemsddy
      241 krrqgelihe ravaadiiis talipgrpap vlikeetvqa mkpgsvivdm aveaggncpl
      301 selnktvvkh gvhligianl pglvaadasa lyarnlmnfl nlmldannge lninredeii
      361 agtlicmgge vvk
//
LOCUS       WP_090662560            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parafilimonas
            terrae].
ACCESSION   WP_090662560
VERSION     WP_090662560.1
KEYWORDS    RefSeq.
SOURCE      Parafilimonas terrae
  ORGANISM  Parafilimonas terrae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Parafilimonas.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Parafilimonas terrae"
                     /db_xref="taxon:1465490"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113702
     Region          23..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrilsvlgf mlitlaawsq erisgtvrdq ngdpvpfatv nvkgtsssva adananfsia
       61 akpgdilvis avgianqevt vgnsrninva vtrtnqelse vvvtaggitr rksevgsaqt
      121 aitgaavtkg kainiagglq dkvaglniqg ttggvnpsyr iilrgnrslt gnnealivld
      181 nvivpnsiln nlnpedvqsf nilqgasaaa lygsqasnga iiittkkgta grtnirvant
      241 ttgehvaffp knqmsygqgg ssygydengq pnfssienqs ygphfdgstr plgvpledgt
      301 qetqlytgnd trekfwktgi tnqtdfslss gdevstiyvs gqytsvkgtt pkdkfnrtsl
      361 rvngsrkiyg nklavnyslg ytqnnyditt qtngiynnml nmpsniditr yanwktdpla
      421 npngyynpwy lnpywqldny rrderneylv gnvelkyspl swlsltarqg itktnqygks
      481 wnnsfkytey akesssnsks diaagvsdne nytmnllsdi yfeikqkand fsfdlvgggq
      541 wnqnaykgtg vsasplvipd lynvgnlvgi pgaseasyla rimgvygtlq vgykdylfln
      601 ltgrndwssi lpaanrsffy psanlsfvas qaidaiknsn titylklrgg vskvgevnlg
      661 nntnfgayql qrtfsqqsgf pygslpgfgl dntivsaslq peitkqyefg fdislmhdrl
      721 tsavtwyhsv tnnqtvttgl sytsggsgyl tnvgetmseg leaelhvtpi rtanwrvtvg
      781 gnfsylnnkv ieigngvdqi rlagygdgsg iyavagqafp vimgfdfvrd deghvivdas
      841 tgeptkdatl kilgnsqpkq rltldfnvqy kgfeltglfq yrggynmyfg sgsdvdwagt
      901 girttlfnrg rfvfpnsvye dpahpgtyik ntnitltdgn gnagfwtsen nrdvssnyvs
      961 sgafwklrel slayhlpqsl frkasfikgi dvsvqgrnlf iwlpktnfyt dpeysevsst
     1021 sngigitgis sappsryygg tiainf
//
LOCUS       WP_090674217             411 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aureimonas
            jatrophae].
ACCESSION   WP_090674217
VERSION     WP_090674217.1
KEYWORDS    RefSeq.
SOURCE      Aureimonas jatrophae
  ORGANISM  Aureimonas jatrophae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aureimonas.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Aureimonas jatrophae"
                     /db_xref="taxon:1166073"
     Protein         1..411
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43444
     Region          2..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvrlfvpreh emgeprvaas pdtvrrligl gtevwverga gegsripdrd feavgahlad
       61 qeggrdadiv lkvrrpsade ipnyrrgavv vaiqdpyghd dalramaeag ltsfamelmp
      121 ritraqvmdv lssqanlagy qavmdaaaiy drafpmmmta agtvpaarvf vmgagvaglq
      181 aiatarrlga vvtatdvrpa akeqveslga kfiaveddef raaetaggya kemsesyrrr
      241 qaeltashia kqdivittal ipgrpaprlv tramvesmkp gsvlvdlave rggnvegavp
      301 gevaevgpar vvgylnmpgr iaatasllya rnlaafvetl vdketktlrl dptdelqrat
      361 mlthegrvvh pnfappapda ptgdpnpaes atpamdaaaa gavtepekgt h
//
LOCUS       WP_090677895            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            guanonis].
ACCESSION   WP_090677895
VERSION     WP_090677895.1
KEYWORDS    RefSeq.
SOURCE      Myroides guanonis
  ORGANISM  Myroides guanonis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Myroides guanonis"
                     /db_xref="taxon:1150112"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115751
     Region          25..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrsklkwtia lfmalvvqls faqektlsgv vtesgmtlpg atviikgtqn gtqtdldghy
       61 sikvnpgdvv ifsfiglddv aytvgasnty nvamkagdem leevtvtafg ikrsskslgy
      121 atqevksdel nktsntslsg alqgklagvs itpssgapga ssqimirgar sftgdntply
      181 vidgmpvsss sdfstgnsvs gsdvanravd idpsdiesis vlkgqaasal yglrasngvi
      241 littksgkgl eagkpvisyn ttssfetisk kpdlqnvyaq gsagkfnpya stswgpkisd
      301 lvndvdnakm klpgyggnlp nstnngvlhp gkyyvpqrat mgldpwvtpq aydnvddyfk
      361 tgytishnln vsqstgktny sfgfgtstqd gfmpgtgmer ynlklnantk lneewntgfs
      421 anyvqtkidk ataandsslp gvygapssyd lkgigygepl dpykqvffrk safnnpywaa
      481 ehnefsektn rfygnafvey apkisvdevh sltfkyqlgl dsyttnyrdv yeyghahtsk
      541 gsvsltgvtk dvvnslftmn ynwditddlr fdvmagteln henykgyedf gnnlnfggfa
      601 tiknaqnvss velrnqertv gffsnaglsy adviflsgsi rkditstmpr gnrsfvypsv
      661 slglvltgie glnqsdivsf akirgsyahv gqagrfkkpy ystpsygggf wsgtpfsypm
      721 ggvgaympsl tvydpdlkpq ntksfeigad vrffnnrlgf dytyseqrad dqifnlplag
      781 svgkaiyvtn ggsmqtnshe lvvfatpiqt kdfewnvnvn ftkvdtkvns leyglenimi
      841 ggfvepqiri sqgdrfpviy gnsfarheng qilvdedglp miggqkvlgd vmpdfilggg
      901 mdfryknwnl gatmewkngg klysgtnktl nfygmteata nrdqdmifng vkadgtpndi
      961 vigngqganr edlesvlvdi tensvydasf vklreitlgy tfpklvnnkl dlrvsafarn
     1021 illwskvpni dpessqgnnn maggfehwsi pqtksigmsl nvvf
//
LOCUS       WP_090677893            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            guanonis].
ACCESSION   WP_090677893
VERSION     WP_090677893.1
KEYWORDS    RefSeq.
SOURCE      Myroides guanonis
  ORGANISM  Myroides guanonis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Myroides guanonis"
                     /db_xref="taxon:1150112"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110526
     Region          25..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwtla lfmalivqvs faqektlsgv vtesgvplpg atvivkgtqh gtqtdldgry
       61 tlkvnpgdvl vfsfigltdl sytvgvpnsy nasmsadeem ldevvvlayg qvknknevtg
      121 nvvtvksdvi antplptidq alqgrvsglq mssssgvpga vqnirirgrn sltatnepli
      181 vidgipvins nfagstdess lsalaaldsn diesmtvlkd agatavygar gtngvilitt
      241 kkgksgatkf elkttlgfqn yavkgprmlt gaqkkelyle gvyntfgvan gfgrdeayaf
      301 teanasglag gtslvnwvkg gevetnwgdl vkkkdapvst vsfsasggde sssfyaslgh
      361 nktegtvigs dfrrisgvfs fnkklsdkfd fntninvsnv kqngllegaa yfsnpnltkl
      421 fmspwipayn adgtynlprs glhnilytte nnittndltr vlnsnvvsyk itdnlkftss
      481 ialdyalaay ksyknpvhgd gdgiggyvvn sinrnfnyva qnsldyrfyv geghrfdvkl
      541 vyefqknksh llegegqava sgftslgtta dnhfasanft dwmqqgyvgl lsynyqnryl
      601 idltgrregs srfsegsqwg nffsvgaawn iseeeflsnq etlsllrlrg sygtngnsti
      661 spnqyqqllk feiydheggl vpsqlggpls wekqkkmdvg lefgfldnri sgsfayyksm
      721 tddliyakpl sytsgyatqy vnlgalensg fevdlnfdiv rskdfnlslg gnigtvknki
      781 templgpdgk plevlgsysa nvegkaigew ymptyagvdv qtgealwfkk dggttnaygq
      841 aekrfqgasa lptysggvnl hvdykgffin slvafsggnk vyedwvaqtn gsgatttaty
      901 ngveklmdrw qnpgdvtdvp ktvnrntans sqstspstrf lydgdyirlr dvsfgynfrg
      961 ailrtlsldg ltlsvigtnl ltkvkddrlk ydpeidptgf tsltappiks vvfslnikf
//
LOCUS       WP_090677998            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            guanonis].
ACCESSION   WP_090677998
VERSION     WP_090677998.1
KEYWORDS    RefSeq.
SOURCE      Myroides guanonis
  ORGANISM  Myroides guanonis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Myroides guanonis"
                     /db_xref="taxon:1150112"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123754
     Region          26..1117
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkivlnffl vmfalcmvhg ayaqgrkvtg kvvsagdnlg lpgasvlikg tqegvtadfd
       61 gnysitvsda natlifefmg yktqevkaqg ktvinvslae etemideiiv stgidkmskr
      121 iftgavsrit aeemkvdgvv nvdrmiegka agvtvqnvsg tfgsapkitv rgsssilgdt
      181 kplwvidgvv qedivnvsfq dlasgnsetl lssaiaglns ndvlsleilk dasatsiygs
      241 ramngvvvit tksgrrespl sisysmenam rtvpsygqyd imnsqesmsv lqemsskgll
      301 eytnvaqsry ggvynilara vgkvnpdgtf qvvnnkigkn eflqqyekan tdwfkvlfrp
      361 sitqshtlgf sgggknnayf aslgyyadpg wtladrvhrl tlnmkntffv tdkfnlslga
      421 nlsirdqkap gsynsktdvv nggtsrdfdi npfsysmnts rtlrpydsng nleynrmnwa
      481 pfnilneldn nvmdlsvkdi kiqldaeyki lpeltynlns siryadsrrd hniyegsnvv
      541 gaynanestv vngqniflyq dpndpdgiki pvlpnggiry rhdnnllsyn vrnslsykqv
      601 fgdkhevdgf lgtemrhvdr tydylaafgl qydrgfipyt dprllekiia dgdsyfqfse
      661 erertvgffg kgtyaydsry ivsltgrydg snrqgrstss rwlptwtasa kwnvseekfm
      721 ldskvvsnls lrgsygltan agpatnsyai yksfitdrqf igerepgisi edlensdltw
      781 ekqheanigl dlglfsnrvq lvvdayqrka fdlidvvtts giggqrsklg nnadmttkgi
      841 efgittrniv sedfkwstti nasyydqrid klqnvsrvid lvtetggnvv grprnsiysy
      901 qftglnddgm ptfiqadgvt dnvsganfqd rnnitdylky egsvepnksl glsntfnykn
      961 wslnvfivas ggnkirmapt fksgysdldv ftrdfenrwi npgdelttdi pviadgalsr
     1021 yygssglaka ynsynysdar iadggfvrlk dvslgyefpd lvkkqlklsn ltlratasnp
     1081 wliyadkkln gqdpeffrsg gvampvttqy tltlnvgf
//
LOCUS       WP_090678385             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            guanonis].
ACCESSION   WP_090678385
VERSION     WP_090678385.1
KEYWORDS    RefSeq.
SOURCE      Myroides guanonis
  ORGANISM  Myroides guanonis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Myroides guanonis"
                     /db_xref="taxon:1150112"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110819
     Region          29..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkyntgyl gllwvcfcfs tsifaqeiit vqgkvedseg pligvtvlik gtqsatvtgs
       61 ngtfrikapk gasllfeymg ytsqerevts pimniklnqn teslkeitin tgyysvkere
      121 qtgsiarita kdlelspvvn plqalqgrmp gvhitqntgi agggfkveir grnslgssnt
      181 asnfpmyiid gvpmtdtsil ngsglsmglf knsmsllnni nskdiesiei lkdadataiy
      241 gsrgangvvl ittkkgiagk trftvnssts fskvakfmnm mntqqfnqmr deafandgit
      301 vpppyeydmv rtwdrnrytd wqkeliggta iskdlslgvs ggndftrfnv nlahgengtv
      361 fpqsgkgfvr nsalinlnhr skddkwninv atnysvstnd lpsadlttps lflppnapsl
      421 yqadgslnwq ngtfenplaq lkktydsear mlvlntqiay kiapstsfkl nagittnnle
      481 ervltphtiy npianftser sksqeasnns nsfiiepqlh wekkwgvhal kalvggtvqs
      541 nhsnissitg snfssnafit niglaktkti nkigssqyky aalfvrlnya yndkyilnit
      601 grrdgssrfg ennkfgnfga vgvawifske sfaknlswln fgklrgsygt tgsdnvgdym
      661 yldtytatta lydglaglyp srlynpnysw ekttkleaal efglfkdrvn asvawyqnrs
      721 snqliaiqlp kitgfpsvtd nfgatvqnrg weftlntsnl qkanwnwttn fnislpenkl
      781 tsfpgleest yknryvigks inivgvynye gidpnsglyk ftdydqnnli nasdkkvfke
      841 vemkfhgglq ntisyknfsl dflfqfvkqt nynydkvmtv pgllssnypv eainrwtptt
      901 pngnytaatt snsnafeqit tmwesnrais dasfirfknl slayqysfpk lgvemirlyv
      961 qaqnlwtwtn yygidpeftn ignlpplrai sfgaqltf
//
LOCUS       WP_090678482             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            guanonis].
ACCESSION   WP_090678482
VERSION     WP_090678482.1
KEYWORDS    RefSeq.
SOURCE      Myroides guanonis
  ORGANISM  Myroides guanonis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Myroides guanonis"
                     /db_xref="taxon:1150112"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111023
     Region          29..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkyntgci gllwlffcls aslyaqeiis vqgrvdgeeg plvgvtvlik gtqsatvtds
       61 ngafkikapk gasllfefmg ytsqekevns nvmivklnqn teslneitin tgyytvkere
      121 rtgsiakisa kdielspvvn plqaiqgrla gvhitqntgl agggfdieir grnsfrssgt
      181 ganiplyiid gvpvsenlvt nnsllsdnlf qnkisvlngi npkdiesiei lkdadataiy
      241 gsrgangvvl ittkkgqagk trftinssts fskvgkfmem mnteqfnqmr deafendgit
      301 yypfyeydmv gtwdrnrytd wqreliggta iskdiglgvs ggndftrfnv nlahgengtv
      361 fpqsgkgfvr nsalinlnhr sqddkwninv manysvstnd lpsadlttpa lklppnapal
      421 yqadgklnwq nntflnplag lgktydsetr mlvlntqigy kitpstsvki nagvttnsie
      481 drvlephtiw psslnrtsdl wsvsqkgtnn sdsfiiepqi hwekkfrdhs vkaliggtfq
      541 snsndlfrit gigfssnafi tniglaktki inqikgneyk yaaffarlny aykdkyivnl
      601 tgrrdgssrf gdnnkfgnfg avgaawifse effaknwswl sfgklrgsyg ttgsdnvgdy
      661 myldtytant alydglsgly psrlfnpnys wekttkleva lelglfndki nvslawyqnr
      721 ssnqllaikl peitgfpsis dnfgatiqnr gleltlntin irkkdwnwst nfnislpenk
      781 liafpgless tyknsyvvgk sinlvstyny egvdpatgly kftdydnnni intsdkrvfv
      841 eremkfhggl qntisykkfs ldflfqfvkq tnfnfdnivt vpgllstnyp veitnrwtat
      901 npnaqytaat tsnsdafnqv vtfqesnrai sdasfvrlkn vslgyqmtfp klgiellnly
      961 vqgqnlwtlt nyygidpeft vmgnlpplrt iafgmqltf
//
LOCUS       WP_090678792             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            guanonis].
ACCESSION   WP_090678792
VERSION     WP_090678792.1
KEYWORDS    RefSeq.
SOURCE      Myroides guanonis
  ORGANISM  Myroides guanonis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Myroides guanonis"
                     /db_xref="taxon:1150112"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111233
     Region          29..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkynisci gllwlffcls tslyaqeiis vqgrvdgaeg plvgvtvlik gtqsatvtdy
       61 ngsfkikapk gasllfeymg ytsqerevka dvlivklnen teslkeitin tgyysvkere
      121 rtgsiakita kdielspvvn plqaiqgrma gvhitqntgi agggfdieir grnsfrssgv
      181 ganiplyiid glpisenita nnsllsdklf qnkisvlngi npkdiesiei lkdadataiy
      241 gsrgangvvl ittkkgiagk trftinssts fskvgkfmdm mntqqfnqmr deafsndgit
      301 vfpanaydmn gmwdrnrytd wqkeliggta iskdialgvs ggndftrfnv nlahgengtv
      361 fpqsgkgfvr nsalinlnhr sqddkwnisv manysvstnd lpsadlttpa lklppnapal
      421 yqpngklnwq dgtfnnplap lgktydsetr llvlntqigy kilpstsikl nagvttnsie
      481 drvlephtiw npsfnrtsdf wsisqkgtnn sdsfiiepqi hlekkfrdhs lkalvggtfq
      541 snssdlfsnm gigfssnafi tniglaqmqi inqvkgseyk yaalfirlny aykdkyivnl
      601 tgrrdgssrf gdnnkfgnfg algaawifse etfaknmswl sfgklrgsyg ttgsdnvgdy
      661 myldtytant dlydglsgly psrlfnpnys wekttklema lewslfknri naslawyqnr
      721 ssnqlidikl pgitgfpsit dnfgatiqnr gweftlntin vrkkdwswtt nfnislpenk
      781 liafaglees tyknsyvvgk sinlvstyny egidlstgly kftdydnnni intqdkkvfv
      841 eremkfhggl qntlsyknfs ldflfqfvkq tnfnfdnimt rpgtlitnyp ervvdrwsps
      901 nlegkylqah ssssaasnsy gflresnrai sdasfirlkn lslgyqlalp klgiellnly
      961 vqgqnlwtwt nyygidpeft signlpplrt isfgmqltf
//
LOCUS       WP_090678689             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            guanonis].
ACCESSION   WP_090678689
VERSION     WP_090678689.1
KEYWORDS    RefSeq.
SOURCE      Myroides guanonis
  ORGANISM  Myroides guanonis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Myroides guanonis"
                     /db_xref="taxon:1150112"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110908
     Region          29..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknknntsci sllwlffcls tslyaqeiis vqgrvdgaeg pligvtvlik gtqsatvtds
       61 kgafkikapk gasllfefmg ytsqerevkv nvmivklnqn teslkeitin tgyynvkere
      121 rtgsiakita kdielspvvn plqalqgrma gvhitqntgi agggfeieir gknslglsst
      181 dankpmyvid gvpisdisvm nssgfttslf nsrisilngi npkdiesiei lkdadataiy
      241 gsrgangvvl ittkkgqagk trftinssts fskvgkfmdm mnteqfnqmr deafandgit
      301 vfptnaydmn gmwdrnrytd wqkeliggta iskdialgvs ggndftrfni nlahgengtv
      361 fpqsgkgfvr nsasinlnhr skddkwninv manysvstnd lpsadltrqs lllppnapal
      421 yeangklnwq nntffnplap lgktydnetr mlvlntqigy kilpstsmkl nagvttnsfe
      481 envlephtif ipsrnltsns gsvsqkannn ldsfiiepql hwekklgdhs lkalvggtfq
      541 snssdmfkit grgfssnafi rniglalike vnqignseyk yaalftrlny sfkdkyivnl
      601 tgrrdgssrf gdnnkfgnfg avgaawifse esfakdlqwl sfgklrgsyg ttgsdaigdy
      661 myldtytant vlynglpgly psrlfnpnys wekttkleaa iefslfkdri naslawyqnr
      721 ssnqllainl peitgfpsis dnfgatvqnr gweltlntvn vqkenwnwit nfnislpenk
      781 liafpgleds tyknryvigk tinlvpsyny egidpvtgly kftdydnnni intqdkkvfv
      841 eremkfhggl qntlsyknfs ldflfqfvkq tnynydniat rpgtlvtnyp srvvdrwtps
      901 nldaeyikan asnnaastsn tlmkqsnrvi sdasfirlkn lslgyqlalp klgieavnly
      961 vqgqnlwtlt nyygidpefi fignlpplrt iafgmqltf
//
LOCUS       WP_090679747            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            guanonis].
ACCESSION   WP_090679747
VERSION     WP_090679747.1
KEYWORDS    RefSeq.
SOURCE      Myroides guanonis
  ORGANISM  Myroides guanonis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Myroides guanonis"
                     /db_xref="taxon:1150112"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124365
     Region          22..1111
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlllfsl lffsslwaqe krvitgfvqd atekyslpga svivesqtis nttdqkgiiq
       61 stslgtvtdf dgnftlevpv qaktivvsfi gyenktihld krshyivgls tdndvlnevi
      121 itgyqtiekr kltsavaqvs mediaqvgva svdqmlsgqi agvavttqtg apggpakiri
      181 rgtaslngpq dplwvidglp legndvpnfn dkdnidqlqn fsiaglnpdd ilditilkda
      241 aataiygara angviavttk rgkkgamrvn fsantfvtqk pdfsklnlmn ssqkvdlelm
      301 lagrtdlnyr sdkgnisrii nangemqnfq nggfsalspi tqntinnlrn qqtdwgdlmy
      361 qtaintqygl slsggndnsd yyfslgyyde egatvgtgfe rynitlknnf qlndklkvgv
      421 alfgtqsdks sfvsdrdasi npanysrnvn pylnpfkedg synydqdidg fddryipfnf
      481 leerentsyn lrnrslkgvf dvnysilddl tlssqfglqi dnsemekylg ketynvrkek
      541 ertryykngg yhyflpeggi ienennnyfq ynwktqatyn tifndiheld imvgseirkt
      601 dskiiktkgf gfdpktlttk pilfpagsda iddkiyetfk kssienayas ffataaytfd
      661 rkytvfgsvr ydgsnlfgad pkykylplwa isgswlvsne kfmenvdfis nlrlrgsygl
      721 qgnidrntsp fvvgeynsst ilpgmdetti vvtnppnskl rwektantnf gidlglfknr
      781 iaieadiynr kstdliglre lplengfeyt smnwaqvtnk gfeislttrn ivrdnfswtt
      841 nfnfahnksn idqidvmnns ilpsgegnav navyglktag idqygsplfw ldgkkvgvve
      901 yfkltdpyae flpgelvasg ltneemrsrf eylgdrdpkf tggiinnfki hnfdlsisaa
      961 fnlkqtvtkt ppyngaqvdp grnyttdiln awsptntnsn lpgiigkdmn agdswmaysw
     1021 fntadtydty kyldiwtkei sylrissirl gysfpssltn klkiqnaris legrnllvfg
     1081 sdysgyfdpe tygniyaqpi sksftlglnf tf
//
LOCUS       WP_090679706            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            guanonis].
ACCESSION   WP_090679706
VERSION     WP_090679706.1
KEYWORDS    RefSeq.
SOURCE      Myroides guanonis
  ORGANISM  Myroides guanonis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Myroides guanonis"
                     /db_xref="taxon:1150112"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112506
     Region          41..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhlllkvvs psllfllwgl fltlpslaat hsftpiqktw klrgvvrdvd gplpgvivtc
       61 sagavitdtn gnyvidtqig dvvffsfvgy stqqvfiknq tildiilktd vtqldqitvn
      121 tgyytvkdre rtgniakvta kdiefqaitn plqalqgrma gvdisqnsgl agggfrvkir
      181 grnslqnlst tsaneplyvi dgvpllqtng kisglslevl rnsfsalsai npndiesiev
      241 lkdadataiy gsrgangvvl ittkkgkegk tqfslnastg fskvgsfmkm mntqefnklr
      301 deafandgit tfpanaydmn gawdrnrytd wqkeligkta idknisfgmr ggneytrfnf
      361 nlahgenstv fpsskgyarn salisvdhqs kdaklkiqss tsysaqsndl paadfttpal
      421 nlapnapalh npdgslnwqn gtfnnplsql nktynsntrt lilntqvsys ffpntflkvn
      481 agittnsike mqlaphtiyn paygytsass qstlndyssd syiiepqfhw nqdwglhevn
      541 alvgasyqas ttdnfgafgf gfssnafitn laaatyqyil ngtnseykya sifarlnygy
      601 keryflnlta rrdgssrfgp dkkygnfgav gaawlfseel lfkdhrwlsf gklrgsygtt
      661 gsdnigdyay ldtyssgyqq iydgisglap tklfnpdygw ektdkleaav elgflknrin
      721 tsvswyqnrs snqlldyslp nttgfsgins nfpatiqnsg wevtfnvspi qskdwnwstn
      781 fnisfpknel ldfpniessp yrnslivges vnivklyhye gmdpttglyk fkdydnnnii
      841 naadkkafks ietsfhggfq ntisyknlql dflfqfvkqt nynfyqlisn ppgflngtps
      901 imtdrwtpen tqalfskatt qynqystqva tmresdhaig dasyirlkni sisynfvipk
      961 mpntnirvyl qgqnlwswtn dyfgmdpefn fdnsqqlpsl csyalglqln f
//
LOCUS       WP_090681461             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            guanonis].
ACCESSION   WP_090681461
VERSION     WP_090681461.1
KEYWORDS    RefSeq.
SOURCE      Myroides guanonis
  ORGANISM  Myroides guanonis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Myroides guanonis"
                     /db_xref="taxon:1150112"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110895
     Region          29..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkyntsci sllwlffcls tslyaqeiis vqgrvdgaeg plvgvtvlik gtqsatvtds
       61 ngafkikapk gasllfefmg ytsqerevkv namivklnqn teslkeitin tgyynvkere
      121 rtgsiakita kdielspvvn plqalqgrma gvhitqntgi agggfeieir gknslglsst
      181 dankpmyvid gvpisdisvm nssgfttnlf nnsisvlngi npkdiesiei lkdadataiy
      241 gsrgangvvl vttkkgiagk trftinssas fskvgkfmnm mntdqfnqmr deafandgit
      301 lfpanaydmn gmwdrnrytd wqkeliggta iskdislgvs ggnnftrfni nlahgengtv
      361 fpqsgkgfvr nsalinlnhl skddkwninv manysvstnd lpsadlttpa lklppnapal
      421 yeangklnwq nntfmnplap lgktydnevq mlvlntniay kitpstslki naglttntld
      481 ervlephtiw npflnrtsqs sqsqkannss dsfiiepqih wekkfgdhsl kallggtfqs
      541 ntndlfsitg rgfssnafir niglarikev nqignseyky aalftrlnya ykdkyivnlt
      601 grrdgssrfg dnnkfgnfga vgaawifsee sfakdlqwls fgklrgsygt tgsdaigdym
      661 yldtytantv lynglpglyp srlfnpnysw ekttkleaai efslfkdrin tslawyqnrs
      721 snqllainlp eitgfpsisd nfgatvqnrg welnlntvnv qtenwnwttn fnislpenkl
      781 iafpgledst yknryvigkt inlvptynye gidhstglyk ftdydnnnii naqdkkvfve
      841 remkfhgglq ntlsyknfsl dflfqfvkqn nynfdkmvtv pgllstnypl evldrwtisn
      901 pngnytaatt snnaafnqim llqqsnrais dasfirlknv slsyqlalpk lgietvnlyv
      961 qgqnlwtwtn yygidpeftf ignlpplrti afgmqltf
//
LOCUS       WP_090686656             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia phenazinium].
ACCESSION   WP_090686656
VERSION     WP_090686656.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia phenazinium
  ORGANISM  Paraburkholderia phenazinium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia phenazinium"
                     /db_xref="taxon:60549"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39416
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ayetrvaatp etvkkyvsqg hrvtiqsgag tgasfpddaf savgaeivda
       61 aaafgadlvl kvqsptdael pqlkrgavlv gmldpfnadn aaklasagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaadlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswla
      241 rqgalvhera kqadivista lipgrpaptl isvetvqamk pgsvlidlaa grgpeyegqr
      301 ggncpltead kvvtkhgvqi vgytnlasmv aadasslyar nlldflklii nkegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_090688845             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas sp. Nm34].
ACCESSION   WP_090688845
VERSION     WP_090688845.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas sp. Nm34
  ORGANISM  Nitrosomonas sp. Nm34
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas sp. Nm34"
                     /db_xref="taxon:1881055"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39304
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaein agetrvaatp etvkkytaka fhtvlvqsga gasasipdaa yqeagavivn
       61 evsqlygqsq iilkvrgpga eevalmrkda iligllsphq vegievlaqh gltafamekl
      121 prisraqsmd vlssqanigg ykavimaanv yqkffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avieafdvrp avkeqveslg akfvevpltd eekakaetag gyatemsddy
      241 krrqgelihq ravaadivit talipgrpap vlikeetvqa mkpgsvivdm aveaggncpl
      301 selnktvvkh gvhligianl pglvaadasa lyarnlmnfl nlmldaksge lkinqedeii
      361 agtlvcsegq vvkka
//
LOCUS       WP_090700157             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas aestuarii].
ACCESSION   WP_090700157
VERSION     WP_090700157.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas aestuarii
  ORGANISM  Nitrosomonas aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Nitrosomonas aestuarii"
                     /db_xref="taxon:52441"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39205
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir ggetrvaatp etvkkytakg thvvsvqsga gagasipdae feaaganiva
       61 daatlysqse vvlkvrgpda delammrkdv vllgllaphk vdgiellakh gltafamekl
      121 prisraqnmd vlssqaniag ykavimaadi yqrffpmlmt aagtvkaarv lvlgagvagl
      181 qaiatakrlg avveafdvrp aakeqveslg akfvevpltd eekanaetag gyaaemsedy
      241 krrqgelvhe rasvadviit talipgrpap vlikeetvka mkpgsvivdm aveaggncpi
      301 seldktvvkh gvhlvgvani pglvaadsst lyarnlmnfl nliidaesgk lninredeiv
      361 tgtlvcsdgg vvshaq
//
LOCUS       WP_090701122            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Daejeonella
            rubra].
ACCESSION   WP_090701122
VERSION     WP_090701122.1
KEYWORDS    RefSeq.
SOURCE      Daejeonella rubra
  ORGANISM  Daejeonella rubra
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Daejeonella.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Daejeonella rubra"
                     /db_xref="taxon:990371"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117155
     Region          34..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrqflqiil kcfilliisp fafyvetfaq ssfsgkvkds knepipgvsv rvkgttngat
       61 tdingefkin assnqgylvf ssigystiei qmdnrkiyev ilaednkfln evvvtalgik
      121 rdekslgfaa qtitadavvd aktnnwinsl sgkvaglniq gtgagpmgss ritlrgessl
      181 nldnnqaliv vdgvpisski tgtgfnshls qdspvdygsg vsdinpddie tvtvlkgpga
      241 talygsraag gviiittksg erkgnglgvt fnsnfnieqv nrwpdyqfey gegrtntyys
      301 yldspdgint sttvaagraw gpkfdgqsyy qydpntpgnk ptqktpwvah ddyisgyfqt
      361 gqtlsnslsi eggsekssar lsithlknkw iipntgferl naalsfnqkv sdklkitgra
      421 nysnkksdnl pmagynnqtl myfliigttp nirpewfkpy wqpglenvvq knpfnpgpdn
      481 pylamyemln kmnknglign vsatyeiskk fdlllrtgvd msnefrsqqr pfsmtryprg
      541 myreqnvfsy esntdlllsf kdkisskisi sasagantmi qqydfagvya dqlaqpgvyq
      601 isnsldqavv dpsrtkksin svygstqiaf dekifldltg rndwsstlpf knnsffypsv
      661 sssfildeif elpkaitfsk fraswaqvgn dtrpyqtary ydriygnsft npnqlfnael
      721 kpeitssyef gldmrflnnr igfdiayynn nsrnqilsip ldpvtgfsta linaglinsk
      781 gwevqingkp iskekfswst tllwnrnrsy vkeltegltn qiiyqhntnv tiearvgglm
      841 gdmygrgfqr spdgqiiyns anglpapldq varkmgnafa dwkgslmnef rykninlsil
      901 mdgqyggemy sqtnhknntl gktrvtlpgr dngiigqgvv kladgsfvpn tklaqasayy
      961 dnyyqisnae tnifdasflk irevrlefgl panllrklgv qktsvaiwgr dlfnftkfpg
     1021 fdpeggnlnn gtltpgvelt qfpsnrlvgt nltfkf
//
LOCUS       WP_090701648            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Daejeonella
            rubra].
ACCESSION   WP_090701648
VERSION     WP_090701648.1
KEYWORDS    RefSeq.
SOURCE      Daejeonella rubra
  ORGANISM  Daejeonella rubra
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Daejeonella.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Daejeonella rubra"
                     /db_xref="taxon:990371"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118885
     Region          27..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miffkkfill alilifcgqs gvfaqnqlkg ivrdsnkqsl pgvsvkikgs stgvvtsadg
       61 sftlrsdlkq gillfsyigf ltqeitidgr snyeillied atvlnevvvt algikkdirr
      121 lgvaiqtvdg aslvkarepn avnalvgkva gltigtqpel lrrpnislrg nrdvlfvvdg
      181 vpinsdtwnv saddiesysv lkgasaaaly gsrgkngail ittkrgskdk rgfqvdfnss
      241 nmmdngfyai pktqdeygpg dhgkyafgdg rggglndgdy dggwgpkfdg qlipqydspv
      301 dpvtgvrqgt pwlargkdnl krfldpgils tnnisisssg dkynlrfsgs hiyqkgivpn
      361 tklnmtnfni ttdysfsdkl kfesslqynr qytpnipdvn ygpnsiiynm tlwagadwdv
      421 ddmrnywqeg kegiqqiyae yqrynnpyfm syewlrghnk sdvigqaamt ykftpfldlm
      481 lrtqvttwdl mrnekmpysa gsygrderrg dyredrrslf enntdllvrf dkdlvkdlna
      541 kiwtganirt fnynsqfgtt dylnvpglyn fsnsanpvki ynfnsnmrvi sayysadfty
      601 kdwltvsttg rvdklstlpk gnntffypsv alstvvsdyv klpsfisffk lrgsfanvkd
      661 gltqstigtt padsypvgyg dqyyspydgp tyqnsayyst pftynnqpaa rytnvlnnpe
      721 lqpsstsqfe fggdirvlkn rigldfsyfk sdegprifnl pistttgyss tlvngiktkk
      781 tgfelalnas lfkksnglsw dvtanystfk etlneifpgv tnlntffkvg drldkfygra
      841 fvrnpngeii ndasgrpiyn pvsqflghin pdfvlginnr lsyknvslgf qfdgrfggvi
      901 snyiqrqtyr ggrhigtvtg tmgearyqdy lgvkafvgeg vqvangaaik ydvdgkvtnf
      961 seltysqntt kqfvqdyvsr yynsdegnlm nrtfgmlrev vvgynfptkl fnnkvqsfsv
     1021 slvgrnllyf aeskdidlnq yigdggsglq tpstrrygvn lnitf
//
LOCUS       WP_090701854            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Daejeonella
            rubra].
ACCESSION   WP_090701854
VERSION     WP_090701854.1
KEYWORDS    RefSeq.
SOURCE      Daejeonella rubra
  ORGANISM  Daejeonella rubra
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Daejeonella.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Daejeonella rubra"
                     /db_xref="taxon:990371"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113101
     Region          25..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiytlffl pillfltlsa saqvreingk vtiaedgstl pgvsvrvkgt stgattdpng
       61 nyriqvpnnd atlvftfigf siqeirvgtq stinvamntd skqleevivt tglgisrqqk
      121 slgyaaqgvk aeelninrqp nilnalqgkv agatissvgg gpgqganiri rginsidasa
      181 sndplyvidg iqidnststq gsgsganvrs vgnrasdinp ddietinilk ggaatalygl
      241 rgsngvvlit trkgkgagvr tnftstygfe nvnktpaiqk eytagilgvy tpiglgpawg
      301 ptiaeakvid pthpdfiyen yknafdtgsq lrntvsvagg sdvvkffssv sqfnhdgmlp
      361 ftdyqnlsar lntdikispk ivagvnmsfn nsggyrydad rygesltyys grwdvrdyin
      421 engtqkyrgt nnpifgaatn rlkdnvnryi aganvgyapt swlnfnyrvg vdtytdsrkr
      481 tapgrlglpg eavydnadgf vgeylttyra instflatat kqitkdisgt lrlgyelydr
      541 stkdngvlgs vlsiyndfrl vnaktlavsq gmneyrsngf fgeatfdykn ylfltltgrn
      601 ditstlsadn rsffypsasl syvfsdnmkl pafigqsklr lsyaqigkda spyststgfs
      661 nytglptgst gltiasnlgd lnlrpeftdt yeaglemafl knrlsfdfty yyslskdqit
      721 raqvssatgf vtasinagti rnkgielvlg gtpiktkdft wdaslnfsan rnkvislkeg
      781 lseivygsgt ggyinspvtf kiipgqpygn iygsyylryy gssvedpmvt dkskplliga
      841 ngfpissltk qkllgnsqpd wiggfsnnft ykkltlstli darwgfekfn rlenfnsafg
      901 iadytanrrs fytfpgnlad gsantksvwl dqrvgpdgvn ygegyyrlyh rslsepfvqd
      961 aswirlrsas lsyslpskwl paktirnani sitgnnlflr tdyygldpes lsadsgsnvd
     1021 gsagmtypaa rtflftlnvg f
//
LOCUS       WP_090703328            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Daejeonella
            rubra].
ACCESSION   WP_090703328
VERSION     WP_090703328.1
KEYWORDS    RefSeq.
SOURCE      Daejeonella rubra
  ORGANISM  Daejeonella rubra
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Daejeonella.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Daejeonella rubra"
                     /db_xref="taxon:990371"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108433
     Region          35..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvlqtfmn rryifavlam mcygqlamaq nprytikgvi tdarnkeplp gavvkltgtt
       61 qgtstdinga ytlvlnvneg typilisytg ykpvtrtill nqssltlnve lsedalnlde
      121 vvvtgtsvat skkqlgnais tvsakelegg aatsidqala gkvsgaqisq nsgnpaggis
      181 vrlrgnstis gssdplyivd gvivnnssae lldlggysqn rlvdinpadi drieiikgaa
      241 gaaiygsras ngvvqiftkk gksgkpvvsf stqfrtnslr kkvetneypf rfanttatdl
      301 tqipvqrydl qneifttayg tennisvsgg sdktqyylsg gylgnqgiik ntdfkrattr
      361 lrldqrfndv ikvsmgasyt fsgsneipng ginsaygamt gfifgnnfin pypdpssgvy
      421 pslaptglrr tnpleavnrf dfsqqtsrfi sdlqvniepl knlsinytlg fdnstqmgsg
      481 yipigntspe hnagfarkgd rintllnndl nvayrsklgs wlesttsaga taqserinsa
      541 iitgtqlspv sqaassgasi vtsdykstin ilgfyiqqtf giknklyltg avrndvsssf
      601 geanrwqlyp kfsgayilse eefwknssis saipslklra sygqsgnlta igaydrfsny
      661 nsvslaglpg vsapsqygnp dikperqtek efgmdvsflk nrlglevsyy dkavqdlllp
      721 vtlrpssgyi tqfqnignmv nkgfelmlkg vpvqtvnfkw nstiifsknk nevtdipggv
      781 vtfpggfgqv aavngyplga fyatsfarts sgellltpag fpqreltgrn tagqpsgsvk
      841 tsvigdpnpk wtgsftnefs igknlslrmq wdasygndvf nftrrvgdrd lygglkgyea
      901 elrgevpkgt savlfgimen wiedgsylkf relsasydlr akflnnnplr itvsgrnlms
      961 idkykgwdpe tnaagqstav rgfdfvevpi prtialglny tf
//
LOCUS       WP_090704419            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Daejeonella
            rubra].
ACCESSION   WP_090704419
VERSION     WP_090704419.1
KEYWORDS    RefSeq.
SOURCE      Daejeonella rubra
  ORGANISM  Daejeonella rubra
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Daejeonella.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Daejeonella rubra"
                     /db_xref="taxon:990371"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109374
     Region          24..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkllmffl safllasqaf aqeitvtgki tsaedglplp gasikikgtn ifgqtdqngm
       61 ysikaspenv lvfnyigslp eertvgtlrv invqlktdsk vlneivvtaf gvkqevrglg
      121 fstqsvkake ivdskqpnlv nalqgkiagv qitnssgsag assnimirgg sslsgnnqpl
      181 fvvdgipvdn ttplgqgglg agsapasnra idinpddies itvlkgpaaa alygiraasg
      241 aivvttkkgs ggaarvnyqn tfsldqvnri ptlqdkykqg eqgvynatas dswgpafssg
      301 eqvydnlgnf fknafaqnhd vsvsgssdqt ryftsaslld qgsivdnsdf krksfrlnad
      361 tkmgekltvg gsanyvrtdr tyvpqgsang vmgalywprn edmknylnpn gtqrvfnvad
      421 ndnpywtiqn kpiinsinrv iaignidynp fsflnvayrl gtdyysenfk airmpgtles
      481 davrgaiaqt sgdnqittst iivtakktva kdfklslalg qnlesasnrt ttstatrfid
      541 ptfpsinntv aadrtvserl yrrrifglfg dlnvdwkgma yvnlrarndw sstlpvtdns
      601 ffypsvsgal iltdilremg ikpgddtfsy gkiraaysev gkdapahvtt tslasvtntf
      661 tinprgfitn annpfgnptl vpeftkafei gtdlrflknr igidvtyyns kssnqilatr
      721 vppsagaflt ylnggsiqne gvefvfnaqa itnpnfkwsv dlnfakntsi vkalpgtldr
      781 ielsdawvsa naaqgaafln gslfgingnv wkrnasgqll lanngypqvq taltnigdrn
      841 pdfttgitnt fthknlsfaf mvdvrvggkv fnatenslvr sglstktldr gtkvfdgvie
      901 stgvkntisv plnqnyyqti yanqgydfve dggwyrlrya tfsykmpakf lekidvkgln
      961 ftltgrnlll itnysgvdpe vsgsgagvgg sgsfgfdnlg ipatrgvdfg lrltl
//
LOCUS       WP_090704866            1237 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Daejeonella
            rubra].
ACCESSION   WP_090704866
VERSION     WP_090704866.1
KEYWORDS    RefSeq.
SOURCE      Daejeonella rubra
  ORGANISM  Daejeonella rubra
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Daejeonella.
REFERENCE   1  (residues 1 to 1237)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1237)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1237)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1237
                     /organism="Daejeonella rubra"
                     /db_xref="taxon:990371"
     Protein         1..1237
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=135311
     Region          71..123
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          130..1235
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrelynkv llpgfsnkkl llmlnwtitl tfffvlkvsa ssysqnlkvd ldfqnvkfkr
       61 alsiieqkgn irllyseqnl ptdrsitlsv kdtpvmdalg milkdtklgf rvlenglvvi
      121 spqnsdvkdi kvsgtvtdak getlpgvsik lkgtsigvts dlngkysinv pdnvstlvft
      181 yigyvtqeva ingrslvnvq laaantalne vvvtalgmsk ekkslgfsvt evkgsdlaat
      241 qqlnpvnslm gkvagvqidq sasgpfgnsr ivirgnstls qnnqpifvid gvivdnesva
      301 ggrdfandls nlnsenfesv silkgssaaa lygsraingv vlittkkgsk angigvdlsq
      361 nfmvydpykg pefqnefggg svgafftdar dpnyqsnqmw ttkvfpinpi tkepyidpai
      421 drenenwgpr fanqrvrnyd gtwteykavp nnyldafqng tlgttslafs gagdkttyrf
      481 sathddqkgi svankmkrdn fnlrithqla swlstdvsga yttsdntnpq nlawapytdt
      541 fagdnwgvay twmfprnydt kywnqqsryt sqvlggaprg snpletnkvm asefwfnmnn
      601 tvatmdsrnf mgrfalnakl tkwanftveg nlnnnydkye nkalgqftdf rggsytlnqs
      661 kkessfvkgi lsfntikiak dlgfsafagg emynsissft qgntsgglmv pgsyfisnsv
      721 nsplvsggvn ynkkinsvya sadfdyksqi ylattwrgdw sssltykdgs gnnfynypsa
      781 slswiasetf klpsiitfak lrtniaalgk dtdpfvinpg yrfagkvigl pgeptragfs
      841 ssstlspnlk perkiskevg memrflksrl gfdvtlyqdn tydqivdist piesgvsgvk
      901 inagniqnrg veisldgtpv qtnnfvwnsr ltfsrnknli vslaegrtdy flggtafdas
      961 swavvgksyg tirsinqslk ytnpanaadp ktgmtvlawr ndaraafpqr snkfqdigdi
     1021 nanfrggfsn dlnykqwsln vlfdakvggd mamsslrsgt htgvlpntlf grdaehggit
     1081 wtskydgity ddgmiidgvf pigqkitqpn gtaadvggmt fkeayaaglv epthapqfyy
     1141 ryassstgvt dfwirestwv alrqiaisyt lpksiatklk vngisvsvig rdlgylynsl
     1201 pydfnpasln snltsavgee gflpmirsig gsvkvrf
//
LOCUS       WP_090705585            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Daejeonella
            rubra].
ACCESSION   WP_090705585
VERSION     WP_090705585.1
KEYWORDS    RefSeq.
SOURCE      Daejeonella rubra
  ORGANISM  Daejeonella rubra
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Daejeonella.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Daejeonella rubra"
                     /db_xref="taxon:990371"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111445
     Region          25..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknylrcls vllltllsit afaqktitgt vrenstpvpg vtvavkgttk itqtnaegkf
       61 sisanptdil vftmigsarq eivvgnqqti nvtlafsese igevvitalg ikrekkslgy
      121 gvqevkgetl vsakepnlan tltgkiaglq virssdgpag sskillrgsn sltgsnqpli
      181 vvdgvpidnf tgapdngywn rsldmgngia dinpddietl svlkgpsaaa lygsragngv
      241 ilittksgra qdglgitvss sygmsniftn pevqnsfgqg ntgvynatst aswgpkadgq
      301 mvtnwngqqi glatynnvdn ymqqganinn sisfqqlykg asiytsynrl edegivpgtk
      361 llrnnltara iskfgsddrw vtdtkiqysn tkannrpigg rdnssaytly llprsmdite
      421 fqaaknnagn mlwfpgagsq inpywsnqnn lnqdsrdrfi vngsvkynfn kwlnaevkgg
      481 adlyttntqs nvysgspias tgryglgkqt fsetnfstll sarkdnlfgk fggmlsvggn
      541 lmqtnfssls ssvgllvvpn lfslnngvsp agvsegvskr sinsvyssaq isydgylyld
      601 atfrndwsst lsrenrsffy psvslsyvfs dmlsnmgaqm pnwfdfgklr asyaqvgndl
      661 apyqlyntfn igkdpngntt agrntvlldp nvrseliksl elgtelkflq grigldfsyy
      721 ktnatrqlid lpmdalsgyt akkvnagdiq ntgielvidg rvlgkpngln wttsfnysrn
      781 nntveelseg vsryglggfd dvavlavvge kygeiygtry srvkdqaspf fgqvllnang
      841 vptrdpeivk lgnqqarali gftnnfeykg vglsflvdar iggeifsath vamqangtsn
      901 vtapnglras fvapgvvsng tggyvantkt vtpqeywlav atannlgite anmydasnvr
      961 lrnvqlsysl srkllanspi ksakfgvsan nvwlikshmn gidpesvyat nsnatgfena
     1021 glptmrtfli nlalgf
//
LOCUS       WP_090705688            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Daejeonella
            rubra].
ACCESSION   WP_090705688
VERSION     WP_090705688.1
KEYWORDS    RefSeq.
SOURCE      Daejeonella rubra
  ORGANISM  Daejeonella rubra
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Daejeonella.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Daejeonella rubra"
                     /db_xref="taxon:990371"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114053
     Region          23..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfl llfiafqaia qertvtgtvt dktdglplpg vsvkvkgtnv gtstggdgry
       61 slrvpggstt lvltyigyst qeaaigsgnt vnvqlttdak qlsevivtgv agattkeklt
      121 vsvtkvseer lnavtgtsla galsgkvagi kassssgtpg asvdiqlrad nnlnnvgsgp
      181 lvlidgvift gsladvnadd vssmevvkga aasalygsra gngviaittk rgnsiglntv
      241 kvnvrnevgm qeiantldls thhpfalaad yqqyvgtftk yqgvtypagy rdaghsplis
      301 gnrvpkadhy mdnpygitrn qqndffnkgi nyanfvsmts rtektgvyas fennsqegii
      361 emtdgykrqn frfnvdqqia pwlkfstsnl lvntkteypg sgggiffnia laepdinlhq
      421 lnpdgqpyyl rmnhwsgett nplytlykte rnnkrfnwvg nfalnarvts wanfdvshsi
      481 ernnyryrny npkdywtptg gtaatngmsy tngnlqdyse dgnsqntqat lnmvkdfgdl
      541 tlrgklsyly enrryenyqv lssqfgvagi ptydnfatin dagsyneter aqnyfailgv
      601 dykdkflvda myrydgsslf gsnerwnpyy rvsgayrise dvkipgidel kvraaygtag
      661 irpgfawqye tftlnngsaa avqrgnknlk psktaeteig lnvdflkkfs feavyaqsvt
      721 ddqflnvpll gflnngftsq fqnagsvesk tlefslsanw mkkkdfswss nlvysrirqk
      781 itdlpvppyv fgdtdgggqq mffiksnety gamyghswvk sldqmskqlp agktiadyvv
      841 nsqgyviaag tqgmitekai krlddkgail fdkigdgnad fnmglantfn ykratlyfll
      901 dlkkggdiyn akgqwltrdl rnpemdmsgv aqadkkaydy flnfydvntp naywvedgty
      961 lklrevalgy tfplksldvf ggvvksitak vvgrnllnfd nysgydaevg sirqpydgts
     1021 kypnfrnyaf slsmdf
//
LOCUS       WP_090705955            1093 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Daejeonella
            rubra].
ACCESSION   WP_090705955
VERSION     WP_090705955.1
KEYWORDS    RefSeq.
SOURCE      Daejeonella rubra
  ORGANISM  Daejeonella rubra
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Daejeonella.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Daejeonella rubra"
                     /db_xref="taxon:990371"
     Protein         1..1093
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120269
     Region          30..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskntslrc lfsvialllf tvaqaqtgri tgrviseddk lplpgvtiqv kgksalsqtn
       61 aegaysieas andilvfrfv gylnqeirvg tsdivntslr mdvshldeiv ilgygtqkrs
      121 titgsvskld pkiletgirs npasalagti pglrvqqtsg rpgavpnivl rggttygggg
      181 splvivdgll rggfsdinqd diesievlkd asataiygar anngvilitt kkgkegvsni
      241 sfkgktgink lnipfnflng rdylywsrka iqtsglyeps rltqltstgp fgtgnlfkda
      301 sgnfldgnvt gnavwstmfl ddvnkiklqn gwetmidpvt grelifnnfs ykdyalrdqa
      361 ltqdynvsmt ggnekgryya glgaydeagm pintfykrlt fvfngeykvk pwltsissln
      421 fadakwrdpa tsgegnyltr algapptmrg vnekgellig rdlsdgnpav ndaklirrnn
      481 snkftlsqaf kvdflpnlsf rasgnwyyde gfsesfnkdy lnspgninvt rassasfgrg
      541 lnqtyngvln yratllekhh fdlmagteff dsyakglsas gsgapsddfm dlaltnsdkd
      601 rraidsyhnr esilsffsra nydfdekyll tlsfrrdgys kllnnrwgnf pgisagwnih
      661 kedffkrfsn vvnslklras ygengnvsgi sqyglqgsys tgkyngsigy lagglpfpnl
      721 lwersatyei glesrlldrl dvsvayydrk ttdkissftl patsgftslt tnngsmqnrg
      781 vevdlnynvl rkrdwtinfs anmayntnkv lklpenglln nriggfevyd pksgqlvfvg
      841 gtqqgqdpnv ayayvaqnly rtqadldada nrrdllgakv lvgpgiysgm ttaqkatvfp
      901 ialgdvkwqd vngdgtinsf drvkmgstvp kwiggfganf kwkslalysr fdyalgfvqy
      961 dgprswflsn aqgtfnttdd vfdtytpent natfptyywa dqlyknntfr essmfykkgd
     1021 ylalrevnvt yslptkwank iksqninlsv sgqnltyfsq stlyspesgs igiggsggyp
     1081 lprtiifgaq ltf
//
LOCUS       WP_090706773            1163 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Daejeonella
            rubra].
ACCESSION   WP_090706773
VERSION     WP_090706773.1
KEYWORDS    RefSeq.
SOURCE      Daejeonella rubra
  ORGANISM  Daejeonella rubra
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Daejeonella.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Daejeonella rubra"
                     /db_xref="taxon:990371"
     Protein         1..1163
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126353
     Region          159..1161
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mifftlnaeh qqknllgynl rlffektfll imqlrlalfi vlttsiqlfs appvksqamd
       61 eveirlelkn esllnafqki ekqspfhfmy ryadvkdidk leipsskksv aaflqemlan
      121 tsldfkqvnn rimiissekk nldpspliln dklireldiv vrgqvkdqkg etlpgvsvkv
      181 kgseigastd idgryslnvp dnatlvftyi gyntkevvvn nqttlnvtld psstsltevv
      241 vtalgikrea ksltyatqgv sakeltetrt lnvvnalqgk vagmtietag tglggaarvv
      301 lrgnrsisgn sgplyvvdgv pmstaianfs pdniesinvl kgpnaaalyg saaqngviii
      361 etkkgkegqv qisvnetfqt grplhyfepq seygqgvtgv ynatseeswg pkmtgqmvnh
      421 wsaapgkagt qvafspqpnn ykdafqnsty ithnvnatag sattqtafsy tredakglmq
      481 nnelrrdnas vrvtsklkkw lsldtklnyi rneidnqngt gdnaannpym niyrmprnil
      541 isdlrqfeyt dasgankqny wnpgstigrn pfwimnrvvn fettdriial gsltidftdk
      601 lklmartsfd ggsstterka widsygggqd nfgsysasis gpgqiwnhda llsynsnitk
      661 nlnvsalvgg tlrktdgsgs isastqqgli ipnffsfgnt altqgafnps trqelqslyf
      721 sgnfgwknyl yldvtgrndw sstlpansrs yfypsvgiss iltdmipglp dvisyaklra
      781 syakvgssas pyqlsrsasf sgtggnygfi tlgailpnan lkpettegye igldtrlfdg
      841 rlglditayk tntfdqlftv slpsgsgaas fftnggdvqn tgielvlsat pvrnangltw
      901 dissnfgknk nwvnkisddr psiivggdpy msdfvvaqgq efgniytrgw arnaqgnviv
      961 gangmptlta grsvlaanfn pdwmgaitnn fsyknfnfaf liehrqggsm vsitdgllyg
     1021 eginketlag rdgglvfgen lfpnetgvla sgapnttait sqtfwrtigg rnapigeafi
     1081 vsatntrvre atlgytfpks mlskvgfisg vklslvgrnl fflkrtgnwd peilsgagta
     1141 sagfqtyvpp tertfglnlk vdf
//
LOCUS       WP_090707941             379 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Beijerinckia].
ACCESSION   WP_090707941
VERSION     WP_090707941.1
KEYWORDS    RefSeq.
SOURCE      unclassified Beijerinckia
  ORGANISM  unclassified Beijerinckia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Beijerinckiaceae; Beijerinckia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="unclassified Beijerinckia"
                     /db_xref="taxon:2638183"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39427
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpiete gnetrvaatp etvkkfiglg atvtvqsgag ikagipdsef etagakvaps
       61 aadalsgaev vlavrrpsae llshvpkgaa viatmdpygn ddalkamada gveafamefm
      121 pritraqamd ilssqanlag yravidgage ygralpmmmt aagtvpaari fimgvgvagl
      181 qaiatarrlg aivtatdvrp atkeqveslg akflavedee fqqaqtaggy akemskeyqa
      241 kqaaltathi akqdivvtta lipgrpapkl isadmvrsmr pgsvivdlav erggncelak
      301 pgevyvtdng vkivghlnvp grlaatassl yaknlyafve tmidkekkal ainwddelvk
      361 atlltrggav vhpnfqpka
//
LOCUS       WP_090717318             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas sp. Nm166].
ACCESSION   WP_090717318
VERSION     WP_090717318.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas sp. Nm166
  ORGANISM  Nitrosomonas sp. Nm166
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Nitrosomonas sp. Nm166"
                     /db_xref="taxon:1881054"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39372
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir ggetrvaatp etvkkftakg vhkvsvqsga gagasipdsa yqeagaaivt
       61 saaelyaqse ivlkvrgpes seiemmrkda vlvgllspqh kdgiealaqh gltafamekl
      121 prisraqsmd vlssqaniag ykavimaanv yqkffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avveafdvrp aakeqveslg akfvevplne eekvkaetag gyatemsddy
      241 krrqgelvha raiaadiiit talipgrpap vlikeetvqa mkpgsvivdm aveaggncpl
      301 seldktvvkh gvhlvgiani pgllaadsst lyarnlmnfl nlmldsnnge lkvdrsdeii
      361 agtlvcadgq mitqpl
//
LOCUS       WP_090735624             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            homiensis].
ACCESSION   WP_090735624
VERSION     WP_090735624.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus homiensis
  ORGANISM  Paracoccus homiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus homiensis"
                     /db_xref="taxon:364199"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55659
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkevi egearvavtp ssaghlqklg hdvfvesgag sragfsdedy rkanvtvlgn
       61 asevigavdv vakvrvpedg eikqmregqt lisffypaqn gellevakeq gitaiamdmv
      121 prisraqkmd alssmaniag yrsvieaann fgrfftgqvt aagkvppaki lvvgagvagl
      181 aaigtstslg aqvyafdvrp evaeqiesmg aefvfldfee katdgaatgg yaapsspefr
      241 eaqlkkfrel apqmdvvitt alipgrdapv lwtkdmveam kpgsvivdla aekggncelt
      301 vadervvten gvviigytdf asrmgaqase lygnnirhfm adltpkkdgv idhnmdddvi
      361 rgatvahdhd vtwpppkpkv aaiaaqkpke kkkeltpeer kaqevaafka etksqvtmla
      421 lgavvlllvg lvapasfmsh fivfvlacfv gfrviwnvah slhtplmait naissiiilg
      481 almqigsgsw lvvilgalav lmagvnifgg fmvtrrmlam fqks
//
LOCUS       WP_090731353             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azotobacter beijerinckii].
ACCESSION   WP_090731353
VERSION     WP_090731353.1
KEYWORDS    RefSeq.
SOURCE      Azotobacter beijerinckii
  ORGANISM  Azotobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Azotobacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Azotobacter beijerinckii"
                     /db_xref="taxon:170623"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40311
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkllgqg htvtvqsgag leaslpdsaf eavgatigda
       61 aaalgadlvl kvvapspael aqmktgavlv gmlnpfddgn iarmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee rqcaegvggy arpmppswme
      241 rqaravhera kqadivitta lipgrkaptl lheatvqemk pgsvvvdlaa aqggncpltv
      301 pdevvvrhgv tvvghsnlpa lvaadasaly arnlldflkl vvdkdghfhl dleddivkac
      361 lmceggrvvr tnggapspsa avpratkena
//
LOCUS       WP_090745115             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            tibetensis].
ACCESSION   WP_090745115
VERSION     WP_090745115.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus tibetensis
  ORGANISM  Paracoccus tibetensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus tibetensis"
                     /db_xref="taxon:336292"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55760
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalresy egearvavtp ssathlqklg hevvieqgag aragfsdeey rrsgvtvvpt
       61 aaeligqadv vakvrqptea elrqmragqt visffypaqn aellalakeq gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigasvslg aqvhafdvrp evaeqiesmg aefvflefdq pvqdgaatgg yaapsspefr
      241 ekqlakfrel apqmdivitt alipgrdapv lwtrdmveam kpgsvivdla aekggncelt
      301 vpderivten gvtiigytdf psrmaaqase lygnnirhfl fdltpkkdgv iahnmeddvi
      361 rgatvahdhd itwpppppkv aaiaaqkpke kkreltveer raaeavafqg etrrqvalla
      421 gggallllig lvapvsfmsh fivfvlacfv gfrviwnvah slhtplmait naissiiilg
      481 aliqvgsgsa wvtilgalav lmasvnifgg flvtrrmlam fqks
//
LOCUS       WP_090753788            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Nonlabens sp.
            Hel1_33_55].
ACCESSION   WP_090753788
VERSION     WP_090753788.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens sp. Hel1_33_55
  ORGANISM  Nonlabens sp. Hel1_33_55
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Nonlabens sp. Hel1_33_55"
                     /db_xref="taxon:1336802"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110648
     Region          22..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mcktlpflfl fasflvigqn trsisgsvtn aageplfgvt vqikgttlgt ttdfdgkfny
       61 ilrnqdntst vlvfaylgyl pkevqigtks vfnirldedv esldavvits sygtkkrree
      121 vvgsissvkp gelaieqpat sidellqgqv agvfietnpn lgepvsinir gqgsltpltn
      181 navgtstqpl iivdgiilte elgidgsaff dagtnalsen flnplarvgi qdiesievlk
      241 daaavglyga daangvilit tkkgtagpik fnasfqggis dsfngikyln geqytelrni
      301 yntnngdlnn irewngvntn wfdllnqqgs ysrytvgasg ggeffrfrgs vsyqnrtetq
      361 iansfeqfnt alstsyvskk lnatlnlsps wiaknnpntl yafavdptip vrdadgnftp
      421 fatygnplav aqqniaeakt fallgslnin yrftdylnat vlygtdysnk deqkffsgln
      481 gsgiyntsgp grrlirdrdt rswnfsttva ydqswnevhn fdaiagfetr gekvnlsfvr
      541 aqgfqnftsp qpienaevid qrddtseryg rsaftqlnyn fdktyfllvn fridqssafg
      601 ddnntafngg agaswvisne kffkentftd flrlrasygt tgnsrigsyr alglytvdnn
      661 dpfdgytgnp sgsatltqda pnpnlgwekn nkfnlgldwn ifnklrmvfe vfndkrndli
      721 vsrpvipesg yaniqingat mrnrgieftl esswvknedf ewttsfniat ldseildlvg
      781 ssssfsaatt araqqigsst taiygfeslg idpatgrelf lvdgqvydsa yvrenfdnsd
      841 wvvlgdsqad fygglrnnfs yksfnlgiit tyaygadqlv nrtlidsynt ltnrnlnvna
      901 fyeawrapgd lagypaptns vsiinssryi ydtsnfqlks vtlsyvapvd kwklpvktls
      961 fnfngsnlyt wykeksapgr ngiaefknty peqrtfsigi nttf
//
LOCUS       WP_090754415            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Nonlabens sp.
            Hel1_33_55].
ACCESSION   WP_090754415
VERSION     WP_090754415.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens sp. Hel1_33_55
  ORGANISM  Nonlabens sp. Hel1_33_55
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Nonlabens sp. Hel1_33_55"
                     /db_xref="taxon:1336802"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110064
     Region          24..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklngilt lllalvvqva faqqtvtgkv tdpagepilg atvlvrgssn atttdfdgny
       61 tilarpgevl tyqfsgydsq nitlgtqsvi nislktslea vvvtsyrtss kaksnvaast
      121 vtnetienrp nasfvqtleg qvaglniftt sgqpggnsvv nlrgigsing nteplfiidg
      181 apvdednfrs lnpqeiaevt vlkdagatsi ygnrgsngvi iiktkrgsfn splrisanti
      241 lsfntlqdnd ynrlnsqqll tlerqqgvgr gatlsdaeia aadnfdwtdy ffrtgvsknn
      301 tlsltsggen ssqftslgyf eqdgilinsn lkrfnvrsnv tgksendrfq yntnlsmnys
      361 rsdepnnvgt gginrnyllg alqsvpyitp ddytnggdlt splsftntpl flldlgrtfe
      421 rfeeeikllg sanfsyqltd nitarsvssf dyqnisltrs erpdsfnall fggeanptag
      481 fqdqsttrqf sfnqltslgf nktfndlhti dvglyteyfk ahlrsfgyfa ngldgrtfsp
      541 gdgsgfvgar lnedadgilf ndtaraniln sglfsyfasa dydydgkygl gatirrdass
      601 rfadtfryat fysvsgrwnl seedflegne tinslklras ygttgnqniv gggyfgglnl
      661 trdffvtggg ysnnnalfpg pipnpflkwe ttsqfnvgvd yalfdnrlrg sldfytrttd
      721 dlyqstpisg tvgtggfltp anfgsltnrg idlelrydii rgqergdfel eaffvgnynq
      781 neldelpgdd gqvigvgreg gpigeyfsvr yagvnpangn llfltadgdl tespnpdtdr
      841 vfldknitpe yqgsfgfnad fkgfffqsqf qyaggidrfd ndlsivqdit slgqfnlsed
      901 llrawtpdnr vtdipslnat nldfastryl resdyvrlrf vtlgysfnrd vlqkmnltnl
      961 klfvnaenlv tftkwrgfda agyqngsrqy ptpkivsfgv eigi
//
LOCUS       WP_090755861             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            chinensis].
ACCESSION   WP_090755861
VERSION     WP_090755861.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus chinensis
  ORGANISM  Paracoccus chinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus chinensis"
                     /db_xref="taxon:525640"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55561
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigalketf dgearvavtp ssaghlqklg hevhvesgag aragfsdaay egagvtvhpn
       61 aaalteavdv vvkvrpptde elgrmregqt lisffypgqn aellerardl gvnaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaatslg aqvyafdvrp evaeqiesmg aefvfldfad qvqdgaatgg yaapsspefl
      241 akqlekfrel apdmdivitt alipgrpapk lwtedmvrmm kpgsvivdla aerggncdlt
      301 vpdakivten gvtiigytdf psrmgaqsse lygnnirhml adltpakdgt lvhnmeddvi
      361 rgatvtrdhd vtwpppppkv qaiaaqkpkp kvkeptpeer raaealafrr qtrsqvgmlv
      421 tggvlmllvg lfapasflqh fivfvlsvfi gfqviwnvsh slhtplmait naissivilg
      481 allqigsgsa livilgalav lmtavnifgg flvtrrmlam fqks
//
LOCUS       WP_090756125            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Nonlabens sp.
            Hel1_33_55].
ACCESSION   WP_090756125
VERSION     WP_090756125.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens sp. Hel1_33_55
  ORGANISM  Nonlabens sp. Hel1_33_55
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Nonlabens sp. Hel1_33_55"
                     /db_xref="taxon:1336802"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116910
     Region          20..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkritlvmlm lcvftgwaqi titgtvsdaa gnpiafanva ergtengttt svngdysitv
       61 aedavlvfsf vgyqsqnlpa tasgslnvtl qegdaldevv italgikrqe relgyavqtl
      121 dtediqevks vnlvdnlqgk vagitvtpga tgvgssskit irgeasfsnn nplfivdgtp
      181 innnsvfnft neaaagfqev dfgngagein qddiasvsvl kgpaaaalyg traangaiii
      241 etksggkkrg lgvsfntsff mdsafklpef qnefgqgnsg qfeyvdglgg gindnisysw
      301 gprldqgtli pqfdspvtlp dgtvvrggdt alysglditp tpfvshpdnl knfyetgyta
      361 inniavsngf ekgdyrlsft dlrsesiipg vnldrqtvaa klnfrpsdkt rinasinyvn
      421 sesdnrpsng ygsenvnysl vawgprslni dslrdywqpg legvqqysfn ytffdnpyfi
      481 lkenrnsfgr drlfgnisis qeltseltat vrtgmdysne krrflrnyss nrfrngayae
      541 hdvfyreint dfllnyqkqf gdfsfdasag gnrlnqtaqt tqiqttslaq pgifslnnaa
      601 spietfgfts ekrinslyaf akagyknfly ldvtarndws salatpftad ntsffypsvs
      661 tsfilsnvve lprvidfaki rasyaevgnd tspyqtqgtf lsqtpvnsqp tfsnqdfipn
      721 anlkpettss ielgfdvrfl kqrlnldfty ynavtddqil slpiaissgf sqqvvnggsv
      781 rnqgveiiln aipvqntnfe wsatanfass raiveslpqe dgrltlglsr vydnsdqtvf
      841 hqveeggrvg dlygtgyirn edgqfiltpa grfiadpelr klgnynadfq lgltnsfryk
      901 dfdasflldw rqggilvsrt lalgavggql ndtsfrpeeg ivadgvintg tpenpvyvqn
      961 ttavtaesyy rqfydrnhee nnvydasylk lrqfsigynf elkdgafgif gdgadlrvsl
     1021 igrnlfaise iphfdpeqla vqgqgfvngv edmsyastrs iglkaginf
//
LOCUS       WP_090756105             967 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Nonlabens sp.
            Hel1_33_55].
ACCESSION   WP_090756105
VERSION     WP_090756105.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens sp. Hel1_33_55
  ORGANISM  Nonlabens sp. Hel1_33_55
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 967)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 967)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 967)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Nonlabens sp. Hel1_33_55"
                     /db_xref="taxon:1336802"
     Protein         1..967
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104578
     Region          21..965
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqklkiatl llllplfala qtvrgtvtda stnlpvlgas vvvqgtsngt stdfdgnytl
       61 nnvpedgiiv isylgyatqe ipytgqqtln ialaedaaql daivligyge vrqenvtaaq
      121 ttvsdeefnk gavvspgsli agkaagvqvt aatgrpgdgp rirvragstl sanadplyvv
      181 dgipldsrna nlntinpadi esftilkdas ataiygnras ngvilittkk gkfnrelqig
      241 ynvqfaidkn tddvdvltgg qfktlvneig taediallgn astdwqdriy qtatraihni
      301 tlskgyents wranlgytnq ngtlktsgye rasinasviq nlfnddlklt lsvqgaledi
      361 nsadegaigs sidfdptqpv fdpngpngff eyfqnngtvd plaprnplgl lnsldagttn
      421 dqirttlqad yqipgvdglt lngtagidyn efdtfsnrlp nsgvglttga lnsssngfrv
      481 nqllngrvdy ktdlenldss leltvgssyq efrresvsfs qdntgapvqp fnafnknvli
      541 syfgraifdi kdllvlsasi srdgtsrfsp dnrwgtfgga saglkltnld fvqesgfvsq
      601 lklrggygvt gqqdigedfl fiprstpstd qarvqigdrf fttvrpeltv dlkweetsqw
      661 nvgldygffd nrlsgsvdly trdtedllqf gplaagslgn falqnvgstr srglelaasl
      721 dliraedfnw eiggnltfne ieitdlslge ndapvpqtpv ggagfnnfiq ewavgadpta
      781 fvvyrqvygp dgnpldgifv drngdnvins ddrvrykkgn pdaffgftsn fnykrfdmnf
      841 tlrgavggyn ynnvrasren adaitenpgn wlnnstdgil ndrfssapln llfsseyiek
      901 sdflrldnls lgytfntdki girasvtgtn lfvitdysgl dpeigngvdq aifprsrgvi
      961 fglnfef
//
LOCUS       WP_090763022            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090763022
VERSION     WP_090763022.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116867
     Region          28..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkflrkls wvlvlltmis gslfaqqrqi tgkvvdkkdg qpvpgvtvgi rgktnnvstn
       61 dkgefalvad pstdalvfsy vgytrqvipl agktnitvsf vedsknlded avvvigygtk
      121 krsevlgava titgaeiqdv papnlagalr nrvagvgvsq vsgrpgspit lnirnstvsd
      181 qarlngatde plyvvdgitv trdafdnida smvenltflk dasasiygas gakgvvlvtt
      241 krgkigkpsi syngylgisd aaqtpemlsa ydhavllndt yrtqkaalsn fflpedlayi
      301 ktlnykswyd evwqpatmqr hnvgisggse ritffaggny qrengnyagm kfdkygfrsg
      361 ltanlanglk adinfnvdyn ikelhhnand qdntfferii sipqwvpisi ngnyvnfsan
      421 nstinplava esgyynkgys kgyrinaalt yeptflkglt akfqisqasg stkstqyvpp
      481 yrlynyvrsg nnqqlftdql vntsatsfyf eptsaasani tpgvsennsy qgfltlqytk
      541 sfakhsvsll vggeqsegns qessvrytnq lipdidqywa fdattlarqs fartavskrs
      601 ffgrfsydfd kkyllevitr ldassnfatg nrwglspnig igwvasqekf fkdanflkfi
      661 nfaklkvnvg ttgddrvgsr lwqdrfqidv tngylygnsn qnslnrarla npditwekkr
      721 tinigletsm fnnkldfsve vfqnrnydaf dlggnnlfpl yfgtaapvvn yretynwgse
      781 fsigykarla tdwslsanvn fgwgnsvvnr tlyapgqlin nvapdwqtqf gtdprvysss
      841 niglktigmf rtqaevdawm akypnyrlyd qvpqpgwlyy edtngdgvis dsdmkpmfkn
      901 tnaflatgis lnltyknfsl ntninarfgg kvfydsrari apsatrnilt iwqdrwtpdn
      961 pmqgklprfd dpsltknsdf wavdgtmiri ntmtlsykap tafanklgig garilltgnn
     1021 lwtivnplpy kdpytssayd ypilrtislg lsvnl
//
LOCUS       WP_090763031            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090763031
VERSION     WP_090763031.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117302
     Region          28..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkflqkis lsmlfmllas tilyaqdrkv tgkvvdqadg qgipgvnvsl kgvpsnvstn
       61 sdgvftiqvk snsdvlvfsy igyvrqqitv gsqsnitvkl vsdnkelddv vivgygtqkk
      121 asltaaiaqp dlkkvedvpa lslsavlrgt mpgvtvsggv qrpgqtasit vrnpsvlskd
      181 sqqgtnpiyv iddvvrtqqd feqldqsmve sisvlkdaea aifgvsgsng vvlvrtkrgr
      241 igtprinfss tvgfsnatkl pelmsglelg nyvndylnas vyaqtasgvp ntnyintdgy
      301 rvingvadlt rqtqwytpde lqyfannnhn wlkeafqtst llrnalnisg gtdkvnyfig
      361 gdyvtqnsnf kginsdkygl rasieaklsk rltvsgsisg dvnstksyfy klnstsesld
      421 ndvaslqnvn pwseyyidgn pvilgssntg gldnvnfflv qnsdnftggk rytmnflgkl
      481 tydipgikgl qatftgnkni nssnskqfgt tftyykyagq glnshipgga llgtytikng
      541 drvrlnpifa enyqlnagfn ynrsfgkhni salalveqre sssegvaamt egvvagglpy
      601 qtftvgtqts tqssqisqdg fqsfisriny dydnkyllql vyrrdgsakf spgnnwgnfp
      661 aasvgwvisq enffknnvkw idflklranv gltgtdatka yqylssynlg tgssggavfn
      721 egdrsiaikt nvaipngavv wdhalktnyg fdmqllkgkl slsgdyfwnh nydmlatlqs
      781 svsfligaav ptenygslnn fgyefsatwk dkigdkftys fspfytwndn kiikydlasg
      841 kvgtiedltg kssdagyfgy kslgiirtqa dadaiiaqra naaggsnkvk ildnflqpgm
      901 inyedvngdg litvadkqfi tkrqnnhnnl glnfsvgyeg inlnviagls wggytsvggl
      961 kasgtgatvy nnrasywadh wtptntgaay pnpyftsale dsdfwlvsat qlgitnanls
     1021 ysipskvtgk iginsirvfv qatnpvqfin pfpnnyrdfl tplgtyptlr tvafglnvgl
//
LOCUS       WP_090763976            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090763976
VERSION     WP_090763976.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114210
     Region          26..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfkkiksiaf illlftaqql laqnvvvtgt vksadgetlp gvsvliketk qttitdgkga
       61 fsinapeknt lvfsyigfkt qeiqiskngp isvilqssdn aldevvvtal gisrekkslg
      121 yavqelkgdr vaeakesnlv nalagkiagv rvtnsqgsmg ssrvvirget siagnnqplf
      181 vvdgipvdns qlnsagardy antisdinpe diesmsvlkg pnaaalygsr aaagviiikt
      241 ktgkskkglg iavnsnavle tlltlpvyqn afgqgsegkf syvdgagkgl ndgvdeswgp
      301 kldgrlipqf fskgvavpfe ahpdnvrdff qtgyslnngv svadagekyd yrisynnlkq
      361 vgivpnsgqg knsfvlntsl kitpeltlta nanysklnsd nlpgtggsrs tstmlqftwf
      421 grqvdinqlk nyldengktf nwnnsyysnp ywvayentvs qnrnriigsl alnykiidgl
      481 dlnfrsgtdy yndrrkvria ygtngtpfgs ytesaftvne nntdatlnfn kqlnddfsle
      541 llgggnirrq yieqndqsap klaiaglytl knsrdplvss nnlsrlksys iyasgqlgfr
      601 nylfanitar ndwsstlpaq nrsyfypsfn gsfvateafd iksealnylk vrggwskvgk
      661 dadpyrlint yvfgapfygn pqlttgaidl npnlkpettt stelgveavf fnkrlrfdls
      721 ayntnsynqi laadvsqstg fsskllnagk innkgieaql gitpvkkaft wdvdfnfaan
      781 rsrvieldae klltnyvvas nsaqviatvg qpygslfgta flrdgngnii vnatgapatn
      841 ptkqvlgkyt pdwiggvynt ftykgislgv lvdasiggsi yngtyatgty tgvlastlpg
      901 raaeyggisy yypgndktkg tvrlngaapa getvyddgii fdgvtadgkr ndkilpaqqy
      961 yksfrnidea nifsasyvkl revklsynlp akwlrplslq gvsvslvgrn lwiihrntvd
     1021 idpevafntg ngqgleslsn pstrsyginl nvkf
//
LOCUS       WP_090764013            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090764013
VERSION     WP_090764013.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111264
     Region          41..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrslqltcl llyasaglya aetannalpl nsisahyqep ikgivkdgtg ltvpgvtvnv
       61 kgtkvntqtn angeykiaak tgdvlvftfv gyqtkevtvg tqttidvtla ndskeletvv
      121 vtalgikrse ksltyttqqv ggeelnkvks pnlvnslngk vagmtispst sgvggsakvi
      181 lrgsrsvsgn nqplyvidgv pisnngnana qqnsvfgggq dggdgisnln pddiesltvl
      241 egasaaalyg sqaqngvili ttkqgkagkt qigfsssltf dkiaykpefq nsygpasttt
      301 rdswgaainn stdnldqffq tgtnatnsin fsggseiaqt yfsyantyas giqegnklnr
      361 hninlretak flnnkltvdg tvnyinqrin nspsiglynn plvglylfpr gvditpykdn
      421 yllannvgta rqnwlggsad inqnpwwltn mnpntairnr fllsgnvkye ftpwlniqvr
      481 gnidrstddf enrrysging nfnsngrgyl sqntqtfiqk yadailnvtv pmknsdfkin
      541 gliggsindq ktsglslagd lsavdlftpn ntivatagny tsdvlsttka sdafhsqlqa
      601 vfananlsyk dwafltltgr ndwssnlsft pnvsyfypsv glsfivsqmv klpeaitfak
      661 irgtyaevgn tvpayltfiq ntlgnggalt intnrafael kpertksfei gtdmrflanr
      721 lnfsftyykt ntknqyipvk papsglvatg ylnagdvqnq glqftlgadv lkgdglnwnt
      781 aingslnrnk iidvaasqgl nsidltgggn nayisriaag gsygdiygyt lqkdasgriv
      841 fsgdgttanp yfpiksadys liananprfq lgwnnsfnyk dfslsflvdg kfggkvlslt
      901 ealmdqagas kvtgdaraqg gvkidgvdas gkavsatinp qsyysflgdr ngvtgeyvys
      961 atvvrlreas lgynlplkgt fksmrlslig rnlfyfykka pydpevtmst gnglsgidvf
     1021 nqpvtrsfgf nlnvlf
//
LOCUS       WP_090764400             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090764400
VERSION     WP_090764400.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107336
     Region          26..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkaiifivl aalcpnfkls aqtttqitgr vvtesdgkal pgatisikns stavqsssdg
       61 tftihtkttg gtlsitytgy rtkeitfngs qknleikmqe stnsfddiqv igygkttkkl
      121 ntgsvssisa eqieqqpvtn vlsalsgrmp gvfiqttngl pggnisvqir gkgslaagtd
      181 plyiidgvpy dgapvgkgnt dvlniagavs plnnispadi esisilkdad atsiygsrga
      241 ngvviittkk aasgptrfel niqqgastvs arpklidlqd ylsmrraafa ndglipssdp
      301 tsanyapdlt iwsqtqqtdw vdyifghtan stnlqtkisg gkgnttfsvs gnfrsegtvl
      361 pgnnsylrgg msaqiqhlse dqkfsirais qlsrqnsdls nivsnldrsy ltapnypfys
      421 pdgsvnwyag nllaeinars knatdnsits ldlsyrilps lsfrvnsgyt rtsydqkfis
      481 pssslqpgil nstnfsftgt qsfisepqld ynlrlgkhkf sfllggtyqm ksserrsiia
      541 rgytleslme npgsaatvta tgtstnyrya slfgrvtynl mdsyiinltl rrdgssrfgp
      601 gnrfgnfgsa gaswifsnls wmkknmpvls fgkirasygs sgndqipdyg ylstysspgs
      661 ivyqgipvir psrisnadfk wentrkldlg velaffkdal sltadyylsr ssdqlvsyai
      721 pqisgfssyq anlpaviens gwefgisssn fkgkhftwts slnltiprni lksfenfens
      781 syasiyeigy disrirgyrs lgidpatgkt ryagqngevs atpyfnytig rsapdfyggl
      841 gnsmrwnsfe fslllqfvrq qskgglirnp ggsgafnefd lpvwsqanpg atvpppstqf
      901 dfyygqssan ifdtsylrik naalayhlpe klakklglgn lkvfaegqnl ytfwkrnsgv
      961 idpesgalss tsgknipplk tfvlglqlnl
//
LOCUS       WP_090766049            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090766049
VERSION     WP_090766049.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111709
     Region          49..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkinllkitg lsaaivllns pafsmnaklg vtggrsgesk lllhapvrki vsgtildesn
       61 qpvpgvgikn vtsgkgavtd vngkfniean vgdlirisyv gyitqnitia nqttlniklv
      121 vsadtklddv vvvgygsrsq reltsaitkv dttqfrqsga rnaldllqgk vaglqitrss
      181 snpntgvaiq lrgvtsisgt asplividgi pggnldllqq ddiesftvlk dgsaaaiygt
      241 ranagvilvt tkkgrkgaaq fsyngyakhe tlyerpdfmn atqfrekiaa gqytakdygg
      301 dfnyfddlin kdnltnyqnl svsggsdksn yrgsftynkl dgfarensre qyqfrmsltq
      361 kgfkdkvtam fnvasninra nllggggwet vltknptesy ynpdgsylft rnitneiarl
      421 aqetskrnqq tysvdgkidi dimkdlkasa fvayqrnqyi dnqyrllgsq nsvengdapg
      481 ggyaykgtel nenfnfepti eysktikdkh rltgmigysy ryevnesfsa nnrgytndif
      541 gennlgsvpv avnrigiasn kndntlialf grvhytfdgk vnleavlrre gsskfgannk
      601 wasfpavsas weitrekfme nakwlnflki ragygetgns gfanyaslvt lstgnlypfp
      661 ggqwlqtygp srnpnpnlrw erkkeynlgl dfalfnnkls gsvdvfkrdi edllytytsp
      721 qppyvansiy tnvgtisakg ieltlsyaai knkdfswnvd fagstidnkl vtfsndefrr
      781 dmeqfgsigg agdlgnafrt yegrnigefw gkrfnsftpd gkwlftnrag qavpnaqint
      841 spfrdqtdlq vignaipkyy lslgntftyk qfdlriflrs kldfdvlntv alsygnkfgt
      901 qgnllnsaft kyaeindtym ysdyylengs flkvdevtlg ytfkfkdkav rslrlyavgq
      961 nlalltgytg ndpdliqdtg lgqeingrsl gidtrspypt trsfvfgvnl gf
//
LOCUS       WP_090766287            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090766287
VERSION     WP_090766287.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116711
     Region          56..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkiyilifl mgfcpviafg qvvfggkils aadsiavpan velmgadglv rklqadrngi
       61 fsvsvpggty rfvatavgfk ayavtvsipl pkgfvvsllp adnqlgevtv stgyqvldrt
      121 ratgsfdkld ktrldqqvgk nlldrleaig ngltfdrsts atgkfsirgt stirgprdpl
      181 ivvddfpysg dlsninpedv esitvlkdaa aasiwgtrag ngvivittkk gkkntplsas
      241 fsassafvqk pdlryeqris sadaldveqf lfgkgyytsq inssqksalt pfvellilna
      301 sgklsdtdla laktgfaahd vyedfdryvy ktgvnqqyal slsgggekhs wlvssgynrn
      361 idnldgenar qnlrlsnsfa llrnlnlntv fsytggkvra grpgiggils tsslypyaaf
      421 adangnplpi tknyrsgyls spaiaqlldw syyplldnqy tdnvtrltdl vasfdlgykl
      481 plgfkaslky nieeqrtnre ilqqlgsyyt rnlinsfaql gsggvvsypv pigaivdrne
      541 grlrseqyrg qldfnrawss hrldaligve wrkaqstgvs grmygvdtdk lttgpidytr
      601 tfpnsvsgsl ayipdgngls qvannyfsqf vnmaytfkdt ytlsasarad asnlfgvatn
      661 dkwkplwsvg vawdisrmsf fnlgfvdqlk vrstlgfsgn adpsmsgvnt iryqvnspyt
      721 qspyaifdky anpelrwesv rmlnvgldfg llkgrlsgsv eyyskhasdl fgvypvdytt
      781 gvgttvlrnv agikgsgvdl qlsgrilqgg ltwsstlnls wyrdkiakyy lpsvqgsnfl
      841 qsnavvsgve glpvysifsy rwegldsatg epmgfvngqp skayssiisg tkltdlvfhg
      901 salpryfgnm vndfgfkrft lsvalsfkfd yyfrrrgidy tslfasgsgh adfsdrwksp
      961 gdeaftqvps mpypisssre sfyrfaevli drgdhiriqy inldyafdrs lakkiglktl
     1021 nvfaslanvg iiyrankhql dpeyvtssfn lppgqtlafg lrasl
//
LOCUS       WP_090767204            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090767204
VERSION     WP_090767204.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114357
     Region          23..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfi vlffavnama qdrtitgtvt saddklpipg vsvkiqgaag gtstdsngkf
       61 sikvsssakv lefssigfaa qtrpisssnv invvlntdsk algevvvtal gvnkatktlg
      121 ysqstlksae vnasapaslf gglqgkvagv nisntsgapg gstkvilrgy ssitgsnqpl
      181 yvvdgvpldn stagsdnnyd fgnnandidp nniesisilk gsaatalygs rgsngvlivt
      241 tkkgaagklk vdlstattlt nvasvyklqd qfgqgwdgty ipsengnwgp kydgqlrpwg
      301 aivdnsqllk pysfiknnvr dalttgieln nnialsggne nstayfsygn iysngylpsd
      361 ndsykrnnft lkgstkygkf sadaslnyvg kttkfinqgg ansgigssfy edilqipgdi
      421 pikdlqdykn kffnvdnyft pyaenpyysi yengsryksd rvygninlny katgwlsfqf
      481 qqgadidnai skiwhnknap spgsynaggn iegssraada gdvidgsvkt feydsklnal
      541 fnkelnshfd ldgligvnyn drgsrvlttg iedlaipgfy qinnsankpt stsaeshrrl
      601 fgayasatfg ynkylyltvt grndwsstlp qdnnsyfypa sslafiasqa idfsktpisf
      661 lkirasyget gsdtdpyrvf nsatrtsvpl gfgtltfpif gvpgysisnq lnsnnfkper
      721 vkevelgaei rflqdrigid atyynklrkd qiiplpidps tgyssyivnf gsvrnkgvel
      781 avnikpiktt didwnlnytf tkenskvtel pagldkvvln taydaqfvar vgqplgiiea
      841 ptrtyspsgq vivdangypv yssenvsfgs tvpdfvmgla nqfrykdfsl sftldwhkgg
      901 vfysgtadll nfvgadaktt yndrrpfivp nsvqklangt yventtpite antddfyyht
      961 snkadayanr ildrsflklr eatlsynlpk sivgkigaqr asvsvfgrnl vtwlaknnnt
     1021 idpevsnfgn dlgsefgefr tappvrffga slkvsf
//
LOCUS       WP_090767422            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090767422
VERSION     WP_090767422.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113571
     Region          34..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikiftkrsv pkralllllc lylgvkayaq tpavkgvvkd aketivgati iaqnvqtgvr
       61 tttssdkngv ftfvrlasgp ykftinfigy eskivtgfvk eggtfslsve lkqsnisldk
      121 evvvtgtgin rnkntftgst atfsgdalkm vgnnniiqsl rtldpsflli ennlagsnpn
      181 vlpvievrgk ssvpsaslrd qfggdpnqpl fildgfessl qtivdldmnr vgsvtilkda
      241 astalygara sngvvvieti rpkpgelqft ysndfrvenp dlsgynmmna sekleferls
      301 grystsdgnp tqqvfldqly nshlaavrkg vdsywlsepi qtgysnnssv fvqggdntft
      361 ygvgmnyktq tgamkgsgrd sysgsinlty rknklnvnnv tyirgysafn spygsfadyv
      421 nanpyyekny tnrylevtrq tngteikvrn plydatlpqy dntknlevqn nlninydltk
      481 dlrlngalqi tkgntnakkf rapessefed vtllrkgtyr dssgtnlsyq anvlltyykv
      541 iaekhtlnan fratvnesqn sdyytilegf pqgsngnprf aygysisnpp gassrvyrtl
      601 ngtisanyay dnrflvdgsy rldgstafgr nkqfspyysv glgwnihned ffkgktwinr
      661 lkifgnigvt gnqnygnvts vsvynynsns nynqfgqgig lttlgnpdla pqkttqisgg
      721 idfmlfssrf tgyinaynkk tdplvvavdl psstgvfsyp lnagtltykg veaklnyspi
      781 ynpakrvvlm igltgsmfks kyadfgntln slnkqqelnk stlrftdgys aetiwaaksl
      841 gidpatgrei fltpsgqysf dynaanilpv gnttptvegv fttnlmykgf nlginlrykl
      901 ggdifnralf ekvenisfss itlnqdrral ydrwqnpgdi aqfksisqta ttpissrfvq
      961 kenvitgesf nlgytfdnnv wvrklgmrsf ninalasdif tastvrrerg inypyartva
     1021 fsfrasf
//
LOCUS       WP_090767078            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090767078
VERSION     WP_090767078.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116508
     Region          35..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msfyntdmtk kyilnllllv tlavwggavs aqtlisvkgk vvdksdgngi pavtimasts
       61 traigmtrdd gsfmvsvpnn atltfkylny kdvviklngk ndlkvvmded rtslkdvviv
      121 gyaqktketv mgavtslkgk diqdvpvsnv telfqakvpg lniqintgsp gaaptinmrg
      181 lsgisvtgsg dnafltptsp lfvidgvpvd lntdyqygfs sngpgispls lippedieei
      241 nflkdasata lygaqgaygv ilintrrgks ktpiiqystn fffntppklr qviggaaesn
      301 lrlweiytyg anvysarqsi dntpmladsl nafynnstdw qsifyrstyn qqhnvnasgg
      361 ddsfnykinv gyydekgiqe ntgftrysls mntrykpspk fnvnlilsss lgntqkgsgn
      421 gllqtgvasg agsssllpgp slinssaalg alivdndnka gniktsvear yefltglals
      481 nitsydysmg ttetfnpail nnnvagvysy ndkrstlynr amlsfnksfq kdvhnlgayv
      541 fsevyvrnfq ahaikqdqyt ndqyqgpfgt aaassgggil dnysdsraas lagsisynyk
      601 tkylieatfr ldgtsstgln apwarnpsla lkwnfnkenf lanskwldvg mlrlswgrni
      661 apvgsvfdan gtydyygnyn gmpttaidfn nlpnikllpt sttqynagld lnlfknritl
      721 tfdtyykmvd nqlweknitt hnaftklktn evsnvnygye lavsfrplps tskvnwtlsi
      781 ngaynkekit alpdatrqll ldggatgqai lyrlgrnslt nilynfkgvf atdddvpvnp
      841 angtryhtfn gavpvyfkag dpyyadingd yvldskdmvg agnsqpling gisnfisyqg
      901 fslnvimayt whrdilnnpl assfqnfasp fsannlvpis ayniwrqsgd ianypnpydy
      961 lrygnygatd kstqflpfry nqtlfqedgs ylklatvtlg ynfkpeltkr lgitslrvfa
     1021 tannihtfsf ysgadpenvs slgrdnsggy pvrrtyalgl niql
//
LOCUS       WP_090767461            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090767461
VERSION     WP_090767461.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115695
     Region          24..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqklllifm vtvmsyfnai aqnktitgkv vdaddglplp gvsikvkgtt qvtqttgqgt
       61 fsmsvpqnaq ililsyvgyt eqevkitgqt ltvrlasssk nlqdvivvay gtskkeaitg
      121 svatmsakql dnriitnvtn vlagvapgvv ttsgngqpgs ssairirgfg sisasnsplf
      181 vldgsvydge lgdinandie sisllkdass salygsraan gvliittkkg ksgtptlnat
      241 ynqgfskrgi peydrvgald yyplmwqalk nslvypasgt gisesaaatq atnsiqgqlv
      301 ynpfnvpnnq ivgvdgklnp naqllyndfd wykqasrvgk rtefnvnssa kgdktdyyfs
      361 mnylkdngyl iktdferfna rinantqlrp wlktginlag slsngnlaqd astgsatafv
      421 nvfnfargig piypvhayda sgnpvltttg eqwydygghp gainrpigas pgrnviyetm
      481 lndvlsrrla lngrayaeik flkdftfkpt isidfinays seyrnrivgd gstvggsstk
      541 rstptqsytf nqvlsynktf gshtvsalag henydydwrr lsatkqsqil dgntefpnfv
      601 tpsdaggykd tyrvesyfgk agysyqdkyf vdasirrdgt srlskqsrwg tffsagaswa
      661 inkedfmksi dwindlrlka sygevgndnl idatlvehns lyynyqafye lgwnngsepg
      721 lllataatpd lkwesvntfn tgvafslfnn rlkgeieyfk rgssnllfav pqplsdpits
      781 irrnigsmyn tgidlqlsgd ilrsenfnwn llsnwswlkn kitkmpaetp tvtsgtkrle
      841 vgrdiyayyl rqwagvdpad gsalfepnag vttdlrtvng rvlttninna rsdysgsaip
      901 dlygsvtntl syknfglsfl isyqiggkfy dqnyqglmat tygsalhadv lnswmapgqv
      961 tdiprldigr ssqfngtssr wlidasyiaf rnvnlsytlp qrwikgatls nvrvfaagen
     1021 lgliskrkgm dptesftgln ttnyvpsrmi sfginvsl
//
LOCUS       WP_090768853            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090768853
VERSION     WP_090768853.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118839
     Region          29..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhfykmtlg imallclmlg peitsaqtki sgivkddaqq pipgvsvlvk gtkkaistdl
       61 sgrftidakt getlllssig fisqevqvsg ntltiilktd sknlnevvvt algirkekrn
      121 lgyaiqevkg adlvkarean pvnglvgkva gltvgvssel lgrsslylrg nnvnlvvvdg
      181 vpinsdtwni npddidtytv lkgpaaaaly gyqayngall ittkkgklsd kgfvvelnss
      241 tqfnkgfial pksqdeygpg ehsayafgdg kggglndgdy diwgpkfegq lipqydspvd
      301 angvrqgtpw vargkdnlkr fiqtgllsan nialssatdk ynlrvsvsnn yqkgiipntq
      361 lninnfnvsg synispklka eayinysrqf sdnipdvnyg pnsviynmtl wggadwnidd
      421 mknywqagke giqsiyaeyq ryhnpyfmsy ewlrghkknd ingyaslnyn ltkgldvmlk
      481 tqistydqlr tekmpfsahp ygreeglgdy redrrsmfen ntqlllkynk nvgdlfeisa
      541 fgggnarnfs ynssftttdy lnvpnvynfs nsknpvkafn fnsnmlvlsa fysvdisfkk
      601 ylninttgrv dknsalspsn nsafypsvsl ssvvsdyvkm pafisfakvr asyanvkdpg
      661 lgtleyigat plqtyplgyg aeytssyggp gyglsspysv rptynnqtga yytdnlidln
      721 avkaqsrtny eggidlkflk nrlgfeatyf ryidgpkiik qnispatgyq tntingrktq
      781 nsgvelslsg tpvltdkfgw dvmvnwstyk qiykelapge tsvdqffkag dridniygsv
      841 lakspsgqvi htssgtpisl pvnqllghad pnwvwsisnk fryqnfsfsf qldgkvggvm
      901 qdyvrlksfq ggrqietiqg kmgearyqdy vhvndpnykg twvgdgvvlt nsgklnfdpv
      961 tgvitnydql tfapnttpvl lqdylgvfyg akentmmsrt yaklrevtfg yqlpkklleg
     1021 tfirsanfsv vgrnllyfin styndvdvdq ysgregtstl qtpttrsvgf nlnvtf
//
LOCUS       WP_090769637            1200 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090769637
VERSION     WP_090769637.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1200)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1200)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1200)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1200
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1200
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131714
     Region          126..1199
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqftqtlkr givlmlvgvs iaagafaqqn sipladalnl iakkynakfa yehrivqgkt
       61 adrneaskak nleealkdvl ypnnllflyv segnytivtr dtktslsvii epnaakvndk
      121 snehyitgrv edengnpmpg atlktnatnq tfltnssgef amfvspdate lsvyylgyep
      181 fsqkinantk slrmvlkatv nqleevnvvs tgyqkisker atgaatvita kelekvpvpn
      241 vlyrletmvp gvkitlnsgd nsfvygntmn ainggtrtrg tsdygmtvrg rgslpgpqgs
      301 esfplividg aisendisti npddvesitf lkdaaaasiw gvrsgngvmv ittkrgknnq
      361 apvinfsvna avsnhpdlnk lplmnaaqti afeqelvnkn liiapsnttp mgqplatvtd
      421 ltfklkagti sqsdyntaia rystmdnrsq vadyllrpan nqvynfsvsg gnnysnyfys
      481 asyanenpya vgnngqrltv tlnntfklfk vatlstnvkg aflkyknngi slntlyapsa
      541 tafmpydqlv ddngnrvays rryyagwvnt lypkgflnwg ynaldevena dntqkdnnys
      601 vnlnlsvpvf kgltanafya nefgfsnarr yyneqsfyyr dfvngytpip ttgnatnsig
      661 lakgagilns qnttannytl rgqlnydrtf gadhqvtaia gseiretnag qttgtlygyn
      721 tgtglsrpvd fftpyptiag yssslsgsyp tlqdkkrrfl syysnaayty kskytlsgsv
      781 ryddynnfgl drsfratply sfgakwdayk etflknvswi snlslrgtyg vngnistqlf
      841 pftwisvgaa dlttglpyas iispanpelr wektymsnia idfgflknrl sgsvdfyhkd
      901 gkdllyqfpi ngtygvttlt rnstrmtgkg vdvalngiiy takdwditsr lnyayntnnv
      961 edtrfvptss fyanpaygsl lagypsdkif vyrnagldat gmtlvydeng nkvaanqnvt
     1021 nvaalkyagr sapshfgsfi qsvrykdftl mavasyqfgs vflkptassy sssrlgvkyd
     1081 lhedvasrwq kagdeattnv pgmagtfagt sllryqqsdi nvlkgdyirl relslsyrip
     1141 tekitskikg atfgfnvrnl gliwtankag ldpdvlpnls sttlglpptv synfslnlnf
//
LOCUS       WP_090769901             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090769901
VERSION     WP_090769901.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111135
     Region          81..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvkiytsicf alflsvfgsq tlhantvvvk gansmyfafq qdttkakkep vtfsvktdti
       61 gqmikalqkf ktvrdtinir satpvpnlsl qqvikgnlag vyvqepngep gteqsiivqg
      121 asgllftkkd myalqpavyl ngvplvadnp fafdvqkydy nrigpatnll sqisidniqs
      181 isvikdpfel aklgpnaang aiyvttknar aglrdislns yfgfvtppav ntvngvyenn
      241 frkpfyqkya taenyanyas ylrdstntay ygpsnwndiy ykttptfsad lgitgggdra
      301 nfrffgsgtk nagnaddtni nkynlffgin mapfkwftvs ssvnaarldr trnrslrdrf
      361 aetryipdls splspnasiy egflqenakn vdnnrntiln gnltlsakin kitissslif
      421 dynegvrdyf tpstlmdgvs yvsnyfgysq rlmlnnsasy kyeinkkhti dfeigqsfqg
      481 dtykynyara yngpndyvkl nlvdgnsgnd dylntlaagg fyvfryidke knnlmsfygs
      541 akysyknlld lsalvrrdgs sngqpdsrwv ttpafsatfn lkeqflknnt lfnslhlsag
      601 wgrnlrifld dryaagpqyr sengwfeept ipgyggrlgi nrpygsgfig ygiklpyadr
      661 tnitldasfl nsrlnaaita ynrdnknqvi gvpvpfetgy slnyqtgmdi nnkglelmln
      721 gvvirntkgl nwnttvnfnc nrnkltalpn gltelisgdd klvvgkpvgs fwlysnngiy
      781 ntnaevpagr tfngiplkag dpnwvdyngd nridnkdkvs tgdrlpkfvg gwnntlaykn
      841 fdlnfnfifa lgqkainqye atrygfinre agndinsvke vsswqvfdne ktypiynpws
      901 dvdayrvdqd lflenasyvk lrsvtlgydf gktslfrrsg tgvrraylya tamnlftitk
      961 ftgidpelvn yngyydganl tiprtfvlgf kldl
//
LOCUS       WP_090770116            1132 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090770116
VERSION     WP_090770116.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1132
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124883
     Region          51..119
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          128..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknepqavl qrsyrsmlkl llmmkivvlf illgtlqtfa trsvaqekvs ismqqadlkq
       61 ifksienqtn ihfvyndeil pagklftasf anqswkevlt tvlantgihy riveenlvvl
      121 tlgdhnrivv rgkvtdaknv gipgvsvlek gtkngavtne ngefninvtd asailifkfv
      181 gyvtqelsas nsfmtvmlke daadlnevvv vgygkqekkf ltgsvvsisg stvsnipvsn
      241 vsnalagrla glvvmspsgl pgvsssvrvr gttsysgqdp lyviddiprs kqefdllspn
      301 diesisvlkd gaaaiygvrg gsgvvlvttk qgaegpakfs fnishgqsep trtpkrlnsy
      361 qdalyrnnyy lnqgvaandp ryytadelef ykagnintdl femikktprt tdanlsvtgg
      421 spnaryyvst gyfsetglfd kleskrfnvl snldfkfgng fsakvnlqat lrpnttpwwy
      481 dgvntttlsd ltraamnftp lspayvnglp dgslyhflvp evikngyikg drsnlngflk
      541 lsynpsylkg fgadvsynyn kqadlyktry qpytlylfnr fggnnhligd qvigtkaaaq
      601 qpydffqeqy iqnktyvfna sahydrtfgn hdlslqvfye qsesagdnfs akgenllsst
      661 idqlfvansd parrsltgtg nefgrssvfg rlnykfkgky lldaivrada ssafapknkw
      721 gyfpslsggw ilseepfikn ampnvdnlki ragygllgyd nidlsqwysy fslqgsavfs
      781 tpvntiapqr ypnpdikwqk iattnvglda sfykglisgs ldlfykktsd llvanqtvip
      841 stfgialaqv nygqvnakgf eltlrhdnqi gqvkyyvgfn fayttnkvik ypeqanipdy
      901 qrrtgrpvnf itgyqangii sntdqlanyl klkygtrafe lgdigfadlf gpsngapdgi
      961 insndnvvls nlsydprity giplgaswkg fdlgvllqgv garkvmlsdr sqwqeqnvla
     1021 fwadfwspqn pnaaypkigg lngtegpass fwlrsgnylr lkslelgytl paratksigl
     1081 ekcrlfltgt nlfiisddik mydpelptne tgygafqypm lrtisagasi sf
//
LOCUS       WP_090770378            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090770378
VERSION     WP_090770378.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115697
     Region          32..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnykiiiill llsfgtkvyg qhifkaqirg sknaplpgal vtdisnekkv stdekgnfsl
       61 tsdsaainir igyvgykvkt lrlfsfdpkq vvinlepldn qladitiisd gyqslpkers
      121 tgsfvqldqs iinrrisani lsriedvtsg lvvnrnpaag gnisirgqst lfsnraplii
      181 ldnfpyegdl nainpndies itvlkdaaaa siwgaragng vivlnskkgk sseakvgift
      241 sltigakpdi yylprmsssd yidieaslfn sgfykdaets lsniaispvv elliskrdgk
      301 isqqdadrmi dqyraidvre dqrkymqrts vdqqyslnis ggsgnslhfi sggfdknlns
      361 dvgnssnrit lnanqvnyff krklelntai sflqaetnnn nqgliaysya rlvdgsegyp
      421 nvtrglresf knemvkkgfl dwqynpladi dqnknslvnt efrintslky nifpflsasi
      481 lyqfakssqd qsnlqrensy ylrnlinqft sinadgsltr rvpiggilde signsishnl
      541 rgqlafdksi gsdhnvsaia gaevrqmvtn ssqtraygys eeyvrsstvd yltrfplsfn
      601 taqfenipfs dgmnqltdrf lsyyvnasys ykqryifsas trldqsnlfg vdankkgvpl
      661 ysaglawnia repfynigfl pllklrttyg ysgnvfrsls ayttasysng tissiklpfa
      721 qiesppnpsl rwekirmvni avdfatkgnr isgsieyysr kasdllgttp vatstgissf
      781 rgntadtkgy gidltlntqn ikgivgwstn llfsvamdkv taypagnlns ayisggllpv
      841 vgkpigaiss yawggldpst gdpigflngv pskdytkiis sstladlvyn gparppvygs
      901 irnnidfgpw sfsanisyrf gyyfhrpsis ygttkglggh sdytlrwknp gdesitsvps
      961 vplvantard efykyanvlt ehgdnirlqd infsyqlpad ktgkvfrrlq vsvylnnlgi
     1021 iwqesksgid pdfqsallpk sialgirgdf
//
LOCUS       WP_090770791            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090770791
VERSION     WP_090770791.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115385
     Region          31..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklnftqtsp kiligiffyl lipwlamaqt kisgvvldes krplpgativ ekgtkngtvt
       61 naegrytltv kssnsilvvs migylgkeea asgktsvnft lgennqtlse vvtigyqsis
      121 rkkataaiss isakelanlp aasfdqllqg rvsgvnvqnf sgapgsaptv svrgnsqvsr
      181 gydefnvins plyvvdgvpq ptesyvgpgv gtgsnylagl npadiesidi lkdasaaaiy
      241 gsraangvil ittkkgisge prinisayag lterpnlrdv tlgtterrqk mevlqrqlsy
      301 adqkqlpyll tdslnpayng ntdwqdlfyq tgritngdln vsgggdngmv yrfsggyyne
      361 egiikatgfk rysgrinltt ralkqklmin pifaysrsdr argngsnnsp islgagnmps
      421 sllnldedkk afylgaysen ldknisnqlt inlnlsyefn khlsltsqss ylqnsarrdl
      481 stsnllnngq gnsaysyadn gitaqtsnfl synnkfgkhs vsviagqdil ynqfqyttas
      541 gyngpsdniq vvsgfqqski gassdyqafg llsyygrlay dfdskyllsi stradassrf
      601 gknnkwgffp sasigwllte esfmknwtkn pftmakiras ignsgndpkr nylqynlyqv
      661 nnggfdgngg atsyngvtai tpnlydgvaq snlsweksmq wnigtdleik ngkygltfdv
      721 ynkesslqlf slnlplttgy dlaltnaigv rnsgaeislm anpfsgafkw ntrlnvsynk
      781 nqimnlpngg rdlvlsgdrf dkshilsvgs pinafylyrt ngvfsktsdi pvnpytgely
      841 rnsngtyqqg dfyladldgd gfidifndgi npdkvpigdp npkytggwtn nftyknfslg
      901 vfatftfdrd vlnlfesdrf snstdgnais nfasfstpdl skiniwkapg dmadyakydl
      961 gtyryyytga qtfflekggy friksvnlay dlpgstlkkl gvskfrvfai adnlfmfqqs
     1021 krlpdaeavn pygeyngagy pipkkytlgi evqf
//
LOCUS       WP_090771020            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090771020
VERSION     WP_090771020.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109010
     Region          26..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtklkitlft lamlcfvqiy gqtslisgki tdalgqpipg isvkikgttg gtssdakgif
       61 sikaanpatl vfsgigyask efaysgqsni tivlsedqqn lneivvtalg vkrekrnlty
      121 ssqevkgdqi tqskepnlvn alagkvsgvq itsssgtpgs ssrivirgan slygnnealm
      181 vidgipvnnd etgnlnsgpg tnriadldpn iiesinvlkg gaatalygsd gakgviiitt
      241 kagslnkkps isfsssfsme kpllpeiqnk yslgsngvyf dgvnqktsts wgarmdtlki
      301 ngqpaqvydq sdlffktgkt ysntvaitgg gaynsyflsy tnfaqdgtvp tssfdrntlf
      361 gkfttqivkd lnvtfslnya ntknrrlpeg yalespvwti fsapvsydlq psvnpdgsqr
      421 lfrfsrnnpy wvldnisnts vvnrflptft adykplswlt iterfgadvy veqgkytesl
      481 lsvsnpngri vnnntnfrqy nndlilnank sfgdfnveal lgnniistys qngyanglgi
      541 tipgfnnigs astvkftets yltrkvgfyl qsnidykkfi ilsltgrydg asvlakdntf
      601 ypygsaatsf ifsnffspgl snvmnfgklr vsystvgnas igayslltpy esqtvrnttf
      661 pyqgqsgfli sqvlnnpnlk nerinevevg letgffksri glevtyfdkk tkngiipsva
      721 lapstgfnat svnsasmrnr gievllnakp ivtkdfswdl tvnysrirnk vlsiykdlnq
      781 vgngftfifv nqpygviygt ryarnasgql ltddgglpfa adtqgiigdi npdwmggivn
      841 nfkykqftfs fsfdmkkggd iqnnvdgygy fygtpkvted rgprvvegvn attglpntvs
      901 vlgqayyqra nsvlesviqd gtyvklrnvs lgynvkptwl qktpfktigf qvtgrnlwiy
      961 aphftggdpe vssfgssngs qgiysfstpt srsvdfslkl tl
//
LOCUS       WP_090771182            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090771182
VERSION     WP_090771182.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120388
     Region          41..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkkytlgls vllcfllasf manaqqinyv kgkiidkkdk qpiigasvvi vdkdrrvikg
       61 vssdidgnyt lpvadksyri svsyigykst apiaidkaii nfqlepadnq mdevqivska
      121 ktdngsgmti dkrdqtsaig tinakeledm qaasidqalq grlagldiaa ssgdpgapmq
      181 irirgtssin gavdplivvd gmpydisips dfnfatsden nygqllniap sdikdisvlk
      241 daaataiwgs raangvlvin tkrgtmgppa isynfkgsys kqpsaipmln gnqystlile
      301 efynagrqfs tsefakefqy dpndpynffn ysnntdwlna itrigylqdh nlsisgggek
      361 aryrasvnyf dqqgttrgts lgrlsarvnl dyqvsnkirf sadivythvd nqnlystrlr
      421 diayqkmpnq avyeydeygn ltsnyfspva taqgtypgty nplamanaas nhqigervip
      481 kfslqyqiip erlrlnanfq vdinnsktkt flpqiatgrl ftdavvnsag didgdgftma
      541 tnltlaytpk lgekhdliaf arfdsndsrr tgqgmfatnt assylddpsi dgrtnaagsv
      601 yssfaqsrsv glllnaqykf ldryilnagv rgdgnskfgp nnrygvfpsa svrwrvsgep
      661 fmkrtqkyid dlsfrasygi vgnaprydyt ylnayqnygf sylgmagvys snlelsdlrw
      721 ekvaqsnlgv tlnmfknain mdfdiyrkrt sdlfypgiai ptyngysgvd mnvgtmdnqg
      781 wefninstii kkknfrwdfs fnishnenii reisplypre nkgkvtsnnv ykvyiqennp
      841 fgsfygfkfk gvykdlnstv aldekgnqii gpngqkvymr faypsidyvf qpgdamyedi
      901 nhdgnidykd ivylgngnpk ltggfgtgit ingnirfgan fsyrtgyqii ngtkinttnm
      961 ngfsnqstav lrrwraegdv tdmpravysv gynylgsdry iedgsylrlr sitlkydfsk
     1021 nfmkrigmks lsanlmmenv ltftrytgqd pevpvkltaf stvidnsttp piktvtlglt
     1081 anf
//
LOCUS       WP_090771190            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090771190
VERSION     WP_090771190.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119231
     Region          56..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhnftiikkg islvlfglml stvafaqqtd tstkdsaqys tdtttvkvkq kklvgqkitg
       61 vvvdgytnkp ingvkltvtd fsgaltdnng kftiivpdyn atllvsftny htkllpvhkg
      121 klatikiyps nynslftevt lpastqnlar ssaalsylnp qggwavnset pdsylqgrma
      181 gvnairrsgt pgigadvfvr gftslyatnq plyvvdgmpy dansygtslt tghrnnplqf
      241 idvrdienit likdasaaav ygtkaangvm littshakdl atlidfsayt gvnlkpknin
      301 vmgvddfrsy lsdvlksqgl sasaiaakpy mnddpnpann anypmyhqnt nwqdqvfkts
      361 idqsyflkvs ggdniakyal sagysadkgv idstsnnkys mrfnsdlnlt kkltgntnls
      421 ftyteqrlkd qglspnsnpv flslvkapfl avneissaga vspnladadt lgvsnprali
      481 ekglnqkkay rffgninfdy afnktfklsn ltgvtydktq etlfiprkgv tnevlpttig
      541 dsklgtqvir yfsvfddlhl sfdrrfgkgh tlhaalgtry tsakseqdya igynsatdvl
      601 isignsnaal ryfggdigkw snlnsyltad ynykdkyyls lnaavdqssr fgrrdisssv
      661 ryiggygldi lgnksailpa vsgawlisse sfmhnykyid llkfrmsygl vgnddignyn
      721 nrqyyisqnl lglqgvvrgn ianpgiqwes iakfntglda sffnerlsfs ldyyihttnk
      781 mlayvpvpai gginsyidnq agmrtsgldf glngrilnkt fkwdigvnlg tyknkvnslp
      841 ggtdiltnya ngtyltrvgq tanlfygqrt ngvyastaea taaglsirns agvlvpftgg
      901 dtkfidtngd kiindadrvv ignpnpdlyg sinntfsykn wsldvlftfv tgndiynytr
      961 svlesgnsyy nqtdimrnrw rgegqvtnvp kasygdpmgn aqfsdrwied gsylrlrtvn
     1021 ltynvplkgr sikyarlyat annvftltny lgydpelsat gsiftqgvdt tlepqfrsfq
     1081 lgvrigl
//
LOCUS       WP_090771539             944 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090771539
VERSION     WP_090771539.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..944
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104095
     Region          59..942
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msifikpfmv llcclfifid gtgaqevtvi rpynqlrnds lltdslknlk qliyfntpkr
       61 lsttssamvl gkefnttpvv ayplalagrl aglsvsqgng eplnegfsyr lrgqsplifi
      121 dgiprsvtei smeeiesvtv lkdavslaml gvrgsggais ivtkkgspgk qqisftgqwg
      181 tqrplqnlis hsldaynyaq lynealvndg lsvagngfsq valngfqtgn npylypnvdw
      241 rdqvlknsat iarynlntsg gnnyvkyfin lehinqngff kesdintnys tnagakgyfi
      301 rsnvdvnltd kitagiyiqg rilnknnpgn aaadnifssl latpnsaypv ynangsyggs
      361 sqftnnilaq sinsgyslsn trtvltdvyl khtlddlskg lwvkvrasff snlnenlvrv
      421 ksfavfepng vsgtgettyr qfgtnseqgn tnsigfqnrs dfqelsigyn rtfskhgfda
      481 vilanrdnlv ngtnlpytiq gisghvayny dekylaelsf aqnganrypn nggfkygffp
      541 aaglgwnink esflkdvswl nnlklytsyg ksgknntayy tymqvynasp tayfgssaaa
      601 gttvgesyla npnitwekak ifnagvdgtl fknqlsfnve yysnvysdls ivrgnnsgll
      661 gisypeenig kqryygwdaq inwaqrfndf gyfisanasl qnskliysae anqryewmyr
      721 tghpvgqnyg ylaeglfqnq qeitgyptie gyspqpgdik yrdlngdgvi nqydqttfgs
      781 ekatvflgsr igfsfkgidf salfqgvlnq qvylsgnsyr efqsgtaqay eiqlgrwtpa
      841 tattatyprl ttssgprnga qnnfvsssyw lrsgnyvrlk tielgytipg kltkkiglqs
      901 triflnglnl ytwssdtfng adpenytggy pigkvfnvgl niql
//
LOCUS       WP_090771582             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090771582
VERSION     WP_090771582.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107976
     Region          27..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myknflrlls ccslfcalgl svqaqtrtis gkvtdkadgq plpgvtvadn nksastttne
       61 sgrysfnipa gtkaitfsfv gyeavtvslg aantinavls sttntleevq vvsvgygtln
      121 krevssaith vsgkdllava ansplmslqg kvpglnisnt agadpnssps vqlrgvssrn
      181 aglgplyvin gvpggnidni nqndiesidv lkggaasaiy gtrgsngvii ittkkgsaqs
      241 qmfydgyasf dyltnklenl sadefianrv knqkgqdykg ntdwlaavtn spafaqkhtl
      301 qfsggsaktn yfasadyrda dgvdlrahkn eygarltinh atdnnmfvaa ltvaprymkt
      361 snsdqgnfnn altlnptysi fdnagkynyi ntgffsnnpv enanviksda eikeldings
      421 lrmnilsnly ttvtlsqisr sakllnftps tlssivyank ttqtnyasqe qqendqknie
      481 wtgnynldlg rhhfkllggy syslynykqv kaqnydfpfd sylwnnlgsg lynggaagqg
      541 qsavgstqng stlisffgrl nydfnnryif taslrregss kfglnnkwgn fpavsaawrl
      601 seeafmkgal pwvnelkvra dygitgnqdf dnylslllyg gagyfpyngq yyqvygpssn
      661 vnpdlsweks vnfnagidft ilnnrisgsl dyyirtnkdl lgyynvpvpp ntqattfsnv
      721 gtmknyglel aisaeaikqt dfgyninval aynrnkfisf sneiykggtf qdvaglpapg
      781 spgniqriqe ghsigefytl rsagvndaga llvyrkdgsi vpanqasndd kqfvgnglpk
      841 figsigntfr ykrfdlgifl rgtfgykifn taafyigtps sqsdanvlks aydssskysl
      901 ltnsattsia sdyflengsf vkidnvslgy rqplaskylk sirlyatgrn lhtftsftgg
      961 dpegvpvngl tpgvntslny ypstlqlifg lqatf
//
LOCUS       WP_090772015            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090772015
VERSION     WP_090772015.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114974
     Region          41..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskiynksav llylrrlcta kilaiwllll cgsysafaqt titgivkdnk gltlpgvnvr
       61 ikntqvgtlt ngagkysika pegnqtlvft fvgfttqeiq vngrttinit ledatqgltd
      121 vvvigygtaq kkdvtgavss ikatqlenen pnsvtdilrg nipglsvgfn nsakgggdll
      181 vrgkttltgt ttplivldgv ifigqlsdin pndiesvdvl kdasslavyg akaatgvvai
      241 ttkkgksgsp titvntnfgm atlakdqpvy dgpgflnwra dvqrsgsvnp ayiyndpnnl
      301 pegvtltqwl ngqtttnptd lwlsrlglla nekanylagk tidwydmllv tgkrqdhtls
      361 lsgrkeeiny ymslgylkne siiagggfst frtrlnlegk aakfltlgmn mqfadrdega
      421 ieaqfsqlpd lspygdfyna dgslrriptd dnglnarnpf ldqtynsrlq kqstlfgsly
      481 aklqlpfgis yqvnfspgld qyrtfnhqss knpnvtipgg saqraqetry nwqldnlikw
      541 nktfakdhnv dvtllvngek ystwytiagn egfaptdvlg fhnlqsgnkp tvssddkvyt
      601 gdallarlny sykgryaftg svrrdgysaf gaskkranfp aaalawtlse esflkevkwl
      661 dflklrlsyg ingnreirda nnvidpyvsi qtlsggkyqs vnssgtpgev ntvvnssrlg
      721 npnlewektk slnlgldfgf lnnringsle lydkktsdll igqslssasg ytnvianlgr
      781 vnnkgielgi nsrnitegni twntsvnfsl nrnkivalat pnddpgngwf igkdidviwe
      841 ykilgvwqen evaeankfnk gikpgdfkle dvdgnyvynd ldkqfigyrs prfnwsmrnd
      901 fnifknfdfs fqlvsswgqq rsdiyaknqp gsvgfgrsss yiipywtpan pindyarlns
      961 glsgvtfnay rkssyirlnt ialaysipkd llsklkvqsa kiyanvsnvg vyapnwnqwd
     1021 pqtadnngnp vptprvytfg lnvtf
//
LOCUS       WP_090772084            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090772084
VERSION     WP_090772084.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111912
     Region          46..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktylkqlm lfsltvyaac palayantir verhvagknk ghrlevtgtv sdnfgnplfg
       61 vsvtiketgn svttnkdgky kisavegdil tftlngylvk evevkealln vslsesqkrq
      121 aatpvlygeq stvtnlqsts tvyntdlikv pvaginnals grlaglytlq sngrpgadgt
      181 sitvrgnapl vlvngiprdy psidpeeies vtilkdglst vmlgqqasng vimintrkge
      241 vgkqrislta qaglqsaikl pkplgafdya tlynealand gkaprytaad lnawatgsdp
      301 ifhpdvdwys tvlkpnttfs rynlntyggg natryfldvd ylnqsgilkq dderntystn
      361 tdykrylvrt nididitptt llnlnlfgri qngnqpggvs astaifttgt tlsnfgsnnv
      421 fsqlasipnn aypvfnpngs lagtsdyqtn lwgattrsgy fynssrdisa dislkktldn
      481 vtkglwlkal asfnhsvsen iirtkqyavy klastnpdvy qkfgvdgqqv nlttntgqsr
      541 nlfvdfsagl dktygnhgis allkynsqsi qgnqvvlinn nlsgrinyny kekylaeaal
      601 sysgvnryve gqrygffygf glgwnmaked flkdiqwlna lkiranyayt gnanpgyfay
      661 nqyyvtgnty nygaptptai tgvaegtlan phitwekanq ynvgidaslf nnklsvaady
      721 fnnknfdlvq trgrssallg ttypaenigv srysgvefdl kysnhvgnfn yyiapnvfsl
      781 qkiieyqdei srpyswmert gqredqtfgy vatglfqnqa einssakiqg ytpvpgdiky
      841 qdlnndgiin eldvralknn npiwfyglnl gfsykgfdfs allqgvqnry vyvsgstewa
      901 fqnnglgqaf eqnlgrwtpa taatatqprl tiganpnnea tssywlhdgs yvrlknvelg
      961 ytlpkvvtgk lklasvrffv navnaftlsa ydrvdpevyg sgyplqrvvn aglnvkf
//
LOCUS       WP_090772762             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            soli].
ACCESSION   WP_090772762
VERSION     WP_090772762.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter soli
  ORGANISM  Pedobacter soli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Pedobacter soli"
                     /db_xref="taxon:390242"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109905
     Region          44..975
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhkglaikhf vlqdttkikf vslkdslrkd slnqikqktl ynklsggvqk ntrdlslfpa
       61 itlqqnlkgn yaglyvqeps gepgtiqnmf lrgatmplls kkdvyasqpl vvldgiplig
      121 ehpfafdiqq ydfnrigpat nllstidinn iasvevlsdl astaiygprg vngvillksk
      181 tpdgiarsis fnsyigmaqk ptvntingky enefrqrfyd iyttngrysd deaypvylsd
      241 slnnvysgks dwtdlyykna lvyginlglt ggsdrasfrf slgntksdgv adgtgldrys
      301 amfninmkpv kwllfsamin gnrlnrtrnr slrdrfaqin yfpdlsapla pnkdyygsyl
      361 neyskgfddn ktnsiqgfak lvgtlgkfki sssfnvdyne gyrdifyart llqgnsyasn
      421 yygfnqrlmm dnkatydlnl knvhdfhfel gqsmiwdiyk ynnayaykga ndyikinlld
      481 skpknddgsd nggyltpvaf preltyrfld ktednllsfy gkvnysyndk yfvsgtlrld
      541 gssnaqptkr wfyspvlsaa wnikndllkd skgvddlvlr asagrmgrtf tydnyaqgpq
      601 ytasvgytgn ltvpgynaig vltrpysfgw vgynvpwsys dqlnigvdva mlknrlhvsa
      661 dfytkaeknq llgipsyaey gykqsiesgl nmsntgvdlt isalviansk fswnsalnln
      721 hnsnkltalp rglneiiign rflkvgqpvd qywllenegi ytannqvpvv ngqplkyngt
      781 plkagdprwk dqngdniide rdkvlkghsl pvlsggfdns ftygnwslgt nlyfnlgrkl
      841 inqdmanrfd fvnregntdv ssvkeitfwe krgdyskypl ynpwstvipy rtdqdlflen
      901 asflklrsvs lgydlgtvlk kknikiskff vygsvnnvfv itpytgqdpe lvsydgidtg
      961 ygqpiprtyt lgvkmel
//
LOCUS       WP_090776752            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090776752
VERSION     WP_090776752.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116270
     Region          24..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkilkifflc vviwglptya naqrkisgqv fnekseplag vtvlvegmpk eitntdgqgr
       61 fqltttkntl vvtyvgyknq rvditgktsv siflestned ldevivvayg tqkkrnitga
      121 vsniksediv rssstttaga lagkvqgvsv rakdarpgrg asieirnmgn plyvidgvay
      181 ggeggtdwvg tqnasgadif nalnledies isilkdaaaa vygfraskgv vlittkkgrr
      241 detarvning yqgwqnltrf ptmanaaqyt kgmveaaqne nrdpnsvytp selakwqngt
      301 epgyksydyf dmvvrknipq rylnanvtgg gknsnyflsv ghmdqdammk dfsykrtnlq
      361 anleatifeg mnigaqisgr qeatkdvglp ggdgyfssil aifknrptvg pyandnpeyp
      421 nhtndfsynp aifsrdiagy kdnnylsgnv nlfasyktkf glsakgtvsy nytnnkfdgf
      481 qytydvyryt ndaytrtggt dsrwryktdr vaisrfgqfq ldytkqlgdh nfsamvgyer
      541 sdwdrtynal ganpssnfis lmklsevngl ddswsyeara gyigrisynf kgkyllevlg
      601 rydgsylyyq gkewgffpga tlgwrisdep ffkpikgivn dmkirasvgq tgleegvgmh
      661 gylagynfaq gsavldgkyy pgvqprplat rnlswvkntt ynigvdmgmf enkltitada
      721 fkiirtgypa rkydvllpse vgyelpnenl nkngyygaeg iityssnige lgytvsanat
      781 ysrfkalesy kprfsnswne yrnsaeerwg gtwwgyqvvg qfqsveqinn hpinndgsnn
      841 rtqlpgdliy kdvnndgvin gmderpigyp tgwapmmnfg griglnwkgi dlnidfagga
      901 mqswfqdyel rnafhgggns paylledrwh radpydpnse wipgrypair ngnsgnngkn
      961 sdfwltnvry lrvrnlelay slpklitekv kaekirvyin asnllsfdnv kdyqidpeie
     1021 araavvypqq kvfmvgfnvt f
//
LOCUS       WP_090776958            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090776958
VERSION     WP_090776958.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115590
     Region          28..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnfkllrtlk givllsllfc atsyaqvkki tgkvtdasdg gsmpgvnvsi kgkpsnvatn
       61 adgiytiqad patdalvfsy igfkrqtivl agkttlnisl asdnadldev ivvgygskkk
      121 seilgsvvni kaediqdlpv pniaaalrnr lpgvgvnavs gkpgasvtin irnsavsesa
      181 kglgvssepl yvidgitvtr ddfdnidptm vedisflkda saaiygasga kgvvlittkk
      241 gkrgkpqisy tgfrgvsdna ssvdmlsayd haillndgfk vaneasnkff seadleqlkn
      301 nktkgwfdel wqtsavnrhn mnvsggsdai tffaggnyyd esgnyggiky skyafrsgmt
      361 akiiegltaq vtlnadfskr tsdtykngge ndqaffqqli ttpkwvpmqi dgkavnynnk
      421 tnpygvmqag nniwdksqgl alnasldykp kflsgltarv qfgknsrsgn snqytpaynv
      481 ynfqmtgqnn llytnipatq nhvveaissa naqlltgttl gssyqaiasl sydktigkhs
      541 fnvmaafdqs egvdeslsvl wrnqvlanid eywgfdrssf tlqnksifet vqrsyisrln
      601 ydydkkyfie giarmdassn fapgnrwgvf pslglgwais eedffkknvk fvnrlkvran
      661 yglvgesrvn arlwqyryiv dpngylygdn ltggvnpsam pnpdisweks rtlnlgldas
      721 mldnklsfty efyhrysyda ydtgnnenfp myagfeaptv nyqertswgs eftvgyrtki
      781 gsdwgistdv lfgfannrid kmfynefqlw ditypdlkyq fgtdtkkyns anygliskgm
      841 frtqaqldaf mnenptytin akvpqvgwly yedtngdgki tekdqvpmfn stnsfgvgfn
      901 vgvtyktlsl stnfvtrfgg kefydskska pasttlnvpa ywkdhwtaen pnakfprydd
      961 asiaagwnsd fwavsgtmir insmtltykm pkaflskigi gdsrlvltgn nlwtiinplk
     1021 ykdpysstiy dyptlrtisl glnvsl
//
LOCUS       WP_090777246            1160 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090777246
VERSION     WP_090777246.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1160)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1160)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1160)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1160
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1160
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129732
     Region          151..1157
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnfsanaary gdpifrkyqh aliycmritl lvsfvillsl qmvysssakg qameninvsi
       61 klenedliga ikkieqltpf rflyrtadvk sidnlninar sisvahlmeq llagtslsfk
      121 qiddrilitr yvsgkvpsli vrennasyal itgtvfdakt kdrlvgvtvr ikngsaralt
      181 dargnfrisa emgdillisy igyetqevtv tkpvleirle esaqslkgvv vtgifsqskt
      241 tftgaartfn aqelskvsnn nvlsalksld psfqmpenln igsnpnvlpd vvlrggntll
      301 distpgnsnp fnyqsapnap lfildgfett lqrvndldmn riasvtilkd agataiygsr
      361 gangvivieq nrpvdgklrv synasmtiea pdltgynlld aqgkfdledr snafidswnf
      421 kqdqldlyre srlravkegv ntdwmskplr tgvgqkhnvy veggadavsy glsltydrnv
      481 gvmkssdrtt ttansflsyr iknfqfrndl tlnfnkanns pygsfrqytq lnpywspyna
      541 dgtlkvylet iidpqtgirl tnfdnynnln gyigrplnpl ynaslnikdq tsfrgitnnf
      601 etrwqakewl rltgrlsytt qndesdiflp aqhssfaekp tfekgsytkg lgknqriegf
      661 ltaeanknfd khflsasatl nvkentfdtq firvegfpnp tldelilgnq ypsggkptgt
      721 egisrsigtl arvaysydnr ylfdatfrld gsslfgsdqr yapfwslgag wniknesflk
      781 dndqvnefrl rytvgttgse sfesfkgvtt sqyytdreyr giiatyllgy gnsalawqkt
      841 fkqnigldlt lfrnrlslna nyfieqtkgs iafissapss gfygyydnmg dvvnkgyely
      901 grfniianpa nrnnwsvfan afhfkntiek vsktiealnn rsntvssttp lpryaegqsk
      961 naiwavkslg idpasgnelf qtlngdvtti ynpadqmivg detptlqgtf gtnmeingig
     1021 fnvylrfnfg gdsynqtlid rvenvnvnyy nvdsrvasdr wqkpgdvaff kgildytgtp
     1081 lnqartyass rfvqknnfla gesasvyyrf adklnkklgl qntkvtlftn dlfrlgsikr
     1141 ergldypfsh sftlqlqttf
//
LOCUS       WP_090777521            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090777521
VERSION     WP_090777521.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111417
     Region          31..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvfylkkhy llvllvltal ganaqtgslv gkvldetglp lpgasvqiks lskntltnad
       61 gtykiiglsn gtvslfisyv gyqpkqesvk ingstvanfs lkpddqslne vvvvgygtqt
      121 rrevtgsisk vtgdkltaip apsfeaslqg qapgvqvttg sglagsgsii rirgigsisg
      181 ggdplyvidg ipitsdpfig gnrggmnqnp latinandie svevlkdaga agiygsrgan
      241 gvilvttkrg klgrptfnls tkygvstyan kpkfvdgpew lqlrqeawan dgntglaplp
      301 ggltwaqaeq nntdwwdlvt qtgrlndqsa sfsqgtekik sfvsanysnn esflkgnayk
      361 rygfrtnfdi kptsyfttsi nvgydrgtnk rvnaawgggl geamstalpi ypafnpdgsy
      421 ynnaanplkn vdlldwktvt drliagvmfe lkpvknlsik aianmdnmdv kenqyqpail
      481 rnqssgyana wpvkvlnhtf tgtvnydlef snkhklsflv gaenqesyrn lykdgiygda
      541 ngpfnkdtqs yekaladqik anslnyvlga drntfaslfs rinysydnky ylqvlarrdg
      601 sskfgpnnky gffpaasasw yisqenflsd nkvisnlklr tsyglvgssn fpsgqyysif
      661 yqgktyngng tvapdnvenp glkweegrnf digldfglfn nrisgefsyy hkktigalld
      721 ggispstgfl rgwvnvgeil neglelslnt iniqsdnfkw itrlnisknr nevlslgdfs
      781 adavrggtnd trisigyplg vnylvrykgv dpadglpiwl nkdgyetktf slddrvntgq
      841 vlpdyvgglt ntfsykgfel ntlftfaigg nlydgsakrq lgivtdwnir sdisdrwqkp
      901 gdiakfprlt mntgtypgls sewqynstmf lydatfvrlr evtlaynlpa sfahklrlqt
      961 lkvfasgmnl ltfskypggd pevardfenn qdrnmspnvt ylttpqqksv sfglstsf
//
LOCUS       WP_090777543            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090777543
VERSION     WP_090777543.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117984
     Region          51..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mirnstnymq fkkpfkylaf awivvfmqlp qlllaetgpv pvylarqetv tvkgtvkdgg
       61 dgqslpgvti sdsqrkvlgv tdgngsftvk avkgtelsfn migyavakrm vtgatntmtv
      121 tlnssssdln evvvtalgik reekslgyai tkvdstqltn aissnwtdal sgkvaglnlv
      181 rnsgpaasnk iilrgennlt gdnealivid gvvassssrr taatgggvyg tsgdimpvdf
      241 gsglndlnpd dienvvvlkg paasalygqr gangaviitt ksatknrktm gisftsnsaw
      301 edinrgparq nefgqgtdgt tsyqfgtgst sssygpafse nymfyqydpa tktkgltktp
      361 wvgygdpvdn ffvtgfesth svsldgtfkn vglrlsanhs dnewivpntg ldrtnvalna
      421 nanitkklsi nfkaqysnrh sdnlpatgyg nqslmywfif aqpnintewy kdywapgkeq
      481 qqfvnlttsf pegpyaiseq ylngqrrngw lgniqanykf skelslmvra sgdynkdtre
      541 tkrpwdtssg gmfaqgsfrv adiksyeina dfmlkydkki nndlqitasv ggsqmrneyr
      601 klekradglk vpgdyrldns inplvyvpdt aryrinsfya tsslsyknyl fldltarqdw
      661 nstlatltrk dnvgffypsa slafvasdlw kfpkavnfak frasiaqvgs gstvpyrtay
      721 nyliaangvy pdsamtnpti lpnpnlkpli tttvelgldv klfksrlnfd lavyagntkn
      781 qilsriidra sgynvgvfnv grvdnkgiel avngtpiksk nfswtvngtf sanrnkikel
      841 adsavvlrtg gfgnsgqiva mvggsmgdly gtgflrspdg qiifdkttgf akpnanieyl
      901 gntlpkfrfs fgtgvtykql smsvlfdaql gavghsftfs rmtsmgksta slpgryngiv
      961 gngvidngdg tyrpndviat diegyynsly ynqaeggifr tdylkfrean ltyafnkrfi
     1021 qgmgiskltl gvygrnlfiw spwpafdpef gtlagsdiqq gfetgqlpst rtygvrlvmg
     1081 i
//
LOCUS       WP_090777805            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090777805
VERSION     WP_090777805.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118727
     Region          37..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfktiktivm aalclnltae aqsqntpals kkqailgkvi sattaqalpg atikitgtsq
       61 slvsnnkgef ilnmangsyn lsvsllgykt snisiliplt apliialqld dknlqeveiv
      121 stgyqniake ratgsftlid nktlnrslgi nildrldgvt sgltfnrgnt tapnssievr
      181 gratlfsdaq pliivdnfpy egelsninpn dvatitilkd aaaasiwgar sgngvivitt
      241 kkgslnaspk isvnsnvslt gkpdlyyrqq lssaefieve dflfdkgryn ntintgyaal
      301 spaveiflak rngniseads lrminklktt dsrdqiskyg ykdwgihqqy sgsiagggss
      361 qkyffsggyd knqdntynns fnritlnann tyyffnnkle fssgiiytgs krkagpsvvs
      421 tpypynsivd esgnplpvvt dfrlaylena gkgklldwtw kpleeqhngy sstisnltdy
      481 rinlmlnynl ikglnaaaay sfgkgmnesn tlneldsyyt rnlinrfsqi dpntgavtyp
      541 lpmgailnss qnkltshngr iqlnynkdwk khvlnlltgy eirdnttisn sgsmygynpd
      601 fatnanntin htidyplfyd ssltgrisdp tsqysstdrf lsyyfngsyn ydgrymatls
      661 arrdesnlfg vstnqkgvpl wsaglswsln nekfyqldwl pllklrttfg ytgtvnntis
      721 ayltavlrgv gpsykqpfsd irnppnpslq wervkninlg vdfglkqnri sgsidywikk
      781 gldlignspi aaqtgvslfr gnsantltrg vdiqvktlnl tgavtwstnl lynfnhskvt
      841 gykvangtna nvvsgnwnnp legypfyaif syryagldas gnprgyvnge issnytdiln
      901 sgnrdelvys gpaaptsfgn irntfayknf elsfniiykl gyyfrrtsls nvdlyagsgy
      961 kiadyhlrwq kpgdelitnv psaiypvnaa rdnlytyadi lvekgdhvrl qdlrfaytip
     1021 kkqwlpienv nlfiytnnlg ilwkvnkhgv dpdypstsgl rpaktiafgl sasf
//
LOCUS       WP_090778224            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090778224
VERSION     WP_090778224.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116000
     Region          71..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msfkihieng aqalfrkvtl nstlgfavvg lfsaqvsaan yspdvfpass fgyhlkangy
       61 glnagnkiqt invsgrvtgv dgeplpgvsv qvsgssqats tdgngryqlt nvpegatltf
      121 kmigfipqqv vanksqinvv lkvdvktlde vvisdgyrtt tlaantsais sikgdvmenk
      181 pystfaqtlq gqiagltapt tsgqpganvd irirglgsls lnsnplivid nmivnsgklg
      241 ynsttanala glnqndiesv dvlkdaaata lygsrgsagv irittkrgks gktqirvdae
      301 ygsskamdnp dagkvlnadd yavlfrealt nsgstptlve taaenyglns gksnnwydlv
      361 trtgrqqqyn vsmnggteqt klfasagyfq qeattigsdl krisglfnfd hqiskrfqlt
      421 aginfsnvgq ntpygtqfsg sptwasrvlr pfqraynddg sintsnvgnt nfpgiynplw
      481 iadndkkyls qtrilgntql kwniwdklny tsyfsvdynt leetlflnav mgdgaglkgr
      541 sknyytryfn wlarnqvdyr ydingdkdfy vtaalgyeaq rskeyllaad gfgfpsaqse
      601 ltalsnaatp ngafgqysny sfnslyalad vnfknkyals asvrrdgssr fptknqgayf
      661 ysvggtwnvh qeeffkkqhv mssfklrssy gttgnasmgn yawvpqvgys ssysyagytg
      721 qqysssgnvd qrwetskkfd agldigfvqd rfmltvdyyy nniyglirnv ptslttgfss
      781 vgknigaman rgweltlkgd llrvndfrwy snlnaafnkn eitrlpentp vqngsfylke
      841 gysfntyymk efarvdpqng dalfykdasr tettnkiada slilldkqai pkvtggfnnt
      901 fsykglslsv dvnynlgywv tsaadiyftn asqylynkyq yifdhrwttv gqvtdvpkya
      961 tnpnndpsts tyrlyrgdhi rlrnislgyd iknvalfkql glskvfvygr atnlgtitfd
     1021 krlpidpevg ysgyddqdml qyrtftfgin vgl
//
LOCUS       WP_090780540            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090780540
VERSION     WP_090780540.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123689
     Region          134..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktnymnrea liegffktly lmrltpiiil lavlqlsard srgqkltynk dnttisqvfk
       61 eikrqtgynv vwyegklnsh msidanfynt pldkvmdnvl fgravtyqii gkaivvkadv
      121 ssfrdklial fanidvrgrv ldenneplag avvkvkgekn ststnsngef mlknvdenvt
      181 lvisflgyet qevkavknip sikltpstdk leevqinagy ytvtdrertg sisritskdi
      241 ekqpinnvlq amqanipgiq vlqntgvpgg gfkvqirgkn slnqgnepfy vidgvpfsst
      301 tisagqgngi llnssplasi npmdieniev lkdadataiy gargangvil ittkkgkpgk
      361 tntsislnqg isrvghklnl mnntqylemr neafandkit paanqydvns iwsptknidw
      421 qeelighnap mtnlqaslsg gdenlqylfs gsyykegtvf lekssfgrns gnigiqynsd
      481 nkkffatfsa nysqirsdlf pgdmtqfiyl ppnfpdlldn egnlnwddnr mninplaqsr
      541 rdftsktnnl ttntslgyki frdlifktnf gftkmdkhdy snnplnlryp gsnfgpesre
      601 avfsdyavet wivepqinwn ktvwrgklqa llgttfqqnl ndgqsivasn fasdallgni
      661 aaaslltvqe rrylqyryta vfgrlnynfs dkyivnltar rdgssrfgne srfanfgaig
      721 aawiisqedf irkkdnfisf aklrvsygvt gndqisdyay lslwstntgt sstyqglstl
      781 spnqisnpey awevnkkfea gidlglfkdr inlsfdfysn rssnqllydr lpyvtgwagv
      841 ttnlpakvsn tgiefiltsk nlstsnfrwn tsinftlpkn kllkypglgk qllyeigqpl
      901 silkvyntyv npqtglyvae dydkngiidd ddrykiefig rkyyggiens ltykgfkldf
      961 lfqvvkqsgs sfysqrgvtg sfnirtpqas nfpvelldrw qnvddrpsfq kfgttstnsi
     1021 snttatkngs laivdasfir lknvdfsytl psnvtkkikf nsirfylqgq nlftitkylg
     1081 ldpetqssvg lpslqvisag fqitl
//
LOCUS       WP_090781094            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090781094
VERSION     WP_090781094.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118973
     Region          42..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrfyyyfp lvmaiiccgl fvhskalsas hinlklllpp vtingkivne dgtafpgviv
       61 tlkgttiktt tntdgrytik lpeakgilvf syvgytaaev pvgsktvidv kmkpnvnsld
      121 avvvigygtq kqrevtssis sikgeeilky nvnsfqnalq gqmpgvemye ssgvpgaavn
      181 vrirgmntin gsagplyvvd gipvmqglng dgdapqsngn dqnsshtnvm adinpndies
      241 ievlkdaass aiygargsgg vilittkrgk agktsfnvnv isgitqiske kkllngpqll
      301 eifdeayrnt fysdpananl plpasplpsm tgytrgmadt tnnnafdhvl qtgvfreltv
      361 sasngtdktk yylsgtykqt vgtiqgtdmn qfnfklnidh dlskrirfga sitpsynteh
      421 klgssstlnl ggyggalssn lpiypyynad gsyfnpwtnp eafkdrdlyn slnkrsrigg
      481 svylevdvik glkfktlaqr edwdqsapsv lsgllnvtnd atisvfandq kgkathtnsy
      541 gysnsfdsff tynrvikkkh nlngvmgmrf sttngfyeal ygdnlinsnl iypsqtgrig
      601 nnyqtgvqgn pdaklgyyfr vqynynrryl asavvnrdgs srfggdkrfg tfpafslgwi
      661 asdekflknk vltflkfrgs fgltgnsggi gnlsakntwq tgspsvsgyl gtaanmpvqp
      721 aneqlhwekg tkydagidme flrgkisstv gwyknittdm llsipvpvtf gynvptldld
      781 flenrgslyn eglefsinsn iltgafkwks sfnishnitr ivslggldpk tvsggqgdvq
      841 lypgknapvf ylveyvgvdp atggelirdk nnntvlatsl taeqladark pqydkpsapk
      901 fyggfsnvfs yksfsmnvff syrvgnylld ageramsyvg nislknnsei anvflgnlpe
      961 silnrwtpdn pnsdipkvyy sdnknnplrs mnttrflsda syvrlknlqi syelperlls
     1021 rikmksvrvn ltgqnlwmwt kfkgvdpeai tiqtnyrern vaygvirnvi plsksvtlgl
     1081 nigf
//
LOCUS       WP_090782394            1198 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090782394
VERSION     WP_090782394.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1198)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1198
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131528
     Region          126..1197
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkiftkpif ylllfttlcs synalyaqvr kitvesalga iskkyktkfa ykhgiienkf
       61 adaeslkakt ldealkrvly pndllflyvs egnytiipkd edlktkqsga enalpetnav
      121 tnemfitgqv sdeagtpmpg vtvksnasnr svatdakgnf slwvpgeady vsfsyigydr
      181 yeaklngksq rfaislnpaa gnalkevaiv sngyqnispe rvtgstvsit akqieqvkta
      241 niiqriesmv pglkvtitag dnsfaygntq pnlnsddsrs igasdynmai rgrsslrtka
      301 fplvvvdgai semdlatlnp ndvesitflk dassasiwgv raangvivvk tksgqnnqap
      361 nvsfsmtgai nakprldylk imtaaeqiny eqelvakrli tkpnaianfg apvaevtdls
      421 yqlidnpagk aaydaritel ssrdsrsqve qyllqpannq qynlsvsggg alstyfysas
      481 ysherpstvg ndakrltigl nntfklfkva tlstnirgsf fnyknngisl nrlygatsst
      541 fmpydqlvdd qgnrtsfssr yysgwtnrlq gqgylnwnts yldeldnadn kqavnnysft
      601 anlnvpifkg lsanaffsne rtfglqtnyy nentfyyrdl vntftplpaa gtaaknsigl
      661 nrgaggilqq vnstdnnytv rgqlnydntf agkhqltvia gseirqtnag qggstmygyn
      721 tgtglsrpvn fatgypgiqy tsnlsgaatr qdkirrylsy ysnagytyng kytlsaslry
      781 ddynnfgvdr kfratplwst glrwdlaked flksqdwisg lglkasygvn gniatsvypf
      841 tnialsesdy qtglpyafvv tpanpelrwe ktyvtnigld lslfkgrina tadfyrkhgk
      901 difyefpvnd tygvssllrn atelkgkgvd iglsgvayrt kdwdvttgln fsyntnkiad
      961 trfiqtsslf snpayssyiq gyptdkllvy knagldargl tqifdengnk vaaerninsi
     1021 dalknagrts apyfgavnqs vkykaftlma iatyqfgsvf lrptitgysg grtgtrydls
     1081 edvakrwqka gdenitnvpg vagayaavsl qryqqsdinv lkgdyirlre lsltyalpla
     1141 rftkvaktad lsfgvrnlgl lwkankegid pdfatglnst tlglpasvsy nfslnvnf
//
LOCUS       WP_090782571            1188 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090782571
VERSION     WP_090782571.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1188)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1188)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1188)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1188
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1188
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132059
     Region          1..203
                     /region_name="LolA"
                     /note="Outer membrane lipoprotein-sorting protein [Cell
                     wall/membrane/envelope biogenesis]; COG2834"
                     /db_xref="CDD:442082"
     Region          117..1185
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkllmilg lfltvtfaqp awaqeqitlq kalaeiqkty gtkfsyqagl vnnvkvglnl
       61 pltksepven vlkkilypnk mlflyvqeny ytiirdtred ekqleaarqn tpepnyrtvt
      121 gkvtdekgnp lvgvtvfpeg tnvrqgviss sdgsytlrll gtadaivfty vgmqpkklal
      181 gksnvvnatl yneqnvlnev qvvstgyaki skeratgsfd litkedikev psvnllekle
      241 getpglqvnl rnntisirgr nsfgsgynps plividgfpv mdnedgravl sktasgngts
      301 gsailsrfnp ddiesitvlk daaaasiwga qaangvivie tkkgrntppm infgtnlsis
      361 apsdlnnikt mnsaqyidle relkdlgfit dpavkpswaa fntnrpqsea lewmfkvdrg
      421 tatiaerdaa laalgqidnr sqikdlllqn avsqqynlsl sggankstyy lstnytkdip
      481 vfrgnkaesf fvnsnlnskl fndrvnlsfg lnynysnsvn npaaldamgt gqrglrpyel
      541 lqdangnnis rairyreevv qdfmnkgyls wryspldeld qtdyntqsnr lrfnmgvdtk
      601 iiegvnfvvs gmlqrnieet nnvdrvgsys vrdmlnyatt vntagklvtg ipyggilgls
      661 nyngweyslr sqvnvdrnvg gllniaflag aeirqnryqs stqqrygfne diyqdktvnp
      721 tvpynnvdgw qstisynntl rkninramsy ysniglsfls gkyvasgsir fddftitgas
      781 rnqraqplws aglkwnakle plvkdinwln alnfrltygv sgtlptgsgn vvtlntsvdn
      841 ltnettaqia spannqiswe kvksfnfgvd failnnrlaf nidaydkrta dilytfpyns
      901 tygwnslmfn sasmkshgfe lgmranvirh kdyswssvfn fsyntnevtd srlkknttsn
      961 iigsslptvg lpvdyiyayr waglddkgqs qvynkngdil nssvgnnqlt addlvymgra
     1021 tapyfggfnn dfrykqftmg vrisysmgnv irkpsvesyp dyspyqgaig mhsdlaqrwk
     1081 qagdenftnv pglknitfns lnryknadil misgsyvrlq qislgyiatn ellkrtpfks
     1141 asinasvrnl gllwvknkyg idpqymasss ynnlapaktf fisintsf
//
LOCUS       WP_090782604            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090782604
VERSION     WP_090782604.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109186
     Region          33..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrfnyalfqr sclcmlllli cqsfnvalaq nerkitgkvv ddqslplpga sisvkgtsks
       61 tasgsdgafs itakkgdvla vksigfetke itvgdaasyt vkltqtstnl sdvvvvgygk
      121 strktlssai tsvkpeelnk gaiadvgqll qgkvagmnis asgdpnkpaa vilrgastvn
      181 spgapyyvid gvpgadiaai apadiasidv lkdaaataiy gnraasgvim vttkrgksgq
      241 pqvaysgyag aekvsntldl mnadqlrafi aangaafspn ddlgtntdwm ktiqrstays
      301 qnhnlslsgg sdktsysasl nyfnkdgila esslnriigr lnidqytfnd kvkfslnlsn
      361 sgsksinvpl qnivllqaak rlpispvyaa dgsyfenlnn tgyfnpvait gnaqdetkyn
      421 vllgsfntev klpfdltyni nlsyqkttss hgefyssyfg kyptsnfynn pdpgigisht
      481 ligslfgsng salrsnfena tktletfltw nkkigdhain avlgytyqdn vygdgfqtss
      541 tnfptdnigf snltlgnpya issyrinlgn dltygrvlmi sdffrvnysy kdkymfqgsi
      601 rrdgssvfge nnqwgyfpsa glawrvseee fmknqttisd lkirvsygvt gnssgigayt
      661 gklvygisgt yynngvqaaa yapvqgsnpd lkwertatkn igvdfgllnn kitgsidvyd
      721 knttdmlfky nvssslvpgg aiwanggsin nkgielslsa spvvtksfsw sstmnmaynk
      781 nkitslkgpy ssgdsirysd pegpgqtnst lqllkvgypl gqffslkyag kdpdgkslfy
      841 khdgsttttp sigtdyfylg naqpkvllgw sntfkykdld lnifirgtfg nkifnatrad
      901 lsytagaavn nilnsaandk isdtrnsfys dryiengsyv rldnatlgyn fksplknvsn
      961 irvyastnnl ftitgykgid peinqggvap gidynnfypk trtfllginv lf
//
LOCUS       WP_090784025            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090784025
VERSION     WP_090784025.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115397
     Region          42..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkftirik tgvltfalfg llgtperlys qvqatqvrav pkiigkvfde qkkpipgvmi
       61 siksnpriat ttnntgefil spdkagetlv issigfkrqe ivlkadtklp lvivmkestd
      121 elkevvvtgy strskesftg sassftgedl krvgnknilq slqnldpsfv ltenltlgsn
      181 pnmlpdiqlr gqaglddvrg eysgnpnlpl fildgfessl qkiydldmnr vasitilrda
      241 sakaiygska angvlvietl apkegklrit ynsnfnvemp dltsynltna seklqverna
      301 grytssspli qqflteqanv iesdiargvd tywlskplrv glgtkhglyl eggdanmryg
      361 vdlnynnlvg vmkeskrdnm ggsinlsyrs gkvsfrniln vnfnksvnsp ygtfgeytkl
      421 npywapndes grinkilgqf qtsataptky yynplynatl ntkdfstyte vtenfytewq
      481 pskelritgr vgftqnrnas elffpgdhtk fiamtgedfy rrgtynitdg ksttlnsdvf
      541 anwnktwgkh lllvngggnl gstqaqthgm aaegflnnrv dfitfaaqya qngvpngsen
      601 iqkeigilgs anysydnryl ldlsirrnas svfgannrwg tfwsvglgwn lhhenliknl
      661 nifdmlkirg svgstgsqsf npyqamatyt fftnstydnv sgtylaalan dnlrwqqkid
      721 nnigldinml krlnirldyy iantknlltd lslppstgfs tykdnlgslq nkgyegtisy
      781 qlyrdsksqs yvsifgsfah nsnkitkisd glkqlnreqq ertdnlsspi irfeegqsms
      841 siwavpslgi dpatgreifr akdgsttyew npndqivagi tdpalrgnfg inleykgwgl
      901 sgtfrytige dyynstlvsr ienvniennv dsrvfnntwl nvgdkvpfkk itvnpivtra
      961 ttrfienksd ltlssvnvyy dfkwrnlkri glknlkcsll mneafvlstv riergtdypf
     1021 artfsfslqt tf
//
LOCUS       WP_090784335            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090784335
VERSION     WP_090784335.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121860
     Region          122..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlvlfllvt gllqigntgf sqtitftgkn vtvekafsii qeqtgyrvag kkellkqgkl
       61 ltvkadkmpl ndflnlvstg qpfvcqvdet niiisvrvra pnteglgqpi kmvpsdlmqq
      121 pikgkvtden gapvsgatvs akddkqqvvm tnelgefmin vplgktvtln hlafqskefm
      181 vakrmydgpf nvvlterdnd lnevkinkgy ystskvlntg svvrvsakei erqpvtnvlq
      241 alqsrvpgli inqqsgnpgg nfniqirgrn sinksnplfv vdgvpfsmda mgqvagvvsv
      301 vgssvnvsgs gsaagsqgls plnsinpedi esvevlkdad ataiygslga ngvilittkr
      361 gkpgplrvsa nfnagfssps smpeymdtkt ylkyrrqlfe ndesspgvtd ydlngtwdtt
      421 rytrwgkeli grqnvnvnsr isisggsdkt qfqigagytt isppydgdfs ndrtslsfsi
      481 sntsannkfk mvfsgnygne vntlpgldis qfvnlapngp vlrnpdgtln wwspsavnpy
      541 asllqkyrat tkniqgngti syqllpslml rsnlgysdrq fnesrlnptt sfnpatntna
      601 saligvnsgs nwiiepqaef nktlfggkis llagatfqdr fstgqttsat gfpsdvllnn
      661 iasanrfvin nryakyrysa vfaranysln dryiinltgr rdgssrfapg rqfgnfgaig
      721 aawifsrenw vsehlpflsm gkfrgsygtt gndqigdyry lesyspvngi tylgvsgllp
      781 srlfnavygw esnrkfelat elgffsdrif ltaayyrnrs snqlvdipla pttgnsviqa
      841 nlpaliqnkg fefdistkqi stknfswstt fnisfernkl lefpnlelss ysetyvigsp
      901 lsispklfkm mgvnpitgiy efmdkdgkaa tspdlavrte rvdmnpdyyg gmgnsftyka
      961 fqldvqlqfv kqigrnpvfs talggalpft nlvnapgyyn gniwmkendi atlqrlsagg
     1021 fsqagaavst anfmlqnsda vysdasyirc knvslswqvd qrlirtlhig qlrvyaqaqn
     1081 lftitnyvgf dpesqgsvlp plrtlafglq ftl
//
LOCUS       WP_090784426            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090784426
VERSION     WP_090784426.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118397
     Region          27..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkikkylgf lclissfsls gfgqdsqikg yifsakdslp iqgaiikmdn yssktdetgr
       61 ftlmavngkh qlsvhhltyl arqievtipl aielriylte svemlkdvvv vstgyqtipk
      121 eratgsftqi dnqllnrtpg snvisrladi vpgltfnrni gatensisir glstinsnae
      181 plivlnnfpy sgdinsinpn diesisvlkd aaatsiwgar agngvivitt kqgttgkvki
      241 sfalngtigs kpdlfarpsm svadyietek nlfskgyfsg aensdnkpal tpavdllial
      301 rdhtmdpvla etklealkqi dtrsqvteyl iqnsflsqhs lnlsggsavn syflgmgydm
      361 drmnsignss srisfsashn yqiinnklel stklsfsqlk trlkqleqsi sypyaqlrde
      421 qgsalpvvrd yrrafidqaq qkgllnweyr pleelnldvg dtniandsrv qlgltykpfd
      481 gfsaillyqt arvnsnnqrl fsqesyytrn linyisaiaa dgsilrpipl ggimdlenri
      541 sktnhlraql vynktwgins lnliggaeis eeeitgqtsr fygydketga fqvvdyskny
      601 tsyvnpsstn npirnldklt glderfisyy snaayslkgl yilsasarfd qsnlfgvatn
      661 qkgvplwstg lgwlvsgegf yrsnwlpylk lrmtyglsgn vnkslsaytt aryipgtlsr
      721 vklasaqiin ppnpnlrwer nqifnlgidf ataakrisgn lewyskkgfd ligtipymps
      781 sgfnsftgnt anlltqgldm tintkniqta lnwnssfifs yakdkvthye yfesatsyln
      841 tgayggitpl qgnalygiys yrwagldpln gdpqgylndt ptkdygniis sanpqniiyh
      901 gaarpvifgs frndfsyrgf tlstnisyrl gyyfrresiq yndnlglggh gdyyqrwqnt
      961 gdenrthips mplspnsdrd qfykfseilv srgdhirlqd iklsyknklt nsrkialsnl
     1021 elfvyannlg iiwqanrfgi dpdynyaklp favsaglkld fn
//
LOCUS       WP_090784746            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090784746
VERSION     WP_090784746.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122141
     Region          135..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mykinymkrg alrqgihkil flmrltliii liaaiqlsak dsrsqtltyn kkettirelf
       61 keikrqsgyn lvwsdrklnt eevievdfyk tpvktvldki lfgravtyki agkaiiimed
      121 drsfrekgig lfdgidvrgr vlgenneplv gatvkikgst nstvtnange fslqnvnakd
      181 ilvisfigyn skeikasenl gniqlvlstd klqeveinag yytvkdkert gsisrvdskt
      241 iaqqpvtnvl galigrmpgv nieqqsging ggykieirgv nslrtdarqp lylvdgvpfp
      301 assislaals iagisnlssp lnyispydie sievlkdada taiygsrgsn gvvliktkqa
      361 kagktaadis fsmglstvgt kikmlnteqy lqmrteafan dnvtpgatsy dvngtwdpnr
      421 ytdwqkelig gtaqqtnlqa gisggsdltq ftfranylkq ttvspgdfad qkgsgalnin
      481 htssdkkfkg nfsttyaidy ntlptfdltq fidaapnapa lydgngnlnw aynssgvstw
      541 tnplfgnnip ylgktgtflg ngrlsyellp glsiistlgf tnlqlketkk ttlnsqlpsp
      601 snsgnrslvh tnietwiiep qinylksfkn akldillgst fqgnsqvter ltgtgytsdl
      661 llenfgsapt rsitntsaqy rynslfgrin ynyqgkyivn itgrrdgssk fgpdrkfanf
      721 gaiglawifs qenfiknnlq wlsygklrss ygitgsdqip dygyqqtyts tplaygdgpa
      781 lvpsrisnpd fswetnkkle lalelgllnd rvqfttswyr nrssnqlvgy tlpdiagfts
      841 vqynlpaivq ntgwefevss nnisgnkfnw qtsfnisipr nklvsypnis gstytntytv
      901 gyslytaiay qylgvdpqtg ihkfadldgn gtlnaadrlp asqslsthwy sgiqnsfsfk
      961 gielsiffqy vdktlknplq lfnspgtisg glnanqpvev larwravgdq tsiqkfsqsf
     1021 ataspytqfs nlmssndyid asflrlknvs lsyllpksls khaglrscrv flqgqnlftv
     1081 tnylgdpeig miktlptlrt fttgltigl
//
LOCUS       WP_090785090            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090785090
VERSION     WP_090785090.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116030
     Region          23..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnktitllil llafsvavwa qerdfsgkvt tsddgqaipg vsvtvkgtsr gtsttvngty
       61 vikastgsvl lfrsigylpk evvvgtqsli svslsqddqn ltevvvtalg ikrsekslgy
      121 atqalkgsdl tltkeqnvig slagkiagvq vtgssgasmg gtqkikirsv nsvtgsgqpl
      181 mvvdgtpisq tnfsgdangv dygntsqdin pediesvnvl kgpaasalyg lrgqygvimi
      241 ttkkgakgpk kvevsvnsaf tidkagnfmp lqniygvgnn qtfltlangq kyvngndesw
      301 gpmmdgtpvr mfysfypldp dfgkltpfvp qpdnikdffe tgynlnngis itgggensnf
      361 rmsynnayin giipntwlkr nnlslsssld ltpkltvgan vnyannsgqr ptqgyqgsyt
      421 ganqwfqrni dinrlrnyry sdgtilnwnv npntttglit nnrpsdwnnp ffdayevlnn
      481 dnrnrlfgdv nvsyqllpel klsgflrsdm ytqnithkea eggrnlsgyk ianyqgtdnn
      541 yellaqyakk wndlsfnlnv ggniynskyt ktedatvggl sapdaytmaa svdrpssisy
      601 lsrkstrsay amasvgykdt yfldaslrnd nssalpknnn sywyssvsgs fifsqlmpsd
      661 ilsygkfras yavagadldp yqilpvygfg gvyapqtgsi ntlyvpdkll npdlkpsfgr
      721 svevgadlkf fknrigldlt wyqqrnenqv inlavsgasg sekmvvnagl iqnrgielsl
      781 tartvqskff nwdmafnfak nknqikeiyg aievyqldvn tyssqsiyln sslgetfgnl
      841 vgpgyikdpa tgkvflgadn mplftvakdf gsvlpqytgg frntfkiwkf dlaamidfqk
      901 ggqffswskm lsaksgqaee talfndkgfn vrdavanggg vkvngissit gqevtayvda
      961 rtyyrtnlgt riydewiyda syikmreisl gynfdeqflk ktpikslkva liarnpfmiw
     1021 qkapkgvdps elssgsasis wiekgelqtv rsygvnlnlt f
//
LOCUS       WP_090785646            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090785646
VERSION     WP_090785646.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117944
     Region          51..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfksitlfks lpvmltllav ssvgfsqqsd slhipgdtvk vvlnkkakgp klkgiiidas
       61 tgkplsalnv rvegysaalt dekgrfsltv pdynaiilvs gigfqekeis lkgrkelnir
      121 lhedsftsfy deaafafssk rlshitgavn tvntqggwnl nsetpdtylq grvsglnair
      181 rsgtagigan llirgfnsin stnqplivvd gmiydnnsyg ssligghvnn plqyidvkdi
      241 dnftivkdat asiygtkaan giifintnha kelatkidfs mygglnlepk rlpvmqsdsy
      301 rlylsellqs ggytsaqisa lpfmndnpns nyytyhnntn wqkeifrksy dqnyflkitg
      361 gddiakyals igylknkgvv dstdlikynt rfnaefkltq kltananlaf tyaeqnlkdq
      421 glstktspiy salvkspflr anevdasnnv spslsdadif gvsnprslin taqavtknyr
      481 ffgsvnfnyq fnkslnfssl igvtydkqre syfipkkgvs ndtlrsaiad srlsaqvqri
      541 yslysdtris yrktfdkhni satagfryis sntesdyart ynsatdqlis igngsaalre
      601 lggeigkyrw lnnyltaeyd ynrkyflnvn vsldgssrfg neategfkig gapfavlpsv
      661 saswlvssek fmsdagfiel lkvrasyglt anddignyta rqyyvkqnll glsglvrgnf
      721 gnpelqwerv akanfgidas flnenlsfsv dvynnrtskm liyeptqtvs glgfsvtnsg
      781 amrtngvdvg inarilnrvf kwntgliyst yknkvlslpn nngslinsya dasyitqvgr
      841 vanlfygykt ngvyatnaea asagysikta lgnpvafsgg dirftdvngd kvidendrvv
      901 ignpnpdftg sfsnqfsykn wsldalftfs ygndlynftr anleseknyn nqsiailnrw
      961 kmdgqvtdip katlndpmgn srfsdrwied gsyfrlrmls laynvplktk alkyvkvyat
     1021 gnnlfvltky lgydpefsat gsiytqgvdv pvepqirsfq lgvrigl
//
LOCUS       WP_090785650            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090785650
VERSION     WP_090785650.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122421
     Region          32..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrfftkniy lvfafilila gssfaqvqta vvirgkvtda kdktgvigas vvevdkdnrt
       61 vggvstdieg nfalkisnpa nkimvsfigy etqrgiving rttinvslkp snnslneivi
      121 ggkrgtdngt gmrvdernrt tavatidakv leemqsasid qalqgrlpgv diaatsgdpg
      181 agmqirirgt ssingatnpl ivvdgmpyet eipedfnfas sdennyaqll niapsdikei
      241 svlkdaaata vwgsrasngv liittkrgti gkpnitytfk gsyskqpsai pllngnqyst
      301 liseeyynag kifsttefak efqydkndpy nyynfsnntn wvdaitrigy lqdhnvsisg
      361 ggeraryygs lgyfnqqgtt kgtdlgrita rinldytvse kikfrtdvsy thisnnqlyt
      421 gskdlgvrqa ayikmpnqsi yeydeygnlt dnyftpatta qgfayyylrs gnyvlggtyn
      481 pvsmalqasn yqlgdrvtph fnvqynvvpg vltatsdvqf dinnskittf lpqivtgrpv
      541 tetisnrasd vdgdqftvtt ktnliytpvl gskhtfqgll slqsndsryv sqqamsansp
      601 sselsdvtsg grtanfdlrl yssvsqtrsv galisaqygf ldrylinvgl rgdgnsrfgp
      661 nnryglfpsv saryrlsgep fmkgvkfidd lsfrasygqa gnapkkdyrf yntyntydyt
      721 ylgetgvsss nleltnlrwe tvtgknigln lnmfdnrvni dvevyrnrtt dlfyenlals
      781 nytgfnsvdm nvgtmdnqgw efslnstlik nkkwrvdfaf niaqnqnmlr eisplypaen
      841 ngkittngty keylqvgnpf gsfygfkfkg vyatteatva kdadgndivg lngqkkymkf
      901 yannasinyq fqagdaiyed inhdgsidyk divylgnsnp rytggfgpsi tfngnlkvsa
      961 ffsfrtgydl ingtkmattn mssydnqsta vlrrwkaegd itdipravyg stnnynwlgs
     1021 sryvedasfl rwrtvtvryd lgknflkrvn mkglsvyvta eniltltkyt gqdpevttki
     1081 sgpfsvaidn smtppiktmt igisarf
//
LOCUS       WP_090785757            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090785757
VERSION     WP_090785757.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113668
     Region          36..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkilyanglp kirlvfwvpi illmltqvan aqtkrftltg rvtdgtssvg vpgvvvkvqn
       61 tnfamatnad gryslnadlt pgtyqvvfss igyksqtksv elgaatqvtv ngalmadnig
      121 ldevivtgts qgttrkqmgs yvssvkgddl vkapsgnvls slqgkapgaq isqnsgdpag
      181 gmsvrlrgvs slnsssdply iidgvivnnt ttrvtntsan ydgggsgvgg ngnfvgaigq
      241 nrmsdinpnd ierievlnga aaaaiygsra nagviqiftk rgvsgkpvis lstsfttshl
      301 rkqievnqsp vkfggtvdel tqdvislvgt paalptntta vtrynyqdyi fqsaigtdnt
      361 vsvaggsent kfytslgyfs nqgiikntdy rrinmranld qkvndwakfs anfnyihsda
      421 nekpdgnsff spmnsvtiig nfhdlftrda lgnikavger grvnpvsvie dikqrqavnr
      481 iisnaklvln pikkitidyt igvdntiqng ttfippfayn vstgfygggl tldpslngya
      541 saasstttlf nhelnftydt klsdvllstt qlggsyqyek thyllsngrg lapftesvdg
      601 astilansda rlqsdisgvy lqqnfkykdh lfvtgaarvd qssvfgvknr tkaylkgnvs
      661 yvlssadywa glgisewwdt fkvraaygqs gnltgiapya rfneyfaspy isktslvskt
      721 qlanvdiape kqteielgmd lsflknrlgl vfnwydkkvs gllvpvviap ttgfstllen
      781 kgslknrgie lmltgtpvas kdfkwntsfi fnrnrnkvvg igatqllstn agapvafidg
      841 apagvfygtf farnadgsll tnpagipqte rgiqnsslsy tpqrgpdglp latgtttlrk
      901 vigdpnpdyt asfvndfsyk kltlhvqlda shgadvwnad wrtrqgvggg kvaeqeqmgl
      961 lprgyvsgvy aieewriddg syvklrevsi aynvgkvkfi qdltinlsgr nlvswdnykg
     1021 ydpelnsggq stqlrnidfg svpiprsfsl gvrakf
//
LOCUS       WP_090785667            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090785667
VERSION     WP_090785667.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115354
     Region          38..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mflpcllfla fsntllaqet dtistkkvav vkratgpqin gvvtdaatgk plpginvsvt
       61 gyaaaltdek ghykisvpdy ravvvisgqg yqskeealkg rktissalye esytsvydaa
      121 llpfgivlkn rtpyavtavn pngswersne tpdsylqgkv agleairrsg tpdigadlyl
      181 rgynslyaan qplvvvdgvl ydintygssi isghqtnhla nvdikdidni tilkdgasmy
      241 gtrgangvil ittsrakdva trldfaaygg yngtvshlpv mqadnyrifl gdmlrtrpgy
      301 tdamikdepy mndnsgpdyy tyhqntnwqd kvmssgtsqn yylkvtggde vatyalslgy
      361 lnneglthkt dltryqtrfn anlnlsaklk aqanlaftrs eqnlrdqgqa ystnplylal
      421 vkspflsshe isesgvlspn lsdtdifgls npvaaaesve avnrnyrfvg svgfdytlnk
      481 sfkistiigv tydkvrenyf tpelgitpvl lptavgynkv aagvqrlfav ntdtrlayqk
      541 nlnhfsklsa nlgfryqsss aeldngttyn tasddfvtlg sgqstlrivg galgkwnwln
      601 tyfnvnyeay skyflsfnva adassrfgke ipdvltlngv klavlpsvag swlvssenfm
      661 annafveslk lrasygltgn deignysakt yyvsqnflgr qglirgnign talkwetnak
      721 lnvgmdasfl kerlnisldi yrnkisdmli yepmltatgf dyglrnggtm enkgvelavs
      781 grlinknnlk wdmgftyaln rnkviglgen qnlitnfsga tiitqpgsaa nlfygyktkg
      841 vyatdaeala sglsnktvdg dfipfqggdm rfvetngdgt idendrqvig npnpdftgsf
      901 snklsykqwt ldalftftyg ndiyngtraa lesmngynnq tlavvnrwrv ngqvtdipra
      961 swddpsrnsr fsdrwiedgs ylklrslals yklpklaffr satvyaiann lltltkykgy
     1021 dpefsagssv fargvdtgle pgtksvqlgv rigl
//
LOCUS       WP_090785760            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090785760
VERSION     WP_090785760.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111811
     Region          24..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklllltv gvfllfahgf aqqktitgkv tssddgspip gasvkvkgtp tvtqtntngl
       61 ysiqakagdi lqfsyigmim qekvvaaavl nvrlnpdnks lnevvvtayg iernakslgy
      121 stpvvsgdav satgrenfin glagrapgvf vnptsgdpga ssqiiirgiv smtgdntplm
      181 vldgvpidns vssqtnmama gnnrsqdytn rasdinpadi esyvvlkgpe atalygnlga
      241 sgaivittkk aksgkasvsy ngsmrietvn nppevqlvyg qgdangifng gsfnffgpky
      301 peglpvydnv gsffktgtaq knnlvveggk egltyrwsne ytnnkgtipk tqyerfvssv
      361 vgvlpvsdki kvttrfsytn aynrkankgv qgylmgllrf psrfdvnnwi dalgnrvttt
      421 gtiytesdnp fwdinknlse dktnsilgna nisyrptkwl svtgilgtni sstngmtvyh
      481 tqsysgsgna atptggtvnt yqqlnkrldg svtasavhkf gsfnntyiig anfsdvnntt
      541 nsakgqnmid qnfysinntl pstqtarlyv gryrnagvfa qailgyqsil fltlsgrlda
      601 asrlmptnpy faypsaslaf nfteleavke lkwlsngklr asygitgkep yklyalatrl
      661 qsagstgggl aydsangenk nlvpeqtrsf etgfemsflt erlsvdftyf rlnshkqiiq
      721 prtsygtgfa lrmmnggdvv nrgfevqlkg spfrakdfgw dmvfnftssk gkvlsiaeel
      781 pefydsdtwv angvrgavyp gsstmalggw vnlrnnrgdl linpatglpi lgndqdfpvi
      841 gdrtpkfnlg fvnniryknf dlsflldlrv ggdvynqtqy elyrrglsvk tldrdvprvi
      901 tgvlrdglen tdnptvntll itpsantnyy tsttsgispd mfvekniksl rlrdvtlayt
      961 fpakmfssts fiknlgtyit ftdlflitny sgmdpdtnan npslggsggy gidygnmgrp
     1021 lgvnigfrlk i
//
LOCUS       WP_090785765            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090785765
VERSION     WP_090785765.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110660
     Region          24..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkilmlfl stfllvahti aqqitvtgkv tsaddklgvp gasvkikgts sgvqtnldga
       61 ysikvakgev lvfsyigfvt qektvgsaav idavlatdsk glsevvvtal gikrdkrtlt
      121 ysvqtvkgdd lrdanqsnii nglqgqiaga qitssggspg lpseiilrgv ssltgdnqpl
      181 mivdgirvsn assdgtinrl adfnpadies isvlkgaaaa alygidaasg aiiittkkgk
      241 egkmqsnlsy ksfietvgrt peqqkiytsg tgsgfdessi sswgrkyrsd eliynnidrf
      301 fktgvvhdvn fnatggaekf nyymsgnynn gssiipntet dkfsmlikgs aqlaknleln
      361 asanyiknni kegivggssg gyangiymyp lrydinryqy engnpyyeyy ensgseetar
      421 ispmwgvmrn prntgtqriv vngelaykan dwinlsfrsg qdyynqefsn itvpgtpgsy
      481 mkdgrlyqtk gnykyqtnif nstfdrniik dlratlilga sseyfeastn sftgtgfivp
      541 diysvnnipa tnlitaeglr krqryavygd fkldyknmls fgitgrndws stlpinarsf
      601 yspsfsgsft fselfenkds wfgklrasya kvgkdapiya tyttlspyyg igggyqnnpt
      661 iggntnlvae ttrekefgve frlfksrlni eaayydkesh dqivtarvpl ptgfvnqtfn
      721 agklrnrgfe lsltgipvkt kdftwsatln twinrskmle fpgqievfpy tfgnpynaak
      781 aasmlnmpvl givgtdylkn ddgytviggd gypvinsans aqyignrepk lnfgflnrfn
      841 ykdfslsflw dfrfggdvyn atrlgmtsrg iskevgdwrd qsftfngvvl qddgsyvknt
      901 kqvsldykyf venyavtgtn fietvnwarv ryitlayslp kkytdrlkla rvgielsaqn
      961 pilitnysgg dpevnsagpn agggggstmg vdygaiplsr sysigisvgf
//
LOCUS       WP_090785943            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090785943
VERSION     WP_090785943.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121228
     Region          148..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfsaksagy ttivfpglys ivrktliyki mrlslftail tiastqlmla srtsgqsmsq
       61 vevnielkke savavlkkie sqtnfrfvyr ndqikelkel elplkkrsve ellrlvfndq
      121 rfrvtqlnnn niqilsipks aslaavrisg ivldefgspl pgvsvmikgn rsvstatdqn
      181 ghfgidipek gvrvllfsym gyqtqevelg tetsvsvrmk pssgslnevv vigygtstrk
      241 dltgsvarvd akiiqeqpvg nvinalqgrm agvevsqssg lpgsgtsiki rgqysiqsgv
      301 eplyvidgvp fnfslnvfqt gangtvnpln slnpsdvesi dvlkdgdata iygarggngv
      361 ilittkkgka gktkldvnls sgigkvgrki dmlsgeqyla lrkeafandk vtptivnapd
      421 ltswsqtsfr dwqddliggt ahytdaqatl sggnedtrfa fspgyhhegt vfpgssaedr
      481 isarlnvdhn srdkrfaalv svaysydknn lpirdlssyy nlapnydpyt atgafnfvsa
      541 yqynpyalla qkykgttanl ignmslryti lsglslkanl gyttlnfdqn gqtpgltinp
      601 afntatssaf faattarsyi vepqveyvke lgkgkltalv gttfqsntst tntvnganyt
      661 ndallgsiga agtlsgstry dnynfssifg rvtynylgky ilnatmrrdg ssrfglnnsf
      721 gnfgalgaaw ifsdeafvkd nlpflsfgkl rgsygitgnd qisnyqnlat ynaagsssgy
      781 qgttiqnpar lanpdikwes nrkaelalel glfnnriqfn vaayrnrvgn qilsistagq
      841 vgfssytgnf patiqaqgle felntknier gdfrwstafn ftlnnskivk fdnlaslnfy
      901 ansfivgypv pfsrqyifng inpangaity qtanangvpt flvdqqptpv gspyyggltn
      961 tfsykrfdfg fffqfkhqmg yinsvtgslg slnnqnsstl dhwrqandnt qfgaptanss
     1021 npafnlysft ynsstaffgn aswlklknvn laytfpkdwi saaklsnlrv yaqgqnlfsi
     1081 snhknvldpe mgagqgggpg mpalrtivvg lnasf
//
LOCUS       WP_090787487            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090787487
VERSION     WP_090787487.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113925
     Region          23..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfi lmfvagaama qdrtvtgtvt gkddglpipg vsvkivgttt gtstdangky
       61 alkvasgqaa ieissigylt qiipigssnv vnvglatdtr qlgevvvtam gitrtakslg
      121 ysvttlkgde ltkaretnvi nslagkvagv rvtsqsgtvg gsskiiirga ssfnststsn
      181 qpifvidglp vdnssqqint istssvpqgs agsdygnrag dinsddieti tvlkgaaata
      241 lygaraknga ivittkkgkk gegsvsfnss trfdnvlklp kfqneyaqgv qgvystgpnv
      301 nssslngwgp kisevqdqlf tdylgnkvtl qaypdnvkdf yetgktyins vsfegggdsg
      361 dyrfgftnti qdgivpnekl kknalslnag rtifkgldvr tsanytrtva dgrpvqssnn
      421 psvlqsivyg lprtidvnvl rdhyvdpitk qqialtptrt gnnpfwvvnn nnfsnvvdrf
      481 ygnaivtykp lewltisdnl gtdfyneyrr gvtrqgtigs ltgdfytanl ynriinndli
      541 ltadkklted lslkviagyn vfesyyrrdl adaqqliadg lynyanagsv vstntsnmrr
      601 iqgvygdvgl sykdylflnv tgrndwsstl piqnrsyfyp svsssfvfse vlpkttwfny
      661 gklrasyanv gsdtdpygga fsyspisaaf aqygygstfp fngvlafsnp atipnfdlkp
      721 qnqasyevgt elrfldsrvn ldltyyytnt sdqiidlalp qstgfsfvnt nagsvknkgv
      781 evglglvpvk grdftwnmni nfaknvqkve lppeltsysl asgwsglsik aetgqsfgiy
      841 gvawqrdpsg nliidaatgl rktvsdkrlg nmspdwtggi entfsykgas lsflidmrkg
      901 gvifsnsvss lrtsglgeet llnrgnifid kgvvagpggt fvpntvpvts mqdywaqyst
      961 tnteanifda syvklrevrl syllptkllq rnlkfiksae iglegrnlwi ihdnvphidp
     1021 eanffgtesv aegvefnsip strtlgfnir lki
//
LOCUS       WP_090786309            1215 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090786309
VERSION     WP_090786309.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1215)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1215)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1215)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1215
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1215
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=135138
     Region          151..1212
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfytrchhg vsmvqqqite mespessrdn wqltkkiimr inltaliial afinvwasvn
       61 gqvislkann mpiekffdai kaqsgygfwy eknnvrniti svnadqknlr dlldtylpdk
      121 nldykivdrt ifikkkdqsv lekignlfkd iiisgkvlde tglpligasv slkgtnksva
      181 tdkngffsle vpetgavlsi ryigyenyey kvtgttditv tmkqatstlq evgvvsdgyq
      241 tiskeratgs ygvisakdlk evqsnniler legkipgvrv dvrnnniqir slntytnntp
      301 plivvdgfpm intgdnqglt kvqnstlang svlsnfnped ieqitflkda vatsiwgska
      361 angvivittk rgkkgapvin lssifstskp vsfsdlnwmt saqyadlete mvnknfirda
      421 aaslntknps evqewlfkvk rgtatqdqan qaiaeissrd nadqitkyll qnaitqqqnl
      481 sisgggednt yyiaanynkd rpvykgnsan ntivtanftn sffknrvtln tginyqyakt
      541 qinqaatdal gltttslrpy dllvdgngnh ilrniqfrpe fettqvakgy lpstynaide
      601 lnysntkgss nqfrfntgln vkivkwlean vsgsyqrnin ntlsineans yigrttinty
      661 ttispttnrp vynlpyggiy tlsdansyvy nlrgqlnmnk nfgsdhtvta ligseiseay
      721 sksysntqyg ydgdsntfgl vdaktqyptm ygysqnipnp nsgvseqktr nlsyygnvay
      781 syrgkydfsa sarfddytqv glqrsqrakp fwsagvkwva kqedflqnvn wlnranlrlt
      841 ygtagrspvg gsnqsiitvt atdpttqqpi atiitpgdqq lgwettktin lgtdisvldn
      901 rlsatfdiyd krsngilanl pynptygwsf lqfntgkmks ngyefsvsgk iadhqdwsin
      961 stfnfsyskn kvtdnryntt lgttiaqggt tldgypvgat fvyrsagldp ttgqtqiydr
     1021 nnniiknttn ltsaftiedl kyvgvkaapy fggfmntfry kslelgvqts fyfghvflkp
     1081 titnyptaas ysgvigkqed layrwrqtgd esftnvpglt gvnnnsiiry rysddlvrsa
     1141 dnirlqqisl nyrvpqsllp knvfkslsvg asarnlgmiw vknkekldpe ylnananyys
     1201 mpptktflfs inasf
//
LOCUS       WP_090787244            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090787244
VERSION     WP_090787244.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122773
     Region          132..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mllrrggivf ifmllgitvr aqklnyvkkn vpllqffkei rkqtgasvvw nekefnidqq
       61 idadfrnvel kkamdklank lhftysmvdk mivvkdqpvv aavaavstvk pkvdnkptaa
      121 eekkevdlpv veivstgyqr ipkervtgsf amvdsaqlnr rvspdifsrl egitsgllfn
      181 kntlnssngn ldisirgrst iyandqpliv ldnfpfngdf nsinpndvan isvlkdaasa
      241 siwgvragng vivittksgk ykqplelsfn snltvsgkpd ifynpnylss kdfidvetfl
      301 fnngkydaal ldqvnfpivs pvveildrqr kgqsatvteq qlnalrgndi rneelkyfyr
      361 spvsqqyyln mskgtdrshh ylsagydrsl sslinnennr itvntqhtvk llknleltag
      421 lyyvrttgkm dstilvtsyq nftpyyrfkd angkatvyng lysagfntqa makgfldwsy
      481 vpldelglsq tnafgndlrl ngalkytlfp glkaevkyly qhirnsseli ggvesyltrn
      541 sinryailqa gqvsgynipl gaiqyetvrk avaknfraql nyekdwkkhs iyaiagyels
      601 efdtqgskyi nygydkrtgs svpidsttvf klnpsgegki stgsdlfgkl drirsayanv
      661 vyaydqkyvv sasarmdgsn yfgvktnqks lplgsagalw hldresfyqm nwlpvlklrv
      721 sygfngnldk sntgittfsn nignaistnl piaaivnign pelrwekigi anfgldfgfk
      781 dniisgkvdy ffkrgtdmlg dkafpastgi kvlrgnfsem kargldisft srnlngivkw
      841 qtnalfstvh dwvtlydvin tngasyfndm akpllgkpvy giysyrsagl dplngdprgy
      901 lndqvskdyn kiftetslde leyngaarpt vfgglnntis frkftfafsi syklgyyfrk
      961 psvnyysmyh lgavqglnnd ferrwqktgd elltsvpsqa nytegsfrdk fyvnssatva
     1021 kgdhvrlqdi slsfdldssn wknipvkqmq lylyannmgi iwkannfgld pdlvpgigdr
     1081 ltspvpmsfs lgikasf
//
LOCUS       WP_090785770            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090785770
VERSION     WP_090785770.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109447
     Region          24..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkllmlfl gmtllsmqvf aqqitvtgkv tsgadglplp gvsvkvkgks igtttdgqgr
       61 ytietanndv lifsfigtls qelavngakv lnvklaedsq vlrevavtaf gvkqevrslg
      121 fstqnvkaqe ivesqqpniv nalqgkvagv qitnssgaag asanimirgg sslsgnnqpl
      181 fildgipvdn stpvsqgglv asvapasnra idinpediet itvlkgpaaa alygikaasg
      241 aivittkkgs ggaarltyqn nfsfdhinkl pelqsqfkqg eqgaynatal gswgpaftsg
      301 eqiydnlgni fknafaqthd vsvsgsseqt hyytsgsfle qgsivdnstf gkksfrvnad
      361 tkigekltvg gsanyirtdr nylsqgsfng imgalswprn ldmkdylkpd gsqkiinttg
      421 tdnpywtinn kpfvskvnrm ivqgnldynp fsflnftyrl gtdyysetfk svrmpgtlep
      481 nvirgainqs vannqittst ailtgkktig sdfnfslsig nnievsalqt ttstalnfld
      541 ptfasinnsk ptdrtvsesl lrrrifswfg dfnmdwkgia yvnfkgrndw sstlpvkdqs
      601 ffypsvstav iitdllkelg aksddqvfsy gkiraaysnv gkdaaaykln tslstltndf
      661 tinprgfiin snnafgnpll vpeftrafea gaevrfiknr igidftyyfs ksdnqildlr
      721 tppssgsfla tlnggsirnk gieiilngkp ivgkdfkwsi dvnfahntsv vkelpakidr
      781 ielsdawaan nvaqgaaflg gslfgingtv wkrnaqgqll ltnagypqva valanigdrn
      841 pdftmgitns fsykdfmfsf midirsggkv fnatenalvr sglslktldr gtkvfdgvie
      901 stgvqntiav plnqnyyqti ysnqgydfve dgswtrlrya tlvyhmptqy lgklkikgls
      961 ftatgrnlfl itnysgvdpe vsgsgagvgg tgsfgfdnlg vpatrgfdlg lkltl
//
LOCUS       WP_090787493            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090787493
VERSION     WP_090787493.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116601
     Region          23..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkliqslfi fvflagaama qdrtitgtvt gkddglpvpg vsvkvigtti gtstdangky
       61 alkiasgsas lefssigyvq qvvaigssnv vnvimstdsr qlgevvvtal gikrevralg
      121 ysaqsvkgdd ltktdqgdvl kslsgkvagv qitsssgtpg sssyiqlrgs nsltgnnqpl
      181 fvidgspidn sqnysgdpsd eknnllqgas nsnrgadidp ndiesitvlk gpaaaaiygi
      241 daangaivit tkrgkagkiq vdfntgvsfd kvnrypglqn qwvkgsggii apfsstnrys
      301 wgpnvkdvsw dgnsneydvh gnvvlntdpt aktpfvpydn lrnffrtgst fsnsvavsgg
      361 netatyrasi snaysnsivp lqnfqrttvs fagdlkisek lklatsmtyi tsdgnmpqqg
      421 snlsgimlgl trtpisfdns ngatkaddpk aflfsdglqr syrngiydnp ywtinnnpyk
      481 tllnrlmgnl qldynigngf satyrggldt yndnrhqyye iqsgaysggr ifddrftyrs
      541 insdlifsyt kelndkwrfd gkvggnlynr kldelyvqgd glvapgfdni ynastlksan
      601 fvtpyrkggi yydlnlsynn mlfiettgrn dwtstlpkgk nsffypsanv sfvfselegi
      661 kggalslgkf rasiaqvgkd pgpfllnsyy vpttfpdgyt sgisfpsngi gsfgldnvlg
      721 npdlkpekti ayelgaqlqf fnnrlgmdlt vyyskgkdli vqspvpgssg yqfvtlnsgs
      781 irnrglelql tgtpvkntef ewssflnfsm nrskvlslap gvnqitlngf tgtviaqlpg
      841 mpagviygyg ysddgkgnmi iddrdnvgyp ltntnvqkei gnpnpkflmg fgntftykgi
      901 slytlidwkf kgdlwngtrg slaaigtsdl tnnrgtmkqf pgvfghmnen gdlvhfdgag
      961 nevagaggin smsvpldeaw ylgdgggfgn lneafiedas fiklrevals ynfprlfnkd
     1021 gkqfvkglta glfarniiiw tpyhgidpet sltgatssqg mdyfnnpgta syglnlkfkf
//
LOCUS       WP_090803055             380 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Paraburkholderia].
ACCESSION   WP_090803055
VERSION     WP_090803055.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39349
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvaqg hrvtlqsgag agasfpdday tavgaeivda
       61 atafgadlvl kvqsptdsel pllkrgatlv gmldpfnadn agklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavl easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswla
      241 rqsalvhera kqadivista lipgrpaptl lsvetvqamk pgsvlvdlaa grgpevdgrr
      301 ggncpltead qvvvrygvqi vgytnlaamv padasslyar nvldflklii akegtlnidl
      361 addivaatll ardgqvtrna
//
LOCUS       WP_090787750            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter sp.
            ok626].
ACCESSION   WP_090787750
VERSION     WP_090787750.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. ok626
  ORGANISM  Pedobacter sp. ok626
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Pedobacter sp. ok626"
                     /db_xref="taxon:1761882"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121539
     Region          32..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksflykgfc ltalivmilg hsaslyaqqv vtvrgkvtdk kdklgvigas vievdqnkrt
       61 itgvstding nfalrvtntk hqlvvsyigy ktfqagvigd rttinviles nsneldavnv
      121 tskkmvnngt glniaernst iasatisaka laelpvtsid qalagrlsgv dfgtvsgdpg
      181 agmsirirgt ssitgsaepl ivldgmpyet eipsdfnfgt adeqgyaqll niapsdimdi
      241 tvlkdaasta vwgsraangv llintkrgek gkpfiaynfk gtmatqpnpi pfltgnqysm
      301 lipeavmnst glplnflgnd gqnkafqydp sdpyyyynys nntdwlklit rtgythdhnl
      361 smsgggekar yyasvgylgq tgttlgtdls rittkinldy ivssklrfkt dltythvnnn
      421 lnynkslrgt ainkmpnmaa fefdeygnnt giyfsplsni qgqfsindkn evkgtynpla
      481 manegfsqli geritpkfnl qydissvlfs tfdvqfdvnn tksktflpqi atgqpstett
      541 vnrasdadgd synmqtkinl iyrprininh nlqglmsfqt ndtksasysl vtantassql
      601 qdpsnpsvtn gvglalksnq sqsrtvgvll qaqyefldry iinvngrvdg sskfspdnrf
      661 gffpgistrw rlsdepfmkk ltfiddlslr lsygasgkap kdnygyfnny tpfdwsyagr
      721 aavypsniel sslkwetlvg knvgfnltmf ksrvkidaei yrnttknmfy ndlkiasttg
      781 yskidmnigs mnnngweimi nttpfknktw nvgfdfniar nvnsiqtise fypressagl
      841 pdlgkyksfl iegnpfgsyy gfkfkgvytd kdatiakdad gnrivgpngq tvymrynypm
      901 vdyvfqpgda iyedinhdgn idekdmvylg nsvpkftggf gpnitfkgnl klqaffsyry
      961 gydivnkaki tttnmagvnn qstavlrrwr npgdvtdmpr alygtgynwl gsdryvedas
     1021 firlssvtlr ynltsdilkr fkmksgsvyi tgqnlytwtn ytgqnpdvts sgenspfkya
     1081 eddaltppsm tftlgltigf
//
LOCUS       WP_090821832             402 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. yr096].
ACCESSION   WP_090821832
VERSION     WP_090821832.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. yr096
  ORGANISM  Arthrobacter sp. yr096
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Arthrobacter sp. yr096"
                     /db_xref="taxon:1761750"
     Protein         1..402
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40841
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkagiareal dgerrvaatp etvkqltglg ltvevesgag laaghsdddy rqagaslvqs
       61 ldlgmldvyc hvrpmepsta galrpgsvtv glgspsselp tvralaaggi tsfalelvpr
      121 israqsmdal tsqalvagyr cvleaamrlp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandirpas adevasmggt fikldletae asggyarels adrgalqral
      241 ltphvaqadv littaavpgr rapllvsrem vqgmrpgsvv vdlaaesggn vegsipgqdi
      301 piptgdgqgv vtlvgikdpa sampadasrl yaknvanllt lmtrdgvvsp dfddevvagt
      361 clthngevrh aptaealaal agdtalgvap sgrpqpgpeg vr
//
LOCUS       WP_090812552             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia tuberum].
ACCESSION   WP_090812552
VERSION     WP_090812552.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tuberum
  ORGANISM  Paraburkholderia tuberum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Paraburkholderia tuberum"
                     /db_xref="taxon:157910"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39475
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 meigipaeak grqalvaatp etvktlvaqg hgvtveagag erahytdday riagaqigda
       61 aaafgaqivl kvasptadel plmkrgavla gmldpfnten aqrlaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vlvaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf lnvayetdee reaaqgvggy arpmpaswlq
      241 rqaalvhera kqadviitta lipgraaptl isaetvramk agsvivdlaa grgrvlnghr
      301 ggncpltepd kvivtengvq ivgytnlasm vpsdasalya rnlldflkli itkegvlnid
      361 laddivaatl lardgevtrk a
//
LOCUS       WP_090829329             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosovibrio tenuis].
ACCESSION   WP_090829329
VERSION     WP_090829329.1
KEYWORDS    RefSeq.
SOURCE      Nitrosovibrio tenuis
  ORGANISM  Nitrosovibrio tenuis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosovibrio.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosovibrio tenuis"
                     /db_xref="taxon:1233"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39383
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaeir ggetrvaatp etvkkftaqg fhtvlvqsga gagasipdda yqaagativa
       61 naaelygqsq ivlkvrgpdp aelemmrkda vllgllaphr iegieelarh gltafamekl
      121 prisraqsmd vlssqaniag ykavlmaanv yqkffpmlmt aagtvkaarv lvlgagvagl
      181 qaiatakrlg avieafdvrp aakeqveslg akfvevplse eekaqaetag gyaremsddy
      241 krrqgelvhq raaaadviit talipgrpap vlikeetvra mkpgsvivdm aveaggncpl
      301 seldkivvkh gvhlvgianl pglvaadssa lyarnlmnfl nlmldaktge fninredeii
      361 agtlvcadge vvkka
//
LOCUS       WP_090836660             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia hospita].
ACCESSION   WP_090836660
VERSION     WP_090836660.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39647
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligiptetr pyetrvaatp etvrkyvsqg hrvrvqsgag taasyldday aaagaelvda
       61 ptafgaeivl kvqsptdsel pllkrgavlv gmlepfnven asrlaaagit afaleaaprt
      121 traqsldvls sqaniagyka vllaadlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpyetdee reaavgvggy arpmppswla
      241 rqsalvhera kqadivista lipgraaptl isvetvqamk pgtvlvdlaa grgpeyegqr
      301 ggncpltead kvvvkhgvti agytnlasmv asdasalyar nlldfmklti tkegtfnidl
      361 addivaatlv ahdgevtrka
//
LOCUS       WP_090838008            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olleya
            namhaensis].
ACCESSION   WP_090838008
VERSION     WP_090838008.1
KEYWORDS    RefSeq.
SOURCE      Olleya namhaensis
  ORGANISM  Olleya namhaensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Olleya namhaensis"
                     /db_xref="taxon:1144750"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116485
     Region          21..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiylcall lvstfsiaqt titgtvtsae dgqtlpyvni vtsnnsgtit dndgqysiti
       61 ldntetlsfs figyktqqia itnqttinva lmedasslde vvitalgler dtkelgyvvq
      121 slsskgltev kavnfldnla gklagvtisq gatgvgsssk itirgeasfs nnnplfvvdg
      181 vpinnntvfn ftneaaagfq eidfgngamd vnaddieevs vlkgpsaaal ygtrasngvi
      241 viktkdgkks kglgisints vfvdsafrlp efqnsygqgn sgqfeyvdgl gggindnity
      301 swgpqldagn fasqfdspvv lsngtiirgg dtalyngdai tptllksnpd nlkdfyqtgv
      361 ttinniaisn gfdtgdyrls ftdlrsesii pgvnldrqtv aaklnfeptd kttistsisy
      421 tnstsdnrps ngygsenany slvawgprsl dinslknywq pglegvqqys fnytffdnpy
      481 filyentnsf nrdrvfgnva fkhqftdafs lqfrtgmdys sekrelkrsy ssnrfkngay
      541 aehdvffrei ntdfllnynk tfgdfkvdvs aggnrldqka stkqaqtvnl aqpgifslnn
      601 aaspievfqf dskkrinsfy giaklgykdf lylditgrnd wssalatpfs vdgtsffyps
      661 asasfilsnv ttlpkavsfa klrasvaqvg ndtnayqtsg afisqtpyng qptfsnqdfi
      721 pnanlkpest tnyefgadlr flndrirfdf tyynaitkdq iislpipiss gyeqqvvngg
      781 kvkstgieii agitpvktnn fkwnttfnfa knkatieelp qadgrltlay sriydsanqt
      841 vwfqveeggq igdfygtgyl knedgqfiid sdgryiadnt lkklgnynpd ftlgwnndfs
      901 yknwtasflf dwrqggeivs rtsalgnvgg qlaeteyrpe dgivaegvta sgqpntvavs
      961 aesyyrqfyd rnheennvyd asylklrqfs igynfklkeg flgleeggdi aisligrnlf
     1021 vitenphfdp eqlavqgdgf vsgvedmsya ssrsfglkas lnf
//
LOCUS       WP_090841294            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olleya
            namhaensis].
ACCESSION   WP_090841294
VERSION     WP_090841294.1
KEYWORDS    RefSeq.
SOURCE      Olleya namhaensis
  ORGANISM  Olleya namhaensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Olleya namhaensis"
                     /db_xref="taxon:1144750"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116057
     Region          25..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktnlnrilt lflvmvasls yaqertisgt itdenglplp sativvkgts ngstsdfdgn
       61 ysiqasngqv lnfsyvgyds vektigasst isvslqpgnt ldevvvtalg ikrekkslgy
      121 atqevagdev skvkssnfvn slsgkvagld vkssgtlggs tnvvirgnas iagnnqalfv
      181 idgipvdngn snsadqvsgr ggydygnaas dinpddiati nvlkgaaata lygsrasngv
      241 vmittkkgkk rkgigvtlns sytvgsadte tlpvyqkkyg agygqfyddp sgffgytdid
      301 gdgnpdlttp ftedasygaa fdpnldvyqw nsiypqltdt yqqatpwvag andpnsvwks
      361 gatavnsvsl dggndtssfr lgftnmlqeg nlpnseikrn tinfsashdl nekltasttf
      421 tytktngkgr ygtgydannv mqqfrqwfqt nvdvgaleda yfatgdnitw nptsatnlsp
      481 iysdnpywtf yenyetdqrn ryfgnfaldy eindwlsvlg rftfdtysef qeertnvgss
      541 nvssysrfnn nvaeynydfi ltanknitek lniegnlgfn lrrndrssiy aqtngglnlp
      601 glyalsnsvn ainapaeyea vskvdglyar aslgydgfay legtyrrdrs stlpiennty
      661 gyfsvasslv fskfidadwl sfgklsanya evgsdtnnyn vfntygigtp fsgtgiasnp
      721 gsknnlelkp erqenyefgl dtqffnrrlg lnvsyyhttn rdqitsvpvs natgytsvll
      781 nagtmenkgw evqlsatpik tenfswdvnv nwaknkslvv sladgidnlq laspqggisi
      841 natpgqpygt irgtdlvynd agqpivqang yyersgsnei igdinpewta glnnsfnykn
      901 fnlsflidmq kggdvfsldt wygyatglyd itagtndlgn pvrnpvttga dsggvilpgv
      961 qadgsvntvr asasnyanpw gyaraansqh iydagfiklr easitykfdd kilsqvpfta
     1021 asisligrnl wiidkstpya dpeaglssgn iqgyqsgsyp sireigaslk lqf
//
LOCUS       WP_090841299            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olleya
            namhaensis].
ACCESSION   WP_090841299
VERSION     WP_090841299.1
KEYWORDS    RefSeq.
SOURCE      Olleya namhaensis
  ORGANISM  Olleya namhaensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Olleya namhaensis"
                     /db_xref="taxon:1144750"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110491
     Region          25..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lflafvvqit faqdktvsgv vsdengiplt satvlvvgts ngtstdfdgn
       61 ysiktkvgdk lqfsyvgygn kevtvggant inmtlapdna ldevvitgfg skkrdqltsa
      121 vttlsaddit klspstsidn mlqgvapgvq vvagngkpgq tafvrirgvg sinassaply
      181 vidgiiapdl nsvnpgdiet msilkdaata slygsraang vviiktktgn knrdarvsis
      241 srvgygqria dnfemmnaaq kiqyerelsa lgignatalp gaqvstqeey dfliardtdw
      301 edellrnsyi qnnsisidgg tekssyfvsf ahdrntgiiq singferlsg rlnlnvqakd
      361 wlqvstnvsi tgtssdeprd rnnvqnpfra mydynpyetk flldddnnqv ldgagnpifn
      421 ptragfpise alinnpesdn tlfiiggisa ianlsdkwtn tfkvgatnta yrreyflkpg
      481 svldgfvgda dnpgsktdsg sneldltvtn llnysttigd khnvsltglf efnkrtfrny
      541 slssdgfsnd fqsvqavati ptaastnlft rsllgyggfl dydydskyla tasirrdgss
      601 tfginnrygv fwsgslawnl skenfladsd ivdelklras agtsgnsngl asyasvatld
      661 fgslngasta iptdngnsdl gfeknyiwgv gvefagfdrr irgvidyyer ttsdlllnap
      721 lsslggepdg sifsnigemt nkglelelsa diiraedfgd ftltvggnia fldnevtklv
      781 ssstdpngad illttngdnn ivrvgeeiyt yylvryagvn pangeplfyd idgnitnqys
      841 addavvldgk spiakfdgga nlnmtykgfd ftadlyykvg nyiqnylegn mlsngtgvds
      901 nqrvdafnyw knpgdtnvlp splfgneagn tsdrllqkgd yvrlrnltig ytlpskftet
      961 lnisslrlfl qgqnlwtyap hfngdpevgi gsgetdtsvn fgnynlysyp qtqslqmgve
     1021 lkf
//
LOCUS       WP_090846802             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            alkenifer].
ACCESSION   WP_090846802
VERSION     WP_090846802.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus alkenifer
  ORGANISM  Paracoccus alkenifer
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus alkenifer"
                     /db_xref="taxon:65735"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55494
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigalkesf dgearvavtp ssaghlqklg hevhvesgag arsgfsdaay eragvtvhpt
       61 aaallaavdv vakvrppted elaamregqt lisffypgqn selleqargr gvnaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaatslg aqvyafdvrp evaeqiesmg aefvfldftd qvqdgattgg yaapsspefl
      241 akqlekfrel apemdivitt alipgrpapk lwtedmvram kpgsviidla aerggncdlt
      301 vpdekivten gvtvigytdf psrmgaqase lygnnvrhmm adltpakdga lvhdmdddvi
      361 rgatvtrehd itwpppppkv qaiavqkpke kpkeltpeer kaaelaafrq qtrnqvtllv
      421 aggavmalag lfapasflqh fivfvlavfi gfqviwnvah slhtplmait naissivilg
      481 allqigsgsa wvvilaalsv lmtgvnifgg flvtrrmlam fqks
//
LOCUS       WP_090851341             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraliobacillus sp. PM-2].
ACCESSION   WP_090851341
VERSION     WP_090851341.1
KEYWORDS    RefSeq.
SOURCE      Paraliobacillus sp. PM-2
  ORGANISM  Paraliobacillus sp. PM-2
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paraliobacillus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Paraliobacillus sp. PM-2"
                     /db_xref="taxon:1462524"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55557
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkesy tgetrvaaip ktveqlkkfg fdilvevgag eqasftdeqy qkagavhasp
       61 advwqsdiiy kinppsedei akmkegatlv slifprqnee lidrlnqkki nvlamdmvpr
      121 israqsvdvl ssmaniggyr aimeashafg rflngqitaa gkvppakvfv igagvaglaa
      181 igtgrslgai vrafdarsev aeqiesmgge flrvdidedg stdsgyakem seafikaemd
      241 liaeqakevd iiittaliqg kpapklitke mvdsmkpgsv ivdmaaltgg nceytvpdel
      301 vvtesgvkii gytdlpgrmp gqasdmfatn lvnltkllck ekdgnitidf ddvilrnmav
      361 trdgqvtfpp peisvsaapv keeenqpale tnvkepknra gwkygfgiaa mllfgwvgqv
      421 sppeflshft vfflaivvgy yviwkvtsal htplmsvsna isgiivvgal lqitsdilav
      481 kiiafigili asinifggfm vthrmlkmfr mdqev
//
LOCUS       WP_090868594             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia diazotrophica].
ACCESSION   WP_090868594
VERSION     WP_090868594.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia diazotrophica
  ORGANISM  Paraburkholderia diazotrophica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia diazotrophica"
                     /db_xref="taxon:667676"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39529
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr pyetrvaatp etvkkyvsqg hrvtvqsgag tgasyldday saagaelvda
       61 ptalgaeivl kvqtptdsel pllkrgavli gmlepfnten ssklaaagit afsleaaprt
      121 traqsldvls sqaniagyka vllaadlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetaee reaaegvggy arpmppswlt
      241 rqsalvhera kqadviista lipgrpaptl lsvetvqamk pgsvlidlaa grgaeyegnr
      301 ggncpltead kvvvkhgvti agytnlasmv asdasalyar nlldfmkliv tkegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_090870140             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia diazotrophica].
ACCESSION   WP_090870140
VERSION     WP_090870140.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia diazotrophica
  ORGANISM  Paraburkholderia diazotrophica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia diazotrophica"
                     /db_xref="taxon:667676"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39327
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaetr aneirvaatp etvkkyvaqg htvtiqagag agasfpdeay aavgaqiada
       61 atafgadlvl kvqsptvsel pfmkrgavli gmlepfnaen ssklaaagit afsleaaprt
      121 traqsldvls sqaniagyka vllaadlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetaee reaaegvggy arpmppswlt
      241 rqsalvhera kqadviista lipgrpaptl lsvetvqamk pgsvlidlaa grgaeyegnr
      301 ggncpltead kvvvkhgvti agytnlasmv asdasalyar nlldfmkliv tkegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_090874291             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bauldia
            litoralis].
ACCESSION   WP_090874291
VERSION     WP_090874291.1
KEYWORDS    RefSeq.
SOURCE      Bauldia litoralis
  ORGANISM  Bauldia litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Kaistiaceae; Bauldia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Bauldia litoralis"
                     /db_xref="taxon:665467"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39503
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavptetd kteprvaatp etvkkfialg aevtvqagag agsritdady egagatiakt
       61 appmlkaadi vlkvrrpsat evknlvsgai lvgaldpfgn dedvkalaes gidaftmefm
      121 pritraqsmd vlssqanlag yqsiidaasn fgrafpmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfiavedde frqaetsggy akemskeyqa
      241 kqadliaahi akqdvvvtta lipgrpapkl vskamvaamk pgsvlvdlav erggnvegak
      301 pgevvdvdgv kivgylnvag riaasasaly arnlyafvet midkekkala idwddelika
      361 tnltrdgkvv hpafaekgge
//
LOCUS       WP_090877289             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosovibrio sp. Nv6].
ACCESSION   WP_090877289
VERSION     WP_090877289.1
KEYWORDS    RefSeq.
SOURCE      Nitrosovibrio sp. Nv6
  ORGANISM  Nitrosovibrio sp. Nv6
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosovibrio.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosovibrio sp. Nv6"
                     /db_xref="taxon:1855340"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39148
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaeir ggetrvaatp etvkkftang lnvvlvqaga gagasipdea yqaagasiva
       61 naaelygqsq ivlkvrgpes gelalmrkda vllgllsphq aegiealarh gltafsmekl
      121 prisraqsmd vlssqaniag ykavlmaanv yqkffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avieafdvrp aakeqveslg akfvevplse eekaqaetag gyaremsddy
      241 krrqgelvhq raaaadiiit talipgrpap vlikeetvqa mkpgsvivdm aveaggncpl
      301 seldkivvkh gvhlvgianl pglvaadssa lyarnlmnfl nlmldaksge fkvnredeii
      361 agtlvcadge iirka
//
LOCUS       WP_090879451            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090879451
VERSION     WP_090879451.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114877
     Region          23..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfv lvfvafhama qdrtisgtvt stedniplpg vsvkavgsqa vavtggdgry
       61 slrisssvta iqfsyigfvt ktvnvtssnt lnvglasdsk slgdvvvvay gtqkkesitg
      121 svssisskdl ekrtvtnlta alqgsapgis vgasngqpga saairirgfg slssssspli
      181 vldgavydgs igdinqndie sisvlkdass salygargan gviivttkkg rggdptinvn
      241 fsqgwstrgi peydrldayq yypavwqgik nnfmftattk ltdaaasara sqdvgtnliy
      301 npfnvpanqv vgldgmlnpn asllyddfdw yggmertgkr tdanvstags tdksdylisl
      361 gylndqgfil ksdfrrfnar vnvntklkpw lrtglnlsgt msdasvasda stgngasfvn
      421 afsfargigp iypvhafdat gnpimnpitg eqwydygihp gainrpsgas pgrhviyetm
      481 lndnafrrsl isarsfvevk flkdftftpn ismdlrnnnt evfwnplvgd gagtngyksq
      541 ttntirsytf nqlltynkti glhnfsalvg henysynfrt fsadrnnlia rgntefpnfv
      601 tslsstgrad ndriesylsk fsysyndkyf vdaslrrdgs srfspnrrwg tffsvggswa
      661 ikkenflkes swiddlrlkv sygqvgnnai lesdgsaryy gdraffdlgl nsnveggvll
      721 atvatpdltw ekqntlntgv sfsffgkrly gelefynknv ddlilnipqp lssavttvvr
      781 ntgsmynrgv elqlgaeilr skdfnwnivt nwsvfknqit klpaetpqii sgtkrreagh
      841 siydywlrqy agvdptdgaa lyipaegtaa tsirtvngvq yvttqanakf dysgsaipdl
      901 lgsvnntfsy kdwslsflin yqiggkaydg vyqglmstgs ygsalhkdil sswtpsntta
      961 sipradygns vninatssrw lvdasywnir nvnlaytlpq sflskidvkn arlfvtaenl
     1021 ylhskrkgln psesfdgvna ntypqgrais vgvnlsl
//
LOCUS       WP_090879774            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090879774
VERSION     WP_090879774.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113118
     Region          34..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikiftkrnv pkrvlmlcfc lylgfsayaq tpavrgvvkd aketivgatv vaqnvqtgvk
       61 tttssdkngv ftfaklvaga ykftisfmgy egktvtgevk dggtfslsvv lkesstsldk
      121 evvvtgtgin rrkdsftgtt avfsgeelka ignnniiqsl rtvdpsflvm envtagsnpn
      181 vlpiievrgk ssipsatlkd qfgqdpnqpl fildgfpttl qnivdldmnr vasvtilkda
      241 astalygaqa sngvivieti kpkpgelrfs ytqdfgfemp dlsgynmmna tekleferls
      301 gryraeesnp tqgvyldtly nkhlasvmrg vnsywlsepi qngystnnsi nasggddsft
      361 ynlgmnyktg kgamkgsgrd sysgsinlty rktnlninni tyirgnsstn spygsfssfv
      421 nanpyyekny dqrylevsrr sngtallvan plfdamqpqy nkasgsefqn nlnvnydvtn
      481 tlringglqv tkgttvrkvy rspemsdfin tptlrkgtys dyraenfsyq gnlmlvyhtv
      541 lagkhvinan wrntvsqekn asyqsiaegf pagnlgnpif aygyqengsp sagsrvyrtl
      601 nttisanygy dnryladavy rldgstaygs nkqfspyyaf glgwnihnes fvkgtawins
      661 lrltgnigit gnqnygntss vsvydyntsa nynqfgqgvt lstlgnpnla pqktrqists
      721 idfslfnnrl tgyinaydkk tdplivpvdl psstgvvafp ynigsltyqg leakltffpi
      781 ynleeritwn igitgssyks kyggfgnvls tlnkqqennk tllryidgns aeaiwaiksm
      841 gidpatgrev fltkngdytf dyatgnitnv gntvsvvegv fstnlrikrf sfgagfrykl
      901 ggdvfnsalf nkvenitlsg talnqdkral ydrwknpgdi aqfkgisqtd vtpissrfvq
      961 teysftseti nfgynfdnaa wlksygltnl sfnlitndll ylstvrrerg tdypfartia
     1021 fslkasf
//
LOCUS       WP_090880755             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090880755
VERSION     WP_090880755.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109309
     Region          31..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhstkqkllk sllclgiics vspvfaqesp vkglvrdvsg qplpgvtvka enentrktav
       61 ttssskglfs fnglamggpy rfiftsigyq adtlsgytlt agqqvalnik lkeqsnalqe
      121 vtigygkskr nqitgsvtsi kqdefnrgvv sspgqllqgk vaglnitrsg npndkpavil
      181 rgpssfrega qepfyvidgv pgasidlvap ddivsmevlk dasstaiygs raangvimiv
      241 trnagkglgk lsysayaase sisnsiqmat gdqlrtylkd ngkvldkvsd ngsntnwlde
      301 vtrtgfshnh nlnfngggen ssygaslnyl dnqgiiktsg lerfiaranm eqrlfdnrlk
      361 lninltnsnt tndriapqvy nnmftylptv gvynadgtfy edptrttgtg gyynpvalle
      421 nntyqgktnl ylingsakvn ilngldfnam vsmqseqine nlynnrysml kqgfngyaer
      481 ssikntqkvf egyfnydknf gdhglkllag yswqenrngd gfqtsgqnfv sddllwnnig
      541 lsngngstvv nygsiyistl rlisfygrai ydykgkyllq atirrdgssa fgvnnrwgmf
      601 psvsagwnid resfmsnvsf vdnlklragy gvsgnsvgfd aytarlvyga qsgsyfysng
      661 kwltaigpiq ndnpnlkwer tatvnigldf slfknklsgt ldfynkkttd liapyqvstt
      721 qypfnvltan vgemtnkgie lslnttpvkt nnfswntain lshnkneits isndlfqane
      781 fytanvggrg qsgalgyqvi keglplgtfy tlryagkdan gkstfydkng vastantgfe
      841 hftvtgsaqp kllygwnntf rykqfdfnff irgvygnkil natiadmnap iyafqtniaa
      901 qtltesindd kaqfvsdryl esgsylrldn atlgytfkik gtktlrvyas gnnlfiitky
      961 kgvdpeinma gqtpgidyrn fypktrsaif glnfnl
//
LOCUS       WP_090881349            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090881349
VERSION     WP_090881349.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118025
     Region          28..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnliflrkis lsllltmlac tmlfaqdrkv tgkvvdqsdg qgipgvnvsl kgvpsnvstn
       61 sdgvftiqvk sntdvlvfsy igytrqqitv gtqtnitvrm ksenkdledv vvvgygtqkr
      121 thltgsvvdi katevedlqa snigaalagk ilgvgvsggi srpgstaklt irnpntifsk
      181 dggstdplyv iddviqinpa ngqpdatlfn nldpseiesl sflkdasaai ygtragngvv
      241 lvktkrgkvg pprisysgay avndeayrtk mlsayqfgmy ynimngpnga nvtpgtvaae
      301 daffsqdeld hfrninydwl edawhsaynm khtlsvsggs dkatyfgdia yfkqngnlss
      361 ldfkrwnfrt gvdvkvatnl kvglqlsgnn gelvktfnki gselddndyr nlilapryvp
      421 tyinglpvkl pgttndfsty hfyeieklgn lattksntft inlnaqydvp fikgltaraa
      481 ysrnngssng sqigtrysiy nftrlgankh iydgatnpva itasngnrly ysntnqsstq
      541 snfvlnynrt fgkhtisgla tverseqayn gevvfradpi qqtngqfnsa tgaidgsttr
      601 seggslsyva ranyayadky laefmfrsda stkfapgnyw gkfysgslgw visqedffkv
      661 egidylklry sigllgndqt kawlwrqryt fqdgkgavfn gdsgatggyk measpnpdat
      721 wsdelknnig idakflknrl svnvdgyfnh atnilteits nipvtvggsv asqnfgiany
      781 fgyeigvgwn drigndftyg vdlrfawqdn kviradfnan dvlypwnprn gvssdigkwg
      841 ydylgmfknq adidayvsqy kitsvnpgng tailakdlkp gmlyyrdvrg plqpdgtfag
      901 pdgiidnndq vqlakkatnh ygfgttlkag ykgvsveavi sgsfggwaei darkkmnnsi
      961 srtfasvpei wgdiydpvln ptgtmpnpnw estsltpasn fwkvsgfrmr mtsfqvnysl
     1021 pksllekvkv snvrvyatal npvnfynpys yrdsdtaydi fpnlrtfsfg lnvtf
//
LOCUS       WP_090881934            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090881934
VERSION     WP_090881934.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120052
     Region          116..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnksypyyll lpvvfllfth lqgfaqiksp ektrvvlrik ekslaevlsd iekqsgysfn
       61 ydqneinsnq kvntnsnsnl kavldglsne lglefaisgr fisvrkapkk kalpartitg
      121 vvkdsdsgip ipgvnivlkg sgkgattnad gafiykinae nidktvlvfs yvgmkpkevv
      181 vgkqvfinvn lendalamge vvvtgsytre krreevvgsi aqvsaerlqt qrpiesfdkm
      241 leglvagvqv etttelntpv kinirgqgsl pnlsssartt ssqplfvvdg lplyeqqrgn
      301 essvfnteky lnplsninpa diktitilkd atasalygan aangviiitt ksgtagntrf
      361 nfnydtgvas finqykwlsg pqyysllrea yindgrsate atqlagsktn nvdwfdltnr
      421 natyhnfdfq adggsekttf lfssgyrnqq assygndlqk iyfrlradhq asdklkigfs
      481 anatytkqns lsnygavtlp pniapynadg tfakflgvpn plavleqndd yskgldfqai
      541 gyagyqltke isidgrlgan syqtkqttfe salnasgenv ngrlriydrn rigyigfika
      601 sydktfakkh kigflvgtel qnedisllrg mgsgftfdrr rvldgaaaqs sassnssnat
      661 vsyysqleyn ydkkyylnfn gradkssifg gdkqvalngs agaswiisne pflkdnktit
      721 slkirttfgs tgnsrignys arglynfgtg tgstyagnva syplltgapn pdlgweknlq
      781 lnfgldfslf driqvtaeyy sntindliss vdvpletgfa tisantskmr nsgfelsina
      841 nviksdnfsw nlaynfgsnk ntllaynnga aalygfrdna yafkvgnsss aiygyqwagv
      901 npdtgaemfy gpdgsiktaa einalpinnv qvigerlpdf qgglfnnfsy knfelsfnvl
      961 ysygasqifs padeadgrnl qnrnqsvnlv drwqkpgdit diprlninrt ivsnssryvy
     1021 dvsylklsnv nlayklsdkl sqklhlkrlm vfanatnlfy lyndagtkgr ngiaekrfvy
     1081 pesmaltagv kvtl
//
LOCUS       WP_090881991            1009 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090881991
VERSION     WP_090881991.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1009
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111440
     Region          47..1008
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkinllkmmg lsaavllnsp vfsmsaneer avtlktpisl rlaqakkpit gkvvdetntg
       61 ipgvgiknvt sgkstqtdas gqysieansg diirftyigy daqqitvgqq nsvniklkps
      121 antklddvvv vgygtlkeke itsaiakvds tkfrqsgsrn pldllvgkva glqisrnssn
      181 pndgvgvqlr gvtslsgsas pliiidgipg gnldllqqdd iesfsvlkdg sgaaiygtra
      241 nagviivttk kgkkgparfd ynayvrtetl vkrpdfmnat ewrariasge ykvvdkggdf
      301 dyfqdlinkn nisnnhnlav sggsdnsnyr vsanyrelqg fakengrkey girasltqkg
      361 fqdklqaqfn vstnfnnanl lggggwenvl tknptesyfn pdgsylftrt itnelarleq
      421 erygvqqqtt svdgkidfev lkdlklsaff atqrnnriws eyrdrasqns vengdapngg
      481 yaakttelnq ninfeptiey tktfgkhkis giggysfrre tnegfnannr gylndlfedn
      541 nlgsvpvkvt tigigsfkne ntliavfarl nyslndkyfa qaifrregss kfgannkwan
      601 fpaisggwni tqeefmknvs wvnnlklrvg ygetgnsgmg nsealvtlst ggiylfpsge
      661 ylqtygpnkn pnpdlrwetk qetnigvdft ilnnkltgsi dgykrkiknl idrytspqpp
      721 fvtseittnv gslsskgiel slsyaaiknk dfswsvdfag sttknvldsy snseyrrdmr
      781 tfgsiggfga lgdafrtyeg reigefwgkr fagfspdgkw tffnrnnevv tnaqintsvf
      841 rdqtdfavlg navpkyylsl tnnftykgfd lrvflrskld fdvlntmais ygnkngastn
      901 llnsaftkya dlkdtymytd yylesgsflk ldevtlgytf klktkyirtl rlnvtgqnlv
      961 titgytgndp dyiqdtgygq linnrslgid trspypatrq flfgvnfgf
//
LOCUS       WP_090882776            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090882776
VERSION     WP_090882776.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114854
     Region          31..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfnltmrrg kllgiiiflm mpfvtfaqtr itgtvtdgkn qpipgasvkq kgttngtstd
       61 nkgaftlalk egsttlsisi vgfktkevsa agktnisiel aeddnsldev vaigyqniqr
      121 kntagaissv kgkdfentpy stfdamlqgr vagltilsts gepggnnivn irgasnvnlg
      181 qsssplyvid gviydvndig saygssplqa inpndiesvd vlkdasasav ygaraangvi
      241 ivktkraqvg appqirvasy fgiankpalk piqtgtaerr lkmdllyggn glynslrdln
      301 mmltdslnta fnnntdwqgl flqtgnisnv dasiagatdk ysyrfsfnry yeegvmkgyd
      361 inritpslff qvsptskllv qtnlfvgltk akhgqgdqnk ypfttwgfps sfwkigtaee
      421 elytgryeel rdddkttsln gntmaqytvl pglnikstis ynifnntrsy fkpsllsssg
      481 qneaygwvnq tnrwelenti nyfkslksgh nfnfvllqgm eknianntys ssvgnadavk
      541 tvagiasgpn lyasntiqqr srlswmgsfv ydykgkylfq avyradassr ysadsrwgsf
      601 psvsagwnas eesffspakn ivsylkfras ygitgndpga yyaqyqslia nanyptsvlg
      661 ngqggaqtty ngtqvlypdy ygaasatsis werspqfnag idlgllkdri tltadyyird
      721 skskvfdvsv plttgyslts nnyvdlrntg ieftlttrnf aptskfqwit nfniayndny
      781 itklpnggrd ftfgppwlqq tlsvgeplft ykvwevngiy srdtdvpvdp ktgrritqfg
      841 gsqfsagdpa rvdqngdyni dyndyvsygn pnpditggmn nsfsykgfsl dvlltfisgr
      901 slrngylsdk lqdagtnnpy vlwgprsgpa snfnvsdfws kpgdiakypg litnnvdkwh
      961 igqsmyieda sflriknirl gytlpekftk kigmrlirfy gvmdnvkvws nstvpdpeav
     1021 gvdgysggnd ypipkkytfg idltf
//
LOCUS       WP_090882655            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090882655
VERSION     WP_090882655.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111489
     Region          38..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknlpqfls fcflvlvilf akssyglsnr pdtiplfkat vldesqaplq rvkiqvqgtk
       61 tsvlteanga faipakindv lllsfddqvf lkykieslsv naiivssqnp vvkqhrmvkm
      121 mfgievpanr tpasvdvvyn adltkmpvts vanaltgrls glytlqssgq pgadgaslsl
      181 rgrtpavfid gvprgfsivn ldeiesvtvl kdalasgqlg gkgfngavli ntrrgtnakq
      241 sisftaqtaf qqslkyaqpl dafnyaslyn ealtnnglat vytqadltay qnqsdpyghp
      301 nvnwvdqvlk entrldqyni nfrggnewgr yfvsmqhlnq tgflqtspen nydtnnkfks
      361 yvvrsnvdvn itkslsagin llgrilnsnd pgyinpggnv vnaqgifsav intprnaypv
      421 fnpngsygts pnfqtnlygq svnsgyvany krdvladlfv krtldeitkg lwvraavals
      481 stisennnrt ksfasfyynp ttktytqygn ngiqgnsnfi nyqgradyle lklgydrsfg
      541 ksdvssvlfa nrdnivsgsd lpytlkglag rtqytynnty taelayavng snyyppsgdn
      601 kygfypsagl swtvsnekff pknsfvndlr ifssygvngn dnpgyftyiq ryfdgpavyf
      661 gssagsntsi feqplartnl tfekankfnl glqtglfqnk lglkveyynn kfydllmqrg
      721 knstiigqty pdenigqyry tgldfnlnwq qaiskqasyf ivlsgglqns evvyidevnq
      781 pypwmrktge mvgqtfgyla eglfqnqtei nnsaklvgyt aqpgdiryrd lngdniinqf
      841 dqtaigqnkp llfmglslgf qfksfdfsal iqgvanrkiy lsgntewafq nnglgqaweh
      901 sldrwtpata asatyprltv gtninneats tfwmksgdyl rlknieigys lpksllnrik
      961 lstirvfasg tnlltfsayd rvdpevyngt yplqrllnvg vnikf
//
LOCUS       WP_090882812            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090882812
VERSION     WP_090882812.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109360
     Region          26..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiklkitfm tmvifcflrv haqtetvtgk vkdesgnavp gisvkvkgts vgastnasgs
       61 ftiktgnpsi lvftgigyqs keviyngqsn lsvsltedqq nlseivvtal gvkrekrnlt
      121 yssqevkgeq ltqskepnlv nalagkvsgv qitsssgtpg sssrivirga nslygnneal
      181 mvidgipvnn detgnlnsgp gtnriadldp niiesinvlk ggaatalygs dgakgviiit
      241 tkagalnkkp tlsfsssfsf ekpllpeiqn kyslgsngvy fdgvsqktst swgarmdtlk
      301 ingqpaqvyd qsdlffktgk tytntigltg ggayssyfls ftnltqdgtv patsfdrntv
      361 fgkfstqvik dlnitfslny antknnrqpe gyalespvwt ifsapvsynl qpstnpdgtq
      421 rlfrfsrnnp ywvldnikns sivnrfiptf nadykifpwl tlterfgadv yveqgkyies
      481 lgsvsnpngr ivnnntnfrq ynndlilnas ktlgdfnida llgnnlisty sqnayanglg
      541 itvpdfnnig sastvkftet syltrkvgfy lqsnidykkf iilsltgryd gtsvlakgns
      601 fypygsaats fifsnffssg lsnvmnfgkl rlsystvgna sigpyslltp yesqtirnia
      661 fpyqgqsgfl isgtlsdpnl knerinefev gletgffknr lslevtyfnk kttngiipnv
      721 alapstgyna tsvnsasmrn kgieillnak piktdnfswd ltfnysrvrn kvlsiykdln
      781 qvgngftfif lnqpygviyg tryarnasgq iltgddglpf aadeqgiigd inpdymagiv
      841 nnfkykqftf sfafdlkkgg diqnnvdgyg yfygtpkvte drgprvvegi nantglpntv
      901 svsgqayyqr insvlesviq dgtylklrnv slgysfkpsw ltktpfknva lnvtgrnlwi
      961 yaphftggdp evssfgssng sqgiysfstp tsrsvdftlk ltl
//
LOCUS       WP_090882921            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090882921
VERSION     WP_090882921.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116225
     Region          25..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyfysivil lifglhnias aqqqiavsga vydgeskkke tmpgvsilsn gkvlgqtdgd
       61 grfrvtvpsn aeltfkylsy vtqtikvngr anisitlqgd nttlkevtvt agyqtktrtl
      121 stgstvsisg kdiqgqpasd vmsllqgkva glniqnntga pgfrgsitlr gisninvsgs
      181 gsssfltpts plfvidgvpv ddntnysygf qqagpgvspi sqippedied ittlkdaaat
      241 alygsrgayg vilittkrgn skvpvvryng aaffsmvpql rtviggkger qlrisqilqn
      301 dstynhaidl insspllads lnayfnnstd wqsyfyrntf nqthnvsvsg gdmafnykvg
      361 lgaydetgiq entgysrynl nmnmqynptp kfklvgqlqn siqkqqtgsg ngllnsglas
      421 tgsastllps pslysaqsgl laqlqtdndn ktlqtfatin aeyeifknfr vatflnytns
      481 sntkdnfspa alngnqskyy tyndratkly nrsqfsyvyg lqdaagedsh tfnlfaftei
      541 nssffkadai lnekgvndql rgpltnmtdy ltslggtidy ndarsvafag afsynyrqry
      601 vldlnyrlda nsanganary ianpsvalkw nfnkekfmes ikwidyadir lsygsniqpv
      661 ggifdaygky vggsrynnan siildlqrlp nldlqptkat tynagfdfsl fqnrfsfvfd
      721 tyykqndnif rykdissans fgtvasneis nvnygwefqt tarplnpnsq fkwtisanla
      781 inreilaqlp dglrdliyyd kdlgqdtyyr lgtnslsnyl fntkgvystn aqvpvdpntg
      841 lpyrvggngy lnyfragdpi ftdvdgnyvl dandrviagn sqpqvtggit sylqwknwsl
      901 evntsftlvr dilnnplanq lrnyyspygs lgslvpldql nywrangdva ayanpldflr
      961 sriidpfrln qtafqedgsy fklnsvkvyy ifdkkftskf gmnrvsinat aanlgfitry
     1021 tgpnpenvts lgrddsggyp sprqftlgln ief
//
LOCUS       WP_090882971            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090882971
VERSION     WP_090882971.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117145
     Region          55..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myravwifsv lsllgggsvw aqltlrgkvv ssddgkaitg atvsvggvvt vsgadgafrl
       61 vlagqkvvgd svllkasflg yigyqqklvf psagelvvrl fpmdnnlsev tvstgynkva
      121 reratgsfvq vdnkllerqi stnvidrlrd vvpglvfnrt kglganelsi girgqstlya
      181 ntqplivldn fpydgdisni npndiesitv lkdaaaasiw garsangviv ltskrakknq
      241 pllvagtvnf tvgeqpdltr nnamsssdfi dverllfdrg fysgtessvv kmpltpavel
      301 fiaardgkls sgelssrlda lkgidvrkey msamgnssff rqyalnvsgs sgpgsyylsa
      361 gydenrlsdk mnsnqrmtln fsdrftflsd rltvelnaim arsvakrpnd gygslrmsvt
      421 qliypyaqla dgagqslavt rdfrsgfldg laggpyldwr yrpvdeiylr enssetldyr
      481 ingtaryrll eglsleasfq fgklatdisd ldplegyaar dlinrftqvs stgsvtypvp
      541 lggildkgkt alrtlnfrgq lnyqkslagf efnglagyew rdlegsgyqt rfygynplna
      601 asttvdyvnp ypqsyftsvt gvipsvdals gtadrflsfy gnaslaylgk ytlsgsvrmd
      661 rsnlfgvsan qkgvplwsvg glwniaregf ydvpllpvlr arltfgyngn idknlsaltt
      721 aryfnglttl trlpyavvln ppnpelrwer vrtvnagldf gfrgnrvsgt lelyhktgld
      781 lisdipfaps sgvttfrgnm antvvkgidf nvstlnikge lewssnfwls ytrervtrfl
      841 anslsraqny aqsadagtlp regyplygmy syryaglddk gnpmgylggv astdyaaifa
      901 aadldniiys gsakpvlfgs lmntlrfkgi slsaniayra gyyfrrssvn yvsvlaaqgg
      961 hsdfaqrwkv pgdealtdip gipltasanr dnmylqseal vergdhirlq dvrlsfdipq
     1021 kyrlgfrsvq lnmyaanlgi iwrankkgid pdyqaiplpr siafglklnf
//
LOCUS       WP_090883620            1145 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090883620
VERSION     WP_090883620.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1145
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123360
     Region          25..1142
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiymrclg llllhlfaia ayaqktitgt vressgpipg vsvtikgttr atqtdgdgkf
       61 sivasegnil vfksvgytpk eiavsssstv nifleqssnt ldevlvttal gvkrekrslg
      121 yatqtvtgdn ltiaqaptia qgligkvagl sitqasggve ggssrvvirg ntsltgdnra
      181 liivdgvaln ndplnnngnn saggavgtaq gadvatyndw gtglnfinpd dienitvlkg
      241 paaaalygar gangvilvtr kkgekrnglg idysystrqt kayqfldfqn dygsglvgsl
      301 wtadqnkqfp tntsgqryqi gtytgsyaag dyktgaygml pynnstqawd lfsfpsglsw
      361 gprfdnqpvl wydgvlrpys aqpdnwkaff pngsvsqhnv sisgggefgt arfsytrddn
      421 kanilnskfs tntfnigssi kvskkvtaei tgsyinfqrl ntppvgsasy lagfsyaatr
      481 dyrsdveqln nfaadgsqkd vtagsnfpag sppypyysym ansfwnltnn nttltrnqli
      541 ggakviaevt dwltltgqgg idnsndgtei rnypkniqgt tgyygqamar slnrnlsafa
      601 rlhkdnlfge singsltggv esyyrndytv sngtsgdfvk pfifsldngk nppvtpneir
      661 ygkkinsafg fldlsynnyl flqftgrndw ssalanefns yfypsanlsy vftegikgmq
      721 tatpwlsfgk ltfsyaetgs dtdpysifnl intaayngqa aqtypstlkf dgikpkrtrs
      781 yelglnlgfl knrinvelta ysmksynqil dtplpvssgf ntiqinsgsl gnkgfefivn
      841 atpvsskdfs wnisvngsta stkvlslsdg vnelqlgtff ggngisqkvr vgdnygtiyg
      901 kdftylngqk vvkdavgann qvmtytvngk tytagtqwvl tptevpigns qpkllggvsn
      961 tfryksfsly alvdakiggd tffgtygaam gnglleetvk ernggglplv ypdgttantg
     1021 isfggvyang tpntnvvnpa wyylgtyssw nhlgvprsas vlkntwvklr evaltyqvpp
     1081 nviqktkfiq nlslslvgrd lfyiytsipk glnpegvngi gnmqgiefss iprvrsigfs
     1141 iktsl
//
LOCUS       WP_090883626            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090883626
VERSION     WP_090883626.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119548
     Region          25..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkmyvkcls llllsiftia ayaqktitgt vkdasgplpg vsvsvkgtak vtqtdgngkf
       61 sisvnpnevl vftaigytkq elnvgsqsai svvlkesanq ldevnvvtta lgikrqeksl
      121 gyavstvtak qlteagntnf asalygkaag vkittapgga ssavnvqirg insinynqqp
      181 lyvvdgvmir ndgqngaaga nnndywgdqr irgngildin padiesltvl kgasasalyg
      241 sdaasgvvvi ttkkgsknrg lgidfnyqgs idrvaflpnf qntygpgydr etnvangate
      301 egwipdaasp sgfrpyfray anfgpkmegq qvrwwdgsir sfspqpnnyr dvyqegytsn
      361 anisisnqte gvnyrfsasr ldykgtqpgn tgskntfnln stvklapkls advvvsyvnt
      421 itknrpyqlg qvlgsfggff sraedmnlmk ekyqtsngyk yatfdqtarp epfifnirat
      481 nlldfywqql knqydenenr llssftlnyd vaknlklrgr vgndytsakt enrqfteipt
      541 alngntstga ytttqgqysv lygdalltys nkigedigis vsggyqgrke tykdlrsnts
      601 qglvtenffs ltnsygilet setrkeqlky aylglmnlsy kdflfaegti rqeyastlpp
      661 gnnqysyysv nggfvfsdlw klpkfwnygk lrasygvvgn appmyeanis ytqnslqtin
      721 gsvpvlvpsr swgnlnlmpe kkyesefgle trflngrlgl dvsyydnkik nqilplevss
      781 tngalgqivn vgevgnrgwe ialnatpvsg kfrwdtrlnf stnkskinsl kdenseipfy
      841 nsdqstakiv aragedlgni yirprktdan gnflinddgy yvmdnsvyvk agnimpkavg
      901 gfsntfsygn faldvtidyr fggkmiapnl kymrgagmle nsmefrdaas ggvaytsngk
      961 tyndgvilqg vnqttglant rvlsaadyyl ttynwgegsl teaeifdnny ikmrevvlsy
     1021 kipasftkkl kitnlrfsli grnlfyihrt lkdldpeapl gnrwwsqgvd vgstaasrnf
     1081 gfslnanf
//
LOCUS       WP_090883956            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090883956
VERSION     WP_090883956.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113564
     Region          25..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklftsiff lcvllsgfss iaqvktvsgk itssddggpl pgasikvkgt stgtstdgng
       61 nfslqvsqpn avlvisligy lpqeipvgsk tvinakligd aqqlqevtvs talgitrqak
      121 slgyaaqtvk sedlnfnhqs nlvnalqgkv agatisstgg gpgqgasirv rgvnsidpti
      181 sgdplyvidg iqidnststa ganpggtdyg srgvtnrasd inpediesin ilkggaatal
      241 yglrgangvv vittkkgkqn gfsvnlsssy gfdqvlispd vqteytqgvl gvytnppggi
      301 gpawgptiae aklldpthpd qlfnnydqaf gtgqqiknsv svtggsdaik ffssvsqlyq
      361 kgmmpytdnk nfsgrlntdf iispkfkasv nmnftnsggy iysadrfges laywsprydv
      421 sdfqnadgsq kfigtnnpiw gaannrfkgd vnrfiggaal syepakwlnf syrlgidtyn
      481 dnrvrtargp mftneamydn elgfygeyns kfrtinstfv atltskltnd itgtlrlgqe
      541 iydkrtkdvg vlgsqlgvfd yfnlanakvl apshslrekr lvgyfgeatf dyknylfltl
      601 tgrnditstl skdnrsffyp saslsyvfsd hfklptainq aklrlsyari gkdateyatf
      661 tgftpntamp pgsagltigs ilgnpglrpe ftntyeagle msflknrlgf dftyyyslsk
      721 dqivrtqiss avgystkfin agdirnrgve lvlngkpivg kdfrwdvnln fsanrnkvls
      781 mpagiteivy gaargygnag vtmkliegqa ygniygsyfn ryygsqaedp ivldknlpll
      841 igangfptis ggkqkllgns qpdyilgmgn tfnyknfsln vlfdarlgfe kynwledfys
      901 afglpdytad rrtfrtfegf langtpntkq vwmgqriapd gvdygegyyr iyyrnvsepf
      961 vtdaswvrlr saslsynlpq kwlpakairn aslsvtgnnl wlwtkyygvd pesssydsgs
     1021 nndgsagfty psartimftl nvgf
//
LOCUS       WP_090884330            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090884330
VERSION     WP_090884330.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120994
     Region          30..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfkrynysff illccllvst ithaqqinyv kgkvidkkdk qpiigasvvi vdkdkrvikg
       61 vstdidgnyt lpvadktyri svsyigykst aavaidkpvi nfqlesadnq meevqivska
      121 kaatgsgmvi dkrdqtsstv tidakeledm qsasidqalq grmagvdita stgdpgapmq
      181 irirgtssin gatdplivld gmpyditips dfdfatsden nygqllniap sdikeisvlk
      241 daaatavwgs raangvlvit tkrgaigppa isynfkgsys kqpspipmld gnqysslile
      301 efynagrqfs ttefakqfqy dkndpynyyn ysnntdwlaa itrvgylqdh nlsisgggek
      361 aryrasvnyf nqngttigtd lnrvsarvnl dytvsdkirf ssdiaythid qnalynplgg
      421 rdrvrdvayn kmpnqslyey deygnqtsnf fspaataqga yavtfnplam asaginhqlg
      481 eritpkfslr yqiqpellft gsflvninnt kiktflpqia tgrpftesvv ntafdqdgds
      541 ftmntsmtla ytpklgskhd lvtflrfdse dsrrtsqyll atntassylt dpsvdsrtnl
      601 snsassaynq trsvgllata qyklldryii nasirgdgns kfgasnrygi fpsvsgrwri
      661 sgepflkrtq kyiddlslra sygksgnvpr ydytffniyq nygfsyldna gvystnmelt
      721 dlkwetvtqs nvgvtlnlfk rlnidfdlyr krttdlfyed lavssyngys tvdmnvgtmd
      781 nqgwefnimg avmkskkfrw dmsfniahne nvirevsply prenrgrvts nnvykvfvqe
      841 nnpfgsfygf kfkgvykdrn stialdengn qivgpngdki ymrfaypsvd yvfqpgdamy
      901 edinhdgnid ykdivylgng npkltggigs aftingnlkl sinfsfrtgy diingtkint
      961 tnmygfnnqs tavlrrwkke gdetdiprai ygggynflgs dryiedgsfl rlrslglkyd
     1021 fgktfmkrig mksvsanviv eniltftkyt gqdpevpirl ngsntvvdns ttppiktvtv
     1081 gltanf
//
LOCUS       WP_090884456            1151 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090884456
VERSION     WP_090884456.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1151)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1151)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1151)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1151
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1151
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127558
     Region          156..1150
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnfsaiavky rdcyvqcthk kllidfmrit sfiilvlais aqmlvassvk gqqmedvrvk
       61 lklnrerlsq alekiekqtp fhfiyrdeei reipllnlge ttttldillt allansnltf
      121 kqidrhiiit kkipvrssql ndanqivnai ttnrdiqisg kvtdekkipi pgasvwvvgt
      181 kistmtgstg nfsinipdsn avleirfvgy ktkrvsarsg ayrfiqmeve qqnldevvin
      241 nglfdrkvgt stgatstfnn aqlkvvtnqn liaglaildp sfiivennnl gsnpnnlpdv
      301 qmrgqtgfpn vgdefanapn lplfildgfe ttlqriydln inliksvtll kdasakaiyg
      361 skagngvvvv etikpeagal rvsysgslnf tapdlssyel tnsaqkiqae iragryisan
      421 pinesaltaq yainqkaale gvdsywlsqp lqngygqrhs vmvdggdqsl rysanmsynn
      481 nigvmkgsnr etisgsvnls yfkekfsfnn iltidrnnan nspygsfaey akmnpywrik
      541 defgrlipty tnfgatvynp lyngelnskd nsrytniven fytewrpsav lrftgrvgin
      601 lqnnssdnyi sanntryasi pinsdlyqqr gqytitngrn sglstdigaa ytlnkgkhqa
      661 ianaiysitq nitningmta vgfpndnldf isagggftag srptgsenta rtmavttavn
      721 yaydnrfltd lsyranassq fgannrwgsf wsaglgwnlh neaflknlkg kvdmlklras
      781 igstgtqnfs ayealtsyry nttqnyngdv gfnlislanp dlrwqkvmdk nigldlgifq
      841 rlslrfdfyi kdtqnllsdq ilplstgfvs ykenigevrn qgyqiganlr vynntasrtf
      901 vnvfvnaahn tnrirkvsss leqlntteda nklnsgtnae eralrqnpst ryvpgqsmst
      961 iwvvpslgid psngkeifvk rdgtqtyvws aadyvagget npymngtfgs nvrykdltvn
     1021 fafafrlggq ayntslvqkv enadfiynvd iraleqrwsv pgqaaiykdi adisptkpts
     1081 rfvqnlseln fssvsiaydf nklkflgpgn ksrisvalnl ndiariatvk tergldypya
     1141 rtvsmsvqan f
//
LOCUS       WP_090884668            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090884668
VERSION     WP_090884668.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113660
     Region          26..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkitlffs lvcfmllsay aqevnikgtv kdkagvgipg vsvkiknaka gvstgadggf
       61 sivapanatl vfsslgytpq evavnkrttf sivlvdepqn lsdvvvigyg tatkrdatga
      121 issvkatqle nenpqslsdv lrgnvpglsv glsssakggg dflvrgkstl sagssplivl
      181 dgviyngqla dinpndietv dvlkdassla vygakaatgv iavttkkgkg deplitintn
      241 agfaelaknm rsyegegfla wrgdvlrsga ttpeylyndp rnlpagvtln qwlngqtgdp
      301 vdlwlnrlgl vanekanyla gktepwyddi frkgfrqdht lslsgrkqei nyymslgyqk
      361 nqnlieggdy tairarinle gqvaksvtlg mnfqfadrde artgdgslea nwnqlinlsp
      421 ygdrylpnge lrriptddsg lnarnpflnm tynermnkqn tifgsvygkv klpygfsyqi
      481 nfspgldfyr tfdyrssrnp dvvtpggsat rsnetrynwq idnlikwnkt fanihnfdlt
      541 llanaekyqt wwtqagnegf vpgdvlsyhn lssgikpttn sedkvytgda llarltysll
      601 qryyltltvr rdgysvfgln skratfpsaa lawvftdekf fknqkwlnyg klrlsygvng
      661 nrdlrnpdng tvdpyaalaq lasgkyqtvt pggtasdvnt vqigskmans nlkweettal
      721 nigldfslfn dringsieaf tkktsdllvr qtlpnvsgys tvysnlarin nkggefnvtt
      781 knlieghikw stnfnisfnr nkiialalpt ndpgngwfig kdidviwdyk vngvwqveem
      841 aeaakftkaa ikagdfkled vngdyaysdd dkqflgyktp ryflamrnef nifknfdfsf
      901 qllsnwgqmk qynqaknqpg svgfarsnsy vlpywtpsnp indyarlnsg ssgtsfnvyw
      961 dnsfirlntv alsysvpvnl ltkirvksak iyanvtnagy yapswtfwdp qndgptpryy
     1021 tlglnvtl
//
LOCUS       WP_090884790            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090884790
VERSION     WP_090884790.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113065
     Region          24..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklvlslfl flywglslth aqsknitgkv iadndglpip gvsvlikgtk katvtgadgk
       61 ftisaspgdi lqlsyigfit qdvpvgnqav lnvklitdaq tlsevtvtta lgikrkpkei
      121 gyatqqvtgk altssrptnl atglsgkvag lqisqannqi dagdqvrvvl rgnrsfqgnn
      181 qallvldgii vplnqlnsin pndiesvnil kganaaalyg sdaangvmiv stkrgsadgg
      241 svsytnstlm nrlsyfpkmq tefgggttqd dfgfgqytpf enqtfgdrfd gslrpvgril
      301 qdgtyqmvpy tykdgekesf fetgideqnd isysggneng ttyinvqrvn skgyvpgdks
      361 nrtafringt rkigkflady sfnytqrnyd kstnqvynnv intpgniplt eysdldskyg
      421 npndfyndyy ispyfglkqy rnkerrddll gnlsltykpv dwlslmargg lstknsqgkd
      481 fnyaytysdf ahdsgkgvaa tqynrssvrd ynefesrytg dflatatktf nqfkftligg
      541 aqviqknyky itaqgnnlvv dnlfnlsnrt geivgseler nsrqlavfgd ltatyndflt
      601 vhvsgrnewd srlnsnnrvf fypavdiaat ltdvipalke skvisnlklr ggiskvsavq
      661 vdpyklisti npasgfpygn tagytvdnqi ndpnlkpent lskelgfdig flnnritlet
      721 svylqntknq qivngidlsa stgfttavin tgesenkgfe fslnaapvig lsngfrwnvg
      781 inysyntnkv lglygdlsql glgdnnyvvl gqsfpslqvs tyqtdpqgrv ivdantglpi
      841 aspinkdfgq tnpnhilgvn tsftfknftl sgvaeyrsgn vfysgmastl dfsgisytsa
      901 qagrerfiyp nsviqtspgv fvpntnvtti qgngsfwsdg irtntasnyv ssaafwkire
      961 lslayqvpaq wlgahasfik nasialvgrn lfmfrpsdni ytdpeinvgt gnaqgvnnln
     1021 qtpptriygf tatigf
//
LOCUS       WP_090884727            1193 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090884727
VERSION     WP_090884727.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1193)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1193)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1193)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1193
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1193
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130914
     Region          130..1192
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktrllmway lpdplfrkii kmmkltclll lagllhvsaa vfpqgkkisl nlkktnletv
       61 ikhieaktgy sflysnnnfp snklvdiyvs dkpvskildi ilkhsgftyk linenlitft
      121 kiemeavvpi rgkvvdeqgl plagasikns egkilaqtdv dglffisdig nnssiavsyi
      181 gyvdqsvaig nantlvqvvl kqqsealktv svvstgiqtl skersagsfa kpdmkvfaar
      241 tgsmniiqrl dglipgltin napgatqvlv rglstinaar gplyvvdgfp isdvstinpn
      301 dveditvlkd ataasvwgar asngvivitt kkgrsgglei eydgfanfrg mpdlayantl
      361 nsaqfiqsar eifnpglnpl ssvvpngsqs pvlppheqil ynlnsgains avadaqlnal
      421 antnnldqmr evwyrnamls nhtlslrggg drykiyssla ytnnqsiyqg eknnaykinv
      481 rqdmdfnkvf saylitdltn nirssgnnfa pdsrflpyvl fkdqsgnslp lswlnmadav
      541 rktfetqsqv slsynpvdef dlrnsknedl inrivagiti kpikglkfeg vygyykansk
      601 nstftdqnsy avrselaaft vapatagglp tyylpttggs lstsnqsqrn wnirnqisyd
      661 knwdnqkhkl tvlagqeiqn qlgisnnsyv rgynpdllty gaidyktlgn giantvypns
      721 gsrsvlfdns ygageqenrv vsyyanagyt fnnkytingn wrldqsslfg kdksaqdrpv
      781 gsgglswyas redflkninw lnrlifrgty gitglsptig taasydivia esnsifpdgk
      841 gvrigtpanr rlswestktl nlgadftifn ringsidvyr kntdhligyl pvnpftgyts
      901 itgnmgeian ngielslssq nfstdkfswt tllnvaynrn kikslstavp istgngliaq
      961 sylegysafs vfayqyagld qlgdpqvfra dgsvtkaina ttpsdilykg tfqpvwsggl
     1021 tnvfsfqnfr lsaniiynlg hvmrrdvttl fsggrllsne naefanrwrn pgdemitnip
     1081 ayiaaigtsn sqrnvnyykm adinvldasf vklrdvtlsy elpkewiaki hlkgislraq
     1141 lsnvmlwkan nfgidpefqd asgqasnigs tsggyrtmpf nqntisigah vnf
//
LOCUS       WP_090885492            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090885492
VERSION     WP_090885492.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111204
     Region          37..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meksypnwsp kflailmipf llllfsemaq aqnkrytisg kvtdasgnaa ipgavvkiln
       61 ttlvtstssa gnytfavdla pgkyqiqfsy vgyksvtqsv dlgtgntvql naslsgdavg
      121 ldevivtgts qgttrkqlgs yvstvkgddl nkapsgnala slqgktpgaq isqnsgdpag
      181 gisvrlrgis svnssseply iidgvivnns ttrvtntsgn ydggnfvgsi gqnrmvdinp
      241 adidhievln gaaaaaiygs ranagviqif tkrgktgepq vsfntslvis elrkqievnq
      301 apikfggsvd aqtqdiltpt ltnttpvtry nyqdyifrtg igtdnsvsvs ggndntkfyt
      361 sagyfsnqgi ikntdfrrmn franldqkin nwvrmtagfn yvhsdanekp dgnsffspmn
      421 svtiignfhd lftrdvlgnl kavgergrvn pvsviedikq rqfvnrvian aglklnpvkn
      481 ltvdysmgvd nsiqngttyi ppfaynvstg ffgggptldp slngyastan atttlfnnel
      541 nltydaklsn llssttqlgg syqyqkdlfs llngrglapf tqvvnsasti lvnndsrsef
      601 sisgaylqqn fkykdhlfvt galrvdqstv fgednrtqyy lkgnvsyvls sadywkklgi
      661 sswwnsfklr aaygesgnlt giqpydrfnv yspgslnsrt slvssgilan tsvkperqke
      721 levgtdmsff nnrlgvtfsw ynknvsdlll pvvvapstgf sslldniggt lrnrgvelml
      781 tgvpvkttdf swtttliynr nrnkvigsga rrtlatnaga pvsiidgypa gvfwgsyfar
      841 nddgtlltna lgiplaeapr vngvpsgtpv qkvigdpnpd ytgslvndft ykklslhiql
      901 davqggdvwn adwrtrqgvg ngkiteaedl gqlprgyvag vynieewrid dgsfvklrei
      961 slsynigkvk fvkdltvnls grnliswdny kgydpelnsg gqstllrnid fgsvpiprtf
     1021 siglkatf
//
LOCUS       WP_090885534             948 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090885534
VERSION     WP_090885534.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..948
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105444
     Region          68..946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikiftqqqk lfwakrsfvi clftaiggqa vaqqpqanlt dslvldsmrk gsnpqnrhvd
       61 lwnrtisklr nvtgsatiys edvnttpvsd itnvisgris glysnrssgr tgpmfdassf
      121 tlrgqspliv vdgvirsfts fnvddiksit vlkdavstsm yglrsangvv yittkdksld
      181 qpfelnfnvq vgvlnqfrrp nfinganyae lyneaqkntf pnatpafsaa tiaayrngtn
      241 dpylqpnndw yntiyknnal qkryainaag ngksyryfts vehlsqdgnf ltsadnpyqt
      301 nnfykrynlr tnaqidfned iqlslnifgs iensnepgat sssimsrife tsplgysprn
      361 pdgtysgsil ytnnilasav nsgyinyner tlsadvglkf klddvtkglw akgllsinny
      421 ylqsisrtkt faifyptvsp tattytkvgs dgtieagkgd paivtqnkqt ffngllgydr
      481 sfgkhninvl asynltnlid sytqlnqlyn nagltatydf nktylaelgl vygsynryap
      541 gkrwgflpsv glgwvisnea wynkntfnfl klrgsvgqta wadptnyysy mqrytlgatg
      601 ynfgatasav sgvaestlkn pgitwekalk idlgvetqlf qnklgvelnw ytnkyydeli
      661 spangyasgi igqsyptvna gksrfsgfeg nisfnnnkqn fgyfikgnft iaqnkiisrq
      721 egnypypwly sagestgtyg yeaigfyqvg edvsktanip gfipqpgdlk yadlngdgli
      781 nfldrkaiag tkplfffgln agfnykgfdf sallegrlnr eiyysasqml afnngygyvl
      841 dyttenrwtp qnatqatlpr ltlgantnne qtssfwvkra dyirlkniei gysfpgkflk
      901 kakiskvrif vnaynpltwt kldyldpetg lsgfanyril nggislql
//
LOCUS       WP_090885948             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090885948
VERSION     WP_090885948.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108884
     Region          26..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktiifivl atlcpilkls aqtnnqisgr vvtandgkal psatinikns nvtvqsakdg
       61 tftilaktas gtltirytgy qsqeigfntn tktleikmqe annsfddiqv igygkttkrl
      121 ntgsistina kqieeqpvtn vlsalsgrmp gvfiqttngl pggnisvqir gkgsiaagtd
      181 plyivdgvpf egaspngtnn avstnniagn isplnninps diesinvlkd adataiygsr
      241 gangvvlitt kkakagetqy sfnlqqgfsr aasspklmnl qqylevrrea fqndnripsa
      301 dptstnyapd ltlwsqtegt dwpaylldnt asftdlqgsi sggknnttfs vsgnyrsega
      361 ilagvnnfqr ggiqtqlnht ssngkftlna rssltkqssv fanpvlnldr sylrppnfpl
      421 llangeinwy gnsniqaeld atsktstdni isnlalsyql lpslslklns gytktsynqk
      481 lifpssslpp gslnttsfsq nsgqsfivep qidyhirike lsvnlmagat yqnrtndsqf
      541 ikandfkvas lmedlgsayt iesrqntysh ykyasifgri nlnlknqyli natirrdgss
      601 rfgpgnrygn fgsigaawvf snnefikdnl swishgkirg sigtsgndqi gdyqylstys
      661 spggnlyqdg vtirpsrisn ddfhwesttk anigleiglf kekvlltady yrstsrdqlv
      721 syslprltgf seyqanlpav ilntglemsi elkiinrsnl nwsaqgnisi pknrllsfen
      781 fenssyaqly kigedltrir gyqtlgvdpa tgnmiyagqd gnasttpfdn ftlgkltpdf
      841 yggfgsslty qnfelnvfaq fvrqqskgdl krlpgtgvfn nfaltyqrwt psnrsttvpk
      901 atlastgviy pnssanvfnt sylrlknisl syrfkeaflk qikvnslrly aeaqnlftiw
      961 nsdaavfdpe sgvvsttalg rnippvktiv lglqlnf
//
LOCUS       WP_090886410             940 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090886410
VERSION     WP_090886410.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..940
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103704
     Region          51..939
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtryikcsgi ilgimcylyt ctalaqntiq qecvtgengn ltdstdklie ipfgtrsree
       61 lnyaqsslry nqltkvpisn lsgllagrls gflfrwtgnq pgggnvsyqi rgrssyaqgs
      121 spaflvdgie rdfedmdise iksvtvlkda aalnwyglng gngailvttk rgkvgenlis
      181 fdaqggfqsa snlikplnsf dfatlynrgl tnagqapayn daalegyknh tdpylypdnn
      241 yldrflnkra stqryalifs ggndrvryfs svsyfnqqgl fketetpnyd snygykrynf
      301 rinldydvtk tltltllagl rsevrndvgd gtstvfsnly nlppnafpil nadgsyggts
      361 lfqnnplgql qatgfsrttt nillasimad qkldfitrgl sanlffsydg ygnygdglse
      421 nyavfnqtvt pvqtyrtpav iayrtaafqt ntknnelwfg ldynrtiatd hqikanvraq
      481 qyvsaavdrl dyrsrmllgr adysfkqrym lgftgsysgs enyapgrrfg ffpavsagwl
      541 iskedflkda svisylklrg sygrsgnigp tydasgnvvr lpyrtlftrd agpflgstfs
      601 tsttarlvsp agnplttwek idrlnlgtdv dlfkgafsfs fdyfdekrtd ilgpanlpgi
      661 vgiaiaqvns gkvsskgfda sgtfnkkige vlistnanft yaknvilert envlpnqsti
      721 gryvnggnyy iaegifqsqa einasprqtl sslvvpgdlr ykdvnndnvi dandavssdy
      781 tdipkifygf gfnikykqfd fgaqfqgveg rtvdlsdimy agpnglnqls ldtwtpataa
      841 sakyprvgis dngnntvnst fwlysgdflk lrsaeigyst prslnqrlrf kgarifvsgn
      901 nifsiskldd ldidpetpna grfssypyvk tfavginvkf
//
LOCUS       WP_090887211             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090887211
VERSION     WP_090887211.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108396
     Region          29..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvfyllkqg llvlllfsaf mvkaqtgsvs gkvldetgqp lpgaslivkg ttrststdan
       61 gnfklagltn gsivlaasfi gyqtleksvn vpgtttitfq lvpdaqklne vvvigygtse
      121 kknltgsitt vgskdfqkgt ittpeqliqg kvagvniitn sgqpgvgsti rvrggaslna
      181 sndplividg vpfsgksidn apsplslinp ndietftvlk danataiygs rasngvilit
      241 tkkggsgdpi infstnnsia tvakkvdvls adqirsfvna npnatydvgk tfvsllgksn
      301 tdwqdeifqn afstdnnlsv agkfhgvpyr vsagyldqqg llitdrfnra tgaitvsprl
      361 ftdhlkidls lkgtltesrf andnnnaiaa slqfdptqsv tannqfgnyf ewlradgtln
      421 pnaprnpvaq vvlrdnsgna arsfgnarfd ysfhflpelh anlnlgydis kgygsifvpa
      481 faatsfstng satqslstsn nkvsefylny akdvasirsr fdvtagygyy dnaktnysfd
      541 eysatgvvrt takfpfsvdr nkllsyygrl vytladkyil sgtmradass rfgeenrwgy
      601 fpsvgftwri igenflkesk avsdlklrls ygetgnkdgd tigdysylak yyansntgqy
      661 qigntfydyy apsqydpdlk wettstynag ldygffkgri ygaldvyykk tkdllatvni
      721 pvgtnfnntl ttnvgnmdvr gaefslnfaa iktediswdf gfnvaynqrk vtnltlnpdp
      781 gskqgagdis ggtgitikyn avnqipgsff vykqvydgtg kplegvyedl nkdgvvnssd
      841 qyfykspdpk vtfgfnsafs ykkwtistvl ranlgnyvyd nissnygirn nilsaaglin
      901 nagvdflntn ftnsqylsdy yvknasflkm dnlglaydag klfknsntnl ritancqnvf
      961 vitnykgvdp eltdgidfkl yprprtytlg lnvgf
//
LOCUS       WP_090887248            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090887248
VERSION     WP_090887248.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116195
     Region          28..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkyirfyaw lvmcliwsaq aysqekniii ngtvidketr tgvpgvsiil estnkgltqt
       61 ngkgqfsvsa pvggtlifkf lgyntqkvkv tgqtsitvti sedrkeldqv iivayqkrsk
      121 etttgssali qgkevqdapt pnietllqgk vpglniqnnt gapgfrgsvq vrglstlsis
      181 gsgnesflqp tsplyiidgv pldadkaaef gfqsqgpgis plslipqedi esiqilkdaq
      241 atsmygsrga ygviiittkr gnskvpriry vtnffaktpp klretlggna erqlkiqqii
      301 lnaqsiddir rigetsflsd slnaywnnst dwqdvfyqtt ynqshnlamd ggdqkfnyka
      361 nlgyysekgv ikntgydryn lnmnmefkps ekfrffgsif gsvgkqnkgn gvgllqsgva
      421 angqastllp ppsfyqasgg vlsalqtynd nnsrnlrani egryefipgl aasstlsydy
      481 tsdtestftp aaangqfarl ndyvgrtfql ynrngityak tfgekhnlfv ntfneiykqg
      541 aqagitaqqr ipndqlqgpv gydayysrgg gvlsnyrnat iasfagsvsy dfdkkyvaef
      601 syrldgtsss glenpysknp svglrwnfnk enwladkkwl dygslrltwg qnivptgnlq
      661 siygiynlng nfnnsptigi nydmipnpal kpttttqynf gfdlgffnkv tiafdtyfkk
      721 vdnllfdrfl anttgfnkla sndlgianyg telmisykvi nnkdfgldfs vngainrdil
      781 lklpaeyngq yirfdgssyl qhnvfrvgrn tlsnylrinq gvyqtdadvp vdpvtgkryq
      841 sngvfflggd pimkdvngdy ildgrdyevt gnsqplvtgg isanlryknw glnvyatyta
      901 drtilnnala driaimrnpy alsavvplnd lniwtkpgdv akypypydyk rfdqiqplra
      961 dqtlwaesgs ylkinnvils ymfpkklirk iglnnlriya stdnlitfss ysgpnpenvt
     1021 plgrdistgy plprtynigl nlelitgn
//
LOCUS       WP_090887254            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090887254
VERSION     WP_090887254.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113486
     Region          78..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrylwlcfvf fvavqlnvla asgslkklnt ttfnysclqd ttkrkalgee dslrqdslsr
       61 ikiktiynkl ssnteketen lsmfpaislq qylkgnyagl yiqepsgepg smqnmfirgt
      121 ampllnkkdl yaaqplvvld giplimehpf aydiqqydfn rigpatnlla gidmnniasv
      181 evlkdlagtv aygprgvngv ivltskspdn vrrisfnsyi gmvqkptvnt ingkyenefr
      241 qrfydiyttn grysddeeyp vylsdslnnv ysgksnwtdl yyknaliygi nlglsggtdr
      301 anfrfslgnt ksegvadqtg ldrysamfni nmrpvqwllf saminanrin rdrnrslrdr
      361 faqlnyfpdl saplapnkdy yasylseydk gfddnktnai qgyarlvgtf gklklssafn
      421 vdynegyrdi fyakgllqgn syasnyygfn qrlmmdnkas ynykinedhd fnftlgqsmi
      481 wdmykynnay aykgandyik inlldsepir ngqpnpdylt pkafprelty rfldktednl
      541 ltfsgkvdya fqnkyflsat lrldgssnaq ptsrwfyspv lsaawnikne flrdnksidd
      601 vilrasvgrm grthvydnya qgpqytasvg ytgnltvpgy nafgvltrsy afgwvgygvp
      661 waytdqvnvg advsmlknrl rlsldvyskt dknqliaips yaeygykqai esglsvnntg
      721 vdltvsalvi nrnkfswnsa lnfnhnqnql kalprgldqi vignrllkvg eavdqywlle
      781 negiytadsq ipvvngqplk yngtvlkagd prwkdqngdn videkdkvlk gnmmpglsgg
      841 fdngfkygnw slntslyfnl grklinqema nrfdfvnreg nsevnsvkei tfwekrgdys
      901 kyplynpwst vipyrvdqdl flenasflkl rsvavgyelg nllkrkniki nkffvygsvn
      961 nvftvtpytg qdpelvgydg ldtgygqpip rtytlgvkme l
//
LOCUS       WP_090889738            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            rhizosphaerae].
ACCESSION   WP_090889738
VERSION     WP_090889738.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter rhizosphaerae
  ORGANISM  Pedobacter rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Pedobacter rhizosphaerae"
                     /db_xref="taxon:390241"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115328
     Region          27..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfknkllifs lfwlfilfnl saqgqgklng tvvgktdglp ipgvsirvqg kiagaitdgn
       61 gqfsidavtg dvltfsfigf stqtlkvtgt nkiqvslees knnlqevvvt alginkekks
      121 lgyaiqevkg sdlaeakesn lvnalagkia gvnitnsqgn mgssrivirg etsisgnnqp
      181 lfivdgipvd nsqlgaggsr dfanaisdin sedietisvl kgpnaaalyg sraangvili
      241 ktksgkrgks rsislnsstt fedllvlpsy qdvygqgsng qfsyvdgkgg gvndgvdesw
      301 gpkmdgrlip qfnsngvavp fiphpdnvrs ffetghtlnn gvsfsgggea ynyrfsynns
      361 aqkgvvpnse lnknslgfns sfdllpklkl dltanyvrts sdnlpgsagr ratstmlqfl
      421 wfgrqvdvaa lkdykdangn tfnwnnsyys npyfiayent vsqrrdrllg tvgltyqitg
      481 dlkanfhtgn dyyndrrklr vaygtngtpf gsyqetgytv nennteasls fnkrlnsdls
      541 ldilaggnlr skfyeennqv aprlavagiy tlansrdplt stsfysklkv yslfssaqlg
      601 fkdyaylnlt arndwsstlp vqnnsyfyps angsfilsea fgwksdflsy akirggwsrv
      661 gkdtdpyqln ntypfnpifd syplvtltdk ylnpnlkpey tnssevgfel aflknrvrld
      721 vsayntnsfn qiysadista tgfaqqvina grinnrglev qlgltpvkqt dglqwdvnvn
      781 ystnrgkvme ldeagslnsv vlgtsgvqvl atigqrygtl fgtayqrdan gqvivnasgy
      841 pqvnpnrqvl gaytpkwlgs inndfsykgf tlgflvdakv ggqiysgtha tgfttgvlde
      901 tlpgrdeehg glayyypgnn kaalpvqlps hnstapgsat vyhdgvifdg vradgtrnts
      961 ilsaqqyyks ianvneahvf satairlrev slgynlpknw iskiglanar ftligrnlwi
     1021 ihknvpnidp etafatdnaq gleslqlptt rsygfnlnlt f
//
LOCUS       WP_090907078             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosospira sp. Nsp13].
ACCESSION   WP_090907078
VERSION     WP_090907078.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira sp. Nsp13
  ORGANISM  Nitrosospira sp. Nsp13
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosospira sp. Nsp13"
                     /db_xref="taxon:1855332"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39372
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir ggetrvaatp etvkkftakg fhvvlvqsga gsgasipdee yqaagaiiva
       61 saaelygqsq ivlkvrgpep gelsmmrkda vllgllsphq aegieilarh gltafamekl
      121 prisraqsmd vlssqaniag ykavlmaanv yqkffpmlmt aagtvkaarv lvlgagvagl
      181 qaiatakrlg avieafdvrp vakeqveslg akfvevplse eekaqaetag gyaremsddy
      241 krrqgelvhq raaaadiiit talipgrpap vlikeetvra mkpgsvivdm aveaggncpl
      301 seldkivvkh gvhlvgianl pglvaadssa lyarnlmnfl nlmldaksge fkvnredevi
      361 sgtlvctdge vtgkt
//
LOCUS       WP_090938018             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azotobacter beijerinckii].
ACCESSION   WP_090938018
VERSION     WP_090938018.1
KEYWORDS    RefSeq.
SOURCE      Azotobacter beijerinckii
  ORGANISM  Azotobacter beijerinckii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Azotobacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Azotobacter beijerinckii"
                     /db_xref="taxon:170623"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40329
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkllgqg htvtvqssag leaslpdsaf eavgatigda
       61 aaalgadlvl kvvapspael aqmktgavlv gmlnpfddgn iarmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee rqcaegvggy arpmppswme
      241 rqakavhera kqadivitta lipgrkaptl lheatvqemk pgsvvvdlaa aqggncpltv
      301 pdevvvrhgv tvvghsnlpa lvaadasaly arnlldflkl vvdkdghfhl dleddivkac
      361 lmceggrvvr tnggapspsa avprstkena
//
LOCUS       WP_090956476             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. ov118].
ACCESSION   WP_090956476
VERSION     WP_090956476.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. ov118
  ORGANISM  Arthrobacter sp. ov118
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Arthrobacter sp. ov118"
                     /db_xref="taxon:1761747"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38659
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqvgvgrepr agerrvaatp etvqqltalg lnllvesgag teagfvdgay keagatvise
       61 lpiagldvll hvrplspqta arlqpgavtv glaspaselp tvqalaaggi tsfalellpr
      121 israqsmdal ssqalvtgyr avleaamryp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vaandiraas adevasmggs finldldaaa egsggyardl gedraqrqrn
      241 llaphvaaad ilittaaipg rpapllvtan mltgmragsv vvdlaaesgg nvegvvagqd
      301 vqvpvdggsv tlvglqdaas amptdasrlf arnvsnflal itasgtvvpd fdddvvagtc
      361 lthagvvrha ptaaalgtaa lgkda
//
LOCUS       WP_090960795             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aureimonas
            phyllosphaerae].
ACCESSION   WP_090960795
VERSION     WP_090960795.1
KEYWORDS    RefSeq.
SOURCE      Aureimonas phyllosphaerae
  ORGANISM  Aureimonas phyllosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aureimonas.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Aureimonas phyllosphaerae"
                     /db_xref="taxon:1166078"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55230
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgvpkerf agerrvaltp esvgrlqklg yeclvetgag daarfsdeay aaagarvvhd
       61 aaslwaeadi vakvrppeda evelvrsgqi lisflypaqn aallealrak gatvlamdmv
      121 prisraqkmd alssmaniag yravieagnq fgrfftgqit aagkvppakv lvlgagvagl
      181 aaigtaqslg aqvrafdvrp evaeqiqsmg aeflfldfag aadgaatggy aapsspefra
      241 kqlelfraqa pevdivitta lipgrdapkl wledmvalmk pgsvvvdlaa erggncdltv
      301 pdevvetpng vrivgytdyp srmatqastl fatnirhmmd dltpkkdgvp vvdmeddvir
      361 gatvthegai typppppkia aiakqapkkv veetaaekaa realtarksg qrqvmllagg
      421 aillmliglt appsflqhfv vfalscfvgy hviwnvshsl htplmavtna vssiiilgal
      481 lqvgtsgwfv sflaglailm asvnifggfm vtrrmlkmfq ks
//
LOCUS       WP_090960884             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosospira sp. Nsp18].
ACCESSION   WP_090960884
VERSION     WP_090960884.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira sp. Nsp18
  ORGANISM  Nitrosospira sp. Nsp18
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosospira sp. Nsp18"
                     /db_xref="taxon:1855334"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39260
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaeir ggetrvaatp etvkkftakg lntvlvqsga gagasipdaa yqaegasiva
       61 saaelygqsq illkvrspep aelalmrkda vllgllsphh aegiealarh gltafamekl
      121 prisraqsmd vlssqaniag ykavlmaanv yqkffpmlmt aagtvkaarv lvlgagvagl
      181 qaiatakrlg avieafdvrp vakeqveslg akfvevplse eekaqaetag gyaremsddy
      241 qrrqgelvhq raaaadiiit talipgrpap vlikeetvra mkpgsvivdm aveaggncpl
      301 seldkivvkh gvhlvgianl pglvaadssa lyarnlmnfl nlmldpktge ynlnredevi
      361 agtlvcigge vvrka
//
LOCUS       WP_090969958            1216 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090969958
VERSION     WP_090969958.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1216)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1216)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1216)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1216
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1216
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133481
     Region          163..1215
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdkftqfigi slsfkqigla ivligfsatq aqpmptrgif ashptqkkna skfislkegl
       61 ellmketdmg iiyepeiikg irvneaaiaa hnyslqevlh vwlkdspltf sklpnsqnyi
      121 imrkaeqhei psvleqdvet gearagrspd lkpvspllvs qervvtgrvt ssedgkaisg
      181 vsitvpgndg gavtdasggy riaiphggdr lmfnamgfer qeevignrrv invelvavta
      241 hleevvvnal gferkadalg ystsqiggnq lsnavegavi ngmagkasgv ritrssgdpg
      301 agshiqirga stiggiqpli vldgipidns ssgnsnggvy qqsrlndinp ddiesmdilk
      361 gaaaaalwgs rasngvivvt tkkgkanekl nisfkssysy dqilnrhplq safgqgdngi
      421 ysqtslrswg dliadrfggp dviddtgpff ravngniyyp ilekrnqtiy hdsnfdqvir
      481 ngyfldnsls lsggdsrsty fvslsdfkqd giiqnssdyr rttfrvnssr kfgdkitlst
      541 nttyalssnn rirkgnassg lylgllrtpp dfnildyege yyssagaapl rhrhrvyrnp
      601 lgananpgfn nplwtinnqe nfskvnrfit smqlnakpsd wmelvlrsgi dtytdernay
      661 fatgsagaiq stgvyedake tdfefntdlm svfrpkfhel lnaemlvgfn fnqrsnqdvw
      721 gqiqgfidpa adirnfingp rgnfdmsnsr tlrrnaalyg svdlsynnyl flvltgrfes
      781 astfgelsks sfffpsatva wqfhrnvalp eaisfgklra sfamvgvepa myrtisqyva
      841 asysdanggs ldgsrfgnga fvpanrvgnp ylrpeiktef etgldmrfhs drlrtsftyy
      901 nnqttdvlfd vpipsstgyt nmqdnageik nwgvevdvny dvfakrdftw tvgvlwdrnr
      961 nvisklpdae sldlgglsgi sgravqgyql galwgsrwlr daanslvlne ngfpqldesq
     1021 gvigdpnptw rgsalttlry knialdvvie tmqgnhifag tyaslldygl apesahisva
     1081 prdlltyngq vipqgtefrg niadfgagdv aldqswyrtg ggyasgaaes fiqdgswiri
     1141 qqltfsyaln serfrtktrl qgielsltgr nlfvwakefr gndpntnlmg vssvrgidyf
     1201 ntpgtrsyvl tlkvny
//
LOCUS       WP_090970022             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090970022
VERSION     WP_090970022.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109276
     Region          30..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miikhtkrml mlclllagtt flahgqggai tgrvvdeqgq pllgasvqvk elrrtastde
       61 dgrfalpdia ngtytvavty vgylpaekrv pvsgaeqvad felkpdeqfl sevvvigygt
      121 qqrrdltgsv atvssrefqs gtittpeqli agkvagvqit ssggrpgags tirvragasl
      181 nasndplivv dgvplavgev pgvsnplsli npndietftv lkdanataiy gsrasngvil
      241 ittkkgtgsr tainfstqha latvdrkvdv lsadqirdyv nangseaqkq llgsantdwq
      301 neiyrpaytt dnnlsiagra gdlpyrvsag flnqdgvlms drlqrtsaai saspmlfnnt
      361 lkvdinlkgs htrsrfanqd gigasiqfdp tqpvrtdnaf ggywewlqyd adndrhvpnp
      421 naprnpvgli elkddqgday rsfgniqldy alpfveglha nlnlgydvsr gkggvfipai
      481 aaqrfstage vtryqtdifn rvgefylnyt rqlaginghi natagygyyd nksrinnynr
      541 tsedgtvlse pafpfdepqn rlisyygrli ythadryils gtirtdgssr fasenrwgvf
      601 psvgltwrir depflrdnrv fsdlklrlsy gvtgqqdgia nysylpnyvs sanesmyqfg
      661 dtfyymhtpl aydrdirwes tatynagidy gfldgrihgs vdvyfkktkd llsvipipvg
      721 tnfsnllltn vgnmensgve wsinttpvrg eaftwdvgfn ftfntnkvtn ltnvddpnyl
      781 ieqggitgst gnhiqahvvn yapysfrvhk qvydqngrpl egvyadlngd gtindddryf
      841 yksplpryll gftsqleyrq ftlttvlran ignyvydnvs snfgsrynvl dpngpinnap
      901 vdflntgfvq kqytsdyyih nasflkmdnl slsyridnll rgsgssltvs anvqnvftvt
      961 kykgvdpeis ngidnqfypr prtftlglnl gf
//
LOCUS       WP_090970059            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090970059
VERSION     WP_090970059.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117316
     Region          30..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvqlstwl nsfvccfllf amqqlyaqei pvagvvrdqq gnplpgvsvv ergtgkgvkt
       61 dengfyeisi tsagrtlifs svgfhaqqhv iraaagsfdi tleedlssld evviigyqdv
      121 trrkttgaia svkgkefent pyttfdamlq grvagmtvls psgepgtnni vnirgssnle
      181 lannsisapl yvidniiydv ndfgsaygan plqsinpndi esvdilkdas asaiygaraa
      241 ngviivktkr pmagkpeirv safygiadrp amkpiqvgta errlkmdmly iggndnwfyn
      301 nqlsmmltds lnpafnnntd wqglflraaa lnnvnasvga stenftyrfs vqryyeegvm
      361 igyendnvtp riflqanptp nlqfetnlfa gltrakhgsg dgvygskypf ntwgfpssfw
      421 qitdeeeavy tgryddlmdn drttsingnt aftvkkvvvp glsfrtqfsy ninnntrdlf
      481 qpglitpnrr nyarswvyqn qrwevesffn yiktikddht lsgvlgygme kntqnnrfas
      541 gwndnstvvk svsgipsgpd lyawtdlaer srvsvfgrls ydykgrylls gsyrqdassr
      601 ysrdnrwgvf pavsagwavs eepffeplkh avsffkfrgs ygltgldpgs yyaqymtlgf
      661 nagyvgavld ngnevapnty ngttvtypny qnaasspgir wertpqfnvg vdanfiedri
      721 svtadyyirn sqslvfqspa plttgfsqlt gnfvdirnsg veltinsvnt ragaafhwst
      781 nfniafnknm vtglpnggre frtgppwmer tlnigqplfp fqvwrvngvf atdadvpidp
      841 ltgnrlrngl tgqyykagdp apvdvngdyi idyldkislg dpnprvvggl tnsfaykgft
      901 lqvlvtfveg rslwngylsd rlqdagsptl fttwgtnsai agdfnlsdfw lrpgdrsrfp
      961 nlfsntvdnw hiaqnyfven asfvrlkniq lgynlpqkiv dklrfrsirl fsvvdnlyir
     1021 swsdtpdpea vepngystgn gypipkkftf gidvsf
//
LOCUS       WP_090970240            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090970240
VERSION     WP_090970240.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122216
     Region          31..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrvksiqy plllvfllla amtagqpsek isvrgrvedt dgnviagasv veldkdgrtv
       61 sgttsdmtgn fvlrvapghr isasiigyqt avqninnrtf ivfrlnpaqt aleevsivae
      121 trpkidygtg lqiaerdltg avsrvsakdl eelsaasidq alqgrlpgvd fgatsgdpga
      181 gmsirirgta singsadpli vldgmpyevs ipedfnfgsa deqgyaqlln itpadiqdit
      241 vlkdaastav wgaraangvl iintkrgqlg kpvvtynlrg ivhqqpqaip lltgdqysml
      301 vpemvmnang lplnlqnnke flydpndpyw yhnysrntdw iqeitqigyt hdhnlsmtgg
      361 gqkaryyasv gylntvgttk gtnldrittk inldytvssr lrfrtdvtya yinnrlnytg
      421 girgvayikm pnmavyeyde hglqtpvyfs paqniqgqys rtynplamae qgygrqigqr
      481 itprfnlqyd iiprtlfttf dlqfdinntk ynsflpqdat grpftetvvn latdeendfi
      541 avasklnlly tpqlkgehtl qsllsiqtqd drnlfrsars sntassvlrd paipgrqitg
      601 alnafgdqyr nigvllnaqy gfkdryiing sirmdgnsrf gpenrygyfp avsaryrisg
      661 epfmekyahw lddlslrgsy gqagkapqhn ymfynryany awsyldeaav fpanielsnl
      721 rwetlvgsni gfnlwmfkgr vrldgelyrn rtkdlifnnl rlptysgynt atfnvgtmdn
      781 qgwelmlntq pfrsenwsig vdfniarnyn vvrevseffp rendarigen gvyktylqig
      841 npfgsiygfr ykgvyrdeea tvardangnp itgldgqpvy mrfnypftdy vfqpgdamye
      901 dinhdgnide ndmvyigntv pkytggfgfn vtykgnlrlm tffsyrlkyd minggmmntt
      961 nmfdfdnqst avlkrwrnpg detdvpraly rsgynwlgsd ryvedasfvr lrsvtlrynl
     1021 tnrllnrlgl rsaglyatve nlftwtrytg qdpdisirgn vdpfryaqdn nltpptknfl
     1081 fgisagf
//
LOCUS       WP_090970248            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090970248
VERSION     WP_090970248.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117890
     Region          46..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkllnrrdg iwfatmvwll gcqlsyaqpv dslnrtpekt gigqltikgk vvsastgepi
       61 agvhvevagy sseftddagg fvigvphtda vlqasavgfl pkrvavsgkp aielslieeg
      121 yptffadvqt ptvgkqplst qpwaihnvsm adkwpanset pdsylqgrva glhairragt
      181 pgsganlflr gfssiyannq plivvdgmiy dnkiyapsii pghasnpfgm ldlrdiddit
      241 vvkdgasqyg trsangvili ttarakeeat hidfaayggl natvaalpvm gssdyrvfls
      301 dlyqsrgmtp qeigripfmr ddpnpdyyry hnhtdwqrev msngynqnyy lkvtggdnia
      361 tyglsvgynh qeglftntgl dryhtrfnga lnlsqkldat vslaftstqq dlrsqgedfr
      421 tnplllsqik apflathvvs degqvspnla eldifnvsnp msvienmigs ssnyrffgst
      481 sfnyrfneqf sahtlfgvtf dkvretvfip ergiapdtmr ravirnqsgv nlsryyalyn
      541 dtrlsfrrsf nhvsrltasl girynhsqse ndsgfgfnsa tddlvtvghg vgelrqlags
      601 lgrwnwlnty ltadyqyrnr yllsmnvaad assrfgtevn slriggvpfa vlpslaagwl
      661 lssepfmaaa ngidllklrv sygltgnddi gnytarkyyt sqnllgmqgl vrgnignpgl
      721 rwetvekvnv gidmaffner lqltadvyrs htrdlliwqq vpaetgmqhm ltnqgamrth
      781 gvdvyafgrl araalkwdmg ilfsmyrnrv vdlplgsivt tfggasyvta egqaanqfyg
      841 yktdglfltq qeaadarqyn rqngvlveva ggdvrfvnih dapedqaagi tvidendrqv
      901 igdpnpdftg mwsnhlkwhr waldvhvafs ygndiynaqr aaletqasta nqslavrnrw
      961 rtdgqvtdmp rlawgdplgn arfsdrwied gsfvrlrtva lsytipgglk finnlsvylt
     1021 annlftltry kgydpemsaa ptifgqgvdm wgepifrstq lgirigf
//
LOCUS       WP_090972080            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090972080
VERSION     WP_090972080.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120140
     Region          23..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktyislifc ftalqaafsq tytvagrvva eqdstpipna svyaaqqets vrtdasgsfq
       61 lrlqgkgatl kvshighlsr evsvtfpqqq plvitlpvam hqldeavvst gyetlskera
      121 tgsfekidna llnrsvsmdv lsrienlatg ihfekgdanf ntagrrpnhd iyihgistln
      181 agtlggnapl ivldnfpyeg dinsinpndi esvtvlkdaa aasiwgakag ngvivltskk
      241 atyeqpvrvs vtsninviek pdlyqhriis tsdyidveql lfqqgfynnk ensrakpals
      301 pvveilikqr dgllsateaq qaidayrqnd vrndmlrymy reglqqqhsl qissgtnrqk
      361 liigggydqs lpsrvgsqns ritlraennl kptrnlelal gvrwaanryq easaaetyqn
      421 sgypfpyial adengrpipv pkdyrmgfld tagngrlldw hyrpldeikn pptlvsseel
      481 llnlglnykl lpwldldvky qfsqfgtkne thhnidsyya rnrinrgsai seagvkyhfp
      541 fggilntsrq tssghrfrgq fnlnkqwlda shqlhailga evqesnnrgd gfiaygynde
      601 lltyagqidf tywypvygnl assesmpfav mdftettnrf vsffsnasys yrdrytasfs
      661 arrdasnlfg vntndkwtpl wsaglswsvh repfftaqwl prlkiratyg ysgnvdnsms
      721 alttinysnq sstgvdlpga glrnppnpsl rwekvrntnl gvdfaisgnr mrgsvdyywk
      781 htedllhfyp idptvgvtsm tmnvantksr glnvnintqn lsgklawath wlfsynnnwi
      841 thsfveytgp ttyvrgrgms qipgtlafpi ysyrwaglnp etgepmgylg gdvsqdyrsi
      901 tsantkledl vfhgstrply fgslrndfsf rgfslsvnis gyfgyyfrrr gmdyaqlinn
      961 gdghidyyar wqkpgdektt hvpafqypis agnsfyqnte plvekgdhir lqdcrfaytl
     1021 psmgswlksg qvylyannlg iiwranklrl dpqvngnipm panfamgvnl nf
//
LOCUS       WP_090973532            1130 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090973532
VERSION     WP_090973532.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1130
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126755
     Region          42..91
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          109..1129
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlqllatptv raqqlkdtkv sisianapls eaigklaqqs glaftyneqq lsnhhvsvsa
       61 esesaesvlq rllsglpfty teragkvaiy psrphygksa tgtqeelevr gaikdtlgsp
      121 lqgvsvsmag kptvstssde ngmyilripa asatltftmv gyrqqtmevg esgvydivmr
      181 eelsdldevv vvaygtqkkt elvgavttis pgelkvpssn lttalagrla giiayqrsge
      241 pgmdnadffi rgvttfgykv dplilidgve ftatdlarlq pddiasfsim kdasatalyg
      301 argangvilv ttkegkegra kvgfrlensl saptrnvela dpvtymqlhn eatrtrdpna
      361 relydqrkid ntmagtnpyl ypatdwrgal fkdyamnqra nlnvsgggkv aryyfagtfn
      421 rdngilqvdp qnnfnnnidl ktyllrsnvn vnvtkttemg vrmygtfdey tgpidggtqm
      481 yrnvmrsnpv lfppyfpkte qyehvhhilf ggteqgnyin pyadmvkgyr dysrsvmmaq
      541 felkqdlsff teglslralg ntnrtsyfsv srqyrpffyq prffdqatgr ldlqllnerq
      601 gaeyldyseg ektissvfym esalnynrif ndkhnvggmv vyimrqrlng nagdlqqslp
      661 frnlglsgrf tyaydsryfg efnfgyngse rfyrnhrfgf fpsggvawhi snekfwepll
      721 pivsllkira tyglvgndei ggpqdrffyl snvnmdnsgr gatfgidngy snsgvsisry
      781 dnrditweta ektniglelk lldkigiqad ffseyrrnil mtrasipavm glsadvranv
      841 geasgkgfdm svdyqqnfgq hlwvtargnf tyatsayrvy eepeyadeww ksrigyplsq
      901 rwgyiaerlf vdddevansp vqdfgapvrg gdikfrdinn dgqitaldqv pmgnpttpei
      961 vygfgfsagf knidlscffq glaqesfwid platapfiry vysgestrfq dvnlenqllk
     1021 ayadnhwsea nnnvmalwpr lntvadpnns qpstwfmrdg sflrlktlef gytfqrdrvq
     1081 rlgmesfrly fsgtnlltws rfklwdvema gnglnypvqr vlniglqvsl
//
LOCUS       WP_090973973            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090973973
VERSION     WP_090973973.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110073
     Region          24..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msktlrwlsi vlvflthgvy aqqitvsgvv tmqgtgepaa gasvqvkgts vgtstgqdga
       61 ysisvtkgqt lvfsfigaia eervvgddgv invslsedas lmdevvvtal gierdrktlt
      121 ysvqnikgdd mraanqpnli nalqgqiaga qisssggspg lpseiilrgs ttltgdnqpl
      181 fivdgirvnn sssnftvnri adinpedied isilkgaaaa alygidaasg aiiittkkgr
      241 qgvlqvngay rsfvetlgrt prqqgvytvg lggtydessg sswgrkfryd epvynnidrf
      301 fetglthdln lnvnggserl qyyvsggyrn agstipnteq erisllvkgt aklstkmtlt
      361 tsanyvknni qeglggasag gwinsiltyp lmydilqyqh pngepyyvyq eqedprnari
      421 spmwgvmknp rnnnvdrvii ngnldykpld witlsyrlgq dytnssyrtv tmpgtpgtyf
      481 dgrvtdskgi tkfvtstfns tfdrtfwddf ratfilgfns eyydghtlay aannflvrdi
      541 pspnvvernd lslteswlrr qryavygdfr veyknllslg itgrndwsst lpkhsrtfys
      601 psysgsftys elfnpddwyg klrvsyarvg kdapiyrtnt nlnqvvtvgg gfsvnatggn
      661 pdlkpeltse levgtelsff rgrlnmdftr yvketkdmim tprvplpsgy viktfnlgsl
      721 rnkgvelsvn aipirnqdft wsttvngwrn tsemlefagd ivtfkytnaq lnagvaattl
      781 gdavlgivgt dyqrteegyv ivgddgypli dgteryignr epefnigwln klsykgfnls
      841 fmwdfrfggd ilnasrqrmm svgtaydigv wrdrefvfng vvaqqdgsyi knatpvvldy
      901 sffannyyqv gtnfvekvnw arvrfitlgy slpkawaarl gvsnlglels aqnpilitny
      961 sggdpevnsa gpnaggtgas tmgvdngaip lprtysfglt vsl
//
LOCUS       WP_090974012            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090974012
VERSION     WP_090974012.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113695
     Region          24..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkllcffm lgillmgsay aqerrisgrv tsaedgapia gvsviavgtn iatqtdelgl
       61 fsisipvsvn elefrfigyi sktvtigsnt ninvaldlda selqevvvta mgiersarsl
      121 gysvseiggd eltkaretnv vnslagkvag vrvtsqsgtp ggsskivirg vssisssgqp
      181 ifvidglpvd ngapqistvs ssvpqgsaga dfgnragdin pddiesvtvl kgaaatalyg
      241 arakdgaiii ttkkgsqgrg tvtinssarf dnmlkvpefq neyaqgiqgv yniantngwg
      301 pkisevqdrt fpnflgeqvt lqaypnnyrd fyetggtyin niafqgaddr gdyrlsytnt
      361 eqsgivpgsk fsrnnigina grkifdgldv rgtvnynrst sdgrpvqssn npnvlqslvl
      421 tlprtvdigl vrdnyvdpit geqitltpsr ngnnpywivn nnnfgnivdr vygngivtyk
      481 plewltisnn fgtdfyyekr lgttrngtig dltgsffqgn iqnrvinndf iitaetrlnd
      541 dlglkviagh niyenyyeri lsnaeqltip glynfsnaas vlttntsnkr rlvgvygdig
      601 lsyrdflfln itgrndwsst lpisnrsyfy psvsssfvfs elletsswfn ygklrlswas
      661 vgsgtepysl afvynpqsag faqygygsqf pfngalafsa pgtipnanlk pqnqttyevg
      721 adlaffnnrv nldvtyyysn tidqivslsi pqstgfsfrs vnagsvinkg feamlgivpv
      781 rvndfnwkvd fnfssnrqsv elpdeiasyt vqsgwsglqv kaetgkpfqi ygvgwerdpn
      841 gnivideatg lrrtiadqpl gnvfpdwmlg innsfsykgl nlgflvdirq ggvlysntas
      901 tlrtsglgye tlqnrgdrfi drgvvlrdge yvpndvpvqs mqdfwgqmst sntegnifda
      961 syvklreivl syqlpskwlq sgpnfirgas igvegrnlwi ikdnvphidp evnffgptsl
     1021 gegvefnsvp strtigfnlr vql
//
LOCUS       WP_090974015            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090974015
VERSION     WP_090974015.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116269
     Region          18..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslylgvlla givyaqerri sgrvtdgvgg eplagvsvva tgtsvgvvtd qsggysivvp
       61 pearsltfsy igymsqtvti gesttvnval esesselsev vvtanviare rrtlgysapt
      121 vsgaeltqgq npsvinslag rvagvnitst antpgsssri vfrggtsisg nnqalivvdg
      181 vpidnssvig gqnalssldf gnrgndinpe diesvtalkg paaaalygsr aangaliitt
      241 kkgrrnaekt eitftttntl ssvlklpdfq neygqgflvg fdsdgnpvye ndpkenwswg
      301 apftgeiqpw gqeingvrle kpysaqpdnv rnffdtgias nnnlsfsggg erstfflgln
      361 slnsngvypt avdnynryga rfngtmefnn kfnagislny trinsstvgg gqndasvydk
      421 vlqtardipi drmgdlsnpy fgfgivdang vfqenlygyt gayaispyyv lenfenlndv
      481 nritgnvnig ykplewldie erigvdtysd rrremtpkye fypadvtsgn ydpndnayin
      541 nggyrisqfn vseivhdlma tarhqfnpdf ygslmignni rqrhvtnnvt atnasgglvv
      601 pgwynlsnsn gpvnviqdnw slrrlvgvyg qlslayrdfl fldatarndw sstlptenns
      661 ffypsisgsf vftellqsnt vlpfgkiras warvgndtdp yqllttfsrs qinssfgstt
      721 fpfgnvaalm sgstignpdl kpeittslel gtelaffrgn rlsvdftwys nsstnqilti
      781 pipnstgygf kvinagtvnn kgvelalrgt pirttdlvwe lygtftrnrn rvsdlgvdqi
      841 viggfsgmsi vaaenrpyge fyavseqkds egrtiidpen gmplitptav ylgsynpnyq
      901 aswgtnlnyk slsfgvlfdt kqggkfwsrt kdimafvgts aetggerina ifpnsvylde
      961 ngnsvtntey tyikqnyfpg reagvsvidg sfvklrtasi sytfnaqqlg rtpfgaltvg
     1021 lygnnlfiwt pdenqfadpe instgagneq gfdftaqpsv rnyglnvrvt f
//
LOCUS       WP_090974162            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090974162
VERSION     WP_090974162.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120107
     Region          27..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkciklnv svmlllglln gafaqevlrg rvygeavgvp lsdvsvtlvn annlilsggr
       61 tnkegifels rhpdavkirf snvgyqsqef rlqsgqhpvf evvlvsdqqq levveitgqr
      121 qqqkadlgfl tidrrelsss iasvdltgve nmpvasvdql lqgmapglqv vaasgdpgas
      181 asirirgiss isgindplwi vdgsevigsn yqvesisdfg fspigdldps diesidilkd
      241 asatalygsr gangvivikt krgkrgrpql tfnsrftlte vprtipmlsg deqriyyier
      301 wtggaddgta hpqlrgdltr ddawmfnnnt dwvdaitrtg vyqqyntals gggerinyyw
      361 glgytnqygt tkgtgydrfn trfnlnytvs dklrvsadlt ytnsltdkrg qrhpvtngnq
      421 einpvlfsre tpayfpiysk nglnyfvnrn agvsshsryn plalidysty lsranrfmas
      481 tsvdytilen lefrsqfsad fresadeyfl pgyatdalpg edlynaghqt egyqlminnn
      541 nrliwsalrq dnhrltftgv fnlnidrdns mevtyfngss pqlraadasa iiagargkfg
      601 trkylgmflq ghyamhdryf ltvtgktegd srygsdnpys ifpaigaawd maresfltdv
      661 kwvnaikprf afgitgnlpn vlnlydiays tgigymgety iypskfandn ireertteyn
      721 vgidwslfdn rlsgqfdyyt rttndlllqe rlsstlgyen qytnfgrvrn sglelgitav
      781 ilkgsetrvr wksffniatn knrllslpdq fnedafsatv ggfssrlypg dviggfyayr
      841 algvyatdad ailrapdgsi iyeadgvtpk ymrfgsntgh qfkggdmiya dingdgiine
      901 ldrvqigdan plffggwnnt lnyrnwvlta nfqyqygndv ingtriqmeq msfshnqsrs
      961 ilarwrrqgd itdipraqpd nawnraassr wvedasylrl ktvsltynad rtftdrlglg
     1021 irqlsvfvtg ynlytwtnyl gvdpevpitg svllfgvdra ttaparqytl glratf
//
LOCUS       WP_090974227            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090974227
VERSION     WP_090974227.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114147
     Region          30..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mivinslkls lwwiilgmai tahaqqdsvv vtgqvtsgyd gkplaravvs vpgfemmvet
       61 gtdgnyrvvl pseaseimfw spgyyrttfp lldrrelnvt lvpdsrpnyy deelvtnplh
      121 rdaaaiyqrd frrgalhves vlqgrfsgln vinksgmpge ggamyfrgvr sfegdnsplm
      181 vingvpylpe ssnsaviggy srnpllplnl rdiqevrllk gaetavygsm gsngvlviet
      241 akpadletvi efnghygvaq npatlpvlgp gdfksyigdv gltqfddmge mlnffpflrd
      301 dpdyyfnfly nsqtdwqgli yrpafvtdnh lrvrggdava kynlslgatn qggaldnssl
      361 trystrmnat vtlgqkfdfl gtvgftyqna nlheqgmlta tnpiltalsr apilspytkd
      421 elnnelpsyd vvrqfnvsnp lavlntaqmr lggydvfvna gisyrpdtyw tigttlgifs
      481 sfmrhtafip gvssrtvmpl engvalntsr agaaqvsnlf yrlngqyerq igvhrveagg
      541 gyqfiiahse ldagsgrntp sdfyrtisnv svdgrqfqgy iepwnwmsvy gfgryhwnnl
      601 ltlsayfsad gtsstgngtd rfglfpggev rwrvanmegl havtwldqld lrvgyaltgn
      661 sryssklsrp sygsqlyrql sgivvanvpn dalrwednqt fdaaidigal nkrvratvgy
      721 yqtlsknviq tmaaspvtgl dfrfvngaei snrgvevdis atlieqrdvg ltvggtwsty
      781 rseiqslagd gqrvfelsng valvsavgha pyafyghvan evipsasaaq slglvdykgl
      841 pfeagdirft dlnhdgvidr adrtiigdpn pdffggafvd vrykqlslsa yfnfsygnqi
      901 ynavrrhses mnrydnqsta vlrrwkadgq vtdmpraeyg dprensrfss rwiedgsflr
      961 lsnlalryri qraavrvleg aeiyvmgenl vtwtkylgld petayahnpm ylgldfgnva
     1021 qprtfragin ltf
//
LOCUS       WP_090974228            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090974228
VERSION     WP_090974228.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122641
     Region          26..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgkiivlcw lllwsgwsva qqsnilrgsi sdeqgnplag atvfienqdk rnlkgsstda
       61 nglfqlevpn qpdltvvfsc igfqtqripy sgqralqirl kmadmqidev tieargtkqi
      121 nsmgisyrdq vssterfdlk evetmpfasi eeglqgrman vdivtsadpg arnsirirgt
      181 sslnanadpl ividgvpypt tiqdgfdfat andedfgalv nispndiesi evlkdaaata
      241 iwgsqgangv llfttkrgrs gktrisfssk ldmrrepdpi plldgnqyvs liqdavwnsv
      301 ndlgyaagsg yldllyntne infnpdwvyf deynqntqwv nhvnqlgyfv dnslsisggg
      361 dkatyrlslg mlddvgttig tdlkrynall avnyrfsnkl evmadmaytr snqnnswtag
      421 glasprgiam trmpnmspwv igangqptne yftprvnfqg gfeegsmank vynpvamvhe
      481 svnrtnsena ranfrlrydv vpslqyhgmv gfdmrssknr rflpqsvtgv swvneyfnqa
      541 sdritdalnl ttenrflynk lfgedhnlig nailrtteel sypyssetsg nassgmsdpa
      601 lggnvvsias dfsairriag ianvfysykg kyninggytw eannsigreh rwgrfpavga
      661 awlfgdepfm qrlnffdlak lryswgrtgn apsgawrylg tfsplvpgym dmpairpqrm
      721 qlenlrweti tqsnfglela mldnrlfvtm erydrrttdv lhrdvripgs tgfsqlawfn
      781 sgelynrgwe livnydvirk sdwglqmmln fsrnqnevve lpenmqfeny vfdnkryahr
      841 ivegnpvgsf ygyrylgvyq nqdetyardl ngnliynlng epvfmtynnq rqaypgdary
      901 adingdgvid qydivylgna mplftgglsl tlrykgftls sffhgrfgnk vvnearmnte
      961 dmrgtsnqsq avlrrwrheg dqtdipralf gegynilgsd rfvedasfvr lrnlslrysl
     1021 pkpflqrfni qrfdvfmtiq dlitwtnytg mdpevslrpn dvymlsrdna stprprryav
     1081 glmfdf
//
LOCUS       WP_090974425            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090974425
VERSION     WP_090974425.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113688
     Region          23..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksllilvv nviyctyvfa qqktitgkvt desggslpnv tvlvkdgrnq aqtdrqgryr
       61 ieaslgdvli fryvgfssee rtvgdntvin vtmlqqasgl devvvtaygv drekkslgys
      121 tvevdgaeva qtqregffsg lqgrvpglsi nstngapgss aqivlrgfvs lsgdnnaliv
      181 vdgvpvdnsi lsegdlvtns pnrdqdysnr gldinpedie sytilkgpea tamfgnqgas
      241 gailittkrs aggrglityn nsfrwetlnr wperqtvygp gqngvfsgtt sifqgpkfpe
      301 gtpmfdnfdl ffrtgmahkh nlvfeggsnr ftyrwsneft dnkgvipntr ytrlssrlga
      361 taeiseklsl ntsfnyvksd ndkarrgpqg ymvtlmrfsp ssdvrnwide ygnrvtsigt
      421 iyseydnpfw dvyrnttwdk vdrllgstnl tykptdwlsv tgilgvdfsq thgesvyhgq
      481 syrgsgsagn etggrfvgyd rlgriltgsl tarsrhqfgk ysatfvlggn fddynyqtns
      541 qsgerffdpd fysinntlps tqraryvlnr yrnvgffgqa vlgyesllyl tlsgrvdgas
      601 rlmpnnpffa ypagsiafnf teldffkdrv pwledgklrs sisltgkqpw rtyatgsnle
      661 pvsssgggfa ysyyggnpdl svettrdfey gfefslfkrr vtadftsyrr lsidqiilpr
      721 lsygsgfvlr mmnggdvenk gveiqlkgnp irkanvswdv tvnytrnrgt vlsvadqlpe
      781 yyesdtwilg gvrsgthpgy sigalsgtrf erndngdili npanglpimg dgtyhpigdr
      841 ipkytvglvn nfrykdfsls flwdlryggd vlngleyemy trgistktln reepriingv
      901 irdglentan ptrnaiavtp yfnslyyttn vepemfiern ikalrlrdit lsyvlparlv
      961 srvvprgnls gfvtvtdlvl itnytgldpe snsnnpsvgg iggygidygn igrpigfnig
     1021 lrlrl
//
LOCUS       WP_090974736            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090974736
VERSION     WP_090974736.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124360
     Region          40..1117
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklriiidsc liyvllatve pmfatasvnp mtseiqqqri tgkvtnsqgq plqgvsitvk
       61 gtgvsvptga dgsfsiaast davlevrlmg yisrevpvag qamlsitled dvqmledvvv
      121 tgyqtvskrr ftgasatlka edvkrdgvtd vsrmlegqva gvsvqnvsgt fgaapkirir
      181 gassingdnk plwvvdgiil edvvnvsneq lstgdpstli gssvaglnpd diesfeilkd
      241 aaatslygar amngvivitt kkgrvgapvv symgnfstyl kpsysqfnim nsydqvslya
      301 emerkgwlny getaraangg iytkmaelin qydatngqfg lrndaesrra fleryayant
      361 dwfdilfnns fmqehalsvs sgteksqlyv stsylndngw skgdaverft gnmratftpn
      421 srlsygiitq gsirnqrapg tlgrvsnavs gelsrdfdin pysyalntsr altafdetge
      481 reyfrrnfap fnilhelenn tidlsfmdlk vqgelrysim nnlkfafega yryaktnqeh
      541 svhensnmpe ayradgdati raankflyrd pdnpeaepfs vlpyggfyli ndtylisynl
      601 rnsldysrqf ganhhirgyg fmelryadrq fkefngygyq fdkggtpyvd pnflkmviea
      661 nqdyysmtrr fdrflaygln agysyrdkyn magtvrydgs nlmgrtrtar wlptwnlsgs
      721 wnvdgedffa rqrvlsratv rasygltass gpatnssvvl rnasanrpyl teresviyla
      781 nlenseltwe kmyklnigad vgflnnrlsl tvdyynhqsy dliglvrtgg iggeavkvan
      841 yadmrangve atlngtvler snwkwtsqln fgynrseitn lknepniwsl vnpdggakeg
      901 yaqrglfsld yhgldsergi prfinekgei sgavflqdrn tnyliyegsi dplltggffn
      961 gisygnfrlt alvtfstgnv vrlrpafsss yseldatpee flnrwllyge qaepsildrr
     1021 evvdlvgsyp ynnynystar vakgdfvrlk qvmfsynlpt kylgqlgvnn lsvslvannl
     1081 wliyadraln gqdpeffgsg gvamplprqf tlslkvgi
//
LOCUS       WP_090974957            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090974957
VERSION     WP_090974957.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122776
     Region          53..116
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          126..1111
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrnllchty fiyvvmryss llflglafsl atfsytrada qhladikiel daknkplatv
       61 leqiekkskf hfvyntgtip ntvlsinlss dletilreig skthtryeqv gnnivvtytp
      121 pqepgkitgk itdtdgtpla ganirilels revmtddqgn initvppgty slqitfisyi
      181 pqrkenirvs agattaldiv lapatdelse vvvtalgikr aekslgyaaq tvgeesvtda
      241 rsnnwtssls gkvagltvqg agtgpmgstr itlrgessln ldnnqalivv dgvpvsnrit
      301 gtgfnsylsq dspvdfgtnv tdinpddies vtvlkgpaat alygsraasg aliittksaa
      361 gkkglgisvn snisfdqvnr wpdyqfeyge grtseyysyg asedgpntst tvaagrawgp
      421 kfdgqlyyqy dpntpdglpt vrtpwvaqkd yisgffqtgl tasnsisieg gsetggtrls
      481 vthltnkwiv pntgferina afstqqqvsd plkinarvny aykqsdnlpa vgynnqtlmy
      541 flilgtapni spswfkpywq agqehiaqrk pfnsgpdnpy aimyemlnpm dkhnmignls
      601 atyafsdrle lmvrsgldfa aenrsqqrpy smtkypngmy reqqvvnyes ntdflftytq
      661 ptggdfqfsl saggnymfqs yrfkgmnadr laqpgiyqla nsmdpvvsda dsynkaiasl
      721 ytfwrgsyre qlflditgrn dwsstlpqga rsffypsanl awllsetfal pqsfsfaklr
      781 lswaqvgndt gpyqtaryyn qiygngltns rvlfngnlkp eitssfevgm dvrmlnnrlg
      841 ldltyytnns rnqilatpvd pvtgftsali naglinsrga eavltakpis naqfqwtsti
      901 nwslnrsyvr eladgipsqi iynnanllti earvggrmgd myglgfrrsp dgqilynsqg
      961 lpesldrelr kwgnafpdwk ggwqnqfegv igdgvvlqpd gtyqkntvav rastfydnyy
     1021 qlanvetnif dasflkvrev rlayqlptaw lsrirvksan faiwgrdlfn ftdfpafdpe
     1081 tgnlnngtlt pgveiaqfps srtlganlsf kf
//
LOCUS       WP_090975214            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Parapedobacter
            composti].
ACCESSION   WP_090975214
VERSION     WP_090975214.1
KEYWORDS    RefSeq.
SOURCE      Parapedobacter composti
  ORGANISM  Parapedobacter composti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Parapedobacter.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Parapedobacter composti"
                     /db_xref="taxon:623281"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119924
     Region          22..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlyfilic lssfnqaaaq ntvngsvrae kdkqpitgai irvlqtdmvv hsnkdgefal
       61 tftgdtaeme itaigyerlr mtvartaksi tvllkehvtl ldevevytgy qslprerltg
      121 sfshidsetf nkqvgvdvls rleavasgla vdrgtsagei invrgintlt atmmgplivv
      181 dnfpydgdin ninpndiesv silkdaaaas iwgarasngv ivittkrgsf nqpitidfnt
      241 nvrvgskpnl syiqqisssd fidvermlfe snyytsqins vtrpalspvv ellirrqsan
      301 paeqeeidqs idrfrgydvr defsrymyqr svdqqyslnl kggserlawt asagmdnnmd
      361 nlgakfrryn vrfhntyrpf erlaltssil ythtvsgngr pgygeigrnd qyiypyarfa
      421 dekgralpid rdvrslwadt vgngglldwk yyplddykhv sqrtsvddil lnlganfrml
      481 egldvdlkyl ferqgtdinn lsgaesyaar ntvnrfsqid esgnvarivp aggildqryt
      541 rlesnnlrlq anfnrkwqsh evaaiggwel rssntsgsss rlygfnvrtl tsaqidfarq
      601 ypyinggslq lipnvtavsd rttnfisyfa ntsytyrgry slsasgrrda snlfglrtnd
      661 qwnpfwsiga swniseetff snrvvpylri ratygfsgni spsmvavtti gyqpvtnnft
      721 qgpmaffqsy hdpelrwekt gmtnlaldfr taknrvsgsv dffykrgmdl fgravldytg
      781 gigptvikna asmrgmgmdv alrshnisgn kvnwhtnfnf stardritey ylanrnannf
      841 vntpsnvqvs gvegkpvyai ysyrwagldp qtgeprgyin geisnnyaql tgsatqledl
      901 vyhgpatptm ygsfgntfsf kgisldfafv yklgyyfrrh sinyqelftn wvghsdfaqr
      961 wqepgdeaft evpamvypta fnknsfyags eilveqgdhi rlqyinltyd fgktdppagp
     1021 frrltiyanv snigivwran gqgidpdyns slrrtpppti yafgirasl
//
LOCUS       WP_090979346            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090979346
VERSION     WP_090979346.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117960
     Region          28..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkflrkis lplllmlvas tilfaqerkv tgkvvdqsdg sgipgvnvsi kgmpsnvstn
       61 adgvytiqvr nntdvlvfsy igyvrqlitv gsqnninvkl vsdnkglddv vvvgygtqkk
      121 tsltgsvstp nlktvedipa lnitsalkgt tpglsvsgga qrpgqgttit irnpvvfakd
      181 ggqgtnplfv iddiirtqad fdnldineve svtvlkdaea aifgiqgang vvmirtkkgk
      241 igapkfnisn slgvstatim pkmmnslqlg tfsndytnas ayiqtvpgvp vdkyinadgy
      301 lvtagvpass rtaawytpde leyfasnshd yfgdafkpay vwrtaanisg gtdkvtyfig
      361 gdfvnqnsnf kginshkygl rasvdakpak glvtslslna nvgysrsywy kltstsenld
      421 ndaaslqnvq pwqeyfingn pvviggsntg gndninffqi qnsnnytggt ntstnilakv
      481 tyeipgikgl tatatfnknl naannkqfgt sfvyykyagl gannhipggn ltgtfnvlng
      541 dkvrltpvfa dsyqinggfn ynrsfgkhni salalfeqre qnsegvnaea tglvagaldy
      601 qsfavgtsns nqsatvstfg fqsiisrfny dydqkylfqa ifrrdgssrf apgknwgnfp
      661 aasvgwvask esfiannlkw ldllkfrasf glsgvdntka yqylanynlg tgssggavfn
      721 gndnrtiaik pnlaipnadv twnkefktsy gvdmaflknr lsftgeyywn hgtdilttls
      781 ssvpatigan tptenytnan tfgwefsltw kdnigkdfsy sfspfytwmd nkmlkvdqsa
      841 aivgtvedvt grssdlgifg ykslgiirtq aeadaiiaqr aaaaggaanv kifgqalqpg
      901 minyedvngd giistdkkdq sfitnrqsnh nalglnwnvg ykglvlnvim glswggwtsi
      961 dglkpanqss satgasiynn rpvywvdhwt ptntdaaypn pffrtnfevt sdfwlvkats
     1021 fnitslnlsy niptrianki gmssvrvftv atnpiqfinp ypgkyrdlqt alysyptlkt
     1081 wsfglnigf
//
LOCUS       WP_090979771            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090979771
VERSION     WP_090979771.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114405
     Region          27..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mirllksiaf illlfavqlg faqntaitgt vksadgetlp svsifvketk qttisdakga
       61 fsinapekgt lvfsyigfkt qeiqiskngp isvilqssdn aldevvvtal giskekkslg
      121 yavqelkgqd lseakesnlv nalagkiagv rvtnsqgsmg ssrvvirget siagnnqplf
      181 vvdgipvdns qlnsagardy anaisdinpe diesisvlkg pnaaalygsr aaagvilikt
      241 ktgkskkglg ievnsnavle tlltlpvyqn afgqgsegkf syvdgagkgi ndgvdeswgp
      301 kmdgrlipqf fskgvavpfv ahpdnvrdff qtgyslnnsi svadagekyd yriaynnlkq
      361 vgivpnsgqg knsfvlntsl kitpkltlta nanysklssd nlpgtggsrs tstmlqftwf
      421 grqvdinqlk nyldengktf nwnnsyysnp ywvayentvs qnrnriigsl alnykiidgl
      481 dfnfrtgtdy yndrrkvria ygtngtpfgs ytesaftvne nntdatlnfn kqlnedfsle
      541 llgggnirrq yieqndqsap klaiaglynl knsrdplvss nnlsrlksys vyasgqigfr
      601 nylfanitar ndwsstlpaq nrsyfypsfn gsfvateafd iksealnylk irggwskvgk
      661 dadpyrlint yvfsapfygn pqlttgaidl npnlkpettt stelgleavf lnkrlrfdfs
      721 ayntnsynqi laadvsqstg fsskllnagk innkgieaql gitpvkkaft wdvdfnfaan
      781 rsrvieldae klltnyvvat nsaqviatvg qpygslfgta flrdgngnii vnatgapatn
      841 ptkqvlgkyt pdwiggvynt fsykgislgv lvdasfggsi yngtyatgty tgvlaytlpg
      901 raaeyggisy yypdnnkang tvrvngtapt gvtvyddgii fdgvtadgkr nekilpaqqy
      961 yktfrnidea nifdasyvkl revklsyslp akwlrplslq gvsvslvgrn lwiihrntvd
     1021 idpevafntg ngqgleslsn pstrsyginl nvkf
//
LOCUS       WP_090980333            1196 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090980333
VERSION     WP_090980333.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1196
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130992
     Region          127..1195
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnknftrply fllvvllafg aafhaaaqnq qislqqalda iskkyktkfa yehsivqgkt
       61 asiaslkaks vdealknvly pnnllflyvs egnytivsrd akglginaqt nlpegsasnn
      121 ssnefyisgq vtdensnplp gvtiksngsn ravttdgngk ysifvpnttt svsfsylgyq
      181 tsnlpvttnt nnlnasltpa asnqlqdvni vsngyqvlpk erstgaasev taedlkkipt
      241 pnvvqrlesl vpglkvtlns dnmftygntq qginsstral grsdynmeir gnntlrgesf
      301 plvvvdgaim eldlatinpn dianisflkd aaaasiwgtr aangvivitt kkgktaqapt
      361 isfsmtaaia nrpnlgylkm mnaaqtiaye qdlvaknlif apsatsalsg pvaeatdltf
      421 klkagtitqa aydsaisrls trdnrsqidd yllrpsnnqq ynlsvsgggk ssdyfysasy
      481 skenpytkgt egqrltlamn nnfklfkvat lsanfrasff kyktgavslt nllspsastf
      541 mpysqfvden gnrvaystay ysgwvdnlqn qgflnwkynv ldemdnvdns qnennynfnl
      601 nlnvpifkgl sanalfsner sfgytknyyn estfyyrnlv ntytpiptsg ravnsiglap
      661 gsgilnnmng snnnytlrgq lnydrtfgsd hqltmiagse irqtkagqgt svlygyntgn
      721 gisravnfft pyatvqgfnq gltgnptqqd kvrrylsyys naaytykgky tlsgsvrydd
      781 ynnfgvdrkf ratplwssgl kwdakkesfl knenwlssls lratygvngn istntypftw
      841 islgsgdlat glpnasiiap anpelrwekt nvanlgidfa ildnrlsgsv dvyskrgkdl
      901 fyefpingty gftsifrnta slsghgmefn lngtmirekd yewnaglnfa yntneitdtr
      961 fivnssflsn pafggvpldg yatdkifvfr nagldanglt qvydqngnkv aanqnvtsid
     1021 alayagrktp pyfgsfntsf rykaftlmav atyqfgnvfm rptisaypss rtgtkydlhe
     1081 ditkrwtkag deaftnvpga agalaptsll ryqqsdinvl kgdyirlrel slsyqipvek
     1141 lkfmraanvg fsvrnlgliw kankegldpd fagslnastl glpspvsynl slnvnf
//
LOCUS       WP_090980368            1150 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090980368
VERSION     WP_090980368.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1150
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126951
     Region          127..1149
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksavtsql ifsvmrfftl iyimlstmlf vgqaspvnaq qldvkvsini kkgsltelfr
       61 tiekktglyf vytnkdaiek qnlsgfkaen eavsalldri lppfqlsyli eknqiiikks
      121 irikgkvtdg kgmplpgvnv iekgsnnats tnlngefnln vlnsqallif kmigyqsrei
      181 alkgetelni nlapdetals dvvvtalgik raekalgysi atvkgsdvnt vkevnvinsl
      241 agkvagvnvv sigadpgsss fitirgqssi atdnqplfvv dgvpvahslr atsevgrssv
      301 dygspiadis pddvesitil kgasaaalyg sragsgvvli ttksglinkk glginfnsna
      361 mydqawmfph fqhtfgggey tddqasstts awgprldvgt khlqwnspld asgkpiatdw
      421 vshpnnpqdf yetgstytnn isisgknadg nyrlsytnls nkgivpntdl krntlnlsat
      481 yvlhpklkvs tnigyvnnks dnrpsayres vtqmlyslpp nmnindlkny wkpgrenieq
      541 fsaddsdnpy fvayehtngy drnrltgniq vvyditknls lmartgldmy neehetkrpf
      601 sskrfkfggy gvdnsffkeq ntdfllsykk llnqdwslsl saggnqmnqt nrftaqktes
      661 lsipgvynia naqagtivns qyisrkrins iyglgqvsfk dmvfldvtgr ndwsstlpag
      721 nnsyfypsas lsttvtdvfk iksdvlsflk lranwaqvgs dtdpyqlynt ipfnqdwgdv
      781 kratiefnlk nnflkpeiat syefggdlrf fksrvgvdvt wyktnkrnqi inipttiasg
      841 ssnrlinagn iqnsgweigl navpfdgafk wetnvnftkn enkvialseg lkeysmgsad
      901 gdnirylike gtkigdfytp sytkvasgpn agaalldktg hyirnnseyl kvgnynpdft
      961 mgfnntfsyk nftlnvlldw rkggnfysyv vkslinaglt dntlvgrdae tgglawtdsq
     1021 grkrndgmii pgfiadangn ltqntvviaa sdfynntynk yyerltypas flkireaslt
     1081 yvfdkklirk lpisnlslsl igrnlytwta nglgydpett msvtegfklg vghwtlpgtr
     1141 sfgfklscnf
//
LOCUS       WP_090980539            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090980539
VERSION     WP_090980539.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118193
     Region          31..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmmkilmlfl vtlglcsgld agaqapvgef rgkvvsadgk rplagatvkl egsdavvltd
       61 qtggfvlkgg lvkgtllvsf lgyapariqv sgdrpvvvtl saaaaqldev vvstgyqtvp
      121 keratgsfvq vdnkllnrrv stgvldrled vtpgllfnrg rsagaglisv rgqntiygns
      181 splivldnfp ydgdintinp ndvesisvlk daaaasiwgs ragngvivit tkkgrynqkv
      241 kvgfnanvtv gdkpdmfyqp rmsaadfigv ekmlfdkgfy asaetgynnp altpvvelli
      301 arrdgkitaa qaeeqiaala ghdvrndfdr yfyrksvnqq yalsftggsd vqrfnlsggy
      361 drnqdnlvgn gldrftfngg qslnllnkkl eistgfyysq shtvnnnpgt gliglntgsg
      421 vslypyarla deagnpiamt hdyrqgfiqa aqqkglldwg ykpleeiyis dktrklidyr
      481 lnvnasykir pylsfsllyq ygqtmadarn lrdertyfmr nlinsysavd asgkiayaip
      541 rgsvldldql tatsqsirgq lnfnrvwmdk hsltaiagye irdfhsvans nraygysdsh
      601 atalgvdyvt lfpqyavtgs lmsipfydsm tdltdrnisy ysnaaytfld rytlsasgrl
      661 drsnlfgvkt nqqgvplysa glawninkep fyhlewlpyl kmrltygyng nvnkslsaft
      721 talyltgnai nttyaqvnnp pnpelrwerv rmvnlgidfa tkdnrisgtv epylkrgmdl
      781 igdiafapss gvttfrgnta ntrgsgidis lnsrnivgrf swqtnfffty vkdkvvdyal
      841 rqpagryaql sdsevyplqg rpfyavysya fagldpqngd pqgyldgkvs kdynqllssa
      901 svdnlvyagp arpvsygalr ntfsygqfsl sanisyrlgy yfrqpgifyn nilsgqgylq
      961 gryserwqkp gdeeittvps mpagintard sfynfstatv ekgdhirlqd islsydfgkr
     1021 llgaislskl qvhlyannlg ilwkstktgf dpdypvadyl qvrtvavgik adf
//
LOCUS       WP_090981235            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090981235
VERSION     WP_090981235.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114854
     Region          23..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfm flclatagya qdrtingtvt aaedklpipg vsvkisgssg gtvtgadgky
       61 slrvsgsatt lifssvgfvt qtktigsstt vnavlisdat slseivvtal gekrearalg
      121 yaateikgek ltiakntdis talagkvagv qlngspsssf dnasvivrgi ngftvgsplf
      181 vvdgtpadqa nvnmdniesi tvlkgaaata lygqrayngv vivtskkgsr kagtsieins
      241 glaiektsll pdyqneyagg ytgqfekfvy dpaihpatwa afngqnmldy gadasfgpki
      301 dgttlyrpyy swypgedfgk lvpltaqpnn ikdylknggs ynnsiaftsg gegynlrvgy
      361 tnqtrslvqe nanrsmniln vngsydvskr ftvstdiqfa kesrigqpye tyrndglnvv
      421 qgfnqwfqrq ldmnylrdhq vladgtvtsw nignpngtgd lneittpqyw dnpfwvvnnn
      481 yrtqrnnrlv gnlglkydlg sglalagflr gninnesgde rmatgglqqd yfktrnwtdt
      541 efnyelnlty nktfgdftln alaagnirhe kreridmata gglsfpnyfn iaaslarptv
      601 tndyyekevr svfgkaslgy knflyldvta rndwssvfap dlnsyfypsv sgsfvfsefl
      661 ptsvknavsf gklrlayaqv gsdvdpyrvn lqyntspayg snpslaigne frdgrlipak
      721 tnsfevgtem kflknrigld fayyinknkn qilavtlnga tgytsnlina gdltnrgfef
      781 sltgtpvqsk nvswdltvnf sksktivnki tdkqtnviyq tstffgntln lregeewgyi
      841 lgrtwnrdan gnviiaasgl ptsttnqfig yarpkfsggv ysslrvfdfd lgfsidfqkg
      901 glfnsttraf nmgsglsqet vgvndkgidw rlpvaqgggy kfagvlangq pntryvaast
      961 afyngmqtgs gelfmisasy lklrevrlgy nlpskvlaks gflksanlgl vvgnawlisa
     1021 pgkkygvdps eienfwqegg qlpssrtfgl nlrvgl
//
LOCUS       WP_090981721             958 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090981721
VERSION     WP_090981721.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 958)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 958)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..958
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106849
     Region          58..955
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqikiisal clavafllpa agsaqtnrqa rknnksvnks eerqsqdtif vmpqvdsvqv
       61 afrkvakrdl lgdvsainls qmleknytts slegldallp gfngniwgmg gylvlvdgip
      121 rdinnimpte idqvtvlkgv navalygsra akgvlyittk rggnyeqkvn vrantglnvp
      181 ksypqflgsa eymtlynear rndglpdlyt qqtiynyasg anpyrypnvd yyssdylrns
      241 ygrndltaei sggnnrtryy tnlgywsigs llnfgeavkn sganrfnvrg nidvklnkii
      301 slnvdatasf ytgkgvntdy wgsaatvrpy rfaplipism iepgdvasla qannsnniin
      361 gsyllggsql dqtntfasiy aggynrnvsr qfqfntginf dlnslmqgls fktmlavdys
      421 safnqsynnt ysvyeatwnn yagidqissl tkygidarsg vqnvsgsayr qtisfsgqfn
      481 yartfkqkhn vtgsllgygf nisessvyha tnnanlglql gynydhryya dfsgayvysa
      541 klpianrgaf sptlslgwrl seeaflknse ivdqlkvtas agilntdldi nnynlyqgyf
      601 tyndaawysw rdgglvhtfd rrrgdnpnlk fpqrreinig legsfyknli nftasaffsq
      661 mrgnvvqpgv lypsylttgf pvysdipfvn ydndqrrgfd fgirmnkrtg eidwtlgvtg
      721 tyydtkatkr aesyqfdyln rtgkpldalw glqsmgffts tadiaaspaq sfgqvkpgdl
      781 kykdqngdgi idtrdevylg kggwmgapmt lgvnltakwk nltlfvlgtg rygakamkns
      841 syfwvdgedk ysvvvrdrwt petqatatyp rlttansdnn frssdfwlys tnrfdlskvq
      901 lsyqfpanlf rngfvrelgi yasgmnllti sperdileln vntspqtrfy nlgvkalf
//
LOCUS       WP_090981242            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090981242
VERSION     WP_090981242.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113952
     Region          23..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfv llffattaia qertitgtvt saddklpipg vsvrvkgtqs gtvtdasgky
       61 svrvpagstv idfsyigyta qsrtigsast lnvslvsdsk alsevvvtal gitrqkkdlg
      121 yaatsvtske itqakavnav nglqgkvsgm nitttnsgvf envkinlrgi rsltgnnnpl
      181 llldgvqsdi nylssinpnd iesvnvlkgs agaalygpda rngvivvttk kgsrddkpvi
      241 tlsnstqftn isffpkfqek fgsggggeyi pyenwswgpa ldgstvelgh qlpdgttqtt
      301 dysakndrkk ffntgvtiqn dvsfaskdfy lsfqdanikg ivpddknrrt girlntskey
      361 grfkvavntn ysqqnynvfd daamggynaa nnvglngglm nlifntpvqv pltsykdflg
      421 dkfstynnyf ndyglnpyfa idnwrkngkr edfltnvemn fkaadwlnft yraaitnqti
      481 nerrsskgei pnafglsrsf klipgaieer sfkntrlsse afasankdlg sdfklsailg
      541 tyyrqdeard trigasslvv pelfnvenrv gqltgsspyr rsrllgfygs vglnykgwan
      601 ievtgrndet svlslnnnsf fypgvngavv ltdaiealkn nkvlsylklr sawnktgnad
      661 ispyllaatf sqpagfpfgt lpgytanntt ydanlkpefi rsfevgaeag fingriniea
      721 tyfnqkmtdq iipinvsatt gytsafvnaa sfvnkgveld lkltplvdlg dvrvnfrana
      781 tynennvtsv ysgldevlig gyvnasnyvv kdnpafvika tdyvrdpqgr vivdrntglp
      841 tqdptakifg qtmpkwilgf npsvswkgln vsalfeyktg nyayhnigpd mawtgvgyat
      901 asnnrqpfif pnssianadg syspntnvti nnsenfytgv yrtvgtnflt saaswrlrev
      961 aigyeipvkv lgnqkvikgl svaltgrnla lwlpksniyt dpdftytdtn tsfgvgssgt
     1021 asnnrngisd stinpptrtf ggnititf
//
LOCUS       WP_090983151            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090983151
VERSION     WP_090983151.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113355
     Region          62..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrylwaclaf faaftlnvlp nyaaskkkyk gltinylifq dttkikivsp kdslrkdsle
       61 qirkktlynk lsggvqkdtr dlaifpaisl qqnlkgnfag lyvqepsgep gsmqnmfirg
      121 aampllskkd lydaqplvvl dgiplvrehp fafdiqqfdf nrigpatnll agidmnnias
      181 vevlkdlgst siygprgvng vivltsktav gkyraisfns yigmvqkpfv ntingkyend
      241 frqrfygvyt tngrysddee ypvylsdsln nvysgksdwt dlyyknalvy ginfslaggt
      301 dranfrfalg ntksegvade tgidrysatf ninmkptkwl lfstminanr lnrdrnktlr
      361 drfaqlnyfp dlsaplppnk dfygsylqqy kkgfddnktn siqgyakleg tfgqfkvtss
      421 fnadysegyr dvfyartllq gnsyasnyyg fsqrlmmdnk vtydmnlnki hdfhfalgqt
      481 mqwdiykysn ayaykgvndy ikinlldskp knddgsdngg yltpvafpre ltyrfldkte
      541 dnllsfygka nysfadkyfl sailrldgss naqptsrwfy sptisaawsl kneflkensl
      601 vddlvlrasa grmgrtfsyd nytqgpqyta svgytgnltv pgynafgvlt rpyqfgwvgy
      661 gvpwsysdql nigadvamlk nrlhvsvdly sktdknqlig ipayaeygyk qaiesgmsvn
      721 nmgvdftlsa qviakskfsw nsalnfnhna nklkalprgl gqlvvgnrfl kvgqpvdqyw
      781 llenngiyta dadvpavngq klkykgivlk agdprwkdqn gdntiddndk glkghalptl
      841 sggfdnnfky gnwslgtsfy fnlgrklinq emanrfdfvn regntdissv keitfwekrg
      901 dyskyplynp wstvipyrad qdlflenasf lklrqvslgy elgnllskkn ikinkffvyg
      961 avsniftitp ytgqdpelvn ydgidtgygq piprtytlgv kmdl
//
LOCUS       WP_090983153            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090983153
VERSION     WP_090983153.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115950
     Region          28..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnillytl livciicctn aysqekniiv ngrvldkdtk qgvpgvsvil qstnkgltqt
       61 ngdgkfsvnv pvgetllfkf lgyntasaki tgqtnitvti senrkdlndv iivayqnrpk
      121 ettagsvqvl gakdvadvpv snietllqgk vpglniqnnt gapgfrgsvq lrglsslsis
      181 gsgndsflqp tsplyiidgv pldadkaaef gfqtqgpgvs plslipqedi eniqilkdaq
      241 atsmygsrga ygviiittkr gnskvpriry vsnffvnapp klretlggns erqlkiqqii
      301 lnaetinqir gisntpflad slnayynnst dwqdvfyqtt fnqshnlald ggdqkfnyka
      361 nmgyyaekgv ikntgynryn lnmnmefkpn dkfrffgfvn gsvgkqnkgn gagllqsgva
      421 angqastllp ppsfyqasgg vlsalqtlnd nnsrnlrani daryefipgl aasstlsydy
      481 tsdtettftp aaangsfakl ydyngrnfql ynrnaityak tlgekhnifi ntfneiyklg
      541 aqssisrqer ipndqlqgpl gydgyysrgg gvlgtyknat iasfagslsy dydkkyvaef
      601 syrldgtsss glenpyskns siglrwnfnk enwlidqkwl dygslrltwg qnivptgnlq
      661 siygiynlng nynntqtigi nydlipnpal kptttsqyni gfdigflnrf sivvdsyfkk
      721 vdnllfdrvl snttgfnkla sndlgianyg tevnlivkai tskdfdlsfs ingaynrdvl
      781 lklpaeyngq yirfdgsgyl qhnvfrvgrn tlsnylrinq gvyktdadvp vdpvtgkryq
      841 tnntffyggd pilkdvngdy ildgrdyeit gnsqplltgg lsltmrykkw glnvyasyta
      901 drtilnnala driaimrdpy alnavvplgd lniwqrpgdv akypypydfs rygniqplra
      961 dqtlwqesgt ylkinnltls ymfdkkmiqr yglanlrifa stnnlitfsk ysgpnpenvt
     1021 slgrdisngy pvprtynigl nlelntgn
//
LOCUS       WP_090983599            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090983599
VERSION     WP_090983599.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112100
     Region          24..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklllifi gtflllahaf aqqitvtgkv tsadgpipgv sirvkgstvv aqtnadgnys
       61 ikalktdvli ftyigyatve rtvgnnasln vvlkdnvnsl nevvvtalgq qvskkalgta
      121 qqqvkgqdla dtqrenfvna lqgriagvev tsssgvpgas ssitirgvss isgsnqplfv
      181 vdglpidnkt lntsafysdn ssttafsnrg vdftnraadi npedieslvv lkgpeaaaly
      241 gidaangaiv ittkrgksgk gsinysnsfr lektrtkpei qgvyglgtng isgpgtlqyf
      301 gpayapgtvl ydnidgffqt altqkhnlsf dgggqdmsyr istsytaqng vvpnsnydrf
      361 tlngstngkl nnwmkvdlsm tytyalnnqp fkgsggplig lllwpqedda rnyltaagtr
      421 rrfttatdlt seienpyfnv nknkinsiqn ritsnfgfti tpvswlnfks nigfdvysnk
      481 nlllshpess rgfnkqgimd vandntrnvn iqnllnltkq kitsdlsida tlgnaiqdlr
      541 snidaqygeg fldpnfisin nttttlrnak ssisqrrlfs lfaratlnyk dylyitatgr
      601 ndwtstipig ansffypsvs gsfvftevpa fkealskvft sgklraafan vgkdarpysy
      661 vpsleskatv gggfgygftg pnlalrpefa ssyevgtela ffkdrlgldf ttyrketsdq
      721 ivndirgsya tgyvlfnlng aktrsegiev tlrgtpiktk dfswnalvnf esarakvlsl
      781 pnelpesyvs dtnvygtirn gttpgystrs ltgtfylrnd rgdilinpvs glpvrssvvi
      841 qgpgkgydrq pdfsigitnt fayknfalsf lldirkggdv lnatqsfltq rglstmtldr
      901 ltprivtgvi qdgkensanp tinnisvtpf yqntyytnls eelfiekdin wirlkdvtlq
      961 yklpqtifsk qnffrsasvf vtgtdlflit nysgldpvvn gntaavggsg ssgidygnfp
     1021 vpiglnfgvk igl
//
LOCUS       WP_090983820             954 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Pedobacter suwonensis].
ACCESSION   WP_090983820
VERSION     WP_090983820.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..>954
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          55..949
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknihilill iglcpliafg qesfsgkils aadstalpsn ieltgaggla fkthtdakgm
       61 fllrlpagty rfvatavgfk tyavtvtvpl trafvvslqp adnqlnevtv stgyqlldrt
      121 ratgsfdkld karldqqvgk nildrleaig ngltfdrtts asgkfsirgt stirgprdpl
      181 vvvddfpyag dlaninpedv esitvlkdaa aasiwgtrag ngvivittkr gkkntplavn
      241 fsgsigfaqk pnlryeqris sadaldveqf lfgkgyytsq inssqkpalt pfvellilna
      301 agklstadle qakagfaahd vyddfesyvy ktgvnqqyal slsggsekha wlissgynhn
      361 vdnldglnar qnlrlsnnft llrylnlntv fsytggkvta grpgiggits ttslypyaaf
      421 adadgtplpi tknyraayla spavaqlldw syypllddqy tdnvtrltdl magfdlgykl
      481 plgfklslky nieeqrtnre vlqglgsyyt rnlinsyaqv gtggavtypi pigaildrne
      541 grlrseqyra qldynrvwav hridalvgve wrkaqstgvs grmygvdtdk lntgsvdytr
      601 tfpnsvtgsa ayipdgngls qtannyfsqf vnlaytfkda ytlsasarad asnlfgvatn
      661 nkwkplwsvg lgwdmvkmpf fkvgfvdqlk lrstlgfsgn adpsmsgvnt iryqvnspyt
      721 qtpyaifdky anpelrwetv rmlnvgldfs mfkarlsgsv eyyqkhasdl fgiypidytt
      781 gvgttvlrnv aeikgngldl qlngrilqgs ftwgstlnls vykdkvaryy lpsvqgsnfl
      841 qanatvsgve glpvysifsy rwagldgatg epmgflngqp skayssiisg tkltdlvfhg
      901 palpryfgnm vndfgckgft lsvalsfkfg yyfrrkgidy tnlfangsgh adfg
//
LOCUS       WP_090984744            1108 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090984744
VERSION     WP_090984744.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1108
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121723
     Region          25..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkmylrcls illlcfitis afaqknvtgt vkdasgplpg vsvsikgtsk vtqtdasgkf
       61 sinvqqndil vftavgfrrn evtvngqnsf sitliedana lsevvvtalg vkreakslgy
      121 avstisskei tqagatnfas amygkapgvr iasapggats gvninirgvn sitnktqpli
      181 vldgvpirdg eyanndywgd qrmrgnglld innediesis ilkgasaaal ygseavngvv
      241 littksgkga kgfsvdfnan ythdkvaylp ryqnvrgpgi dpfysnagqa adgfiyqdld
      301 gngsketrgv gafsinfgpl fdgkptltwd gqirpyeaqi dnyakffqta nnsnvnvais
      361 nttdnsnirl sltrqdnqgv sygtknekni anlntsfklg krfttdlivn yinqythnrp
      421 fmvdrminnf tgmigrfdnp ewynarykts rgykfvtgtn qsltpsenii ypgfkadvad
      481 yiwnvrenne nefsdriigs ltntlsitdn lklrarvssd itsqktetsk pnevpiafnp
      541 nsgffglmny nskilygdal ltyskkitkd igitamggyt atretynsvq retngglsve
      601 nwydlsasnn matfnnglny rrtlvkdall gtlnasfrdy lfvegtvrrd rtstmnpnen
      661 sfvypsvnsg fvfseafklp eaisygklra swgivgnyps iylanvaytq ntlgtqggsn
      721 svlyttipts fgnelikper kkelefglem rflkdrlrld msyynaqind qilpltipss
      781 sgatsilanv gtlrnkglev alsatpirtt nfswnstinf snnknvvekl angateliha
      841 dydgnaaqlk sivgqpmgdi yvhpiardan gnaiinsdgl ykidannmik agnampkvig
      901 gfinsfaykn fsmdivmdfr ygghvmptgi nwmisrgllk eslnymdtes ggltyyrnaa
      961 gigiqttgtq gpngekvyhd gmlmqgvlen gqantnvisq syyywntynw ggpqysssry
     1021 elyviknnyi kmreitfgyk ipvtvakkig aknlqvsafg rnlfylyrti kdldpeqlts
     1081 gsrwtqtitn agsnpatrtf gfmvragf
//
LOCUS       WP_090985475             940 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090985475
VERSION     WP_090985475.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..940
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103475
     Region          51..939
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtryikcsgv mlciisyllt ctafaqtngk qdtirvrkan ytdstdklie ipfatrsree
       61 lnyaqsslry nqltqvpisn lsgllagrls gflfrwtgnq pgggnvsyqi rgkssyaqga
      121 tpaflvdgie rdfedmdise iesvtvlkda aglnwyglng gngailvttk rgkigenlis
      181 fdaqggfqsa gnlikplnsy dfatlynrgl tnvgqvpayn daaldgyknh tnpylypdnn
      241 hlerflgkra atqryaltfs ggsnrvryfs svsyfnqqgl lketetpnyd snygykrynf
      301 rinldydvtk tltltllagv rsevrndvgd gtstvlsnly nlppnafpil nadgsyggts
      361 lfqsnplgql qstgfsrttt nillasimad qkmdfitkgl sanlffsydg ygnygdglsq
      421 nyavfnqtvt pvqtyrtpav iayrtaafqt ntknnelwfg ldynrtfatd hqvkanvraq
      481 qyvsaavdrl dyrsrmivgr adysfkqryq lgftgsysgs enyapgrrfg ffpavsagwl
      541 iskedfmkda svisylklrg sygrsgnigp tydangnvvr lpyrtlftrd agpflgstfs
      601 tsttarlvsp agnplttwek idrlnlgtdv dffkgalsfs vdyfdekrtd ilgpanlpgi
      661 lgiaiaqvns gkvsskgfda sgtfhkkige vqistnanft yakniilert envlpnqsti
      721 gryvnggnyy iaegifqsqa eintspkqtl sslvvpgdlk yrdvnndnvi dandaissdy
      781 tdipkiyygf gfnirykqfd lgaqfqgvag rtvdvsdivy agpnglnqls ldswtpataa
      841 takypriais dngnntanst fwlysgnflk lrsaeigyst pqslnqrlrf kgarifvsgn
      901 nifsisklge lgidpetpna grfssypyvk tfavgltvkf
//
LOCUS       WP_090985554            1201 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090985554
VERSION     WP_090985554.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1201)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1201)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1201)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1201
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1201
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133440
     Region          120..1200
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnlyfrfvr tgrsnllnwl allclalffs lnvnaqnnqy kffqaplntv iaeiskktsy
       61 efvydadlvk kakpitfnla tpdirtlmda vtkgqdftye isngrtivlk nrsedvseyt
      121 lhgmvtdsig gplpgasvkl kgttrytmad gnghfniglt dqynaleisy mgylsqtqki
      181 dkaaasnilt irlkpnssll advvvngfqt iskerstgaa tkinndklne ninsdilgal
      241 egrvaglvyn knpnrigadq pvlrgqatfn llggsaplvv ldglptetal edinpydves
      301 vtvlkdgaaa siygsrsang viviatkkgn tplkislntd ffidtkptfg smhyastadi
      361 vdfetdvynk eraryantet mfaaygtvan gsikyysply qlfrdrdagk vttdqfnqql
      421 nnlkntdyye qyrdnvwqna frqrynllls sansksntfa sinydrsaer vignhnqkit
      481 lyfkntynik kwlstnigfn gaystststd dsynyyntis pryasivnpd gslvysnyvn
      541 ladgiagspi ngavagalln tpqykpyrfn ileslneglt nantvalraf tnvqakimeg
      601 lsfssqfqye mgttkseqiy dvnsykmraa ynalvaftpa tnaytfglpa ggrisqnmqq
      661 rnsytfrnql sfdksfdegk hsiaaivgte mrqtflpigm ndirygydpv tltstvinna
      721 tvsqtglpsy ifgrnltlgi agrsfqetkh rnlsyfsnas ytylnrynvt gslridqadf
      781 fgadpefkyr plwsvglgwn asnekfiesl gwinllklra tygvngnqnt ettkfltarr
      841 vndnlftslq ylniiglpnp klrwektety nlgldmaflg nrlrgtidfy drkstdlmvt
      901 tdldptvgaa slvinngvlr nkgieftvng dwlksgdlml sstfvlgfnr skigkvnral
      961 staanyvgsp styytegtdy ntlyayrygg mingypyfld engkstldfd vngnpivass
     1021 rdinnyaalv dmgsliptyn gsfsqrisyk nfelnallif sggnvmrkdi tplgandisd
     1081 lditqrykng itpelprlfv dyseaminra ssistmwqka dvnvvkadyi klrtislgyn
     1141 lpksfikkfn ipsakftaqa nnlwyasaag ddidpesysl nsgtrtlqnp ksfvlginlt
     1201 f
//
LOCUS       WP_090986364            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090986364
VERSION     WP_090986364.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116917
     Region          31..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekistrhcy vkfltatlfy llipwlafaq ktikgtvvdq tntpipgvsi iekgtkngta
       61 tnaegkfslt vqkegaivta rivgyrsvek tvsasgtvnf sleednntln evvtigyqki
      121 trkkttaais sisgkelanl paasfdqllq grlsgvnvqn ftgqpgvapt vsvrgnstgs
      181 tgydqfnvir splyvvdgvp qssddlvppg tgtgtnymag lnpsdiesid vlkdasaaai
      241 ygsraangvi littkkgvgg dtrvtfnsyy gmvqrpnlrq atmgtterrq kmevlqrqls
      301 ydqrvqlpyi ltdslnpafn ghtdwqdlfy qtgkindnnl sisggtdngt tyrfsggyyd
      361 edgivkgtgf kryttrlnlt sramnkklmi npifsyssas rgrgnedpnd pskptkvgsg
      421 nlpsslfnis pekldyfvsk dgenlnrnvs nqflanlnla yefnkhftln sqssytnnnn
      481 rrdvsmsnll nngfgnssss fsstdmglrt snylayngsi kkhsfsavag qdieyslfqs
      541 tqasgyggas dniqtvtgfk qqnifaysny iahglvayyg rfnydydsky llsgtirtdg
      601 ssgfgennky gvfpsisagw llseenfmkn lsnnpftlik irgsygvtgn edkrnayvqy
      661 ntyqvnngyf sgnggatsyn gvtaitpnfr ngvaqkdlsw ekstqwnigt dmeidngrya
      721 isfdvynkev kqklfnvdlp vtsgydnaft nafavrnagl eltltanplr kefkwnssfn
      781 isynknqims lpnggrdiil sgdrfdknhv lsvgsplnaf ylyrtkgvfs tsadipqnpy
      841 tgeryrnsng tfsagdfyla dldgdyfidi fndginpdka pigdpnprft ggwtnnfsyk
      901 nfslsvfvnf tlkrdvlnlf dsdrftnatd anavynfasv sspdlsrlni wrnpgdqaey
      961 akldlgsyry yytaaqsffl ekggyarirs infsydfspk avrklglsql klyavvdnvy
     1021 mfqqskklpd aeavngygey ngtgypiprk ytlgvqvqf
//
LOCUS       WP_090986926            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090986926
VERSION     WP_090986926.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122925
     Region          129..1136
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrilylrrva ghscltlmfc actlfcsaql larnvahvng ikaqslsdnk lslktalqli
       61 ktrfdikiay kagilenkds nltetqlmaf gdaktaltfa lngssldfnk isesqyiiin
      121 tqagnaadvi kgtifsasdn lpligatvyi kgtktgastd aqgqfsitip nelagkpitl
      181 siasvgyetl efpvndfktp isiklkesas slndvvvtal gikrdskalg yavtevkgse
      241 ftqarennva naltgkiagv natglstgpg gssrviirgn gsfngnnqpl yvvngmpidn
      301 svpggaattn glatnvdrgd gissinpddi esitvlkggt aaalygsras ngvilittkk
      361 gvkqkgigve ynttftiena indndyqyey gqglggvkpm tkndaiatgr lsfgakidgs
      421 dyvaadglth pysavkdnik nfystgtnft ntiafsggtd giiyrlslsd ldskgiisst
      481 rfkrqtanln inakitdkik veglaqynle kgfgrtlagd algnpnwtpy evantvdvrw
      541 lapgydaagn qtpwndagia tngyfvinky qqndvknrfi gqgsitydiv knfqlkgvis
      601 rdfynynyvn ilptgdiyip kgqysgiksd vsetnslitg nyknriadki gisilggans
      661 rrfenkqlnm dgntftipff ysyknlatss tiptyqrirt nsvfgsadvd yksilfltyt
      721 arndwfstls pdnnsilyqs vggsfvvsda fklpssidil rvraswaevg ggaadpyrin
      781 lsysnvpssg qplqnvttnd itnpnlkpyt sttyeagvel kmfkgrlgld ftaysrkttd
      841 dilnaaisst sgynnavlnv gelsnkgief lltgtpvqgn kfgwnisynv aynksevlkl
      901 vegtttfema rtvgnwgyin qtvgsaygti vgtrmlrnea gqivynsttk rpvatglqel
      961 gngvapltmg ltqdfrfgnf nlnflidgkf gnkvlsikev yatrlgllks tlpgrenglt
     1021 isgvdqagnp ysalipvsdl rayyndmrny selfvhdgsf iklrqailsy nipvkkldfl
     1081 kiqsasisfv arniltfykk tdnfdpessf tngnaqgfes iglprtrtfg lnlmvkf
//
LOCUS       WP_090986965            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090986965
VERSION     WP_090986965.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113419
     Region          52..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkllplvf tctvfmlfll fepmfasagg pgtadfsktv tgkklkiafi gitgkvtdeq
       61 gvalpgvsva ekgtrnaivt nssggyainv annnavlvft svgykpveis vnaktvinvs
      121 mvaitnalne vvvtalgikr eakslgysaq kadvqalqtn rttnlanale grvagldvsp
      181 paagpggstk irlrgqssft adnsplivin glpmsqgass sngytqnvdq gdnlqginqd
      241 diesmtvlkg staaalygsr avngaiiitt kagskntgig iefnsnftvn qaldftdfqy
      301 eygqgennir pssqgtaqss gawsfgvpfd nvptyqfdgv qrpyapvkdr ikaffrlaps
      361 wsntvaisgg ndkgsfrvsl snqdaqgivp nndfhkkifn vginykltdk lsaqfyvnyd
      421 hqfnnnpplv gvqgnsipts iyrlansisf dvlkagaida ngnetptsrf atitnpywil
      481 anqfqrqtkd hllgtavvry qffdwlylqg rantdllqtt yesntptgtl avsaapagly
      541 ngsygisttn trqnnfdfll ggghkwkdfs fnatvggnnf plitstfnes vtnfyirgly
      601 tigngvtans synlskqtvn slygtaefsy kdlfylnvtg rtdwysvlsr didhyfypsi
      661 sgsfvfsell pnakwlnfgk lrvavaetgs aqgvgpynal tfalaqnsfn glplgsingt
      721 aspntqikpf gvnekeigle lhlfnnrvnl dvaaydkktt nqavpislsa asgysttlvn
      781 lgglenkgle fnlelipvqn nkftwktafn safnsskvls lannqsqlvv gspeffgsiv
      841 dvvglplnqi rgatykrdaa gnillsggkp iasatpvnfg sglpkatggw lntlnykgft
      901 fiahidykag gkllsstsln llreglskes lpgrvggvif pgvnatdglp nttavnaedf
      961 yasyrstnil dpfiysssfv klrnlslgyd lsrfinkkyv ksmvlsavch nvliikkytp
     1021 nidpeaiass gdnltgyeqa slpttrtygf nlnikf
//
LOCUS       WP_090987209             945 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Pedobacter suwonensis].
ACCESSION   WP_090987209
VERSION     WP_090987209.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..>945
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          23..>85
                     /region_name="CarboxypepD_reg"
                     /note="Carboxypeptidase regulatory-like domain; pfam13620"
                     /db_xref="CDD:433354"
     Region          55..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkiyiliil igfcpfitfg qdtfsgkils aadstalpsn ielagadgla fkthtdakgm
       61 fllrlpagty hfvatavgfk tyaltvtipl trafvvslqp adnqlnevtv stgyqlldrt
      121 ratgsfdkld karldqqvgk nildrleaig ngltfdrtts stgkfsirgt stirgprdpl
      181 ivvddfpyag dlaninpedv esitvlkdaa aasiwgtrag ngvivittkk gkkntplavn
      241 fsgsigllqk pnlryeqris sadaldveqf lfgkgyyasq inssqkpalt pfvellilna
      301 agklpdadla lakagfaahd vyddferyvy ktglnqqyal slsggsekha wlissgynhn
      361 vdnldganar qnlrlsnnft llrnlnlntl fsytagkvta grpgiggits ttslypyaaf
      421 adadgnplpi tknyraafla spavaqlldw syypllddqy tdnvtrltdl magfdlgykl
      481 plgfkaslky nieeqrtnre vlqglgsyyt rnlinsfaqv gaggavtypi pvgaimdrne
      541 grlrseqyrg qldfnrvwps hrldalvgve wrkaqstgvs grmygvdtdk lntgavdytr
      601 tfpnsvtgsa ayipdgngls qtannyfsqf vnlaytfkda ytlsasarad asnlfgvatn
      661 nkwkplwsag lgwdmvkmpf fkagfvdqlk lratlgfsgn adpsmsgvnt iryqvnspyt
      721 qtpyaifdky anpelrwetv rmlnvgldfs mfkarlsgsv eyyqkhasdl fgiypidytt
      781 gvgttvlrnv aeikgkgldl qlnglilqgs ftwgstlnls vykdkvgkyy lpsvqgsnfl
      841 qanatvsgve glpvysifsy rwagldgakg epmgflngqp skayssiisg tkltdlvfhg
      901 palpryfgnm vndfgckgft lsvalsfkfg yyfrrkgidy tnlfa
//
LOCUS       WP_090987980            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            suwonensis].
ACCESSION   WP_090987980
VERSION     WP_090987980.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter suwonensis
  ORGANISM  Pedobacter suwonensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Pedobacter suwonensis"
                     /db_xref="taxon:332999"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117394
     Region          35..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mryilfltaf lislstaaqe klagirifna emktplegvi lqftktnktf isdstgkvsi
       61 pkyigeytve vgqmgyektl iklslplkad liiylqptvr lldevqvhtg yqtlpkerst
      121 gsftnldntl laqqvgpnii srleavssgl ivdrstnsgg rlmirglssi qgpkaplivl
      181 dnfpyegdin ninpndvesi tilkdaaass iwgaragngv vvitskngrf nskvkidani
      241 ntsfvqspnl srlkqispad yidneiflfs kgfyqsqvnn aqqpalspiv elllkkekgt
      301 vsgndaqaei drlksldvrd qykkyfysag lnnqasvnvs ggqelfkwys svsvddnrsv
      361 tdavfrklna kmsmtykpyk smevstgfyy tnstartgkp dygsissvsg nlypyaefad
      421 adgnalaipk drrasylsgl aggllgdwry ypltdyqhvn nqikvgdlll daaliqklpy
      481 gfsvtlkyqy enqerknpvl sdeqsyfarn lvndfaqyan nvlsykipkg gildnsfnsl
      541 qvhnlrgqln yslstpvhvi agfigaetra ssvnglssrl ygfrddiisa gvvdyttayp
      601 slvtgnnsfi pdrngiistd trfvsvfsnl sysyksrytv tlsgrrdasn lfgvntndkw
      661 nllwsagllw nvsnehffnk dlfsslkira tygltgnidp amtsistivy vgsstntglp
      721 yarfntysnp slkwetsamt nlgvdfsmwk drlsgsleyf hkrgkdlfgi esldysggvg
      781 qsiiknaaem sgngweiqln sintegrliw ksnfnisgyr dkidkylfsn yqgsnflgia
      841 ggpsisgiig spvysiygyr wggldpangd pigylngnas kdynlitgqg tqlsdlvyyg
      901 savprifggl gngfrygnle lnvqfsfkld yffrrnsiqy anlnntgqgh adyslrwkqp
      961 gdelntdvps qiyptvsard nfyrgsevli skgdhirlqy inlsyspkiq skvfrsltvy
     1021 atisnlgliw vankqgldpd yeiglnglvp pktvsiglrt sf
//
LOCUS       WP_090991553            1139 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090991553
VERSION     WP_090991553.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1139)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1139)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1139
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126104
     Region          118..1134
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miklihktir slpiffmvav ltvtfntaya hsqvitmqkk ginlnelfke lhakynydff
       61 yeeglldnsk rfdisvanst indvlnktvl pfsleyqink nivvikaslk yqqssihgrv
      121 ldeekkplpg atvlhvnskq kgttdnngnf rlanvkiegk iiisyigyep vevnaaanlg
      181 diilkiassd lqeveinvgy glrkvidltg svsrvtaael egapphadia smlqgkaagv
      241 nvmvangapg spvsvmirgt tslignsqpl wiidgvpqyt svgtqgtqns eigqmlydyn
      301 vndiesidil kdasataiyg sraangviiv ttksgrkygk pqidvsynqg vqtqrdsfrt
      361 ltsdeykavi tdatrnyfat ggiattsgai atvldaskvv pgtevdymsa pflstaffng
      421 qtnwwdeltg saverkldis lrgsseasny yvaigipqqd givngsrrrg ftgrfnfdsk
      481 vannflmgft lngsnskldn kdnmvakiwd frpdfpmyga dgkifdpgvn eenplttlkn
      541 rdlsvrkgvn gsaflqftpi kslvfksais inynqtitdr fvragsanit hngqanisqn
      601 etnnwvfent vrynklfnkt hdvevlggfs mergaysaft agiqnfpdqd imtnltsgtt
      661 plkptstkts talvsaftra nykfkdryla tftfradgss rfgpdtrwgi fpsgalawiv
      721 tnegfmknln qdvfsllklr gsygisgsqv lgnndwrtly taaqfeelpg ftpfqlgnng
      781 lvweqtltke aaldygffks kitgsigvyd kktqdiiynk nipsssafis vkenvatiqn
      841 rgveffidyn vyrkgntnvs vnfnlahnvs kvnkingvdk fidlyggnal airmqeghpl
      901 gewfgykwsg ryyqsmeeyn llstqnpttg akiwyqngln svrpgdlkyd dvdgdgvvtd
      961 kdrvplgtfq pkyfggfaan frkggvslnm nftystgslr ywwgntqnwy gvglflknyp
     1021 eyvldswstt nrtsqwprms ygqgssntfs dfwlskadyl rlsmvrvnyr fpdkwiqski
     1081 nggldlsvsa snlltltnyn gidpegnfrl aggatgtgtd ygtypsirtf nfsiryslr
//
LOCUS       WP_090991621            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090991621
VERSION     WP_090991621.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111704
     Region          23..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklvlslfm lcaitvtafa qermvtgtvv asedglpipg asvkvkeapa isvatgvdgk
       61 fslrapssgk tlvisylgyt tlevaipasn nlgtvqlatd skslnevvvt aggvsiqrre
      121 qgnqattvka keltqgkafn vasalsgkva glqinavssg vnpqvrlvlr gnrsllgnnq
      181 alvvvdnviv psnilgnlnp ediediqvln gagaaalygs dasngaliit tktgkngvta
      241 ikvghttafe tisflpklqk efgsgtgpdd vptytayenq qygprfdgsi veigkplvdg
      301 siqkvpyswn esegknqfwd tgvsnqtdls lsagdekaky ylssqyfdnk gtlpgdkynr
      361 ftirlngsrd lgkvnlsfna nyvqnrndtg nggtafnnvl mspgqipltr ykdwrndpys
      421 tpdgfyneyy dspyftlgna rtltrndylt gnvqikyspi eslsllfrts iatrnvsnks
      481 wsdkytfsdy rlgitsnfan rpgsvsdlsn yttqlnpefq aqyikklsnd fslnvilgas
      541 ardniaknvs anssvmvtqg lynvsnttgn vfgaesnsrq rqvgvygdar lgfknflylh
      601 vtgrndwrsi lskenqslfy paadvafias dalsflkesk aisvlkirgg iskvgqvnid
      661 pydltatfgq qfgypyagvp gfgvgnrvva pnikpevttq veagfdleml ksrvnfsvtl
      721 yksntvdqtv evnipittgf nrfltntgev qnkgletslr lvpvrtasgl evsvggnyty
      781 nknevlsiss dqdfisigts viarvgqafp ilvgttynkd dqgriivdri tglpsattsn
      841 sdlgiteprh rlgldltasf kgfrfatvfe yrtgnvifss vstgydfsga girttyfnrd
      901 rfvvpnssyl dpatntyvan tsiqtrtggv dfwtngpsnt gvtqnytysa afwkmreasl
      961 syqlpksllg nlkfvkgaei svqgrnlfqi vpktsiytdp eysnagsgsn avgvttlgqt
     1021 ppgryyglsl sltl
//
LOCUS       WP_090991848            1219 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090991848
VERSION     WP_090991848.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1219)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1219)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1219)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1219
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1219
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=136514
     Region          118..1218
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meknfykrka vmhcyrtvll vfaifwtsla naelsqgkwk perlenylkk ielaykvsfv
       61 ydadeiskam iievpeklgt iqesleplkq knigyrqvgn qvilkievpa vkpikkdiii
      121 ngvvkdkkeg tgvpgvsifv kgtnvvvasn ekgeyqisvk dessilvfky lgyktvevav
      181 ggrrtinidf eedanqlrei nivstgyqtl drklftgsat kisakdsers gvpdisrmle
      241 gqaagvsvqn vsgtfgaapk irvrgatsls gdnkplwvvd giiledvini snealstgda
      301 stligssvag lnpddiesft ilkdaaatam ygaramngvi vvttkkgrdt egkaninyss
      361 tfttylkpny nnfdimnsge qmsvllemen kgyythssla nssnggvfnk mynqmydyni
      421 gsdsftlnnn lgsrlnflsr yasantdwfd ilfknsllqe hslsvnsgta rsqtyfstsy
      481 thdsgqtlgd nvkrytanlr ssfkvsdrls aellmngsir dqrspgtltr qsdpvygqys
      541 rdfdinpysy slntsrvltp yaedgsleff trnyapfnim nelqnnylkl qmldlkvqag
      601 vkykilsklt ysidgayrya rserqhhilg nsnmagafra npnpavndan iflyddpdlp
      661 nepsvvvlpe ggffnvnnnn ilnyylrnnl efdskfgenh rlnvfgsyem rytdrqnsnf
      721 dgvgyqydng glvnpnyryf kkaieggapy ygmgygydrf laamaraays fkerysfnat
      781 vrndgsnlmg rskvarwlpt wnvsgawdid qesffkgvkp yisgarvrat yglvgslgaa
      841 tnssavfynr vtyrpyenek esqiytssle nseltwekly elnigtdltl fnnkinltfd
      901 yykrnifdli gairtsgigg qftkfanyge mkaygyeltv sgspvkttdf kwrtqfnfgf
      961 nknevtrldi dqniwtlvra egaakkgyaq rglfsiefdg lnpqygyptf vglngvrnet
     1021 niplqdtnve slvyhgpvdp iftggfwnqf syknftlsal ftfstgnyvr lqptftstys
     1081 dmtamskdll nrwimpgdek vtnipsimdr fsnasriyrp dgttvvnpay pynaynysdq
     1141 rvakgdfvrl knisfsyllp aklsskvgla naqlsivgnn vallysdkkl ngadpeffnn
     1201 ggvampipkq ytlslkvgf
//
LOCUS       WP_090992471            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090992471
VERSION     WP_090992471.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115528
     Region          28..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlknylsrl fgviaimiip wavfaqtkit gtvkdatgpi pgvsilekgt kngtltnseg
       61 qftltltkps avlefkmlgf itkdlstegk sslsvileed trslsevvli gyqritrkkn
      121 tasissisak elenlpaasf dqllqgrvsg vnvqnfsgqp gtaptvsvrg nsllsrgyde
      181 fnvvnsplyv vdgvpqptes yvgpgtgtgt nylaginpmd iesidilkda saaaiygsra
      241 angvilittk kgtsgdprvg intyygvtar pelrdvtlgt verrqklail enqltyadqk
      301 qlpylltdsl nsafngntdw qdmfyqqgri snvdlnlsgg gnggmiyrfs ggayneegii
      361 katgfkrytg rlnlsskalk erltinplva fsrsdrargn gssgspialg sgnmpsslfn
      421 mddekrafll geydenldkn isnqltlnln msydfspnfr ftsqssykgd ndrrdfnrgn
      481 alqnnqgnys ysfasnaidl ltsnflsynn tfkkhslsav vgqdiqynqy qtitasgsng
      541 asdniqvvng fqqakigags dyqaygllsy yariaydfds kylfsfsara dgssrfgknn
      601 kwgyfpsasa awllseedfm kdnklfsmvk lrasignsgs lptsnylqyn lynvnaagyf
      661 ggggstsyng vtaitpnfyd gvaqknlswq ksmqwnigtd ielkngkfaf qfevynkess
      721 lqlfsvnlpl ttgydlaltn sigvrnsgae vtvianplka sskfrwttqf nisynknrim
      781 slpnggrdlv mdgdrfdksh ilsvgspina fylyrtkgvf ksdadvpqnp ftgekyrnsn
      841 gtflggmfyf ddldgdyftd vfnsginpdk lpmgdpnpky tggwtnnfsy kgfslqifsa
      901 ftfdrdvlnl feadrfstst dgnavanyaq fsspdysnid iwrnqgddar yakvdlgsyr
      961 yyytsaqsff lekggwfrik sinvgyqlpa pmtkklgmsk lkifgiadnv amfqqskrlp
     1021 daeavnpyge yngagypipr kytlgleiqf
//
LOCUS       WP_090992378            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090992378
VERSION     WP_090992378.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112580
     Region          25..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikiltill flitatclvs naqertvtgt vissedglpi pganvtvkev psatvgtsad
       61 gkfsfrvaae gktlsisylg fktqeiaipa ngnvgviklg idpqslnevv vtaggvsiqr
      121 reqgnqsttv kardltqgka invaaalsgk vaglqvnavs sgvnpsvrlv lrgnrsllgn
      181 nqalvvvdnv ivpsnilgnl npediediqv lngagaaaly gsdasngali ittktgkkgv
      241 ttlkvgqtst metisflpql qkrygsgtsp ddvptytpye nqqygpefdg smrvigkpli
      301 dgsiqmvpya ynakegkqqf wdtginnqtd fslssgddng syylssqyld qkgtvpgdky
      361 nrftirlnga kklgdkfefn fnanyvqnrf dtgdagtayv nvlmspgqip ltrykdwrnd
      421 kystpdgyyn eyfdnpyftl gngrtltrnd yltgnvqlkf npikeltllf rtsiatrnvs
      481 tkswsdkytf sayrlgitsn fsnragsvsd gsnyttqlnp efqaqyikkl gndfslniia
      541 gsslrdniak nvnasssamv tpglynvsnt tgntsgsesn srerqlgvyl dgrigfkgfl
      601 yfhvtgrndw rsilavnnrs lfypaadisf iasdalsflk esktisslki ragvskvgqv
      661 sigayaldpt fsqasgypya svpgftvgnt qvsqkinpev ttsmeggfdl emlksrlnms
      721 ltvyksntid qtvpvgipss tgytqfltnt geventgiet smrlvpvrte sgleitlggn
      781 fsfnqnkvls isadqdfinl gtfgfaniva ekgkafpllk gttynkddqg riivdritgf
      841 psattltsnl gstepkhrlg ldmtvsfkgi rlatvfeyra gnviyngant gfdfsgagir
      901 ttyfnrerfv vpnssyldpv tnqyvantsi ttrtggvdfw tngptntgvn anythsaafw
      961 kmrelsisys lpksllanlr fikgaeisaq grnlflwtpk tniytdpeys algansnaig
     1021 faslnqtppg rlyglslslt l
//
LOCUS       WP_090992714             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090992714
VERSION     WP_090992714.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106867
     Region          29..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvfypiklc mlllfalgal tvaaqtgsvs gkifddanmp ipgatvqvvg tqmvmptdan
       61 gnykfsnlas gtytisaryl gftaqsltat vgsgnvvlnf slkpdlqnls evvvigygta
      121 ekknltgsia tvnskdfqkg tittpeqliq gkvagvtivn nggrpgggsv irirggasln
      181 asndplivvd gvpfsgssig napnplalln pndfetftvl kdanataiyg srasngvili
      241 ttkkggsgap vfnfstnnsi atviknvdvl sadqirsyvn angttaqkal lgnantnwqd
      301 eifqnaftsd nnfsvggsfh nvpyrfsagy ldqqgllitd kltrasgals ispnflsnhl
      361 kvelnlkgal teshfandga issaiqfdpt qpvhatnsfg nyfewtqgav pnpnaprnpv
      421 alirlqdnng kaarsfgnik fdysfhflpe lhanlnlgyd nntgygftrv pnfaaqsast
      481 sgffgnrkns esnivsefyl nyaknvssin srfdatlgyg yydntakgyn fstykgtgel
      541 lttpvfpysl eqnkllsyyg rvvytlaeky ilsgtmrada sskfsednrw gyfpsagftw
      601 riigedfmka sntfsdlklr lsygetgnkd gignydylsk yyansntgqy qigdtfynyy
      661 spaaydpdlr wettttynag ldygfakgri ygsvdayykk tkdllstvni pvgtnfsnll
      721 ttnvgnmevr giegsinfav iqsenttwdf gfnvaynkrk itnltlnpdp askigagdia
      781 ggtgttlkyn svnqipgaff vykqvynagg aplegvfedl ngdgiistgd qyfykspdpn
      841 ltfgfntnfn ykkwsvntvl ranignyaye nvssnfgirt nilspsgiin ntgadflntn
      901 fqtnqylsdy yiknasflkm dnigisynvg rlskvnnstl risancqnvf vltkfdgldp
      961 elssgidynl yprprtytlg lnvgf
//
LOCUS       WP_090992733             942 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090992733
VERSION     WP_090992733.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104992
     Region          63..941
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdkkstlfql ksqlilwllc laavgqvlaq qqksddenlm vpdsvlkkik lqdrhinqwf
       61 sttqkrknve gsttiynedv mttpvsditn viagrlpgly sskssgrtgp mfdassltlr
      121 gqtplliidg vqrsftsfnv ddiksitvmn dalsnamfgl rsgngviyit tkdrsiekpf
      181 elgfsaqfga neqfkrpnfi tgadyarlyn eaqqntfpga tplyseeria alqngtndpy
      241 tnpnndwynt vykksntqqr yainaagngk nyrfytsveh faqdgnfltn kdnpyntdny
      301 ykrynlrtna qidfnediql glnifgsven nnepgvtgst imsriygtsp leypaknadg
      361 syggttsflt nilastissg yiqynersls advslkykld ditkglwtka llsinnyylq
      421 riartksfai yypnlstgey tkvgsdgvle agagiqsiss qykqtffngl igydkamgnh
      481 efnvlatynl tnlidsytql nqvyqtaglk anysynekyl aelalaysgf nryaegnrwg
      541 flpaiglgwi vskeewfnsk ainllklrgt igksayadps nyytylqnys vastgynfga
      601 tatavagalq nsmnnpnitw ekalkidvgi eaqflnhfni alnyynnkyv delispangy
      661 asgiiglgyp svnagktryf gyetslgyqs endginyfik gnlsiaknki israegnypy
      721 swmyragqps atfgyeaigf yqagedftkt anipgytpsa gdiryndlnk dgvidfldqk
      781 aiagtkplvf fglnfgfnyr nfdfnalieg rvnreiyyas ssflafnnnn gnvldytten
      841 rwtpqnpvna tlprltlgnn tyntqsssfw vkradyirlk naeigytipa kllskakisk
      901 lrvfvngynl ltasklayld petglsgfan yrimnagvsl kl
//
LOCUS       WP_090993001             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090993001
VERSION     WP_090993001.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112356
     Region          55..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgknftkifc fllffafaak ansnkhvdsk iafnvnllmf qqdsiqadts ikdsigrsir
       61 erarfkgnrd sikvstarnl pnlslqqmik gnvsglyvqe tsgepgseqs miiqgsstpi
      121 ftkkdiynmq pavyvngvyl vqehpfayev qkydynrigp atnllanvdi dniasievik
      181 dpvslaklgp naangaiwit tkaaksglre isfnsyfgmv qaggantvng vfenkfrqpf
      241 yqkyasqanl nnyasylrds tnldyfgksn wsdlyyqnap iftanlgitg gsekanfrff
      301 gsgtknagna detsltkyna ffninmmpfk wltvssflna srmdrdrnkn lrdryaevry
      361 lpdfvnplsp nkdnyqlfln eyskvvddnr nnllngslsl nfkltpklnf ntavvfdyne
      421 girdaffptt lmdginfvsg yfgynqrfgl nnqlnyqydl nkdnvfdfev gqsvqgdtyk
      481 ynyargydgn sdfikinvve gnsndddyln ainnfylfry tdrtrngmms fygsakysyk
      541 nllsfgaiir rdgssngqpd srwittpafs adwnlknqfl tknkffnqln igaswsrvak
      601 ifledrfgag pqyrseygwy eeptiptfgg fqgitrpynt gwvgygvslp yadrlnisas
      661 stmlnnrist svtlynrtnk nqllnipvsg esgytsiykn gmeinnmgvd fdftatiipn
      721 ekalswtsgl nlnynknelk alpdglselv igdnklkvgk ssgsywlytn ngiynsdsev
      781 ptnpsngqkl afngltlkag dprwvdyngd ynitdadkqf tgdrlpklig gwmndfkykn
      841 felnfhlffa lgqkainqfd asrydfanre sandinsike vttwqtsdki ktypiynvws
      901 nvipyradqd lflenasyvk lrsvtlgydl tkskfisnak lgfrraylyl tgsnlltitn
      961 fsgtdpelin ytgyyngtsl piartytigl kldl
//
LOCUS       WP_090992996            1134 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090992996
VERSION     WP_090992996.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1134)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1134
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125018
     Region          24..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklllifl gtfllfadaf gqektitgkv nsqdgpipgv svkikgtnva sqttgngtys
       61 ikasatdilv fsylgyvsve rpvgtnttid vtlledsksl eqvvvvgfgt qkkesltgav
      121 tsvnvskvfg nrpipdlgrg lqgavpglsv vvpsgevgsd piikirgqig sisgssnpli
      181 lvdnveipsi qyvnpndiet isilkdaass aiygskaafg vvlittkkga kvegnnvtys
      241 nnfvmqtpfk eidiagidgl eytldahenm kqpgpaggfw ridrtsfeki kewqtkyagv
      301 vgnndpvvyg rdwywdgaqk fgyriydpve amikdhnlsq mhnlglngks gntiynlsvg
      361 ylgqegmmkp akhddyrrin palsvstkat syltlrgdlr yaegtkrnpn slnaaafaad
      421 pwlymyrwsr lfpigvqeqg qdiidpafsa rmsndqirne kflnmnlgat lnltknwdvq
      481 adyaystqnn lttasvpyvq grthwygvea lrdengqvyv dedgnptqsg gmpayrfplt
      541 dhtlksatyf sqnnfrsqrk tfnattnynl dlkdhqvkfl lgtnivsfdy ssqfstlgnl
      601 lnndnpqyey svgtqeaggg anwdsqagff grinyafkdk yllegvlrrd gtskfpthlk
      661 wrtypgvsag wivsnegfmn gvksvlsfak lraswgnigd qsvinslylp tmdiaknswl
      721 nsggipyfql gtpppvsrni gwqniehinl gadlrffegk lgvtaevfqr ytrdmiidgd
      781 alpatfgata prgnygdlrt rgwelnldfa hqfdnglrls fdanmadavt fitkgsdyqm
      841 pwenrsvgsa fstgrrygdv ygfvtdrlfq kddfvyddng nfvqtnivfn gtskrtnlla
      901 gnnpvyqtyf edgnqtllis pgdvkfkdln gdgyidagkg tngdsgdrvv ignttpryqy
      961 gfrlgadykg fdlsvffqgv gerkiwgdgq laipgyfake gampqviaed ywkadrtdaf
     1021 yprawnmnga segyvmrpqt kymldmsylk iknitvgynv pnafmkkvgi knarvyvsle
     1081 nfitfdnlrg lpidpeaisg fsmlgsgstn ynlgrtgtsn pafrsasagl qigf
//
LOCUS       WP_090993018            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090993018
VERSION     WP_090993018.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124543
     Region          30..1136
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknyqsnvs klvltlvmsf mmlianaqnr nitgrvtdas gvgipsagvl ikgtkittlt
       61 dgtgnfsipa kngdilvfsf igliakevvi gnqssiavtl eednqalnev vvvgygtikk
      121 skltgsvskl dpkvletgmr snpaqalagt ipglrvsttt grpgsvasit lrggtnfdgs
      181 gsplilmdgq vrnslsdins eeiesmeilk dasataiyga rasngvilit skrgktgsss
      241 islksrtgvs ylntpydfls aedyikwtrl gvveaikngt lgtvasnsal aavgprgtgn
      301 vykdgagnil dgnyssnaiw stmrltavnq ellskntgwk tmkdavptna qgnydpngty
      361 adliykdfny gdyglhktal sqdynismng gndkgsyfan igyyneggls lktfyrrlnf
      421 svngdynvke wlksesgvqf ikanwrdqsl fngeanywgr mlsapptmrg tnekgdlllg
      481 rdasdgnpii nidkykvdnq sdkftlsqaf kvdftkdlff kvkgtlfyee gfyesfnrdf
      541 rtgimsltnp ntgwnrdrts aasfnrttrq tynailnykk lihknsfdam vgaeyfdays
      601 kgfsadgkla ptddfqdlnl takdvagiga rnivsshsre rilsqfaran ydydekylls
      661 ftvrrdgfsr ligdnqfgif pagsagwvis kenfmqstqn wlsflklras ygkngnigig
      721 tsnaiglyel qgaygpqnay ngvigflntp anpnlrweks ttleggldma flknritagv
      781 gvynritsdk lanvqlptss gvssvrtnng smqntgvele anykiiqksa vrweiganaa
      841 wnknrilklp fngnennrqg gqqiydpatn rlvwvaglqe gqepgeiygf vkegiirnad
      901 dlakynkidl aagqvwyggs agkkvasqsl iasknlnpna nsptfiatrl gdvkwkdidl
      961 ndtidtrdmv klgrtlprwt ggfntsiswk glslfaridf algykqmdfm qlwalgsfqg
     1021 efnatevvkd twtpenpnaa yprytwadql nsknfdrpsd mfwvnsnyln frevslsysl
     1081 ptkllqkaki ggltitatgq nlgyltnkql nlpertgsqn sayiiptqvi fganltf
//
LOCUS       WP_090994018            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090994018
VERSION     WP_090994018.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109721
     Region          53..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktilpnkak hyckvgkvll lataiqlttn tqsmafkrsa fiselrnnsq fvtikgkitd
       61 kngqpiigas vmikgsqigs lsdangdysi naertsilvf syigftpkei tvggqttinv
      121 eleesstslg evvvvgystk kqseisssis vvtgdklrdv tsnevssllq grapgvvvst
      181 asgsptsgss iivrgtgsin astaplivvd gniggnynpt dvetitilkd aaatglygsr
      241 aangviiitt ktgksgksvv synttmgfte astgnfslmn sqelydyqsk fysgltperl
      301 nnntdwwdlg frkgmvntht lsasggseks tfylsgnyyk eegtlihndk tgynlrgnft
      361 qklsdkfkis sflngifind vynaggtlyd syvnmpfdpa ynpdgtpida rygtwygrdr
      421 dnflhtlqyn tsraksfnvs adinldynvl knltlssynr gnlvnyrsds fndkrtksga
      481 tnngtayasn synntfltsn rlrysnnfgk hslavlavge ieqgysesls anvknlpagr
      541 dafstatdiv tnpsggndty qfskylgqvd ysfnekyyav asyvseyssr fgsnkpngnf
      601 yqlgaswias nedflknnka itflklrssy gttgnaygig yyaalglysi ssgasyaglp
      661 gaapsqkanp dltweksksa nigvditlfk ridlsvdayh keaasllffr plpattgysg
      721 vyenvgnvrn rgiefnlttk nfvkdfkwet nlnmafnrnk vlevnqgrte vstgarqpia
      781 vghdmdewfm pvwsgvdpat gsplwenrvk dadgkeflty ttnynaasrl ytgkssapkf
      841 tggltndfty knftlstffn fvygnyvynd srfffdsdgl yesynqmnla kgwsrwekpg
      901 dlathpkpvh gradnsnats trylengsyl rlrnvtlgyn lptawlnkak vnkvrifisg
      961 dnlwtltkft gtdpevelgd gvssikypis kkflfgvnis l
//
LOCUS       WP_090994258            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090994258
VERSION     WP_090994258.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118032
     Region          27..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknsliiill vglfqsaiaq ktmvfngtvk sattklplne vnvaiagsqq vivtdnsgrf
       61 sisslgnewl tfthfgyksl tvrlgtdpnm pmqiemvete qqlqevvvns gyqqipkhrv
      121 tgsysqlnnq lltrkvssni lqsledmvpg lafnrsgssv drysisirgt atinssnnpl
      181 ividnfpydg ditsinpndv etitilkdas aasiwgarag ngvivittkk gmngepivst
      241 tanytigerp nlfynsrmns gdyidvekml fgkgyynaai ssinnqpltp avelmlahkn
      301 gkisesemnq gldalkkidl rndlssylnr nnvsqqyavn lkggsisnny flsfgydgel
      361 anlvgnenkr itlnaatnyl ffknklelsn sfnysnnngq lnnpgnlyfs gatelypyar
      421 lvddhgntqn viknyrasfv esatqkklls wnynpldnig lsdrntgqqe yrfntglkyk
      481 wnqdlnfelr yqfnrndthd ytlnseksyy arnlinnftq vaadgkltyn vpiggiyekt
      541 mgkleghyar aqlnynktwn dinnitgiig teikdlttit nsynlygyds ehatsrdvdy
      601 ltpfeqlayp gllvsvpsgv sstelseryl syftnivysy knrytfsgsa rldqsnlfgv
      661 dynqkgvply slgaawniss epffkskvvn hlnlrssfgy ngnvnrslsa yttarysngs
      721 tsasllpfav venppnpslr wervkiinlg vdfglfssri ngtidiyrkn gidligaipf
      781 dpttgiktfn gntantkghg idlsinsnni vsasfiwntn llmafnrekv syyganatvd
      841 sylqfagipk tgfpifsvys ydwagldplt gdprgyldgv pskdyakvis gitpenlifh
      901 gslrpdffgt irnsftfknf tlsanisykf ghyfrrqsir ynnvltakgg hgdyslrwqk
      961 agdelitsvp smptalnnsr dnlylyssvl vekgdhirla dvrfsyavkk tllgvknlel
     1021 yayasnlgii wkatkfaidp eyfniaplgk siamglklnf
//
LOCUS       WP_090995958            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090995958
VERSION     WP_090995958.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121793
     Region          39..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlnyyltfnn ykwrvfnsll ilffamliaa pqvvygqskt itgkvtdagn giplvgaavk
       61 vqgsgngtst dsqgafslqv annsvlvity igydpqtvsv gdrsniqikl vensktlnev
      121 tvvvgygsmk kkdltgaitq irpdkiadqn pntvqdilrg tpglsvgfda sakgggsiqi
      181 rgirsvysag ghndpliild gtifygefse inpddieqid vlkdasasav ygaksangvl
      241 ivttkrgkig kpkinftsnf gmvekaadre vfdgagymqy rkdwytapsy glnaatgnye
      301 pyqstfktqp gyyeeptdan lakygitlaq wkaytnnpav ttdneiwakr lllqstvltn
      361 ylggqtfdwy nhsfqkgvnq dynisasgat dqmnyymsvg ylsnkgvavg neysairgnl
      421 klegkitkwl elganvnfqn rtdgdlavdw srqilnnspf anyrdaagnl avhpmgdnmv
      481 nnygynydfn rgyldldkgf tvlntifnak iklplginys fngsprfqff hdrywesash
      541 pdwkgtnglv nreqakrldw sfnntlswer efakkhrvni tlvqeaekrq ywqdriearn
      601 ilpsdalgyh etlfgdknls rfdsddvket adgmlarlfy syndrymltt svrrdgysgf
      661 galnpratff saaaawtftn esffkwkams ngklrvswgq ngnrqlanpy lalanlglgg
      721 gatagyidns gnliqykyll mdrlanpalt wekteafnag ldfgfldnri tgafdyyitp
      781 tvdmimlrsl vdftgfgsin tnlgkvenrg felsvnsqni rnknfswntt fgiskyknti
      841 qhlyyvydnv vdangnvtst kerddvgngw figqpigaiw nyrvtgiwqt nevaeaakyg
      901 qrpgdpkvan yytaddnngv pvyndndkef lgqtnppimw slrndftykn fnfsfnmysy
      961 mghkslsgay lnqdngtslv tnlantwqke ywtvnnptnn farldargps gvsapgmlyd
     1021 rsfirlenvt lgyvvpnsit skigidklkv yssvrnvavw qkdknwqywd ietgalapri
     1081 ytfglnvnf
//
LOCUS       WP_090996639            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090996639
VERSION     WP_090996639.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111428
     Region          25..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknylkcls alllallsit afaqktitgt vkenstpvpg vnvavkgtak ttqtgadgkf
       61 siaasptdil vftmlgytkq eivvgsqqti nvtiastesq lsevvvtalg ikrekkslgy
      121 gvqevkgetl vsakepnlan tlsgkiaglq vvrssdgpag sskillrgsn sltgsnqpli
      181 vvdgvpidnf tgapdngywn rsldmgngia dinpddietl svlkgpsaaa lygsragngv
      241 ilittktgra qeglgitvas sygmsniftn pevqnsfgqg nsntynatst aswgpkvegq
      301 mvtnwdgrqv glatynnvdn ymqqgininn sisfqqlfkg tsvytsynrl qdegivpgtk
      361 llrnnltara lskfgaddrw vtdtkiqysn tkannrpvgg rdnssaytly mlprsmditq
      421 fnaakngvgn mlwfdgagsq vnpywsnqyn lnedsrdrfi mngsvkynft dwlnaevkgg
      481 adlyttntqs nvysgspiaa tgrygmgkqt fsetnfsall sarkdnivgk fggmlslggn
      541 lmqtnftsls ssvgllvvpn lfslnngvsp agvsegisrr rinsvygnaq inydgylyld
      601 atfrndwsst lskenrsffy psvslsyvlt dmltsmgtel pnwlsfgklr asyaqvgndl
      661 apyqlyntfn igkdpngntt agrntvlldp nvrseliksl elgaemrflk nrigldfsyy
      721 ktnatrqlid lpmdalsgyt akkvnagdiq ntgmelvidg kvmgkpngfn wntsfnysrn
      781 kntvealseg vskyglggfd dvsvlavvge kygeiygtky srvkdnsspf fdqillnadg
      841 vptrdpeivk lgnqqakali gftnsfeykg vglsflidar iggeifsath vamqasgtaa
      901 vtapngsrds fvvpgavsng sggyvantkq vtpqqywlgv atannlgite aniydasnvr
      961 lrnvqlsytf srkllantpi knakfgvscn nvwlikshmn gidpesvyat nsnatgfena
     1021 glptmrtfli nlalgf
//
LOCUS       WP_090997259            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            insulae].
ACCESSION   WP_090997259
VERSION     WP_090997259.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter insulae
  ORGANISM  Pedobacter insulae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Pedobacter insulae"
                     /db_xref="taxon:414048"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117650
     Region          49..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mifkliincd vikmnsntii snkkryrkai llmllnvfat alfaqnvavk givkdeigep
       61 lsgavvmqvg ttnttrtdkd gafelknvap gatlrasyvg rntvelilkp geikvkftlk
      121 nsnltlkevt vntglykrpv gnftgsakty sgealktvnp rnvisalavl dpsvriaqnn
      181 vlgsdpnslp nlqirgannl pvslqggsav anpvsngdim snylsnpnqp liildgfett
      241 lqtlfdmdvn lianitvlkd aaatvaygsk aangviviet kqpvpgklrv tysvyanadl
      301 vdltsynlmn aeqlleaqrl tgifsdpnnq yndlakkqwy dyrlgqvrsg vdtywlsqpv
      361 qtglglnqsl slgggagplr ysfglnynta egvmkdsgrd ryslnynvsy lvknirfsns
      421 mavgytkgnn svwgsyesyv nqfpyfrnkd angnlikvle psssaldfii qapggtfanp
      481 aynstlnvkd ystilsltnn tnvewsltde lkltgslgws snspgaeafy padhtkflan
      541 vivqqpnigs yqqlkgknsa lsgrlnasyh lslgkstila nlgatlqkts snsttvqvyg
      601 ipndylgelg langfdytsv kprssnnltk nlsnffsvsy nydnrytaef tvnqsgssqf
      661 gsnskfatfy agglawnian ekwfkpndii qvaklnasig ttgnqnfssd masqvytyny
      721 lnnyrlmvgs stlsfanpdl kwqqtlkani glnlgffkgk lnanveffre ttdnlilpld
      781 iapstgfany qdnlggtkne gwevgitapi irnsarnvfw tvsvnaghfn ttitrlspav
      841 tainngfnsn ldpnnledtr yqtkplprfe vgqsmnriwa vpslgidpas gkevfvklng
      901 sytftwdard krpiaettak ikgsassnlt yknfilnvif syqyggymyn qtlvdrvenv
      961 nlmagnadlr vlterwkqpg dhssfkslva ngaqgfqqtn vtsrfvqkdn flqlasltvg
     1021 ytvpstakwv kaahlsapkf mitqndlvrf atiktergts ypfarslnfg istnf
//
LOCUS       WP_091009955             380 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Paraburkholderia].
ACCESSION   WP_091009955
VERSION     WP_091009955.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39380
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvaqg hrvtvqsgag ngasfpdeaf taagaeivdv
       61 aaafgadlvl kvqspteael pqlkrgavlv gmldpfnadn aaklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgsvi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmpaswlt
      241 rqsalvhera kqadivista lipgrpaptl isvetvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvtkhgvqi vgytnlasmv aadasslyar nlldflkliv tkegtlnidl
      361 addivaatll ardgavtrkp
//
LOCUS       WP_091025099             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides szechwanensis].
ACCESSION   WP_091025099
VERSION     WP_091025099.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides szechwanensis
  ORGANISM  Nocardioides szechwanensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Nocardioides szechwanensis"
                     /db_xref="taxon:1005944"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52780
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresr tgetlvaata ktadqlqqlg ydvvvqlgag vaaaqpdsaf devgvrvgsa
       61 ddvwasdviv kvnapstqei armrpgatvv slmaparspe llerlqsagv tglamdavpr
      121 israqsmdvl ssmanvagyr avieaahefg rqftgqvtaa gkvpparvfv vgagvaglaa
      181 igaagsmgai vrafdvrpev aeqvesmgaq fvtvdmeqev ssdgyakemt aeqeqataam
      241 ydeearaadi vittalipgr papkliraet vagmrngsvi vdmaaanggn cdltvtddki
      301 vtanlvtvig ytdlagrlaa qtsqlygtnv vnlfklltpe kdgqltldmd dvvqrgitvv
      361 kegesmwppp pvqvsaapva avapveakap kpppdprrkv faaglgavlf avlasyapav
      421 flnhftvfal avfvgyyvis nvahalhtpl msetnaisgi ilvggilqvg stnvavsila
      481 tvavlvasin ifggflvtlr mlemfrkd
//
LOCUS       WP_091013360             311 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Paenibacillus amylolyticus].
ACCESSION   WP_091013360
VERSION     WP_091013360.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus amylolyticus
  ORGANISM  Paenibacillus amylolyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Paenibacillus amylolyticus"
                     /db_xref="taxon:1451"
     Protein         1..311
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35788
     Region          4..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mifdlfskrg kkpdtemfiy dnfpaefriq vihlwsdaig rwyhetdfyg ethtspsnki
       61 wlqihkqlck eygifslseq gdnpytqcqy fiqnatterv ldiiemsflw idevvrnwnd
      121 svlqnanitq raedaideln qrfrehaigy qyikgqivrv dsdyiykeav qpaismlsee
      181 gfegasqefm sahehfrkgr hkeaisdalk afesvmktic krkgwevren atakplintl
      241 fqngllsisl qtqfsslrdt lesglptirn knsghgqges ivhlpphlva yalhlaatni
      301 vfliesykal d
//
LOCUS       WP_091031397             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium oxydans].
ACCESSION   WP_091031397
VERSION     WP_091031397.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium oxydans
  ORGANISM  Microbacterium oxydans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Microbacterium oxydans"
                     /db_xref="taxon:82380"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52498
     Region          4..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mavigivrep agearvsatp atiaslrklg htvrvergag aaasypdaey eaagaalver
       61 aeawgseivl aitapgpeei alladgatli allspalrpd lveslaqrgi tavaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvtsiggt ylpvdvavaa stdgyakats adydrraaei
      241 yteqaadvdi iittalipgr aaprlitasd vaqmkpgsvi vdmaagqggn vegsvagerv
      301 vtdsgviilg ytdlasrlaa qasqlygtnl anlvalltpa kdgrlvidfd dvvqrsvtvv
      361 hdgevtwppp avqvaaapaa kaaatpveva ppkkmstark vtlivvgiaa lfavnafapa
      421 plpqhftvlv lsvvigfyvi gkvhhalhtp lmsvtnaisg vivvgamlqi tsplpvvqvl
      481 aaiavllasi nifggfavtr rmlamftlgn sakgsqk
//
LOCUS       WP_091043752             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides sp. YR527].
ACCESSION   WP_091043752
VERSION     WP_091043752.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. YR527
  ORGANISM  Nocardioides sp. YR527
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nocardioides sp. YR527"
                     /db_xref="taxon:1881028"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52192
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvtretk pgetrvaatp atvkqltglg ydvvieggag eassfkdeay aeaggrigtd
       61 adawgadlvf rvnapsvgev ellksgatlv aplapaqsae lldalaarkv dafamdavpr
      121 israqsmdil ssqaniagyr avveaahhfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvkslgge ylkvevevek stdgyakats eaydqraaei
      241 yseqaedvdi ivttalipgr papklitaad vasmksgsvi vdmaaamggn vegtvkdevv
      301 itpngvtiig ytdlparlpa qssqlygtnl vnlmklvtpe kdgvlaldle dqvqrgltvv
      361 hdggvlwppp pvqvsaapav aapaevavke tqkplsagak lalvgtgala lfllnavapa
      421 eitrhftvlt lsvvigfyvi ghvhhalhtp lmsvtnaisg ivvvgallql tvadnvvlvl
      481 agiatllasi nifggfavtr rmlsmfrka
//
LOCUS       WP_091083799            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091083799
VERSION     WP_091083799.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112808
     Region          25..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkisrknllf llllfcvhlv naqtksisgk vtdssgfplt gttilvkgtk tatiadrngn
       61 yniktekgkt lvfsfmgfts kevlinneen qnivlddnsv slgevvvtal gikrdkralg
      121 yasqelksdd inkvnsanfv snltgkisgv qisgsgngia sssritirgd kslninnngp
      181 lfivdgipin nnvygvggss tsqtdlptdy gngaseinqe niesvnvlkg aaasalygsr
      241 aangvivitt ksgkrskglg vsisssfmts ealrlpeiqg vygagskqiy dagadtnlgp
      301 rfdsgisllq ngssgysvgq gqvlpfefry nlndffrkgs sisnsvsvsg sdektnfrls
      361 ygkttsediv pnsnlkreni slnlnynisd kwklatvaty tksssdntpv tgygsqgvmy
      421 nllwnhtnvd ldwlkdywiv kdvkqnsmfg wgdnpfkiay eninafkkgr ifgnisstyq
      481 isndfsfmar igmdnsndfr wsrrpigssr ytqgmyreqt iafteynadm llsydhtfgd
      541 fsfkisygan smnqytsesk iegqgisipg iynlqninvm piqsrniykk rinsmyslan
      601 igykdylyld vtarndwsst lptnnnsyfy psaslsfipt svfemnknid flklrvnaas
      661 vgndtdpyrl vktysngala gtltnpssil nsnlkpeiat syeagievqf fkkritldms
      721 yyitnsknqi vgldisqatg fnsnvinagk iqnkgieigl gltpirskdf ewslnanftq
      781 nrgtvkeltp ginnyiiaqg pnggtiearv germgdmygr gylrspdnqi vydntgspil
      841 dtkikkigny npdwmlglst nlryknlnln alfdvrhggk iysmtnaigm esgilavslp
      901 gretgiigeg vvkntdgsys pnttsisaen wyysnafrrd nieansfdas yvklrevsln
      961 yrlstkwtka vkmqnvsigl vgnnlalwtk vpnidpetqa isggtllpgf evlqlpssrn
     1021 ygiklnasf
//
LOCUS       WP_091084240            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091084240
VERSION     WP_091084240.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114857
     Region          25..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlkfkwift llialsmqfc faqekivsgv isdangpipg anvfnkavnr stqtdfngky
       61 siiaksgqvl evsyvgmknt svtvgvsntl nvkmtaaaee mdevvivayg kakkssitgs
      121 sttikgesld nrattnvlsg iegsvsgvqi qsasgqpgsq psvrirgfss isgsntplyv
      181 vdgvpftgdi nninsadves mtilkdaast slygskaang vviittkkgt sakdkftlnm
      241 ssglntrsip eyervdafqy ypliweairn srpmstpall atanafastr tpidlvnnpf
      301 nvtnanlfda ngqlnpaakl lyandldwak qlqragvrrn vdfsyqgkte rsnyfvsign
      361 lseeasilns dfkrttarvn vntklkewfk tganvattyt dsnqavdgaa ntssfnnpfr
      421 tirymgpiyp vlshnsttga vildatgnpv ysqlrgsgas ngrnvvyetl nnenrdksls
      481 fngrtylelt llkdfkfttn fafdnahfnn nvfwnkvigd gapdgyasrt ntvttgvtfn
      541 qlldytkvin nhnisallgh esfdyeynym fgskrgqgvp nnnefinylt vsnlnsytrn
      601 yatesyfsrl gydydgryil sasvrrdgss kfaaankwgn fwsvgaawnl gkesfvekig
      661 winelkfrgs fgevgndshi sygglnyyig aptfslglnn asevgiltnd qgapnlkwek
      721 ntqkdialdf affgnrlrgs veyynrttdg lifdvpvpvs sgldskveni gsmfnqgiev
      781 sidgmivktk dfswninvna stikneital pqkeiisgsk kysvgssiyd ywlrsyagvd
      841 padgyalykv dpllttptdt dsrtvngvnv tinqnkalye yhgsalpdlf gsftntfkvg
      901 gfqmdvlfty qiggqtydtn yaalmhsgnn ygsalstdil krwkkpgdit dvpllnisrn
      961 tqnsaasdrw lvdsdylslr qvslaynlpk elisklkida akfyvngenl klfakregmd
     1021 pqanyngttq nrfspsrtis lginlnf
//
LOCUS       WP_091085359            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091085359
VERSION     WP_091085359.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112141
     Region          24..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkylilll lflgiitsys qnttvkgkvt dakglplpga nvnlkgskst vatdmdgtyq
       61 iqasngasli fsyigfknqe ikvsgntina slkedtetkl devvvtamgi knktkslgya
      121 nqtikasdie rpgqlnalqs lqgsisgvti sktsgeaggg vdilirgvss lstgsnnqpl
      181 ividgnpvnn stisgnvlss annsspgsne qfgfsnrsid inpndiesyt vlkgagatal
      241 ygilagngvi iittkkgkeg ktrvnisssv tmsdvnkype lqskwregss ltprvlsmna
      301 ttpsgisfyp gftsafqsng paysstddas ikfrhfykdf fktginttnn islsggtekm
      361 nyyvsastsk degivpntdy arktlkfngg yklsenlklg tsvsyansgg srantgdksi
      421 msslsywsps iyvndyltka gaekdwtsgi idqpvyfakt snlndnvdrw iasadlnwqa
      481 kswlnityrg svdnyaesrn ryagpdldpg spvngfivne kinfkglnsd flvsatkkfg
      541 dfntsamign qifetnsdys lsrgegllls nfnniantin kyaaqtnevv rtvgyftelk
      601 adykerifla atgrrdyast lpaanrafny fssnlafvfh dlidkegsvl sfgklrgswa
      661 qvgkippfgi grysypdipf ngvggvsigt vdsdpnikae ivtttemgtd lrffnnrirl
      721 eytyfdrksd gqilkvtlpq stgltgtwtn sgslqttghe ltlaadifkn kdftwttian
      781 ftayktevlt lpfdnidfay nggadiysri kvgdaagsly grtwtyvngq rligtnglpv
      841 iakdtngavl yskvgnafpd yvvtlnnnfk yknwdlafmf eykkggegfd paerngirng
      901 ilkmtedrnh tqvlegvkad gtqnntpvti dgnsyyrnti inqaseiliq dtswlklrnv
      961 sltynlasdl tsklklsnas fsvsgnnfll wtpfrgfdpe gqqfgsgsnv ygfsglnipl
     1021 tqsytlglni gf
//
LOCUS       WP_091085868            1013 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091085868
VERSION     WP_091085868.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1013
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111477
     Region          49..1012
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknislnkgr rvwyfticcc lyftvsfaev skkedsgdps fvgmtsqqqq itgtvtdkgn
       61 plpgvtvhlk rnnttvltdf dgqysinalp tdvlvfsfig yktiavavnn qtilniqlqe
      121 tatnlqevkv nagyysvkes ertgsiarit aaaietqpvt nvlavmqgrm agvnvtqtsg
      181 vpgggfdiqi rgqnslrtqg naplyvidgv pyssesigyn qtsvgtpstt splnsidpas
      241 iesievlkda dataiygsrg angvvlittk kgkegkttvt insstgkgsa tkfidlmntk
      301 qylamrrqaf tndgitpypy daydvdgtwd qnrntnwqke llggtalitg iqatvsggss
      361 ltqfllsgny rnettvfagd frykkgglhf smnhqsedkk lkvsfsagyi sqnniqpgfd
      421 ltriaatisp napalydaeg nlnwengtfq nplsnldiqf ksvtadlvgn gvlsyeffpg
      481 fqmkssfgft dlrndetrav pstiynpayg igpeysslft ndtarhswii epqlqwhkdf
      541 gtdklevlvg stmqnqksdv lyqagfgfss nslihdfsss tykavynsse tlykylaffa
      601 rvnyninsry ilnvtgrrdg ssrfgpensf anfgavgaaw vfsdeplikd kvsvlsfgkl
      661 rtsygitgnd qigdyqfldt ysssgtnyhg iiglqptrly npnfgweknk klevaleigl
      721 lkdrifftaa gyqnlssnql vgiplpgttg faslnanlna tvenkgyeft lrtqniqdsh
      781 fswitnfnis tsrnkllsfp dlstssyset yvighslniq kayhftglnp qtgvyefedv
      841 ngdgvisapd dkqtvldfsp ryfgglqnqf syygwqldfl fqfvkqqnwd yaagyaggmy
      901 nqpaaiansw qqsgdttafq qftsgtngei vqaysnytls dagvvdasyi rlknialsya
      961 lpqhwsksvh ckislqgqni ltftnykngd pefrnpgylp plktynlgvq ltf
//
LOCUS       WP_091086616            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091086616
VERSION     WP_091086616.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112018
     Region          22..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklflisll flfvqttfaq tktitgtvkn kadgipipgv tvlikgttks svtdldgnyt
       61 inasstdalv fsyigfetke fkvtekttny sinlseelnt lnevvvlgst vrvtrkelgn
      121 avtslkaegl nqakpvdlss alqgkiagaq vsqnsgdpag gfsiklrgts silgssdply
      181 vidgvvlnna ttnltnlnvs kgnsnlqigq nrssdinpnd iesieilngg aaaaiygsra
      241 angvilistk kgksgdtkyt fstsmtsnsl rkkvyvnmsd kqfvnsspal fpiqgqpasa
      301 ttvlvagrnl etrtisgikr ydyqddvftt gigndtyfsl rggddktkyf ssigylkneg
      361 ivkntdferl gaklrlqhdf sdkltasigl nyitsssnek pdgnvfwspi nsititnniy
      421 dinqrssngd llavdpnrvn plsvienfki tqktdrmvsd iqlnfkpfen fnadfifgld
      481 nynqkgkvfi prypyapvng tyfndgyvse asnrvvqfnn dlnlrylwni tknikltsfa
      541 gyniqtyrde lfaiegrnlk pfvetinafn tllpgspnag eskynlwgyy lqetigfkdk
      601 lfitiagrqd astvfskenr sqfypkvsas yvisdekfmq nspitsarlr gswgesgslt
      661 aitpyarftn yatgnlignt sftlegfkkg nldlrpekss tyevgadigl lkdrvnlsfs
      721 yynadikdll lpvqlasstg stntiqnige mnnkgieigl rydvikkedl nldlyvnysr
      781 nrnkvtglpq qrfkldsnps gapvfvekgq pigiyygtyy arnadgslll ttagypqvek
      841 gdtstgtair dasgqptgti lnkqignpnp eyiisfganl nykkfgmsil fdgvqgvdvf
      901 dadyrtrqgv gsgelvekel ngelprgyiw siygieefrv vdgsyiklre vslsysfgkl
      961 nnffddltin asgrnlfswd kftsfdpetn sggqssvaky nfgtvpipks yslalkfqf
//
LOCUS       WP_091088982            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091088982
VERSION     WP_091088982.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115610
     Region          23..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikklilcti tilmssgylf aqrtvkgsvs dksgplpgat viikggtigt ttdfdgkfsl
       61 svpnnnavlq vsyigykavd vavgekttfn vmlagdaqal devvvnvsgf kekrdnmast
      121 ysvigvesvs kakeptlins lagkaaglsi tgtsadpgag sniqirgvss ingssplivv
      181 dgiplnnsnl egiasgssgg vsqqsrlndi npddiesiqv fkgasagsly gsqalggviv
      241 ittkrgkagk lkaslsstis idkinrrhal qtsygqgskg iysptsansw gdkiadrvgg
      301 adivntsgry feaadgslyy plvtknskdv frdsnfdqif qdglaqdvkl nlsggnergt
      361 fyfsashldq egiirqsnyf kntitfgnty kfndwlntsa kvsyinsssn riqqgsntag
      421 vylgllrnpa dfdisdyigt yydnvgtptp srhrsyrryl gdtenptynn plwtineqts
      481 etvvdrvfgs idfnvkatpw lnfvlrsgld tynddrtyff pmfsgdsank gryqneiykn
      541 teisadlisl msfdltdkls akvtvgsain drkrkqiyve aidflfnsrl qnpsiasikd
      601 eqeqnrrirn vrlygqssfd yndvlnlnlg ltyedasssv ksivypsvev glkfsellql
      661 dndsplsfak lrlaygevgl apdphgwetg yetatytgys dpisltafgg gyrlnddqgn
      721 pylefekkke yeagldfrlf knklklsgty yfnktddmll pislnpssgf dsllgnvasl
      781 qnkgfefefd ynflkrkafs lnlygnistn rsevtdlagv asvdfsagss iqsaavvgqp
      841 vgvligsaal rksdgsydld angfpqldts gnkvlgdpnp dwrgaagira nyknfslnvl
      901 fetsqgndla drtrfvlygf gthadvgnev tltqdlknyk gatiasgstv rgniqnfgng
      961 pvlldenwyt tlgggiggsv inefavvdas wtrlrevsls yslkgslikk tglesidlsv
     1021 tgrnlglwtn vkgidpdvnq fgtgvakgie yftnpssrsi vvgmninf
//
LOCUS       WP_091091572            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091091572
VERSION     WP_091091572.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117085
     Region          25..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngilv llvvlmaqlt faqertvtgv vsddagmpip gvsvlvkgtk sgaqtdfdgk
       61 yaikaapsqi llfsyigmkt qslsatstvv nvtmigtave legvvvtalg ikrekkalgy
      121 atqqvsgeev snvkssnfvn slsgkiagld iktsgnfggs tqvvirgnns iagnnqalfv
      181 vdgvpidngn sngasqqagr ggydygnaas dinpddiesi nvlkgaaata lygsrasngv
      241 vmivlkkgrs rkglgvtiss sltlgnadke tlpkyqnkyg agygpyydsa dgyfnladin
      301 gdgiddlttp ftedasygaa fdpslmvyqw nsiypqltet fgkatpwvag knnpnsvwgt
      361 sstavnsvsl dggtdkssfr lgftnllaeg nlpnsnikrn titfsgsqdl sdkltasasf
      421 nfikadgkgr ngtgysagnv mqqfrqwnqm nvdfgaqkda yfltgdnitw npngpsnlkp
      481 iysdnpywtf yenyetdtrs ryfgnvaldn kitdwlsamv rfsfdtysel qeerinvgss
      541 dvssyyrrns nvseynydam lnfnkdltek lnlegnigfn lrnnvrnsia aqtngglnlr
      601 slyslsnsvt pinapleyds ssmvdgeyir aslgydgfaf legsyrsdrs stlpkannrf
      661 dyfsvsgslv fsqlvdapwl sfgkvranya evgsatdpyn vfntfnigtp fngtgiasnp
      721 gaqanlnllp erqesyelgl emsflnrrvg fdvsyynnqn inqitaipls tstgysqall
      781 nagtienkgi evqfnatpfk ttdfrwdlnl nwtqnkslvv ellngienlq laslqggisi
      841 natpgqpygt irgsdfiyad ngqpiinqtg sasrigtyqr tgesnnvigd inadwkagln
      901 nsftyknlnl sflidmqkgg dvfsldtwyg yatgmydfsa annelgnpvr divtgtpgny
      961 gansggvilp gvapdgttnt vrananiyan awgyarapnk lhvydagyik lreasltynf
     1021 gaktldrlpf ttaslsiigr nlwiidkntp ysdpeaglss gnvqgyqsga ypsireigas
     1081 lklqf
//
LOCUS       WP_091091785            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091091785
VERSION     WP_091091785.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110198
     Region          45..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkislskgi ramgysfilg vsllsssisa nnslaystvq qqpskisgii tdgvgplpgv
       61 tiavkgrflt aisdyngeyv iaanptdilv fsfmgfktie isissqkivn vqlkedatvl
      121 qevkvnagyy svkekertgs iaritakdie sqpvtnvlaa mqgrmagvsi vqdagtaggg
      181 ftirirgqns lrsdaneply iingvpysse nigfsetsta tlgatsplns inpsdiesid
      241 vlkdadatai ygsrgangvv littkkgkvg qttftvnass gvgkitrfld lmhtqeylam
      301 reqafandai avypeaaydi ngtwnknryt dwqkeliggt aeinalqgsv sggstqtqyl
      361 lsgtyrkett vmpgdfqynk gsahfsmnha asdgkfkaqf sasyttqknd qpaadltyaa
      421 rslapnapal ytenaelnwe ngtwnnplan lnqkftsrty dlfsnavlty sivknlelks
      481 nfgytdtknn ekrtipstiy npsygmtsss sslytnntar rswliepqln ynlhrnkhki
      541 ealvgataqs ttterlhvig ygfssnalis dlasaslrlv ftsdeniyky qafyarinyn
      601 ydkryilnat grrdgssrfg dgkqfatfga igaawlfsne nflkdnrims ygklrgsygv
      661 tgsdqigdyq fhdtyvssgn ayqgviglqp srlfnpnfgw esnrklevai dagffhdrif
      721 ltaawfrnrs gnqlvgiplp gttgfnvlna nlnatvqntg leftlqaanf qtvnfkwsta
      781 initanqnkl lsfpnlqssp ysnsykigqp lsiqkvyhfs glnpqtgmye fddvngdgai
      841 aapedketia nlspkyfggf qntfnyknfq fdflfqfvkq qgvkylpgpg ggmtnqlqav
      901 snswqqtgds ssqqklttgl nydiisayyn ftesdgaitd asylrlknis lsydvplpps
      961 skikcrlslq gqniltitpy dgdpefkfag ylpplkmyta nvqltf
//
LOCUS       WP_091092166            1148 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091092166
VERSION     WP_091092166.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1148)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1148)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1148)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1148
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1148
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124158
     Region          67..1147
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklltkkkpr nfwlssqrwk asntavlllt aftiqvsaae sttknimfen ssaiikettn
       61 klnlvqkivt grvtnekges lpgvnilakg snvstqtdfd gtftievpdn vttlivsyig
      121 lqdqevtigt tplkivlkei geqmneviiv gygqqnrrtl stsvskldkk vlenvpysnv
      181 tqalqgnvtg vvvrtasgqp gkasnilvrg gtsidnpaga tpmyivdgvi rtqiddinsf
      241 diaslqvlkd aaatsiygar asngvviitt ttgkvgktki tynvstqssq igkkydfldg
      301 gnfirlsrlg iqnaadifgg trpnardnil tgatpagtgn nllkntpfat llksnlsast
      361 iselqakgwq eivdplnsan timykstnwn dvlfqtaitq nhtlgisggs dkgvfdlslg
      421 ylkgdgitif tgyqrftskl naslnvsdnf tlngrvlysk asnnqvvsns vvfnrylgna
      481 pttklyledg tlapgqnnin gnplyqmgkv kginennklq mgvdgdlkia enliftpsls
      541 lysetdagnt fqqaflsgsn gntdntrtat kfsnqltqiq yegvfsydks ldkigdfeak
      601 lgvskfdrti kafnasgkgs psdlaqtlds spipvsvfsn ntklvlnsvf grvnydyksr
      661 yfatasfryd gssslgpdnr ygffpgvsag wnaheekfws vmptrvssfk lrgsfgvngn
      721 lgtlgdfqag glysgatngi ansyngqsai vnsqiansgl kweqsqtfna gfdlginqdk
      781 irligdfynk ltsnlltnlt lpsnsgfstv ltnlgglrsk gfelelnanl ynrnelkini
      841 ganishntnt ieklpsngnl nnriggteiw daasssykfv gglqeggkig dfyahkqlyi
      901 lptqaaaday nlivrdnyvg ktsatggnpt gnkfagdavf edadnngvid srdrrfmgnm
      961 fpkfvggfnf nadykgfsla vrtdyslgat iynesrarfv gqfqgnygli seslqswqke
     1021 gditdvpryr wadqtnqnnl frseasgaay ntnqfqgnsr yyesgdylcl reitvsynip
     1081 eaiinrakls svrvyvtgsn lyyftkysgl spevqgidgg ssqglnsaga tgtypvprni
     1141 ilglnigl
//
LOCUS       WP_091093086            1007 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091093086
VERSION     WP_091093086.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1007
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110424
     Region          44..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknislnkgi ramlysliig lfltpllvma riplpksisq qqnitgtvrd sqgvlpgvtv
       61 siqgksigti tdyqgkysit atatdvlvfs fvgystlnip iagrtvvslq lqedatnlqe
      121 vkvnagyysv kesertgsis ritskdietq pvtnvlaamq grmagvnitq qtgtggggfn
      181 iqirgqnsvr rggnsplyii dgvpysseei gngmsmsvms mntnplnnin pidieslevl
      241 kdadataiyg srgangvvli ttkkgkkgkt rfsasvaqgt gsvphfmkmm nteqylamra
      301 eafandgite ypesayding twdqtrstnw qkelmggtsk itningsisg gseetqfmls
      361 gtygkettvl pgdfgynran vrssinhasa dqrfkisftg gygiqnndqp stdltteawr
      421 lapnapalyd aegnlnwenn tfenplrylk glskskthdl vantalsynl lenieikssf
      481 gytdlnhhes stfpstmynp slgigsetsr ifytdtkrns wiiepqlnwk ptlgvvktel
      541 ligsafqsqn ntslsvqssg fssnsmiynp aaatntsilg fdesvykyqs ffgranfnlk
      601 eryiinltgr rdgssrfgag krfgwfgavg aawlfsrekl lqdntvlsfg klrasygttg
      661 ndqignyqfl ntytpsnany dgvmglvpsr lynssfgwet nkklevaiet gflkdriflt
      721 aawyrnrssd qlvgiplpgt agfteiqsnl nasvenrgve ltlhtlnvkt tdfnwsttin
      781 faasknklrs fpdlesstys nsyvigqpln ivkvyhytgi dpetgiynfe dvngdgilte
      841 pedkqivkdl npayfggiqn tvrfqrwqfd flfsfvkqqn ynvprtlgva gtmnnqsvai
      901 vdrwqspgdv assqlytsga ngtaenalyq yaasdagitd asfiklknvs isyefserwl
      961 knvnckatve gqnvftitgy kgadpefagy gflpplriit vglqfnf
//
LOCUS       WP_091093292            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            gillisiae].
ACCESSION   WP_091093292
VERSION     WP_091093292.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium gillisiae
  ORGANISM  Flavobacterium gillisiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Flavobacterium gillisiae"
                     /db_xref="taxon:150146"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110696
     Region          45..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnsfykgr lafwclivfg flisytpals ktalkpiqys pqqnqisgti tdgtgplvgv
       61 titikgqqkg aisdfdgkft inalpndmli fsfmgfktlt ipvdghsila irmqedatsl
      121 qevkinagyy svkesertgs iakitakdie kqpvtnplaa mqgrmsgvni tqatgvpggg
      181 ftiqirgins iraegneply ivdgvpyssq slgfssassg ilagttspln ginpsdlesi
      241 evlkdadata iygsrgangv vlittkkgka gktkfnlnay ssfgtltrtl dlmhtdqyls
      301 mrreafsndg ittypgyayd vngkwdqtry tnwqkeligg tattnnlqat lsggssgtqy
      361 lisgtmhket tvfpgdakyg kgalhtnlth rtedgrfkin fsanytadkn ilppsdftyk
      421 aavlapnapa lydangnlnw eknswtnpla tlngrytgtt aaliantlls yqileglelk
      481 tnlsytdnrv eesrinpstm ynpafgigse rstlylnnas shswtiepql nwlkkigkse
      541 inilagatfq dqkssqlaqt gsgfpsngli ynlaaasrls issntfseyk yqaffgrinf
      601 nykskyilna tgrrdgssrf gpgnrfanfa avgaawvfsk esfldtstfl sfgklrasyg
      661 tsgndqigdy qfldtydvtg nnyngiiglq psrlfnpnfa wetnkkleia ielgfvndrv
      721 flstayyrnr ssnqlvgipl agttgfsslq anlnatvqns glelelrvep frsknfnwts
      781 dvnlslpknk llefpnless pyanryligq sisiqkvyhy tginpqtgly sfedydsdgq
      841 isspndqqwi edtapkwfgg fanqlsyknw smdflfqfvk qkarnylynt swagdmvnqp
      901 vaignhwpld glnsqtqlyt tgengealda wssysnssat isdasyirlk slslsytipt
      961 kgsaistarv ylqaqnlltf tnykgadpen qssffiaplr qislgvqlgl
//
LOCUS       WP_091098003            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paenimyroides
            marinum].
ACCESSION   WP_091098003
VERSION     WP_091098003.1
KEYWORDS    RefSeq.
SOURCE      Paenimyroides marinum
  ORGANISM  Paenimyroides marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Paenimyroides.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Paenimyroides marinum"
                     /db_xref="taxon:1159016"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113010
     Region          24..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskftwilt lffalvvqvg faqkpvtgvv ktqdgepipg atvmlvgtnq gtdtddegky
       61 tlnlkkgdki qvvyegfkpt tvtatdsgil nvtlveddsw lipevivdty rtvskeentt
      121 svssvtskti egrpnasiiq tlqgqvpgln imtgsgqpga esrvtlrglg singnteply
      181 iidgipmssn rfrslnpnei drvdilkdag ataiygnrga ngvivittkr gsfesdlsir
      241 yigttgissi qrnqynlmnt adyddfvrta rqdypgiggn lsnaqrsvnt dwtdvffnda
      301 ltqthtvmfs agsknlstft svgysefggt lkgtdlkrfs frtnldgknn sekltygtti
      361 nanfsrsnme nasgtngvnq nyflgafqsl pyvdpnsytn gydlfqdyla qrigisngmp
      421 lflmdkrats gfgqdefkll vngninykls dkfkisnqtg vdyqtinqns wtrydafney
      481 lfavqgqdyr gyvatidedr mvfntntnlr yedtfndvhk vsagvfleyl kahlrsknmq
      541 ktgfdpifws dggmtgwigg eenyqlyapt agmsrfdagl fsyfgtasyd ydrrygldat
      601 irrdasfrft ddnrwgtfws vsarwnisne kfmensvfnd lklrgsygss gnqditgggm
      661 fsgaqlydtr fisavgynge tglslgqlpn pnlqwevitq anigvdfgvw nnrlrgsvdv
      721 yqkqtddlyl nnplsainga sslnanfgtm rntgvevnlt gdiirnents lslrfvgayn
      781 knevieipne ngefwngtsl vgyregsmvn efympeylgi npdngnmmfr skdggvtenp
      841 ndgdnqwlgk ssmpvyqggf gidfahkgwf ltadftyald awrydndyyf ftaptfikqn
      901 nlsndmrdyw tpdnrdasfp altgsnfsya sgssfylqda sylrlryltl gynfnqkdid
      961 fmklsglrvy aqaenlytwt kwrgwdaess rsidygqypt prtvsvgvev qf
//
LOCUS       WP_091099567            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paenimyroides
            marinum].
ACCESSION   WP_091099567
VERSION     WP_091099567.1
KEYWORDS    RefSeq.
SOURCE      Paenimyroides marinum
  ORGANISM  Paenimyroides marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Paenimyroides.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Paenimyroides marinum"
                     /db_xref="taxon:1159016"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118227
     Region          45..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknprtaah flkmmlfasa tlstsyiwss pthsqnvial qqtgkiitgk vvdknnqple
       61 gvtvyvkgad ygtetnasgv felevpenat lvfsylgysd vtqtitganf lnivlhedte
      121 gqldeivita lgiareekql gysqqklsne tftdarsnnw vdnmkgkvpg msftssssgp
      181 mgstqvvlrg nrsvdsnkng alivvdgipi nsgmsssgeg ngylssdspv dfgngmsdin
      241 pediesvtvl kgagatalyg sraangaimi ttksgkknqg lgitfnsnls vdviqrwpdw
      301 qtqygsgtgk vfntngelyy syqasedgaa tqsnlgfgpr fngqyyyqyd patgtmgtqr
      361 tlwqnydnar kgfwrtgttl tnslsfaagn dkgsmrasvt ysdnewimpn tgfervaist
      421 kgdyeiakgi klnstmnyyn rssgnlpstg ynnhtisyfm iltnannnid wyrkmwldeg
      481 ktqlnspfst yldnpfalvn evinsansdt ftgnlsldid fsknlklmmr sginsqnefr
      541 elkrpydlvk fatgyyerqm iksqeintdf lltykgnetd hfnyslsagg nimsnkyrrm
      601 dasanglavp dvyklsnass nvytesadan kkvnsiyalg sfsyrnllfl dltarndwss
      661 tlpqgnnsyf ypsanlsfil sdavatplwi dftklraswa qvgndsqpyi iskyydnspf
      721 vgsaitdnql fnadlkpeet tstefgidar lfgdrlgfdv ayyntvsdnq ilsvpldyat
      781 gyssqyinag kvqnrgieam lyfspiktnn fqwkttftya knkneilela agieggeeqv
      841 latsgtvsii gkvggstgdm ygygfvrnee gkiiydantg lpvrpteety qgnayadwkg
      901 gwmnsftykg wslgvtldgs fggklysqsy hkmmehghln gslpgredgy iigdgvvqna
      961 dgsyspntkk vavpdyysey yrranveant fdatwvklre isisysfpks flerhklkgl
     1021 tvsafgrnly twsdfpiydp etaalnganm vpgvemgqlp spatygfnlk vsl
//
LOCUS       WP_091111012             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides psychrotolerans].
ACCESSION   WP_091111012
VERSION     WP_091111012.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides psychrotolerans
  ORGANISM  Nocardioides psychrotolerans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Nocardioides psychrotolerans"
                     /db_xref="taxon:1005945"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52345
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresk agetlvaata itaaqlttlg yevvvesgag fladqpdsaf eaaditvgsa
       61 ddawscdviv kvnaptpaei gllrpsativ slmaparspe lveqltaagv talamdavpr
      121 israqsldvl ssmanvagyr avieaahafg rqftgqvtaa gkvppakvfv vgagvaglaa
      181 igaagsmgai vrafdvrpev aeqvesmgaq fvtvdmtqev ssdgyaqemt aeqeaataam
      241 ydeevraadi vittalipgr papvlvraet vaamrngsvi vdmaaanggn celtvtderv
      301 vtdnlvtvlg ftdlasrlaa qtsqlygtnv vnlfklltpg kdgqltldfd dvvqrgitvv
      361 hdgtlmwppp pvqvsaapva aappaepvap kpppdprrkt yaaalgavtf lalaayapav
      421 flnhftvfal avfvgyyvis nvahalhtpl msetnaisgi ilvggvlqvg stnpaiaila
      481 tvavlvasin ifggflvtlr mlemfrkd
//
LOCUS       WP_091126620             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides terrae].
ACCESSION   WP_091126620
VERSION     WP_091126620.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides terrae
  ORGANISM  Nocardioides terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Nocardioides terrae"
                     /db_xref="taxon:574651"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52965
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresr pgetrvaatp atvkqliglg ydvvvergag elssfadeay adagatigsl
       61 sdvwgcevvl rvnapsedel gllreglihv sllapalnee lvdeltkrgv talamdavpr
      121 israqsldvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgav vratdprpev adqvrslggd ylaveveeqm vssdgyakat seaydrraae
      241 iyseqaadvd iiittalipg rpapklitaa dvasmksgsv vvdmaaaqgg nvegsvadqk
      301 vvtdngvtii gytdlagrlp tqasqlygtn lvnlmklltp akdgtvvldh ddvvqrgitv
      361 tregeklwpp ppvqvsaapa aapaerapek epkkpvspit rlalavlgla vlflvnatap
      421 dpipqhftvl mlavvvgyyv igkvhhalht plmsvtnais giivvgaflq latddtairv
      481 lafiavllas invfggfavt rrmlgmfrkg
//
LOCUS       WP_091129921            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091129921
VERSION     WP_091129921.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110442
     Region          25..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfifsfla llllptymmg qaqaikgkvv dssgmgvpga iitasesrtt adadfdgnft
       61 inakvgetlk ismlgfdsvs ipaavgdmki tlkeagdtal kevvvigygt rkkidntsav
      121 aslkaedvtk tkvlnasqai qgkaagvqvt ssdapgstps vvirglgtal ggrnplyivd
      181 gmpteninni ntnditsyei lkdasalaiy gtraangvii ittkkgkgdk vsvevesfag
      241 vrtplkkvkm angdqyaays naalgtntfa anqpvntnwl deitrtgsyt qnnvsvsgas
      301 enikyffsag nyeekailng ldysrttfrn nnefklskkv tlnqnlsfts sksapkplga
      361 ftnaykqspi vpvrfadgqy gvsrvdangv agsvgssfnn vgnpvaqldf ydeqqrsvtl
      421 qgglkldwei idglkftsqf ngeyynwkqy nfedkqgiwm aanpnttaad yvathasdpv
      481 nlltrgreey fnwnlsnyft ynkvfanihd veltagieas vkgpretlti arknvsensn
      541 ywslyntkda kgvdyvadit slydikynes rlasyfgrvq yklmdkylft gtirrdgssn
      601 fakdyrwgtf psfgigwvmt kesflsdikg vdliklrgsw gklgnqnvpl ntqayasgln
      661 aylggsllyq gttinsqidp slswevteea sagvdfefln nrlkgsfdvy dkntnnviln
      721 tkpyttsgmt istpahvgev snkgfevalr wddkindnls ywvggnfshn tnklaslkdf
      781 displiggnl gngqdtkiln ktsvgqplgs fylyeyagid ptngkmlyyn aagdkvtqnl
      841 ldankdkkyv gsilpknnyg vtlglnykni dfsvdgygtg gakvyngkka qrftgeniea
      901 sltnnywtpt nttaanpkpf nevpvastyy mesgdffrin nitlgyklpl tetsfinycr
      961 lyvnainpfi tqkfsgfspe lngngdpygt qgieldaypt lrsfviganl kf
//
LOCUS       WP_091131189            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091131189
VERSION     WP_091131189.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112182
     Region          23..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrilavlgv illsslsaaa qnrlitgivt daenkgivga sievqgkpfs aisdaegrfr
       61 mnvpegkvtl nvssigfqsq svavqekdtr vavtlvettq elkdvvvtsf gvkkqkkslg
      121 yavgelkged ltknkeinlg nalqgkiagv nvsapvtgps gssrvvirga tsasglnqpl
      181 yvvdgipidn tqqgnagmwg gadkgdgmss fnpddiasms vlkgsaasal ygyrgsngvi
      241 littkkgkng tgigvdfstn ssfntpasll kwqdqygaga pnasgvptrf nnlqelrdsy
      301 yfawgdkydg tpslsldgkt rpyqaygkdn venfyrtgys fsntlaisgg nestnfrlsf
      361 gntkdesimp ettfgrnnva lslnsapnkr isiesnaqyi sekshnrpyl ndsprnpsfp
      421 ttfmtpgsdi rwlsnpydan ggeedflgan vyhtnpyfat ksplnddlrk rfigsakvny
      481 nitdkiyaka vigiddinye yteieptgin ynpggsienr ietrsevnas gflgykgdia
      541 kdisldafig anrqhnrysg ikmkgnnfiv pfkyfygntq pdkteklfse sevnslfysa
      601 digykdflfl sltgredwfs tldpannstf ypsvsssfiy seviglpewm sygkvrvgwg
      661 nvggalpday alaltyttpd gqtdslgqpi lgvngetipn rtlkpynvst iefgfentff
      721 nnrvstdltf yskkttndit dadvsqasgy rttkinvgei lnkgvefavn vkaiktpsfs
      781 wnvaynfayn dsevlnlsdk ittktlegnr dgranvvlek gqpfgvikay dylrdangni
      841 vlgtdgkflr gnliiagqgv aptsmglsnd fsyknftlsv fvdakfggei ysatnqlgtr
      901 yglseitlpg rengvqvngt dvngnpvntn vsaynywrsy sdvtsnfvyd adfvklrais
      961 faynfpkayl qktpfqsvsl afsahnlwti ydkvpnidpe snysnsnaqg merasmpltr
     1021 nygfalnvkf
//
LOCUS       WP_091131810            1236 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091131810
VERSION     WP_091131810.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1236)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1236)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1236)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1236
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1236
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=137314
     Region          143..1235
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkpvvkqrl lhqimkitlf qfvlalvfss vtlannvngq kkldtkvtit vdnltldnal
       61 skieksahvk fsynsrlpql gekvsieanq etlssilsri lvpfnitfse vsnqivlqks
      121 avsfsnsnnh dslfeilafg piikgkvtdq sgsplpgatv lakgtktavl tdfdgnfsie
      181 mpanvdrlvi syvgmetkei gisnptptvv lteagqnlke vvvttgyekt skrtftgais
      241 kisgaelkvd gvvdvsrmie gkaagvtvqn vtgsfgatpk itvrgsssif gdtkplwvid
      301 gvvqediinv tfadlasgns atllssavag lnandiqsie ilkdasatsi ygsrslngvv
      361 vvttkqgrrd splkinysve ntvrtvpsyt qfdilnsqes msvfqemrtk gyldqssslt
      421 srfsgvygil akqinlydss ngqfgvrneq pyinqflkky elantdwfkv lfrpsitqnh
      481 slsfsgggkn ntfyaslgyy tdpgwtvadn vkqlsanikg tfyindklni tlstlgsvrd
      541 qeapgtyesk ndvvfgkvtr dfdinpfnyv lstsrtlrpy dengnleyyq nnwapmniln
      601 elenntldik vndirfqtdl dykinknlty nltasaryan tsrehkiyen snvvgaynag
      661 vgetlntqiq kdnvflyqnp ndltapkvsv lpnggflrky tndmtsynvr nsityrntfn
      721 ekhelegffg tefrsvdrnn dnftaagiqf ekgltafidp klieklvneg nsyydfgaer
      781 ertvgffgkv gytydrryta svtgrydgsn rqgdtgssrw lptytvsgkw nikeesfmkd
      841 vesvntlalr asygltatag patnslaiyk sfitdrfavg drenairied lqnkdltwek
      901 qyetnigvdl gmfrnrvqft tdvysrkafd lidyvitsgv ggqsvkqgnn admetkglei
      961 gfttqnivsk dfkwsstvnf siydqkitkl ankpavfdli atnggntvgh prnslysyqf
     1021 tglnneglpt filqdgaenn iteanfqdtn dvtkylkyeg svepnksigf antftyknls
     1081 lyvfivgsgg nkvrlnpvys ntyndqtvft kdfanrwinp gdenytnvpv iadkllnrny
     1141 gandlqiayn tynfsdvria sgdfvrlkni slgwefpsdy krklglttfn lkasavnpwl
     1201 iysdkklngq dpefrntggv afpitsqytf ainisf
//
LOCUS       WP_091131951            1186 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091131951
VERSION     WP_091131951.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1186)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1186)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1186)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1186
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1186
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132314
     Region          52..118
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          132..1185
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkhnseky fseryhyyly lllmrsvtaf iwismcslya npslgqnkih vrfkntplte
       61 vfstlekqtn yvffynddvl ksantitldk datleeilnn aftnnnltfd iidkqvivkk
      121 nkkkaeqley eltgkvtdkn gapmvgvnvv lkgkqtwdit rkegdyrmrv spydtivfss
      181 lgyktvivav nnkriinatl vpdvmelhsv eipasngyte iprervtgai gvigakelae
      241 vptvdiqsrl egklagvnvd prtgsisvrg tnnfsgtgqp lividgfpqs redfafskrg
      301 vpgtsilsfl npddvesitv lkdaaassiw gsmaangviv ittkkgkkge psitfnttts
      361 igekidlgkl rvmntaqyid yekdlvaggf vadnisnwqa lnpsaaqeim frqkrgqisv
      421 serdallsql sqndnlgqin ryllrnsvtt qydlsinggn ekstyylslg ynkdqaamqg
      481 nnsqsynitl nnsfqlksyl klntgvnyvp styqnnnvan ealsnvsata lrpydmiade
      541 ngkgidryfl frpevakgfe akgylpwsyn yldelnysnv itkganlrln asltatitdw
      601 lnfeasgmyt nitnkiksls eldsyytrnm inqatsvnta gklvygiplg sylyntnssn
      661 dtqsmrfqmn inknfnenns lhflagseir eerregssqr yygynidtns gqsvnptvyy
      721 ttvygwqsii gstdnsisks rnrylsyygl gsydyknryh vsgsirfddf nllgasrknr
      781 alplwsvggk wdinkeifls dvnwlsslal rvtygksgss paggfgsqsp visigsvdfn
      841 tqlptasisi penpeikwet tatlnygldy gffknrlrgs ldlyykktnd ilaslpfnpt
      901 ygwsfvtynt aslkghgvdl slsgtvinta fkwntnfnfs yntnevtdsr yvlnstnqyf
      961 gsaamvgnsi gtiyaynwag ldatgqsqvy kkdgtivnst qgiaaidkdd lkkmgtsfap
     1021 yfggflndfs fknfklgvqi tyyaghvfrn tvlqnypsys gvqsgavakd elvanrwrka
     1081 gdeaitnvpg ltnisfnsln ryqmadinvl padnirlqqi slgynvpsew lektfiksls
     1141 fnfaarnlgl lwvkndlgid pqylsnanyn tlapqrnysl qfnctf
//
LOCUS       WP_091132992            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091132992
VERSION     WP_091132992.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109351
     Region          22..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiflifmi vftaqvslaq vksvkgvitd sdgmplpgas vavqggqkgt ttdfdglyti
       61 evqkgqslvf tyvgletqti vvgdaatinv klvqgasnal nevvvtslgi kktrkslaya
      121 aqelkgeelt rvkdanlint vagkiagvav trsssgaggt tkvtirgnss fvnnqplyvi
      181 dgiplyngga gqpngtfgdl nggnkdggdv vslinpddye gmtvlkgaaa svlygsqgan
      241 gvillsskka kagaesfnvn svttfetaay lpefqsdyts npgdprswgp kqkvegdkei
      301 kdffevgntq itsmtftkat dgastalsya ntngsgiipg nhikknnfgi rqtskffndk
      361 lsvavtanyv tqtinnrptn glyfnpiagv yshpraftln dlktyevfdp vknmmqqnyp
      421 gfatvnesne npywqinrqk svdknnfftg aialdykiae wfhltsrysy nrnesnfqkg
      481 mygssatslv hptgryinsn ligtqnyadl ialfntkind nfsfngtlgt sinhsrttgl
      541 tidsgigggl vydniftlgn fvnnngnvqt gserevqsvf aaatfgykdy lfldvagrnd
      601 wsstlantqd pgyfypavga tailsemttm pefvnygkvr atfaqvgndi astitsptss
      661 ivagnivnpt vgprrgtslk nelkselelg tewrffnnrl gfelsyytse tknqflqvpa
      721 estnpdgftf yginagsisn kgfevvlfad ivrgekfnwd trinfsqnrs rvndipsest
      781 ggrivltdpg snsyryslie grpfgviegf dfkrdaqgri lvnddntlqr tdwkeignan
      841 pdfmlgwsnt fklgaftani lldgrfggev lsltqaindf ngvskatgda rnagtvning
      901 vkasdgtavt smdpyeyysn vagrngvssq yiydatnvsv revsigytfn ktklpvfqta
      961 tvsliarnlf fiykdapfdp nvalstgegl qgvdvfgmps trsiginlnl tf
//
LOCUS       WP_091133159            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091133159
VERSION     WP_091133159.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123758
     Region          22..1111
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkilhalll flaiagysqe srtitgiiqd eadlspipga svfvennsis nktamagiih
       61 seaigttsdf dgkftlkigk nvtslrvtfm gyksytlels aqksytvnlt setaklqevv
      121 vtgyqkiekr kltaavskid msaiqqtgvs sidqllvgqi agvavstpsg apgapakiri
      181 rgtaslngtq dplwvldglp legndvpkny dkdnidqlnn fsiaglnpdd ikditilkda
      241 aataiygara angvivvttk kgkagkmvis fntntfitqr pdfdklnlmn asqkvdfelg
      301 lasradltyr ddageisril ngsnelaayr aggfsalspa tqqsindlrk nntnwgnliy
      361 qtaintqhgl slsgggeksd yyfslgyyde kgttigtgfk rynltlknnf eitdkfkvgv
      421 gifgsenktt syltdtdayt spssysrnvn pyltpynadg sykydqdisg ysdryvpfni
      481 leerantshd lktraikall daeykitrdl kvtsqlglql dnsssekfad kntyytrkek
      541 ersryftnga fnyflpeggi iqnantdffq ynlktmvnys ktfgekheve amignelrrn
      601 ytttiatkgf gfdkntlttk pimfpnssfa ndaiyrtyqk senenafasf fatasytynk
      661 kysvfgsvry dgsdlfgvdp kykylplwst saswavseed flkdnltlsn lrlrasyglq
      721 gnidkntspf vmgrysntti lpgqteqtis vesppndklr wekttntnlg mdlglfnnri
      781 sivtdfygrk stdliglrav pfengfeysn mnwaqvsnkg yeitlstrni drpnfkwnts
      841 infshnksnv drievrdtdl lpsregrpvn avfglktngi dengyplfvn kngetvntqt
      901 ffklydpyad ffpgeltess ltpaeyrdlf vylgdrdpkf tggitntiqv hnfdftvaaa
      961 fnlkqtvvkt ppyngtevdr gqnystdiln awsptntssn lpgivgkdsg tgdswmayqw
     1021 fssgtpldwn kyldtwvsem symrlssmrl gytfpkaftd hiniqsirls vearnlfvis
     1081 sdfkgyfdpe tygniyaqpv pksftigcnv tf
//
LOCUS       WP_091133784            1007 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091133784
VERSION     WP_091133784.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1007
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111876
     Region          45..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnisfykdg ralycliftg illsfsstfa snptrlfksi fqqhkvqgnv tdgtnplsgv
       61 tiavknksnv tvitdyngqf eitcapydtl tvsylgfkta fiavqgrtki avklqydttt
      121 lqevkinagy ysvkesertg siarisskei eiqpvtnvla tmqgrmagvn vvqttgapgg
      181 gfdikirgqn slrsdanmpl yiidgvpfss dpighfqtss pfptvsspln sinpdsiesi
      241 evlkdadats iygsrgangv vlittkkgkk gktsfsvnss tgagkitkfp dlmnteqyla
      301 mrrqafindg laqyndwdyd ingtwdqnry tnwqkellgg taqindlqgt isggseqtqf
      361 llsgnyhqet tvypgdfryk kggmqlnlnh isadgkfrit fsggynsqnn nlpaydlsfd
      421 arylppnapa lynpdgslnw engtwenplr nlnaqfrsqt sgliantvls yeiakdltik
      481 ssfgftdlks setrtqpsti ynpaynitsa rsaiylygtd rsswiiepql nysraiakgk
      541 ldaliggtfq sqtndilyqt angfssnsli ynlaaaknit iysndqtqyk yqaffariny
      601 nwqqryilnl tgrrdgssrf gpgnqfavfg aaggawifsh enfladsswl sfgkirssyg
      661 ttgndqigdy qflntyttsg inyggmtglq psrlynpnfg weinrklefa lelgflqdri
      721 fttaswyrnr ssnqlvglpl pgttgfpslq anldaevenr gleltlrtin fngskfkwst
      781 sanisfaqnt llrfpnless tysqkyrigq plniqllyky kgvdpqtgiy qfedlnkdgi
      841 isfpddrqta vdlnpefygg lqnqlsykkw nldflfqfvk qksrtypmgp agmmsnqlqr
      901 mnqtwtqsdn iapyqiattg ynyeavmgdy yytfsdgtva dgsyirlkni alsfdlplgl
      961 qetgckimlq gqnlltmtkf kdgdpefgga gflpplkiis agiqltf
//
LOCUS       WP_091134119            1122 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacterium].
ACCESSION   WP_091134119
VERSION     WP_091134119.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium
  ORGANISM  Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Flavobacterium"
                     /db_xref="taxon:237"
     Protein         1..1122
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124987
     Region          55..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnfirikmg pngvsgfslk tklmlfcilf slsqvhgytl sskgaaksqn vqqqknitgq
       61 vndengmplp gvtilekgsk naaltdfdgk fslkvenena vlvfsflgyt ntevsvkgkt
      121 ivnvkmqrtt asleevvvvg ygkmkkkdlt gavvqvspdr lvnqnpqtvq dilrgtpgvr
      181 vgydpsakgg gniqirgqts vytagghnsp liildgmqfy gelseinpdd iaqldilkda
      241 saasvygsra aagvilistk kgktgkpmvs fstnttisnk sayrkvyspe gylkyredwe
      301 taqtygvnta tgqyeafiag tvangkpgyf snpndlskwg iteaqwlayq pasqtngkss
      361 kevwgarlgl nfdpslmanf lankthdwsn ssfrtginhd nnlsisgaad rvnyyvsfgy
      421 lksegaivgn dykaarsnmk vdakvtdwld lgvnvnfqdr sdgdvtpslg tnagdnnmmr
      481 tspfgtfida ngnyerqpmg knvsgqnyny yyerqfidke tgyttlntif nakvtlplgi
      541 tyafniapry qffhdryfrs tqnpnwpaat tgvnrnnstr fdynlnntit wdytiaqkhh
      601 iiatfvqeae errfwsdgmd ayniqpsdal gfhlvntatm ansalrsndt hetadalmar
      661 lfysfdnrym ltatvrrdgy safgasnpya vfpsfgvawn fknekwfnwe pmstgklrls
      721 wgkngnrsla dpyvslanlv ntgtmgylda sgkaleikyl aldrmanpnl ewekttstni
      781 gldlgflrdr itatldfyka sthdmimsqs lpgftgfsti atnlgevqnq gfelslntln
      841 mkkpnfewrt sfgisynenk ivslygnmvd ikddngnvig kkegndsang wfigrpisqi
      901 wdyrvtgiwq kdewkeaqky gqrpgdpkva nsytaddida vdsdgkpykk avynekdkqf
      961 lgnsnppvqw mlrndfkiyk nwdlgismya nmggkslnsn ymntfndasl ykfnfnpyvn
     1021 pywtldnptn dwarldakgp agtpvapgrl ydrsfirldn islaytlpkd lmdkvhiksi
     1081 kiyasvqnva twaaskewky fgdpetggla trqfnlgfnf ql
//
LOCUS       WP_091134312            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091134312
VERSION     WP_091134312.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116895
     Region          27..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkinfrki avlffvlltk ltfaqdrvvs givsdengvp lpgvsilvkg tqngsqtdfd
       61 gkysikaean avlvfsfigm qtkevqardk nvnvkmsags tqlqeivvta lglkrekksl
      121 gyatqeingd qltkintgnv snnisgkiag veirrnnnig gstnvvirgt tsltgnnqal
      181 wvvdgivlnn dntnsadqks ggnvggydyg naasdinpdd ietmnvlkga aatalygsra
      241 sngviivtlk kgsktkgglg fdfssgvnvg vvdkktlpey qnqygggygd fygtvdlgsg
      301 vhpyaatdda awgpkfdpsl lvynwnsfyp elptygkatp ytavknnpns fyqnsltyin
      361 sisfsaandq gdfrfgytny nqqqgilpns nnrkdnfnfs gsykvtpktr istsanylts
      421 naigmnetgy gdggnnylss vrqwyttnad fgdlkeayei tgknttwnvg spdnlavqfh
      481 dnpyfqrynn ynslkrdrff gnvvvktevt nwfdimgrga vdfyhqlqee riavgskrtp
      541 nalgqysryd knfreinldl vlnfkttitd ginfngmlgg ntrrsvnnsi yavtngglvv
      601 pgiyaltnsi dpinspdemq qtlgtnsvyg masfnfldty flegtyridq sstlpkdndt
      661 ysypsitaty ifsnhikadw lsfgklrlny aetgndapfa vtstlypknt nfgpggirfs
      721 tdnsrsnsdl kneltkgvea glelkffknr lgvdfsyykt nttnqilsie tptqtgytra
      781 winggdvqnk gfevtvnatp iktkdfswqa tvnwstnkne vislggasqi slgsfqgvny
      841 vaevgkpvgq lvgsgytyln gekvirsngr ylqsagvvig nvapdwiggf nnvltyknia
      901 fnflidvkkg gdvysldqqy ghttgiyest vsnnhngvpq repvtqgggi lldgvkqdgt
      961 pnnvtasvtg tdgyyfynsm pqqqyvydas yvklreigls yklpkrflen tfisnmvfal
     1021 ngsnlwiihk nlpyadpeag assgnlqgfq tgvlpttkey sftmkvqf
//
LOCUS       WP_091134658            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091134658
VERSION     WP_091134658.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116119
     Region          25..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqklkglmm lffililqss iaqekkitgv vsdnagiplp gvsvlvkgtk lgtqtdfdgk
       61 ymikassnqv lvfsyigmkt seitanssvi nvkmldagaq elesvvvtta mgikkqkrsl
      121 gyatssvsak dltdvtnvnv feslsgkvag adittpaqag asskvvirgf nslsnssply
      181 vvdgtpinns sngggttadg ksinstrsfd agngisdldp nniesmsilk gaaasalygs
      241 raangvvlit tksaknkski sidfltstdf nqvarvphlq nefgqgwsgl systwsgvan
      301 anntasneng swgakyngev rpwgaiingv qqakpyvalp snikdfyttg ttftnsmris
      361 gggensnfsl nastvnsdgi fpttadaykr ntlginagis tgkftvrtsv nyinknqnvv
      421 ntgqggtegg tvaqalaqtp rdidvvglkd yknnpyntps nlyspyvdnp ywdlqenstn
      481 ikgnrffgnv nlsykitdkl tatyqiggdy rnekiksyga imdyfpgsan adaskapvvg
      541 gvtektaeni etdtnfnlty vtpvgkdfsf ngmigfntnq rsgsslkanv tnldvpnfye
      601 lsnsilspiv vqddylrrsy gvfasveasy kekiyltvtg rndwtstlpq gknsyfypsl
      661 slsgvvldnt qhfvklrgsi asigndtgyy qtkssmipan aalgfgnill piggvngyel
      721 sgnlgnpnlk pertteyelg fesnffnkrv nldfsvyhkk ttdllfsrpl aastgftsqt
      781 dnildlqnrg vevvlnvvpv kvkkfqwdft ttfsknvskv ldiaygldkl tlasmygvnf
      841 vaekgqplgm ftaftprltp dgrpivspst gyytvgndqs nvgtsqrkfv mglrnnfkyk
      901 nftlgssfdw kqggkmysyt krinefsgng iettfndrnt yiipnsviev kdatgnitya
      961 entvpmttsk vtsfwntssn pgieaghvid ktfirlrdlf ltynvpttfv qkfkiatasl
     1021 siygknlfmw tpkanpyvdp elstygdgll seagefatnp sqrsygasfk vtf
//
LOCUS       WP_091135089            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091135089
VERSION     WP_091135089.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123371
     Region          29..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqalikrcs fllftlmsvl syaqsnqvtv tgavtdnvsg llpgvnvtek stkntvttdf
       61 ngkyqikvkp gatlvfsfig mkkleipvng raivdaklse dsnvlddivv vaygtqkknn
      121 itgaiatlkp ddfqdlpvsn lseslrgltp gvsvsggstr pgdaaslqir qtfgfskdgn
      181 sniplividd mvqvdpqngk ptldtfnqld pseiesitvl kdgsaaiygs rasqgavivk
      241 tkrgksgktk ftyysqyain davshsktmd ayehgiwknr flnsnleadk skyfsaaele
      301 qmkgldydwl kkawkpaiqq rqsisasggt ekatyfagvt yfdqganlge qdykkwnfrt
      361 gtnikisqdl efsasvsait tdvnksfska sanlndssfg saaggeqady ayllhmpkyi
      421 pwdttvngkt ywmspfprtd rnlgsansnt tiagwnyfag ldagkqieeq fsynvnlsle
      481 ykvpflkgls lkgsfarsqs snyteqyqlp ydlaritnyq ladnhlenpn siyavetnir
      541 gsrvyyttdl dkliqanffa tyartfgnhn vsamfgyeqs eawnknvrla yegtskdflg
      601 nsttagpist nsqavkvesg tqsylgrlny sfkdkylvef ifrsdastkf apqnywgffp
      661 gaqlgwvvsk edwftdnvsw innlklrysi gktgkdnidy wrwlqfyepl pdkgvqfgsn
      721 ggllgggitp rpnpnenvhw dttiknnfgi dvsflknrla vsadfyydks tdmliglage
      781 agtpitvggg faevnyaaid awgsefslnw ndkikdnfsy svgvnfgfsn nevkkypdla
      841 rtdantnite vgsstyfpty gfktwkgtst gdgilrtded vtnywnylte ratavggvpt
      901 ymginnvtam rkgmlayedt agvynattgt qagadgrimr nedyvklann srvygfttnl
      961 gfkyktvyfk tqiqtswggy raidlvkqgt ssahndwahe sfwtdmydat dnpngkypnm
     1021 aqqdyifaps dfwqldtfrc vvrnltvgfe lpreamkqin iqkatlgitg nnlwdlynpy
     1081 pdhyrnmydd sasryptlrt wsinlnvsf
//
LOCUS       WP_091135152            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_091135152
VERSION     WP_091135152.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119217
     Region          43..108
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          125..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myfkpsylnl ksfvflvlal lafqsgyskt nllkepkvtn kiekatlvsi fskltqqtdy
       61 kfsygqavia dntvyavnyn sesitailnd lskkanfnyn ingklvliqk taapkavntk
      121 avdrikvkgk vvdenklpip gatitetsss nstvtnfdge feitvgegkt idisymgykt
      181 ktvavqtgfm tiqldpntae lnevlvvgyg kqskkdvtga vtqleaanfk qgvnvsvdnl
      241 iqgkvagvrv vntsgepgag vnvtirgvgs irsgstplfv vdgvplsndd vspsgsnvgf
      301 gtssaknpln flntsdiesi tvlkdasasa iygargsngv vlvttkkgsk gegtltfdty
      361 tgvatvankl dvlsaseyrn aikdkafdhg gntdwqdviy rtaittnnsl sfskqtdsgn
      421 yyasiaqmdq egvvrnsnfk rlsgrinaae sfldnkrlkv kmnltasetk ddgvptsddg
      481 gsngqlivht lmanptrsvf dangnytnfn mnahynpayl lsiyqdqtrt lrvlgnleas
      541 lriidgleyk lnigvdrsma ernttifpnl tdlnpkgkyv qnnldsknsl vehyltynln
      601 ldkhkiealg gfsyqkfers gtsfsidgia nqgegvppsi npgfkgtqsg ttgyaqenel
      661 qsyfgrlnys fdnrylltas mrgdgstrfg knnkygyfps falgwniane sflrdsstln
      721 nlklraswgq tgnqevenki tqasyslsga dgyylyddln lvngvsvnrt pnpdlkwevv
      781 tqynvgldfn lwndklygtl dyfnktttda ilnvpsqals ptttiwtnid gkiinkgief
      841 mlgskivdtk nfswnidmng atlhnkiedl pvseiltgti sgpgqsgvna niyksgyaag
      901 sfyllehigf danganifkd qngdgkidns driiiegalp tfyygfnsdm ryknftfsfs
      961 iigqtggyll nntglnalni nnlasdrnva tnyyesganp anspilstlf leksdfirln
     1021 tarigynfdl kglnwinglt lyitgqnlit itnytgydpl inspksnggn qsigidyasy
     1081 ptsrtfsfga tlkl
//
LOCUS       WP_091137099             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosospira sp. Nsp14].
ACCESSION   WP_091137099
VERSION     WP_091137099.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira sp. Nsp14
  ORGANISM  Nitrosospira sp. Nsp14
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosospira sp. Nsp14"
                     /db_xref="taxon:1855333"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39466
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipvetr ggetrvaatp etvkkytakd lhtvlvqsga gagasipdea fqaaganivg
       61 saaelygqsq illkvrgpep gelemirkda vllgllsphq aegieslarh gltafamerl
      121 prisraqsmd vlssqaniag ykavlmaanv yqkffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avieafdvrp aakeqveslg akfvevplsd eekaqaetag gyaremsddy
      241 krrqgelvhq rasaadiiis talipgrpap vlikeetvra mkpgsvivdm aveaggncpl
      301 semdkivvkh gvhlvgisnl pglvaadasa lyarnlmnfl nlmldpknge fvmnredeii
      361 agtlvctgge virkt
//
LOCUS       WP_091137494             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            guangxiensis].
ACCESSION   WP_091137494
VERSION     WP_091137494.1
KEYWORDS    RefSeq.
SOURCE      Microvirga guangxiensis
  ORGANISM  Microvirga guangxiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Microvirga guangxiensis"
                     /db_xref="taxon:549386"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39214
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsete gaetrvaatp etvkkyktlg advavqagag akagitdaef eaagaaiass
       61 reealkdadv vlkvrrpaeg elsgvkpgal viaimdpygq daalkalada kvaafsmelm
      121 pritraqvmd vlssqanlag yravidatae ygrampmmmt aagtvpaarv fvmgagvagl
      181 qavatarrlg avvtatdvrp aakeqveslg akfiavedee fkqaetaggy akemsaeyra
      241 kqaelvashi akqdivitta lipgrpapkl vtkamvesmk pgsvivdlav erggncevsk
      301 pgkiathngv kivghlnvpg rlaatassly aknlyafvet lvdkesktls vkwddelvka
      361 tcltrdgavv hpafqpaa
//
LOCUS       WP_091140444            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            caeni].
ACCESSION   WP_091140444
VERSION     WP_091140444.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium caeni
  ORGANISM  Flavobacterium caeni
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Flavobacterium caeni"
                     /db_xref="taxon:490189"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110658
     Region          21..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvillvfl fclgpitafg qqisgtvsdk tglplpgvni nsatgksavt dfdgkfsida
       61 aagegltftm igyvtqslpa sanmavsmpe eenklnevvv vgygtrklgs itgsvsliks
      121 adivktpaqs avqaiqgkaa gvnivandep gaapsirirg lgtilnsrdp lyiingveay
      181 glngispndi esinilkdas slaiygqkga ngvvivttkr gkqgdikvsy dsyfgqkdvl
      241 kkvkmadsyr fsyynnsalg dadyfnmnsq pystdwfeei trkgevtnns vsitgatekt
      301 nfsfgvshyt esgillgtey krtnfinrne yklvddkvki shfvngsieh gtpkplsaft
      361 naykqspimp vrypngrwgv plvnlatgqn dlngtaynky nnvgnpvaql tnthdksrlf
      421 tltanvaaei klykdltfts sfgstakwyk aysfvptrei wlsqnpteda sdyattqsga
      481 pvnslsqtrg eefdwnwdny ltykkewekh altvvagisr ttrdndeylr vmrynvpeqr
      541 nywyldfsss neevapksli tnnhltpivs layfgrveye flerylltgi vrregissfq
      601 gdkkwavfps vsagwvvsne aflrdskivt nlklrggyge lgngngpsfn ftsftpnvny
      661 pfgngqvinp gsyidaavdp nltwesmnel dlgidfglle nrltgtfdyy nrksenlilp
      721 vqvpyvlseg esyvnsgeit nkgieltlrw dgkigdnfty yiggnlsknk nevskidspy
      781 fqnfsgsgsl gngeftklvk lgeplgsfyv feqtgydsgg vptyrdtngd grltsddrin
      841 agsyipdvty gfnigftyrn idfsadaygv sgnkiyngkk aqrfggenie ydilddfwtp
      901 snpnaenpkp nndvprasty yiedgsflri nnitlgytlp kmfdkldkvr lyvtavnpfl
      961 fteysgyspe ivgnenanpl rtagielday ptnktflvga nvsf
//
LOCUS       WP_091141132             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            caeni].
ACCESSION   WP_091141132
VERSION     WP_091141132.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium caeni
  ORGANISM  Flavobacterium caeni
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Flavobacterium caeni"
                     /db_xref="taxon:490189"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107526
     Region          37..977
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnhtkttart pwalqslali ltlllsvgsf aqdkklltgv vsdnagvalp gatiletatk
       61 ksvvtdengk ytievtsgnt ieisfigfet hiavvnastp stlnvslkes atmldavelv
      121 svgygkmrks dltgsistvr gddlvkgvva steqalqgkv aglsiiqgtg dpasgatmrl
      181 rggtsltann splvvvdgva gvdinivqpq diksvdvlkd asataiygsr gangviiitt
      241 kagtksssvt ysgltgisea annldllsan qwrqyvrenn iadavdyggn tdwqkelqqq
      301 gfmqqhnlgl tsggeesglr aslsylkneg vikttelerl sgnisgyqya lnkalkfdvg
      361 lfanidkwhp ldyrvfersf nlnptipvyn ndgsftevgg tlyenpveil tnrrvdnerh
      421 rllgtfktea klfrdltaia nlslehnamq gatykptyav legrtengya qrtyseytta
      481 qaevylqyar efgkhnvnvm ggysylenvy dgfgaqrsgf etdlfsynnl gagsnyrlgd
      541 vysykgksnl vsifgrlnya fdsrymltat vrrdgssrfg dnnkwgvfps aavawtisne
      601 kfmdatdnwl tnlkfragig vtgnqdgige ykslsilgvg rdsyydpetg mwslayapiq
      661 npnadlkwes trqtnigidf slwnritgtf ewyqketndl lytyqvpqpp ylvgtmlanv
      721 gdlsnkgiel slnadivkne kftwntnlvf gknkqkierl snqtyqadvi ysgslhglag
      781 msnqfsqvia eqfavgtfwg refygfneag eeilsedykv igdvqpdftm gvgmnftykn
      841 fdlgwtgygm fgndalnata mmlsdpnrmp synipdayyy nygttaptys srwiedasff
      901 rlqtvslgyt ipfkeskskl rlyvlgqnla vitgyngvdp eiplvsgddq tglanpgidr
      961 fnnfprprtf svglnftlgn
//
LOCUS       WP_091141404            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            caeni].
ACCESSION   WP_091141404
VERSION     WP_091141404.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium caeni
  ORGANISM  Flavobacterium caeni
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Flavobacterium caeni"
                     /db_xref="taxon:490189"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117873
     Region          25..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfnglla lffalitqit faqeitvngt vqdqaglplp gvnvlvkgtt tgvqtdidgk
       61 fqikatqgqa lvfsflgmkt verpaslnmt vsladdsvql egvvvtalgi trdkkslgyg
      121 tqkvdgdevn rvpntnfinn lsgkvsglqv ktngnlggst nviirgyksl nnnnqalfvi
      181 dgvpldntnn nnvnqttgrf gydygnaaad inpadiesin vlkgaaatal ygsraangai
      241 mittkkgkqg sglgvtldts isvgnidkkt fvdyqkvygq gyfgelfrts rdvngdgead
      301 tavrtgddas fgpaftgnlv yqwdsfvpeh pnyqkatpwv aaqndpskff qtaftrsntv
      361 slnggndkga fnmsftnlgs tgimpnseqk knsvlanasy nltdklkasf manfidtrtq
      421 grngtgyngn lvagfrqwwa tnvdvydlrn iynatgknyt wnaslggvsl aggqpnlspa
      481 ywnnpyfery enyqndqrtr fvgnaavtye iakwldvtgr lsvdtyaevq eerraqgsya
      541 gdtfgtqntn essgymkfmr nrtesnydmf fdyhfdltek lnlkgvlgvn irreemsslr
      601 astlggiyvp nhytinnsln anaivpegqy trevdgyyas aslgyddfly ldgtyrhdvs
      661 stlpdgfndy gyyslsgsfv fsglvdanwl qlgkvrvgya qvgndapsys lvdtfptvpa
      721 fysnmysvps tkqnpdlkpe rtesieagle lqmfqkrvgl dvsvyktetr dqivdlpise
      781 atgytrkwtn vglvenrgie aslnlvpvkt enftwdmtan wavnvnevke ldegidnyql
      841 gnfqggvsin aqvgqpygvi qgsdyiyvng qrmvdpetgk wvisstndkn lgtflpqwtg
      901 glnnrftykn vslsflidvq kggkvfsldq wygqgtglyn ntvvnggqai rtpvdgdtgg
      961 vilpgvfpdg tpnnvrldqs tgtdgylgyl gsassdyvyd asfvklremt lgytfskkvl
     1021 nntfqdlyig lsgtnlwiih knlpdadpea glssgnlqgf qsgvlptvrt falnlkakf
//
LOCUS       WP_091141743            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            caeni].
ACCESSION   WP_091141743
VERSION     WP_091141743.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium caeni
  ORGANISM  Flavobacterium caeni
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Flavobacterium caeni"
                     /db_xref="taxon:490189"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112546
     Region          24..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykklll lllllpfsal aqstlkgtvv dgaskqpipg vnvviqgasg gtqtdfdgnf
       61 tlagvkngdt ivfsylgytn ysvaysgqan ltvnlreeaa qlsevvvqig ygsvnkkdat
      121 gsvslvtakd fnkgaivsvd qlltgkaagv rivngggapd atpeilirgg asisasnrpl
      181 ividgvpisn dypagianpf nlinpndves fsilkdasat aiygvrasng viiittkkgs
      241 sgepqfnysg svttgqvdek idlmsgteyt qfirqyfper vgdlgipdgs giaddpttsa
      301 iegrtlydvd wqdqifrtsi stdhtfsara nlykkipfrf slgynntqgl vktsdyerft
      361 yslkmtpkll ndhlkidvna kgsysdknai dqdgaiygal smdptkpvyg vpnslfgnyy
      421 qsttlnggrn iidgatnpla lleqrsrper vtrfignaef dykmhflpdl ravlnlgida
      481 sqsrihelyd mgaiatyrfn qanepvlnpg vnyvenqant nttmdaylvy akdlngfvnk
      541 fdltggysyq nfvidgnkqn frynespgtg ireeiinpnn vnnryyniln lqaffgrani
      601 dfagkyllta sfraeassvf tgkdqqwgyf psgafawkik eesfmkdvnf vddlklrlsy
      661 getgqasitg tvgyypsrpl flpgsptsqy lpgsltysal afnpditwet sktynagldf
      721 sffkngrlsg svdfysrete dllarvpvpv gqyltneair nfgsteskgf evalnvkafd
      781 aekvqinvgg niaynysevt kldggvtavq atesriptqt glflanhavg yqpysawvfq
      841 qiydaagnpi pgafadlnad gqitnddkyy rslrpnwtyg fnlninaynf dfsagfhgqi
      901 dgmaynssvi kygfteratq gttnalnnvm dfnqgaadpt fanfngnsaf sdylleeawf
      961 lrcdnitlgy kfpkfvknts lriygsinna fiitdysgqd penynaidnn fyprprmytf
     1021 glsfdf
//
LOCUS       WP_091144107            1126 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091144107
VERSION     WP_091144107.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1126)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1126)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1126)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1126
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1126
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124308
     Region          30..1125
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrllkisr wllivltsvf tygnlyaqtq tirgivldqa nqplagvsvq ikgttigtvt
       61 gsegrftisa eqgqvltvkf igfasqeiti gteltlsiql kndsralsev vvtaygvkke
      121 vkklgyavqe vkgsdlikar dpnpinslag kvaglsigan aemlgrpeiv lrgskdllfv
      181 vdgspinsdt wnisaddiet ytvlkgpnaa alygsrging aiiittkkgt kdkkgwqvdf
      241 nsstvfdgsw iavpkaqtey grgngyhyey qakdgagsal ytpqadvlyd ngnrlgeygp
      301 rfegqllrqy dspydvvtgk rtptpwtarg kdnydnfaqq gytntsniam sasgtnystr
      361 fsyshlyqkg ifpntalnsd nfnlsasyni nskltvegni nfnkqyspnv pdvtygpnsy
      421 iymfkvygsa dydvrdledi ykgptgvpnl vqyaqeygrl nnpwfvakkw lhshdktdiy
      481 aylklnyalt kdlnvslrsq istwtqrrte qvpssanlns ytgliadytf gwygdyrqdd
      541 rqlfenntdf alnynhkfgk wsvggllgan drtfnynsfy gttralalpn vyvlsnsvqp
      601 aleytwdssm qvysgyysfd fgydkylnin ttgrvdklst fakghdtffy psvslstvvs
      661 dyitlpefis flklrasvad vkgggtqsti tsaynqvtgn stntflgyst dvvssydgps
      721 ysnqnkaafa syynntasva ysntlanpll kpyqrlswey gadirlfqnr lnfdatyfdt
      781 qngpqiypyl iapstgytaq nlnvittkrt gfevaanlgi lrnsggfnwd lgmnystfre
      841 tltsifdgnk sistlalgnh vynigdrlde vygtkylrdg ggnviykadg tlltasgtna
      901 qttgslgyln pdytfgitnr fsyksfglsf qfdgriggki ydynyyaarq ggtdlstvtg
      961 vvgaarlaew qstktgtqap tpalignedg hgvvitsgtp vfangvisna nqltfspnnt
     1021 pilvqtylng tiknideawm vsrsfaklre vtfsyslpqs alkntfirsl tvslvgrnll
     1081 yfaarkdfdi dqyasgynss drttennngl qssttrkygf nlnlsf
//
LOCUS       WP_091144467            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            caeni].
ACCESSION   WP_091144467
VERSION     WP_091144467.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium caeni
  ORGANISM  Flavobacterium caeni
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Flavobacterium caeni"
                     /db_xref="taxon:490189"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116920
     Region          25..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwifa lllafsmqfs faqektitgt itdgglpmpm vnvvnkntkv gvqsdfdgny
       61 aikaktgdvl efsfvgysnv litvaaatkv nvpmksdaqq lgevvvtsqg ikkekkalgy
      121 avttikaeef aakpstdvvr altgkapgvn iqqtsglsgs gtniiirgys sitgsnqplf
      181 vvdgipfnad tnsdgnfleg atnassrfld ldpnniesis ilkglaattl ygsagskgvv
      241 lvttksgntk elnkkmeisv aqsmfmteis dlpdfqnnyg vgndneyrtt fgnwgpsfat
      301 rgeggigmdg tvdhpyayyg agvfpeylna dgtpkkvawr pydnvspfft tgtvsttsvn
      361 iggraegtny nlgvghtddt gfiennnyrr lnlntggstk lgngftlstv mnyvrtdkta
      421 pltgygygsg svtpstfati lytprnldlf glpyedpnth esvmyrrdit nprwllkngs
      481 deeavrrfyg nftamydins wsnvsyrlal dnytqskryy inkggnesrd gymrttfnen
      541 tifdhtfsyn fnanldkdqs wtldgtvgln srmegydyty lesynqfvyg fnehqnyeeh
      601 lgysdhqnqn ivglygsatl gfkkylflnv qgrndwfssl qkenrslfyp saslsfipsd
      661 afefmkgska vnylkmrlsy gssagfpppy qtiiglesat tqfvtpsget vnyiapssrv
      721 gnldlkpely kelefgletk lwnnrigidl slydktstdl iivrdvdpas gatdrydnis
      781 emsnkgielg lsfalfrsds dgftwdlsgq ftsnrnrver lgdgverfay agftnlgnfa
      841 vpgrplgvim gssimrdgng nyvvgsdgny lvnnelteig dpnadwrstv inqisyknvt
      901 fgfqleyqqg gdiysntana llsrgvtedt nwdrsrtyvl pgvnvdgnin qiqigatqyg
      961 fnnsgffide qsvfdatnlr lreislsydv pkrilektpf grmsisiigq nlwykafnfp
     1021 ehlnfdpevm slgvgngqgf dyltgptakr ygfninltf
//
LOCUS       WP_091144565            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091144565
VERSION     WP_091144565.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112184
     Region          31..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqnvtfhfwr rfcwlaftll tlsisgvyaq qtvtgtvtak edgntipgia vlvkgtqqgt
       61 atdatgkfsi kaangavlvf sgigydthev iitgnvanvv leskqnglne vvvigygttt
      121 rqnittavtk vdpkkipqaa nnsipqllfg rasglqvsqg ssqpggninl sirgrgnply
      181 vvdgvifpgd alepgngtia getngvsrgg laglnpedve sievlkdasa aiygvnaang
      241 vilittkkgk sgrlnitysg sysfeknypy lqplkanqye tlynqlitdq ylggqptpqq
      301 pygsapqsgv papkysdaai aaagngtnwl gqifrtgnin nhqininggs ekatyyfsgg
      361 yyneegtlkg aglnkytgra nlsfmpakfl tlnanftgnt nsylnsssgg qtggsgtqgf
      421 giiqaalgyp anvpvrdang nytrygvian pvslldvqdn tsyhslnanl sadlkvipgv
      481 laghllfgdn yeaanrtffv pstvfyfsqn lsraslnynn renqtleatv tykkdvtsfl
      541 nidavagagq ykttynsfgs qgaggadaig atnlaaetsn igitsfksat tlrsyfargs
      601 fnfldrylls vsyrydgfsl ffpenkyasf psasvgwkis nesfmknltf idqlklrgsi
      661 gitgntiggn aayggyapdg nviffnnggs nyvtisrygi dhpelkwqkt inknigldfg
      721 ffkgrvsgsv dvfkdditnl lgntttapls ylptqpvngg hqyrqgydfs istqnvklnd
      781 fswnstinvs hftykwksrf vydylysfrd vtyqavndpv neiyyfktng llqvgqtvpa
      841 wqpttggasl pgsplyvdkd gdgkltgsdi yklnpdpkis mgfgndfhyk qfdlsiffys
      901 qfggksinyn nawgdpvsia sstqsgtiqa lnvwtsvnqs gtrpsvnyie natglpqgtd
      961 inlvstnfvr crnltlgyti nspwinkfak sirvfadaqn lfiitkykgv dpevsyasvk
     1021 ggyapypmfr tfsfglkagf
//
LOCUS       WP_091146069            1144 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091146069
VERSION     WP_091146069.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1144
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126676
     Region          69..118
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          139..1143
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkltflynav cairavkykf llvlkittil llvgamhlsa atysqtvsis kkntnlesvf
       61 knikqqtgyl ffysgkvnls gktlnidlkd vsleealttc lknynltyni vdktivirnk
      121 apeddvisav navmnkqfit gkvidsvdka aipgvnislk nskgfigqtn atgdfvvsad
      181 igdvlvfsfi gykpkevkvd gkpivvklsp qvnaigdvvv tgyqvikkdn ytgsaiivkg
      241 ddlkrvnpnn liqslatfdp sfridqnnll gsdpnampki nvrgsttlps ingdiidrnn
      301 lsssynlpif mldgfsvslq kvtdldinri asitilkdaa atavygsraa ngvivittka
      361 piagklqvqy nydltvtapd ltdyhvlnak dklqyeklag lysavnntan tqdeldqqyy
      421 sklknvvsgv ntywlsqplr ntfghahsly aeggdttfry gvnlryqntp gvmkgstrnr
      481 ysggmnfnyn ptrnllfkne vtvtqvdgvn skygnfadyv amnpyypird dsgnilreva
      541 nwkvdthqsg aaqyksipvy nplfeaglgn fdksgylevl dnfsidwklt palrliglis
      601 vndskstadt fvspfsnsff ngptadiqnr gsytytasns lsfdgnirfv ynkqigdnsv
      661 navfgsnvts sksdyksfqa rgfsndkftn igfartytpd sapggdvsns rlvgtffnts
      721 yafknrylld asfrldgsss fganqrfapf waggigwnlh nesfmhenfp aisrfkltat
      781 agltgsvdfp pylskttyty qtsnwystgi galvngygne nlkwqkttey dygldmglfn
      841 drvlinpryy hkltkglltd iniapstgyt tykenlgdms nngyelyvvv naykskdlnv
      901 nftgnlahnk ntivkisnsl ksynqsvddy qsnpdnnaqg rpllrfnegq slntiyavks
      961 kgidpengke ifikrdgslt yvydiadtqp vgdetpkveg ffgssvtykq fllsfsfhyq
     1021 lggetynqtl vdrvenadpr fnvdsraldq rwkqpgdvtf ykniadlgts fassrfvqkv
     1081 nlvelksvyl sydlkksvaq klgmrtlrag itandifras sieiergiqy pyarsltcsl
     1141 tatf
//
LOCUS       WP_091146132            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091146132
VERSION     WP_091146132.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115913
     Region          28..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrysviifsl illlgfrnea raqqkkvvvk gtvidktekr plpgvmvwgg kpavvlaqtd
       61 akgnfsvsvd pdgelsfsfl gykritrkie gatiiniimv eevnalkeit kigyaiktke
      121 vstgssvvit akeiqdapva nvmdliqgkv aglniqnnng tpgmrgsani rgvsnvnvtg
      181 sgfltptspl fvvdgfptdd nsnysygfdq aspglspisl ipvediqsie ilkdaqatsl
      241 ygsrgaygvi littkrgnsk ipiikytgaf tfsqppplrk viggkgerlm rideimqndt
      301 nyyhglntvn stpflsdsln afynnatnwq aqyyrstfnq dhnvemsgge skfnykvnag
      361 yydqkgivqn tdfrrytlim ntlyqpndrf klaaavnnql aynstgggns itqggvgttg
      421 asssllpaps lftasnglln tldiqnenkt vnittnldid flivkglrvt nsfsfnyltm
      481 gnekfkpeal indvsglkpa diyqiynyfd rkntlydrtg laydksinsk hnfrvnifse
      541 instnyradv iqqsstpndq ikgplgydwy nssggtlnsl tdlktaslag sfsynykqiy
      601 vldlsyridg sstngpdagy sknpsiglrw nfnkenfmqs lnwldyssfr fsygknivpt
      661 gsvydvygry tagtnynqdp tvqldygtip ntgltptttt qydggfdagf lngkfsvtfd
      721 ayykqvdnll rqkdiatina fqkvstnems lvnygyeltl tarplptdsk lswqisvnga
      781 fnkdimahlp dnasqllvvd pstgqnilyr lgrnsltnvl lntkgvystn ssvpvdpmtg
      841 lryrtgglsy tyfkqgdpsw tdvngdyild qndfvaagns qplitggfss smqygpfsln
      901 isgsftavrd ilnndlasrf qsfanptnqs glvpltayny wkasgsnaty pnpydytras
      961 qtspfrydqt lfqedgsylk inqvtfsynf kkqvikrwgi ssariyctay nvhtfsnysg
     1021 anpesvtdlg kdisggypnp rnytlglqvq f
//
LOCUS       WP_091146209            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091146209
VERSION     WP_091146209.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115397
     Region          32..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtktftfyrk llivciflcw lipwsafaqs fikgkvvdkd nvpiasatvt ekgttnvtst
       61 nekgeftikt tkpgavlvat tvgfipfelt vgekttvtli lqenqqtlne vvligyqkia
      121 rkkstaaiss isakelanlp sasfdqllqg rlsgvnvqnf sgqpgatptv svrgnslvss
      181 gydeynvvns plyvvdgvpq pteqyvgpga gtganylagi npadietidv lkdasaaaiy
      241 gsraangvil ittkkgvsge prvtigsyvg itqrpelrdv tlgtterrqk msilqsqlsy
      301 adqtqlpyil tdslnsafng ntdwqslfyq tgkinntdls msgggngnss yrfstgyyne
      361 egiikatgfk rfstrlnlis halngkltin pliafartdn argngnnasp islgagnmps
      421 sllnldpdkk ayylgaysen ldknignqft fnlnlsydfs khltlnsqss ylyntnrrdl
      481 sqsnllqngq gnysysyadn siavttstfl tynnvfkkht isfivgqdin ynqfqntias
      541 gsngpsdniq vvngfqqski sassdyqayg llsyysrlsy dydskylfsv sartdassrf
      601 gknhkwgffp aasvgwlise esfmkdnpdn iftllklrgs igtsgslpnq nylqynlysv
      661 nnggfdgngg atsyngvtav tpnfhdgaaq dnlswqrskq wnigtdieiq ngkyglqfdv
      721 ydkenslqlf gvnlpvttgy dvaytnsvgv rnsgveltls anplggafrw gtrlnisynk
      781 nvitslpngg rdlvlsgdrf dkshvlsvgs pinafylyqt lgvfptdasv pqnpltgekf
      841 rngngtyqag dfhvadldgd yfidtfnsgi npdkkvsgdp npkytggwtn nfnyknwslg
      901 ifctftfdrd vlnlydsdrf ansqdgnavn nfaaystpdl skiniwtptn tnatyakydi
      961 gtyryyytsa qtfflekggy friksvnvgy dfpknvlktl glskfriygv adnvkmfqqs
     1021 kklpdaeavn pygeysgggy pipskytlgf einl
//
LOCUS       WP_091148579            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091148579
VERSION     WP_091148579.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116061
     Region          28..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgkrilfltl cylfsaligv aqaqtngtat gqvkdsegki lpgvtvaekg mpgngavtda
       61 ngdfklklkg tsnaitisli gfrrqelkvt dkpltvvlqi eenslsdvvv vgyqkqnrre
      121 vtaaisslng kdianipeas fdqmlqgrla gvsvlsssge lgaktsivir gsanidfgna
      181 nggntgplyv idgvifdvna igsaygnnnp lslinpndie sidvlkdasa aaiygaragn
      241 gviivktksa kagkpqvsis ayagmvtapn fikvstgaae rslklgllqq ltygdrqlgl
      301 iplaitdsln safnndvdwq gllvrqqsyv nsqdvalsai tgttsyrisv nhyneqgvlh
      361 gyglekfsph lnltikplkg meitadllms sqrqshgvgg agaylfnayn fpssfapltp
      421 tqydvytgkk syydddrafs ivgslnlkqq ittdlvfnst ygstnytnky gyfsplelng
      481 vqntaydiyt snpswsfenf lqyskqvgkh rfilaagaal ysyenyynya saagitvsgi
      541 stvqtvpagt nlnastyygr kttesyyarf nydyagkyll tasirrdass iysseyrwat
      601 fpavaagwia sdesffepvk kvvnffkira sygitgkdpg qwyskyqsls ndasyfggtn
      661 gtinnygvls gnastyngts vvspfsyynn fynfgtkass tvrwekdpql dfgadvelfn
      721 srvnltvdwy rkdskdvffy nvpaqatsgy qylsgnyvdl rnqglefstn invlgarsaf
      781 qwnfnfnisf nknlvtklpn nnrdflfdap yfyktltlgk pifsyrvfhs ngvyatdaev
      841 pydpitgnkm tangvpltag dpryvdvngd yninnddkyd agnpnpkytg gfgsnfrykr
      901 vtlsffssyv fgrkilngal sdalngskyi gsyginagva tyvnslnqfw qspgqqtkya
      961 kliysnaean vkdpwnignd yfvedgsfvk lknvtlgydl pekwyksigl trfnvyvmgd
     1021 nlamwkkakd iadpelvdpt tgssntvypt aakftlgvni gl
//
LOCUS       WP_091149820             989 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091149820
VERSION     WP_091149820.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..989
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106672
     Region          31..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvylfkyg ltvlflicaf ssafaqksvf kgkvvdelnq plpgatihvk etdqstvtda
       61 ngvfslvgnn qsvltvqvtf igydvanlvi kanetaaikl vpnsksltev vvvgygtvkk
      121 tdltgsvanl gakdlnpgsv tnplqqiagk aagvninevg sepgvapsir irgitslsgg
      181 ndplvvvdgv qgnmeflnqv ppseiasidi lkdasataiy gsrgatgvii ittkkgaagk
      241 atveynents ldvipkqlqe ltasqwtkqa elqgvdvsan hgsntdwynl ltrngvtqnh
      301 tlafgsgsng fnyrasvsai nqtgvvlgsn ykkyiariva tqkalddklt ltmnvntgvn
      361 danyspigvg naaftsntis qayiarptdp vyntdgtyft dpnvfhytnp yaiaktvsnv
      421 vnqdelfgsl radldiykgl sagwfgswrk vnqntgyyap vastitdavt yngqahinnd
      481 htdeklmdin lsykrdfgls hidatavyey qiqtyfgsys aargfandia tynglqlgtl
      541 asaqngdvss ykndrklvsy lgrvnysynn ryyltasfra dgssvfganh hfgyfpsasa
      601 awridqesfm anqkvfsmlk lrggygvtgn qqglpvqgsi slyglstnnp ttyfggqqis
      661 lydyiqnanp dlrwesrset nlgldfglfn drltgtveay tskttnllyn ynvnisgpfk
      721 vnhifanagt lqnkgleasl syaviktkdv sltlagngsl mqnkvlklsg vidgiqqstn
      781 yqpwgtnawl vegqpigtyl iykhtgvnsn gvetfagqna dgsfdataqs kirynagqsl
      841 pkynyaftps ftyknfdasm vwrgaggnkv fnglrsklsm lenlgkqnll qsaiatgihs
      901 savqsdewle sgnylrfqnl slgyrinvtn ikfisalrvs ltgqnlalit kykgldpevd
      961 asggsssggd ygiyprtrtf saglnvilk
//
LOCUS       WP_091150812             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus africanus].
ACCESSION   WP_091150812
VERSION     WP_091150812.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus africanus
  ORGANISM  Geodermatophilus africanus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Geodermatophilus africanus"
                     /db_xref="taxon:1137993"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52058
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpretr pgetrvaatp atvrqltalg ydvvveagag taasspddgy reagarvgta
       61 ddawgadvvl hvakptpeev grlragavlv salapaldpd llatlaarpi talamdavpr
      121 israqsldvl ssmaniagyr avieaahafg rsftgqvtaa gkvppatvlv vgagvaglaa
      181 igaasslgai vratdvrpev aeqiasmggq yvgvpadepl sgrgtgyasv tsedydrraa
      241 emyaeqarev divittalip grpaprlite emvasmrpgs vlvdmaaaqg gnvagsvpde
      301 vvvtpngvti igytdlpgrl pgqasqlfgt nlvnlvkllt pgkdgrlvld ledvvqrsmt
      361 vvrdgellwp pppvqvsaap aaapaprpap papapraprs partaavvgv aaallflaaa
      421 fspnqlignl tvfalavvvg fyvignvhha lhtplmsvtn aisgiivvga lvqightgav
      481 vtvlatvavl vasinvfggf avtrrmlgmf trs
//
LOCUS       WP_091151129            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091151129
VERSION     WP_091151129.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114806
     Region          26..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkifkyllii iflyplslla qqtvnisgkv tdtndglplp gvtvtagavv avtntsgeyk
       61 iaapanatel tfkfigmkpv iekiggrtei nisltslqsn ldevvvvgyg vqkratitgs
      121 iatlqnkeit ttknesvinm ltgkipgvri lqttaepgsy snvlnirgyt saplvvidgv
      181 iggdqstigr mdpneiesis vlkdaaasiy giraaggail ittkkgskng kvninysfnd
      241 avqtflgmpe gvgavdfmml tnekakrdfa nnfvsnitpv ysyndmkpwi dgkrqaadwi
      301 glvfrktanq lnhnlnidgg ndklnyffnf gylkqdgvfk tgdlnynkyn frsnvtakit
      361 kglqaqvlts awmdeknqpy tdewtvykyt wnqkpvnqiy andnplypnl ipggdnqnpa
      421 imtdadkvgs kryrnkavts qlnltydipg iqgltakalf nidygvadnn elkksyflyt
      481 ydaanniylp nqvnlpagvs rayythlnts sqltlnyaht ffndhnvaam ftyeqshqta
      541 dnfnahrdve ipveylfggl pnsnmsggmd inglqdvgyr svigrfnydy kgkyllefvf
      601 rrdgsnkyqp gpdqwgffpg gsvgwvitke kffhdlvsdn iisnlklras ygqtgndggn
      661 afnyvagyty pinsyifgps avngstpklg npgltwsvlt ksnlaldfgl fggkvdgtie
      721 vfrsdetgla atpstalpgt vgadvpqiny nsqrvqgldf nisyrntfgd vgvsiagnig
      781 ttrlenlkvl rgnsgneysn wkenqtnryq niwwgkeyag qfttynqiyn ygvntgggnn
      841 ntipgdyyyk dwnndgvidg kddhpiatsd iplynygltl glsykgfdmn mvlqgaagvy
      901 vqygeqfasp lmydrsaltr fldswhtvdp aanvfdpntq wvpgfypamg spdaqgtkai
      961 qsasylrvks lefgyslspa vlknigikkl rvyvnsynll tftglknydp ehqgpsprng
     1021 ndgisgytyp mnrtfnlgan vsf
//
LOCUS       WP_091151228            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091151228
VERSION     WP_091151228.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116053
     Region          28..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrkllfyta lfvclislnl kaqaqtvtis gtvmdkttkt afpgvtivle kpykalaqsg
       61 vdghfsvtvp vnstlkfnfi gyvtqtekig tvaknitvtm sedqksladv vivayqkrtk
      121 etttgsatii sgkeiqdipv snveqllqgk vaglniqnnt gapgfrgsvq lrglstlsis
      181 gsgndsflqp tsplyiidgv pldadkaaef gfqtqgpgvs plslipqedi esiqvmkdaq
      241 atslygsrga ygviiistkr gnskiprvrl tsnffvnapp klretlggns erqaklqqii
      301 lnatsindir ridatpflad slnaywnnst nwqdifyatt yntehnlald ggdprfnyka
      361 nlglrtengv ikntgfdryn lsmnvelkpn dkfrffgsiy gslgkqqkgd glgllqsgva
      421 angqastllp ppsfyqssgg iisalktndd nstrnirsnv egryefipgf aitsslsydy
      481 tsdgeatftp aaanaqfakv ydyvgrnytl ynrnaityak sfgsngdhti fvntfneiyk
      541 rgaqqgiinq vrtpndqyqg plgfdsynsr gggvlstykn atsasfaaal sydykkkyva
      601 elsyrldgts tsglenpysk npaigvrynf qketffnnls wlstgslrlt wgqnivpsgt
      661 lqsiygtynl ngnynntpti gidygfipnp nlkpttttqw nfgfdlglwq dkvyvvfdty
      721 ykkvdnllfd rpltnstgfg tissndvgia nygyelmitg klvtakdfnl tmsangainr
      781 dvllripqey ngqvikidgs sypqrivyrv grntlsnylh inegvysrdt dvpvdpvtgk
      841 kyqtggipfl ggdprwkdvn gdyimddrdy eitgnsqplv tggistniny kkfglniytt
      901 ftakrtvlnn alsdrlsimr dpysllavvp lnnldiwraq gdvskyptpy dyarfnqiqp
      961 lrpdqtlwae egsylkinnv tfsytfeknf vrrfgfnnvr vyfstnnlvt fsgysgpnpe
     1021 nvtslgrdis ngypvprlyn lgfnielntg n
//
LOCUS       WP_091151650             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091151650
VERSION     WP_091151650.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108500
     Region          24..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllaslc flllcvtqvf aqnrtitgtv isksdglplp gvtvkvtgtt igtqtntsgk
       61 yslsvpasak tltftfigfa dyqatigsgd vdaslvasss qlnevvvvgy gsgrkasdvv
      121 gtvssvsgkd ienrpspnaf dalqgkvagl nilsssgeps stpslslngl sslgasstpl
      181 vvldgipvdp stvltlnpnd iesfnvlkda astsiygsra sngviyvttk kgslnraari
      241 tltsqygvsk lantdffenf mnaaefkafq vssgqltqtq lnntlnalev knadtkwykv
      301 yykdntpqym enisisgggg ktsyyvsggy tknegiayrs aykrytlrsn insvvtdwmq
      361 fglnlglayd drqtnpsgsn stnlglaqla apyyspndpt gqqykfipgw gryhpayras
      421 vftdannnaq fnptaylqln pikgltlktq ggmdaydyre tptqlpsylg svgngniaey
      481 ftrgvsktft ntaeykfsvq tehhftalag qeytdgstnv fgassaglsd drivllgsgp
      541 nnknvtstnp qglgnedyay nslfgrvdyd ykeryfvegs vrtdkssrfg inhrsatfws
      601 aggswkakqe nflkdvswld dltvrastgt tgnssignyq slatvstian gdasgfnisa
      661 agnpdltwek qrlttfgitt sffdrirlea syyirtttdm lvdvpfpyts gfslvtsnvg
      721 alqnhgfdie lnfdawkdkt hngyitpfiv aninhnkvts lfldkdyyvv pntgvawivg
      781 kpvslvyply kgvnsqtgap ewylpdptnp tktrkdpnav tseftddlqq ntgisqypwl
      841 tgsfgldggy agfyvhtlfn falgkhlinn dkyfyenpni fpgfnqtkrv tnywkkagdn
      901 alfpdienyq ftqfdsnlie nasfmrmkel tigyafpkal lertkvlkgv klfltgrnlf
      961 tvtkytgpdp evdsnlalgn ypntkqytfg aevtf
//
LOCUS       WP_091151706            1145 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091151706
VERSION     WP_091151706.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1145
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124633
     Region          35..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          133..1144
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitfsqimi aimisgmays splkaqdiln ktyslsfnna tlqevltyfq knhdvkfiys
       61 knsvnlsqrv svnfvdqplr nvldqllkkn gidyevlknr iilgkltatg tgdfkaaisa
      121 enadaadqqe lgipitgkvv dekglplpgv tivekgttng vntdingnfk lsvsdknavl
      181 vvsfigyrkt evavgdqtsi sislsenisg lnevvvvgyg tqkksvttgs isgvsarefe
      241 dqpvtrieqi lqgrtsglti ttndgqpgdg atvrvrgvtt fnnndplwvv dgvvvdnggi
      301 sylnqsdies ievlkdaass aiygtraaag vilvttkkgk agrtqinysg yvgtsapark
      361 ldlldatqya tlrnessvag gkgilfpdpa slgkgtdwqs vifnkgakqq nhelsvaggt
      421 dkstyytsfg ylqqdgivat diskykrinf rtnstfkpsk yvnfgenigy tynksiglgn
      481 tnsvfggpls sainldpttp viitdptvaa kapyirnagd ppalqnaqgy yygisnyvgq
      541 eitnplayiq kqlgnhswah nivgnaymei npikglairs tvgtkmafyg desftpvyfl
      601 nastigsrnn ynrdqtrvfs wnlentasyt rsinqhnitv llgqgayvda atiasgvtey
      661 glpvtnynda slnfaipaid rigygsegqp hhlsslfarl nydyqekyii qgivrrdgss
      721 rfgsnfkygt fpsvsvgwvp skesfwpkte aidfvklrgg ygvvgndair dnaflstigg
      781 grnysfgtgd tyisgyspna psnpnlkweq tsqtniglda ilfhdfnltl ewykkkttgi
      841 lqqpslpfyi gaidnpyani gdmenngqel qlgyhkkvge fnlgfdgnvs hlsnkvtrla
      901 pgqdylngag vqniqggvtr sqvgyaygsf ygyentgifq tqadvnnyis pktglpiqpn
      961 akpgdfrwvd tdgdgtisdk drkfigkslp swqfgftata ayknfdvvvf aqgqagnkif
     1021 qglhrldilt anyttaalnr wtgpgtsnty prltdkddns nfgynsnfyl qsgnylrikt
     1081 lqlgytfdkn linkiglqkv riyatgqnll tftkytgydp disgsidqgf ypqartflvg
     1141 lsvgf
//
LOCUS       WP_091152332            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091152332
VERSION     WP_091152332.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120613
     Region          21..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnryillsil igfssvafgq inirgkvise ngnqplagat iklknthitv itdgngdfnf
       61 tikltsdtil vnyvgymvqq ltissnktty ytvrlkenma alsevvvntg yyqipkerat
      121 gsftqinnql lnrsvttnil drlegitnsl nfdrrlitge ntvkrspdir irgvstiesn
      181 ekalivvdnf pyegdistin pndvesitil kdaaaasiwg aragngvivi ttkqgrynqk
      241 srisftsnvt sinrpdlfyn qnwlpsptvm siekelftrg nylernqtal plyvellikk
      301 rngaisdadf taqedvmknt dvrndalkyl yrqglnqqya lnasgggaay kyyfstgydn
      361 nkenvtensn srlslrllns fqplknleft adiwytrqqq qtnglnysgl ttagvgiisp
      421 yarladdngn alaiprdyrf tyqqqaaang lvdwlyrpld elkladntar nneiklnggl
      481 kytffkdfni nasyqfiqnn atgvsyyspq tyyvrnlvnr ftqtdgtkif pnggvltgat
      541 pvttqaqagr lqlnynhdft nqhqlsalag aevrqqvaet lpgymllnyn kdvltsntaf
      601 dyytayptrp tgaatlpsin gyqlhriltd rylsyfanaa dtykerytls gsvrwdgsni
      661 fgvntnqkgv plwsigsswe lskepfyqlk wlpylrlrat ygssgnvnts vsafptalyn
      721 tdaitglpna sltsagnpdl rweqvktfna gidfalsnrr iegsiefynk nasdligidn
      781 mdpttgiilg vtpalqnkin yanmntrgvd iqlnsrnltg kfrwetsvlf syvrnkvtky
      841 naalantita ytatpgpava gssrdmiyaf pwngldhntg kpiiyingvv stdyqtyyns
      901 fktsdlvqag vtsppyfgsv rntfsyqnfq vsaniiwkag yvfrrssmyp gyeyysssny
      961 nmdyfkrwkn pgdelitsvp aaippgttvg nnymalvykn sealitkgdh irlqdvnlsy
     1021 rfqgkilknm nlsqlqvyay arnlgilwra nknnldpdya nasypepqtf alglkvdf
//
LOCUS       WP_091152551            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091152551
VERSION     WP_091152551.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112584
     Region          19..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkylylliil lspvinfaqt itgtvrnisn eplpgvtvtl kginqfvitn ekgeftisvn
       61 dvtailrfta atveplevtl agqkninvtl ltkvnkldev qiiaygtntq rynvgsvtkv
      121 taddiskqav snplaalqgr vpglvvsats gipgaafnvq irgqntiksn lqtivtprdn
      181 plfiidgvpy apqngsvnqf pslaspgiag vynnayggls pfnsinpsdi esievlrdad
      241 ataiygsrgg ngvilittkk gkagktdfnl nasngisvvg htmpmmntqq ylgmrkeala
      301 nggltpnltl yddgfapdll afdttrytdw kkvflgntah ntnvngsvsg gstntqfris
      361 ggynrdtyif pgdfadsras flmnlhhtsl nqkltldfss nysydknnsa gapnlltays
      421 mepnypslld gngnlvwdyk gislssytpn inpfsylksr yyiqnkslns nlqigyklld
      481 gltfrsslgy ntfysqeyyg npksaqnpag nptasarfgn nnyttwiaep qleyrntlgk
      541 gaysiliggt yqrnsnskte vdgsgyindn liesisgapt qnasdsysey ryaaifgrin
      601 yrwdnkyiln inarrdgssr fgpnkqfgdf gsvgagwlfn eesfvnsnla flsygklrgs
      661 ygitgsdava dyqylsrwap tnytyqgglg ylpqnlynpt fswattkkle fglelgflqd
      721 rilfnstwyr drsgnqlity qlpaltgfns vvenwdavvq ntgleltlqv svikskrfsw
      781 tssfnmtlpk nkvlsfpnle kssysttyta gqsintvygf ksagvnattg vfqfydtngq
      841 itdsplppss gkfndyynig nldpkfyggf qntftyngvq ldvfvefkkq lgvnylqqvy
      901 yslpgmeqnl pvallnrwka pgdqtniqky svqygaeyda gsnffqssgv ysdasyirik
      961 tvslsynlpv kltkkfniqn lriyasaqnl ftitrylgnd petqtlygvp plktiscglq
     1021 ltl
//
LOCUS       WP_091152619            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091152619
VERSION     WP_091152619.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121585
     Region          29..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkiykklkl vlsvlllciv paivfgqski tgkvtdesqq plpgvsvsvs gtktvsvtda
       61 ngnysiaaqs gqvlifkfig ysqqsltigd spvynlsfkv enkvlnevvv talgvkketk
      121 rlgysvqeik gaeltkarea naingltgki aglnvginqe ilasptvllr gsplnfyvvd
      181 gipintdtqn ispddidsyt vlkgptaaal ygsrgingai littkrgkad nkgfvielns
      241 stqfnrgfia ipkvqnnygg gdndkyafgd gagggvndgd ydvwgprlna glmlpqydga
      301 ydptqtyttt fkdgstfkgh ikptpwvarg vnnlegflqt glltsnnvsi ssstekanvr
      361 msvtngyqrg itpntglnti nfnllgslnl skqfkvegni nynrqfskni pdvtygpnsi
      421 iydvdlwtga dwniddmrny wqpgkegiqs vfveykryqn pwfqsyewlr ghykndvyaw
      481 gaftyspdkn lditlrsnit tnnvlrteke pfsahpygde hnhgnyredr rdlfenntdl
      541 lvkynlnnis nsgvsisala ggtlrtmkyt ssfvttdqll ihdvytfqns inpvksynfd
      601 sdlittsaya sadityknyf tisatgrtek ssallnqsyf ypsvsisspi sdyvklpeai
      661 sflkvrasya nvkdggtsaf vgpagyplgy gnsyqttygg psyqvstpay iigpsygnit
      721 sasaptytvd pkikpssrsn yeggidlrfl kdrlgfsgty fiykdgpqiy sqpqsetngs
      781 dqsfltngya tkrtgyevsv ngsaiatrnf kwdvlmnvst ykevydafpg qqkikdqffk
      841 vgdrvdklyg akeaqtvdgk vihdkdgipv ylpvaqylgn adpdftwain nkfrykeftl
      901 sfqfdggvgg kirdyvyrkl ieggrgaatd egiigqaray esehwgdpgf kgavfadgtp
      961 mlghdgvtva pgspaiqfdp itgvitnmdq vkfaanttpv kyvqdyvnkf yndpqhtvis
     1021 rtyaklrevv vgyslpkpfv qklrlskvef slvgrnllyf fkkgykdidv dqypgrnqlg
     1081 qtslesglqt pttrsygfni nvvy
//
LOCUS       WP_091152939             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091152939
VERSION     WP_091152939.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106915
     Region          29..979
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknyskkyv llcaflmmsv mafaqtgsik gkvldetnqp lpgasvsidg ttmgsttdln
       61 gnytisgvkt gnvtvtakfv gytpikkavs vssgvnelnf glkpdnqnln evvvvgygtq
      121 rkkdltgsvv svtakdfnqg pittpeqlit gkvagvqits nsgapgsgst irirggasls
      181 asndplivid giplsntais gvanplslin pndiesfnil kdasataiyg srasngviii
      241 ttkkgksgkl svnfnslssl seitkevsvl nadqfrtavq tyspdhvall gkantdwqsl
      301 iyrkaytydn nisvtggikg ipyrlsvgfl nqdgivktdn lkrttatfni nhdfldgdlk
      361 vdltlkgaht eshfaadvig savsfdptqs vysndktkfg gyfewldsgn pntlaprnpv
      421 gllneqnavg kstrgigtls ltyifpflke lqanatfggd lsngegsnli pataaskfaq
      481 kgsytsyynq nytyntdyyl kyskdfkdik shfdiqagys yqyyntyvkn fqektgdkvt
      541 pvnslvdptf gqyyiespfa ranfsfddky lltasirddr ssrfsekyrn gyfpsvafaw
      601 rakeesflks vdvlsdlkir asygitgqqd lptsyfpyla vydpsnvsaq yqfgssfvnt
      661 lradsynvnl kwestattnl gldygffngr ltgsidvynk ktkdlllnap iaagtnlsny
      721 lyvnvgnltt kglefnania aiaskdlnwn igynvslnkr titnisltgd pnqkiatgai
      781 pggvgntiqq wqagqnpgaf fvyqqvynng iplegvyvdr nnngtttddk ylykqtdpkv
      841 fmglnsnvny krwnlgfsar aslgnytyna qaaanaayvg lkfskylvnl pssvlktnft
      901 qyqlysdyyv enssflrmdn atlgytfgkt ggpytlrasf nvqnvfvitn ytgldpegsg
      961 idnnfyprpr iyslglnlgf
//
LOCUS       WP_091154127            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091154127
VERSION     WP_091154127.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119816
     Region          27..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktiliivl aalclnfrgk aqsityltgr itdstgnrpl ygatvrisks qistatdeng
       61 nfkissnqks gtliisyigy ktvqlnfsqe tpapfkimis pdqtalievv vstgyqtvpk
      121 erasgsfdqi dskllnrnas pnildrlagi ssglrfngdv npavavgsad rylginirgv
      181 stlsgnvstd plivldnfpy egnlsninpn dienvtilkd aaaasiwgar sgngvivitt
      241 kkgyknekvi idvnstltfq nkpnlfydrn ylpssdyvdl ekslfkqgyf dpyvqdnyyw
      301 spvspvvdll aaaqagtitq qqannqinal rtqdvrndye kyiyrntvdq qysiglrggs
      361 elnaynmsvg yvknqdpmvr ngfdrltina gntytplpnl sitanvnysr nttalnnnly
      421 ygsgisvggp iaglypyaqf adangnhlai vkdyrssyva gapasglfdw tykpldelal
      481 gndnttvndl lfkisatyrf lkhwnvnvqy qnenqavdnt ndqsknsyaa rnlineftii
      541 npgaaptyqv pigdildlsh nelisnnlrg qlnynqlfgg khdlsgliga evrqlsntgy
      601 trnslgynne fgtatesldf hdyllvnptg yniipspggn ingstnrfis yysnlgytyd
      661 skytftlsgr kdgsnifgvk tndritplws agavwdiare tfyksdwlpl lrvrasygfn
      721 gnvyngsayv tgnyttvslt gapaiynlta pnpqlswekv kninlgvdfa tknnringtv
      781 eyyikngedl ienvplftss gfssffgnaa ststkgfdit intknivgkf qwntslllst
      841 lkdkvtrydq sltnysiqsv sgmpvvghal yglysykwag ldpangdpmg yldgkvskdy
      901 tniinnfnpd slkyngslrp tiygsirndf aygpftfsan igfefgyvfr rnstsisasd
      961 iisvpgsqni dyeqrwqktg dektttvpsv iypsddnrsa fykysstlve nannirlldl
     1021 rlgysldram hhslpfkkie vfayatnlgi iwrankygid pdlttssyhp iptpftlalg
     1081 fnanf
//
LOCUS       WP_091154934            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091154934
VERSION     WP_091154934.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113324
     Region          42..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mansylkksl tgfvilmlil vktgyaamqd ttgrvsahpd wisgtvldey anplkgvkvt
       61 ikgkkadavt tgpdgrfein aalndqlift apnynarlit vkgknavtvr lidtyiqspe
      121 kidvlygtkk vsdnlgavst iytnqltttp atlytsalpg qlpglfthqf tgfgapqtas
      181 qtvgdfignv vqhnnysand nfeiglslrg qqpitiidgv qreissidpe siesvsvlkd
      241 alsnilmgin ssrgvllitt khgrpgapri sftaqsgtqt pldlptplsa yqyaylynea
      301 lqndgkpaly kaddfnayrn htdpighpdv nwfktilrdn spmtayklnv nggtgvaqys
      361 vslnyfdqkg mfktdpsvgy ntnndlnryi insdlsvavs kkftvdlqlf griqqvtqpg
      421 ggfgniltdl ystpnnaypi rngngsfggt tlfsnnllse tefsgyqrtn sndvmanldl
      481 nydlsgitqg lafkakgnla fesqgllsrg lvnsaflftk dstyaavnsp asqvnsfssv
      541 ssarysyaql avnydrqfgk hnvtgmlmyd trsavlnfdl sgvttnraak vgynydgkyf
      601 veasvnssgy sryppghqfg lfyavglgwq mgkedfmkda twvtswkwra tygktgngni
      661 dnygyynflq tyskpngyay vlgttragiq gfqdnglanp feewekarkl digtdislfn
      721 dhfkitadyy hdryydvmqi rgnsiallgi qypyenigin lykgtelslt yqdhinsfny
      781 fisgnasmqk vidvysdeep qpypwlkhtg qspeaiwglt slgffkdadd aaksatttgy
      841 takagdvkyk dlnndgvidq fdqsiignnk pllyygtslg fnykgfslsv ilqgvanrql
      901 iynnnlvngf tgvgflgltf sgqgydaltg rwtpetanta tlprlslgns nnglqstlyl
      961 rsanymrlkn aevgynlpyg wvhrlrlsgi rvfangenll tlygykgvdp evygtaypmq
     1021 rvfnagvtvk l
//
LOCUS       WP_091155543            1183 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091155543
VERSION     WP_091155543.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1183)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1183)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1183)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1183
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1183
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130065
     Region          134..1180
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlknlrsklk yssfvltvas tcflncalat eiarsqdldk risidvekkt lketldqisk
       61 qahvniiysn akgilknpvt ihakdqqvsk vltdllsplt ltyevigdqi vvkfdktssr
      121 spsqeqtekh rlpvkgrvtn tngsplpgat ikikngpala ttdsngefei hnvadstvlq
      181 vsfigyltke ivitntnylt itlengsnql nevsvvstgy qtipkeratg sfaqpikamf
      241 ndrvstdifs klngitsglv fnsnttaaqn gqldinirgr stifandqpl ividnfpyng
      301 dinninpndv edvtvlkdaa aasiwgvrag ngvivirtkk gklaqplrig fnasitafdk
      361 pnlaynpnql nsssyvdlet ylfkqgyyda nlndvtnypv ispavellta qrngtisass
      421 lntqlsalkn lnvndqigky llhnannqqy glnfsggssk atyffssgyd ynlpsakdns
      481 yqritlnsqn tfkpianlei svglnvvkgr nqtdntlsnt lnhvfpysqi adaggqprpi
      541 sygyrdsyvq aapsngfldw sysplkdlga annittitdt rltsgikytf ieglsgeiky
      601 qyertniqnr dfesqdtyyt rnlinqfaiq sngqvtgyni plggisglgn tniisnnlrg
      661 qlnynrswkn stiaalvgye fsqvssasng sslygynddn atfvnvnttt fyninpsgnt
      721 ttinnginig gtldrirssf anlaysykdk ytlsgsarid gsnyfgvatn qkslplwsag
      781 gkwdinkenf yniswlptld fratygfngn ldrsvtgvtt llyqsnalyt nlpyatilni
      841 gnpdlswekt aitnlgidfs skkniisgsl efyfkketdv lgyktfpnna gilslegnys
      901 dmsghgfdvt ltsqnlsgrl kwsttvlvsh atdkvtrydl aplasqlvga dgngtvavpn
      961 lgkpvfglys ykyvglnpst gnpigyvngv ksedydaiin nssvsdlvyf gparptyfgg
     1021 lnnhfsykgf dlnvqinykl gyyfrkpttn ysqiisngsa ylivnqdynk rwmksgdekt
     1081 tnipsliypf sstrdqfyqg sdinvekgdh irlqdislsy nfnrsvypkl pfsnlqlfmy
     1141 annigilwka nqsgldpdav pggndrtttp nprsiafgik gnf
//
LOCUS       WP_091156045            1169 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091156045
VERSION     WP_091156045.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1169)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1169)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1169)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1169
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1169
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127654
     Region          127..1167
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkpllrsrf lswillrmlp svllivslsg yaqsstpvys fswknsalpv vftqiekaas
       61 vhfsynpkdl dlqkkislti skqslpqvid lltqqlhaqy kivgetvmiq sqktppkvts
      121 qvvaddfslt gkitdqdnlp lpgvtitntt knrsatstet gnfvitanng eivtfsmlgy
      181 eptsivatdk lkvvritlkq katelntvvv talgikreer slgysvsevd gnllkkaret
      241 nvinslagkv pgliinstag gpagssrvii rgntsitsnn qplyvvdgvp idnsnygqvg
      301 gakysggfdf gdaisainpd didkisvlkg psasalygsr agngvilitt kkgtskkelg
      361 ielnsttsie nqlthyndyq yiygqgtaeq lvidpgqakn tlfnnfgprl dpslqvigfd
      421 gkyrpyalvk nnidnffrtg atttnniafs nandnssfrl sigdlrsrdi vpgsnmrrst
      481 fnftgssklg skltvsakvm ylnenvvnrp aladdpgnig nsfvglannv dqayfknsyk
      541 dsegsyvdwg ggqyrldpyw vinemkntts knrfigglqg nyvitswmnl qgristdfty
      601 lkyskfsprt tpgalageld qldqrlgtte gdllltlqkq vtpslnlaar fgsslsnisn
      661 pgstltfitl nvpdvvspns fadksvvenh yrkkntgiya lfsagykswl yvdaslrqda
      721 sstlpvennt ylypsvaasf vftdffkidp svlsfgklrl seaevgndtd pyllnlnytl
      781 splpfngvsl gtvanttipp rglrptrtrs feigtqlkff kdrinldisy ynsksrdqin
      841 lvpapessgf nmqlvnagvi gnkgievaln gsaialkdfg wdvnvnfakn tntvlslaeg
      901 ipylslsdar wlgvsvvakp gapygailgy dyqrdpqgni ilnpqtlapa qaeersilgk
      961 gtwswtgglt nsfryknfgl smvmdikhga nlfsmtnmfa iirgshvstl pgraewikse
     1021 edrqtqgqti eawraagkvq gyvpqgvlat tdasgkttyt knttavdpsn ywsqyysdgn
     1081 gvatpfiyda syikmreitf syrfpantis klgikdltva vvsrnpfiih knvpnvdpds
     1141 nynngngqgl eygslpsrks wgfnlnfrf
//
LOCUS       WP_091157839            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091157839
VERSION     WP_091157839.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118679
     Region          22..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkillltclm allfstvraq ytvygkvidq ktkeplagas ikindsqrvi stdsfgqfhf
       61 nsnskdiiit asyvgyinse tkvvaamsds vvialnrisn elkevvvstg yqnipkerat
      121 gsfekvnadl lnrrvstdvi skledlvpgl vfnrstsnas yqtqisirgq stilgkadpl
      181 ividnfpyeg ninninpndv esitvlkdaa aasiwgakag ngvivittkk grfnqapkvs
      241 fnsnvtvggr pnlfyqsrms tadyideeqa lftkgyynsa eksanktplt pvvelliarr
      301 dgkisasdaq sqidalknqd vrndfekyly qksvqqqynv nvsggsanqt yyvsagydkn
      361 aanlvnngyn rltvdannty sflhnhldvf tgisyiqsdn imnnpgttgi llsstsgtsl
      421 ypyakladas gnplsithdy raafvttaqq kgllnwqysp ideinladnh akqtdyrlnf
      481 nvvykifpgl saralyyygr tegitrnyqs qdtyytrnli nrltqvntdg slsypvplgg
      541 ildqntssai sqnfrgqlny sknwsnksdl taiagyeirn thtitdqhre ygyddehats
      601 tkvnyltyfn nyynpaltqq ipyldsqgdl tdnyisyytn aaynydnryt vsgsarides
      661 nlfgvktnqk gvplwstgis wnvsneafyh iswlpllklr atygysgnvn ksvtayttav
      721 ysngsdnlsg lpyatitnpp npylqwervk mvnlgidfea lnhrisgsle yyhkngidli
      781 giapyapstg ivqfkgnlan naghgvdisi hsrnlngafk wstdlifsna vdevtkydvk
      841 tdvlsflqlv yplagrplyg iysfkwggld pktgeaqgyl ngqiskdysg iinastpdni
      901 vyngparpti fgslrntfsf kgfsvsgnis yrfnyyfrrn svnyatvlsg qggnrdfalr
      961 wqkagdevft qipslpatnn gnrnnfymys sslvekadni rlqdvnvsyt itkeklrslp
     1021 faniqlyvyg nnlgilwkat ktkldpdypl nqfppvktys igfkadf
//
LOCUS       WP_091157851            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter pineti].
ACCESSION   WP_091157851
VERSION     WP_091157851.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter pineti
  ORGANISM  Mucilaginibacter pineti
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Mucilaginibacter pineti"
                     /db_xref="taxon:1391627"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117660
     Region          22..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkylliiig ssfslfsaaq ttlrgqvtet gthrpltgvs iviqestagt itdttgrfsl
       61 ktgltnltli ishvgfkpen ikikspfsal ieislqpqnt alqevvvstg yqtlpkerat
      121 gsftqvsnaq lnrkvstdil srlqdavpgl ifnqiinght vnssitirgv stingnaepl
      181 iivdnfpydq ditninpndv esitvlkdaa aasiwgsrag ngvivittkk gkynqapkvn
      241 fnsnitfgak pnqfylpqmt svdyieiekk lfasgyysaa etsinktpls pvielliakr
      301 dgtmpagtvd aqiealknnd vrndynkyfn rvavnqqnal svsggssnqk yfvsagydhn
      361 lqnlvgnqyq rvtlnasnty nlfnnklelt tsiyytgsnt qdnnpgtgnl glsyqnlypy
      421 ahladangnp ltiardyrls faqaaqqqgl lnwsyqplae iglannhtvv tdyrintglt
      481 yhiipglnaq llyqyghtvn dfrnlnsqdt yytrnqinnl tavgsngilt rpiplggild
      541 lttgdlinqd vrgqlnytkd wkknsltaia gaevsdshnt ansyrlygyd ddhatsqain
      601 ytstfpryvs sqansvaipn nesesdltdr fvsyyanagy tydnrytlsg slrfdqsnlf
      661 gvntnqkgvp lysvglgwni sqesfykssw lpylklraty gyngnidknl sayttalyns
      721 gssaltlqpy atvqnppnpe lrwerdnikn lgldfatknn iisgtieyyr ktgldligtt
      781 pfppssgist ftgnfantfg hgldltinsr nidqqfkwlt affisftadk vtnyaaaslt
      841 pgssivdngs yipvvgqply siysyqwagl npqtgdpqgy lngqasnnys airaaatkdn
      901 ivyngsarpt vfgaftntft yknislsani syrlgyyfrr hsimygtdng lssqhgdyek
      961 rwqkpgdeaf tqvpsvpasp nslrdyfytw ssvlvdkadn irlqdinlny tflksklhwl
     1021 pfdsaqmyvy annicllwka skssldpdyi ngpppsrtia fglkagf
//
LOCUS       WP_091160943             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus africanus].
ACCESSION   WP_091160943
VERSION     WP_091160943.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus africanus
  ORGANISM  Geodermatophilus africanus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Geodermatophilus africanus"
                     /db_xref="taxon:1137993"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51707
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgvvkegr pgearvaatp atvgqlrklg ydvvvepgag aaatfpdeay lqagadvgda
       61 vkadvvlgvn altaeqralv rpgatvvgil gpatdatlla elarlgvtal amdavprisr
      121 aqsldvlssm aniagyravi eaanvfgrff tgqvtaagkv ppatvlvagv gvaglaaiga
      181 agslgaivra tdprpevadq vrslggeyla vpsaeaevsa tgyakemsdd ynaraarlya
      241 eqlrdvdivi ttalipgrpa prlitaemva gmkpgsvvvd laaanggnve gtvageavvt
      301 gngvtilgyt dlagrlpaqa sqlygtnvvn llklltpqad gelvldledp vqrsitvvrg
      361 geitwppppv svsaapaatt adqprapvqa peprqrpvav rvtalasaaa avfllvaasp
      421 aalrghltvf alaivigyyv ighvhhalht plmsvtnais giivvgailq lgspsllvts
      481 laavavlvaa invfggfavt rrmlgmfrrg pa
//
LOCUS       WP_091162980            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypii].
ACCESSION   WP_091162980
VERSION     WP_091162980.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypii
  ORGANISM  Mucilaginibacter gossypii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Mucilaginibacter gossypii"
                     /db_xref="taxon:551996"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114138
     Region          27..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkiykllla iilpfilvqt vagqsvkisg vvtaksdglp lpgvsvsvkg kttgaqtnvd
       61 gkfiinanvn dvirvsyigf ttqeiavtqg tttlnvvlve apnslnevvi talniskdkk
      121 slgyavqglk skdiseaket nfvnalagki agvqvtnsqg dmgssrivir getsisgnnq
      181 plfvvdgviv dnsqflgnng srdfanaisd lnsediesvs vlkgpnaaal ygsraaagvi
      241 lirtktgkga kglgvtinsn tsfsnvqvlp eyqnqygqgs ngkfsyvdgk gggvndgvde
      301 swgpaldgsl ipqfysngqa vpfvahpdni kdffktgvtl nngiaiasss dksdfrlsyn
      361 nlhqtgivpn tsqgrnsfal nssyrvnnkl tvntivdysk ddadnlpgay gkratstmlq
      421 ftwfgrqvdi nrlknykdan gntfnwnnsy ysnpywlaye ntvgqhknhl igsielnyki
      481 idglsanfrt gtdyyndrrk ikvaygtngt pfgsyeeday svnenntear lqytkklnnd
      541 fsldvfgggn iavrttennd qlapklavag lytlsnsrdp lvstnyygkl ktysyfgsaq
      601 lgfrnyafin fttrndwsss lpadalsyfy psvngslils ealgiksdvl syaklrggws
      661 kvgkatdpfq linvytssnl fgsnpqqsis nidlndhlkp etttsaeagf elgffhdrvh
      721 ldvsayntns inqiltvqvs sstgfsqkvi nggrlnnkgi evqlgvtpik sngftwditt
      781 nyslnrskva sldadgrlqs vvlgtdrtvq vlaslgqpyg alygtaytrn asgqiiidan
      841 gtpvfnttkr ylgkftpnwl gsinnsfsyk ginlsflvda rfggsiysnt nrtgtytgvl
      901 astlpgrgaa ngglsyyypg nntsaaavqv tgaapagvtv yndgmifkgv kadgspntti
      961 ipaqsyykgf tnideafvyd asyiklrevk lgyslpakwv nkigfqgatf svvgrnlwii
     1021 hknapnidpe tafnagngqg ledltlptvr nigfnvnlkf
//
LOCUS       WP_091164394            1143 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypii].
ACCESSION   WP_091164394
VERSION     WP_091164394.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypii
  ORGANISM  Mucilaginibacter gossypii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Mucilaginibacter gossypii"
                     /db_xref="taxon:551996"
     Protein         1..1143
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127024
     Region          136..1139
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkltflynav cairgvkckf llvlklttil llvgvlhlsa asysqtvtis gknkslesvf
       61 kdikqqtgyl ffysekvnik gktvdadfhd tqlvdvlsac lknfdlsfti vsktiviqnk
      121 ipeprtepvt inkvsvsgrv ldsvskttlp gvniavkggr gvigqtndkg efnvqadagq
      181 tlifsfmgyk saevkvvagq sivvrllpdi nnikdivvtg yqvikkdnyt gnaitvsgad
      241 lkrnnpqnvi ksiasfdpsf kvldnnfigs dpnklpkinv rgataipsin dkildrnnls
      301 snynlpafil dgfevslqkv vdldinries vtllkdgaat avygsraang vmvittkapv
      361 agklqlsyny eltfngpdls dyhvlnakqk vayeqlvgly dtktstsgdt kqdeldaqlf
      421 trlknvasgv ntywlsqplr nayqqkhsvy aqggdqsfry gidlryqtqp gvmkgsdntr
      481 ysggvnftyn psskliirnd ltitqvnqan spygdfstyv nanpyfpird stgrlvqela
      541 nwrvntfreg kdqyitenvf nplyeaslss fdklayteil esfsvdykls kslrlralms
      601 vnktgttsdk yvsplssvfy nfaadqannk gtydygtnas lnldgnvtig ynkqlgdhyf
      661 nlvlganila skadvktfsa qgfsndrftn igfariyken sgpygdvtrs rtagaffsgn
      721 yafqnkylld asvrvdgsst fgadrryapf gslgigwnih kesffrgsnv isqlrlkgsi
      781 atlgsisfpa yqsrsiylyd tqhwystgig atilgygnsn lewqktrttd vgmdiglfkd
      841 rivispryyy kltkglitdi nlapstgfst ykdnlgdmsn kgyelylvaq vfhasdwnin
      901 ltgnlahnvn kivrisdalk afnsnidnfq tnkdnnafst pltryvegks lntiyavksl
      961 gidpengkei lvkkdgtlty iwdvkdvqdv gnttpkaegf fgstvsykrf mlsfsfhyrf
     1021 ggqafnqtli drvenadprf nvdsrvleqr wkqpgdhtff knitdltdty vssrfiqkdn
     1081 lielqslyls ydfkpnairr lglqnlrlaa tandifrast iqaergiyyp farsltfsll
     1141 gsf
//
LOCUS       WP_091168210            1149 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypii].
ACCESSION   WP_091168210
VERSION     WP_091168210.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypii
  ORGANISM  Mucilaginibacter gossypii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Mucilaginibacter gossypii"
                     /db_xref="taxon:551996"
     Protein         1..1149
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124443
     Region          <42..126
                     /region_name="LolA_fold-like"
                     /note="family containing periplasmic molecular chaperone
                     LolA, the outer membrane lipoprotein receptor LolB and the
                     periplasmic protein RseB; cl19192"
                     /db_xref="CDD:473147"
     Region          139..1145
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkldssnfl rcccflmvll gqsaygyaqm sltnnnrlha rnfsypisqv teskvllkda
       61 lenlkkqfnv qiayqeglld nkfvptnlts nisqftlddn lkqllsafql tyrkindnqi
      121 siftvkdltl nnvsvaavtl tgkvvdagdg qpvvgasvyl kidnkvgait dvtgsfklvv
      181 pdkyagkplt lvvayvgynq eevpvsdpvs plqiklvqnn kalnevvvta lgiskqkksl
      241 gysvtevkgt eftqarennv analtgkvag vnaaglstgp ggssrvvirg ngglagdnqp
      301 lyvvngmpid nsvpggpatv ngitnnvdrg dgiaainpdd iesisvlkgg taaalygsra
      361 angvilittk kgriqkgvgv efnstatydn vavfpdyqye ygqgdggvkp ttlaaaqasg
      421 rrswgskidg stdyvavdgl thpyvaqknn lrnyyqtgst ytnslaflgg neaftyrfsa
      481 adlnskgilp gttydrktfn lalngklsdk lsiealaqyn vetghnrtga gdalgnpnwt
      541 plevantvdv rwlkpgydal gneqiwndas iasngyfvin kykeddvknr figqgsviys
      601 pvknltfkat isrdffnyny tnilptgtly ipngqyagik sdvsetnela tvsyktkiis
      661 dlnvnvlggv nsrkyttnql tlngsqftip yfysftnlav ssttpynaki vtnsvfgsad
      721 fdykslffls ftgrkdwfst lspksnsify psvggsfils davklpeffn laklrgswaq
      781 vgggapdpyv inltysnvps agqplqnvts nnitnsnlkp ytsttfeggf elqmlksrlg
      841 ldvtlydrkt tndivntais stsgynnvil nvgevsnrgi evllngtpvk tssftwttsy
      901 nvayndnkvv klapglntiq latsvgnwgi ldniegksfg mivgtrmqkd angnvvfnat
      961 tglpvqtplq qlgksvaplt mgltnefryk rfslnflvdg kfgnkvfsvm evyatrlglm
     1021 kstlpgreng lvlngvdqtg apytrtvpvs glrsyydnyk tysdlflhdg sfvklrqvil
     1081 syalptslln kvkiqsasis fvarnlwtiy kqtdnfdpeq sftnsnaqgf esiglprtrs
     1141 lgvnlavkf
//
LOCUS       WP_091168921            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sinopsychrotolerans].
ACCESSION   WP_091168921
VERSION     WP_091168921.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sinopsychrotolerans
  ORGANISM  Flavobacterium sinopsychrotolerans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Flavobacterium sinopsychrotolerans"
                     /db_xref="taxon:604089"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110897
     Region          46..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkislnkgr lafwyliiig fslsytpaqa stilrqnqyq qqqnqisgti tdgtnplpgv
       61 tisikgkatt gtisdfngqy rltaspndtl vvaflgfktt tvsisgrkii niqlqeditt
      121 lqevrvnagy ysvkekertg siasitaati ekqpvtnvla amqgrmagvs itqttgvagg
      181 gfdiqirgqn slrpdgnrpl yiingvpyas dpigfnasat imptltspln nlnpgdiesi
      241 evlkdadata iygsrgangv vlittkkgka gktsytahys hgfgkvtrfm dlmntdqyvq
      301 mrkeayandg ytkypasaye vngtwdqtrn tnwqkeltgg sstitnlqts vsggdeqtqf
      361 iingnygket tvfpgdfgyk kgnvrinlnh latdkkfgit fssgytvqdn nqpstdltti
      421 srklapnapa lydtegqlnw enstwenpls nlngkslskt ydfvansils yalpyhlelk
      481 ssfgftdlkh tesstfpsti ydpaygldsa fssiftttts rqswivepql nwhtdigrgk
      541 iavlvgstfn qltgqqlvls gegftsnsli ydlasastvs imssgsteyk yqaffgranf
      601 swkdqyfvnv tgrrdgssrf gpgnkfanfg avgaawlfsk sfidngspsf lsfgklrasy
      661 gttgndqigd yqyldtysss gnpyqgvvgl eptrlfnpdf gwesnkkfei atelglfndr
      721 ifltagwfrn tsssqlvgip lpgttgfnsi qanldasvqn dgieltlrtv nfqkknfgws
      781 tnfnisilnn kllrfpdles stysnkyvig splnivkvyh ftgldpatgl yqfedfngdg
      841 qlsakddkqy lidlnpefyg glqnqlhykg iqldflfqfv kqlnynsast lglpgsrnnq
      901 ttdvlarwqn pgdtgpfqqy stganaavan aytkyrdsda titdasyirl knvalsyqlp
      961 pswlkgveck lniqaqnvlt ltsyrgadpe fktrgvlppl kiittgiefi f
//
LOCUS       WP_091173010             991 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sinopsychrotolerans].
ACCESSION   WP_091173010
VERSION     WP_091173010.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sinopsychrotolerans
  ORGANISM  Flavobacterium sinopsychrotolerans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Flavobacterium sinopsychrotolerans"
                     /db_xref="taxon:604089"
     Protein         1..991
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108760
     Region          24..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykklli lllllpfsil aqntvsgivl dkvsgqpipg vnvnvqgaan gvstdfdgky
       61 qltkikkgdk ivfsyigykn tvvdyvtqns lnvsleedan qlqevvvqvg ygtvkkkdat
      121 gavtvlaakd fnkgqnvtae slitgrvagv sitgggspga kanirirggs slnasnepli
      181 vldglplsna vpngstsils tidpndietf tvlkdasaaa iygsraangv ivittkkgsk
      241 dglkvsfnsq tglstvantv dvlsadefrt lvnangsaaq kaklgtantd wqdeifsnvf
      301 tsdnniavsg slfkklpari svgntntpgi lkntsfertt tslslnptfl dnhlkiding
      361 nlsfgknqfq degrvigsai gfdptqsvyq dgsryggyfe wleangdvnl laaknpvall
      421 nqnnrrstst rkwgnirvdy kfhfleelra vaelgidkfd sngfeetstn sitgfqlntf
      481 ssgqwtnagd ykkytdtrqn knlnaylnyv kefgkfkvdl tggynyqmfe regyvsgdlr
      541 rpnpaqdvat dpdinlqsyf granlgydsr ylitlnyrrd gtsrfseenr wgnfagaafa
      601 wniaeesflk dnetvsglkl rvgygttgqq disasydylr rvtlgtvnsn yifgstayqv
      661 aktegynkdi kweetseini gldyglfndr ingsvnyfqk eandlladia ypdganlrns
      721 gfsnigsvtt kgiefninad vvknenlnwn lafntayihq eitdlgltvp gfqgyetgdn
      781 iaggsnnkvk insvgfnpga fyvfeqlydt nkrpiqgayv drnadgkidn sdryrfhkpn
      841 adytfglfst lnykkfdftm swraslgnfi fdninsdkgy lqaalrrdsd lanitpdyya
      901 tgftfedngt qrylsdyfvk dasfikldnv tvgysmdksl lkdvslrfsl gvqnalvfsk
      961 ydgldpenfs gvdgsvypra rtfvfgvnan f
//
LOCUS       WP_091173302             997 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter].
ACCESSION   WP_091173302
VERSION     WP_091173302.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter
  ORGANISM  Mucilaginibacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Mucilaginibacter"
                     /db_xref="taxon:423349"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108888
     Region          38..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknyrfilr lffeksktic lfllmfiass avfaqdgtik gtvtdesnlp lpgvvvtvks
       61 sgrststnan ggytvktsga gdvlkftflg svpkevtige kntvnvtmvt dtkqlkdvvv
      121 igygtasrkd vtgaitsvka edfnagvltt paellqgkva glnitksgdp nkqpatilrg
      181 pstlregaaq qpfyvidgvp gasidllapa diesidvlkd asstaiygsr aangviivtt
      241 rrakagqtrl tysaygaven vsknidvltg delrkyltdn gvpklsaadd dgsntnwqkl
      301 aertgysqnh nlsyggagtn seygasvnym knngilrnts lertiykgyi nqrffndrlk
      361 lgitltnsat knndifqsqv lsgilfylpt vspfnpdgty kenytrtgsg plnplslinn
      421 nftktennkt lingfasvdi lkglkftisg stqkeqnnvn tystsqsgiy vnqngvavrs
      481 aytntsnvve ayfnydrvfg khslkllggy syqqdrnndg fgvqtqnfsn daltynylal
      541 snptqlsqiv fnpnyistlr fvsfyargqy efsdkyllqa slredgssaf ginqrhgyfp
      601 aasagwkiin edfmksvpvi sdlklragyg vsgnslgfda ftarliygvp pgggkflsng
      661 niinpigpvr ndnpdlkwes tattnigldf glfnnrltgs vdyyikktsd liytypvstt
      721 lyfypfytan vgkiknsgie vvlnavpvks qaftwrtsfn vshnknvvqs lsnsqfglnf
      781 iqtaqlggkg qsgnysqiiq pgyaigtfdl whymgknang vstyqkadgs viatqpltsd
      841 qfikydaqpk lvygwsnsff ykgfdlnflv rgvygnkiln atlaslnnpa dsklqniprf
      901 tlgesfkdvn aylisdrfle sgsylrldna tlgytvkphi qaikslrfya sgnnifiitk
      961 yrgvdpevni ggltpgidnr dfypktrtfs lgitasf
//
LOCUS       WP_091173680            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sinopsychrotolerans].
ACCESSION   WP_091173680
VERSION     WP_091173680.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sinopsychrotolerans
  ORGANISM  Flavobacterium sinopsychrotolerans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Flavobacterium sinopsychrotolerans"
                     /db_xref="taxon:604089"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113633
     Region          27..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngilv lllvlvaqlt faqeravsgi vsdntglplp gvsvlvkgtq tgtqtdfdgk
       61 ytikaspsqv lvfsyigmrt qemaassanv niklqedsvq legvvvtalg ikrdkkslsy
      121 aaqevkgstl neggsnnavs alsgnvaglq vtapssmggs trivlrgvgs vtgenrpliv
      181 idgipldngn yntsntqrga ggrdygdasa dinpddiesv tvlkggpaaa lygsragnga
      241 ilyttksgkr gsgkseisfn tgitfedayi apklqnqygg gssmtfenqi ingktyklad
      301 yatdeswgpk ydptlmylpw nafdpefasd ylkekawvas pndvdsffrt gitrsnslsf
      361 tksnedsgir fsyanqkteg iipnstltkn tfsinanskl seklkvegma tyvqtrgfnr
      421 pevgygdngl aqkfyqwsqr qldfselkny kladgtqrsw nriawddatp nysdnpywii
      481 nentsadtrn rlygngkity nitpdlyavg nvygdtysln inervaigsq atssftttar
      541 tltdfnyegr lhydkkfdkf slnsfvganr rsynlsrvtg atlgglvlpn vynlsnsasa
      601 aqatnyeekt rtnsiygfls lgyddflfle vtdrndwfst vnqdvnyasl tgsfifselt
      661 dlswlnygki rggwaqagna ttpyrlsfdg vadtpfqgdi rysqpntasn pnlkpelktt
      721 kevglelslf nrrvgldvsy ydvvttdlit pvqqdpaagy pfalknagkl qnkgfeatvt
      781 lnpvrtedft wditwnfakn nnklielapg lneliigtap fqatllavtg qeygqiygtd
      841 ftyddngnkv vdadgayipt arkslgtitp dynmgirnsf kyknlslgfl idiqkggsyf
      901 stthmwgsys glleataann irengiivda vyedgtknts vlpgqawaqq hygldamnvf
      961 dasyvklrev tlgytlpkki ignfgdlrfs lfarnlfawg ldwngmdpem asygsgntqg
     1021 leggslpstr tygmnlelkf
//
LOCUS       WP_091174342            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sinopsychrotolerans].
ACCESSION   WP_091174342
VERSION     WP_091174342.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sinopsychrotolerans
  ORGANISM  Flavobacterium sinopsychrotolerans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Flavobacterium sinopsychrotolerans"
                     /db_xref="taxon:604089"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113722
     Region          68..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkisvyrsw kpfiyplilg iylnsisptl ahnpspnnnn nnnnnnkerp qtkrsavvpl
       61 wqykqqnqin gtitdgtspl pgvtisikgk rnntvnsdfn gqytltatat dtlmisfigf
      121 ksatipingr ktvniqlred itslqevrvn agyytvkese rtgsiskita kdietqpvnn
      181 plaamqgrms gvniiqstgi pgggfsiqir ginsirsdgn eplyvvnglp yssqslgdst
      241 iastailgvt nplnnlnpad iesivvlkda dataiygsrg angvvlittk kgkagetkfn
      301 inasttvgkv tstldlmhtp qylamraeaf tndgitqypa daydingtwd qnrytdwkke
      361 liggtayinn vqasvsggnp ntqyllsaty rkettvfpge snysrgvvhs sithksadkr
      421 fnlnfsadys sdkntlpgrd ltarayalap napalydaag nlnweegtfd nplaylqaty
      481 lnsmqnlian tllsyqilpr lelktslgyn ntsvsqsytr ptsifnpfdt stheaslyls
      541 sgngkswiie pqlsyekswg kiamnfligt tfqnqkttql aqsgsgftsd alinnldaat
      601 rvsvlnhkvv eynytaafar lnlnfkekyf inltarrdgs srfgpenrfa sfgaigaawl
      661 vsnesflknn evlsfakfrs sygitgndqi gdyqyldtye vsrylydgvv gltparlfnp
      721 nfgwetnkki eaaielgfln dnifltaayf knqsssqlvg vplpgttgfa siqsnldatv
      781 qntgfelelr tvnfrkkdfs wtttlnltvp knklmafpnl esstyanslv vgeslfinkv
      841 fnhtgidpns gaytfqdyng dgqitfdsdr qkvvdtapky yggfgnqlsy knwgfdflfq
      901 yvkqqgknyl yssslagtft nqpaeignhf plngtgaiaq qyttgdnsav vdafynfies
      961 daafsdasfi rlksvnlsyt ipsawsktft grvylqtqnl ftfthyrgad penqstitvp
     1021 plrqftlgfq lgf
//
LOCUS       WP_091175574            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypii].
ACCESSION   WP_091175574
VERSION     WP_091175574.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypii
  ORGANISM  Mucilaginibacter gossypii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Mucilaginibacter gossypii"
                     /db_xref="taxon:551996"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120398
     Region          30..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqfylnlkr wvvlllplfi sanlfaqtnv tgvvrddagp lpgvtvlvvg tttgvqtnin
       61 gaysikvakg avlkfssvgy tpkevtvgdn avinvtlaag kgelnevvvt sfgikrqeks
      121 lgyatttita kqlteagntn fasalygkap gvkittapgg sssavnvqir ginslnyntq
      181 plyvvdgvii rnnseagagg snndgywsdq rirgngildi npqdietltv lkgasataly
      241 gsdamsgaiv ittkkgsksr glgvdfnyvg taeqvaftpn fqnvygpgyd ratnlaggft
      301 edgwladans psgyrprfss yaqfgpkmeg qkirwwdgei rdytpqpnny kdlfqtgyss
      361 naniaisnqt dnvnyrlsat rldytgiqrg qkqqknsfnl nttvklsnki sadivasyvn
      421 tlthnrpyql grvlanfggf lnrsekadvl ldnyqtslgy kyvtlgnaar npaeafkynm
      481 sgadimdffw tqlknsedet enrlitsatl nwdvlknvkf rgrigsdytg rntesqqyne
      541 yptafngsss tgyygvtkgq ysvtygdlll tyspkltkdl smsvsggyts rsetyrdqss
      601 gtngglvten ffsisnsygv pntsatrgyl ksqaffgiln fnyknylfle gtarnesast
      661 lptqnntyfy psvnagfift dafkmpefis ygklrasygv vgnkapryvp nvlynqsslq
      721 tqngsvtqlt fdatygnlql kpemkyeqey glearflkdr lgldftyynn qvknvimaln
      781 vapttgassl lanaatlhsd glevgfsgkp itgkfnwdvr lnfainhskv nnlapgfdrl
      841 tfytgdqsal lvvaqpnqpi gnilvypiak dangnkivns dglytidksk yvnvgniqpk
      901 ivggiantfn ykgfsldvlv dyrfggkmvs nplkygtaag myestlqyrd aahgglayyi
      961 dgnggkhlgt apnggktynd gvilpgvnen geknttivda asyylntydw gensvnenav
     1021 fknnyvklre vvlgyrlpas vnkalhlnnl rfslvgrnll yvyrtlknld peapigdkwy
     1081 rqgvdegssp atrsfgfsln anf
//
LOCUS       WP_091192067             311 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Formivibrio citricus].
ACCESSION   WP_091192067
VERSION     WP_091192067.1
KEYWORDS    RefSeq.
SOURCE      Formivibrio citricus
  ORGANISM  Formivibrio citricus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chitinibacteraceae; Formivibrio.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Formivibrio citricus"
                     /db_xref="taxon:83765"
     Protein         1..311
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35691
     Region          5..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifdlfskr qkklrgempd vyqysdipha lrvqivhiwm dtlgnaenyw ngkvneaykf
       61 ivdtlcreyg ifrlagakny gnreyleefv naflnerdte kcldfielaf kvidlftrdy
      121 eylrrsrasq kadesideln srfkehgvgy qftdgemirv dselihsevi kpalrllnqk
      181 hyagaheefl kahehyrher hkeslneclk sfesvmkaic dkrswaypsg atakaliqvc
      241 ldnnlipsfw qqsfgslrsl lessvptgrn klgghgqgse sfsvpshlva ymlhmtaasi
      301 vflaeaeasm p
//
LOCUS       WP_091201384             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides alpinus].
ACCESSION   WP_091201384
VERSION     WP_091201384.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides alpinus
  ORGANISM  Nocardioides alpinus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nocardioides alpinus"
                     /db_xref="taxon:748909"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52172
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresr pgetlvaata ktasqlaalg ydvvveagag aaadqpdtsy adagvaigts
       61 advwssdvlv kvnaptadei arlrsgatvi almaparspe lveqlaaagv tglamdavpr
      121 israqsmdvl ssmanvagyr avieaahefg rlftgqvtaa gkvpparvfv vgagvaglaa
      181 igaagslgai vrafdvrpev aeqvesmgaq fvtvdmeqev stdgyakemt aeqevataam
      241 ydeearaadi vittalipgr papqlitaet vaamapgtvv vdmaaanggn vaatvkdekv
      301 vtangvtvlg ytdlagrlaa qtsqlygtni vnllklltpe kdgrltldmd dviqrgiavt
      361 rdgqtmwppp pvqvsaapaq atavlpveka ppkevdprrr tyavglaavv flalatlapa
      421 sflpsltvfv lavvigyyvi gnvhhalhtp lmsvtnaisg iivvgavlqa pvdnlavqii
      481 agvaillasi nvfggflvtr rmlnmfqkg
//
LOCUS       WP_091202345            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            xueshanense].
ACCESSION   WP_091202345
VERSION     WP_091202345.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium xueshanense
  ORGANISM  Flavobacterium xueshanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Flavobacterium xueshanense"
                     /db_xref="taxon:935223"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110576
     Region          25..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskykwiit lflalsmqls faqektvsgv vsdatgplpg vnvsvkgskl gvqtdldgky
       61 sikaktgdvl vfsfvgmtet sktvgssnnv nvamqdgvsl nevivqtnlg yyskdsrkvs
      121 ssvstvsade iakqspalti qnalqgqaag vqvtaqngkp gaaayvtvrg avsitggtae
      181 aiyvvdgafv sgteasalss ndiesvsilk dgasaaiygv rggngvvvit tkkgknakgk
      241 fqfnnsigft qkiadpfdmm nadekiryeg ligagsttaa tvtparlall rsydhnwqdd
      301 llrkgfvqnn nfsysggndq ftnfmsvgyt edsgiidklk gfnritgryn seykandrvk
      361 fgfnvggsye kfndsrdrnn aqspiramyd ynpyepfyar datgnvindv lgnpvfntnl
      421 lagfpiqeai itnteqrrff rlygrpyvel givkdltfkt qmnmnyeryq resftkpgsf
      481 ldqivgdaaa rgsktdngwd sleyqltnsl nykysingkh nfestvlyey fksnfrsytm
      541 trkgyvngdl ptagtavigv patgrsenat vsifgnidyd fdskylvsly grrdgssvlg
      601 tnnkysfakg islgwnvtse sfmsnvkwln nlklrasyge lnstngigsy taqslfstsq
      661 ygggigtvlt nstvgnnnlk fekaekyeig iesavlnnwl tfsgsvfkdk rndfiysdnt
      721 tvgtafsali nagdwtskga evelkafaik nanttlsfyv naavfdrein elnrpgdpnn
      781 qlsrgltwnk vgrspddffl vpyagvnptn gratytkldg tvtdvysagd rvftgktpya
      841 kyeggfgmqf aykgfdistd fvfkegnyty nymwqnmtad gaapnrnqav aafdfwtatn
      901 ttaslpapqq ksginsnles drfledasyi rfrnlnigyk ftkkafsnlp vddvriytqm
      961 qnlftwskfn gdpevgigsa esqtgllvpg qfalysypsv qtflfgvsin l
//
LOCUS       WP_091203671            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            xueshanense].
ACCESSION   WP_091203671
VERSION     WP_091203671.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium xueshanense
  ORGANISM  Flavobacterium xueshanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Flavobacterium xueshanense"
                     /db_xref="taxon:935223"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119235
     Region          27..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv lllvlvaqit faqeravsgv vsdnagmplp gvsvlvkgtq tgtqtdfdgk
       61 fsiratpsqv lvfsyigmkt qeilasssnl nvklkddsve legvvvtalg ikrekkslgy
      121 atqevkaedl nsgagsgnfi nelsgkvagv nikrnnnfgg sssivsrgvk sltgsnemli
      181 vidgmpinns lvtgstgnqa ggaggtydyg naamdinped iesvnilkga aasalygylg
      241 gngvvmittk rgrakkglgv tvssefvgst idkstfvkyq dkygagygpf yedasgyfls
      301 rdingdgied lvvptsedas ygaafdpnlm vynwnaftpw sdsfgkatpw vaakndpttf
      361 fqtgtsfnns vsledgndtt nfvlnytnsk qtgilpnsdm kknsvsakin hqfsdklsas
      421 vfanynaqst vgrnstgyne nimsmfrqww qtnvdvqelk qvyersggqn inwnysdpsd
      481 ltqiywdnpy firnknfqsd ernrfigysk ldykiaewlt atakistdsy selreerraf
      541 gsiaglfgin rldetsgyqk yqrsfseqny dfiltfkkdi senisfsgva ggtavrtrii
      601 stlnstqggl ivpnlfslsn svqqvpfple sevnqginsy ygsasfgfkd yffvdatarr
      661 dafsslpaak naiwsysasg syvftnhinq pwlsfgkira gysesplgtp glslvdtyvk
      721 ndpfgsnqly svagtknnpn leavktntqe iglemqflnk rlgfevsayk nvnngeafqv
      781 pfstatgnsa ryinaatven rgievqfnvt piktkdfawd vfvnwsknkn evtklaagie
      841 nlrlnsfqgg vtlnasigqp ygvlkgtdyt yydpsfvpsf pgevnkngpk vvgangryvv
      901 nasannvigd vnpdwlggir nkftyknlsf gflidmkkgg difsldqsyg latglydvta
      961 glnelgnpir ntiangggvi lpgvkadgsv nttrtpapnq ygnvsgyrra pnkafvydas
     1021 fiklrevnit yslpttlvsk mnlqemkfsi vgsnlwiidk nlpyadpesg lsasassagy
     1081 svgslpttrn vgvnvtfkf
//
LOCUS       WP_091204348             978 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            xueshanense].
ACCESSION   WP_091204348
VERSION     WP_091204348.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium xueshanense
  ORGANISM  Flavobacterium xueshanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 978)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 978)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Flavobacterium xueshanense"
                     /db_xref="taxon:935223"
     Protein         1..978
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107226
     Region          24..977
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykklli lvlllplsvl aqntvggtvl dkvsgqpipg vnvnvqgatn gvstdfdgky
       61 qlsnvkrgdk ivfsyigytn tvvdyvaqns lnvslqedan qlqeviiqvg ygtvkkkdat
      121 gsvtvlttkd fnkgpvtsad qmiqgkvagl qiingggspg esatirirsg sslsagndpl
      181 yvidgvpvnn ggieggknpl stinqnnies itvlkdasat aiygsrasng viiittkkgk
      241 ageiqvsyng nlqvsevtnr vdalsatqfk dfvaangsvt qqklvgaadt nwqdeiyrta
      301 igtdhnials ggvdnvvyra svgyanlngi lkrdnmerst lgvsvtgnfl dkhlkievnn
      361 ntsliksnys nrgaigsain fdpsqavrna dgtyfqwyas pteinqlagr nplslinqqn
      421 nfgnsyrsig niqteykmhf lpalkavanf gydqlsgtgs ggtnaeflng lngsgynnty
      481 kniesrknkv mdlylnynkk vdaintiidl tggytyqdfq dsknksnynf qndvttiesf
      541 tpsrinlqsf fartnitiad kyiltasyrr dgtsrftpdy rwsnfpavav awklneesfl
      601 kdvssistlk lrggwgitgq qnigiypsip lylasnntaq yqlgntfytt yrpqpynsnl
      661 kweetttvna gfdyglfnnr ftgsvdvykr ttkdlllntf npsffgfsnk dnynignidn
      721 kgiellaevi pvrtadlewt iggnvtfqds kitkltttqp ntpgidvggi aggtgnfiqn
      781 hqvgyapnsf yvyeqaygad gkpidevfvd rnkdgliteq dkyrfhkpaa dvfygfntsv
      841 tyknfdmgmn wrgswgnymy nnvdsnfgty nnvllrqtdl sngvanllet gftksndlql
      901 hsdyyiqdas firldnvnvg ytfnqkpnst slvkltlsaq nvllitkyeg ldpeisdgid
      961 nnlyprpitf tlglnvnf
//
LOCUS       WP_091206326             993 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091206326
VERSION     WP_091206326.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107550
     Region          27..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqikhllnvc ffavflflme pamaqnkvit gkvtdkkdgs pligvsvvta vgasggaitt
       61 adgsyrisvp staksltfty vgysnltvpi ngqsqinvsm esaskalnev vvvgygtqrv
      121 kdatgsvasl stkdfnkgqi atpdqllqgr iagvtvtpgs gepgsgasin irgtgsirag
      181 ndplyvidgv pvsndsyaas saaspigmss arnplsflnp adienisvlk dasasaiygs
      241 rgangvvlit trkgrkgqgi qfsentsyst aanrykllsa sqflqavaat gadadainkg
      301 antnwqdqil rkvfsqnfnl gfggatggfv yrvsgsyddq ngiikksglk rgtvrinatq
      361 slykdvvkld lnvlgsnvkn vyapitnnag fqgsligati glnptypvkn pdgtyyydgs
      421 slnpvdmlnn twdrdnvdrv lanlglsvkl trnltyrgty gndyslakry tfydpriqgy
      481 tssstirgkt tpaisgtgmg alqtvklgne iteqtltydk kwtdnsslti lggysyqvfn
      541 nksfndiryk tsqanvlvkn indfqnpfpv fgdtsrsklq syyarinysf kdrylltatv
      601 rtdgsskfgk nnhyatfpal avkwkimnes fapkgifddl slrlnygktg nqefppyqsl
      661 pvwqydlagg ssqlyaanpd lkwetttnyg agidfaifnn rvtgsidyfn kstkdllflk
      721 yfaqpapfpa iwvnlpgnvv nkglefglsv aavqgtkftw dvnynmtflk nnvkgfeqlv
      781 vqtgaisgqg lsgafsqviq nnyplftfkv aqyngldkdg fgiypngidv qtlqgsalpk
      841 ftasltnnft ygnwnlsvfl navtgfyiyd ntanayfyrg slltghnvst dvaftnenpl
      901 nsgqvstrwl ekgdfvrlsn vtlgytfqlk nskfikslra altgqnlaii tsykgldpei
      961 nvnkdinsvp srgidytayp kartytfglt agf
//
LOCUS       WP_091206508             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091206508
VERSION     WP_091206508.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108218
     Region          27..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mykklllrls afalccifts aalaqnrtvt gtvtdaadgs plpgvsvvvt gmsvgttsna
       61 kgvytlsipa saktisfsyi gystrvvplt sdgtlnvslt tsskslqevv vvsvgygtld
      121 krevssaith vsskdllpva snsplmslqg kvaglnitnt atadpnsspk vqlrgvssrn
      181 aglgplyvin gvpggnidni nqndiesidv lkggaasaiy gtrgsngvii ittkkgssqa
      241 rtfyegyasf dyltnrlqnl tpdefindrv knnqgqdyga ktnwmdavtn spafaqkhti
      301 qlsggsgktn yfasadyrna dgidlrankk eygarinvnh atdngifvas lsvaprymnt
      361 knsdqgnfnn altlnptypi ydtahkynyi ntgffsnnpv enanviksea eikeldings
      421 lrvnilknls ttvtiseisr sarsynftps tlssivhagk itqtnfasqr qeendqknve
      481 wtgnysfdlg rhhfkalggy sytlynyntf yaqnydfpfd sylwnnlgsg lynggaagqg
      541 qsavsstqng stlisffgra nydfnnryil tasvrregss kfgtnnkwgn fpaasaawrv
      601 seesfmkgal pwvndlklra dygvtgnqdf dsylslllyg gagyfpyngq vyqvygptsn
      661 vnpdlrweks infnvgldfs ildnrisgsl dyyirknkdl lgyynvplpp nsqtqtfanv
      721 gtmknyglel alngavvrns dfnynvtfal aynrnkfisf sndiykgapf velaglpapg
      781 spgniqriqe grsigefytl rsagvnkdga lqvykkdgti vqanqasadd kqfvgnglpk
      841 figsmgntfr ykrfdlgifl rgtfgykifn tsafyigtps sqsdanvlks aydkkskysl
      901 ltnpattaia sdyflengsf vkidnvalgy tqpfktkylk sirvyatgrn lhtftsftgg
      961 dpdlvevngl tpgvntslny ypatlqlilg lqatf
//
LOCUS       WP_091208352             752 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091208352
VERSION     WP_091208352.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..752
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=82372
     Region          <16..749
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqslpapftq eaidqlnsst dwykaitrta fredntlnis ggnektsyyl sgdyltdkgt
       61 vlasqnnras lranlssdvn nwytvkaqls ltrqktsrai tlsngfpgsd gvildalras
      121 pivavdysgf ngegipgftd gnifsnpvte lqqktdnlys dftianiend fkiakglkli
      181 vnlgtnqnls hrevffpatt asgyntngsg innisntyny nanayldyrr efkgghnvni
      241 tggveynhnt vemlntstsg ydipsfgiyn igsaqiqstg sfkeakviqs aflranytyk
      301 dryvlnasvr ddgassfaen kkygvfpaig lawnlsnetf mkkfnwisnt klrasygetg
      361 sqaiqpyssl aqygnafyqt gttntintal ypatlgnanl swertkqlnv gldfsliksi
      421 lsvsfdyynk etdgllqprs lpnqtgfgsv ednygsmrnr gveatvnani vssgafryst
      481 kvtishnknv llnlgdltap qyvslggnlq ggvsgilkpg qeiglfygyt vaglvqtgdi
      541 vngvpkypyp gaasgqiagq wkfadvngdg qinsddmrvl gksnpdftyg wnndisfknf
      601 slnlfftgsq gnsivnltrf ylsdgtadys giffnqtadw yahrwtptnp tnnprypgiq
      661 kslpiadlns sylengsyfr lksatvswyl pknnilknar lfvtgtnlft itkytgadpe
      721 igsygqsllq qgidygayag yrtytigfst nf
//
LOCUS       WP_091207589            1237 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter].
ACCESSION   WP_091207589
VERSION     WP_091207589.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter
  ORGANISM  Mucilaginibacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1237)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1237)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1237)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1237
                     /organism="Mucilaginibacter"
                     /db_xref="taxon:423349"
     Protein         1..1237
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=137101
     Region          180..1236
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiyfmgkll pfhpyvrrpp aalnqvpyai fktlfkrnfk mpirpflqla fkriclialc
       61 lfvlipltqt nkafgqdlsk lisvdvtdkp lkdvltiigk kakvgiiysn vsgnlnakls
      121 lhetnqplkk vltdllvpld ldfdiignri vikskiinte krdlssqnss ptdgrnlklv
      181 hgtiisaetk lplngasiyl dnkiiaqtdp sgvfyfrtsd ttgtfrivfi gyasqeisfd
      241 qrktgpfnit lipdqtslne vvistgyqni pkerssgsyd lidnkllnrn pgdnilnrls
      301 giasglrfng eantniatgs dsrflginir gvstlsgnvs rdplivvdnf pyegnlsnin
      361 pndvenitil kdaaaasiwg arsgngvivi ttkkgrknqk msvevngtlt fqnkpnlyyd
      421 rnflpssdyi aletdlfkqg yfntaindvs ywtpvspvvd llaasqagti sqadaaarin
      481 slmnqdvrrd yekyiyrksv nqqysigmrg gseqnaytms lgyvnnqnpl irngfnrltv
      541 naqnvytpit nlsittglny srnvtalnna lnygtgisvg gniagiypya qfadndgnhl
      601 aitkdyrasy atkatssgll nwlykpldel gfgdntttvn dlvlniaaty rflkhwninl
      661 qyqnenqqvg grnyqnkdty aartlinqft klnpgaspty qvpvggilnl snnqlianng
      721 raqlnydqtf dnkheitgla gaeikqlqni gynrnllgyd defgtavqnl nysdyvlinp
      781 sgygvipspg gniygstnry lsyfanlayt ydskytltas grkdgsnifg vktndrvtpl
      841 wsigatydia rekfykidwl pslrlrasyg fngnvyngsa yvtgrygasq itgatailnl
      901 tapnpelrwe kvkninwgid fgtinnrvtg tieyyikdgk dlieriplfs ssgflafngn
      961 aastttkgfd itlnsknitg kfqwitsllf stlkdkvvsy dqsltntsiq svsgmpvvgr
     1021 siyglysykw agldptngdp qgylngkisk dyttiinnfn sdslkyngsl rptvygsirn
     1081 efsygplsls anigfefgyf frrpstsina adiisatgsq nidyqqrwkk pgdealtnvp
     1141 sviypsnnnr ntfyryssvl vdkadnirll dvrfayvldk ntlktlpfkk ievfayasnl
     1201 giiwrankyg idpdisalgf nsiptpftma igfnanf
//
LOCUS       WP_091208486            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091208486
VERSION     WP_091208486.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115359
     Region          24..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkykyllil fflfplglla qqttingkvi dltdgstlpg vsvkikdtnt gaitdvagkf
       61 qlqvpgpnai lqlsyigyvt qeiavkdikd gtialktnnk sleevvvvgy gvqkratitg
      121 siatlqskei tttknesvin mltgkipgvr ivqntaepgs yannlnirgy tnaplvvidg
      181 viggdqstig rmdpneiesi svlkdaaasi ygmraaggai littkkggkn gkininysvn
      241 daiqtflgmp egvgavdyml ltnekvkrdf annfvhnvtp qysyadmkpw ldgtrksadw
      301 iglafkktan qiqhnlnidg gtdkisyffn fgyqkqdgvf ksgdlnynky nfrsnvtasi
      361 tkglkaqvlt sawmdeknqp ytdewtiyky twnqipinqv yandnplyps lipqgdnvnp
      421 aiatdadkvg skrfrnknit sqlnlqydip gvpglsakal fnieygtadn niikrsfnly
      481 tynaeddtyl pnlvnspggi trqyythlnt lsqvtlnyah tffkdhnita matyeqshet
      541 adnfnayrdv eipvdylfgg lqnsnmaggm dagalqdrah rsiigrfnyd ykgkylaefs
      601 frrdgnnlyk pgpdqwgffp ggsigwvltr enffrklvse niltnlkira sygqtgdean
      661 apafnyvdgy typinsyifg asavngsapk lgnagltwsv stikniavdf slfggkvdgt
      721 vevfrndktg lpvtpavalp gtvgapvpsi nyesnraqgl dfnlsyrntf gpvglnvtgn
      781 igttrlkkik vlegragney eqwknsqanr yqniwwgpey agqftsynqi ynygvntggg
      841 nnntipgdyy ykdwnndgvi dgkdshpiat sdiplynygl tigvsykgfd mnmllqgaag
      901 vyvqygeqfa splmynrsal trfldswhtv dpsanvfdpn tqwipgfypa mgspdaqgtk
      961 aiqsasylrl ktlefgysls psvlkaigvr kfrvyvnsyn lltftglkny dpehqgpkpg
     1021 dngfgatalg gytypmnrtf nlganvsf
//
LOCUS       WP_091209112            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091209112
VERSION     WP_091209112.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119311
     Region          32..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkishisfiv fliltlysek tsaqnpfyfi ygevysssge piaganvywk knktemtsds
       61 kghfrlvfnp psdtlivscl gyktltraih endptplkit llpsitelke vavstgyqni
      121 pkeratgsfy qldrkvleqr vgpdiisrld gitsglifdn hdieqhtiqi rglstliyda
      181 asplivldnf pysgdinnin pndiesisvl kdaaaasiwg aragngvivi ttkkgragqp
      241 isvsfnsnlt vsprpdlfka nqisvssyid lekqlfangf yddalndpsy pgyspvvdll
      301 nqvrngeits gdantqidkl athdvrtdmk nylyrpsvsq qyylnltgsg pnvrylfsag
      361 ydknlatlrg ngnerftirs nqqinltknw tlqtdliltr tnghnnspgg ygsystynng
      421 mapyaslvda agrpaaidly hnraftdtag ngklldwkyr plqdlanndn rsstndilin
      481 igtsykflkw ltadfklqhq qswsdsrqvn nlntysardy intftqiddg ipayivpkgg
      541 ivyansggsk qdavrgqinv drqwgtdhrl taiiggeirk tqsdnsyqti ygydsntltt
      601 rpvdyanmyp tydeingdgy iadgtrltry dnrfvsvfsn aaytfldryt isasarrdas
      661 nlfgvatnqk wrplwssgll whvdrepfyh lswlpqlalr itygesgnls pnesaltrit
      721 yydasrspvh apyvginspa npylsweqvk tfnagidfsf lnnrisgsle yynkhadnli
      781 nsvitdpttg fsavnrnsaa iftkgadlvl nsinldgnfr wsstllvsyi nykltknlap
      841 vsteglvsdg tyifpvlgyn pyiiasykwa gldpqtgdpm gyvngqiskd yaaitknpvd
      901 qqvingsavp slfgsirnti eykgiaaafn ityrfnyyfr kpatnygtll ssgvgykdye
      961 srwqkpgeen ntnvpsfiyp ddserdqfyh ysavnvakad nvriqdiyls ydvplrsssr
     1021 ifkklqvyly anqlnvliwk ankfgidpdf iygiktpaay sigfktnl
//
LOCUS       WP_091209357            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091209357
VERSION     WP_091209357.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120408
     Region          35..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkslyinill tccclalhlp anaqsnsknf drldgvvhdi nnkplnevqi hvkgkkaqty
       61 sgtdgsfslk nihvsdtlif akpgymhqev viysgsfini rlwpdvqqvg eikvvstgyq
      121 tlaqekatgs feqinsslin ratgtgvlsr ldgvssiafd krigqeniln irgrstlfan
      181 saplivvdnf pyngdlsnln pndvesitil kdaaaasiwg vrasngvivi ttkkgrknqa
      241 lavsfnanat maakpdmfyl prmssadfvd menmlfskgf ysddensylh apispvvetl
      301 iaqrdgtist aqanekikay kqqdvrkdlq kywfrqsinq qyalnisggg eksafvfsag
      361 ydhnlsalsg tyerlnlrsd nsfypteqlq idvgayltns ktiagrddyt slitgnsksi
      421 ypyasladar enalpvlkdy resfkqdaea kgfqnwdyyp ltdyqnnsnr tdltdllfnt
      481 gityrvlpgl kaeakyqlet aqtqgsqlyg kdsyfarnli nqytqtnang sltlpiplgg
      541 ilqssdnrli snslrlqlny kkdwgknqlt alagyeyrtd qnryrlsgdy gynadiqtsq
      601 qvdyktsyfl snysyyidnt ipyinqfetr rnynlsyyan avynydsrys lslsarkdes
      661 nlfgvesnqk gvplyaggaa wtvskegfyh igwlpylkfr ltygyggnvd ntlaaqttir
      721 yvglsslgkq tyaivvnppn pslrwektgt lnigtdfall qnritgsvdy yrkngkdlig
      781 fqpldqttgv lnpatnlfqy kgnvaamkgq gleinlhsnn lngnfkwqtd llfnhtsnnv
      841 tqyyqysdng anfvanglsv tpivgkplya iltykwagld petgdpqgyl dgkvskdyag
      901 ilnntkvgdl qysgpavpqy ygnlrntfny kgfslsvnfs ykldyyfirs avsytalfnn
      961 wntlsgdyak rwqkpgdekt tnvpsltypa nsqrdafyna ssanvekgdh irlqdmtfgy
     1021 dldqrklkgm pfkhlglyvy aanlgvvwka tktsldpdyp ysvkpprtis lgikanf
//
LOCUS       WP_091209924            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091209924
VERSION     WP_091209924.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114352
     Region          24..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllvslc llvlsmtqvf aqnrtvtgtv takddglpip gvtvkvkgtt igtqtnaagk
       61 fslsipenst lvfsfisyet qeiasaqrin fnvvmvsaak qlgevvvqaa ygvqkqarav
      121 gyasttvdsk llteskvtni angltgkvag lqintvnngv npdvrivlrg nrsingnnqa
      181 lvvvdgtpvs snfinqinpn didnvtvlkg agaaaiygse gsngvllitt krgsgaptit
      241 ytnstqienf syfpklqref gggagevidp ntgfygyvpy enqsfgpkfd gstvqlgvpv
      301 adgsvqsvky astgkdprla ffdtglteqn dlsyqsgdan ssfymsaqdv ytkgivpndr
      361 nrrtglrvaa mkkygifttd ysigytkttt nvsgpdffqg rgvywnvlnq qadvdlrkyq
      421 nltdkfsdvn gfynayypnp ywqtvysrqk ttkdalvgna sfkiapvkwf datykvsmsy
      481 gwqqykatva etdfspyavs dpfgtsnias qvkfkpgsva dasyfgdggt gysrlqgdlf
      541 ltfkhkigdf tgnlllgntv ytkyinvvtn gsnnllinnf ynlayrtgep lagtaqfrqn
      601 ligyfgdlni aykdwaflev tgrndkssll sqanrsffyp sakltvvltd aipalknkkt
      661 lsyakvrgsy skvgqvdinp yslqnvfast agapfgstpa lslssqlnnp nlkpelsyek
      721 evglelgfld nrvyfagtyy nthtknqtfp vaispasgys tsvqnlgeve nygwefelkg
      781 spvvkagdfs wdlganlsll qnkvlslqdg tnefqllynn gtasnsyaiv gkpfpyikgt
      841 dlvrdpqgrv vvnastglpt ltanvvplgn aapkailgit tsfkykfvtl savaeyrggy
      901 finnivgqal nftgtsavsa sagrqrfiyp nsviqtgant yvpntsisip dgntgfwtss
      961 ayynatstyv nsaafwklre valnfdlyrf iknqkvikgl qfglvgrnll lfrpksnpwt
     1021 dpeysidnsn avgttnenqt pptrlygasl tvkf
//
LOCUS       WP_091210540            1124 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091210540
VERSION     WP_091210540.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1124
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122943
     Region          31..1123
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqnllkisr lllvmivcmf tysslqaqtl tirgivlddn nqplpgvsvt ikdtkqgglt
       61 neggrftisa skgqtlvfht igfatqevvi gtevylsvnl ksdtkalsev vvtalgvkke
      121 fqklgysqsq vrgdalttar danplnslag kiaglsigan aefagaptvv lrgskdvlyv
      181 vdgepvnsdt ydynaddiet ytvlkgpnaa alygfrging aiiittkrgs kdkkgwqvdf
      241 nsttelekgf lvlpksqtey grgsnfayty gnvlydntqr lpewgprfdg vfqtqqydsp
      301 ydaatgirqk tpwlargakn fenfvqtgit ntnslsiaas gsnydmhisy ghtyqkgdfp
      361 ntklnidnfk iaagyditpk lrvegdlnln qlyspnipdv dyspqsyvym fkvygsadyd
      421 vnalkniyqg pqgvpglqqy aqeygrlnnp wfiadkwlkg rtkqtiygsl klsykitqdl
      481 nvslrealnt ydeqnteqvp aganlnqyls wytfgwygdy rqddrnlldn ntdltftynh
      541 kfgdwnisgl lggnarsfsy ksdwgttqvl alpgvynlnn sagkpyiynf dskmqvysgy
      601 ysfdfgykny fsinttnrvd hlstlpsgnn tffypsvais svvtdyiklp efisflkvrg
      661 sfadvkgglt sptigtsyna lnstalgtgw nskpvtgllg ygtelytpyn gptylnaspi
      721 atatfyngtp svtlsntisn dkikpfdvks yeagfdakfl gnrlglngty fttengpnif
      781 plgvatstgn tnqlvngvtt rkrgfevelm gsvlknpngl nwdvnvnyst yketiksiyn
      841 gvstlqqnnh nyvvgdrpda iygtkfvrdg ngnivntysv datgkvsggv pltspggisn
      901 qgllgyanpd fsfgitntft ykgfilsfqf dgriggkiyd rtyyqamngg tdletatgaf
      961 gaarlaewks tnegtvgatp syvgpgvhiv sgtpifvggq ianlkdltfa pntipvtvqs
     1021 yvssgiggnf deyymisrsy aklreaslgy slpasmlrgs fikkvtfsvv grnllyfaar
     1081 kdidldqfas gynasdrslv ggnggsdles ptarrygfni hltf
//
LOCUS       WP_091210615            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091210615
VERSION     WP_091210615.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117936
     Region          24..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllaswc lfmlfisvvh aqnktvtgrv tskddglplp gvsvrvvgtt vgtqtnadgk
       61 fslsvpssak slsfsfigft sttveitsap ldvkltssan klsevvitga ygtkqssrsa
      121 syaaqvvksd alntirqpnv nnalagkvag vqvrsqsaaa lgrntnirlr gatgfgsgnn
      181 plyvvdgtim pnaddlsndd idnisilngp aasaqfgsqg aygaivistk kgkkskgvgv
      241 elnlganfdk ayilpnyqnt ygggasadfi qyhwkdgdpe gwkaldgkyy pdytddsswg
      301 pkmvgqeyip wyawaagtky sfktakwtpq pdnakdffrt gvalnnsvaf tkaaddynir
      361 msynnqhttg ivpetwlnkn nftlnanfdl nkhltagasi nysgtqlhgq isdayasass
      421 gsfnswfhrd ldmgimkelq dlkspdgtyv swnhqnpnsy dpsnpgafya gnywynpylw
      481 qkqwqnlntr drlygniylq ykinndlsfk vtyrrnqtnt wnegkissei qasgtqtgqk
      541 atyatsnsys nrenyetlln ydkqikdfhl nvnagsdfyn wsykdnsatt nnglsvpdly
      601 tlansvdpis asngrtqeqy ravfakasan ykrivyvdat lrndwfstis tvnnansvls
      661 ksfggsfvfs ellpeykdwl sygkvrgswg qvplalgttt etfgayrnnt lygiaankwn
      721 gallqggptq fvdpalhgtt ttskevgldl gffndrltfg atywaaddkd iplglavnaa
      781 sgvssiltnv glikrrglei tasgtpiklp nfswtvstnf aqlldntvve isnkygvdrv
      841 qvagvwgtdm pylinqkgkw wgqiygngik rnsagipilt ssgayindpn vyfgsalpky
      901 tgglqnsftl fkdfvlsani dyqfggkfvs lsnrwgqysg ltantaalnd kgmsvrdpva
      961 dgggvkvtgv dannnpvtyy vdaksyyqgl tnnktydpyv ydltfiklre vaigynlpik
     1021 kwglgnvfqs arldltgrnl lliyakskdf dpseisateg etaqypgtrg igfnlkvtf
//
LOCUS       WP_091210990            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091210990
VERSION     WP_091210990.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110131
     Region          30..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfkqllkrf ilpllsvfvf cystyaqtvt lkgkvtdekg epiagasvki kntnvgsvtn
       61 agglynlnyt gqgtlivtai gftaqevklt gqaqvnialv ednkvlnevv vtalgikrdk
      121 riltyssqei kseslaqske pnlvnaiagk vagvqvtsss gtpgssariv irggssffgt
      181 neplmvidgv pvdnsetgnl ntgpgtnria didpsiiasm nvlkgaaata lygskgangv
      241 viittkngal nkkplitfss dfsfenpllp qiqskyslgt ngiyydgvtn ktstswgaem
      301 dtlkingqpa kvynqsdlff ktghtynntv niggggnnst ylvsysnfnq qgtvpttkfl
      361 rntffakysa qvlknlnttf qlnysnsqnd rlpegyales pvwtvftapv synlqpylna
      421 dgtqrlyrfs rnnpywvldn iknhssvnrf lptftadykp lpwltiterf gadvytemdr
      481 yhestqsvsn pngrlvdnnt tyrqynndll lsankqfgdf nvdvilgnnl istysentya
      541 ngvgltvpgl ynmasastvn ysesstlqrk igfylqsnie ykrflllslt grydgnsvls
      601 tdhnfypygs aagsfifsef fspelskvmn lgkvrvsygt vgndgsigay slltpynkat
      661 irnlafpynq qagflisdvl gnpnlkneri nefeagfeag ffnnrislea sfyskktidg
      721 iipnvaiaas tgyastgvns avmrnrgiei llnatpikgr dfnwdltlnf trnrnkvlsi
      781 ygdqqvlgng ftnivvgqpy gviygtryar naagklltdd tglpyaddtq givgninpnw
      841 lgginnnfry kqfnfsfffd ikrggdiqnn vdgygyfygt pkvtenrglr vvdgvnattg
      901 qpntvavngq ayyqrinsvl esviqdgsyv klrnvslgyt lkpswlsksp fksatfsvtg
      961 rnlwihaphf tggdpevssf gssngsqgiy sfstptsksv dfslrvtl
//
LOCUS       WP_091211003            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091211003
VERSION     WP_091211003.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113934
     Region          27..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkiykllla ivlpfiliqt vaaqsvkisg vvtaksdglp lpgvsvsvkg kttgaqtnvd
       61 gkfiinanvn dvlrvsyigf ttqeipvtqs sstlsvvlve apnslnevvi talniskdkk
      121 slgyavqglk skdiseaket nfvnaltgki agvqvtnsqg dmgssrivir getsisgnnq
      181 plfvvdgviv dnsqflgtng srdfanaisd lnsediesvs vlkgpnaaal ygsraaagvi
      241 lirtktgkga kglgvtinsn tsfsnvqvlp dyqnqygqgs ngkfsyvdgk gggvndgvde
      301 swgpaldgsl ipqfysngqa vpfvahpdnv kdffntgvtl nngiaiasss dksdfrlsyn
      361 nlhqtgivpn tsqgrnsfal nssyrinnkl tvntivdysk ddadnlpgay gkratstmlq
      421 ftwfgrqvdi nrlknykdan gntfnwnnsy ysnpywlaye ntvgqhknhl igsielnyki
      481 idglsanfrt gtdyyndrrk ikvaygtngt pfgsyeeday svnenntear lqytkklnnd
      541 fsldvlgggn iavrttennd qlapklavag lytlsnsrdp lvstnvygkl ktysyfgsaq
      601 vgfrnyafvn vtarndwsss lpsdnlsyfy psvngslils ealgiksdvl tyaklrggws
      661 kvgkatdpyq llnvftsstl fgsnpqqssp atdlndhlkp etttsaeagf elgffhdrvh
      721 ldvsgyntns tnqiltvqvs sstgygykvi nggrinnkgi evqlgltpik skgftwditt
      781 nyslnrskva aldadgrlqs vvlgtdrtvq vlaslgqpyg alygtaytrn asgqividan
      841 gtpvfnttkr ylgkftpnwl gsinnsftyk ginlsflvda rfggsiysnt nrtgtytgvl
      901 astlpgrgaa ngglsyyypg nntsaaavqv tgaapagvtv yndgmifkgv kadgspntti
      961 ipaqsyykgf tnideafvyd asyiklrevk lgyslpakwv nkigfqgatf svvgrnlwii
     1021 hknapnidpe tafnagngqg ledltlptvr nigfnvnlkf
//
LOCUS       WP_091211039            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091211039
VERSION     WP_091211039.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114864
     Region          23..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklflllsv llclgsalka qdrnitgsvv dekgaplpgv aiqvkgsntg titnadgkys
       61 ikatnlqsiv vgakflgyny qektlkigem nadfkmlpsq naldevvvvg ygtqkkvhlt
      121 gavaavdmkt iqdipttnla aalrgtnaav svtggiarpg qsgtitirnp vflaknggst
      181 tplyvidgvq rteadfnlld qsevenisil kdaaaaiygi lgangvivvt tkrgqaggpk
      241 vsfsssvgva daiqlpkmms gvqmatylnd ieqtrynhti tpegyingdl snkdlkyytp
      301 deleyfknnn qnfleqafkp avtsrnalsi tggndkvtyf aganyvnqns nfkgvntnrf
      361 gfrasvdakv akglklslsl sedlakskiy wyklssttes pdndflslnq appwqkyfid
      421 ghpvylgtsn ndnlnffavq nsnnytgnnn tvfnglanls yeipgisglt anvsynrnin
      481 nafnkqygst fyynqysgeg dnnhipggtv vsvkaikngd kvrltpslad nyqfnanlsy
      541 hkrfgaheit alalyeqyes ysegvaaead gvivggkdnq tfttgdqssn qatlvkeygr
      601 kavagrvnya yadkylvela mradantnfa pghqwgyfps asagwvvske nffksvsfvd
      661 mlkfrgsvgl lgsdntpsyl yavnyqfgtg nkggavfggn gdrglgalln iaipnanltw
      721 dhdlktnygl daaflnnrls isadyfwehr ydmlaslnts vpvtigaaps aenygiintf
      781 gyeisaswkd kigsnfsysf spffswsdnk yikydiaaaq vgtiqdltgk sgdpgtlgyk
      841 slgiirtqad adaiiaqraa aaggaqnvki fgytpapgmi nyvdkngdgi ikqndindqf
      901 ylghkasnhy nlglnfggay ktlslnvvmg mswggtqsie saaikqatan qnrpvfwadh
      961 wtptntnaky pdpyysddvs vtsdfwfvsp ftwnissanl sytlpagltk rlgmssiray
     1021 vvatnpinfv npfpdhyrdi sspfgvypnl rtvsfglnlg f
//
LOCUS       WP_091211160            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091211160
VERSION     WP_091211160.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121919
     Region          50..118
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          131..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknahrinp lrlnqflkvl lmfkficilv lvsslqafsk gygqtrinvn fqnvslkkal
       61 keiekksdyr flynddmllk ndmpaslntk dasleevmki vlsntnlnyt vsdnnlvilt
      121 ekgaamapga ingkvtdesd lpmpgvtvkv kgtnvsaqtd lqgrytlnip dsntsgvvlv
      181 fsfvgyasqe itvngsslin vqlkaasnsl nevivvgygt qkkenltgsv avvnlkeank
      241 rvtpdvaral qgqvagvqvn gsgvpgegvs irirgvssli nnnplyiidg vptmepfdfp
      301 ttdieslqvi kdasagaiyg frgangvvii ttkkgrngam kinyngyagf qknpktlsvt
      361 drvgyqkiad aaetnaglsl apgndpsssk fisnvntdwq ksgfrtgytq shdlglsggn
      421 enmsysvafd yfnqtgttvs gpsytrynls gniqgkkgiv sfgskfayte gdynnlayph
      481 lhgtgnqivd lvtaiptmpi ydpnrvggyg gvdqntqrai slniigvnnl lnstgqrnrm
      541 masawmevef iknlkyrlsa sydrndfknt yfdpiydlgw fypnttayys dargnyytal
      601 ventlsykfd iskhhvella gtayqkdknd nltgiaynlp qpylfafdnv snttdktvfg
      661 nsnerkfysp ifgrvnynyd drylltanyr rdgtsqlpey nrfgnfagvs vgwninkekf
      721 lhlpetisql klkagygtlg nvnalafypy qavvnanasy vfgntlasga tqtqvfdqtn
      781 kweqkqttni gldlslfhdq lsfsseyyin kikgillsvp ipvsvgaint plvnaasftn
      841 kgieftvtyr srdtgpfnyt isanastvkn kvtslgnggn piygayskta vggevgelya
      901 fktegifkda advaahatqt gaapgdvkfv dtnkdgiind adrvylgsai pklyygfnls
      961 anyknfdasv fiqgnygski angvyqalmt gqytnastde lnywtpnntn tnvprpiigd
     1021 pnannrnsdr fiqsgsyarl qtaqlgytlp agllnrthvi rslrvylsgq nlytitkykg
     1081 fdpdfindgt inrgfdygsf pnprtllvgl qlgl
//
LOCUS       WP_091212017            1195 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091212017
VERSION     WP_091212017.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1195)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1195)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1195)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1195
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1195
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132046
     Region          122..1192
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknllvllm lyafnlmcps sykalaqsrq sletalkkve nvygakfvye knlldnkvts
       61 yqvrdkgdvp iekvlkelly pqgflflyve knyytiikds rdktqlqdnt vqsvvnlkdg
      121 rrtvygrvvd ekgiplpgvs vipdgthagv stssdgtysv tfdpqiqnir fsfvgmatqi
      181 ipattdkinv tmaieanglk evqilstgye kipkdratgs fgyinakeie ktpsinlmer
      241 lqgkiagvkf dtrnntiqir gqnnygtsga qgplivvdgf pliseqsgdt qaltklgnnt
      301 tsvssvisri npsdiesitf lkdaaaasiw gakaangvvv ietkrgskka ttvnfgsavs
      361 vsapadlsql ntmnsaqyig leqelfnkgf vtdpaswstg yykfnpnqnt sdalewmfrv
      421 nrgtatasqr dsalaklagn nnyaqikkyl lqkaitqqyn islsgggdnt tyyvsanftn
      481 drpvyksnfs rsynitsnts tdffnkrvtv ttglnfnsty skanlaaata lgksiyglrp
      541 ydmlvdgngn ninryiqfrp nvidsltnkg ylpwtynaid elnysniitk enrvranagi
      601 kvkvfdwldv nalgqyqnni sdlsnedeln syntrtllnt atsslangnl vygiplggvl
      661 rstnysgydy sfrgllsahk iwdnihqlnv iagaeiretn sksygqtryg yddltgisqt
      721 vnpttyyqti ypyqsyigaa dniitrskkr ylsyysnagy tlldkytasa svrfedytml
      781 gvsakdrgkp lysgglkwnv krekfmepvg visdldlrlt lgtggtipst gynstvisin
      841 gtdyytgkpy asvsspqdsq lswettrqwn egidlglfnn rlnltvdvys kksfgilynm
      901 pynatygwst llrnagtlss hgvdvtiags pvnhkdwgwn snltfayntn kvtdsrltqs
      961 tsvsivssst ptvgyptdyl fvyrwagldn tgqsqiydkt gkvisstiss naagltsadl
     1021 kyagrksppy fggwsndfry qnftlnvmmn yyfgakflky svgnyptyvg tylgvigtqa
     1081 dlanrweqpg deaktnvpgl sginsnsitr yqysdalvrs adhirltqls laynipanll
     1141 mrtpfkslsa sfsarnlgii wrknkdgidp dyvttnsynn lppaknfvlg fnasf
//
LOCUS       WP_091212121            1093 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091212121
VERSION     WP_091212121.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1093
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121885
     Region          48..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkaifclmgl lclkfkrfip plvfsisliy cvfltenvvs qqgnaiysgi vidsvsrkpl
       61 agatitnpyn esrvftdglg rfsisaprrg gflvvtyigy nstkfsykqs gsdfliqltp
      121 vtlnvaevsv stgyqlisre ratgafahvd sallnrrvgs nvinrlegvv pgllfnrsti
      181 ssatggldls irghstlfan dqplvivdnf pydgdinnin pndvasisvl kdaaaasiwg
      241 vrsgngvivi ttkkgkynsa lladfnanit vgdkpnafyd rsfldskdfi dvekqlfnlg
      301 yydsqlsdsa hpvvspvvql ladqrdgkin qaavdkeidk figtdvrkdi erylyhksin
      361 qqyslnlrgg nerstyyfsa gydnqignlt gnnnsrltln aqnvfkllpg lemsvalnyi
      421 eahntnngig nltaggqygq iypyarladd sgkpmpivkd ynyswitdas aqqgylnwqy
      481 npldeihyad ntsvsretri ntslkytflk nlnaeiryqy etantsgkny fdkntyytrn
      541 iinefttvkg aaithivpvs gilqqsenal asqhfrgqln yhvnendrhe vtalvgaevn
      601 etvtnsnant vygydkelgt yqnvdfntyy plypsgfysq vpgtlgfskf tdrylsyfgn
      661 aaytfkrlyt isasgridrs nlfgvnanqk svplysiggv wnaaqegfys idflpllklr
      721 ttygyngnid knvvavttik rntsdyytpg lsnssianpa nadlrwekir minfgldfgf
      781 kdriltgsfd iffkkgidlf gdsplapstg ftmfrgntan tkghgfdlvl nsnnlaignf
      841 rwqstflisr avdkvtkynl nqtaigslsd gsvvlpitgk plfgiysykw aglthetgdp
      901 qgylnesist dytsiiastk ladlvyngps rptsfgslkn tffykqlsms fnlvykfgyy
      961 frrpsisysg lysgwfghsd ftkrwlkpgd esytdvpsmq lppvnddret fysyastlvd
     1021 kadhirlqdi slnysltrsv wknlpvrqld fygyinniai lwrankehld pdmysasayp
     1081 iprtyafgfk vgl
//
LOCUS       WP_091212222            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091212222
VERSION     WP_091212222.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114229
     Region          27..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrysailfsl iallsfchpa gaqqkkitvs gtvidakekk plpgvlvrsg kpsivlgqtd
       61 ikgnftvkad ddaeltfnfi gfksitrkvt gpvmnivmae evnalketvi igyskktkev
      121 stgssvvita kdiqdapvan vleliqgkva glniqnnngt pgmagsinir gisnvnvsgs
      181 gfltptsplf vvdgfpvddn snysygfdqa spglspisli ptediqsiei lkdaqatsly
      241 gsrgaygvil ittkrgnskv piikytanft laqppalrkv iggkgerlmr ideilqndtn
      301 yyhalntins tpflsdslna yynnstnwqa kyfrstfnqt hnveisggen kfnykvntgy
      361 fsqkgivent dftrynlnmn tlyqpndrfk lsaainnqla ynstgggnsl tqtgvassga
      421 sssllpapsl ftassgllnt lstqndnktv nitanldldv lifkglratn sfsfnyfsqg
      481 tekltpaaln gdfnqlynyf drkntlynrt glaydksfan khnfrlnvfg elnstnfrad
      541 viqqsgtpnd qilgplgydw skslggtlnn lsdlktasla aafsynykqi yvldlsyrmd
      601 gsstngpdag ysknpsvgvr wnfnkekfmq sfnwldyssl rfsygknivp tgsvydvygr
      661 yvaggnynqd ptvnldygvi pntgltpttt tqlnggfdag flngkfsvtm dayykqvdnm
      721 lrmkdianin afsqvstnem svvnygyelt ltarplptds klswqlsvna afnkdvmvhl
      781 pdnvsqllvv dpttgqnily rlgrnslsnv llntkgvyss nsavpvdplt glryrtgglv
      841 ytyfkqgdpa wtdvngdyvl dandyvavgn sqplvtggft ssmqygpfsl singsftair
      901 dvlnndlasr fqsfanptaq tglvpleayn ywktsgnnat ypnpydytra gkvspfrydq
      961 tlfqedgsyl kinqvtffyn fkkamikrwn issariyvta ynvhtfsnys ganpenvtdl
     1021 grdisggypt prsytlglqv qf
//
LOCUS       WP_091212447             945 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091212447
VERSION     WP_091212447.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..945
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104537
     Region          57..944
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkdyknfla wmlafcsfsa anaqtagtap adtikkassy kdfvdgglri dkswrntgav
       61 ftlsgedltr mtsgnllntl qgripgltvv tgsgepgydn ptfymrgvss wnlqgnqvli
      121 yldgfqvdmg aisglsayei esvtllkdaa alavyglegg sgvlsirtkk gavlnktqvf
      181 vngkygilsp idlpkvmday gyttnynnal tndglpikya npelykatnd pfhpnvnwyn
      241 ellkktsaiq dynfgfrggn ntakffvlmn ytnfeglykn advidkdfgt nakytklnlr
      301 anielqlnkn lvvtanisgi tedrntpsgf tadqlfnnim aipaaafpvk npngtwgnss
      361 vykfnpiqll qqngvyqsht rnlqtnfsfv qkldkltkgl dlkgevsfan qyvgiyqkqf
      421 svnsyeitgq daqgnaiygs tpvtpisqss sdgggahwnr ttvrmgfdyd rtfgkstftg
      481 miqarrqgyt hdgivyqvrt qgiagnvtyd ydkkyivdls gsysgsadfg pghrygwfpa
      541 vglgwiaske dflkdnstin flkvrasygt vgnineayrf lyqqfavgap gwitgtgnta
      601 hggltegpfa nldfawekkt tlnvgldftl wknlsgtldv ftekrtgile ipssgvpdyt
      661 gfnlqyantg evhnkgleas lkyeqndnkf kyyvggsiay arnkivkrse dpqpfnylyt
      721 qgypigqmkg lvytgfyqqs dfdangnlkp gvvassytnv kpgdlkfkdq dgngiindyd
      781 kvpmkysvlp eitlgfnlgf kyagfdfday lqgvlhrtvs llnsaytyth pfvfnnnise
      841 fsanswtpqn attatsprls tlanpnndqq sdfwmrngnf lklrsvelgy tlpqrgflrk
      901 ldavrvfvng tnlftwdkiq dleaerlsmg yplvkavtfg mkvkl
//
LOCUS       WP_091213537            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091213537
VERSION     WP_091213537.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115485
     Region          25..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrlllilc sfvfavtqlf aqnhtvtgtv takedglplp gvsvkikgtt tgtqttvdgk
       61 fslsvpnnav lsfsfigyat qdvpvgasan lkvvleasak glnevivtal gisrqqkslg
      121 yaaqqvkgdd ltvtkqsdln talagkiagv qvlggsgakf gtstirirgv nslsggnpiy
      181 vvngvvtdpn avnnddiesl svlkgpaata lygqrasega vvitlkkgsn kgigvslnqs
      241 ttfekvyqlp eyqneygggt sttwktytyd pangspasfa qfngvkyydy gvdeswgpkf
      301 dgtmyapwyf wdpsnpdfgk lkpfvaqpnn vrdfyrtgvt yntnaafska gddynfrvsy
      361 tnidrtgitp nsdqkrnnvg lngelkltkk ltvsanlnfs qinsnnvpqe gygtqtagsf
      421 sqwfhrdiei dklknyqrad gtytswniis pdniaphywd npyteayvnt nksnsnrvyg
      481 nitasyqftk dlslsliare dllnrddnsr vgsgtinvds ysqsqytyke nnyvanlays
      541 hnfkdlsvka glyaetrqdr ylytsgntng glatpdlyil tnsidaptaf synalsrvns
      601 yygytslgyk dflyldfnar ndisstlpvn nnsywyggls gsfvftelme kndwltfgkl
      661 rlsaakigsd tqpyqvytty nlsttpygsh piqtvpntlt nptlkptlst ayevgtelhf
      721 lkdrvkfdfn yytrtakdqi lplpvngtsg ystaivnage iknhgielsl ggtpikskdf
      781 twnvdfnvsf nrnkvisiyp ginslqvspd glggyglagg nqtagaksfg fvgspsfgvn
      841 gvvgssygqi igsgftrdak gniivdesgl pivnntvnlg smlpsytggf tnsfnyknfv
      901 lafsldfqkg gkfvsvtqqn lngsglgiat vglnakgnpk rdavsagggt lfpgvhedgt
      961 pnttyvstrl lyesalsqiw enytfdatyv klrevslgys fpkkmlgrlp fqsayfgitt
     1021 qnpwmiyskl kgvdpsqlqt sfyeggqlpn trnigfnlkv tf
//
LOCUS       WP_091214038             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091214038
VERSION     WP_091214038.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106218
     Region          28..981
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiyflrcn lmlflvclcn waiaqsgtia grvidetnqp ipgatvhvkg isqatvtdak
       61 glfkisaggs aaivvvsyvg ydplektina getvtlqlvp nqktlsevvv vgygttkkkd
      121 ltgsvstiga kdlnpgtvtn plqqmagkaa gvnivqvgse pgvaptvrir gitslqggnd
      181 plvvvdgiqg nmdllnqvpp teiasvdilk dasataiygs rgapgviiit tkksgtgkta
      241 vefnenasvd vipkklqvln aaqwtqeana lgvdvsanhg sntdwfdllt rngitqnhnl
      301 afggganefn yrasitaidq tgivansnyk nyiaritatq kalddkltlt mnvnnginea
      361 ayepngigna afssnlitqa diarpsdpvf ntdgnyfrda nvfqytnpya vnqtvrndvk
      421 tnnlfgslma nldiykglsa gwfgswrkvd gntgyylpsv stvqtaidnn gignisnwhn
      481 deklmdinls ykhdfgknhv datavyewqa qtyngsfvqg rgfvndlasy nalqlgdisk
      541 vlqgdissyk ndrrlisflg rlnysfanky lltasfrrdg stvfgannkw anfpsaslaw
      601 rvleedfmkn qhlfsnlklr igygitgnqq gigpqnsial vgqagtvffg gttipnyaat
      661 qnanpnlrwe tikqanagld fglfndvltg nvdvytartd nllfnytvpl egpflttnil
      721 anvgslqkrg velslnykvi htdkmtltla gngsylqskv lslggniegy diptnyvawg
      781 snaylvvgkp igtylilkhs gvnaqgvetv igqdasgnvd qgpqskyrye egqslpkyty
      841 aftptftfkn fdmsmvwrgs ggnkiynglr rnlsmlenlg kqnlltsaip tgihsspfgs
      901 dewlesgnfl rwenmsvgyr fnvtnvkfin alrvsvtgqn lalitkysgl dpevdasggs
      961 ssggdygiyp rtrtfslgln vilk
//
LOCUS       WP_091215811            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091215811
VERSION     WP_091215811.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120998
     Region          29..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkiyqrlra vitvllfcva psilfgqtki sgtvtddkhs plpgvsvkik eqnkgtvtdi
       61 dghysitata gqtlvysfvg yapvyvvvdn kttinvslig dskalnevvv talgvkketr
      121 rigystqsvn gadvtmardp npitgltgkv aglsvgpsae llgnpsvlir gnsvtlyvvd
      181 gfpintdtyn ispddietyt vlkgpsaaal ygsraqngai littkkgekn kkgltvdins
      241 stvmntgfla fprtqntfgp gentfytfvd gkggapggvd sdydvwgpyf agqlipqyds
      301 pvvngvrqgt pwvargkdnl knflktgyqt nnnislgsvg dtyvtrfsvs qqhqtsyips
      361 qyldiananf ygqftpskrw kfeanvdfnr qstdnfpdvq ygpnsiiyni avwtgadwni
      421 napdikaiwq pgkegvqsvf aeytryhnpy lltekwtrgh ykndvygyls gnfkindnln
      481 vtlrsqidty nilrtedlpy sahpygregn qgdyredrrn lfdnntelfv nynytiknfv
      541 nlsglvgsnl rsfnynsswt stdylnvpev yafsnsknai qstnfssaer vlsgyysida
      601 tfgkyatlss tgridkssaf qnvttyyyps lsaatvisdy vklpevisfl karasystvk
      661 adassatigp apfnaisvyg gstttsnpns nplflnplgy gstynspyng psyqlnsfyl
      721 tskpynsqpa asasdflyqn giktstrvny eegfdikflq nrlglsattf qyidgpqila
      781 nsistatgyt tlylnalktk ktgyefsleg tpiknlggfs wnvlvnvatf kdvyeelppn
      841 qdtyqtffkk gdrtdklygt afartpqgqi indaagkpla lpvpqylgne nakyswsfsn
      901 klryknfnmg fqfdgsvggv iidymhnktm rggsnietat galgdarykd wqnfgkagyn
      961 gtyvgegvtv sngaainydp atgkitnqga lqfapnkqta lvqdyvskyy nvdesnlmsk
     1021 tfsklrevtl gydfpkawld ksfikkasvs vygrnllyfy gdkrfkdvdl dqynyatsst
     1081 vlqsptvrsy gfnlnvsf
//
LOCUS       WP_091214455            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091214455
VERSION     WP_091214455.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115330
     Region          24..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkitlifv llitiltrsf aqditvkgiv kdsqglpipg atvknkstga vtvtdikggy
       61 sitangnatl vfsfvgsatq eqpikgrtti dvtltdankq leevvvigyg travkdvtga
      121 issvkaekle nehpasatdi irgnipgisv alntsakggg tgdlqirgka slsgnvqpvi
      181 vldgviypgq ladinpndid rvdvlrdpsa lavygaqsag gvvaittkkg kkggtqitln
      241 anfgiaqllq nqkyytgdgf lnwradgars sntsnpyyyy snpnklpdgv tlaqflngat
      301 gdpttiwlqr lglfpneian yqagkmtdws klifrngfrq dytgsfsgss etvkyyvsgn
      361 ytknqnliqg gqytdgrfrv nlegkaakfl tlgvnaqfas rdegaastpl sgqaidgtea
      421 dwtqiinssp ygdmynadgs lrridtddsg lnqrnpflgn rynqnvavqn tlfsvlfarl
      481 dlpfgikytv nyaptiesyr nfffrpvanp nelsggtair tqenryrynl dnilswnksf
      541 gihsfdatfl lnkekystwy tnasntqltp tdilgyhnig agtlpvessd drvynadaim
      601 grinytllgr yiltatvrrd gfsafglqhp revypsgaia wvfsdesfmk gdafkwldyg
      661 klrfsygang nrtstttadp sislavlggi kyptannsgt vtnnsgiyvs slqnaqlkwe
      721 rtvgpnigld ftilhnrlsg sidvydrktt dllvkrsild vqgynssgdl vngannsnpy
      781 tnigqvnnkg feisldgkim ksenfnwnas gtfflnrnki vhlygafpvt dangvttnve
      841 kddigngwfi ghdinavwdy kiqgvwktte adeaakygak pgdfklqdvn gdfkftnddk
      901 qflgsqnpsf swslrndfni fkhfdvsfll vssigqlkqy nqalnnpgsv gfarmnsyvl
      961 pywtpdnqid dyarlnsgss gttinvwrka sfvrlqtasi gytfspqlik rlgissakif
     1021 vnasnaavfs swplwdpqng gptprylsag fnvvf
//
LOCUS       WP_091216951            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091216951
VERSION     WP_091216951.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113985
     Region          73..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrylwlcfvv faaittnalt slakgnegkk skvkrpdpaf ynkphirrdt takdsllkds
       61 iniiirhtly nkladsvtkk pyelskfpaa slqqllkgqf aglyvqepsg epgsmqnmfi
      121 rgvpmpllsp rdvyqsqplv vldgiplvte hpfaydiqly dynrmgtatn pfagidmnni
      181 asvevlkdls atavygprav ngvivltskt pvaaksitfd syiglaqrph vttingkyen
      241 afrqrfydly ttngrysdde nypiylsdsl nnvysgksdw sdlyyrnavv yginfgisgg
      301 tdranfrfsl gdlknngiad gtvlnrysam fninmkplkw llfstmvnan rldrqrnkyl
      361 rdrfaqinyf pdlsaplppn keyyadylaq ykkgfdnnkt nivdgyakig ldlgrfkfvt
      421 tfnvdynegy rdvfyartll qgnsyasnyf gssqrimadn ratydltink vndfhfelgq
      481 stqwdiykys nayaykgvnd yikidlldsn pknpdgsdnp nylnptafpr eltfrfldki
      541 khnlvsfyak tdysfkekyf lsatvradgs snaqptsrwf yspvisaawn ikkevlnnst
      601 iindlilkas agrigrlnaf dnyaqgpqyt asvgytgnlt vpgynafgvl trpystgwig
      661 ygipwsysnq lnigtdagfl nnrlhlsvdw ylkqeknlli gipafaeygy kqsiesgmav
      721 nntgidvsvs anivqntrfg wtsslnlnhn inklkalprg lnqiivddkl lkvgspidqy
      781 wllindgiyk seseipvvng qplkyngial hagdprwrdi ngdnvidnnd kvlkghslpk
      841 isggydnnfr ygnwnlninl yfnlgrdlih qemanrfdfi nregnsdvns vkeitfwekr
      901 gdyskyplyn pwstvipyrv dqdlflenas flklrtvsig ydltkamrlk kikltrfyvy
      961 atannvftit pytgqdpelv nydgydtgyg lpiprtytlg vkmel
//
LOCUS       WP_091217659             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus siccatus].
ACCESSION   WP_091217659
VERSION     WP_091217659.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus siccatus
  ORGANISM  Geodermatophilus siccatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Geodermatophilus siccatus"
                     /db_xref="taxon:1137991"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52170
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpretr pgetrvaatp ttvrqltalg ydvvveagag aaasfpddgy reagarvgth
       61 vhawgadvvl hvakptpeev grlrdgavlv stlapaldpd llsdlaarpi talamdavpr
      121 israqsldvl ssmaniagyr avieaahafg rsftgqvtaa gkvppatvlv vgagvaglaa
      181 igaasslgav vratdvrpev aeqiasmgge yvgvpadeeq agggtgyasv tsedydrraa
      241 amyaeqvrev divittalip grpaprlite emvaamapgs vvvdmaaaqg gnvagsvpde
      301 vvvtpngvti igytdlpgrl pgqasqlfgt nlvnlvkllt pgkdgrlvld lddvvqrsmt
      361 vvrdgellwp pppvqvsaap aaapaprpap papapraprs partaavvgv aalvlflata
      421 fspnqlignl tvfalavvvg fyvignvhha lhtplmsvtn aisgiivvga llqightsal
      481 vtvlatvavl vasinvfggf avtrrmlgmf trs
//
LOCUS       WP_091220333            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091220333
VERSION     WP_091220333.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114554
     Region          23..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklllicsf lillisegya qsrtitgtvl dnsskpidgv tivvvetqks tlsdasgkfs
       61 iavkngqsvr fsyvgakpiv ititadtktl dvvfkdaenk lnevvvtgyt serkkdltga
      121 vavvdlapvk nnssgntmqa lqgrvaglyi ekdgsangat srilirgant lgnnnplyii
      181 dgipttrpev fqnlspsnia svqvlkdass esiygsrasn gviivttkng gntdgkvqfq
      241 fnnstsiqse kslrfkmlna vdrgkalwqa svndgqdpaa gygeiynfdw nnnfnnpvln
      301 svtpkpyvgg dqntpvgdtd wqsvlyktaf vynndftasv gnknssiqin fgnikntglv
      361 rftkygrttg sinaitkafd skvtfgvnik itnsnetltt tdlggattpf lavtlaptip
      421 vyqkdgvtya gesgagysdr nnplhmqdla kwnntnklnt fgnvfleiqp iknlffrsny
      481 gadnsdylsk vitptfsega lnrttnslff dqnhylsttl sntlrysydl nnkhhfkilv
      541 gteyvktftd fqttlkqgya iqtedyftld agtgntivtg rstgnqlfsq fgrfdynyag
      601 kylvsatvrr dgssrfgann qygifpsasl gwkidqenfm kngslfselk lragigrvgn
      661 qeigdlsrya lyntrygttq nqltpgfweq ymnvgtaysl sgantgslps gfvqtqaenp
      721 alkwettdel ntgldfailn gkisgsfdyf trkttgilit ppvasalgeg qsktvngask
      781 tnkgwefsvt yhgqhagdfn ynvtlnfshf rdkitdlpen vrpaypgnid ntiighsqfd
      841 ifgyktaglf qsqaevdaap tqigagpgri ryvdinhdgk idandqtwig ttlpaleyga
      901 ridltykkfd lsifgsgvag rkgfdvytly nnlmhsrenv gpgvfdgwtp qhtnttvpal
      961 tlkdnnnegr tsdyfivnts yfklrniqig ytilpkavft rlrvfamaen iftvksskyl
     1021 spdperidln pipiprifsf gvnasf
//
LOCUS       WP_091220609             525 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091220609
VERSION     WP_091220609.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..525
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=58115
     Region          <5..523
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msgdytgrnt gdaighatis nsevnhwlie nifsynrsfg khtidftgly ssqkdytftn
       61 tlnantfind ltnfynvgsa qiqqtassyt qstllsqmvr inysyagkyl ltatarrdgf
      121 sgfsaahkyg tfpsvalawn vneesflkgi ssisqlklra sygisgnqgv ssyntlttlg
      181 stqyiygstt tvglvpsaig ngnlkwestk glnigldfsi lrdritgsid aydtktynll
      241 lsrkipyitg yttildnigk tankgielsi tsrnirgtnf swetnvnfsa nrnklvqlyg
      301 dnkdditnnl flgkqlyavy dykligiwqk gddftvdpsa kpgdlkfadl ngdgkintad
      361 rtylgsrlpk yiagmtntfr yknftlsafi qtfqgalkpn piydyrdqag rinlpagigy
      421 wtaanqsntr pslsysnsrq ytypvsgsyt rikdvtlsyn fpkqmleglk ianlqvyasg
      481 rniatfskwl gwdpetdfys yaanqgssfy plvatavlgi nitlq
//
LOCUS       WP_091220602            1144 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091220602
VERSION     WP_091220602.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1144
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126840
     Region          135..1140
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkltflynav cairgvkckf llvlklttil llvgalhlsa asysqtvtis gkskslesvf
       61 kdikrqtgyl ffysekvnlk gktvdadfhd tqlvdvlnac lkdfdlsfti vsktiviqnk
      121 ipeprpapve pmskipvsgr vldsvskttl pgvnialkgg rgvigqtndk gefnvqadag
      181 qtlifsfmgy ksaevkvvag qsivvkllpd innikdivvt gyqvikkdny tgnaitvsga
      241 dlkrnnpqnv iksiasfdps fkvldnnlig sdpnklpkin vrgttaipsi sddildrnnl
      301 ssnynlpafi ldgfevslqk vvdldinrie svtllkdgaa tavygsraan gvmvittkap
      361 vagklqlsyn yeltfngpdl sdyhvlnakq kvayeqlvgl ydtqtstsgd tkqdeldaql
      421 ftrlknvasg vntywlsqpl rnayqqkhsv yaqggdqsfr ygidlryqtq pgvmkgsdnt
      481 rysggvnfty npsskliirn dltitqvnqv nspygdfsty vnanpyfpir dstgrlvqel
      541 anwrvntgrm gtdqyiteni fnplyeasls sfnkaaytei lesfsadyki tkglrlkalm
      601 svnktnsttd ayvsplssvf ynvaldklnt rgtydygtna slnldgnvti nynkqlgdhy
      661 fnlvlganil asksdiksfs aqgfsndrft nigfartyke nsapygdvtk trtagaffsg
      721 nyafqnkyll dasvrvdgss afgadrryap fgslgigwni hkenflqgsn visqlrlkgs
      781 iatlgsisfp ayqsrsiysy dtqhwystgi gatilgygns nlewqktrtt dvgmdiglfk
      841 dkvvlspryy ykltkglitd inlapstgfn tykdnlgdms nkgyelylva qvfhttdwni
      901 nvtgnlahnv nkivkisdal kafnnnidnf qtntdnnafs tpltryvegk slntiyavks
      961 lgidpengke ilvkkngtlt ynwdvkdiqd vgnttpkaeg ffgstvsykr fmmsfsfhyr
     1021 fggqafnqtl idrvenadpr ynvdsrvleq rwkqpgdhtf fkniadltdt yvssrfvqkd
     1081 nlielqslyf sydfkpqaik rlglqnlrla atandifras tiqaerginy pfarsltfsl
     1141 lgsf
//
LOCUS       WP_091220653            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091220653
VERSION     WP_091220653.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116082
     Region          29..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklilyfil cciccslldp vcaqttgatv qgyvkdsegk avasatvsek gipangtitn
       61 meghfelklk gnsntivisl igykrleaki ggknvytlqv deqslndvvv vgyqsqnrre
      121 vtaavssikg kdianipqas fdqmlqgrlp gvsvlsstge lgaktnivir gstnvdfgna
      181 nggnsgplyi idgvifdvna igtaygnnnp lalinpadie sidvlkdasa aaiygarggn
      241 gviivktkqa krgkpqvsis gfagvstspn likvttgaae ralklklleg qlgynniqqg
      301 vipkaltdsl npafnndvdw qgllirkttv vnsqsasvag yagttsyrls vnhyneqgvl
      361 ngyglekitp hlnltiqpik kmsiavdllm ssqkqshgvg gagaylftaw nfpssflqls
      421 peqeavysgk qhyyddnrtf tivgsihltd tlaknltfns tygstnytdk ydyfspqiln
      481 gtlntaystv ssspswsfen flqynkdfgk hrfifavgas lysyennyny ssaaginisg
      541 intvqtvpag tnlntstsys rkttesyygr lnydyagkyl ftasfrrdat siyspqyrwg
      601 tfpaaaagwi isdesffnpi kkvvnffklr asygvdgkdp gqwyskyqtl stdassyvgt
      661 ngtitpngyl ggypstyngt tivspfpyyn nyssfgvkss nsvrwekdrq vdiggdmelf
      721 nsrvnitvdw yrkdakdvff ynvpaqatsg yqyysgnyvd irneglefat ninvlgpksa
      781 fkwnfnfnvs inknlvtklp nnnrdflfgd swfyktltlg eplfsyrvfh tngvyatnad
      841 vptdpttgkk etyygvplqa gdpkyvdvng dynitnddky iagnpnpkyt ggfgstfnyk
      901 ritlsffasf vagrkilnga lsdalngtrn lggwgtvagv atytntlnqf wqvpgdqtty
      961 arlvypngsq tdpwnigtdy firdgsfikl knvtlgydlp drwlkslglk rvnvymmgdn
     1021 laiwkkakdi adpelvdstt gssnviypta akytlglnid l
//
LOCUS       WP_091222699             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091222699
VERSION     WP_091222699.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108811
     Region          37..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meknyrsilr lwqrsgksic lfmlmlvass aafaqqrtir gtvtdesnlp lpgvvvtvks
       61 tgkatstsan giyqvvvsgs ddvikftflg slpkevtigd kkvvnvtmvt dtkqlkdvvv
      121 igygtasrkd vtgaitsvka edfnagvltt paellqgkva glnitksgdp nkqpatilrg
      181 pstlregaaq qpfyvidgvp gasidllapa diesidvlkd asstaiygsr aangviivtt
      241 rrakagqtrl tysayaaven vsknidvltg delrkyltdn gvpklsaadd dgsntnwqkl
      301 aertgysqnh nlsyggagtn seygasvnym knngilnnts lertiykgyi nqrffndrlk
      361 lgitltnsat knndifqsqv lsgilfylpt vspynadgty kenysrtgsg plnplslinn
      421 nftrtennkt lingfasldi lkglkftvsg stqkeqnnvn tystsqsgiy vnaggvavrs
      481 aytntsnvve ayfnydrvfg khslkllggy syqqdrnndg fgvqtqgfsn daltynylal
      541 snptqlsqiv fnpnyistlr fvsfyargqy efsdkyllqa slredgssaf ginqrhgyfp
      601 aasagwklin edfiksipvi sdlklragyg vsgnslgfda ftarliygvp pgggkflsng
      661 nivnpigpvr ndnpdlkwes tattnigldf glfnnrltgs vdyyikktsd liytypvstt
      721 lyfypfytan vgkiknsgie vvlnavpvks qaftwrtsfn vshnknvvqs lsnsqfglnf
      781 iqtaqlggkg qsgnysqiiq pgyaigtfdl whylgknang vstyekadgs ttatqplttd
      841 qfikydaqpk liygwsnsff ykgfdlnflv rgvygnkiln atlaslnnpa dsklqniprf
      901 tlgesfkdin aylisdrfle sgsylrldna tlgytikphi qaikslrfya sgnnifiitk
      961 yrgvdpevni ggltpgidnr dfypktrtfs lgitaqf
//
LOCUS       WP_091221287            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gossypiicola].
ACCESSION   WP_091221287
VERSION     WP_091221287.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gossypiicola
  ORGANISM  Mucilaginibacter gossypiicola
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Mucilaginibacter gossypiicola"
                     /db_xref="taxon:551995"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120348
     Region          30..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqfylnlkr wvvlllplfi sanlfaqtnv tgvvrddtgp lpgvtvtvvg ttngtqtnan
       61 gaysikvakg tvlkfssvgy tpkevtvgdn svinvtlaag kgelnevvvt sfgikrqeks
      121 lgystasita kqlteagntn fasalygkap gvkittapgg sssavnvqir ginslnyntq
      181 plyvvdgvii rnnsetgagg snnggywsdq rirgngildi npsdiesltv lkgasataly
      241 gsdamsgaiv ittkkgsksr glgvdfnyvg taeqvaftpn fqnvygpgyd ratnlaggft
      301 edgwladans psgyrprfss yaqfgpkmeg qkirwwdgei rdytpqpnny kdlfqtgyss
      361 naniaisnqt dkvnyrlsat rldytgiqrg qkqqknsfnl ntsvklsnki sadivasyvn
      421 tlthnrpyql grvlanfggf lnrsekadvl ldnyqtsegy kyvtlanaar npaeafkynm
      481 sgadimdffw tqlknsedet enrlitsatl nwdvlknvkf rgrigsdytg rntdsqqyne
      541 yptafngsss tgyygvskaq ysitygdlll tyspkltkdl smsvsggyts rsetyrdqss
      601 gtngglvten ffslsnsygv qntsatrgal ksqaffgvln fnyknylfle gtarnesast
      661 lptknntyfy psvnagfvfs daykmpefis ygklrasygv vgnrapryva nvlynqsslq
      721 tqygsvtqlt yasaygnlql kpemkyeqey gletrflrdr lgfdftyysn qvkdvimaln
      781 vapstgaanl lanaatlhsn gfefalngkp itgkfnwdvr lnfainrskt nnlapgfdkl
      841 tfyygdqsal avvaeanqli gnilvypvak dangnkivns dglytidksk yvnvgniqpk
      901 ivggiantfn ykgfsldvlv dyrfggkmvs nplkygtaag myestlqyrd aahgglayyi
      961 dgnggkhlgt apnggktynd gvilpgvnen geknttivda asyylntydw gensvnenav
     1021 fknnyvklre vvlgyklpas vnkalhvnnl rfslvgrnll yvyrtlknld peapigdtwy
     1081 rqgvdegssp atrsfgfsln anf
//
LOCUS       WP_091239378             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aquimonas
            voraii].
ACCESSION   WP_091239378
VERSION     WP_091239378.1
KEYWORDS    RefSeq.
SOURCE      Aquimonas voraii
  ORGANISM  Aquimonas voraii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Aquimonas.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Aquimonas voraii"
                     /db_xref="taxon:265719"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39393
     Region          4..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maatvcavve rvpgerrval tpeiakklra agvavvmekg agssaafpds aytdvefvds
       61 aaaalaradv llkvqppead eiaalkegai vigylqphtg dervrslrdr rltsfamell
      121 prttraqamd vlssqagmag ykavliaaqt sgkffpmltt aagtirpskv livgagvagl
      181 qaiatarrlg aqvegfdvrp etreqieslg akfldlgvsa agsggyarel tpeeraeqqr
      241 klaehlkgvd vivttaavpg rpapkiitas mvegmkagsv ivdlaaetgg nceltkaget
      301 vrtangvdvv gpthlasmgc ihasemyarn lynflvlsik egaisadwnd elvaqtclth
      361 ageikhgpsk qriegvaa
//
LOCUS       WP_091249903             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. ok909].
ACCESSION   WP_091249903
VERSION     WP_091249903.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. ok909
  ORGANISM  Arthrobacter sp. ok909
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Arthrobacter sp. ok909"
                     /db_xref="taxon:1761746"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38232
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqvgvgreqr agerrvaatp etvqqltalg ltlvvesgag teagfadaaf keagatvise
       61 lplaaldvll hvrplapdta arlrpgaitv glaspaselp tvralaaagi tsfalellpr
      121 israqsmdal tsqslvtgyr avleaavryp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandiraas adevasmggt finldldaaa egtggyaral gedraqrqrs
      241 llaphvaatd ilittaaipg raapvlvttd mvagmragsv vvdlaaesgg nvegviagqd
      301 iqvpveggsv tlvglqdaas ampsdasrlf arnvsnflal mtdggtvapd fdddvvagtc
      361 lthggtvrha ataaalgeda
//
LOCUS       WP_091254694             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            omnivorum].
ACCESSION   WP_091254694
VERSION     WP_091254694.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium omnivorum
  ORGANISM  Flavobacterium omnivorum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Flavobacterium omnivorum"
                     /db_xref="taxon:178355"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109790
     Region          43..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiislnkgw lalyypiifg fylcclpvma rtplpksiiq qytitgtvrd gqgvlpsvti
       61 svagkstati tdyqgkysit ataadilvfs fvgyttlnip iagrtvvsvh lqedatqlqe
      121 vkinagyysv kesertgsig ritakniekq pvtnvlatmq griagvsivq dsgspggafs
      181 ikirgtnslr adgnqplyii dgvpysseti gsiatsgtap tltsplnsin pqdiesievl
      241 kdadataiyg srgangvvli ttkkgkaget rfsinssssf gtvgetpklm ntkqylamrq
      301 lafdndgvst ypsyaydvng twsperntdw qkkliggtak ihnlqasvsg gsrrtqylls
      361 gnyrtettvf pgdfkytkgs ahfsmnhtse derfkltlsg nytsqnnsqp aidltavsrt
      421 lapnapelyd engnlnweng twnnplagld sefesrindl vantvfsyrf lpnlefktsf
      481 gftdlhnnes rtqpstmynp syglgsefsa lssnftnrns wivepqlnyn ttirkgkfav
      541 llgstlqnqr terlfqngfg fasnrlihdl asasiktvdl sdvtiykyqa lfarlnynwd
      601 tryilnitgr rdgssrfgpg kqfatfgavg gawlfsneaf lkdntvlsfg klrssygitg
      661 ndqigdyqfl dtyvssgnny qgtiglqpvr lfnpefgwes nkkfevalet gfledriflt
      721 sayylnrssn qlvgiplpgt tgysslyanl datvensgle ftlrtinfsr ehfewttnfn
      781 isinrnklis fpglesstya ntyvvgqpin imklyhyiam npttgiyqfe dvngdgtiss
      841 iadrhtlanl spryfgglen qfqykgvqln flfqfvkqea fgalpgvpgt gvnqlasvsd
      901 saaqqpytag sngaiinayy ryglsdgavq dasyirlkni sltydlpfkv gdrlrcqlyw
      961 qgqnlltftn ytngdpefkf ggylpplkvn avgvkltf
//
LOCUS       WP_091256086             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. ok909].
ACCESSION   WP_091256086
VERSION     WP_091256086.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. ok909
  ORGANISM  Arthrobacter sp. ok909
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Arthrobacter sp. ok909"
                     /db_xref="taxon:1761746"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53881
     Region          4..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mthigivael gnesrvaatp vtvkqllelg yevvvekgag esssfrddmy veagalivga
       61 deawgsevvl rinpptedei rrladgatli gmlspglrpe lvealatrpi talaldavpr
      121 israqsmdvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksiggt ylkveveeem kssdgyakat seaynaraae
      241 iyseqaadvd iiittalipg rpaprlltae dvaamksgsv ivdmaagqgg nvegsvager
      301 vvtdngvvil gytdlparlp aqasqlygtn mvnllklltk dkdgqlnidf ddvvqrsvtv
      361 vrdgektwpp ppvqvsaapa qtetkraqer aadkavkktg lgparkaglf aagiavlfgi
      421 navapaplpq hftvlmlsiv vgfyvigkvh halhtplmsv tnaisgiivv gallqvtsdn
      481 vvmqvlaava vllasinifg gfavtrrmla mfsagkars
//
LOCUS       WP_091256186            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            omnivorum].
ACCESSION   WP_091256186
VERSION     WP_091256186.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium omnivorum
  ORGANISM  Flavobacterium omnivorum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Flavobacterium omnivorum"
                     /db_xref="taxon:178355"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114211
     Region          63..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkksvyrsr kpfiyplifg iflnsisptl ahnpfpsnnk ekerpkikfc ivvplwqykq
       61 qnqisgtitd gtsplpgvti sikgkrnntv ssdfkgqytl tatatdtlmv sfigfktaiv
      121 pinsrktvnv qlqqdlttlk evrvnagyys vkesertgni aritakdiet qpvtnvlatm
      181 qgrmagvnit qttgvpgggf dikirgqnsl raeanaplyl idgvpyaadp ighnqtatsf
      241 ptvtsplnsi npssiesiei lkdadataiy gsrgangvvl ittkkgkpgk tsfrvqassg
      301 agtvtqfmkl mntsqylemr kqaflndglt dynpwdydin gtwdqnrntd wqkellgnta
      361 qfndiqgtls ggseqtqfll sanyhnessv fkgpfaykkg ganinmnhqs ennkfkvsfs
      421 gaytlqhndq pafdfsyear slppnapaly kpdgslnwen gtwenplrnl nakfesktkd
      481 liantllsye llpglvlkss mgytdlstie triapstiyn paynvtsdrs alfnnttsrs
      541 swiiepqinw ekesaigkir vlvgstfqqq ttnmlvqgan gfssnsliyn laaakyinvl
      601 vheetlykyq aifgrfnydw qgryivnlta rrdgssrfgp gnqfanfgai gaawlfsken
      661 flednswwsf gkirasigtt gndqigdyqf fntytttgis yngtiglqps rlfnpnfgwe
      721 tnnkleaave lgflqdrifa taswyqnrss nqlvgmpltg ttgftvlqsn ldatventgl
      781 emtiqtanfn nhnfswttsl nltlsknkll rfpglesspy nqqyrigepl niallykykg
      841 inpqtgvyef edtnndgvis fpedrqtaad lnpkffgglq nqlryknwkl dflfqfvkqk
      901 nrsypmgaag mmsnqrttai nswlqpgdqt nyqiytagnn ydaliadyyy sesdasvida
      961 sfirlknial sfdvplklre tqfkiiaqaq nlltftkfne gdpeftsygf lpplkvitag
     1021 vqltf
//
LOCUS       WP_091257570            1148 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            omnivorum].
ACCESSION   WP_091257570
VERSION     WP_091257570.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium omnivorum
  ORGANISM  Flavobacterium omnivorum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1148)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1148)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1148)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1148
                     /organism="Flavobacterium omnivorum"
                     /db_xref="taxon:178355"
     Protein         1..1148
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126887
     Region          121..1147
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnfknqflip lkltkyiyll sclflfsgvn aasfisgeei enlsldvrev kiievfdmie
       61 kktkctflfd ekissstqrl tlvvnketld vilnkitrkt gfkfhkinni isvtkpaltq
      121 qvingkvsdv nglslpgatv lekgttnstt tdfdgnfnli isnalailsv syigydtkei
      181 slkndgfqqi tlienlnils evvvtalgik rqekqlgfsq qtisgdnlaq tapnnwssgl
      241 kgkvaglnfv ssgsgplnsq qitlrgsnsl npngnnaliv vdgvpmnski tssgsssaym
      301 gkdspvdfgn gisdlnmddi esvtvlkgpg atalygsraa ngaliittks gktskglgit
      361 ynsgvtfdvi qrwpdyqyey gqgtgksfdk nknpyysygs sadgsntgst ssawgpkfeg
      421 qyyfqydpkt emqgtertlw qpyknnikdf wrtgitinnn itlqggdkng smrmsvghsk
      481 newimpntgf eritasvnad ykisdrikia svinynnrss dnlpstgynn gsiayftifq
      541 npnadlnwyk piwekgktqi qqlqpfssyi dnpylianea tnslasnqiv gnlnatiqlt
      601 pnldlllrta lntyhqdreq krpysinryv kgffraqdvf mqevnsdfll nyknklsdhf
      661 slsvsaggna msykyqrmda eveglvvpnv yklsngvsnp ivsvndsykk vnslygilsl
      721 sfkdqvfldl tgrndwsstl pvqnnsffyp slntsfiisd ifhfpksfqy lkyrlslaqv
      781 gndtdpyrts kyydqsafas savapstlfn atfkpeitts fetgfegrlf knrinfdatv
      841 yqsttknqii avpldittgy ssgimnsgev rnrgmeltlt gkiidftkfk wsstltwskn
      901 wnrvmelaeg iqgqqtigsa gsasliakvg gtttalygyg fvrspdgqiv ydnaglpayp
      961 deiqyigdan anwkaglyns fkfgnlslnv mldgqlggiv ysqthhklte mgkimstmkg
     1021 reegviigeg vvlnpdntys pnakealtpd wysryyrran vesnsfdasf vklrevslqy
     1081 kfssywlkns gitsldfaif grdlavvsdf pvfdpetaal ngdtllpgie igqmpspasy
     1141 gfnlkvnf
//
LOCUS       WP_091257641            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            omnivorum].
ACCESSION   WP_091257641
VERSION     WP_091257641.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium omnivorum
  ORGANISM  Flavobacterium omnivorum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Flavobacterium omnivorum"
                     /db_xref="taxon:178355"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117454
     Region          25..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv llvalvaqit faqertvsgi vsdnaglplp gvsvlvkgtq tgtqtdfdgk
       61 fsirttpsqv lvfsyigmkt qeilaassnl nvklkddame legvvvtalg ikrekkalgy
      121 atqqvsgeev snvksqnfvn slsgkvagln iktsgnfggs tqvvvrgnss itgnnqalfv
      181 vdgvpidngn snlgsqqagg ggydygnaas dinpddiesi nvlkgaaata lygsraskgv
      241 vmivtkkgkk rkglgvtvss smtmgnadke tlpryqnkyg agygpfygpn edayfneadi
      301 ngdgipdltt pftedasyga afdpslliyq wnslypqltd tyqkatpwva gknnpnsvwg
      361 tsstavnsvs ldggtdsstf rlgftnllse gnlpnsnlrr ntitfsgsqd lsdkltvsts
      421 lnfvkadgkg rngtgyssgn vmqqfrqwnq mnvdfgeqkd ayfatgdnis wnpnsatnlr
      481 piysdnpywt fyenyqndtr sryfgnvald hkindwlsvm grfsfdtfge iqeerinvgs
      541 advskytrrn rnvseynyda mlnfnkdlte klnlegnigf nlrnntinsi saetngglnl
      601 rglyslsnsv npinapieya ssslvdgeyi raslgydgfa ylegsfrsdr sstlpkknnr
      661 fnyysvsgsl ifselinapw lsfgkvrany aevgsdtnpy nvfntfgigt pfngtgiasn
      721 pgaqanlnll perqnsyelg lemsflkkrv gfdisyynnq ninqitpipl ststgysqal
      781 lnagtienkg ievqlnatpf ktadfkwdln lnwsqnkslv vellngienl qiaslqggis
      841 inatpgqpyg tirgsdfiya angqpivnqt gsatrigsyq rtstsnsvig dinadwkagl
      901 nnsftyknvn lsflidmqkg gdvfsldtwy gyatgmydfs agtnelgnpv rdavvgtpgn
      961 ygansggvil pgvapdgtpn tvranadtya npwgyarapn klhvydagyi klreasltyi
     1021 fsgktldrlp ftnasfsiig rnlwiidknt pyadpeagls sgnvqgyqsg aypsireigv
     1081 slklqf
//
LOCUS       WP_091258970            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            omnivorum].
ACCESSION   WP_091258970
VERSION     WP_091258970.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium omnivorum
  ORGANISM  Flavobacterium omnivorum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Flavobacterium omnivorum"
                     /db_xref="taxon:178355"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111781
     Region          45..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiisfykgs stfwcliiig fslshtpila nkllrqiqsl pqqsqisgti tdgtypltgv
       61 titvkgqqkt vvsdfdgkft iivspsdili ftymgfktvt mpvdgrsiin irmqedattl
      121 qevkinagyy svkekertgs iakitskdie kqpvtnvlaa mqgrmagvni tqttgvpggg
      181 faiqirgqns lrstgndply iidgipysse stgssstasl lggltsplns lnpdtiesve
      241 vlkdadatai ygsrgsngvv littkkgkig kthftanysk gtgsvtrfmd lmnteqylam
      301 rreayandgi ttyprsaydl ngawdqnryt dwqeeltggt aeytdlntsv sggnsatqfl
      361 msgnfskqtt vfpgdfrykk gnihvtanhe sdnkkfrisf sggytvqdnn qpyldltres
      421 rllapnapsl ydvagnlnwq nntftnplrh lngtykalty dllantvlsy nlfpnleiks
      481 afgftdlrhd esstapstiy npslgigsdn svlflnttnr qswivepqln wnklygkaki
      541 svlaggtfqn rtgsqlvhqa lgfpsnsliy nlaaasnvti tqndeseyry qaffgrtnls
      601 wddryilnlt grrdgssrfg pgkqfttfga vgaawlftne kvlkenrils fgklrasygt
      661 tgndqigdyq fldtytttgv aydgvvgllp srlynlafgw etnkkleval etgflkdrif
      721 ftagwysnrs snqlvgiplp gttgftsvqa nldatvenrg leltlrtvnf qnndftwttn
      781 lnfsssknkl vsfpgleast yrnqfvigqp lnivkvyhft kvdpatgiyq fedvngdgei
      841 netddkqtvk dlnpkffggl qnqlkykqfq fdflfqfvrq enynanttfn mpgtrsnqla
      901 sttnhwqnag dvsphqmysa tngvvrtayf nytesdasis dasyirlkni aftydvpqkw
      961 lnkvrcrlsl tgqnlltftn ykgadpefki ydylpplkvv taglqftf
//
LOCUS       WP_091262257             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gillisia sp.
            Hel1_33_143].
ACCESSION   WP_091262257
VERSION     WP_091262257.1
KEYWORDS    RefSeq.
SOURCE      Gillisia sp. Hel1_33_143
  ORGANISM  Gillisia sp. Hel1_33_143
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Gillisia sp. Hel1_33_143"
                     /db_xref="taxon:1336796"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110275
     Region          46..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnysrlkw valiiiagml lflaqaamag nkplvtnsfp qqeiigkvtn megvpligvt
       61 vmvkgtntgt itnlegifql nvpqnntlvf sfigyktlel pfngekevnv slaediatlg
      121 evqinagyyn ttrrestgni sritaeeiel qpvvsplqal qgrmagvevs sggvnpggat
      181 tirirginsl rsegnyplyi idgvpinstp ietnsiignt gldplntlnv sniesievlk
      241 dadataiygs rgangvilit tktgkqretg leariytgvs tmpnrlnlln teqyleirrt
      301 afendgvepn efnaydlvlf dqnrytdwqd flfggtaett nanlafsggn entsfriggs
      361 yftqgtvytg nynyhkitgd islnhrskdn kfninlslny gvdvnrlvgn vslnsatfll
      421 ppnapsifnn dgslnwedwg eanldnplkg yfnatntesn nlisnvglsy elfkglklkt
      481 tlgyskydsn elwklpsrsy npadaspnss fhlssnrnsw ivepqlvyes qlmklnvaal
      541 igatlqenkq dqqnfqatgy aseslignia aaekiinatn tqtdykysal fsrlginwdk
      601 kyyinltgrr dgssrfgpnn rfanfgavgv awifseepwv kkslpflsfg klrgsygttg
      661 ndqigdygyl dayeatvgpg glyptalanp dyswevnkkl eagielglld dkirlglsry
      721 rnrssnqlvg ytlpsttgfn svqanlratv qnsgwelean svnvetknfr wqtalnisfp
      781 knellsypni eqstyantyr vghplnisll yeytgldpet glytirdvne dgsfdfqdri
      841 iiqdqsrkfy gginnnlsyk gftlqflwef vkqngrlvlf dagapfnild lddsslngqn
      901 eyqtisqsfq anraysyvle ttfpnqdasf lrlktlslgy nlpkgfiqsv glkqakifmq
      961 aqnlltltpf kgldpefpts tigfgnlrti sgglqinl
//
LOCUS       WP_091259113            1016 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            omnivorum].
ACCESSION   WP_091259113
VERSION     WP_091259113.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium omnivorum
  ORGANISM  Flavobacterium omnivorum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Flavobacterium omnivorum"
                     /db_xref="taxon:178355"
     Protein         1..1016
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111649
     Region          25..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwifs lllalsmqfa faqertitgv vsdasgpvpg vnvlikgtns gvqtnfdgay
       61 sikaktgdvl vfsfvgmtqs sktvgaasti nvsmqddakm laevvvqgyr tvtkkmavvs
      121 datvssktie nrpnanaint lqgqlagvni tastgqpgak stvvirgvgt itgnsdplyv
      181 idgfpsnsdn frsinpndie stsvlkdaaa iaeygnrgsn gviviktkra kfgeskttfr
      241 assqygvgel qkpkysyans kqllqieknf gsglgatltd aqiaaydint dwvdyffnqs
      301 nttshtiave nssqnvssyt slgyfeqqgi lattglkrft lrnnvngrst nekfkyqvnt
      361 afgfsknnea tslgdgainr nyvlgafisa pyvspsiytg pqsaldyynn tpgllatpim
      421 lvdklqqykn qtdevrvdva tdfsyditkd ltvrsrlngq lldtrffqse fpnsfnallf
      481 qaagqtftgf edinsrrewy fnnlwqinyg ktlgdhtfnv nanmeynhsr lytnnirqrg
      541 liagifvpnt gagyagdtgt ndfyvptisa rnvrndlisy fgsfdydfkg kygivgsvrt
      601 dgssrfidek qwgtfysvgg rwnideeafm ddvsfidvlk lrgsygtvgn qrvvggdvfq
      661 ginpprfadi yglvnnayng gtgygisfgy pelqweittq wnagldfemf kgrlrgafdy
      721 ydrsttklfl enpvtstsgt svltqntdvt vtnkglelnl aydiirnpek eialtirang
      781 sqntnlvsni ttnatgqifl pgglfvseng gsinepfvyh ylgvnpvngn llfedaagnp
      841 teapvqadkr ragvnnlpky qggfgfdfsi kgfyastlft faydvarfdy dldnlysvgn
      901 igqftvtddm lnawtatntn tdvpalnagn lgltdesdrf lkdasyirmr nvqvgynvpq
      961 kflkntfmta vsfslqgenl ltfskwkgfd vessrtndvy qyptprlytf gvdvkf
//
LOCUS       WP_091263384             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gillisia sp.
            Hel1_33_143].
ACCESSION   WP_091263384
VERSION     WP_091263384.1
KEYWORDS    RefSeq.
SOURCE      Gillisia sp. Hel1_33_143
  ORGANISM  Gillisia sp. Hel1_33_143
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Gillisia sp. Hel1_33_143"
                     /db_xref="taxon:1336796"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107869
     Region          27..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqiqlrcvr lifllfvfps ilmaqetlng kiidestgep vpfvnviqkg tsngttsdfn
       61 gvfslevnal ptilvfsyig fetqeinvts nspmainfaq saaaldevvv tglatsvkrt
      121 nsanavasis aaelvgtttp ptldgalygk fpgaivsans gapggglsvk lrgatsiqgn
      181 tqplyivdgv yvdnssiaag lnavsgaaag gsasnqdnps nriadinped ianieilkga
      241 saaaiygsra aagvviittk rgvagetsyr fsqsvgwtev inllgvrdyn edrvresfgd
      301 aavqdfidar dgnrlvdyee elfgnkgllt itnfstsggg ektkffagvt hnsedgivan
      361 tgyekislrl nvdhrandfv klalstnyih sssdrgyfnn dntgtsvgva ltgtvpwlql
      421 fpdengnypd nplgssnilq trdlvtnnek inrlimggsa nidlyrndks nlelilrggl
      481 dfygfntlaf fpkelqfqkp snggqngvsv qgstqnknyn lsaflvhnyf tdnninfrtq
      541 agltreyfdr ngylitatdl vasetnvdqa tntgvdqnrl kqedagffaq eevnfqdkvi
      601 atigvrgdks snngdankln yypkasvaln lnefgfwnqn skfnqlklra aygeagnfpp
      661 igalftsyns ftnvgqggvt lkgisligtr gnpdlkserq kefetgvdfg ffndrltgsl
      721 tyyiktvddl ilnaskepss gfttefvnag slenkgveia lnaaifrged fnwdfgmnff
      781 knkseitrld vpafnaggfg atlgtfriee gksatqivgi gpdpdanglq kfgdaepdfq
      841 msfnnsisyk gfdfnflwqw kkggdninlt alltdlsgts hdydeidldp egqigngpyr
      901 vsqlgssaav fiedsgylrl revglyytip saitdsflng tfdrikfgfs gnnlinifdy
      961 nsydpevsnf ggggifnave vtpfpsskry mfnvafnf
//
LOCUS       WP_091263597            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gillisia sp.
            Hel1_33_143].
ACCESSION   WP_091263597
VERSION     WP_091263597.1
KEYWORDS    RefSeq.
SOURCE      Gillisia sp. Hel1_33_143
  ORGANISM  Gillisia sp. Hel1_33_143
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Gillisia sp. Hel1_33_143"
                     /db_xref="taxon:1336796"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117447
     Region          21..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiifmclaf claatgfaqt kitgkvsdas gngiafanvv lkntntgttt nddgfyslel
       61 pnlngtlevf tlgyqtvsiq ingqnninvt lnesatglne vvitalglkr etkelgyavq
      121 siqqkeisev kavnfldnls gklagvsisq gatgvgstsk itirgeasfs nnnplfivdg
      181 tpinnntvfa ntseaaagfq evdfgngame vnpddiasvs vlkgasaaal ygtrasngvi
      241 iietkngska kgmgisints lfidtafqlp efqneygqgn sgkfefkdgl gggvndlity
      301 swgprldqgt lipqydspvv lpdgtivrgg dtslysdlpi tptpfnshpd nlkdfyetgv
      361 ttinnvsvss gfekgdyrls ftdlrsesii pgvnldrqtv aaklnfkplq gmsinstiny
      421 vnsgsdnrpa ngygsenlny slvawgprsl niqnlkdywq pgledvqqis ynytyfdnpy
      481 fmlyentnsf nrdrvfgnls ikqeitdhls lavrtgmdys senrqfkraf ssnrfkngay
      541 gehevffrei ntdfllnynk vfgaisadis lggnrldqna sttqsqtttl aqpgvfklnn
      601 aaspievfqy esqkrinsly giakfgykdf lfvdvtgrnd wssalatpys vantsffyps
      661 vsgsfilsnv telpqffsfa qlraswaqvg ndtdpyqttg afvsqtpyms qptfsdqnii
      721 snpnlkpert tsyevgadir ffkdrlnfdl tyynaltedq ilslpigiss gytqkvvnag
      781 kvrsqgieii agitpvrnsn fswnstlnfs knvskveelp qeagrltlay nriydnpdqt
      841 vwlqveeggk igdlygtgyl knengdfilt eagryiadnn lqklgnynpd fmlgfnnqfn
      901 yknwdlsfll dwrqggilvs rtlalgavgg qleetsyrpe agiiadgvvn tgtsenpiyv
      961 pnttavsaes yyrqyydrnh eennvydasy lklrqfavgy tfnlnegalg fmkdgatinl
     1021 slvgrnlfaf seiphfdpeq lavqgngfvs gvedmsyatt rsfgfkagin f
//
LOCUS       WP_091263742            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gillisia sp.
            Hel1_33_143].
ACCESSION   WP_091263742
VERSION     WP_091263742.1
KEYWORDS    RefSeq.
SOURCE      Gillisia sp. Hel1_33_143
  ORGANISM  Gillisia sp. Hel1_33_143
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Gillisia sp. Hel1_33_143"
                     /db_xref="taxon:1336796"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119308
     Region          27..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfskilt lllafvvqvt faqqqpitgt vvdesgvpip gvniivkgtt ngvqsdfdgn
       61 ysiqasrgdv lvfsfiglkk aeypvgdsat vdvtleadsa qldevvvtal gikrekkslg
      121 yatqevsgde vsdnpsqnfv nslsgkvagl nvkssgtmgg stnvvirgss sltgdnqalf
      181 vidgtpvsni ntndatqrgg gggydygnaa sdinpndias invlkgaaat alygaraang
      241 vviietkkgk kgkgigvsvq ssltvsnadm etlpeyqkqy gagygpyyds edgyfnlydv
      301 dgdgildest pftedasfga afdpnrniyq wnsiypqldt yqqatpwvag andpnsiwqt
      361 gftaissval dggtdkssfr isgthlnqeg nlpnsnikrn tlkfsgshdf tdkfsaqtni
      421 tftktngkgr ygtgysslni mqqfrqwfqt nvdwqeqrra yeatgenitw npnspsdlsp
      481 iysdnpywtf yenyqtdtrt ryfgnvnlsy efndvfsllg rfsfdtydel qeerinvgsa
      541 diakyerynn raaeynydli lninkdited lnldgnigfn lrrndrnsir astngglnap
      601 gfyalsnsas pmnppleyen trmldgiyar ggvgylntyy legtirrdrs stlpiednnn
      661 vfyypsvsts iilsniidge wlnfaklran yaevgndtdp ynvfntytvy apfdgagvas
      721 nngslknpal kpertnsyef gleadffnrr vgfdvsyynn qtedqitpvp vstatgftsk
      781 llnagtienk gfevslnlnp irtenfnwnm tinwaknest vleltdgidn lqlaspqggi
      841 sinavpgqpy gtirgsdfvy dndgnklina ngyyvktpns nyiigdfqpd wtggiqntla
      901 yknlslgfli diqkggdifs ldswygratg iyassvgdnn lgnpvrdavv rnedgtyaan
      961 sggvlldgvq gqvtfnpdgs yqvtntspnt vradastyan pygyarapsa ehvydagfvk
     1021 lreanvtytf gdkildstpf tsgsialigr nlwiidknip ysdpeaglss gnvqgyqsga
     1081 yptmreigas vklnf
//
LOCUS       WP_091290916            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. fv08].
ACCESSION   WP_091290916
VERSION     WP_091290916.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. fv08
  ORGANISM  Flavobacterium sp. fv08
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Flavobacterium sp. fv08"
                     /db_xref="taxon:1761784"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110231
     Region          42..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiislnrap fafilwllly sahvqahrse agssslyyqt svsgivtdgk nplpgvtvii
       61 kgtsvstvtd fdgryaisap kgatlvfsyi gfvseertvt gnvldvslre esttlkeivv
      121 nagyysvkdk ertgsisrit skdiekqpvt nvlatmqgrm agvdiiqdgg tpggafqiki
      181 rgqnslrsga neplyiidgv pyssssigss dtstataspt splnsinpad iesievlkda
      241 dataiygsrg angvvlittk kgkkgkssvs lssstsfgsv trmiklmdts qylemrrqay
      301 andgispypd taydingtwd qnrytdwqke llggtarinn ftgsvsggse stqymlsgsy
      361 rnettvlpgd frynkasvrf ttnhrseddk falsftagyt nqdnlqaasd ltrtarylap
      421 napalydgng ylnwengtfe nplaalesef raktndlvsn avlsyrllpd lelksnfgyt
      481 tlsndetrtl pstiynpsyg igsessilsv snnkriswii epqlrwshvf ghlavdalag
      541 gtaqqqldnr llqmgigfss nsliynlasa adkyvfisde ikyryqayfa rlnlnwdqky
      601 ilnltarrdg ssrfgpdnrf aafgavgaaw ifssekfvge dsflsfgklr asygtsgndq
      661 igdyqfldty tssgtdyggv vglnptrlyn pdfgwetnrk feaaleagfl kdrifitasy
      721 ynnrssnqlv gvplpgttgf ssisanldat ventgfeftl rtenfrtkdf dwstsfnisa
      781 aqnrlvefpn legstyagry sigrslniak lyafqgvdpq tglyqfrdyn gdgiisadkd
      841 reiiadltpr ffgglqnqlr yknwnldflf qfvaqdnydy isnaagglav nqrndmtvaw
      901 qvpgdsrpfq qntsgsngea vqaysiysqs datvvdgsyv rlknialsyd lpatalkdik
      961 criflqgqnm vtftsykggd pefryqgflp plkvytmgvq lnf
//
LOCUS       WP_091299968             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis xylanica].
ACCESSION   WP_091299968
VERSION     WP_091299968.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis xylanica
  ORGANISM  Amycolatopsis xylanica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Amycolatopsis xylanica"
                     /db_xref="taxon:589385"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37898
     Region          7..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(21,76,95,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(50,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maeteqltvg vvkesrsger rvslvpklie rltkrglriv vesgagegay ladsvfeeag
       61 avigdawgad ivlkvappta devaklktgt lligflnprs dpdgitalek agvrafavea
      121 iprisraqam dalssqsgva gyravllaae klprffpmlt taagtvppak vlvlgagvag
      181 lqalatakrl gaqttgydvr pevgeqvksl gakflelgie asgeggyare lteeeraeqq
      241 rrltdaitkf dvvittalvp grkaptlvta eavkgmpaga vvvdlagesg gnceltkpge
      301 dvveydvtit splnlpaemp ahaselyarn vtellelivd kegklaldfs deivagacva
      361 gkgae
//
LOCUS       WP_091301477             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Gemmobacter aquatilis].
ACCESSION   WP_091301477
VERSION     WP_091301477.1
KEYWORDS    RefSeq.
SOURCE      Gemmobacter aquatilis
  ORGANISM  Gemmobacter aquatilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Gemmobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Gemmobacter aquatilis"
                     /db_xref="taxon:933059"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55133
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreif egenrvamtp dsalqlvklg hvcvvetgag akagfsdaay akagvevlas
       61 aqavfeaadv vvkvrgpeps evemlrpgqt lisffwpaqn pdlleaarak gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtsvslg aivmafdvrp evaeqiesmg asfvylefda selpdgaatg gyaapstpaf
      241 qakqlakfre lapdvdivit talipgrpap klwtedmvam mkpgsvivdl aaerggncdl
      301 tvpdqkivte ngvtivgytd fpsrmaaqas tlyatnirhm ltdltpkkdg vifhnmeddv
      361 irgatvakda aitypppppk vaaiaaakpk ekakeltpee rraqetaafk aqtrnqvgml
      421 viggglilla glfapasfms hfivfvlsvy vgvqviwnvs hslhtplmav tnaissiiil
      481 galmqigsgs flvivlaals vfmaginifg gfmvtrrmla mfqks
//
LOCUS       WP_091307029             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis tolypomycina].
ACCESSION   WP_091307029
VERSION     WP_091307029.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis tolypomycina
  ORGANISM  Amycolatopsis tolypomycina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Amycolatopsis tolypomycina"
                     /db_xref="taxon:208445"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38413
     Region          10..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(24,79,98,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(53,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdseqsqql tvgvvaesrp gerrvamvpk lvgrlaqrgl rvvvepgags gahlsddayt
       61 qagaelgdaw gapivvkvnp pspeevakls rgavlvgfld prgnpeglak leeaglrafa
      121 meavprisra qamdalssqa siggyravll aaqklprffp mlttaagtvp pakvlvlgag
      181 vaglqalata krlgaqttgy dvrpevgeqv kslgaqfldl gieavgeggy areltveere
      241 eqqrrlteai tkfdvvitta lvpgrkaptl vtadavkgmp agsvvvdlag etggnceltk
      301 pgedvvehdv tissplnlpa empshasely arnvtellel lvtkegelkl dfedeivaga
      361 cvagregsas
//
LOCUS       WP_091309424            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            terrigena].
ACCESSION   WP_091309424
VERSION     WP_091309424.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium terrigena
  ORGANISM  Flavobacterium terrigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Flavobacterium terrigena"
                     /db_xref="taxon:402734"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114991
     Region          25..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaftmqfs faqqktvtgt vksdganlpg atvsiagtqq gtqtdengkf
       61 sikasegdvl eisflgkdtk tvtvgasnvv nvvlatssts ievvqivgam gikrkpdavt
      121 nqqqtvtnke ltqaaqpnai ialtgkvsgl qinttsngvp agtrivlrga rtitgnnqal
      181 vvidnaissa ailgqlapse ienmnvlkga qggalygaqg vngviivttk kgsksdklsv
      241 sinssvdfet vsfvpdrqtk ygqgwiydpt fnasghvpwe ngawgpafdd payagqlvet
      301 glpqadgnfq mlewkgdkdn ikkffrtgti fqngisvnag gadsyagvsf srqntsfmvq
      361 ddelkrnnfn ikfgkklgkf radgnvsyin qrtsttssel yddlmqiasn ipvrnfnnaq
      421 iqhgwsvyid npywtiknnr ndsasdfvng nislgyelnk ninvtyngni qlrsteaqsh
      481 vngfedyyyd imggsyvdyg ghgitssfyg nqsrqrnfyg dlmfnfdyel tdnigmkani
      541 gnniqdsyfk vitqggtnld vdgwyhinnv lnpdpaysla ntetrtrdfa lfsnfdfnyk
      601 dylflnvtar eerrstiakw ffypsvgmsf iptkafdalk dnkvlnfakl sanytkvgna
      661 savaayatde igvfptgfpf gslssyisnq rqvnkninpe iattfevsaa lgffndritl
      721 dgslyrtntk nlitfattss atgmsafqdn tgrlhtdgfe idlgltpvrt esfkwnikas
      781 ystyktiidk vtddsksvtl lsnanvsiva eegeefplik gttyerdpng nivvnpatgt
      841 plktglvnig kstpdyilgl tnsfeykglr lavvadyrtg hsfysetkst lgfaghlees
      901 aefdryesfv ipgsvyesap gvytanttpv gtgngsngga lglypgvvdy yggtsyrsge
      961 aflidatslk irelslsytl pkkmlknsgi nsftfgvnar npfifladgk flkaknggen
     1021 qhfadpeasi sstsnaqgfa nagqypssrt iggsinitf
//
LOCUS       WP_091324771             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus ruber].
ACCESSION   WP_091324771
VERSION     WP_091324771.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus ruber
  ORGANISM  Geodermatophilus ruber
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Geodermatophilus ruber"
                     /db_xref="taxon:504800"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53402
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvprear pgetrvaatp vtvrqliglg ydvlvqsgag sassfpdeaf aqagarvgta
       61 aeawsadvvl hvskptpgev aqlrdgalli ssltpaldpe lvdtlaarpi talamdavpr
      121 israqsldvl ssmaniagyr avveaahafg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvavraaetq vssdgyarem sddynlraae
      241 lyaeqardvd ivittalipg rsaprlitee mvasmrpgsv ivdmaaaqgg nvagsvpdek
      301 vttphgvtii gytdlpgrlp aqasqlfatn lvnlvklltp gkdgqivldl ddvvqrsmtv
      361 vrdgetlwpp ppvqvsatpa aaqaspppap arekppaspa rtfavvgiga vllflvtafs
      421 pdqlienftv falaivvgfy vighvhhalh tplmsvtnai sgiivvgall qlghtstlvg
      481 vlafvavlva sinvfggfav trrmlgmftt trptrtps
//
LOCUS       WP_091325953             402 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. cf158].
ACCESSION   WP_091325953
VERSION     WP_091325953.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. cf158
  ORGANISM  Arthrobacter sp. cf158
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Arthrobacter sp. cf158"
                     /db_xref="taxon:1761744"
     Protein         1..402
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40811
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkagiareal dgerrvaatp etvkqlaglg ltvevesgag laaghsdddy rqagaslvqs
       61 ldlgmldvyc hvrpmepsta galrpgsvtv glgspsselp tvralaaggi tsfalelvpr
      121 israqsmdal tsqalvagyr cvleaamrlp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandirpas adevasmggt fikldletae asggyarels adrgalqral
      241 ltphvaqadv littaavpgr rapllvsrem vqgmrpgsvv vdlaaesggn vegsipgqdi
      301 piptgdgqgv vtlvgikdpa sampadasrl yaknvanllt lmtrdgvvsp dfddevvagt
      361 clthngevrh aptaealaal agdtalgvap sgrpqpgpeg vr
//
LOCUS       WP_091331873             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Allochromatium warmingii].
ACCESSION   WP_091331873
VERSION     WP_091331873.1
KEYWORDS    RefSeq.
SOURCE      Allochromatium warmingii
  ORGANISM  Allochromatium warmingii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Allochromatium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Allochromatium warmingii"
                     /db_xref="taxon:61595"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37994
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipletr pgetrvastp evvkklvsqg ftvivesgag lragypdady aaagaslsdr
       61 asayavdlll kirrpdesev aamqagglyi gllescgedv ivaamlakkm rvlglermpr
      121 ssraqsmdvl ssqsnlagyr avleaaaryg rffpmmmtsa gsakparvvv lgagvaglqa
      181 iatarrlgad vyaydvrpet reqilslgak pidldlgesg agaggyarel sddakarqqa
      241 aladelakah viittalipc rpapvlvtee vvkrlrpgsv ivdlaaasgg ncpltvaddi
      301 verhgvtlvg ltnfpalipa dasafyarnl lnlieimier sdagpqlkdl sadditaaml
      361 vpaaa
//
LOCUS       WP_091345561             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Micromonospora rhizosphaerae].
ACCESSION   WP_091345561
VERSION     WP_091345561.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora rhizosphaerae
  ORGANISM  Micromonospora rhizosphaerae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Micromonospora rhizosphaerae"
                     /db_xref="taxon:568872"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52813
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpregr pgetrvaatp atvrqltglg ygvvvesgag lassfldesy vgsgarigst
       61 seawsadvvl hvakptaeev arlrrgallv slltpaldse lidtlaaqsv talamdavpr
      121 israqsldvl ssmaniagyr avveaahafg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaasrlgai vraadvraev aeqvrslgge yvavpdaeqq vstdgyarem sddyhrraae
      241 lyaeqardvd iiittalipg rtaprlitee mvasmrpgsv ivdmaadqgg nvagsvpnqv
      301 vttangvlii gytdlpgrlp aqasqlfgtn vvnlmklltp gkdgqavlal ddvvqrsmtv
      361 vrngeklwpp pqvqvsaapa aapvarpatp apaekpaasp artfavvglg avllflvtaf
      421 spgrlienlt vfalaivvgf yvighvhhal htplmsvtna isgiivvgal lqmghastlv
      481 tvlafvailv asinvfggfa vtrrmlrmft rg
//
LOCUS       WP_091368701             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinokineospora alba].
ACCESSION   WP_091368701
VERSION     WP_091368701.1
KEYWORDS    RefSeq.
SOURCE      Actinokineospora alba
  ORGANISM  Actinokineospora alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Actinokineospora.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Actinokineospora alba"
                     /db_xref="taxon:504798"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51738
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvlkear pgetrvaatp atvaqlrklg yevvvepgag vassftdday veqgavigtp
       61 laadivfgvn apsteqldgl apgatlisll spglnpdlve dlakrpital smdavprisr
      121 aqsldvlssm aniagyravv eaahvfgrff tgqvtaagkv ppakvlvaga gvaglaaiga
      181 agslgaivra tdprpevadq vkslggeyla veapdvevsa tgyakemsdd ynaraaklya
      241 aqcedvdiii ttalipgrpa ptlitaemva smksgsvivd maaanggnve gvvageatvt
      301 dngvtiigyt dlagrlpaqa sqlygtnlvn lmklmtpgkd gelvldwddv vqrsmtvvks
      361 gelawppppv qvsaapaaaa paapvkaahv kqpapasrrf vvvgiaaall fvlaalspqa
      421 lqghltvfal aivigyyvig hvhhalhtpl msvtnaisgi ivvgallqig qgdtaitvls
      481 availfasin vfggfavtrr mlamfsrs
//
LOCUS       WP_091368897            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091368897
VERSION     WP_091368897.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113851
     Region          46..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilpiill lpcvalgang ltkvnsmann rittvqvrhl gdnkaftikg fvrdasgqpl
       61 agvtvtikgt stgtqtdikg afslsadpgq vlvfsyigyi rkevtvttns ltveldedsk
      121 qlsevvvtal gikkerkalg ysvsevkgse lttarevnfa nslegkvagv nvstisggpa
      181 ssvninirga asvtgfnqpl yvingipmnn idntqivgls mngggeysns pdqgdgigni
      241 npddietisi lkgaaasaly garakfgvvl ittktgsskg tvefnsnyqa dnvinptdyq
      301 yeygngaqgv kpttptaafn agnsswgakl dgsnvmqfdg varpyvaqkn nfdefyrtgs
      361 tftntvafgk aydlgafrfs asdlhneapt pnsgydrrtf nfggnfspik rlmvdahvnf
      421 tndaatnrpi lgdgagnsay qllflptsvn vnnlnpgskg tvtsqdiqng ytgaalgnel
      481 lfannnyatn pwfaaqqfvn nssrnriigs asvrytfdng lfaqvriged yyterytniv
      541 pngtgyyaqa nqnlgetfdn vgefntdfli gkdfkihdft itpnvggnie kqriesttes
      601 gvgfvipyvy tisntksksi ayaddksdin slygtlalsy ksliyiegsa rsdwfstias
      661 sespnnklsi lypsvsgsfv ftelwkptwl dfgkiragwa nvggttqtpy qtllnyglsp
      721 vqlngmplgi itntatpnsd lkpsdasele igtelhtlns rlnfdvtwyn klskdeiita
      781 pasitsgyqg avlnigkirn kgwevlvtgv pvkmkdftwt ssvnfaynan tvvalaagqs
      841 slpvaysrta vgfttdvvgm aadqvqafdy krdasgnivv dpttgipvqg alknygsayg
      901 pwsggfsndf kyknfdlsfl idtklggkif agdeyyayyn glskatlpgr etgfgpgdkt
      961 taetyyttla nnvsgqfvqn dsyikfrqit lgynfpasmf nnkiqginls lvgrnlfyim
     1021 kkttdidpes sygtlsqglq lgdqlptrtf glslnvkf
//
LOCUS       WP_091368979            1007 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091368979
VERSION     WP_091368979.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1007
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109230
     Region          29..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikpllkki iplclgimal clngfsqsiq lkgtvvdsag msipgasvkv kgtslgtvtd
       61 vdgkfainye gkaelvvssi gftprlipln grttlnivll searglnevv vtalgikrek
      121 rlltyatqei kgaeimeakq pnvlnalegk lagvqitsst gspgasvnvv irgaisisgn
      181 nqalivldgv pidnsetgtv asgasgagss risdidpnti esvnvlkgaa attlygsaga
      241 rgvilittkn gskgkkalvt lsqdysfdna llpkrqtaya qgtngifyng ddaaqkists
      301 wgpamdtlki ngvaaksydp ystyfktght sntalsvegg tdkssyfvsy syldqtgtep
      361 nsdfkrnalf tkfsnaitnd lnltfqlgyt nsnqdrlpeg asngplfvlf sepvswnpyp
      421 yvnadgsqrl yrnsrnnplw aaenesnhyv vnrftpvmtl nftptkwlti teragadiyg
      481 eqdkywenps aaigtlgeii dqnnnfrqfn ndlivnatkq fgkfninvla gnnilstynq
      541 tyyelgsgln tlgyynigaa stitasenhs ierkigfyaq anieydkfls lnltgrydgs
      601 svlstakdfy pygsvasgfi fsellspels riisygklrv syatvgndnv gpyvlstpyk
      661 qaeintiqfp fqgqsgflis snygnpylqn erlneaetgl emkflnnrlg fdfsyydrkt
      721 tdgliaavgi apstgysttt vnsaslsnkg ielllqgtpv kgekfqwdvn fnfsrnrskv
      781 lslypgtdql griivgqpyd vfygtryarn skgqlligdd glpeedanqg vvgnpnpnwt
      841 agltnslryk sftfsfafdm kqggdiendv dlygnyygts yatenrapkv vdgvnattgk
      901 pntvsvsaqt yyqyinsiye ssiqdgtyik lrnvslsydl nkdllkktpf ktvslgvtan
      961 nlwiysphft gadpevssyg tgngvwgiya fstptsrsfi fnikasf
//
LOCUS       WP_091369019            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091369019
VERSION     WP_091369019.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117272
     Region          30..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskillflml ccifqfslnp ayaqntavrs gqvkdsngkp lagatvsekg ivnngvitde
       61 agnfritlkg nsntiiisci sykrqeikig ttpeiifmqs ddralndvvv vgyqsqkrrd
      121 vtaavsslkg sviadipess fdnmlqgrla gvsvlstsge lgakpnivir gstnidwgnl
      181 hggnsgplyv idgivydvna igtsytnnng vnnatndpls linpndiesi dvlkdasaaa
      241 iygarggngv iivktksakr gkpqvtlsay tgittapnfi nvttgaaera lklkllesql
      301 pynsieqgli paaltdslns afnndvdwqg llvrssaivn sqdvsiagfs gttsyrlsfn
      361 hyneqgiing yslqklsphi tlninpikgl nittdlmmss qtsnhgvggs naflftsigq
      421 lpssllqlsp tqtsvysgkt hyydndkvfa ingsvqvtdt lahnltfhst fgannytddy
      481 gyyvpqaing tlntayendn rspawsfenf vqydkrikkh hfsvvggtsl ysneqyssss
      541 saagisisgi ytvqtvpagi nlnastsyar kttesyyarv nydfddkylf masvrrdass
      601 iyspeyrwgt fpafsagwia sdehffepik kvvsffkira sygidgkdpg twyakyqsly
      661 ndasylygtn gtvnqnatlg gipstyngtt vdspfpygnn ffntgvkass tvrwerdpqt
      721 dvgadielfd nrvsftvdwy qkdadniffs dipaqvysgy eyysgnyvnv rnrglefatn
      781 invlgnksaf kwnfnfnisy nnnfvtklpd gdrdfffgps flqqsltlge plfnykvwrt
      841 ngvyatnaqv ptdpttgkke tfngvtlqag dpryidmngd ynitnddkvd ygnpnpkltg
      901 glgsnfsykr ftfsfffsym fgrkvlnggf sdalnstkgv gswgalagvs altgslsdfw
      961 qvpgdvskya rlvyptytgt dpwdistdyf vesgdfiklk naslgydlpt rwiehlgmkr
     1021 lnvylmgenl wmwkkskdla dpeladpttg lvnvvyptaa kftlgvnidf
//
LOCUS       WP_091369112            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091369112
VERSION     WP_091369112.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114949
     Region          45..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlhcyskkcf tgiiiilmli lakssyasiq kdttaktatn ppglitgkvv dednralkgv
       61 rivvngrsds sktdlagrfl vrakigdklq fsypnhyinn vvinnaadtl svrlldhylk
      121 spekidvlyg tinpanelgs istiynnqit ttpgptyvya lpgqlaglyt qqtsgftsaq
      181 nvailqhfls sttanfapvh nvipsdntef iltsrgqnvt tiidgiqqni taidpssies
      241 isilkdalst illginsskp vllittkkpd lgdpritftt eagiqqslgl ptdqlpayqw
      301 aylynealqn dgkptfytna dieayrnhtd pyghpdinws klllktyspl itdklnvsgg
      361 tenaryyvsl gyldqggifn eapgldystn tnisrytlns nisvdvnknl nvdlqmygrv
      421 qqmfepgsgy asiltniftt pnngypvynp dgsfggssti snftnnllsq aqysgytqtn
      481 ikdvlvnldl nykldnvtkg lsfkakgnla iesqvyitrt qqnnaygysi vdsavkltsv
      541 gtttpltnvf atelsarysf aqaalnydrq fgknrfggql lydtkssvvs ydlsavttdk
      601 alkvnygydd kylfegainn ssynrytpgh qagwfyaagi gwqmgkedfm ksikwidswk
      661 wrltygktgd nsnagyytye qtftsgggyp qglnygsgsg yqevtpiadp slrwanaekl
      721 dfgtdisllh nhlqiaadyy heryynlvtt rgatiellgt ayppenigin lykggeltlt
      781 yknnidnfny fitgngslva skvlyfdeep pkypwnahtg lpvtaifgyk nigfysvedv
      841 akhaatiagy saqpgdlkya dlngdgvvdq ydqtaigglk plvfyggtlg fnykgfsfsv
      901 ilqgvfnrqv svdnsydapl qglgllgtga sgqayanavg rwtpetaata tlprlsvvqd
      961 eangnnvqms sfyvksgdyf rvknaeigye lplrwatrlr lsgirvfvng enlftvagyq
     1021 gfpgydpevn gvgaypiqrv inagltvkl
//
LOCUS       WP_091369361            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091369361
VERSION     WP_091369361.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114697
     Region          25..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklkyllil fflfplslla qqtsisgkvi dltdgstlpg vsvkikgttt gavtdaggrf
       61 tltvpgtnai lqvsfigyei kevtvknikg gvialnptnk sldevvvvgy gvqkratvtg
      121 siatiqnkdi ittknesvvn mltgkipgir ivqktaepgs ydndlnirgf qtaplividg
      181 viggdqstlg rmdpneiesi svlkdaaasi ygvraaggai littkkgstn gqvninysvn
      241 davqtflgmp qgvgavdyml ltnekakrdf qnnfvsnvtp vysyadilpw lngtnksadw
      301 sdlvfnktan qishnlnidg gndkisyffn fgyqqqdgvy ktgdlnynky nfrsnvtvsi
      361 akglkaqilt sgwmdqknqp ltpewevyky twnqipinqi yannnplypn vmpdnqnpai
      421 mtndsevgsi vaknksftsq lnltysipgi sgltakalfn vdygvydynq iqntfnlyty
      481 daandvylpq svnspsgitr qyythfntls qitlnyahtf fqdhnvtamf tyeqshntad
      541 nfnayrdtni pidylfggla nsnmsggqda galqdfahks figrlnydyk gkylaefsfr
      601 rdgtslyqpg pdqwgffpga svgwvltkes fvrnlvsdki lsnlklrasy gkvgdeagna
      661 ynyvtgytyp vnsyifgatp vngsapklgn pgltwpvsti knigldfgll ngkingtiev
      721 frndrtglva tpstvlpgtv gaptpqinyn sdrvqgldfs vsyrntfgql gvnltgnigt
      781 trledmtvlq gtfgnefqqw qssqsnryqn iwwgptyagq ftsykqiqny gvnmgggnns
      841 vipgdyyyqd tnhdgvidsk dntpiatsdi plynygltig lnykgfdmtl llqgaagvyv
      901 qygeqfaspl mygrsaltrf ldswhtvdps anvfdpntqw vpgyypamgs pdaqgtkaiq
      961 nasylrvktl efgysisplv lkhigvkklr fyvnsynllt ftglknydpe hqgpnptdng
     1021 nfsvalggyt ypenrtfnlg asvsf
//
LOCUS       WP_091370332            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091370332
VERSION     WP_091370332.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117874
     Region          23..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllfilll iffafnsyaq nlvikgkvtd dkgnplpgvt itlketqirt itnqdgmyai
       61 nlgaatsrll vftyisyklq evnitgkttv dvsmaseskd lteivvsaln isrtkkslgv
      121 aqqsvnvddm tqarasnitd lldgkvaglq ittsgqttgs trvvlrgmss itgnnqplwv
      181 vdgvpvdntd sngqvgnydy gnnaadldpd diasievlkg pnaaalygsr aangailvtt
      241 kkgtknaglg isvnsnymas rvlqfpdfqn iygeggsgay sgtrsnngag iveegsntrs
      301 wggpmlgqpy lsfsgqpity spdpgnvssl yqtgyaytqn vaianatdns sirfsytrtd
      361 andvvknqnl qtknnlqlnv srdftpfiri dtriqylqad vknrtarned pnnpnniynn
      421 lvrsassssf fpyvdpsgne yaggstnlen pewvinenhn editntiigg isatinifkd
      481 lkfraqtsan liwgdrnmfi qkgsvtnvng sytefqqnnq nwnteglfsy nknigkfsim
      541 anaggnirtl nyyntsatan qlivhdvasl snnasvlsgv esltksqtns lygtasvgyn
      601 eylyvdvtgr ndwsstlpaa nrsffypsvs tsfifseffn ipqnimsfgk frasiaqvgn
      661 dtspyntmgs fstvstpfng lplvdydqvl rnsnlkpest tstelglelk flhdrisfdg
      721 svyskkttnq ilqgainpas gystqfinag evtnkgveis inatpirten fswdlttnas
      781 mnrnmvvsls pgltqfklgg alltsvyaev gqpigtirae dqakdaqgnv iiqktsgipy
      841 sestpfttdg katpilgnfq pkalgsfgst fryksfdfnf lltgrwggqi fsgsywradq
      901 ngvtteslgg rqawllsnei ygegtlqqng tttlyglpyp dasrpkgsif vgyypetdkn
      961 gniiydkngn miadkskpnt qyinpqtywq rayhinselv fddsyikltq viigynvpkt
     1021 llrrtvfksa rislvgrniw tilqntpkgi dpesanssgn aqglelggal pyatygvdlk
     1081 fsl
//
LOCUS       WP_091370531            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091370531
VERSION     WP_091370531.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120927
     Region          47..95
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          107..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklirllili lifqvsknac cqtkvtlnyq hvhfeeiita iqhqtayrfi yradqlpnqq
       61 vtvsakdeev lsvldnllkg thyyyrlisn nliaigtekd siksvavsgv vtdekgepls
      121 gasvriknss ygtqtdgqgr fmincikgtt ieissigyvl qqviitatdq plkitlqnsy
      181 rslnevvvta lnikkenwkv gysvatisga dlttareanv amslegqvag lnvsgtsggp
      241 asssrlllrg aasmsagspl lildgipidn tqrgsaneyg gadygdgfsn inpddiesit
      301 vlkgsaasal ygaraangvi lintktgekn sstqveynln lsfdhainnt dfqyvygqgs
      361 qnqrptdvqs aiasgllswg ekldgkptiq fdgnyypysa vknnidefyr tapaltntie
      421 vnggnsktaf rasasnlnye siipnsglnr ktfnlntsyd itdklklsfn gdyiyemakt
      481 rsylsdgpmn anygieflat sanqlslkpg ynpvtgnetl wnsnvyitnp yfvinkqvdn
      541 strnrfitat vlkykfsdni ylqgrlgydi sndgilnvlp tgtaftvneq gglnglsksq
      601 tgelntdllf vadknlshdl tlnfsaggny rkrqynltei tgsqfitpyl ytpsnlvsts
      661 snydiseivt esayysadfd yknlldinat grydvfstlp pnsrgifvpg vsasflfsnl
      721 lalpyltsgk frisyaktsg epsqpyttql yftsnntvng iplgsfsskl pnynlkpftl
      781 tefetgfnls ffqnrltlda tyfnrithne ianaqqsvat gftsayvnvg ktkntglelt
      841 lsgglirtan fswntginfs hvhnvllsid gssqylltgt yrplnantal vvgksitqvm
      901 aydykrdamg niiigsdgip ergalkamgg tlptfyggft nsfrykkfnl sflidykfgn
      961 kvlsatedys yvyglnkatl pgretgivak gvndngqint invpaynyyp dlatnisals
     1021 vlngsfikfr qlilgyeftp pllrnvfrtv tvslvgrnif tilkytknid pesefspqlt
     1081 yagiegeslp atrtlgfnln fkfk
//
LOCUS       WP_091370537            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091370537
VERSION     WP_091370537.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111387
     Region          48..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklltcfi vcssagafat gsamasassr hflakheqfl evkadqsikg vvkdetgatl
       61 pgvsvvikgs tkgtqtdang nftlaankgd vlvfsyvgya skevtlsgdp vitvtltsss
      121 sqldvvvvta lgikrsqksl tyaqqqisgs qlndvktdnl mnslngkvag laiqpsasgv
      181 ggsakvllrg srsfagnnqp lyvidgvpma npvnysgttt tnggqpgdnf ggspdggdgi
      241 snlnpddies itvlegasaa alygsqaang vivittkkgk vgkaeihyss sfqasnavse
      301 pkfqnqygqt sagaatswga pisnsennlk dfyqtgtnwt nsvdlstgse iaqtyasyan
      361 tsangiepgn tlrrnnfdlr etghflnnkl tvdgnvnyid qdiknspglg lyinplvgly
      421 lfprglnilp yknqyllpnn tgaarqnwit nnddsqeqnp wwvtnmnpnn lqrnriifng
      481 sakydftnwf nvqvrgsldr tndnynqdly sgtlktfnsn gnghysysnq vteqkyadai
      541 anftpgkfgd fkfdglvgaa indsklsglg asgdlstpdf ftpyniiagh sapiafgyht
      601 qiqsifeaan lsyndwlyla ltnrtdwnst laftdkldyn ypsvgltail sqilslpkvi
      661 syakirgsya nvanglpayi tniqntqtss galtfnttap lhtlkpetth syefgtdwkf
      721 ldnrinfsft yynthtynqy faltppaatl tsigyinagd iqntgfeilv gadivrskgf
      781 twnssvtasa nknkiisvdn tdnlnqailt gndgggfgye sviakggsfg diygyttvrn
      841 akgqmiltgt sastyapqks tvmsyvgnpn pkfqlgwsns fnyghfnldf lvdgkfggqv
      901 lsltqamlds ygvsqvsgta ranggvtvna vnsagtpvtt vnaqtwyqti ggrnaltdqy
      961 iysatvvrlr qaalgytwpv ansvvknvkl sligrnliyf ykkapfdpev ttstgnglsg
     1021 vdvfnqpatr nvgldlnvtf
//
LOCUS       WP_091370729            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091370729
VERSION     WP_091370729.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109454
     Region          28..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiyflrys flllficlsn wvmaqsstit griidednqp lpgatviikg tsisagtdvn
       61 gyfkltnapg gqqtlvvryv gyeslekpit tanglvvnlq lksssvllnq vavigygtik
      121 kadatgsvdv vtakdfnkga vnsiqdavsg klpgvvitsn sgapgntsti rirgttsina
      181 ssdplividg vplsnvvagg taniltsinp ndvenitvlk dasataiygs rgssgvilit
      241 tkrgtkdfsi nyngtfslsv ipkevpvyta sqfrdlintp stfstpgaqa aaqallgtan
      301 tnwqnqiyqk afgddhnlsi sgstknmpyr vsvgyddadg vlktynfqrt tvavgldpsf
      361 fnhtlnlhin lkglyntnnf adqaaigsav nydptqsvyn gntrwrgytt wttngntnin
      421 gapvtlatan pvarlnetdn tstnrrsign iqadykipgi dglranvnlg ydyadafgkn
      481 nvldstqwiy lpvasggqki syntvnrnql aefylnykkd lksiksvidv tggysfshfy
      541 tegntmssdy nettfnpssp ykteyylasf fgrlnytfds kyiltftird dgtskfapan
      601 rwgvfpagaf awrikdedfm kdntlfsdlk lrlgygttgq qdltnnnnyp ylpqytisdn
      661 asryqfgntf yntlrpgpyd agikwesttt snigldfgfl ngrltgsida yykktknlln
      721 vvnvpvltnf aatllenvgs mqnkgaelsl naviidqkdw hwqmgynvsf nknkilnlvg
      781 stnpgfvqvn pnsgisgtts gtiqanevgy pinsfyvyqq iydkngkpie dgyvdrngdg
      841 qinssdlyld hspnptvlmg insdlaykrf dfsfsgrvsl gnydynnvaa gstyrglyss
      901 lgylsnqttn asvtqfttal ttnqsdyyiq nasffkmdnm nlgytfptyi knklklrvsa
      961 gvqnvftitp ykgldpeiqg gldnnffpra riyqlgvnas f
//
LOCUS       WP_091371598            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091371598
VERSION     WP_091371598.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117659
     Region          39..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikffykkil yriclipmlf agvfaanaqs ttgsaplvtv sgivkdmngp lpgasviitg
       61 ttngtptnnn gkfsitvesg ktitirmigy itevikvnap nsnlvvelkn dqhmlkdavv
      121 igyqevsrrs vtaaitsldp ktiedipapt fdallqgrva gldvqnfsge pgvsstvair
      181 gntavarnis sdnttaagka slaravsgpl yvidgvpqtt ddiaaisygs gtgtdvlagi
      241 pisdiadiai lkdasaaavy gsrgasgvie ittkkgvagk tkinfstyhg itdkpaldki
      301 ltgaaetrak laliehygdy gnlkdipqil tdtlnpafnn andyrkqiyq tglvdnydfa
      361 isggndkvty ryglnyyned giikksglkr ytfnsnigln lasnfkintq iryyrldrpr
      421 svsdlsggad pftggyyass plpssnlyls pamqnfifgn tsintddnts nsisispnin
      481 wqiskkwsfn tvisyeatns rhdtytpgay rlsgegyaas fadnqfnylm sntiqyntnl
      541 gkdhhinllm gqnmeyhqyr atdaeadgip ndqisvvdvv nknastafsd lqengietef
      601 lrlnydykgr yllsgvlned asskfgsgnr agffpsisag wiisdeaflk dqsswltllk
      661 lrgsfgitgr qpddgnnyls ynnysvgags fpgssspqtg anlsytyngi paispnfngg
      721 isnkdltweh skqtnigidl tmldgrfsfv adayvkstaq gifsldvpit tgyttittna
      781 igtqnkglem tfiahyfkps rafqwetdfn iafnqnevts lpnggrdili nggstsyilr
      841 qgqpintyfl fqqtgiyktd advpvnpvtg avlnfygypf kggdpiwkdq ngdgvldqnd
      901 yvasgnpnpg ivggvnnnfs yknwsltvfc tftldrtiyn dylvgklshl vptndgnsnv
      961 yddlvnsafp dlsginywqn pgdnakypsl ssvsgtryky aavstawlqs gdylrvktvt
     1021 igysfnpdai kklglsrlrv ygmvdnlhif qakgvpdaea vdafgvyngn gypipkkftl
     1081 gldlsl
//
LOCUS       WP_091372524            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091372524
VERSION     WP_091372524.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111378
     Region          48..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllplill ipcipvrass lykehmvint glhvsqslht ktllnvstik gtvkdatgqt
       61 lpgvsvsikg tsvgtqtdan gqftisakvg dvlvftsigy tkkevtiani nalvvelntd
      121 arnlnevvvt algvkrseks ltystqqvag selttvktdn lvnalsgkia gvtitpsasg
      181 iggsskvllr gnrsldgnnq plyvidgvpi sndgnnfgqp gdayggnpeg gdgignlnpd
      241 diesmtvlkg gpaaalygsg aangvivivt kkgkagktti nfsssasfdh kayepalqnr
      301 ygqtsagatt sfgpaitsap dnlsqffqtg nnytnslsla ggsdiaqtyf sytnttsrgi
      361 epgnklgrnn fdlhetakfl nnkltvdgna nyitqtldns palgyysnpl tglylfprgq
      421 niapyknfeg pdgtngvptq nwpfqediqq npwwiinrnt neatrnrill ngsikydits
      481 wlsiqargsl drrndagdqk ywagtlapla apngngswng fnstntqrya dailnfnvpl
      541 kskdfkvdgl fgasitdntg tglsfgpgpq aptlfglfip nlftiqniev apagsnnpyg
      601 snvsggttye dqtqavfgsa nlsykdwayl svtdrvdwss tlaftptyhy sypsvglsfi
      661 lnqmfslpqa ityakvrgdy asvgnspgay qtnpvnypna ntvtfnstap yptlkpeitk
      721 tyeggadlrf lndrlsfsft lyktntinqt igfaplatsg ygsgninaan iqnkgieitv
      781 gynmvrsqqf swnsqinfsr ninkvldvas kigidsielt nsssyvsevk kggsygdiyg
      841 qtllknssgq llleadgtpq kgdfvkianp epkfqlgwnn sfnyqhfsls flvdgkfggq
      901 vvsvmqsild sygvsqaygd araaggvkvn gvgpngkpit tvnaetwyta iggrnaalge
      961 yvysattvrl remafgytlp vnnsvfksfk lsltgrnliy fyrkapfdpe itsstgngls
     1021 gvdifnqpal rsyglkldvt l
//
LOCUS       WP_091372886            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091372886
VERSION     WP_091372886.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113216
     Region          37..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknfytqki nlvlkiaaln llfmvlfsnf aaaqaninik gkltdgvtne tlpgvtiqvk
       61 gtanavstda nglysitags tstlvfkfig yapkeiaiag rtaidvklqp ettelkdvvv
      121 talgitkqnk avgysvstik gatitearqn sfvnslegrv agvnvsgvat gpngasnvvi
      181 rgitnmtgnn qplyvlngip lvnnnyntgd qghdgyggkd ggdgigdinp ddietisilk
      241 gaaatalygy rgsngvilit tkkgktgegl gveinsnfvr envidetdfq teygqgsnga
      301 kpvsaadals smesswgakl dgsntyqfdg verpyseaak gnlsrfyrpg nnftntvsfs
      361 kgfgddgatr fsvsdlndes yvpnaglqrl tfnqttnlkf gkhltldlss qyvseytkna
      421 pnisdaignl nwapmfvppn inittlkgpn gngtvagdsg velnafgdpy ttnpyfaaye
      481 lqgaihrnrf tgsantkytf ddgffiglqv addytndrtt niepagtgyv vdegltgdmm
      541 eenvkqteln idltggkkfk fgkdftldll lggnyrksqq eyltakgnnf aipflytign
      601 lenpieslqt nneeyqslyg sadvgyksfl yltvtgrndw ystlspgkit ylypsvsgsf
      661 vfsellhmpd mdlgklrlsy advggaadnp yqtlqtygiq gtytppgggi ypigvagslq
      721 vpnsalkpss rreieagtem dffknrlrfd ltifqkrvtd diipvtidyt ssytsallnv
      781 gtlryngvel elggtpvksq nftwdvdfna ayikgkvisl ggqpqitlgs eaqdwgsgay
      841 taqvvgkeps qifapspald angkiiidpg lgapdqtlsq pkdfgsaenp wagginnsfk
      901 ykhftlsfli dgkfggkifs ntniiayqqg lskatlagrd llygtdkqta sayyndwafa
      961 dqgmfvydds fikfrqvifg ydfpstlfnn kiihglrlsf vchnvftimk htpnfdpest
     1021 ysasvysqgl eapavpysrt lglnlnikl
//
LOCUS       WP_091373426            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091373426
VERSION     WP_091373426.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117874
     Region          23..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkiylllsv llllstvlka qnrtitgtvt deknaplpgv tvqvkgstss tatdadgkys
       61 ikvtnlqsvv igvkflgyny qektlreger nadfklvpnt snldevvvvg ygtqkkatlt
      121 gavvtispkd iqdipslnlg aslagqvagl avaqdqrpgq patltirnpv vlnssaggst
      181 nplfiiddiq rsqadfnlld pndiesisil kdaeaaiygv sggsgailvr tkkgkigapk
      241 isfssqfgsa navqlpkmlt gpqmatfind yqqigemapn gvqtgntidv ngyvngnasq
      301 kisgwytpde layinnpann snflkqefha advereamni sggtdkatyf vgadyvnqns
      361 nfsgisnykw giranvqakp akgltaglnv sfdqsynkef wykqksttes lnndvvtlnq
      421 alpwqkyfin gnpvylsstt fddinvmlfq nsnnyednrq fltnflgtls yeipgvkglt
      481 anatfnynin tnfptqfgtg fnysqysgtg annhipggtl lktieidngn iitfnpsyak
      541 ayqldaslny qnsfgknnit glvvyeqret ndnfvnanva gvvpgglpnf nfttglqqtn
      601 qangsllges gaesvierin ydynqtyllq lvgrqdgttn fasgerwgnf ggvsvgwvas
      661 nekfvkdlap wvnqlkfras igivggnsia sanyqyyqqy giatgspngg avfdeqvrgi
      721 giksgnladp nttwdhrtet dygvdmqflk nrlsitgdyf wthgydlltt lsgavpflig
      781 ntppaenygi vdnfgteitv gwadhinsdw gynvkvfysw sddkniredi apgligtaqd
      841 rtgksddggv fgyeslglir tqsqadqiia sraaaaggaq nvkifgltpa pgminyadld
      901 gngiienndt kdekylshkv gnhnnagfnf gfsyksisln vvsglswggt ssisgtelts
      961 ndnqnassgg adlqenraaf wsdhwtptnt natypapyyy kewdvvsnfw fvnsfnwniq
     1021 qaniswalpt kwikvvglas arlfgqctnv lslynpypdh yrtdqvgien ypllrtftfg
     1081 lnagf
//
LOCUS       WP_091373613            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091373613
VERSION     WP_091373613.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120767
     Region          29..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiyqqlki aitallffli paitfgqtki sgivtdenkl plpgvnvtik ggqkgtvtdi
       61 dgrfevkans dqtlvfsfig ydkkeilvss qtvinvsmqg gakalnevvv talnvkkdvk
      121 rigyatqtvd gdalttardp npitglagkv aglsvgasae llgtpnvlir gdavtlyvvd
      181 gfpintdtfn ispddiesyt vlkgpaaaal ygsralngai littkkgnkn kkgftvdlns
      241 stiinkgfla fprvqhsygp genefyefvd gkggapggvd sdydiwgpyf agqlipqfds
      301 pvvngvrtat pwtargannl anflqtgyqt nnevalsavg dtynirfsas qqhqqsyipd
      361 nyldiananl yasfhpidsr ftieanidfn rqttdqfpdv tygpnsliyd laiwtgadws
      421 vnqpiikavw qpgkvgvqse feeytryhnp wfmvedwkrg hykndtygyl sgnfkidnnl
      481 nvtlrsaidt ynilrtedlp ysahpygreg nmgdyredrr dlfdnntell lnynytikkf
      541 vnlsglvggn lrnfsynssw vstdylsvpg vysfnnslnp lqatsfnsqm rvlsafysld
      601 atfgnfltis stgrvdkssa fqtpttyyyp slsaasvisd yvklpdfisf lkvrasysnv
      661 rsdetsptvg papfssitaf ggstgpslyd nplgygstyl spyngpnysl npaynqgkpy
      721 nnqpagyntn nlyqtglvts trvnyeegfd ikflknrigl satafqyidg pevlantist
      781 atgynieytn alktkktgye asltgtpvks ndftwnamvn vstykqvfde lpagqtlypy
      841 nngyftkger idnfygtafv rnkqgqivng sngeplvnpv dqflghlnad yqwsiynsfr
      901 ykqitlgfqf dgsvggvmvd ymhkktmvgg anletaegal gaaryqdwvn fgkkgyngsy
      961 vgpgvvisng vapnydsktg ailnynqlqf apntqtafvq eyvsqyyntd eanlmsktya
     1021 klrevtiaya fpkewlahtf iqnasaslfg rnllyfykda rfkdvdldqy nspqatsvlq
     1081 sptvrsygld lklsf
//
LOCUS       WP_091374857            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091374857
VERSION     WP_091374857.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114726
     Region          25..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkillimg lclvifcqaf aqnhtvtgtv tgkddglavp gvtvkikgtq vgtqtnsagk
       61 ytisapngsv lefsfigylp vqltvqgdvl nvtltpassq lnevvvtsqg ikrekrtlgy
      121 saptvsnkel teggnpsalt sltglvagvn itstsntpgs strivlrggs sitgnnqalm
      181 vvdgvpidns siisgasslt avdfgnrgnd idpndiasit vlkgpaaaal ygsrasngal
      241 mittksgtkn gkkleitlns tntfssvlkl ptfqneygqg ymsgsatspg yvtgindasd
      301 nfswgapftg kvepwgqeid gvtqtkpysa lpnnikdffk tgfaadnnvg iasgddknsf
      361 ylglnslnss gifptndsyd kygvrfngka tlannftasv nfnynkiqan tpsggqgsng
      421 iwtnlmqtpr dipintmgnl nnkyngynsi tntygfygaf ttnpyyilqn ysnlddvnrv
      481 tgdvnlawkp lswlniverv gadsysdrrk liqpkytflp adesgsglwg kitnkgsyev
      541 dqynvnevvh dlmvtathdf gkdfhtslll gnnirerstt snltstntsg glvvpgwynl
      601 dnsngpvnvi tddieikrli gfyadlnlsy kdylflegtl rndrsstlpl nnysyfypsv
      661 sgsfvfsell knsgiadils ygkirssfaq vgsdtdphel tttygrttvn gsfgnttfpf
      721 gnvpayqigs tlgnaalkpe qtssfeigte laflqsrlsf dfsyyvnnsk nqiipipvpg
      781 stgygfnevn ageiqnkgie ltingtpiqt sdltwnifgt ftknnsdvla lpngagqivi
      841 ggfsgmaiva akghpygefy gvtnqtdaqg rtivskttgq piatttaqyl gsyepkfqts
      901 lgtnvkyknf tvsvlfdvkh ggvlysqtks ltdfvgtsae tggprfgqpf pnsvtldasg
      961 ksvpntsipy svynyytnvi gntpgmnvvd asyikmrsas isytfdktql kslpfgaltv
     1021 gvfgnnlflw tpksnayvdp evnssgagne qgfdfsanps vrnyginlkv sf
//
LOCUS       WP_091376676            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091376676
VERSION     WP_091376676.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110654
     Region          45..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllpiill lpciamgana spnansrasf titgtsrnvn lpapvkgtvk ddtgsplpgv
       61 svsikgttrg tqtdadgrfn ldaksgdvlv fsyigylkke vpvsssliya vtltsdsknl
      121 nevvvtalgv krseksltya nqvvdgaaln tvkndnvmns lngrvagvdi spsssgvggs
      181 vkvilrgsks fagtnaplyv idgvpitnns ntngqpnsty ggspdggdgi snlnpddies
      241 mtvlegasaa alygsqaang vilittkkgk agkteinfss sytndaisyk pefqneygvt
      301 pkgnqswgak lstpatadnv gdyfqhgnnf tnainlsags dvaqsyfsya ntsatgvqpt
      361 nslkrnnftf retghflnnk ltvdvntnym nqkvintpgq gfyfntlpgl ylfpvgvdit
      421 pyknnygipq parnglptqn wianediqqn pwwilyknpn fsnrdrllin ssvrydindw
      481 lniqargnvd rtsdafeqdl yagtnpvltq glngsyqhsi qtitqtygdf ianfkvpmks
      541 dfkldgllga sitdnntvgt lfgqgtglli pnvfedqnvl tsgssnvskl panhnqiqsi
      601 fgslnlsykn wayltltdrn dwssnlaftn kdsysypsvg lsfivsdmtk lpdfisyakv
      661 rgsyaevatt vtqyvtnlts tngsggvtlv npvpnsdikp tntksweaga dlrfldnrlv
      721 lnytwyksns ynqfiqytps agspyttgyl nagniqntgm evklgydiak gqafswnsal
      781 nysynknlii qlnpadpnan iqltgngana yesvlkaggs ygdiwgvkfe rnaagqimvn
      841 ssdapinsgi fekvgnpspk fqmgwentfn ykkfsfdflv dgkfggqvls mtqmlmdsyg
      901 vsvasgdarn aggvtvnavd pngkavtkvd aetwysaqgg rsgiaepymy satvvrlrsa
      961 slgytepian sfvksirfsl igsnliyfyk kapydpeitm stanglggvd vfnqpttrrf
     1021 gaqlnvtf
//
LOCUS       WP_091376607             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus sp. DSM 45219].
ACCESSION   WP_091376607
VERSION     WP_091376607.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus sp. DSM 45219
  ORGANISM  Geodermatophilus sp. DSM 45219
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Geodermatophilus sp. DSM 45219"
                     /db_xref="taxon:1881103"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52816
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpretr pgetrvaatp ttvrqltalg ydvvvetgag aaasfpddgy rgagarvgta
       61 eeawgadvvl hvarptveev grlrdgavla stlapafdpe llaalaarpv talamdavpr
      121 israqsldvl ssmaniagyr avieaahafg rsftgqvtaa gkvppatvlv vgagvaglaa
      181 igaasslgav vratdvrpev aeqiasmgge yvgvpadeeq agggtgyasv tsadfdrraa
      241 vmyaeqarev divittalip grpaprlite emvasmspgs vvvdmaaaqg gnvagsvpde
      301 vvvtpngvti igytdlpgrl pgqasqlfgt nlvnlvkllt pskdgrvvld lddvvqrsmt
      361 vvrggellwp pppvqvsaap aaapvprpap paptpraprs partaavvgv aaallfvlta
      421 fspsqlvgnl tvfalavvvg fyvignvhha lhtplmsvtn aisgiivvga llqightgal
      481 vtvlatvavl vasinvfggf avtrrmlgmf trgparatte r
//
LOCUS       WP_091377444            1220 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091377444
VERSION     WP_091377444.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1220)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1220)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1220)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1220
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1220
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132796
     Region          73..122
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          137..1217
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkfyrtkly kylkysfrps iicyilafif ltyssitasa aegqsintvh islnvtntri
       61 kevfnlieqk tnfsigydna ldinqrvsvh idnltvnqtl qavlknyngt isqvdnyhil
      121 ikvekkaspn psskqkrkvi gkildetnsp lpgvsvrekg tgngvltdvg gnysiavdeg
      181 atlvfsfvgy tsqevitgtr eqinialkpn snilnevvav gyqtvrksdf tgsissvkas
      241 eintsaptlg qglvgkiagv qvlqvsgapy etpkitvrgv gslyassdpl yvidgypagn
      301 dlfinpqdve svdilkdaas aaiygsraag gvvlittkhg pkkdspgkfe ydldigmdql
      361 akkvklldad qfaqlaidgr nntyrdlwva kgntwnnsmy sddnatrian vgnaasvsiq
      421 pstydfatqt lihqttntdw qnelyrnalt tnnnlsfsgn sgdtryyfst gyqnqngiml
      481 gtgqqkinlr anvdgkigkk ltimaniaft qntnqetqdg rwdhspalga liylpnfpay
      541 npdgsiatnl vaalsplygy qsienpiata teikitrvgn ratyntqaty eilkdftfka
      601 nlgmqtygen ynyylptsls ngsfapysaa siaaakavqq tidyrdelge ftlnyskqik
      661 knhfdalagy saqktinnvl evqgtgfqnd nipnitgaap ssitlitpts gsipegtqpt
      721 gnavytlvsy fsrinynydg kyflsgsirt dgssrfgpdn ryavfpsvsa gynlsdesfy
      781 hnwlgeqssi klraswglsg nnnignyntq qtvnspistv fgngtaltta itpgsikdqk
      841 lgwettsqyn fgvdvgllkg rlfiignyyl sdsynllfnq pvsalsgsqs iltnlnnskv
      901 snkgfdlqld gkpvvgkdfn ldisgnisfn rnkvlalgng ntiitngaer syltnitetg
      961 epigmfygyk vggivqqsdm aniaadqavy kangnkypag yvlkghaqss fsttplepgd
     1021 lwfvdtnhdg iinskdagvi gnpypkftyg favnatyknf yfstsfngsy gnqvldgqdy
     1081 ylynmegsgn qyedvanryi naanpgagtv yrasrggdqs nstrlstfyl qsgsylrctn
     1141 atigydiksp fvlknlglss lkvfgstnnl ftitkykgyn pdvdydysfs gsqgtnitpg
     1201 vdygvyplvr synlgikaif
//
LOCUS       WP_091377889            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091377889
VERSION     WP_091377889.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117170
     Region          24..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllvslc flmlsitqvf aqnrtvtgtv takddglpip gvtvrvkgst ggvvtnsagk
       61 ysisapagat lqfsfigyna lavapkggvq nvslepastq lgevvvtgal gvkkeakelg
      121 ysvatistke ltqakvtdva tglagkvsgl qvnladngvd pqvrvvlrgn rsitgnnqal
      181 ivvdgvpidd pnylntinpe diesttvlkg ataaaiygsk asngvliitt khgskvapsi
      241 tvsnttylqq lsylpklqnq fggyggeggs yvnangtvnp vgyeneaygp afdgrqllia
      301 lspifaadgt tvtgydslys pytykknavk dffktglqnq fnvsysagtd hgtfylgfqd
      361 attdgivpdd hsrrdnitis gnqdygnfha dykvsydqnn vnvagnsynq attsgglesa
      421 gvfsgrplyf eiintppnip ledfkdptsq ygnpnsyysa ystnpywtia nsrrkrdtyd
      481 llgtlnlayk itpwlsiadr igitqtteqf kytragitfa pwaiadpqsa gnvpssqgyl
      541 apsefdetyf eqrlnndlya tfnkkfgdfs vnglvgynme qryqrgiqlq gdalqfpndy
      601 nigsvlgvpd yaefsytqrd ysfyeqatvg ykdflyltgt nrdewnsvla aghdhfeyps
      661 vnasyiftnn ikalkdnkvl sygkltaays kvaniniggt ngnpygaysl inpfvpptgy
      721 pygsiggysq stlylnpdiq pektteyefg telgfldgri slkadyyqsk trnesltadv
      781 saatgftqkl vnaglvtntg eefdlnviai ksrsvtwdig atyshyhnli nqlpggevql
      841 ssfsdgvggg iyaiqgqsfp viktndwtrd patgkvivdp ttgrptvdpt ektygnttpt
      901 qilgltnsis yknftfsfvl dyrggysimn digaylnftg igaqsaengr qrfifpnsvv
      961 sqggkyvtnt svavnnggni agdgfwplvy gsnlgsiyvt saafwkvrea nltydvpksf
     1021 lasnlpfikr asvsligrnl lmftpksniy tdpefsesgn gnavgatsdg qlpptrfyga
     1081 nltvtf
//
LOCUS       WP_091379633            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter mallensis].
ACCESSION   WP_091379633
VERSION     WP_091379633.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter mallensis
  ORGANISM  Mucilaginibacter mallensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Mucilaginibacter mallensis"
                     /db_xref="taxon:652787"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121432
     Region          61..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltiylvr amlcpkikkq ftlalpalcv llihgnslla qqspqfhikg svfsgedsgi
       61 lpkatiknnt dgkqtitnsa gefqlltadt sgtftvsyig fkpltliynh shpgpfritl
      121 madentlrev tvstgyqtlp qeradgsfaq vdnkllnrrv stdilsrleg vvpdllfnrn
      181 tingsagqvd isirgqntlf ansqplivvd gfpydgdlnn inpndiesit vlkdasaasi
      241 wgvrsgngvi vlttkkgkqn qplaielnan vtignkpdly ysknyilssd figleqslfn
      301 rgfydsalqt gyaavspavq lmaeqragli sasdlsnqln llgqndirkd eseylyrhsv
      361 nqqynlnlrg ggdksdyfls lgddqdnsfy qgnqtgriti nsrlnfypvk nlqisvgany
      421 vqstsvsnnp lteygglsvg snglypyaql vnangtpaai pkdyalsytd tvghgklldw
      481 nyrpldefhn adnstksien ridlgvnykf fkdfhaelky qyehsdltql nnynsntyya
      541 rnlindytqi npdgtlsypi pvggilqqae ngltsqdvrg qlnfdhiwnn khqvtaiigs
      601 evsstiasin dytaygydkg tgssvanidy sdsfgllpkg sgmipntlgf gkttdnflsy
      661 ysnaaytylg ryvfslsgri dksnlfgvst nqkavplysa gagwemsked fyhlnwlpyl
      721 klratygytg ninksatavt tisqlsnnyd sgdsydqidn pgnpelrwek drminlgldy
      781 afknqvlsgs ieyyikkgid lfgnsplpps tgqttffgnt adtkgngldi vinsrnissg
      841 nfqwttnfmi shvidivtky dvtatsanyi afsnsssilp ltgkslfgly syawaglthn
      901 tgdpqgylng kvstdyagii antsvndmvy ngssrpttfg sfrntfaykq lslslniiyk
      961 lnyyfrktsy ssqglpysgn qdfysrwqkp gdetttnvps lqyppyttdr dlfykyssvl
     1021 idngdhirlq dinlsydfdr svykglpfkh lqvygyinnv gilwranhdg ldpdlssntt
     1081 aaayplprtf slgikatl
//
LOCUS       WP_091386704             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbulbifer marinus].
ACCESSION   WP_091386704
VERSION     WP_091386704.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer marinus
  ORGANISM  Microbulbifer marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Microbulbifer marinus"
                     /db_xref="taxon:658218"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54711
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miiaipreta pgearvaatp esvkrlrdlg fsvavekgag aqasfndeay veagaeirdd
       61 ikqcldgagl vlkvqapsde elelipegvt lvaflkpaqn adllkkladk kinalavesv
      121 prisraqkmd alssmaniag yravieaahn fgrfftgqit aagkippakv lvigagvagl
      181 saigtakgmg avvrafdtra evreqvesmg aefltveiee egsgtggyak emskefidae
      241 malfreqakd vdivittali pgkpapklwl admvdsmaeg svvvdlaaem ggncdytvad
      301 ekvvksgvti igytnlpsra atqssrlyat nlvhllsela pekngeidin fddevirgat
      361 vvkegeitwp ppppkisaqp kpaaekkaes savveekpak kksplsfllf wlvagglllw
      421 lgkvappdfv shftvfvlai fvgwqviwnv thalhtplms vtnaisgivi vgallqvgat
      481 gsglvtllaf vavlvasini fggffvtyrm lkmfrr
//
LOCUS       WP_091391297            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            noncentrifugens].
ACCESSION   WP_091391297
VERSION     WP_091391297.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium noncentrifugens
  ORGANISM  Flavobacterium noncentrifugens
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Flavobacterium noncentrifugens"
                     /db_xref="taxon:1128970"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115548
     Region          25..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwilt lllafsmqvs faqektvtgt vtedglpmpt vnvinkstka stqtdfdgky
       61 sikakagdvl vfsfvgytdt nvtvgasnvv npvlktdaqq lgevvvtsqg ikkekkalgy
      121 avttikaeef askpstdvvr altgkapgvn iqqtsglsgs gtniiirgys sitgsnqplf
      181 vvdgvpfnsd tnsdgnfveg atnassrfld ldpnniesis ilkglsattl ygsagskgvv
      241 lvttksgntk dvnkkmevsv sqslymteis glpdyqnsyg igneleyrtt fgnwgpsfnt
      301 rgeggigmdg tvihpysylg nsvfpeyvgq rvewkpqnnv kpffrtgyvn ttsvslsgrg
      361 estsynvnvg ntsdsgfien nnykrlnlss ggstklgngi tlstslnyik tdktapptgy
      421 gygsgaitps ifatilytpr sfdlfglpye npkthesvny rpditnprwl lknasddehv
      481 rrffgnfsal ydvnswsnvs yrlamdnytq akryyinkgg yqtprgymrt tnnentvfdh
      541 tfsynfnkel dkaaswnldg tigvnsrlea ydytalesfn qfvygfqehq nfqnhlgyse
      601 kqsfnkvgvy gsatlgykky vylnlqarkd yfssllkenr slfypsasvs fiptdaftil
      661 knnkyvnyak lrigygssag fpspyqtnig lyeqtsaftp tvggtvnvlr pdsqlgnpnl
      721 kpelykeief gleakffdnr lgidfsaynk kskdliidad lapengyvvq aqnvseisnk
      781 gielgvslgi ivpkedgfgw nlsgtftknk nivgtlglgv dkiaiagftn rgnfaipgrp
      841 ygvimgssil rdangnfivg sdgnyvvnse lteigdpnad wkstvineis yknitfgfqf
      901 eyqkggdiys ntanallsrg vtedtnfdrn atfvlpgvsa ngnvntvqis stqygfnnsg
      961 ffideqsvyd atnlrlreis lsyslpkrml ektpfgkisi avtgqnmwyk afnfpkhlnf
     1021 dpevmslgvg ngqgfdyltg psakrygfni nltf
//
LOCUS       WP_091391743            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            noncentrifugens].
ACCESSION   WP_091391743
VERSION     WP_091391743.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium noncentrifugens
  ORGANISM  Flavobacterium noncentrifugens
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Flavobacterium noncentrifugens"
                     /db_xref="taxon:1128970"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110671
     Region          45..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktisfisgr rhvsylfllv fyisttnala htnivplsat eqqqqtvtgt vtynnmpmtg
       61 vtitvkgknt taisgedgkf sisangtdtl ifeylgfktq sialnnrtil niqleedvnd
      121 lkeviinagy ysvkdsertg siskitakdf ekqpvtnvla amqgrmagvn itqntgiagg
      181 gfdieirgqn slrsggnnpl yvidgvpyas dligarvtsp empmptspln slnpgdiesi
      241 evlrdadata iygsrgangv vlvttkkgka gktkfianvs sgfgrvtrfr klmntqqylq
      301 mrkeaftnen iteypswatd ingewpqdrd tdwqetlagg nagfttvqgs vsggsentqf
      361 lvsgnysret tvfpgdfryt kanvlstinh ksenkkftlg ftagytardn kqpsidfmqe
      421 aialapnapa lyddagnlnw qnntfnnplr ylqteagakt ydllanaqlg ysilenlqlr
      481 ssfgftdlrh ketsalpstm fapstgrtps ssslfattan rqswiiepql dykisigkak
      541 lqalagatfq qqdasqmtqq fygfasnall ynpgsasrit tlssgesvyk yqaffgrvnf
      601 nfaqkyiinl tgrrdgssrf gpgnrfanfg avgaawifsn ekliseklpf lsmgklrasy
      661 gtsgndqigd yqyldtysts gysygvsglq ptrlfnpdfa wesnkkleaa letgflndri
      721 sttvawyrnr ssnqlvgipl pgttgfselq anldaevens gwevtlrtvn vktenfswit
      781 sinytiaknk llsfpgless syanqlvigq plnivksyhy tgldpqtgly tfedangdgr
      841 isepedktai knlnpqyfgg vqnqlrygnl qldflfqfvk qlnynqyygt aapgnmmnqp
      901 aavvshwqqp gdtgpyqiya tdlndaaita nsqfgssdaa isdgsyirlk nislsydlpl
      961 kwtrgigcrl svqgqnmltv tsfkgadpef kspgylpplk tittslqltf
//
LOCUS       WP_091392247            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091392247
VERSION     WP_091392247.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114989
     Region          27..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqkllllfc fglflignsa laqkvsvtgt vqnqqgeaip sasvklkgtn vgaltdengq
       61 fkisaeigqt ilitsigyqd ksivingknl aivlqatnnd ltdvvvtagg itrkkielga
      121 aqtivageqi tkaksvniag glqdkvaglq iqgttggvnp nyriilrgnr sltgnneali
      181 vldnvivpne vlgnlnpedv esinvlqgag aaaiygskas ngaiivttkk gragntaikl
      241 sqtatiesva ffpkmqnkyg qggsaygyde ngyptfsnie nqsygpafdg stvnlgeple
      301 dgsqqtipyt gndsrkdfwd kgltnqtdfs ltsgdavstf ymsgqyatvk gttpkdkfnr
      361 aslrvngsrk iyndkvvaty slgftqnnyd ittqtadiyn nmlnmpsdvd itryanwqtd
      421 pfanpngyyn pwylnpywel dnyrqhsrns ylvgnvqvty kplewlefta rqgithrnys
      481 dktwngsfty seyaktsssn sksdisaavs dgefystnll sdlffqakfk andfsfnflg
      541 ggqwnqdeyk gvnvsasplv vpdlynvsnl vgipgasegn ykartmgfyg dfrvgykewl
      601 flhmtgrndw tsilpvntrs ffypsadlsf iatnaldflk nsnvihflki rggvskvgev
      661 nlpgtygsyq lqrtysqqng fpygdlagfg ldnrivsnql kpemtrqyef gfdlnlfprd
      721 ivtaavtyyh sttsdqtvst gisyasggss yltnvgktms rgletelkin pirnedwdvs
      781 fgvnytyldn kvisidgdli nqialssysd gsgsyakagy afpvimgldy yrddqghviv
      841 daetglptkn ptlqvlgnav akhrlgldfn vnfkgitlag lfeyrggydm yfgggntydw
      901 agtgirttif nrgrfvfpns vyedpnnpgt yikntnitit dgngnsgfwt ddlnravssn
      961 yitsgafwkl relslsydip qsflrktkai kkmtvslqgr nlfiwlpktn lytdpeysev
     1021 sstsngvgit gissappsry yggtisltf
//
LOCUS       WP_091392257            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091392257
VERSION     WP_091392257.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117825
     Region          25..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskklfllfc vsslftissv fgqnitvhgk vqnekgeavg aasvkikltn qgaltndqge
       61 ftlsvekgki lmitaigyee qdvraeenlt itlkeaeaas agsdvvvtan sirrekrtlg
      121 ysapiiksde lmqgqstspl atlagrvpgv nvtsstgapg sstrvvlrgg ssitgnnqal
      181 ivvdgvvmdn ssiigggslt avdfgnrgnd inpddiasvt vlkgpaaaal ygsrasngal
      241 iyttksgssh kkqeitfssa ntfssilklp dfqneygqgy wdgtydkdsn lnvvldpren
      301 gswgpaftge lqewgqeing vrlkknysal pnnirnffst gfvtdnnvsi atgndkagyy
      361 lglnstnsng iypgdndtyn kynvrfngka qlsnkfysav sfnynkihqn qvgggqgggs
      421 vlsnlyqtar gipidkmgdl nnpyfgygyt dangvthnde ygfygvytms pyyilknykn
      481 yddvdrisgs ftigynptdw lnvvervstd fysdrrrlie pkyeyypidp gnsdwytqgd
      541 vqtsngsyve nnitvgevnh dlmitaqhef nkdfsgslmv gnnirqrsyt ndytstnqss
      601 glivpgwynf gnsngpiyat nytstkrlvg lyadlnlsyk dmlyldatar ndwsstlpke
      661 nnsffypsvs gsfiftelmk nsnitsvlny gklraswaqv gndadpylls ttysatsisd
      721 gfastqfpfn gvpglqvgst ignpdlkpei ttsyeigtel sflhnrlsld fsyytnkskn
      781 qilnipipgs tgygykvvna gvirnrgiel slrgtpiktq nfslelygty yknnskvlsl
      841 mdgvsqvtig gfnsmaivaa vghpygefya vtnqtdgqgh tvvsasngip lqtdsaqylg
      901 synpdyqasf ggkaqfknwt lgflfdtkqg gkfysqtkay idfngtalet ggdrnpqiwp
      961 nsvintgtsk npvyeantsa kyikqdyfgs yipagmdvid gsyvklrtls ldysvpasal
     1021 qktpfgsmsv glygnnlfiw tpsenkfvdp emnstgsgne qgfdfaaqps vrnyginikv
     1081 tf
//
LOCUS       WP_091392262            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091392262
VERSION     WP_091392262.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118786
     Region          26..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqkllllfc siiflstgif aqeklvtgtv kneagdaivs asvkivgsnk gaitdengsf
       61 kigvtaldkl eisainyqtq vvtvgdqtil qivmvaaegs nlsdvvvtal gikrsksnlp
      121 yavqqvggdq ftetrasnfa nalsgqvagl qitqnnnlgg stnvvlrgfk sltgnnqalf
      181 vidgvpidns ntntssqkqg fagfdygnsa advnpddias vtvlkgaaat alygsraang
      241 vilintkkpn kagigvtanf gvttgsmdks tfvhyqdqyg agyydpdvaa thysntdhpa
      301 ffyydvdgdg kndyvapsgd dasfgekfdp slmvfqwysq dpsspyynka tpwvaakngp
      361 stffinpwsn sssvtvsgan ekggfkmgyt rnedkgimvn skiikdllnf gahyklldnl
      421 tvegdinysr irgrgrygng ygdpssiaan frewwetnvd iqdlknayfn nnktnmtwnw
      481 kqigknnkpa ywdnpyfsry enyetdernr yighasvnyq atawlnimgr vsldhydeiq
      541 eertatgsln pdgytrynha fseynydlia tvdkdlgedl nlhallggni rksttssiya
      601 etngglvvpn wfalsnsvnp ieapvetyqp irvngvfaga tldykklisl dlsgrndiss
      661 tlpkgdnsyf ygsasasfvf sellkeagwl nhgklrlnya svgnsapfas lvdvytkptg
      721 ygsiplfslp dtknnadlkp ertnsfeigl nmdmfsnrvg fdvtyynths idqilpvais
      781 datgygfkyv nagdiqnqgf evsvnltpvr nsdfrwdmnl nwtrnrnkvi klfgdnknlq
      841 lggfqggvsv natvgqpygt lrgsdfiyyg deegqtvada igkhvilssg dpaltgsnev
      901 igdvnpdwig ginntfkykn fslaflidik qggdvysidq wygqgtglyk nsvalnangk
      961 svrdpvdegg gilnpgvted gqpnttyavv sgvrglgyna mpnkafvyda syvklrsvsl
     1021 aynfpqkwfd nkaikgatls vfgrnlwiih knlpdadped aassgniqgf qvgsyptyrm
     1081 ygfnlnvrf
//
LOCUS       WP_091392421            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091392421
VERSION     WP_091392421.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107536
     Region          28..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnskrlssrf alclgwllls lagfaqtrtv tgtvtsetge pvpgasvkav gtttgtstda
       61 qgsfalsvpp svtqleisfv gyatqkvsia gkesvtvqlq pssaealdev vvigygqvrk
      121 kdltgsvasi gakdfnkgvi tapdqliqgk tpgvmiinnt gqpggsttvk irgnssirag
      181 nnplfvldgi plsgtsarpg gsggfstdgg npltylnpsd iasidilkda sataiygsrg
      241 angvviittk raksgeptln lgasaglssl lkkpdvldas qfreaiqhyt psdvatadfg
      301 sdvdafdait rkaptqnyyg ditggtengr yrlslgyldq agivrtselk kytanlsssf
      361 kfldnkrlgl dvnllvtqtn enlapidvgv gftgnvisqa lqwnptrply ddngnptyis
      421 pnqinpmtsl aaykdravvn tivasvspyy kitdnleykl iysvtrqtgd rtgryiagmv
      481 dssqvqngma fvgnntetdq qltqtltfnk qlsdafnlna vagyefldyk yywnsesgsg
      541 fsdvgldyyd yllystissr sinshrdpsi qlqsfflras anyldryllt atirrdgstk
      601 fgsnnryanf pslafawnls neaflkgsnv vnqlklrlgw gqtgnsafps gasrprftfg
      661 tqsitqanfg npdlkwessa tlnagldfal fnsrlsgsld yfnkkttdal festiaqpap
      721 psgkiwinlp geisnkgvel sltgniiskk dwgwnltana tyiqndvsgl tgyyttaalr
      781 gqgfsgvlgq rmvngqplnv wylakyagid pttgtsmyma qdgtvgtpat dskydpslnk
      841 fyvgspnpky llgittdvty kkftatfnmn gafghylfnn tmatvlglsn lpsrnignyy
      901 dnpaaneals nsasastryl ekgdymkmsn itlsyrvgni gntiknlnis ltgqnlfvlt
      961 gyngfdpevn tdgsdsdips lgieylpypp artillgvnf sl
//
LOCUS       WP_091392461            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091392461
VERSION     WP_091392461.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122849
     Region          37..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrinnkyil allllmstcl vfgyqqvyaq ggkraivrgk vidantklpl sgatvieidg
       61 ddrtingtst didgnfalrv ndpehnrisg ayinykptvl rikdsanili alqdeesaln
      121 dvqvtayndq vdngtgmkir erdntlstas iqqkeienls spniaaaleg rlpgvnvsvp
      181 tgdpgaglsi qirgtating sgnplivvdg mpysttipsd fnfgtadaeg yaqllniaps
      241 diqditvlkd aaatalwgsq aangvlvint krgktgkpsi sytfrgtysk qpksvplldg
      301 nqystlipee vanaggnpld isankefsfd pldpywyyny snntnwidai tqtgysqdhs
      361 ismtgggqka kyyasvgyfh qdgttigtgl dritakvnld ynvsnririr snftfahlnr
      421 dlnflpsnks ayqirniayn kmpnmsiyey diygnqspny ftpesniqgq ypstynpval
      481 aenakyvqng dritpsfqlq yqmvpkvlla tfdvqfdinn sgahtflpqn atgrplsesi
      541 vneakasdgd aysvttktnf iytpksndrn hqfqallslq tndsksnayn vlttntasse
      601 fdypfngsra tnsaalltst ladvrsigtl lqaqygwldr yilnagvrmd gnsrfgpnnr
      661 ygffpslsar wrlsgenfmk kysgfiddls frasyghags appdktvwqy fntyspysys
      721 ylgesgvyss nveltnlkwq tlvgtnlgfn lwmfknrfri dfevyrnriq dmfyddldip
      781 sytgfssmpa nvgtmdnqgw eallntipyq tknwkigfdl nfasnqniir sisdfyprtn
      841 vesldangky ktflqvnnpf gsfygfkylg vystkdqtva rdaagnqitd pngnllymrf
      901 qypsidyvfq pgdakyadin hdgniddkdv vylgnglpki tggfglnvtf kdrlklitff
      961 dykldydivn aadmattnmy sfdnqstavl grwrnpgdvt nipralykkg ynwlgssryv
     1021 qdasyvrlqa vtlrytfqpk llnklnirsa scyvtvenly twtkykgqnp dvsiignnsp
     1081 faypvdnalt ppsrnvllgi nlsf
//
LOCUS       WP_091392467            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091392467
VERSION     WP_091392467.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117027
     Region          62..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhrtniifkv lpltfftalv fftnvdaqnn vptklnsasv vkdtvfvngv irsaasknai
       61 ggisvsvpgy aaaisddsgy fkiavhdlqs vlylsgdglq dkqvalrgrn kvtvdlfeqg
      121 ynsqyasasl vfgkkpkdyi pysiqafsad nrwgqsvtet pdsylqgkia glnvirhsgt
      181 pgiganmaln ginsfnatnq plivvdgvpf dnneyghslv lgnmynplsd idikdidnit
      241 vikggnstyg tkgangvili ttarsqelat ridfaayggy nflpsnlpvm naddyrimls
      301 ellktkglsa eqiddlpymn dhksaddyyt yhnntdwqrq vlnssynnny ylkvtggdni
      361 akyalslgyl tnggvlknad lnkyqmrfng dlllskklta svnlglvstq qnlmeqggeg
      421 vlsplsiali kapflgvnvr ddngvaspnl sdydtfrvsn pvaisnnmqg knksyrftgt
      481 vkfnyelndn fsiktilglt fdkmqedmfv peagivpdtl qtavafnrsg snmaryssfy
      541 nntalsytkq fnsnhklqvd lgyrvennky eneyghgyns atdefvsvgm gssslrtvgg
      601 sngkwnwmnn ylhgdysikd ryyialnvaa dassrfgkqa pdglslggvk falnpslalg
      661 wlisseqffk nvrfvdnlkl rasfsrvgnd dignysarty yesqnlvgsq givrgnignp
      721 alewettdql nvgldaalfn erlnfsfdyf hnksynviti dqtaeyvgid nivsnnstlg
      781 nnginlalna rlinhkfkwd fginlgkytn kvskfpigal ltdyvgatyi tkagaaanqf
      841 ygfktqgvfs sdaeaqasgl qyedaagniv sfaggdvkfy dkdgnhiind adrvvignpn
      901 ptlfggisnd fswkhwtlnt lftfsqgndi ynytrmqles msnynnqsda vnnrwrydgq
      961 qtsvpraawg dpagnarfsd rwiedgsylr lrtvtlsydi pvktatlkyv riyltgnnlf
     1021 twtkylgydp efsstnslyg qgvdlglapv yktvqagvrl gf
//
LOCUS       WP_091392695            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            noncentrifugens].
ACCESSION   WP_091392695
VERSION     WP_091392695.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium noncentrifugens
  ORGANISM  Flavobacterium noncentrifugens
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Flavobacterium noncentrifugens"
                     /db_xref="taxon:1128970"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116049
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngfla lllvlitqit faqdiavtgv vqdqagmpvp ganvlvkgts ngvqtdfdgk
       61 fkisaakgqv lvfsflgmkt qempasanmt vkladdsvql egvvvtalgi trdkkslgya
      121 tqkvdgsevn vvpntnfvnn lsgkvaglqv ktnnnlggst nvvirgyksi gfnnqalfvi
      181 dgipvdnsnt nsrnqetgry gydygnaaad inpadiesin vlkgaaatal ygsraangai
      241 mittkkgkeg tgfgvsfess vsvgsidkdt fakyqkeygq gyfgdlfrts rdingdgvad
      301 tsvrtgddas fgpkfdgqlv yqwdsftpes pyyrtarpwv aakndpikff qtpfthsntv
      361 rfdggndkga fslsytnlsa tglmpnseqn knsflgnasy klndkltasf manyintrtl
      421 grngtgyngn lvsgfrqwwa tnvdvkelrd iynatgknys wnptsntnlt paywnnpyfe
      481 rfesyqndtr nrilantsln ykllkwldvt grltvdnyse vqeerlavgs yggnsfgtaq
      541 tnessgyqrf nrnysefnyd lmfnynwdit ekfnlkgvag vnirrqkins vmvstsggly
      601 vpnvyslans vnlledpiqa eqnrgvdgyy isasfgyddf lfldatarkd ysstlpsrdn
      661 gyfypsvsgs lvfsnlvkad wlslgkvrig yaevgndapi ysiydtyqkp akfgttlysv
      721 nstknnpalk seltrsleag lelqffkkrv gldlsvyktn tvnqivdlpv seasgytrvf
      781 knvgdvqnrg ieatlsltpv ktesfswdit anwavnenkv velapgidny qlatyqggvs
      841 vnaqvgkpyg iiqgsdyvyv ngqrvvdqtt gkyvisatnd kdlgtftpkw tgglnnrlty
      901 knvtmsflid vqkggkvfsl drwygegtgi ysntvgnirn pegvvlagvt pegapntvav
      961 dqttgldgyl gylgsansdy vydasyvklr evtlgytftk kalnntfqdl yiglsgtnlw
     1021 iidknlpdad pesglgsgnl qgfqsgvlpt trtfalnlka kf
//
LOCUS       WP_091393896            1119 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091393896
VERSION     WP_091393896.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1119
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122977
     Region          27..1118
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqhvllkkml lvisvfltls syaqsntysg svldentgqn legatvtnqs nhaavitdaq
       61 gsftingnks dsliisyigy gsttialkdn lrlfirltkn dnsqldevvv vgygtqkrke
      121 fagavtkvnp lgfehspnsn vatalqgtvp gimvrqstga pgaspnivfr ggtgfdgsgd
      181 plivvdgvil nslygismdd vesmdvlkda astaiygara angvilittk kgkkgrtqvn
      241 ysikqsinkp rsiaddylna aqyihmnrlg lrsryiadsi tgsnpqadkn qlngawgwaf
      301 gstntspvgl yttqlvtdln rdklgeagwk llldpnpfnp glmdsilyke sstqereaml
      361 mrqsnsteqs lsfsgadeng sfslnlnsvk dngtiieswm krinvnfngs lnigknlniq
      421 lmtnayrttv gspysdpgda fgtaatgglm qrflgvaptv ryyndtsgam lpgpndltlg
      481 npnywknini nsvnqerymg slkltynilp ylkfiangsg ymlyqnnnaf ttsyqagsgg
      541 ainttrpssf snykdmqyty ngflqfdknf nghnisimag geyydykryt fsgagsgast
      601 dlipwvsaan tpyvqngviv ngqsassafa yweriasaig rvsysykdry faqgilrldg
      661 ssrldpsnyy glfpgisagw nmqnenffkn sklseyisti kprisygeng nlqyfgsnyy
      721 ptaqvyanag tyngqgasya ssyinpgvrw ertnsvnygv dlgilhdrvt lvadyfvrnv
      781 fdklaslgis swtgfssyst nlsqlrnkgi elslnaklvl pkrpegffld fganfysvkn
      841 yavklpyngl pgnrqgtiqv wdpnhpgqlm qvgglvegkr igtdevwvpk wdgiyrtqae
      901 ldadanvvns flpytgaigq kfkqlgdakw hqvyqndtid srqyvfagrt tpkasgsfff
      961 ntgykafrly aafdyaygfi ilnqsrirgl sqvqgsqnst kevldtwtee npdaslprfy
     1021 wanqgrnygi ngsgdnvaan lwekgdylml revtlsysfp kevlsqwfnn rikglelslt
     1081 gnnlsyltsy tgifpevggi dngryplprk itfganitl
//
LOCUS       WP_091394124            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091394124
VERSION     WP_091394124.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117367
     Region          30..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkiifnrl siwitligic ltsnimaqqq tvsgqvqdss gaalvgvtvq lagtkqaslt
       61 dktgtfsika qtgdvlvfth igyistqitv gsqlnyqitl qasadnnlkd vvvtamdikr
      121 nsrelgysvq tikgddiqqt qrenfvnalq graagvtinp tsgqagassq ivlrgfnsas
      181 lnnqplfvvd giiidnttfn etsnggsgig laddrpnrts dyanrisdin psdiasitil
      241 kgpeatalyg sqassgaiii ttkkpgmngq vhvsydnsfr fnkitrfpev ldeygqgkng
      301 eatnipseaf lyfgpayaag tqkydnissf frtgfantqn vaadmgtknv gfrltgsyfn
      361 nsgvipnnky rrynfklsnn tklwdgklvi spsisyinse nlkptrgagg yildlyawpt
      421 idnasnyqda egnkrllyad dpnsevlnnp ffsayrnygq dnvsrwiatl gidlkpvdwl
      481 tiagrfgydt ydqdgysltd pqsstltaas qgflsnyyln ykgynhtita tatkkvgkfg
      541 lramvgtmwq dyqtreyala gsqlldadnk lshstdssni gmvssrlarn keglpnesit
      601 rqvayfgeaa vsynnvlfls ythrfeqasv fapdkrsyny pgisfsails diipgikgnf
      661 lnylklrasr aqtarlmppy lnqavfvdny assdipaysy syynnnpnlv pekqktyemg
      721 letrlldnri sleaayynth nldqisvgyr asygtgyiln tqnatesrnq gieitmninp
      781 vrkkdfnwdi efnfnhmwsk vldipasiad kndyyisdtw iylntrggfv rgyptteltg
      841 ysfernnngq ilispetgmp vvntsfspig drnpdftlgt nntfryknwq lsflwdlrvg
      901 gdiynateqy ltymgksqlt kdrmkstvie gvlqdgnent anptkntisf ipnevastyy
      961 setkgfpdev fiqkdinafr lrdvtltyqi pqtlidkwkv fkslsffftg ndlvlftnyk
     1021 gadpnvsgtt agsvgvggfg mdygnvaapv synfglkanf
//
LOCUS       WP_091394678            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091394678
VERSION     WP_091394678.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123398
     Region          26..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msrqnmkfvf lflltlccta lfaqertvng vvvdgksgeh lpgaiisakg rpsnvstkyd
       61 gtfsikllpt dsvlvvsfig ykrvqqkvgs edfitirlds tvsadlndvv vvgygtqnkr
      121 ditgsmatvn lkqiedmpaa sisemlrgqv pglnvsggaq rpgematlsi rqqfnwgkdg
      181 gneaplivid dvlqvdpqtg lptldrfnql dlsevesitv lrdasaaiyg srasqgvviv
      241 ktkrgqigap kvtysgkfer ndavshskvm narqygeysn sfnkalgrsd dyqysadeln
      301 mmdtlnydwl gndwraantm qhsldisggs dnatyfmgas yytqganlgk qdfdrwtyrg
      361 gadvklmsgl hlgatiaasn tnveksftki nfsdgyangg eqndysvllh mpkyipwiyn
      421 vdgqdvyvsp plgsnragnv kgnnslsnwn yyallnngsk ttnknfnynv nfslaydvpf
      481 iqglsfklny glsqaatnte qimmpqmlyq attiasagmh lfsetedgkf katnntansr
      541 vtydnttsks eqsnffinyt rsfgdhnita masvekstne ledryqiydn ptagiyngts
      601 vsagtlndgn titykyesgs lsylgrasyn ykhkylfdfv frtdastvfa penywgffpg
      661 vsagwvisde pffknniqwm dflkfrtswg itgnnnikaw kwlqvytaqt dkgfgfgsdg
      721 glyttgmtpg vtpnrdvhwd rtlqrnfgld mdflknrlsv tfdqyfnsts dmltdmskai
      781 ntpisvggaf aeqnyaavna wgselsitwk dhvgdfsysi gvntglgnyk vtkyydqafa
      841 ypsesttrra mgnygivpvw gfktwkqtsg gdgmlrtdad idnywnylsq naassgvdga
      901 apnflgitdk sglkkgmlvy edvagdldan sktiagpngr ieadedyvkl kksnrsygls
      961 tninlgwksl slymqvatsw ggtrfldyvk qgtsstnamw gqpiylvdmy dedtnpngky
     1021 pniayydnfg gsqsdffmlp tfrmvirtls lgytmptklv nkarlksarf flsgnnlwdl
     1081 ynpypkkfrn mydaadvgyp tlrtwalgvn igf
//
LOCUS       WP_091395067            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            noncentrifugens].
ACCESSION   WP_091395067
VERSION     WP_091395067.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium noncentrifugens
  ORGANISM  Flavobacterium noncentrifugens
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Flavobacterium noncentrifugens"
                     /db_xref="taxon:1128970"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110024
     Region          48..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlslfrvw lilycvlscf lfnqafatsh tafstqqqqt itgtvtynnm pmtgvtitvk
       61 sknttvlsge dgkfsvaang tdtlifeylg fktqifainn ktnltielee dvndlkevtv
      121 nagyytvket ertgsiskit akdiekqpvt nllaamqgrm agvnitqntg iagggfdiei
      181 rgqnslrsgg nnplyvidgv pyasdligsr vtspempmpt splnslnpgd iesievlrda
      241 dataiygsrg angvvlvttk kgkagktkft anvssgfgqv trfrklmdtq qylqmrkeaf
      301 anegiteyps watdingawp ldrdtdwqet laggnagftt vqgsvsggsd ntqflvsgny
      361 srettvfpgd frytkanvls tishksenkk ftlgftagyt ardnkqpsid fmqeavglap
      421 napalydddg nlnwqdntfn nplrylqtea gaktydllan aqlgysilen lqlrssfgft
      481 dlrhketsal pstmfapstg htpsssslfa ttanrqswii epqldyniai gkaklqalag
      541 atfqqqdasq mtqqfygfas nallynpgsa srittlssge svykyqaffg rvnfnfaqry
      601 ivnltgrrdg ssrfgpgnrf anfgavgaaw vfsneklvse klpflsmgkl rasygtsgnd
      661 qigdyqyldt ystsgysygv sglqptrlfn pdfawesnkk leaalelgfl ndristsvaw
      721 yrnrssnqlv giplpgttgf selqanldae vensgwevtl rtvniktesf switsinytt
      781 aknkllsfpd lesssyanql vigqplnivk syhytgldpq tglytfedvn gdgriseped
      841 ktaiknlnpq yfggvqnqfr ygnlqldflf qfvkqlnyne yygtaapgnm mnqpasavsh
      901 wqqagdtgpy qvyatdlnda aittnsqfgs sdaaisdgsy irlknislsy dlpvkwtrgi
      961 scrlsvqgqn mltvtsfkga dpefkslgyl pplktittsl qltf
//
LOCUS       WP_091395475            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091395475
VERSION     WP_091395475.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113127
     Region          28..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklliiliiy macafgavgv kaqsvleiki sakvydqnqn pianaliqsq eradvhtltd
       61 sngafslmae pgenifvsap gftslylpas kqlniiklnp tsldtidvqa pfstsrkedl
      121 fgdvtvvnqq eimaknytty sldglvayvp gyngnsiwgm gsylllvdgv prdannvlpt
      181 eidqiavlkg veavalygsk gakgvinitt krgqafnkkl ivradmgtyv pvsypkylgs
      241 aeymslynea rsndslpaly deatiyhyas neneyrypnv dyysdsylkr aynrydatae
      301 isggndrary ytnmgfyteg slldfgmake nrnsrfnlrg nvdikinrfi ngridatatf
      361 ydgrgvnady wsaaatvrpn rftplvpidm iesndeasll lvqnsdhvid gkyllggtql
      421 dqtntmatiy aggynkyisr qfqfssgida dlkdilpglk fksnfavdya tayslsynyd
      481 yatyepiwnn yagqdlissl nkygndatsg tqnvsnswyr qtiafyglfs ydqtfgtknn
      541 vsseliangy qqsesevyhr vsnanlglha gynydhkyyi dfkgayihsa klpenhreal
      601 sptlsiawri skepfmhnkt gvvndlkita sagilntdid isdyymyqgy ytvagswygw
      661 kdgtgfqate srrgnnpnms fprrkeinig feglffnssl qlsshffrnt idgniiqass
      721 lfpsyftsyw pvssfipyin ydrdqrtgvd fgldwhklig kldvdfglng tyyttkatrr
      781 aevyedayqy rqgksldgiw glqnlgffes qedidnsptq sfgevhpgdi kykdqngdgv
      841 insqdevflg kggwfgapft igmnltvkyk kltlfmygtg sygaygvknn syywvygdgk
      901 ysevvrnrwt eetkatatyp rlttnssdnn frtsdfwmyk anrfdlskvq lsydmtgllk
      961 skgfintlgv yvsganllti skhkdimqln igsapqtrfy nigvkanf
//
LOCUS       WP_091398363            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091398363
VERSION     WP_091398363.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119007
     Region          26..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msksilfifl clnmynmvng qdltikvkdv stgqpipgvs lelrnsgihr mtddngtali
       61 pmkfkedtlv aqmvgykilf rkidstsphn lieyleatdy slenvtvqtg yqhiskerat
      121 gsyeyldski lnqqtgsnil drlngvannv vfdndgnrqq pitirglsti nglrsplivv
      181 dnftyegsvs ninpndvesv tvlkdaaats iwgvragngv ivittkkgsq sgkqsvsfna
      241 dmitsgkpnl fylrpiassd lidveqmlfe kgyyndkesa ssfpalspvv ellikkrdgl
      301 isavdfdqqi ndlrlhdvrn dlekymyrkp ftqqyalnfs ggtqnvsyyf sggydrnmdn
      361 lgginnrttl rselsirlap rlsvnssvai nlissktgah gysyltnntg gpiytytrla
      421 dnlgqplsfa knyrqsfidt agggklldwn yyplqdykhd ftktfisdiv ansswkysin
      481 kmlslnfyyq yerqstqnkn lsdiqsfaar dminlftqfd afgelvynvp nggilnrsda
      541 tiesnngrlq vnfdhswgns dltaiagaei rqvhtfsgsa ttygydddfl syksvdyvdy
      601 fttylggyqn iadgtsfadr tnrylsgyin aaysykgrys vsgsmrkdqs nlfgvkandk
      661 giplwsggla welskegfyn fnaipylkfr atygfsgnvd psrsavtteq yldlpasysg
      721 fqqarilqyg npdlrwekia mtniavdfas rnhtisgsfe yylkhgtdly gitpidptag
      781 isdgtsimkn vasmigrgwe lslttrnlkg elgwhttllf shsvskteay ylnpalpssf
      841 isngntinpm ngfdlysiis ykwggldpmt gdpigylnge kskdyqaiyn akdkddliyd
      901 gsaipkytga lrntfdwkgf eldvnitsaf gfyfrrssid ygglfsmdag nadyagrwqk
      961 pgdekhtnip smiypdnsyr dlfylysean vekgdyiriq yinltytfpk vskrpnilns
     1021 lqiylnaanl gllwrsndvg idpqyidvtp qpktytigik cnf
//
LOCUS       WP_091398503            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091398503
VERSION     WP_091398503.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120232
     Region          23..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnitllila lilsksitaq nsfvfkgnvt ntvsdkpien vsihsiengs tvnsdslgnf
       61 sikvkrtdtl llshigfqtk kiitypntpf lqiglvpknn sledvtintg yqqlkpnevn
      121 gsyevidnnk lnqqtgmkil drlngvtnsl lfnvgkhnnn sqnttgitir glstingpld
      181 plividnfiy dgdlnninpn dvqsitilkd aaaasiwgar agngvivitt kkgnfnsklq
      241 idfnsniiit nkpdlyynpq isssdyidfe qmlfnkgyyn sqftnrshpa ispavqifqd
      301 kkdgiisaed satkinalkk idnreqynky yykrgltkqy ainlrggssn lawllsgtfd
      361 esisnlrney kkanlrfdnr ykpisqlsid vgvyytnsns ksgladynst sqinskqiip
      421 ylsligengq siavpsyynq rfldtlgqnr llswnyyple eykhsysttn tedilahikl
      481 eykicqglnl simyqyekqn sevnrisdts syfarnlins fsqidrntgi inyivplggi
      541 lnksqsslns ytfrgqlnyd rsfkrhrfsa iggyeirdsw snnsamtlyg yngdpltavs
      601 nlnyatyypn lvtkgnsmip fssgigstdn rfvslfanfs ysyqnkytis gslrrdgsni
      661 fgakendkwk plwstgigwn lskekfysld wlpfvrvsat ygvsgnvdls ksalpvgiyy
      721 qgmlgtlrmp tmtitkinnp elswersyqt nfkiafsskk niingsleyy lkkgtnlyap
      781 tpydytawga sstitsnaad mkgrgidisi htkninrafs wttdfiynyn kstttkyfat
      841 tatsvssflg ggniitpvig kplyaiaayr fggldasgnp mgyiddtlts dynslaknai
      901 geglkggtit yigsatptty gsimnsfayk gfslsfnivy kfgyylwkpt inyyalavng
      961 ignpdyknrw qnpgdeatts ipsfsypldq krdafyngsd invikgdhir lqfinlsysf
     1021 lndkalrlpf nglqlyfnas nigiiwrsnk yevdpdvtng ipapktytig ikanf
//
LOCUS       WP_091398882            1152 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091398882
VERSION     WP_091398882.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1152)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1152)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1152)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1152
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1152
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126361
     Region          31..1150
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkinalcrr tlliflllsf vrlevsaqqn kvhgliknqe gtvvsgatvq vkgssryavs
       61 dnngnfdiqa sigdslvvth igldpitvai ssediqivmq iseaatagtd vivtalgikr
      121 eaksigysvq kvsgdditka sapdlasglm gkaaglniss sngvqgnsqr ivirgnnsil
      181 gsnqplivvd giqvqndpig gqsastnstd lvspkdwgsf lnslnsddie ditvlkgasa
      241 aalygargsn gvilittkkg kskpglgidy nfstyatdpy qyqdlqnsyg ygganamwsa
      301 nldfpkttdg qlrypgnypw dgtpagdqye iagpipggys twdvfswygp aaswghkldg
      361 teiiwwdgvk rkwdpqpdnr safyrtghtt thnvafsnag dwgsfrvayt rqdnsaiiqn
      421 sdysqntfnf ggtfkisdkl haevtgtytn ynrlnvpdia ndngwsqfti ynmsrdykpl
      481 efdsyknadg sknvftnssa fgfypynnnw aqdlfwhvfe qnqnltrnql lgsvklsadl
      541 lpwlnitgrt sinyantnie skyspidagg vegqygmesi qnkdinlelf ttihkdnflt
      601 sglnaslmvg nsalksrsyd nsawnsgepg atygrastsp wsvpfkyfls nttatgmtpp
      661 tevwndynin slfgivnlsy qdylylqvsg rndwsstlpv etssyffpsa slsfvftqai
      721 ksmknikwld ygklrvsaag sangtdpyls tytyssdvvs nylngtapts fgglpvrgyk
      781 tvlppagflv pqrnssyelg leasmlknrl svdftyyktk atsqilqgnl awssgaskvt
      841 fntgelsnqg fefiirgtav ksrnfswdlt lngahnqnkv islaegidky plqdlwgvsg
      901 vemyvkagen ygtiygydyt ylngkkvvkq vfdksdptkv vgtqyvttqd lvpignatpk
      961 ltgglsnnfr yknfslyflt dfklggqiws gdysaamgtg lspetlkere ggglpytypd
     1021 gttanhgvil dgvladgtpn tdvvhylwky agqyeawsnv pmprsnaift nswvklrevt
     1081 ltysvpkdwi rksrviqgld isligrnlfy fytslpdhln peaingigng qgvqwaeypw
     1141 trdygfsvkv qf
//
LOCUS       WP_091399646            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091399646
VERSION     WP_091399646.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113943
     Region          26..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhryvftll liliglhlqa qlkqpiqgtv qsetgqplsg vsirvlggka tlstnlgnfn
       61 ldanvgdtls ftyigyestq lvisslntpi kvtlhqaage lsevvvtalg iskekkslgy
      121 avqelkseql nttqtpnlvn dlsgkiagvr vtnsqgdmgs sriiirgets iagdnqplfi
      181 vdgvpvdnsq lgaggsrdys naiadlnsed iesvsvlkgp naaalygsra ahgviliktk
      241 agkkrkglgi tlnsnntfss llslpdyqnv fgqggngefs yvdgngggln dnvdeswgpr
      301 megqlipqfg sngeavpfva hpdnvkdffk tgfstnnsis iadagdkfsy rlgfndghqt
      361 gvipnsklnk rnislntnfk itdklslsav anylitaapn lpgvggkrat stmlqftwfg
      421 rqvdmqslkd syfttgspdn wnnayypnpy fgayentveq rrdrligdig ltyeitqglt
      481 ahfhsgtdyy ndrrklkiay gtsgtpygsy eeiayslnen nteatlnydh qlnsdfsvni
      541 laggnirnkt yeendqkapr lavggiytld nsrdplvssn yyshlkvysl ygsaqigfrn
      601 yafinatarn dwsstlpsdn lsyfypsing tlvftdllki ssntlsygki rggwakvgad
      661 tdpyqlynty gfslfgsnpl lstsgiqmns nirsesttst elgldlgffh srttlgisly
      721 ntnsfnqilk vditptsgyt qqllnagkin nkgleialgv tpvrqqnlsw dfglnfalnk
      781 sevkylddqg elenytlgtd gtvqvvaavg ktygtiigta yqrdangqiv isasglpqtd
      841 pslkdlghft pdwtggftnt lrykswgltf lidasvggsi ysgtnstgqy tgvlastlpg
      901 rgaefggisy yypgddkkql pvaasgsapn geklyddgii akgntsdgda nsqiipasly
      961 yktissvdeq yvydasyvkf reinlsyklp aawlnrmgiq gasvalvgrn lffiykkapn
     1021 idpetafstg naqgledltl ptsrsygvnl tvqf
//
LOCUS       WP_091400033            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            rhizosphaerae].
ACCESSION   WP_091400033
VERSION     WP_091400033.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus rhizosphaerae
  ORGANISM  Arachidicoccus rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Arachidicoccus rhizosphaerae"
                     /db_xref="taxon:551991"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119459
     Region          37..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mstkllsnff kqriqlallp ilflmffalp awsqqqrtif gtvhsltgdp lvgvsvvivg
       61 eregtqtder gqfsisvkpe arlvithvgy dkkeviakdg mdiqlvanss dlsqvmvvgy
      121 gtqsrkkvtg aistvngddi kntpavsfda mlqgripgvt vqnssgepgs ksnivirgst
      181 nmdygnlngg ntqplyiidg viydlnnmqg sydlanplsv idpnsiesie vlkdasaaai
      241 ygarggngvi ivktrrsqak hpmvtlnvyg gattgprlid vitgnaersl klgllndqlp
      301 ytdiyngsip iqltdslnta fnndvdwqgm mlrknayvnn eeltvsgsfd nkntyrfgls
      361 hyneqgavrg yqveriapnl dlqlnpvakl svglslqmsk ekrqhggnis gnpyyfstws
      421 fptsfaylsd etvalyngta nrfddnnifi ynanlrltdt ltkdlhlttt mglnsyqdky
      481 ayfspvelng vqntaydisa nnpnwtwetf aqydkhfkgn nltlvggfsa yqakqyyaym
      541 daaginvsgi ytlqtvppgs nlyaystiqt kttqsyygrl nydynskylf tasfrrdass
      601 iysqdyrwgt fyalsggwnv sdekffeplk ktinslklra sygvtgqdpg swyakyqqly
      661 adasflgatt gsvggssdws yltgtpstyn gttvvtpfpy ndnfasssyk sssevrweky
      721 pqldlgidws mfnnrinfvl dwyqkdaidk ylwavpaest tgyayysgny anvrnqglel
      781 ainstnmspk aafqwntnfn isfnkgwvtk lpnegkdmlf geswwyktls mgeplftyrd
      841 yvtdgvyate ddvptdpitg nkmtyfgatv hagdskiidq ngdyninldd kvntgksmmp
      901 tvtggitntf sykgfslsvf anyayrnyli ngtmsdalng sgyaswgava gpaglysqil
      961 nqfwmkngdq ttyprlvygs gsssldpwnv ardyflykgg yfkiqqirlg ytlpskfvqr
     1021 lhmrsvnvys vfdnvhtfkq skglvdptvf dyttgssnat yptslkftlg lylnf
//
LOCUS       WP_091407156            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            amphilecti].
ACCESSION   WP_091407156
VERSION     WP_091407156.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina amphilecti
  ORGANISM  Aquimarina amphilecti
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Aquimarina amphilecti"
                     /db_xref="taxon:1038014"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112908
     Region          23..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqkkltlis flflvigvla qekkisgiit davnntplpg vnvivkgtst gaqtdfdgay
       61 tinastgdil vfsyigfktv eksigssnti nidleedaeq ledvvitafg irqeskklgy
      121 svqqlkseti tqtadpnigs airgklagvn insnsggigs svsinirgis slgannqpli
      181 vldgviiddn qggqgdfasg ldygntlsnl npndienisl lkggnataly gfrgingvlv
      241 ittkkgrsdk ptveinssit assilvspkf qneygqglfd tstnqlvydi tngssfgprl
      301 dgtqrerfdg vgtasysand ndfkdffrsg fsflnsvavs qgtekfdyrf sysrlddesi
      361 vpgsnlkrqn fsvkagasit swlkilgkvd yihqdarnrp eltggqtnit ralslrprni
      421 sntllrdnfl esdgtpnnwa gafitnpyyt sntllnedev dryislleln idiapglkgl
      481 mrlsqdhits sqqifnpfga fdiagngrfs dtnstartnn ydliftyntd igsnfnlgat
      541 lgfshsdvsf kslqaigetf llpnffslnn fesisvvpgn aknssnsifg smtigfnnyl
      601 faeftarndw sstlpindas ffypsvglsf vatdafpslq dneilsnlkl rgsfaqtgna
      661 tgafslvnty nvssnlfngq rffffgnaee gagtgpelnn pdlvpeisna lefgldarfi
      721 nnriglsaty ytirtedqil rltlppssga anqiinaglv tnkglelsld adiiktdnfk
      781 wsttvnfttn enkveelaqg vdrnilirqf ndvvqvaaev gssaqglfgt tfskddngnv
      841 iydtnglpvi nteisqigdv apdaflnwgn sfsykqfsls flfdarfggd vfslseiqrh
      901 tqgtaietle greffsggqg islpqnavid gtldpnvqqr gvnpqtywgr vgqisenwvy
      961 dgsfikfrel tfgytfpert ikglhlsnls isyvgrnlai lhsntdnfdp etgfntsfgg
     1021 veffgipsas shglrvnltf
//
LOCUS       WP_091408115            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            amphilecti].
ACCESSION   WP_091408115
VERSION     WP_091408115.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina amphilecti
  ORGANISM  Aquimarina amphilecti
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Aquimarina amphilecti"
                     /db_xref="taxon:1038014"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108096
     Region          27..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqtqiskg lllflfffpv vlfaqetitg kvinentgeg vsfinvvedg tsngtasdid
       61 gnfsitvnsl pvtlrvfsig fttklvtven agaitvqvae slealdeivv tglgssikra
      121 nlanavstvs seelvgntgq ttvdgalygk vtgvnitass gapgggtalr lrgissingn
      181 nqplfivdgv yinnveipsg lrfasganrg neenagnrla didpndieni eilkgasaaa
      241 iygtranagv viittkkgkg gktkirfsqd tginviqnrl glrpwtatsv fdafftpnpd
      301 dpaaearsra aaeaevaafn naiqngglid yedeiygnvg fisetklsas ggndktrfyi
      361 ggsyrdeegi iqktgfdrfs irsnidhkis difdvslssn yvrsnssrsf tgneneggls
      421 fgytlaftrp wnnlfpdadg nypnnpnypg npifvrdqak nedsnnrfiq gvkfttkllt
      481 kendrvkfvv nggidylane tyvyvpethq aqvgnqegfv aegrnnftqf nllafavwdh
      541 tafdgnlnlt tqggvsyleq qanlvnsrgs nlfggqtsvd qsvnqvidqt rsnqkdfgyf
      601 aqvegnykdq iigtlgyrld kstlngdvnk fygfpkasla invanfdfwq fepinqlkir
      661 taygetgssa afgsaftsln pnniggnggl gvgtrgdrdi epetsaefev gldlgildsr
      721 isfeasyynr kvsdlilsrn vpassgftte ttnladlvnq glelavrgdv yrsdnffwnt
      781 giqfyfnrse vtrldvpafa qpgagfgtgl gtffieegqp vtqivgnidp dgdgpleasl
      841 kqvgnvepdf qmafnnqftl fkqidvsfll qwkqggenln lsrfltdlgq tspdletpeg
      901 qarlgtaana erfvedagyv rlreasiyyr fpsniieglf gevvegiklg vsgrnlftit
      961 dyssydpevs vnggaglssg ievtpfpssq qfyfhlnvnf
//
LOCUS       WP_091408924            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            amphilecti].
ACCESSION   WP_091408924
VERSION     WP_091408924.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina amphilecti
  ORGANISM  Aquimarina amphilecti
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Aquimarina amphilecti"
                     /db_xref="taxon:1038014"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116584
     Region          25..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myfkkiitvf livlshctll aqdsitlegt vtsredgipi pgvnvlilks ntgtttdfdg
       61 lyqlkvkkgd vvsfsftgkk titvaidnqt rldialeeea seleqvvvig ygvqkksslt
      121 asvsklentn ldelpysdvs nsikgkiagv qirnttgnvg depeiivrgi gsislssapl
      181 vvvdgfpfdd glqfinpsti esievlkdas staiygsrga ngvilittke gkaektsfef
      241 kslsgfkqaa rridildaie fsdldrsrdq lvenfnaqqe nrepnfvnyd nvqigkrtia
      301 qniggptnwq dealrnpari enyqlnvygg ssrtnylisa nyiyneglrk dndlerlnls
      361 arlksklsdn lsfdlkinps ytltrrssin ftdtgryetw ipvrhnqyts dltgqpvgsf
      421 ahalhfrnln fdyvnpttgl tentgniesl wtssnfnpis rqeasrrnrf eyrllangsv
      481 kwkiaqgltl rsslggyvry rtgeeyfgsa gdrdgetegi ladqltvkyi nentlnynrd
      541 fnghdlgill gityentter fsnlritnfd detittlngg tiidlnntft lkdktilssy
      601 lgrinyaykd rylisvagra dgfnkfgknn kygffpsvsv gwnvanenfw rnsigntinn
      661 lklrsswgis gsapalfdfl aptivdfany slgntggvtt gqgevdflqg npditwetnt
      721 efnngidlgl fngavnltvd yyyklsekll lrqqisnstg fdeqwnnigk vqnsgwefdl
      781 stnlgkgklk wqgsanisfn enklisfggs eriinngert dqyitrvgep yiqfygyrtd
      841 gifqnaddla nspsgiadav gglkrvdvng dgiineddrt vigdpfpdfi wgftntftyg
      901 nldlnfsfqg sqggevvwge afynevaryg ttyaedqwfn enipasrpgi rigvpwletd
      961 yavqdasyis lrevvlgysi pthsvnkmgl ekmriyisgq nlwysaaddy lgnnpegttd
     1021 rnnvlirgyq rgvtpvqrql algldinf
//
LOCUS       WP_091409692            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            amphilecti].
ACCESSION   WP_091409692
VERSION     WP_091409692.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina amphilecti
  ORGANISM  Aquimarina amphilecti
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Aquimarina amphilecti"
                     /db_xref="taxon:1038014"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110489
     Region          25..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksmilkklm fllvfisgnm mfaqitvtgv tsdangpipg vnvlvrgttn gaisdfdgnf
       61 tlnnvaedat lifsyvgfqt kavsvggktv invtmtedaa eleavvvigy gtqsikdatg
      121 avavvtsedf nqgsivspeq liqgktagvq itqasgepga gvalrirgtt svrsnnnplf
      181 vvdgvplagd dtaaggsdlg lgtssarnpl nfinpndies vsilkdasat aiygsrgang
      241 vviittkagr gapkgvfeys sslsiskpae efdllnreqy laaidqfggn vsaqdfgant
      301 dwqdeitrqs esinhslsys hnyqngnvra sfgygkqfgv vkksslerit grinathrff
      361 nnklklnlqg tlsrvndeap pitnnagfqg dllgaaysan ptwpaqtgfv pggsninpla
      421 llnfsqnetk tnrylvnfsa eyaitpelsa kvnlgydnse stainvlsgk itgfnngapg
      481 ngrgtlndid venrllevtl nyekefgnsk lsalagfsyq dfgregrtvq gfgfgttdld
      541 qmgrsleasa nliessiegs yqqygvapng sfvnrlfpdi vqgevlnaps tpvtsvlgdt
      601 fdftdelqsy fvrgiytiad kyiltatvra dgssrfgpnn rygyfpsgaf awkldqedfi
      661 gesfstlklr vgygitgnqd glgfgnftir rrfsaggiaq dgvinapgts qvsfvnddlk
      721 weetsqanvg idfgffgdrl tgtldfyhkd tkdlllsaan aqptpqpfsf tnidgnvinq
      781 gvefainydi iqqdelnwnf gfniaynkne lqnfdgqiqs gqisgqgltg afaqllaedq
      841 plfsyylref agfdangqsi ypngdvqefv gksalpdinv gistsfeykn wdasvffagq
      901 yghyiynnta nafftagsin ggrnvttdvl tngesasnap dvstrflekg dflrlqsasi
      961 gynwplsgeg vfkslrlfan gqnlfvitdy sgldpevnvs aplngiptag idytafprpr
     1021 tytfginatf
//
LOCUS       WP_091419505             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. OV608].
ACCESSION   WP_091419505
VERSION     WP_091419505.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. OV608
  ORGANISM  Arthrobacter sp. OV608
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Arthrobacter sp. OV608"
                     /db_xref="taxon:1882768"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39860
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiprerr egerrvaatp esvkqlvalg vdvlveagag daaghadtay nqagaqvvpe
       61 ldlaqldvla hvrpldpntv rslkrgavta glgspsselp tvealtdagv tafalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplymtaa gtvpparvlv lgagvaglqa
      181 igtakrlgar vfandirpas adevasmggt firldletae aaggyarqls sdagtrqrql
      241 laphvaqadv littaavpgr rapllvttem vqgmrpgsvv vdlaaesggn vegvvpgqdi
      301 pvptadgsgh vtlvglkdap samasdasrl yaknvanlla lmikdgalal dfddevlaga
      361 clahdgavrh qptaellaar agsrregvl
//
LOCUS       WP_091411352            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            amphilecti].
ACCESSION   WP_091411352
VERSION     WP_091411352.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina amphilecti
  ORGANISM  Aquimarina amphilecti
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Aquimarina amphilecti"
                     /db_xref="taxon:1038014"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116095
     Region          25..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfrgilt lllafvvqlt faqektisgn vtdnsglplp gvnivvkgts kgtqsdfdgn
       61 ytiqvnrgav lsfsylgftt kevvvgdnda isvqltedaa tleevvvtaq gikrerkslg
      121 yaistvasdd iqeqssadlg rilsgeaagl nitatngtag sgtniiirgl stvsgsnqpl
      181 fivdgvpfsn ntnqqnaffd nvtessrfld idpnniesvn vlkglsasvl ygqegrngvi
      241 littktgsgk tsnkkfevtf sqslfaeeav lpdyqdeygg gfhqnfgfff snwgpsfnrd
      301 isgnslyrsg gpgntfvanp lsqladqtlv tgfedlaase yayrpydsvd qffktgfisn
      361 tsigmtggne nasfsanysy fdqdsftpgn qltrnnigfg gkaklsnklt fqgtanytis
      421 rlktppisas agsgtigggs svfgdvlytp rsvdlfglpf qaqdgrsvyy rsgndiqnpl
      481 wtianakvtq etdnifgsas ltynfndnys ltyraglnty tefntngqnk ggvdgdvtgf
      541 yrtiqvrnsi fdnslilngy eqlseslglt figglntrrn tyqqegtyst qqlafgvlrh
      601 ynfvnqstvd vngqnidfet edntigvyad lsldyknylf fngtvrndwf stleqennsi
      661 fypgasvsli atdaipglqg dmfnylkarv aygesagapg afstrnslal nsrafvdaqg
      721 nvissnsvsn rlgnqdlkpe rfqefevgie trfinnrvgl nvslfkrnte dlitdqaldp
      781 gngftvkrvn agksenegie vdfditpwkt enfkwlingn fyadenvite lptdqialta
      841 siggrpanya iageafgilq gtavqrdadg npivgsdgly lattdieiig dpnpdwtgti
      901 kntfsykglk fsfdfqyrhg gdifsqtaat lvgrgvvdsd npidrrgtyi lpgvlqdgtp
      961 nnipitstnv ffnnfgfgpn epqvfdgttl rlnevslsyd fkkeflsntp fgslsitllg
     1021 snlwykafnf pddvnfdtnt lstgvgngqg idfitgpssr ryglsfratf
//
LOCUS       WP_091410935             983 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            amphilecti].
ACCESSION   WP_091410935
VERSION     WP_091410935.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina amphilecti
  ORGANISM  Aquimarina amphilecti
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Aquimarina amphilecti"
                     /db_xref="taxon:1038014"
     Protein         1..983
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108443
     Region          25..981
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktftksalf llwlipmsff aqssvsgtvt dagngqpipg vniiikgttn gtssdfdgny
       61 vlngvnngdi iefsyvgfia qefpysgtsr idvalqedaa eleqvvvigy gsvrkkdltg
      121 svttvtaddf nqgvnaspdq likgrtagvt vidnggapge gstirirggs slnasnnpli
      181 ivdgvpldpg pggtrnnlns inpndiesft vlkdasatai ygfrasngvi iittkkglnt
      241 dgklkfnyng nvtfseivdk iealdgnqfr eyvtangsqa qidllgtent dwqdeilqna
      301 vstnhnisls sgwdwinyrv slgllseegl iktdqldrts lsanirtkff dnhlrintni
      361 ktaiedytya ttnigaalgf dptqpvfqdn nfgnyfqwld gsgnaialag qnpvaaleqn
      421 dsrglifrsl gnlevdykfh flpelranln vgyeiasakt envtsansva naartgndsf
      481 srsqqkrenl lfdfylnyrk dvedlnttfd vtagysyqkf ldsgsnfsrg fdlveidnpf
      541 nnprevllgf fgratisiad kyiftgsfrr datsrfsgle nqwtnspsga fswnahnenf
      601 lkdsnlisql kfrvsygvtp qqsigdatps lariltsdpq sqyqigqepd gtpifistgl
      661 alpynpdltw etttqynvgl dyglfdgrvs gsidvyrket edllflaalp sgslsneddv
      721 nlgnltnegl elslnvtpiq tenlrwqigg nitfqkgevt elfavdnpnf egffntgfvg
      781 sniniqtvgf apnsywvfeq iydangtpve gayvdrnndn iinekdkyiy rkpaadffyg
      841 fntildyknw nfsmfwrgsv gnynynfvda gsngrrilnf qntlsntttd llqsnffdgg
      901 vdrfssdyyi qdasflkldn islgytfknf lnyknidmkl ygtvnnvlii tdytgidpei
      961 ssgfdstiyp rprtyqfgvn ldf
//
LOCUS       WP_091420570            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa sp.
            Hel1_31_208].
ACCESSION   WP_091420570
VERSION     WP_091420570.1
KEYWORDS    RefSeq.
SOURCE      Formosa sp. Hel1_31_208
  ORGANISM  Formosa sp. Hel1_31_208
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Formosa sp. Hel1_31_208"
                     /db_xref="taxon:1798225"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111873
     Region          25..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkltwlmt lfmafvmqls faqektvtgt vtsaedglpl pgvsvivkgt trgvqtdfdg
       61 kysikastge ilvysfvgmk saekpvgass tinlkmaedl aeletvvitg ysgatnsski
      121 ssslstvsae sieqvpinsi dqllqgqaag vnvstasgqp gqsatiiirg rnslngdiep
      181 lfiidgvpvd qdnfrslnqn dietmsvlkd aaataiygnr gaggvilitt ktgkkgsgvk
      241 vqyrslygta iepqvrfdvm naqqfltfqr dllpgtqfgd slddaaiali anqsntdwtd
      301 iffrrgktrs heitvttgge ntssfssvny yeqegitigs dlkrfsfrnn fngssrdnkf
      361 nfatnltmny svssfvvdaa rggntggqld npfivpyigl pyqspynpdg sinlwgsgpt
      421 sgggsgafna dgslnadgan gfqntpyial ntaalntdqe seikivgris gdynfaknlt
      481 vgasygidyt nveslfitap esirgvitpn qgselkgsqs esffrnanmi anafvrydnn
      541 iteklnlnva vfgeynytnt qndgytafgl npalpgsgag ftagdltege dndvynyipg
      601 vfsseseial gsifatmdld ydgkygfaas irrdatsrfv enregtfwsv agrwnidnea
      661 fmenvdwvst lklrasygvv gnqnvgsryq glqtvnsgag yqnanayllg tlidpaiqwe
      721 tsnqanvgls fgfwqnrltg eldfynnett dlfagkplsi sgtgttsvqt nvgdmtnqgi
      781 dlqisydllr ksdtnpwsvr lnangnynkn evtslpggft gntlriaegr qaftwflprw
      841 agvnpangep lyldvdgnvt nvyspdnavy ldknfdptyt ggfgadisyk gfsmnmlfaf
      901 qadrwkqnss laiiedagla gfanqsvsml nawttpgqvt dipslafggl ravdgdryle
      961 dasflrlrnv slsysvdrkv leqtkvftgv rvfvqatnlv twtkfrgfdp egtssatffd
     1021 ypvprtftlg fdltf
//
LOCUS       WP_091424569             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. OV608].
ACCESSION   WP_091424569
VERSION     WP_091424569.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. OV608
  ORGANISM  Arthrobacter sp. OV608
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Arthrobacter sp. OV608"
                     /db_xref="taxon:1882768"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53289
     Region          3..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivael gretrvaatp vtvkqllglg yevvvekgag eaasfrdeay aeagalivga
       61 deawgsdlvl rinppsgeei drlakgatli gslnpglrpd lvealaarpi talaldavpr
      121 israqsmdvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksiggt ylkveveeam essdgyakat seaynrraae
      241 iyteqaadvd iiittalipg rpapklltad dvaamksgsv ivdmaagqgg nvegsvager
      301 ivtdngvvil gytdlparlp aqasqlygtn mvnllklltp dkdgalridf ddvvqrsvtv
      361 vregektwpp ppvqvsaapt vktdagtaae ntapkkkqgl spagkaglfa agiaalfgin
      421 tvapaplpqh ftvlmlsvvv gfyvigkvhh alhtplmsvt naisgiivvg allqvtseni
      481 imqvlaavav llasinifgg favtrrmlam fsagkars
//
LOCUS       WP_091421230             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa sp.
            Hel1_31_208].
ACCESSION   WP_091421230
VERSION     WP_091421230.1
KEYWORDS    RefSeq.
SOURCE      Formosa sp. Hel1_31_208
  ORGANISM  Formosa sp. Hel1_31_208
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Formosa sp. Hel1_31_208"
                     /db_xref="taxon:1798225"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107313
     Region          24..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnntlslkll lfaflfipll slgqqvtgkv mdgasnlpla gatviikgtt tgtttdfdgn
       61 fsinvssfpv tlvfsslgfe sleerltevr ivnvtlqesn tsldeivitg lasttkrsns
      121 anavasvsae qltgvtvqsg ldgalygkfn gaeikansga pgggismrlr gvtsifgdqq
      181 plfvvdgvyv dnssiglgnn ivseaagggn pssnqddasn riadidpddi esieilkgas
      241 aaaiygsraa ggvviiktkr gkqgrpvvqf sqvvgfrspt qllgirdytp qqitdlggpa
      301 navlrdyeae ifdqtqvsst trfstsgake ntdyffgath rnepglvdnt gytkssvrln
      361 igqkfnewld lyvttnyins esdrgffnng nanrtvgyal aftypwedls pvngaypqgg
      421 agsnaletia ittnreevnr figsatsniq llsgannrlk mvleggfdqf tlrttsifpr
      481 alsyfsdpts lggvsisgtt vntnynlsaf lvhnldldng lgfttqvgsf fqnfdrntvi
      541 tiatglngsq tnltqstnvs tqqtirpqkd tgffvqeein fndqiigtvg irgdkstnng
      601 dsnkmyyypk anlavnlhkf dfwnikqisy ikpriayges grfsnfndrf tlmdpqfigg
      661 qsglspgnls gnpdigperq seleygidfg lfdkrlnfev sfynkkiddl lirsqiptss
      721 gftnrvvngg elenkgiels lnanvlqked fswnvglkww knkseitrld vpafttggfa
      781 aslgtfliqe gqsatqivgt fdpsaytaee iairdpegdg ffvygnaepd fqmswfneis
      841 yknfdftflw hwkkggdnin lttllydlag ttwdyndfgl dptgqlsngd yrasqafvnp
      901 dpviedagyl klreigifyt lpdglikyad kikvgisgrn linifdynsy dpevsnfgnn
      961 vlgnnvevtp ypmskfinfh lnvnf
//
LOCUS       WP_091428561            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            degerlachei].
ACCESSION   WP_091428561
VERSION     WP_091428561.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium degerlachei
  ORGANISM  Flavobacterium degerlachei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Flavobacterium degerlachei"
                     /db_xref="taxon:229203"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111623
     Region          23..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktylilll fffgittgys qnitvkgkvs daktlplpga nvslkgsktt vatdmdgnyq
       61 ieaskgatlv fsyigfisqe akvsgstlsv slkedgetkl devvvtamgi sskskslgya
      121 nqtikaadie rpgqlnalqa lqgsisgvti sktsgeaggg vdilirgvss lstgsnnqpl
      181 iiidgnpvnn stisgnvlss antsspgsne qfgfsnrsid inpndietyt vlkgagatal
      241 ygilagngvi iittkkgkeg ktkvnfsssv tmsevnkype lqstwregsg lsprvlsmna
      301 dtpsgvsyyp gftsgfqtng paysssddss ikfrdfykdf fktginttnn islsggsekm
      361 nyfvsasssk degivpntey arktlkfngg yklsenlkmg tsvsyansgg trantgdksi
      421 msslsywsps idindyltas ggekdwtvgt idqpiyfamt snlhdkvdrw iasadlnwqa
      481 kpwlnivyrg svdnysetrn ryagpdldpg spvngfivne kinfrglnsd ilatatktfg
      541 dfntsamign qifetnsdyg fvrgeglllp kfnniantin kyaaqtteiv rtvgyftelk
      601 adykervfla atgrrdyast lptanrafny fssnlafvfh dlvdkegsil sfgklrgswa
      661 qvgkippfgi grysypdtpf ngvggvslgt vdadpnikae ivttteagid lrffqnrirl
      721 eytyfdrksd gqilkvtlpq stgltgtwtn sgslkttghe ltlaadivks edfkwtaian
      781 ftayetevls ipfdnidfay nggadiysri kvgdaagsly grtwtyvdgq rligsnglpv
      841 iakdvngavl yskvgnafpd yvltlnntfk yknwdlgfmf eykkggegfd paerngirng
      901 ilkmtedrnh tavlegvkad gsqndipvti dgnsyyrnti inqaseiliq dtswlklrnv
      961 sltynlssnl vsklklssas fsasgnnfll wtpfrgfdpe gqqfgsgsnv ygfsglnipl
     1021 tqsytlglni gf
//
LOCUS       WP_091430401             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aliiroseovarius sediminilitoris].
ACCESSION   WP_091430401
VERSION     WP_091430401.1
KEYWORDS    RefSeq.
SOURCE      Aliiroseovarius sediminilitoris
  ORGANISM  Aliiroseovarius sediminilitoris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Aliiroseovarius.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Aliiroseovarius sediminilitoris"
                     /db_xref="taxon:1173584"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55537
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkevy egenrvamtp esaqmlqklg yecvietkag naagfsdaay keagvevvkt
       61 aaalwkaadi iakvrppnda elkrlsadkt lisffnpggn eagmekakas ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee dqqdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvkam kpgsvivdla aekggncklt
      301 vpdekivtdn gvtiigytdf psrmasqass lyannirhmm sdltpekdgk inhnmeddvi
      361 rgatvthqge itfpppppkv paiaakpkav vpeltpeekr aaevaafkaq tkqqftllgv
      421 ggalmllagl ytpasfmqhf ivfvlavfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsif maginifggf lvtrrmlamf qks
//
LOCUS       WP_091430250            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            degerlachei].
ACCESSION   WP_091430250
VERSION     WP_091430250.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium degerlachei
  ORGANISM  Flavobacterium degerlachei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Flavobacterium degerlachei"
                     /db_xref="taxon:229203"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111943
     Region          22..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklflisll fllvqsafaq tktitgtvkn kadgipipgv tvlikgttks svtdfdgkys
       61 ivaeptdllv fsyigflsse iktseksnii nanlseelns ldevvvlgst vrvtrkelgn
      121 svtsikaegl nrakpvdiss alqgkiagaq vsqnsgdpag gfsiklrgts silgssdply
      181 vidgvvlnna stnltnlnvs kgnsnlqigq nrssdinpnd ietievlngg aaaaiygsra
      241 angvilittk kgrsgdtkyt fstslttnsl rkkvyvnqsd kqfvnsspal fpiqgqpasp
      301 ttvlvagrnl etqtisgier ydyqddvfvt gighdtyfsl rggddktkyf ssigylkneg
      361 iikntdynrl gaklkiqhef nskltasvgl nyitsnsnek pdgnvfwspi nsititnniy
      421 dinqrnsngd llavdpnrvn plsvietfki tqktdrmisd iqlnfkpfen fnadfifgld
      481 nynqkgtvfi prypyspvng tyfndgyvse atnrvvqfnn dlnlrylwni nkkvkltsfa
      541 gynvqsyrde lfaiegrdlk pfvqtinafn tllpgspsag qskynlwgfy lqetigfnnk
      601 ffvtiagrqd astvfskenr sqfypkvsas yvlsdekfmd nspissarlr gswgesgslt
      661 aitpyarftn ystgnlvgnt sftlegfkkg nldlrpekss tyevgadlgi lkdrvnlsfs
      721 yynadikdll lpvelasstg stntiqnigq mnnkgveigl rydvikkedf nldfyvnyss
      781 nrnkvtglpq qrfkldsnps gapvfvekgq pigiyygtyy arntdgtlll tangypqvek
      841 gdsatgtalr dasgqptgti lnkqignpnp dyiisfganl nykkfgmsil fdgvqgvdvf
      901 dadyrtrqgv gngelvekel ngelprgyiw siygieefrv vdgnyiklre vslsysfgkl
      961 nsffddltin asgrnlfswd kftsfdpetn sggqssvaky nfgtvpiprs fslalkfqf
//
LOCUS       WP_091430426            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            degerlachei].
ACCESSION   WP_091430426
VERSION     WP_091430426.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium degerlachei
  ORGANISM  Flavobacterium degerlachei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Flavobacterium degerlachei"
                     /db_xref="taxon:229203"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117345
     Region          25..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngilv llivlmaqlt faqertvtgv vsdnagmpip gvsvlikgtn sgaqtdfdgk
       61 yaikatpsqt lifsyigmkt qevkatsstv nvkllgtave legvvvtalg ikrekkslgy
      121 atqevkgdav snvkssnfvn slsgkvagld iktsgnlggs tqvvirgnns iagnnqalfv
      181 vdgvpidngn sntegqkagr ggydygnaas dinpddiasi nvlkgaaata lygsrasngv
      241 vmivtkkgkk rkglgitins sltlgnadse tlpkyqnkyg agygpyygpn edayfneadi
      301 ngdgipdltt pftedasyga afdpslmvyq wnslypqlpd tyqkatpwva gknnpnsvwg
      361 tgstvvnsia ldggtdtssf rlgftnlaqe gnlpnsnikr ntisfsgsqd lsnkltasay
      421 fnfvkndgkg rngtgyssgn imqqfrqwnq mnvdygaqkd aylltgqnit wnpngpdnls
      481 piysdnpywt fyenfetdtr sryfgnvald nkindwlsat vrfsfdtyse iqeerinvgs
      541 advssysrfn nnvaeynyda mlnfnkdlte klnlegnvgf slrnntknsv faatnggisi
      601 prlyslsnsv spilapienq yssmvdgeyi raslgydsfa ylegsyrtdr sstlpkannr
      661 fgyysisgsl vfsslidapw lsfgkvrany aevgsatdpy kvfntyavgt pfngtpmasn
      721 ngtlanldll perqesyelg lemsflnrri gfdlsyynnq ninqitdipl ststgysfat
      781 lnagtienkg ievafnatpf kttdfrwdln lnwsqnkslv vellngidnl qlaslqggvs
      841 inatpgqpyg tirgsdyiya dngqpivnqt gsssrigtyq rtstsnsvig dinpdwkagl
      901 nnsftyknfn laflidmqkg gdvfsldtwy gyatgmydfs agtnelgnpi rdvvvgtpgn
      961 yaansggvim pgvapdgtpn qvrananiya nawgyarapn klhvydagyi klreasltyn
     1021 ftektlstlp ftnvalslig rnlwiidksv pyadpeagls sgnvqgyqsg afpsireiga
     1081 slklqf
//
LOCUS       WP_091431529             979 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            degerlachei].
ACCESSION   WP_091431529
VERSION     WP_091431529.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium degerlachei
  ORGANISM  Flavobacterium degerlachei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 979)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 979)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 979)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..979
                     /organism="Flavobacterium degerlachei"
                     /db_xref="taxon:229203"
     Protein         1..979
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107242
     Region          24..978
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykkllf lllllplsil aqntlngtvl dkvsgqpipg vnvniqgttn gvstdfdgkf
       61 qisnvkkgnn vvfsyigytn sivnyngqks itvslgedan qlkevviqvg ygtvkkkdlt
      121 gsvtvlstkd fnkgpvtsad qmiqgkvagl qiingggspg vdpvirirsg sslsasndpl
      181 yvidgvpvas ggveggknpl stinqnnies isvlkdasat aiygsrasng viiittkkgk
      241 sgelqvtyng nlqvseitkk vdalsstqfk dfvaangnda qkalvgtadt dwqdeiyrta
      301 igtdhnials ggvdnvvyra svgyanlngi lrrdnmqrtt lganvtgnff dkhlkieinn
      361 ntsviksnys nggaiggavs fdpsqpvrna dgtyfqwlts pteinplagv npvsqieqqn
      421 nygsfyrsig niqfdyklhf lpelkavanf gydqmsgrgy gdtaadyryg ftgsgygnty
      481 eniesrdnkl mdlylnynkk vdaidtqfdv tggytyqdfk esktkssynv ergvtnvels
      541 tptrlnlqsf fartnitiad kylltlsyrr dgtsrftedf rwsnfpaval gwklneenfl
      601 kdvasisalk lrggwgitgq qnigsfypsi plylasnnsa qyqlgdtfyt tyrpepynsn
      661 lkweqtttan vgvdfglfnn rftgsvdayq ritkdlllyt ynpsffgfsn qdnynvgtid
      721 nkglelaaev ipvrndnfqw tvggnvtfqn skitkltttq entpgidtgd idggtgntiq
      781 nhqvgyapss ffvyeqayga dgkpldgvfi drnkdgiins ddkyrfhkpa advfyafnts
      841 vsyknwdmgm nwrgswgnyn ynnidsnkgv annvltrntd lsngvanlle tgfaksdnfq
      901 lhsdyyvqda sfirldnvsv gytfnqkena tslvkltlaa qnilvitnyd gldpeisggi
      961 dknlyprpit ftlglnvnf
//
LOCUS       WP_091434174            1237 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            degerlachei].
ACCESSION   WP_091434174
VERSION     WP_091434174.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium degerlachei
  ORGANISM  Flavobacterium degerlachei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1237)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1237)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1237)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1237
                     /organism="Flavobacterium degerlachei"
                     /db_xref="taxon:229203"
     Protein         1..1237
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=137361
     Region          146..1236
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkpvvkqrl llrimkitlf qfllafvfst vtmansvkgq kkldtkvtls ienlslsnal
       61 aklektanvk fsynsrisql nqivsykand ellssilsni lkplnityse vsnqivlqnk
      121 tsltndligm itptslvpnt vlativkgrv lderglplpg atvmvkgtki avltdfdgnf
      181 tidapanstr lvvsyigmet qeiaikstpi tiilsefgqk lnevvittgy ektskrtftg
      241 aiskitgael lvegvvdisr miegkaagvt vqnvtgtfgt apkitvrgss sifgdtkplw
      301 vidgivqedi vnlsfadlas gnsetllsss iaglnpndvl sieilkdasa tsiygsrsln
      361 gvvvvttkqg rresplsvty sleqtarvvp nynqydilns qetmgilkem eskgflglpd
      421 taqgryggvy nilanainty dttngtfgvk ndepnrnafl rkyelantnw fktlfrpsit
      481 qnhslsfsgg gknnayfasl gfysdpgwtv adkvsqltsn ikntffindk lnltlstqas
      541 vrdqsapgsy dslrdgvsgs ttrdfdinpf nyvlntnral rpyddngnye yyrnnwapin
      601 iveelennym dikvkdirfq adlaykispk ltynftanar yanttrehni lensniigay
      661 natettlvrd aniflyqdpd dltapkvsvl pnggmlrkfs ndltsynirn sfnyknvfsn
      721 khelealfgq elrsvdrnsn nftayglqyd rgltaftdpr ileklingge syysfneere
      781 rtvgffgkvg ytydrrytgs itgrydgsnr qgnsnssrwl ptytfsgkwn vmeedfmknv
      841 kaintlslrg sygltatagp atnslaiyks fitdrlilgd retglnidel qnadltwekq
      901 fetnigldlg lfdnrvqftt dvysrkafdl vdfvttsgig gqklkqgnna dmetkgiefs
      961 lstknlnntr lkwstsfnfs iydqkitslq nnpsvlglvd gtggntlghp rnalysyqft
     1021 glnnqglptf imadgeedni aganfqdsen itkylkyegs iepnksagis ntftydnwsl
     1081 nvfivaaggn kvrlnpiyas qyddltvftk eftnrwinpg deaftnipvi adqrlianyd
     1141 adskdlkray naynysderv adgtfvrlkn vslsyefpkd lkkklglnlf smkastanpl
     1201 liysdkklng qdpefyrtgg vsqpitsqyt fslnvsf
//
LOCUS       WP_091434334            1007 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            degerlachei].
ACCESSION   WP_091434334
VERSION     WP_091434334.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium degerlachei
  ORGANISM  Flavobacterium degerlachei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Flavobacterium degerlachei"
                     /db_xref="taxon:229203"
     Protein         1..1007
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111771
     Region          45..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknsfykgg safwyliiig fslsytptla nkllrqnhsl pqqtqisgti tdglnpltgv
       61 tisikgkaks taitdfngqy tieaapsdtl vvtfigfkta iipiggrkti nirlqedits
      121 lqevrvnagy ysvkesertg siskitskni eiqpvtnvla amqgrmagvs itqttgvpgg
      181 gfevkirgqn slrpganapl yvidgvpyss dpigynqtst ifptvtspln sinpdniesi
      241 evlkdadats iygsrgangv vlvttkkgka gktkfsvias tgsgqvtsfm klmntqqyls
      301 mrakafindg lteyqawdyd tngtwdqnry tnwqeeligg taeisklqgt vsggsettqf
      361 lfsgnyhtes tvfpgdflyk lggaqfslnh rsedtkfkmt fsanynaqdn dqpafdftyd
      421 aralppnapa lyddagnlnw engtwdnplr nlaakfeskt ndllantvls yeiapalvik
      481 ssfgytdlrh tesrispstm ynpsygigsa ysgiylnnts rsswivepqi nwekelgkgk
      541 lnmlfggtfq nqgtsrlfqs gtgfssnsli ydlasaanvr vklsdetlyk yqafftriny
      601 nwqeryilnl tgrrdgssrf gpgnqfayfg avgaawlfsn etflknnswf sfgklrasyg
      661 ttgndqigdy qfldtysssg tpydgviglq ptrlfnpdfg wetnkkmeva meagflhdnl
      721 fltaawyrnr ssnqlvgvpl agttgfsvlq snldatvent gfeftlrtln fstknfnwst
      781 slnltidrnk llrfpgleas sykeqyrinq plniqllyky tgldpqtgvy qfedvnndgk
      841 iafpddrqtv vdlnpeyfgg lqnqlgykrw kldflfqfvk qknrnyptgf agqmsnqpvk
      901 mlnswqqpgd ngpyqiytig yndaavtady lysesdaais dasfirlkni alsydlplnv
      961 kntqckimlq sqnlltftky edgdpeftny gylpplkvit agiqltf
//
LOCUS       WP_091439829             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus poikilotrophus].
ACCESSION   WP_091439829
VERSION     WP_091439829.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus poikilotrophus
  ORGANISM  Geodermatophilus poikilotrophus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Geodermatophilus poikilotrophus"
                     /db_xref="taxon:1333667"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52112
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpretr pgetrvaatp ttvrqltalg hdvlvetgag aaasfpddgy reagarvgta
       61 dqawgadvvl hvakptveev grlrdgavlv stlapaldpd llatlasrpi talamdavpr
      121 israqsldvl ssmaniagyr avieaahafg rsftgqvtaa gkvppatvlv vgagvaglaa
      181 igaasslgav vratdvrpev aeqiasmggq yvgvpadeeh sgggtgyasv tsadydrraa
      241 amyaeqarev divittalip grpaprlite emvaamrpgs vvvdmaaaqg gnvagsvpde
      301 lvvtpngvti igytdlpgrl pgqasqlfgt nlvnlvkllt pgkdgrlvld lddvvqrsmt
      361 vvregellwp pppvqvsaap aaapvprpaa pvavpkpprs partagvvgg aalvlflaaa
      421 fspnqlignl tvfalavvvg fyvignvhha lhtplmsvtn aisgiivvga llqightsal
      481 vtvlatvavl vasinvfggf avtrrmlgmf trs
//
LOCUS       WP_091442132             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Ancylobacter rudongensis].
ACCESSION   WP_091442132
VERSION     WP_091442132.1
KEYWORDS    RefSeq.
SOURCE      Ancylobacter rudongensis
  ORGANISM  Ancylobacter rudongensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Xanthobacteraceae; Ancylobacter.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Ancylobacter rudongensis"
                     /db_xref="taxon:177413"
     Protein         1..>381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaivkess aseprvaasa dtvkryvglg atvvvasgag vasgvgdgey egagatvvad
       61 naaavagadi vlgvrrpeas alkginpgal viaiadphgh eaalteiagt gaslfamelm
      121 pritraqvmd vlssqanlag yravvdaaae fgrafpmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqveslg akfiavedee fkqaetaggy akamsaeyqa
      241 kqaaltaahi akqdivitta lipgrpapkl vsadmvaamk pgsilidlav erggnvegav
      301 pgevattang vkivghlnvp grlaatasql yaknlyafve tlidkgskal avkwddelvk
      361 atlltkdgav vhpgfapaap a
//
LOCUS       WP_091463941             406 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paenarthrobacter nitroguajacolicus].
ACCESSION   WP_091463941
VERSION     WP_091463941.1
KEYWORDS    RefSeq.
SOURCE      Paenarthrobacter nitroguajacolicus
  ORGANISM  Paenarthrobacter nitroguajacolicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Paenarthrobacter.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Paenarthrobacter nitroguajacolicus"
                     /db_xref="taxon:211146"
     Protein         1..406
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41200
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkagiaretl dgerrvaatp etvkqlvalg levdiesgag masghsdddy raagaavvqs
       61 lvlgsldvyc hvrpmepsta galrrgtvta glgspsselp tvralaaggi tsfalelvpr
      121 israqsmdal tsqalvagyr cvleaamrlp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandirpas adevasmggt firldletae asggyarels adrgalqral
      241 ltphvaqadv littaavpgr rapllvtrem vqgmrpgsvv vdlaaesggn vegsipgqdi
      301 piptgdgqgv vtlvgikdpa sampadasrl yaknvsnlla lmtqdgvvap dfedevvagt
      361 clthdgqvrh aptaealaal agetapfgsg hagtfptgns gsegvr
//
LOCUS       WP_091466445            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            urocaniciphilum].
ACCESSION   WP_091466445
VERSION     WP_091466445.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium urocaniciphilum
  ORGANISM  Flavobacterium urocaniciphilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Flavobacterium urocaniciphilum"
                     /db_xref="taxon:1299341"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115007
     Region          27..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqfs faqkkavtgt vtsegkplqg aaviikgtke gtqtdengkf
       61 siqaaqgdvl efsyleketk tatvgasntv nvtltsvskv ietivvdggy ksttkatsvv
      121 sqstvnakqi edrpnvnfln slqgqvagan issfsgqpgt nkidviirgv sslsastdpl
      181 yvidgvpmtq affrnlngne iesvtvlkda aataiygnra tngvisirtk kgsfrksfsv
      241 nysssyglte frgddynlpn aidhlklqqk gfnegvgilg safavtgsyl ggaythtvdp
      301 tnleaysvnt nwkdiffrtg ttkshdlsfs agsenlnnyt slsyfdqdgi vpttnfkrft
      361 frsnfngkst nekfnyglnv fgayskrnql eqetragins nvlqnpltgy inspafvdps
      421 fyqggqqlfd elgnpaldmt pymlmdlfgr nnapsffnei ktivtgnasy klsknltast
      481 vagidfaddk rnfaigpnay lsivrasgag qpfhglenqs ttsefsfnlt nkltykktfl
      541 ekhtveasvf qeyvkahrks yvyqqiglnp ltwepgagtg yvtyttalpl syapsvgask
      601 ldagllsyfg svdydydqrf gvaatirrda tyrfvddykw gtfwsvagrw nlsneaflkd
      661 vswmnelklr asygltgnqn iqargidsnl stifnlpqav rdlnsvqagy lgsssfgvss
      721 yanrdlrwee taqwdlgvdf gifkrltgsf dyynkrttdl yknliissan gipninandg
      781 dienkgiela lkydvlkntk fklsvnanga ynrsayrthg asdidgdgvv inggniarig
      841 gplfeyfavp ylgvnpangn llfldingne tesptvadsr atkksripky tggfgfnasy
      901 kgffadalft ysfgawkydt dynglmdirn adlfpvstdl fnawtpnntn tdvpalaatn
      961 fdsgdisdrf lrdasyvrvr nltvgysvpn eflnktflkq vrfrvmaenm ltftkwkgfd
     1021 pesfvssqtg yyptpkiftf gvdvnf
//
LOCUS       WP_091467642            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            urocaniciphilum].
ACCESSION   WP_091467642
VERSION     WP_091467642.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium urocaniciphilum
  ORGANISM  Flavobacterium urocaniciphilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Flavobacterium urocaniciphilum"
                     /db_xref="taxon:1299341"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110549
     Region          25..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkltqltl llfllatqif ygqeknvtgk vldqegkall gasvivketn kgtqtdangn
       61 ftikvsptqt llitylglkp qeisggasdf titlednaka idaivvtalg ikrkpdeita
      121 sthivktgel nqakatnaai gligkvsglq intvnngvnp dtriqlrgfr sisgnneali
      181 vingvvstag afaelnpeii esvnimkgss gaalygsqgs ngviivttkk gnknaekfkv
      241 tlnssfsfdq layipevqtr fgqgyqgaqd ftentnwgpe ldgslqptgl aqnlytyear
      301 knnikdffni gstalnsvai ssgdengymt favgnqnteg iipgdvfkkn nfnlsagkta
      361 gklsvsgnmr ytasnantag gvessiynsl lqvpvnvpis efssgnqaeh wtywelspfw
      421 rlknerrqtk aqtfegvael nykfnknisa iyrgsfrsvs snssrffngy tqpvvywdsp
      481 msytssyfas ndnsrriysd imlnfdydlt ddisfkanig nnitnfetnf lsmegqnliv
      541 pglynisnit gnatptdfks rqrgyayfan vdlgykdflf lnltgrkewt svlsknnnsf
      601 fypsagmsfi ptkafegfgg dilnymkvsa sivkvgnavv spydindrfg tatgagfpya
      661 dinsfvqnln itdrnlvned nlstelnlnl eflkrritld asyyssknsn qiieispsta
      721 sganaatinv getkstglel dlgltpfktk dfswdlklsy sapkttvtkv senskevpvg
      781 qflgtvgika iegqqfpmiv gtgyardeng nviidaatgd plkasnvnlg kttpdyilgl
      841 ttnmkyknvk lsavfdyrtg hvfyagtkdd liqngsdvvt aengrepfif pnsvietapg
      901 vytantsvtt sgdqnyftgi yreidenfvl datafkcrei alsydfskka lnntfldsls
      961 igfnvrnafm vlpkenrhys dpefsfttgn nvglstssqg pstrtygfnv nisf
//
LOCUS       WP_091473349            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            swingsii].
ACCESSION   WP_091473349
VERSION     WP_091473349.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium swingsii
  ORGANISM  Flavobacterium swingsii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Flavobacterium swingsii"
                     /db_xref="taxon:498292"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112544
     Region          25..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqls faqektvkgi vtdasgpmpg vnvvvkgtqr gvstgfdgay
       61 sikasegevl vfsfmgmsdi sktvdasgsi nvkmqddakq letvvitglg ikrkqdaits
      121 sytvvkaeel nrasspnavq aligkvsglq inttnssvag enrvvfrgar sitgnnqalv
      181 vidgaissla tlqqippeti lsvnamkgaq gsaiygsdgv ngviivttkk ggsdkfsvti
      241 kssldiseia ytpirqmryg qgwdgahsnv engswgpeyd gslqpvgmmq adgsfvmapy
      301 tgnqdnikef fnngltsqng isisggslet gyvnfsanrq vndfivdgde lkrnsfllka
      361 gkkigkfsve gnlnyitqnv rqteselfsd llqaatnipi ssfqsgnehh wtvyannpyw
      421 krdnqrqilk gdvvaaiatf gyqfnknisa sylanlrmnt nnnlkyrnay vdvvgpdtyg
      481 aspaaidaal vsstdfrrvf ygdllvnfdy kltdnvslka tvgnnlqdns fksnevggtn
      541 faipgvynis nvlnpytaga lvfdndggsr tlanrsthfr kvgvfasael gykdylflna
      601 tgrndwssvf dkslysffyp svglsfiptk afesikgnvl nymkifgsft kvgndsavga
      661 yainqtattg fgypfgnnsy vqqlrptysq iepefvttke asinlgffnd rltldgsyyv
      721 adtdnlitqt nvpfstgyqt vldnvgslqn kgyeidlgft piknsdprgf rwdnklnfsh
      781 nkttitaleg gltsislrap satagifadl gdefplikgt kytrdsmgrv ilgangnpti
      841 dpsqqklgkt tpdyilgysp svsyrgikls atmdyrtghq fvsyvkqdls fngstiesae
      901 nrggfimpns sydyngdgvy gadetnttvv tggggtasyi agynngfysr tgenlvldat
      961 afklreasls ysfpesligk tglsalsigv narnpitifs kqnrnygdpe asetsgnaag
     1021 idpftsrypa qrsygfslnl tf
//
LOCUS       WP_091490676             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091490676
VERSION     WP_091490676.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109123
     Region          24..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkkinfilf flcaitmqaq qtnvkgkvvd enkapvpsvn vtikgtnkgv stdmdgnfsi
       61 slskdqtlvf ssvgfenkev vykgqsleti qinskstald eiivtgvakg tsvkklgfsi
      121 ekigekqlkq vpandaasal lgkmpgirlv pkggapgsgf diqlrgaksi tggsapliiv
      181 dgvldgdmni ssddianiev lkgaaassly gsraangvis ittkrgssla pgkvevdvrt
      241 eygqnflgfv pkqssttnri iengivtsnv spdqiydnky pqtfdhvkef fnpgsyltny
      301 vglkgnssdn kisiytslqt trqegivkmv rgldrtnykl nldykilpkl tlrtsnfyts
      361 nkqegvqgdi fgsllrsdpn adlnlpnadg tpykvnvntf sdgqvnplyt vyntknesss
      421 ktlqslfsld ydfskeikfk asygftaang stfymqpkgm lnynleegtg fisrsmwesk
      481 qknitfegsy nkqfgnfnsv tkaqflyess dysdlygsas nlalggfdlt tvnagaipst
      541 tssitstnay nyslisaidy kgkyifdgli rrdasslfgp dvrwqtfyrl sgawrisedf
      601 kingidewkl rssygiaglr ppygaiyetf alnqgvtgsq etlgnsnlkp sfskefeigt
      661 dinflkrfsl sltysvannt dlilkvpvsp lsgaayqwqn aaamksksfe aslnanifkt
      721 sewnldtrln fdtysqkvte lnatpyfidg trfiiekgmn fgtllldkfa hsldevanqv
      781 pagssvndvf vvnnqgfvvk rtqvgtidet pikvtddkgi alpaakintt pdftmnfntt
      841 lsykkftfym lwswqqggym ydhsvrymte pslfdqsgka pnevksatyy snggqyigll
      901 gwdndalvyd atfvklrevs laydfkidqw kfiknirfnl igrnlltftk ypgfdpetga
      961 skggvdssaf kfdsnntypt prmvsgaltl tf
//
LOCUS       WP_091478006             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium azadirachtae].
ACCESSION   WP_091478006
VERSION     WP_091478006.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium azadirachtae
  ORGANISM  Microbacterium azadirachtae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Microbacterium azadirachtae"
                     /db_xref="taxon:582680"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52418
     Region          4..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mavigivrep agesrvaatp atiaqlrtlg hdvvvergag sdasypdeay aaagaelvdr
       61 arawgseivl aitapgaeqi alladgatii allspalrpd lveslaqrgi talaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvtsigge ylpvdvavek stdgyakats eaydrraaei
      241 ytqqaadvdi iittalipgr aaprlitasd varmkpgsvi vdmaagqggn vegsvagert
      301 vtpngviilg ytdlasrlaa qasqlygtnv anlvtlltpg kdgaftidfd dvvqrsvtvv
      361 rdgeitwppp pvqvaaapak apvastpiea pqkqglsagr kallivlgia alflvnafap
      421 aplpqhftvl tlsvvigfyv igkvhhalht plmsvtnais gvivvgamlq itdpdpvvqv
      481 laaiavllas inifggfavt rrmlamftkg gqk
//
LOCUS       WP_091491650            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091491650
VERSION     WP_091491650.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123901
     Region          22..1111
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkilqalll fltiagysqe trtitgiiqd atdfgpipga sifvennsis nktamagiih
       61 seaigttsdf dgkftlkvak nvtslrvtfm gyksytleld gqknytvnlt setaklqevv
      121 vtgyqkiekr kvtgaitkid maaiqqtgvs sidqllvgqi agvavstptg apgapakiri
      181 rgtaslsgsq dplwvldglp legndvpkny dkdnidqlnn fsiaglnpdd ikditilkda
      241 aataiygara angvivvttk kgksgkmvvt lntntfitqr pdfaklnlmn asqkvdleld
      301 masrsdltyr ddvgeisril ngsnelgtfr tggfsalspa tqqsinalrn nntnwgnliy
      361 qtaintqhgl slsgggeksd yyfslgyyde kgttigtgfk rynltlknnf eitdkfkvgv
      421 gifgsenkts sylsdtdvyt npgnysrnvn pyltpynadg sykydqdiag ysdryvpfni
      481 leerantsyd lktraikall daeykitrdl kvtsqlglql dntssekfad idtyytrkek
      541 ersryftnga ynyflpeggi iqnsntdffq ynlktmvnys ktfgekheve amvgnelrrn
      601 ytttvstkgf gfdkntlttk pimfpnvtya sdaiyrqyqk qenenafasf fatasytydr
      661 kysvfgsvry dgsdlfgvdp kykylplwst saswtvseed flkdnltlsn lrfrasyglq
      721 gnidkntspf vvgtyknisi lpgqteqiis vesppndklr wekttntnlg idlglfnnri
      781 sivsdfygrk ssdligfral plengfdysn lnwaqvtnkg feitlstrni drpnfkwnts
      841 infahnksnv driavrdtdf lpsreglpvn avfglrtngi dengyplfvn kkgetvnaqt
      901 ffklydpyad ffpgeltdss ltpaeyrdlf vylgdrdpkf tggltntfkv snfdftvaaa
      961 fnlkqtvvrt ppysgtqvdr gqnysidiln awsptntssn lpaingkdsg tgdswmayqw
     1021 fanntplnwn syldtwvsem symrlssmrl gytfpktftd hiniqsirls vearnlfvis
     1081 sdfkgyfdpe tygniyaqpv pksftigcnv tf
//
LOCUS       WP_091491937            1128 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091491937
VERSION     WP_091491937.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1128)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1128)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1128)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1128
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125450
     Region          136..1127
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnfkltdvlf ffrrrliiti mrtfiflfcs tifgfspasv fsqntkitie tdkmvtvdev
       61 fdiikqqtnc tfiyqedlfk elpkvhlkkg tikvgdllkt sfpakgftfs ftpnntivin
      121 evkpspekkv eqstwievkg vvtnqrkepl pgvnikvngt nttrqtdfdg kysitapsdg
      181 tlffsyvghk vemvavnnrk vinvtlqeet keltgvtint gvtvrkkeli tgavtsfrge
      241 elrqvstqna vqalksldps fivvnnnlvg snpnvlptie vrgqtsisan qvesqfkddp
      301 nqplfildgf pttlqqvvdl dinrianitl lkdaastaly garsangvvv ietikplqgk
      361 lqvsyvynsa fevadlsvyh lmnaeqklef erlsgafnay sgaspatqfe wdqvynkrla
      421 dvrrgvntyw lnepiqmgit sghslnlggg teefrfniag nyksltgtmk gsehntwgyn
      481 aglvykknkl slsntffvsg gtnqespygs fatwaktspy ypkynengvi tryldgttap
      541 lpdkvyipvn qapnplynvf lpsynkgnnf nftnnfalny dvnthikttg alsiskmdin
      601 ntvfvspddt qfikknatek gtytrqeari dkwnaniggt ysnvfnnvhs fnytirasal
      661 etrnnsytsa lrgfpigvdg npafafgyep yakpkiytdl irsvdltnqi nyaydrrflf
      721 dftqtisgat nfgsnkkysp ywgiglgwnl nnefkmnedi vnvlkvrani gqtgnqnlvg
      781 yasydvyayn pntnvfgsgi aisqianpnl eaqktkdlsv gldlamfrnk ltatigayrr
      841 kttpqivaid lasstgidgy pinlgyltte glelkmnynf iynvkdnfiw gvglmatsns
      901 nklggfnnal sslndaaqka gsltryydga stndlwavps lgidpatgqe vflkkngqtt
      961 yifdkkdevv mgnsrekatg vvstnltykg fsfglfvrys lgadrfnsal fnkvenisss
     1021 nifdnqdara ltdrwttpgq maefkaislt sstpissrfi qkdnylsges vrlgyrltdr
     1081 ewlkrngltg lginvlanef frvstikaer gidypfarty slslnlsi
//
LOCUS       WP_091493014            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091493014
VERSION     WP_091493014.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109280
     Region          22..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiflifmi vftaqvslaq vksvkgvitd sdgmplpgas vavqggqkgt ttdfdglysi
       61 eaqkgqtlvf tyvgletqti vvgdattinv kmvqgasnal nevvvtslgi kktkkslaya
      121 aqelkgeelt rvkdanlint vagkiagvav trsssgaggt tkvtirgnss fvnnqplyvi
      181 dgiplyngga gqpngtfgdl nggnkdggdv vslinpddye gmtvlkgaaa svlygsqgan
      241 gvillsskka kagaesfnvn svttfetaay lpefqsdyts nagdprswga kqkvegdkei
      301 kdffdvgntq itsmtftkat egastalsya ntdsngiipg nhlkknnfgi rqtskffddk
      361 lsvavtanyv tqtinnrptn glyfnpiagv yshpraftln dlktyevfdp vknmmqqnyp
      421 gfatvnesne npywqinkqk sidknnfftg aialdykiae wfhltsrysy nrnesnfqkg
      481 mygssatslv hptgryinan ligtqnyadl ialfntkind nfsfngtlgt sinhsratgl
      541 tidsgigggl vydniftlgn fvnnngnvqt gaerevqsvf aaatfgykdy lfldvagrnd
      601 wsstlvntqd pgyfypavga tailsemttm pdfinygkvr atfaqvgndi astitsptss
      661 ivagnivnpt vgprpgtslk nelkselelg tewrmfnnrl gfelsyytsd tknqflqvpa
      721 estnangytf yainagsisn kgfevvlsad ivrgekfnwe srinysqnks rvndipsest
      781 ggrivltdpg snsyryslie grpfgviegf dfqrdaqgri lvnddntlqr tdwkeignan
      841 pdfmlgwsnt fklgafrani lldgrfggev lsltqaindf ngvskatgda rnagsvking
      901 vrasdntpvt smdpyeyysn vagrngvssq yiynatnvsv revsigytfd kakipfvqta
      961 sisliarnlf fiykdapfdp nvalstgegl qgvdvfgmps trsiglnlnl tf
//
LOCUS       WP_091494052            1022 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091494052
VERSION     WP_091494052.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1022)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1022)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1022)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1022
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1022
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111361
     Region          24..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykkllf lflllpftvl aqstlsgtvt dratgqpipg vnvnvqgavg gtstdfdgkf
       61 qlpnlkngdk ilvsfigykt etiafngqkn lavslsedtn qlqevvvqvg ygtvkkkdat
      121 gavavlsanq lnkgpvgsad qllvgraagv rittdggqpd anpnirirgg sslsgnnnpl
      181 iiidgvpidn tnpagianpl tlinpndidt failkdasat aiygsrasng viiittkkgv
      241 sgapkfnfss tittgkvnnp vdmmsgpqft afmqkyhpgy tsllgvpngt avidnpatpe
      301 iegrtlyntd wqdliyrqsi stdnnfsara nlfgkvpfra svgyaknegv vktndleryt
      361 gsiklsptlf nnslkidfna kgisvkknai dadavigsal gmdptkpayd npgassnifg
      421 gyyqllnann sisgaqnpla ilnqrsrpee vqkllgniel dyklpfvdgl ravvngglev
      481 skskirevys dnaiqtyqid nsagtnppty vfnpglnyae nqtvnnktld ayfaynksls
      541 gfvtrvdaqa gysyqnfvtd gnkeifrynt snglrevtpn psnpnnryyn ernlqsffgr
      601 gnfdlldkyl ftltlradgs slfsedkrwg yfpaagfawr vkdetflkds ktfndlklrl
      661 gygitgqqdi tgvagsypys alfaptsass tyipgvngyy akpynedltw ektttynvgi
      721 dfglfendiv tgsidayqky tkdllsvvsa spgqaltnef vsnvgsmknr gfesnlnvkv
      781 irkedfnlsv ngniaynigk itdlnnrttn vdnasnipvg tgqkiayntv gqqpysawvf
      841 qqvydsnnrp ienafvdkng dgvindsdrs yvalrpnwty gfgltanykk fdlsttfngq
      901 iggkvynark lqsgfidkal pansisltnv ldtefdfkti ngnvpfsdfy ledasflrcq
      961 nitlgynfdn aikgavlrly aaannvfivt dytgvdpenf naidnnfypr srtfsfglnl
     1021 df
//
LOCUS       WP_091495283            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091495283
VERSION     WP_091495283.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116027
     Region          32..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilnryig lciflisiga taqekqpliq skvggtvida vtkepiigas ivikgtthgv
       61 qtdfdgkfyf qtgqklpytv ivsylgykkr efvinensvv idlteeqnql sevvvtalgi
      121 skekkslgyt tqalknkdia etketnflns lsgklagvri tnsqgdmgss riiirgetsi
      181 agnnqplfvv dgvpvdnsql gsvggatrdf knaiadlnpn dietltvlkg pnaaalygsr
      241 aahgvvlitt ksgksqkglg itvnsgitis qvatlpsfqn sygqgsngrf sfvdgkgggi
      301 ndgvdeswgp rldgrlipqf fsngeavpfv ahpnnvkdff ntgltydnsv svarsddksd
      361 frlgvnnqkq lgtvpnsevn ktnftintny qisknikvgv tgnyittnap alpggpsgnr
      421 aagvmlqflw fgrqvdinel qnnrnvnwnn syysnpywna yynttsqqrn rfigdvhlda
      481 tladglnfrf rtgvdyyndr rkytikygtn gtpfgsyaed aytvneqnte giftytkkln
      541 ddfsldalag fnirnhsdan nyqkaprlav pdlytltnsr dpltssntls rlrvysayas
      601 aqlgyknyay lnvtarndws stlpssnrsy fypsingslv lsealnlkss tldflkirgg
      661 wsevgndadp yqlstiynfq tafdgnpiqt ssqrklnenl kpettrstev gleatfwknr
      721 lhfdvayynt nsfdqileik ttassgytsq linagkinnr gleiqldgsp iqtenfkwni
      781 ganysrnrsk veildyakqi qnytigssgg vevlasvgqa ygalygtayl rdangnivvg
      841 englpkadpt krvlghytpd ylagvtntlt yknlelsvlv dasvggeifs gtnrtgtytg
      901 vlastlpgrg aengglsyyy pnnntangrt lvngtapsgv tvyddgmifn gvyengspnt
      961 kvisaqeyyk asyniseayi ysstfvkmre iklaynfnks farklglega sitavgrnlf
     1021 fiykdapnid petafntgna qgleslslpt trnfslnvnl kf
//
LOCUS       WP_091495213            1186 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091495213
VERSION     WP_091495213.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1186)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1186)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1186)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1186
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1186
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132534
     Region          52..118
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          132..1185
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkhnseky fsgryhyyly lllmrsvtaf iwismcslya npslgqnkih vrfkntplte
       61 vfstlekqtn yvffynddvl ksantitldk datleeilnn alrsnnltfd iidkqvvvkr
      121 nkkkaeqley dltgkvtdkk gaplvgvnvi lkgkqswdit rkegeyrvrv spydtivfss
      181 lgyktvtvav nnrriidatl vpdvmelhsv eivasngytd lpkervtgai gvmtakelae
      241 vptvdiqsrl egkmagvnvd prtgsisvrg tnnfsgtgqp lividgfpqs redfafskrg
      301 vpgssilsfl npddvesiti lkdaaassiw gsqaangviv ittkkgkkge ptinfnttts
      361 igekidlgkl rvmntaqyid yekdlvnggf vadnisnwqa lnpsaaqeim frqkrgqisv
      421 serdallsql aqndnlgqin ryllrnsltt qydlsisggn dkssyylslg ynkdqaamvg
      481 ndsksynitl nnsfqlkkfl klntginyvp ttyqsnnvan ealsnvsata lrpydmiade
      541 ngngidryfl frpevsqgfe akgylpwsyn yldelnysnv itkganirln asltatitdw
      601 lnfeaagmyt sitskiksln eldsyytrnm inqatsinta gklvygiplg sylyntstnn
      661 dnqsmrfqmn inknfnenns lhflagseir eerregssqr yygynidtns gqsvnptvyy
      721 ttvygwqsii gssdnsisks rsrylsyygl gsydfmnryh vsgsvrfddf nllgasrknr
      781 alplwstgak wdinkefflr dvnwlsslaf ritygkagss ppggfgsqsp visigsvdfn
      841 tqlptasisi pqnpeikwet tstlnygldy gffnnrlrgs idlyykktkd ilanlpfnpt
      901 ygwsfvnynt aslkghgvdl slsgtivnta fkwnstfnfs yntnevtdsr yvlnstnqyf
      961 gsspmvgnsi gtvyaynwag ldatgqsqvy kkdgtivtst qgiasidkdd lkkmgttfap
     1021 yfggfmndfs fknfklgvqi tyyaghvfrn tvlqnypsys gvqsgavakd elvadrwrka
     1081 gdeaitnvpg ltninfnsln ryqmadinvl padnirlqqi slgynvpsqw lertfiksls
     1141 fnfaarnlgl lwvkndlgid pqylsnanyn tlapqrnysl qfnctf
//
LOCUS       WP_091495368            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091495368
VERSION     WP_091495368.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123254
     Region          57..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnfirkika pdygsgfdlk kkltllcvlv slsqvhafst epssrigaek vqpqnsisgq
       61 vkdskgaplp gasvlikgtk ngtitdfdgk ftlagdgnsv lvvsfvgfvt kevavnsrtn
      121 inivledsaa sldevvvvgy gkmkkkdltg sivqvkaeal anqnpqtvqd llrgvpglkv
      181 gydpsakggg slqirgqtsv ynpdganhns pliildgmqf ygelseinpd dvgqidilkd
      241 asatavygsk aaagvivist kkgktgkpii nvttnmtivn esayrdvysa dgyikyrqdw
      301 etaktygtnt atgnyeawvt gtaagkpgyy aspsqlsqfg iteaqwlayq pasqiqgksl
      361 nevwglrlgi tdatllknft egkthdwyns tfrtginrdn nlsvsgasdk vnyymslgyl
      421 tsegaiqgnd ytavranmkv dakitdwlef ganvnfqdrs dgdisvgtgt nywdanmlrn
      481 spfanfkean gdyarqpmgp tiggynyyyd rqymdldrgy tilntifntk vtlpfgitys
      541 fnaapryeff ynryfqsagn knwnaanigv drengkkftw nlnntitwdh tfnekhhiia
      601 tfvqeaedlk twsdridann iqpsdalgyh nianatlans tftatdthqt gdalmarlfy
      661 sfddrymitg tvrrdgysaf gasypyatfp svalgwnfnk ekwfhwepls tgklrlswgk
      721 ngnrsladpy lalanlssgt gatmgyidas gnivdmkylg idrmanpnlq wekttasnig
      781 idlgffndri tttidvyksv thdmimsqrl peftgfssia tnlgevenkg ieisltslnm
      841 kkpnfewttm vafsynknti nklygnmedi kdangnvigr keaddktngw figkpisqiw
      901 dykvigiwqk deaveaakyg qrpgdpkven sytaddvngk ptynekdkqf lgqttppinw
      961 slrneftfyk nwnlainmys ymghksmdgr ymntyndgsl ytnnynpfvn pywtidnptn
     1021 dwarldargp agagtaklyd rsfirldnis layslpkdli nrlhvrnfki ytsvqnvatw
     1081 saskqwkyyg dpetgglatr mfnlgfnvsl
//
LOCUS       WP_091495643            1131 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091495643
VERSION     WP_091495643.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1131)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1131)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1131)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1131
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1131
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125937
     Region          30..1130
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqalikrcs fllftlisvl syaqnsnvvt vtgtitdnlg gllpgvnvte kstknsvttd
       61 yngkyqikvk sggtlvfsfi gmkkqeipln nrsivnvkme ddfnqleniv vvgygsqkkk
      121 eltgaiatik addlmdlpvt nlsdalkglv pnlnvssgsg rpgeagsiqi rqtfslskdg
      181 gfdipliiid dmiqidpsng kptleqfnrl dpseiesmtv lkdgsaaiyg srasqgaivv
      241 ktkrgkagka kfsynsqfai ndavshskvl nayefgvfsn ryfksrvaap avidpatiys
      301 daeleqmkgl nynwldeawk paiqqkhsfn vsggnedity fagatyltqd anlgyqkyek
      361 wnfrtginak iaknldfsas vsgnvgfidk sftkassnis dgsygsaagg eqadygfllh
      421 mpqhvpwqtt lngknyyvsp fpnsnknfgs anannniagw nyfanlnngs hqttddntfn
      481 vnaslnykva avkglsfkvt ysrnqsstyn eqiqlpydlv rirdyqlqdk hlasaanpsf
      541 ynattnptgs yvletnvrns rvyynntdgk stqgdfliny drtfgdhqig amvggeasev
      601 yntftrlaye qtgkdylgdy rtagtlstsn sqatkveggt lsyfgrlnys fkqkylfqfi
      661 lrsdastkfa pehywgtfps vqlgwvmske nwfeksvpwv dffkirysig ktgkdnimpw
      721 rweqyydliv dkgfqfgpgt atsgggwngn gltprvnpnr dvtwdttikn nvgvditllk
      781 nrlsltydfy ydknkemltd mssavgvpis vggayaeqny gridawghei slnwsdkiks
      841 nmsynvglnf aynnneikly pdqgnmvpsn qtkresystf npvwgfavwk gtstgdgilr
      901 tdedianywa ylteratavg gvpryfdins aagmrkgsla yqdvagqlnp dgsmsgadgq
      961 iikendyvkl anssrtynvi anlgfkydsf slrtqistsw gganfvdlvn qgtssahnmw
     1021 sresfwrdmy sednpngkyp nvaqwtymss psdfwqistf rcfvrnlsln ydipkkvfad
     1081 tkiaaitlgi tgnnlwdlyn pypdhyrnmy dnssvnyptl rtwslnfnvs f
//
LOCUS       WP_091495729            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091495729
VERSION     WP_091495729.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111676
     Region          25..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miknvlkllf vicifgfqtl eaqttvkgti tdavsgipip ganiivkgtr tsassdfdgk
       61 ysisvpnqss vlvftyvgsa tkevavgsqt tinvslgadt qqlgevvvta lgikrekkai
      121 tysaqniavd eisearslnv anslsgkvag lnfsttsngv gsssritlrg nrsltgnnqp
      181 lyvvdgvpis ngtgagndns dtggttqpdg isninpedia smtvlkgpsa aalygtrasn
      241 gvivittksg kagktsvtls snfmassayn ltnfqneygq gdlgnyssss psswgprfdg
      301 rqvpawqlvr npnyagpatt sytaqpnnvq dfyktgynla ntlsvtsgne kaqgyfsytn
      361 traegivggn qmdrhnlnlr ftskltdkls ldaktnyivq eidnllktge esigtsayll
      421 prsmkyndyk dfeyvdaage lqknyfvdrs gtpggnpfwt alrdndrtdk rnrfiglasl
      481 kydftstlsl qvragldqtt nkivtkrfat eefnqnvgny nefyetatef ntdallsyne
      541 kfgdfsvgin aganilkqns sslsaggrlg krnyftmrnv pdptattsnl dkqinsvygf
      601 sqigfrnylf ldltarndws salpannrsf fypsvglsgv isdmvdlpet isfaklrasy
      661 akvgndtdpy qtssrltyig anggilfpqs tagnpnlrpe msssvefgad vrffnnrlgl
      721 dvtyfetntk dqifyintpe sssksraivn ggeiqnkgfe avltatpiqt nnftwdittn
      781 fstykskvvs iyegrdelil gegrlvrskv vlggeygdly vkgfkrdpng nvivndaglp
      841 vatnsfdvra gnfnpdwtag frnsfkykdf slsflvdfri ggevvsytqa rmaglgvsdv
      901 tlagrdgfvv pgvvdngngt ytpntrsvta eeywvsigqr dplaepfiyd atnirlreav
      961 fgyslpkrll gdsgfksidf slvgrnlfff lneakhfdpe agagtgnlqg vesfnipttr
     1021 eyglnvkfgf
//
LOCUS       WP_091496304            1007 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091496304
VERSION     WP_091496304.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1007
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112238
     Region          30..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrfiqlkiml cfavftllpa kilaqnnqki vltgiitgve gkpienatls stqdnvsitt
       61 daagsyyitv tpdadlqvqa egyqslsika svgiedislk sitvdqvqia fkkedaqnlm
      121 ggisyinvpe iisknyttys ldgaqalvgg fngslwgmgg ylvlvdgvpr eassvlstei
      181 eqitflkgas aatlygsraa kgvvyittkk gkiqkqqits rldngvfipk slpkylgsae
      241 ymqyynqara ndgldplytd etiynfasgk npyrypnvny yapeyvkkfy fnydanveit
      301 ggnkvaryft nvnfmsqqdp lqefgeaann nmnrfnirgn vdlsindris atiganaiys
      361 ntrgvntnyw qnaatlrphl fspllpismi epgdaatlal anssnyiidn qyllggtqln
      421 ptnpfatiya ggyntftsrq fqfntgvdvk lgdlldglsf htnfavdyat synqsynnvy
      481 atyeanwnty agfdqigslt kygkdaksgv qnisnsafaq tvafsgqfdy vkkineqhnf
      541 samliasgfq qsqsavyhkt snanlglnla ynfdqkyfae fngafvhsak faegnreafs
      601 ptmslgwkls nedfikniks idnlkvtasa gilntdldvn nyylyqsiyt qtdgawfswr
      661 dgalnrstds rrgenlnltf akrkeitfgl egsffnrlit lntnffinkl egniiqaasl
      721 ypnyyttgwp ntsfipyiny nddkrtgldf dlrfnkkaga vdltlgftgt ylnteaskra
      781 elyedsyqnr qgkpldalwg lksdgffrda adiqnspsqt fgqvkpgdik ykdqngdgii
      841 dmkdevylgk agwngapltf ginftakwnn ftffaivtgq tgaygmknns yywidgedky
      901 sinvrnswte etkdtatfpr ltslnsdnny rssdfwiyst nridlskvqi tydfpkkaln
      961 qtffnglsvy algadlltla kereymelni gsapqnryfn lglkalf
//
LOCUS       WP_091496660            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091496660
VERSION     WP_091496660.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114942
     Region          27..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv lllvlvaqlt faqeravsgt vsdntgmplp gvsvlikgtk tgtqtdfdgk
       61 fsikaspsqv lvfsyigmks qevvasstnv niklkddsve lgevivsgav gikkkksavt
      121 ssystvnnde lkaasnpdav rslvgkvsgl tinnttngvg gttsirirsm lsftgnteal
      181 vvidnvissa dvmasipsdl ienvtvlkga qgaalygsqg kqgvvlvttk kgsrnenltv
      241 afnssadiek vsfvperqqr ygqgwynvqd qqenggwgpl ldgsikpvgi pdadgnsima
      301 pysalgndei kkfyqtgtil qnnlnisagg aegyvnlnlg nvrrdfileg delnrntvvl
      361 tagkkinkft vggtftftnq rtkqanvnaa tsrsdytllt tllqaasnvp itqfkdrgly
      421 gwngyyqnpy warennrlee tknfvnlgin agyeinknie lvyngsvqmr ntnqvsysnq
      481 aispadadgg fdspsefyqs nlnstfyygd imanfnydls dalklkfnvg qnmqynytkr
      541 isqggtnlei pglynisnvl npanpstldn rtietrstat fanvdfsykn ylflnltgry
      601 egqsvaavgn qfyfypsagl syvatnaiea lkdksvlsnl klyanytqvg sldpvaayni
      661 ldlaqiatgf pfpntgnsyn nsyfptdpni kpetyttyeg ginfgflkdr itldvagyit
      721 rttdlitdas assasglqtl ksnngelegk gieidlavmp fntptfkwna rvsytsndtk
      781 visagdtdkv vitdggnsqi ngdisavkgl pfpyitgtdw mrdseghviv daqgrptpda
      841 tfknlgkvtp dyilgltnsf eykgvglsft mdyrtghsfl sqtkynltwn ghlvdsaefd
      901 rnvgflypgs vidnpatatv gdyipntsvl tggfssltga anrtqayfnq aasvgshnli
      961 datafkvrei alsysfpkkv lekagiqtfk vslnarnpfi ilassnkgya dpeasnqvnt
     1021 ststaaknpn anstltntsr nglgfigdaq ypstrtfgfs inttf
//
LOCUS       WP_091497114            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091497114
VERSION     WP_091497114.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109523
     Region          25..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfifsfla llllptymmg qaqaikgkvv dsngmgvpga iiassdarat adadfdgnft
       61 inakpgdilk vsmlgfdavs vpataapmti tlkesgdtal kevvvigygt rkkidntsav
      121 ssiksdeitk mkvinasqai qgkaagvqva tsdapgstps ivirgvgtal ggrnplyvvd
      181 gmptdninni nsnditsyev lkdasalaiy gtrgangvim ittktgkgkl vvdidsyagf
      241 rsplkkvkma nadqyiqynn aafisqfpng rfstnqpynt nwfdeitqtg vytqnnvsls
      301 gsgenikyff svgnyeedgi lkgteygrtt frsnneykis eklkisqnfs vssikntpqp
      361 msaftsayrq splvpvrfpd gkygvpfikn gvisetgdsf nsvgnpvvsl dynneqqktv
      421 vlqgglkldw dimkslkfts qfngeyftyk qynfvdnlgl wlaadpsrve agydkkslnt
      481 ntltrntddy fnwnlsnyft ynkvfaeihd vevtagiean vigtrsktta dirnvnpnsn
      541 ywgldginya qnggvttyka vnenqarlas yfarlqyklm dkylltgtvr rdgssnyssd
      601 yrwgtfpsvg lgwivtkesf lsdikgldll kirgswgklg nqkvplniqs ftsgvdyngg
      661 sgttinsqid pslsweivee asagldfelf nsrlkgsfdv ydkntnnail nvkpystsgi
      721 tlespthvge vsnkgyeial rwddkitdnl sywvggnfsh nknelaslkn vqiatvnggs
      781 lgngqvtkil dntsvgqplg sfymyeyagv dptngqmlyy tangnkvaqg aldqtkdrky
      841 vgsvlptsny gvtvglnykn idfsvdgygt ggakvyngkk aqrfygenve asllndmwtp
      901 tnttgsnpap fnqvpvasty ylesgdyfri nnitlgyklp lredgfvnyc riyvnamnpf
      961 itqkysgfsp evlgngelvt gtqgvelday palktfvvga nlkf
//
LOCUS       WP_091498295             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            phragmitis].
ACCESSION   WP_091498295
VERSION     WP_091498295.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium phragmitis
  ORGANISM  Flavobacterium phragmitis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Flavobacterium phragmitis"
                     /db_xref="taxon:739143"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110558
     Region          39..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnftnhsvlq nfgnklfkkk lgftifflft vlvsvaqtki qgsikdihgv pisgvsimek
       61 ntsnngvlsd fdgnfqmtlq kansklvvsy igfasqevtv sgnkvevvli enteqladvv
      121 vvgygtqkks rvtsaiasik ekdftrgdir dasdlirgkv aglsisngsg dpsatpnisl
      181 rgvstllgga gplvlingvp gsidtvapne iasidvlkda saaaiygtrg angvilittk
      241 tvnkdmpsti tysgftsvsd fankakflda gqqrslrsqg ftipfadgga stdwlkeisg
      301 sgfsqnhnla fkggnaktny ivnlnyvdqt gvfkntfnee yrfsfdvnhs mfndklrvnl
      361 gllngtrnmg ldegtvgyay rqsmirnpta pvynpdgtyn edpakfqyyn pvaivnetiq
      421 drkdtwqrft anltldllpg wdvgamfakn rntgfngyae tkkhysntin krngvasrdt
      481 gntdndymel ttkyhkkldk heftvlggys yqysmnegfs asnydfptds fsynnlgsgn
      541 altdgkagms sykndnklig ffgrlnydfn nkydllvsir regsskfgan yqwgnfpavs
      601 agwsinkesf ledvaainnl kiragygvtg vipndsymsk tlynysgyff nngqwikglv
      661 pasnpnpdlr wekttevnig ldfgfannri sgsfdvynkk tsdmlwnygv ptppylfptm
      721 tanvgkmenk gfevllntip vktenfvwns smtfshnknk ltslsndlyk iegdylnvgn
      781 tgdpisfath rlevgqsign fwglksvdit tdgkwivelp dgtrqtltta myndnnkqyl
      841 gngipqyyag wtntfsykkf dlsviltgaf dfqilnsqrm fyenptiayn mldtaydkvy
      901 dkavlnynqt yvsyyieqgd yvkvdnvtls ynfdvkpfkf lsamrlyvsg nnlgtftkyk
      961 gldpeikred pltqgmdnrd kypstrsftl glnvtf
//
LOCUS       WP_091509877             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbulbifer yueqingensis].
ACCESSION   WP_091509877
VERSION     WP_091509877.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer yueqingensis
  ORGANISM  Microbulbifer yueqingensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Microbulbifer yueqingensis"
                     /db_xref="taxon:658219"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54723
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miiaipkesv pgearvaatp esvrrmgelg fsviveagag aaasftdday reagaeired
       61 aesclrdagl vfkvqaptds eielipsgat lvaflkpaqn eellnklaek dinalavesv
      121 prisraqkmd alssmaniag yravieaahn fgrfftgqit aagkipparv lvigagvagl
      181 saigtakslg amvrafdtra evreqvesmg aefltvdiee egsgqggyak emsqafidae
      241 malfreqake adivittali pgkpapklwl admvdtmaeg svvvdlaaem ggncdytekd
      301 ekvvksgvti igytnlpsra atqssklyat nlthllaela pekngeinid fddevirgat
      361 vvrdgeitwp ppppkvsaqp kpapakepep kpeaaekpak rksplsilaf wlvagslllw
      421 lgrvappdfv ahftvfvlai fvgwqviwnv thalhtplms vtnaisgivv vgallqvgat
      481 gsglvtllaf iavlvasini fggffvtyrm lkmfrr
//
LOCUS       WP_091510164            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flexibacter
            flexilis].
ACCESSION   WP_091510164
VERSION     WP_091510164.1
KEYWORDS    RefSeq.
SOURCE      Flexibacter flexilis
  ORGANISM  Flexibacter flexilis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flexibacteraceae; Flexibacter.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Flexibacter flexilis"
                     /db_xref="taxon:998"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110771
     Region          25..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktllisfv lmvavltsvl aqvtktvtgk vtsaldgspl pgvnvvvkgt tqgvisdvdg
       61 kysievpsvg gtlvfsfvgm ntsevavgdn atinlametd iaqlsevvvt algierekrs
      121 vgyavtqvgg sqltnsretn mvqalagkva gvqvmggggt pgasskiilr gnksfgdnqp
      181 lfvidgipmd nstdasnagd npyeptleqv nysnravdin pndiesmtvl kgpaaaalyg
      241 vrggngvimi ttkkgkfgqk trvdinssid fsqvnklpdl qttygqsdgs pqswgakntq
      301 agvnnaekff ktgvttsndv aitsgtekns yrlsvghlhq dgiipttnfs rftarltaqs
      361 elrkdltast tvsftnsggr raqqgsnasg vmlsllraps sfdlldaynh pnadgsqnny
      421 wagydntyws lhhnpfkdnn krlignisln ytpmdwlkvt yrlgldnytd yrrgiydiga
      481 hnsaevangq itenykrhle iysdliisan keftekihgs lslgnninqr ensdlysrgr
      541 gfsidnffnm nnaasfyssq yderirsaaf fydgnisynn mlfigstgrq eysstfgpnr
      601 rhfffasatg sfvfteleai knsnitnfgk lrlsyarsan tpsaydwiky pykqpsfadg
      661 ytngfslpyl gtngyghsnt ignpdlkpef tagpevglev nflkdrikad vtyynqkttd
      721 iilespasps sgytaklsna ativnkgwei slsgtpvktk dfdwtidvny trnrnevtal
      781 akgvseqela sgfedarifa ivgkpygsiy gtkwqrdsng kiivgangrp lktttlydlg
      841 npypdfimgi rntftykdfk lsalldihqg gkmwngtnar lnrfgvsaas asvdrsqmmv
      901 vdgvkedgsk ndiqitpqey ytyykgdlga veenvqdisw vrlrevslgy tirkikyvqa
      961 vditftgrnl wlksnyvgmd petsltgags nyngidwfgm pntksynial hitl
//
LOCUS       WP_091521261             412 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aerobium
            aerolatum].
ACCESSION   WP_091521261
VERSION     WP_091521261.1
KEYWORDS    RefSeq.
SOURCE      Aerobium aerolatum
  ORGANISM  Aerobium aerolatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Aerobium.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Aerobium aerolatum"
                     /db_xref="taxon:561088"
     Protein         1..412
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42242
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqiifvpre vdaaearvaa spetvkrlsg lgftvviekd aganaripda dfaangatig
       61 saadvksadv vlkvrrptta elknykpgal vlasmdpygn daaiaamaga gvsafamefm
      121 pritraqsmd ilssqanlag yqavvdaaye ydralpmmmt aagtvpaakv fvmgvgvagl
      181 qaiatarrmg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk agsvivdlav erggnvegav
      301 agevvttang vkivghlnvp grvaasasll yaknlytfle tmvdketktv slnledelva
      361 atllthggkv vhpnfagvvt saavdeavae kktaakkvaa kkspgdkpkg ds
//
LOCUS       WP_091522664            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paenimyroides
            ummariense].
ACCESSION   WP_091522664
VERSION     WP_091522664.1
KEYWORDS    RefSeq.
SOURCE      Paenimyroides ummariense
  ORGANISM  Paenimyroides ummariense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Paenimyroides.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Paenimyroides ummariense"
                     /db_xref="taxon:913024"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113290
     Region          24..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskftwilt lffglmvqvg faqkpvtgvv ktqdgdpipg atvmlvgtdl gtdtdeegky
       61 tlilkkgdkv qvtfsgfktt tvtasdsgvl nitlvedmda mleeiivdty rttskpksnv
      121 aantvtskti egrpnasfiq tlqgqvpgln iatgsgqpgs sntmvllrgi gsingstepl
      181 yvidgvpmss anfrsinqnd iervdvlkda gatsiygnrg angvivvttk rasfaqdlqi
      241 kyvgttgist lqkhkynlmg gqelmqfenq tqknnvrwta aqirngaetd wmdyffreaf
      301 sqnhtlsfss gssnlsqfts igytahegtl kntdlkrfnf rnnlngknqn grltyntsit
      361 gnysrsnqai slgtgsvnln palsalrgvp yfspneydin dpygsivgvy saspnnqnlv
      421 kiaplmiidq lnyfknysde lksivsggln ydlgsgfsvg tnlgidytdv kqiqfdspys
      481 fnselfrean qeyvgyerey ntrivsfnst snlkwskifn qkheiragay leylkahytf
      541 ssfsqngldp yfsapgagtg wigdtedndl yvpnisknva esglfsyfgm vdydydskyg
      601 igltlrrdas frfseenrwg tfwsasarwn inredfmkds kinelklrgs ygtagnqdiv
      661 ssglfggnsl freqyslsgl syndqpttfi snipnpnlrw etieqanvgi dfgvwnsrfr
      721 gsvdvyqktt kdlyqsrpms aihgassisd nigsmrnrgv ellvsgdivr nenltitlna
      781 ngsynknefv elagadengv vwnggltvmq eggafgqfyl veyaginpdn gnllfldkdg
      841 naverfvdad rkftgksyip kyqggfgldv dykgwflsss ftfvkdvwrf dydysslvhp
      901 dnignwnmsr dmydywtptn rnasmpsvna tnmpyqnfsd rnirdasyir lrfatlgynf
      961 kqddlrfigl sglrvfaqae nlftwskwkg wdaessrgsd qsqyptpkti sfgvevqf
//
LOCUS       WP_091538099             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Modestobacter sp. DSM 44400].
ACCESSION   WP_091538099
VERSION     WP_091538099.1
KEYWORDS    RefSeq.
SOURCE      Modestobacter sp. DSM 44400
  ORGANISM  Modestobacter sp. DSM 44400
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Modestobacter.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Modestobacter sp. DSM 44400"
                     /db_xref="taxon:1550230"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51483
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvvhesr paetrvaatp ttvgqlrglg yevvvaagag lastfpdeay aaagatvgta
       61 aqawaadvvl avnapsaqei aglrdgavli slltpalape lldalaarpv talamdavpr
      121 israqsldvl ssmaniagyr avveaahtfg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igtasslgai vratdvrpev aeqirslgge yvavapaeqq vssdgyaret sadhdrraaq
      241 ayaeqaadvd iiittalipg rpaprlitee mvasmrpgsv vvdmaaamgg nvagtvadel
      301 vvtsngvsii gytdlpgrlp aqasqlygtn lvnlmklltp gkdgqvvldl ddvvqrsmtv
      361 vhagektwpp ppvpvsaapp papaaqvpvv paavpsasrr figvglaaal lfvltalspg
      421 pliehltvfa laivigfyvi ghvhhalhtp lmsvtnaisg iivvgallqv grgdpvvtal
      481 aslavlvasv nvfggfavtr rmlglftr
//
LOCUS       WP_091538676             993 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflexibacter ruber].
ACCESSION   WP_091538676
VERSION     WP_091538676.1
KEYWORDS    RefSeq.
SOURCE      Thermoflexibacter ruber
  ORGANISM  Thermoflexibacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Thermoflexibacteraceae; Thermoflexibacter.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Thermoflexibacter ruber"
                     /db_xref="taxon:1003"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108404
     Region          30..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnysnyfk vlgalcllll isgvswaqyt vkgtvrdeas ktalpgvnii vkgtntgait
       61 dalgnfqiai nnndkatlvf tfigylsqnv evspsktnve iilvedvtkl eevvvtglas
      121 dikrsnlana vstvsakeli gttqiqtvdn alygkltgvn intnggapgg gvsvqlrgia
      181 slvgasqply ivdgvyinna tnrsgratvt qagasnqdda pnrladinpn diesievlkg
      241 psaaaiygtr anagviiitt krgkagkski sfeqdlgfar pqrllgvdnw seekirtffp
      301 aarqaieier frqsagrtyd yekyfydnta llsntrlnis ggndkttffi sgaltdedgi
      361 irrtgfkrrs lranidhklt egiklnvssn yinsetdrgf tgnqnntgas igyniayvpn
      421 yfnlfpneag vypinpyfse npvavtdkgi nnskvhrfiq sfnltanllk tdnsllrfia
      481 qggldftqns tlvylpedlq fqvgqanpgd alvgktenln tnlqlaltyn fnvgqvnfns
      541 qvgtvrlnfr ensllnrsrg lapgqknlrq gtvqeiiqdf gvfakdvgvf aqqeanwndk
      601 viatvgvrwd kstlngnadk fyafpkasla vnvanfdfwk fksvvnqvkp rvaygetagl
      661 pdfgrtftal naaniggllg stvstiagnt nilperatel efgldlglfd nrvvieatyy
      721 dkktknniqn ltlspsvgis stpsnlaels nkgwevslgg tpvqkdnirw ftrlmywnnr
      781 lltsrlgipt yttgafgtal gtfliqegvs pntivgtpqi spgvftvwgn sqpdfqmswf
      841 nevnflknfq ftmlwhlkqg gdninltafl tdsggttpgw fgddngdgip ngrqrppapy
      901 nnagrwvqda sylrlreial yytlpknvls nlfkdkvdri rigvsgnnif tstkyfgydp
      961 etstfgaqsi asgvdiapyp tqrrifghlv idf
//
LOCUS       WP_091540086            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflexibacter ruber].
ACCESSION   WP_091540086
VERSION     WP_091540086.1
KEYWORDS    RefSeq.
SOURCE      Thermoflexibacter ruber
  ORGANISM  Thermoflexibacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Thermoflexibacteraceae; Thermoflexibacter.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Thermoflexibacter ruber"
                     /db_xref="taxon:1003"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120213
     Region          29..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnfyrffl flgvaigllf smnmqaqdkm lrgkvtiast geefpgvsvf ikgttvgtvt
       61 gtdgtyslkl ptnanivvfs fvgyksveva iggqstidaq lvedvqslne vvvtalgvek
      121 ekkalgyatq tiqsndliqa retnlvnsla gkiagvtvvg nptgiggsar viirgersln
      181 innnqplfvv dgvpisnnny gssgrsnqea dygngagfin pddiesmtvl kggaasalyg
      241 sranngvivi ktksgrgtkg igatvnstlt fenvlrlpey qnvygqglgg vfefrdgngg
      301 gladgvdesw gpayngqlir qfdsptsngr rggdvgnlnt rigpvnlaaq laargeiqpt
      361 pwvarpdnvk nffqtgltft qnvalagsne ngdfrvsyty ldqkgivpnt dlnrntfafa
      421 ggynlskrlk aravinyikn tsgnrpnlsy gtenimylfn cwlgrqvdvq amrdywqfgr
      481 eglnqfgfny nyhdnpyfnv fentngqsld rvygnlslty qftdwlnlmv rsgtdfsnef
      541 rdrrraystq rfplgsyree kifyeerntd fllsanknls etisltasvg gntltqvfnt
      601 sdvsapelav pgvyslgnsr vaiqasafrs kkrinslyas aqlgyknfly ldlsarndws
      661 stlpkgewsy fypaanlsav isdmvelpkl isfakarvgi aqvgndtqpy qlqavynaet
      721 pvkglpayge ssvipnlnlk pelstsfeag idvrllegri gidftyyntr srnqiigipl
      781 snttgyssri inaglienrg ielmlnvvpi qldnsirwsi dfnfsrnrse vkelaegiqn
      841 fvmasrylsv earvggrmgd mygigfarvq ntdpngkyyd ptgqfvgqvv yntagkpipt
      901 dqvinlgnyn pdwmlgitnt lsykginfsf lfdirqggkv yshtqtvgre ggmiietleg
      961 rangydlslp gngvigqgvv qnadgsfrpn dfklsarewh tsitlgrrll egmvydasfv
     1021 klrevklgyt lpnkfmgrlp frdvnisfvg rnlflwtnvp hidpetasta ggtiipgies
     1081 valpstrsyg fnlgfkf
//
LOCUS       WP_091540316            1221 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflexibacter ruber].
ACCESSION   WP_091540316
VERSION     WP_091540316.1
KEYWORDS    RefSeq.
SOURCE      Thermoflexibacter ruber
  ORGANISM  Thermoflexibacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Thermoflexibacteraceae; Thermoflexibacter.
REFERENCE   1  (residues 1 to 1221)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1221)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1221)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1221
                     /organism="Thermoflexibacter ruber"
                     /db_xref="taxon:1003"
     Protein         1..1221
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=135722
     Region          55..118
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          163..1220
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkllyktn wrfyyfitaf alllqtslqa qtlarrqddl slryqvgdlk kenvqslknv
       61 lknleskynv rfvyagtvka dkltvttipq sdkieqvlen llvplglryq qmesqlfiit
      121 pekpkenike ipntassvft pleistlpll nagikrellr iekritgtvt saednspipg
      181 vnivakgtnv gtitdsegky slsvpdnttt lvfsyvgfat qeveignrtt idvkmaldvk
      241 tlqdivvigy gerdkkdltg avsvvgaedi aksvamqpel smqgrmagvf vstpggnpna
      301 rpqvrirgvs tfgyaeplyv vdgipltefg dgvsggligd irgnvnvlnl inpndiesis
      361 vlkdasaaai ygvrasngvi littkrgksg rpkvefnasr gvqnipkkfd mldvnqytrl
      421 yqeayannpd eaknlppefn pqspaflgnr ptvdwqtpli qrnaitedys akvyggndat
      481 tyyvsagygr tqstlvqndm erysfatnvk sniskifevg atyrlgyina ldntrtdlgy
      541 vsrtspwqqi fdpthptgfa psisarfrpn pelgqntqrp lfllpipaqv fdgdptllwg
      601 vetnnnvfaq qalndtrynm lrnmgtaylq mepvkglkfr gtfsadwyyn krndwndfnn
      661 ylfsqtpgnp ysgndgtskg gygerhtrnt nfvkefsvsy nksfgdhsfd vilnamdqey
      721 kydflqassg qipfsdplfr ninnlppfsn agsfrninrl qgymgrvsyk yadkyyadvt
      781 vrrdgssrfa pgykwgtfps falawrisre dfmkdltfin dlklrggwgq lgnqetasfa
      841 flssvsttpd yatgsgagna vgnlrfgvrl pdfpvvdlsw evasttnvgf dgvflnnkit
      901 atveyysrlt sgilqgsqlp asvgnenqpi lniasvrnsg velqlgyngk igedftfnig
      961 gnlttvrnrt isvfrdqpfg geggrievgy plfflwgykv ggifqsqeei nawtatkrda
     1021 nngnnfkpgd myfedvrsap tepgktysde pdnvvnafdr tyigktiagy fyginlsanw
     1081 knfdlsiffq gigdvqking erwggesmss tgvnqwttvl nrwtpqnpst tmpravrndp
     1141 agnnrfssrw venagfmrlk nfqlgyslpr slmsktgvid rcrvfisgtn vftftrwtgp
     1201 dpendilppa rtfmlglsat f
//
LOCUS       WP_091548882            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflexibacter ruber].
ACCESSION   WP_091548882
VERSION     WP_091548882.1
KEYWORDS    RefSeq.
SOURCE      Thermoflexibacter ruber
  ORGANISM  Thermoflexibacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Thermoflexibacteraceae; Thermoflexibacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Thermoflexibacter ruber"
                     /db_xref="taxon:1003"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117718
     Region          30..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkmkrslpcc gialllslll ftqsfaqnrv sgtvssakdk splpgvsviv kntqrgtitd
       61 segkysiavs sgetlvfsfv gfalreiais nqsvldvale edvtqlgevv vtalgikkea
      121 kklgyatasv tpdqininrt vnfmnalqgk magvnittlg sgpagtskvr irgqssfggt
      181 naplivingv pidntnfala qgnqgsdgsi qsrgnnnsdg gdglssinpd diesmtvlkg
      241 ataaalygsr akdgvimitt ktkgvgkgig vefnsnfttd ipmiltdwqy eygqgeggvr
      301 pttanptsgv wsfgekfqpg mtqvlfngvt vpyvpqrnqi reflrngntf tntislssgt
      361 drggfnlsis nmdntgimpn nsfnrktfnl gftqtlgekl ivsgnanysk einrnppqfa
      421 qqdfsvptvl ytiansmpmd vlrdnafdaq gneyiwsrfr nrtnpyfnma rkfenifrdr
      481 lfgnitlryn ikdwlyaqvr vgqdfwtrqq eynfptgaas lapapagfvn gsfiqevrrl
      541 revntdflig atrkfgnfgv datfggnqly vqselnsaqg tdfvvrdlyt imntrvrdpi
      601 ygfserkvns lygaaefsyk nflflnvtar ndwfstlspe nrsilypsvt ssfvfsdafn
      661 nmpswlnfgk iraayaevgs dtdvgsyann lfyginanlf pigttsgqap lgfisgltvp
      721 nanlrpmrvs eaevglelkm fnnrvsvdfa fynkvtkdqi vsaqisdasg ftstrinsgq
      781 srnrgfeylv nvvpfqsdnf rweisfngsy nttlvqriit ddngtdrdyn gdgrpeqivv
      841 gnsiwnpgqg qirqvvgqpm gtlfanayak daqgrrvfdn agfpvivplq pfgttipkwv
      901 ggitnsfnyk gimlsflidy klghimssgt nfnawrhglh kgtlpgreqn rivgegvnqr
      961 gevntvaapl qqyyeqvrsr digeqfiyna gfwklrqita gydftkhlps swfikglrln
     1021 fvannvlilr kwvenidpeq mgygsdnlng leatgvpttr sfgfnlnvkf
//
LOCUS       WP_091548992            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflexibacter ruber].
ACCESSION   WP_091548992
VERSION     WP_091548992.1
KEYWORDS    RefSeq.
SOURCE      Thermoflexibacter ruber
  ORGANISM  Thermoflexibacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Thermoflexibacteraceae; Thermoflexibacter.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Thermoflexibacter ruber"
                     /db_xref="taxon:1003"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114778
     Region          23..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrllltgil cvfflgslla qdrtisgtvt ssedksalpg vnvvakgtna gvitdtegky
       61 klnvpagatr lvfsfvgfvt qeveignrtt vdialdpdtk qlsevvvtaq giarekralg
      121 yavasvgqda iadrpladvg rvlqgkiagv ninqvsgvsg tgtniiirgy ssitgsnqpl
      181 fvvdgvpfns atnqrggftq ggqaapsrfl didpnniesi nvlkglaasv lygdqgrngv
      241 ilvttknasa knkpaeinft qslfansail pvyqntymgg fqqnpgyffs nwgprldqvp
      301 dnnplklnhp faslsnaalr aemaewvann pftlqfypnn vrdffrtgli stsnlnltgg
      361 nattsynvsv gynreqgyip nndlkrltlg lgartqvikg vtiqtsfnfi ntdmqtppls
      421 gsggnnayda psvlanvfft prtvdlmgwp fespvtnqsv yfrspndipn prwilkyykt
      481 psitnrffts nsvivdlaen lsvtyrvgld tynelqenqy nkggvnfvqg ryetrnitnt
      541 iwnhdvifsy skqlnenltl aaklggnmrn drfeqqsats vnqlafglmr hqnfidnvag
      601 sfteeqtrmg vygevtadyk nylyaniaar ndwtstvele nrrifypsas vsfiptsafe
      661 glqsnflnfl kiragvgtsa gfpspystrn ilnqnarafl dasgnvtqth tvdnflgnpn
      721 lkpeliteye agletklfnn kigvdltlyr rettnlitnt pidpstgfts tainigkirn
      781 sgielainat pvrtdnftwe tvvnysrvvp vtvelggslq evvvagftnl gnfavpgrpf
      841 niikgtailk dangnrvvgg dgnylsdpni relgnpnpaf ntswintlsy kglslnvmle
      901 yrhggaiyss tagavigrgl skdtefdrda tfilpgvkqd gspndiqvta sdthfnnyyf
      961 fgdegrmfdg ttirirevsl syslpknivg ktpfkgvsfs lqgnnlwfra vnmpkylrvd
     1021 penlglgvgn glgfeflagp aarrwggtlr ltf
//
LOCUS       WP_091557790             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. ok362].
ACCESSION   WP_091557790
VERSION     WP_091557790.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. ok362
  ORGANISM  Arthrobacter sp. ok362
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Arthrobacter sp. ok362"
                     /db_xref="taxon:1761745"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38483
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqvgvgreqr agerrvaatp etvqqltalg lhllvesgag teagfadaaf keagatvise
       61 lpfealdvll hvrpitpeaa arlrpgtvti glaspatelr tvralaaagi tsfalellpr
      121 israqsmdal ssqslvtgyr avleaavryp rffplymtaa gtvpparvlv lgagvaglqa
      181 igtakrlgar vsandiraas adevasmggt finldvdaaa egtggyaral gedraqrqrs
      241 llaphvaaad ilittaaipg rpapllvtta mvasmragsv vvdlaaesgg nvegviagqd
      301 vqvpvdggsv tlvglqdaas ampsdasrlf arnvsnflal mtdgglvapd fdddvvagtc
      361 lthggavrha ptaaaletea
//
LOCUS       WP_091566766             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oryzisolibacter propanilivorax].
ACCESSION   WP_091566766
VERSION     WP_091566766.1
KEYWORDS    RefSeq.
SOURCE      Oryzisolibacter propanilivorax
  ORGANISM  Oryzisolibacter propanilivorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Oryzisolibacter.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Oryzisolibacter propanilivorax"
                     /db_xref="taxon:1527607"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55620
     Region          11..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtpnapqaq rigvpreifp gekrvatvpd vveklaklgf tvaietgage aanfdddsyr
       61 aagaqvlpda dalwaasdiv lkvrpptpee varlrpgsil igfvwpaqhp elmqqlsqrg
      121 atvlaidslp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee dgsggggyar
      241 vmsegfqaaq rqmyaqqare adiiittali pgkpapklit aemvrsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti igytdlpsrl akqsstlyat nllrlveelc kakdgvavvn
      361 meddairglt vvkdgaitwp applaappap apkaaaapva ekksahgpga pmsaktltiv
      421 favlavlfwa igayapeafl ghftvfvlac figymvvwnv tpalhtplms vtnaissiia
      481 igalvqiapp eaglngrpdg litwlafaal vltavnmfgg favtrrmlam frk
//
LOCUS       WP_091580923             427 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium qingshengii].
ACCESSION   WP_091580923
VERSION     WP_091580923.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium qingshengii
  ORGANISM  Mesorhizobium qingshengii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Mesorhizobium qingshengii"
                     /db_xref="taxon:1165689"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43959
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvvvetg agtrsripde efskagatig
       61 kasdvakadv vlkvrrpmda elksyksgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedde fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegav
      301 agqvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggki vhpafikadq qphvepaaip akamvadasg kpaaakkaap rkpaasksps
      421 skskgta
//
LOCUS       WP_091592721             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium muleiense].
ACCESSION   WP_091592721
VERSION     WP_091592721.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium muleiense
  ORGANISM  Mesorhizobium muleiense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mesorhizobium muleiense"
                     /db_xref="taxon:1004279"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43314
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripde efakagaaig
       61 kagdvakadv vlkvrrpdea elkayrpgsa viaiidpygn daavdalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fvmgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqatltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafle tlvdktaktl ainrddelvk
      361 atmltdggqv vhpafagkpa vmiasaepak paaakdpaqp kkaaasrkaa apkspanksk
      421 gia
//
LOCUS       WP_091605285            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            dokdonensis].
ACCESSION   WP_091605285
VERSION     WP_091605285.1
KEYWORDS    RefSeq.
SOURCE      Maribacter dokdonensis
  ORGANISM  Maribacter dokdonensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Maribacter dokdonensis"
                     /db_xref="taxon:320912"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112989
     Region          26..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktyhvlsv lmlmlfslst yaqtstvsgt viaedglplp gatillkgtt tgastdfdgn
       61 fsiqlsnsns ktlvisyigy kteeialtgm nqtinvtlme dsnaldevvl vgssvtqsrk
      121 klgnaittvk svelvkaspa nittslqgkv pgaqitqnsg dpaggfsirl rgpstikgss
      181 eplyvvdgvi tsnlttnvtn lnvdagdaap gqnrmvdinp ndienvniln gaaaaaiygs
      241 rasngvvvit tkkggnyedg pefyfkstfs vntirkkldl nligeefetv pnsdlsgrlw
      301 pifgfdpndg nalttyrnls tdkfettryd yqdeifqtgf gsdnyfstkg gnekmgymas
      361 igyltnegii kntkfdrfsa rvnfnhkvtd wmsydlglyy ansksdekpd gnvfwspins
      421 initnntfdi tqrdangnlm aventrvnpl tiietfditq dvnhfipnlh lkikptekls
      481 idqiigvdty nqkgniyipv ypyenvnpay yddgyigsae akvfnwnydi nmayntnitd
      541 klnsvttagy sfqsselsfe gtqgrgldsn neptiplqtq pidtnldiyg fflqetlswd
      601 nklfltlagr idgatnfdvd ersnfypkvs gsyvlsnepf wntesflnsa rlrasygeag
      661 nltaispyer ygsytsndfl gsstlqqntr lgneglkper tkefeigtdl sffnnrasll
      721 ftyyrqnied livsrvlaps lggstrtenv gtmrnngiel yakitpiktd dltwdlnfny
      781 ssnrnkvlst vggditiesv tgappivreg eslgvfygty yatddngeli ltgestdgsp
      841 vgvpqqergd lttntpqrda dgqptgdvlr kvigdpnpdy ilgigtdlty knfnfsmlwe
      901 avqgfdvfda dkrtrqgvgv gqlaaqeltg elprgyiagi ypieefried gsfvklrevs
      961 lgyefpslfn sslenvrlsl igrnlvsfdk ffsydpetna ggqsnllrsv nfgnvpipmt
     1021 islslsanf
//
LOCUS       WP_091606479            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            dokdonensis].
ACCESSION   WP_091606479
VERSION     WP_091606479.1
KEYWORDS    RefSeq.
SOURCE      Maribacter dokdonensis
  ORGANISM  Maribacter dokdonensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Maribacter dokdonensis"
                     /db_xref="taxon:320912"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116917
     Region          25..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktllitml vflasfvaha qtvftgkvld enqvplpgat vvvkgttngv atdfdgnfsi
       61 elngsndilv vsyigyiaqe yntankitgt inlqpdsqql devvvtalgi erekkslgya
      121 sqeldndevv qaresnllns msgkvaglqi tnsptglggs arvsirgdas lningnsplf
      181 ivdgtpisne ivgssgsgtq svdygngaae inpqdiesin vlkgpaaaal ygsraangai
      241 iittkkgksq ssklgvsfnt gitvenvlml pdwqneygqg nnqqfsfvdg sgsgiadgvd
      301 eswgprldtg lmiaqfdspr tdgtrggdts vsnadiiptp wvsqpdntkd ffetgitktn
      361 siaisksgem gnmrlsfqnl dqegtlpntd lnrntlsfsg tmnvsdkvkv nanlnyvktd
      421 sdnrpavgyg tesimylfiw ygrqlntnnl rdywqpgleg iqqfnynyny hdnpyftmye
      481 ntnaqdkdrm fgnvsltydi senwklllrs grdfyrdfrv rkrafstqrf pfgtyqedni
      541 ffeesnsdfl lsydktfgek fnlnisaggn qlrqkqdftk svapqlinpg vysfnnsrqa
      601 vqvssnnsek rinslygyar fgydnvlfmd itgrndwsst lpegnnsyfy psvtlsaias
      661 dmfnmpdwvt fakvraayae vgndtdayrl rsfyqnetqf dsstpiltes slipnanlkp
      721 eitgsyefgl dlrflqsrin ldmtyydsat knqiinistd iasgyssqli nagevrnygf
      781 eaianfvpvl tdnfkwsstf nfatnksevk dlgddiqftl teangayiqa reggsisaiy
      841 grgfqrvede tseyfgqmii nnqgipertd dlvyqgdyap dftlgiqntf kyknvdlgfl
      901 idtrqggivv srtktigsts gqlqetlegr etgivaegvi ntgtaenpvy tpntinvdar
      961 tfnnryyerd nveaakydas ytklrevslg ysfpqkmidq lpitnarisv tgrnlilwtd
     1021 nphfdpetvg vsggtlqpgi enmsypssrs ftfnlqvnf
//
LOCUS       WP_091606605            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            dokdonensis].
ACCESSION   WP_091606605
VERSION     WP_091606605.1
KEYWORDS    RefSeq.
SOURCE      Maribacter dokdonensis
  ORGANISM  Maribacter dokdonensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Maribacter dokdonensis"
                     /db_xref="taxon:320912"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116411
     Region          25..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngllt lllalvvhis faqqktvsgt vtdqgglplp gvnivvegtt tgtqtdfdgn
       61 ysimasqget llftyigqka vrksvgagst vnvqmeedaq aleevvvtaq gikrekkalg
      121 favssvdeed lesraegdva rvlsgkasgv qitsaggmsg satnvvvrgl ssfsgsnqal
      181 fvvdgvpfss dtnaqdtngg gsnfltgntg ssrfldldpn niakievlkg laaatlygsq
      241 gkngvilitt kagssvggkk kteitvnqsy fvnefaslpd yqdeygngfd qafgwffsnw
      301 gpsfeesgls gwgrqsaide ngtlehpyss tavaatreaf pelqgtrydw kpydsvedyf
      361 kpgsvsstsv ningasedgn ttfnanfgyl ddesfvpgng ltranvslgg rsklsnkftv
      421 sgamnysrtd yssppiaase gngttglsif gniyftprsv dllglpyqnp idgssvyyrn
      481 gndiinprwt ennvkysqlt trvfwnasvq ydindnlnmt yragldyyne rneqysnkgg
      541 vaftsaifgf lntydnnnti wdhylalngn ydlseklgls fnagattrst tfdqqgvast
      601 gqivfdiqrh fnysnqspiq ysekrniagl lgqvtldydn mlfltastrt dwvsnltten
      661 nsqtypsasa sflptaawpg iksekglnfl klraglgqsa tfptayptvs vveqntqvyg
      721 eggevttnqv aafkanpdlk pellsefevg feskffnnrv sldftyfdrt tkdlivrepl
      781 spstgftftq snvgkiegdg ieidlgvdwv rgdnfnwntr anftknkfiv teqeqdiiiy
      841 agsstlsvgg naaikgeqlg vivgdaiard adgnfliddg gdyvttevda ngnvpvignp
      901 npdyimniin slsyknwnlg fqfshtkggd ivsntigtll grglitetld rentyilpgv
      961 sqstgevnnk qinnstyyfn nilfgptelk vydasvvrlq elslgytfpa kalertpfgs
     1021 ltitaqgfnl wydayntpdg anfdpniqga gvgnsqgfdf ingpssrryg vsikatf
//
LOCUS       WP_091607182            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            dokdonensis].
ACCESSION   WP_091607182
VERSION     WP_091607182.1
KEYWORDS    RefSeq.
SOURCE      Maribacter dokdonensis
  ORGANISM  Maribacter dokdonensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Maribacter dokdonensis"
                     /db_xref="taxon:320912"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110561
     Region          25..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkissflt vavllffqav igqdktvsgv vtddtgsplp gvnvvekgtt ngtstdfdgn
       61 ysinvdanst lvfsslgykt kevgvngrst vntsiaedas eldevvvtal girketkalg
      121 ysltevdaee iatiktpnai nslqgkiagv nisqnatgaa gssrvvirga sslsgnnqpl
      181 yvvdgipign gnngsaslwg gsdggdgiss lnpddiesis vlkggaasal ygsraaggvi
      241 ivttksgkgq egfgievgss vtfdkvdtsl qdfqteygqg vrgvrpssqs aaleagsssw
      301 geaydgvnsp qfdgvsrpys ylgnnvdkfy rtgstfintv aitsakenlt yrlsasnldn
      361 advlpnagln rksfsfnssa ilgdkitssv nakyiiekvq nrprlsdspg nanfsvallp
      421 gnidvttlqp stnpdgserq fsnntfstnp yfaaynfnne dvrnriiast slrydildwl
      481 sltgrigidn diirrtsvep fgtaykplgg ineeerrynq vdadlilaae kditdkfais
      541 alvgannnhv ksenlflggn dfivpgledi gntvsqsrsr eyserkigsv ygslelsydr
      601 wayvtftgrn dwfstlsfpg kttpnddfyp svngslilsd afnmpsfvsf lklrggysev
      661 aggaqdpytl alnyeifgip isgqplgrvs gsivpnanlv afskseteig ldmrffnnrl
      721 sfdvayysne ttndivdvst siysgytgas anlgkvtneg veflisgtpi rtndfswnmt
      781 vngayneglv vatddvnsdv nldeprtqnv rithivgety gsivgvsyer dengtivyev
      841 gddgvprave gerkilgegv ppltlgfsns ftyknfnlnf lidgkfggqi fsgtntilys
      901 nglhkntleg rengltvsgv dqtgaafttt vapenladyy geiadiaeef vedsdyikfr
      961 qlslgyslpk kaldnvfltn vnvsliasnl fyikrsvdni dpesaysvgn sqgleyfgvp
     1021 ssrsygltin vkf
//
LOCUS       WP_091607891            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            dokdonensis].
ACCESSION   WP_091607891
VERSION     WP_091607891.1
KEYWORDS    RefSeq.
SOURCE      Maribacter dokdonensis
  ORGANISM  Maribacter dokdonensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Maribacter dokdonensis"
                     /db_xref="taxon:320912"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117378
     Region          21..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhlllvltl fictmvnaqe titgtvkdtd gntipyvniv lsgtlngttt nengiytidv
       61 pnlsgalefs vlgyetkift innrrtidiv lgdssevlde vvltalglkr etkelgyvvq
      121 sldakgvtev ksvnfldnls gklagvtinq gatgvgsssk itirgeasfs nnnplfivdg
      181 vpinnnsvfn ftneaaagfq eidfgngame vnpddiaevs vlkgpsaaal ygtrasngvi
      241 iietksgkns kglgisynts ffvdsafqlp dfqneygqgn sgefafvdgl gggtndlity
      301 swgprldvgn lipqydspvt lpdgtvvrgg dtalysgipi tptefrsqpd nlknfyetgt
      361 tlinniaisn gfdtgnyrls ftdlrsesii pgvdldrqtv sarlnfqpvd klrinssisy
      421 insnsdnrps ngygsenany slvawgprsl nienlknywq pglegiqqys ynytffdnpy
      481 filnenrnsf nrdrvfgnis asyditdhlt atvrtgmdys selrqlrray ssnrfanggy
      541 aehdvfyrev ntdfllnytn qfndfnidvs lggnrldqka ftsqsqttsl aqpgifrlsn
      601 aaspievfef esnkrinsfy glakigykdf lfldvtgrnd wssalatpfs vdntsffyps
      661 vsssfivskv vnlpevisfa klraswaqvg ndtdpyqttg afvaqtpfng qptfsnsnti
      721 anadlvpelt ssfevgadlr ffndqlrfdv syynaltkdq iislpigiss gytqqvvngg
      781 evrskglevi vgvspiisqn fkwnstlnfs tnrstveslp qdegrltlay sriydsqnqt
      841 vflqaeeggr vgdlygtgyl knengdfilt degryipdne lqklgnynpd fmlgfnnqfn
      901 yknwnmgfll dwrqggiivs rtralgnvgg qlaetafrpe tgivpegvvn tgtddnpvye
      961 antvavsaes yyrqfydrnh eenntydasf lklrqlsigy tfnnlslfnq datlslslig
     1021 knlfaitenp hfdpeqlavq gqgfisgved msyattrsig fkagfnf
//
LOCUS       WP_091620697            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            orientalis].
ACCESSION   WP_091620697
VERSION     WP_091620697.1
KEYWORDS    RefSeq.
SOURCE      Maribacter orientalis
  ORGANISM  Maribacter orientalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Maribacter orientalis"
                     /db_xref="taxon:228957"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110433
     Region          24..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitflksll vlstflcfgl sqaqevsgtv sdasgplpga svlekgttng tqtdfdgnyt
       61 ltaqdgavli vsyigyktqe vaingrssin ftleedaeal eevviigygt ttvkdatgsv
      121 tavtakdfng gniaspeqli qgktagvniq etsgepgagi qinirgsnsv rannnplfvv
      181 dgvplgggdt spqgetgfgq savknplnfi npndiesmsi lkdasataiy gsrgangvvi
      241 ittksgkgss kgvfdfsssl siataantyd lldgpeflag vaavggdana vnfgsntdwq
      301 qvvlrstasq nqnlsyskny gsgnvratfg ygkqfgiven sdleritgri nfnqrflddk
      361 lvlglqmsva rindsqapis aqagaagdvl ggayaanptw passsfnagg lnvnpqnald
      421 ntqnltntdr yllngsvqyn ftpeisakln agldkaeasn tsviskninn ingvsgvgrg
      481 nysvlernnk tfeatvnynk efenssleal vgfgyqdfqt fgfnaggrgy ntgdlnamgs
      541 dlrsavsdlq nsvtgsyqqa yyatnsngvl inrlfpnvvp qeelgrslss svtsvytdaf
      601 dntdelqsff arlnytlnnk ylftgtmrad gssrfgpenq ygyfpsgafa wkineedfvg
      661 envstlklrl stgitgnqdg lgygnfvarq rfsgltiqqn leitpngtei vatdrpdlkw
      721 essfninagi dfgfnndrfs gsfdvyrtkt tdvllqtppa spavdpfqfs nvdasiinqg
      781 velalaydfv qsddttfsad fniaynnnev qdfaglidtg avngpgltga faqrfasgqs
      841 lysyylpvfe gfdnagnpiy qdvdgngvgd pfgdkkfvge dalpdittgl slnlrvkdfd
      901 asvffqgqfg fsvynntdna yfnagalsns rnvtqnvign genpgasada strflekgdf
      961 vrfqnasvgy nfplsgegal dalrfsltgq nlflitdysg ldpevtantg dlgsgvpsrg
     1021 ldygsyprpr titfginasf
//
LOCUS       WP_091608671            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Maribacter].
ACCESSION   WP_091608671
VERSION     WP_091608671.1
KEYWORDS    RefSeq.
SOURCE      Maribacter
  ORGANISM  Maribacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Maribacter"
                     /db_xref="taxon:252356"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110549
     Region          24..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitflksll vlgaflcfgf lqaqevsgtv sdasgplpga svlvkgttng tqtdfdgnyt
       61 ltaeegavli vsyigyktqe vavngrtsin ftleedaeal eevviigygt ttvkdatgsv
      121 tavtaedfng gniaspeqli qgktagvniq etsgepgagi qinirgsnsv rannnplfvv
      181 dgvplgggdt spqgetgfgq savknplnfi npndiesisi lkdasataiy gsrgangvvi
      241 ittksgkgss qgvwdfsssl siskaantfd lldaseflsg vtsvggdasa vnfgantdwq
      301 qvvlrstasq nqnlsyskny gsgnvratfg ygkqfgiven sdleritgrl nlnqrfledk
      361 lvlglqmsia rindsqapis aqagaagdvl ggayaanptw passsfnagg lnvnpqnald
      421 ntqnitntnr yllngsvqyn ftpeisakln agidiseasn tsvisrdinn ingvsdigrg
      481 nygvlerdnk tleatvnynk efenssleal vgfgyqdfqt fgfnsggrgy stsdlnamgr
      541 dlrsavndlq navtgsyqqa yyapntngvl inrllptvva qeelgrslns avtsvftdsf
      601 dntdelqsff arlnytlndk ylftatmrad gssrfgpenq ygyfpsgafa wkmneedfvg
      661 envstlklrl sagitgnqdg lgygnfvarq rfsgltvqqn leinangtai vatdrpdlkw
      721 essfnlnagl dfgfnndrls gsidiyrtet tdvllqtppa apavdpfqfq nvdasiinqg
      781 iefalaydfv rtddatfsad fniayndnev qnfdglidtg evngpglsga faqrfasgqs
      841 lysyflpift gfdsagtpty qdvdgngvgd pfqdktfvge dalpdittgl slnlkvkdfd
      901 asvffqgqfg fsvynntena yftagalsns rnvtqsvlts gedpgasada strflekgdf
      961 vrfqnasigy nvplsgegal nslrfsitgq nlflitdysg ldpevtantg dlgsgvpsrg
     1021 idygsyprpr tftfginasf
//
LOCUS       WP_091621960            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            orientalis].
ACCESSION   WP_091621960
VERSION     WP_091621960.1
KEYWORDS    RefSeq.
SOURCE      Maribacter orientalis
  ORGANISM  Maribacter orientalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Maribacter orientalis"
                     /db_xref="taxon:228957"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115599
     Region          25..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngllt lllalvvhis faqqktvsgt vtdqgglplp gvnivvegtt tgtqtdfdgn
       61 ysimasqgqt llityigqka vrqtvgagst invqmeedaq aleevvvtaq gikrekkslg
      121 yavssvgeed leqraegdvg rvlngkasgv linaasgvsg satniiirgf tsisgsnqpl
      181 fivdgvpfss dtnnqgdaid gnvgssrfld ldpnnianvn vlkglaaanl ygtagrngvi
      241 littkagstg tgkkkseitv ssslfyneis tlpdyqdryg ngfdqaygef fsnwgpdfni
      301 anpnsfgdkw rgttsdgtil ikhpysnnaa vsaafpeyqg qtyeykpydg vknffrtgtv
      361 tnnsvsasgs sddgkisyna svgnlrdegf tpgnklqrtt fsiggkaels nrftvngtmn
      421 ftksdvkspp iaaslgngat gdgasvfghl fftprsvdlm glpfqspidg rsiyyrggnd
      481 iqnprwtaen afanqltnrv fgstqftyki ndninaffrt gldfyserne igqnkggaeg
      541 yiqgryqtyd nkntiwdhta qingmwqlte kldmnvnlga tsrrtefsrq gvtsdqqsif
      601 gvfrhynfat qapvqrdetq nimgvyaqte fgydnfaylt laarndwvsn fiensifyps
      661 aslsilptal idglqsqngl nflklragyg tsagffggyp vantatldtr eflkdgtlvs
      721 sitvddelan pglspellke lefgletrfi nnrvsldvsv ykknttdlis eqpldpstgy
      781 tstvtnigev qvkgieadlg ltlfrndnpg gfnwninanf tadestvidl gqdtdninig
      841 gifsdlsnfa vtnrpfgiim gsrvlrdend nkvvssngff veenglfeig dpnadwrlnv
      901 sngfnfknfs fnfdisyrhg gdvysntisa lvgrglttdt edrvstfvlp avkadgsvnd
      961 iqinnsdyyf snvafgpsel qvydgstlrl relrlgysvp skaleqtpfg slsftvsgqn
     1021 iwfkglnvpd gtnfdpenlg vgvgnalgfd finspgsrry gmsikatf
//
LOCUS       WP_091625182            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            orientalis].
ACCESSION   WP_091625182
VERSION     WP_091625182.1
KEYWORDS    RefSeq.
SOURCE      Maribacter orientalis
  ORGANISM  Maribacter orientalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Maribacter orientalis"
                     /db_xref="taxon:228957"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117742
     Region          21..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhifmvltm fmitivsaqe titgivtdtd gnsipyvniv lsgtltgstt nengmysidv
       61 pslsgaiefs vlgyqsklvp innrntinvt ledsseilde vvltalgfkr etkelgyvvq
      121 sldakgvtev ksvnfldnls gklagvtinq gatgvgsssk itirgeasfs nnnplfivdg
      181 vpinnnsvfn ftneaaagfq eidfgngame vnpddieevs vlkgpsaaal ygtrasngvi
      241 iietksgknt kglgvsynts ffvdsafqlp dfqneygqgn sgefafvdgl gggtndlity
      301 swgprldvgn lipqydspvt ladgsvvrgg dtalyssipi tptefksnpd nlknfyetgt
      361 tlinniaiss gfdkgnyrls ftdlrsesii pgvnldrqti ntrlnflpid klrinssisy
      421 insnsdnrps ngygsenvny slvawgprsl ninnlknywq pglegvqqys fnytyfdnpy
      481 filyenrnsf nrdrvfgnis atyditdyit vsfrtgmdys selrqlrray ssnrfknggy
      541 aehdvffrev ntdfllnyan qfndisfdis lggnrldqka ftsqsqttsl aqpgifrlsn
      601 aaspvevfef esnkrinsfy glakfgykdf lflditgrnd wssalatpfs vdntsffyps
      661 vsssfilsev vdlpktisfa klraswaqvg ndtnpyqttg afvaqtpyng qptfsnsnii
      721 anpnlqpert ssfevgadir lfgdqfrfdv syynaltkdq iislpigiss gytqqvvngg
      781 evrskgleii lgispvlsen lkwnstlnfs tnrstveslp qedgrltlay sriydsqnqt
      841 vffqveeggr vgdmygtgyl kndngefilt eegryipnnd lqklgnynpd fmlgfnnqfn
      901 yknwnlgflf dwrqggiivs rtkalgnvgg qlaetafrpe sgivpagvvn tgteenpvyt
      961 tntvavsaes yyrqyydrnh eenntydasf lklrqlsigy tfdnlslfnq datlnvslig
     1021 knlfaitenp hfdpeqlavq gqgfisgved msyattrsig fkagfnf
//
LOCUS       WP_091628126             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis saalfeldensis].
ACCESSION   WP_091628126
VERSION     WP_091628126.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis saalfeldensis
  ORGANISM  Amycolatopsis saalfeldensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Amycolatopsis saalfeldensis"
                     /db_xref="taxon:394193"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37929
     Region          8..358
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maesgnrltv gvvaesrpge rrvamvpklv arlaqrglrv vvepgagaga qladdayvqa
       61 gaelgdawaa dvvlkvapps etevgklktg tvligfldpr gdpegiaale ragvrafame
      121 avprisraqa mdalssqssv sgyravllaa ekftrffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgsqttgydv rpevgeqvrs igakfldlgi eavgeggyar eltaeeraeq
      241 qrrlteaitk fdvvittalv pgrkaptlvt adavkgmpag gvvldlages ggncelsrpg
      301 edvvehdvti saplnvpsgm pthaselyar nvtellellv ttegelkldf sdevvaganv
      361 agregsas
//
LOCUS       WP_091643176             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aquisalimonas asiatica].
ACCESSION   WP_091643176
VERSION     WP_091643176.1
KEYWORDS    RefSeq.
SOURCE      Aquisalimonas asiatica
  ORGANISM  Aquisalimonas asiatica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Aquisalimonas.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Aquisalimonas asiatica"
                     /db_xref="taxon:406100"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40207
     Region          3..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mairvavpre tqtgerrval vpsvikqldk lgveilmesg agkesgfndd ayegvrives
       61 adelykdadv tlkvqpptve eagklkqgsi vmgfmapheg dtriktftkn kvtsfsmelv
      121 pritraqsid alssqasivg yksvllaanm mpklfpmltt aagtirpstv vvigagvagl
      181 qaiatakrlg avveaydvrs atkeqveslg gkfiktgvsa egeggyarel tdeekqqqad
      241 vladhiakad avittaaipg kpapklidta tvermkrgav iidlaaetgg ncevtkagke
      301 vdhngvivyg pkntasalcq hasemysrnl ynflaliikd gelaldwddq vqtdsclthd
      361 geikhgptre rleggkks
//
LOCUS       WP_091651051            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            ornithinivorans].
ACCESSION   WP_091651051
VERSION     WP_091651051.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus ornithinivorans
  ORGANISM  Algoriphagus ornithinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Algoriphagus ornithinivorans"
                     /db_xref="taxon:226506"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116078
     Region          25..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkallfvva lftmtlsyev saqqrvitgt visdedglgl pgatvlvkgt tvgtttdldg
       61 nysisvpags nvlifsfvgl vskeeaignr tvinvtlttd aaqlsevvvt aigierekka
      121 lgyavtsvgn eqlenrpeqd varvlqgkvp gvnitstngm sgsgtnmvir gyssatgsnq
      181 plfvvdgvpf ntstnnqngf ttggattssr fldidpnnie aisvlkglsa tvlygdqgrn
      241 gvilittksg askrkaaevt inqsvftnea aslptygqvy gngfqqapgf ffsnfgprmd
      301 egrtvnhpya tssvqkvrea fpqfwvdgiv ggtpvqyeyk ayadpseiff rtglisntsv
      361 qvaggsdkts fnasfgytde egftpgnelk kynfglgvns avsdklsvrs sftfaitdlq
      421 sppvnaafgs gpsggipsvf ahvlytprsv dlgglpfenp idrssvyyrg gndivnpnwl
      481 vryyqntsdv qrffnstavn ydltddfsit yrigldtyte lqelrynrgg pssslattsg
      541 yyrsvnvtns iwnqdliinw kkqfsdkfgm saliggnsry dtysqngvas qgqlafglfr
      601 hsnftnsssn daysggglnf tqeerrmgiy anvtldysny lffnlsarnd wtstvepenr
      661 rilypgasvs flpstafnwn sstindlklr lgygtsagfp spyrtrniln qsarafdrdg
      721 avtqthsvsn llgnpnlkpe lheetefgie avmfnnklkf dislyqkntr dlitqapidp
      781 stgftstain igkirnrgie fqatvtpvst asgfawnsti nwglyrskti elgggleeiv
      841 vagfttlgnf aipgqpfnii kgvgferdeq tgqpivlsng lykpsaelkv lgdpnpawtg
      901 swinsftykg ftlnammeyr hkgaifsntv tatlargvtk dpvidreltf impgvkedgt
      961 pndiqitasd yffagyqgat depnvfdgsm irlrelslgy qipsnlmskt pfkrasials
     1021 gtnlwflaln fppnmnydvd vlgtgvgngl gfdfvtgpss rrfggtvtlt f
//
LOCUS       WP_091652773             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            ornithinivorans].
ACCESSION   WP_091652773
VERSION     WP_091652773.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus ornithinivorans
  ORGANISM  Algoriphagus ornithinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Algoriphagus ornithinivorans"
                     /db_xref="taxon:226506"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108845
     Region          30..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnylqqlks lmlvmalvfg aslaanaqsr titgtvldas lgdpvpgatv lvkgttrgva
       61 tdldgkftle iqsgdrvlvv sfvgyltkev eignqstfti nleediqsle eavvigygsq
      121 dkkeitsavv gvkpedfnrg nvanptqllq gkvaglsitr aggnpnggfd irlrglstfg
      181 anssplivld gvigasldnv dpndiqsidv lkdgsaaaiy gargssgvil itttkkgtre
      241 psttvsinsf atldqatnli pilspeefva rggqdfgsrt dwrqelidda lsyttnasvs
      301 gsfnnttyma svnyrdnngi vngvgnerln trinlsqsai nnrlrmnvnl sftnvdsesi
      361 ndaafryati ynptapifen tedanqrfgg yfqrdlfdfy npvalanqqk fvneiksalt
      421 syraefdilp nltasaqysq drrneliggf wsiqdfqvgl gargsaerit ndrqqkifes
      481 tlryetevmd glnmtllggv afqstknqgf garvrqylfd lgwnnlgaga irlgnntnly
      541 syanedqlns afgranfnyr nllflsasvr aetysgfgen nqtgvfpafs igsdftqifd
      601 mgvfsqfkpr vsygvtgnlp psptlalgvf gngnridldg dplttddiyv givqnsnpnr
      661 flkwetkkef nvgvdyamfd gkvngsvdyy vrnisdllfn vpvsggpnif dpgrfntvgs
      721 twvnladlra agfefaigva rigkgtlkws pnfnftiydk ttieslsagg lgfdelrfat
      781 pgspgqnnnp iiynrvgqtl gdfygprllg iseageyils ttnpdeferl gnglpqgefg
      841 fangfeygqw slnvflrgaw ghdlynsyrg fyenadapsn twnsvitdkt ptsplitstp
      901 tfnssyieda sfirldnmel gynfktnspn lssfrvyfaa qnlftitnys gidpevrvrd
      961 lengdaftts lspgierrnt yfqtrsftlg lslnfk
//
LOCUS       WP_091653650            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            ornithinivorans].
ACCESSION   WP_091653650
VERSION     WP_091653650.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus ornithinivorans
  ORGANISM  Algoriphagus ornithinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Algoriphagus ornithinivorans"
                     /db_xref="taxon:226506"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110492
     Region          23..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvllgill gvmtvmsala qsktitgkvt sseepqgvpg asivvkgttv gaitdidgty
       61 sinvpenatt lvfsfvgylt kevniqnrsv idvqletdvk vlnevvvvgy gtqerrevtg
      121 svssisnesi anlvapsfds qlagrapgvq vttpngilga rpiirirgvn sltssadpli
      181 vidgvpivdd drsavnasnp laninpadiq syevlkdgsa taiygsraan gvilittkrg
      241 sdgkakvsyn tsmgfneeve rfqllngdqf vtianekrsn agqsplanpg vntdwqdliy
      301 rkgftqqhni sisggsaatk yffslgftdq esairpndlk rysfranidh sisdairigt
      361 slsyslteif glnngansls gaiynstral pnvpiydpen iafdgynvta ngattgfgan
      421 lagpdnnipn igfvidnnly rsrahrilgs vygeadlatg ltartqigtd ltladdfqsl
      481 dprhgdgrss ngyvymaynp airwnwqntl nyqtvigenh ninvtggvey qftrlynfag
      541 wgtdisdnfy reqnlisgsy nnqfsgggys eqgfdsyfgr fnynyggryl lsltvrndgi
      601 sdligdnkrg tffggsvgwr vsdeaffnsn lisdlkvrgs yaevgnvgla sfaafggfsp
      661 vlggagagig yarvangglq wetskkfnvg fdmtigpvsl tadyfinnid glilaaptpp
      721 slgvpgnsin qnvgamrnsg lelralatvl srgkftwntd fnitflnnev tnliqpltgt
      781 ynrtevggpv aqlygfkwag vnpangnply hrgeeivqyn lqrgaigwrt ydpanpgnvs
      841 ttasgptqef lgntlpkwqg gwsntfkygn fdaeiftrfs ggnfimnesl rgllgqgfsn
      901 nhasimnrwt esgqvtdmpk lysgqdanmw qtsasnsrfv ekgdfvriqn ivlgytlpsn
      961 vlqsafagki tnarvfaqvq npfiftnytg ldpesntfsg qqsfgvdwnv apiirtytlg
     1021 vnvgf
//
LOCUS       WP_091653654            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            ornithinivorans].
ACCESSION   WP_091653654
VERSION     WP_091653654.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus ornithinivorans
  ORGANISM  Algoriphagus ornithinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Algoriphagus ornithinivorans"
                     /db_xref="taxon:226506"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115219
     Region          23..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvllgfvi mlltavsvma qnrtitgrvt speepeglig vnvlvkgtti gvvtdldgry
       61 tilvpanast lvfsyigyis veeqignrse invtmredaq nlqeviitay ggtadkgnft
      121 gsaialkgdq ianrpinnvv naiegqapgv ittsasgqpg stpavrirgi gsvnsssapl
      181 yvvdgvpydg dlsnlnpedi admtilkdas saalygsraa ngvimittkt gqknkptfnv
      241 rvqqgvssra lpeydrvnad qyyplvwesl rnsqlgngat pdaaatfasn nlinilgynv
      301 ynvpnnqivg tdgrlnsnav nnfvglnwfd elqrtgdrke ynmtysggse ktdfytsfny
      361 lnekgfiins dierftgrln vntqatnwlk tginlsatms egnnardggs ssfvnpffta
      421 rsmgpiypvf aqnmqtggfi ldefgnkifd lgdleefglp rrgagaypgr hvvqetllnv
      481 drfdrdviss rayveakflk dftfrtniat ditsllnigy dntivgdgap agrtrrenir
      541 insltfnqll tysktfndkh fvealvghen ydfrrtrqfi skqdqilagn iepdnfvtin
      601 sasgrtdvdr iesylsrvny vyddkysfsa swrtdgssrf frdvrwgtff svgaawsidq
      661 enffnsnffq lfklrasyge vgnnnvggfy pwqalydlgf nnasepgilq aslsaldlqw
      721 esnntydlgl dfafgnrfsg tleffnress nllfevplsl ttglenrfqn igtmsnkgie
      781 fniggdvmrr gafkwnanvn vstfknefke lpfeeqivgt kkyvvgrsif dfwlrdwygv
      841 dpetgeglyr aeeyaendpt triigqdtvt trfqnarfhf agnaipdffg glsntfsykg
      901 lslnvlvsfa vggdiydgiy aglmgadpdg gaahvdilnr wkqpgdvtev pkmdvtgaaq
      961 tnvasdrwlt dasylnlrai nlsytlprtl lerwkmrgat vylagenlgw lssrsgmyvs
     1021 gtfsgttsnt ftpartftlg lnvnl
//
LOCUS       WP_091654770             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus ornithinivorans].
ACCESSION   WP_091654770
VERSION     WP_091654770.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus ornithinivorans
  ORGANISM  Algoriphagus ornithinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Algoriphagus ornithinivorans"
                     /db_xref="taxon:226506"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40388
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,72,91,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtigllkepe gehrvallpe svkslislev nvwvesqagn hafvsdtdfe ksgakisqre
       61 evlkadlilg inpptstele tlkaeqvlvc vfqplsnkvl verflklgit sfsmdnvprt
      121 traqamdils smatvagyka vlmaashspr ffpmfmtaag siipskvlvl gagvaglqai
      181 atarrlgavv eafdvraaae eevkslgakf ikvegakdea taggyaveqs eeykakqqal
      241 iqehakksni iictaqipgr kapllitket vaemvpgsvi idlasssggn celtqdnqti
      301 nsngvsiign snlpstmpld askmygknmv nflkliigef galnlnwddd ivfntcvthq
      361 gsiqservks ilfpsnpv
//
LOCUS       WP_091655148            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            ornithinivorans].
ACCESSION   WP_091655148
VERSION     WP_091655148.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus ornithinivorans
  ORGANISM  Algoriphagus ornithinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Algoriphagus ornithinivorans"
                     /db_xref="taxon:226506"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112536
     Region          25..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknsyksall fligflacis lyaqqtvsgi vtakedgapl pgvsiviqgt stgvvsdidg
       61 kysisvpntq avlvfsfigf etqrvpvgnr stldvslate tsnldefivt afgisqekka
      121 lgyaaqsina deitktrqpn vvnalqgqva gvqvtnsgga pgqsariiir ginsldpsad
      181 nqplfvvdgv pvdnstiesn gtprgmsnri adinpndies msvlkgaaat alygvraang
      241 aviittkkgk sgqirvdfns slgfdnlakl pelqdqfgqg fsgvrndssf wpswganiae
      301 endpnyvyqd nwnrafntgm qfdnslsvsg gnevatfygs fgrldqegii pfstwdrtsa
      361 klsgtvkase kfnfsgsfny tnsggnrvph drflermmyw settdvrdyi npdgtmktyg
      421 ntnpiydarf atyednvnri igninlnysp tewltfsyrl gmdnysdsrt eitpgpmgid
      481 gevplsstgf leetrinsrd itsnfyitlk kqwnsdwnts lrlgndvfer kfdrvtatgt
      541 nfvipgfynl nnttqifasq gksirrlvgf ygdlmvdykn flflnitgrn disstlpknn
      601 nsffypsvnl gyvfsenfdl pswvtfgklr aswaqvgkdt nphilgatfv spgvfplngq
      661 vgfsrnstfg dpnlrpettt svefgtqfaf fnnrasldvt yyksnaadqi ipvpisdatg
      721 fssyitnage ienrgfeivl ggtpiergdf rwdvtanltt nqneikaire gidqivvgsq
      781 fgyagsrvtm ilkegqaygn iygssyirpg apegteelnr dlpvligang fpvrtgnqli
      841 lgnavpkffg glrnnfsykg lefsflidfr agleqydqfg nflsafgkqk dserrndfvv
      901 fpgiladgsq ntkevwlgqg vgpdgvnyga gywrnyyrtt senfvkdasf iklrnvtlay
      961 nlqpnllert pfrtarisva anniilytpw dgfdpesfsa gaggnavgft glgfpgvqsl
     1021 fftlnlgl
//
LOCUS       WP_091655339            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            ornithinivorans].
ACCESSION   WP_091655339
VERSION     WP_091655339.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus ornithinivorans
  ORGANISM  Algoriphagus ornithinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Algoriphagus ornithinivorans"
                     /db_xref="taxon:226506"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113079
     Region          26..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilsisyg lafmlflslq ayaqnriltg tvvgetdglp ipgvtvldkt nqtgtttdvd
       61 gkysisvnsn svlvfsfigy atkeftvgnq svlnvtlsed vsdlsefvvt sfgmerdkka
      121 lgysvtqlsg dkftesrain lgnaltgkva gvnvtppatg aagstrvvir ggssltgndq
      181 plyvvngvpi esgnlgsagl wggndagdgl aainpddies lsvlkgntaa alygaraang
      241 vilittkagr arkgvgvsfn snftvesvvd qtnfqriygp gqdgrkpmtq deaintanng
      301 wgsrydgsqt iqfdgqqrpy sylgedftdf ynmgktwnns ialfggnent tyrfsfsnld
      361 nrdvvpnagf trnvaninvn skqgkftlav tgqyskqnae nrprlsdspg nanfsmvvkp
      421 gnipldvikg dpnkpgalpd gtelryqsnv fqtnpywavy qwgredvtdr vlgnmslkyd
      481 ftdwlyaqgr fgtdfqvrde yafeaygtaf kprgsynttm ttirennadl ligfdksfgd
      541 fdvdgfvgsn imrrtienqr gggndlvvpf fhsvtnvaap tfgygfselg insyfaaanv
      601 gyknmiflnl tgrqdqfstl spansklfyp svglsavisd mlempnfvtf aklrgnwgqv
      661 gggapnpyal nltyglvgag hlganlgqin ngsipnanla pytsteyeig adirfmdnrl
      721 gidvayykrr tsddilatgi satsgfgstt vnigelenrg iellinatpi mnefrwdisf
      781 nfannqsevl slgtnaagdp iefinldear trrerirhiv gqplgmisgf khleingqkv
      841 ydangfpvtt ngyetiaegr hpisggitnt fsykgfrlma lidfrqggsi msgtdyfayq
      901 yglhqntlng rdgsltvsgv tpegtpktwt ipadpsdptk ylidnywqry aqvtenivyd
      961 asfaklrefs fgytfprafi ertpfqslsl slvgrnlail wkntpnidpe aayttsgnaq
     1021 gleffsvpan rsfgfnlsan f
//
LOCUS       WP_091655661            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            ornithinivorans].
ACCESSION   WP_091655661
VERSION     WP_091655661.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus ornithinivorans
  ORGANISM  Algoriphagus ornithinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Algoriphagus ornithinivorans"
                     /db_xref="taxon:226506"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118099
     Region          26..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfsftllll lriqlvfgqs mtyesrildv sgipipgatv telgtsnvai sdqdgrfris
       61 sskqnltlri sfigfetqdv vinngvleke irllestenl eefvvtalgv erqrqslssa
      121 vttigarels dvpqtnlins lsgqvagvqi tngssgvgss sriiirgens isgnnqaliv
      181 idgvpiineq itsdlfndga niqevdfgng aaeinpddie sitilkgpgs aalygaraan
      241 gvvlittkkg rkkqgigvtt sslltfdgll tlpdyqneyg ggsngqysfq ngigagvndg
      301 gissygprln qglliaqfds psvdingnpv ragdvisrrr pdgtftaitp tpwiarpdnv
      361 rdffrtgvts qnniavtsgn ekggariays nlrnegilpn tdlkrdglal sinqaltekf
      421 rvdlftnfin srsdnrpnlg ygyenvmygf nwtgrnfdis slrdywqagq vgiqhfdfny
      481 lwltnpyltl fentnsfvkn rvlgnlalty dftnklslrv rtgidnssds rafrrafstn
      541 rrvfggyred dvrlfemnsd illtysdqfn sdwlysvsag anrldqkiny syteanqlal
      601 pgiytiensr vplrgssqif dkrinsvyaf gnfsyrsvlf idltlrndws stlpaennsf
      661 ayysgglsyv lskglplpks isnatvrfnv asvgndtnpy qlnntfqfnq nygsftrvtn
      721 gtvlnnpnlk perlnsleag mafglwrdri qtdiavfqnt sinqiigrpi stasgfsnii
      781 enggevrtrg leasvqalmf ergafswslg anfttyrsvv telpegvdqy vtgeasvfrg
      841 aggsnsvfyi arkngrigdm ygsgfqefeg qtifgsnglp iqdgrlrllg nynpdffvgl
      901 tnqfrykklq lgfvfdwrqg gtivsrtral gstsgvlket legretgvvg qgvmnvgtpe
      961 npqyvpnttv vpassfynnf fdrgneasal ydasylklrq lslyydlpqq wvnsigfnyi
     1021 kvgfvgsnll lftenphfdp elnamqgrnl tygvedmsyp strsfgfsik tef
//
LOCUS       WP_091676906             409 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium sp. 275MFSha3.1].
ACCESSION   WP_091676906
VERSION     WP_091676906.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. 275MFSha3.1
  ORGANISM  Methylobacterium sp. 275MFSha3.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Methylobacterium sp. 275MFSha3.1"
                     /db_xref="taxon:1502746"
     Protein         1..409
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42108
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd saeprvaavp etvkkfktlg aevvvqsgag qkagildsey eaagasiags
       61 aadaagdadl vlkvrrpsae elpqlkrgat viaimdpygn edalkamaea gidgfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrampmmmt aagtvpaarv fvmgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsaeyqk
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 agevvtndrg vkivghvnvp grlaatsssl yarnlyafve tlidkeskal ainwddelvk
      361 atnltrdgsv vhasfqpktd gaaseaasvg lakseaskas gaatpegaq
//
LOCUS       WP_091681656             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylocapsa palsarum].
ACCESSION   WP_091681656
VERSION     WP_091681656.1
KEYWORDS    RefSeq.
SOURCE      Methylocapsa palsarum
  ORGANISM  Methylocapsa palsarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Beijerinckiaceae; Methylocapsa.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Methylocapsa palsarum"
                     /db_xref="taxon:1612308"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39335
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaipaetd paesrvaatp etvkkfiglg aevavetgag ersgvadaay ekagaviapd
       61 aasavsgadi vlrvqrptss eirgakpgaa viaimdpyey vselqalase gvcafamelm
      121 pritraqvmd vlssqaniag yraiieaaaa yervipmmtt aagsvppaki fimgvgvagl
      181 qaiatarrtg gvvtatdvrp atkeqvlslg akfiavedee fkqaetaagy akemsseyqe
      241 kqraltashi skqdivvtta lipgrpapvl itadmvasmr pgsiivdlaa erggnceltq
      301 pgetvtseng vkiigsvnga grapatasel yaknlfafae tlidkethtl aikwddelvk
      361 atlltkdgal phprfqaas
//
LOCUS       WP_091690963            1013 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter polytrichastri].
ACCESSION   WP_091690963
VERSION     WP_091690963.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter polytrichastri
  ORGANISM  Mucilaginibacter polytrichastri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Mucilaginibacter polytrichastri"
                     /db_xref="taxon:1302689"
     Protein         1..1013
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110606
     Region          24..1012
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknllvlll sglfalsgaf aqsrkimgkv vgaddglslp gvsvklqgtq kgvltdgdgn
       61 fvlpastgqt lefsfvgyki qqlvipagnl pliklkqdsr llsevvvtdg ystttkkayt
      121 gsattvkgsq nenkpfstpq qalqgevagl avsvnsgqpg aniqvrlrgl gstyldanpl
      181 yvidgmiins gdlsrsatta namaginend iesiqvlkda aataiygsrg sngviiittk
      241 rgkngktqvr fdaeggvttn maipdagkpl tasqygelyt eglknagysa atilssqnay
      301 ginsgqsnnw ydlvtkrgsq qqynvsvngg sdntkvfssl gyfhqdattl nskltrisgl
      361 lnidhniskr isistnlnvs nvnqntpyns tyysapiasa yflrpyqlay nadgslnsst
      421 sggtnfpsfy nplyisqndv hglsqtrgli getlkwtiwd qlkftsfasi dynvleetyy
      481 anptmgdgsv yggyggdyyt ryfnwltrnq ldyrynvkgv qdfyidatvg yeaqrsqeny
      541 vtaegtgyaa saptlttlsl astpvtaqgt ysnytynsiy srfsanyknk yvlsgsfrrd
      601 gsskfgsnvk ygnfwsvggs wnideenffk qqnivsaakl hasygtsgna nglgnyaskg
      661 satissdyty agysganydv ignnsltwes arkfdigidl sffknrltis peyyhnsing
      721 liqnvavsqt tgfsnaieni gamlnkglel tiqgvpiksk dftwstnfnv afnrnkmtsv
      781 aegttgvhdt yyylakgldy ysyytkqyag vnpangdalw ytdatrtktt tnyaeakyvv
      841 nhqadpkmfg gfnntwnykg fsltaefyyn fgnyvydpig ryfsggayss ynkyqyiytn
      901 rwttpgqvtd vpkyvvggia dnngsdaavs srywysgdyi rlknlslgyd fkdvgllkrl
      961 glsklnvyvr gtnlwtktyd srlpfdpevd ingynslsip kvktytvgin vgl
//
LOCUS       WP_091690983            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter polytrichastri].
ACCESSION   WP_091690983
VERSION     WP_091690983.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter polytrichastri
  ORGANISM  Mucilaginibacter polytrichastri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Mucilaginibacter polytrichastri"
                     /db_xref="taxon:1302689"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110543
     Region          31..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkhvlkkl tsacfcvvvl ccnaysqtlp vkgkvldikg aplpgatvki kgtskgttts
       61 vdgsfalqap qnatiiisai gynpqevpag qsisvklten nqslnevvvt algvkrekrv
      121 ltystqqiks deiqqskdpn lvnaldgkvs gvqvttssgt pgssssivir gassfygsnq
      181 almvidgipv nndetgnlnq gpgtnrladi dpsiiesmdv lkgsaataly gsagaagvii
      241 ittksgakdk aptvnfssdf sfekallpqv qnkysqgnng vyfdgvnqkt stswgalmdt
      301 lkingqkapv ynqmkeffkt gttrnntvsv nggnnnntyl isysnfdqkg tvpntsflrn
      361 tvfgkysaqi lknlnttfql nysnsqnyrl pegyalespv wtiytapisy nlqpyedasg
      421 nqrlyrysrn npywvlnniy nkssvnrflp tfttdykpls wltvterfga dvyteqdkyk
      481 eaagsvsnpn gkiidqtinf rqfnndfflt akkqfgdfnt dlilgnnvys kytqylyavg
      541 tglnitgfdn issasnityt enhylqrkig fyaqsnidyk rflilsltgr ydgssvlstd
      601 htyypygsaa tsfilsdffs prlsevmnfa kirvsystvg ndgvspysll tpyqsqtasa
      661 ntavrnisfp yngqagflln ttlgnpnlqn erinefetgi etgffknrir leasyfdkkt
      721 tsgiipgvti apstgysgtt vntgvmrnrg ieallnvtpl ktknfswdft vnfsrirnkv
      781 isingdlpqi gngfttiivg qpygtiygtr yarnaqgkll igtdglpyad dtqgvignin
      841 ptwtggftnn frykqfnfsf ffdvkkggdi qnnvdgygyf ygtpkvtedr gprvvdgisa
      901 atgqpntisv sgqsyyqrin gitesviqdg tyiklrnasi gytlkpswlt gtpfkalnfs
      961 vtgrnlwvya phftggdpev ssfgassasq giysfstpts rsfdfslklt l
//
LOCUS       WP_091690992            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter polytrichastri].
ACCESSION   WP_091690992
VERSION     WP_091690992.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter polytrichastri
  ORGANISM  Mucilaginibacter polytrichastri
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Mucilaginibacter polytrichastri"
                     /db_xref="taxon:1302689"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114785
     Region          58..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkslplfm ctvltvtmll qsagiamagg rtvlkiiynt ntpnetsras aeseivsiai
       61 tgkvmdekgm tlpgvtvtek gtknatitts sgtyklnvag ksavlvftfv gykpieipvn
      121 netivnasma pavsalnevi vtalgirrea kslgysaqka dvqalqtnrt tnlanalegq
      181 vagldvsppa agpggstkir lrgqssftad nsplivingl pmsqgasstn gytqntdqgd
      241 nlqginqddi esmtilkgst aaalygsrav ngaiiittks gakntgigve fnsnftlska
      301 ldftdfqyey gqgennkrpl tqgdaqssga wsfgvpfdna ltyqfdgvqr pyapvkkrin
      361 tffrnapsfs ntlaisggnd kgsfrvsfan qdakgivpnn dyhkkifnig inyklteklt
      421 aqfnvnydhe fnnnppvigv qglsiptsiy rlansidfdv lkagaidang neaptsrfst
      481 vtnpywimak qfqkqtkdhl lgtavlryqf fdwlylqgra stdllqttfe sntptgtlsv
      541 gaaptglfng gyaintsnlr qnnfdfllgg grkfrnfgfn atvggnnypl vnstfnesvt
      601 nfyirdlyti gngvtatssy nlskqtvnsl ygtaefsyks lfylnvtgrt dwysvlardi
      661 dhyfypsvsg sfvfsellpn akwlnfgklr vavsetgsaq gigayntltf alaqnpfngs
      721 plgsinntss pnprikpfgv kekeiglemh mfnnrinldi aaydkkttnq avpislstat
      781 gysstlvnlg gldnkglelf lelvpvqnsk iswrtsfnta fnsskvlsla nnqkqlvvgs
      841 peffgtiadv vglplnqiqg atykrnaagq illtggkpia salpvnfgsg lpkatggwtn
      901 tvnykgftfv ahfdykaggk vlsstnlnll reglskeslp grvggvlfqg vnstdglpnt
      961 tavnaedfya nyrstnildp fiysssfikl rnlslgydls rfidkkyiks lvlsavchnv
     1021 wvikkytpni dpeaisssgd nltgyeqasl ptvrtygfnl nlkf
//
LOCUS       WP_091691079            1208 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091691079
VERSION     WP_091691079.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1208)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1208)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1208)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1208
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1208
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133398
     Region          119..1175
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meitftkknp lpprslwlll llflphwaea glhrseriie mhqtklslre fiteietqse
       61 fkfiyadgvh ellgqqikvs pkatvqqhlk taetftpfqf kitgenilir ksqqtraaip
      121 itglvldedn qplvgatvli kgstsgvvtg idgtfsidvp sneavlvfsy igfesqevvv
      181 qnqsyikvvl lssfadmegv vvtalgierd erslgysvae vgenafqngs qdnalrsiag
      241 rvpgvsvnst ggagssvsmi irgisslsgd nqplfvvdgv piintlnnvs eigadnkvdy
      301 gnaisdlnpe diesmsilkg psaaalygsr agngvvlitt ksgrkvnevt vsvssntlle
      361 ipykylpfhs rfatgvrpyt pdnnpypggq lvieegssag agpeldkgye aiqwnsplda
      421 ngnriptplv shpnnvsdfv rtgvtttngv svannnefin yrigytnlsn wgiipnsdfg
      481 rdnlsvnttl ridpkltlss sininqtgsd nrpagnrgan pleaaykvsp hidinelqsy
      541 wvpgqegiqq rsqaigdydn pyflayevnn sfkrnrifgn lgleyqften fkvkasymld
      601 myserreski pisytadpng gyglinldrt ernadilaty tkdydnfhmt lstggnlrfn
      661 rnhavqnstk aegsglivpg vytlsntsad nliynssise kavnsiygla nfgfrdliyl
      721 dvtarndwss tlpeanrsyf ypsaslslil nemldmgssi dllklragwa qvgndtdpyn
      781 lyqvlannge wdsqtrltvp dnlktpdlkp eistsyelgl emaalqnrlr fdltyfntdn
      841 knqilpvtlp sssgftskfv naglvnskgw evmlgftpvk ttdftldlnf nyskyrsriv
      901 eltdevdvfy lwsdsrggaw tyvgdeigdi ydrglvtved respyfgypi ldedgswqai
      961 nqasaknkig nfnpdflagm qvnmsykrfs lslnfdmrmg gdfvsqtfry sesdlktqrw
     1021 ldqiinpngl sgdalrdylv dnqdqfitdg lnvvggptae sggfpfdynv tvndgvfnpg
     1081 viaqydeegn itgytenlgg entkyipyad nypwsffkpa tfdasyiklr eaaisyqlpv
     1141 dlvnklkmks invgvytsnl ilwtkakvgi dpenafqpea ngtfkqgier ynvnpwvipv
     1201 gfkinasf
//
LOCUS       WP_091691104             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091691104
VERSION     WP_091691104.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107860
     Region          25..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 minkplltmi llfctigvsw aqynirgtvs dertgeplig asilikgtts gavtdldgny
       61 sldisssgsv elivssigyl kktitvnqnq tevniqlnqd atnleevvvt glassvkrsn
      121 lanavtsvss rdltgtttiq ttdgalygkv pgatirsngg apgggisiql rgisslqgas
      181 qpliivdgvy innasqrtgr atvsgaggsn qddganrlad inpadienie vlkgpsaaai
      241 ygtranagvi iittkrgaeg rtnvslsqdi gfakplrllg vddwseekin fffpesrrpi
      301 eleryraaea sgtfidyedy fynntallln trinvsggte ktkffvsgni tnedgtvknt
      361 gferysiran idqkitdrir lgvstnyirs ntdrgftgnq nntgasigys isyvpnyfdl
      421 rrnedgtypv npyfsenpvs vtdnaqnnsl vnrfiqaftl dfdilktqns flkatvsggl
      481 dylqnstqiy lpeflqfqra qanpgdlfvg rqesfntnfq aalvynwnlg sinmnsqagl
      541 vrldfdnnsl fnrgrglvpg qrnlkqaniq eineqfnski qeagvflqqe anwedkiigt
      601 lgirwdkstl ngdpneyyaf prasvafnlg nfdfwnstvi sqlkprlayg etagpvpfga
      661 tftplggtni ggllgstvst signtqiqpe taselefgvd agffnnrisl eatyyikntq
      721 nnlqnlnlap stgvnttpsn eaelqnkgle lslsgtlvdn snfrwfsril ywqndiemtr
      781 lgiptyisgg fgsglgtfly aegyspttiv gtpadpsipg gftiwgdaqp dfnlsfsnsf
      841 siykgiefsf lvdwrsggen vnlssflsdg ggttngwfdd dngdgipngr qrepepynna
      901 grwvqdasfv kvreiglyyt lpketltnwf gntvqnlrvg ssvnnaflft dyegydpets
      961 tfgaqavann vdiapyptsr riffhvtidf
//
LOCUS       WP_091691146            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091691146
VERSION     WP_091691146.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116199
     Region          25..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknyaitll flfgflvsip myaqqtvkgk vtaqedgepl pgvsivvqgs stgtvtdldg
       61 nysiavpgte svlvysfigy etqnkivgns seinislsed isqlgevvvt algitrders
      121 igystqevkg enltytkeqn vlgslsgkva gvqvtgssga smggtqkiki rgvnsisggg
      181 eplmvvdgtp isnsnfsgas gqdygnlgqd inpddietin vlkgpaasal ygirgqygvi
      241 mittkkgkkg sdvkvelssa vfvdkvtnlm pyqnlygggs sqtwrtlpng dkyvdmsvde
      301 swgpktdgtl vrqimsfypq dptyeqltpf qaypdnikdy yetgtnvnng vtitgggass
      361 nfrvslndtr iqgvepntsl krnnvglglg idltkklrlt tninyaankg rrpgqgsedg
      421 srylgqwfqr smdmnrlkdy qyddgtflhw nlrrpssstg eitnynplyw anpyflayen
      481 fsddnrdrff gdvgvsyqim pelkvsafvr sdmytqnins rasfggtgnp gysvgkyqnt
      541 emnyevlaqy nkvwnkfsld anvggnlydr nysylsmatv ggltspgfyn inasidrpst
      601 ssyqqkkqik sayamvslgy nntyfvdasl rndnsstlpv dnnsywypsl saswvfseli
      661 ksetmtlgkl rlsyaqagsd lspysttsff nvgstytgas tvntlsvpdn lnnpnikpsf
      721 ahsyeagvdf kfyegrvgls ftyynqrnen qilnldvsgt sgfgsatina geivnkglel
      781 aitatpfrse kfnwdvafnl srnrnevvel ypgidvyqyg sttysstssy lnsyvgkpfg
      841 slvgqayqrd eatgkillgs nnmplytdat hdfgtvlpdf nggfqnvlny qnfqlaamid
      901 fqaggqffsr skmlavrtgl dpisaaindn gmnvrdplae gggvkvegvs aetgeevtay
      961 vdakayygvv arriyedwly dasfirlrev slsynfnkaq yaklpvenvr vafvgrnlam
     1021 lfqnapkgin paelstgsqa igwyesgqlp svrsfgvnln vtf
//
LOCUS       WP_091691048            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091691048
VERSION     WP_091691048.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117252
     Region          30..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtakksiwqc litavllfii nfsfaqqgmi egkvidtnnd plpgatvlvk gtsrgtvtdi
       61 dgkysiqase getlifsfvg fealekavgs stvidvtlse glalnevvvt algvkreska
      121 lgysvqavdg dkftearetn vinslsgrva gvqvtnsssg iggssrvtir gesslninan
      181 qplfvvngvp isnnivgssg ssnqevdygn aageinpddi esmtvlkgpa aaalygsraa
      241 ngailittks gknkkglgit insnttfdnp lmlpdwqnty gqgnggqfef vngagsgiad
      301 gvdeswgprl daglmipqfd sprdvpgfrg gdlnapagst itatpwvssp dnindffqtg
      361 vtlsnnials asnenanirl sytnldqkgi vpntdlkrnt ismngglnlt dkltvnstin
      421 yqrsdsgnrp nisygtenlm ylwiwygrqv ntaslrdywm pglegeqqfn ynynyhdnpy
      481 fnvyentngq akdriygnis vnykftdkls lmlrtgldty nelrdrkraf stqrfpkgny
      541 redalyfsem nsdflltyse ssndvftysi avggnqmrqe nryvqtvapq llipgiynft
      601 ntavnlqvnq ytsekrinsl ygfgqigykn ilfldltgrn dwsstlpadn nsyfypsatf
      661 gavisdmvim pkflsflkar vayaqvgndt dpyslsnvys sqtawgsiqa ksesnrlsns
      721 elkpeqtaaf etgldarffn grlgldftyf dnrtknqiip ieldiatgya sriinageiq
      781 nkgieivlsa npvnttngfn wsflanftrn rgkvlelteg lntytltgrn ganiqarvge
      841 rmgniygqgf arvedensef fgeiihnstg tpitapelky qgnynpdwml glqnnfsykg
      901 inlgflfdfr yggivvsrtk tigstsgqla etlygretgy dlegegngiv spgvvqnadg
      961 sfspntyett srnwhntyyn rsnveaakyd atflklrevt igytipksil srtpfedvkv
     1021 slvgrnlalw tenphfdpet lsmgggtlip gvedmafpst rsmgfninvk f
//
LOCUS       WP_091691857            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091691857
VERSION     WP_091691857.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113984
     Region          44..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpknlpkfpp pkmpisygvy srklclslif tlslalsafa qqsvsgkvts tddelpmpgv
       61 svvlkgtttg tttdvdgnyt lsvpsdeail vfsfigfnsq eisvgsrsii nvaldvnite
      121 lesvvvvgyg tqkksdvtga iagvdseiit ergttsaiqs lqgtvagvqv snntgrlgdg
      181 fsmtirgnns lssssplyvv dgvitnsidf lnpndiakie vlkdassaai ygsraaggvv
      241 ivqtkggtni pdattfsfet fygiknparl pemmsleqwr dyhmaaylgt tnngagmsqe
      301 ayenvvlgnn npvlkerfen ldgydwydgv lqngmqtnnh ltishrsgls tynmgvgyql
      361 etgnienesl dkytfnmnin qhinskfrag snlamsfgtn qrgssiamqe afrlnpflsp
      421 waidengdei vgqlygqpgk llypdgrsaa dktstynpll eiantsdetr ylrgvgnvfl
      481 qydplewmsl kstfsvgvnn nrrgyfwgaq tntgisngnl pssqvnysdn mnttwdnqln
      541 lnktfndhsf sfltlqslfv drsetanmss arqpfetefy nvgsglqety glgngfrknq
      601 lasfalrlny afqdkyllta snrwdgssll segnkwqafp slalgwrink egfmensavi
      661 sdlklragyg tvgnnnvapy ttvntlttqt yydfngstan gwvqnsiank sltwekttev
      721 nlgldfgffm nrlsgsidyy nrlsddllvt qklpleigfs nirsnaasvr nkgvevmlna
      781 ivfennlvnw sttltftknt nsieslygqs etddvgngwf igesinshyn yvydgvwqag
      841 edaaafnqke gqakvkding dgridpnndr vilgasnptw tggiisrlqv ggfdmnftva
      901 tqqgvlaysd fhsnftnvnd rgrqkaaies yyvpentvgv paqvsnvypq prnegqywgt
      961 giayyknasf vkinnislgy slpssileka nieglriyvn vlnpftftdy egydpewaea
     1021 slgvgrvsni ttqfglslkf
//
LOCUS       WP_091692135             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091692135
VERSION     WP_091692135.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108362
     Region          30..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnyllklkt fllalalifc anlvanaqsr tvtgtvmdpi lgesipgatv likgttrgta
       61 tdldgkfsld lqagdevlvi sfigylpqev eignqtniti nleediqsle eavvigygtq
      121 dkkeitsavv avkpedfnkg nvsnpaqllq gkvaglsitr pggnpnagfn vrlrglstfg
      181 anssplivld gvigasldnv dpndiqsidv lkdgsaaaiy gargssgvil itttkknpkd
      241 grvnvsvnsf gtmdqatnli pilspeefve rggtdygsat dwrdelidds fsyttnasvs
      301 ggfnntnyma svnyrnnqgi vngvsnerln trinlsqgal dnrlrlnvnl sftnvdresi
      361 nndafrfatl ynptapiydd sqaalerfgg yfqadvldff npvalanqqk fvgetksalt
      421 syraefdllp nltisaqysq drsntlsgdf wskqdyqvgl nadgsaqrrt ndrvqkifes
      481 tlryeldltd glnmtllggv atqstenqgf narvkqylfd lgwdnlgaga irvganteva
      541 syanqdqlns lfgranfnln nqfffsasvr aetysgfgen nqtgvfpavs lgsdftqlfd
      601 mglfsqfkpr asfgvtgnlp psptlalgvy gngnrvdldg dpltqndvyv givqnsnpnk
      661 elkwetkaei nvgldfgvwn nkltgsmdyy irnisdllfn vpvapgtpnv fdpgrfntvs
      721 stwvnladlr aagfefavsa hdislggikw hpsvnftlyd kttieslsag dlgfdelrfa
      781 tpgspgqnnn piiynrvgqt lgdfygpvle gftdggeyil sttdpdkfek ignglpkgef
      841 gfannfvygg wnlsfffrga wghdlfnsyr gfyenqdais ntwnsvvtdk tpfvtssptf
      901 nssyiedasf irldnmelgy nfttrspnln slrvyfaaqn lftitnytgi dpevritdae
      961 ngngftssls pgierrstyf qtrsftlgva lnfk
//
LOCUS       WP_091693966             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus locisalis].
ACCESSION   WP_091693966
VERSION     WP_091693966.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40211
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvlketk egekrvalsp dvikqlikke fqvavqqgag lgsnfsdqdf aeagavigse
       61 aevfdsdill kvniftkeei aqmktgsacm simyaynhpe ilaelnkksi tsfamdavpr
      121 israqkmdcl ssqanlagyk svilganyle kifplmmtas gtitpakvli fgagvaglqa
      181 iatakrlgav vevsdvrpet keqveslggr fltvegaeev kveggyaaev saeflqkqke
      241 liqskikdsd lvittalvmg kkspilvtee mvktmkkgav ivdmavesgg nceisekdki
      301 vqkhgvtiig esnlpslmst nasqlyatni stlllhlask dgfnldreee itkgvlitfe
      361 gqvvheftnk ilnn
//
LOCUS       WP_091693788            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091693788
VERSION     WP_091693788.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112867
     Region          24..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklrliiil tllsignlla qsltvsgkve ssedglpipg asiqikgttd gvisdldgny
       61 titvpnaesv lifsfvghvt qeeivgnrss idvtlkssis dlgevivtgv avgtptkklg
      121 faigkvdkel lqeapatdpg nairgkvsgv qivqgtgrpg taptirlrgv taisgsqqpl
      181 iivdgiitqg sladinmndv esmevlkgaa asslygslag ngviqiitkr gadregvtrv
      241 tvrqelgnsy larevplsyh hryqlnpdgs yvltnpnnpn trveeadgim dniypqvfnn
      301 qellfkaqpf yttnvsiant gaktnffmgf enlnqggivv dmpaykrqsl rlnidhmlln
      361 kikltsstlf inskspnnge ngqsglfypi lahepdqdly anrdggilpr sqsnlqnply
      421 elrhrffrrd rkrllqnvev syqvldwlrl sgqysmdlef nnnenytpkg yitqntpqgg
      481 lgslsqtwsn nsaeiatlta aaqkkfgnwn tqaviryqfe kyldeannts gsnfavvdip
      541 rfsaldpttl nitnslsdvr aeniflnlgf dykdkyiieg lvrrdgsslf gederyqlfy
      601 rgtaayrlse dvqipgfqel klrasygtsg arpgfsaqye tyslsrgvat ksvlgnrflk
      661 pskigelevg lnatflntws fefnyanika ddqilqvpls svagfssqwq nagtvrthay
      721 efslgsylie nqdfswnfni vasnskstve elgvptilrg dgitsgmfri aegeefgvmy
      781 gnvfakspsd fildnngfit nisgylpdse snkmpsdfeq nsdgymvaag tentpaetat
      841 ilydpttgqk ldakignsap dlilgltntl ryknislfvl mdaqiggdiy nsskqnlyfq
      901 erhgdldqfn kpegqrksvp yysgatslyn gaapaqhfve katymklrei altyrvdetm
      961 mnsigigkif hdakisvigr nlltftdysg fdpevaslsa gdpttfrsds yvypmfrtft
     1021 aaielrf
//
LOCUS       WP_091694046            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091694046
VERSION     WP_091694046.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115541
     Region          22..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkillfsfl mvltgiawaq trtiegtvts stdgttlpgv svlvkgtqng titdidgkyq
       61 ltvpstggvl vfsfvgmtst eiaignqsti daqladdvtq lnevvvtaln verekktlgy
      121 atqevtsdnl rvaretnlne alagkvsgvq visgsgakfg eaavrirgvr gfgsssplyv
      181 vdgiptadpa tinmdnvqsi nvlkganasa lygsrardgv ilitmkkaka grmnidfnnt
      241 ttfenvsvmp kyqneygggy sqefqtftfn patddpalsg lngalipefy adeswgprmd
      301 grqvaqwdaf tpgtdtygqt rpwspnpdnv knffntgval nnslsvskag egynitatls
      361 nvnrtgvlpn tkqektflnl natvdlaknl tlttlanynr tnvfgnmteg yqggsigqnf
      421 nqwfqrqldm dllkkyyqmp dgrytswnin sarnprplyw nspyteqygn iaentkdtys
      481 gkfgltyeli dglsvsanls ryftsyfsdg rtasgtlnld sygqskyqek ednyeflaqy
      541 nkvtenfsvs aliggnirme eytsnsista gglsvpnlyn isasinrpna snyfsqrqvn
      601 sifaqasfgw keivfvdgsi rrdydsvlpe tsnaftypav sasfifsell pntnvlsfgk
      661 lragyaevgg elnpyqldpa fslgtpyngn ptmtypnsli dpnlrasttg aleggielaf
      721 lqgrirtdfs yyyydntnei lstevpsttg issytinagk tftrgwdati ggtpiqtsnf
      781 nwdvnlniar srnvieeiyp gidaiqlang flgdrvsggw gsisarakvg edwgtiigek
      841 fqrdeagnil idedgypmte qnqvlgtllp dytggifnrv sykgfelsft idwqiggkiq
      901 sitnmfnays glgemtvgdn drgtpmrdpv seggglrfdg vfadgtennv yleaseyfks
      961 qfglheawiy dasyvklrei rlgyslpqsl lqrtnfvrta sfavvannpw liktnvpgld
     1021 psqvsgdtrn srnngawvds gqlpatrsig fdirlgf
//
LOCUS       WP_091694247            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091694247
VERSION     WP_091694247.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112345
     Region          26..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilsiafv lamivglsvs anaqqrilkg vvtatsdglp lpgvtildke tkagtttnad
       61 geysinvnen tvlvfsfigf tsqeftvgnq telnvalded asdlsevvvt afgmerdkka
      121 lgysvtqlsg dkftesravn lgnaltgkia gvnvtppstg aagstrvvir ggssltgadq
      181 plyvvngvpi esgnlgnagm wggsdagdgl ssinaddies mtvlkgntaa alygaraang
      241 vimittkkgs trkgigvsfn snftidqvvd rtefqrtygp gqdglrptsq dqaintatng
      301 wgsvydgans iqfdnvqrpy sylgedfndf yrngstwnns ialfggsent nyrfsfsnld
      361 nkdvlpsagy krnvasinvn sqqgkftlav sgqyskqdae nrprlsdspg nanfsmvvkp
      421 gnipldvikg dpnnpgalpd gnelryqsnt fqtnpywaay qwqrqdqtdr vfgnmslryd
      481 ftdwlflqgr fgtdfqtrqe dsyeaygtaf kprgsyntsa rssrennadv mlgfnksfgd
      541 fdvdaflggs tlrrtiesks gggndlvvpf fasvtnvaap tfgygfsefg insiygsanv
      601 gyknvvflnv tgrqdqfstl spenskifyp svglsavisd mitlpdfftf ikvrggvaqv
      661 gggapdpyal nltyglvgag hlganlgqin ngsipnsnlg pylsteweig tdlrfwenri
      721 gldlayynrr tnddilntgi salsgfgttt vnigelsnkg vevllnvapf igdfrwdvsf
      781 nyahnisevl slgtnaagdp iefinldesr aqrerirhvv geplgviagf khrmingqpv
      841 ydangypvtt dgyetiaegr hpisggltnt fsykgfrlmf lidfraggsm msgtnyfayq
      901 lglhehtleg rdgslsvsgv naegaplnvt ipadpseptr ylidnywqqy srvtenvvyd
      961 asfaklrefs fgytfpssfi sktpfqslsl svvgrnlall wsnvpnidpe aaystsgnsq
     1021 gleyfsvpan rsfgfnlsan f
//
LOCUS       WP_091694788            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091694788
VERSION     WP_091694788.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118876
     Region          38..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkinlsyl ktvvltcigl fvliaciqaq qpttryevrg kvlqrtdsla lpganvvvsg
       61 tsqgtatdgq ggfmlslpag nttltvsfig fvtkeiqvev plseellivl edeyelegve
      121 vlstgfeelp aerstgsfaf ldrelvtrrv stnlvdrled vtpglifnrd rtdlgygesi
      181 sirgvstirg enqplividn laydgnlssi npndvesitv lkdaaaasiw garagngviv
      241 ittkkgsfes plrvdftant tviekpdpfy qpqmsisdfv dkeqvlfdrg yydgqvnsfr
      301 ktrlspvvet llshregmis dselseslda yrsrdvrnel erfiyqpavq qqyavnvsgg
      361 skkhnylist gwddnrgssr tvsdsrftll trqnwklakd rlqvsvgana iignrssavp
      421 sianlypydv laddagnplp vyrdynnrfk qglegaglld weyypleelg msptlirtne
      481 lrlnaqvdye ilpglkamay yqywhnvrfg etlnpvesyl ardlindftq vdeeggltyq
      541 vpmggildqd rtrsqshnfr tqltytkqfg qehelnvlag feakdfnssg sanraygynp
      601 gngtsapvny nefytrysig fpasipfses fsgntnryls gfvnmgysfr drylitgsar
      661 kdasnifgvn tnqrgvplws agagwilsee nfwnvdavdy lklkasfgyn gntnpnataf
      721 ttanyfgags ntlighpyln iisppnpelr werikiinvg tefdlfngrl ngsfeyytka
      781 gldllgeqam fpssgvlsat rnyastetrg ldlvlnsrnt qgklvwltnf flstvnekvv
      841 dfesqptpvq ivtsrsvvpv pvlgkplyhv fsyawagldp atgdpmgfvd gepsteyasi
      901 ineaeiddlv yhgssrptvf galrntlnyk gwslslnisy rlgysivrpt vnyddlnrgd
      961 ishsdyglrw qnpgdeltta ipsdpesvnn lrtrfhlssa sviekgdhvr lqdvrlaysf
     1021 ptlfsaagks levygyannl gilwkasdri edpdyifnpa ltsfsiglrm gl
//
LOCUS       WP_091695197            1161 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091695197
VERSION     WP_091695197.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1161
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127795
     Region          131..1158
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklppalk tlamrlftac llscwmhsmv fangvnaqkl eetivslsan elvlsesfvq
       61 iekqsgfkfs yetglnlnsk itftnrktdl qtileeisaq snlkfkqina tiavstkkks
      121 vmqslqidkv qisgivvdee tgetlpgvni iikgttkgtt sdldgkfait vdegavlvfs
      181 yvgydkqevt aqnqteliir lrldsdvlge vvvtalgikr eekalgyatq kvdseellda
      241 rsnnwsdalr gkvaglnvls agsgpmnssq islrgdnsln pngnfalivv dgvpmnsglt
      301 ssgvsnayga gsgndvpidf gngiadlnpd diesinvlkg asatalygsr aangalivtt
      361 ksgsqrtkgl gvtinsnfsf qnalkwpdrq yeygqgtgra fneegdlfys ygvsedgsnt
      421 ggtssafgpk fdgqsyfqyd ptlegqsaer qlwrpyednv tgfwrtgfnm vnsvslegan
      481 eggslrasit qtknewimpn tgfdrlvaal sasqqiskkl klnakvnytn kssdnlpatg
      541 ynnqsiayfm ifqnpsidle wyrpiwkegq envdqihpfs sfidnpylia yemtnsvnnn
      601 smfgnlsany tfndhfelml rtslamsqee raqqrpysta nfqrgyykeq nitnyeqnsd
      661 flftytgkla ekislrasvg gnhmsrkyrm msayvdglvi pgvyklangi nnpvlstnsn
      721 nrvinsiygl mtldfdekif vditgrndws stlptqnnsf fypsvstsfv lsdiftlpep
      781 isfaklrvsg aqvgndtdpy rtskyygqse fpgsasvpst lyntnfkpei ttsfetglem
      841 iffnrrlgfd infyisetkn qilqvpvdit tgyssailna grvqnrgiel vlngsplktn
      901 nfqwnsfitw aknenevlsl pdevdgsqvi gtggnatiia kvggttgdiy gfgfvrspeg
      961 eivygsnglp arpaeieyqg nayakwkggf rnefvyknlr msvlfdgqyg givysqthhk
     1021 mseqgkltht lkgredgfiv gegvvdngdg tfspnttevn lasyyadyyr ranvesnsfd
     1081 asfiklremr leygvpvkfl qktsirqasi alygrdlamw tkfpmfdpet aalnggtllp
     1141 gvemgqlptt rnmgvnltlk f
//
LOCUS       WP_091696971            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091696971
VERSION     WP_091696971.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116834
     Region          29..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mryklyknlw livfflcisv smahaqdvqi tgtvldetdm plpgvtvllk gtttgtttdl
       61 dgkysinapr dgilvfsfig ydpierevgn qsvidlvmnp ntsdleevvv igygtakkrd
      121 vtgavssvnp nklenenpns vqdilrgnaa glnvgmstsa kgggsleirg qtslnagnsp
      181 llvldgaiyy geladinpnd idnlevlkda saaavfgaka angvilittk kgtlgkpvik
      241 fnvnsglatm atfpdvygpd efvswredvf ksinaggydp yefsdprtlp sdisieewma
      301 ydgsagdpvt vwlqrlnmqp veienylagr svdwrdkifq tgfrqdytvs lsgrtenfny
      361 ywslgylnne giiigdeyst irsrvniegk vnkwltvgmn tqfalsddsh vpinddpapm
      421 yanwglyrtl spwgseyned gsykwrpnee qsggthpfyd mshtdrdqkg fsinstlfas
      481 iklpfgfnfr tnfsprfqyd erfyhrsaah eawaaeggva nrrnqkqyyw qidniltwqk
      541 tfaekhdfng tflinaekfq swdnsmnnng fephdrlgyh nmggginpii ssndeystgd
      601 almgrliysy dgkysttlsv rrdgysafgq snpralfysa avgwvfsden finidwldfg
      661 kmrfswgsng nrdigryvai sdlstgkyfy erpsgelylv nqlyvnrmen knlqwertes
      721 fnlgidfsvl ktrltgtiel ykmstrdllv qrslpdflgf nfvwdnlgqv dnkgfeltln
      781 stnfersnft wrstanfqln rneivslygd ldengveldd psngwfigra idqiwnyktd
      841 giwqldeaea aaeygvkpgd fkvedvdgdg rftnadrqfq gytsprfrws lrneftlfnn
      901 fdisfmvysy lghtgsfnqm knrdgfldrt ssyvtpywte enpnnewarl nsseggaggf
      961 svyrkksfvr menismgynf pkqltekani tnlrvygnir nvgfyapewd fwdpensgpi
     1021 pryftlgidv tl
//
LOCUS       WP_091695569            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091695569
VERSION     WP_091695569.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118214
     Region          24..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknyyllliy illagmplla qtqrtvtgtv tdsqdksalp gvtvlvkgtt ngtvtdeegt
       61 yslnapgesv vlvfsylgys tleqeltsgq smlnvqmtls dfaldqvevl atgyqeipre
      121 rangsfvgld kelvnrrvst gilerledvt pglifnregt esisirgrst iqanaepliv
      181 vdnfpydgpi eninpndves itvlkdasaa siwgaragng vivittkrak qgqsfrvsfn
      241 anttvvekpd lfynpkmsis slvdlhrtlf drglynssin srnkssvppa vevllqaqng
      301 ditqaeadal legfkrrdfr neldqyyyrp avnqqyalnl sgagtvhqyn lslgydrnss
      361 qivgnensrl tlsqnnawkl ldnkldigag iywvqgkdin rttlargvay drltddegnp
      421 iaiseaysdr ylnsveaehp dllnwryvpl eeiglldnks lssdlrlnan lgyrilpdlk
      481 aeiryqywtn ltetrdhipq eafyvrdlin qfseydadgi ltrhmplggi ldhgtgrges
      541 hsfrsmlsye klfasgnrin aiggfefknl iayndamryf gyddelglsv avdpntryrk
      601 lfnnilgslp anqshtgstd rfvsyfanas yqigtrfnfs asarkdqsnl fgvnanqrgv
      661 plwsvgggyt lseekwykmk elpylrlrat ygyngnvdkr tsayttaryf isssstipnl
      721 piaaitsppn pnlgwekiri anlgldfssk nsrisgtlef yqkkgedlig dievpassgf
      781 skfrgnfant atfgfdfnfs tlnidkgfqw ksdffwsyvn ekvtrynytl spsnflntga
      841 inpyegrplf gvygydwagl npengnpmgy ldgvpsedyr gilnaatldn lvyagpgrpv
      901 hfgsirntfs wkglelsani sfrlgyyyrr asvsyrniys gsfehgdydk rwqtagdell
      961 tqvpsmpeva ntfrdsfylc sealiakgdh irlqdvrlay sfregrlsgs lirnlsvyty
     1021 annlgiiwka tkdeldpdfr tsrpqrsiaf glnwnf
//
LOCUS       WP_091697137            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091697137
VERSION     WP_091697137.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111683
     Region          29..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyiksilvc cvvivaipfq lfaqgtlkit lspvvksnig etitgaivts eedgvsavsd
       61 slgvvklqvs tnsylsvsaa gyetkllvas pdleeivlfg nlegnqvnva fqtkdkndlm
      121 ggvsyvnmpe ilrdnyityp fenmeafvgg yngnlwgnss alvlidgvpr digsvhptei
      181 aqisflkgvs avalygskaa kgvimvttkr gvansqnitl rtnagvntpk rypqylgsge
      241 ymslyneart ndglsplysn ediynhssge niyrypntdy yspeylqeay tkydgnleis
      301 ggnetaryyt nvgfmtegtv mdfgqaaena nerfnvrgni dlnlndfisa kvdasaifyn
      361 sngvntdywg gsttlrpfrf tplipleyie egdeasmgfv etsdhvidgk yllggtqldq
      421 tnpiadiyag gsnkftsrqf qfnagvdadl rnvieglsfs slfglnyats ynlsfdneya
      481 vyqpnwtnyn gedqiasltk ygqdassrtq nitnnwfsqt vsfsaqlnyq rsfkgkhnvs
      541 amllangyqi aesaiyhkts nanlglhlgy nfqqkyyaef sgafihsaml akqnrqafsp
      601 tmtlgwrmse egflssssvi dnlrisvsag ilntdldisd yylyeaiytd egswyewkdg
      661 lnntgtdvrr genpnlkfpk reeislelda slfdnlltln gsvfnsrmtg lfvqnnvlyp
      721 syfvtgwpis swipfvnynn dlrkgadfql nlnkrvgeve wslgvsglyy tteaakrsen
      781 fedsyqnrqg mpldaiwglq sdgfftgmdd ienspsqafg evrpgdikyi dqnndgiina
      841 qdevylgrgg wsgapltmgv nlsarfknft ifaigtmrsg ayamknnnyf wvnaddkysv
      901 evrdrwteet qntatfprlt tlngannfrn sdfwlystnr fdlakvqisy sfpksilgng
      961 fikelgtyis gsnlltvgpn sellemnigs apqtrfynfg iraqf
//
LOCUS       WP_091697368            1157 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091697368
VERSION     WP_091697368.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1157)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1157)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1157)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1157
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1157
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126306
     Region          140..1156
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlikftryll vagvtgvlal pisangqnlt qfakgptsne klvsknlest lkeledlyai
       61 siaypsslve seakipaain skltaeenlq rilkgsqiny rkgagdfyml eksetqstta
      121 ptannftyqi ptqaveever tiegvvlded qvpipgasil ikgtmngtvt didgkfslsl
      181 edentdailv vsfigfttye tkvgansmft ielassdlal nevvvtafgl erdkkalgys
      241 tqsvdgsalt esrptnvans lsgrvagvqv tgnsmpgsga hvvirgsssv agnnqplvvv
      301 dgvpleqtss rqygnglsei spdnikemti lkgataaaly gsraangvim vttkngsgtk
      361 gigiefnsnm tmdnplvtpd fqntygggag yrtwyvdgrn gfdadgirgt agvdeswgap
      421 mdgsmvplwy sapekvallp qpnnfadfwe tgksfsntia lsggneqgsf rvaigrldqt
      481 simadndyfr nnfklntsyk fvpklqmsvn aeyiksgsdn rgftgsqdfi wahrhtdytk
      541 lknwedyyei qrqtfrpgdd ypyanwqhey fsnpffnqky lpnsnekdrl vgsialnydi
      601 nehfsimars gtdywsdtri ninsaesfkn nvkrfgsyte svlnsqetns dviltfdknl
      661 fprlslkiqa gannrvnnyk stsvnvgqlt idglynlgny aspvtpssti rkqtvnsvfg
      721 saqfgynnyl fldvtgrndw sstlptnnns ffypsvamsa vltdifdvqs gflsfakirg
      781 siaqvgndad pyllnqvyss eglwagttpt yaesneianr slkpeittgk evgldlrfle
      841 grvgidftyy hqstvnqila vsistasgys sqilnageit nqgveltina tpfntasgfs
      901 wytavnfarn rnkvvelaeg lenyilgtqn sltsearvgq pygslygrry lrspegelvy
      961 nnglpileeg thilgniqpd wiggwtnsfa ykgielntli dvkmggdifd vgtglarktg
     1021 qyaetaagre egvigqgvin vgtaeepvyv pndviasatt fwnsqnprty hesgifdgty
     1081 vklrelslgy vfpksflgnk fiqsmkisfv grnlailykn hphmdpevdg kggngqgfsy
     1141 gempstrnlg fnlnvtf
//
LOCUS       WP_091698102            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091698102
VERSION     WP_091698102.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119950
     Region          25..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtlryllig lmvfvfqtlq aqeflqgtvl ekdsgipmag alvlitpdvg stvadeegef
       61 rmeleagsye lrisfmgykt ltskvtvpvg eelllelepm emgldevevv stgyqeipkd
      121 rasgsfvtld eelidrrvst nlvdrledvt sglifnragd qtrdpisirg rstlgvfsqp
      181 lividnfpyd gslddinpnd vesitvlrda aaasiwgara gngvivittk lgkrnqemkv
      241 sltansnwiq kpdpflspvm ginefitiee qlfesgyyns tfsnptrpav tpvvetlyqe
      301 reglitaeea drriaayrsy dlrediqqyl yrpqlnqqyn iglsggsash symislgydd
      361 qrlsevgnsn nrftlnvknd frlvndklgv qvgfygaksr evdqnagpgd lsftsaqtmy
      421 pyarladeng nplavtnrfi nsfkqeaeaa glldwdyvpl deiglsptkd ylddwrlnlg
      481 mdyallkglk akilyqywqm nsrsetlydq dsyyareein lfsefdengn lirnipyggi
      541 lqhssrlsns hsaramveya gdwgnkwefn slagaelkml dfetssqrly gynaetgstq
      601 kvdylsvfpq ynfplimspv thadgvgaga drfyslfana slsysnryll tlsarkdasn
      661 lfgveanqra vplwsaglgw tlseedfyhw egmpylklrv sygfngnvdr slsafttari
      721 atrntltnlp yaqivnppnr nlrwerikit nvgldmeskn grisgtlefy lkdgldligq
      781 spyppsagil tftgnnasmr ttgydlqlnt rnltgglkwn tafllsglke rvtdyeiesp
      841 vasildrgas gggggvnypv egrplfsfys lpwaglnpdt gaprglldge psedyrtlvn
      901 easlesivfh gparpttfgs lrntfsykgv slsanisyrf gyyfrrtsvq yssiqmgrgg
      961 hsdyelrwqn pgdelvtqip sqpasidnlr dtfyrnssvl vekgdhirlq dvrlgysipk
     1021 qgtglfskme raelflyann lgmiwkatdt dwdpdfgrqi prksiafgiq ldf
//
LOCUS       WP_091698457             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            locisalis].
ACCESSION   WP_091698457
VERSION     WP_091698457.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus locisalis
  ORGANISM  Algoriphagus locisalis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Algoriphagus locisalis"
                     /db_xref="taxon:305507"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107998
     Region          36..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnknyilkts iavrclavfl mivfstnfse alaqsktisg tvsdnygmtl pgvsvlikgs
       61 tqgtvtdleg kyvltsdgdi gtlvfsyigy ttqevvlgnq nvlditleed llgldevvvv
      121 gygvqqkkdi tgatssiske dmnqgaitnp lqqisgraag vnitqigsep gsrptvrirg
      181 itsliggsdp lvvidgvqgn ldllnqvpps eiesidvlkd asataiygsr gapgviivst
      241 krsksgqati eytgsvsvdq ianelevlda egwreqariw nvpfsedhgs dtdwydiltq
      301 tgmtqnhtva lgggsqnfny rasvsailqd gvvinssnkn yiasisatqk aiddrltmtf
      361 tmnnsirqni gspggvgrag ftsnlisnay vskptdpvlf engdyffdpn vfqyinpyav
      421 aetiineres rsqfttfrtd feiidglkag wfgswrkvdv nsgyyapaas tlagaidqqg
      481 ianvntnltd eklmdislay dkdfgkhkin aigvyewqrq tyqghfaqtk gfindlteyh
      541 alqlgsvsry lpgdissykn drtlvsflgr vnysfadkyi ltasmrrdgs svfgeehkwg
      601 hfpsvsaawr igdegfmqgq nlvstlklra gygitgnqqg lspqqslqlv gasgstyfng
      661 glitnfqvtq nanqnlqwet rrqtnvgidf gfaqdkingt idvytattdn llfnyavpqp
      721 pypfgsiaan vgslrndgle lalnyhlldn sdwsitlagn vtfmrnever lsgtiggvev
      781 ntnyvgwgfn syliegqpig tfyilendgk esgtneelvv drngdgvidq gnespdryia
      841 gtalptftya ftptvkfknf dlsmvwrgsg gnmifnrirr dfslyeslgk snmlvsaenl
      901 glftsqyasd lwlekgdyvr fenlaigytf ntakirniss mrlsvvgnnl alftkysgld
      961 pelnlsggng sgldagiypr trsiavglhv sf
//
LOCUS       WP_091716053             409 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium phyllostachyos].
ACCESSION   WP_091716053
VERSION     WP_091716053.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium phyllostachyos
  ORGANISM  Methylobacterium phyllostachyos
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Methylobacterium phyllostachyos"
                     /db_xref="taxon:582672"
     Protein         1..409
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42088
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd saeprvaavp etvkkfkalg advvvqsgag tragflddey eaagatvags
       61 aadaardadl ilkvrrpgge elplfkrdat vvaimdpygn edalramada gvagfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrampmmmt aagtvpaarv fvmgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsegyra
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 pggivtterg vkivghvnvp grlaatassl yarnlyafve tlidkeskal ainwddelvk
      361 atnltrggsv thasfqsktd gaaseaasvg laksevnkas gspatsgaq
//
LOCUS       WP_091719752             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudarthrobacter equi].
ACCESSION   WP_091719752
VERSION     WP_091719752.1
KEYWORDS    RefSeq.
SOURCE      Pseudarthrobacter equi
  ORGANISM  Pseudarthrobacter equi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Pseudarthrobacter.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Pseudarthrobacter equi"
                     /db_xref="taxon:728066"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53344
     Region          3..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivael gsesrvaatp ttvkrllelg yeivvekgag essafrdedy esagasvvga
       61 deawgsevvl rinppsedei grladgatli gmlapslrpe lvealavrpi talaldavpr
      121 israqsmdvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksiggs ylkveveeem kssdgyakat seaynrraae
      241 iyseqaadvd iiittalipg rpapklltad dvagmkpgsv ivdmaagqgg nvegsvager
      301 tvtengvvil gytdlparlp aqasqlygtn llnllklltp ekdgqlridf ddvvqrsvtv
      361 vregektwpp ppvqvsaapa aqapataevt napkkkegls pagkavlfas giaalfgina
      421 vapaplpqhf tvlmlsvvvg fyvigkvhha lhtplmsvtn aisgiivvga llqvtsenpv
      481 vqvlaavavl lasinifggf avtrrmlamf sagkars
//
LOCUS       WP_091723721             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudarthrobacter equi].
ACCESSION   WP_091723721
VERSION     WP_091723721.1
KEYWORDS    RefSeq.
SOURCE      Pseudarthrobacter equi
  ORGANISM  Pseudarthrobacter equi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Pseudarthrobacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Pseudarthrobacter equi"
                     /db_xref="taxon:728066"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39899
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiprerr dgerrvaatp dtvkqlagmg ldvlieagag daaghpdrey teagaavvpe
       61 ldtgavdila hvrpldprta sglkrgavtv glaspsselp tvqalaeaga tsfalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplymtaa gtvpparvlv lgagvaglqa
      181 igtakrlgar vsandirpas adevasmggt firldletae aaggyarqls sdagtrqrql
      241 laphvaqtdv littaavpgr rapllvtldm vqgmrpgsvv vdlaaesggn vegavpgedi
      301 avptadgagh vtlvglkdpa samasdasrl yaknvanlla lmvrngelvl dfddevvaga
      361 cfthagevrh rptaellget ararqegvl
//
LOCUS       WP_091730463             372 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Roseateles].
ACCESSION   WP_091730463
VERSION     WP_091730463.1
KEYWORDS    RefSeq.
SOURCE      unclassified Roseateles
  ORGANISM  unclassified Roseateles
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="unclassified Roseateles"
                     /db_xref="taxon:2626991"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38793
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpqeta agearvaatp etvkklvaqg htlrvqqgag lnasvtdeay aaagaelvgr
       61 eaafacdlvl kvrapepgem alfkpgavla gmlnpfdrdg lqrlaearlt afaleaaprt
      121 traqsmdvls sqanlagyka vmlaafhyqr lfpmlmtaag tikaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpavk eqveslgakf idvpyetdee rqaaegvggy arpmppswlq
      241 rqqvevakrv aqadvvvtta lipgrpapvl vteemvramk pgsvivdiaa paggncplte
      301 pgrtvrkhgv tlvgetnlps lvaadasaly arnvldflkl vltkeggfal padddivtac
      361 lvahegqvlr qa
//
LOCUS       WP_091737011             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phenylobacterium immobile].
ACCESSION   WP_091737011
VERSION     WP_091737011.1
KEYWORDS    RefSeq.
SOURCE      Phenylobacterium immobile
  ORGANISM  Phenylobacterium immobile
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Phenylobacterium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Phenylobacterium immobile"
                     /db_xref="taxon:21"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38424
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,95,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 madiavtrer rdgetrvaat petvrkliam gfaltveaga glaasfpdad yeaagaklap
       61 daktavagad ivfgvrgpap etigalkpga ivaaalnpyv drvtldalaa ggatafamef
      121 vpritraqam dilssqanla gyravieaae aygrampmmm taagtvaaak vfvmgvgvag
      181 lqaiatarrl gavvtatdvr patkeqvesl gakflavede efknaqtagg yaremsaeyq
      241 akqaalvssh iakqdivitt alipgrpapk lvsaeqvasm rpgsvlvdla veqggnvvga
      301 qpgekvvteg gvmilgapnl pgriaadasa lyarnlmafa glfldkegkl apdyedeilk
      361 aalvtqggav thpnlka
//
LOCUS       WP_091738789             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium azadirachtae].
ACCESSION   WP_091738789
VERSION     WP_091738789.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium azadirachtae
  ORGANISM  Microbacterium azadirachtae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Microbacterium azadirachtae"
                     /db_xref="taxon:582680"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52359
     Region          4..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mavigivrep agesrvaatp atiaqlrklg hdvvvehgag sdasypdeay aaagaelvdr
       61 aqawgseivl aitapgaeqi alladgatii allspalrpd lveslaqrgi talaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvtsigge ylpvdvavek stdgyakats eaydrraaei
      241 yteqaadvdi iittalipgr aaprlitasd varmkpgsvi vdmaagqggn vegsvageri
      301 vtpngviilg ytdlasrlaa qasqlygtnv anlvalltpg kdgaftidfd divqrsvtvv
      361 rdgeitwppp pvqvaaapak apvastpiea pqqrgpsagr kallivlgia alflvnafap
      421 aplpqhftvl tlsvvigfsv igrvhhalht plmsvtnais gvivvgamlq itdpdpvvqv
      481 laaiavllas inifggfavt rrmlamftkg gqk
//
LOCUS       WP_091748019             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brevundimonas sp. 374].
ACCESSION   WP_091748019
VERSION     WP_091748019.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. 374
  ORGANISM  Brevundimonas sp. 374
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Brevundimonas sp. 374"
                     /db_xref="taxon:1150400"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38663
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavaiavtre rregetrcav tpetvkklia lgatvtveag tglgssipdv dyaaagavvk
       61 pdtravldga divlkvrgpt aqetsalkpg svviamlday rdkatvdala gagatafame
      121 fvpritraqv mdvlssqanl agyravieaa yaygkgfpmm mtaagtvaaa kvfimgvgva
      181 glqaiatarr lgavvtatdv rpatkeqves lgakflaved eefknaqtag gyakpmsaey
      241 qakqaeltas hvvkqdvvit talipgraap vlltaahvas mkpgsviidl aveaggnveg
      301 srlnevvtta ngvtvvgwsn lpgriaadas alyarnltaf vglmvkdggl avdledeilk
      361 tavvthagav vheglkgth
//
LOCUS       WP_091759721             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Pedococcus
            cremeus].
ACCESSION   WP_091759721
VERSION     WP_091759721.1
KEYWORDS    RefSeq.
SOURCE      Pedococcus cremeus
  ORGANISM  Pedococcus cremeus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Pedococcus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Pedococcus cremeus"
                     /db_xref="taxon:587636"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53043
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpqesk pgetrvaatp ktvgqliglg yevvveagag rrasfsdaaf qeagasvgts
       61 advwdsdlvi kvnaptdeev grlrpgaila sllapalnpe lverlagqgv talamdavpr
      121 israqaldvl ssmaniggyr avveaahefg slftgqvtaa gkvppakvlv vgagvaglaa
      181 igtanslgai vrafdarpev aeqvesmgae flrvegleqe gpsatgyake mgedfnrraa
      241 elyaeqakdv diiittalip grpaprlita dmvasmkpgs vivdmaasng gnvegtvadq
      301 lvltdnqvri igytdlpgrl ptqasqlygt nvvnllkllt pgkdgkavid fddvvqrgmt
      361 vcrdgqstwp pppvavsaap vaaapaaekp appppkvrdp rrryalmgla avlfglvaay
      421 spatflghft vfalavivgf yvisnvahal htplmsetna isgiilvgal lqigsedpvv
      481 rtlafvatvi asvnifggfa vtnrmlqmfr kd
//
LOCUS       WP_091768296             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Maricaulis
            salignorans].
ACCESSION   WP_091768296
VERSION     WP_091768296.1
KEYWORDS    RefSeq.
SOURCE      Maricaulis salignorans
  ORGANISM  Maricaulis salignorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Maricaulis.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Maricaulis salignorans"
                     /db_xref="taxon:144026"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38871
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriailkerh agetrvaatp dtvkkftaag hvvavekgag ltasvtdday asagaelgtl
       61 aatlkgadal fsvqmpddat laklpkgmll vahldpygaq erakalakag idalamefvp
      121 risraqamda lssqsnlagy rsiieaaqiy grafpmmmta agtvapakaf imgagvaglq
      181 aiatarrlga vvsatdvrpa skeqvaslga kfvavedeef kqaetaggya kqmspeyqak
      241 qaelvaghia kqdivvttal ipgrpapkli tkamveamkp gsviidlaap nggnceltka
      301 deivthqgvm iagfsnlpgr laadssalya knlanllpll vgedgaraph wddeiiqgma
      361 ltrdgavvhp tlvkesa
//
LOCUS       WP_091776344             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia steynii].
ACCESSION   WP_091776344
VERSION     WP_091776344.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia steynii
  ORGANISM  Paraburkholderia steynii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Paraburkholderia steynii"
                     /db_xref="taxon:1245441"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39240
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipkesr cgetrvaatp etvrklkllg yelliqhgag dnshfpdaay veagaalvdk
       61 esafgadlvl klwapddeel gllkggtvli gmlepfnadl rhklgnaglt afalelvprt
      121 traqamdvls sqaniagyra itlatglyqr fmpmlmtaag tvkaarvlil gagvaglqav
      181 atakrlgavi easdvrpaar eqieslgakf vdvpfetdee rqaaegkggy aqpmpaswle
      241 rqarkvrera taadivicta fipgkpapll laenvvsemr pgsvivdlaa grgqagagnc
      301 alsvadetvi chgvqiagpt nlaasvatda salyarnmle fvrnltakdg sfalnmddei
      361 vsaslichqg atplaa
//
LOCUS       WP_091779235             409 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium sp. UNC378MF].
ACCESSION   WP_091779235
VERSION     WP_091779235.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. UNC378MF
  ORGANISM  Methylobacterium sp. UNC378MF
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Methylobacterium sp. UNC378MF"
                     /db_xref="taxon:1502748"
     Protein         1..409
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41996
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd saeprvaavp etvkkfkslg advvvqsgag rkagildaey eaagasiags
       61 aadavgdadl vlkvrrpsae elpqfkrgat vvaimdpygn eaalqamaaa gidgfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrampmmmt aagtvpaarv fvmgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsaeyqk
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 agevvtndrg vkivghvnvp grlaatassl yarnlyafve tlidkeskal ainwddelvk
      361 atnltrggsv vhtsfqpktd gaaseaasvg lakseantas gtatptgaq
//
LOCUS       WP_091787057             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia steynii].
ACCESSION   WP_091787057
VERSION     WP_091787057.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia steynii
  ORGANISM  Paraburkholderia steynii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Paraburkholderia steynii"
                     /db_xref="taxon:1245441"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54915
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligiple latgerrvat vpevveklik lgfmvavqss agaaanfddd ayraagaevm
       61 asaselwacs divlkvraps sdevasmreg gmligfvwpa qnpelmqqla akratvlaid
      121 alprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfvagagv
      181 aglaaigtaa slgasvrand traevadqvk slgsefvkvd ydeegsgggg yarvmsegfq
      241 qaqramyaqe ardadiiitt alipgkpapk litaemvrsm kpgsvivdma aeqggncelt
      301 vpgeavvrdg vtivgyiela srlarqssml ygnnllrvve elcktkdgti nvdfdddair
      361 gltvikegsi twpppplrqp avapapqpaa aaaavaprkg hgssepmsak slafafgiga
      421 laflmvglya patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiivigalv
      481 qvapplggsa agdrpsglil glavgalalt avnmfggfav trrmlamfrk
//
LOCUS       WP_091787785             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Pedococcus
            dokdonensis].
ACCESSION   WP_091787785
VERSION     WP_091787785.1
KEYWORDS    RefSeq.
SOURCE      Pedococcus dokdonensis
  ORGANISM  Pedococcus dokdonensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Pedococcus.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Pedococcus dokdonensis"
                     /db_xref="taxon:443156"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52258
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpaesk agetrvaatp rtvgqliglg ydvvvergag arsaftdeay aaagasvgeg
       61 agawesdvvl kvnaptdaei allrpgalla slvspalnpd lverltaagv talamdavpr
      121 israqsldvl ssmaniggyr avieaahefg slftgqvtaa gkvppakvlv vgagvaglaa
      181 igtanslgai vrafdarsev geqvesmgae flrievedeg psatgyakem gddfnrkaae
      241 lyaeqakdvd ivittalipg rpaprlltee mvasmkpgsv vvdlaaangg nvagtvadqv
      301 vttpngvkli gytdlpgrlp tqasqlygtn lvnllklltp gkdgrvvldl ddvvqrgmtv
      361 crdgetlwpp ppvqvsaapa aaaapvpepk apkpppdprr kyvamalaav vfglvaansp
      421 evflghftvf alavivgfyv isnvahalht plmaetnais giilvgallq igsddpliav
      481 laflgtvias inifggfavt grmlqmfrkd
//
LOCUS       WP_091793391             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. WP9].
ACCESSION   WP_091793391
VERSION     WP_091793391.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. WP9
  ORGANISM  Burkholderia sp. WP9
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia sp. WP9"
                     /db_xref="taxon:1500263"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39508
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigiptetr ahetrvaatp etvrkyvsqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatlv gmldpfnaen ssklaaagit afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvdtvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvirhgvti vgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll ardgevtrks
//
LOCUS       WP_091796709             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. WP9].
ACCESSION   WP_091796709
VERSION     WP_091796709.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. WP9
  ORGANISM  Burkholderia sp. WP9
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia sp. WP9"
                     /db_xref="taxon:1500263"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39501
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvrkyvsqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatlv gmldpfnaen ssklaaagit afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvdtvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvirhgvti vgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll ardgevtrkt
//
LOCUS       WP_091800176             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Prauserella marina].
ACCESSION   WP_091800176
VERSION     WP_091800176.1
KEYWORDS    RefSeq.
SOURCE      Prauserella marina
  ORGANISM  Prauserella marina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Prauserella.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Prauserella marina"
                     /db_xref="taxon:530584"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38059
     Region          8..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpdpespltv gvvketkpge rrvalvptlv grlarrglrv viesgagega rladevfeea
       61 gaeigdawaa divltvspps vadigklges avlagflapl tnteelaamk kagirafave
      121 siprisraqa mdalssqagv agyravllaa qrlpkffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgaqatgydv rpevaeqvrs vgaswldlgi eavgeggyar elteaereeq
      241 qrrlteattg fdvvittalv pgrtaptlvt aeavrgmrag svivdmaget ggnceltepg
      301 keivahdvti csplnlpaem pvhaselygr nltellellv naegelvldf sdpivsgacv
      361 agadeevr
//
LOCUS       WP_091803793             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. WP9].
ACCESSION   WP_091803793
VERSION     WP_091803793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. WP9
  ORGANISM  Burkholderia sp. WP9
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia sp. WP9"
                     /db_xref="taxon:1500263"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39384
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaesr agetrvagtp etvkkltaqg htvlvqsaag ehahfpdvay aqagatlvda
       61 aeafaadlvl kvqaltetel gqmtrgailv gmlnpfdadh vahiraagvt afalesiprt
      121 traqsmdvls sqaniagyka vllaaglyqr fvpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpcetdee heaaqgaggy arpmppswla
      241 rqsalvhera kqadivitta lipgrtaptl lnedtvramk pgsviidlaa gkgavvddrr
      301 ggncpltead avvlrhgvqi agytnlpamv atdasalyar nvldflklii dtcgnpkidt
      361 sddivaatll ghdaamlqta
//
LOCUS       WP_091813376            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091813376
VERSION     WP_091813376.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123716
     Region          24..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrltvflt alllsigvaf aqnkitgtvm qddgepaiga tvkvvgnnng vvtnvdgkft
       61 idvpsgkkle fsyigyvtkr lapkngmkvt mtqdskviee vvvtgmqkqd krlftgaatk
      121 idaekakidg vadisrsleg rvagvsvqnv sgtfgtapki rvrgatsiyg askplwvvdg
      181 vvmedvtevd adalssgdan tlissaiagl naddiesfqv lkdgsatsiy garamggviv
      241 vttkkgkagq shisytgeft mrlkpsysqf nimnsqeqms ayremynagw ltfsdtyrgs
      301 esgvygkmyq lmntydpatg qfllpntdea myaylqeaef rntnwfdelf stsisqnhsi
      361 smssgtdkaq yytsfsvmnd pgwterskvq rytaninaly nlskklslnl ignaayrkqe
      421 apgttnqsad pvsgqvtrdf dinpysyain tsraldpntf ytrnyapfni hnelannymd
      481 ldvvnlkfqa elkykpirql elaalgayny svatrthmik ensnqsmafr amddatmrdn
      541 npflyqdpdv pnslkysvlp eggfyrtykn vmnsknfrat asyndafgqe eehivnvfgg
      601 mevndierna nyfngvgmqy emgmlgaydy hffkqaseen nmyyevsnny ernvaffgta
      661 tyswkhryti tptvryegsn qlgrslkarw lptwnisgaw naheeswfad tfknilnhat
      721 lrlsysltgd kpavnnamvi iesvnpwrpf asdketaldi qqfgnpdlty ekkhefnvgv
      781 dlgllnnrin vtfdwwmrnn fdligprmtt gvggsitkya nvatmkshge elsistkniv
      841 agdfkwntdf ifshnktevt dldsrspiyy ltgqnqrngf tmvgypyral wsidfqglde
      901 hglptfinqd gnlttsdhdf qsyvldhlvy egptdptitg slgntftykn lhlnvfasys
      961 fgnvvrldpv frssysdlda mpkefndrwv vggdelktni pvladrrmnq adpylsyayn
     1021 aynystaria kgdfirmkei slsydvpasw inplginsln lklqgtnlfl iysdsklngq
     1081 dpeffntggv avpmarqftf tlragl
//
LOCUS       WP_091814105             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Allobrachymonas denitrificans].
ACCESSION   WP_091814105
VERSION     WP_091814105.1
KEYWORDS    RefSeq.
SOURCE      Allobrachymonas denitrificans
  ORGANISM  Allobrachymonas denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Allobrachymonas.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Allobrachymonas denitrificans"
                     /db_xref="taxon:28220"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38862
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpletv pgearvaatp etvkklvgqg htlkvqagag iragitdaay eaagasivda
       61 atalgselvl kvrapseael aqikpsatlv gmldpfdran lermaaagit afaleaaprt
      121 traqsmdvls sqaniagyka vmlaadkypr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetdee reaaegvggy arpmpqswle
      241 rqkaevakrv aaadvvista lipgraaptl vtedmvkamk pgsvivdmaa gkgpngtdgn
      301 cpltqagqtv rvhdvtivge tniaglvpad asslyarnvi dflklvlpae gglkvdmedd
      361 ivaaclmtqn gevkrk
//
LOCUS       WP_091814758            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091814758
VERSION     WP_091814758.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122645
     Region          32..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskrfarilg liifscqlsi issyaqkagd iisgtvtdaf gpvmqanvie idaanrivaa
       61 attdmngnfs fklknpkdkl kisyvgcktq ilpinkthyn iklvdqttlt gveivsskka
      121 ggsglqipvk eissarqsid mkefeglsvt tvdealqgri agldivansg nlgsgtsmrl
      181 rgvssinsss eplivvdgnv lqggapsdfd fqsandekfa ellninpedi esisvlkdaa
      241 ataiwgsqgg ngvieiktkr gargntrvty sfrltgtyqp ngmkllngde ytmllkeeyf
      301 nphmnpnasd dineinyvsg gkfseyqmyn nntdwvdavk ktgwrqnhyv slsgggekan
      361 friaagydhe tgsiikqqld rfttrvaldy fvsdrikiat nvsltytdnh knysdllsva
      421 yrrmpnlsiy eedkngnsls efynmlpssn kvfednqykd ynpialayla qseessynie
      481 pefklnyell gieneqtrlt yegkivfnis nryndmfrpv elstggwtsk danlatstan
      541 kslgvtttht ltfvpqfrnk dhslmmllrg qltkgtstnq ntseyglpsg tirstsaagi
      601 idafsaspgq wrslyftysa hyaykgryva dfsvrrdgtt kfgndkrwgn fpalsgkwiv
      661 sdepwmkkgl pfvsmlaarl gwgivgnppg geglyyskyt ggkgymnygs vyqkniqlkk
      721 lkweqketin fgldfgfwne lisgnvevyr qkttdllmgn rslpsssgfp sldyqnvgam
      781 envgwefnln gnriikagkf svdfnvtfan nrnkltemde tvlaslnndf dkkngsylsr
      841 velnrplggi ygfrykgvyq yskysevevp gvsgpnapva rdkdgnvivd nygrtkpmrf
      901 cytgieedek efkggdaiye dinhdgqine ldivylgssl pkftggfgfk lhfgrltlnn
      961 qfnfrygnki inkarmnaen mysnnnqsra vlwrwrvegd iapipralyn ygynwlgsdr
     1021 fvedgsfirl nytqlsyavp qkhlkklgln qlslyvsann lfvltkysga dpevgyggyg
     1081 vvtdnaqtpr aksftggvti sf
//
LOCUS       WP_091816493            1093 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091816493
VERSION     WP_091816493.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1093
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123899
     Region          22..1090
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlyllfisf vilfagevka qrmvtgtvsd tkgeplygvt iavkngkhta vtgldgkyri
       61 pvdnenavll fryvgmepyq ttvkgqvtvd vkmkdqttql aeavvvstgy qrlsrersta
      121 afgfvdstkl nrvmhkdils alegqvaglr mdinpntgeg spvlrgvgtf stsigtkpli
      181 vvddmatdme lseinlydve svtvlkdaaa asiygalaan gvivittkqg ksekttvsvn
      241 adwyistkpt fdamhyasts diidyetnvy narvnssgsv atlfnsfsrn yysplyqlyr
      301 dqaegritqd dvdrtlgqwr qndyynqyrd lvwrsavtqr ynvslsqksq rsnhfasfny
      361 ehdknrvknd nsdafsiylk snfklnkwls iklgidtrfs nsqvpdyayt nyniqeryas
      421 ivdaqgnlvm tpyvnisgfa ggslngsaia dsqqqlassd vlmpfsfnvl qsldesltqn
      481 rnlrmrpfvn veakflkwfk ynlmfqyewt qsrtekydep nsylmrmthn alidldgvsq
      541 lpsggryrqt tnntrrytfr nqlnfeksfl eskhhvnaim gfelrenraa rpieqqmygy
      601 ndvaltsvrm dwaslnnvgv eslvygntvk lggpatsqte ifhryasfya nvgydylyry
      661 nitgsirwde adlfgldtkn qhhplwsvga gwniseeafm kdfswldflk lrltygvngn
      721 vdqssttyfv aryrtenndp tntqylrytd dnlpnsrlrw ektstfnagv dfrvlnnvls
      781 gslefynrvg ddllvrkyld stlgatqrvi nngkmrnqgv elqlnanllr tkdwtlsagf
      841 niawnhnkml rvehsstdia snfitapany fvegtsyntl wayrlsrvvn gypvildadg
      901 nematfdadg nptevqvsst lkgtdalvnm gslvpvyngs ltlslrwrel elntllvyag
      961 gnklrldatd mnsyqmvtdh vndhtvkhyy emptgsvaqq yastfsewwr ycdaqvkpad
     1021 yikmrsisma yhlpeavtkk lhigqtrltl qvnnlfywsr vghdidpesy slnsasrtll
     1081 qpktfsigfs tsf
//
LOCUS       WP_091818069            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091818069
VERSION     WP_091818069.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123907
     Region          48..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkryilfgmt llmafplcav aqdedteeee evvqvkrvvr vqkhyetrtv kgyvfdaasq
       61 kpvsgaivra adidgysvlt dddgsyslkl plfstslyis spdhnpvkig lskdeaqksv
      121 nlypsaftae ygvqtnvrgd yeatdfkysp ainikdevqk qlggqvytin rsgtpgigsv
      181 mfmqglnsln vnaqplivid dviidqqygr tllhdgfynd vlnninpadi ekvtvirngt
      241 alygskgang viliqtrrnk smatritani sagvtmepny isvmnadqyr syasemlkst
      301 nttlrdfkfl kseydargnk yyyydqyhqn tdwkdyvyrt amtqnyginv eggddvanyn
      361 lsvgytnaks tmkyndmdrl nvrfntdisl snklsvrfda sfanqtrdir ndgapegyde
      421 gtpiapsfla yvkspfmsay syghdetgag rfskehydid tesylseala nynnynwqlg
      481 npaainqyae antknrfets mlnltvtpkl eiardlfvse hfsynlvntn emfyipingt
      541 psyyvsslgg yrqnetrsla skqnsvmsdt ridwkkrfda hflhlfggar inwesftsts
      601 qvgyntgsdk tpflsgslqd kdvvgisenw nslswyaqae ynykgryyaq anltidgssr
      661 fgqeggdfrl fkaawgvfps fqagwvvtne pwmadvkgid ylklsagydi sgnddidyya
      721 arsyfrasqf lhtisgiafe gigntkiqwe ttrrlnlgle gsffdnrlsl gfnyfrsktd
      781 nlltlqqlgy lsglkenwsn ggklknegfd vsftakvlnl knwqwqigas aghyknqite
      841 lpdgkqfvdn eiygatvrtq vggvanafyg yktlgvfstt aeaqaasaaa agaatydpng
      901 lyfvgengvd hvyfeagdmh fadlnndgmi tdadrtfigd pnpdiygnif tslsfkrfkl
      961 dvnfnyslgn diynymrsql eggsrfmnqt tamlrrwqve gqqtdiprit fqdpmdnarf
     1021 sdrwiedgsy lrlksvtlsy dlpvkseylq gfqfwiqgnn lltftkylgs dpemtatssv
     1081 igqgfdlgrl gqsrsivagv kinl
//
LOCUS       WP_091818073            1133 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091818073
VERSION     WP_091818073.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1133)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1133)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1133)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1133
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126684
     Region          27..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkilksvimt ialllsttls aqnitsvhgt lsddmgplmg atvceidatg riiesaltdl
       61 ngnftmkvrn tkdkirfsyv gletvtmpin kttyvlkmks ktklkevtvt skrrmqgntl
      121 pipqreisya tqtismkefe glgitsvdea lqgriagldi vgnsgnlgsg stmrlrgass
      181 istltdanpl ivvdgnirev nldnfdmaga ndekfaelln inpediasit vlkdaaatav
      241 ygsqggngvi elttkrgvrg apkvtyslkl tgtyqpqgya llngddytmm lkeayfnprq
      301 ndnasnkyai peinyvddps iladwrqyra ntdwrdavtq wglrqnhyat itgggekasf
      361 rigagydhet gtiiqqkmnr fstrvnldyn vsqrirvstn fsltyskydd nsddllaial
      421 kkmpnmsiyq idpvtgketd kyynmpqsgt yigsevfknd qrnyvnpvas aylakkqrrv
      481 ydmnpeliln yqllglddeh wqlnwrssvy mnisnhynds fypqelvtkr wedkvntsas
      541 sssksvsfnt kqtltlipaf ankdhsvmmm grfeltsgss ssqstdgygl pstngvivsp
      601 saggiingms sgysqwrsmy ytfsahyayk gryvadftvr adgttkfgpg nrwgyfpsvs
      661 lkwivsdepw mqklkptlsm lairpswgrv gnqpgqnylf tskygsadry ldmaamkpln
      721 irltdlkwql vssynfgidl gfmdgrlnlt iegyqsttsd mlmgsfrips ntgfatvpyh
      781 nngkmrntgw efhintnrmi kagkfsmdmn anfgnnrnei lemdeyilen knskygynng
      841 etlrrvqlhn pfgaiygfky kgvyqynylt iknhvqdmve agatkddiqa wwrewsgsgk
      901 tapvavgadg nlilegnnvp krmmydyrsd ntghdgafpg fnggdaiydd lnhdgqinal
      961 ditylgsslp kltggfgfsf nygqwrlstq ftyrvgnkii nkarlqaeam tgndnqsqav
     1021 nyrwrqegdv tpipramygg nsnyntlisd rfvedgsylr msyaqlnysi nkknltwigl
     1081 nrlsfyasvn npfvltkysg vdpdiafgge dpaidnmqtp rsrsytlgit vdf
//
LOCUS       WP_091818494            1150 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091818494
VERSION     WP_091818494.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1150
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128201
     Region          24..1149
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskskfllti lftfiaqvmm aqsrvisgtv edamgpimma nvverdgnnr iisatqtdmm
       61 gnfsmeiknp knklvvsyvg sktkilpign qktfkikled dktvlgevkv vgrrtnaggl
      121 nidkrevsvs qqtmnmaeve gmaftsadea lqgeiagldi vtnsgnlgag tsmrlrgvst
      181 lsgsaepliv vddkifeyda adfdpenmde ekfssmlavs vddiasitvl kdaaataiwg
      241 sqgangviqi ttkrgargkp kvtlgykftg twmpagydll ngdnytmmlk eefynptqss
      301 satstinein yvpaeswaea nnwnkntdwv saikqfgeqh eanfnisggg qkatfrisas
      361 ynhqtgtvik qkmdrlttrl vldynvsdri rfstnfalty tdnlknytyg sskssgshnn
      421 llamalamap nasiyrydry nnntgeyflm nptvtgmtpd dgnytstqla dvvaignpva
      481 yansswqkeq tysivpdfnl kyellgtgtg qhrltfdgrv yfdiyayskp tympgslsng
      541 sytdtnynyl tntetnqfkm gsrvtltytp afknedfylt mfaryeagtq kntyqyiaqs
      601 sipngmesat idarlndmnn qpsatksawq dfvynahfsy ksrysvgfsl rgdgnskfgp
      661 knpwfyspsv slrynlseep fftplkkyvs mfgirgswgi tgsssvsvdn yfnqytsrag
      721 rystsyfttm sgmklddlrp qkkigtnigl nigflddkfe vdlnfykekt kdlimkgipi
      781 ptsaawntst tlsygnvgem enrgwemsvs ankiitykkf slsasfnmaq ninkllemdq
      841 rvldnlnsqp syskrgsasi lnrvvvgdpl csiygfnskg vfqysydylq nyntkqqqlq
      901 tqaaargesy dwnyeawinq qlaegktfpv atdengkvim tntgvpkrlt yyygdteyef
      961 kggdaiyedv nhdgnineld ikylgnslpk mqggfsltlq ygnwklvsrf nyrwgnkiin
     1021 tarmglesmy gtqnqcssvt yrwrkdgdvt pipralygtg ynyqvssrfv esgsflrlnn
     1081 lqlsysvpks aikkfglnnl sayvtmnnlf cwtkysgidp eigagtyspa sdgattprsk
     1141 sitaslnfgf
//
LOCUS       WP_091818511            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091818511
VERSION     WP_091818511.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123133
     Region          61..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksmiynyiq rqslrlslca ialtacsvay aqddvdaeee stgfkapkrt qvvdnnptcn
       61 vqgivfddat klplagvriq alndkryvam tdddgkffik vptfttalfv qtptylsqqv
      121 sikpgdeqqr vsiyllsdaf atmyadgtti taqnsfvsng nglsideemt aklggdirmn
      181 mhsgnleqga amfirgissl ngnaqplvil dgveldmqqs rsslhlgdif nmlstisped
      241 idkvtvlkna talygargan gviiidtkrg hsmatridak lgvgwtftps ypkmmnaaqy
      301 rnyaveqlgt iaevqnrigs stnplqfnfl ndakdgyyyn tyhndtdwsk yvyrtalthn
      361 ysinvqggdd vgmynlsvay iqtmknikst sfdrinvrfn tdirllwnlt tkfdmsfsrt
      421 ntnlfddgia edlnsgvits paflsliksp llnpyqynkn inaftsllad addlystlke
      481 gnysqanpla lmrngngerk nrnentffnv aiaptyeins dwsvtshfsy ylnrnsqayy
      541 rpnigmpsfa iknlgtvysk tasifskein vlsnthvdwk kkigahtiaa tggfrytyfs
      601 ydnsdlstqy stkgeddknp klatgndvyd tvagvddvwk nmqwyasgdy nyinkyfatv
      661 sllaeansrf gsnanggvkl agvkwaifps vqlgwvlsne dwfpknagin ylrlnagfdm
      721 sgnddisnya artsfnsvrf nyqeigtqlt nvgneeikwe ttskfniglq anflhnrlgf
      781 nanyfihntk dllalksfen pigginnywt ndgelrntgf evgingkpis lkdwhleiga
      841 tvghyknevk alangnytss iygkdnilts vgnpvgvfyg yktkgvfstt adaqaaalyl
      901 vdetgaqqyf qagdvifddl nddhqiderd ktiigdpnpd iygniflnln wkrftlgmtf
      961 nyslgndvyn yqrsilnsgs tlynqqvaei ahwryegqqt slprlnygdp mgnnrfsdrw
     1021 iedgsylrmk svmltyqvpm pdswqswlqg isvwaegrnl ftltkytgsd pefaagnnql
     1081 yqgidcgtia qgrifsmgvk inl
//
LOCUS       WP_091818575             989 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091818575
VERSION     WP_091818575.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..989
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108752
     Region          22..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlrhflpvl llaistsaaa qqklrgqvvd ersqqpviga ivvdrntnna tttdvsgqft
       61 levgkgkkar leitylgynk qtilveeide ellvelreda sqlqevivsg iaskvrrenl
      121 anavttvsak dlvgtvtpqt vdnalygkvp ganirensga pggglsiqlr glsslqgasq
      181 plyiidgvyl nndalrsgrs tltsaggsge ddaanrladi npadieniei lkgpsasaiy
      241 gtranagvii ittkrgqagk akvslsqdlg ftklkkkvga aswdedkiry ffpqsqwdte
      301 ierynanlak nggpidledl lygesgfirn tnitvsggnd ktrffvsgnt sqekgiiknt
      361 dfkrnsirln lehnlnkyvt lslnsnysyt nsnrgfmgne nvggstigyi lgytpnyydp
      421 rpdangnypd npyadqnplq lrdfaqnnvk vdrfieagtl kfqfiktkqt dlrlalqggi
      481 dfltqrstqy fpeflqfqqt kqnpgdllvg titnknlngq afliwdqkaf nldfstqagi
      541 vglqqeqtsi fnrgrglvsn qtalgqstvq sieqhyrqkv qdfsivfqee lnwkdrivtt
      601 lgirfdkstl ngdkdkyyaf prasvalnln nfdfwkvnpq avsllklraa ygqtgglpsf
      661 gvvytsltst vtggllgsiv sssagntsik peragelelg vnigflhnrv ifeatyynkl
      721 vkdliqnltl ssstgistkr vnaadlrnsg ielgltvvav ntrdvnwtnr flfwtnrtkl
      781 trldvpsyts gvygvsfgty lfkegysptt ivgrpqdeng nytifgdsqp dfqtswnssi
      841 sflngfefsf lldwkkggkl mnitqyntda ggtspdwnnd wdndgipdgn gdrvgagsag
      901 vyvqsasylk lrevglrytl pskltneltk gllsriqlgv tgtnlltwsp ykgydpeins
      961 fgttatntns dlfnypatkr flfniqldf
//
LOCUS       WP_091820151            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            kh1p2].
ACCESSION   WP_091820151
VERSION     WP_091820151.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. kh1p2
  ORGANISM  Prevotella sp. kh1p2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Prevotella sp. kh1p2"
                     /db_xref="taxon:1761883"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115369
     Region          46..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mssqkhekrl rkvscafllg lfclnggaak avthvpgtll aqqqerting ivldetgepv
       61 igasikmdgt gvgavsdvdg kfsitikgeg nllvsylgyq sqtiatagks dfrvvlqpgd
      121 nsldevvvta lgikrekkal gyamqevktd gltenknfsv anmlqgkvag vqiaqsgtgl
      181 ggstriimrg lnslsgnnqp lwvvdgmpis dnsvgqadqw ggsdysgaaa einpediesi
      241 silkganaaa lygsraqsga ivittkkgrl nqplrveyng tlsitnaysp ydyqniygqg
      301 nagkydiqsk mswgprmqgq tidnwrsvfy gdtryepyal tpqkdyikdf yetgvaytnt
      361 ltataggdnl mgrfsftdsr andivpnykq nrqyfdlnte frsgfltlga kvnymhekty
      421 nrpgqgeygl mvqlvkmprg irladlrspr gignyiynnv nwsgpsdnya npyaltmsen
      481 gnrmdrnrli gqvsasfrft dylhltgrag vdwfndqikn fntlpdptss asqyvnnslt
      541 nkefnadlil yfdktfgdfs vnanagasvm nrrndglagy sglfatpgvi glangltqtv
      601 seayakkeiq slffsasfgy knfaylditg rndwsstlpk tnrsyfypsv sasvilseal
      661 klpawvtywk vrgswaqvgn dtdpyklael yylwtsgdkl dasgdkvnpa iikeykskvk
      721 aladlkpekt nsaeigteah fldnrlsvdf tyyttsttnq ilsvnmpgss gyisksinag
      781 kikshgvelm lagtpvktqd wqwdvslnwg lnrtrcetld peisrfslgg trvgevvvne
      841 ggkfgdivgn aykrdangni vvdanglpek esdkvignml pnwtgslgtt lrwrdlsfsa
      901 lldirqggkf isntdnyacq qgtsaktvyg rengeqivvk gvtadgqpnt kgvsaenywt
      961 niagpegiae aflysgsyvk mremsvgyil pqawfsrtpi kyvklslvgr dlfylhksap
     1021 vnpegafsrn dyaqafelas mpptrsigfs lnvkf
//
LOCUS       WP_091821643            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            kh1p2].
ACCESSION   WP_091821643
VERSION     WP_091821643.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. kh1p2
  ORGANISM  Prevotella sp. kh1p2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Prevotella sp. kh1p2"
                     /db_xref="taxon:1761883"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122294
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 merrltlila slflcvgmam aqtkvtgtvv sqedgepivg atvtlagtkt atvtdvdgrf
       61 tltvpsgarl tvsyigrvtq tvvarngmkv tlsadnetle evvvtgmmkv dkrlftgast
      121 klnaedakid gmadisrsle graagvsvqn vtgtfgtapk irvrgatsiy gsskplwvvd
      181 gvimedvvdv dadalssgda stlissaiag lnaddiesfq ilkdgsatsi ygaramagvi
      241 vvttkkghsg qahinytgey tmrlvpryge fnimnsqdqm avyqeleqkg ylryaetana
      301 ansgiyghmy qllsaydstt gqfllpntpe akaqylrdae yrntdwfdql fstsimhnhs
      361 vsisggtdkl qtraslsamf dpgwtrqskv qrytanlntt yninqkvsvn lisnasyrkq
      421 rapgtlssti davngqvtrn fdinpysyal ntsraldant yytrnyapfn ilhelnanyl
      481 nlnvtdfraq glltykpitk velnllgavk ysatsqehni lddsnqamay ramatstire
      541 nnsylytdpd nifalpvtvl pyggifertd nsmfgwdfra saayndvfne dhivnlyaal
      601 etnsydrhqt wfrgwgmqys mgeianyaye vfkkskedgn dyytmsntht rsaafaanat
      661 ysykgrytvn gtfryegtng lgmarssrwl ptwnisgawn aheeswfekl rptlthltlk
      721 asysltadrp svtnaqavig sqnpwryitk dsesslyird tanpdltyek khelnlglea
      781 gfldnrinfa fdwykrnnyd ligvadvdgt dgatqkygni asmksdgfel slsttniktk
      841 dfswstnfiy shthneitdl ntstrlidfv sgtgfaregy pvrslfsipf nglngeglpt
      901 flnsdgsttv sgiyfqtsdp eelaflkyeg ptdptstgsl gnlfrykgfs lnvfitysfg
      961 nvvrldpvfk nsyddltstp kefknrwmha gdeaktnvpt iatrrqnwnd sdlsiaynsy
     1021 nystariakg dfirmkeisl gydfprtlvs pigistlslk lqatnlflly adkklngqdp
     1081 effnsggvav pvpkqftltl rlgl
//
LOCUS       WP_091820934            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            kh1p2].
ACCESSION   WP_091820934
VERSION     WP_091820934.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. kh1p2
  ORGANISM  Prevotella sp. kh1p2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Prevotella sp. kh1p2"
                     /db_xref="taxon:1761883"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114958
     Region          31..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvnvlwys mrvcltlmlm lfalqvsaqs itvkgnvkdn tgepvigatv kvlgsttgvi
       61 tdvdgnytie cqgnsklefs yigsktqvve vgnrqtvdvt lteestaide vvvtalgikr
      121 qsrslgystt kvggdefqlv rdpnlgnals gkvagvsvag natgsmgtsr vvirgnssmt
      181 gnnmplyvvd gvpfdnanqg sagqwggadm gdglsnlnad diesiqvlkg aaasalygfr
      241 ggngailitt ksgkknqpts vevnenltfn tiydyrdwqk nfglglegnk ptsvnaaieg
      301 esnswggald gseavnflgn kyaysyvdnw knfyrtgitt ntsasisgss dkvvyrfgas
      361 ynkeksilpn agnrqvglnm nttyqifknl saivtanyvf dksngrsnls dgngntnasl
      421 iyrgnsfdvr wlegtsrgwg tkldggemig gnnvyfnnpy wlqyrktndm drnrltgsvt
      481 lkwditdwly lqgavqrdgy niefkqvqpi gaaadpngwl teyeknfhet nynfllgfsk
      541 qfgdwnvsat fggnklnniy kiyytsnggr pftvdglwsv nnitaagqsp qkvvsrfqvn
      601 slygtfdlgw knqlflnltg rndwfstlad dsnsyfypsa tlswvftdtf reqlpkwfdf
      661 gkvrlgyafa sngteayqnl lryklrnytv ngqqtatqnn ddrfpnpalk pvhisefevg
      721 lnlsflnsrl nfdlayyvkn tkddivyvst ssasgfgssv enigelrnsg fefmvdaypv
      781 rnqdfswntt lnfaynnsev knlgagtkri svvggqsrng nvgiyqvvge pyaeiigary
      841 krneagqlll kkglpqagdq evlgnavykw tsgwkntfty knfmlsfmld akfgaklfsg
      901 tnyqlyyygm hkntlegrta qnpagsivav gideatkqan ttavsaqsyy raicdaniae
      961 efvysadfik lrelslgytf pkamleplkv vkglsvsvva rnlwtimkht pnidpesain
     1021 atnaqgleln gypatrnigf nvnvkf
//
LOCUS       WP_091821900            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            kh1p2].
ACCESSION   WP_091821900
VERSION     WP_091821900.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. kh1p2
  ORGANISM  Prevotella sp. kh1p2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Prevotella sp. kh1p2"
                     /db_xref="taxon:1761883"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123634
     Region          52..101
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          119..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvhkslkyh llvlllcvcw agagaqnqtv sihmknaslk qvfkaiesqt tyrfsyrsgl
       61 idnrsditln htkasvpsvl nealkgrslk ysivseksiv itdkmetnds rqqssnqris
      121 gkvsdengep iigatvrvkg vsggvvtdvd gkfsidapig stleisyvgy qtkvlsangg
      181 nmdvamnvds qnlneiivvg ygsstrrdli ssvstvktdq isnipvtnia qglagrspgm
      241 iikasgggvn stpnisirgg gtplyvidgv vrseqdfvnl saddiesmsi lkdasatavy
      301 gsratngivq vttkqgkagk vsieydfnqs yaqpsiwpep lnsyeraeyg niarkndgld
      361 evysaeaiqa mrdgsqpqty nntnwrklvl ndwapqtkha arltggsenh hyyaslghiy
      421 qnslyknnnh ymkrtnfrla esslissinl qinaaldgyv qinthpysst assyyhifsh
      481 indksplspg vnlyglpynl ndnpvaetas gngynrnkmn vingkgeliw gvpwvqglkv
      541 rvasdyryys stskqwrkds pkydwdstep lvgnkpllyh ssstgyaftn qafveyaref
      601 glhhvsalag feqyyekget ywsqrenyef sidqmgvgsa ntmkndgsea elgraawigq
      661 akynyankyy aeaslrydgs dyfapgkrwg affsgsigwv vteekfmkpl vernilnslk
      721 frasygetgl dssagrfayl tayslnpqay vvngeyaagf tegnlaspdl twyttkqtdf
      781 gfdfsslnnr lygqfdyfyy stkgylvsps gqsylntalg vampkvksrs efrragfeiq
      841 lgwrsnigal kydistnftf fdqlwaldes esetsymnpy vrsqqqkgyy gtmlhnlgyy
      901 tsvedvynsv givsaynsgy mtagdikyed angdgritsd dmrrlgknsy prgqfgvnin
      961 lsykgfslga lfqgstafdm yisgsasmqt gqagslpviy dyqtdywtps ntngqyprlm
     1021 sntglnannn yqtsdfwlvn gaylrmkdfq lsydlkysll krvawlskir vgvsgqnift
     1081 iskstkygld pensstvgyg ypvertiaft lnlgf
//
LOCUS       WP_091822133            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            kh1p2].
ACCESSION   WP_091822133
VERSION     WP_091822133.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. kh1p2
  ORGANISM  Prevotella sp. kh1p2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Prevotella sp. kh1p2"
                     /db_xref="taxon:1761883"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122615
     Region          24..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekklivfla clflcigeal aqskisgtvv fqddgspvlg atvkagsgka vaitdadgkf
       61 tidaaggtrl vvsyvgmetq tvtarsgmvi klqsnttlne vvvtgmqhid rrlftgasts
      121 inageakldg vadisrsleg raagvsvqnv tgtfgtapki rvrgatsiyg dskplwvvdg
      181 vimedvtevg adelssgdav tlissaiagl naddiesfqi lkdgsatsiy garamagviv
      241 vttkkgragh skisytgeyt mrlipsysnf nimnsqeqmg vyremrdkgw lnfaesyras
      301 esgvygkmyq lmntydpvsg tfamenttda enaylqqaef rntnwfdqlf sngiqhnhsv
      361 smsggtdkln fytslsvmvd pgwykasdvk rytgnlnaty nisdklsfni itsasyrrqk
      421 apgtlsqsvd pvygevkrdf dinpysysln tsrtldanty ytrnyapfni laelennyid
      481 ldvvdlkfqg elkykpikgl efsllgaaky attgqahhim ddsnqamayr amadatirna
      541 npylytdpdd pyalpvsilp nggiyqktsy kmnsydvrgt vnwnhtfaqd hivnlfggfe
      601 vsdisrnkdf fngwgmqytr gelpfyvyqf fkksietnsd yyslsntytr tsaffanaty
      661 sykgrytlng tyryegtnrl gkarsarwlp twnvsgawna heepwfdatf knvlshltlk
      721 asysltgdpg psnvtnssvv lrsykpyrpf tniqesgldf tdlankdlty ekkhefniga
      781 dmgfvnnrin ltvdwykrnn ydligpikta gaggqiqkla nvatmeshgv efslntkniq
      841 tqnfswtsdf ifsyaknkvt elestaqivd vvsgtgfale gypvrglfsy kfeglsdkgm
      901 plileedggq ttnggeidfq srklenlvye gptdptttgs fgnifsyknf klnvfitysf
      961 gnvvrlasaf keeysdldam pkefknrwvq agdeavtnip viltdrqvtv drelktlyna
     1021 ynystariak gdfirmkeis lsyqfpkpwl tplkisdlsl klqatnlfli yadkklngqd
     1081 peffrsggvs apmpkqftlt lrvgi
//
LOCUS       WP_091823658             901 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            kh1p2].
ACCESSION   WP_091823658
VERSION     WP_091823658.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. kh1p2
  ORGANISM  Prevotella sp. kh1p2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Prevotella sp. kh1p2"
                     /db_xref="taxon:1761883"
     Protein         1..901
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98445
     Region          46..900
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkwqntllp alllvsigtq aqtqkprqsi lltdsittql lterasgsaa vvteermnkg
       61 lvtnslsals gqaagvnisn genrmamlss vrvrgttslt ggndplviid gvysdlatls
      121 tiypadiesf tilknaseta qygsrgasgv ievktkqghg gqfhiaydgn agfesvykni
      181 emldaatyia takalgqdyn dggsatdfrk aitrtgfvqn hhiafsggse ksnyraslgl
      241 mdhntvvdkk ryqnfaakld itqlafddkl kvdfgvfgss qksddifdaq glfysaatqn
      301 ptfgaderrk ngtasqinpp rtlllerndt rnqnfnthlr ltlsllqdlk limtgaysfn
      361 stenaqfcpt wvwaqgqayr gehksedwlg nvslnwqhtw gshrieatlm geyqqnkrsg
      421 fwtlvkgftt ndfgynnlga asirpfggtg snyeapalas vmgsasytll gryslaltlr
      481 adgssmvgrn htwgtfpsvs gywdirqepf mrqakavsll klrmgygssg nlggissynt
      541 lntvmpvglv sqggaptvtm gtlrnmnpdl rwetrstfni gadlglfrnr vlltaeyyys
      601 kttnmlyqyd vpvptfaydk llanigsmqn sglevgiglt piskkdmeln lnvnlswqkn
      661 kllslsgqyn gyhmsaaait sigqlngagf hggnssilyq ivgqplgvfy lphctgivdn
      721 ghghnkyeia dldengvidl sdngdryiag qatpkmtlgs nisfrykafd islqmngafg
      781 hkiyngttls ylnmssfpdy nvmkgapern ivdqnvtdyw lesgsylnld yltlgwnvpv
      841 rskyisalrl scsinnlati tgysgltpmi nsyivnstlg iddkrsypiy rtysvgvsis
      901 f
//
LOCUS       WP_091825305            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            kh1p2].
ACCESSION   WP_091825305
VERSION     WP_091825305.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. kh1p2
  ORGANISM  Prevotella sp. kh1p2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Prevotella sp. kh1p2"
                     /db_xref="taxon:1761883"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123191
     Region          38..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqatlntdp atgratakrl fvtgvltlmi alpavaqktv tgtvtdeqge plygvsivmk
       61 gtargvtsda kgqfslkvdd estilvfryl gmepqqasvr grtrlevklr essstlsevt
      121 vvstgyqrls rerstaafgf vdstrlnnqn frnletaleg qvaglrvntv ndgtsqqpii
      181 rgvgtlsadv gtqplividn mptgmsltdi npyivesitv lkdaaaasiy garaangviv
      241 vttksarneg vhvsvnadwf ltskqnfdal hlqsasqmid fqtqlfdsyv adagsidayf
      301 dnrgaayyqp lyqlyrdrhd gkltqaevda qlagwrkndy yaqyrdhlwr tavnqrynvr
      361 lsqragksnh sltfsysnsk gqdkadfgtn afavylhsny klakwlsvda gidvnlaqgr
      421 qgtsygynsq erylqlidae grsvtypnas fggyagqgtn lnaiaavahp dlympfsfna
      481 idqlhesmtk tksvslrpfv sidaqflrff rytlsyqyew nqnktelfde qnsyamrmth
      541 ngmitadgks llptggryrq telgsnnytl rnqlgfdrtw lhhavnaivg mefrqnhrpr
      601 iieqlmygyn pqtltsvnmd watlhdtgwe selygrnmtl ggpatrqqit rhryaslyan
      661 agytfmqkyn ltasirwdea dlfgldtneq khplwslgag wllseekfmk tvrwidylrl
      721 ratygingnv dqasatyfva tyktqrnpvt styldygddd lpnprlrwek tattnvgvdf
      781 rvldnvlsgs leyynrrasd llvkryldpt lgaenrvvnn gamrnrgvel tlnaniyrnr
      841 dwkvaaslty srnsnrilev dvnqnataad firapqnnfi kgtayntlwa yrlgrvengy
      901 pvilddegnd mvtfgadgdv asiryssslk gtaalkncgt itpkynggvg lqvgwrdiel
      961 namfifaggn klrmptpsls qggdntresl tswngtsgvr lyhdmsvtar qyasafdeww
     1021 qysdarvksa afmklrnvsi syhlprplcr kagmsgialr lqasnllsws aagddidpet
     1081 fglnggsrsm krprtfsigl sanf
//
LOCUS       WP_091826148            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            kh1p2].
ACCESSION   WP_091826148
VERSION     WP_091826148.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. kh1p2
  ORGANISM  Prevotella sp. kh1p2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Prevotella sp. kh1p2"
                     /db_xref="taxon:1761883"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119066
     Region          54..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdenhkkknt aprtlwaaav lsalvlgsgt asanvasagr tlhaeslqqq qnritgsvrd
       61 angepvvgas vvikgsskgf vtdmngnfsi dapvgsviei syigfetqev kignsrtynv
      121 tlredartvn evvvtamgir kdkkalgyai tdlkadelmk nkqtnilnsl agkiagvtit
      181 qgggaagggs eiilrggtsl erdnqplfvi dgiiydnstt vpgnsafdgt vsaastnanr
      241 vmdvnpedia disvlkgpaa aalygsrasa gaviittkkg qsgrvelnfs sklttshvwq
      301 lpdvqqtykr gysqdvfdaa gnylrtdydn rsydswgeka eageptydni gnffksglat
      361 dnnvsisggn dkgnfflsgs yydqsgiiph tgydkatfrf ngeqkwkmlt fganvaysva
      421 htdktltsaa lygsagsgtm tsvyrwsafd dmthymnedg sryrlpgvsd aleywderdn
      481 pywivnknki kdstqrltgg iqvraditpw wwvsyrlgid ehetnnykri arggvvksdw
      541 qkgmysendy kyryfsnnim tnlshsigdf ngnlllgfts edtktvsnyr mawnlivpdf
      601 ysfdnsnstd rnfknvksqh rllglygear ldwksiafft ysarndwsst lpkanrsyfy
      661 qsfngalvft elmpkndilt fgkvraswar vgkdaspyst ntslwpigtf iggktgmgns
      721 wtagnaflkp eitestelgl elrffqnrlr ldyayytnns ynqimsprls nyigyilrdv
      781 nagdvynkgm elsisgtpvm tkdfqwetgi nlsgnrgtvk nlmdgvdily vtdvqignvr
      841 aasfndghfm aisgsqwsra edgqvildkn gmpsydgsdk hevgnreakv rggwnntfty
      901 knlslnmlwd fsfggdvfng tqyamtvagm sklsenresi tidglqqqgd syvpasytfe
      961 rgktydyngk ptsgdaiieg yyqtyypres rnfitkvnyf rlrslnlvyn lpaawlqktg
     1021 fikaasvnfa annlllftny dgdpevsyag sgsigsssvg mdyccvpatq sftfginitf
//
LOCUS       WP_091836414             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Allobosea
            lupini].
ACCESSION   WP_091836414
VERSION     WP_091836414.1
KEYWORDS    RefSeq.
SOURCE      Allobosea lupini
  ORGANISM  Allobosea lupini
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Allobosea lupini"
                     /db_xref="taxon:1036779"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55582
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspkelf agearvamtp dsaqqlqklg ydclietgag laagftdday raagvtvves
       61 aaalwdeadi iakvrppeta eaerlkagkt lisffypaqn kellefckgk danviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfkg qqqdgaatgg yaapsspefr
      241 eaqlkkfrel apqidivitt alipgrdapv lwtadmveam kpgsvivdla aerggncelt
      301 kpdekivtpn gvtivgytdf psrmaaqsst lyatnirhmm tdltpakdgk pvhnmeddvi
      361 rgatvtfega itfpppppkv aaiaaqkpke kakeltpeek rakeaaafka qtqsqlmllg
      421 vgtvlmlivg ayapvsfmsh fivfalacfv gfqviwnvsh slhtplmavt naisgiivlg
      481 allqigsssw lvtflamisv liasinivgg flvtrrmlam fqks
//
LOCUS       WP_091843512            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            ne3005].
ACCESSION   WP_091843512
VERSION     WP_091843512.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. ne3005
  ORGANISM  Prevotella sp. ne3005
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Prevotella sp. ne3005"
                     /db_xref="taxon:1761887"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114040
     Region          22..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlvlyifc lvttlsasaq dvlkgrvlde rteepiigaa iqikgtrnaa vtdingqfsi
       61 tlagkspytl vvtytgynqq dlevydassa vdiyirensr llnevvvvgy gvaksrdvis
      121 sissiskekl egvtghsidn llegkaagvm istagsqvgs apvinirgva sitssvtply
      181 vvdgvpints diasntdynp vadinpadik sidilkdaaa samygsraaa gvvlittnsg
      241 yagktkltyd fnlgfnsatk llepltaqef tdiknrgwln nggdpnklpy atmtdsqgri
      301 vstnwvdlif htgisqnhnl nvqggndkgt yylsgsyttq egitvdakyd rfsfkgngty
      361 slnkyvkvgf nsgytyskih taddsrggsl samggltrla yvdlpnvpay nedgsiyrst
      421 iapqnlgkgn naievfyyna mglidggqya eskthrvlan gyvditpikg ltlkslygid
      481 wtlvqnesfs tplhgggypd grsntgtssl rswtwtntad ytfdikkhhf dilvgvease
      541 nkrntvsrtg ttlsnpdqmy veapyitysg sgniqessmf syisrltydw nsryyltanw
      601 rrdglsklgr kwgnfyglsg awrisderff rslredgifd dlklklsygi vgnanvdwya
      661 sksvysasty ngdvsyvssg indpdlgweq tattdigfsa slfkgrltvd vdyfyskskd
      721 lilnasqays tgivgasist nlgktrntgi elsvggdiir kkkfswnstl nisfvsnkvl
      781 eladdiisgs nittegysla qlytyptdgi dpqtgrrvvl ikradggydr qlliykygqg
      841 gaqiyemdge tkskytlsdw kpeisgntkp tyyggwsnti hyknwdvnln fhfsggnkil
      901 nsmratlsdg rmwsgckewy dniwqqpgdh akyakasynd nysngtanpi sdliengdfi
      961 rlqslaisyn fktrrwpkal gitsfrlyaq aqnlfcitgy sgfdpeinsy yndanlrsgi
     1021 dsnttpltrt isfganisf
//
LOCUS       WP_091843884             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            ne3005].
ACCESSION   WP_091843884
VERSION     WP_091843884.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. ne3005
  ORGANISM  Prevotella sp. ne3005
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Prevotella sp. ne3005"
                     /db_xref="taxon:1761887"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107643
     Region          26..974
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlmksvvm vltimlfald vsaqttisgh vkddtgedvi gasvvvkgtq ngtvtdfdgr
       61 fqlkcesgvt lvisyigftp qevkaahnme itlkedvaql nevvvvgygs lakkeisssv
      121 vqvnkdqfnq gaasdamali agkvtglnvs ataeanpnam tdiqvrgags ltasngpliv
      181 idgiaggdlr niatqdvesi tvlkdagsaa iygtrgangv ilvttkkgsg tagvtnvtyd
      241 syialnvakp hpeilstdef rrsrrgqdyg adtdwwdeit rpvsyslnqy isidsstkng
      301 yfglsanykk gngldivsgr eeygarfvge qrvlnnrlqf naslsgrkvh edwgnnglfd
      361 taltmnptip vknpdgsyyq pnsptdihnp vndlkenisq gdriyllgna dvklnilqte
      421 qhnlntslsy alqyndqksn fytpstsses fwngyagran vnyqkwwtnr lewlvnytlt
      481 lnqhqlkavl gyswerskwe qsgnenkdfv ydsmgwygig ngtalqegka nlwggssest
      541 ligffgrlny nyndmlfasa slrregstkf gantkwgsfp saslaweitq tpfaegvkti
      601 fqslkprvsy gvtgrsdfda yrslstyssy gaylidgewi ngyapslnan pdlaweksta
      661 fnvgldfvaa nsrlrgsvey fdrrsqdlly nytapqppfi ystilvnvgt tkntgievsl
      721 dydvlakkdl kwttginwsm getkltklss dvyqmayldl yqkpgpgsse yffrveeggk
      781 igqfygyeha gidengllli ydnegnkvna sqadpsykrn idngapkhfl swnnsfrykn
      841 wdlsmlfrsa lgyqifnmrk ygmglqgagt dnvlrtaytk ygnvmssggi issyflengd
      901 yvkldnvtlg ynftpkkrel ieslrvylta knlftltgye gndpsivtst gitpgidtns
      961 aypqatqlsl gvtlrfh
//
LOCUS       WP_091846176             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Palleronia
            pelagia].
ACCESSION   WP_091846176
VERSION     WP_091846176.1
KEYWORDS    RefSeq.
SOURCE      Palleronia pelagia
  ORGANISM  Palleronia pelagia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Palleronia.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Palleronia pelagia"
                     /db_xref="taxon:387096"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55750
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgvitehq psearvalsp asaeqlqklg hecviqsgag akadfadevy rdagvevlds
       61 akavfdaadv vakvrppsee evemlregqt lisffypaen eelmkkaaak gatliamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfltgqvt aagkvppaki lvvgagvagl
      181 aalgtatslg aivrafdvrp etaeqiesmg aeflfldfed tegvgeggya apsspefrek
      241 qlalfreqap eidivittal ipnreapelw tedmvkamkp gsvivdlaae kggnckmtvk
      301 dekivtdngv tiigytdfps rmakqsstly atnvrhmmad ltpekdgqiv hdmddqvird
      361 stithkgevt wpppkrenps pakpkqekkk eptkeekaaa etaafrkqtq qqvgllavgt
      421 vlvlllgtia pasfmqhfiv falscfvgfq viwgvahslh tplmavtnai ssiiilgala
      481 qigsssilvt ilaalavfma ginifggflv trrmlamfqk s
//
LOCUS       WP_091849046             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter segnicrescens].
ACCESSION   WP_091849046
VERSION     WP_091849046.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter segnicrescens
  ORGANISM  Marinobacter segnicrescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter segnicrescens"
                     /db_xref="taxon:430453"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55780
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigiprevy pderrvaatp psvqkliklg yevvveagag eaadysdesy qnagaaiavd
       61 tlslwkesdf ilkvrapteh pgthkheldm iregahlagy iwpaqnpqll etlaekqvna
      121 faidalpris raqkmdalsa maniagyrav ieaanqfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig tansmgavvr afdtrlevke qvesmgaefl eldfggeegs ggggyakqms
      241 defikaemal faeqakevdi iittalipgk papklitaem vqsmkpgsvi vdlaserggn
      301 celtepgkvv erhgvrligy tdlpsrmakv asdlyatnlv hlmteltpek dgqpvvnmed
      361 avirgvtvvh qgdvtwpppq peaptstapp pgteepspat ttatkgpspa krltgkiall
      421 avtalalygv gayapesflr hftvfvlacf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gallhlaqae haavgilsfv avliaminvs ggfrvthrml kmfhr
//
LOCUS       WP_091853098             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Aquiluna sp. UB-MaderosW2red].
ACCESSION   WP_091853098
VERSION     WP_091853098.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Aquiluna sp. UB-MaderosW2red
  ORGANISM  Candidatus Aquiluna sp. UB-MaderosW2red
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Luna cluster; Luna-1 subcluster; Aquiluna.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Candidatus Aquiluna sp. UB-MaderosW2red"
                     /db_xref="taxon:1855377"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52883
     Region          4..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msvigivaea pgearvaatp etvkkiitlg yevqvekgag irasfpdaay vaagakivtk
       61 akvwncdvll kvdapslaev kymragvtlv gmlspafkpa llkalakqgv talamdavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqitaa gkvppakvli agagvaglaa
      181 igsasslgai vratdprpev aeqvksiggs ylpveideqm qtgdgyakat seaynkraae
      241 iyteqamdvd iiittalipg rpapklitak dvalmksgsv ivdmaaaqgg nvegsvagkk
      301 ivtkngvtil gytdlpsrlp aqssqlygtn lfnllklltp gsagkleldl ddvvqravtv
      361 vnagkvtwpp ppiqvsaaat avaekpvvae kkkmsastks vliglgivll aavisfappi
      421 lqqhflvltl stvvgfyvig kvhhalhtpl msvtnaisgi vvlaailqik dpslliqila
      481 aigvllasin vfggfavtrr mlnmfskget r
//
LOCUS       WP_091851202            1093 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091851202
VERSION     WP_091851202.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1093
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123933
     Region          22..1090
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlyllfisf vilfagevka qrmvtgtvsd tkgeplygvt iavkngkhta vtgldgkyri
       61 pvdnenavll frymgmepyq ttvkgqvtvd vkmkdqttql aeavvvstgy qrlsrersta
      121 afgfvdstkl nrvmhkdils alegqvaglr mdinpntgeg spvlrgvgtf stsigtkpli
      181 vvddmatdme lseinlydve svtvlkdaaa asiygalaan gvivittkqg ksekttvsvn
      241 adwyistkpt fdamhyasts diidyetnvy narvnssgsv atlfnsfskn yysplyqlyr
      301 dqaegritqd dvdrtlgqwr qndyynqyrd lvwrsavtqr ynvslsqksq rsnhfasfny
      361 ehdknrvknd nsdafsiylk snfklnkwls iklgidtrfs nsqvpdyayt nyniqeryas
      421 ivdaqgnlvm tpyvnisgfa ggslngsvia dsqqqlassd vlmpfsfnvl qsldesltqn
      481 rnlrmrpfvn veakflkwfk ynlmfqyewt qsrtekydep nsylmrmthn alidldgvsq
      541 lpsggryrqt tnntrrytfr nqlnfeksfl eskhhvnaim gfelrenras rpieqqmygy
      601 ndvaltsvrm dwaslnnvgv eslvygntvk lggpassqte ifhryasfya nvgydylyry
      661 nitgsirwde adlfgldtkn qhhplwsvga gwniseeafm kdfswldflk lrltygvngn
      721 vdqssttyfv aryrtenndp tntqylrytd dnlpnsrlrw ektstfnagv dfrvlnnvls
      781 gslefynrvg ddllvrkyld stlgatqrvi nngkmrnqgv elqlnanllr tkdwtlsagf
      841 niawnhnkml rvehsstdia snfitapany fvegtsyntl wayrlsrvvn gypvildadg
      901 nematfdadg nptevqvsst lkgtdalvnm gslvpvyngs ltlslrwrel elntllvyag
      961 gnklrldatd mnsyqmvtdh vndhtvkhyy emptgsvaqq yastfsewwr ycdaqvkpad
     1021 yikmrsisma yhlpeavtkk lhigqtrltl qvnnlfywsr vghdidpesy slnsasrtll
     1081 qpktfsigfs tsf
//
LOCUS       WP_091853259            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091853259
VERSION     WP_091853259.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123837
     Region          24..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrltvflt alllsigvaf aqnkitgtvm qddgepaiga tvkvvgnnng vvtnvdgkft
       61 idvpsgkkle fsyigyvtkr lapkngmkvt mtqdskviee vvvtgmqkqd krlftgaatk
      121 idaekakidg vadisrsleg rvagvsvqnv sgtfgtapki rvrgatsiyg askplwvvdg
      181 vvmedvtevd adalssgdan tlissaiagl naddiesfqv lkdgsatsiy garamggviv
      241 vttkkgkagq shisytgeft mrlkpsysqf nimnsqeqms tyremynagw ltfsdtyrgs
      301 esgvygkmyq lmntydpatg qfllpntdea myaylqeaef rntnwfdelf stsisqnhsi
      361 smssgtdkaq yytsfsvmnd pgwterskvq rytaninaly nlskklslnl ignaayrkqe
      421 apgttnqsad pvsgqvtrdf dinpysyain tsraldpntf ytrnyapfni hnelannymd
      481 ldvvnlkfqa elkykpirql elaalgayny svatrthmik ensnqsmafr amddatmrdn
      541 npflyqdpdv pnslkysvlp eggfyrtykn vmnsknfrat asyndafgqe eehivnvfgg
      601 mevndierna nyfngvgmqy emgmlgaydy hffkqaseen nmyyevsnny ernvaffgta
      661 tyswkhryti tptvryegsn qlgrslkarw lptwnisgaw naheeswfad tfknilnhat
      721 lrlsysltgd kpavnnamvi iesvnpwrpf asdketaldi qqfgnpdlty ekkhefnvgv
      781 dlgllnnrin vtfdwwmrnn fdligprmtt gvggaitkya nvatmkshge elsistkniv
      841 agdfkwntdf ifshnktevt dldsrspiyy ltgqyqrngf tmvgypyral wsidfqglde
      901 hglptfinqd dnlttsdhdf qsyvldhlvy egptdptitg slgntftykn lhlnvfasys
      961 fgnvvrldpv frssysdlda mpkefndrwv vggdelktni pvladrrmnq adpylsyayn
     1021 aynystaria kgdfirmkei slsydvpasw inplginsln lklqgtnlfl iysdsklngq
     1081 dpeffntggv avpmarqftf tlragl
//
LOCUS       WP_091853986            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091853986
VERSION     WP_091853986.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123891
     Region          48..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkryilfgmt llmafplcav aqdedteeee evvqvkrvvr vqkhyetrtv kgyvfdaasq
       61 kpvsgaivra adidgysvlt dddgsyslkl plfstslyis spdhnpvkig lskdeaqksv
      121 nlypsaftae ygvqtnvrgd yeatdfkysp ainikdevqk qlggqvytin rsgtpgigsv
      181 mfmqglnsln vnaqplivid dviidqqygr tllhdgfynd vlnninpadi ekvtvirngt
      241 alygskgang viliqtrrnk smatritani sagvtmepny isvmnadqyr syasemlkst
      301 nttlrdfkfl kseydargnk yyyydqyhqn tdwkdyvyrt amtqnyginv eggddvanyn
      361 lsvgytnaks tmkyndmdrl nvrfntdisl snklsvrfda sfanqtrdir ndgapegyde
      421 gtpiapsfla yvkspfmsay syghdetgag rfskehydid tesylseala nynnynwqlg
      481 npaainqyae antknrfets mlnltvtpkl eiardlfvse hfsynlvntn emfyipingt
      541 psyyvsslgg yrqnetrsla skqnsvmsdt ridwkkrfda hflhifggar inwesftsts
      601 qvgyntgsdk tpflsgslqd kdvvgisenw nslswyaqae ynykgryyaq anltidgssr
      661 fgqeggdfrl fkaawgvfps fqagwvvtne pwmadvkgid ylklsagydi sgnddidyya
      721 arsyfrasqf lhtisgiafe gigntkiqwe ttrrlnlgle gsffdnrlsl gfnyfrsktd
      781 nlltlqqlgy lsglkenwsn ggklknegfd vsftakvlnl knwqwqigas aghyknqite
      841 lpdgkqfidn eiygatvrtq vggvanafyg yktlgvfstt aeaqaasaaa agaatydpng
      901 lyfvgengvd hvyfeagdmh fadlnndgmi teadrtfigd pnpdiygnif tslsfkrfkl
      961 dvnfnyslgn diynymrsql eggsrfmnqt tamlrrwqve gqqtdiprit fqdpmanarf
     1021 sdrwiedgsy lrlksvtlsy dlpvkseylq gfqfwiqgnn lltftkylgs dpemtatssv
     1081 igqgfdlgrl gqsrsivagv kinl
//
LOCUS       WP_091853984            1133 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091853984
VERSION     WP_091853984.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1133)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1133)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1133)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1133
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126685
     Region          27..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkilksvimt ialllsttls aqnitsvhgt lsddmgplmg atvceidatg riiesaltdl
       61 ngnftmkvrn tkdkirfsyv gletvtmpin kttyvlkmks ktklkevtvt skrrmqgntl
      121 pipqreisya tqtismkefe glgitsvdea lqgriagldi vgnsgnlgsg stmrlrgass
      181 istltdanpl ivvdgnirev nldnfdmaga ndekfaelln inpediasit vlkdaaatav
      241 ygsqggngvi elttkrgvrg apkvtyslkl tgtyqpqgya llngddytmm lkeayfnprq
      301 ndnasnkyai peinyvddps iladwrqyra ntdwrdavtq wglrqnhyat itgggekasf
      361 rigagydhet gtiiqqkmnr fstrvnldyn vsqrirvstn fsltyskydd nsddllaial
      421 kkmpnmsiyq idpdtgletd kyynmpqsgt yigsevfknd qrnyvnpvas aylakkqrrv
      481 ydmnpeliln yqllglddeh wqlnwrssvy mnisnhynds fypqelvtkr wedkvntsas
      541 sssksvsfnt kqtltlipaf ankdhsvmmm grfeltsgss ssqstdgygl pstngvivsp
      601 saggiingms sgysqwrsmy ytfsahyayk gryvadftvr adgttkfgpg nrwgyfpsvs
      661 lkwivsdepw mqklkptlsm lairpswgrv gnqpgqnylf tskygsadry ldmaamkpln
      721 irltdlkwql vssynfgidl gfmdgrlnlt iegyqsttsd mlmgsfrips ntgfatvpyh
      781 nngkmrntgw efhintnrmi kagkfsmdmn anfgnnrnei lemdeyilen knskygynng
      841 etlrrvqlhn pfgaiygfky kgvyqynylt iknhvqdmve agatkddiqa wwrewsgsgk
      901 tapvavgadg nlilegnnvp krmmydyrsd ntghdgafpg fnggdaiydd lnhdgqinal
      961 ditylgsslp kltggfgfsf nygqwrlstq ftyrvgnkii nkarlqaeam tgndnqsqav
     1021 nyrwrqegdv tpipramygg nsnyntlisd rfvedgsylr msyaqlnysi nkknltwigl
     1081 nrlsfyasvn npfvltkysg vdpdiafgge dpaidnmqtp rsrsytlgit vdf
//
LOCUS       WP_091854732            1150 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091854732
VERSION     WP_091854732.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1150
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128198
     Region          24..1149
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskskfllti lftfiaqvmm aqsrvisgtv edamgpimma nvverdgnnr iisatqtdmm
       61 gnfsmeiknp knklvvsyvg sktkilpign qktfkikled dktvlgevkv vgrrtnaggl
      121 nidkrevsvs qqtmnmaeve gmaftsadea lqgeiagldi vtnsgnlgag tsmrlrgvst
      181 lsgsaepliv vddkifeyda adfdpenmde ekfssmlavs vddiasitvl kdaaataiwg
      241 sqgangviqi ttkrgargkp kvtlgykftg twmpagydll ngdnytmmlk eefynptqss
      301 satstinein yvpaeswaea nnwnkntdwv saikqfgeqh eanfnisggg qkatfrisas
      361 ynhqtgtvik qkmdrlttrl vldynvsdri rfstnfalty tdnlknytyg sskssgshnn
      421 llamalamap nasiyrydry nnntgeyflm nptvtgmtpd dgnytstqla dvvaignpva
      481 yansswqkeq tysivpdfnl kyellgtgtg qhrltfdgrv yfdiyayskp tympgslsng
      541 sytdtnynyl tntetnqfkm gsrvtltytp afknedfylt mfaryeagtq kntyqyiaqs
      601 sipngmesat idarlndmnn qpsatksawq dfvynahfsy ksrysvgfsl rgdgnskfgp
      661 knpwfyspsv slrynlseep fftplkkyvs mfgirgswgi tgsssvsvdn yfnqytsrag
      721 rygtsyfttm sgmklddlrp qkkigtnigl nigflddkfe vdlnfykekt kdlimkgipi
      781 ptsaawntst tlsygnvgem enrgwemsvs ankiikykkf slsasfnmaq ninkllemdq
      841 rvldnlnsqp syskrgsasi lnrvvvgdpl csiygfnskg vfqysydylq nyntkqqqlq
      901 tqaaargesy dwnyeawinq qlaegktfpv atdengkvim tntgvpkrlt yyygdteyef
      961 kggdaiyedv nhdgnineld ikylgnslpk mqggfsltlq ygnwklvsrf nyrwgnkiin
     1021 tarmglesmy gtqnqcssvt yrwrkdgdvt pipralygtg ynyqvssrfv esgsflrlnn
     1081 lqlsysvpks aikkfglnnl sayvtmnnlf cwtkysgidp eigagtyspa sdgattprsk
     1141 sitaslnfgf
//
LOCUS       WP_091854651             989 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091854651
VERSION     WP_091854651.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..989
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108786
     Region          22..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlrhflpvl llaistsaaa qqklrgqvvd ersqqpviga ivvdrntnna tttdvsgqft
       61 levgkgkkar leitylgynk qtilveeide ellvelreda sqlqevivsg iaskvrrenl
      121 anavttvsak dlvgtvtpqt vdnalygkvp ganirensga pggglsiqlr glsslqgasq
      181 plyiidgvyl nndalrsgrs tltsaggsge ddaanrladi npadieniei lkgpsasaiy
      241 gtranagvii ittkrgqagk akvslsqdfg ftklkkkvga aswdedkiry ffpesqwdte
      301 ierynanlak nggpidledl lygesgfirn tnitvsggnd ktrffvsgnt sqekgiiknt
      361 dfkrnsirln lehnlnkyvt lslnsnysyt nsnrgfmgne nvggstigyi lgytpnyydp
      421 rpdangnypd npyadqnplq lrdfaqnnvk vdrfieagtl kfqfiktkqt dlrlalqggi
      481 dfltqrstqy fpeflqfqqt kqnpgdllvg titnknlngq afliwdqkaf nldfstqagi
      541 vglqqeqtsi fnrgrglvsn qtalgqstvq sieqhyrqkv qdfsivfqee lnwkdrivtt
      601 lgirfdkstl ngdkdkyyaf prasvalnln nfdfwkvnpq avsllklraa ygqtgglpsf
      661 gvvytsltst vtggllgsiv sssagntsik peragelelg vnigflhnrv ifeatyynkl
      721 vkdliqnltl ssstgistkr vnaadlrnsg ielgltvvav ntrnvnwtnr flfwtnrtkl
      781 trldvpsyts gvygvsfgty lfkegysptt ivgrpqdeng nytifgdsqp dfqtswnssi
      841 sflngfefsf lldwkkggkl mnitqyntda ggtspdwnnd wdndgipdgn gdrvgagsag
      901 vyvqsasylk lrevglrytl pskltneltk gllsriqlgv tgtnlltwsp ykgydpeins
      961 fgttatntns dlfnypatkr flfniqldf
//
LOCUS       WP_091854759            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            communis].
ACCESSION   WP_091854759
VERSION     WP_091854759.1
KEYWORDS    RefSeq.
SOURCE      Prevotella communis
  ORGANISM  Prevotella communis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Prevotella communis"
                     /db_xref="taxon:2913614"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123025
     Region          61..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksmiynyiq rqslrlslca ialtacsvay aqddvdaeee stgfkapkrt qvvdnnptcn
       61 vqgivfddat klplagvriq alndkryvam tdddgkffik vptfttalfv qtptylsqqv
      121 sikpgdeqqr vsiyllsdaf atmyadgtti taqnsfvsng nglsideemt aklggdirmn
      181 mhsgnleqga amfirgigsl ngnaqplvil dgveldmqqs rsslhlgdvf nmlstisped
      241 idkvtvlkna talygargan gviiidtkrg hsmatridak lgvgwtftps ypkmmnaaqy
      301 rnyaveqlgt iaevqnrigs stnplqfnfl ndakdgyyyn tyhndtdwsk yvyrtalthn
      361 ysinvqggdd vgmynlsvay iqtmknikst sfdrinvrfn tdirllwnlt tkfdmsfsrt
      421 ntnlfddgia edlnsgvits paflsliksp llnpyqynkn inaftsllad addlystlke
      481 gnysqanpla lmrngngerk nrnentffnv aiaptyeins dwsvtshfsy ylnrnsqayy
      541 rpnigmpsfa iknlgtvysk tasifskein vlsnthvdwk kkigahtiaa tggfrytyfs
      601 ydnsdlstqy stkgeddknp klatgndvyd tvagvddvwk nmqwyasgdy nymnkyfatv
      661 sllaeansrf gsnanggvkl agvkwaifps vqlgwvlsne dwfpknagin ylrlnagfdm
      721 sgnddisnya artsfnsvrf nyqeigtqlt nvgneeikwe ttskfniglq anflhnrlgf
      781 nanyfihntk dllalksfen pigginnywt ndgelrntgf evgingkpis lkdwhleiga
      841 tvghyknevk alangnytss iygtdnilts vgnpvgvfyg yktkgvfstt adaqaaalyl
      901 vdetgaqqyf qagdvifddl nddhqidetd ktiigdpnpd iygniflnln wkrftlgmtf
      961 nyslgndvyn yqrsilnsgs tlynqqvaei ahwryegqqt slprlnygdp mgnnrfsdrw
     1021 iedgsylrmk svmltyqvpm pdswqswlqg isvwaegrnl ftltkytgsd pefaagnnql
     1081 yqgidcgtia qgrifsmgvk inl
//
LOCUS       WP_091857019             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Allobosea
            robiniae].
ACCESSION   WP_091857019
VERSION     WP_091857019.1
KEYWORDS    RefSeq.
SOURCE      Allobosea robiniae
  ORGANISM  Allobosea robiniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Allobosea robiniae"
                     /db_xref="taxon:1036780"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39068
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaetq gaetrvaatp etvrkfkglg aevvvetgag kasgildady eaagatiakt
       61 aaealagaai vlkvrrpses eiaglpagal vvatmdpygn eaqvaalaka nvdafamefm
      121 pritraqvmd vlssqanlag yravidgaae ygralpmmmt aagtvpaaki fvmgvgvagl
      181 qaiatarrlg aivtatdvrp atkeqveslg akflavedee fkqaqtaggy akemskeyqa
      241 kqaeltashi akqdivitta lipgrpapkl isaamvesmk pgsvivdlav erggncelan
      301 pgevvttgng vkivghlnvp grlpatsssl yaknlfafve tlidkaekkl avnwddelvk
      361 ataltkdgav ihpnfsaka
//
LOCUS       WP_091858422            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Prevotellaceae].
ACCESSION   WP_091858422
VERSION     WP_091858422.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113943
     Region          40..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 makvynlvet ivgwpqktrv yfalltlifl fsqnteahpl kgkvvdangn pligatirvn
       61 nskegtvada egnfnlqlts nklpvvitin ylgyekqevk visnksnlgt iklhedgysl
      121 ndvvvvgygq qsrkkltgav skvkgdvvse atqdapimal qgtasgvyva qasgvpgggs
      181 tsmvirgant ltgskdplyi vdgvplnsnp enpiaytstg llglpdelsl inpsdiesie
      241 vlkdadatai ygtrgskgvv littkkgreg rvkvnlkmst taqfmskrld flnteeytal
      301 rhkafetdka kgyvtdadlt pakfpdltlw dqhttydwqd ilfgntawgt diqlnvsggn
      361 kntsfmisgg yyssgtvtvg ddkytrwtgr snvqhqsddh rlhldagisl tklkmdadaa
      421 gsgysavvsq pnmppydeng dpywlmensn yssplsilny sgtndatsln asfngsyriw
      481 dqlafklqag ynysssdqkd lyprsyyhpl sttaynqary ysmntstliv epqltfncqi
      541 lggktdfllg ttyqssdthv lylygqkypg diflkdanaa slinyhknps tqtksasffg
      601 ritydwqdry llnatfrrdg ssrfgknhry gnfysiglgw lfsnekfikn nlkwlsygkl
      661 rlslgrtgnd gisdyqymtk yttsqypyeg svgivpsnla nddlhwettd kfdvglelgf
      721 fsdrilltan yyyntskdll trqylpnqtg fsymmtnlda eivnkglele lntqniktkd
      781 frwttqltlt ipsnkltkfa dlensgyynt yeigksvnii rgykylgvdn qtgvpmvqdq
      841 ngdgkinsnd dyitlgsqdp kyyaglqnti kwknltfdfn lyyrnkpiey gylwifyypl
      901 gmsenvtrem asnywttpgv dakypglttt sasdiydayy rymsysdaaf stgsylrlqn
      961 vrlaydfdqk vigrlgisal qlyvqgknlv titnydaydp etsvkavppt qsvvfglnvt
     1021 f
//
LOCUS       WP_091858513            1120 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Prevotellaceae].
ACCESSION   WP_091858513
VERSION     WP_091858513.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1120)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1120)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1120)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..1120
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124230
     Region          18..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmaicllfaa vvnaqnvtvk gsvldtkgdp iigatikveg aqagtvtnyd gdftiscrng
       61 atlnvsyigf apkqvkaetg kvlkivleee attlnevvvt algikkdqkk lgyaissins
      121 deliktgasn fasalygkap gvriqsapgg ntsavsisvr gmssitgntq plivmdgvpi
      181 hngntnnegy wdnqrirsng lvdinpedie nisilkgaaa salygseaan gvvmittkka
      241 akgtgtrvnf sanvswdkia ympdmqtefg pgydnwvlgn dnqealtgmr nvyvdrngns
      301 ittpraayys ygprydgrev tyfdgtkray spiggnqwne vfrtgfnqny nvaitnsser
      361 snirfsynfn dvkpmqfnsa nhkhnfnvng sfditntikl nytatyqkqf iknrpyrisr
      421 ivqnysgmfg sftdvkyire htmtslgyin svyaanggtt ntltpdeqfl yspmgstsli
      481 seyfwnilgk eqledhqrfi gsvnptweii pgltlgaria tdltsdkien knraesahif
      541 ssngqysday alenskyeiv ygdvmlsfdk tfadvhnvqa nfgynarqet yymssvstsq
      601 glsqenwfnl aasvgtknan mnkqdmlrtg mfltasygyd nwayiegtir nektstlkkg
      661 nnsfwypsas asilftelmk dnkpawydyg kirasygivg napeiyranl aysqgnlqhg
      721 dtyiynymst svgnesikpe kkyefeigle skffnnrlgf efsyyhndik dqilqttsay
      781 smgaqsmlmn vgeltnsgae fsiygtpfen kdwrvdlran iavnknkvkk ladgldvlsh
      841 anwdngaatl eshvgepmgd fytytwktde ngnrivgedg lyitdtserh kvgnampdav
      901 ggfaasvsyk nftldmsfdy riggdvinqp wqyymdtgii kdavgardyq sggifyystt
      961 envddkasiv rvdpsqvpny qrgvtkidgh yvwdngviqk gvkedgtpnd iittqfaind
     1021 mqygwgtsat qsyqeaiqkn syvkcreisl syqlpvewtk rfgcsnltvs afarnpfyly
     1081 rtlklfdset tdgtnwiyqa qvggstasar tfgvslrasf
//
LOCUS       WP_091860000            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Prevotellaceae].
ACCESSION   WP_091860000
VERSION     WP_091860000.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115998
     Region          24..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksltmlmv slflcvgtal aqtkvtgtvl sqedgqpiig aavkvdgtst gmltdvngkf
       61 sltlpegkks ltisylgyea ktviakngmr vflksdatal eevvvtamgi krsakalgys
      121 atsldgeeia evrtndimsg lagkvagvqi sttssdpgas nsviirgvss lngsnqplyv
      181 idgvpmtnss vyssdglnng ydfgnganav npddvenmti lkgaaataly gsraangvil
      241 ittksgkkqn gvgveynggl qwesvlrlpq sqndfgmgwy gnktddengs wgpkfdgstl
      301 rygsiydysq kmksyvaikd nmkdffdtgm rynnsvsfsn atdattyyvs lsqihddgii
      361 ptsadsytky tfsangsqkv knvtistaln yayqknsfvs tgqggssmyn aimqtprdis
      421 iaemkdlsdp fntpgyyytp ygitnpywil nnyenkqese rfygklqldy eflnyfkaty
      481 rfgldtqtrh hnqgepnles mfkdtynada stiagatgav tqqttrqrei nqdffvtfdm
      541 pvsdfninav agfngnerss sylyghvenl tiptffdlsn sserpevaqy sqkrrlygiy
      601 gqaelawknm ayltvtarnd wsstlpkenr sffypgvtas flfselfked mkkiinfgkv
      661 raawgktgnd asvymtqsvy aqasssssgw assafpfskt gtnaytagnt lgslnlspem
      721 ttefelglnm gflqnrivvd fsyydrksdk qifslnmdpa sgytamntnl gkignkgiea
      781 litlvpvrtk dfewaitwny tknknkvisl peelggevni ygfsggtgly aiegeemgif
      841 kcyrtktdge ghivvnnkgi plqtddiekv gsmnykyqmg igntfrykgv slgidfdirk
      901 ggllfsrtad isyftgnamq tayndrnpfi ipnsvqsdgn ggyventtpl dptqiynfwn
      961 nggflsdesf lldksyvklr svvlswelpk kwlsgtplqg vkvsffgnnl flwtpssntf
     1021 idpeltsfgn dlsgnfgeys anpssrkfgf nvnvkf
//
LOCUS       WP_091860261             933 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Prevotellaceae].
ACCESSION   WP_091860261
VERSION     WP_091860261.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 933)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..933
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104268
     Region          35..932
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiiknial gaallpvaav aqtekeytds vasqvnvafr tvneadlmgg vstvnmveqa
       61 kkdyttysld gmdalvggyn gqlwnqgeal vlvdgvprda snvlpteieq itflkaasav
      121 vlygsraakg vilittkhgr ndglnvsvrg naslyvpksy pkylgsaaym elynealqnd
      181 gkaavysedd iyhyasnenp yrypninffd sqyikktyqr ydgtaefsgg grlahfyani
      241 glsnvgslmn fgegknnhtt rlnvrgnidl rlndwidgyv nanatfydar ndnsnfwses
      301 atmrptsqyp lvpfipisyv eeadavtlkt iqnsnyiidg kyflggtqsq qtnpfaamya
      361 agynkytsrq mqfdmgmnfd lnslvkglkl ktkfavdyht qyntsinney avyeakwnny
      421 sgqdlitsit kygtdkrtgt qnlsnshdkq lilmqaqldy drsfgdhnln atllahgyqi
      481 sedgkyhrts nanlglqlay nyahtyyadl smaaihsakl aeghreaisp vvslgwrlkn
      541 esflrnvkav ddlkltasyg iinqdldiek yymydyvfta tgtwwgwnev ansmqtsdsq
      601 qgsnynlgfi krkefraglt gslwegalkf danffttstn gllttastiy psyfqtywpv
      661 stflantnyn nqrrtgvdlt lnvhqkfgef dtnfgvsamy ytskntkwde nveydwlkae
      721 gqsieamrgy eclgffkdad dvansakinn ntkpgdlkyk dqngdgiids kdqvvigkwt
      781 apfqmgvhft vkykdftlfa qgsgtfggng lkngkdtwvy gdgkysdvvl nrwtpetast
      841 atyprlttes gdlnfvasdf wkystsafrl nkvqltydlp qsifagdsfv kgvsvyvsgs
      901 nlltiakerk ymelnvgtap qtrmynlgvk vnl
//
LOCUS       WP_091861773             409 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium brachiatum].
ACCESSION   WP_091861773
VERSION     WP_091861773.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium brachiatum
  ORGANISM  Methylobacterium brachiatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Methylobacterium brachiatum"
                     /db_xref="taxon:269660"
     Protein         1..409
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42053
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd saesrvaavp etvkkfkalg aditvqagag lkagildsey eaagaeiags
       61 aadaardadl vlkvrrpage elsllkrgat viaimdpygn eaalkamaea rvsgfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrampmmmt aagtvpaarv fimgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsagyqa
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 pgevvvtdrg vkivghtnvp grlaatassl yarnlyafve tlidketkal ainwddelvk
      361 atnltrdgsv vhasfqsktd gpaseaaavg laksetgkae aapapsgah
//
LOCUS       WP_091865748            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pricia
            antarctica].
ACCESSION   WP_091865748
VERSION     WP_091865748.1
KEYWORDS    RefSeq.
SOURCE      Pricia antarctica
  ORGANISM  Pricia antarctica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pricia.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Pricia antarctica"
                     /db_xref="taxon:641691"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108158
     Region          26..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqtlfkrvf lvlfftlpgv lmaqgtitgn vtasvdglpl pavnvvvkgt tvgtttdfdg
       61 nyeitvndfp vilvfsslgy aekevevtsa takdvilees atgldevvvt glatsvkrsn
      121 sanavasvsa eeltgrtpps tldgalygkf agaivnsnsg apgggisvkl rgatsitgnt
      181 qplyiidgvy idnssipagl nvvseaagqg sdsnqdnpsn riadinpedi anieilkgas
      241 aaaiygsraa agvviittkk gkagetqfkf sqstgftqai nlyglrnyte dkvfdffysp
      301 sddpgedqss rdaanaqval fsqarssgnl vdyekeifge kglisitsfs msggdektrf
      361 fsgithnnen givkgtgyek tslrlnlehr atdflklsls snyiysssnr gfynndntgt
      421 sigvalvsty pwynlfpnad giytdyalga snilqtrdlv tnnekinrai mggtanldiy
      481 kaeksnleli lrggldfyql qtraifpkel qfqkpsnggr ngvsvqgeti nknynlsafl
      541 vhnyftenni nfrtqagltn efferntdli tatglvaset nvdqaantgv dqtrvqqeda
      601 gffvqeevnf qdkliatigl rgdkssnngd anklayypka slavslnefg fwkedsawnq
      661 fklrvaygea gnfpqsgalf tsynsfstdg ilgislrgir gnsnlkserq kelefgtdls
      721 ffggrlglta tyytktvddl illaslepst gytqqfvnag slqnkgiels lnavpiaten
      781 fqwdlgvnff kntseiteln vpayntgafg aglgsyrlee gksatqivgs ypdglrvigd
      841 geadfqigyn nnlsyknlql tflwqwkqgg dninltnlls dlngtsadyd dltldpaget
      901 vngkfrpnan aevfvqdasy lrlreiglyy tldskvlpnv fgdtiesikf glsgsnlini
      961 fdyngydpev snfggstift gvdvtpypss kkymfnvain f
//
LOCUS       WP_091865302            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pricia
            antarctica].
ACCESSION   WP_091865302
VERSION     WP_091865302.1
KEYWORDS    RefSeq.
SOURCE      Pricia antarctica
  ORGANISM  Pricia antarctica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pricia.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Pricia antarctica"
                     /db_xref="taxon:641691"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116240
     Region          22..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntaligllq lcaamafcqt ntytatvvdt enrpipfaav relgtnnytt adveglftit
       61 teatdftisi tsigfkplei sveggnlsst itletsseql eeivvtalgi ererqslvsa
      121 vttvtpeqlt evpmtnlvns lagqvagvqi tngssgvgss sriiirgens lsgsnqplfv
      181 vdgvpisneq itsdlvndga lqevdygngg seispddias isilkgagsa alygaraang
      241 vvvittkrgr rhkglgvsis ssltietllt lpdyqneygl gsngqyafqn gigagtndgg
      301 issygprldq gqliaqfdsp stdidgnvvr ggdviartlp ngsfsaitpt pwisrpdnvr
      361 nffepgitnq nniaitssgd ngssrisysg lrndgivpnt dlkrdglais ldqnvgehlk
      421 vkafvnyins rsgnrpnlgy gyenplygfn wtgrqtdisa lkdywqagqs giqhydinyl
      481 wltnpyltvf entnsfnknr ilgnvsgtyk ftdklslgvr vgmdtyddnr efrravstnn
      541 nplgsyredv vrfrevnadl llsysdtiad dwkytisags nildqgiryk fdeasqlsvp
      601 gvytlansrt plkgnsqvfd krinsvygtg nlgyknslyl dltyrndwss tlpsdsnffg
      661 yysaglsyvv snmfefpdvi sylnlrlsaa svgndtdpyq naqsflfnqn ygaaarvtne
      721 talknanlkp erlnaleagv eawflngriq ldlagyqnts idqiisrpis qtsgfanfnv
      781 nggevrtrgf easlngavvr ltdfkwessl nysmyrsivt elpegvdqfv tgsanifsga
      841 ggnqvlyiar kdgrvgdmyg tgfvevdgqi lyganglptq dpnlrllgny npdftvgfnn
      901 kfsykgldlt ilwdwrkggt ivsrikalgs tsgvlketlv gredgvigdg ivnvgtvenp
      961 qyapnatsvp assfynnfyd rgneasalys asyvklrqva lyynlpdklt nsigfekikl
     1021 gvvgsnlllf tenphfdpel navqersviy gvddfsypst rsfgfslkte f
//
LOCUS       WP_091862429            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Prevotellaceae].
ACCESSION   WP_091862429
VERSION     WP_091862429.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117861
     Region          24..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrltmfiv slflfvgtal aqtkvtgtvl sqedgepiig atikivgagt gaitdydgqf
       61 tvtmpegkdm ieitylgckt etlkavngmr vmmkpdtetl eevvvvaygt akkqsitgsv
      121 stvdqkviek riasnvtsal egaapgvqvn ntygepgaep tirirgigsl ngsntplyvv
      181 dgiiyngnia dlnpediktm svlkdaasaa lygnrasagv viittksgvs hegnssidlk
      241 inhgfynrgi keydrlgvnd ymetswkamk nwamtgsmgl sedeakayas ahlasdvmhq
      301 niwdrasdql fdadgnivan vldgytdldw ekniertgqr qeyilsgnft ndktnvyasl
      361 gylnekgyii ssdyerytar vnstftpnky ftagvnlngt istrhfndna kgtaysnpfs
      421 tarymapiyp iyshnvdgsi atdqngeyvy dtksdyldnr niayelrkdq dtrkrnvlng
      481 tayltlnlpy dfsvtvkgnl shrsstrqqy nnpeigdgaa nggrlsnysn eyedytmqel
      541 lnwgheygnh hidamvghen thyqtenfmg mntkmvadgi yvlsnflnns ylngyndeya
      601 tesylarvry nydqryyvda slrrdgssrf hknnrwgnff sfgatwnakk eeflrtvkwv
      661 nqlrvrasyg evgndagvny ygyqalyyie knggegalmk qslsaddikw etaqtvdaai
      721 egrlfgrmnf sigyfdkrnk dllfavrlpl sagsfsygey fnmtvnknig tianrgiels
      781 vdadvlqkkd wnvnvgldat fiknkiiklp ngdnilsgvh nytegrslyd fytyhfegvd
      841 qmtgrslytl dpekketaaq qgelvtlngv dyttdtaygk rdfhgtaapt vygsvhgnvs
      901 wkdltlslla tyslggktid ytyqtlmstn amssgsalhk dalkawngvp egmtetsanr
      961 idsngvpamd ynlssknnat cdrwltsasy lvmknislsy slpkkwltcl nagvngatlt
     1021 agvenlftlt grkgmnpqyn ftggsddtyv tarvwnfsln vnf
//
LOCUS       WP_091866944            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pricia
            antarctica].
ACCESSION   WP_091866944
VERSION     WP_091866944.1
KEYWORDS    RefSeq.
SOURCE      Pricia antarctica
  ORGANISM  Pricia antarctica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pricia.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Pricia antarctica"
                     /db_xref="taxon:641691"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118450
     Region          25..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrarhkgllt lllalvvqls faqeksvtgt vtdqnglplp gvnilvqgtt ngtqtdfdgn
       61 ytisanegdv llftyigqad kaetigasdt vdvqmvedaq aldevvvtal giskekqalg
      121 yattqvtgde vntaketnfi nslsgkvagl dikkssslgg ssniilrgyt sltgnnqplf
      181 vvdgtpignd naistdqdtg rggydygnaa mdinpedies vnvlkgaaas nlygsraang
      241 viivttkkgs kskglgitin sgvtlanydk dtfpkyqnqy gagygpfygn gpgdyfsald
      301 vdgdgvddlt tpftedasqg gafdpnllvy qwdafypesp nylqatpwva rkhgpeyifn
      361 tgvtlsnsvs vsagsetgsf rlgytsldqt givpnskikr nsidfngsqq lsekltagvk
      421 atftktdgkg rygtgydgkn imqqfrqwnq invdykqqee ayfdtgrnis wnyggnpltp
      481 egqaaiffdn pyftqyenye tdtrnrlfgn inlnydatdw lsitgrtsld tysefqeerl
      541 aitsvgvsqy ervnrtytel nydllfnydf dlaekltldg vigatarqns ieavrastsg
      601 glvvpklysl snsvnllepp tedldklkqy gffanasfay dgflyldlsg rydisstlpe
      661 dsngffypav stslvfskll nvdwlslgkf ranyaqvgns trpyrvfdty fsptnfsvpl
      721 fsvasqksnd nlvnelsdsf elglemtfan kragfdvsyy ktntidqifp vtvsratgfs
      781 srvinsgevq ndgieaavfv spvrtedfew rinatwaknn skvislftne ttgesvdnvq
      841 lgsfqggisv natvgepygs iwgsnftylr daegnitnps pvinaetgky vrdatpqpig
      901 dinpewkggv sntltyknls fsflidvqkg gdvfsldtwy gfatgvydvt agynelgnlv
      961 rdpvetgggi lleginpdga pnttrslvdf enalgyrsap nalhvydasy vklremtlsy
     1021 klpaallkni pinnmtfslt grnlwiidkn mpysdpeagl sagnlqgyqs spyptskeyg
     1081 fnirfdf
//
LOCUS       WP_091864619            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pricia
            antarctica].
ACCESSION   WP_091864619
VERSION     WP_091864619.1
KEYWORDS    RefSeq.
SOURCE      Pricia antarctica
  ORGANISM  Pricia antarctica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pricia.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Pricia antarctica"
                     /db_xref="taxon:641691"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109885
     Region          24..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitwirtlm mfgaflclaf vqaqevsgtv sdatgplpga svvvkgtttg aqtdfdgnyt
       61 lsevpddgtl vfsyigyanq eiavngqtti nvtleedaqa ldevviigyg tttvkdatga
      121 vssvksedfn kgiisspeql iqgktagvqi sqssgepgag islrirgtas vrgnnsplfv
      181 vdgvpvsnes vsasgadigv gssgsknpln flnpndiesm silkdasata iygsrgangv
      241 vvittksgkg ggtegqwgft snlnisqaan eydllstqef verggadlgg stnwqdyvfr
      301 ttastdnnls ysqnygsgnv ratfgyskqf giientdler itgrinvgqr ffddklkvnf
      361 qgtvsrindk kpfisrtags tgdllaasyy snptlnanpl antdpdlnpa nllayyddnt
      421 qtdrflgnls leysitdnls akvnlgldts tssrgqvagp allglgngvq dngrgsvrnl
      481 dtenmllelt vnytkefens nldalvgfsy qdfnrqgenl lgqgygtsdl naiakitqea
      541 fddtenlann yqgygigtfq dnadagnqlr vlsltpgvsd ttlplpnipi dafaadtfdf
      601 tdelqsffgr inytlfnkyl ftatvradgs skfggnnkyg yfpsaafawk lneenfinee
      661 kvstlklrls wgitgnqdgl gygnylnrtr wnglgvlnns qlttpatsev afanpdlkwe
      721 staqyglgfd fgfnndrfng nidvyrkett dillnlpavq pattpfvfqn vdgtlinqgi
      781 elglnydiat sedfywnasf nisynenelt nyngptiqag nlygqgltgt tsqvltdgkp
      841 iytynlrsvd dnfnvatdpe vldksalpki isglstsasy knwdaslffs gqfdfyvynn
      901 tanalfaspq igsrnnlksv vdegvvlsat npstfflekg dfvrlqtasi synvplsgdg
      961 lfktmrlsai gqnlflitdy sgldpevsts dipanglpsa gidylsyprp rtysigfnvt
     1021 f
//
LOCUS       WP_091870089            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pricia
            antarctica].
ACCESSION   WP_091870089
VERSION     WP_091870089.1
KEYWORDS    RefSeq.
SOURCE      Pricia antarctica
  ORGANISM  Pricia antarctica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pricia.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Pricia antarctica"
                     /db_xref="taxon:641691"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112012
     Region          25..1019
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrklnyfff igalflclgt yaqektitgt vtsaadgmpl pgvnvlvqgt tngtqtdfdg
       61 nyaidatdsd ilvfsyigtk sqsvnigdss tidvilveda sqleevvvta lglerqeksl
      121 tyanqqvdtd eltkarsvnv leglsgkvag vsvtrsssgv gapvkvvmrg nrsidgssqp
      181 lyvvdgilld gdinnispdd iqeisvlrga naaalygsra angaiivttk sgkgaregvs
      241 atlgfastit saihlldfqn eygqgsagty sptattswgp rfdgsqvahw sndpnysafg
      301 gtyayeaqpd nvkdffqlgh elatnlgvni nseksnvflg ytftdagglv pgndlkrhsi
      361 sarvnsnvte kleidaklny irddfsnvls agegfdnpvr ylyktprnir tedfehyefi
      421 ndegklrqhy flpqfngggn pywtinnvir prldervlam lsvkyditdd laifarsamd
      481 rtsrseeqiw yndtytqapl gqytkrasns ydwntdvlit ynknlsedfk iglnaganqr
      541 vykrneltgs gtnftienff alsntqnpva sealdrfevq siyglgefsy knaiflnlta
      601 rndwsstlpe snrsyfypsv gltavvsdlv dfgsglsflk lranwaevgn dtgsfrlsrr
      661 adirngtldi nptqpntnlr pestqslelg fdsrffdnrl rfdvtyyktn tfdqifstpt
      721 pvasgianvf qnganienrg vevvlgativ nndnfswdld lnfatnqnev leiaegfdkl
      781 tvnsdfirdy vlevggeygd iysrgferdd qgrvivdalg lplitpgrda vkvanfnpdw
      841 lggirnsfry knfnfstlid irqggsvtsf seailardgv ldytangrdg glifgenifs
      901 getavredgs pntisvsaed yynrvggrnt pvgeafvrel snirlremvf gytlpqkmls
      961 dtfltsanfs lvgrnlffit nkaenfdpei vnsvsndseg reafalptsr svgvsinfgf
//
LOCUS       WP_091869242            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pricia
            antarctica].
ACCESSION   WP_091869242
VERSION     WP_091869242.1
KEYWORDS    RefSeq.
SOURCE      Pricia antarctica
  ORGANISM  Pricia antarctica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pricia.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Pricia antarctica"
                     /db_xref="taxon:641691"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112331
     Region          20..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksltlilfv llysynsygq titgnvtdas daplpgvtiv iggttngttt dfdgnysiva
       61 nsgdvlqfsy igmqskevtv gssnlinvil qedseqldev ivtafgisqe kkslgyaaqn
      121 idadaitktk qtnlvsalqg qvagvqitns ggapgqssri iirginsldp sadnqplfvv
      181 dgvpidnsti esgnndtprg ltnraadinp advesmsvlk gaaatalygv raangaviit
      241 tkrgksgrvs inlntsvgfd elnslpklqk eygqgfsgey dpesfwpswg apisevaqtv
      301 pghkyqdnwn rafntglqtd nslsvsggge natfygsfgr ldqkgiipfs dwarttakls
      361 gtvkvsekfd fsgsinysns ggnrvphdrf mermmywset tdvrdyinad gtmktygntn
      421 piydarfsty eddvnrmign lnfnysptdw ltlsyrlgtd yysdsrtkit pgpkgivgev
      481 plsstgtiee trinskdits nfyltlkkqw nddlnttlrl gndvfqrkfd rvslrgedfv
      541 ipdfynvnvt rqgflgqdks irrlvgfygd lmvnykeylf lnvtgrndis stlpkdnnsf
      601 fypsvnlgyv fsehlelpsw ftfgklrgsw aqvgkdtnph vlgityvapd vfpldgqvgf
      661 srnssfgdpe lkpelttsie fgtqlsffes rldldvtyyk snavdqiipv pisdgtgfsq
      721 yitnageiqn sgievvlggd iiknedfqwt atanvsmnnn eikairegid eivvgdqfgy
      781 agssvtmkli rgeafgnlyg tsyerfgade nnifldselp ivigddgfpv tggnqlilgn
      841 avpkwfgglr neltyknfel svlvdfrtgl eqynqfdnfl safgkpeysl arndfrvfeg
      901 vladgtpntq evwlgqgvgp dgrdygagyw rnayrgvsen fvqdasfikl rnislaynls
      961 dkmldripfk slrislaann iilyspwdgf dpesfsagag gnavgftglg fpgtqsyflt
     1021 fnfgl
//
LOCUS       WP_091872865            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pricia
            antarctica].
ACCESSION   WP_091872865
VERSION     WP_091872865.1
KEYWORDS    RefSeq.
SOURCE      Pricia antarctica
  ORGANISM  Pricia antarctica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pricia.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Pricia antarctica"
                     /db_xref="taxon:641691"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124685
     Region          25..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrnlpflt lfffsmvigt lsaqqevtgv ikdntgevlp gvtvllketv tgvtsdfdgn
       61 ysisvpnnsa vlvfsylgms tqeivvgnrs tidvvledss qeldevvvta lgisrdkksl
      121 gyavsevggd aidnvpqena lnalsgkvsg vainstgaag asvsmvirgs tslsgdnqpl
      181 fvvdgvpifn tlnnvggvgs dnrvdygnai sdintddias mtvlkgasaa alygsragng
      241 vvlittksgk srkglgvtvn sstvfdipyl yldthtkyaa gsrpytpdnf ptnpygaiqi
      301 setasawagp alnqgikaih wpytaqeles gipvarelrs hnnarnffnt avttannisi
      361 qdntekinyr lsynnlknkg fipntdlnkh sinlnssinl nsaisvsssl nytktysdnr
      421 pagnrganpi qamyelaphi dvrdlkqywl pgyeglfqns pfefgddpte tewnnpyfla
      481 nevnngfvrn rfygnvrgdw kitddfsamv rynfdeineq retkisngyt neingaygit
      541 dlfrkeinvd flltydkkfd dwdfsvsvgg nqrkfdastv snatknrgqg lltpnlftlt
      601 niaasnldfr ssqqekkvns lyglasigfk dmfyldvtgr ndwsstlpds nnsyfypsis
      661 gslllnntfn mgnkvslvkl ragyaevgnd tdpynlqpil nsggawgnas llsvpgnlln
      721 aelkpesqns wevgadlaff gnrlrldaty yesdnrdqif pvnnpissgy etkfinagll
      781 sskgveagln gtivasndwn wdmgfvftkn rtkvveladg mnsitlwtda kggaitwlge
      841 eignivdrkl vrvedpnspy dgwpiiddeg fensdstled edgnrvapvi gnfnpdfilg
      901 mttsvsyknw slsmnfdwrk ggqfvsqthr ygesdmhtqr wldklhnfnd vgdlptylke
      961 negefltedg efyvlvggpt aeeggfpvdd ggitlsdgvf mpgvqgeydd ngnfvvtten
     1021 lggpgtaytr yqdhygwdft rtslfdsdfv klreislsya lpsqslrqig iqnmtislfs
     1081 rnlilwtkag igidpemafq pesetqgrsg iqfkqgierf nvnpfaipig fkvnlsf
//
LOCUS       WP_091875855             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Massilia
            yuzhufengensis].
ACCESSION   WP_091875855
VERSION     WP_091875855.1
KEYWORDS    RefSeq.
SOURCE      Massilia yuzhufengensis (Telluria yuzhufengensis)
  ORGANISM  Massilia yuzhufengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Massilia yuzhufengensis"
                     /db_xref="taxon:1164594"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39018
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaarh qllvqagagv rasipdaaye aagasivdaa
       61 tafgadmvlk vrspdsaera qmrpgtvlvg mlnpfdadnl allaaaglsa faleaaprit
      121 raqsmdvlss qaniagykav mlaantygrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpyvtdeer eiakgaggya rpmpadwmrr
      241 qaelvherar qadiiittal ipgrkaplli seetvramkp gsvivdmaie qggncpltel
      301 drtvvkhgvh iigepnlaam vpadasalya rnvldflklv idkedkfvid redeivratl
      361 vcadgavlrt
//
LOCUS       WP_091888211             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. Rc2d].
ACCESSION   WP_091888211
VERSION     WP_091888211.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. Rc2d
  ORGANISM  Bradyrhizobium sp. Rc2d
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium sp. Rc2d"
                     /db_xref="taxon:1855321"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39249
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneas lktmadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa dmvksmkpgs vlvdlaverg gnvegakage
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkeqklavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_091891491            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. KT25b].
ACCESSION   WP_091891491
VERSION     WP_091891491.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. KT25b
  ORGANISM  Polaribacter sp. KT25b
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Polaribacter sp. KT25b"
                     /db_xref="taxon:1855336"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111457
     Region          25..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lllafvvqis faqqktisgt vsdksgslpg vsilvkgtnv gtesdfdgky
       61 sikakagdvl vfrylgykmv qktvgssnsi nvameedssv ldeivvtafg ikrkpdeltt
      121 snqvvkaeel tkagaqnlaa altgkvsgld vrqvssgvnq dftitlrgmr sfsannealv
      181 vidgvpstaa lffaldpdii envnvlkgan gaalygprgs ngvvivntkk ggngsekgyt
      241 iniktssefe syaylperqt rygqgwasag lfqhfvyeng awgpefdgss ipvglpledg
      301 tfryspyetl gsdnigeffq tgntqnysas isggnledgy anfsvshlnr efiieddtqk
      361 rttislragk qlgkfslegn iqyvtfrtqn agtslygdll htatnidlsq fsdgnnathw
      421 ngyfdspywn rknirtfsls drinasvnlg ykvndninir sttslysstg sgynynngyv
      481 dptsvsdlsg ftrtitssyg sntssyirly sdlianfdyq ltedfnlnan lgatvnqttt
      541 tnngqsgtnl tipglyniqn vintnpatds ktisrqqaif advtlgykdy lflnatarnd
      601 wlstlngqnf fypsagvsfi ptkafesltd ndvidrikls ysfvqvgnan avsaydtnnl
      661 ysqasgtfyg typfgtanaf lpsasitdpn lkpeftnshe fgltaeflkr kirfdvsgyi
      721 gsttdqisei stsyasglts ntinigaadt kgieidlglt pidtenwtll lnasyaasrm
      781 evtkvsdqsd evqvaggtvg ifaevgeqfp iikgsdyvyd peghvvvdtn gdplvseelq
      841 ilgkttpdyi lnfngslryk dftlsvtady rtghsfysgt ksqlawsgyl vesaengrng
      901 fifpnsviet spgvyttnts vvtggpddsa flnyysgrys diarnfvlda talkvreisl
      961 sytmpkayld gtgvsglsvt avarnpftil saenrgyadp easnqggngv glstvgnypn
     1021 trtfglnlnl tf
//
LOCUS       WP_091878299             456 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium sp. OV277].
ACCESSION   WP_091878299
VERSION     WP_091878299.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sp. OV277
  ORGANISM  Phyllobacterium sp. OV277
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Phyllobacterium sp. OV277"
                     /db_xref="taxon:1882772"
     Protein         1..456
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46953
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke tdavesrvgg saetvkklig lgfsvivesg agvssripdr efeaagatig
       61 ktadirnadv vlkvrrpssa elksykkgav viamldpygn daavkelada gvtaftmefm
      121 pritraqvmd vlssqanlag yqavvdaaee ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdiiitta lipgrpaprl vtremygrmr pgsviidlav erggnvegav
      301 agkivdvdgv kivghlnvag riaatasqly aknlfafvet lvdkdakaik vnfddelvka
      361 tvlthggkvv hpnfagaaps atapaakpaa kkpakakaap aatvavttep kkapataapk
      421 kaaapkaapk ktppkpaatk taapktaaqk ttegea
//
LOCUS       WP_091892768            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. KT25b].
ACCESSION   WP_091892768
VERSION     WP_091892768.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. KT25b
  ORGANISM  Polaribacter sp. KT25b
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Polaribacter sp. KT25b"
                     /db_xref="taxon:1855336"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117375
     Region          25..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkflskfl ilmsfflsti afsqqvlsgk iidetgsplp gatvnvknsd kwatsdfdgn
       61 fkiefkeekn iirveflgyq skdivignkn nititmlpev nslsevivta lgikrsqkkv
      121 gyatqkveas tikeivapna aglitgkvag ltvsnptglf qapsftlrgk tplvvvdgip
      181 vstdfydisp ddivditvlk gtsasalygy rggngaiqit tsrgqksngl eitvshntmv
      241 sagftvfpet qteygngsng qyefwdgqdg gisdgdmiwg pkfepgveia qwnspikdnv
      301 tgevtpwwgd vsgtkyddks rysrvpiawe yhnnlkdflr tgvinttsfs vansskngsy
      361 rlsgnyksht drvpnaslkt agltfnsstk lsdkltldsk laynkvyspn yprhgygpkn
      421 hmytiliwmg ddvngkelne hryipgqegy rqanfnyawy nnvyfaanel nqkydsnvln
      481 gqlklnykvt ddfsiqamgs avmkdrfedr espksylnyg dprdgdyktw ntnsvdvdyn
      541 llatynkeis nklsfsanvg asseyhkyqq eynatdgiiv pelyslnntk gnikgstnfs
      601 ersvnslygm leldfdsklf ltftgrtdkh stlptdnnsl fypsvslssm isdwfqlpes
      661 inylkafgsw aqvkrslsay qinsyydnag tydgspelsy sgslvnpdie gslttnvelg
      721 lsagflnnri gldfayynav densiidlpi slgsgfssrk enahqfttng fevsvratpi
      781 kntdfrwdvl anwskkvqrl trldedaeqy nslrlndrtd ayyatvweks adgklildan
      841 tgmptknpyk qnignknpdf rfglennfky kgfslkvgid gvwgglmrsl tvekmwwggk
      901 hpnstlyrda eyangigtvy vptgvnvigg svqrdlngnv tsdtrtyath tspvswqaws
      961 qnypyraqvt eeeseifanv fdrsylklrt vslsydltki anikgvkqln asfngynlfi
     1021 lkkadiidpd fgdddnlqdp strylglglt fkf
//
LOCUS       WP_091893815             969 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. KT25b].
ACCESSION   WP_091893815
VERSION     WP_091893815.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. KT25b
  ORGANISM  Polaribacter sp. KT25b
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 969)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 969)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 969)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..969
                     /organism="Polaribacter sp. KT25b"
                     /db_xref="taxon:1855336"
     Protein         1..969
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106993
     Region          23..968
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiklllig lllstsftmf aqqtvkgvvk ekstgtalpg vsvvvkgtvr gsqtdfdgmf
       61 iiekvktgdi lvfkylgysd keivigsnfn ltveleesle qldeivvvgy gsvrkedltg
      121 ttdlltskdf nkgpivsaqs lisgkvagvs viagsgapge gqsinirgtg slsltsqply
      181 vidgipldng gvagsrnpln finpndietf vvlkdassta iygsraangv vlittkkgkd
      241 kefkfnissq ttvytlrdkv dvlsanqfts lindigstsq iallgnsdtd wqdeiyttai
      301 gqdhnfsaig nlygmpmras lgysehegil kgdnlarttg sinlsptlfd khlkielnak
      361 gmytenkfan rgaigsavsf dptqnvydat skyggyfawl dingnqnsla ptnpvallnl
      421 iddtaeirrf vgnakfdyki hgfedftatv nlgydtsnsh grtvtsslip ktetgfngsl
      481 tsyiqnsdnk vfdayltyqk tfneahnltv vgghayqsfe ydnysydsea qedgntyefi
      541 dksknvllsy fgranydyng kyyltatlra dassklnpdd rwglfpsfaa awsihkedfm
      601 qdsffnelkl rvgygetgni ngledylflt rytgstdtas yqfgnqyyqt yrpeeinenl
      661 rwevgrtlni gvdfafldrk isgsvnayvk etndliassi vdpftnfgnr iranigdmen
      721 rglefminat pirtenfews lnynislndn eitklstdqp qggistgvgg qvqvhreget
      781 ansflvyqqv ydangkpleg vfvdrnsdni indddkyidn dpfadvlmgf ntnlnyknwd
      841 lsiqtrasfg nymyndiaas kgilqnatnn nilsnlhady ynsgftvisn dtalsdhfvq
      901 dasffkidni sigytldqle nttfrfygsl qnvliitdyd gldpeislgi dnnfyprprs
      961 fvlgvnvnf
//
LOCUS       WP_091897227             931 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. KT25b].
ACCESSION   WP_091897227
VERSION     WP_091897227.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. KT25b
  ORGANISM  Polaribacter sp. KT25b
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 931)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 931)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 931)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..931
                     /organism="Polaribacter sp. KT25b"
                     /db_xref="taxon:1855336"
     Protein         1..931
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102599
     Region          62..930
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitikelkg fvfcvlnvla inigvaqntp lnnlavqdsl ktkgnnellk tpfgvfnigq
       61 ttgavfrisg delrksggdn linslrgrvp glrivrtsnt pgnggysytl nggtpnvlid
      121 gqprglqvdl rdvdevivls datfnallgn lgdngliyvv tkgnklskpa ievnyqvgys
      181 tpthlpklls aseyatiine asnndglgnv yspeaieayk ngsdpinfpn vdtqetylsn
      241 laasnymsln lygasekvsy saflgysdwe glekvgskid grnitfrtki dtkindlvka
      301 hasvygrfge nerpvigpdd tfrwitntpa nafplmvgds ayvvnnqfqt nllselengg
      361 trtdytsnmi fdigfdfdld qfvpglaydt yimmktynah slltnnqpal ytlenledtn
      421 gldslalkvy knevldlsig rtggaiqrnf ayggnlsyvk etakgilnln lshllfyqpn
      481 itasqtdqrn ftvnlngsya lenkyilfan ansssssrfl dnhktkmypt vgaawvasne
      541 nflkdskvid ylkfrtsygi vgteygfttl lyldtwsggr nngttylgtn gnlsqdelgy
      601 rlnttgndei dwveynqlfa gvelqmfkkl kldfnyfnil innqvirasq lyasalgndv
      661 ylpqlnfkes rnkgfntnit fsdskdsfky hisanagynk vigekiaevq ypdeyrlqqg
      721 qaqdnivgyv sdglytaeni gsalpqfgdl qvgdvkyvdl ngdnvidsrd tktignsnpr
      781 vnyginfgfe ykginldvvg mgvtgydinl nsyayyqhgg lgnyygsvns dlpngnanpr
      841 lstltsinnn knsdywllng gyfkianvel gyslpesiis dssfadvklf lrgsnlavfs
      901 kmkdldpeni nagfsqypmm rtftlgasin f
//
LOCUS       WP_091896444            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. KT25b].
ACCESSION   WP_091896444
VERSION     WP_091896444.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. KT25b
  ORGANISM  Polaribacter sp. KT25b
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Polaribacter sp. KT25b"
                     /db_xref="taxon:1855336"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123105
     Region          21..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrliyllif ipailmgqnq kvitgqvvdk ttktpiigas vyvssaiigs ksntegvidg
       61 rmlgtttnfd gefkltirqd ikyflvsyig yetekiavsa ektnytivlk esdevldeii
      121 itgyqkiekr kitsayekik vaeieqsgvs sidhmltgqi agvvvqptsg apgapakivi
      181 rgsatlngss dplwvldgip ldgsdipedf rdkdnidnle sypiaglnpe diesitvlkd
      241 asatsiygar aangvivits ksgkkgsmri qangnffvtq kpnfsklnlm nssqkvdfel
      301 ylagrsdlty qqdrgsvari lnyygeydnf qnngfeslsl ntqneinnlk qtntnwgdql
      361 yqtavnqqys vsisggddqn nyyfstglfd qkgtttgtgq qrynvtlkdk fsindklkvg
      421 vslfgsqtkt ssyitgaday tnpsyysrta npylsltden gdyvydpdlv ersdlnlnyn
      481 vleerentny elisnslkai ldvnykiakd feinsqlglq ldfdktekfs deesyytrky
      541 eqrsqyntss gsayympkgg iiqnwnsdvf qynwkttany stifnnrhel dvmigtefrr
      601 nkkteihakg fgfnantltt iaitderalt nslfdtysks yyenayasff gtasytldkk
      661 ytfftslryd gsnlfgvnpk yrylplwsva gswnvfredf isdidfisdf kirasygvqg
      721 nidkstspyv igeyytetil pgtseeiira tsapnanlrw ektvssnigf nlglldnrih
      781 itsdyytrts tdliglqsvp lesgfsfint nwasvsnkgf efllhtvnik kddfkwsssf
      841 nishnksive dieireedfk pslkgyssta ifgiktagld snglplfwrd gvkvsavdfy
      901 nleegtdgsq ltreehrnly syigdatpkf sggfnnsfty kqfglriltn fnlkqtvkat
      961 psynltqaqp gnnystdilk agkgnlpali gfntpgfdtd lvynwfnssd dgrtyddldi
     1021 wikdisylri ssikfsysfp kkaveklnfs slnfniegrn lfvigtnydg ffdpetygsi
     1081 yaqpipkiis vgfnltf
//
LOCUS       WP_091895306            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. KT25b].
ACCESSION   WP_091895306
VERSION     WP_091895306.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. KT25b
  ORGANISM  Polaribacter sp. KT25b
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Polaribacter sp. KT25b"
                     /db_xref="taxon:1855336"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117650
     Region          21..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhlylwmfl lftsisisqt kitgtitdkk tkeklpyvsi tsspkngtvs dingfysitv
       61 lkenkfltfs ylgyktqkip innltniniq leedetglde ivvtalglnr ktkelgyvvq
      121 eikakdvanv ktvnfldnls gklagvtisq gatgvgsssk itirgeasfs nnnplfvvdg
      181 tpinnnsvfn ftneaaagfq eidfgngamd vnpddiesit vlkgpsaaal ygtrasngvi
      241 vintkdgskk kglgvsinss itfdsafrlp dfqneygqgn sgnfeyvdgl gsgvndvity
      301 swgpkldagn lipqfdspvt ladgtvvrgg dtslynglsi tptlfesnpd nlkdfyqtgv
      361 ttinniaind sfergsyrls itdldsesii pgvnlerkta alklnfnpse ktkitssiny
      421 vnsssdnrpa ngygsenany slvawgprsl nidnlrnywq pglegvqqys fnytyfdnpf
      481 filhentnsf nrdrvfgnia lqhyftdnls vslrsgmdfs senrefkrnf ssnrfkngay
      541 aehdvfyrei ntdflinynn nfgdvsfdvs fggnrldqna stkqtqttnl aqpgifslnn
      601 aaspievfef eskkrinsly giaklgykdy lflditgrnd wssalatpfs vdgtsffyps
      661 vstsfilsny tdlpesisfa klrasvaqvg ndtdpyqtsg afvsqttfng qatfsnqdfi
      721 pnsdlkpeit tsyelgadlr ffkdrlnidf tyynattkdq iislpipiss gynqqvingg
      781 kvntsgveii lggtpirnen fkwnttfnfa snksvikdlp qndgrltlay sriydsanqt
      841 vwfqveeggq igdmygtgye knadgeflld ddgryianne likignynpd ftlgwnnsft
      901 yknwnasflf dwrqggeivs rtralgnvgg qlaetayrpd agiiaqgvnv ntglpntvav
      961 taesyyrqfy drnheennvy dasflklrqf sigyvlelne gflglknpst mnfsfignnl
     1021 fvitenphfd peqvavqgng fvsgvedmsy atsrslgfkv gfnf
//
LOCUS       WP_091900855            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            stanieri].
ACCESSION   WP_091900855
VERSION     WP_091900855.1
KEYWORDS    RefSeq.
SOURCE      Maribacter stanieri
  ORGANISM  Maribacter stanieri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Maribacter stanieri"
                     /db_xref="taxon:440514"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110297
     Region          24..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitflksll vlgafmcfgl vqaqevsgtv sdasgplpga svlekgttng tqtdfdgnyt
       61 ltaeegavli vsyigyktqe vaingrtsin ftleedaeal eevviigygt ttvkdatgsv
      121 tavtaedfng gnisspeqli qgktagvniq etsgepgagi qinirgsnsv rannnplfvv
      181 dgvplgggdt spqgetgfgq savknplnfi npndiesisi lkdasataiy gsrgangvvi
      241 ittksgkgss qgvwdfsssl siataantfd lldsseflsg vtavggdasa vnfgantdwq
      301 qvvlrstasq nqnlsyskny gsgnvratfg ygkqfgiven sdleritgrv nlnqrflddk
      361 lvlglqmsia rindsqapis aqagaagdvl ggayaanptw pansgfnagg lnvnpqnald
      421 ntqnitntdr yllngsiqyn ftseisakln agldvaeatn tsvisrdinn ingvtdigrg
      481 nygvlernnk tfeatvnynk efesssleal vgfgyqdfqt fgfnaggrgy ttsdlnamgr
      541 nlrsavsdlq navtgsyqqa yyapntggvl vnrllptvva qealgttlns svtsvftnsf
      601 dntdelqsff arlnytlndk ylftatmrad gssrfgpenq ygyfpsgafa wkmneedfvg
      661 ekvstlklrl sagitgnqdg lgygnfvarq rfsdltvqqn ldinangtai vatdrpdlkw
      721 essfnlnagl dfgfnndrfs gsldvyrtet tdvllqtppa apavdpfqfq nvdasiinqg
      781 velalaydfv rtddatfsad fniaynnnev qnfdglidtg avngpglsga faqrfasgqs
      841 lysyflpife gfdssgnpty qdvdgngvgd pfgdktfvge dalpditsgl slnlkvkdfd
      901 asvffqgqfg fsvynntena yftagalsns rnvtqnvlts genpgasada strflekgdf
      961 vrfqnasigy nvplsgegal nslrfsitgq nlflitdysg ldpevtantg dlgsgvpsrg
     1021 idygsyprpr tftfginasf
//
LOCUS       WP_091901335            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            lc2012].
ACCESSION   WP_091901335
VERSION     WP_091901335.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. lc2012
  ORGANISM  Prevotella sp. lc2012
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Prevotella sp. lc2012"
                     /db_xref="taxon:1761886"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117387
     Region          24..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkerltmflv gfflcagsml aqtkvsgtvl sqedgqpiig aavkvdgtst gmltdvngrf
       61 sltlpegknq ltisylgyqs ktvaakngmr vflasdsqvl qdvvvtamgi krsakalgys
      121 atavdgdkia aartadimss lqgkvagvqi sssasdpgss nsviirgiss lsgtnqplyv
      181 idgvpmnnsa vystdglnsg ydfgnganav npddvenmti lkgaaataly gsraangvil
      241 ittksgkkqe kglgieyngg lqweqvmrlp qmqnefgmgw ngdktddeng swgprfdgst
      301 lkygtvynns qqiksylpie nnmedffdtg frysnslsfn gatdksdyfv sfsqikddgi
      361 iptdadsyqk ytfsargthk vkaltfsssl nyayqknnfv qtgqgfenmy nsimqtprdi
      421 aivelkdldn pfntpgyyyt pysvmnpyyi lnnhlnenes erfygkfqmd ydflkwfklt
      481 yrvgldtsta hhhigipnye slfpntpnwe sefhnkqtgk tsrkttrrre inqdvmltfd
      541 mpindfnina vvgfngnerq yshmftettn ltiptyynit nsagiptvee yqwkrrlygv
      601 yaqaevawkn qlyltltarn dwsstlpken rsffypgvtv sylfsellke ktpwlsfgkl
      661 rlawgktgnd asvymtdpyy iqgnfdssgw aeskfpftkt stnaytvgnv lgsntlspem
      721 ttetevgvql affknrisvd atyynrnsdk qitrlstdaa sgytaqnvnl gkirnrgvel
      781 lvtvvpvrtk dfewsltwny tknnnkvikl peemngrasi ygfsggtgly aiegdemgvf
      841 eayvaktnge gkiivdkngl pqnsdklvki gsinydymmg ignslrykdf tlsfdfdirq
      901 gglmfsrtqd ityftgnamq ttyndrnpfi vpnsvidngd gtysential ygttlynywd
      961 ngaaamgsas lisksyvklr qvvfgwnvps kwlaktpltg vrfsifgnnl lmwtpssntf
     1021 idpeassfgn dlegnfgeys snpssrkfgf nvnvkf
//
LOCUS       WP_091901618            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            stanieri].
ACCESSION   WP_091901618
VERSION     WP_091901618.1
KEYWORDS    RefSeq.
SOURCE      Maribacter stanieri
  ORGANISM  Maribacter stanieri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Maribacter stanieri"
                     /db_xref="taxon:440514"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117199
     Region          21..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhlvlvltl fmlnmvnaqe titgivtdtd gntipyvnil lsgtltgstt nedgiyslev
       61 lnlsgaiefs vlgfetqivs innkrtinit lndssevlde vvltalglkr etkelgyvvq
      121 sldakgvtev ksvnfldnls gklagvtinq gatgvgsssk itirgeasfs nnnplfivdg
      181 vpinnnsvfn ftseaaagfq eidfgngame vnpddiaevs vlkgpsaaal ygtrasngvi
      241 iietksgknt kglgvsynts ffvdsafqlp dfqneygqgn sgefafvdgl gggtndlity
      301 swgprldvgn lipqydspvt ladgtvvrgg dtalyngnti tptefksnpd nlknfyetgt
      361 tlinniaisn gfekgnyrls ftdlrsesii pgvnldrqti strlsfqpin klrinssisy
      421 insnsdnrps ngygsenany slvawgprsl nienlknywq pglegiqqys ynytffdnpy
      481 filnentnsf nrdrvfgnis asyditenlt asirtgmdys selrqlkray ssnrfsnggy
      541 aehdvfyrev ntdfllnyan kfndfsvdvs lggnrldqka ftsqsqttsl aqpgifrlsn
      601 aaspievfef esnkrinsfy glakfgykdf lfidvtgrnd wssalatpfs vdntsffyps
      661 vsssfilsev velpktisfa klraswaqvg ndtnpyqttg afvaqtpfng qptfsnsnti
      721 ananlqpest ssfevgadvr lfgdqlrfdv syynaltkdq iislpigiss gynqqvvngg
      781 evrskgveii lgispvisqn lkwnstlnfs tnrstveslp qdegrltlay sriydsqnqt
      841 vflqaeeggr vgdlygtgyl knengdfilt degryipdne lqklgnynpd fmlgfnnqfn
      901 yknwnlgflf dwrqggiivs rtralgnvgg qlaetafrpe tgivpegvvn tgtqenpvyt
      961 pntvavsaes yyrqfydrnh eenntydasf lklrqvsigy tfenlsvfnq natlnlslig
     1021 knlfaitenp hfdpeqlavq glgfisgved msyattrsig fkagfnf
//
LOCUS       WP_091902114            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            stanieri].
ACCESSION   WP_091902114
VERSION     WP_091902114.1
KEYWORDS    RefSeq.
SOURCE      Maribacter stanieri
  ORGANISM  Maribacter stanieri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Maribacter stanieri"
                     /db_xref="taxon:440514"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110900
     Region          25..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkflsflt itlllffqgv tgqdknvsgv vtddtgsplp gvnvvekgts ngtstdfdgn
       61 yaisvdanat lvfsslgykt kevgvngrst vntsiaedas eldevvvtal girketkalg
      121 ysltevdade istvktpnai nslqgkiagv nisqnatgaa gssrvvirga sslsgnnqpl
      181 yvvdgipign gnngsaslwg gsdggdgiss lnpddiesis vlkggaasal ygsraaggvi
      241 ivttksgkgq egfgvefsss vtfdkvntdl qdfqqeygqg vrgvrpgsqq aaleagtssw
      301 geaydgvstp qfdgvsrpys ytgnnvdkfy rsgttfintv aitnasenlt yrlsasdltn
      361 edvlpnagln rksfsinssa ilgekltsnv nakyiiekvq nrprlsdspg nanfsvallp
      421 gnidvttlqp stnpdgserg fsnntfstnp yfaaynfnnq dvrnriiast slrydildwl
      481 sltgrvgidn diirrtsvep fgtaykplgg ineeerrynq vdadlilaae knitdkfais
      541 alvgannnhv ksenlflggn dfivpgledi gntvsqsrsr eyserkigsv ygslelsydr
      601 wayvtftgrn dwfstlsfpg kttpnddfyp sinaslilsd alnlpnfvsf lklrggysev
      661 aggaqdpysl altyeifgnp iqgqplgris gstvpnanlv afskneteig ldmrlfnnrl
      721 sldfayynne ttndivnvat seysgfsgas anlgkvsnkg vefllsgtpi qtkdfswntt
      781 ingayneglv vatdnvdsdv nldeprtqnv rithivgety gtivgvsyer ddngtivyei
      841 dgdgvprave gerkilgegv ppltvgftns fryknfnlnf lidgkfggqi fsgtntilyg
      901 tglhkntleg rengltvsgi dvangqpftt tvapedlety ygeindiaee fvedsdyikf
      961 rqmsigyslp kksldnvflt dvnvsliasn lfyikrsvdn idpesaytag nsqgleyfgv
     1021 psarsyglti nvkf
//
LOCUS       WP_091902480            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            stanieri].
ACCESSION   WP_091902480
VERSION     WP_091902480.1
KEYWORDS    RefSeq.
SOURCE      Maribacter stanieri
  ORGANISM  Maribacter stanieri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Maribacter stanieri"
                     /db_xref="taxon:440514"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116527
     Region          25..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngllt lllalvvhis faqqktvsgt vtdqgglplp gvnivvegtt tgtqtdfdgn
       61 ysimaaqget llftyigqka vrksvgagst vsvqmeedaq aleevvvtaq gikrekkalg
      121 favssvdekd lesrsegdva rvlsgkasgv qitaaggmsg satnvvvrgl ssfsgsnqal
      181 fvvdgvpfss dtnaqdtngs gsnfltgntg ssrfldldpn niakievlkg laaatlygsq
      241 gkngvilitt kagsavggkk kteitvnqsy fvnefaslpd yqdeygngfd qafgwffsnw
      301 gpsfeesgls gwgrqasida ngtlehpyst tavaatreaf pefqgarydw kpynsvenyf
      361 kpgsvsstsv ningasedgn ttfnanfgyl ddesfipgng ltranvsigg rsklsnrftv
      421 sgamnysrtd yssppiaase gngttglsif gniyftprsv dllglpyqnp idgssvyyrn
      481 gndiinprwt annakysqlt trvfwnaamq ydindnlnvt yragldyyne rneqysnkgg
      541 veftsaifgf lntydnnnti wdhylalngn ydlseklgmt fnvgatsrst sfdqqgvast
      601 gqivfdiqrh fnyanqspiq ysetrniagl lgqvtldydn mlfltastrt dwvsnliten
      661 nsqtypsasa sflptaawpg lksqnglnfl klraglgqsa tfptayptvs vieqntqvfg
      721 ddggvttnqv agfkanpdlk pellsefevg feskfidnrv sldftyfdrt tkdlivrepl
      781 spstgftftq snvgkiegdg ieidlgidwf rsdsssgfnw nsranftknk ftvteqeqdi
      841 iiyagsstls vggnaaikge qlgvivgdai ardadgnflv ddggdyvtte vdangnvpii
      901 gnpnpdfvmn vinsfsyknw nlgfqishik ggdivsntig tllgrglite tldrentyil
      961 pgvsqstgev nnkqinnsty yfnnilfgpt elkvydasvv rlqelslgyt fpakslertp
     1021 fgsltitaqg fnlwydaynt pkganfdpni qgagvgnsqg fdflngpssr ryglsikatf
//
LOCUS       WP_091902524            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            stanieri].
ACCESSION   WP_091902524
VERSION     WP_091902524.1
KEYWORDS    RefSeq.
SOURCE      Maribacter stanieri
  ORGANISM  Maribacter stanieri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Maribacter stanieri"
                     /db_xref="taxon:440514"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116692
     Region          24..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtllitmv avlasfvahs qsmltgtvld enqvplpgat vvvkgtsngv atdfdgnfsi
       61 eltgsndill vsyigyikke vdvtgksati islepdsqql devvvtalgi erekkslgya
      121 sqelnndevv qarepnllns msgkvaglqi tnsptglggs arvsirgdas lningnsplf
      181 ivdgtpisne ivgssgsgtq svdygngase inpqdiesin vlkgpaaaal ygsraangai
      241 iittkkgksq ssklgisfnt gvtienvlml pdwqneygqg nnqqfafvdg sgsgiadgvd
      301 eswgprldtg lmipqfdspr tdgtrggdtf vsdadiiptp wvsqpdntkd ffetgitktn
      361 siaisksgem gnmrlsfqnl dqegtlpntd lkrntlsfsg tmnvsdkvkv naninyvktd
      421 sdnrpavgyg tesimylfiw ygrqlntnnl rdywqpgleg tqqfnynyny hdnpyftmye
      481 ntnaqdkdri fgnvsltydi nenwklllrs grdfyrdfrv rkrafstqrf pfgtyqedni
      541 ffeesnsdvl lsydknlgek fklnvsaggn qlrqkqdftk svapqlinpg vysfnnsrqa
      601 vqvssnnsek rinslygyar fsydnvlfmd vtgrndwsst lpegnnsyfy psvtlsaias
      661 difnmpewvs fakvraayae vgndtdayrl rsfyqnetpf dgstpiltes slipnadlkp
      721 eitgsyefgl dlrffqsrvn ldltyydsat knqiinistd iasgyssqli nagevrnygf
      781 eaianfvpvl tdnfkwsstf nfatnksevt dlgddiqftl tesngafiqa reggsisaiy
      841 grgfqrvede nseyfgqmii nnqgipertd dlvyqgdyap dftlgmqntf kyknidlgfl
      901 idtrqggivv srtktigsts gqlqetlvgr etgivaegvv ntgtaespvy tpntvnvdar
      961 tfnnryyerd nveaakydas ytklrevslg ysfpqkmiqq lpisnarisv tgrnlilwte
     1021 nphfdpetvg vsggtlqpgi enmsypssrs ftfnlqvnf
//
LOCUS       WP_091903722            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            stanieri].
ACCESSION   WP_091903722
VERSION     WP_091903722.1
KEYWORDS    RefSeq.
SOURCE      Maribacter stanieri
  ORGANISM  Maribacter stanieri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Maribacter stanieri"
                     /db_xref="taxon:440514"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117725
     Region          53..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikliklskw klqtmipllv gfvvlctnqa faisasstlt sdvhllneeq qltvtgnivs
       61 sddgmglpgv avvvkgtttg tvtdfdgnys itvpssdail visylgfikq eiavgsksei
      121 nvalapdtta ldevvvvgyg takketltgs ieqvkaeafe dlavgspala lqgrtpglvv
      181 trtssrpgde gvnflirgas singiepliv idgipsinss sfndmnpndi esisvlkggs
      241 asvygsraag gvilvttkkg kgkikidist isrvgtigir pptptmsqyg qlyaaaared
      301 iasgkppryf fwndletvdr iasgeegyyd lpingniwlg naprfdemfg nsyssqhnis
      361 isggtessnf risagydnnv gglkvaddss drynfsmnyg adisdrlsin tnvtyfnndf
      421 sgpsgglgre aatydaplfp tynadgqyya nfggdlitgd rngvaqvidg grenktveqf
      481 kisalakyqf tdhldftgsy aisrqnseyq tyavsvplys wggsfsnnin ntnfiqegtg
      541 pdkndgnity knykgalnys nqfgdhnlsg llaieaeknd vneynirrng fvdygvydin
      601 lgatdqlvtt sgggtswgff gyigrlnydy kskyllevqg rrdgssrfae gskwsnygsv
      661 sggwvisaee flnesnlisf lklrggygel gstsgigdfg ylstvgfgtt vfgqtnagqq
      721 atsrasslfs snttwerivt kevgvdfrll kskifgsfdl yqkdnvgmlv rgietdllgt
      781 atpftnigtl etngweamlg yqgkigevdf svsanmsdsr neiteydgaq tifenlnaae
      841 dgenilgrpi nsfflwetdg yfdsqaevda yyaslneggi lpsqssndal rpgdmkvvds
      901 ngdgtldned ltysgdaaqh yvygfnfdvk yknfdlsaff qgalehniyr tgyfaqpfqa
      961 ewqnqsntwl grtwtednrn aefprlttqr glsawnyrsk dhilqnnrym rlksliigyn
     1021 fkdlqigktp idniriyfsg ndlfeltsvk dgydpefqas snnsaypfmr twalglkvsl
//
LOCUS       WP_091905536            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Proteiniphilum].
ACCESSION   WP_091905536
VERSION     WP_091905536.1
KEYWORDS    RefSeq.
SOURCE      Proteiniphilum
  ORGANISM  Proteiniphilum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Proteiniphilum"
                     /db_xref="taxon:294702"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124937
     Region          36..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkyqnwckv ilslafllfs igvgfaettd tkqntitltg kvtsaidgmp ligvsivvkg
       61 taegtvtdve gnyrfnvpsn atlvfsyigh itqeiavegr tsisivmees tetlsevvvt
      121 algigreeks lgysvgklgs eelakvvhen vltsmagkvt gvtinqtgga gstvsmvirg
      181 atsmstdnqp lfvidgvpmt ssvnnvggfg ngnlvdygna isdidpesie svsilkgpsa
      241 aalygtragn gvvlittkks drkggmkvev vsntvfdips kyldvqnrfg fgarsytdtt
      301 fpggilppfs pseqagagpe lnkgywqvqp fapldangvp vptelvsypd nyknfingsa
      361 itttnsvais sssdrvnyrl gvsnmtnkgl vpnsdlnrnn ltlaassevv kgltvstdin
      421 ytqnwadnrp atqerganpl qwaawtppnv dirkmkdydl gggqvltige gwenpyflay
      481 ginnsfkrnr lignvsatwe itpqlslmgr yalnrsdetr etkidpgysq epnngaygiv
      541 tsestetnad vlatyknhwd dfsltasvgg nllysrwanv snsskpgsgl iipylytiqn
      601 ientslnysn aryerainsl yatanlgwkd miyldltarn dwastlpaen rsyfypsasl
      661 slllnnmidm grnvnllklr ggvaqvgndt spyslyatyy dvgqwgdair lgkpgdllnp
      721 illpeesksy eigvdlkmfn nrlrfegtyy qadnrnqils vplagsagfn sikvnagllq
      781 skgvelmlgf tpietkdwrw dlnanftknk twllelsegt dfvefwnear vrniayakde
      841 slgrdglign lytrkilrvt dknspyynyp llpendedae wqseddyskv gnynpnfimg
      901 lqtsityknf tlsmtfdwrs ggqyvsqtwr yltegvvsnt wlnqlitppe glgggpsqal
      961 rdwvvanadr liytnnprpv ggptpdfggy yndfytgiga ydgvfapgvy ghyddngnfi
     1021 lskenlgneg tefrpyvmsy pwdigeanlf dadyiklrei slnyrvpdka aqklrmrdln
     1081 isvysrniml waksagmgid perayqsgsn gsfkqgverf naepwvvpvg fklsftf
//
LOCUS       WP_091915376             429 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. YR577].
ACCESSION   WP_091915376
VERSION     WP_091915376.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. YR577
  ORGANISM  Mesorhizobium sp. YR577
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Mesorhizobium sp. YR577"
                     /db_xref="taxon:1884373"
     Protein         1..429
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43946
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifvpke vdpneprvaa spdtvkrlaa lgfdvvvetg aglasriida eftaagakig
       61 ktadaakadv vlkvrrpsda elkgykagaa vlaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgaae ydralpmmmt aagtvpaaki fvmgvgvagl
      181 qaiatarrlg givtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk vgsvivdlav erggnvegav
      301 pgkvvttang vkivghlnvp grvaasasll yaknlfafle tmidkgtkql ainreddlvk
      361 atmltdggkv vhpnfanaap aqaepavkat rtaeakseaa pkkaaakkpa akkpatvkpi
      421 vpgknrgda
//
LOCUS       WP_091915607            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            aff. ruminicola Tc2-24].
ACCESSION   WP_091915607
VERSION     WP_091915607.1
KEYWORDS    RefSeq.
SOURCE      Prevotella aff. ruminicola Tc2-24
  ORGANISM  Prevotella aff. ruminicola Tc2-24
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Prevotella aff. ruminicola Tc2-24"
                     /db_xref="taxon:81582"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117324
     Region          24..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkerltmflv gfflcagsml aqtkvsgtvl sqedgqpiig aavkvdgtst gmltdvngrf
       61 sltlpegknq ltisylgyqs ktvaakngmr vflasdsqvl qdvvvtamgi krsakalgys
      121 atavdgdkia aartadimss lqgkvagvqi sssasdpgss nsviirgiss lsgtnqplyv
      181 idgvpmnnsa vystdglnsg ydfgnganav npddvenmti lkgaaataly gsraangvil
      241 ittksgkkqe kglgieyngg lqweqvmrlp qmqndfgmgw ngdktddeng swgprfdgst
      301 lrfgtvynns qqiksylpie nnvkdffdtg frysnslsfn gatdksdyfv sfsqikddgi
      361 iptdadsyqk ytfsargthk vkaltfsssl nyayqknnfv qtgqgfenmy nsimqtprdi
      421 aivelkdldn pfntpgyyyt pysvmnpyyi lnnhlnenes erfygkfqmd ydflkwfklt
      481 yrvgldtsta hhhigipnya slfpntpnwe selksqtgkt srqttrrrei nqdvmltfdm
      541 pindfninav vgfngnerry symltettnl tiptyynitn saeipkieey qwkrrlygvy
      601 aqtevawknq lyltltarnd wsstlpkenr sffypgvtvs ylfsellkek tpwlsfgklr
      661 lawgktgnda svymtdpyyv qglfdssgwa eskfpfsktg tnaytvgnvl gsntlspemt
      721 tetevgvqla ffknrisvda tyynrnsdkq itrlstdaas gytaqnvnlg kirnrgvell
      781 vtvvpvrtkd fewsltwnyt kndnkvislp eemngrasiy gfsggtglya iegdemgvfe
      841 ayvaktndeg kiivdknglp qntdelvkig sinydymmgi gnslrykdft lsfdfdirqg
      901 glmfsrthdi tyftgnamqt tyndrnpfiv pnsvkknadg tysendiply gttlynywdn
      961 gavamgsgsl vsksyvklrq vvfgwnvpsk wlaktpltgv rfsifgnnll mwtpssntfi
     1021 dpeassfgnd legnfgeyss npssrkfgfn vnvkf
//
LOCUS       WP_091922048             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_091922048
VERSION     WP_091922048.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54799
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ataadlwgrs divlkvrpps seevallreg stlvgfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgti nvdfnddair
      361 gltvikegnv twppppiqqp vaapkpatpp vaaaaskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflahftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa agdrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_091925778             435 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium sp. CL33Tsu].
ACCESSION   WP_091925778
VERSION     WP_091925778.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sp. CL33Tsu
  ORGANISM  Phyllobacterium sp. CL33Tsu
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Phyllobacterium sp. CL33Tsu"
                     /db_xref="taxon:1798191"
     Protein         1..435
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45024
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke tdanearvgg spetvkrlig lgfnvvvetg agtasripda eftgagasig
       61 kaadvndadi vlkvrrpasp elksykkgav viamldpygn dsavkelada gltaftmefm
      121 pritraqvmd vlssqanlag yqavidaaee ydralpmmmt aagtvpaakv fvmgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaalvndhi akqdivitta lipgrpaprl vtremyarmr pgsvlidlav erggnvegav
      301 agkiteidgv kivghlnvpg riaatasqly aknlvafvet lvdkeakvlk infddelvka
      361 tmlthdgkvv hpnfaqaaaa vaapaetpaa kpvakkaapa kpaalkdaav kpaakkaapk
      421 kaaaskaapk tegea
//
LOCUS       WP_091926655             409 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium sp. yr668].
ACCESSION   WP_091926655
VERSION     WP_091926655.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. yr668
  ORGANISM  Methylobacterium sp. yr668
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Methylobacterium sp. yr668"
                     /db_xref="taxon:1761801"
     Protein         1..409
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42052
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd saeprvaavp etvkkfktlg advvvqsgag qkagildsey eaagasiags
       61 aadasgdadl vlkvrrpsae elpqlkrgat viaimdpygn edalkamaea gidgfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrampmmmt aagtvpaarv fvmgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsaeyqk
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 agevvtndrg vkivghvnvp grlaatsssl yarnlyafve tlidkeskal ainwddelvk
      361 atnltrdgsv vhasfqpktd gaaseaasvg lakseaskas gaatpagaq
//
LOCUS       WP_091933933             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus sp. DSM 46786].
ACCESSION   WP_091933933
VERSION     WP_091933933.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus sp. DSM 46786
  ORGANISM  Blastococcus sp. DSM 46786
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Blastococcus sp. DSM 46786"
                     /db_xref="taxon:1798227"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53618
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpretr pretrvaatp atvtqlvqlg ydvvvetgag taasfpdday vaagaridaa
       61 aeawaaevvl rvnapardei grladgatli sllspalnpe lvealaarpi tvlamdavpr
      121 israqsmdvl ssmaniagyr avveaanvfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igtasslgai vratdvrpev aeqvrslgge yvavpageqe vssdgyarem gedfnrraaq
      241 myaeqardvd ivittalipg rpaprlltee mvasmrsgsv ivdmaaaqgg nvagsvadev
      301 vvtpngvtii gytdlparlp aqasqlygtn lvnllklltp gkdgrlvldl ddvvqrgitv
      361 vregeltwpp ppvqvsaapp paappagata gtpavpqrtp apgrrfalvg lgaallflva
      421 afspdellgh ltvfalavvv gfyvigkvhh alhtplmsvt naisgiivvg allqlgsddg
      481 vvrvlafvat lvasinvfgg favtrrmlgm fsrgpspesa vr
//
LOCUS       WP_091939459             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Trujillonella endophytica].
ACCESSION   WP_091939459
VERSION     WP_091939459.1
KEYWORDS    RefSeq.
SOURCE      Trujillonella endophytica
  ORGANISM  Trujillonella endophytica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Trujillonella.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Trujillonella endophytica"
                     /db_xref="taxon:673521"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53370
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpreta pgetrvaatp ttvrqliglg hevvvesgag gaasfpdeey aeagariaaa
       61 adtwgadlvl hvtppsavei gllrdggmlv gllapafdpd liqalagrpi talsmdavpr
      121 israqsldvl ssmaniagyr avieaahafg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdvrpev adqiaslgge yvgvpadepq pgggtgyasv tsedynaraa
      241 vmyaeqardv divittalip graaprllsa emvasmkpgs vvvdmaaaqg gnvegsvadq
      301 vvttangvti igytdlpgrl paqasqlygt nlvnlvkllt pgkdgrlvld lddvvlramt
      361 vvregevlwp ppsvavsaap ataappppap lvrhekpams agrrsalvgl aaallflata
      421 fapnqlvgnl tvfalavvvg fyvighvhha lhtplmsvtn aisgiivvga llqlghisga
      481 vtvlafiavl lasinvfggf avtrrmlgmf trgpartavs aptagahr
//
LOCUS       WP_091946351             435 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium sp. YR620].
ACCESSION   WP_091946351
VERSION     WP_091946351.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sp. YR620
  ORGANISM  Phyllobacterium sp. YR620
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Phyllobacterium sp. YR620"
                     /db_xref="taxon:1881066"
     Protein         1..435
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45038
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke tdanearvgg spetvkrlig lgfnvvvetg agtasripda eftgagasig
       61 kaadvkdadi vlkvrrpasp elksykkgav viamldpygn dsavkelada gltaftmefm
      121 pritraqvmd vlssqanlag yqavidaaee ydralpmmmt aagtvpaakv fvmgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaalvndhi akqdivitta lipgrpaprl vtremyarmr pgsvlidlav erggnvegav
      301 agkiteidgv kivghlnvpg riaatasqly aknlvafvet lvdkeakvlk infddelvka
      361 tmlthdgkvv hpnfaqaaaa vaapaetpaa kpvakkaapa kpaalkdaav kpaakkaapk
      421 kaaaskaapk tegea
//
LOCUS       WP_091946454             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylorubrum salsuginis].
ACCESSION   WP_091946454
VERSION     WP_091946454.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum salsuginis
  ORGANISM  Methylorubrum salsuginis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylorubrum.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Methylorubrum salsuginis"
                     /db_xref="taxon:414703"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39261
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrisvltead paeprvasvp etvkkfvglg gevvvqsgag anagvpdsey eaagakiags
       61 aeealsgadl vlkvrrpnae elgkigkgat vvaimdpygh edalkamada gvnafamelm
      121 pritraqvmd vlssqanlag yravidgaae ygrslpmmmt aagtvpaari fimgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedee fksaetsggy akemsaeyqk
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 ageivtvgng vkivghtnvp grlaatasal yarnlyafve tlidkesksl avkwddelvk
      361 atnltrdgqv vhpnfqpka
//
LOCUS       WP_091952244            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. Hel1_33_78].
ACCESSION   WP_091952244
VERSION     WP_091952244.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. Hel1_33_78
  ORGANISM  Polaribacter sp. Hel1_33_78
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Polaribacter sp. Hel1_33_78"
                     /db_xref="taxon:1336804"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111227
     Region          25..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiytilia vfsivftlnv qaqektisgt vtsksdastl pgvsvvvqgt tkgtetdfdg
       61 kytikasvge klsfsylgmk tqtvfigass tinivledda dqldeivvta lgikksrktl
      121 tysaqdvkgd dltrvkqtnp inslsgksag ltitrsssgv ggatkvvlrg nsstsnndpl
      181 yvidgvpmqn ngngqngetp ganifgsqtg nrdggditsl inpddvesmt ilkgasaaal
      241 ygsqgangvi littksgkeg kikvnfnstl tidnvvslpk lqteyqslsv ggaisengrv
      301 tdpkswggkt sglsntvddf fntgqtltns fslsagnkia qtylsfants akgvmpgnrl
      361 nrnvlnvret asllddkitv sanislsdqr iwnrptsgly snpltglyln pvgidlniyk
      421 nnfeyfntst nmmdqyatsf deniqqnpyw ltnrntskdg tqrvmasisa kyqinedlsi
      481 qsrgsfdksf fsfdkqlyag sdltfvpatg ryinektent qqyldfiany skdisedfnv
      541 gvilgssltk ykigdqtlld sgpeglrfpn eftianfnss ngiaqsvsnr evqsvfgaan
      601 fgyknmlfld vtgrtdwsst lvntnsssff ypsigltnvl temfempesv sfakvrvsya
      661 evgkdipvga tiplrtigtt nsggtigsan qasfaprege tlepekqksf eigtewrffg
      721 srlgvdltyy nsktenqiff iaaqpnvqgy tqnivnagki snsgielvin gkpivndnfk
      781 wnsslnyasn knkvisvhps ldngeailta pgvngygfsl iegedfgsir gksvirnsng
      841 lpvvnddgag nltieatefe tiahaqpdyt lgwsntfdfk nfsvnflidg kfggevvsvt
      901 eaindfygvs qasadarnng midvvtttgs atqmsaqdyf tktggragll geyvysatnv
      961 slrelsvayt lpkvskyfes vklsliannl fflykdapfd pniasstgig lqgvdiygqp
     1021 strsiglnmn inf
//
LOCUS       WP_091955787            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. Hel1_33_78].
ACCESSION   WP_091955787
VERSION     WP_091955787.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. Hel1_33_78
  ORGANISM  Polaribacter sp. Hel1_33_78
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Polaribacter sp. Hel1_33_78"
                     /db_xref="taxon:1336804"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116627
     Region          25..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lllafvvqis faqektvtgt vsddsgplpg vsilvkgttr gtdtnfdgky
       61 sikaktgdvl tfrylgyeti nktvgssnvi dvslkeggqi leeivitaqg ikrekkalgy
      121 avaevgsedi eqraegdvar ilsgkasgvq itsqsgtsgs atnvvirgys singsnqalf
      181 vvdgvpfssd tnaqgnflng nvgssrfldl dpnniasvsv lkglaaatly gtagrngviv
      241 ittkagsass gkkkkneiti nqsffvndia svpdyqdqyg ggfdqsfgwf fsnwgpsfna
      301 dgvdgynndp agtiqpdgtv ehpygssafl nnflggnnil nnqftgerye wkpynsvenf
      361 frsgsvqnls vnfngssdsg dvtynanfgh ldeegftpgn rvgrttlslg graklsnkft
      421 vsgsmnysqn kvvsppvaas rgngtlgwst fgnvfftprn vdlmglpfel penggsiyyr
      481 ngndiinplw siknaqngqv tnrvftsatl syeitenlgv syragidfyn ernkaysnkn
      541 gvnfnnaifg fldtydnnvs ifdhylafng sydlsedfsl sfvaggtsrs rtfdqqgvss
      601 tgqivfgvlq hfnfenqtpi qftskrnivg vfgetaidfr nyayvtlsgr ndwvsnlpte
      661 nnslfypsis gsfiptaafe glksdsgkgl nylkvraglg qsagfpsgyp tintvsqstq
      721 vnaggfgpit tnsvsdfqan pnlkpelise ievgfdarfl dnridvsfsy fdrttkdliv
      781 tkplaptsgf tstqanvgkv egsgvevdlg ldifkndgdg fnwnsrvnft qseqivteqe
      841 ddqilyagsa sanlganaai kgeqlgvivg trirrndage flvgsngsyl sesnvvlpdg
      901 rsitpiignp npdyvmnlnn tlsyknftfs fqinhtkggd iasstiatll grglingdrn
      961 ktfilpgile stgeantlqi nnsqyyfsnl lfgpkeltiy dasvlrlqev slgyslpqsa
     1021 ldktpfgavs ftfsgfnlwy dayntpdaan fdpnvagvgv gngrgfdyln gpsskrygfs
     1081 vklsf
//
LOCUS       WP_091953452            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. Hel1_33_78].
ACCESSION   WP_091953452
VERSION     WP_091953452.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. Hel1_33_78
  ORGANISM  Polaribacter sp. Hel1_33_78
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Polaribacter sp. Hel1_33_78"
                     /db_xref="taxon:1336804"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119700
     Region          24..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meklklslil lffpliifsq kniikgkitd ktgepllgvs illkdsqigt tsdldgnysi
       61 ntkektegvl ifnylgfavk nvnftkntkd ltvvliesae qleeivvtal gikrdkksls
      121 ystqgvnted mtearssnfl nalsgkaagv qitnsstptg strviirglt sitgnnqply
      181 ildgvpldss sgdagvsvwd egddidlgsp isginpddid siqilkgana salygsrasn
      241 gvviittkka kkgtskinvn vnsnlsivsn reypnyqysy gagnggrlvq ntgqldpttg
      301 lpmvgsynra ygapflgqqv ldyngtvgty apdinnvkdl yqtgvvntnt fsisratdkn
      361 tlrfsygkti gdhvikrmee inrdnialrm sqnitdklta nvsfiythqk vnnrmyqngs
      421 nrnpannymy mlpnmsqsnl lpyinennea fqyegdfnnp ywnifensnq ditnrvvani
      481 tlnwtilkgl klktringai nnvdrqefnn kgadydpngl yrevnisren wnyeailnyt
      541 kkfndlslvs ligvnrfdvr tdgnrltais lverdimsls ngdefapeif innnkrinsv
      601 ygsvslgyqk tyfldftarn dwastlpasn nsyfypsvgg tilfsefipr ndiltfgkir
      661 asyaqvgndt gfnqirnsyv qggnynntdw valerirknl elkpeltsst efgieakffn
      721 nrisfdgtyy ksstnnqiin vsttptsgfv gkflnageiq negmelflsa klfdkkfkws
      781 tdinwsknes fvaslfdgve srlvrswfnv gvfaevgepf gnirgnsqlv dpetgtplvl
      841 angraawesn qllgnaqpdw igsirnsfsy kgfslnflvd vkmggdlysg tmaktynhgv
      901 hagtlegree wllstlilge nnnerqgrgl fgnnyadsdr pkgriyensa lgvqdadgnw
      961 aaerdangei iytqrwlnpq vygfdglqdq rrfvydasyv klrevtfgyn iphrlikkik
     1021 iknakisvvg rnlwtiyrnt pqgidpesgt tsgngqgiey gsflptrtfg vnvklvf
//
LOCUS       WP_091956445             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Bradyrhizobium].
ACCESSION   WP_091956445
VERSION     WP_091956445.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39307
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pleprvaasp dtvkkfkalg aeiaiepgag lksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygneaa lktiadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake msreyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegakpge
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkeqklavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_091960060            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            tc2-28].
ACCESSION   WP_091960060
VERSION     WP_091960060.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. tc2-28
  ORGANISM  Prevotella sp. tc2-28
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Prevotella sp. tc2-28"
                     /db_xref="taxon:1761888"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118770
     Region          42..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqnnrkiac lvaigtlmlp aavlsakaap avgvqsvqqa akvfgtvtdg kdpvigasir
       61 vkngnqgtit dmdgnfkldv apgteliisy vgykditika sanmnivlee estalnevvv
      121 talgikrerk algyalsevk geeltkaket nvinslsgkv aglvvqntag gasgstrvll
      181 rgntemtgnn qplyvidgvp ldntnfanag qsggydlgdg isainpddie nmtvlkgpaa
      241 salygsrash gvilittkka ekdkvsveyn gsltfdsqla kwdniqqtyg mgytgtsirt
      301 atsgtnsswg tkaddflvey fdhekrpflm ypnntsgffr tglttqntai lsvnsgktgv
      361 rfsvtdmrnk dilpnthmsr dnfnlrvtta agpvdldfta nytredvknr palgdsqsni
      421 gknlmslast ynqewlkhyq nedgsyanwn gndqynknpy wdlyknents akdvfrltak
      481 aiwnisdhlk lqgtigtdmn fmnfeefism ttpgkmagql qnqkfnnrtl naeilalynn
      541 tfgdfdvnat lggnifkvsn ktdiftgmdq qmkdvvaimn yaeqsiqqnt ykkqinslyg
      601 sasvgykhty ylegtirgdk sstlptsnni yvypsvsssi vfsefiknks iinygkiras
      661 faqvgsdtdp yqlalnysta kysypgnvig minntvipnk dlkptrtnsf elglemkffh
      721 grlgldvtyy nqlskdqiir latsstsgyt yslvnageiq nkgieialng ralqigdfaw
      781 daginfsknr nkvnslvdgm nyfelekasw cgvsvgaevg kdygsitgkd fkrtddgqfi
      841 inastglpev dektrtlgna swdwtggfys tftyknfrls agfdvkvgad lfsmsmrqay
      901 esgkanetle greayyqsee rrkqlnlskd ewdsnirtal saeqdaqkrv emgrqygyvv
      961 pgvidngdgt ytpnyipvnp enywqsaarn cpslfiydns yvkcreitfg ytfpekllsk
     1021 lkvvkdlsis fvarnpfiiw knipnidpds gyntsglgle ygslpsrrsy gfnvnvkf
//
LOCUS       WP_091961074             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            tc2-28].
ACCESSION   WP_091961074
VERSION     WP_091961074.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. tc2-28
  ORGANISM  Prevotella sp. tc2-28
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Prevotella sp. tc2-28"
                     /db_xref="taxon:1761888"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107754
     Region          29..977
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meqrkvffrr mlslaaamlf tltisaqsti sghvkddtge diigasvvvk gtqggtvtdf
       61 dgnfkvqckp gttlvityvg fvpqevkaqd gmditlkedv aqlnevvvvg ygslakkeis
      121 ssvvqinkdq fnqgaasdpm alvagkvagl nvstsadanp namtdiqvrg agslsasngp
      181 lvvidgiagg dlrniatqdv esitvlkdag saaiygtrga ngvilvttkk gsgtagvtnv
      241 tydsyialnf qkgkpdilst deyrrsrrgp dygadtdwwk eitrsasynl nqyisidsst
      301 kngyfgasvn ykkgngldiv snreeyggrf vmeqrvlqny vqfnaslsgr kvheewgndg
      361 lfdtalttnp tipvknadgs yfqassptgv hnpvndlren vsqgdriyll gnadvkvnil
      421 qleqhnlnts lsyalqyndl kdnfytptks sesywngyag rarinyqkww tnrlewlvny
      481 tmtmgkhqlk avlgyswern kweqsgnenm gfvydalsyh gigsgsylkd gkanlwagss
      541 estligffgr lnynyndiif asasmrregs tkfgtntkwg sfpsgslawe itntpfaesv
      601 gaffqslkpr vsygvtgrsd fdaykslaty styssyyidn qwlngyapsl nanpdlawek
      661 stafnvgidf valnsrlrgs veyfdrrskd llynytapqp pfiyntilvn vgttkntgle
      721 vsidydvlak kdlkwttgin wstgdtkltk lssdvyqmay lnlyqkpgpg ssefffrvee
      781 ggkigqfygy ehagvdengg llvydndgna qaaasadpaw krnigngapk hflswtnsfr
      841 yknwdlstlf rgafghkifn mrkygmglrg agtenvlrta ytddadvfss ggiitsyfle
      901 ngnyfkldnv tvgysfvpkk relieslrvy ltaknlftlt aykgndpsiv tstgitpgid
      961 snsaypqatn ftlgvtvrfh
//
LOCUS       WP_091963659             941 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            tc2-28].
ACCESSION   WP_091963659
VERSION     WP_091963659.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. tc2-28
  ORGANISM  Prevotella sp. tc2-28
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 941)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Prevotella sp. tc2-28"
                     /db_xref="taxon:1761888"
     Protein         1..941
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105571
     Region          36..939
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnivkyigi lplslfalfs qgvmaqeaae adtinvafrq sdardvivpv stvnvkdlle
       61 knyntysldn mqalvagyng qlwnqgdalv mvdgvprdan nvlpteieni tfmkgasavv
      121 lygsraakgv ilittkrgki apmkitarad yqldaakafp kyidgaqymt lynqalkndg
      181 laakyteedi yntalganpy rypnqqfyns dyvkrtrsrw dvtaefeggg kfaqfytnis
      241 yyrigdfinf gegkdnftdr lnvrgnidlr ladwatgwvn anatyynqrn snsdfwgaas
      301 tlrptrvapf vpvsyldpdd answalinnt kniivdpagl pagryffgat pddrtnafad
      361 mygagyntwt srqmqfdmga kfdlasilkg ltfktmfavd ystsystain dkydsfrvnw
      421 tqydgkdvvg tldgmseykh tgtlessnsa ekqtiawngq fdyvnafgah nlhatlvang
      481 yqqtisgeyh kvsnanlglq vsynyahkyy adlagnvvhs aklekghrea fspsitlgwr
      541 ltgeefmknv nwlndlrlta gytvlnqdld iesfymykgi ftatgtwwgw sdannsiqts
      601 dsqrgsneel sfikrkeftv glngamfdnk ikfavnyfnt ttdgllaqpd yiypsymhty
      661 wpvstfipyi nygknrrqgm dfsvmyndkf gdvdfgaqif gqtttsknlt vaenveydyl
      721 rregkytdgl wglqclgyyn sneeitgada kssfgevkpg dlkyvdqngd gtidskdeve
      781 lgrwsakftg glnltvkykn ftlftmltgq fggnalkndt ynwvfgerky sdvvlgawta
      841 ekyangeais yprlttqggd nnfrasdywm ystnrvdlqr vqltydfdkk ifgansivkg
      901 lqvyvngssl ltiakereql ernvgsapqt rsftlgakvq f
//
LOCUS       WP_091969675             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Propionibacterium cyclohexanicum].
ACCESSION   WP_091969675
VERSION     WP_091969675.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium cyclohexanicum
  ORGANISM  Propionibacterium cyclohexanicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Propionibacterium cyclohexanicum"
                     /db_xref="taxon:64702"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53632
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresl pgerrvaatp ktvpqllklg yevavergag araalpdaey eaagaelvdt
       61 vtawgadivl avnepsveel aamhagatli tflhprenpg lvealqragv tgmsmdmvpr
      121 israqsmdal sstanisgyr aiveaayayg rtfggqvtaa gkvapakvfv igtgvaglaa
      181 lgaansmgae vyatdvrpet aeqvesmgat flnvraagde qavssdgyak qttddynkra
      241 gelyaeqcpk vdvivttaai pgrpspklit aemvasmkpg svivdlaalg ggncvltrpg
      301 ekyttdngvt iigytdmpsr lpgqasqlys tnlvnllkla tpgkdgqlvv dfddevlrnm
      361 tvakdgqitf ppppiqvsaa pavkpaavad rqpeavkppr pwyvsfavvg vlaialiall
      421 tfapasfisl fsvfavavvv gyyvvwnvth alhtplmsvt naisgiiivg amlqlpkdnp
      481 aimiiaalgv liasinvfgg fsvtrrmlnm frka
//
LOCUS       WP_091972279             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium gossipiicola].
ACCESSION   WP_091972279
VERSION     WP_091972279.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium gossipiicola
  ORGANISM  Methylobacterium gossipiicola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Methylobacterium gossipiicola"
                     /db_xref="taxon:582675"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39019
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavltesd paeprvaavp etikkfvglg agvtvqsgag lkagvpdady eaagatlags
       61 aaeaagdadl vlkvrrptad eigllkrgat vvaimdpygn qealgalaqa gidtfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrampmmmt aagtvpaarv fvmgvgvagl
      181 qaiatarrmg avvtatdvrp atkeqveslg akfvavedde fkqaetsggy akemsaeykk
      241 kqadlvaahi akqdivitta lipgrpapql vsqamvasmk pgsvlidlav erggnvegak
      301 ageivttdhg vkivghlnva grlaatassl yarnlyafve tlidketksl avkrddelvk
      361 atnlthggav vhpafqtqs
//
LOCUS       WP_091976525             409 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Methylobacterium].
ACCESSION   WP_091976525
VERSION     WP_091976525.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium
  ORGANISM  Methylobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Methylobacterium"
                     /db_xref="taxon:407"
     Protein         1..409
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42036
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd saeprvaavp etvkkfktlg advvvqsgag qkagildsey eaagasiags
       61 aadaagdadl vlkvrrpsae elpqlkrgat viaimdpygn edalkamaea gidgfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrampmmmt aagtvpaarv fvmgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsaeyqk
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 agevvtndrg vkivghvnvp grlaatsssl yarnlyafve tlidkeskal ainwddelvk
      361 atnltrdgsv vhasfqpktd gaaseaasvg lakseaskas gaatpagaq
//
LOCUS       WP_091989035             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter gudaonensis].
ACCESSION   WP_091989035
VERSION     WP_091989035.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter gudaonensis
  ORGANISM  Marinobacter gudaonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter gudaonensis"
                     /db_xref="taxon:375760"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55656
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipreif egerrvaatp psvhkliglg ydvvveggag epanysdaay ekvgasiaad
       61 ttslwqeadf ilkvrapmen palgkheadl mkegaflvsy iwpaqnpell eklagrnits
      121 faidslpris raqkmdalsa maniagyrav ieaanhfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig aansmgavvr afdtrlevre qvesmgaqfl vldfegedgs gtggyakqms
      241 defikaemel faeqakevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgkva hqhgvtligy tdlpsrmakv asdlyatnlv hllteltpek dgkpvvnmed
      361 dvirgltvvh ekditwpppk peapvspkpa pgteepsaea kaaakkkadq rsvigksall
      421 vvtalalygv gayapesflq hftvfvlscf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gailhlaqag siavgvmafl avliasinvg ggfrvthrml kmfrk
//
LOCUS       WP_091993163             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia lycopersici].
ACCESSION   WP_091993163
VERSION     WP_091993163.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia lycopersici
  ORGANISM  Paraburkholderia lycopersici
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia lycopersici"
                     /db_xref="taxon:416944"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39566
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anetrvaatp etvrkyvaqg htvtiqagag agasypdeay aavgaqvada
       61 asafgadlvl kvqsptvsel pfmkrgavlv gmldpfnaen aaklaeagvt afaleaapra
      121 traqsldvls sqaniagyka vlvasnlypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atarrlgavi easdvrpavk eqieslggkf levpyetdee reaavgvggy arpmppswla
      241 rqaalvhera rqadivista lipgrdaptl lpsetvqamk pgsvvidlaa grgpvadqat
      301 grrggncplt eadkvvthhg vqicgytnla smvaadasal yarnlldflk livtkegtln
      361 idladdivaa tllardgqvt rka
//
LOCUS       WP_091998169             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter pelagius].
ACCESSION   WP_091998169
VERSION     WP_091998169.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter pelagius
  ORGANISM  Marinobacter pelagius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter pelagius"
                     /db_xref="taxon:379482"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55832
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipreif ederrvaatp psvhkliglg yeviveggag eaanysdaay ekvgaaiaad
       61 tgslwkesdf ilkvrapmen palgkheadl mkegaflvsy iwpaqnpell eklaarkits
      121 faidslpris raqkmdalsa maniagyrav ieaanhfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig aansmgaivr afdtrlevke qvesmgaefl vldfenedgs gsggyakqms
      241 defikaemal faeqakevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgkva hhhgvtligy tdlpsrmakv asdlyatnlv hllteltpek dgkplvnmed
      361 evirgltvvh edditwpppk pespvspkpa pgteepsaea kaaakkeadr rsligkgalf
      421 vvtalalygv gahapesflq hftvfvlacf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gailhlaqse niavgimafv avliasinvg ggfrvthrml kmfrk
//
LOCUS       WP_092005270             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polaromonas sp. OV174].
ACCESSION   WP_092005270
VERSION     WP_092005270.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. OV174
  ORGANISM  Polaromonas sp. OV174
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Polaromonas sp. OV174"
                     /db_xref="taxon:1855300"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38390
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeit agetrvamtp etakklksqg htvrvqsgag vaasvtdeay aavgveitda
       61 agayaadivl kvrcpldsem alarsggvlv gmlnpfdasg lqrlaaaqlt sfaleaaprt
      121 sraqsmdvls sqaniagyka vmmaaekyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvayetdee reaavgvggy akpmpaswle
      241 rqkaevakrv aqadvvitta lipgraapvl vteemvksmk pgsvivdlaa pqggncplte
      301 pgktvikngv tligetnlpa lvaadasaly arnlldflkl iiskdgalti dleddivaac
      361 lmtqngevkk k
//
LOCUS       WP_092010773            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092010773
VERSION     WP_092010773.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122557
     Region          30..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktftrffa lsalimilsg imsatyaqvr tlkgkvvstd gtqlpginil vkgttrgtss
       61 dvngnyslsi tndntiltfq sigfasqeik vgnrnsldvi lapddkqlee vvvtalgikk
      121 etrtigyttq dvkgselvka repnplnsla gkiagltvgp saellgrpqi ilrgnsdilf
      181 vvdgvpvnsd twnisaddie tytvlkgpna aalygfrgqn gailvttkkg tkdkrkfsvd
      241 fnsstmvetg flaipkrqse ygygvnyqya ygnkpydedg kfrrtniwgp rfegqnvpqy
      301 dspvdpvtgi rqgtpwlakg annfqnfmem gvistnnvsl aasgekydlr msisnnyqkg
      361 mapntklnit nfnissgynf tdrlklegnl nlnlqnspni pdassgpegy tyifqvygss
      421 swdindmrdy ykgptgkpgv qqyyaeygre nnpyfmayew lrehqktdiy gyaklsykin
      481 dflnfsartq vttwnqlrte klpysmityk spdlrqgdyr edrrdlfenn tdvllnfnkd
      541 itknfhisai aggnlrtfry nsnlsttdfl ivpgvydfsn skfpvkaynf rsdmevasay
      601 ytadfsyknf ltlgttgrid qlstlpkenr sifypsvsvs tvvsdyinlp eavsfmklra
      661 syanvkgglt sstigtayka vtgsnlsgli gygsevttsy dgpsytnqnt ynisnlynnt
      721 psanysgtla nrslqsysvt syeagldmkf lknrlgldvt yftsingpqi fpldiasstg
      781 yysqtvngvt sqkngweisl sgsvikntng fnwdvlanws tyketlkdiy hgetsiylag
      841 pdhvfkigdr ldgyygykfl rspdgqiins stgvplnapt gtnnkqllgy tnpdfvigvn
      901 nkfsyknlsf sfqldgrvgg viydnvyaya lnagnqielt egaygaarlk ewqstklgtv
      961 aatpayvgqg vvitdgtpkf datgnisnyn elkfapngka vtvqtyaqsv ynntideayl
     1021 tsksflklre iiigytipsr flnnnkfiks asvsivgrnl lyfaertdfd ldqypsgyns
     1081 sdrstlknpg lqsattrrfg mninltf
//
LOCUS       WP_092011112             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter daqiaonensis].
ACCESSION   WP_092011112
VERSION     WP_092011112.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter daqiaonensis
  ORGANISM  Marinobacter daqiaonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Marinobacter daqiaonensis"
                     /db_xref="taxon:650891"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41478
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mmigipreka agenrvaiip pgvtqllesg yevivesgag lgahftdeey rhcgaiiadd
       61 aeslyrqsqv ilkvlapepd eaaliqpest licllnpwfn rplleqladr svqafsldlv
      121 prttraqsmd vlsamagisg yravlngama lpryfpmlmt aagtihparv lvigagvagl
      181 maiatarrlg avveaydlrp evkeqvnslg adfieievpp ptasgsdgya kaqnaefyaa
      241 qrqqlaecva radlvvttaa vpgkpapkli drdmihrmks gsvivdlaad rggnvegtvl
      301 nrkvdldgvt vvghanhpsr vpvhasqllt rnitafllnm tregaldpdp eddivaatrv
      361 ihegrilhdq epagtvkaek tetdvevna
//
LOCUS       WP_092010862            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092010862
VERSION     WP_092010862.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122366
     Region          141..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkmnqdsqrl lliimkvtli qfcmvvlfts lvmgrdahaq evlnqqitlk aensdiksil
       61 slverqvdvk fmysaeviqs krkvsisakn erlsellmkl ltplkisfev nkkrilltss
      121 eipsveales rslaetesal itvsgtvinn kgegipgvti rekdtntgav tdvngkftis
      181 vrneqsvlif tsigykpsei qvskqkiinl tlsddntqln eivvigygtq kkseltsava
      241 tvksenfikg avtdagqllq gkvagltigs psgdptstsq ivlrgissin sstdplvlid
      301 gipgglntva pediesidvl kdgsaaaiyg trgtngvili ttrrangnie psieyngyvs
      361 tqtiarkpem fsasdyrnli kqgvpfedlg sdtdwlkatt rtplihvhnl tlrggnsrtn
      421 ylanvnyrsf egifqksdnr tltgrldvnh nmfdgklkln infintnnay tttgdgvsfn
      481 ggayrqalir nptspiknpd gswfeqpgiy vyenplarly esdgentsqn trlagslsfl
      541 pvnglemkal fsqnrfnqir gysetknhis tirdtkngya srgttqntdg lieltaeyrk
      601 tmddhkfsal agysyqdfls edywmqnwdf ptdkftynni gtgnalkkgl apiysnklas
      661 nligffgrvt ysyadkyill aslrheassk llgaiepwgn fpavsvgwki nkesflsnak
      721 gidelklrag ygvtgtvpga sflgvsrlgy sgnflvngqw vqnlapinnp npylrweekh
      781 etnvgvdfsf lksrvsgsld fynrrtngli ydypvptppn lypfttanvg vmenkgievm
      841 vnvavvrskd fdwnasfnys tnanklvsls ndqykttndf fttgytgepi qtythrvqvg
      901 ekignfygyk vvdvtddgkw iyetktgers tdkggeenkk ilgnglpafy agwnnnfryk
      961 nfdlsitmrg afdyqilnfq rmyyenpgit qynqlktaqd kvfgkavlnk ntpleynsyy
     1021 iengdfwkid nitlgynfth pifkvikrar lyvavlnslt itgykgidpe vnrgglspgn
     1081 ddrdkyptvr tftfgmnlnf
//
LOCUS       WP_092012653            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092012653
VERSION     WP_092012653.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117897
     Region          23..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkflfnlll lmalvgqaia qdrqvtgkvv ssddssplpg vsvtlkgttk gtntdaqghy
       61 kisvpsggtl vfsfvgfkkq siavgsqnsv dvkleadvaa leevvvtaln qsrdkrslgs
      121 ssqsvstekl natrntnvad alagkvsgvq vfgqsgakfg tptirirgin sltgadplyv
      181 vdgtptdiny vnmddvesin vlkgpsatal ygnrasggvi vittkkgtkq dgvgievnhs
      241 ttfdqvsllp tyqneygggy sqdygifkfn pavhpaswaa fngqkildys adeswgpkmd
      301 gtlyrpwysw ipsdpdfgkq vplspnpnnv rdffntgvti nnniafskrg dnysfrvsyt
      361 nitadgiipn snqkrdylsv kvkndlskkf smnlnlnyan ertlnrpadg ysgsnqtvgs
      421 fnqwfqrqld mtqlknyrnp dgtyrswnit gpenttplyw dnpytqvyen nstvrndkif
      481 gdlgltyklt dflsasvvar kdinnynfds kiasgtkrla nytigsvfav ednyegllsf
      541 nkkfgditvn angggnirqn slnfisesta gglatpdlyn ignsigrptt vnfmskrevr
      601 svygsasidy kdmiyleata rndwsstlpk annsyfypsa slsfiftelm dnrrvlsfgk
      661 irgsvaqvgs digpyqinpt flainpaetg tgttiagnpt qynparlpnt nlkpglstsy
      721 eggfdlkffq nrlglevsvy ttdnvnqivp lsvpsssgyt salinagnir ssgvelhlna
      781 mavksrdfsw eidvnvdknr skvieladnl kayrldniga tygnqgaqss pfagvpifgg
      841 sgltlvareg sdwgvivgkk irtyqaldaa gnkidspsng krmvgpdgfy lydagqdias
      901 vlpdfkggvf ntfkykaftl kvmfdfvvgg kfysttrmfn agsglseqta glndrgkpkr
      961 ddpstgggvr lddavkadgs pndiyvdaqt lyetklfdln eywtydktyv kmreinlgys
     1021 lpglllrktp fktasiaflv rnpfliyskv gggvdpsets smwgeggqlp pvrsygvnlk
     1081 fsf
//
LOCUS       WP_092012658            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092012658
VERSION     WP_092012658.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118552
     Region          23..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilfnfll litlvgqama qdrqvtgkvv saddssplpg vsislkgtsk gtnsdasgnf
       61 kisvpsgstl vfsfvgfkkq svlvgsqtsi sikleadvas ldevvvtalg ltrekkslgy
      121 atqeikgdav ntakesnfln slsgkvsgve irrnnnlgas tnivvrgfks lsgnnqalfv
      181 vdgvpidntn tnsldtqngr ggydfgnaaa dinpddieti nvlkgaaata lygsraangv
      241 vmvttkkgrk nkgigvtvsa gytvgsidrs tfpkyqnqyg ggygnyyesp dkkflyrdin
      301 gdgvndlvvp tsedasygaa fdpskmvydw tafdptspny gkarpwvaak ndysaffnds
      361 ktfngsvald ggnengnyrv sytrfdqtgi lpnsslqkns fsfggsydfs kkltattnin
      421 fvrqdgkgry tngyndnims sarqwnqrnv dilelrdayd rtgknitwnw adptdlkpiy
      481 wdnpyfqryn nyetdwrnrl fgnaalnykf sdffdvlgrv smdsytelqe ervavgsinn
      541 ngtarygrfd htfseinydl ianfhkdine nfnlkglvga nvrrtkddri rastqggliv
      601 pglyslgnsa saisapvedf yelyqdgifa saslgykdml fldatarrdr sstlpasnna
      661 yfypsvsgsf ifsnamanns wlsfgkirvn yaevgntapp lsivntyikp tnlnsdnrds
      721 fngqplfqvn atlnnpnlkp ertkstevgl emkflknrlg fdlalyktls vdqilpvsvs
      781 katgydrkyv nagtienkgi elalngtpiq tknvtwkttv nftmnrnkvl elydgvdnlq
      841 igsfqqgvtl natvgqpygv lkgtdfvfnd kgqkvialda egnntgyyar tgadnnigni
      901 npdwkmgisn avsykdfsfs flidiqkggn vfsldqaygl atglypetvf lndkgnpvrs
      961 siasgggyiv pgvlpdgsan tkrvsaenyg lfgyvrnpns afiydasyvk lrevaisykl
     1021 pvslfggesg vvknatlsiv grnlwiihkn lpyadpedgl ssgniqgfqs gvypavreig
     1081 aslkfsf
//
LOCUS       WP_092014410             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter daqiaonensis].
ACCESSION   WP_092014410
VERSION     WP_092014410.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter daqiaonensis
  ORGANISM  Marinobacter daqiaonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Marinobacter daqiaonensis"
                     /db_xref="taxon:650891"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55642
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mnigipkeif qderrvaatp asvqklvklg ydvvvetgag efanypdeay keagaaiavd
       61 tvslwgeadi ilkvrapmeh pgtgrheldm mkegaflagy iwpaqnpell eklakrkita
      121 faidalpris raqkmdalsa maniagyrav ieaanqfgrf ftgqvtaagk vppakvlvig
      181 agvaglaaig tansmgavvr afdtrlevke qvssmgaefl eldfgdeegs ggggyakqms
      241 defikaemal faeqakevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgkva ehhgvkligy tdlpsrmakv asdlyatnlv hlmteltpek dgqpsvnmdd
      361 avirgltvsh qenvtwpppk peepaiktpa pgteepskak akpepsprrk lagklallav
      421 tvlalygvga yapesflshf tvfvlacfig wqviwnvtas lhtplmsvtn aisgiiviga
      481 llhlaqaena avgvlsfiav liaminvsgg frvthrmlkm fhr
//
LOCUS       WP_092014692            1144 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092014692
VERSION     WP_092014692.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1144
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126259
     Region          47..114
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          140..1143
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkcsislilk ntgsmiragi ilfllsrdfs iysqipgsae evkltvrfen rpvlevfkel
       61 ekktgfrfty ndaylneklk vslraenkni qeilsylske tnlafkiikk hihvmafedl
      121 lssgsepdpk nfsfriegmi tgtdtgepvf gatvaikgst rgtvsnekga fvldadnena
      181 illissigfv kkelkigkkt kvqitlqpdi ipleevvvig ygtqkkkdlt gaistidper
      241 iikiatndvt kamqgqiagv svhgsgepgm npqvivrgig sfnstsplyi idgvqapigd
      301 lpvsdiesvq vlkdasaaai ygsraangvi iittkrgksg kmkvdysfyh gwqniakrle
      361 vanreeyqml vneasanaep alakkpands dsplfvnnid tdwqkeafkt gkiqehtlgv
      421 sggnetvtyn vslnyfdhtg tivgsgpgyt ryglrvntdf khqrfkfges lgftgvdqnf
      481 mtfvhdgtpl gyivgaiptl pvydnttkng fgsasqtihg sytanaigfn stlqsktdrn
      541 rligniygey ailedlkfrl slgyertdwr dfnfqpkydf gwfyvnniak mndwrgygyt
      601 gtiegtlsyd kiigkniisa iagysvlqsa isrvqahaeg fsepyfpvls ngtsgisvtg
      661 yeeenrllsy fgrvnysfnd kylltatirr dassrfsrqn rwgtfpslal gwkmhnerfm
      721 kalpfisqfk lrasygllgn qeipsyqyea vinpyahavf gnqlapgatq lefatpdikw
      781 esreshnigl dagflgnkit ltveyyqnts kdmllrvrip estgvynwks pfvngasven
      841 sgwefqagyk ntsggltygf naylttlknk vlslgygdqp igdgitrtev ggevgalygw
      901 vtdglfqtqd eidqlnrksp igryqevltr pgdirfkdin grdangkltg kpdgkidddd
      961 rtflgsaipd vsfgisanla fkafdlsvma sgvsgnliyn glrasleygg gwdnyaknsl
     1021 nrwtpantdt evprvvmfdp nknnrasarw lekgdylrit tvqlgyslpk kvlsklkmsr
     1081 lrvyvsgqnl ltltgytgfd pdfgndglfn raidqglapn rnfnayaggl pnprsfmagv
     1141 qlgf
//
LOCUS       WP_092015279            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092015279
VERSION     WP_092015279.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115825
     Region          23..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilkfmlp vlflalqvna qsqkvigrit aksdgqpvvg aavlvkgtsr gtvtnaqgey
       61 tisaqtndvl rfsfvgfksf elkvpasgkl dvvfeneetv lnevvvtalg iakekkslgy
      121 avqelktkdl aearegnlvn alsgkiagvq itnsqggmgs srivirgets iagnnqplfv
      181 vdgipvdnsq lgvgttgsrd fanaisdinp adiesisvlk gpnaaalygs rasngvilik
      241 tksgksasqk glgvtlnlgy tadkllvlpe yqnvfgqgtg gqfsyvdgkg ggvndatdes
      301 wgpkmdgrli pqffsdgkpa pfvahpdnvk nffitghttn vglsvagsnd kidyrfsynn
      361 snqtgvipnt ditkntfgvn stfrlndklt lttsanfvrt gsdnlpgtsg rgnsvmlqfl
      421 wfgrqvdtel lkdynkggfd ynwnhsyysn pylqqyentv eqrrdrifgn vnlaykitdw
      481 ltanvrtgnd yytdkrkfkv aygtngtpfg sytedgyvvn enntdfnlsl hkglnkdfdl
      541 dwlvggnlrs nfneqnyqqa pklavsglyt lnnsrdplvs ynilrkqrvy safssaqlgf
      601 rnyaflnlta rndwsstlpa gnnsyfypsv nasivltdaf diksdvlsfa kirggwaevg
      661 kdtdpyqlin typfnlpfgs splltvsdvl lnsnlkpeit rstevgldva llknrvrvdl
      721 syyntdsynq ilkadvsptt gfkqkllnag hinnhgfeam vnftplqtes gfkwnvginy
      781 srnvskvisl ddqgflndyk lgtngslsvl askdkpygal fgtaylrnan gdivvnsngi
      841 pardpnlqvl gyytpkwmgg itnsfsykgf nlsvlidtkq ggsiysatna tgkytgvlie
      901 tlqgrdaehg glayyypnnn tsavpvqvin ntsapqgvtv yndgiivngv tadgkpntti
      961 vsaeryykgv ysnssginea svfdasfikl revklsyvip qklvnrfglq nltlsvygrn
     1021 laflqrkatn idpetafntg ntgqgleslq lpttstygvn lsvgf
//
LOCUS       WP_092016733            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092016733
VERSION     WP_092016733.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117975
     Region          24..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkfllmsll lifssclsvf aqdrkitgkv tsaedgsglp gvsvqlkgsn kgtttdatga
       61 yslsvpsgng vlkfsfvgms tkevsidgks vvdtkletda rqlsevvvtg vgvatskakl
      121 gfavesitsk nlpqaptasv dqalvgkiag aqissvsgtp gapvsivlrg intinkgtsp
      181 iilidgiqva stdlnsidln tiervevvqg aasatmygaq gangviqlft kkgkpgqlni
      241 dfsssvsrne ylnvgglrqa qyhafttdas gnvigasgkp ltqdpvtgly senvqynald
      301 pksqlnkpyn anlkfydnys fffvpaytyn nsvsvtggke kldfafslsn ntqgsnivnn
      361 gnysrtnlva nigaelaprl kfrsttqlvy tkntlktpdr tilysinntr pfanyqavls
      421 dgnyaayvgd aagvnglnpn fyqqytdrqd nrvdviqnln lnyevnkfle ldakyginyq
      481 rdedvyqyan qsqngnirvr ptnyvgnyas nalgeidnfs iskvfqnfla tatirtdfqk
      541 dfnlslpitt ttqvafdyrk qnnnqyvtyq lglptytpyt paqgtttltr pldfnsvtgn
      601 prgtfsepfv tygylvnqrf eygdiagvsg gfrtdyssaf gagskpftfp radgylrlsq
      661 ldfwkdsqis gtfsefklra aygqagiqpr pfdryvtlgt rnigsnsafy yptaqsnpdl
      721 nvevstetel gadfgfnlsk gsnwfndlrl satywkrstd gaiwnvdaap ssgagtiktn
      781 afgigsngiq asinatvfkk gdftwnttvn fskqssqidw vtgngeivil snagstnyvl
      841 kagekigqly gfkavhdlka rkpdgsyeip egdqskyeva sngfvvdktt kqpyfttdky
      901 sfgdpnpkfn lsfindftyk gfinfgfqfd wvngshiynq tkewmyrdgi hsdyekpiti
      961 ngetgawtaf yrgvytargn natkdyfyed asflrlrnvs igvdlakalh iktfrklqlv
     1021 fsgrnlltft gytgfdpeis sggsaavgep agnnsawdrg tdhntmpnir syqvslnfgf
//
LOCUS       WP_092017084            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092017084
VERSION     WP_092017084.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110624
     Region          27..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkaskftmfi tallflswqq iyaqqaikgk vsdsnqsglp gvnillkgts kgtisdasgn
       61 ysinatkgat lvfrslgyat kevvvgdqts idivletsdk tleevvvtal gvakdkkslg
      121 yavselkgte ftqarevnlg nalsgkiagv natstatgpg gssrviirgn gslggnnqpl
      181 yvingvpidn tnvnsagmwg gfdtgdglss inpddiesis vlkggasaal ygsragsgvi
      241 littksgkaq kglgvdftst ytaetplkis dwqyqygagt rgakpatqqe aidngvmswg
      301 akldgtsviq sdgvsrpyva qkdniknfyn vgstfsntva vsggnqtvnf rfsasnsdaq
      361 svvpnstfsr ksfnlstnan lsnkvvfesv mqyniengen rtflsdtpkn pnfaaqmlat
      421 stdirilapg vdsrgyeslw nsnvysqnpy fattkvkntd drnrfmgnfs lrynltdnly
      481 vrgrlgtdyn qlkywsiept giaystrgsl sqstrkivet naellvgfkk dfdqislnal
      541 iggnkmlrtn egqgisggqf nvpfnyfpsn litsnwnydy tklginslfa sadlgyknlv
      601 fltlsgrqdw fstlakenns lfypgaslgf vfsdamaerp swltygklrt swaqvggayp
      661 tpyalnltyg lqsnpyngmp lmnigtntip nkalqpnttt tteigvelkt lnnrlgidlt
      721 lynrvttnda vqastssasg yqavllnvgk vqnqgievll tgtpvkaasg fgwnvsynfa
      781 yndnkvikia dgltalsmde srtrngyvyn fegqpfgmia gyrakrdaag nivynkdtgl
      841 pmqgefaalg rgvppvtmgl tntfnyknfq lsflidakfg gmlysatnaf atryglaqrt
      901 vandvrttgv tvkgvdqnge aftktisaqd yfsgisttit defvykadfa klrqltfgyt
      961 fpksmlgktp iqslslsfva rnllmlynsv pnvdpestyn ngnaqglemf giptvrsfgl
     1021 nlmakf
//
LOCUS       WP_092017622            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092017622
VERSION     WP_092017622.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121051
     Region          26..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskftmfii sllflswqqv yaqqhvikgk vsdnnqsglp gvnilvkgtt kgttsdadgn
       61 ysisaskgav lvfssvgysn kevavkdqsv initldpsdq aldevvvtal gikketkalg
      121 yavstvsakd itasgntnfa salygkaagv kittapggat sgvnvqvrgi nslnyntqpl
      181 yvvdgivird fnqagaggln nggywsdqki rgngildinp adissltvlk gasatalygs
      241 eaangvivit tktgvkgkgl gvevnytyne ervaftpqyq nvygpgydra tnlqvganed
      301 gfiigsdgsk rvnyraygqf gpkmdgqmls wwdgtkqayt akpdnynqfy qtgynstmna
      361 afsnatdkas yrfsytgtdy qgimrgsslk rntfnlntsl klsdrvtadi ivsyvnstvh
      421 nrpeqinrvt anyggffsra edmnnflnry qtskgykyvm ladkqrnpde afkynirggd
      481 lmdllwnglk nsedevqdrl lssvtlnyki skefslrgrm gndftslgve tkkyneypil
      541 fngsnstgey rlqsgrysiv ygdamltynk slnkdldlta sggmqgrqek yydqsigtng
      601 glvienwfsm nnstnllsss anrkellkya yigtanlayk nmlffegtar kefsstlpak
      661 nnnyfyysfn sgfvfsdafq mpsflnygkv rasygvvgna pplyvantty sqtilqtgng
      721 avpalsanss ygndyirpeq kyesefglet klfnnklgfd ltyytsried qilqtdvpts
      781 igaasvltnv gelgsrgwev slystpvrtk dfswntrini annrttvhkl aaginqlvay
      841 nadggalkiv sdegdllgni ythtratdkn gnfiitddgl ykmttdykkv gnvmptvvgg
      901 flntfnykgf sldltvdyrl ggqlvsspll yatgagmfen tmqyrdeang glpyyvdnag
      961 kkvllsshsa aapngarvyh dgvlldgvte sgdkntrive aayyymnsfg wstgwyekga
     1021 vydnsfvkmr eavlsytipn kvaqklhlqn irvslvgrnl fyiwrtlknl dpeapigtsw
     1081 nrqgvdegss aatrsfgfsl hasf
//
LOCUS       WP_092017684            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092017684
VERSION     WP_092017684.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113990
     Region          27..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqklrllsv iwlllsslig yaqkqsisga iistedsspl pgvsvqikgt svgtttnseg
       61 kykisvakgd alifsfvgfv tqeikianqs einikletdt kvlgevvvta lgierdkkal
      121 gyalqavkgs divqaretnl vnalsgkiag iqvtssngtp gasarilirg insiggnnqp
      181 lfvvdgipid nttfnsasps atapnvtvdy gngasalnpd dvenisvlkg anaaalygsr
      241 aangvilitt ksgkgtkgig itvnsnitfe spfrlpdyqn sygqgaggkf eykdgkgggv
      301 ndgvdeswgp kldgrllpqy nspidangnr iatpwvanpd nvknfyetgv srsnnialsg
      361 gndkgefrls ytnldqkgml pntnytrntl alnaglhltn klsvkaavny indgsanrqn
      421 lllywtwfgr qadlqdlkny ldpvqdptnw avqrnwntny wnnpyfvlnn slfanskdri
      481 ignvsatykf ndwlsltgrt gtdfytdrrt tkrpkmvglv ngmywednyf vkeqntdfll
      541 afnkkvssdi sisanlggnq rtnliqrdyi easelsipnl fnlansktrp vvanslqkke
      601 vnslyasgqf swkdevfldv tarndwsstl paanrsyfyp svsasaivtd lfkmnsevlp
      661 yakvraswak vgndtdpyrl qqvysgasaw gstttfaenn tifnsalkpe ittalefgve
      721 arlwnrvnae ityyeknssn qilrigvpqs sgylnkyvna geisnkgiev qlsatpiklp
      781 ngfrwdvgvn fakntskvva ldgvlstyqi ndfsllrnvi learvgdpyg nfygtyyvrd
      841 pqgnivysgg kavissdrkv lgnvmpnwtg gisntftyks islstlidik nggnifsqsv
      901 glsrytgvla etvvgreegi igagvknvgt aenpqyvpnd vrvssedyhh sfysysnnea
      961 yifdasyvkl reakisfaip nkwlsktpfr nasfsvvgrn lllihsnvph idpetsyysd
     1021 gnvqgfesgq tpsarsigfn ltfgl
//
LOCUS       WP_092017824            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092017824
VERSION     WP_092017824.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111630
     Region          26..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkllmsfv fvlalvfqvl aqdraitgkv tssedgsplp gvnigvkgts rgtttdangn
       61 ykinasgnav ltfsfvgfns ysvnagsrtv idvklvnnnq eleevvvtal giekskreln
      121 yatqnvkgsd laqksepnvl nalqgrvagv qitgasgeag astninirgi tsftgnnqpl
      181 fvvdgipvsn dldrtnggpn gtlggpqssn raldiapeni esinilkgpa aaalygsras
      241 sgaviittks gkggslnkkm evtvsssytv qnmygypelq ndygqgsagi ylgtttnswg
      301 pkfgttptla ngllkadgtt vpykaypnnn ndfykqgsia snsvnlaggn atqsysmtlg
      361 nttqkgiipg sefnrtnvaf ggttllanki kfggsfnytl tgqnnfltgn gasapgvlss
      421 lprsydlqgl pykdangrsi yitsndnpyw svennkttst vdritgninl gyditpwmsv
      481 tyrlgldnyt drrkqvfaig aarlptgail edvfyrnein sdlifrfkkd klfsddinft
      541 gligynvnqr kfqnvsaygg gltlpnyyni nnattytsan gatgesntlr rligyyaqas
      601 fdyknylfle ltgradqsst lpkdnntffy psaslgfslt dafkmesdil sfaklrvsya
      661 kvgkdadpyk lasvytvtsq gnnvssisfp ingqagfsig trigsgnnlt pefttsyeag
      721 gnfgffrnrm nldlavyqti stdqildvav agstgystrt tnigkmtnkg levmlsykvi
      781 tgknfdwtvt gnltmnrnkv deigngvtsf svpgsaftgs vpsivegrpy gvilgnkrvr
      841 nadgkfvinp vtgfwvaatp nqeisnpnpd aiigisnsfk ykgvgfsfli dsqqggsivs
      901 ftaatlkgvg alketavdrd kpriidgvil nsdgtyrpnn iqidaqnyws qqgtqtdlnv
      961 ygattyrlre vvlsyqlpks vlaklpfgdv nisltgrnlf fiapdspidp elntqgagni
     1021 rglelqsapn trnygvnvrl tf
//
LOCUS       WP_092017863            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092017863
VERSION     WP_092017863.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110931
     Region          27..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqllrnli ilsvflcygm tsyaqkislk gkvtdqegka lqgvsvivkg ttrgtltsqs
       61 glfeisasqk tvlvfryvgf rteersfens nnnidiqlkq ddsaleevvv talgvkrdkr
      121 altyssqdvk gdelvkakep nivnglagkv sgvqitsssg apgsssrivi rgttsvfgdn
      181 qalivvdgvp inndetgnln sgpgsnrlvd idpsiiesvn vlkgaaatsl ygsagargvl
      241 mittksgsae kkpvlsfsad ysfenpllpq tqtkyaqgsr gqfidgeank tslswgplmd
      301 tlkvngapak rydlqkmffk tgitqnytvg lsgggsnssy yisysdfnqq gsvpntsfnr
      361 halftkyttk vfkdltsnfq fnysntsndr mpegyalenp iwtvlagpvs wnplpylnpd
      421 gtqrvyrysr nnpfwvldnv ynkstvnrfi pimtftyspl swltvterlg adiygeqsky
      481 keapsstlat lgriieqntn frrfnhdlii sankdfgnfe lnallgnnvt siytqnhyik
      541 gtglnidgfd nvgsastita yennflqrkv gfyaqanley khflalsltg rydgssvlsk
      601 eksfypyssv atsfifsell sgslsevinf gkirlsyatv gndgvgpysl ttpfiipnsp
      661 ntpnfnnlsf pfqgqagfll sptlgnsnlk netlneyeig leakflhnri gleasyfnrk
      721 tidgiipgva iapatgytgt tvnsaslenk gfevllnltp iktshlkwdi afnftrirnk
      781 vlslygdtkq lgngfsqiiv gepygvkyga rfkrttsgel lidakglpir deqdgivgni
      841 spdwlagmnn tirykqfgls fffdmkkggd iennvdgyga fygttkased rtprvlkgis
      901 ivdnkpntvp admqtyyqnf ggmlesiiqd gtyiklrsvs vnydlhpnll kktpfrsasi
      961 vvsgrnlwiy sphftgadpe vssfgssngs qgiysfsapt srsinfslkv tf
//
LOCUS       WP_092018013            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092018013
VERSION     WP_092018013.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112020
     Region          29..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfikilmvl callifskaa vmaqnppiik ikarvtgsdk qpvigavvss sdetgktaat
       61 dasgnfsiei pekqmisvva kgfktkhita dpkiteivif peehrepvhl afrnadkedl
      121 pvgvasvnvk ellnknyfty ilegmesfvp gfngnsnwgm gsylfmidgv pretgnvmpt
      181 eieqivflkg anavalygsr aakgvvnvit krgvagqsrf dlrvnsgvnv pkalprylgs
      241 aeymtlynea rrndgltnly setdiynyas ginkyrypni dfysseylks sygsydltae
      301 isggnervky ytnlgfatsg sllnfgeakt nnnsdrlnfr gnidvnlndy islnadatai
      361 fytgrgvnad fwgsaatvrp nrfaplipls mieqddaasq iliqnsnnii dgkyllggtq
      421 ldqtnpiaai ysggnnqfan rqfqfntgik adlrnvlkgl sfksgfavdy ateytlsyny
      481 syatyapvwn nysgkdliss ltvynqdaks gtqnvsgnry rqtiafsgql nydrtyneah
      541 hlsaillang fqqsesavyh ktsnanlgfl agynfkhryy ldfsaayihs aklppanrqa
      601 fspslslgwr lsqedflkns diiddlklta sagilhtdld ipnyylyqgv ytgagswygw
      661 kdgtgiqate srrgdnpdmq fpkreevsvg fegsffkgll tlngtffanr isgniiqasv
      721 lfpgyfttgf pvssfipyvn ynedqrigfd fgvnlnkkyg dvnlslgvng tyyqttaskr
      781 aelyedayqn rqgkpldamw gleslglfqd qkdianspvq tfgqvkpgdi kykdqngdgi
      841 insrdevflg kggwfgaplt lginftaqwk kltffaiglg rfganamrss syfwvdgedk
      901 ysvavrdrwt eetkltakyp rlttltsdnn yrssdfwiyq tnrfdltkvq itydlsdvlk
      961 lksfvrelgv yvsgfnllti sdnremmeln vgsapqtrlf nlgvkalf
//
LOCUS       WP_092018940            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092018940
VERSION     WP_092018940.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115215
     Region          49..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkirllkts rqllllslvg sislngysnv ekstnsafst taetlltelk gkvtsakdat
       61 pvvgasvflk enprigtstd vdgnfklnvp enlekgkltl vistvgfekq eialssgqtq
      121 vdvtlkeslq vlsevvvtal gvkrdkkala ysvteisgge ftqaretnla nslsgkiagv
      181 natslatgag gssrvvirgn gslsgdnqpl yvingmpidn stpggspttg gggqnvdrgd
      241 gigginpddi esisvlkggt aaalygsraa ngvilittkk gavkkgigie ynstatidqv
      301 vdytnwqyqy gqgdggvkpt sqaqaiswgr rswgakmdgq pyisfdglqh pyspqknnis
      361 nfyntgttfs ntvafsggne ttsfraslad idnksilpns tfnrkvanls lsskigqrit
      421 idalaqynle kahnrpsagd apgnpnwsny miantvdvrs lspgydangr eiqwnetpya
      481 snsyfvvnry tnddtknrfi gqfgirydil qnlfikgnvs rdfsnynyvg iiptgtvytt
      541 naageyqgik savsetnsll tlnyntklrs lqvnamfggn qrnftreeiy tngtqyiipf
      601 fysftnlata ttrpatqrla tnslfgsldl dykgilflna sarqdwfstl giknntilyp
      661 algssfilsq avelpsviny aklraswaqv gggvpdpytl nqtysmvtss gqplqqittt
      721 ngeyllnnpn lkpftsttye agldaklfnn klgvdltyyl rrttddivkt aisgtsgyqy
      781 syvnvgqvdn qgiellltgs llktknfswd asynfaynqn kvvkladgvn tiqlatsvgs
      841 wayvntdigq pygiikgytm vkdakgnivy dtstgypmks gltqigqgva pytmglsnkf
      901 nyknfsldil ldgkfgnevf svmnvyatrf glqqstlagr etglalsgvt asgdsysnni
      961 pvanlrlyyd nlknysnlfi ydgsfiklrq iifsyripsn flkfakiqsa sisfvarnlf
     1021 tlykktenfd pessytnsna qgfeafglpr trsfglnlsv kf
//
LOCUS       WP_092019376            1038 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092019376
VERSION     WP_092019376.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1038
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113920
     Region          29..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknvrerfm giltiwgiif sfssfaqnrq itgkisdpsd gsalpgvsvq vkgtargttt
       61 dasgvykiqa sdnavlvfss vgylkkevkv sgqsvidvtm esdvsqldei vvtalgqtqe
      121 kralgysvqe iksdaiknsg eqnlvgalqg kiagavitgs ggapgsgvni ilrgitslss
      181 gsdnqplfvv dgiiisnttn agnplpsags sspgaseqfg ntnraadinp edveaisvlk
      241 gpaatalygl rasngaiiit tkrgksgklr vnvsstvgid nvsktpdyqn rfiqgrfgef
      301 iseteiaqrs ifrsfgpalm gdtnpndkiy dnfrdfyrtg frnnnnvsis kggdkgniyf
      361 slgrnyqsgi ipntdferts lklaglynvt ksfsvsgsvn yvnsggkrpp agdksifssl
      421 sywpnsydvn dyikpdgsqk nitlgvvdnp rylvekspri dnvnryiadi alnyafnswl
      481 sakyqvtydt yhetrsrtvd stfdvgvqvk gflvkedlnf reinsnfylt akksfnenwn
      541 gsvmvgnsiv dskkpdsyyt rgerllgsnp seigsyknte trfyspgqyr ivsffgdakl
      601 nykdvlylnv tgrndivstl pvqnnsffyp svslgyvfte slpkgnilsy gklraswaqv
      661 gkgadpyits tyfapvtnfp ynnnvpgysr vtttadpnlr perttsievg aelrflknrl
      721 svdatyftmd skdqivnapv tnasgyanyy tniglirnqg vellvsgkpv qtknfswdvs
      781 vnwsklsgkv lemppalqei vyfdntktfl kvrqgsnlgd lwgfeyvksp dgqtviqang
      841 fplvsttatk vgnampdwqg gltntvtykg lslsfllewr qggnvvdmae ensvrngitk
      901 fterryeqvv ykgvvaqknt dgstsyvpnt klvylddnfy rsanqfyyws gftvqdgswf
      961 rlrsvnisys lpkkliansv fkngvrfsft gtnlflntpf rgydpealsf gsgtnrigfv
     1021 grnnpstrsf qfgvsvnf
//
LOCUS       WP_092019374            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudarcicella
            hirudinis].
ACCESSION   WP_092019374
VERSION     WP_092019374.1
KEYWORDS    RefSeq.
SOURCE      Pseudarcicella hirudinis
  ORGANISM  Pseudarcicella hirudinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Pseudarcicella.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Pseudarcicella hirudinis"
                     /db_xref="taxon:1079859"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113215
     Region          27..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkllgpll gvialvfmsa tafgqnftfk gkvsskknge pligatiivk gtttgtitni
       61 dgeytlntnl kagtyellfr sigyqtatkl islnaktsis ldvaleedaf gldevvvtgs
      121 tltssrrqlg naitsikadq lqntgssnls salqgkipga qitqnsgdps ggisirlrgv
      181 kslqgssdpl yvidgvvisn astnvsqlas anqagndavq gtnrladinp qdietlnvln
      241 gsaaaaiygs rasngvvvit tkrgksgtpk vtfstsvnvn elrkkvyist ygkqfgsaal
      301 rlhtigaapa gvesvgivrd gvttklatnl vdvtrydyqd nifqtgygnd nylsinggtd
      361 ktqyfasisy mknqgiiknt dfqryglrlr ieqrladwak vsagltytns fsnekpngnv
      421 fyspinsvni tnniyditqk dpltgglkav epsrvnplsp iedfdfnqsv srtindlqfn
      481 ltplkglsid yilgvdyfsq lgknyippyp yqaeaglpae rypngfagia ngnstqintd
      541 lnvsyekdlt sslklnavag fnyqftrrdy skttgenlts fiqtvsgaas ntvlasygld
      601 rysvsgqfaq ttfgyknqvf ltgairrdgs tlfsssetnq fypkvsgswv isdadfwkng
      661 slsntvnglk frasfgdagg lsaigtydrf wqflptayqg fntfvpsskl ansrvrperm
      721 relefgldvs llkdrvslgv tnysqnisel vvnrtlasst gglsfinnvg emenkgweai
      781 lsvtpikkkd ltwdltmvys rnrnkvisag spsvaintvs gapsyliegq pasvfyafyy
      841 arnpdgslll tpqgfpqrer gtieglygtp krdangqptg dylkkiignp npdytaslts
      901 sltykrfnfr flldavqglq vfnadkrtrq gvgigdyaek elkgelprgy ifsiytieew
      961 riddgsyvkl revslgysfk npikgmsnln lsligrnlys wdkyngydpe tnaggnsdil
     1021 rgvdfgnvpi prsyqltlta nf
//
LOCUS       WP_092030720             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter sp. DSM 26671].
ACCESSION   WP_092030720
VERSION     WP_092030720.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. DSM 26671
  ORGANISM  Marinobacter sp. DSM 26671
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter sp. DSM 26671"
                     /db_xref="taxon:1761793"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55693
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeif ederrvaatp psvhkliglg ydviveggag eaanysdaay ekvgaaiaad
       61 tsslwkeadf ilkvrapmen palgkheadl mkegaflvsy iwpaqspell eklaarkits
      121 faidslpris raqkmdalsa maniagyrav ieaanhfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig aansmgaivr afdtrlevke qvesmgaefl eldfgdeegs gsggyakqms
      241 defikaemal faeqaeevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgkva hqhgvtligy tdlpsrmakv asdlyatnlv hllteltpek dgtplvnmed
      361 evirgltvvh edeitwpppq pespvspkpa pgteepsaea kaaakkdadr rsligkgvll
      421 vvtalalygv gahapesflq hftvfvlacf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gailhlaqae niavgimafv avliasinvg ggfrvthrml kmfrk
//
LOCUS       WP_092034610             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. OK095].
ACCESSION   WP_092034610
VERSION     WP_092034610.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. OK095
  ORGANISM  Bradyrhizobium sp. OK095
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium sp. OK095"
                     /db_xref="taxon:1882760"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39199
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake msreyqakqa
      241 altaehikkq divittalip grpapklvsa emvksmkpgs vlvdlaverg gnvegarpge
      301 vaevdgikiv gytnvagrva asasslyarn lfnfietmvd ktskalavnw ddelvkatal
      361 trdgavihpn fqpkv
//
LOCUS       WP_092041209             409 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium pseudosasicola].
ACCESSION   WP_092041209
VERSION     WP_092041209.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium pseudosasicola
  ORGANISM  Methylobacterium pseudosasicola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Methylobacterium pseudosasicola"
                     /db_xref="taxon:582667"
     Protein         1..409
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41962
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd saeprvaavp etvkkfkalg adivvqagag lkagildaey eaagaeiags
       61 aadaareadl vlkvrrpaae elsllkrgat iiaimdpygn eaalkalaea gvagfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrampmmmt aagtvpaarv fimgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsagyqa
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlidlav erggnvagak
      301 pgevvmtdrg vkivghtnvp grlaatassl yarnlyafve tlidkeskal ainwddelvk
      361 atnltrdgsv vhasfqaktd gpaseaaavg laksetgkaq sapapsgan
//
LOCUS       WP_092060558             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Poseidonocella pacifica].
ACCESSION   WP_092060558
VERSION     WP_092060558.1
KEYWORDS    RefSeq.
SOURCE      Poseidonocella pacifica
  ORGANISM  Poseidonocella pacifica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Poseidonocella.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Poseidonocella pacifica"
                     /db_xref="taxon:871651"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55536
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtprevl qgearvamtp dsalqlqklg ydcaiesgag dragftdaay aaagvevvgs
       61 taelwessdi iakvrpptee evgylssdkt lisffypasn enlmqlaadk gasvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqtdgassgg yaavsspefr
      241 eaqlakfrel apemdivitt alipnreape lwtedmvkam kpgsvivdla aerggncklt
      301 vkdekfvten gvtiigytdf psrmatqsst lystnirhlm tdltpekdgm pvhnmeddvi
      361 rgatiahane itfpppppkv kaiaaapkka aakeltpeek raqevaafka qtkqqvtlla
      421 vggalllgvg lvapasfmqh fivfvlavfv gfqviwgvsh slhtplmavt naissiiilg
      481 almqigsgsf lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_092067286             989 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            tf2-5].
ACCESSION   WP_092067286
VERSION     WP_092067286.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. tf2-5
  ORGANISM  Prevotella sp. tf2-5
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Prevotella sp. tf2-5"
                     /db_xref="taxon:1761889"
     Protein         1..989
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109095
     Region          38..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtfehsrq tgngvslrai llmlamvffa ldvsaqttin ghvkddtgeg iigasvmvkg
       61 ttngtvtdfd gnfqlkcetg atlvityigf vpqevkaknn lditlredva qlnevvvvgy
      121 gslakkeiss svvqinkdqf nqgaasdpma liagkvtgln vaatadanpn amtdiqvrga
      181 gsltasngpl ividgiaggd lrniatqdve sitvlkdags aaiygtrgan gvilvttkkg
      241 sgtagvtnvt ydsyialnfa kpkpdilspd efrrsrratd ygastdwwde itrstsysln
      301 qyisidsstk ngyfgaslny ksgngldivs kreeyggrfv meqrvlqnyl qfnasvsark
      361 vhedwgndgl fdtaltmnpt ipvkgangny yqpsspsgih npvndllnnv negdrtyilg
      421 nadvkvnilq qemhnlstsl syalqyndlk snfytpttss esywtgfegr anvnyqkwwt
      481 nrlewlinyt ltlkkhqlka vlgyswersk weqsgnenmn fvydsmswyg igngtalkdg
      541 kanlwggsse stligffgrl nynyndmlya saslrhegst kfgknkkwgt fpsislawev
      601 tstpglkdtf kmfqslkpri sygvtgrsdf daykslstys syssyylnnq wvigyapsln
      661 anpdlaweks tafnvgidfv tlnshlrgsi eyfdrrskdl lynytapqpp fiydnilvnv
      721 gttkntglei sldydvlskt avkwttgvnw stgttkltkl ssdvykaayl dlyqkpglgt
      781 seyffrveeg gkigqfygye hagidetgql liydnegear pvaqadpawk rnigngapkh
      841 flswsnsfry knfdlsmlfr salgykifnm rkygmglkgc gtdnvlrtay tdynnitsgg
      901 gvissyflen gnyfkldnvt vgytftpkkr elieslrvyl taknlftlta yegndpsivt
      961 sngitpgidt nsaypqatqv slgvtlrfh
//
LOCUS       WP_092073216            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            tf2-5].
ACCESSION   WP_092073216
VERSION     WP_092073216.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. tf2-5
  ORGANISM  Prevotella sp. tf2-5
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Prevotella sp. tf2-5"
                     /db_xref="taxon:1761889"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123075
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrltmfma clflslgmal aqtkvsgtvi sgednqpiig atvlvqgqkt gtvtdadgqf
       61 tisvpsgkki vvsyigmetq tvtpksgmti tlqpsaalee vvvtgmtrmd rrmftgatdk
      121 vnaedallng iadvsrsleg rsagvsvqnv tgtfgtapki rvrgatsiyg sskplwvvdg
      181 vimedvtdid adalssgdpe tlissaiagl nsddiesfqi lkdgsatsiy garamagviv
      241 vttkkgksgq ahinytgeft trlkpsysnf nilnsqdqmg iyrelqdkgw ltfsdvlngs
      301 dygvygkmye lintynpetg afalantesa rnaylqnaef rntdwfself sgaiqqnhsl
      361 svsggtaksn yyasisamvd pgwykqskve rytmnlnvsh kildnltinl igsgsyrkqr
      421 apgtlsqdvd vvsgnvkrdf dinpysyaln tsraldpdty yqsnyapfni mhelntnyid
      481 vnfvdtkfqa elkykpipdl elsalgalky tttsqeykil ddsnqaeayr aagnsiirda
      541 nkylytdpdk lyalpitvlp nggmykrtdn kmtdlnfrlt anythtfggk hyvnafggme
      601 stsiersrsw fngwgmqyak geipyyvyqf fkksleentd yyslsntnsr svaffanaty
      661 gfdnryving tyryegsnam gksrsarwtp twnisgswnv dqekffekfn kvlshlklkl
      721 sysltatppp taycsstnvf kaynpyrift qdketgiels dlenseltye kkhefnfgfe
      781 agflndrinv afdiysrrnf deigpvatqg iggqiirwan aadmkssgqe lsisttnikn
      841 kdfswttslv yshstteitn lasrdrvidl itnfggrreg ypvralfsip fmglnedgmp
      901 tflneageit tydinfqere kldflkyegp tdptvqgsfg nlfkwkgftl nlfitysfgn
      961 vvrldpvfag kytdltsmtk efkdrwmvpg delrtnvpvi lsktqydnnr ylrygynayn
     1021 ysdvriakgd firmkeislq ydfpktwikp lnnlslklqa tnlfliyadk klngqdpeff
     1081 rsggvsspvp kqftatlkvg f
//
LOCUS       WP_092075733             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Poseidonocella sedimentorum].
ACCESSION   WP_092075733
VERSION     WP_092075733.1
KEYWORDS    RefSeq.
SOURCE      Poseidonocella sedimentorum
  ORGANISM  Poseidonocella sedimentorum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Poseidonocella.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Poseidonocella sedimentorum"
                     /db_xref="taxon:871652"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55442
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevl egearvamtp dsalqlqklg ydciiesgag vaagfadady eaagvavakt
       61 aaalwkdadi iakvrpptdt evkrlngdkt lisffypasn ealmeaasqk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aqfvyldfee eqadgsssgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvkam kpgsviidla aerggncklt
      301 vkdekivten gvtivgytdf psrmatqsst lyatnirhlm tdltpekdgv avhdmeddvi
      361 rgatiahkse itfpppppkv qaiaaapkke apkeltpeek raaevaafka qtkqqvtllt
      421 vgavlllavg lvapasfmqh fivfvlavfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsf lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_092080777             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium brasilense].
ACCESSION   WP_092080777
VERSION     WP_092080777.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium brasilense
  ORGANISM  Bradyrhizobium brasilense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bradyrhizobium brasilense"
                     /db_xref="taxon:1419277"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39017
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aevavepgag iksglpdsef tavgatisad
       61 alkdadiiik vkrpeasels kykrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapmlvtg emvksmkpgs vlvdlaverg gnvegarpge
      301 vvetdgikiv gytnvagrva asasglyarn lfsfietmvd kankalavnw ddelvkatal
      361 tkdgavihpn fqpk
//
LOCUS       WP_092099063            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            chinhatensis].
ACCESSION   WP_092099063
VERSION     WP_092099063.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter chinhatensis
  ORGANISM  Pontibacter chinhatensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Pontibacter chinhatensis"
                     /db_xref="taxon:1436961"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116948
     Region          27..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklylstll lllvcwcgta laqqvnvsgt vtgadsgipl pgvsvivkgt ttgvttsadg
       61 tfqisvpnqe svllfrflgy evqetrvgnq rvfnvrlnpd skqlgevvvt algiareers
      121 lgyatqevkg edltltkeqn vlgslsgkva gvqmtgssgs smggtqkiqi rgvnsvtggg
      181 qplivvdgtp isnanfagrs gadygnlaqd inpedvesin vlkgpaasal ygirgqygvv
      241 mittkkgkkg pkkvdvqlns afsvekvgnf mpmqniyggg gsqtwrtlan gekyvdgtde
      301 swgpkmdgtp vrhmhsfypq dpmygqlepf vpqpdnikdf fetghnlnng vsisggnens
      361 sfrlsynntr iegvepntwl krnnlglsas ldlsdkitas aninyannda qrpsqgyyeg
      421 srnfmqwfqr nldmkrlkny kyddgtfyhw nigrpnaqgv itnwrpsdwn npyfeayenl
      481 nndnrdrffg dvgltyqvlp dlkvsgfvrs dmytqniesr iaaggrsvna aystgkyqnk
      541 emnyeflaqy tkewndfsfn vnvganlfdr nytylsqatr ggltspgfyn iegsserpav
      601 asyllrkqln siygmatvgy kdtyfvdfsl rrdhsstlpd pyyypsvsas fvfsellnwq
      661 plsfgklras yamagndvsv yatsmnyeig glygtvntsf vpdvlnnpli kpsfatsyev
      721 gadlkffngr lgadvtyyeq rneddvitln vsgasgysss yinaglmvnk gieialtgtp
      781 iqtqnfswdi afnaarnrgt vkelypglds rllesntysg vsmylysnvg eqfgsivgqa
      841 yqrdpetgki llgsnnmply ttathnfgsv lpdatgglqn sfrlgkfdls amidyqlggq
      901 fiswsrmlav kaglapetaa inengknvrd plaegggvkv sgiygpgvki ndedvsgref
      961 tgfvdartyf rntlgtriye ewiydasyvr lreirlgysl dkaslgslpf qkvgiafiar
     1021 nplmiwqkap eglnpaelat gsssfgwlet gglntvrsyg vnlnisf
//
LOCUS       WP_092098506            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            chinhatensis].
ACCESSION   WP_092098506
VERSION     WP_092098506.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter chinhatensis
  ORGANISM  Pontibacter chinhatensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Pontibacter chinhatensis"
                     /db_xref="taxon:1436961"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115537
     Region          25..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnsftllvl llmccwvpal aqentvsgrv tgadegmplp gvsvtvkgtt igtttdadgr
       61 ftlnvpsdes ilefrflgyr iqeirvgnqr qvnvvmatdt qqldevvvta lgitrekkal
      121 gyaaqevrse elvqnrqpnv lnamqgkvag vtisstggap gqganiqirg insidpnrpn
      181 qplfvidgiq vnnststfge gaelrgmsnr ladlnpddie sinilrggaa talyglrgan
      241 gvvvittksg kkgemrvnft stagweevnk fpkiqdtytq gytgvydpts fwpswgptwq
      301 earqidpthp egiynhfeda yetgsqfrnt ltfsggtdai tfssslsrld hegvlpftdy
      361 qntsarlntd vklsekfstg gnfnyirsgg krynadrfne mlsywsprwd vrdyvkpdgt
      421 mqsygndnpi yaastnqfed dvsrfiggln fsykplswld fnyrigldty tddrtrtapg
      481 prnvpderll ddngqgfvhe yttkfrsins tfitslnksf gdkfnatlrl ghelydehik
      541 sfgvqgeels vfdyfklsna rflsssenes eyrlmgifge asfdygdflf ltltgrndit
      601 stlskskrsf fypsasisyi asehlelpdf inqtkvrlsy aqigkdaspy sissgyapyt
      661 nlptgytgvt raallgnpgl kpeftntfea glemsfldnr igfdftyyys lskdqilnid
      721 vasttgfvra ainagemrnk gveivlnatp vrttnfnwds klifsanrnk ilslpeglee
      781 vtyasqfgyv gstvtmklie gqpygniygs hwqryygpgq eedplfides rpivigadgf
      841 pvraplssqk llgnsqpdwi ggftntftyk glsltallda rvglekynqm dnffaafgia
      901 eytenrnqtr vfegvlsdgt pntkevwlgq gtgpdgvnyg dgyyrrfyrg vsenfvedas
      961 wvrlrsltlr yslpqrwfen ifirnaalsf tgnnlwlstd ykgfdpetsf spsgsnvdgf
     1021 sgftypavrs ylftlnigl
//
LOCUS       WP_092099839            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            chinhatensis].
ACCESSION   WP_092099839
VERSION     WP_092099839.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter chinhatensis
  ORGANISM  Pontibacter chinhatensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Pontibacter chinhatensis"
                     /db_xref="taxon:1436961"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113124
     Region          28..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkvltkqfv lcmllclftg lafaqqtrti tgtvkdekgt pipfasvqvk gtttgtttge
       61 dgtfslsvne gavlvvnslg ydskevsvga gstlnvtlgs sssqlsevvv talgierekk
      121 slgyavqevk geslvesrea nlanaltgkv aglqitrssn gpagsskiil rgnnsltgdn
      181 qplivvdgip idnftgrnnn dywnpgldmg ngladinaed iesisvlkgp saaalygsra
      241 gngvilittk sgkpqdglgi tisstvgyde iftypelqnt fgqgtegthd pmsglswgpr
      301 aegqtvqnwr genvplriyd nidnffrkgl yssqnisfqq qynntsiyts fnrfdnegvs
      361 pgvnlsrtnl maravsnfgk sdrwttdtkv qytksnaenr piggnnpnns fgtlfglprs
      421 mdirdfeqav dgegkmiwyg tssqmnpywn srynlnqdlr drfilngsvk ydftdwlsae
      481 lkggadmhyt ttesklyggs pqtpsgrysl gkqnftetnf stlitaqrdn vvgklggmvt
      541 lggnlmaqkf ssmngsagel evpnlfflnn sisnpsvgqd yrehkinsvy gsvqlnwdgy
      601 lfldatfrnd wastlnqdnr syfypsvsas yvltdmlett gtvlpswlsf tklrasyaev
      661 gnslpayqly ntywigkdpn gnttagrnni lfdpnvrsel ikayeaglea rffdnrigvd
      721 vawyksnatr qlidlpmdpl sgysfrkina gdiqnkgvei mvdadvirnp egfnwnisgn
      781 ysrnrntvee lygdieiypl ggfddvrvna vvggeygeiy gstfrrvddp espyhgqlll
      841 nadglpvige qgvklgnqqa dalvginnrl rykglglsfq vdariggeif sgthvamqrs
      901 gtgaatlrdg gresfvvegv iqdptsgqyn tnttavtpqn ywnavagvnn lgiteaniyd
      961 atnvrlrnvq lsyalpggll sktplqrasv gitatnvwli sshmdgldpe svfatgtnav
     1021 gfengsmptt rsilfnltlg f
//
LOCUS       WP_092099977            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            chinhatensis].
ACCESSION   WP_092099977
VERSION     WP_092099977.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter chinhatensis
  ORGANISM  Pontibacter chinhatensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Pontibacter chinhatensis"
                     /db_xref="taxon:1436961"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114388
     Region          25..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvlllslm lalllpllgy tqgartvsgq vtdqesgqpl pgvavivqgt tvgtttgasg
       61 eftlnvpena ntlvfrflgy aevvreigna ttinvamgld seqlqevvvt algreeeert
      121 lgyatqqvgs eqitqgrers vanalqgkva gvniqsqggg pgastrvvir gaksisqsnq
      181 alfvidgipv dnsasgttda lnagvdvgnr andinpddie sinilkgpaa aalygaraan
      241 gvimittksg rgatkkaeit yltsytvedi lrypelqnry gqgffgapdl lentswgprf
      301 tgellpwgqi idgqqrvkpy salednikef fdygynwtnt vslsgaadna tyyasysttq
      361 qegvvpttey srhslavkgs tkllnkfnst vsltytksgg dfaltgqgns vfnqiiqtpr
      421 dipvreledl espfndeagf yspytinpyw slrnqtyene vdrlfgnitl gydimeglnv
      481 tyrigtdfyt drrkqfmair nvqgqnaann dngmyaerqv yyrevnsdli vsynrdlsdi
      541 ltldllvgnn inqrenddlt atadalanne frslsniigt pltvsfrdkr rlvgiygsak
      601 lgyrnflwle vtgrndwsst lpiddnsffy psvnlafdaa eafglaettp infakirany
      661 anvgndalpy strsvfvsgn isdgfagtdl nfpfaglpgf evsnvignan lepentsswe
      721 vgadmrffne rlrvdaayyn skstdqiinv plsfatgfgs aflnaatirn egvellvggi
      781 pieigdfswd isvnftknen tvedvagdne islgglssaa lvisegrpyg tflaedflrd
      841 pqgrivvnps tgrprlateq tyqgsiqpdw qgglvntfry kglrmsvvfd trqggkiysr
      901 trgtqrfagt apetlfndrq pyiipnsvvq vgnsdeyien ttpltnsnly eywgnlpegt
      961 niidasftkl revsisyslp raitektffg nievglsgrn lvlwtpdent yidpevnsfg
     1021 ngnlqgyefs sypstrswga nlrvtf
//
LOCUS       WP_092101343            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            chinhatensis].
ACCESSION   WP_092101343
VERSION     WP_092101343.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter chinhatensis
  ORGANISM  Pontibacter chinhatensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Pontibacter chinhatensis"
                     /db_xref="taxon:1436961"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115026
     Region          21..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maavfllllc cqlavaqsls vqgkvsdtkg malpgasvav kgtatgtvtn mdgsyalrvg
       61 gaedvlvvsy igfqtkvipv gnqstinitl seddnslnev vvtalgiere ekalgyatqt
      121 vtgesltnar snnfasalsg kvaglslvsp gsgpvnstri slrgdnsldp ngnnalivld
      181 gvpmnsdmts sgvdnaygag sgndipvdfg ngiadinpdd iesitvlkgp saaalygsra
      241 angvliittk sgssrkkglg vtvssnysin dvlqwpdyqy eygqgthnln kdgipyysyh
      301 asedgantgs tssaygpkfd gqyfyqydpt legqsaerql wrpykdnikg ffrtgstitn
      361 svavdggner gsaraslths knewimpntg fermtaalsl nykvsdklkl nskvnfthkk
      421 sdnlpgtgys nqsiayfmif qnpnvdlawy eprwkkgkeq ieqihpfssy idnpyviaye
      481 mtnalnnyst vgnlsatyef spkldllvrs gittsqedre qrrpfntanf plgyykeqsi
      541 fdyeintdfl vtykeqigsd idirtsfggn trrekyrhta gvldglvipg vyklsngisn
      601 pmmttshank hvnslyglat fsyqdkvfvd vtgrndwsst lpvqnnsffy psisssfils
      661 diftlprqvs yaklrlsaak vgndtrpyrt rkyygqsdfa gsgsmptilh nadfkpeltt
      721 syeagleyrl fqgrlgmdit lyrsftenqi leipldpttg ysravmnagk vrnqgvelmv
      781 natpvetrdf rwntsvvwsk ndnqvmelae dlgadqqvih mggqasiiak vggstgdiyg
      841 fgfvrspdgq ivydnaglpa ypqetqyign ayadwkagfn nefsfknfrl nvlldgqygg
      901 iiysqthhkm aeqgklkstl mgreegfiig dgvvdngdgt yspnttkvtp qayytryyrr
      961 anvesnsfda sylklrevrl eynlpkalls ktrflqgasv alygrdlaml tkfpifdpet
     1021 aalnggtimp gvemgqmpst rtfgmnvtlq l
//
LOCUS       WP_092104910            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            chinhatensis].
ACCESSION   WP_092104910
VERSION     WP_092104910.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter chinhatensis
  ORGANISM  Pontibacter chinhatensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Pontibacter chinhatensis"
                     /db_xref="taxon:1436961"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118109
     Region          24..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvillsfl lvavlinqgl aqgrtitgrv tdattsqplp gvtvlvkgtt vgtatagdgt
       61 fslnvpegsn tlsfsfigyq avertignas tidvalstdt eqlqevvvta lgiersrnel
      121 aysaqqvsge qitrtrpadf vnslsgkvag ldirsnntmg gstnvvirgy ssitgnnqal
      181 fvidgvpvsn annntntray qqnpdfgdqq ggragtdwgn aaadlnpdni esvnvlkgaa
      241 atalygsraa ngvimittkk grknslnivv nsgvtwseid kstfvryqke ygagysqefr
      301 dpadlgsgva pvvrfqddas ygprfdpnlq vyqwdaidpf hpnfgktrpw vaaendpstf
      361 yetgvnsnqs vvvsgggdrt tfnlgytrnd irgnlpnsti dkdlfnfngs ydatdkltvs
      421 asanysrtva vgrygtgyqg rnpnqafrqw wqtnvdieeq rdayfrnrqn itwnwnstnt
      481 gpiftdnpyw tryenfsnds rdnfygyata tykftdwfnv mgraafnttt dfqeeriavg
      541 sadvsqyqrf drdfnesnfd lllnfnknit edisftgllg snlrrsrmns irattngglv
      601 vpglyalsns anpptppfee gerigvdgif asanfgfrem vflelsgrrd ksttlpednn
      661 syfypavaan fvfsnaleip wlslgkvrvn yaevgndapa lsvldvydkp tgfgniplfs
      721 lpdiknnenl qpersksfea gleaeffnsl fgfdftwyts ktvdqiipvs ttsasgysqr
      781 fvnagevenk gfevaafvtp vrtsnltwtm nlnfsrnrne vvslfedvqn vllqnfqggv
      841 slnaavghpy gvirgndfvy tngqrtvnsd gyylvtpgan diigdpnpdw lggvnnsitf
      901 kditlaflid irdggdifsl dqwygeatgl ypnsaglndk gnpsrlpvae gggillpgvn
      961 esgapndvya enqdgngqtp fgyaanngvg apkswyvydg sfvklreval syalpqtlie
     1021 nlgfikgvdl qligrnlwii hknmkysdpe egissgnagr gyqsgaypal ktygfnvrln
     1081 f
//
LOCUS       WP_092104914            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            chinhatensis].
ACCESSION   WP_092104914
VERSION     WP_092104914.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter chinhatensis
  ORGANISM  Pontibacter chinhatensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Pontibacter chinhatensis"
                     /db_xref="taxon:1436961"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117106
     Region          26..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilflsll lvtallhqam aqvraitgrv tdaatsqplp gvtvlvkgtt vgtatsadgt
       61 ysinvpeggn tlvfsfigyq tverpigssn tvdvnlpvnt qqlsevvvta lgiareeksi
      121 gyssqtvsge elsqvretnv vnslsgriag vqvgtnsgam ggsarvtmrg vssisgnnna
      181 lfvvdgvpie nsntnstnqq rggggydygs aiqdinpndi aeitvlkgaa atslygsrga
      241 ngvivittkk gerkgggigv tytlgltmdk vyilpkyqnk ygggyalskl yynenpeafp
      301 egrqgayddg dgkgsydlip dydvdeswgp kfegqlyrpy wswdkelgnp nfgelarwea
      361 qpnnirdffe tgttltnsia vdgandkgsf rlsysnldqn filpnsemtr hnlsfnggyk
      421 vtdrlnvsas anyvtheakg rpgtgydgsn vlqqftqwgq rqidndkqkn ymlpdgtqls
      481 wnrtswdnva pkysnnpywv ryknyqndgr drifgnvnan ykitdylsad vrvstdtyse
      541 tqeeriapgs qeisdytlyk idfmenniqg llnfnkdlsd dfslnafvga nrmtrtrnif
      601 agstvdglss evynlgasvg rpaitdekte kqinslfasa sfgfreqlfl dlsarndwss
      661 tlpegensyf ypaaslsyvf tdlidapwln lakvraavaq vgndtdpynt iltyalntpf
      721 gsesrvsvpn tlpnaelkpe isteyefgte wrvfddrlgi nasyynrktk nqiiplslsa
      781 atgftfryin agevenkgve lnlygtpvrt ndfswdinls waknqnkiik ltddqktmvi
      841 tnapfavqlq aregesfgsi igydyqyddq grkivlpqgy yarsaeqkvi gsvlpdftgg
      901 vtntfrykgl slsalvdfqk ggdffsttqm fgrysgmlee taegsiredg lvtpgvlsdg
      961 tpnaqvidae tyfyvnggyr igaadiidas yiylreaslg yslpnslver tpfnsvrlaf
     1021 vgrnlwliks nsdhvdpsni tnsitnvqgi eggalpsvrs ygftltlgl
//
LOCUS       WP_092109038            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            KH2C16].
ACCESSION   WP_092109038
VERSION     WP_092109038.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. KH2C16
  ORGANISM  Prevotella sp. KH2C16
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Prevotella sp. KH2C16"
                     /db_xref="taxon:1855325"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114408
     Region          40..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrilislmla ftfmaghayp vsmdvmndsk aveqaqediv tgvvtdadge pligatvqqk
       61 gtenksitdi dghytlrlks gasrilvity vgmkpqtvqv sgnvanatle edanqlqdvv
      121 vvgaygtaqk rsdlvgsayq vnsdqlkglp qqrldvmldg lipgvkitpn tedpgsprtr
      181 fnvrvrgeas lnasneplwv vdgtpmytgd rtnmmpgtsy tvsplsflnp ddiesitvlk
      241 datatsiyga dgangvilvt tkkgkkgktd ihanvqygva nidestapkv mnaaqwmdla
      301 rqayqnagld mrtfpyqdnd mnsysttdtn wrdvfygtgt tfltnvsldg gseksdyyvs
      361 gqyyhnkgtv kgneqqrlsl rsnlgfqllk klkltvelsa syndndlfal greyyellpi
      421 yspynadgty rlynkivsgi dadgnpiyar qkflsnsvle rdqninnqka wylhtnfqls
      481 ydimkglkyt gqfaydyqst leqtydsqkn wtgmdtagdp vgyarrssad ivnwatihrl
      541 nynntfgkht vggvfgfead srnyttmyvt gsgfindhiq dvsqaslrqg ynsssksrkv
      601 sflgqlsysf dhryyltvng rkdgnsqfgt dvrwanfasv gaswnihnek wfnipwmkvl
      661 kfkasygang nsrigsqesm gtysygdsya yngesggaqg qspnsklswe ttymtnlgfr
      721 iaafnridfe fewynnltkd llsqlpvslt tgdtrvyrnv geiqnrgfei nmttrnfiak
      781 eegdftwttd fnlarnsnkl kksyrgtqvn ftdgiswieg edirtyylvq wagvdpydgs
      841 plwydangdi tktydsannr vrgkksnstv tgglvntlty kgfslrvlln yqfggytyss
      901 fasignsdgy svisnnqaie qqdywkapgd ialnpkpisg vstgssrqst rflykkdlvr
      961 lqnivlgyqi prdwvrkwgl tsadvsligd nlfayspyag snrnsyktvm sgyplertft
     1021 lslnvgf
//
LOCUS       WP_092109684             959 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            KH2C16].
ACCESSION   WP_092109684
VERSION     WP_092109684.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. KH2C16
  ORGANISM  Prevotella sp. KH2C16
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Prevotella sp. KH2C16"
                     /db_xref="taxon:1855325"
     Protein         1..959
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108846
     Region          11..955
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlflsrtrvf qvtyigykpk eftvgkkrnf niyleenatq ldqvvvtgfq elkknsftgn
       61 ativtkedlq kantkdavka lqvfdpsfri ldnlgfgsdp nqmheinirg assisqergl
      121 dvenqrltqr tnlrdnpnmp ifmldgfevd vqkiydmdin riqsmtilkd aaatalygsr
      181 aangvivvtt vapkageiri dynttmeltf pdlsdynlan aaeklqvekd agiyigtfdv
      241 atidlerqyn kklnevrrgv ntdwlarplr naynwrndvq vsggvesiry mlnlnydkns
      301 gvmkgsqrnr ygagmtldyr lrnwlqiqnk vsldrtnyed spygyfndys tklpydaiyg
      361 edgeylqmlp msdkvnplwq eqhlqsytgr ggitditdnf minihftqnf ylrstfsisq
      421 vktdsktfrd pkdpsfknlp nnrkgslats gdtrlkwnak allyfnqrfg khfvnltggv
      481 daqetkdsrv sytqegfslg vlsdpiysaq qpnktqdtks ttrlfgvlgs lnytfdeiyl
      541 ldasfrldgs sqfgkdkrfa pfasiglgln mhnykfikni pwintlrlrg tygstgkvnf
      601 srfdvissyi idssswyytg pavllntmgn prlswettkt ldfgimaeff knrfyieany
      661 yrkttdgmid riairpssgf tsyngnvgsi vnkgfelktn vtlfrnrdws vvvnanmasn
      721 snkiskldea ieeynkkird nydaenpqyk nlqnrpliqy yvgastsaiy ampslgidpa
      781 sgveifrkkd gtitkewnas dmvvcgdtnp daqgsfglnv aykglyvnas flyafggqqy
      841 nqtllekven adiknsnvdr rvitdrwrkv gdvapfyglg erkatkpssr fvqndnhiyf
      901 nsiaigydfg rkfvsklkls alsvsfnasd larwssikqe rglsypyaht ysislrasy
//
LOCUS       WP_092110657            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            KH2C16].
ACCESSION   WP_092110657
VERSION     WP_092110657.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. KH2C16
  ORGANISM  Prevotella sp. KH2C16
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Prevotella sp. KH2C16"
                     /db_xref="taxon:1855325"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112693
     Region          44..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkqisllk lcfsvvlcva tstvgadntt sastvkstqq andkqvsgtv ldetgepvig
       61 atvtvkgtsl atvtdidgnf sfrvpagstl vvsyvgyssk evaatgtglk vqlsqdeevl
      121 nevvvtalgi kkeakalsyn vqqlnssdvt tvkdanfmns lagkvagvei nsssagvggg
      181 vkvvmrgaks lshdnnalyv idgiplpsls aaqptdyfsg mgqsgdgasm inaddiesis
      241 vlsgaaasal ygmdaangvi mittkkglvg kprltysnnt sfytpfqype fqntygtstt
      301 gsmfswgakl aeassydpmd ffrtglnesn sltfsvgser nqtfvsaayn daqgivehng
      361 vkrynlairn stdflndkmh ldlsamysnv reqnmissgq yfnpvvpvyl fpagedirkf
      421 yayeqfnqsr gfktmywpyg nqglamqnpy wivnrddfin hkdrfilsag ltykfakgfs
      481 laarammdkt nataekkysa ggdtffagqy gayyigqedt rqlyadailn mdkyfgdfsv
      541 nanlgtsikd vnynytyvgg qlntmasnan tdyahgfvln nvnrkgitdd wfnqipnqhh
      601 qvqsifataq vgwksmiyld atarndwdsy lgntrfknkg ffypsiglsf iltdmfpqlk
      661 stavsfiklr gsysevghap vafapggtye ykngsiatss qmanpelepe rtksweagle
      721 thfwgnklnl nvsvyktntt nqyftpslsa asgytsvain gglvenkgie asltlnqplg
      781 pvkwsstiny tlnrnkikql lrpttlngqt vsldaldvln lgsvkvrlte ggsigdlyvt
      841 tlqtdehgfi kvdytsrqia gidaghyeya gntaakynls wrnnfsykgv nvgilltgrf
      901 ggrvvsltqg ymdaygvska tadardlgga lvngaripaq nfyqtvgpsv gswyvykatn
      961 vrlaelslgy dvpihkyvnw iqglnvslvg rnlimfynka pfdpelsast gtfysgidyf
     1021 mqpslrnlgf svkvdf
//
LOCUS       WP_092109826            1091 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            KH2C16].
ACCESSION   WP_092109826
VERSION     WP_092109826.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. KH2C16
  ORGANISM  Prevotella sp. KH2C16
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Prevotella sp. KH2C16"
                     /db_xref="taxon:1855325"
     Protein         1..1091
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122630
     Region          32..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktkgkglk silfmlwfls sslllqaqvr gtfsgkvvdq qgnpmigvtv rpdggktgvi
       61 tnadgefryd dkgqesrtfv fsylgmksvt ralrsgffat immeddaekl devvvtgyqt
      121 msrresaaai stvkmadvyn psamnidqml qgriagmdvm iqsgepsstp virirgnsti
      181 ngnkapvwvv dgvimsesvp fsasdlnspd asylignsis glspqdiesi svlkdasata
      241 iygvkaangv ivvttkkgrv tapeitydmn lnlntrptyg lfdrmnsqer vqlskdiyda
      301 rlqyprvptg esyegalqsy iskkisadef aslvrnyetm ntdwfkllfr etvsqshgvs
      361 lnggtnkvry ytslnyndsp giakgsksdr ftalgrifvr inrifnaevk ldmsnqnnhg
      421 yssvnpfsya fntsraipay ndgelyyysr silsndvnfn vlnelnttgm kanvrkmggv
      481 fnlnafildg lkfssilsyy wsntrtrtwa tdhsyevgai rgynygvyer gstqfeasal
      541 piggtyrfsd tsgrsyswrn sleykqvlsd rhevnlfggi eirsekysgf sqllygwdpt
      601 ygqsvspayt tryktllegg mfepsitekt tqvasyfata sytydnryvl nanirsdgan
      661 kfgsnpkyrw lptwslagkw fissekfmkk vsfvnnlslr asyglqgnih ddstpyllvq
      721 ldridditgl rpgsvyrlpn pdlrwektrs ynlgldasff dhrlsltldy yqkhtsdlit
      781 dlqvspstgq lymfmnagea fnkgfeevvs vdvlrgknle wniscnathn ineikyayna
      841 slsaketyeh mlqgnvatig qplgtfysfr faglsaengy plfytkdgrk vhegdfevmd
      901 lvasgsiyph vfggfdtrft ykknltlsig fsyqmggkrr lpeiynnvsk afdptqnvps
      961 afsnrwkqqg deryttipal ydtriaddfp eelkglydtg rdvdvrmvrm ydycdirvas
     1021 sdflrlrnim lsyrlpkkil vplhiksltl ratasnlkvw kskkwggmdp esvyanmplm
     1081 psfnfgvnvl f
//
LOCUS       WP_092110692            1135 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            KH2C16].
ACCESSION   WP_092110692
VERSION     WP_092110692.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. KH2C16
  ORGANISM  Prevotella sp. KH2C16
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1135)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1135)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1135)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Prevotella sp. KH2C16"
                     /db_xref="taxon:1855325"
     Protein         1..1135
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125454
     Region          32..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkenafkl slraalavlm mffavslsaq nitvkgsvvd qvgepivgat vkvlgsamgv
       61 itdvdgnyti scpsnatlef tyigyaskav dvrgkqsinv vmeessasvd evvvtalgik
      121 kdakkvgysi ssigsadivk tgapnlasgl ygkaagvrin sapggglgav sfqirglssi
      181 trssqpllvl dgvpirfgdt nndgywdnqr insnglvdin pedienisil kgaaasalyg
      241 seaangvvmi ttkkgtgkgt hvelsaglsf dvvaympeiq kqygpgydnw algdtpesas
      301 gfrqsrvdrn gnsivtpvre tyysygakyd asksvtyfdg tvrpftpigg nlwdevfrtg
      361 vnqnynvsvs naterntlrf sytynnnlpt qynsnnnkhn fnlngtfevf palkinysat
      421 yevqhiknrp yrisrivqny sgmfgsftdv kyirehtmts lgymnsvyag nggtaetltp
      481 deqflytpmg stslmseyfw nvlgkeqlen hnrfigsvnp vwtiipgltl sgriatdltt
      541 dkienknrae nahifstngq ysdsygltns hykiiygdvm lswdktfsdi hnitvnagyn
      601 arredywlss vstsqgltqe nwfhinasvg qknsnmtqqr llktglylta sygfdnwayl
      661 egtirqekts tmhhgtntfy ypsislsaly tefmkdkrpa wwdygkiria ygvvgnspgi
      721 ysayngfsqg sltrdmnyty nyvpttigne nirperkhef evglenkffh nrlgfelsyy
      781 nntvkdqilt ataaasmggr smlmnvgels nngiefsvyg apimnkdwrw dlrfniaknn
      841 nkvnkladgl dlfthatfdn gaatfeshvg epigdiyayt wktddkgnyl vgsnglyitd
      901 tearhkvgna mpdaiggfgt slswknftld lnfdfriggd vlnqpwqyym dtgiiedavg
      961 vrdastgglf yystandmsn kssivrvdps qvpnykrget kidghlvwdn gliqrgvked
     1021 gtpndiivtq fevndnqygw gtgasqsyrd avqknsyvkc reislaytlp taltkkfhcd
     1081 rltvsayarn pfylyrslkl fdaetsdgty wvyqaqvggs tasartfgis lrasf
//
LOCUS       WP_092110701            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            KH2C16].
ACCESSION   WP_092110701
VERSION     WP_092110701.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. KH2C16
  ORGANISM  Prevotella sp. KH2C16
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Prevotella sp. KH2C16"
                     /db_xref="taxon:1855325"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113639
     Region          44..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkqnsllr lgfsvalcva tltvnadnai saspvksvqq asekqvsgkv ldetgepvig
       61 atvtvkgtnl atvtdidgnf sfkvpagstl visyvgyssk evaasgtglt islsqdeeil
      121 nevvvtalgi kkeakslsyn vqqldgdavt kvqdanfvns lngkvagvqf sqnaagvgsa
      181 trvvmrgiks ingnnsalyv idgipmpnlq agttndmfsg agatgdsssd inpsdiesis
      241 vlsgpsaaal ygsdasngvi mittkkgqqg rldvtytgsf qfsrpfvthk fqntygpssa
      301 gafdswgskm stpsaydpnd ffqtgtnftn nvaistgnaq nqtylslgat naeglihnnd
      361 ftrynlnlrn tskfandklt ldlsytlsni keqnmissgq yhnplytlyl fpaggdwqgi
      421 qyysrhnler nletqywpwl dqnelmenpy wiaenerfin hkvrnmvias lkwdvtdwls
      481 ltgrvkydns qnryeqkfaa gtknlfasda gfyglrnqns rqlyaeflaq inkywndgew
      541 sltsvigtny dqrdisqest sgnlssvpnk ftlqninpad pkfklgqeyn errrkealla
      601 saqlgyksma yldlsarndw ssalapnnds yfywsaglsg iwteifpaik snnwlnylkt
      661 rlsysvvgnd psqtfltttt yaingssgps lsttmknadl kpektnswea gidfvlfqnr
      721 lkvnttfyks rtynqffnis ldpttgytnv wvnggsvdnk gvelaarynq plgpvqwety
      781 ltwtlnrnkv kevdasytdp qtgitykase ddlklggfng tqnkvvvggn ltdiyvrtla
      841 tgehgeiyvd pqdhsvrkna ndyilaghat pnynlswgns fswkgfnlgf lfnyrqggiv
      901 vsltesmmda fgaskateaa rdaggvting ingitpqayy qtissttetv asmyvysatn
      961 lrlaelslgy dvpvtkavpw ikglnlsfva hnlwmlycka pfdpeltant gtysqgidnf
     1021 mqpssrtmgf svkvkf
//
LOCUS       WP_092110750            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            KH2C16].
ACCESSION   WP_092110750
VERSION     WP_092110750.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. KH2C16
  ORGANISM  Prevotella sp. KH2C16
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Prevotella sp. KH2C16"
                     /db_xref="taxon:1855325"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122695
     Region          24..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrltmlla clflgigmal aqtkvtgtvv sqedgepvig asvmvkgtkt gvitdtegrf
       61 slsvssanpt ivvsyigmkp qelrgrqdmr ivlepddktl qevvvtgmqk idkrlftgas
      121 tkvnaaeaki dgmadisrsl egraagvsvq nvtgtfgtap kirvrgatsi ygsskplwvv
      181 dgvimedven vsadqlssgd antlissaia glnaddiesf qilkdgsats iygaramagv
      241 ivvttkkgka gqahisytge ytmrlvpsya efnimnsqdq mavyqelfqk gylpyagtan
      301 asdsgiygkm yqmlsqyddt tgqfalantp eaiadylraa eyrntdwfse lfstnimhnh
      361 svsissgtek sqtyasisam fdpgwtkqsk vqrytanvnt sydiskklnf nmianasyrk
      421 qrapgtlsss idavtgevkr dfdinpysya lntsralean tyytrnyapf nilhelenny
      481 ldlsvinfra qgrltykpit qvelavlgav kydatsnehn ilddsnqaqa yramgtstir
      541 sknpflytdp edltalpvtv lpyggiyert dnrmfgwdfr atasyndvfn edhivnfygg
      601 letnsydrhk swsrgwgmqy kmgevanyay qvfkqskeqg tdyftlsnth vrsaaffana
      661 tyswkgrytv ngtyryegtn glgmarsarw lptwnisgaw nvheepwfsk lqpalshltf
      721 kvsysltadr psvtnaeavf ksrtpwryft rdsetgsyid dvanpsltye kkkewnfgle
      781 agfldnrinf avdvyrrnny dligvattgg idgfiqkygn iasmksngle lslsttnikt
      841 kdfswttsli yshthnevtd letstriidl vsgtgfareg ypvrslfsip faglnshglp
      901 tfytsdggtt isgisfqesn qkeldflkye gptdptetgs fgnifrykgl tlnvfitysf
      961 gnvvrldpvf kdsyndltst pkefknrwmv agdenktdip aiatqrqnwn dtdldiayns
     1021 ynyssarvak gdfirmkeis lgydfpesly qpvglsnlsl klqatnlfli yadkklngqd
     1081 peffntggva vpvpkqftlt lrlgi
//
LOCUS       WP_092112017            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            KH2C16].
ACCESSION   WP_092112017
VERSION     WP_092112017.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. KH2C16
  ORGANISM  Prevotella sp. KH2C16
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Prevotella sp. KH2C16"
                     /db_xref="taxon:1855325"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123608
     Region          40..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgkiisflw vllmiplska sagtvirsqs vqqdmkaghv ygkvedrngv alpgvtiqvk
       61 gtkimtvtna vgnyeidmqg iksgtivfsy vgmttqeiny rgqislnvil qddatllddv
      121 vvtgygtynr gqyvgavnqv kaedvlvage nsidqmlqgv ipgmsvmnit gkvggtpkir
      181 irgtstllgn qeplwvvdgv iqtnpvpipn dasplssdmd emlqtagnai swlnpndies
      241 itvlkdasat aiygsqasng vivittkkak anqplsvnys asltvtqrps yglydmmnsq
      301 qlmefnqqay ldrdaytqri lpvgyagliq rlhdksitke efdhefrmme nmntdwfdll
      361 yrtpvstqqn vsvsggsqkf qsrfslglnn spgeaknndl fqvtassnnt frpidkltid
      421 fmvagsyrkn ndyysgvspy dyamntaryl paynadgsyy fypvygqtsy aiqdlnyyny
      481 nilneiansg nrnitqtfqs tlslrwdvak hlqvqgdasl slasvntkqy ateytnviaq
      541 irgyevggvv pnslaenssp lpyggllnts sqstrnysfr gslvynntfa mkhsltfnlg
      601 aqvtsnkvdg ntnlrygylk yrgegfasip distlasatn yrsntdlnkl mrqgtnvvnt
      661 isntlseyft avysydnryv inlnsrldas nrfgqdankr fnpslsfgak wrigeepwmq
      721 wahswydmfd isfsygwrgn avtevspyli ardqglhdyf kqyylgiisl pypdlgwekt
      781 kdwnlgvdfs ffngrlsatf nyynkiskvi ssatvgaeyg vasayidgtk mknygyefli
      841 sgtpirtkdw twslsfntsr dfnhvennnf tntpaeylsg saivrdeayg tlyafdfggl
      901 epktgkpiin glkpdktptd frgylvkigk inpdisggvn tslryknfhl ratfamqfga
      961 kaylpkyfat tglprpeanv ptymfdrwrq pgdeshtdip sipagnpndt yvtlyygtsg
     1021 tymsslydmy nsstarvadt dfircrtlsl qydlpnslys rlgmrnayvs asltnpffia
     1081 fdgawkgrdp etaswparrs fslsvnltf
//
LOCUS       WP_092113226             900 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            KH2C16].
ACCESSION   WP_092113226
VERSION     WP_092113226.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. KH2C16
  ORGANISM  Prevotella sp. KH2C16
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 900)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 900)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 900)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..900
                     /organism="Prevotella sp. KH2C16"
                     /db_xref="taxon:1855325"
     Protein         1..900
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98462
     Region          38..898
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mltylrpclv alltatsipa caqriqnadt asvisrlgsa dritekrmnk glvtnpleal
       61 ngqaagvnvs ssgsdrmaml ssvrvrgtts ltggndplvi idgvssdlat lstiypadie
      121 sftilknase taqygtrgas gviqvatkhg hegqfhisyd gnigfesvyk tigmlgregy
      181 igtakllgld yndgghdtdf qqeitrtgfv qnhhiafsgg teksnyrasv gfmnhnmvvk
      241 inkyqnfvak idltqsafdd flkidlgvfg ssqkawnifd kqklfysaat qnptfpfgrd
      301 adgnwnknst asqinppgal lgekndeksl nfnthvkllf alaknlnlsl fgsysynsle
      361 naqfcptwvw aqgqayrgeq ktesllgnim ldykyaagph aldltllgey qrqnlsgfwt
      421 lakgftdnaf gydnlgagsi lpyggtgskf enpalasgmg sigytllgry klnltlradg
      481 ssmvgknnrw gffpsvsaew dlrkepflss vplkavsqlk lrtgygesgn lggispfnsl
      541 qlfspngvvp fngsttvtmg ilrnvnpdlk wetrgtfnig adlgfwnnrv vmtaeyyysk
      601 trdmlylydv pvppfaydkl lanigsmsns gfelgmgitp ilkrdmelnv nvniafqknk
      661 ilslsgdyng trmsapdits igqlngagfh ggnnnivyqi vgqplgvfyl phctglqqnv
      721 dgsyryqied ldhsggvnie dggdryiagq atpkmtlgsn isfrykdfdi smqlngafgh
      781 kiyngsalty mnmgsfpdyn vmsdaprqni kdqtatdywl ergdylnldy ltvgwnvpvk
      841 sryisllrls csvnnlltit sysglspmin syiadstlgi ddkrsyppyr sfsfalsiqf
//
LOCUS       WP_092113655            1126 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            KH2C16].
ACCESSION   WP_092113655
VERSION     WP_092113655.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. KH2C16
  ORGANISM  Prevotella sp. KH2C16
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1126)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1126)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1126)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1126
                     /organism="Prevotella sp. KH2C16"
                     /db_xref="taxon:1855325"
     Protein         1..1126
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125247
     Region          132..1122
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitrgfkkg yvlwlliglt lmpclafgqd tkttvwkdtp vtlrksnval gkmlelvahs
       61 vgatvefrnv slvgidkptt lnitnrpldk vvddligdqn vlvtyeegrh iiisayqtaq
      121 sdkashedec flqgivqdgk taeplvgati mitsasqtae vargsvtdan gkfeikvprk
      181 asirisylgy ktqsievlrs nndmkinlqp dgainmdevv vtgiskrskt sftgnyvevs
      241 geklrqlnpn nflkglqffd psfkvlenns lgsdpnaqpe frmrgdqslg sssnantmdl
      301 mldnvsskpn tplfvldgfv vsmsrilqld pqrianvtil kdaaataiyg srasngvivi
      361 etkvapdgal svsyngglti mapdltdynl mnaeeklnfe ymagvynsan atsmnrynql
      421 rrnvlagvdt ywlsqplrta wqqrhslsaa ggtevfrysl dlnatfspgv mkgssnntks
      481 vnfnmtyrkq natvgasinl aetdghnspy gsfseytrvn syyrpyddhg kplqdldsyv
      541 gassvlianp lynanvgikd athnmnisss lnleyrllen lriteqlnyt rgiaraerfl
      601 pashtsfinv mdktlkgsys kntgemtswa snfglnynqs lgkhllsmfa nwnvhedrsn
      661 yvnlsatgyp dphmddfifg nkmsqnpsgt esivrsmali gqlsysydsr ysadfnisge
      721 vnssyarhtl tpfwsvgarw nayrekfleg rvsnlvlrat ygvtgsqnfs padaieyytf
      781 sgtmkpyvsf pmlgavmsrl nnadlkwakt ynlslgidlg fwknranmsf nyydnitrql
      841 ltnydlapst gfssqiinag elqnkgfdat lnvivlqnir kqiywtiagg inhnrnkirk
      901 isdylrkmne eqlasasapl pvyqegqstt tyyavrslgi dpmtgkevfl trddqktfvw
      961 daadkvpvgd tspdasgtfs tslnwkdfsa slgftykwgg vvynqtlvdk iensniaynl
     1021 drraaedrwq kpgdiakykk vdlngsetpa strfimddne vrlaslnvgy rfnaekygfm
     1081 ktlnlqalnv nfttndlfri stvrmergls ypfarsftft vsaifk
//
LOCUS       WP_092117120             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium erythrophlei].
ACCESSION   WP_092117120
VERSION     WP_092117120.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium erythrophlei
  ORGANISM  Bradyrhizobium erythrophlei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bradyrhizobium erythrophlei"
                     /db_xref="taxon:1437360"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38955
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid aseprvavsp dtikkfkalg aevavepgag vksglpdsel iaagatvsad
       61 alkdadiiik vkrpeasels kykrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tipaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegarpge
      301 vvetdgikiv gytnvagrva asasslyarn lfsfietmvd kaskalavnw ddelvkatal
      361 tkdgavihpn fqpk
//
LOCUS       WP_092116800             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium erythrophlei].
ACCESSION   WP_092116800
VERSION     WP_092116800.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium erythrophlei
  ORGANISM  Bradyrhizobium erythrophlei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bradyrhizobium erythrophlei"
                     /db_xref="taxon:1437360"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38993
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid aseprvavsp dtikkfraig aevavepgag vksglpdsel vaagatvsad
       61 alkdadiiik vkrpeasela kykrgalvia imdpygneaa lkamadagvl afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tipaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvtg emvksmkpgs vlvdlaverg gnvegarpge
      301 vvetdgikiv gytnvagrva asasslyarn lfsfietmvd kaskalavnw ddelvkatal
      361 tkdgavihpn fqpk
//
LOCUS       WP_092119220            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Proteiniphilum
            sp.].
ACCESSION   WP_092119220
VERSION     WP_092119220.1
KEYWORDS    RefSeq.
SOURCE      Proteiniphilum sp.
  ORGANISM  Proteiniphilum sp.
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Proteiniphilum.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Proteiniphilum sp."
                     /db_xref="taxon:1926877"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121596
     Region          33..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maallqgtgc iytvhenhiv iskapvvaqr vkknitgtvt deqgeaviga nivekgttng
       61 tvtdidgnft lsvennavlh isyigylaqd intagktavd iilhedtkal eelvvvgygt
      121 mrrrdltgsi vqirpdniai enpktvqdil rgtpglqvgy nasakgggtl mlrgqnsvyt
      181 sedhnsplli ldgmpfygel seinpddiaq idilkdasaa aiygskaasg viiimtkkgg
      241 qgkpvvnatt nigvtqltty lnrrgpeayl qhrqdwlekn tygvnsgtgl yeayqtgvyt
      301 aqpgyytnpg qlsnvsldaw rgyttnesge sdlsiwarrl gfqgntlanl lagktvnwkn
      361 htyrtglnqd ynvsisgatd kvnyylsfgy lqnqgtvvsd dyqatranmk mntkvnswfe
      421 vganvnfqdr sdgsigvdqd qnmrnspyad yadedgnplq yplsseysqr gynydfqkqy
      481 lelekgytvl ntivnakltl pynitytfna spryqffydr yfmsadlpgs dpaargvnre
      541 qakrfdwsln ntinwdytfn kkhhvmvtlv qeaeelqywq driearnmqp tdalgfhntk
      601 nstkedssys sedtyqtada llarlfyayd nrymvtgsir rdgysafgss npyatfpsia
      661 gawtftnekf fqwndvmnng kvrlsygkng nrslsspyla lanlyegagk mqgyinasga
      721 lelyrylman rmanptlqwe ktaswnlald fgflndrisg sieyynksth dmimnqrlpe
      781 ftgfssittn lgqvdnrgie lslhttnirn dllewntslg lsynkneikh lyyeyedvld
      841 tngnvigtke sddltngwfi gqpintiwny rvtgiwqkde weeaarygqk pgdpkvannh
      901 tdddvinadg tvtpvyndnd keflgqttpp fhwslrnefi lwkslsfsfn iysymghksl
      961 styylnnddd ggrmsygman liereywtid nptnkyarie aqgptgassp gklydrsfir
     1021 lenisvgytv pkkimkqwdi etvkiygtvr nvavwakdwe ygdpetagya srvwtlglnl
     1081 tf
//
LOCUS       WP_092123493             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium erythrophlei].
ACCESSION   WP_092123493
VERSION     WP_092123493.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium erythrophlei
  ORGANISM  Bradyrhizobium erythrophlei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bradyrhizobium erythrophlei"
                     /db_xref="taxon:1437360"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38939
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid aseprvavsp dtikkfkalg aevavepgag vksglpdsel vaagatvsad
       61 alkdadiiik vkrpeasela kykrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tipaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvtg emvksmkpgs vlvdlaverg gnvegarpge
      301 vvetdgikiv gytnvagrva asasslyarn lfsfietmvd kaskalavnw ddelvkatal
      361 tkdgavihpn fqpk
//
LOCUS       WP_092131521            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bizionia
            paragorgiae].
ACCESSION   WP_092131521
VERSION     WP_092131521.1
KEYWORDS    RefSeq.
SOURCE      Bizionia paragorgiae
  ORGANISM  Bizionia paragorgiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Bizionia.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Bizionia paragorgiae"
                     /db_xref="taxon:283786"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123896
     Region          22..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkflyvvfl lafttgwsqd mrtisgevtg aedgfplpga svyvaknmvp setgvdgvle
       61 nisigvvtgf dgeftlkipv dvtqivvsyl gyetktinit rattyaialk edvaslnevi
      121 ltgyqkvekr kltssvskvd medigqigva svdqmlqgql agvvattetg apgtptkiri
      181 rgtaslsgpq dplwvvdglp legndvpdfs dkdnidqlrn yaiaglnpdd ikditilkda
      241 aataiygara angvivvttk kgksgrmrvs fsantffssq pnfdklnlmn aqqkvdfelg
      301 lasrtdldfr tgkgeiaril essgelaayq mngfsslste tqlainalrn stvdwgdlly
      361 qssankqysl glsggtdtsd yyfslgyyde egttigtgle rynitlknnf eindrikvga
      421 siflsqskke syltgtdaft npanysrnvn pyfnpyqadg sfnydqdieg tdgryvpfnf
      481 leerqntsyd lknqaikaif dgayeitndl tfstqlglqf dqtstekyaa qetyfsrker
      541 eksrrydssi gdyyyflpeg giiqnwnddf fqynwksllt yttrlgdkhe iegllgaelr
      601 rskftsimsr gfgynsntlt ttpvifpnes tanestyemy nkmsaenaya sfyatgsyty
      661 drkytffgsv rydgsnlfgv dpkykylplw svsgswlase eeflsesqvi snlrlrasyg
      721 lqgnidrnts pfvvgeydtt silpgtseev vvvtsppnsk lrwekttntn vgmdlglfng
      781 rinlaadvyh rnstdliglr svplengfef tnlnwaevtn kgyeislstr niqtesfswt
      841 ttinmshnks tvdniqvren sflpsreglp vnavfalkta giddngyplf qrgdevvsav
      901 effklkdpwe tffpgqlves elsneefrdl fsyvgdrdpk fsggvintfk yknidftiaa
      961 nfnikqtvve rppyngtemd rgqnystsil nawspsnsss nmpgivgqns gtgdswmayk
     1021 wfsgvnpiet mplldiwvke msyvrinsmr lgysfpeavt sklninsfrl siegrnlfvf
     1081 gtdydgyfdp etygniyaqp itksvalgln vtf
//
LOCUS       WP_092132350             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polaromonas sp. YR568].
ACCESSION   WP_092132350
VERSION     WP_092132350.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. YR568
  ORGANISM  Polaromonas sp. YR568
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Polaromonas sp. YR568"
                     /db_xref="taxon:1855301"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38211
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeit agetrvaitp etakklkaqg htvrvqsgag vaasvpdeay tavgaeitda
       61 agaygadivl kvrcpldsem glakaggvlv gmlnpfdaag lqrlaaaklt sfaleaaprt
      121 sraqsmdvls sqaniagyka vmmaaaeyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslggkf idvpyetdee reaavgvggy akpmpaswld
      241 rqkaevakrv aqadvvitta lipgrpapvl vtedmvkamk pgsvivdlaa pqggncplte
      301 pgktvvkhgv tligqtnvpa lvaadasaly arnlldflkl iitkegtlnv dleddivaac
      361 lmtqggeikk k
//
LOCUS       WP_092133890            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bizionia
            paragorgiae].
ACCESSION   WP_092133890
VERSION     WP_092133890.1
KEYWORDS    RefSeq.
SOURCE      Bizionia paragorgiae
  ORGANISM  Bizionia paragorgiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Bizionia.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Bizionia paragorgiae"
                     /db_xref="taxon:283786"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113590
     Region          25..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lflafvvqlt faqeksisgt isdenglplp gvnivvkgtn sgtqsdfdgk
       61 yalsastgdv itysfvgykd vnktvgtsnt isfsmevdva tidevvitam gikrekrets
      121 yvtesvdsdk lltvqpqsaa salagkvagl qinvqdngvk pstqillrgl rsitqsnsal
      181 ividgsistq gafdqlnpnd iesintlkga taaalygsra angallittk tgqkgdkfti
      241 gvnssytieq vaympdfqtq ygsgwqgayd pyentnwgpa fdgvrrrvgp ifndgsyqsl
      301 ayapikdnlk dfyntggssn ntvyvsgsde knrfymsfgr letegivpdd tytrnslrvn
      361 asrkmgklel gltssyttdk sdlvgqtigs qdrplywfil nttaniplsq ykdwrndkya
      421 spngwynayy qnpywaidtn rdtdksnrlv anmnadwevt ewldltgrig vnslnsigke
      481 wrdaqayapn sdyletagrp dpvssfvedy eaqsleysad flaqsefels ekfnlkailg
      541 attltqklrq sayrannlsi pgfydlsntt gqlagglvgg afvnervkrt yglfgdfslg
      601 ydnflfasfs grqdytstls sdnnsyfyps fglsflfsdl lnfdalnfgk vtysnatvyn
      661 dlgpysinet ygqqagfpys stglngfvvs gvavdtnvqk ekiktdeigl nleffkrrvt
      721 lnaayyqttt tdlittatta psagsnsilt nigsvegsgv elslglvpfr aendgdfnwd
      781 vnvnfttnen kvvsiqpgld qiqigggats glwavvgedf pqvravgyer ddqgrvivna
      841 ntgnpvvggl kdlgkttpdy ivgltnavsy kgftltgtmd yrtghvyisq lgdameftgr
      901 saesvssnrq dfvfpnsvvn vgtandpvyv annnipvtgg rqnfwtntyn dikenyvkda
      961 talklrevsl rydmpskyld nafisklsia ligrnlitwl peenrfsdpe fnnsagngig
     1021 lggyfqsppt rsfgvnlnle f
//
LOCUS       WP_092135296             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus sp. YR651].
ACCESSION   WP_092135296
VERSION     WP_092135296.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. YR651
  ORGANISM  Cupriavidus sp. YR651
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus sp. YR651"
                     /db_xref="taxon:1855315"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39264
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipqetr agearvaatp etvkkyvaqg hqvtvqagag vrasipdaaf eavgarigta
       61 aealgaelvl kvrapddaer aqikpgsvlv gmlnpfdien narmasaait afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyrr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfltdee reiaqgvggy arpmppdwmr
      241 rqaelvhera kqadivitta lipgrkapvl lqedtvrqmk pgsvvvdlaa aqggncpltv
      301 pdevverhgv ivightnlag mvaadasaly arnvldflkl ivdkdarftl nleddivaac
      361 lmckdgqlvr qaa
//
LOCUS       WP_092161273             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Allobosea
            sp. CRIB-10].
ACCESSION   WP_092161273
VERSION     WP_092161273.1
KEYWORDS    RefSeq.
SOURCE      Allobosea sp. CRIB-10
  ORGANISM  Allobosea sp. CRIB-10
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Allobosea sp. CRIB-10"
                     /db_xref="taxon:378404"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38998
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaetq gaetrvavtp etvrkfiglg advavekgag lasgitdgey eaagaklags
       61 aaealagadi vlkvrrpaeg eiaglpagal vvgimdpygs eaqvealaka nvsafamefm
      121 pritraqvmd vlssqanlag yravvdgaae ygralpmmmt aagtvpaaki fimgvgvagl
      181 qaiatarrmg aivtatdvrp atkeqveslg akflavedee fkqaqtaggy akemskeyqa
      241 kqaeltashi akqdivitta lipgrpapkl isaamvesmk pgsvivdlav erggncelak
      301 pgevvttang vkivghlnvp grlpatsssl yaknlfafve tlidkaekkl avnwedelvk
      361 atcltkggav ihpnfaaka
//
LOCUS       WP_092167624             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_092167624
VERSION     WP_092167624.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38790
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvgqg hkvtvqsgag ikasvidsay eaagatigsa
       61 sdafgaelil kvvapsdsel tliksgtvlv gmlnpfnnet ivklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_092167652             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Allobosea
            sp. OK403].
ACCESSION   WP_092167652
VERSION     WP_092167652.1
KEYWORDS    RefSeq.
SOURCE      Allobosea sp. OK403
  ORGANISM  Allobosea sp. OK403
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Allobosea sp. OK403"
                     /db_xref="taxon:1855286"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39968
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaetq gaetrvavtp etvrkfiglg aeivvekgag lasgindady eaagasiakn
       61 akdalkgaai vlkvrrpsea eiaglpsgal vvgimdpygn eaavealaka kvaafamefm
      121 pritraqvmd vlssqanlag yravidgaae ygralpmmmt aagtvpaari fimgvgvagl
      181 qaiatarrlg aivtatdvrp atkeqveslg akflavedde fkqaqtaggy akemskeyqa
      241 kqaeltashi akqdivitta lipgrpapkl iskamvesmk agsvivdlav erggncelak
      301 pgeiavtang vkivghlnvp grlaatssql yaknlfafve tlidksaktl avnwddelvk
      361 ataltkdgav ihpnfapkpa pvvegsv
//
LOCUS       WP_092168179            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092168179
VERSION     WP_092168179.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116871
     Region          36..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkstlhlpc hraslclgll lflglfasea naqnrvsgtv rnesnevlpg vsilvvgtti
       61 gtvtdidgqy qlavpegser lsfsfigfes qtvdvngrst ldvvmredsq dlgevvvtaf
      121 gvqrerkelg ytvqalkped ltsandfnlv nslsgkiagv qvtnsgsqvg assrivirgn
      181 asfsgnqplf vvdgipidns ssnlggaggl dygntaadid peniasltvl kganaaalyg
      241 nrathgvili etkkgqqgkq glgvelnssl vfdvpsffmd fqndygpgqr ggeydwqqyl
      301 qnnpgsnlsy neyakqnsyn yvngigggin enatswgpry dagllldqwv kgpnspwesi
      361 pnnihdhyfq tgsnlinqva vtargkeayg rvafsnrqmt gtffntdqtv ntfnasltll
      421 ptdklkvstd fnyvnrfsdn ipvvsygsmt klawgafrni pldevkkvyr ehgnemgsgy
      481 nqnannfyyd lentnsmdrk rffgnvnidy qlndwlsanm vtgldyytee rksitlsrtr
      541 aninnnrggq fsltnlsrqe fnsdirlnin kqflndfslv alvggnfrqn tadflslsap
      601 dlavpdlfni snvrgtpgts msesqretys iyssatlgyk gylflgatgr ndwsstlpee
      661 nrsyfypsvn laltlsealn mtsrtlshaq vraslaqvgs dtdpyqlmgt ygtttfnnis
      721 lftptavkpp tnllpemtts fevgadlrff sdrlsldaty yrqvtenmil qvptarstgy
      781 asqlinaaei enkgieiilr gslvqrgdfs wdatvnwakn tstveslyqg lenitissgf
      841 ggvrlvgtpg qpwgdlsglp yvrddsgnim inpngtpmtt nqqvilgnvt pdwiggiqns
      901 fryknvtfgg lfdfrmggdf fsttywhsyp tgafensvqn nvraegivve gvqgdgspnd
      961 vrisaqdyyn gswvwnnhey siidgsfikl reltlgyrfs vwklqnvnvs vfgrnlailh
     1021 rsakakelgl dpesasqmgg geagtgfenf mpptnrsygf nlrial
//
LOCUS       WP_092169828             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cyclobacterium xiamenense].
ACCESSION   WP_092169828
VERSION     WP_092169828.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39165
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgilkeps petrvslhpe avkvltgsgn qvlietgagd ssflsdavyq eagatvksrv
       61 evletaemif qitpldaedq kklsrgkylv gvyqplvare lmkslaetgv tllsmdsipr
      121 itraqsmdvl ssmstvsgyk avllaaanlp rffpmlmtaa gtiapakvli igagvaglqa
      181 iatakrlgav veafdtrpsv keqveslggk fvevpgaved kgaggyaveq seeykqkqse
      241 mleksiiksd vvittalipg rkapilitrs mlekmkagav vvdlaaangg ncegtennkt
      301 vtlsgvtiig nsalpasmpe daskmysknv qnllklllne dkinlnfede iikgtcithd
      361 gaiiyepllk
//
LOCUS       WP_092169801            1153 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092169801
VERSION     WP_092169801.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1153)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1153)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1153)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1153
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1153
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127501
     Region          135..1152
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhvllkpik nlkvrllafg ilcflvahtg yafdsvksie evmikldirq gslqeildhi
       61 etktdyrffy tdngiddeqi lklnqvkgsv adilkelare krlhfkqvnn tisvrfltek
      121 tgrkaleivv evadievsgk vvdpsgeplp gvavsvsgtn igtitnidge ftltapedgv
      181 lqvsyigfst qrieinsrsi initlqedia gleevvvtal gikreakslg yatstvesee
      241 mtinrtpnfm nslqgkvagv nitsmgsgpq gsskvrirgv ssfggnnspl ivvngvpidn
      301 tnfgvsgdvs evgsnrnsds gdglssinpd ditsmsvlkg aaasalygar akdgvimitt
      361 rnrasgsgiq velntnytnd tpldftdyqy eygqgeggir pnsprpvsgv wsfgerfqpg
      421 mtqilfdgie vpyepqpnki rdyyrngstf tntitissgg enggfslsas nmdskailpg
      481 snynrktinm gftqnfkklt vsgninyske drinppniae qdfspvviyt latsmpmdll
      541 eqyafdengd efpysrftnr tnpyfalsrf ennvrdrvyg nitaryditd wlyaqgrigq
      601 dffsrdseyn lptgsrrqsa pppgfvngqf vqdmrtfrev nadfligmdk tfgdfgllvn
      661 lggnqmyrrl dvntllgenf ytrdlytign sskittnyti serqvnslya stelsykgfl
      721 yvngtarndw fstlspanrs ilypsitgsf vfsqafanlp nwisfgkvri ayaevgsdtd
      781 vqpyannlfy ninqqqfpns ngiaqpvgsi sgsvvpndnl rpmrvserei glemtlfdnl
      841 rfevsyydkl ssdqilqaqv sdgsgylnql invgeskntg lemfaaispi tgpnfnwnfs
      901 anaaynqsev lslgddvegt fitvgradfh gevrqevgkp maqlygwgyr rdeqgrqifd
      961 pnngrplrst eqlnfgtaip iwvggftnsf nyknlnftfl idyklghkmi sgthtnayrh
     1021 gldkatlegr eqgfvvgdgv npngeintaq spiqtyyeti rsgrmseqsv fnagswqlrq
     1081 vtvgydftph lpdnnfirgl rlnlvsnnva vlkqwvphih pdqngiisdn ragleatglp
     1141 vtrsigfnln vkf
//
LOCUS       WP_092169135            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092169135
VERSION     WP_092169135.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119805
     Region          39..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksllylrs rffgpsyglg iltlvvllgn anmllaqtrt vrgqvtessd sepvlgasvl
       61 ikgttrgtvt dldgnfelev psdeailvfs yigfqsqeiv vgnqsllnvv meysseelne
      121 vvvtalgver etkalgysvq avdgdrftea retnvinsls grvagvqitn sssgvggssr
      181 vtirgessln inanqplfvv dgvpisnniv gssgsrnqev dygnpagein pddiasmsil
      241 kgpaaaalyg sraangaili ttksgknkrg lgvsinsntt fdtplrlpdw qdkygqgnng
      301 lftfvngaga giadgvdesw gplmdqgtli pqfdsprdva gfrggdlnap agstitptpw
      361 vsqpnnindf fqtgrtlsnn isiasgners nfrfswtnld qkgtipntdl krntlafngm
      421 sqitdrlsit tainyqnsas gnrpsisygt eslmylwiwy grqintqnlr dywmpglegr
      481 qqfnynynyh dnpyfnvyen tngqskdrif gnvvvnykft dklnlmvrtg ldlyndlrdr
      541 krafstqrfp fgsyredavf fnerntdfll sysetekpnw sytvslggnq miqenrftrt
      601 mapqllipei ynftntavnl qvdhmvsekr inslygfgqi gyknilfldi tgrndwsstl
      661 pvsnnsyfyp satmsgvisd mvtlpdfvsf fkiraayaev gndtnpyslt nvfnpavawg
      721 siqsktesnr lanaelkper tgsvefgtdi rllkgrlgld ftyydnrtrn qiipieldis
      781 tgyasriina geiqnngiel vlsgsplqnv nglnwniman ftrnrskvle ltdeldsysm
      841 vgrngatiqa rigermgniy grgfarvdda nspyfgqiih ntsgtpltsp elvlqgnynp
      901 dwmlgiqnsf nykkftfgfl fdiryggivv srtktigsta gqleetllgr engydlsmdg
      961 ngiispgvir nadgsfvpnd rkissrdwhn ryyersnvea akydasfvkl revtlgytip
     1021 gtsmgklpfq earlslvarn lalwtenphf dpetmsmsgg tlipgvedma ypssrsigfn
     1081 lnlkf
//
LOCUS       WP_092169948            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092169948
VERSION     WP_092169948.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118372
     Region          58..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekilqsygi qgarrigltl wiglwlvstg farptvvnpa slspsdqpnl aipaedditv
       61 sgtvtdesge gipgvtvfia gtgtgtvtdi dgayslsvpe gseltysyvg fvsqtitvgn
      121 qseinvtllm dtasleevvv igygtarkrd ltgavssvta trlenenpns vqdvlrgnia
      181 glnvglntsa kgggslevrg rtslnagssp livldgaiyy gqlsdinpnd iesidvlkda
      241 ssaavfgaka angvvlvntk kgalgkpqvk intnwgvatm aknepvygpq gflswredvm
      301 esinaggfep yrfsnpntlp pdipletwln ydgsdgdpet vwlqrlnmqp leianykage
      361 svnwynmmfq nglrqdhtvs lsgrsedfqy ywsmgyldne glvvgdkftt vrsrfniegn
      421 vnewltvgmn tqfadrdesq ipvswgnmvn lspwgepfle dgvslrfrpn eevsggrhpy
      481 ytpsftdrlq kettinstlf asielpfgik frtnftprye fyerynhesa ghqdfenmgg
      541 rasrqqrkvy ywqvdnilsw nknfnnihnf dvtllanaek fqswdntmqn vgfephdrlg
      601 yhnigaginp imssndqyht adalmgrviy slsdkyittl svrrdgysaf gqsnpratft
      661 saafawlftd edfvnipwld ygklraswgv ngnrdigrya alsdlqtgky fyqrpsgely
      721 fvsqlyvntm qnsnlrwekt tstnlgldfs lfnsildgti evydmsttdl lverslpdil
      781 gfdfvfanlg evrnrgvevs lnsqlvnrsn lswranlnfq mnrnrivsly gdldengeel
      841 ddignrwfid haideiwdyr tdgiwqtpea deaanygvkp gdfkiedvnn dglytnadrq
      901 flgfreprsr wslrnefkiw rnfdvsfmmy aylghlgtfn qrknrqgfld rsnsyilpyw
      961 teenpsnewa rlysseggag gfnvyqsrsf vrmeniamay tvpqtilera kiqnlrlyln
     1021 vrnvgfyape mnfwdpesgg ptpriftlgl dltl
//
LOCUS       WP_092170682            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092170682
VERSION     WP_092170682.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113190
     Region          27..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrftlyfv lltcfllqgs vllaqqrtvs gtitstedge vlpgvsivie gtstgtvsdl
       61 egnysldvpg pnavllfsfi gfatrseqva nrqtvnials peagdldefi vtafgisqek
      121 kslgysaqsi daeaitkmkq pnlvnalqgq vagvqvtnsg gapgqsarii irginsldpg
      181 adnqplfvvd gvpvdnstie ssgtprglsn rmadvnpndi esmsvlkgaa atalygvraa
      241 ngaviittkk gkegqirvny sgsvgieeln rlprlqdeyg qgfsgqyqpn sfwpswgapi
      301 sqvqqtvpdh ryqdnwnraf ntgvqvdnsv sisggnekat fygsignltq egiipfstwd
      361 rttaklsgsv kanekfdfsg sinfsntggn rvphdrfmer mmywsettdv rdyinedgtm
      421 rtygntnpiy darfatyedd vnriigninl nynptdwlsf syrlgndfys dtrteitpgp
      481 kgidgerals stglleetri nsrdltsnfy itlkkqfnsd wntslrlgnd iferrfdrit
      541 argenfvipe fynlnnttqi fasqgkslrr lvgfygdlmv dyknflflnl tgrndisstl
      601 pkdnnsffyp svnlgyvfse nlslpswvtf gklraswaqv gkdtnphilg atyaspsifp
      661 lngqvgftrn svfgdpnlrp elttslefgl qtafwdnran fdvtyyksna qdqiipvpis
      721 datgfssyit nageiensgf efilggtpvq tqdfswsina nlsinnneik siregideiv
      781 vgsqfgyvgs tvtmkliege aygnifgssy qrlgadpdnl fldrslpvii gangfpvrtg
      841 tqlvlgnavp kwiggirndf tykgfelsfl vdfrtgveqy nqfanflsaf gknefteare
      901 dfrvfegvla dgspntqevw lgqgvgpdgv nygagywrnh yrttsenfvt dasfiklrnl
      961 tlgynlspgi lestpfrsar vsvaanniil ytpwdgfdpe sfsagaggna vgftglgfpg
     1021 vqsvffnlnl gl
//
LOCUS       WP_092170066            1135 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092170066
VERSION     WP_092170066.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1135)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1135)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1135)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1135
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123733
     Region          56..1129
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknekkllvn svgikrnvff lfqgivlacv latqalaatn paapaafeaa aaeldirvsg
       61 tvtdendapm pgvtitvqga smgtvsdieg kyslnapdna tlvfsfigfk tqtiqvgnrs
      121 tidvtmqedv gsldefvvts lgvpreqral gyatttiksd elvkvgtpnl atalygkapg
      181 vriqagagga tsavnitirg insitgrnqp liildgvpir neevtnnnyw gdqrlrgngl
      241 ldinpediad isilkgasaa alygseavng vvlittkkgt skgftvdfna nytqdeiayl
      301 pryqnvrgpg apqhvqalsw anngvnedgf fiyedgsrgl pntninygpr fdgqparswd
      361 gemrpyvaqe dnyaalfnnp vssqvnvais nstdvadfrv sltrqdneal slnsknskni
      421 anlnatfrvs kkvrtdvmvn yinqytanrp ysvdrlinnf ggmmtrfdng awyldkykts
      481 lgyrfvtgng qsltpdenit fngfqgaigd yvwrvnehra selsnrvigs itnfidftde
      541 ltlraristd ftyrssenet sttrplafgp sggfsmsnet fnilygdlll tyrkqltddf
      601 tfsamagyta nkesfssisr gtngglssen lfdivasvni pnngsrrtsr vidaalgtvn
      661 ldykgiwfve gtvrrdrtst mnpdnnsfvy psantsfils davdlpsfvs faklrgswgi
      721 vgnypdvyra niaynqntlg vqqpggapvl ytnipssfgn dgirpeqkhe fefgldsrff
      781 agrlnlefsy ynaqirdqil pltlpatsga nsvlanigtl rnkgieialn gtlyqarglt
      841 wmagvnfarn mnvveklann atellhadyd gnaaqlrsvv grpmgdffar pvetnangek
      901 ivqpngmyki dannwilagn ampkavggvf nnlayknfsl dimadfqigg hvmptginwm
      961 isrglteesl kymdaesggl ayylnaegqg vqtsspqgpn getvyndgml megvtadgnp
     1021 ntnvisqamy yqrtynwggp qysqaryely ikentymklr elslgyqvpa afaqklgats
     1081 invsafgrnl fffyrnikdl dpevltggsr waqtltsagt npatrtvglm lrarf
//
LOCUS       WP_092171537            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092171537
VERSION     WP_092171537.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118257
     Region          39..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfthapnr rsggrnsftw lflligflsv gsvqaqsltv tgkvvdenam sipgasvlvk
       61 gttkgaatdi ngefsltlse sekelevsfi gynkkevaig nqseitislt peetalsevv
      121 vtalgvkrde ralgytvqqv dtrgldeake tnivnsltgk iagvqisnss gniggssrit
      181 irginsisgn nqplfvvdgt pidnsnynst dqvsgnggrd ygnaaqdinp ddvesisvlk
      241 gpsasalygs rasngvilit tksgaknkgi gvsinsstmv snvfllpemq neygggfsld
      301 feevvdpldg ltykvvntna nnswgprfdg tpvrhwdsmy pgepnygevr pwqatpnnir
      361 dffetgvtls nnvsisggdd kssfrlsytn ldqtgvmpns slnrntiavs antqitdkfs
      421 agakinyirt ealgrpatgd wsperpvnvl tywyawtqrq idparlrnyq sdryyhmtwn
      481 tqglgrhteq synnnpyftl fesynndlkd rvfgninisy qilpelsvtl fartdfytdv
      541 redrasiggy lqnayekdly nfrednfell gqyntefgdd fslgvtfggn irkntftnny
      601 trtqgglsvp nfynlvaslq rpeirdfkse revhsiyasg nlgyrdflfl easlrndwss
      661 tlpvdnnsyl ypavsssfvf snlmtgadfi sfgkmrlgwa qvgndtdpyr lintyangdp
      721 yantsvftvd dvlrnsnlkp eivsnleagl dlrflenrig ldftvykvnt fnqilalpvs
      781 sttgfqsliv nagemenkgi evmlsgtpie rndfswdvnl nlarnrnrvl elaegqdnfe
      841 lggrdgtnsv natvgqpygt iitpnviyhe etgkpivgsn gfylrnpgev vgsilpdvtg
      901 gfsntftyrg islsalidfq sggsfwsetv qngiangqfi esvgdndrgv pkrspvsegg
      961 giradavfen gepntvylea qnylkqmysl dglsvydasy vklreislgy nvpsvmlrnl
     1021 finglrvsvf srnvallhsn vphidpseia ygssnvqgle gaslpaprmi gfninikl
//
LOCUS       WP_092172806            1143 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092172806
VERSION     WP_092172806.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1143
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124855
     Region          33..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgkqlhanrl gvvlilfwfl tgtcyldala qsrqvrgtvr ssedglgipg vnvliqgsqa
       61 gtatdaegnf slevpgagtv lvfsyigfqp veetvgnrsv lsiemipdas dlgevvvtal
      121 girreeislg ysiervdgee mtrvaqesfl namagkvaga tisstgatgs svsmvirgat
      181 slssdnqplf vvdgvpiant lnnvssvgte nrvdygnais glnpddiaei silkgpsaaa
      241 lygsragngv vlittkrgnv drltvsvtsn tvfdvpfkfl kwhsefgsgq fsaipadisg
      301 tplsnpfgsl vqenvnaafg aaldkgyeev qwnspldeng nripiplvsy pdnvrnfmqt
      361 gitsansfsi anstkamnyr isysnmrnkg iipnadlfrn tlninssvav ssrlnvstnl
      421 dvsrnnsnnr pagergtnpl qwvyetsphv nildlkdywl pgqegleqkt vdadqpvrvt
      481 nnpyflanev nnsfirdrvf gnikadwqls psfslfarya ldlyretres kiarsysqep
      541 egaygitelq gfesnadfll tyakdfgpys vslsgggnir yqngsnlfag skpgaglitp
      601 gvytvqniap dniqyansrf ergihslyal anlgykdmiy ldltarndws stlpdaapyf
      661 ypsaslsllv neildfsepf slvkirggya svgndadpyr liaalsnaga wgniprlslp
      721 gtllnpslkp eiatsyeggm dlhlfnnrir fsgtyymven rnqifstglp pstgysakni
      781 nagllrskgi eltlgadlvq spnwnwtanf nltrnrtriv eladelpyyt lwtdarggaw
      841 tyvgeeigdi ydakvvtved pespyfgfpi ldqtgkwqdv davnsrnkig nfnpdfilgm
      901 qtslsyknfh lnltfdwrng gdfvsqtyrf geehgrsqif ldklihpgdr sgaalkeyll
      961 enresmilin gnnfplvggp tpdyggypft fgpftlpygg vfipgvyata fdengnptef
     1021 aenlgenigq pggtltlpya gstawsfara flydasfvkl revsfgydap qrfaqalrmq
     1081 qinfsvysrn iilwtaakin vdpemafqpq agvqagsqfk qgierwnvmp wvmpigfkvn
     1141 atf
//
LOCUS       WP_092172923            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092172923
VERSION     WP_092172923.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110794
     Region          22..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksllvlfl alfaiqgmaq ertvtgtvid adadaplpgv silvkgtntg titdidgqys
       61 isvpgssatl vfsylgygqq eravgnnsei nvslaaeesa lsevvvtafg lerekkalty
      121 tvqdvkteel sqarelnvmn slsgkvagls inrsgsgvgs ptrvilrgnr sitgnsqply
      181 ivdgvpaagi enlnpddies invlkgpnaa alygsranng aivvntkrgr eggfqvnint
      241 symfdtpill tnfqnvygqg sggvysrase fswgprmdgs svpfwspdpn sgienypfsp
      301 qpnnvsdfyq tghnfattlt vsggneknqt yfsytfndaa gvvpgnalgr hsvnlrltnk
      361 ltdrltldsk inyikqdidn qltqgenysn ptrhilrlpr nirtedisnf efvneagllr
      421 qnyfnpgsng ganpywaanr nlrtntldri iaftslnyel aeglnvlara aldrstgdse
      481 eklwadsyii aqggrysvgf sesmeintdf lityekslsd dwyfnvnagg narinrnsgl
      541 nsntgpqlti pnffalsntq qvlsthnvga prnvnslygf gqlawknsif lditarndws
      601 stlpranwsf fypsvglnav lsdlvafpew ftfakvrgsf aevgndtnpy qlqrtaslaa
      661 gglggylsls ttlpnenllp ettqsieiga dmrfldnrvg ldftyyrtns fnqlftvalp
      721 vgsgasqfft nggnvqntgv etvltltpvr ksdfnwdism nfarniplvv einddrpsve
      781 iggdflrryr veegrpfgev ysrgylrddq grvivgangv prttpgftvn vanynprwlg
      841 giqnsftykn franftidfr eggsiasltn aiiyadgvte etlegreggl ifgenfmahe
      901 tavlesgepn nipitaeqfw vnmggrnapi gevfsysatn irmreavigy tipssklgnl
      961 pirslginfv arnlffflne agnidpdvtv gtgaaaegfd sfgpptarsy gfnlnigl
//
LOCUS       WP_092173193             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092173193
VERSION     WP_092173193.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107995
     Region          27..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrniyrfslv mflsllsmgw thaqysvsgv vtdertgdpm igasilvqnt tkgtvtdldg
       61 rfnlnfddns patliisslg ylsqnvdvsp gnntslevsl kedatnleev vvtglastvk
      121 rsnlanavss vssreltgtt tiqttdgaly gkiaganirs nggapgggls iqlrgissli
      181 gasqpliild gvyinnsfqr tgratvtgag ganqddganr ladlnpadie sievlkgpsa
      241 aaiygtrana gviiittkrg segrtkvsla qdigfaqplr llgvdgwsee kintffpenr
      301 rptelqrfre stgtidyedy fynntavlsn trltvsggde ktkffvsgni nsedgtvknt
      361 gfdrfslran ldhnitdnik lgvssnyiks ntqrgftgnq nntgasigyn iayvpnyfdl
      421 rpdengnypv npyfgenpia vtdhavndsd vqrfvqafnl dvdllrtnns flranvaggf
      481 dfyqnstlvy lpeflqfqrg qanpgdafwg kqesfntnfq aalvynfnwg kvnmnsqagm
      541 vrldftnssl fnrgrglvpg qtnlrqasiq eivdqfnsev qeagvfvqqe anfedkiigt
      601 vgvrwdkstl ngdpnqyyaf prasvafnva nfdfwnssvl tqlkpriayg etagpvefgn
      661 tftrlegani ggllgsvvgt qignteirpe tatelefgvd lgllnnrfsl eatyyikntq
      721 nniqnlnlap stgvnttpsn eaelqnkgle lslsgtvvdr gnfnwfsrim ywqnrvnmtr
      781 lgipqytlgg fgpalgtfyy aegfapttiv gtpadpnhps gftvwgnaqp kfnasaynvl
      841 riynnlelsf lvewrqggen inltsflsda ggttngwfgd dngdgipngr qrppepynna
      901 grwvqdasfv kvreiglyyt lpkaaltntf gnalegvrfg msvnnaflft dyqgydpets
      961 tfgaqsvann vdiapyptpr riffhvnldf
//
LOCUS       WP_092173372            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092173372
VERSION     WP_092173372.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121139
     Region          67..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknlpncrg lvsksslaai lfalfnggli aapngpdrnl kntekmplla snenlegfrs
       61 napfdvtvtg tvtdsngepi pgatvsvpgt sigtatdidg qysitvpegs slvfsfigfe
      121 sqtievnnqs tidvtlsesa qaldevvvig ygtqqkkdlt gavvnvqaee vmkykptsvs
      181 eilrttvpgl svgyatnarn vpdfevrgdn smkansnder aanrplivld gvifqgdlae
      241 inpntiesvd vlkdasaaav ygsqatngvv ifttkkgqyg kpqitfssrv glvtgarrqq
      301 tyqgeevldw ltdmnetitn sitepwtrfr dfndidpqyq ddwlaangip getdpevirm
      361 trinnfgfwd nevenyrngv tydwqdflfh tgvrqdydlg vsgrtdrvay yfslgysdre
      421 svrlgesfqa itsrlnldvn lgerlsvgtn tqftfidegq efignggyrv ysvydqpwan
      481 gaprtrenln dqaagsnisn pyqgpswntr lhnqiminpt lyaqlelpfg fslrqdytpr
      541 fsirkrfdld ergnpqravd aaerryneaf nwqsntilnw nkefgehrlg ftglyntern
      601 qrwetramtn nfsptaslgf hamqlglnpt mssydevnsr tglmgrvtya ygdrynfsas
      661 irrdgfsrfg vnnllgnfps lsaawtlsne dfmqntgvls ylkvrasygv ngnssgledy
      721 nayarlnsnl ylnydggyfa aprteitria npflswerna sfnlgidygf fndrvsgsld
      781 iyqsetrdll ldqklpeltg fgsvktnvgn lqnrgfdlgi rsinvtrtnf twtsnfnvty
      841 ainkittlgn apipmtdaqg ntvmrepddl qngwfigenk diiwdwdldg vyqmdeadea
      901 aeyglfpgdf rfvdqdsdgd ididdrvflg ltdnpwyitf rndfewknfd lglvflgkfg
      961 wkggtrepfn nsqqyiknkn wytipywtpl ngennfarin sinlgggqvw lnrdyvrlqn
     1021 vsvgysvpps ilekingtrl rlalnienaa vftpwhrslg dpesarempr tysfsldftf
//
LOCUS       WP_092174018            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092174018
VERSION     WP_092174018.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116958
     Region          23..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlllilcl amltamgssv qaqtvsgkvt dqsdgmplpg vsvlikgtst gtatdvdgnf
       61 nlnvpgeqtv lvfsflgfet veetvgnrst inialaedaa elsevvvtal gierdvralq
      121 ysitevggee ftqarennia nqlagrvagv nvsnvasgpa gssrviirgn tslqggnqpl
      181 yvidgipmdn tnfgqagvwg gadqgdgmts vnpddietms vlkgasaaal ygsraangvi
      241 littkrgtsr rgigveinsn vvferinnqt dlqtefgsgr yqgdlitgsa vrpttvrqgy
      301 dwgtqawger lgsgtamhfd gverpyvyag dnwnrfyetg taftnsisla ggsdtqtfrf
      361 nvtdmrsssv vpnagfdrln msiatsgkfg kkltfdakvl ysnertqnrp rlsdspgnaf
      421 qsifalppnv nvewgkgdpn rlgtipigtd pallstwgfa eqeeylmtnn pwgqnpyfst
      481 hqlsindtrd riitsgslry ditdhlylsg ragmdwftrr gttltpqgtg yqrngsmses
      541 errvneinle amlgynrefg dfgvnafvga nrmrredeni sangqgfnvp ffhainnsvi
      601 rnfgygysgw ginsvfgsae vsyknflflt atgrtdwfsv ldpqfndity psvggsfvfs
      661 damnelpswl sfgkvrgswa rvgnstvgpy qiqnvyslrp apavdhggnq vamasfatag
      721 grsgtipnrf lkpllsteie agfdvrffqn rlgldftyyr qrstddqlna qislssgfgs
      781 tlvnlgemen rgieilltgt pirtsdfnwd vsfniarnrn evisliegsd ilnveeprtr
      841 tvfvqhrtgf pfgvlagwvq krspdgqpvf eengapvqsd qmevigngip dwtgginnsi
      901 tfkgfnlsal vdfriggdly sgtnvrltqw glhkqtlqgr ageepltvsg viqsgtatdg
      961 spiyesfskt lspgeannyw nqmgnrvqdf fiydgsfakl rqvtlgynfp rsildktpft
     1021 nlnlsfvgrn lsilwknven idpesgyssg ngqgldyfgm pqtrtfgfnv ratf
//
LOCUS       WP_092178179            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclobacterium
            xiamenense].
ACCESSION   WP_092178179
VERSION     WP_092178179.1
KEYWORDS    RefSeq.
SOURCE      Cyclobacterium xiamenense
  ORGANISM  Cyclobacterium xiamenense
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cyclobacterium.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Cyclobacterium xiamenense"
                     /db_xref="taxon:1297121"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110268
     Region          26..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilsisyg lalllflsfe ghaqtrtltg tvvseadgmp ipgvsvldkt nqtgtatdmd
       61 gnysigvtdn tvlvfsfigf asqeytvgnr srldvelsed aselnevvvt algltkekrk
      121 lgyavstiss dvmdkarepn vansligqva glvvkgtngg pqgssnivlr glpsisgtgs
      181 plfvingvpm dntqrgaagq wggsdngdgi gnlspddies mtvlkgqaas alygarasng
      241 vilvttksak kgedwalsyn lnvmtdqamd ftnfqneygq grggrrpqsa sdarttgrfa
      301 wgepmggsai aydgnqypyv psdetyldfy dvgtnvtntv avskglgddg afrlslsnln
      361 snsivpnsgn drlninlnvd qnitdklnvs aminyidqks tnipnlsdgp knpnnflfla
      421 pnvapsifap gydeegreiv fsddifvtnp yfiankgind rgrkrtistl sakysfapki
      481 yallrvgndv snddffsvdp tglayssdlk gnlngrglst rselnvdalf gadlmltndi
      541 sldalaggtf rnnrfeqvgv ggtrfvipel yspfnvevfn rsygfnerev vsgfysmgfg
      601 ykdyltlttt grydvystlp tdnnsifsps vtgaflfdqf lnvpaldfgk lrasyavtsg
      661 epfaayqtqf yynsansfng vaagssplgl pnlflkpftt deiefgfdls fynsrltfdv
      721 ayfskttnne imnasysias gfssavvatg stnnkglevm itgvpiqtsd ftwrtslnft
      781 nvrnevlstn ldnnpinlgq nratlgnavt ayvpglpgpq iraydyqyda ngdivvndag
      841 lpvrgelknw gsvlpthygg wnnefnykgi gfsflvdysf gnkvlsatef yshfrglhqn
      901 tlvgreegit tneitapaen yyqalvqnvt rtsvvdgdfi klrqltlgyt fpqkwfnsvp
      961 vfkgltaslv grnlailmrk tdnidpeatf gsninylgie gtslpptrsi gfnlnfklh
//
LOCUS       WP_092186853             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. cf659].
ACCESSION   WP_092186853
VERSION     WP_092186853.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. cf659
  ORGANISM  Bradyrhizobium sp. cf659
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium sp. cf659"
                     /db_xref="taxon:1761771"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39087
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag lksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygndaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegakage
      301 vvdldgikiv gytnvagrva asasslyarn lfnfietmvd kgskalavnw ddelvkatal
      361 trdgavihpn fqpkv
//
LOCUS       WP_092194493             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_092194493
VERSION     WP_092194493.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38883
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lhasvpdsay eaagavigdt
       61 hqtyaaelil kvvapdeeal sliksgsvvi gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqatiagyka vllashhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_092203184             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus tunisiensis].
ACCESSION   WP_092203184
VERSION     WP_092203184.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus tunisiensis
  ORGANISM  Blastococcus tunisiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Blastococcus tunisiensis"
                     /db_xref="taxon:1798228"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52263
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpretr aretrvaatp atvgkliglg ydvvveagag aaasfpdday aaagatvtta
       61 eeawradvvl rvnapageei grlrdgatlv gllspglnpd lvdalaarpi talavdavpr
      121 israqsmdvl ssmaniagyr avieaahtfg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvavpdaeqq vssdgyarem sedfnrraaq
      241 myaeqagdvd iiittalipg rpaprlitee mvasmrsgsv ivdmaaaqgg nvagsvpdei
      301 vvtpggvsii gytdlpgrlp aqasqlygqn lvslltlltp akdgqlaldl ddvvqraitv
      361 vragektwpp ppvqvsaapv aavpvppaep apppkpatpg rrfalvglga aalfgltafs
      421 pdeliqhvtv falavvvgfy vighvhhalh tplmsvtnai sgiivvgall qighgdavvs
      481 tlaflailva sinvfggfav trrmlgmftr s
//
LOCUS       WP_092205744            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bizionia
            echini].
ACCESSION   WP_092205744
VERSION     WP_092205744.1
KEYWORDS    RefSeq.
SOURCE      Bizionia echini
  ORGANISM  Bizionia echini
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Bizionia.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Bizionia echini"
                     /db_xref="taxon:649333"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114281
     Region          24..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkttfnsilf lllllptflv aqnqvsgtvt eegssfplpg vnviikgstk gtatdfdgny
       61 qlqvtngdil vfsyvgyvtk eitysnentl nvvlaedaaq ldevvligyg svkksdatgs
      121 vslvttkdfn kgnivstdql lngkvgglri tnsggqpdsa lnirirggss lsgrndpliv
      181 idgvplsnin pagvsnplsl vnpndvesfs vlkdasatai ygsrasngvi iittkkgtsg
      241 apqfnfstdm sinkakdgld mfesneyvrf iqeyhpelan klgvtlgsvq tneaisqiiq
      301 vtnsdgdles raiyntdwrd nvlrtaftsn tnfssraylf nalpfrasvg ytnaegvvkt
      361 ddyervtasl nlspkffddk lkvttnakvt yadknaadvg galggslvfd ptkpvyntas
      421 dnrfggyyfn tnvdgnnlil dgqynplall eqrdrpertt rflgnleldy afdflpglra
      481 vvnlgldask sdkterfydn aaatyrfnse ntdinnnfvf npgvnyrenq tltnttldaf
      541 aqytksyndt fvskfdaqlg ysyqnfkndg nseqyrynei tglrevnenp anlnnryyne
      601 mnlqsffgra nvdlldrylf tfslradass lfvaddpwds nawgffpaaa fawkiksenf
      661 mknanfvndl klrigwgktg qqditaavgy ypntplfvag snssqyipga glysalpfnp
      721 dltwekttty nlgidfsffk nnfisgsfdi yqkftddlla rvtvppgqgf sdtfvknvge
      781 iegkgfevnl nmnayqtedw nislngnvgy vynevtdigg qaninrggsl rgtgsfllsd
      841 vvgeqaqsay vfkqvydtng npipgafvdl ngdniindnd ryyaqiapnw tygfglnvsy
      901 kkwdlssgfv gqvggnlynf nklnygftda vvpannnsit nalnfydgaa npafetvngn
      961 iqfsdyfled atflrcnniv lgytfdnmik ngnvrmygav snpfiitdys gldpenpggi
     1021 erdfyprptt ftlgvnfdf
//
LOCUS       WP_092209840            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bizionia
            echini].
ACCESSION   WP_092209840
VERSION     WP_092209840.1
KEYWORDS    RefSeq.
SOURCE      Bizionia echini
  ORGANISM  Bizionia echini
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Bizionia.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Bizionia echini"
                     /db_xref="taxon:649333"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110906
     Region          25..1023
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lflafvvqlt faqektisgt isdenglplp gvniivkgtt tgtqsdfdgn
       61 ysinaspgdv lsysfigytt kemtvgasnn isfamevdse aleeviital gvertagelt
      121 aatkvveaee ltqaanpnvv qsltgkvsgl qinttnngvn qttrivlrgn rsltgnnqal
      181 ividgvissa ntlanlapei iastnvikga ggsalygsqg sngviivttk sgsssekiev
      241 sinssisfed vafvperqtk ygqgwngiht syenggwgpe fdgtlqpvgl pqadgsyima
      301 pytgdsdnik effktgtilq ngvtlsagdk tgnillsvnn qqtefvvegd elnrttvlfk
      361 gnkqlgrwnv ggnvtyntss vktttsslft ellqtasnvp velfensgne ghwtsyyrnp
      421 ywmrdnirns snttrmngva nikydindni nvvmnssvrn fksysrnytn eyidtigigg
      481 gdhstisqfg qsnseetniy ndifvnfdym ltddisltal vgnniqdnmf sstavsgsnl
      541 tipgyynidn itgrpttsnt iqrdrrfsll gsmdlgykdf lflsltgrnd wtsrladdrn
      601 sffypsvgls fvatnafpgl kkggilnyak isgnwakvgn drvgpyqins tlnqatgypf
      661 gglnsfvldq tiadpllvne fiesyefnln laffkgdrvr ldfsiyeskn sdlvtgitts
      721 aasglanttv niaesttsgf eidlgltpir tkdfrwdldv nfatnetiid kisdqsdeva
      781 laafadigif atageefpli kgtayqrdpq grvlidpttg nplktgsfqv lgksnpdyiv
      841 glntavnykg irlaavmdyr tghqfwagtk dwlswsghlv esadggrrgf ifpnsaintg
      901 taanpvyean tnvitggtty anyldyfsne yrsvsenfvl datafkvrel slsyafskdm
      961 lknvglsslr lgvnarnpfi vlpaenrgya dpeigrssgn dqglsvtgqy pitrtygmtl
     1021 nltf
//
LOCUS       WP_092212592             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Desulfoluna spongiiphila].
ACCESSION   WP_092212592
VERSION     WP_092212592.1
KEYWORDS    RefSeq.
SOURCE      Desulfoluna spongiiphila
  ORGANISM  Desulfoluna spongiiphila
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfolunaceae; Desulfoluna.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Desulfoluna spongiiphila"
                     /db_xref="taxon:419481"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55143
     Region          1..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mnigipreth ddekrvaatp esvktlirlg ygvsveagag eaagfldgay eaagaavada
       61 qtvwtasdmv lkvrppslse aeqmkegaal vsfvqpavnp ellellktrq itslameqvp
      121 ritraqklda lssmaniagy ravveaagaf grfftgqvta agkvppatvl vigagvagls
      181 aigtagglga vvrafdtrpe vkeqvesmga sflmldvdee gggtggyakv mseafikaem
      241 alfteqakev diivttamip gkkapvlitk emvasmkpgs vivdlaaeqg gnceltepga
      301 avvkegvtli gytdmvsrla nqasrlyatn lthlldnltp dkggeavydm edevvrgmmv
      361 tcdgevtwpp papkasspgp qapkeaekaq vpeagalrkt warwspqvmp flllavggfl
      421 lyemgrvvpq aflqhmtvfv lacfvgymvi wnvtpslhtp lmsvtnaisg iivigallqi
      481 sgpffslktf laalavliat invfggflvt qrmlkmfrkg gdhe
//
LOCUS       WP_092216851             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium arachidis].
ACCESSION   WP_092216851
VERSION     WP_092216851.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium arachidis
  ORGANISM  Bradyrhizobium arachidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium arachidis"
                     /db_xref="taxon:858423"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39158
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aevavepgag lksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygneaa lktmadagva afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegakage
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpka
//
LOCUS       WP_092227195             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. Gha].
ACCESSION   WP_092227195
VERSION     WP_092227195.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. Gha
  ORGANISM  Bradyrhizobium sp. Gha
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium sp. Gha"
                     /db_xref="taxon:1855318"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39307
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag iksgfpdsef savgatvsad
       61 alkdadiiik vkrpepsels qykrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvrsmkpgs vlvdlaverg gnvegarage
      301 vvetdgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_092250844             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_092250844
VERSION     WP_092250844.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38772
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_092225698             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. NFACC08-1].
ACCESSION   WP_092225698
VERSION     WP_092225698.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. NFACC08-1
  ORGANISM  Pseudomonas sp. NFACC08-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. NFACC08-1"
                     /db_xref="taxon:1566238"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38777
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvidsay eaagatigsa
       61 sdafgaelil kvvapsdsel tliksgtvlv gmlnpfnnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lnaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_092254740             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Bradyrhizobium].
ACCESSION   WP_092254740
VERSION     WP_092254740.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bradyrhizobium
  ORGANISM  unclassified Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="unclassified Bradyrhizobium"
                     /db_xref="taxon:2631580"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39296
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pleprvaasp dtvkkfkalg aeiavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygneaa lktiadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake msreyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegakage
      301 vvdrdgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_092275375             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas prosekii].
ACCESSION   WP_092275375
VERSION     WP_092275375.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas prosekii
  ORGANISM  Pseudomonas prosekii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas prosekii"
                     /db_xref="taxon:1148509"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38551
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag avaadasaly arnlldflkl vfnkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_092277086             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Duganella].
ACCESSION   WP_092277086
VERSION     WP_092277086.1
KEYWORDS    RefSeq.
SOURCE      unclassified Duganella
  ORGANISM  unclassified Duganella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Duganella.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="unclassified Duganella"
                     /db_xref="taxon:2636909"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39012
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrisvpaetr pgetrvaatp etvkklaakh qvlvqagagl aasvtdeayv aagaqivpas
       61 evwaadvilk vrapnadera qikpgtvvig mlnpfdadnn aamataglqa faleavprit
      121 raqsmdvlss qaniagykav mvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpyltdeek eiaqgvggya rpmpadwmrr
      241 qselvherak ladiiittal ipgrpapvli sedtvkamkp gsvivdlavs qggncplsel
      301 nktvvkhgvh ivgepdlath vaadasalya rnvldflkli idkedrlvid redeiikatl
      361 lcsggellrk
//
LOCUS       WP_092291996             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. Ghvi].
ACCESSION   WP_092291996
VERSION     WP_092291996.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. Ghvi
  ORGANISM  Bradyrhizobium sp. Ghvi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium sp. Ghvi"
                     /db_xref="taxon:1855319"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39218
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasels qyrrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa emvksmkpgs vlvdlaverg gnvegatage
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_092297047             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. NFIX28].
ACCESSION   WP_092297047
VERSION     WP_092297047.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. NFIX28
  ORGANISM  Pseudomonas sp. NFIX28
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. NFIX28"
                     /db_xref="taxon:1566235"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38651
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrmgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapll lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_092306427             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus alkaliphilus].
ACCESSION   WP_092306427
VERSION     WP_092306427.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus alkaliphilus
  ORGANISM  Cupriavidus alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus alkaliphilus"
                     /db_xref="taxon:942866"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38829
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvvvqagag lnasqpdgay eavgatigsa
       61 adalgaqlvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaasit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vvdkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_092309974             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus alkaliphilus].
ACCESSION   WP_092309974
VERSION     WP_092309974.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus alkaliphilus
  ORGANISM  Cupriavidus alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus alkaliphilus"
                     /db_xref="taxon:942866"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54047
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvkellk lgyqvvvetg agleasfsdd dyraagaaiv
       61 daaslwasvd vvvkvrppqv hpslgveeaa llkkhatlig fvwpaqqmam lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyakems
      241 pafieaemrl faeqarqvdi iittalipgk papklleagt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpgk dgqlvvnmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevpvpaea apprrrtgtt lialalaaaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_092311646             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brevundimonas viscosa].
ACCESSION   WP_092311646
VERSION     WP_092311646.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas viscosa
  ORGANISM  Brevundimonas viscosa
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Brevundimonas viscosa"
                     /db_xref="taxon:871741"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38117
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavaiavtre rrdgetrcal tpetvkklta lgatvtveag tglgssipda dyaaagatva
       61 pdtkaalaga dvllkvrgpt aqetsalrpg avvvallday reketvaala gagvtafame
      121 fvpritraqv mdalssqanl agyravieaa yaygkgfpmm mtaagtvaaa kvfvmgagva
      181 glqavatarr lgavvtatdv rpaskeqves lgakfvaved eefraaetag gyakpmspey
      241 qakqaeltas hivkqdvvvt talipgrpap rlvtaahvas mkpgsvivdl aidnggnveg
      301 akagevattp ngvkivgwtn magriaadas alyarnlvaf tgllvkdgal avdleddilr
      361 aaavthggav vhegvrg
//
LOCUS       WP_092312064             535 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus alkaliphilus].
ACCESSION   WP_092312064
VERSION     WP_092312064.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus alkaliphilus
  ORGANISM  Cupriavidus alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Cupriavidus alkaliphilus"
                     /db_xref="taxon:942866"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55618
     Region          11..535
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqpnpssapq rigvpretlp gekrvatvpa vvekliklgf kvavesgaga aadfsddayr
       61 aagaevidga aqlwaasdiv lkvrppsrde valmreggtl igfiwpaqnp elmqqlatkn
      121 atvlaidclp rtlsraqkmd altsaagvsg yravieaaha fgsyfngqit aagkvpparv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvrslg aefvkvdyde dgsggggyar
      241 vmsegfqaaq rqmyarqaqd adviittalv pgkpapklit aemvrsmkpg svivdmaaeq
      301 ggnceltvpg eavvchgvti igytdlasrl arqsstlyat nllrlteelc ktrdgqaivn
      361 meddairgla viqdgaitwp applkaapap apkaaaapap ekkaghghgs rapmsaralt
      421 ltvaiaavlf wcigafapaa flghftvfvl acfigymvvw nvtpalhtpl msvtnaissi
      481 iaigalvqia apevgmdgrp dglirwlafa alvltavnmf ggfavtrrml amfrk
//
LOCUS       WP_092318335             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_092318335
VERSION     WP_092318335.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38668
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapndsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_092322716             382 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Cryobacterium].
ACCESSION   WP_092322716
VERSION     WP_092322716.1
KEYWORDS    RefSeq.
SOURCE      Cryobacterium
  ORGANISM  Cryobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Cryobacterium"
                     /db_xref="taxon:69578"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38684
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvgvpresr egerrvaatp etvgqlkdlg veiqieagag taagypdsay tdagarvvpq
       61 ldtagldvyc hvrpltpaqa tglsrgtiti glaspaaeld tvsalatagv tafalelvpr
      121 israqsmdal ssqslvagyr avleaairfp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsaydvrpas adevtsmggt finldldave gaggyarels edrsvrqrel
      241 lapyvaaadv littaaipgr papllvtgam vaamragsvv idlaaetggn vegvvagqdv
      301 gvpttagdga vilvgmkdap samptdasrl yaknvanlla lmtsadgiva pdftdevlag
      361 aclthdgkvt haptataleg er
//
LOCUS       WP_092333636             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_092333636
VERSION     WP_092333636.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38739
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvidsay eaagatigsa
       61 sdafgaelil kvvtpsdsel tliksgtvlv gmlnpfnnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_092347827             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Desulfuromusa kysingii].
ACCESSION   WP_092347827
VERSION     WP_092347827.1
KEYWORDS    RefSeq.
SOURCE      Desulfuromusa kysingii
  ORGANISM  Desulfuromusa kysingii
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfuromonadia; Desulfuromonadales; Geopsychrobacteraceae;
            Desulfuromusa.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Desulfuromusa kysingii"
                     /db_xref="taxon:37625"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53782
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeih qgerrvastp evvaklsklg fsvaveagag aaasytdday aaagceivgs
       61 andlwaqsdv vlkirapegd evkrlksgqt lisflwpaqn pdllknltdr gitaiamdci
      121 prisraqkmd alssmsnisg yraiveaaeh fgrfftgqit aagkvqpakv lvigagvagl
      181 aaigtargmg aivrsfdtrp evkeqiesmd aqflmldfkd engtgeggya kvmsdefika
      241 emalfaeqaa dvdiivttal ipgkpaprli taemiksmka gsvvvdlaae qggnceltep
      301 gkvvvkhgvs iigytdipsr matqssqlys nnlynlitdm tpgkngeili dmddevirga
      361 tvctggkttw pppapklsaa pkkvaptpap vavekkksvw gpiltigiaa lalfglgsva
      421 ppdlmehltv fvlacfvgym viwnvtpalh tplmsvtnai ssiivigali qvsstgsmik
      481 wialctllit sinivggfav trrmldmfhk
//
LOCUS       WP_092349586             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Chryseopegocella kryptomonas].
ACCESSION   WP_092349586
VERSION     WP_092349586.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Chryseopegocella kryptomonas
  ORGANISM  Candidatus Chryseopegocella kryptomonas
            Bacteria; Pseudomonadati; Candidatus Kryptoniota; Candidatus
            Chryseopegocella.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Candidatus Chryseopegocella kryptomonas"
                     /db_xref="taxon:1633643"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40638
     Region          2..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,101,297,323,325)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,134..135,144..145,148..149,152..153,155..156,
                     158..163,165,167..169,172,195..196,287..288,330..331,335,
                     338..339)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,134,137,140,181..184,204..206,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,134,144,187..188,195,211..212,214..217)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(164..168,171,174,197,199)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mikigvpket ypgetrvali panvpnfkkm gaeiivesga gekagypdse ylekgaqivk
       61 sreevfsnad vilqvralga npvegkkdia llkngqilig fmepflakdl ieevaqkgvi
      121 sfalellprt sraqsmdvls smatisgyka vliaasylpk mfpmlttaag tilpanvfvi
      181 gagvaglqai atarrlgavv raydirpatk qeveslgakf velglesqea edkrgyakdm
      241 geefyrrqre mltkvvaesd vvistasvpg kkapvlitee mvkgmkpgsv ivdlsaergg
      301 nceltkpgei vekygvkiig pvnvpatvpy hasqmyskni tnfcsllikn geininlndd
      361 ilsstlltkd gkltnsifd
//
LOCUS       WP_092353614             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Collimonas
            sp. OK242].
ACCESSION   WP_092353614
VERSION     WP_092353614.1
KEYWORDS    RefSeq.
SOURCE      Collimonas sp. OK242
  ORGANISM  Collimonas sp. OK242
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Collimonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Collimonas sp. OK242"
                     /db_xref="taxon:1798195"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38545
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaetr lgetrvaatp etvkklvaak hqvlvqsgag ilssitdeay aaagaemvta
       61 aaafgvetvl kvrapgadel allksgtvvv gmlnpfdadn iavmashglt afaleaaprt
      121 sraqamdvls sqaniagyka vlmaantyqr fmpmlmtaag tvkaarmlim gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfitdee reiaqgvggy arampadwmr
      241 rqaelvhera kqadiiitta lipgrkapvl isedtvkamk pgsvildmav dqggncplse
      301 sgktvirhgv hiigegnlat lvaadasaly arnvldflkl iinaegglvi nreddivagt
      361 llcsggevlr k
//
LOCUS       WP_092362872             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cribrihabitans marinus].
ACCESSION   WP_092362872
VERSION     WP_092362872.1
KEYWORDS    RefSeq.
SOURCE      Cribrihabitans marinus
  ORGANISM  Cribrihabitans marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cribrihabitans.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cribrihabitans marinus"
                     /db_xref="taxon:1227549"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55694
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeil egearvamtp dsakqlqklg ydcvietgag aaagfsdaty keagveivkt
       61 aaalwkaadi iakvriptet elkrltrdkt lisffnpgan edglelaksk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg amtyafdvrp evaeqvesmg aefvyldfee qqqdgsatgg yasvsspefr
      241 eaqlakfrel apemdivitt alipnreape lwtedmvkam kpgsvivdla aekggncklt
      301 vpdekivtdn gvtiigytdf psrmatqsst lyatnirhmm tdltpdkdgq inhnmdddvi
      361 rgatvayqge itfpppppkv aaiaakpqek pkeltpeerk akelaefkaq tksqvtmlta
      421 gglalllvga vapasfmshf ivfvlavfvg fqviwnvshs lhtplmaitn aissiiivga
      481 lmqigsgnwl vlllaalsvl magvnifggf lvtrrmlamf qks
//
LOCUS       WP_092378769             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sihuiensis].
ACCESSION   WP_092378769
VERSION     WP_092378769.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sihuiensis
  ORGANISM  Pseudomonas sihuiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sihuiensis"
                     /db_xref="taxon:1274359"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38737
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikklvgqg hqvtvqagag vsasipdsay eaagasignd
       61 aaalgadlvl kvvaptdael ahmrggavlv gmlnpfcndt iarlnargit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpqswme
      241 rqakavhera kqadivitta lipgrkaptl lheatvqemk pgsviidlaa aqggncplte
      301 adqvvvkhgv tlvghtnlaa lvpadasaly arnlldflkl vidkegqfql nleddivaac
      361 lmcnageivr kng
//
LOCUS       WP_092365952             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phytopseudomonas seleniipraecipitans].
ACCESSION   WP_092365952
VERSION     WP_092365952.1
KEYWORDS    RefSeq.
SOURCE      Phytopseudomonas seleniipraecipitans
  ORGANISM  Phytopseudomonas seleniipraecipitans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Phytopseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Phytopseudomonas seleniipraecipitans"
                     /db_xref="taxon:640205"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38843
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikkliglg hqvtvqsgag iaasitnsay eavgasigda
       61 aaafgaalil kvvapddtel armqpdtvlv gmlnpfsvet ierinargit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaegvggy arpmpaswme
      241 rqaravhera kqadivitta lipgrkaptl lheatvaemk pgsvvidlaa tqggncplte
      301 ldkvvikhgv tlvghgnlpa lvaadasaly arnlldflkl vidangtfhl nleddivaac
      361 lmctggeikr vnk
//
LOCUS       WP_092397250             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Collimonas
            sp. OK412].
ACCESSION   WP_092397250
VERSION     WP_092397250.1
KEYWORDS    RefSeq.
SOURCE      Collimonas sp. OK412
  ORGANISM  Collimonas sp. OK412
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Collimonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Collimonas sp. OK412"
                     /db_xref="taxon:1801619"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38427
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaetr pgetrvaatp etvkklvaak hqvlvqsgag isssitdeay aaagaeivta
       61 aaafgvetvl kvrapgadel allksgtvvv gmlnpfdadn iavmashglt afaleaaprt
      121 sraqsmdvls sqaniagyka vlmaantyqr fmpmlmtaag tvkaarmlim gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfvtdee keiaqgvggy arpmpadwmr
      241 rqaelvhera kqadiiitta lipgrkapvl isedtvkamk pgsvildmav dqggncplse
      301 sgktvvkhgv hiigegnlaa lvaadasaly arnlldflkl iinaegglvi nreddivaat
      361 llcsggevlr n
//
LOCUS       WP_092410725             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. NFACC02].
ACCESSION   WP_092410725
VERSION     WP_092410725.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. NFACC02
  ORGANISM  Pseudomonas sp. NFACC02
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. NFACC02"
                     /db_xref="taxon:1566250"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38577
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikkligqg hkvtvqsgag vtasvpdsay eaagasigsa
       61 aaafgadlil kvvapsdsel alikagtvvi gmlnpfnnei iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee reaavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkapvl lsaetvsqmk pgsvvidlaa aqggncpltv
      301 adqvviehgv tivghtnlpa lvaadasaly arnlldflml vftkegqfei nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_092410798             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Dokdonella
            immobilis].
ACCESSION   WP_092410798
VERSION     WP_092410798.1
KEYWORDS    RefSeq.
SOURCE      Dokdonella immobilis
  ORGANISM  Dokdonella immobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dokdonella.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Dokdonella immobilis"
                     /db_xref="taxon:578942"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39541
     Region          3..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpvvvavlre saegerrval tpevakklka rgaqivmekg agasayfpda afadaevvad
       61 gptalsradv llrvqpptve eighlregtv viahlaphlg pervkalrdr kitafamell
      121 prttraqamd vlssqagvtg ykavliaaer apkffpmltt aagtirpskv livgagvagl
      181 qaiatarrlg aqvegfdvrp etreqieslg akfldlgvsa agsggyarel taeereqqqq
      241 alanhlknid vvvttaavpg rkapriisaa miagmkpgav ivdiaaesgg ntelskpget
      301 vvtdngvsvi gtvnlpattp inasemyarn lynflelsla dgaltlnwed eliaktclth
      361 ageikheptk qaiegass
//
LOCUS       WP_092416096             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Collimonas
            sp. OK307].
ACCESSION   WP_092416096
VERSION     WP_092416096.1
KEYWORDS    RefSeq.
SOURCE      Collimonas sp. OK307
  ORGANISM  Collimonas sp. OK307
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Collimonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Collimonas sp. OK307"
                     /db_xref="taxon:1801620"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38598
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaetr pgetrvaatp etvkklvaak hqvlvqsgag ilssitdeay aaagaemvta
       61 aaafgvetvl kvrapgadel pllksgtvvv gmlnpfdadn iavmashglt afaleaaprt
      121 sraqsmdvls sqaniagyka vlmaantyqr fmpmlmtaag tvkaarmlim gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfitdee reiaqgvggy arqmpadwmr
      241 rqaelvhera kqadiiitta lipgrkapvl isedtvkamk pgsvildmav dqggncplse
      301 sgktvirhgv hiigegnlaa lvaadasaly arnvldflkl iinaegglvi nreddivagt
      361 llcsggevlr k
//
LOCUS       WP_092419573             435 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Devosia
            crocina].
ACCESSION   WP_092419573
VERSION     WP_092419573.1
KEYWORDS    RefSeq.
SOURCE      Devosia crocina
  ORGANISM  Devosia crocina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Devosia crocina"
                     /db_xref="taxon:429728"
     Protein         1..435
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45090
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlretv sgehrvaatp etvtkliglg aqvsvetgag sgsripdaaf taqgaaiapt
       61 vsaavhgadl iltvrrpwag rlaganpgal ligaldpfgn daeisdlara gitaiamelm
      121 pritraqvmd ilssqanlag yqavieasah fdralpmmmt aagtvrpakv fvmgagvagl
      181 qaiatarrlg avvsatdvra aageqveslg akfiltealk dasgvggyar eltlaeseaq
      241 aalvaghiak qdivittali pgrpapklls aemietmtsg aiivdlaaer ggnveltrpd
      301 eivehngiri lgftnlasri patasqlyar nllaftetli dkstgqlaid wndelvratv
      361 ltrdgavvhp hfaataapla rpqeeeieav drpseprqmp aeavpqhepe aqrpapphrv
      421 pgeprttsge aegkk
//
LOCUS       WP_092420901             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Alloyangia
            pacifica].
ACCESSION   WP_092420901
VERSION     WP_092420901.1
KEYWORDS    RefSeq.
SOURCE      Alloyangia pacifica
  ORGANISM  Alloyangia pacifica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Alloyangia.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Alloyangia pacifica"
                     /db_xref="taxon:311180"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55642
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpteif egearvamtp dsalqlqklg ydcliqsgag akagfadaay eaagvtvvad
       61 aaalwaqadi vakvrppsee evayltpekl lisffypasn ealmkqaadl gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqadgassgg yasvsspefr
      241 eaqlakfrel apemdivitt alipnreape lwtedmvkam kpgsvivdla aerggncklt
      301 vmdekivtdn gvtivgytdf psrmatqsst lyatnirhmm sdltpgktdg tvvhnmeddv
      361 irgatiahak dvtfpppppk tkaiaaqkpk ekapeltpee kraqevaafk aqtkqqvtll
      421 tvgavlllgv glvapasfmq hfivfvlsvf vgfqviwnvs hslhtplmav tnaissiiil
      481 galmqigsgn wlviilaals vfmaginifg gflvtrrmla mfqks
//
LOCUS       WP_092436213            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Williamwhitmania taraxaci].
ACCESSION   WP_092436213
VERSION     WP_092436213.1
KEYWORDS    RefSeq.
SOURCE      Williamwhitmania taraxaci
  ORGANISM  Williamwhitmania taraxaci
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Williamwhitmaniaceae; Williamwhitmania.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Williamwhitmania taraxaci"
                     /db_xref="taxon:1640674"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119270
     Region          23..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlsallal lmlvtlfvqa qqrqvtgtvt gsddgkalpg vsiqvkgtts ggttdmdgkf
       61 sitvpdgsgt lvfrfvgykq qetvvgdrti vnviletesl kveevvvtal gisrakkalg
      121 yavqdvqgdd ltkvrstnvv ssltgrlagv qistasgqmg ggakinirgn tsftgsnqpl
      181 fvidgipldn sdfsygatgg ggydfgnlaq dinpddiesv svlkgasasa lygsraangv
      241 vmittkkskn eekktigvsv nssltldkis iipqyqkeyg ggsilggtdg fdqvaiggkt
      301 ynivdyatde swgpkydani kylpfnafds wdtenylvek pwlypkndyn yffktavtnt
      361 nnvsmtagdq nstfrlsytn mnstgnyaks elkrntlsfn vthklhksve gwananyvvn
      421 davgrpetgy gdrnpvqkmw qwihtsidyk dleawqnpdg tqrpwnrtaw ndgavnytdn
      481 pywsryknye tdrrdrfygn agvhikflpw lkltgrvgad yytfnmqerm avgsqatsey
      541 lldtrsmsev nsefyftldk rvmddkigln aiiganrmds qkwrsggvti gglvvpelyn
      601 lsnsatkats ydykswkrin svygnftmdy drlvylelta rndwsstlps glnsyfypsv
      661 nlsfvlsels avkdlgfvtf akvragiaqv gndtqpynle nyyaagasfg dnpryslptt
      721 rpnfelkpek tnsweigtem kfldnrfgld vsyyyketvd qiiparvsgt tgfgafnint
      781 gkmvnkgwdl sfsltpvkva gfqwdimina gilnnevvei dpsleylalg napfkvqvga
      841 fkgysypiiy gtdfvmdaqg nkvispggny laseikplan atpnltggit ntftykgfdv
      901 svlvdmqrgg nmyytsymwg mysgimeesa ktnefgvnir ediainggvl ldgvygtydp
      961 iaklvsytda tgapsatpvv nttrldgkdw aqhhydgpdk qnifstnfvk lrevrfgytv
     1021 pgrftgpikg lrvsaygrnl atwgrasqhf dpeymqmags naqgveggyi psvytigfgi
     1081 nfnf
//
LOCUS       WP_092445023            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Winogradskyella sediminis].
ACCESSION   WP_092445023
VERSION     WP_092445023.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella sediminis
  ORGANISM  Winogradskyella sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Winogradskyella sediminis"
                     /db_xref="taxon:1382466"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116811
     Region          20..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiytglll clcffsnaqi titgivtdav satplpfvni tsntglgttt nddgtysimv
       61 ssnadtltfs ylgfksqtiv vgdqtlinia lqedsaalde vvitalgler dtkelgyavq
      121 aisskslnev ktinfldnlq gklagvtvtq gatgvgsssk itirgeasfs nnnplfvvdg
      181 vpinnetvfn ftneaaagfq eidfgnggme vnpddiasvt vlkgpsaaal ygtrasngvi
      241 vietkngsnq rglgisints lfvdsafrlp dfqnsygqgn sgqfeyvngl gggindnity
      301 swgprldagl lipqfdspvq langsvvrgg dtalyngldi tatpfisnpd nlkdfyqtgt
      361 ttinnisvsn gfdtgnyrls ftdlrsesii pgvnldrqti aaklnfnpse kteintsiny
      421 insssdnrps ngygsenany slvawgprsl nieslkdywq pglegtqqys fnytffdnpy
      481 filnentnaf nrdrifgnis itqelaknls islrtgmdys tekrqlrraf ssnrfsngay
      541 aehdvmfrev ntdflinykn qfndfsvdvf lggnrlnqta ttnqsqtvsl aqpgiynlnn
      601 aaspietfqf esekrinsfy gitkfgykdf lflditgrnd wssalatpfs vdgtsffyps
      661 vsssfilsnv telpsifsfa klrasvaqvg ndtsayqtsg afvsqtpfns eptfsnqdfi
      721 pnsnlkpert tsyefgtdlr fldnklrldf tyynantedq iislpvaiss gysqqvvngg
      781 kvntqgveii lgitpiqtdn fnwnttfnfa tnrsvikdlp qsdgrltlay sriydsanqt
      841 vwfqveeggr vgdfygtgyq knengqflid dngnyiaddn lkklgnynpd ftlgwrnnfn
      901 yknwnlsflf dwrqggeivs rtralgnvgg qlaetsyrpd dgivaqgvnv ntgqantvai
      961 taesyyrqfy drnheennvy dasflklrqc aigytfnfkd gflglkegad lnlslvgnnl
     1021 faitenphfd peqlavqgng fvsgvedmsy attrsigfka gfnf
//
LOCUS       WP_092445124             965 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Winogradskyella sediminis].
ACCESSION   WP_092445124
VERSION     WP_092445124.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella sediminis
  ORGANISM  Winogradskyella sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 965)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 965)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 965)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Winogradskyella sediminis"
                     /db_xref="taxon:1382466"
     Protein         1..965
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106107
     Region          24..964
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktvlnalll climlpatll aqttvtgtvt dkanamplpg vnviikgtar gtstdfdgkf
       61 alevsqgeii vvsylgyttq eieytgqasi niaieedasq ldeviligyg tttkkdatgs
      121 vdavtskdft rgnivtpenl lsgrvagvtv ntsgapgsgs eikirggssi nasnnplivi
      181 dglpitndnv ggsrgvlasi npndidsftv lkdasataiy gsrasngvii ivtkkgksef
      241 svdydvqytf gdideqievf sadeyrelvt aqnlpdnfvs qlgdantnwq deifretvsv
      301 nhnltlrgsl fnaiparfsf gvteqegail tseferrnls lslnptffdn hlkvnlntnl
      361 syednrfgds gqigaaigyd ptqpvydsts pfggfyqhrn gntlllggsn pvasllqtnn
      421 igdserfygn infdykfhfl pemklvlnlg ydktegitrn nsvyatndpi kgnrsfsyqe
      481 rtnqsldgfl nykkdfgsig tdltagysyq kftnegnytg nqidpnsfgd tfadpdtvli
      541 gffgranlsv aekylmtlty rrdgtsrfse dnrwgdfyag afawqlsded flkdsntisn
      601 lklrvgygit gqqeigerdl flsryqagqn nsqyqfgngi vsslipsein pdlkweetkt
      661 leigldyglf enrvsgslnv fqkdsedllf napvpdgsnf snsivqnign lriqgleftv
      721 ntdvirkedf nlnfnfnatl ldreitelaf gqdvttggia ggtgnfvqlf regespnsfy
      781 vfkqlqdgqg nyiegayadl ngdniinded rylkenpdad vilgfqtnve ykgfdlsfnl
      841 ranignyvyn nvnssraqyd llrsnavlgn iptsvldtnf qttsdviisd vyvenasflk
      901 mdnitlgytf knlskfissi rlwagiqnvf titeysgldp evfngidnti yprprnilig
      961 anfkf
//
LOCUS       WP_092446381             721 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Winogradskyella sediminis].
ACCESSION   WP_092446381
VERSION     WP_092446381.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella sediminis
  ORGANISM  Winogradskyella sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Winogradskyella sediminis"
                     /db_xref="taxon:1382466"
     Protein         1..721
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=81153
     Region          2..>642
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
     Region          <639..721
                     /region_name="SusD_RagB"
                     /note="SusD family; pfam07980"
                     /db_xref="CDD:429768"
ORIGIN      
        1 mndvesfeil kdaasaaiyg skgsngiimi tmksglegkt ritystytgf kearksdayg
       61 yttqewadqq madngeisiy iqaqlqtgtd rswqdvffdg gtitshamsf rggnkntkys
      121 aslnysddeg vllgdnytky garlkldnki nekfsvginl spsftervrf aesvhnvarh
      181 qpwlpiynde ytlqmvnpea fpveagdyvr qnhftifdfn gdgvfdeelf nignstnqnp
      241 farvternrm dkkfkmfgsf ygkykitkgl rftttlsgsi qdtkrtdymg tlareqttda
      301 ymvetsqkeq yyifdnflny dvsfgkhelg vtlgnsietr dyffstikgi gyendivqqi
      361 sgatsivdae tfgmewqkrg isfisrlnya yddkylmsls mrrdgssifg sdfkygnfaa
      421 aslgwnvaee nflrdsniis slklrasygv tgndrlntgs vnpdaqgsts vlssenvlqd
      481 yyphlslldl tsyvvdgtit tgysplnlan pelkwerlie itpgidfgfl nnkitgsvdw
      541 yqrksdqlll nnpvssttgf nsalvnlgev knegfefelr trninkrnfs wqstviatsn
      601 entlvnfads dgqitsidps rpaewinqeg qpissfygyv vesedpltei tvddllmerr
      661 velafenhrl fdlirlgkaq evlsaysely gfgftssdll lplpqnevni sdglmtqnpn
      721 y
//
LOCUS       WP_092447556             307 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Winogradskyella sediminis].
ACCESSION   WP_092447556
VERSION     WP_092447556.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella sediminis
  ORGANISM  Winogradskyella sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Winogradskyella sediminis"
                     /db_xref="taxon:1382466"
     Protein         1..307
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35937
     Region          5..170
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifdlfskr qkrlrgeipe vftydeipnd lrvkivhiir dvvgqddfdn qkidsvyefi
       61 qktlcreygl fklgegynes neqqvlnfll qsndndrvld vieltfrfvd rviredreys
      121 yyakpkikpd dsiselndrf keqgigysfe agemirvdst yvhseitkpt isllwnrkfq
      181 ganeeylkah ehyrhgrnke clteclktfe svmkiickek ewefnktdts rkliqicfrn
      241 elvptftqnq ftslqnlles giptirnklg ghgqgqtpqk vddemtryal nltgtniifl
      301 ikqsgie
//
LOCUS       WP_092456024             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thermoflavifilum thermophilum].
ACCESSION   WP_092456024
VERSION     WP_092456024.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum thermophilum
  ORGANISM  Thermoflavifilum thermophilum
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Thermoflavifilum thermophilum"
                     /db_xref="taxon:1393122"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40510
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvigickepe genrvsclpd vvkqlvqlkq evwiesgage rayasdadyk avgahvadqk
       61 evwlhadmlc rmhfpesdel laqarektiw vgmyqplyha aeiqkmasrg mtvcsldaip
      121 rttraqsmdv lssqaniagy kavilaaahy phyfpmlmta agsiqpakvl vlgagvaglq
      181 aiatarrlga vveafdtrpa vkeevmslga kfievegaad psaaggyave qsadyqrrqk
      241 ekiaatiaka divittaqip gkrapllvtr emvesmrags vivdlaastg gnteltrnge
      301 tivhhgvtii gnsnlpstvp adasklygrn llhflqllig kdgrlqfnfe ddivsaacvv
      361 yegkirdari lqtvqqa
//
LOCUS       WP_092456968            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum thermophilum].
ACCESSION   WP_092456968
VERSION     WP_092456968.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum thermophilum
  ORGANISM  Thermoflavifilum thermophilum
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Thermoflavifilum thermophilum"
                     /db_xref="taxon:1393122"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113671
     Region          21..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpllltltf llacmlsfaq rsihgkvvde sglpvigati lvqgtqlgtt snnngefsls
       61 ipesathlqv rsvgyeavti pvtaetsyti tlhattqsln qvvvtalgir rdvrslgyas
      121 qevnaqeltv shqpnlvnal qgrvagvmig stgggpgqga silirgvnsl dpgknnqplf
      181 vvdgipvdnt tstlgttggr gvqmtnriad inpddiesit vlrggaatal yglrgangvi
      241 vittksakag qfrvsydmny sydvidktpk vqslytqgyn gvydstsfwp nwgptvadar
      301 kidpthpakl fdhykhayts gnqirhtlsl sggtdkasvs ssvsyfhqng vlpftyyqdi
      361 strlsgklvl skkvetgtti lyantggnfy dadrfneemt ywaprwdvrd yltpegtekt
      421 ygngnawyka atnkfksyvn hviassyfsy qpfnwmnlty rfgvdayqdn rtatapgpkg
      481 ipgeyvdddn gqgfvhkygi nyrqlnsnll ltlqhnwgrf gtslrlghdl ldravdevat
      541 egdeldiynl ftlsnakiih aseyrsqyhi igaygelels ydqalyltlt grndwtstle
      601 kgnrsffyps anlsyifset mhqlpswlsy gkiraslaqi gkdadpysts ivyiptgtpv
      661 ngvnlwtrsn aaglqslkpe kttsfeigtd lsflnnritl nftwyhsisq dqiipvatap
      721 stgftsitln agkirnqgie ltlqatpits ksfswetdin vshnenkils iypglqriev
      781 gsqfgyagat vtmyyvpggs agdiygshwl ryypdgkqpp thvdkkaplv idsngfpvra
      841 sdqqilgnsy pkwlvswnht ltygnwtlsf lfdahlnvqk ydqlnnfmaa fgiaaytlnr
      901 netiifpgvh adgtpnttpv wlgqgtgpdg knygagyyrn yyrgvsenfv edaswirlrt
      961 lslsyqlpar wlkgtfikgl nigftgnnlw lhthyigfdp esssapagsn angfagftyp
     1021 alrnfmvhlh asf
//
LOCUS       WP_092458503             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum thermophilum].
ACCESSION   WP_092458503
VERSION     WP_092458503.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum thermophilum
  ORGANISM  Thermoflavifilum thermophilum
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Thermoflavifilum thermophilum"
                     /db_xref="taxon:1393122"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108755
     Region          29..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmhsrtftrp wlatlffltl aqfafsqart isgrvvdaqs gssmagvtvr vkevsgvgtt
       61 tnaqgvfqln vpaeaktlif sfvgyqnqev pitgneinvs lkpgealqev vvvgygtqra
      121 qdvsaaissi snkdfnkgiv tnpmqqiqgk vaglvitqpg gdpnqnviir lrgqtsitgg
      181 qtplivvdgv plddpsqian ippgdiesyd vlkdasatai ygsrgangvi iintkkgrag
      241 qtsvtyngyv gldwqakyyd lltadewrta tkqlgnyqas ldkgantnwq kaitqtafsh
      301 ahnlmvsggt dkftysaagn yinqqgivin sgktevglrf naqqkalddk ltlnyglltt
      361 rtnrkyvdys iftyvfstpp typvynpdgs yfgyfdfeqq npvaqqmlql nrgnenlniy
      421 sagadyellk glklgmlgsl syfnkqtdff qptlpgvgni nngakyaenr nskkgnihie
      481 ytrtwnnvhh fdftgvyeyn dfeydnfraa gqqylveenq dnalqngnta fnqissykee
      541 yklisflgrv tynykgkyyi dasfrrdgss kfgvnnrwgn fpavsaawri seegfmrnis
      601 windlklkig ygvtgnqdai tpyatqllvg sigryynpvn payaypqsya ptqnanpdlk
      661 weerhgfnvg anfslfndrl ggdvnvfndk tksllynytv ptppfyvnti lanvgtltnk
      721 gveialngti ikgskftwta ngqitfiktr vtslsgtyag yklstdnipg gyaegrglss
      781 npitflkvgy spyvfylphw egvdangnql fdsagvkipn ygnatfryid papkfnyglg
      841 stlnygnwsl nfffrgvygq kifnntlldv efikrlpgnn vtkealtngi qdaavasdhw
      901 lenasylrld nvslsysfkq vkgigsidvy ltannvfvit pyrgldpeir nadtneayid
      961 anygsdgyyp rtrsvvfgvn vsfk
//
LOCUS       WP_092459869            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum thermophilum].
ACCESSION   WP_092459869
VERSION     WP_092459869.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum thermophilum
  ORGANISM  Thermoflavifilum thermophilum
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Thermoflavifilum thermophilum"
                     /db_xref="taxon:1393122"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118804
     Region          23..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvllflta llfstvwafg qqrtitgkvi sqdgnpipfa tvqikgttsg tttnqngsft
       61 ieapadavlh issigyeaqd vqvgaqnqlv irllptaqnl keivvtalgi ernknelpya
      121 aqqvsgdqvt ntrsdnflsa lsgkvaglqi ktnnnlggst divlrgyksi tgnnqalivi
      181 dgvpvdnsnf nsnrqrngfa gydygntgtd inpddiasin vlkgaaatal ygsraangvi
      241 littkkgkkg lgvtfnigga tgsmdkstwp kyqhqygagy fdpdyytysd appspdphfl
      301 yekvngqyal vvpttedasf gakfdpsllv yqwdafdpss pnygkptpwv aakndpttff
      361 etpysyntsv fvqggddrqt fklgytrtgd kgilpnshlt kdmvdfssty nitpklkata
      421 sinytkenai grygsgyday npatnfreww emnvdikeqk aayfrtlkni twnmtdpvgg
      481 nigpiywdnq yfvryqnyet dnrnryfgyl mlnydptswl slmgrvsldq yaglqeergn
      541 vgsvnvpyys rynnnfkefn ydflanfnkd itsslnfkal lggnlrrtyf nsiyastngg
      601 lvipglyals nslnpinaps etaeqievgg vfggitltyk nflildatar qdqsstlpan
      661 knkyfypsis ggfifsqllk nvtwlsfgkl rlnyaevgnd apwafisdvy dkptpygsva
      721 lfsvpnrknn aelkpertks yegginlgfi nnrigvdvty fktntinqii nisipaetgy
      781 tskvinagnv enkgwevtln lvpvrtndfs wnldlnwary rnkvislysg vqniqlgafq
      841 ggvtlnatvg qpfgvlkgkd fvylngrpvv ksngyyqits stdnvignin pdwtggvsnt
      901 ftyknfrlnf lidikqggdl fsidqwygqg tglyiesval nangksirdp vdqgggyifp
      961 gvtadgkent kyaaitglrg fgylnmpnka yiydasyikl revnltyslp esvvshmhpf
     1021 ktidisvygh nlwiihknlp yadpeegpss gniqgfqvgs yptyrmygcn lkftf
//
LOCUS       WP_092460223            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum thermophilum].
ACCESSION   WP_092460223
VERSION     WP_092460223.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum thermophilum
  ORGANISM  Thermoflavifilum thermophilum
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Thermoflavifilum thermophilum"
                     /db_xref="taxon:1393122"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118093
     Region          41..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnyivscs iifswlilfn sfqgicqqkk etihdslsih gividavtkk pvsginvtvp
       61 dysaaitddr gnfelkvpsy qvsilisgag yqdkeialkg rheitakiyq epfqsfydma
      121 rlpyrqerls hvtysmnalq lndkwsrtsl espaaymqgi tsglnvirrs gtpgigaelf
      181 lrgynsllat nsplividgm iydnneygns fmsgyfhnpl sdvdirdiee itvikdgtst
      241 fgtkgangvi littgrakel atridlevsg gynlvpaiip vmnandyriy ltdlltsqgl
      301 tqqqianlpy mndnlsnpsy fayhsntnwq kevlhnsynq nyylrvtggd nvatyalslg
      361 yrnnegiikn tndtkyytrf ngdlnisqkl kaalnlslis gsrnlqeqgf lnaysplnia
      421 likapfipvh vlnnqgvasp nlspantfnv anpvailngm qginqsyrff gsvrfsyqln
      481 nswdiqsllg vtfdkvresy fmpsngvppd tlvkgvaynq tgsnverlys iyndtrisyq
      541 htfeqihhvq ahlgiryqan qseahyglsy ntptdqyvsv gmgqpalrta ggqlgkwnwm
      601 ntyinasynl ldkyfingdl sfdassrfgk qvregiking qpfavmpsis agwvissenf
      661 msrlpfiell klrasysqlg nddigdytyr qlyisqnllg leglyrgnva npylqwetvr
      721 kfdigidasf mnerlnvqad vytdhtenml tyqplptssg fdsvmvnggs mknngwelsl
      781 ngriinhpql kwdmginvsh yknrvlsipg gqmttnyaga tiltkpgyaa nvfygyktng
      841 vftsdqeana sgltyidang naitprggdv rfvdlngdhi indsdrtiig npnpklfggi
      901 setftwkrwq ldalftfslg sdiynaqrrq lesmdnynnq tlairnrwra dgqitsiprv
      961 awgdpsgnar fsdrwiengs ylrlryisls ynidfqnsai kylkiyitgn nlwtwtkylg
     1021 ydpefsstsg pigqgvdigl eplfktaqlg irigl
//
LOCUS       WP_092460434            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum thermophilum].
ACCESSION   WP_092460434
VERSION     WP_092460434.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum thermophilum
  ORGANISM  Thermoflavifilum thermophilum
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Thermoflavifilum thermophilum"
                     /db_xref="taxon:1393122"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113999
     Region          29..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskalpirvl wlsflavams favalaqekt lsgqvlapdg splvgvtvkv kgttrgtttd
       61 vngrfqlsaa sgetlqfsfi gyapqelkvd dqstlrvtlq ptrsqlnevv vtalgqqqqe
      121 rtlgyavqki sgadienthr tdfvsalqgr vagltvnsts glpgasdaiq lrginsigls
      181 nsplfivdgv pvdnstfsta sltsinqsav dyanrrfdft nriadlnpnd iesitilkgp
      241 eatalygiea tsgaivittk sgkagkptvd yngtltttkl yrfpevqrvy drgfngvfdp
      301 ssvsyfgpri pagtqlydni hhffrtgirq thnlsfsggn nqityrlsss ylddqgvvpn
      361 tdykrinval rvnarisnkl stdasisyiq adntkaekgp tsfllglylw ppymdvrdyl
      421 npdgskklvy pnhtpdqeyd npffsvnknh fydktrrmig nfgvtydplr wlsisgrign
      481 dayttngmiy ynanstfayq fkgridqyts ivqnlytqll vkashnfgsw ntslllgnav
      541 ynnsnhteaq sgqnflvndf vslnianplt isnltslvrk rligvfgefn lgykeifhlq
      601 itgrndwtst lpigrnhffy psanlsfaft eipalaglkq vinfgklras vaqvgkdapp
      661 yqvypgllpq tttgggfafn fngpnpylrp eqttsysyga hlefynsrli vdgeyyktks
      721 ihqivplvrk syapgfvlyt inggsltnhg leltltatpv qtsalqwnit vnyafnrskl
      781 lslpsgvtef ynsdtwlygn lrngmkvggp lttftgatwm rnnngdilvn plngyplkdn
      841 sfqvvgdrnp kftggvnnsf ewkgftlsfl fdfrrggdvf natalqlyrl glstatlnre
      901 tpvvvkgvlk dgmensskpt pntiqitpmy nsnyfsnvsv esdfveknin wirlrdvylm
      961 ynfpkkwlgr qhtiqdlsvs isssnlfmit nysgqdpdvn gttpatlgsg gagidynvvg
     1021 kprvfnftvn arf
//
LOCUS       WP_092461018            1096 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum thermophilum].
ACCESSION   WP_092461018
VERSION     WP_092461018.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum thermophilum
  ORGANISM  Thermoflavifilum thermophilum
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Thermoflavifilum thermophilum"
                     /db_xref="taxon:1393122"
     Protein         1..1096
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122680
     Region          31..1095
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllttlla ltsgwliftq eakaqniqer iiirgkvtda sshmpvigas vaeldkdnri
       61 ingtttdidg nfalkvndpv nnrisisyig yktlvqpirn qremnihles ssrtlsevqi
      121 tagrtvdngt glmipernst fatttidaqq lenlsfpsid malegkvagv digattgdpg
      181 agmsirirgt ttingsdnpl iildgmpyni dipsdfnfgt adeqgyaqll niapsdikdi
      241 tilkdaasta lwgsraangv ivintkrgti grpsvgysfk gsiswqprgi pllngyqytt
      301 limeevanag gapldirnnk efaydptdpy wyynysrntd wigaitqtgy sqehdismmg
      361 ggekaryyas vgyltqtgtt vgtglnrits tinldynvsd rihfrsdisy thiitngnyv
      421 pnssyqvrsv ayrkmpnmsi yeydiygnqt pnyfspasni qgsyyqtynp valaktalnr
      481 qvgervtprf hiqydifpsy ligtfdvqfd innskvntfl pqiatgrpit epvvnqagls
      541 dgdvfdvytk tnlifnhnlp denhqlqall siqtddnksi afneitsnta ssslqdpasp
      601 snittsaqtl sstkaetrsi givlqgqydl mdryiinagi rmdgssrfgp ahrygffpsi
      661 sgrwrisgep fmkqfafind mslrlsyghs gstppdkpiw nyfntyspfs ysymgmsgvy
      721 psnvelsdlr wqtligsnlg yniwmfhnri rfdmelyrnr ikdmfydniq ipaytgynti
      781 psnvgtmdnq gweimlntip yrsknwelgf dfnisknani irsispyfpr tnipsitqng
      841 vyktylqinn pfgsfygfry lgvykdkest iardasgkei igpdgnpvym rfgypnvnyv
      901 fqpgdamyed vnhdgviddk divylgnglp kisggfgini tykehlklit ffvsrlgyql
      961 vnyadmvtsn mygfdnqstv vlkrwrnpgd itdipralyr sgynwlgssr yvqdasflrl
     1021 qavtirynfs ndllnrlkir aaafyitgen lytwtkykgq npdqsiignn npfaypvdna
     1081 ltpipidvvi glnvsf
//
LOCUS       WP_092466059            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Winogradskyella thalassocola].
ACCESSION   WP_092466059
VERSION     WP_092466059.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella thalassocola
  ORGANISM  Winogradskyella thalassocola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Winogradskyella thalassocola"
                     /db_xref="taxon:262004"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116754
     Region          28..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgikhfklta flcvfiitsf cnlqaqeiqi tgkvtaledg mpmpgvsilv vgknkgtntd
       61 fngvysidan kgdilqfsyi gfseqkitig dnsvidiqlv esvealnevv vtalgisrke
      121 qalgyaiskv dgeelaeiks inavnslagk vagvdiaqpn tgsggsskii irgntkfngs
      181 nqplyvidgv pmdnnsfgqa gqyggqdlgd gissvnsddi etisvlkgpa aaalygsrgg
      241 ngvvlittks fnknskskfn infstnstfd evisgyedvq hvygqgigtp prdigdatgm
      301 wswggkmdpd lqfisfdgqy rdygvkkdni esffrtgyti qntislsggn esanllfsas
      361 dvkmedivpn sglhrnnftl kgymkmwekl tldakvnfti edvdnrpylg ysgantalal
      421 lglpgnidqq wlrdsavdan gdyvfwnsat riinpyysly qmkneskknr vlgyaslnyn
      481 itdwldfkfk sgidtftydy ynysprttpl aewgeltkid srtteintef lisankeind
      541 nwsigaslgg nimnfesstn silgknqgse dvisinnyne fivgrdnprk svrsfygfan
      601 vsfkdyafid vtgrqdwsst lkkgnngyfy psvtgalvlt kaienlkskt isyaklrasy
      661 aevggdtdpy ayntffdypy ssnganfstv ndntyftnin psrtkgyefg ldaklfnwrv
      721 gldithynqt tydeimnipi snsngfesas inageinnkg wevmvnivpi ktedmrwdlt
      781 fnfahnenei velheeaktq tiaradwiss litaeeggsy gdivgydfkr tddgtpiigp
      841 nglplrsdeq vslgngqykf tggitnaiqy kgfklraliq vksgadilsm tnqklhqqga
      901 hiatlegreg wamseseres agelpsswva tggylaqgvi edgvgvdgnp nyrsndvyvd
      961 pkdywgsian shiikpfiyd asyvklrevs lsyslgpkal knikylnglt fsiigrnlwl
     1021 ihsnvpnvdp estynisngq gyeygslpqr rsygfnltak f
//
LOCUS       WP_092466434             965 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Winogradskyella thalassocola].
ACCESSION   WP_092466434
VERSION     WP_092466434.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella thalassocola
  ORGANISM  Winogradskyella thalassocola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 965)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 965)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 965)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Winogradskyella thalassocola"
                     /db_xref="taxon:262004"
     Protein         1..965
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106293
     Region          24..964
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktvlnallf climlptill aqttvtgtvt dkanamplpg vnviikgttr gtstdfdgky
       61 slevnqgeil vvsylgyttq eieftgqtsi dvaiaedasq ldeviligyg tttkkdatgs
      121 vdavtskdft rgnivtpenl lsgrvagvtv ntsgapgsgs eikirggssi nasnnplivi
      181 dglpisndnv ggsrgvlasi npndidsftv lkdasataiy gsrasngvii ivtkkgksef
      241 svdydvqytl gdideqievf saneyralvv aqnlpnnfis qlgdantnwq deifrktvsv
      301 nhnitlrgsl fnaiparfsf gvteqegail tsefdrrnls lslnptfldn hlkvnlntnl
      361 syednrfgds gqigaalgyd ptqpvydpts pfggfyqhrn gntlllggsn pvasllqtnn
      421 igdserfygn infdyklhfl pemkfvlnlg ydktegisrn nsvyatndpi kgnrsfsyqe
      481 rtnqsldgfl nykkdfgtig tdltagysyq kftnegyytg nqidpnsfgd tfadpdivli
      541 gffgranftv aekylmtlty rrdgtsrfse dnrwgdfyag alawkisded flkdsktiss
      601 lklrvgygit gqqeigerdl flsryqagqn nsqyqfgngi vsslipsein pdlkweetkt
      661 levgvdyglf deritgslnv fqkdsedllf napvpdgsnf snsivqnign lriqglefti
      721 ntdvikkedf nlnfnfnatl ldreitelaf gqdvttggia ggtgnfvqlf regespnsfy
      781 vfkqlrdtqg nyiegayvdl ngdniinded rylkenpdad vilgfqtnle ykgfdfsfnl
      841 ranignyvyn nvnssraqyd llrsnavlgn iptsvldtnf qttsdviisd vyvenasflk
      901 mdnitlgytf knlskyitsi rlwggiqnvf titeysgldp evfngidnti yprprnilig
      961 anfkf
//
LOCUS       WP_092466487            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Winogradskyella thalassocola].
ACCESSION   WP_092466487
VERSION     WP_092466487.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella thalassocola
  ORGANISM  Winogradskyella thalassocola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Winogradskyella thalassocola"
                     /db_xref="taxon:262004"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117014
     Region          20..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyiysclll clcllgnaqi titgtvtdav sntplpfvni ssnngngttt deqgtysivv
       61 nssteqltfs flgfktqtis vgnttiinia leedsaalde vvitalgler dtkelgyavq
      121 aisakkltev ktvnfldnlq gklagvtvtq gatgvgsssk itirgeasfs nnnplfvvdg
      181 vpinnetvfn ftneaaagfq eidfgngame vnpddigsvt vlkgpsaaal ygtrasngvi
      241 vietkngknk rglgisfnss lfvdtafklp dfqnsygqgn sgqfeysdgl gggindnity
      301 swgprldtgl lipqfdspvq lpngtfvrgg dtalydglei tatpfksnpd nlkdfyetgv
      361 ttinnisvsn gfdsgnyrls ftdlrsesii pgvnldrqti aaklnfkpsd nteinssfsy
      421 insssdnrps ngygsenany slvawgprsl nienlknywq pglegtqqys fnytffdnpy
      481 filnentnsf nrdrifgnls itqeltknls islrtgmdys tekrelrray ssnrfnngay
      541 aehdvmfrei ntdflinynn qfkdfsldvf lggnrlnqta stkqsqtvnl aqpgiynlnn
      601 aaspievfqf ksekrinsfy gitklgykdf lflditgrnd wssalatpfs vdgtsffyps
      661 vsssfilsnv velptaisfa klrasvaqvg ndtsayqtsg tfvsqtpyns qptfsdqnfi
      721 pnanlkpert tsyefgtdlr ffenklrldv tyynantedq iislpvaiss gynqqvvngg
      781 kvntqgveii lgitpiqtdh fnwnstfnft tnrsvikdlp qadgrltlay sriydsanqt
      841 vwfqveeggr vgdfygtgyk kndngeflid degqfiadnd lkklgnynpd ftlgwsnnfn
      901 yknwnmsflf dwrqggeivs rtralgnvgg qlaetsyrpd agivaqgvni ntgqantvav
      961 saesyyrqfy drnheennvy dasflklrqf svgytfnikd gflglkegad lslslvgnnl
     1021 faitenphfd peqlavqgna fvsgvedmsy attrsigfka gfnf
//
LOCUS       WP_092488070             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. NFACC42-2].
ACCESSION   WP_092488070
VERSION     WP_092488070.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. NFACC42-2
  ORGANISM  Pseudomonas sp. NFACC42-2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. NFACC42-2"
                     /db_xref="taxon:1566193"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38610
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag lkasivdsay eaagatigna
       61 gdafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaeqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vfnkegqlei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_092470489            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Winogradskyella thalassocola].
ACCESSION   WP_092470489
VERSION     WP_092470489.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella thalassocola
  ORGANISM  Winogradskyella thalassocola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Winogradskyella thalassocola"
                     /db_xref="taxon:262004"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117451
     Region          35..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkltwllt lfmafvmqfs faqektvtgt vttvadglpl pgasvivkgt srgqqtdfdg
       61 kytiqvnqgd vlvisyvgmt pgevlvgagn tydvaledan tldevivvgy gtttkdaftg
      121 tatkiaaenl eaktvsnisq alkgevagvn vvtgngapgs datirirgfg svngnqaply
      181 vvdgapynsd issinaadie sttvlkdaaa tsiygsrgan gvilittkqg ksgssvisvd
      241 fqtslntlll pqydviespe eyielswlsl knkgvllgqa dplayasanl ygtaeginnq
      301 yniwnaagad linpstgkfn sgierkytpt kwsdaafnts frqeaniqfs ggnektrfat
      361 sfgylddqgy aikssykryt trinlehkak dwltiggnla ftggrytnsg gdenvssssg
      421 nvfaltattp riydiylrdn dgnriddpif ggfqydygge ygrrswtntn giadanynle
      481 qtdvvtmlgn fnvgvdftdy lklevrysgq ynnsdnssra npfyggsadv ggtlfkdqrt
      541 ntnqnflqll rfnksfgesn ieafvahest enrykrfgag aqtailpntl dlaqyttpfg
      601 kaysfsqgwt ldsyfaqlny syaqkyyvtg svrrdgssrf lndkwgtfgs vglgwvaske
      661 dflsnvdfmd ylkvkasygv igdqgtnlqy gwqlynindt adgsysftqg stlanpdltw
      721 etskiaqvgf estwfndrld ldvdyyvknt tnlffnqslp gssgsaqiqy ndgtmrnsgi
      781 efnalvriik dgdfrlsagi ngelfdneit empkdfytge akvldgrysk gkslydwymr
      841 ewagvdpasg aalwnlyydd ldnngilssg dieissmtly lddnpnanvk rtttdtytna
      901 tnkyvgksai pkvrggfrin tgfkgfdlta qfsyslggyv ydggyavlmn nrnligsdnf
      961 htdvrdswke pgditnvpri sagyntdtqf hststrfltk adylslnnvn lsytlpkkai
     1021 sdmnltnvrl yvsgdnlmml sardglnpst lissgnsgiy mpmttfslga kief
//
LOCUS       WP_092494569             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Faunimonas
            pinastri].
ACCESSION   WP_092494569
VERSION     WP_092494569.1
KEYWORDS    RefSeq.
SOURCE      Faunimonas pinastri
  ORGANISM  Faunimonas pinastri
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Afifellaceae; Faunimonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Faunimonas pinastri"
                     /db_xref="taxon:1855383"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39669
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,92,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlredp sleprvaats etvkkfiasg atvaveagag rpagildady gtagasvveg
       61 reavladadl ilavrrpaal hgakhgaalv almdpfgneq alaelaqagi ssfslelipr
      121 itraqvmdvl ssqanlagyq avieaaahfg rampmmmtaa gtvpaarvfv mgagvaglqa
      181 iatarrlgav vtatdvrpaa keqvaslgak fvavedeefk aaetaggyak emsadyqakq
      241 aalvadhiak qdivittali pgrpapklvs aamlssmreg svvvdlaaer ggnvegvtpd
      301 qvtqkdgvtl iaytnmagrv aastsallar nifafvesmt dketkalrid rndeitaatl
      361 lthegsvvhp rfapaapvap vveegav
//
LOCUS       WP_092500879             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Meinhardsimonia xiamenensis].
ACCESSION   WP_092500879
VERSION     WP_092500879.1
KEYWORDS    RefSeq.
SOURCE      Meinhardsimonia xiamenensis
  ORGANISM  Meinhardsimonia xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Meinhardsimonia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Meinhardsimonia xiamenensis"
                     /db_xref="taxon:990712"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55885
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeva rgearvamtp esaralqklg yecliesgag eaagfsdaey eeagvevvkt
       61 aaglwkaadi vakvrpptet eakrltkdki lisffypaan eellklcaek kstviamdmv
      121 prisraqkmd alssmaniag yravieasan fgrflngqvt aagkvppakv lvvgagvagl
      181 aaigaavslg aqvyafdvrp evaeqiksmg aefvflefde nqdsaatggy aapqseefrq
      241 kqlekfrela pemdivitta lipnrpapkl wtedmvkamk rgsvivdlaa erggncdltv
      301 pderivteng viiigytdfp srmaplastm yannirhmvs dltpnkdgva vvnmeddvir
      361 satvthggei twpppplkvq aiaspakapk pkeltpeekr aqelaefraa trrqvslltl
      421 gglamllvga yapasfmahf ivfvlavfvg fqviwnvahs lhtplmavtn aissiiivga
      481 lmqmgsgswl vvvlaaasvf maainifggf lvtrrmlamf qks
//
LOCUS       WP_092511463             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Afipia sp.
            GAS231].
ACCESSION   WP_092511463
VERSION     WP_092511463.1
KEYWORDS    RefSeq.
SOURCE      Afipia sp. GAS231
  ORGANISM  Afipia sp. GAS231
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Afipia sp. GAS231"
                     /db_xref="taxon:1882747"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39173
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvavsp dtvkkfkalg vdiaiepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygndaa lkamadagis afamelmpri
      121 traqvmdvls sqanlagyra vieaaeafgr afpmmmtaag tipaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehvkkq divittalip grpapklvsa emvksmkpgs vlvdlaverg gnvegakage
      301 vadvggikiv gytnvagrva qsasslyarn lfnfietmvd kttkaldvkw ddelvkatal
      361 tkdgavihpn fqpka
//
LOCUS       WP_092514953             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Afipia sp.
            GAS231].
ACCESSION   WP_092514953
VERSION     WP_092514953.1
KEYWORDS    RefSeq.
SOURCE      Afipia sp. GAS231
  ORGANISM  Afipia sp. GAS231
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Afipia.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Afipia sp. GAS231"
                     /db_xref="taxon:1882747"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39179
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvavsp dtvkkfkalg vdiaiepgag iksglpdgdf tavgatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygndaa lkamadagis afamelmpri
      121 traqvmdvls sqanlagyra vieaaeafgr afpmmmtaag tipaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa emvksmkpgs vlvdlaverg gnvegarage
      301 vadidgikiv gytnvagrva qsasslyarn lfnfietlid kanktlavnw dddlvkatal
      361 tkdgavihpn fqpka
//
LOCUS       WP_092522651             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Onishia
            taeanensis].
ACCESSION   WP_092522651
VERSION     WP_092522651.1
KEYWORDS    RefSeq.
SOURCE      Onishia taeanensis
  ORGANISM  Onishia taeanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Onishia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Onishia taeanensis"
                     /db_xref="taxon:284577"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55509
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkera pgearvaltp esaqqiqklg heclietgag vaagfadaay rdagvsvved
       61 akalweqadt vikvrepsde eadllhdgqt lisffwpaqn eallercran gatvvamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgsesggy aapsspefre
      241 kqlacfreqa pdvdivitta lipgkpapkl wledmveamk pgsvivdlaa ekggncdltv
      301 pderivtdkg vivvgytdfp srmatqssll yatnirhmlt dltpekdgvv nhnmeddvir
      361 gstvthagei tfpppppkvk aigaskpkqk ekeptheekk aaehaafvtq tkrqvgmlav
      421 ggavmwllgq vapasfmqhf ivfalacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 vlqigsgnwl vgllasisvl iasinivggf qvtrrmlamf qks
//
LOCUS       WP_092532920             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces ruminicola].
ACCESSION   WP_092532920
VERSION     WP_092532920.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces ruminicola
  ORGANISM  Actinomyces ruminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Actinomyces ruminicola"
                     /db_xref="taxon:332524"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53258
     Region          1..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgipcqpp drslaaatpq tverlirlgy dvvvqrgaga pahfpdtaye eagaqladra
       61 evwacnivvt ayapddaeld lmhpgatlig rldparhpdf vqklqdhslt alaidtvpri
      121 sraqsmdvls sqanlagyra vieaaghfgr llngqvtaag kfppasvyvi gagvaglaai
      181 gtayslgavv rgtdvrpeva dqvksvgaef vpvptaqevs adgyakemst dqaalanaly
      241 aeqaaaadiv vttanipgrr apllldraav eamrpgsviv dmaaanggnt eltvpgevvt
      301 tpggvtivgy tdlaerlpaq asqlygrnil nlltlltpgk dgelaldled qvvraitvcq
      361 agellwpppp vsvsaapkap taaappqsas daaadaeaea aaqarsrrrk tigialaata
      421 aaalvlvtpa aatshyivla laiilgfhvi snvtpalhtp lmsvtnaisg iillgaisqv
      481 gnanpaisgv afiaimlasi nvfggfavth rmlamfrke
//
LOCUS       WP_092539793            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092539793
VERSION     WP_092539793.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111138
     Region          25..1019
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrqfkrpvl llfllfsiqi waqerdisgt vvdedqiplp gvnvrvknsn igtvtdfdgk
       61 fslsipnaeg ailvfssigf ttqevqvedq safnitmavd teslnevvvt sfgierekka
      121 lgysvqevts eevlegnqqn vvsglqgkvs gvtignsgga pgsssvilir ggtsitgdnq
      181 plfvvdgipi dnstgssltv asinraadln pedienisvl kgpaaaalyg iqaaegavii
      241 ttkkgkagss tvsysgtfsv devlgtpdvq qnygqgtqil stdgfsyetq spfswgpevs
      301 gaqtydhisd fyqtavtqnh nvsysggtek gtmylsigdl sqdgvidgts ydktsfkint
      361 ssqvndkltv gasanyivse igstrqgnas gssyssllsy pvnidiqdyy nddgsqrmfy
      421 ndqtfdnpyw slenspnenk vnrllgivnv sydflndfni syklgtdyfr efskqvigtg
      481 slienrsegy isqferenrr ttsnliisyn kditedfavd alvgnmvedl kvhtvytygd
      541 gfqapgiysi gnvsqenqsi teiirrrrav gvfgevkfgw kdalflnftg rndwsstlpq
      601 edrsffypsi gssavltdll sqggnditsd ngltylklra twakvgkdap igalesflgt
      661 ninslassay tyngvdignp elepeftnsy efgfdsrffe nrlgldmsfy ysksenqile
      721 dirvppsagt fyatlnggsi enkgieallt aklfpresdf qwdmtynlgv nqsdvielpg
      781 qldevylsds wtfgntaaga ailggslfgl rgyqavrnda gefiigadgl peletviydd
      841 vnrlpdwtlg itntlsyknf nftflldivq gqeaynatks alayyglaee tlgrstggtr
      901 vvegvtangn pntvevtdqq yfqqyysqna enfiedasya rlryvtfsyd lpsdfldkfn
      961 vvsaqlsvtg rnlftiteys gvdpevntyg agiqgagsmg idnlgtpntr gfdvglrfkf
//
LOCUS       WP_092540198            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092540198
VERSION     WP_092540198.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112619
     Region          37..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlqetnshpl plmfkqkihi lflmlfisga nlfaqnqitg kiidnngmpl lgatvavrgt
       61 nngtqsdmdg nftlqvanpq dailvisyvg fstkevping knsieitlee dsealsevvv
      121 talgiksekr algyataevd gdnlsnvkat nnfvnalsgk vagvqissss sqpgsgariv
      181 irggssitgn nqpllvvngv pfdaangsss sgladidpns ieslsvlkga aasalygsea
      241 angvilvttk sgtfnmkpvi tlsssvsfdd iyeiplqdqw sqgywenddw vyidgnssft
      301 stsfgprise vpgaelydrw difetgitne nslsitgggd kasyyvsysn linngilspl
      361 efrrnsinan tsfkftpklt vssnilyttq knerlfedss nssfmntlms tpntwnpypi
      421 yaedgslrsy rggsrdpytw vldnvganne rdrfagtfii eyevldnlkf rsvtgistts
      481 ahsdsfynlg gyasvqgsys sserfsrdie stetitydnd fgdfevnami ghniqenkwr
      541 gnyfngngli lpniynsanv sgysayddrg mfrsysffgq amigykkmly ytvtgrndwa
      601 ssladsffyp shslglvfte lfpkndilnf gklrasyakv gspagayarn nplvsaggdg
      661 vmwpfngqqs ylssaripnp nltnefksev elglelrtlk srlnfdiayy hnwsenqils
      721 eqflastgyt ygsvniggit hkgvevgina tpiqseffnw dlslnwskdn snvdrlgtnn
      781 episvgsygy aivdqpypvi fglgflrddq grlvlddtpg lsygrpladn rgnqilgqta
      841 pewisslrnt fnyknlslmf qfdmsrggnl yslndhylty ygmaehqndr pdnnmttfdg
      901 vmghydsatg evvvtsetpe ptrydlyyqt vaqsvledni mpkdyiklre vqlaynlpnk
      961 ivasaglqdv qiafsgrnlw rsfhddfegp dpeintdgit ngngylsysl pttktysitl
     1021 takf
//
LOCUS       WP_092540242            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092540242
VERSION     WP_092540242.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110679
     Region          24..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfkkiifsfl lvmglnqiav aqsqtvsgti teaetgmplp gvtvmekgts ngtstdfdgn
       61 fsldvgddat lvlsmigyvt qeipvtggdi nvematdtea ldevvvtalg ikreskalty
      121 aaqtlgsdev tqgknvnfaq glngkvagve irqgtagags stkiqlrgas nitssnqplf
      181 vidgipmany qtsdasgfyg grdsgdglsn inpediesit vlrganaaal ygsqgangvi
      241 lintkqgeeg ktrinisstt kfesvydypd lqfrygatde pgadsswgap gdyenhvddf
      301 fdtgitlqna islsggnnrt ttyfsyanty atgtmptnef nknnltfkqt skffddklkv
      361 tsnvlltdqk vdnkmlngyy fnpllglytf prgldfdeya nnyqvldpqr nimtqnwpil
      421 gnseanmnpy wilnntpnve rtkrfignas ieytisdalt lsgrgsydft rqiyeqkama
      481 gsspvvisdn gryvyenves wqayadmilt ydqqfgedwd fhgvlggayq kriigegisv
      541 dsqtfglyap nifniqnitg lqafsgaqrv nsrlikqsaf anaslgykdm lfldlsarnd
      601 wastlsften ssylypsagl tflpseafel pefisfaklr asfaqvanev pafrtnpint
      661 aaysqvginm elpftelnpe mqdswefgad frfldsrinf satyyqidtr dqflpmdail
      721 gtpyqvyyvn aghvrnygve itlgadvfet edftwntnfn fthndneiid lnetyngqrn
      781 rivggggegy etfivqggsl gdiyvnaylr ddsgniivse dgvpvnatst dgmklvgnan
      841 pdfmlgwnns isfkkinlsf lidsrfggkf vsqteaylda lgatettaaa rdaggvqvdg
      901 vlndgtpfsg vvdardyfsg vggrngiker yvydatnirl rqftlgynfg feedsfvknl
      961 nvslvgnnlf ffyneaptdp dfaistgngt qavtnfgppi trnfglnlsa nf
//
LOCUS       WP_092540240            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092540240
VERSION     WP_092540240.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112075
     Region          24..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkiifsfl lvlgltqmaf aqsqtvsgti teaetgmplp gvtvmekgts ngtstdfdgn
       61 fslnvgddat lilsmigyvt qeipvtsgev naematdtea leevvvtalg ikrekkaity
      121 saqnvevdel searslnvsn slsgkvagln fsttsngvgs ssritlrgnr sltgnnqply
      181 vvdgvpisng sgnrnsdidt ggttqpdgis ninpddiani svlkgpsaaa lygtrasngv
      241 ivittksgng aqgtsitvss nfmassaynl lnlqneygqg tngeyvpnss sswggrldgs
      301 qveawqlvrn pdyegpatya yapqpdnvid ffqtgynlan tlsittgank tqayfsytnt
      361 taegivegnk ldrhnanlrl nsqltdrlsv dvktnyivqd idnllrtgee sigtsayllp
      421 rsiahsqyed feyldaegql qtnyfrdevg apggnpywsa lrnddrtdrr nrfigmaslk
      481 yqftdhlslq vrtgiddmsn ktfrnryatn afnndlgayn eyyetvreln sdallsydnt
      541 fgdfslnmnl ganmlkqsnt slnsggvlsl rnffalanve tisststkre kqinsvygfa
      601 qlgyqsklfl dvtarndwss tlpeanrsff ypsigisgiv semvelpeff tyakvrasya
      661 evgndtdpyq lspqlsyigg nggmlyaqtt aanpnlkpei snsvefgadv rflsnrlgvd
      721 ftyfktntkn qifsintpes sgysnaivng gevqnsgiel sltatpvete nfswdilany
      781 asydseivsi fegreelvlg qgrlvrskvv vggqygdlyv qgfqrndege vivneagipl
      841 atnsfdvygg nfnpdwtggl kndfrykdfs lsflidmrig gdvisytqar qaglgvnemt
      901 lagrengfvv dgvvdngdgt fsqnttnita eqywtaigqr tpvaepfifd atnirlrelv
      961 lgyampkrll enspfksvnf slvgrnlffi lneaeyfdpe qgagtgnlqg iesfnipstr
     1021 dygvsvkfgf
//
LOCUS       WP_092540278            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092540278
VERSION     WP_092540278.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112764
     Region          61..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnniqfkivf salflflpyl gfsqtseeid veatvrgksg dpiagatiit sssttltdsl
       61 gvfevsvplf seitiqanqy qprliivked ienislepie aykdvnvafr kvekrnlisg
      121 vttidveqlm eksyntssle nmtalangfh gniwgmneyl ilidgvprda gsilpteidq
      181 isflkgvaav alygsraakg vvqittkrgk iqkqkievrm naglytpksf pkylgsaeym
      241 tlynearand glselydeet iynhatgnnp yrypdvnyys sdylqesynr ydataqisgg
      301 netaqyytnl gfytagslld fgeasknsnq rfnirgnvdi ditdylyatv gasavyyngr
      361 gvnanywgda arlrpnrfsp lipigmiees densmqyvnn ssflidnqyl lggtqldqtn
      421 pfaaiyaggs nnytsrqfqf ntgigadltn lleglsfhss fgvdystsyn qsynneyavy
      481 qpswtnynge sliagltqyg qdarsgvqni sdswyrqtis fsgqfnyetk iedhnisail
      541 langfqqsvs eeyhrtsnan lglhlgysyl dkyyadfsga vvhsaklpeg nrqafsptlt
      601 lgwrlseenf lknssvfddl kltasagiln tdmdidqyyl yesiytqtdg awfnwrdgal
      661 srstdsrrgq nydltfakre einfgleasl lnnlfyvqgs ffanrisgni vqnsilypny
      721 fttgwpnssf ipfvnynede rigfdfrvdw nqkigevett lgfvgtyydt kaskraerye
      781 dayqnrqgts ldgiwglend gffmneeeie nsatpsfgev qpgdikyidq ngdglvdnqd
      841 vvylgkagwf gapftlginf taewknfsff algmgrfgah amrnnsyfwv dgedkysevv
      901 rdrwtpetse tatyprlttt tsnnnfrssd fwmystdrfd lakvqisynl pkamfnrsfv
      961 qeigvyvggt nlltvspere ilelsvggap qnrfynlgik aif
//
LOCUS       WP_092542767            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092542767
VERSION     WP_092542767.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118939
     Region          29..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiitkvft iflcllggll yaqdlgdqrt isgdvtdsng eilpgvnvfv kgtqngvvtd
       61 meghytiraf grdtlvfsfi gmksveryig gesnidvvle ndneqlddvv vvgygeqkre
      121 hltgavetvd meeiedlpvg nlatalrgkl pgvnisggsv rpgrkptlti rnpitlskdg
      181 gnnqplyiid gvlqidaqgl ndntlfnqld pseiqsisil kdaaaavygs rgangavvik
      241 tkrgqagppq fsyngsygit deqqrtkmls gaefarfine lngpygnpnv sredsnsdny
      301 ffsddeiayf edneydwldr awssastqrh svnvnggaeg atyfggasyy kqtgnlaevd
      361 ydkwtfragt svditrglna nlqvsgnfsn rsstfnkvsg eneeddynnl lrapgyvppy
      421 inglpvnipg ggvggdgyhy faiqnldnyk rdqdqtltfn mnleyevpfv dglafratyg
      481 rnmgagkysq lgsvyqlynf ettgenghiy lpdaqvvgdp ievengdrif yrnsdnfseq
      541 ynfvatynnt fgkhaiggla tiergetegt qqqvlreeva ansngqfnsa fgnvdgytwk
      601 yesgslsyvg rlnyryddky llellyrsda stkfapenyw ghfysisggw iiskenffns
      661 dvfdflkirf shgklgkddt kmwawrqryt fqlargavfg gdaprsdgfk melspnrdav
      721 wsddyknnlg idmqffdrrl nvtvdafynq grnmliertg avpfsiggtv aaenygevnf
      781 wggefsvgwq dnigqdfsyg idvnsgwstn kvlvgnfdet svlpwnasqg emsevgtwgy
      841 dylgmfkdqa didayvdqyn iqqvfgipae nlrpgmlyyr dvrgehlgdg efadpdgiin
      901 endrvelerp nssfglgsti rlkyknfslq atlgmswggf daidardidi nsqidqsfqn
      961 vpkiwndiyn petnpngrmp npyysqinav asefwrvssf rftmpnlnig yslskdaaqs
     1021 lnlsalsvrl talnpinfyn pysykgangs wygypvlrtf slglnirp
//
LOCUS       WP_092543046            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092543046
VERSION     WP_092543046.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116445
     Region          26..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkftflal lsfmftttff aqnqivsgtv kvaednmplp gvnvivkgts ngtvtdmqgs
       61 yslevppnsi lvfsaigfvs qeieidgqee ldvslvqdte sldevvvtal gisrnkkslg
      121 yatqeveged lnltnqqnvl gtlsgriagv qvtgssgasm ggtqkikirg vnsinggdep
      181 lividgtpis nsnfsgsaga dygnlaqdin psdiesvnvl kgpaasalyg irgqygvimi
      241 ttkkgkkgpk dvrvqvnssl mlefagnflp kqnmygggss qtfrtlangd pyvdlsvdes
      301 wgprmdgtpv rqvfsfypqd ptygqltpfi phpdnienyy etgvnlnngv tvsggnentt
      361 yrlslndtri egiepntelk rnnlgvnasl dlaenitvst ninyarndaq rpgqgseygv
      421 ayfnqwfqrn ldmtrlkdym yddgtilhwn lrrpnsdtge itnfdplywn npyfnayenl
      481 sndsrdrffg dvtlsynilp eleirgairs dmytqnienr tafggtglpa ysvgkyqnke
      541 wnyellaqyn kkfgdisldg tlggniynrn ysylsqatvg glsapgfyni dasidrpstt
      601 syklekqirs lfamvslgyl dtyfldasir ndnssalped nnsywypsvs gslvfselvn
      661 wevlsfgkfr asyaqagsdl spyrttvayg vgtvyngvnt lyvpdnlnnp diepsfshsy
      721 etgldlqffg nrlglnftyy kqrnknqiis ldvsgasgyg sstinaglie ndgieislsg
      781 kpiqsndfsw eaifnisqnk sevvelapgi dvynygstty ssvssylnsy egkpfgslvg
      841 qayqrdeatg dilvdgngmp lytdstydfg tvlpdftggf qntirwknls lnamidfqgg
      901 gqffsrskml gvrtgqdplt vatnengmnv rdpledgggv lvtgisaetg ervenfvdar
      961 syyrnvlgrr iyeewlydas yiklsevrfg ytfgtktmem lpfdsvnial iarnpamiwq
     1021 napdgidpsa istgsqsisw yesgqlatvr syginlnitf
//
LOCUS       WP_092543181            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092543181
VERSION     WP_092543181.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118988
     Region          25..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvklssilt lllvliahit faqertitgt vtdddglplp gvtvlvkgtn ngtqtdfdgn
       61 ysisaqsgsv lvysfvgmtt qeftvtesst idvtlqmdsa qldevvvtal gierdkkslg
      121 yatqevdgsa vsdvptqnfv nslsgkvagl kisnsgtmgg ssnvvirgns sltgnnqalf
      181 vidgtpisna nnnrsgqasg rggydygnaa sdinpndias inilkgaaat alygaraang
      241 aviietkkgq knkgigisis stlmtshvnn ktlpeyqdqy gagygayyqs edgyfnladi
      301 dgdgnldrtt pftedasfgg rfdgspvyqw nsiypqlagt dydyyqqatp weagehtpnd
      361 iwetghtsin tvaldggtdk ssfrisatnf mqegnlpnse ikrntikfsg ahdftdkfsa
      421 qanitftktd gkgrygtgys stnimqqfrq wwqtnvdlye qraayfatge nitwnpngpd
      481 nlspiysdnp ywtlyenyqt dtrnryfgni nlnyeisdvf svlgrfsfdt ydelqeerre
      541 vgsadlgyys rfnnraaeyn ydlilnfnkd issdlnldgn lgfnlrrner syilastngg
      601 lnapnffals nsaspinpps eyendrmldg iyaraglgyl dtyyiegtir rdrsstlpke
      661 nntfyypsvs tsiilsnlin adwlgytkfr anyaevgndt spyrvfntyq isapfgsagw
      721 asnnsqlanp nldperkkay eiglegnffd rrlgfdlsyy nsqtenqitp vpvstatgfs
      781 qqllnagtie nkgieasltl npirtddfnw imninwaqnr sevveladgi dnlqlasvqg
      841 gisinaapge pygairgsay vyddagnrvi tdagyyertp nanyiigniq pdwtggvsnt
      901 fsyknlslnf lidvqkggdi fsldtwygra tglyetsvgl ndlgnpkrnt lengggvild
      961 gvqgdvsyns dgsyevtnts enttrartdy ygnpfgygrd aneghvydas fvklreagit
     1021 ynfgpsvida tpftraslsl igrnlwiihk nipysdpeag lssgniqgyq sgaypavrei
     1081 gasiklnf
//
LOCUS       WP_092543442             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinoplanes derwentensis].
ACCESSION   WP_092543442
VERSION     WP_092543442.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes derwentensis
  ORGANISM  Actinoplanes derwentensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Actinoplanes derwentensis"
                     /db_xref="taxon:113562"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52317
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigvprdpd pgerrvaatp ttvtqlvklg yqvvvepgag aaasfsdesy adagatvgda
       61 laadivfvin pppvaqrdkl adgatligml nprldpelva dlagrpital smdavprisr
      121 aqsldvlssm aniagyravv eaahafgrff tgqvtaagkv ppakvlvaga gvaglaaigt
      181 agslgaivra tdprpevadq vkslggeylp veaadvevss tgyakqmsdd yndratrlya
      241 vqagevdiii ttalipgrpa prlitagmva tmrpgsvivd maaanggnve gtvpgevvvt
      301 angvtiigyt dlagrlpaqa sqlygtnlvn lmklmtpgkd gqlvldfedv vqrgitvvrd
      361 geltwpppav avsaappkas essvnpdnsv kgeavgskrr lntltvvgag atglflltal
      421 apaalrghlt vfalaivigy yvigkvhhal htplmsvtna isgiivvgav lqlgdsqdli
      481 tvlscaaill asinvfggfa vtrrmlamfs rs
//
LOCUS       WP_092543692            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092543692
VERSION     WP_092543692.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118292
     Region          22..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhfyllliv finlvwtsyg qqeisgvvtd pdglplggvn isvknsnqig avtdidgdfl
       61 inavqndtli fsyigfktqe vavgnennft vtlqvntesl dqvvvtalgi tkaekkigya
      121 tqeietnnle nlpvpnvanl fsgkvaglqv ssppgmfqsp sfslrgktpl ividgipvet
      181 dffdvpqnni aainvlkgta asalygsrgr ngailvttks atqdglsiei sqnvmvsagy
      241 aifpetqhey gngsngqyef wdgadggiad gdmiwgpkfd enllipqwns pivdsqtgkv
      301 ipwygsvtgt qydnrsrysr qplpwvrhdn lddflrtsii sstnftvsqk sekgyyring
      361 nfshnrdrvp nsslsqggls yksltqlsdk msltsklsyn kvyspnypny gynpsghmyt
      421 lliwmgedvn gqdlknhqwv pgmegyrqan wnyawynnpw fganhyqkey nsdllnvqlk
      481 layefdehfr lqlrgsgvlk snfedlespk syfnysapre gsyqtwnsrr lnidydvlat
      541 ydnsisedfk ivvnagastf frryqqefaa tdgltvpgvy nmgnstgpvr aennlwkkai
      601 nsvygtldle flntyfitms arndwsstlp kenrsyfyps lsgsalisni fempedieyv
      661 klfsswarvs sdldpyqlsa yynssgnfan vqrlvypsgi vnpnispets tsfeigvnts
      721 fldnrfafda tyyntvdtdq iinqpislas gfssrkingn eyttnglels lrfkpmvneg
      781 lkwsallnws kkvtkltkit sgedkfgnls lndridsyyd qewmkspege vilnastglp
      841 trdtylsylg hfdpdwtfgf vndfkyknwn lniamdgvwg gvlrsqvvek mwwggkhpks
      901 vqyrdeeyaa geaiyvpkgv nlvsgelvrd vsgnivsdnr vfeehtapis wqtwsqnypy
      961 rarvtedese tfanvfdrsy lklrsislsy nftdllnskt ikdanvsfng ynlfvlkkgd
     1021 yytdpdykts dnnniqdpss rylglgvnfk f
//
LOCUS       WP_092543672            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092543672
VERSION     WP_092543672.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115262
     Region          29..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkynfril kilfviitts lfcdtisaqq vsgvvsdakl gepllgvtvi ekgssngttt
       61 dmdgrfslrv rdkkggalif sfigykrdtv pianqdymki elneelgqlk evvinagygq
      121 mkkdmttgsv asisgedlqd lptttvveal qgriaglnvl gtsgapgaqg iitlrgntsm
      181 npdtrsqply vidgvimdpe vsgaaqagln plallnpndi ksidvlkdaa aatiygarga
      241 ngviivttkr assnkpqitv rteigmstrp alrpvmvgaa errfkmnylk nnltnpeqrr
      301 llslmltdsl ntafnnnsdw qdmliqgalt kegnvaisgr tetsdfrmsl nyydeegvik
      361 nsgfsrmsan lmynfrpvek frinsnvsft hvgrkqgngd ylfrfsgwnf pssfwqitet
      421 ereyhtgale dvrnkndffl fngnlnlqyd fnnhlkftsn ivgnlnysre drfqpgyvaw
      481 ngianatsns sdnryysven yfnfttkfnt eshnfnavig qsfeeqysan tysqgrdipv
      541 taiktiqglp dkntttstyn gerslasfft rlsydykqky lisanyridg ssrfgrdnrw
      601 ayfpsisggw iitnenffpe skafsfvklr gsygitgrep gglyqsyqgl rsdinyynni
      661 ytqsyggagf ivpnyvenvs spglsweqts qtnlgielrf lenrisltge vyerytadll
      721 fsrqipaitg ysnaldntmd vlnqgweltl gasivqnekf rwrsdltiah nenivaktpg
      781 grditsawfs vsqggplyny kvwetdgvyp rtsdvpvdpl tgermrqgws ggnqyeggdp
      841 rridqnndyi idgndlvsyg ssdpdlyggw nntfnykgfs lsvqcnfvyg rnilngylsd
      901 klngasnnan nmwgsisgpa sdlgdysfwi npgddteypr iipnnidqwn iqsssfiedg
      961 sffrvkfinl gysipralse nlgldrarlw gsvnnvwtys dstlldpeav apngyasaqa
     1021 ypvpnkfslg ievaf
//
LOCUS       WP_092543772            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092543772
VERSION     WP_092543772.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111945
     Region          40..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mliskllisa vgkirkgfrf ffilmmmlgm ssfaqsqeli tgmvtsegdg mplpgvnvii
       61 qgtstgtvtd idgnysieas endvlvfsfl gfkqqeiqvg tqteinvsla edmnalddvv
      121 vvgygtqrke dltsavssvd sedfiqsnvt dagqliqgkv aglsismpsg dptassqirl
      181 rgtssilgsn tnplilidgi pgdlktvppe diksidvlkd gsaaaiygtr gtngvilitt
      241 krasgaytnq vdysvslstq qifnqldvls asdyrrqien gtrdasadag sstdwldeit
      301 qtpftqvhnl tlrggnnttn ylatinlrdl egiflksdnt iftgrvdinh ymfdeklkin
      361 lgiigrsvny tttgdgssfn gytyrqalir nptepiknpd gswyevpgnf nydnpvsrln
      421 esdgenksqf lrynaqltye piedlklsal gslsrynqtr gyaeskdhis nvrggvngfv
      481 sngtretedr lleltaqysk tlmddhdfnl lagysyqeny yrdyymtnsd fptdiftyhn
      541 iglgrrleeg qagmgsnttk tnligffgrl nynykdkyll mgsvrheaas qlyktnepwg
      601 tfpafsagwr vseeeflrns niidnlklrf gygvtgipnq lgfgavallg ygqyfyyndt
      661 wvrtlspsqn pnpdlkweek heynygidft lfnnivsgsi dyynrnvqdl lfdfavptpp
      721 nlygttranv gemknsglev mlninpinke dfqwstnvgf stnsnelvsl snnlyqtend
      781 yfttggtgep iqtfthrvrv gdpignfygf kvvdidddgr wiyetpsgei qnydefghsf
      841 edkqvlgngl pnyyanwnnt fkykdfdlsi tmrgafdyqi lnfermylen ptidnynrlq
      901 ssedavfgkt altspleyns yyiedgdfwk idnitlgynf seigkyiksa rvyvstlntf
      961 tftgydgidp evnrsglspg ndgrdkyptt rtytlgfnvs f
//
LOCUS       WP_092543825            1187 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092543825
VERSION     WP_092543825.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1187)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1187)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1187)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1187
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1187
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131731
     Region          138..1186
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllkpkrr pkplfdklkm rislllflsv fsmkandsla qktkitfdhk dvsiyqlide
       61 ienqsdfhfi yrvknvnlsr kinirvvkkp lievlklmfd ksstaytvve qdkqihltek
      121 kplpshsest nkqqqflvkg misdenglpl pgasviekgt sngvvtnfeg efsisissen
      181 amlivsfigy ktqeiavner atiniqlsps aadldevvit algmkrekka lgyavgevds
      241 erlnlvpqen vlgglsgkvs glnvsragnd vfapsyvtir grtsltgndq plvvidgapv
      301 gdasvmgdis amdiesvsvl kgasaaalyg sragngvili ttksgkgiqk gigvslnstl
      361 tinnpykyfd lqnrftngqr glfneatwqh wygaeegaqa vqwntngeaa plqfydnsle
      421 dyfttgvtti ndakvsgsye kgdfrlgish lngegitpea elkriglnlg tnykiaenvn
      481 lslnlnltns nsdnypsnli ggndeyfdiy niaphinind lkdqiwlenn vqqrnitegy
      541 nnpwwfsrer qnrfdrirgf gnlelnwkis defnalarvs hssnnnrqei irpwsyqgfg
      601 ntqpfgsyfi nraldresna evlfsytkdl kdfnvsasag gnilnskges fnaggdnlvl
      661 pglftlsnva rgglnyasaf sekaiysayg llslgfrdia fidvtarndw sstlprenrs
      721 yfypsvsgsv liseitqmps wisliklrsg waevgkdtsp yaihpilsqg ywgedftysl
      781 pgsmpntqlk peiatsyevg adlkffnnrf gvdatyykne nrnqilnvna splsgytstt
      841 inagkvenyg velgmhlvpi ksedflwnmd fnfttqkskl velvdgidrv sfgggrdmgs
      901 ftrvggeigd lyspyiqkve egpyagwnll dtngrwvvdr tyenqkkvgn fnhdftigmt
      961 tsisyknftl sasfdwrqgg qffsesmkrm arsgkienwq ngvssstfsg ildansfggd
     1021 realaneirn npvyrdndvw iggrteelgg fenngnynga ffpgvidngd gtytenfggp
     1081 gtrmfdayrv vessgsfwrt gyafmydasf vklrditfty tlpeklaski sannisfsly
     1141 skniilwtea gigidpelay hggqqghekw nlapwtapvg frlnvgf
//
LOCUS       WP_092543916            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092543916
VERSION     WP_092543916.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113268
     Region          31..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknntifllf ifslgivfch ntyaqtdtey rtvsgqivdk dnepvakakv itvlaknvve
       61 tgengeftve isgeeadflr vvkkgyesqs mfvsadleap ivlqeapyly gtndlkipyl
      121 dlkssknvsa intitgeelr tfpsiqflea legrlpglmm sqsnytpgae wvtgvvrgep
      181 aiyyidgiqr nprdltvyei dkvevikdfs gratlgisga spivwittik gqenkneini
      241 taetgyseaa nlpnyldsyn yatlyneala ndgldplysq ealdayqtgn ntlrypnidy
      301 ydryvkdfsr ftranvdfqg gsdkltyfsn lnyvgsggye evgqettydr ykirgnvdik
      361 ltdfmrmnvn lsgtygraey pnqgdgayry nmfsvlssyp snatpiyyed qlivsdnypv
      421 nltnelvygg yaestelntq nlvsllidle svakglefya saaldannvl vnnlggtaal
      481 yrrvtgtdne lervveqevq snmyngddsy drrisamanl sykfvkeehd ldldlsyyqs
      541 mqenrvvggn yqpdriqdlg franylydgk yalqfdasyt gnmrlpdger fnfyptvgaa
      601 wnvseesflk nsnvvdylkl yssygimgvn nfnfggtynp yylyqtlwqn vgtwssgieg
      661 qrsgadnvye vlqygstgfs lperqyfnig fkseffdrki aleanyfdqk dvdilspmsn
      721 ftpsiygtgg flpiqnfeef rrygvdgmvq yndefgdfkv slgvnamylr senlvvdepa
      781 alaeyrqrtg ngddvffgyn alglyqsqse idsrgvtqsw gtlapgdimy edynndgvit
      841 eqdihaight priayginis laykgfdlfv langrangem mlngtyfqnn ttnnnyseam
      901 ldrwpvsnnm prlttvsqnn yqissfwled gaylnlrnvq lgytfpnsis rklnmqelkl
      961 flrgrnlasf skihseygln peslssgilm ypisrtltfg lstkf
//
LOCUS       WP_092544636            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092544636
VERSION     WP_092544636.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111555
     Region          37..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnyrccnl vvlipllyii lqletgkvys qtnqnqqtis giisdqdglp lpgvnvlikg
       61 satgtmsnmd ghysilvsig dtilysfigy qtiekkltpg fngdlimhpa tdalsevvin
      121 agyynttere rtgniarvta eeielqpvvs piqalqgrma gveivqqtgv pgaaptirir
      181 gqnslrtgfn dngnlplyii dgvpvnsapi nsinrfnssi gidplngidl ssiksievlk
      241 dadataiygs rgsngvvlit tnnknysqqq ekflirvysg vsnvsnylem lntpqylair
      301 reafendgve ptvanaedlv lwdqerdtdw qkelfgqhsp tfnayinysg gneytnfnig
      361 asyfkqgmvf pgnysfqkkn islnlnhrsk nqrfqtnlti nygltdndlf stsnfvgnal
      421 slppnapaiy nedgslnwen stwsnplapl ngsgknegki lisslnlsyk lfegfylktn
      481 lgyntldsrd dlklpiviyd paiwdrvsnq srllinnris wiaepqinyt ktfkknqfdl
      541 llgttfqhse dsrlgfngtg yanaqlignl naadavvsta dqsliykyha ifarigynfd
      601 krlflnltgr rdgssrfspk nrfsnfgavg aawifssskf lednldfisf gklrgsygit
      661 gndqigdyry ldayratpgp gglyptqlan snfswestkk lefalelglf knrtnlnlsw
      721 yrnrssnqlv gytlpsitgf tsveanlpat vqnqgwelel ssdiiknknf nwrssinlsi
      781 pkneliafed ieqssyaraf evgeplsiqk vyhfngldte tglyqiedan ddgrydyqdq
      841 iinedlgrvy fgglynqlsy knfslsllme fvkhkgnefy intpgffgyl idngqyvngl
      901 avndgvqgps qsidallaye nvvrsdlwis dasflrmktv dlsykipekl fssqslpdiq
      961 lfvqgqnlft itnykgldpq spgsrnlppl rtisaglslt f
//
LOCUS       WP_092544783            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Zunongwangia
            mangrovi].
ACCESSION   WP_092544783
VERSION     WP_092544783.1
KEYWORDS    RefSeq.
SOURCE      Zunongwangia mangrovi
  ORGANISM  Zunongwangia mangrovi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Zunongwangia.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Zunongwangia mangrovi"
                     /db_xref="taxon:1334022"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114787
     Region          26..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrihynlgcl llflltsist faqnntitgt vsdtdgmplp gvnvivkgtn ngvqtdfdge
       61 ysikasegdv lvfsfvgmit aeitvqqatt idatleqnta qldevvvtav gierekaslg
      121 satttvnaee itrgaqsnia dalkgkvagv nisaastdpg assgviirgi stmggsnqpl
      181 yvvdgvpinn gsafssslgg gydfgrgsqd inpdniksmt ilkgasatsl ygsraangvi
      241 iittksgqsg klsvelgsts fftrisrtpn yqstygqgwd fthrlnengs wgprfdgtpr
      301 vwgnvvdnsq rlkpylfqed qlenffdtgt ffqnniavsg gnenstvrls ysnlqqdgiy
      361 ptdadsydrn tiglsaqskm gklkisgnln yvntegasva tgqgltvlnn llqipndlni
      421 tefkdynnkf nnisnyytpy gitnpyftln edgsnyeker vygaleasyd ltdwskvtyr
      481 fgldqytdnt qfwtaivdpe pgspnagsst vqpgsysest rmvkqlnhdi lydlnaevne
      541 nlgiqstfgf nynirtsrsl aasvgsqdlf gfyslsnsge npqasssese rrlyglynnt
      601 tfsfkdqlyl tgnirndwys tlpeenrsvl ygginaswlf tktfedisei lnygklragy
      661 gevgvdtdpy qinpvyvags adnqgfgsln fplggvnaye vgnraanpnl kperrkefev
      721 gldleffksr isldftyyna rvenqilslp laattgytsq tanlgeisne gieallklav
      781 frnskgfnwn mafnfatnds rleklderlt qvslgglstt slvalegmpl aliegsvpqt
      841 ndegqivvds ngipiaastk eiygdtqydy tlgftnefsy knlslnftfd lregglmysr
      901 taditrfvgn svttmyndrq pfivpnsvqq svaddgsity venttavsra niddyysata
      961 lsrntvidks flklrevvls ysipgkimdk tfldnlslsi igrnlflwtp esnqfidpei
     1021 stfgtdlssq fgefsanpst rslgfsvktr f
//
LOCUS       WP_092578191             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hyunsoonleella jejuensis].
ACCESSION   WP_092578191
VERSION     WP_092578191.1
KEYWORDS    RefSeq.
SOURCE      Hyunsoonleella jejuensis
  ORGANISM  Hyunsoonleella jejuensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Hyunsoonleella jejuensis"
                     /db_xref="taxon:419940"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39563
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigilketq kgekrvslsp niakqliakg ftviveesag eassykdenf tevganiekr
       61 gvvfkeadvl ikinpfdeed lklvdkshvl isqlyhksnp klikaiaakg asafsmdamp
      121 risraqdmdv lssqnnlagy kavilgayem tkifplmmta agtitpskvl iygvgvaglq
      181 aiatakrlga vveatdirse tkeqaeslga kfisvdnqge qseggyatea sedyvrkqke
      241 avnkslfqad lvittanipg rkaptlitke qveqmkngav iidlaaaqgg ncelsklnet
      301 vfvngvkvig ttiapesvst naselyakni ynflvhlted akfnwdleee itdetliike
      361 gtirkn
//
LOCUS       WP_092571186             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aidingimonas halophila].
ACCESSION   WP_092571186
VERSION     WP_092571186.1
KEYWORDS    RefSeq.
SOURCE      Aidingimonas halophila
  ORGANISM  Aidingimonas halophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Aidingimonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Aidingimonas halophila"
                     /db_xref="taxon:574349"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39853
     Region          2..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mmkiliprer rpgeqrvald patakrfard gcqvaiekga gehahfpddh ygdplavver
       61 eegmqdatav lcvrapsvee aealpegcvl vgllaahanl eqveiyrkrn italamelvp
      121 risraqsmda lssqaavagy haalqaaera pvffpmltta agtvrpakvv vigagvaglq
      181 aiatakrlga qveaydirae areqveslga kmidtgvdas geggyarelt eeekatqaea
      241 lsqrlaeaha vistaalpgr papkiitqam vermkpgavi idlaaegggn celtepgdtv
      301 vhqdvsihgp ldipsrlavp asemyarnly nllspfiedg elsldfedav igpmcltrgg
      361 eivndqvrkw medks
//
LOCUS       WP_092579556            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hyunsoonleella
            jejuensis].
ACCESSION   WP_092579556
VERSION     WP_092579556.1
KEYWORDS    RefSeq.
SOURCE      Hyunsoonleella jejuensis
  ORGANISM  Hyunsoonleella jejuensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Hyunsoonleella jejuensis"
                     /db_xref="taxon:419940"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112403
     Region          33..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkinklyrfy glvcltmlcf ctmvtaqsag tevsatvvde qgnplsgvni ygpegarast
       61 dsngifkitl psseaaviek kgyesqlvsl ttlsgditlv ksdflasedd einmgvatrd
      121 rreivgsvss vntkdrltyd ntqfvrdyin gltvgvrgss nirgignalf vidgvfgrdp
      181 nvlnmeeveq itvlkdanav alygsqgqng viiintkrgk rnkkevnvnv rsgirtplal
      241 pnyldaatfm elrneafvnd gldlnivgfs qeqiqntrsg lnpiefpdvn lydfvqpfvn
      301 thnvisefsg gndksqyyvn vgwlynedwv ninedinagt nrfnvrgnid frvndwitss
      361 idgvaiinta kssranllna attfipfdya pllpvsalen dpaletllag atifdgnllg
      421 tslqlggntp apvaqaiagg yqnrvfrvtq fnnainfdls riteglsakt ylsfdffdty
      481 ttsisnefra ytlvdpdtnn girlrdfgqd rrdlsentvs ngfvsrigmy alvnyekala
      541 knhsinttvl gyynsqkrag alqtdrdshl gfqmtydfkk klfvdfsgay ahslklpegn
      601 rggfsptvgl gyiiseepfl kdndfvnylk lkasggiiks drgidgyyly denyssgsnf
      661 swadgvfans rqnisqganp dlgfeeridl nigfesylmn slwleanyfr teldkqlvfl
      721 adqypsyyna frplnnfngn lytgfelgln fnktfndfsi giganvlysq teaskrsetn
      781 efayqnrqgl elssifgfed lgfysesdft vdtdgnfiln sglpqpnlgt nvkpgdirya
      841 dqngdsvvdl ddqvalgqss spwtyginln lnykrfnlfv lgtgqtgalg nkltgfsnyy
      901 spngtdkyse vvlgrwtpqt antatfprlt sgdnqnnfrt ssfwlydnsf feisraqlty
      961 eftdalcdki gvedfslnfq gtnllevaen kdirqlsigg npqsrtytlg irmsf
//
LOCUS       WP_092580712            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hyunsoonleella
            jejuensis].
ACCESSION   WP_092580712
VERSION     WP_092580712.1
KEYWORDS    RefSeq.
SOURCE      Hyunsoonleella jejuensis
  ORGANISM  Hyunsoonleella jejuensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Hyunsoonleella jejuensis"
                     /db_xref="taxon:419940"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118370
     Region          24..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslrtklilv vmllvsitit aqsktisgvv tsaadnipip gvniiivgtt tgtttdfdgn
       61 yqikatkgdv lqfsyvgfts kttivgdgtt invsmaedis qldeivvvay gdqkqrnvts
      121 altkvsakdi qnfsvprved alqgkvaglr iqtvaseagg dpkitlrgpg sitgssspli
      181 vvdgivlgnd adilatidnn niasisvlkd assvaiygsr gangvilvsl kegvvgktsf
      241 syntftgyky anknknfntt iaqertrlng lqsvvdaiss dspnydriig dynnafaele
      301 aqefiaslgd geqnwqdeif iggvirshsl aglggteltk ysaslgyled egialkdnfq
      361 kfnarikvds ksknkkikfg tslrvnyndq drlparftdp lrqyghlplr lnedhldyit
      421 qsdpgdagfq fenigvgsyg fsrafdhvft vdpnnpraia rdpntglplv spltsggltl
      481 sttknvhplv fflersrtkk kldfnasayv dfelakglnf rqtvssvfrh nktneadyff
      541 gqenrdqesy rlerrdelnq yafesiltyk nsfgkhnfnt iagfeytrrd ffrqqseavg
      601 ftddfnnnia iadggttftd ngtdklvsyf grldynynek yllqlsartd gstrfgantr
      661 fgffpaasag wilssedfls ssdvitflkl rasygvsgsn eisnnifdsl yrfeetfsti
      721 gyngatgvkg vtlanqnlgw ekllefnpgi ditfgrnllk ltadyyirts edlilfapia
      781 atygadnwlq nigevknegv elalssrifa nenaswvasg qftlnrnevv slgnneqiis
      841 ridqdtrpte fiarvgqpit sfygwvydre iplewvdnpf nrfnndfadv yvkdlnndgi
      901 iddedrtelg spypdftwgf nsdftlydfd fsfqwqgshg aevrvadldq lyyasesavn
      961 elasfpdrdl tvhrrftddh iqdasfvalr nvtlgytvpe sftsryninr lrfyvtgenl
     1021 lffmakgyeg fnpdaagqts snantpltag yqrgdgpivr tisaginfqf
//
LOCUS       WP_092580858             981 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hyunsoonleella
            jejuensis].
ACCESSION   WP_092580858
VERSION     WP_092580858.1
KEYWORDS    RefSeq.
SOURCE      Hyunsoonleella jejuensis
  ORGANISM  Hyunsoonleella jejuensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Hyunsoonleella jejuensis"
                     /db_xref="taxon:419940"
     Protein         1..981
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107935
     Region          24..980
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktktqkllf flmllpvfmf gqsvvkgtvt eqatsiplpg vnviikgttt gtttdfdgny
       61 qieanngdtl vfsyvgyatq eitysgqssl dvqlaedaaq ldevvvigyg tttrkdatgs
      121 veaitsegft kgnivtpenl ingriagvsv ntsgapgsgs qirirggasi ngsndpliii
      181 dglpidnngv tgsrgvlasi npndidsfsv lkdasataiy gsrasngvii ivtkkgkskf
      241 satydtqyaf gevtntvdvf sadayrqlia sqpingatid esllgdastn wqneifrstv
      301 ssqhnismqg alfkvlparf tfgvvdqega lktskferrn lslalnptff ddhlkvnlna
      361 nfafednrfa dagqigaamr ydptqpvfda sspfggfyqh rngtqiangt nnpvaqllqr
      421 tnlgdanrlf gnlnfdykfh flpelkavin lgydrteakg ldrrdrlqat tdqdilfkge
      481 frentqertn elfdgylnyk kdldnlgldi tagysyqrft nsgkngrnit dplsvddfya
      541 dpdvvligff granfslndk yaltltyrrd gtsrfskenq wgdfpaaafa wtisdedfmk
      601 dsstfsnlkl rlgygitgqq svnerdifln ryrggrpdsq fqfgnqviqs liaseinpdl
      661 kweetttmev gidyglfnnk isgslnffqk nstdllftaa vpdganftns iiqnigelqi
      721 qglefsvntd viktddlkvd fnfnatlldr emkelalgqd vrtggisggt gnniqihreg
      781 eapnsfyvfk qlydtngrpi egayadlngd niindndryv kenpganaif gfqsnvfyrn
      841 fdfafnlran lgnyvynnvq ssraqyelll dnavlgnipt tvldtgfqrt adviisdifi
      901 enasflrmdn itlgytfndi skmlksvriw ggvqnvftit nysgldpevt dndsdltltl
      961 gidnvvyprp rtvlvganik f
//
LOCUS       WP_092581664             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter sp. NFACC18-2].
ACCESSION   WP_092581664
VERSION     WP_092581664.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. NFACC18-2
  ORGANISM  Achromobacter sp. NFACC18-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter sp. NFACC18-2"
                     /db_xref="taxon:1564112"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38599
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkyvggk htvvvergag saaryldday vaagatlgsa
       61 qealgaelvm kvrapspdel phmkpgavvv gmldpfdeeg laqlaaaglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgtggy aramppgwma
      241 rqaalvserc kqadivista lipgrpaptl vseetvaamk pgsvlvdlav erggncplse
      301 kgrivdkhgv tiigltnlpg lvatdasaly arnildflkl iinadgalai qrddeivaac
      361 lmceggnvmr rt
//
LOCUS       WP_092588783             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            mongolense].
ACCESSION   WP_092588783
VERSION     WP_092588783.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium mongolense
  ORGANISM  Rhizobium mongolense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium mongolense"
                     /db_xref="taxon:57676"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55334
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mfigsprerl agearvamtp dsatqlqklg yqcavetgag klagfsdday ravgvtvvds
       61 vdalyasvdv iaqvrppeas diarlsaskt lisffypaqn kelleqvkti ganvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsislg aityafdvrp evaeqiesmg aefvfldfke qqqdgaatgg yaspsspefr
      241 eaqlkkfrei apdidivvst alipgrdapk lwladmvaam kpgsvvvdla aerggncdlt
      301 vadqkivsen gvtvigytdf psrmaaqast lystnirhmm tdltpkkdgv lihnmeddvi
      361 rgatvafqge itypppppki raiaaqkrqe kakeltleer raaeasafks atqqqigllv
      421 vgglltalig ayapsafmgh fivfalacfv gfqviwgvsh slhtplmavt naisgiiiig
      481 allqvtaggw lvtalaavsv aiatinivgg fmvtrrmlnm fqks
//
LOCUS       WP_092586942             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            mongolense].
ACCESSION   WP_092586942
VERSION     WP_092586942.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium mongolense
  ORGANISM  Rhizobium mongolense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rhizobium mongolense"
                     /db_xref="taxon:57676"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39690
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfitke sigsetrvaa saetvkkmrn lgfdivveag agvlsrmpds efeaagarig
       61 sagdaatadv vlkvrrptea eiagyksgav viaimdpygn deaiaamaka glsafamelm
      121 pritraqsmd vlssqanlag yqavieaasv ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemskeyqa
      241 kqaalvaehi akqdivitta lipgrpapkl vsrqmlasmk pgavavdlav erggniegvv
      301 adavvdvedv kvigfanlpg rvaasasaly aknlvtflet mlnketksvl lnlddelika
      361 tmltyagdvv hpafggtkkg iadgq
//
LOCUS       WP_092601425             374 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderiaceae].
ACCESSION   WP_092601425
VERSION     WP_092601425.1
KEYWORDS    RefSeq.
SOURCE      Burkholderiaceae
  ORGANISM  Burkholderiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderiaceae"
                     /db_xref="taxon:119060"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39167
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipletr agetrvaatp etvkkyvaqg hqvtvqagag vrasipdaaf eaagarvgsg
       61 adalgaelvl kvrapddaer aqmkagsvlv gmlnpfdven narmasaavt afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfvtdee reiaqgvggy arpmpadwmr
      241 rqaelvhqra tqadiiitta lipgrrapvl laedtvkqmk pgsvvvdlaa aqggncpltv
      301 adevverhgv vlightnlas mvaadasaly arnvldflkl iidkdgrytl nleddivaac
      361 lmckdgqvvr qqaa
//
LOCUS       WP_092605471             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Raineyella
            antarctica].
ACCESSION   WP_092605471
VERSION     WP_092605471.1
KEYWORDS    RefSeq.
SOURCE      Raineyella antarctica
  ORGANISM  Raineyella antarctica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Raineyella.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Raineyella antarctica"
                     /db_xref="taxon:1577474"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53793
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipress psenrvaatp attpqlvalg yevlvergag aradfpdday vqagarlgta
       61 qeawgadvvl scteptpeel almhpgatlv smlspairpe vaetyatagi salsldavpr
      121 israqsldvl ssmaniagyr avieaaesyg gmfagqvtaa gkmppakvfv agagvaglaa
      181 igiagsmgaq vrafdvrpev geqiesmgaq fvevgavden vssdgyakem tadqaelaar
      241 myadesanad ivittaqirg rrapvlltae mvaamkpgsv vvdmaagsgg nteltrpdek
      301 vvtdngvtii gwtdlagrlp rqasqlfgtn lvnllklvtp akdgrfvidf edevvrsmtv
      361 trkgavtwpp ppvkvsaapa vpaaapvepv rpaeapevva krrrtqrlyl galamvaffv
      421 igglspitil ghwmvlmlav fvgfyvinnv thalhtplma etnaisgiim vgallqmgss
      481 swavtiiswi avlvasinvf ggflvtnrml amfrka
//
LOCUS       WP_092607962             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces ruminicola].
ACCESSION   WP_092607962
VERSION     WP_092607962.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces ruminicola
  ORGANISM  Actinomyces ruminicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Actinomyces ruminicola"
                     /db_xref="taxon:332524"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53329
     Region          1..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgipcqpp drslaaatpq tverlirlgy dvvvqrgaga pahfpdtaye eagaqladra
       61 evwacnivvt ayapddaeld lmhpgatlig rldparhpdf vqklqdhslt alaidtvpri
      121 sraqsmdvls sqanlagyra vieaaghfgr llngqvtaag kfppasvyvi gagvaglaai
      181 gtayslgaiv rgtdvrpeva dqvksvgaef vpvptaqevs adgyakemst dqaalanaly
      241 aeqaaaadiv vttanipgrr apllldraav eamrpgsviv dmaaanggnt eltvpgevvt
      301 tpggvtivgy tdlaerlpaq asqlygrnil nlltlltpdk dgelaldled qvvraitvcq
      361 agellwpppp vsvsaapkap taaappqsas daaadaeaqa aaqarsrrrk tigialaata
      421 aaalvlvtpa aatshyivla laiilgfhvi snvtpalhtp lmsvtnaisg iillgaisqv
      481 gnanpaisgv afiaimlasi nvfggfavth rmlamfrke
//
LOCUS       WP_092619075             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter marinus].
ACCESSION   WP_092619075
VERSION     WP_092619075.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter marinus
  ORGANISM  Acinetobacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter marinus"
                     /db_xref="taxon:281375"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39658
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipteti adeyrvaatp etvkkltsag hqvviqrgag ikaayvdsay eqagatmtdn
       61 ayqgsqlilk irapqgdeia qiesgasvva sfdpyrnpel drfatqnisa falellprtl
      121 sraqnmdvls sqanlagyks vllaaneyqs lfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak eqveslggkw ldvpmspeeq aradeaakng ygwtpgeqyi
      241 qdqaaivdka vanadivvtt allpgrnapr lihgatvakm kpgsvildma vetggnvegs
      301 vvgetvmten gvkilgipni pstvateasa lyarnifnfi dtlfdenknv kinledeiqk
      361 allvthggev llkrg
//
LOCUS       WP_092621109             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseospirillum parvum].
ACCESSION   WP_092621109
VERSION     WP_092621109.1
KEYWORDS    RefSeq.
SOURCE      Roseospirillum parvum
  ORGANISM  Roseospirillum parvum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Roseospirillum.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Roseospirillum parvum"
                     /db_xref="taxon:83401"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40200
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipkerr pnetrvaasp dtvkkyvgfg fdvavekgag agssftdeaf kqvgatiaad
       61 akatlkdadi vlkvarpmmk degtdevall pkgatlvcql aalqnkplae alakagvdaf
      121 amelmprisr aqsmdilssq snlsgykavv daaaaftkcf pmmmtaagtv aparvlvfga
      181 gvaglqaiat akrmgavvya tdvrpatreq veslggkfvv vdeeaekqae taggyakdlg
      241 deyrkkqaev mseqiakadi iittalipgk papklvtaeq vksmktgsvi vdlagetggn
      301 celteygktv tkhdvtiisp anmpatvard astlfaknll nfltpfvdke agkvafdwed
      361 dlvkgtliar dgkvvhsalt gsggn
//
LOCUS       WP_092642111             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Jannaschia
            faecimaris].
ACCESSION   WP_092642111
VERSION     WP_092642111.1
KEYWORDS    RefSeq.
SOURCE      Jannaschia faecimaris
  ORGANISM  Jannaschia faecimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Jannaschia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Jannaschia faecimaris"
                     /db_xref="taxon:1244108"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55578
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkevl egearvaitp esaghlqklg hdvfieagag maagftdeay kaagvevvks
       61 aaslfkmvdv vakvrpptdt eakrltkgqt lisffypasn ealmdlvksk gataiamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvflefed selpdgaatg gyappsspef
      241 qakqlekfre lapdidivic talipnrpap vlwtkdmvea mkpgsvivdl aaerggncel
      301 tvpeekivtd ngvtivgytd fpsrmatqss tlygnnirhm madltpekdg vvnhnmdddv
      361 irgstitheg eitwpppppk vaaiaakpke kvkeltreek raneiaafka qtkqqvglla
      421 vgggllllvg lfapasfmqh fivfvlsifv gfqviwnvsh slhtplmavt naissiiilg
      481 alvqigsgsf lviilaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_092648055             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Schaalia
            radingae].
ACCESSION   WP_092648055
VERSION     WP_092648055.1
KEYWORDS    RefSeq.
SOURCE      Schaalia radingae
  ORGANISM  Schaalia radingae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Schaalia radingae"
                     /db_xref="taxon:131110"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53670
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mlvgvpasna dqplvaatpd tvtklkklgf dvcvqrgagq taqfpdslfe dagatlvddr
       61 gawgadivlt ldaptseqia amqsgatlis rlaparhpel ldelaranit alamdtvpri
      121 sraqamdvls sqanvagyra vveaahqfgr lftgqvtaag kmppariyvi gagvaglaai
      181 atansmgaev yatdvrpevg eqvesmgatf vpipvgrqes sdgyakemda dqaraaeily
      241 aeqaacsdiv ittanipgra aprllsadai damrpgsviv dmaaanggnc eltspgeivr
      301 teggvtiigl tdlagrlpaq ssqlygqniv nllrlatpdk dgqltldmdd eiirsitvth
      361 egdvmwpppp vnvsaapapa ptpredpaav aaraadesrk eashkrnrvi givvaialaa
      421 lliltsplmv sshyivlala vvvgfyvitn vthslhtplm svtnaisgii lvgallqigs
      481 snvlvtiisf aailvasini fggftvthrm lamfkkd
//
LOCUS       WP_092669627            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            arizonensis].
ACCESSION   WP_092669627
VERSION     WP_092669627.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter arizonensis
  ORGANISM  Hymenobacter arizonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Hymenobacter arizonensis"
                     /db_xref="taxon:1227077"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109133
     Region          31..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhpylakll flllfaglgf psgayaqtgs vsgrvtdskn egipgatvli egtslgsssn
       61 vdgtysiqnv pagaqtlvis fvgyntvrrp vtvvagqnte tsaalvenat qlseavvvgy
      121 gtqrrqdvtg avatvdsref vqgqvttpeq liqgkvagvs ittgggapga anvirirgns
      181 slnansdply vidgvpvdkt tisgasnpls linpndietf tvlkdasata iygnrasgwv
      241 ilittkrglq geklrvelns qtgvstvarr yetlstdefr rqinqfgsps qiaslgtant
      301 nwqneifrta atfdntvsli gsvakvpfrv sygnlyqegi vitnqlkrnt gsvsltptll
      361 ndrlridina kgsvidnrfv dygtvagaal ydptqpvrsn earftrfggy sqflnpttga
      421 plgnapanpv aalnnsnnts nvkrlignvq fdykvhgveg lranlnlgld asrgrgnnvi
      481 spndfgnyev spdpglsgrf tqyaqdrdmk lleaylaygk qfggtkfdvq aghayqsfin
      541 qgpnfldyrs nrdtlvtrge tlslpgfydk nvlisffgra tmnvqdkylv tatvrndqts
      601 rfrkgfrsgv fpalglawrv kneeflkdnn tlselklrag ygrtgqqdig gaydtqpryv
      661 vgsstsqypf gngntipgit yspqgynsvl twettntyna gvdlgfldnr ltatldvyqr
      721 tasdllaevd qsagsnltnr lnanigslrn rgvelglnyg vfrsenltwd vnlngaynvn
      781 kitdlgsqqe gfpgynvgsi pggtgnfiqi navgqpvgtf yvrrqvygpd grpvqglyvn
      841 sernaanadv gdyyykqpap lvtlgfssnv vyekftfaft lrgnvgnyvy nanaaglgnf
      901 anaqgstnfv snlnpdvlnt gftrqqlfsd yyvqnasflr cenislgynv gkvlgastlr
      961 vtgnvqnafv ltkykgvdpe iasvdalsgq atfgidnsfy prartytlgl algf
//
LOCUS       WP_092673978             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Agromyces
            flavus].
ACCESSION   WP_092673978
VERSION     WP_092673978.1
KEYWORDS    RefSeq.
SOURCE      Agromyces flavus
  ORGANISM  Agromyces flavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Agromyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Agromyces flavus"
                     /db_xref="taxon:589382"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53054
     Region          3..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigvvteq gsetrvaatp atvkqliglg yevvveagag aqssfpdday aavgagivsr
       61 eaafasptvl kvnaptpeem allqpgttvv sllspalrpd llealaargv talaldavpr
      121 israqsmdvl ssmanisgyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksigge ylkvevaveq stdgyakats eaydrraaei
      241 yseqardvdi vittalipgr paprlitaad vasmkpgsvi vdmaagqggn vegsvageri
      301 vtpngviilg ytdlasrlpa qasqlygtnl vnlvklltpg kdgqltidfd divqrsvtvv
      361 rdgqvtwppp pvqvsaaptp akvatdgaga tsaapkrtrt ltrggriali aagiaalfvv
      421 nsiapdplpq hftvlalsiv igfyvigkva halhtplmsv tnaisgiiiv gaivqvtsdv
      481 pavqvlsaia illasinifg gfavtrrmlg mfakgdrtss
//
LOCUS       WP_092677201            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            arizonensis].
ACCESSION   WP_092677201
VERSION     WP_092677201.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter arizonensis
  ORGANISM  Hymenobacter arizonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Hymenobacter arizonensis"
                     /db_xref="taxon:1227077"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112063
     Region          26..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkkywllfl llgvllappg waqtartvtg vvtsatdqsp lpgvtvlvkg tttgsttgad
       61 gryslqaapg gvlvfsfigy spqertigad gnidvalres ttgldevvvt ayniaqdkrt
      121 lvtavqevks kdiidsrqtn ivnalqgkia gvnitssgga pgegasivir ggtsldgnnq
      181 plfvidgmim dnssfsesaa pgagsqfngl lgrsvgasnr agdlnpedie sitvlkgpaa
      241 aalyglraag gavvittkkg vagrttlnfr tqvsvdevnr lpklqdqygq gsnglfdgtt
      301 rvsfgprflp gqtvydnlen fyrkgytyqn flnmsggsdk atffvsasnl qqsgvtpqsk
      361 ydkttvrmsg taeispklnv sgsaqylttg gerpiqgpgl fgssggylls llnwprgdda
      421 rnylnpdgtr rrllalgngt dadadnpyft vernpqtdrt nrfigntqls fkafkfltls
      481 hnigadvyts rntsvravgt sqvgnqnggi aetveqfrll tattlanfsh nfndnfggsl
      541 ilgnsieenk sqavdyigli fqnpgfvgln ntvnrsalqr dntrrlignf aqlnatmfnq
      601 vflqmqaryd qsstlprpde nkiygkgfly gsvglgyeft ktlgleqnni lnygkirgsi
      661 aevgkdtqpy riqaalaqnt yigggfrndf fgsnpnlkpe rtrtyeagvn lqflknrlgl
      721 dfnyyysrts eqiiaprvsq aagfilqyin ggvvtnegqe ialtgtpvkt kdftwdvian
      781 ffhntnrvee lpfpltvvfq sdafitdvhq ggafigrsit gvgaydfnrv tdvnseffgq
      841 vligaggyps anplftyagn raprfttqft ntftykglsl tslldfrvgg vvingndwyq
      901 trvgtsqrta dryktvvfdg vvrnpdgsyt rnsrpveltq nyyatilggv gtpfiedgsw
      961 arlryvtlsy avpasllsst kfikgaelsv tgrnlllvtk ysgadpetaa agagvrgggs
     1021 ngfdfgnvpa trgvdmalrv nf
//
LOCUS       WP_092677550            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            arizonensis].
ACCESSION   WP_092677550
VERSION     WP_092677550.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter arizonensis
  ORGANISM  Hymenobacter arizonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Hymenobacter arizonensis"
                     /db_xref="taxon:1227077"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114955
     Region          24..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksiflvfa limallqqaq aqdrtisgkv tdrstnqgip gatvlakgtt vgtgtdadgs
       61 fslsvpstat tlifsfvgya sqeqaigasn tinvtlvtdt kqlnevvvta lgvernrnsl
      121 aysatqvdgs ditvarnpnp inglsgkvag laitqsntlg gssnvlirgt kslfgnnqal
      181 fvidgvpisn qntnsagqqq gqsgydfgna aadlnpddia sttvlkgaaa talygerasn
      241 gvilittkkg rrglnvtint gvtagridks tfikyqkeyg ggylqafrta sdgsrvvrtg
      301 ddasygprfd pnlqikqwda ftpgsptfgq arpwvaaand pstffetavs tlnsfsvdgg
      361 netatfklgy indiqrgvlp nskitkdvvn fagslnltpk lttsasvnvs ringlgrygt
      421 gyssenlvsg frqwwptnvd ikeqeaafhr nrtnatwnft npvtnnlsai ywnnpyftrf
      481 anyendsrfr tfgnvsatyk vsewfnilgr atldtydeqq eersavgstt asylpyysry
      541 nntyreanyd lignfkfqls dafsfaglig tninrirses ifantngglv vpglyslsnt
      601 vdpltppter lsrigrdgif asttfgfrdr vyldltvrrd ksttlptann syvypsaalg
      661 yvfsedlket tpwlsygkvr vnyaqvgaga aplsvldtys kptafgsvpl falntiknnp
      721 elkpektrsa eagveaafld srvgfdftiy qqntidqiip vnissatgfa qryvnsgevr
      781 nrgveiaafv vpvksenfnw rvnanwtrnr nvvlslfddv etirlasyqg gissnatvgq
      841 afgalrgsdy iylngqrvvd qetgiyattd gnaiigdpnp nwrggitnsv syknvsltfl
      901 vdvrkggsvf sldryyglss glqpetatln dlgnqsrlpi aqgggiilpg vaadgspntv
      961 rienngeiap ygyggnpnag fvydasfvkl revnlsyslp taftsrigfv kgidlsiigr
     1021 nlwiihknlp dadpeeglss gnlgqgyqsg sypttrtlga nirfnf
//
LOCUS       WP_092677207            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            arizonensis].
ACCESSION   WP_092677207
VERSION     WP_092677207.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter arizonensis
  ORGANISM  Hymenobacter arizonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Hymenobacter arizonensis"
                     /db_xref="taxon:1227077"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109768
     Region          38..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mshtyslsgl rhhvvgllvl lfllasgpas aqntryslqg rvtdangqpl pgttvrllnt
       61 vlgttsgadg rfsleaalsp gayqleissv gykpvrrpvt lgaettvavg daalsedrvg
      121 lnevvvtgts vatskrqlgn tiatvsgdel rttvptqidq alqgkfagvq itqnsgnpag
      181 gisvrlrgps tvagssdply iidgvlvnnd spqlldlggy aqnrlvdisp ndidrievik
      241 gaaaaaiygs rasngvvqif tkrgrdgapq vtvssqflvs qlrkkldyne ypfrfntlgg
      301 tlaanadrsq tavtrydlqe difrtavgtd dyisvsggan gtkyfasgny frnqgivggt
      361 dfargggrvr leqtignkar vsvganytls rsnerpnggi neaygvltgf ifsnnyinpa
      421 pdpitgryps taanivrtnp leainrfdfq qrtsrfigda qlnftpftgf sidyvlgyda
      481 stqvatgfip rgstaptfgt glarradatt flvnndltas ykrdlsenfi stttvggtlq
      541 ylqnvntgiq sidlspgpvt tvsgtlgrsg efrgertivg afaqqtfglf nrffltgalr
      601 vdaaslygak qrtqlyrkls gsyvlsdeaf whdgplariv pqfklrasyg eagnltainp
      661 yqnvtnydpl vlgslpglap atlqgnrnlg perqreieag idasffgdrv gvefsvydkr
      721 vtdlilqrdl alssgfssrf dnignmrnrg vevllrvapv rttavtwnvt gtfthntnai
      781 tnipgglvtf pngfglvaav egrplgtyyg tysarrpdgs llltpdglpq rergiqgtfg
      841 rpntpqrgad gqpsgtllnd vlgdpnpryi aslinevsvl nnrltlrlqf dtqqdvsvfn
      901 ftqrvgsret fgglkiyeae lrgevpkgts vneyttfdkw vqdgsfvklr easlsyqlkp
      961 kflglrdlrf slagrnllvf tkyngydpev naagqsnavr gfdfvevpip rsasvgftan
     1021 f
//
LOCUS       WP_092677554            1125 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            arizonensis].
ACCESSION   WP_092677554
VERSION     WP_092677554.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter arizonensis
  ORGANISM  Hymenobacter arizonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Hymenobacter arizonensis"
                     /db_xref="taxon:1227077"
     Protein         1..1125
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119785
     Region          24..1124
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslfmvfa lfvallqqaq aqdrtisgkv tdrstnqglp gvtvlakgtt vgtstnadgg
       61 fslsvpsgat tlvfsfvgya tqeqqigssn tiditlatda kqlsevvvta lgltanrdel
      121 gtaqatvqgq alvrsgetnv italsgktpg vlitrtsgdp gasaniqirg astitgnlqp
      181 livvdgipvf nssvgdegil vsnggagsnq vagvvqqsrl gdinpddias mevlkgaaas
      241 avwgtraang vivittkkgr nnsagrlnls yrtsygidqi nrvpglqrsf gqginglfnt
      301 ttgnswgdki adrtggpdte itdpsapgyn gfitfadgtr ryalangtaa nphggknsrd
      361 tydqartpft tgstwdniat lsggddrgnf yvslgntyqr giarfnsdyd rttarvnvdr
      421 qlsdklrasv ntsyirtrsn raqqgsntsg iylgglrtsp dfdnsrfvgd ytdrngnvfl
      481 drqvgyrnki gavsadgitr tvydnplwtl drvqntsrvn rflgalelty ditpwlniln
      541 rtgvdtyadn rrayfpvgaa aaiqgsltee viqetqvnnd lilranrsls enititglig
      601 ynlngrrssq vgatatqfin pfsppqlsnt passrspfnl vveqrtaaly gqvdlglfnq
      661 lflsgtvrge qastfgnean stfiypaasa awqftklgal aenrilsfgk arasfgtvgv
      721 qptpyltrty ytgassaiig dgwgtaidaa nygggfvrst tqgnatlkpe rkteieggld
      781 lrffsdrvgl tvtgyanktv dailsvpvaa stgfqstngn vasiqnrgfe lsldgdvikt
      841 ggftwnvatn fslnrnkvle lagaesiflt gftgtssrav qgqqlgalwg tefgrnesgg
      901 yildangfpv ladggtervi gdpnpkwrgg lnntfsfkgl slnvlvdhvn sfdvwngtkg
      961 alyffgtsde leqettvsad vaanllryng ttvasayplv ngnytfrgtv gnfggnnval
     1021 deqwyraglg ngfsggpakp fienvsytrl revslnysit qdwlrnatkl aaidvsvtgr
     1081 nlylwtnytg vdpetnltgv sngrgldyfn npstrsvifs ikfty
//
LOCUS       WP_092678636            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            arizonensis].
ACCESSION   WP_092678636
VERSION     WP_092678636.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter arizonensis
  ORGANISM  Hymenobacter arizonensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Hymenobacter arizonensis"
                     /db_xref="taxon:1227077"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118131
     Region          59..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqtrypqrg agwrralagl gltalspava haaslpappi trvavgaayp pgaakadpkp
       61 vkgrvvdakg eglpgvsvrv kdattgtitn adgsyelavp pgsvlifsfv gylphevavg
      121 enstynvalr eeitgldevv vtalgikree kalgysvttl ateqlteaks nnwtdalsgk
      181 vaglnlvrsg ggpagsnkii lrgesslagd ndalivvdgv vlggshrpql sgngstaylq
      241 sespvdfgtg lsdinpedie svtvlkgpga talygsrgsn gavvittksg karkkgigvt
      301 fnsnaavdmi srwpdyqyey gqgaagenyy sygatadgps trssssawgp kfngqtfyqy
      361 dpatnaagte rtpwvpyenn rqdffqtgkt ftntisldgg tdrtavrlsl tnlqnswiip
      421 ntgyqrnsva lsasqkitdq lqvstkvnft nrasdnlpst gynnqslmyw lmfqlpnadl
      481 nwvkdywlpg svgitqrypf sslvdnpyli tyemlnksnr nsltgnvqvn ykfskdwnlm
      541 lrsaldysye arsqqrpkdt ekykegmfrt qnifsqemnh dfllqyahqf grfetsvsgg
      601 gsalrnrynr delraerlly pqvftfansr dlpialpyra efavnsfygl aslgyhkfly
      661 ldltarqdwt stlatansta ntgffypsas lstvlsqvlp lpeivsfakl rgswaqvgsg
      721 tttpyltayt yavapgfpsg lsnpgaians glkprrtesv elgadlrfla nrigldvavy
      781 rnntydqilq vpvdrasgyn qavlnaglvr ndgleiqana qvisnpqgfg wkvfgtytan
      841 rnqvvalads vftyqlqrgp ggrgtvearp ggsmgaiygr gyerapdgqi lyqngypvlg
      901 dqikylgnal pqwrasagte fsyrhlrlnv lfdaqygaka ysmtnavlae qgkstltlpg
      961 ryngiigdgv trnadgsfrp ndvvaenlpn yyvahygrdn veanlfrtdf iklremrldy
     1021 alpapllskl kltqasigvy grdlfiftkw pafdpefgtl ndgtidlgfe lgqfpstrtv
     1081 glnltvgi
//
LOCUS       WP_092681499             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Albimonas
            donghaensis].
ACCESSION   WP_092681499
VERSION     WP_092681499.1
KEYWORDS    RefSeq.
SOURCE      Albimonas donghaensis
  ORGANISM  Albimonas donghaensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Albimonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Albimonas donghaensis"
                     /db_xref="taxon:356660"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55288
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif agekrvaltp esakrlqklg yeclveagag eaasltdeay rdagvtvvgs
       61 aaelwdqadi ivkvrgpees eveaapegkl lisfiwpaqn pelldklnak kltviamdmv
      121 prisraqkmd alssmanigg yravveaann fgrfftgqit aagkvppakv mvigagvagl
      181 aaigaaqalg avvrafdvrp evaeqiesmg aeflfldfed sqdgagtggy aapsspefre
      241 kqlelfraqa pevdivitta lipgrpapkl wledmvammk pgsvvvdlaa erggncdltv
      301 pdekivseng vtvigytdfp srmatqssnl ygtniahmlf dltpekdgqp nvdmeddvir
      361 gatvvhggei tfpppppkvk aiaaaapkek vkeptaeekr aaetaafkkq tksqvtllav
      421 gaalllgvgl vapasfmqhf ivfvlsvfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgswl villsalsif maginifggf lvtrrmlamf qks
//
LOCUS       WP_092690134             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter kyonggiensis].
ACCESSION   WP_092690134
VERSION     WP_092690134.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter kyonggiensis
  ORGANISM  Acinetobacter kyonggiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter kyonggiensis"
                     /db_xref="taxon:595670"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39797
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv lgenrvaatp etvkklisag htvvierrag vkaayidsay eqvgakitdd
       61 aytgsqivlk vrapkgdeiq klaantavia mfdpyrntel dqfasaqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptar dqveslggkw ldvpmsddek qkaadaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr liraetvakm kpgsiildma vesggnvegs
      301 kcgenvvtdn gvtilgipni patvateasa lyarnvfnfl etlfdadknf vlnqeeeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_092687918             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tranquillimonas rosea].
ACCESSION   WP_092687918
VERSION     WP_092687918.1
KEYWORDS    RefSeq.
SOURCE      Tranquillimonas rosea
  ORGANISM  Tranquillimonas rosea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Tranquillimonas.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Tranquillimonas rosea"
                     /db_xref="taxon:641238"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55996
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtptevm sgearvamtp esakalqklg hecavqsgag mragftdaay reagvevvdd
       61 aaalyagcdv vakvrpptde evgmlrrdql lisffypasn eallerakeq gasliamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvyldfde etkdgsesgg yaapsspefq
      241 ekqlekfrel apdvdivitt alipnreapk lwtkdmveam kpgsviidla aerggncelt
      301 rkdekfvten gvtivgytdy pskmatqssa lyatnvrhmm tdltpekdgq vvhdmeddvi
      361 rgatvthhge itypppppkt kaigaapkte kpkeltpeek raqelaafrs qtkrqvtllg
      421 vgavamllvg lvapasflqh fivfvlavfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsf lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_092700920             533 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Acidovorax].
ACCESSION   WP_092700920
VERSION     WP_092700920.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax
  ORGANISM  Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Acidovorax"
                     /db_xref="taxon:12916"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55547
     Region          12..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqanpippvq cigipretfp gekrvatvpd vvekllklgf rvavesgagd aanfsddayr
       61 aagaqiagda aalwaasdiv fkvrppssde valmregttl idfiwpaqnp elmqqlaark
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rkmyaeqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg qavvrhgvti vgytdlasrl akqsstlyat nllrlteelc kakdgvavvn
      361 meddairglt vvkdgaitwp applkqapap apkpaaapva vkksshgpge pmsaktltiv
      421 favlallfwa igayapvafl ghftvfvlac figymvvwnv tpalhtplms vtnaissiia
      481 igalvqiapp dagingrpdg lilwlafaal vltavnmfgg favtrrmlam frk
//
LOCUS       WP_092712510             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            multihospitium].
ACCESSION   WP_092712510
VERSION     WP_092712510.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium multihospitium
  ORGANISM  Rhizobium multihospitium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium multihospitium"
                     /db_xref="taxon:410764"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40535
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msnlvfvake svaeetrvaa svetlkkmkn lgfdvvieag agtssripdt eyeavgarig
       61 sikdakaadv vlkvrrptsk eisgyksgai viaimdpygn eaalaemara gltsfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg alvsatdvrp aakeqvaslg akfvavedee fkaaetaggy akemsreyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vgrdmlkamr pgavavdlav erggniegae
      301 ygkiadvegv rvigypnmag ripasasaly aknlvtflet mvdkdtkslg lnrtdelika
      361 tmltdggevv npnfvdpdqp tikkgdl
//
LOCUS       WP_092712004             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Janthinobacterium].
ACCESSION   WP_092712004
VERSION     WP_092712004.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38729
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qvvvqsgagl qasipddaya aagaqigsaq
       61 eaygcaivlk vrapdaeera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvvkhgvy ivgepnlatl vaadasalya rnvldflkli idkedqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_092720860             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Acinetobacter].
ACCESSION   WP_092720860
VERSION     WP_092720860.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39950
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv igesrvavtp etvkklistg htvvierrag vkaayidsay eqagakitdd
       61 aytgsqiilk vrapqgeeik kiaantavia mfdpyrntel dqfassqisa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgaiv eatdlrptar dqveslggkw ldvpmsdeek qkaadaakng ygwmpgeqyi
      241 kdqativdka vsnadivitt allpgrdapr likaetvakm kpgsiildma vesggnvegs
      301 kcgenvftdn gvtilgipni patvateasa lyarnvfnfl etlfdqdknf sinpeeeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_092721375            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092721375
VERSION     WP_092721375.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119381
     Region          32..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhqliryfk alllslttlv mcahlsaqsv svkgkvtdaa tkrpvegvsv tvkhtnigtt
       61 tnangefelh vapansqlli nyvgyaqkqv natsqfldil idpsskqlde vvvtalgvkk
      121 etkklgyavq evkgadlvka repnpvnglv gkvagldvai sremlaapav slrgynisly
      181 vvdgipitsd twnlspddie sytvlkglaa taiygsraqd gailittkka kkndkgytie
      241 fnsstqldkg fiavpktqal ygggdysqya fgdgkgggin dgdydvwgpk fegqlvpqyd
      301 spidpvtgvr kgtpyiargv dnlkkfiqag llttnnlsfs sandrsnirm slshtyqqgi
      361 vpntklntvn fnintgynls dklkiegsln ynrqfspnfp dvvygpnsvi ynltiwtgad
      421 ydvnqlrnyw qpgkegvqsi faeyqryhnp wfmsyewlrg hyktdvygta altykpnshi
      481 eailrtnvst fdimrneklp ysahpygrel nrgdysedrr smfdnnvegl vkytgkirgg
      541 ftidglggvn arnfsynssf vktdylnvpg lysfantlnp lkaynfnskm lvlsayysls
      601 vdykkylsvt ttgrvdknst lrlnnntyfy psvsvasvis dyidlprvis flkirgsyat
      661 akapstspyl gpagyplgyg tpyttvyggp syslsdpayg igtvynnqtg ayapgnkvdp
      721 nikssvstsa eygldikflk nrlglsatyy dnikgpgivt salsetsglt giitnaikte
      781 ikgaelsltg spiqnrkgls wdvllnwstf retykelpan lsnyqfqqgd rvdklyasvt
      841 aktpdgqvin dasgypvylp kaqyvgngdv dwswavynkf tyktfslafq fdgkvggkvq
      901 drvlrkgieg gsnietvqga vgaareyefh hytdpgfkgt yvgegvqiis gtpkydpvtg
      961 vitnykdlqf apnksvvnyi qdyvssyfnd fehtsvakty aklrevvlty slpqrflgkk
     1021 sfitkidvsl vgrnllyffp srfkdmdvdq ysgrniysgn srepnlqtpt trsygfnlni
     1081 vf
//
LOCUS       WP_092721611            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092721611
VERSION     WP_092721611.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114248
     Region          22..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknllfliv mlfalqyana qkqltgtvra artneplaga nitfqgtagg tatnaegkfs
       61 itvpnkvkfi lvsyigyesq tvavegkqqi diiltaagka ledvvivgyt aqrkqdltgs
      121 vavvdmapvk nntsgnamqa lqgrvaglyi eksgspngst srilirgant lgnndplyii
      181 dgipttrpev fqnldpania svqvlkdasa esiygsrasn gviivttrng gntngkvdfq
      241 fnsstalqse kpfrlkmlns ldrgkalwqa svndkqdpta gygqiynfdw nkdynnpiln
      301 svslqpfvgg dpntpvgntd wqsvmyktgi vtsnsltasv gnknssvein lnqlsnsgml
      361 rftgynrigg sinaitrafn dkvtfgvnlr mansnerlta rdlggalttf lavtlaptip
      421 vyqkdgttya gelgagysdr nnplhmqdla kwnnanrlst fgnvfveiqp vknlffksnf
      481 gadnatylsk vitptfsega lnrttnslsf dqnhflsttf sntlrynwdl sanhhfkflv
      541 gteyikttld fqttkkekfa iqtqeyftln agtgnttvsg gstgnqlfsq fgridysfsn
      601 kylaaltvrr dgssrfgsdn qygifpaasl gwridkesfm knnrlfselk arvgigrvgn
      661 qqigdlarfg lfdtrygtvl sqlvggfweq ymnigtaysl sgastgtlps gfvqtqaanp
      721 glkwettdei nvgidfsils nkifgsfdyf trnttgiliv ppvasalgeg qskavngask
      781 snkgwelvlg yhgpqtgdfk ynvtlnfshf rdkitdlpek vrpaypgnll ntiighsqfd
      841 ifgfktaglf qsqaevdaap kqigaapgri ryvdvthkgq idddartwig ttlpsleyga
      901 ridmsykkfd lsvfgsgvsg ragfdvytlf nnlmksrenv gpgvfdgwtp thtntsipal
      961 tlkdnnnegr tsdyfivnts yfkirtvqlg ynivpksvfs rlrfylmaen lltikskkyq
     1021 spdperisld pipiprtfsf ginasf
//
LOCUS       WP_092722058            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092722058
VERSION     WP_092722058.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121179
     Region          52..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpkqlrsvlt rwldfsyrkl nlllicfalt saqlsanaad shlhylpvqi gtlngkvtds
       61 knqplegvsv tvrgtkkgvt tnaqgafvlk nvdehailvf sytgfvnkei plrgnagnlv
      121 vmmeeqslql ndvvvigygt qtkkdltgav aqvkatqlen enprsvqdll rgnapgldvg
      181 fdastkgsna sltvrgrgsl taqsppvivl dgvifgggme dinpndiati dilkdassaa
      241 vygarsangv ilittkrgss kshkptitfn dniginvleq kphlldgnem infrqdyeaa
      301 akywflpgla ptvggvkfdt astpgiqyyy kdprtnpggl staqwmglrp gsagdpvvew
      361 lnrnefkpie isnimagkml nwenliynkn alqhdhtvsm sgrkedfnyy lsmgylsnqg
      421 ltvgdqykvf rtrvnlegqa tkfltvglnl qysnrdessv pvsmsdvqqt tpwgsyyadd
      481 gvtlrlspnd dpgnnthpfm eqtytdrmkk fdnffgsvya kgklpwgfsy qvnftprlen
      541 yryfnfrspl nptiaarngv airqsqtiyq wqldnvikwy hqfgkhtfda tflinaekfq
      601 swgdstnaen fspnsnlsyh nlggaailnt ftkdeyatgd almgrlayny dqryfltgtv
      661 rrdgysafgq qnpratfysf gaswalsqer fmrrfdkwld yaklrasyge ngnreigrya
      721 siaqlnasky vyitpsgtvy dvatlstgnm ansnlkwern asvnlgidys ilrgrisgsf
      781 dyyqrntkdl lvsrslpsvt gfsnvisnlg evqntgfems vsslnldrrn ftwrstfsfw
      841 lnrnkivhly gpvpvvdasg kttyvekddl knnwyigkdi ntiydyrilg vwqvadasna
      901 asygykpgdf rlqdtngdgk ytiddkqfig sttpdfswnl rnefrvfrnf dvsltlysri
      961 gqlsqlneak nvdkfynrsn fylrpywtpa npindyaain snaagavswn vyrkssfiri
     1021 snvsvayslp selahrykme avkmyvnvvn pyvysswnyf dpenkgitpi tfnfglnvtl
//
LOCUS       WP_092722299            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092722299
VERSION     WP_092722299.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109634
     Region          28..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnftklakpm lmgllaclcs flvqaqtkti tgkvtdrkdg splsavsvtv kgaktgtqtd
       61 atgafrinvp asartlviss vgyanqevsi enktsiqvsl gsvseqlsdv vvigygtrkv
      121 kdatgsvaal takdfnkgai atpdellqgr tpgvivtpas gepgaaatin irgsasirgn
      181 qeplyvvdgv pispggttgn ntslgssspr nplafinpsd iesisvlkda ssaaiygsrg
      241 angviiittk sgkgtggfqa svstgvatpa srynllnaqd fllavkkani dagtnpadaa
      301 aavqlvdkgy stnwqdqiyr tginqnynls wgfshkstal rlsgsyddiq giikssgmkr
      361 stvranltqk flndrlrfdi natysrvknq ypplsnnagy qgsllgaait fnptypiynp
      421 dgtffdpkdg nrnpaemlsy fndndknnrf ltnvsgsyel ikglvykatf gydkstserf
      481 sfadprlssn afggtnnvfg kdlgnqiegn grgtkqnldl ksvlvehtlt ydksfgnqvl
      541 navvgysyqs teatyagqvg wglatpvvka tdvfalnysq fknfynfvpd ytkyelqsyf
      601 grinytiadk ylltatmrad gsskfgtnnk ygyfpafaak wkllkegfaa nslgkifsef
      661 siranygklg sqdgigayda vnlqqtyvgn sgqpetqflh qgnpdlkweq stttgvgldf
      721 atldnrltgt idyyytkrkd llfytptpgg fsaqafwwvn lpgyvtnegv elglnysaiq
      781 grkftwnigy nmsliknrvq dfnvtvntga vngqglsgay aqtfangypl ftwkmptfqg
      841 fdgngnarya aggkdqlqgs alptflaglt nsftwgrwna siffnavrgf yeynntanal
      901 flkgsiktah nvnytvansp enpinpgsvs trflekgdfv rlsnasigys fnmkkskvik
      961 tltvtasgqn lalitqysgl dpevnidhqi sgvpsrgfdy tgypkprtvt lginvgf
//
LOCUS       WP_092723529            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092723529
VERSION     WP_092723529.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118021
     Region          23..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkmsslfvl llcicnmasa qtrpvtgtvt dkkgqaipfa siivkgtrtg vtadaegrfi
       61 ikakagdvle iesqgqikke isvtsdnsvt vvmdrneket laevvvttaf eikksarttp
      121 ysaqtissdn lnlirqpnln nalagkvagv qfrgqspial drdallrirg gstlsgdagp
      181 iyvmdgtivn sidinpddve sltvlkgana talfggraan gaivittrkk gsgngigvev
      241 ntgvtfdrvy vlpryqdkya ggasptlmty twkagdpvew kaldgkkfpd ytddsswgpa
      301 mdgseyvpwy awigghsrsf ktaslvpqpn nvrdfwetgv ttnnninftk sgqgynvrls
      361 ytkqyvkgil pysksdrnni nlsasfdldq hltastnity sqqqidgifn dgyanassgn
      421 fnqwfhrdld fkimkelkdl ttpigtyasw nfssnpdgyd panplnfygg nywynhytrl
      481 qnntttqnrq rlfgdvslky kfnnhfyvkg tvrknqlttl yetifsskla asatqtgdla
      541 sfgtgysnyq ednfellagy tqrfgdldvs atiggnklsi rqygltafts kglnvpdlys
      601 isnsvaqpni gstrnnwetk slfatgdfey rkfasitwai rsdwystlpq vpqgnnrlis
      661 pslgaglvfs eftksslpwl sfgkvfgswg kkprdldvyk nnflygvnpn pwngnflmat
      721 prqlldpalk gslittyeag idlrffknkl glnvvyyned nngepvsvaq sgvsgftskl
      781 inaarikkqg ievilsatpi nkqnfswqvn lnysylinnp vvalqpgaaa gtrqllagga
      841 fgtrfarafq elgsdwgqli gggikrndag dlvinpnngn yvadvnkhwg svvpktnggi
      901 vntftykrft lgfnldfqsg gkffslsemw ggfsgiteat aatndkgknv rdavsagggv
      961 hvkgvssvdl ktvvdtyvpa dayfqqfyfn riaepyvhdl tfiklrevnl gvnlpvekwg
     1021 lakyvksanf sviarnpwli ytktksfdps eisaiqgedg qypgtrslgv nlrlnf
//
LOCUS       WP_092723412            1148 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092723412
VERSION     WP_092723412.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1148)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1148)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1148)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1148
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1148
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127739
     Region          34..178
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
     Region          187..1147
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhlcgvmam vlsmlyafpq sklpasksnt gvlsigdtlp aiaiqvfdkg niqssntasy
       61 kgkgllldfw atwctacykk fglldslqkk ysnqlqiilv cakntgdnre kidaftknit
      121 vdlpsfslpv vigdtiadhl fphkiiphyv widahgvika itgsepvtee niarllsnks
      181 iknlptelpe vvvqtgyqsv pkeratgsft qidnklfnqq tstdvlsrle aiassvmvdr
      241 ktgvgmmirg lstlsgdksp livldqfpye gdigninpnd vesitllkda aaasiwgara
      301 gngvivittk kskfnqpisv elntsisiit kpdlwylkqi nssdyidver mlfskgykfs
      361 dtasinklpf spvyeilfqq rrnaisenea narinalrqa dvrndfskyf yrnavnqqya
      421 fnvksgnsns awlvsggydk niselyapys raslrfnhtm tpvknlqvsa gvylaesrtg
      481 sgrpaygsis mansalppyt sfadangnpl pvaksyrqsy ldtagrgrll dwnyypltdy
      541 shtaltgstq dvlvnlgiry sfnnalsfdi kyqyekeasa nsvlsseqsy svrnyvnqft
      601 qlgntaandi yrvprgamld lssstmtvnn lraqlnysht wgssslsvia gsevreahit
      661 gnsgrsygyn dntlntaqvd yatpyptfit gykayivdyt sytdllnrfv svytngayty
      721 knkytvsvsg rkdasnvfgv ttnnrwtplw sagiawqidk erfyhaatwp flrlratygy
      781 sgnvnqkipa lttisylsns pytatpsavi kqyanpelrw ekvrtlnmgi dvrsknnrvs
      841 gsveffikqg idlmgntpid yttgigstit knaasmkahg ididcnslni drtfkwvtql
      901 nlswytdkit ryylsskras nfingsrpgi sglegspvys ffsyqwagld patgdpqgyy
      961 kgqvskdynt lmgntivind lvyhgsampt fygsmgntfs wknwsvtvrm mykfgyyfrr
     1021 ntisynnlya sgighadfak rwqypgdeki tdipsliypa isardgfyqa saatisnash
     1081 irlqyvtiny eldkqkikql pfkqiqlycn asnlgilwsa nkygidpdys esatppsisf
     1141 tagvriny
//
LOCUS       WP_092723772            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092723772
VERSION     WP_092723772.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109584
     Region          22..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrinvltvl lflgltaiaq nrklsgvvtd gttgkgipsa tvsikgnkgs nratdadgrf
       61 slsvvngkit lqvsaigyva kdlqvdagtn evtvslaqsv enlsevvvta lgirrekktl
      121 tyasqsingd elrkaaninf mdalsgkaag vniftsssga ggstkvvlrg nkslnglsep
      181 lyvidgipmv nnkggqpgsy ggtdqgdgls ainpediesm tvlrganaal lygsqgangv
      241 vvittkrgrs gkvtvnfnss ttfdkvfnlp afqydygavn gsdyswamtk gsgykrgyie
      301 nffrtgvdat nsvsiaggsd ktsvyfsyan tsatgvmptn tytrhnitln qstkllkdkl
      361 tlssnvmlss eisrnrpgag yynnpltgly lfarerdfds yknnyqvfds trnlykmnwy
      421 steekqnnpy weinndpkfa ktyriiasak aayeitknlk feargsidya dklfdnryaa
      481 ggnsvsvspn gtwsytkytd qslytdgiln ynnkfgdfsv taiagasyqr nvfndgmtvg
      541 ngtvslqypn fftfanipnn vmfkqtinrs ikegvlanat igykemlfld lagrndwast
      601 laltgnqsyf ypsvgltaiv semikmpeyi sffklrastt ktandvpfnv vspnntiggt
      661 gtanatggis rntqvpfsnl kpeeiastey gaemrflngr lgfdftyyna tstnqflrls
      721 apsgsgytfy yvnagkitnn gfeltvnaep irkadfrwtt avnlaqnknk iveliasnpn
      781 yqvggddegf asiikaggsf ndvyiykfnr ndagqiildt kgvptkaktq tlvgnvnpdy
      841 llgwnntfny knfflsllvn gkfggvafsk teafldaygv sarsaadrng gqmsinaiqg
      901 ttavttiapd vyyssigdrn rimepyvfsr tnvrlaqfvl gytfpaknkn avikdasvsl
      961 igrnlfffyk kapydpeqam stnnsmqsnd vfsmpatrsy ginvkltf
//
LOCUS       WP_092723884            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092723884
VERSION     WP_092723884.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118330
     Region          24..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mriyciitac clfvcsitsg qvsitgtvls yatgspltga tvqcetkntl tddqgnfria
       61 vhkdsftlkl sfsgyttwek tyrapypkhi dilleprtal lsevtvstgy qklpkeratg
      121 sfttigeqlf nqqvttnvmd rleaiangys vyrgqngqqr nmvrgmstik gmtdplvivd
      181 nfpyegdlan inpnmvesit ilkdaaaasi wgtragngvi vittkkgsfn kplqidfsan
      241 ltttakpdlf yqkpisssdf idveellykk gyynfwinsp drpaltpvie lliqkengai
      301 taddyqqkta alrkidvrne fakymyrkaf nqqyflnlsg gdshhswifs sgvdrnisnl
      361 dakdsrinlr fshtykpfkk wtfttsllyt lasqtngrpg ygsiftasga lypyarfrdd
      421 ggaplsimkd yrqpyidsag ggrllnwnyy paedylfqhm tatrqditan ldlgyqvfnt
      481 lsaeikyqyg rqsletvntq glnsyftrnl inrfseidat gafvrhipvg airdqsnnvi
      541 sshqvrgqln yhntwsrhsv saiagaemrd issvggnyrl fgfdedllth gsvdytrpft
      601 swfgggpdfi adpsanrqss nrfvslyana aytlgnrysf sasgrkdasn lfgvhandkw
      661 nllwssgfsw tlsrerfyhs rlfpflklra tygysgnvdt rraavttiiy ngvspytllp
      721 farfenfpnp dlrwekvatl nlgidfklks diltgsveyy qkkgadlfgt vpvdytsvaa
      781 ftilknvasm sasgvdisls sinvnrtvkw ysdlnvnyyq dkvtdyylss ndassflngg
      841 aqiaglkgkp vysifsypwa gldpatgdpr gylkgavskd ytaltgssvq vtdlqyngpa
      901 mprmiatlgn tvswknvsls frlmgkfghy fkkssinyts lfaykighad fsnrwqqpgd
      961 erttnvpsmv ypanssrdrf ytnsealidk gdhirlkyia lsydwirsgl plkrislhfn
     1021 vnnigilwrs nkdgldpdyf mgsipeptsv tigikgtf
//
LOCUS       WP_092723954            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092723954
VERSION     WP_092723954.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112377
     Region          26..1023
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklmlssicf llagllsfvp lhaqerllkg rvqdgtshlp itgvyvscke nhanvitdss
       61 grftlkitnq lctlviksmg yetrqmtvts sdndlvipla advqemrevv vtgytqqsrn
      121 kttgavstik aaaidnnpvg sfdvmlqgra pglyvgtptg qpgeagrvti rglgsingdt
      181 nplyivdgvp iaaasfaaln tddfesinvl kdaastapyg sraangvvvi ttrkgmalpd
      241 gkvrinyktq mgfsavnssk wdmmntsqrl qfeeilqdpn mpgwaysann pnkivngvst
      301 pktaadyafg khyldslkti ntdwrkyllr kaftqshtln lsggndrtlf yiavsylnqe
      361 gialnsglkr yslraniqnt sgrlksslsv glstasvryi qdegvapqgg aavggggite
      421 knpiaslyya lpyqsptdsa rpgnfgsnal dvyrnslrkd nqikavvsln edfrlssdlh
      481 listvgidyq qsnftnylnp dsyygaqepn gnrgsyqrsl atrlglivng glrynkkwgd
      541 heleanllae mnrikgegfg ftgyglnsll lntpagvsqg tadnnfipai sgqttpdnll
      601 lsqiaiarys ysnkytlsas lrrdgssqvp alnrykyfya vggswnvlse sfaerlrthf
      661 sylrlrasyg ltgnaggfas dygyrelyap anyagqsaye lqtpgnpayn wemnriadva
      721 veagffknrl rteldfynri tdglfvnrnl slttgfatis snegkirnrg velmiegdii
      781 kqkdwkvtag lnlaynqnlv ltlgneskif adeasmslpg ytlgtfyavr wqgvdpatga
      841 piyltkdgkt tntynsgdav pmagkvydpp ykggftlnvt ykqfefsllm sfikgmyrln
      901 ypnlyahsgd anyrqynqsa dmlniwqkpg dhaayagaqy ptfftsrdim sadyiklrnl
      961 siayhvplga nlskyihglk vfaygqnlfs fmkwrgfdpe dandiaqyey pmprmitggi
     1021 nisf
//
LOCUS       WP_092724448            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092724448
VERSION     WP_092724448.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119297
     Region          46..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknwplessf agrgrpprrg tvhgkkqlll lfllgcffta qsqtlltgrv vdsagnkplq
       61 gvtvatdmsk rsavtnalgv yqirvtdkdk klvfsyvgmk pvtrmlgssa vydvtmvtdi
      121 sglsdvvvvg ygtqkrsatt gsiatittkd idrvhggatv sttlagklpg vtfrmpdgrp
      181 gssaniqirn mgtplyvidg iqqdegqfnn lapndiesis ilkdasaaiy gvraangvvv
      241 vttkrgatgk nnvnidaysg wqqwfrfpkv lnnsydymsy laeaqvnsfg stnitqteld
      301 kykqgasagl qyrsfdwrkf imsndfapqn sinvninggs dkvnyyvsat nfyqnsvlgk
      361 eyqfmrtniq snitaklasg fkvgmdvngr iesrenpgvp glddywlarf avlrntpler
      421 pyandnpayl nnightetny aflnerlsgk frsdwrvlqa nfhadyevpg vkgltlrgly
      481 syyiadylln nheftynayt fnptdssynv tggstnpwre reqikqintt mqgqisynnt
      541 fgdhtigatm vaerlksqrt rnwihaspvs nnlpliyfpt adtyqdsddk qarvgyivrl
      601 nynyanryyl elsgrrdasy lfapgyrvgy fpggsvgwri teepffrnll hnnknilsdl
      661 klrasygilg ddnpngspiv apyaylpgyn ynqgtaiidg naltvsrdkg ipttnitwlk
      721 sritdlgldf vllkgkltgs idyfyrkrtg lpaskndviv pqelgyslpl anlnsdaqyg
      781 eelsiaytgk inavnisvgg nisytrsefl qsynplflns wdqyrnsseg rftnigwgyt
      841 vvgqftsqdq inhypvnidg kgnktllpgd liykdwngdg kidqydmrpi gygygtqpni
      901 nfgfnfalay nhfdfhadfs gasgytwyqn wemrwafqnn gnlntiftdr whhsnpldpt
      961 spwipgkypp trlnpgtghs dynanstfwl hnvtqirart vefgytmpts lvkkaglqra
     1021 rfyanvynlf sidnlkqygi dpeviddngl qfpqsrvynv gvnltf
//
LOCUS       WP_092724598            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092724598
VERSION     WP_092724598.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121386
     Region          27..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktrmqvlfa llcllccntv llaqekrtva gvvkdprgaa lasatiretg tsnkttsdan
       61 gafslkvkpg ativisyvgy ddftlktgsg ssytvtlqdk igsvqdvvvt slgvskgkka
      121 lgyaqttika eqltetgtpn fatalygkap gvrigatpgg atssvnitir ginsitgktq
      181 plivldgvpi rngeannsny wgdqrlrgng lldinpedid nisilkgasa aalygseavn
      241 gvvlvttksa skgkkglgvd vnmnysaddi aylpryqnvr gpgisknvvd lgqsddgfly
      301 qdyngsgvkd trgvlgssin fgpkfdgkpt lawdgkirpy vaqinnyagl frtansssvn
      361 vaiskasena smrfsltrqd nqgislgadn tkniavfngs frlhpkfstd lmvnyinqht
      421 hnrpysidrl tnnfggmmgr fdnadwylak yktskgyryv tgrntqsltp aeniiwpglr
      481 gdimdyvwrv keynedeysn rviasmtnnw qiiddlrlrt rvsndftsmr tetkqsteip
      541 lafgnsgyfg lndyqnslvy gealltytkk ltsdldltam ggynaskeit ttisrgtngg
      601 lstenffdis asvnlpssgs srfsivkdaf lgtlnanykg ylfvegtvrr drtstmhpnk
      661 nsfvypsana sfifteafkm pdfinygklr aswgivgnyp daylaniayn qntlgvqavg
      721 gqpvlyttip ssfgndgikp eqkrefeigi easflkkrie leasyynaqi vdqilpltlp
      781 attgatsilt nigtlrntgi evavrgipvq tkqfkwevgv nlaknngkve klapgltrml
      841 hadydgnaaq lisdvgrpmg dfyahpvatd dkgnmivdpn gmykvdpnkm vrignampkl
      901 tggitntlsf kgfivdatvd frvggyvmpt alnwmtsrgl teeslnymdk ehgglsyyqk
      961 asgervltsa aqgpngekvy ndgivlagik adgskndyia sasdyywtvy nwggpqyspn
     1021 tryelyiken syvkfreiti gyripdhlar kigaqrlqfs vfgrnlfyly rtlkdmdaeq
     1081 ttagsrwfqt lnnigtnpst ktfgvmlrat f
//
LOCUS       WP_092725250            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092725250
VERSION     WP_092725250.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113781
     Region          29..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkwklfslv mlvlmsmmtn nlaaqgvpis gtvladdgtp lagvtvtvsg tnrstvtddk
       61 gkftinankn ttlqfsyvgy ttqkvkavag mqvslakdta qlndvvvtam gikkerkalg
      121 ysvtdlnaqe lmknkntnvv nslagkvpgv nitqfsgaag agasitirgg nstsegrqnq
      181 plfvidgviy dnsttvtgnt gtdglsrsnt tfsnrimdvn pedveslsvl kgaaaaalyg
      241 sraadgvvii ttkkgaegvv kvnatskvst swanklpevq tqfgngvyss ngvlnnisys
      301 nwgqkltaad tlynnignff qngivydnnv nvsggskngs fflsgsnfdq tgivpntkyg
      361 kttfrfngeq kygaltlnan vaysianinr tlttaglygs gvgsmqslyt fpqtfnikny
      421 lnpdgsqhri fagtlplend idnpywiink dnltsqtkri tggingtyki akwwdviarl
      481 gydqyttndy tyiapgsala plyqngrlsk dlydyryitt tvmsnlhktf gdfdthlmlg
      541 ttsentlian qnhwgynfit agtisfnnma stnkfftdgt trkrlvgayg evgasyknia
      601 fitvtsrndw sstlplenns yfypsvsgsf vftellpknn ilsfgkvras warvgkdana
      661 yatntyvnpp isiggytgig nqyysgnpyl ipeiqnswev ggefrflngr igldytyyhs
      721 etenqigqpr laqsggfifs tlnsgsvlnt gmeialtgkp iltkdftwda tlnfsynkgr
      781 lgafipgvay fyptdaqfgt ikaasipngg yflgmtgqpy lreldakgve ipngryqvdp
      841 stgfyklntt npvvgnreps wiggfnntfr ykkfalsfll dirrggdvfn gteyamvtng
      901 lsklttqndr qsvtvsgvns ltgadfnqty tagqsyving ttysgnyliq qywqnyaans
      961 ynfitsvnwv klrslslsyd fsdyfknkki vkglsatavg tnlftwtnyk gmdpevsaag
     1021 gtggsgstgi dylgvpatas ftfgvnimf
//
LOCUS       WP_092725258            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092725258
VERSION     WP_092725258.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121510
     Region          27..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklstktllv tvmlltafsl ksfsqermvs grvhtkngig iagalvqvtp skrsaitdsi
       61 ghysivlkdg dktisinsig fisqsfplta vqhfdfalld dpkslteviv taygikketk
      121 kigyavqelk gsdlikardd npinslvgki aglsvgaspe mlgrpelvlr gskdllfvid
      181 gvpvntdtwn ispddiesys ilkganasal ygfrgingai iittkrgtks kkgwqvdvns
      241 stmlekgfva ipqsqteygr gtafvysygd rlydnkqrlp ewgprfegql vkqydspydp
      301 vtntrtatpw targadnfnk fmemgvintn nvalsaatdr sdirislsnm nqkgmnpntk
      361 lnsytmavnv gyritdklsv easinlnkqy spnipdvnyg pnsyiymfkv ygssdynidd
      421 lkniykapmg vqdlipyaqe ygrensawfi akkwlrshdk tdvngyvkat yqfspslnls
      481 lrsqittwtq lrteqvpagt nlntytpwyy fgwygdyred rrnlfenntd lilhfdkrvg
      541 kfnisalagg sersftynsl wgttkamavp nvyalsnske qyasftwgsk mqvysgfysv
      601 dfsydkyltl shtgrvdnls tlakgyntfy ypsvslstvv sdyvnlpsvi sffklrasya
      661 nvkggltapt iasayyqntg mstnsflgyg tdlyssydgp tyknqnayst vtyynngqsv
      721 dftstianqa lkpytvssye agldmkflkn rlgvdvtyft slngpqifal qvpsstgyts
      781 qnvnaitsek kgyeisvsgs piksarglsw dvavnyatyk etlqdiygde svlslnghny
      841 rkgerldaiy gagfvrdgnn niiyngglpl rapsdinnns flgyanpdft fginnkftyr
      901 nfsvgfqfdg riggsiydev ykdgmnggta yesasgdfgv arlaewqstn ngsvaptaky
      961 iapgvkiisg tpvyaggkii nlkdltfapn dqattvqkfi ssgignvtey wmtdrsfvkl
     1021 revsisytlp agllaksrfi ksatfslvgr nllywakrkd idldqfasgy ndtdrslnng
     1081 gvlqsvtarr fgfninlsf
//
LOCUS       WP_092725349            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092725349
VERSION     WP_092725349.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115063
     Region          25..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktllmgfc alffvsmtai aqkstvtgkv tddkgrpidg asvvekkskn gtatdangaf
       61 klsvspgavl vvsgtgyerk eiatssgval tislknides lsevvvtalg ikrekkalgy
      121 avtsvakkdi elrpegdigr vlagkapgvd ilgtsgisgs gtnivirgvs titggsvppl
      181 fivdgvpfdg stnmpsgftf ggqtssrfld idpnnienit vlkglsaaiq ygdlarngvv
      241 littkngsan nkqnkkteit vsqslfankv anlpdyqdty gggfnlapsl afsnwgaafk
      301 nppdsfnhpy srsalnvafp eykgkkyayk aynsvpaffr tgwvsntavn vsggnavtrf
      361 sgnysytsdq gflpgnsvik nnfgfggltk lsnnftlsgt infattdyit pttstsfgss
      421 adnpsvygdl iytprsidlm gwpyknpidg ssvyyranng iqnprwtven slirekiyrt
      481 fgniqmkydi mkglsvlyrl gidvyntlne ltvnkggttg glqyttgmyr tlnstnsild
      541 hnilvnyvkd lnedwnltld gglslrndny tqngmkstqq lvfglfnhgn fvnheavged
      601 ggnlnfesqq krfgaflsas ggyrnylyln vggreswvst leesnrkify psasismipt
      661 aainglknnk wvnflkvrvg ystsarfpdp yttrtalniq tnafvdrngn vinqnaipnr
      721 lanpdlkpel lkeyeagleg tfinhrltvd ltfykrissn qildrsldps tgytvtsvna
      781 gdvrnegiel glgynvvkar dwnwqlnanw tinkslvydl psyikqinfa gysnlgnfai
      841 ngqplgilqg svtsvdpktg qkllddngyy vqdpnigilg splpqykltg iseltwkslt
      901 fraqmdysvg gkmislttas llargltkdm dfdrtipitl pgirqstgkp ndiqtgatsa
      961 yfntyfgpnd fqvwdatlir lrevslsysl pskwlaktpf gsvsvvasgq nlfylapnfp
     1021 kyvrfdpets slgvgtgrgl elltgpssrr fgasirvtf
//
LOCUS       WP_092726300            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092726300
VERSION     WP_092726300.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116374
     Region          34..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfktiaaklk rrkrifllfi lsvfstiiha qsrisgtitd avskkpvaga tvsvkgsttr
       61 tisdesgrft lksatiavir vtaigykele ttagadlsnl qltpvsqdle qvvvvgygsq
      121 kkatltgsve tvtakafqdr avsniglalq getpglvvtr tsprpgnegl nfvirglssv
      181 ngsaplivvd gtpvlnsysf lnmnpddies isvlkdasas iygsaasngv ilvttkrgkg
      241 kthydfgsnm rfttngitgy spsmqqyati wlnankeevt pnwwvwgtkd nmlkmqqgve
      301 gayhfatwpt vdyfifntnr inelfatrys yqnnlsisgg ndksayrlsf lmadnkgnla
      361 taydgqkqyn lrfnydikls drlkletgvs vvnaktatps vgldatlyan dmpffpaknp
      421 fgqwfpifng vdgganrnpa altsdggrdn qnsltgrvdl katyqivkgl sleakasvqn
      481 erftqekyvl aipiynwygt kqtgwaggid ttktsyyaks wtstlqyysa llrynttfkq
      541 lhnisafagm eaqktnynwi dasrvgftdl gvqsiglast avqtnngfss qygnyaylgr
      601 fnynyaekyl lelqgridgs srfatghkfq nyggaslgwv ftredflrsl ssvlnfgklr
      661 asygssgnqa aglgefdyls lvnigttvlg lpaalqnsss llnngiisyd rtwervvmkn
      721 ialdlvflkn rlsatfeyfs kdnvgmlvnv nypsvlggaa pktnsgkfnt kgwetilkwd
      781 dhvknfayni aitlsnattk vtgvqgadsy spgkmgivng ypyqswfvyk tngyfkdqad
      841 vdayyakygn spdlsglpqn ntavalrpgd tkkvagpggt itgsgngtsa lvyagdgtph
      901 ytfginlgas wkgfdisaff qgqlkqlimr ngwmsypfna iwtnqnpafl gktwttdnpn
      961 aifprltvnp nrarwdyann dfmlqnnryi rlktlivgys lppsllkkar lervrvyfsg
     1021 ndlwelthik dgfdpemget sqnsgypfar twsfgvnigl
//
LOCUS       WP_092726759            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hydrobacter
            penzbergensis].
ACCESSION   WP_092726759
VERSION     WP_092726759.1
KEYWORDS    RefSeq.
SOURCE      Hydrobacter penzbergensis
  ORGANISM  Hydrobacter penzbergensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrobacter.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Hydrobacter penzbergensis"
                     /db_xref="taxon:1235997"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121589
     Region          29..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrkktmlwk gmicllallc stalqaqdrk vsgtilsqed nnplagvtvt vkgkkrvsqt
       61 qpngtfvila qkgdqllfty tgfisqewrv gdndevsikl kpdvsklgev vvvgygkqsr
      121 qtlsgavtsl dqnalkssps tnvatalqgt mpglkiqqst gqpgttpsis frggtdfngg
      181 gspmvvmdgv ivpslyginm ddvesidllk daastaiyga rasngvilvt tkkgkkgkaq
      241 vnysfrqttn yirrnpleyl taaqyisknr egiasryqad ladgnnsaaa tdrgqnlgsw
      301 gwavnnawtt piglystqlv saanrkyign pqwgllidpn pfiagqmdsi lyhsldvktr
      361 enmilqqqtt qehylnlsga neqgsfslgl gmakdngiii gsslkrlsmn fngglnvgkn
      421 lkvsmstsay tvsqlvpyvd pagggagglm qrfigvaptv rytndtsgav lpgpndntlg
      481 npnywsqlyn nnssqqritg slnieysilp slkflasgsg yllynnanaf tkayqqgngg
      541 afnttrpasf snyndvqysy naflqydksf gshklsvlgg gefyefteks fsasasgapt
      601 dlipwlyasl pasvvngviq npvsassdfn awdrltsaig rvnysylnky fltanfrydg
      661 ssrlannrfg lfpgisagwn mhkedffeks flskyinvlk prvswgqngs inplgyyata
      721 qvyssagiyn glggiyapsy intdlkweka stfdvgvdig ilnnrvtlia dyfvrdvydk
      781 iaslpisaqt gftsfttnlg qlrnkgiele vkakiikpvk adglsvdvsa nfytfknyvv
      841 klpynglpgn rqstiqvwdp nhpgqlmqva glqegsrvgt deiwapsysg iyrsaadlsk
      901 dasvynafmp yihknlhqlg damwnqvykn dtidsrqfty vgrsvpnilg gfstmvgykg
      961 fslyaqfdya lnfmilnnek lrglsqvqgs qnstvdalkt wsptnpngtl prfywanqgr
     1021 nyatdasgnn pfkefwekgd ylalreltls ydmtpallrk alnnkvhnlr lfatgsnlfy
     1081 ltqysgnfpe vggvdngkfp lprrltlgvn itl
//
LOCUS       WP_092728877             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus alkaliphilus].
ACCESSION   WP_092728877
VERSION     WP_092728877.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus alkaliphilus
  ORGANISM  Algoriphagus alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Algoriphagus alkaliphilus"
                     /db_xref="taxon:279824"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40850
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigviketk efekrvalsp dvvkllrkke feviiesgag egsyfsdqdy rdagaevsdl
       61 pgvfssdvil kvnipsleei aqmkqgsaci symyayqhpe iiealnkksi ssfsmdavpr
      121 israqkmdal ssqanlagyk svilganylg kifplmmtas gtitpakvli fgagvaglqa
      181 vatakrlgai vevsdvrpet keqveslggr fltvegaeav kieggyakev saeflekqqk
      241 liqdkikdad lvittalvmg rkspilvtee mvksmktgsv ivdmavesgg ncaisekdkt
      301 vvkygvtlvg esnlpsllpv nasqlyatni stlflhlfns fglipnleee itkgvlithe
      361 gqlvheftkn ilnshpkns
//
LOCUS       WP_092729112            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            alkaliphilus].
ACCESSION   WP_092729112
VERSION     WP_092729112.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus alkaliphilus
  ORGANISM  Algoriphagus alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Algoriphagus alkaliphilus"
                     /db_xref="taxon:279824"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117345
     Region          25..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkallfvva lftmtlsfev saqqrvitgt viseedglgl pgatvlvkgt tvgtttdldg
       61 nysisvpags nvlifsfvgl ksqeetignr svvnitlttd asqlsevvvt aigierekka
      121 lgyavttvgs eqlenrpesd varvlqgkvp gvnitstngm sgsgtnmvir gyssatgsnq
      181 plfvvdgvpf ntstnnqnsf aqgggvtssr fldidpnnie smsvlkglsa tvlygdqgrn
      241 gvilittksg askrkaaevt inqsvftnea aslptygqty gngfqqdrgf ffsnwggrld
      301 qgvtinhpya tssiqsirea fpqfwvngiv ggtpvqyeyk aykdpsevff ktglisntsv
      361 qvsggsdktg ynasfgytde egylpgndlk kynfgmgins aisdklsvns sftfsitdlq
      421 sppvnassgs gsaipsvfgh vlftprsidl enlpyehpvd kssvyfragn ditnpnwlvk
      481 nytntsnvkr ffnstslnyd inddfsltyr lgldtyselq evrynkggat anlatrngyy
      541 rsininntiw nqdlilnwkr dlsdkfsmsa llggnsrfdt ydqngiasqg qlafglfrhs
      601 nfrtsastda ysgaglnfir eerrygvytn itldysdylf lnlsarndwt stvekqnrsi
      661 lypgasisfi pttafdwgss tlndlklrlg ygtsagypsp ystrnflaqs arafdvggav
      721 ttthavsnil gnpnlrpelh gelefgiegv mfnnklrfdi slydkntrdl itqspidpst
      781 gftstainig kirtrgaevq atvtpvstas gfvwnstlnw styrteviel ggglqevvva
      841 gytnlgnfai pgqpfnvikg igfdrvpagq efagqpiils ngvhkpspgl vvlgdpnpaw
      901 ngswinsfny kgfnlnfmle yrhkgavysn tvtatlargv tldpvvdref sfimpgvrqd
      961 gnnadgspry ipndyqitas dyffsgyqga tnepnlfdgs mirlrevsls ynlpntliak
     1021 tpfkratfav sgtnlwfnal nfppnmnfdv dvlgtgvgng lgfdfvtgps srrmggtltl
     1081 tf
//
LOCUS       WP_092731173             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            alkaliphilus].
ACCESSION   WP_092731173
VERSION     WP_092731173.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus alkaliphilus
  ORGANISM  Algoriphagus alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Algoriphagus alkaliphilus"
                     /db_xref="taxon:279824"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109174
     Region          30..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnyllklks ltlalaltig aivvanaqtr sisgtvmdar lgdpvpgatv ivkgttrgsa
       61 tdldgkftip iqagdqvlvi sfvgyltqei eignqntiti nlqediqslq eavvigygsq
      121 dkkeitsavv gvkpedfnrg nvsnpaqllq gkvaglsitr pggnpnnpfn vrlrglstfg
      181 anasplivld gvigaslenv dpndiqsidv lkdgsaaaiy gargssgvil itttrqgkke
      241 gatnvtvnsf atmdraanli pilsaeefva rggnnfgsnt dwrnelidda fsyttnasvs
      301 gsfgnsnyma svnyrdnngi vngvgnerln trlnlsqgal nnklrfnvnl sfttedresi
      361 ndaafryati ynptapvfen tedarnrfgg yfqrdlfdff npvalarqqk fvreaktslt
      421 syrveydils nltltaqysq drrteldgnf wslqdfqvgl gatgsaernt fdrkqrifet
      481 tlryetdlsd klnmtllgga glqyttnqgf narvrqylfd lgwnnlgaga irlgnntnvs
      541 sfanedqlns lfgranfnwd nmiffsasvr aetysgfgpk nqtgvfpavs igsdftqvfd
      601 mgvfsqfkpr vsfgvtgnlp psptlalgvf gngnridldg dpltqndifv ginqfsnpnr
      661 elkwetkrel nfgvdfglfn nkvtgsvdyy trnisdllfn vpvatgapnp fdpgrfntag
      721 stwvnladlr aagfeflvsv nqigkgslkw sptfnftiyd ktsieslsag elgfeelrfa
      781 tpgspgqnnn piiynrvgqn lgdfygprln gltesgeyil sttdpnqfek lgnglpkgef
      841 gfansfmygq wtlnfffrga wghdlynsyr gfyengdtas ntwnsvvtdk tptspliksp
      901 ptfnsslved asfirldnae lgynfqtksp nlsslrvyfa aqnlftitny tgvdpevrin
      961 dsennnpfts alspgierrn tyfqtrsftl gvtvnfk
//
LOCUS       WP_092731652             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            alkaliphilus].
ACCESSION   WP_092731652
VERSION     WP_092731652.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus alkaliphilus
  ORGANISM  Algoriphagus alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Algoriphagus alkaliphilus"
                     /db_xref="taxon:279824"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107900
     Region          26..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfklyktilt laflwgsvgw afaqytvsgt vvdertgeal igssillkgt ttgtitdldg
       61 rfsinlptnd patlifssig fltqsvdvap gvsilnirlr qdatnleevv vtglatsvkr
      121 snlanavtsv sardltgttt iqttdgalyg kvpgatirsn ggapgggisi qlrgisslsg
      181 asqpliivdg vyisnasqrs gratvsgagg snqddssnrl adinpadiet ieilkgpsaa
      241 aiygtranag viiittkrgq egkttvslsq dvgfaqplrl lgvdnwneak infffpesrr
      301 pielerfraa qssgtfidye dyfynnqatl lntrinvsgg tdktkffvsg nitdedgtvk
      361 ntgfnrysir anidhkitdr ikigvssnyi rsntdrgftg nqnnsgasig ysiayvpnyy
      421 dlrkkddgty pvnpyfsenp vavtdhgvnn tlvnrfiqaf tldidllkte nsflkaqfsg
      481 gldylqntsl vylpeflqfq raqanpgdvf kgkqesfntn fqaalvynwn lgsvnlnssa
      541 glvrldfadn alfnrgrglv pgqrnlqqaa iqeinqefns riqdagiflq qeanwedkii
      601 gtlgirwdks tlngdpqqyy afprasvafn ianfdfwnvg fmnqlkpria ygetagpvnf
      661 gatftplggt niggllgsvv stqigntlil petakelefg vdagffnnrl sleatyyiks
      721 tqnniqnlnl apstgvnttp sneaelenrg ielslsgtpi etanfrwfsr vmfwknellm
      781 trlgiptyia gafgtglgtf lyaegysptt ivgapavpgn pggftfwgna qtkfnmsffn
      841 sirimkglel sflvdwkkgg dninltsfln dgggttkgwf dddngdgipn grqrppapfn
      901 nagrwvqdas fvkireigly ytlpkttise wfgssvsnir mgtsvnnafl ftkyegydpe
      961 tstfgaqaia nnvdiapypt prrmffhltv df
//
LOCUS       WP_092732372            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            alkaliphilus].
ACCESSION   WP_092732372
VERSION     WP_092732372.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus alkaliphilus
  ORGANISM  Algoriphagus alkaliphilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Algoriphagus alkaliphilus"
                     /db_xref="taxon:279824"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118849
     Region          27..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrllvalftv llytgaheic gqttspvngs vvdiasgqal agamitaepg ritvvadkng
       61 efnldlspgs yvltaqflgy atfkiqlrip lessltlqms alelgleevq vlatgyqeip
      121 ksrasgsfvs vdrelitrrv stnlidrled vtsglilnrt gdvgrdpisi rgrstlgrfs
      181 qplividnfp ydgsledinp ndvesitvlr daaaasiwga ragngvivit tksgkpdlpt
      241 rvsfsansnw vappdafwnp llspedyidv ermlfntgff natennpsrp vlspvvetli
      301 lardgkisga eangiidnfs rndlrrdink ylyqnqlnqq yslgiagggk shayrvgfgl
      361 denqenvvgd enrrislnik ndfslmndrl kiqtglygvk ststgagvdp nslqfnnasy
      421 mypyarladd ngtplaverd lragfksqal esgllewtyv pleeigrspq ksvrndwrln
      481 fganyqilkg lsaavqyqyw enrssnetiy aeesffvrnl vnsftqlnat ngllsypipk
      541 gsiydwsnfn sgshngriql dyqkswadkw dltmlggtei kslaavnlmg ryygfnpefy
      601 sslpvnyqgq fsqynnpfsa slipnrdgqs kttdrftsvf anaalshqkr ylltlsarkd
      661 asnlfgvaan qkgvplwsag lgwtlsdegf ynwnalpyvr lrlsygyngn idrslsaftt
      721 attvtfnpit qipysrivnp pnenlrweri kiinggldfe nksgtlsgsl evyrkagidl
      781 igiapfapst gislftgnna atnttgfdln lesfnlkgtw nwsavfllsg ireevrdykn
      841 evpvlnllnn gasglggtyf pvvgkplfai yslpweglnp ntgapvgild gepsedyrai
      901 vtgatldnii yhgparpsff gslrnnltvr gfslsvnisy rlgyyfkrts veydpillgr
      961 gghsdyalrw knpgdelitq vpsmpsprnt lrdlfyrnss vlvekgdhvr lqdirlgyql
     1021 pqnrswakaf qraeiffyan nlamiwkatd tdwdpdfgtf rplrslalgv nlef
//
LOCUS       WP_092735550             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Riemerella
            columbipharyngis].
ACCESSION   WP_092735550
VERSION     WP_092735550.1
KEYWORDS    RefSeq.
SOURCE      Riemerella columbipharyngis
  ORGANISM  Riemerella columbipharyngis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Riemerella.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Riemerella columbipharyngis"
                     /db_xref="taxon:1071918"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109535
     Region          31..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttsvlv vvlsssfamv naqqkkdtik tkniegvvit algikrekks lgyasqevkg
       61 galtdgttkt gnaaallsgk aagvqinsnn nfggstnivi rgykqlggng gsplvvidgs
      121 pisntyvsgd ydlgnflsdl npddiasmni lkgaaasaly geralngviv ietkkgrngk
      181 ngswgvtlst dvnfgfidks tfptyqtryg agygpyysmk snpffdegpd gkpmapfged
      241 asygaefdpn llvwqwgsfd kfsshygkpy awtaakngpi tffdtpftts nsitlekgna
      301 knnfmlsynn flstglmpns kqkkntfsar inyqltdkls asvystltle dtrgrnktgy
      361 sdnlvtgfre wwqtnvdlqe lkdvyfksgg lnrtwnrssv ddgspaywnn pyfqvyqnye
      421 sdgrtrnfsy aqvkynfnkn fgllakvsnd fynmlveqrl adgsltqafg vsgrnassgy
      481 wrqnrtgfet nfdvignykf disgklnvqg ivggnvrrsg yeslttsteg glavpgiyai
      541 snskgqvldp veyyarsasa sayasasfay dnflfvdaty ridkssnlpk gnnvygypsf
      601 tgalllsdli qkdwlnylkl ranyaevgss tgnynlvntf skngifrdqa lffapstlan
      661 pnlkperske velgieskmf nnrfgfdvav yrtktfdqii nlpvsnasgy navvvnagei
      721 dnkgveiqmn ltpiktsaft wdisvnwakn inklvslhpd akvlrldayq ggvslnaveg
      781 qaygvlygtd yvyqdgqkvv dpktgrylkt tesnkeigni tpdwtggirn nfkfgknfsm
      841 gflidvqhgg sifstdmyyg latglyqeta vgdyrtkgvv hpgvnpdgkp nqtytagaqa
      901 fgnvdgyrrm pnkrfvydas yiklreanit yklpkylian tfleeakisl vgrnlwiiyk
      961 nlpyadpegs sggglqsrgs svgvlpttrd igvnvtlkf
//
LOCUS       WP_092736261             909 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Riemerella
            columbipharyngis].
ACCESSION   WP_092736261
VERSION     WP_092736261.1
KEYWORDS    RefSeq.
SOURCE      Riemerella columbipharyngis
  ORGANISM  Riemerella columbipharyngis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Riemerella.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 909)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Riemerella columbipharyngis"
                     /db_xref="taxon:1071918"
     Protein         1..909
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101211
     Region          30..908
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 minfyklkaa plfllagtfl yaqqkdsikt knidqvvlvg ygtkkkkdlt gsvtsisakd
       61 fnggmvsspe qliqgkaagv qitsnggapg sgssirirga aslnasndpl ividgmpldn
      121 ngingaanpl slinpddies fnilkdasaa aiygnratng viiittkhgk kgklrvgyss
      181 ttsvsekfgk ikvlggdqyr alvneispne ykalltnynt dwqdaiyqla pgfdnnitfs
      241 gglgslpyrl sigylnqdgi iktnnikrtt agislspkff knslsvnlnl kgtyaenrfa
      301 dsetigyaia fdptkpiydk ampqlggywe wldpaknepi tlapknpvsn lfqrwdisyv
      361 rrvlgnvqfd yklpflpdlr anlnlgldya dsnghviaap tlasafytkg tnrdysqnkk
      421 nrllefylny tkklpslksd fdlmagysyq kwnentpfsp tiygdgtqvp atgvdfftqn
      481 illsyygrln ytfdkkyllt asirrdgssr fseenrwgyf psvslawrmd qedflkdnks
      541 istlklrggw gitgqqdigs nypylaiygy sdgganyqig dhfytlirps gydknikwet
      601 tetknigldf glfkdrvlft vdaykrktkd llsivpvpag vnftnllmsn vgdmeskgle
      661 fsltskvidn ndftwdisan atfqkaeitn lsvtnnpdqk vltggikggt gntvqvqtvg
      721 yapnsfyvyq qkydsngkpi egeyvdrngd gkineqdlyq dhspmpkaif glsssfrykn
      781 wdlgfalran ignyvynnmn seygyshale ssshlrnlta dyyntrfkda qylsdyyved
      841 asflrmdnis igynfptfig ngklrinatv nnvfvvtkyr gldpevfngi dnnfyqrprv
      901 yslgfnikf
//
LOCUS       WP_092736442             932 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Riemerella
            columbipharyngis].
ACCESSION   WP_092736442
VERSION     WP_092736442.1
KEYWORDS    RefSeq.
SOURCE      Riemerella columbipharyngis
  ORGANISM  Riemerella columbipharyngis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Riemerella.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Riemerella columbipharyngis"
                     /db_xref="taxon:1071918"
     Protein         1..932
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102337
     Region          33..931
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlav gtvfflgaqs vlaqktkkds vktkdldevv mvgfgrkkav qeitgatsvm
       61 kaksiqdvpv tsvdkmlqgr vsgvqvgsas gqpgsstivr vrglssingr vspvyvvdgv
      121 rvssgdltsn tatanilssl dpdsiesiti lkdavstavy gadagagviv ittkqgkkgk
      181 akfnlgmsrg vsfravdgyr alttpqykqy lfdaikngyn eatatnyinn rfddtyntdw
      241 ravtertsga svsninlsas ggtdrlqyyv sgnyfdqdgv vknssfsrfs fnskvdyqat
      301 dklklssstq mayskqssla ggaafsnpil qqyfllptdp vrnpdgtyfg lednqvsngl
      361 ynpaalleyn siktgtakvf anfsaeysil knlryklvfa peyinieenn yasplhgdgf
      421 anrgqaraay tryfnynvqn ilsysanagl nnfditaiqe ayqsqyyyls gfaqnvgalg
      481 letlsnfvkp vsidntksts srngyaltgh ydydrlvlld lsyrrdilsn fvpgkkggnf
      541 wsaglgidla rlpyfknirs vsmlkfrssy grvgnevstl pyalygftns ynskpaitys
      601 gvynpnltwe tvspfnigld fgffdnrftl saeyyhkktd nliyniplsp sqgltsyfnn
      661 igslvnkgfe isfnadifkn grdgfnwsig gnfntldnkv tqlyggavrg sstilkeges
      721 vgtyylrkwa gvdpdngnpl wykngvdget tsnygeaqqa vqgarfnkyf ggvnttlsyk
      781 gfsidaqaty gfggkiynga wgryflsdga flhapysgys damdywtpen rnaqnpkpvy
      841 rneslsnehs trylfksdyi rlstaklayt fdrslieksg lsslqiylsg tniltyrfdk
      901 klkldpeigl agtadldlpi mktyslgvni gf
//
LOCUS       WP_092736611            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            psychrophilus].
ACCESSION   WP_092736611
VERSION     WP_092736611.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter psychrophilus
  ORGANISM  Hymenobacter psychrophilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Hymenobacter psychrophilus"
                     /db_xref="taxon:651662"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111690
     Region          31..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklywlapa lgaalalspq aavwaqataq rtitgivtda nrvplpgvtv lvkgttngas
       61 tgvdgryslq aapgstlsfs figyatqers vgdsgsvdis lkedatalnd viitafgikq
      121 errqvnygaq evsgkdiies rqpnivnalq gkvagvqvts sgggagegas ivirggnsld
      181 gdnqplfvid giimdntsft estapgggsa fngllgrsvs sqnraadinp edvetmtvlk
      241 gpaaaalygl raangaviit tkkgksgvvt vdfrtqvsvd qvnrlpklqg vykqgglgvf
      301 dattrnswgp qfapgetvyd nldnfyqtay nyqnyltvtg gtekgsflls ashldqtgva
      361 rnsefdkstv rlsgtlqvap kirvqssaqy lnsggrrplq gpglfggsgg ymvsllswpr
      421 nddarnylnp dgtrrrligg igssdadnpy ftvernpitd rtnrlignaq vtyepakwat
      481 isynlgtdfy tervrsirav gtsqpgnqdg gisetttqnr llnsnltaif shsfndnvsg
      541 slllgnsveq slrettdiig lvfrspnfns inntvnrgal ttnslrrlvg nfarinldlf
      601 kqvtaevsar ydmsstlprp sqnknfgqgf lygsatlgye fsrtlgldnn silnygklrl
      661 avaevgkdtg pyrvdsplaq styifggfrq gffgsnallk pertrsyeag ldfqflkgrl
      721 gldagvyyse trdqliaprv sqasgyilqy inggtvtnkg veialngrpv qtasgltwdv
      781 lanffhnenr akklpsflte vnqsdswvid vargsafpnr pitsigvqdy arvtdpasey
      841 fgqviisptt gypsvvagtf vyagdrapqf ttqitntvay rglslafmld frkggkvvng
      901 newlavrsgl snktldrnqt aviegvvraa dgsyspntrp veltqgyfit qvggtglafv
      961 edgswtrlry atlayrlptt llgkgfvkgv elsvtgrnll lftnysgadp etaaagagvr
     1021 gggsggfdyg stpatrgvdm alrvnf
//
LOCUS       WP_092736615            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            psychrophilus].
ACCESSION   WP_092736615
VERSION     WP_092736615.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter psychrophilus
  ORGANISM  Hymenobacter psychrophilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Hymenobacter psychrophilus"
                     /db_xref="taxon:651662"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113693
     Region          34..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpnhysllrp lvllgalaal plaaaraqap qaytlqgriv deqgqglpgv tvlvtgttlg
       61 astdaagnyq lavnlapgpy rltisaigfk teirpialgs sptvstsitl naasqalddv
      121 viigstvavn rrelgnaitv idgtqlqktg sgqllnslqg kvagaqivqn sgdpsgsisv
      181 rlrgitsltg ssdplyvidg vivsnqsnnv sqralsndig vanpgqnrla dinpndiesl
      241 nvlngaaaaa iygsrasngv viintkrgka gaarvsvyts fqinelrksv pvntygkqfg
      301 feglrlypis gvsaaqiaan pgtttvgitr agataqlasn lvdvprydyf keifrtasgt
      361 dngvsisggs ertqyfvsag ylnnngiidd tnfrrynlra rvdqrltnwa kvsagvsyin
      421 ssasekangn vfyspinavn itnniydirr rdtngnllav eptrvnplst iedmtftqet
      481 nrtisdlqvn ltpfkgfsld yivgvdaysq vgqgyirpyp yqataglppa rypdgfasdg
      541 nnteinlnsd inlgyeynfs edfklnlrag ynyqylrntl atqqgqfltp fittvrgaat
      601 asvqadysla qstvsgyygq atvgyrnlaf ltgalrrdgs srfsasetnq yypkvsgslv
      661 lsdiggwkna afaqkfntlk lrasygeagn lqgigpydrl yqfnavpfpr nalvpgaqla
      721 nnsvrperln eleggvdlgf fgdrlglsvt ayrqkitdlv vtrnlapstg gssivnnvgt
      781 menrglevll ngtairttdf swdmtvvfsr nrnkvlelpg slglaqtisi pnsagapvfl
      841 lqgqpagify gstyatnpdg sllltpqgfp qdertsgqit gsvnyvpsrg adgqpsyapg
      901 tavaqalign pnpdwtgsft tnftykklsl rvlldavqgv dvfnadyrtr qgvglgdlae
      961 kelrgelprg yifavyntqq friddgsfvk lrevalsygl ptfskyisal dlslvgrnly
     1021 swddykgfdp etsaggssdl lraidfgnvp iprtyqirla atf
//
LOCUS       WP_092738849            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            psychrophilus].
ACCESSION   WP_092738849
VERSION     WP_092738849.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter psychrophilus
  ORGANISM  Hymenobacter psychrophilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Hymenobacter psychrophilus"
                     /db_xref="taxon:651662"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113741
     Region          24..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkvlltaal fapvllqqaa aqdrqisgrv tdrasgqglp gvtvlvkgtt igvstnadgt
       61 ytisapssat tltfssigfv slerpigtas tvdvglstds kvlnevvvta vgierqeksl
      121 ayavdvinnk sltqgketnp iaslqgkvag anissssggv nsskrivlrg nrsfqgenqp
      181 vfvvdgiiin nsniqpstgt inqvdtgnrv gdinpediet mtilkgpsaa alygsvaang
      241 aiiittksgk naaelgkkaq isysssfvae tplklpdfqn eygsgfdnef ypeentnwgp
      301 rfdgsevqyg ftlpdgskni qryeakpnnv rdffntgttf lntlslqggn aktnyylsfs
      361 davqkgivpd dkfrrnnlkl taattvaekl tastsiaynh nftdvtfqgs giiddlynvs
      421 rgintpdykd inspfgskeg ffsgyyynpy qsinddrfes kldriignvt lnyapvewfn
      481 ltyrvgsdys ydrrngrnai kvgttaytrp tddpgrynet riflqdfttd llgtfrknvt
      541 pdlsvqlilg gnvraseqnt lsttanalvl pnffnlanrs geaatdteif rrrligaygd
      601 ltvtfrdylt ltatgrndws stlpknsrsy fypsvglafv ftdaipvlkd nntltygkir
      661 asyakvgnda tpyylqntfp vaagfpfggq tgftvsnraa ndqlkleqit sfeagielgl
      721 lndrvngqvt yytttstdli sslavppstg ftsailnige vynnglettl ritpvkldng
      781 frwdiganft iqdsevkklf gnarelaaga gnpvptfiig epspvlkgta flrdpagniv
      841 vrptvasngd ilgydpvadp vqrilgrvsp kylwggnttf sykglratvv vdakvgasiy
      901 sgtkstlaft gssaetaeyn reafvypnsv venvdgngnv tyspntnvts dggfglwysr
      961 lsnpiaefni isadflklre asitydlpqg llqntflgra svgfsgrnll lfvpkenkfi
     1021 dpeasifgtg nsqgrefgti pttrsygvnl svtf
//
LOCUS       WP_092739388            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            psychrophilus].
ACCESSION   WP_092739388
VERSION     WP_092739388.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter psychrophilus
  ORGANISM  Hymenobacter psychrophilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Hymenobacter psychrophilus"
                     /db_xref="taxon:651662"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113384
     Region          26..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrilfsvlp lvalsatqvv aqtravsgrv adrttgeglp gvtvllkgts ngistnadgs
       61 ftltvpatgg tlvfssigyv sverpigtdn titvslssds kqlsevvvta lgieqqkksl
      121 gysvsqieae eltqarqtnv vnslagkvag vrvqasngmv gassnifirg lttfngsnqp
      181 lfvvdgipid nggganalqg gvsnsnraid inqddiesvs ilkgpaaavl ygsraasgai
      241 iittkkgatl gnkkqsvtvt ssynvvktgr lpdyqnaygq gargdfnria qgswgplvtg
      301 qtvqnyrged evltinpdnv kdifktgsnf qnnvslsgat ertryyasyg nlhevgvldn
      361 ndlkrntvtf ngsadltekl rtgvsviftn nassrtpqgn qlanpffrtw fiprtfdvrk
      421 ypfelpnggq qgaavvgtft pnntwystdd nplwtiknnt yddelnrivg ninlaydftd
      481 wltlnyklgt dtyaqnikyv nardsrgtsi angtpsvign irdqtitrre lssylnltik
      541 rnitedfsas lllgneinqr rltdnrvtgs niqirgfdni tntidilpfg qqenqrlvgf
      601 ygdlqlgfkd faflsfagrn dysstfgaak rsyfypsasa slvftelips lkdnriftsg
      661 kirgaaaqvg reapvystds yyasnnnpad gfgpalnfpf rnqlglsydn tggnpnlgpe
      721 ftttyevgad lnffsgrlnv eatiynqqsk diiftvpvag asgftnifqn igkseakgve
      781 llissvpvki gnftysnsin wtrirnrvis lapgveqitl ggftspstrl iagqpygvif
      841 gsvfqraeng qlllssqgra qlaldnqivg dpnpdwtggf tntftykgls lttlldiryg
      901 gdiisrnvsd lrrqgaaeet gdrsnvyvid glipqadgtl vqnnvqitae qyfddlygfg
      961 kaefvvfdas wirmrevalt yslpqsltnk tflggvqlsv narnlflyap nvphidpevn
     1021 aqgqsnsqgl efnalpqart fggsirltf
//
LOCUS       WP_092739616             883 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            psychrophilus].
ACCESSION   WP_092739616
VERSION     WP_092739616.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter psychrophilus
  ORGANISM  Hymenobacter psychrophilus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Hymenobacter psychrophilus"
                     /db_xref="taxon:651662"
     Protein         1..883
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=95517
     Region          66..879
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvrllpfsfl lplslpalaq rtdtvrlrdv hvtdsvtsvv tscpvqilvs qyqfspflpl
       61 qeqlrqvagv qatpysgapg vqvavrirga aslgidaqpl yvvdgmpvfq ntfrpnagss
      121 iitlvpaevq eldnnpllsi ptediaqvev lkggyetaly gsqglngvir ittrrgqagk
      181 prlsysgygg vqhartrydl ldareyatlr nevaqrfnqp apysaaqlad lgrgtdwqde
      241 vlrtaavqeh hlglsggtat tryyaaadyl nqegvvlnsr lrryavrtal nqqigqhlrl
      301 eatggfsqte qrvpnynvvq ealftpptqs ptdnprpgyy vnpldrarqs yqtpeqqrll
      361 aqlgahyeva tgltvdlran leratlrsrs yraafgpipg gqngdltfty rqltlnpalr
      421 yarsfggarh avtaslealr qsrqttteqs tytpgtaanv pggggsssrs ageaganfyq
      481 ltagytfaer yqvlgtlrad assafapdnr wswlpgaqvr whaakenfwt aapgkldvwv
      541 gwgrtsgagn fgrnsflipv pnggnlsqta plflpdpsqq ldagleagll nnrltvtaqa
      601 yarrttvsps fsgfpsspst tdnvylrntg leltvqgswq agqlagssql aaaanrnrfv
      661 tgnatsynlp yqrtldgqsi atfygyrtrp lgptgtleye dtngdgrvdf qdqqplgsgl
      721 prqllsftqq ltlgrleaql qadgmfgyqv nntallelda prgdanasgr vrnrwtptnp
      781 atdvpvagsr llgggvnpgf stytlqsgnh vrlsavtvsy kvwerdarnv rlwlggqnll
      841 vltkyrgydp nvssagsnnq qagldagayp tartvllglr atl
//
LOCUS       WP_092742859             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paracidovorax valerianellae].
ACCESSION   WP_092742859
VERSION     WP_092742859.1
KEYWORDS    RefSeq.
SOURCE      Paracidovorax valerianellae
  ORGANISM  Paracidovorax valerianellae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Paracidovorax.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Paracidovorax valerianellae"
                     /db_xref="taxon:187868"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38221
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpaesm vgetrvaatp etvkklkaqg havrvqtgag vaasvpdaay aaagaeivda
       61 asawgadlvl kvrcpteset pllrpgatlv gmlnpfdaag lqrlaqagat ayaleaaprt
      121 traqsmdvls sqaniagyka vmiaadryqr ffpmlmtaag tvkaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvk dqveslgakf invpfetdee keaaqgsggy arpmppswle
      241 rqkvevakrv aqadvvitta lipgrpapvl vteamvesmk pgsvivdlaa pqggncplte
      301 agqtvvrhgv tlvgetnlpa lvaadasaly arnvldflkl iinpegalhv drqddivaac
      361 lvahegavtr a
//
LOCUS       WP_092751718             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            aethiopicum].
ACCESSION   WP_092751718
VERSION     WP_092751718.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium aethiopicum
  ORGANISM  Rhizobium aethiopicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium aethiopicum"
                     /db_xref="taxon:1138170"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38922
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvake fadgetrvaa saetvkkmks fgfdvvveag agaasrildg efeaagarig
       61 sfadaaaadv vlkvrrpgps eiagyksgaa viavmdpygn deaiaafasa glsafamelm
      121 pritraqsmd vlssqanlag yqavveaaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vsramlasmk pgavavdlav erggniegvv
      301 agevadvegv rvigfanmpg rvaasasaly aknlvtflet mvdketksvv vnlddelvka
      361 tmltyaggvv hpafggakkg dl
//
LOCUS       WP_092757540             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodoferax
            sp. OV413].
ACCESSION   WP_092757540
VERSION     WP_092757540.1
KEYWORDS    RefSeq.
SOURCE      Rhodoferax sp. OV413
  ORGANISM  Rhodoferax sp. OV413
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Rhodoferax.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Rhodoferax sp. OV413"
                     /db_xref="taxon:1855285"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38772
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,300,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpqeta tgetrvaltp etakkltalg htvrvqsgag vaasvtdaay aaagaeivda
       61 agafgcdlvl kvrspsdaea almrpgttlv gmlnpfdapg lerlaaaglt sfaleaaprs
      121 sraqsmdvls sqaniagyka vmmaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslggkf ievsydtpee qeaavgvggy akpmppswla
      241 rqqievakrv aladvvista lipgraaptl iteemvksmk pgsvivdiaa gkgpmgphgs
      301 aggncplsea dktvvkhgvt ligetnlpal vaadasalya rnlldflklv ltkegtlnvd
      361 maddivaacl vtqagavtrk
//
LOCUS       WP_092760836             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Jannaschia
            helgolandensis].
ACCESSION   WP_092760836
VERSION     WP_092760836.1
KEYWORDS    RefSeq.
SOURCE      Jannaschia helgolandensis
  ORGANISM  Jannaschia helgolandensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Jannaschia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Jannaschia helgolandensis"
                     /db_xref="taxon:188906"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55657
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkevh egearvaitp esaghlqklg hevfieagag tlagftdday rdagvevvkt
       61 apslfkmidv vakvrpptet eakrltkgqt lisffypssn ealmetlksk gataiamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvylefdd selpdgaetg gyappsspef
      241 qakqlakfre iapdidivis talipnrpap vlwtadmvks mkpgsvivdl aaerggncel
      301 tvpdekivtd ngvtiigytd fpsrmaaqss tlygnnirhm vadltpekdg vvvhdmeddv
      361 irgatvtheg sitwpppppk iaaiatkpkq kvivptaeek ratevaafka qtrnqvgllv
      421 igaalllfvg ffapasfmqh fivfvlsvfv gfqviwnvsh slhtplmavt naissiiilg
      481 alvqigsgsw lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_092768299             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter sp. DSM 11652].
ACCESSION   WP_092768299
VERSION     WP_092768299.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. DSM 11652
  ORGANISM  Acinetobacter sp. DSM 11652
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter sp. DSM 11652"
                     /db_xref="taxon:346222"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39742
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgesrvaatp etvkkligag hsvviqrnag vkaayidsay eqvgakivdd
       61 aytgsqlvlk vrapkgeeiq klapnttvva mfdpyrntel dqfaaqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgaiv eatdlrptak dqveslggkw ldvpmsaeeq aradeaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgraapr likaetvakm kpgsvildma vetggnvegs
      301 kcgetvvtdn gvkilgvpni patvsteasa lyarnvynfv etlfdqdkny sinqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_092768426            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            actinosclerus].
ACCESSION   WP_092768426
VERSION     WP_092768426.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter actinosclerus
  ORGANISM  Hymenobacter actinosclerus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Hymenobacter actinosclerus"
                     /db_xref="taxon:82805"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116242
     Region          24..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkvlltaal lapvllqqaa aqnrqisgrv tdratgqglp gvtvlvkgtt tgvstnadgt
       61 ytisapstat altfssigfv gverpigtas tidiglstda kqlgevvvtg algiqrqeqq
      121 vgyatatldt keltqarptn vvngltgkvs glqiqnvnng vnpnprvtlr gtrsllgnne
      181 alivvdgvis tndvlgtlns ddvasisvlk ganaaalygs qasngaliit tkkgsntnrv
      241 tisqtsqfes isflpkfqdk fgngantytn tlpdftadns idndyntkyq sfenqqygpr
      301 ydgslrpfge kladgsiqmi tfesrldekr kffnnayqaq ngisfaggde ktkfyasyqn
      361 vhnngivpkd kydrnsfrfn asrelgrlta gfnvsyvqqr tdittndaqa nsvywnifnt
      421 tamspitsyk dwqnnkfanp ngyynayyyn pyfiidtyrt ndakntilgn ldltykvtdw
      481 lklnyrigtt stdqsslisq nkfnfnpyiq alntnksgag ltgavtdiss nltrinsdlf
      541 asmdktfgdv svqaivgnnv qqltsrfnsv gstalavpdl fnlgnrignl tganataksr
      601 lyafyadltl gyqdflyvhg sgrydntsvl dannrsffyp gvdvsfiftn vapalkdlaf
      661 ldygkirggi skvsqinlag sgpgvydtgg ayrlastysl gtgfpfgsla sfqannglvq
      721 pglkpeetvs ietglelsfl qrrvsgavty ysqksnnqti ptsissttgy tslllnagev
      781 qnkgvevdln lvpvrlengv tftiggnfny nqnkvislpp gldqlnlstg gnaqlyaikg
      841 qpypilrgty yqrtedgqik mtkvkdpftg edryfplraa dskafgntqp kyrygfnssl
      901 tvkgftlagq aelrtgyvvy nsigedldft gggersvkyd rqdfvypnsa ilgadgktye
      961 pntsgltpgg sefwsstayn rgvaenyvts gkffkirelt lgyalpasmv skvgfvkgat
     1021 lnifgrnlft wvpkeniytd pefsfsnsna igintnlqtp ptrlygatit atf
//
LOCUS       WP_092768825            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            actinosclerus].
ACCESSION   WP_092768825
VERSION     WP_092768825.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter actinosclerus
  ORGANISM  Hymenobacter actinosclerus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Hymenobacter actinosclerus"
                     /db_xref="taxon:82805"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112571
     Region          31..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqklywlapa lgaalalspl qaawaqttaq rtvtgvvtaa ldrsplpgvt vlvkgttvga
       61 ttdaegrfsv aapagstlsf sfigyttqer aveagdgpis ialkenttal ndvvitgyni
      121 aqdrrdivta vqevkakdii dsrqtnivna lqgkvagvni tssggspgeg taivirggts
      181 ldgdnqplfi idgmimdnss fqestapggg sqfngllgrs vgtpnragdl npediasmtv
      241 lkgpaaaaly glraangavv ittkkgtagr ttinyrtqfs vdevnrlpki qdqyqqgsgg
      301 vfdattrnsw gprftpgqpr ydnvenffek gyafqnflnm sggtekatff vsasrldqsg
      361 vtpenkydkt tvrlsgtaql spkfdvsasa qylnsggrrt lqgpglygss ggfllsllnw
      421 pgnddarnyl nadgtrrrll ppnngtdvda dnpywsarfn pqtdrtnrfl gntqlnfkvl
      481 pfltlshnig tdvasthsts vravgtsqvg nqnggiaetv dlnrlitatt lasfrhtfse
      541 nlrgslvlgn tiehsrdeav dytglifqnp dfisinntvn rgalqrvamr rlignfaqls
      601 atlldqvtve lqgrydrsst lprpdegknf gkgfgygsaa lgyeftrtlg leqnnilnyg
      661 klrasvaqvg rdtgpyrvqs plttntyigg gsrndffgsn pilkpeqtrs yeaginlqfl
      721 knrlgldfny yfsrtkdqli aprvsqatgf ilqyinggvv tnegqeitln gspirsasgf
      781 nwdilanfyh ntnkteslpf pltvvfqsda fitnvhqgga flgrpitgia aydfqrvsnp
      841 sspdygklli npttgypipg ttftyvgnra prfttqftnt fsykglglsf lldfrvggkv
      901 vngndlystg tgtsprtaer ykevvfdgvv tnadgsyspn trpaeltqgy yqnilgavgt
      961 pfiedaswtr lryatlsyal paallertgv ikglelnvtg rnlllltkys gadpetaaag
     1021 sgvrgggsng fdygnvpatr gvdmglrvtf
//
LOCUS       WP_092769407            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            actinosclerus].
ACCESSION   WP_092769407
VERSION     WP_092769407.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter actinosclerus
  ORGANISM  Hymenobacter actinosclerus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Hymenobacter actinosclerus"
                     /db_xref="taxon:82805"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108342
     Region          30..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknpylakmv lpllcagagi ssayaqgigt vsgrvldekg qglpgvtvll egtslggstn
       61 gdgtfliqna pagpqtliis fvsfttqrqt invtagqnta vptltlsent tllneavvvg
      121 ygtqrkqdvt gavtaitekd fvkgqvtnpe qlvqgkiagv sittvggapg aaatvrirgn
      181 sslnanndpl yvidgvpvdk dgisgasnpl tlinpndies vtvlkdasst aiygnrasng
      241 vilvttkkgl sgekltvnls sqtsvsqrfk eydvlnagel rdivnangsa rqiaalgtan
      301 tnwqkeifrt aatydnnisl tgsvgklpfr vsygnlyqdg ivitnnlkrn sgsislspvl
      361 lndrlkvnvn akgtrvdnrf iddgqvgsav lfdptqpvfg tgdqyglygg yfqflqpngt
      421 plglapgnpv aslrntnnvs tvdrfignvq ldyslpmveg lranlnlgtd vskgegattn
      481 qptdfgnfna kelgtpglng rykqfnqrkn mqlleaylay gkqfggtrfd iqggysyqsf
      541 vnkgdnflay rfdqntlfnp edkltvpgyy sklvllsyfs ratlnvkdry lltatvrndn
      601 tsrfapgnrs gwfpavglgw rlkgedflan nntiselklr asygrtgqqd iggvydylpr
      661 yvlgdaaaqy qlggqgivty rssgynrdlr wentttwnvg ldygfldnri sgaievyerk
      721 stdllanvnv aaggnltnrl nanvgslrnr gveflingaa vrsqdwnvdl nfnlaynkne
      781 itslgpqteg ftgyqvggip ggtgntiqiq tvgfpsnsfy aqqqvydang rplqgvfvdi
      841 dgngmvtpna tdfyrykqsa prltlgftps vsyrkvslst lfrgnvgnyv yngvaanlan
      901 fanakgstgf vqniprdiyn tgftsqqlls dyylqnasfl rcenitlgyn vgklfndkan
      961 lrlsaavqna flitkydgid peiasgidnn fyprartftf glnlgi
//
LOCUS       WP_092776941             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinokineospora terrae].
ACCESSION   WP_092776941
VERSION     WP_092776941.1
KEYWORDS    RefSeq.
SOURCE      Actinokineospora terrae
  ORGANISM  Actinokineospora terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Actinokineospora.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Actinokineospora terrae"
                     /db_xref="taxon:155974"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36847
     Region          6..358
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(19,74,93,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtantvvgvp aetaggerrv alvpkvverl aarnisvvve pgagsaalip ddayvhsgat
       61 lgdpwsadvv vkvavptdde iarlragavf igflapltqp ekaqalraag vtafamesip
      121 risraqsmda lssqanvggy raalvaaehl trffpmltta agtvppakvl vlgvgvaglq
      181 alatarrlga httgydvrpe vadqvrsvga qwldlgieat gsggyaralt dderaeqqrq
      241 lakaitgfda vittaqvpgr taptlvtaea vqgmragsvv vdlagesggn celtspgavv
      301 vehavtiaap lnlpatmpeh aselyarnva alldllvakd galaldftde vvagacvtgq
      361 ev
//
LOCUS       WP_092773298             902 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            actinosclerus].
ACCESSION   WP_092773298
VERSION     WP_092773298.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter actinosclerus
  ORGANISM  Hymenobacter actinosclerus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Hymenobacter actinosclerus"
                     /db_xref="taxon:82805"
     Protein         1..902
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=99225
     Region          76..898
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvrllplsfl lpltlpalaq qadtvrlpdv ciekslildq tiykscwplg qtplldnqcp
       61 ehyipsllpl qeqlrqvagv qatpysgapg tgevvrirga asidshvqpl yvvdgvpmfq
      121 yrfssfmpqe anspyssdfn feagsnplls ipvadveqvq vlkgayetgq ygflgqngvi
      181 littkrgkag qaprvhyagy ggvqqarhry dllgarelae vhneanrnng ydpeyspaql
      241 aafgrgtdwq sellrtaaiq ehhlstdgsf gtadtqfgtr yylgadylrq tgivlnsslq
      301 ryalrfnldq qlgrrahfsa glsygetqer rlaqtglqqa mpvalyylpm ipvyapngdy
      361 atdydnpnpv qrarqnyatp rnrrllargq mqfelltglk ldlrvslerd alqaseyegp
      421 rvvsstaptd gqeirqreat yrqrllnpal rfdrtfggkh avqasieaah wqrdesrsvl
      481 tfgrgglppf nvppgrndfg yssyetsqqy qaitarvgyt yagryavaas wqrnatpllg
      541 gseasqylpa aqlswhagee awlkdrgiis rldarvgwgv tsnrgnfags hgfnqplggn
      601 lgsyflflde lttqydagld vglwqnrltl saalyrretd irlgigspde sellnrglet
      661 tvaaswqagk lsgtsslaas fnhnryqrpa dapiqifvpg pnfvlisdqp vstfygsryl
      721 gpdasgdpqf asqnrealgs glprqllsls qtarygrlsl qfqvdgmfgy qvydpnlall
      781 dvptgyfnas trvrnrwtpt ntntqvprag asytrfgqvs nytlqsgnhl rlsaltlaad
      841 vwkhgarnaa vfvsgtnllv iskyrgfdpn vsggeadprq agldrgyypt artvavgvra
      901 tl
//
LOCUS       WP_092779059             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Jannaschia
            pohangensis].
ACCESSION   WP_092779059
VERSION     WP_092779059.1
KEYWORDS    RefSeq.
SOURCE      Jannaschia pohangensis
  ORGANISM  Jannaschia pohangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Jannaschia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Jannaschia pohangensis"
                     /db_xref="taxon:390807"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55509
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkevh dgearvaitp esaghlqklg hevfieagag mlagftdday raagvevmkt
       61 aatlfkmvdv vakvrpptpd eakkltkgqt iisffypasn eklmdlvksk gataiamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvflefda selpdgaatg gyappsspef
      241 qakqlakfre iapdidivic talipnraap vlwtkdmvea mkpgsvivdl aaerggncel
      301 tkvdekvvss ngvtiigytd fpsrmatqss tlygnnirhm madltpgkdg avvhnmeddv
      361 irgatvtheg eitwpppppk vaaiavqkke kpkeltaeek raneiaafka qtknqvtlla
      421 aggallllvg lyapasfmqh fivfvlsvfi gfqviwnvsh slhtplmait naissiiilg
      481 almqigsgsf lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_092781070             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodospira
            trueperi].
ACCESSION   WP_092781070
VERSION     WP_092781070.1
KEYWORDS    RefSeq.
SOURCE      Rhodospira trueperi
  ORGANISM  Rhodospira trueperi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Rhodospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Rhodospira trueperi"
                     /db_xref="taxon:69960"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41129
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,104,301,327,329)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,137..138,147..148,151..152,155..156,158..159,
                     161..166,168,170..172,175,198..199,291..292,334..335,339,
                     342..343)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(132..133,137,140,143,184..187,207..209,241,252,
                     269..271,278,280)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(134..135,137,147,190..191,198,214..215,217..220)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(167..171,174,177,200,202)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpkerr pdearvaisp evakklvglg vevvvesgag lgadvtdaml qdvgatiapd
       61 akttlgdadl vwkvqrplma negtadegmd eialmkrgat lmchlnalte kslvdalaaa
      121 gisafamelm prisraqsmd ilssqanlgg ykavieaana fsrafpmmmt aagtvpparv
      181 lvfgagvagl qavatakrmg avvlatdvrp atreqveslg gkfvtvdeem ekqaetaggy
      241 akemppeyfe kqkqvisevl kktdivitta lipgrpapkl vtaeqvrsmk kgsvivdmav
      301 eaggncelse pdkmvevegv kiigypnlps rvaadasplf aknllnfftp qfdkeakalk
      361 lnwedetvkg tcvthdgkvv hprlvegsn
//
LOCUS       WP_092789088            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            hitonicola].
ACCESSION   WP_092789088
VERSION     WP_092789088.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus hitonicola
  ORGANISM  Algoriphagus hitonicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Algoriphagus hitonicola"
                     /db_xref="taxon:435880"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114843
     Region          23..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvllgfal tlltvvsvwa qnrtitgriv addqpeglig vnvlvkgtti gvvtdldgny
       61 sisvpesatt lvfsyigyrs veeqignrsv idltmtedsq nldeviitay ggtadkgnft
      121 gsaislkgdq ianrpinnvv naiegqspgv ittsasgqpg stpavrirgv gsvnsssspl
      181 yvvdgvpfdg dlsnlnpedi admtimkdas stslygsraa ngvimittkt gkkdrptvnf
      241 rvqqgvsgra lpeysrvnad qyyplvwesl rntqlglgds ptdaaafasd elinvlgyni
      301 ynvpnnqivg adgtlnpnav nnfqglnwfd elqrtgdrke ynltysgatg ktdyytsfny
      361 lnekgfvirs dierftgrln vntqatdwlk tginlsatlt egnnassggs ssfvnpffta
      421 rsigpiypvf aqnmqtggfv lddlgnriyd tgdleqfglp rrgpgsfpgr hvvqetllne
      481 drfdrdaiss raymevrflk dftfrtniat ditsflgigy dntivgdgap agrtsrsnvr
      541 tnsltfnqll tysktfnekh fvdalvghen ydlkinrqfi skqdqilagn iepdnfvtin
      601 sasgrldret iesyfsriny vyddkysfsa slrsdgssrf akdvrwgtfy svgaswaidq
      661 edffnfdniq llklrasyge vgnnsvggfy pwqalydlgf nnasepgilq aslsaldlqw
      721 esnntfdigl dfafgnrfsg tleyfnresq nllfevplsl ttglnsrfqn igtmanrgie
      781 fniagdiirg ndfkwtanln vstfenefke lpfdeqivgt kkyvvgngiy dfwlrdwygv
      841 dpqtgeglyr vdeydasden qqiigqdtvt trfqdarfhf agdaipdffg gltntftykg
      901 fslnvllsfa iggdiydgiy aglmsadpdg galhqdilnr wqepgdvtdv pkmdvtgaaq
      961 tnvasdrwlt dasylnlrsv nlsytiprat lerwkmrgat vylagenlgw lsgrsgmyvs
     1021 gsfngttant ftpartftlg vnvnl
//
LOCUS       WP_092790479             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Rheinheimera
            pacifica].
ACCESSION   WP_092790479
VERSION     WP_092790479.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera pacifica
  ORGANISM  Rheinheimera pacifica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Rheinheimera pacifica"
                     /db_xref="taxon:173990"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108897
     Region          47..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqtfalsa lccalqsagl aaqvqqdavp delvvqqqdt eaqqralekk ekeietivvv
       61 gysstrqedi tgaaidvkia dvkdlssani mqnlqgrvpg vqiltngnpn staqvkirgq
      121 glgplgyndp lyvvdgvpmn sglheinsnd ieslvvlrda asasiygara angviiittk
      181 kgsgdskfev klntstedfe ydlnplntrq raevvwraav ndranpnnvs plyqydwngd
      241 ydnpqlnnvi lntyidsaqt mrpadtdwfd evtrrstskd lnlsyssasd tsavyasfgy
      301 ldrngvvkss eftrisgrvn shvelfdgkv rvgenltltd qkqnlvndla ggilglaieq
      361 qsiipirted gtgwggptag itdrdnpvrl lemnkdntnr fnkvlgnvyv eylplddltl
      421 rtnyglsygn fkfrnftkaf qagslnfndr ltvtddwnkt tvwsntaeyk yllnydhmft
      481 llvgnetvef eseffsasgs gfasqdrdya fleqatsgit angfadawtl ksyftkldyd
      541 ydrkylasft lrrdgssrfg qnnqwgnfpa asvgwrvsde dffkfdamnq lkfraswgqn
      601 gnqeintrat ssifqsryat qslftneqde gtaydlagsd qgnlpsgfak vssgnpdlkw
      661 etstqlnlgv dfdffdsaly gsfdwfrkrt ediltttqpl ategegaqmi vnggtientg
      721 ielmlgytde ftvaslgnft fditgnista knkvialpds vvnsfggngr dktilgksvn
      781 svfgyvtdgl fqsaeevaah arqpgaapgr iryvdlngdg vindqdqdff tntdpdfiyg
      841 lnftltygrw dfnmfwqgvk ggsvrnswrl ftdftslnig snygdrtlna wtpdntgsnv
      901 paltlldnnn earessfywe dgsylklrnl siaynidpai idarvylsaq nlltitpsgt
      961 lsqdpeapns vfpiprtvtl glsmtf
//
LOCUS       WP_092790590             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            hitonicola].
ACCESSION   WP_092790590
VERSION     WP_092790590.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus hitonicola
  ORGANISM  Algoriphagus hitonicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Algoriphagus hitonicola"
                     /db_xref="taxon:435880"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107898
     Region          26..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtrfyklslt llflwcsigw awaqytvsgt vkderngepl igasllvkgt ttgsvtdldg
       61 nftlniptne gatlvvssig ylskevevss sltriditlr edatnleevv vtglassvkr
      121 snlanavstv sakdltgttt iqttdgalyg kvagatirsn ggapgggmsi qlrgistlsg
      181 asqpliivdg vyisnasqrt gratvsgagg snqddganrl adlnpadiet ievlkgpsaa
      241 aiygtranag viiittkrga egrttvslsq digfaqplrl lgtddwseek inffftearr
      301 pvelerfraa qssgnfidye dyfynnqatl lntrinvsgg ndktkffvsg nisdeegtvr
      361 ntgfkrysvr anidhkisdk irfgvssnyi qtdadrgftg nqnnsgasig ysiayvpnyf
      421 dlrrnedgty ptnpyfsenp vavtdnginn aqvnrfiqaf tldidllqts nsflkasfsg
      481 gldflqnrtm vylpeflqfq raqanpgdll kgkqesfntn fqaalvynwn lgkvnmnsqa
      541 glvrldfnen slfnrgrglv pgqtnllqaa iqqinqefms evqeagvflq qeanfedkii
      601 gtvgirwdks slngdpnqfy sfprasvain lgnfdfwnss finqlkpria ygetagpvpf
      661 gatftplnga niggllgsvv stqvgntsir petatelefg vdagffnnrl sleatyyikn
      721 sqnnfqnlnl spstgvnttp sneaelqnkg ielglsgtii eksnirwfsr ilywkneiem
      781 trlgiptyta gafgaglgtf lyaegfsptt ivgtpadpdt pggftiwgns qpdfnlsffn
      841 sinlfkglel svlvdwrqgg dninltsflt dgggttngwf dddngdgipn grqrepepyn
      901 naarwvqdat fvkvreigly ytipkatind wfgtavqnir vgssvnnafl ftdyegydpe
      961 tstfgaqava nnvdiapypt prrvffhlti df
//
LOCUS       WP_092790665            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            hitonicola].
ACCESSION   WP_092790665
VERSION     WP_092790665.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus hitonicola
  ORGANISM  Algoriphagus hitonicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Algoriphagus hitonicola"
                     /db_xref="taxon:435880"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112836
     Region          25..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknsykftll flmslltsls lfaqqtisgk vtaeedgqpl pgvsivvqgt stgtvtdidg
       61 nysinvpdse svlvfsfigf esqeilvgnt ntinvvmate esqldevivt afgisqekks
      121 lgysaqsida eaitksrqpn lvnslqgqva gvqvtnsgga pgqsariiir ginsldpsad
      181 nqplfvvdgv pvdnstiesg gtprgmsnri adinpndies msvlkgaaat alygvraang
      241 aviittkkgk sgeirvdfns slgfdklvkk prlqeeygqg fsgerndssf wpswganiae
      301 endpnyvyqd nwtrafdtgv nfdnslsvsg gnenatfyts igrldqkgii pfsnwdrtsa
      361 klsgtvkvne kfnfsgsmny tnsggnrvph drflermmyw aetqdvrdyi npdgtmktya
      421 ntnpiydarf atyednvnrv igninlnysp tdwltfsyrl gmdnysdsrt eitpgpmgid
      481 gevalsstgf lsenrinsrd ltsnfyislq kqwnedwnts lrlgndvfer rfdrvtatgs
      541 nfvipgfynl nnttqifasq gksmrrlvgf ygdlmvdykn flflnitgrn disstlpvdn
      601 nsffypsinl syafsehlem pswvtfgklr aswaqvgkdt nphilgatfv spsifplngq
      661 vgfsrnstfg dpllrpeqtt svevgtqlaf fnnranldvt yyksnakdqi ipvpisdatg
      721 fssyitnage ienrgweivm ggtpiergdf rwdvtanitt nqneivaire gidqivvgsq
      781 fgyvgstvtm ilkegrpygd iygssyvrpd adpdsevldr slpqligang fpvrtgnqlv
      841 lgnavpkvfg glrndfnykg felsflvdfr agvdqysqfd nflsafgkqe aslarndfrv
      901 fpgvladgsq nnqevwlgqg vgpdgvdyga gywrnhyrtt senfvvdasf iklrnitlay
      961 nlqpnlikrt pfrtarlsva anniilytpw dgfdpesfsa gaggnavgft glgfpgvqsv
     1021 fftlnlgl
//
LOCUS       WP_092791584             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            hitonicola].
ACCESSION   WP_092791584
VERSION     WP_092791584.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus hitonicola
  ORGANISM  Algoriphagus hitonicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Algoriphagus hitonicola"
                     /db_xref="taxon:435880"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108832
     Region          30..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnylqkakt ltlaimllfg atlvanaqsr titgtvldas fgdpvpgatv likgttrgvp
       61 tdldgkftle vrpgdeilvv sfvgyltqei eigsqstfti nleediqsle eavvigygsq
      121 dkkeitsavv gvspedfnrg nvsnpaqllq gkvaglsitr pggnpnagfn irlrglstfg
      181 anssplivld gvigaslenv dpndiqsidv lkdgsaaaiy gargssgvil itttkkgske
      241 graevninsf gtldkaanli pilsaeefva rggtdfgset dwrqelirda ysyttnasvs
      301 ggfnntnyla avnyrsnngi vqgssndrin trinlsqaaf dnklrmnvnl sfstiesnsi
      361 ndaafryati ynptapifed tedanerfgg yfqrdlfdff npvaminqqk frnerktalt
      421 syraeydilp nltvsaqyse drsndliggf wsrqdfqvgl gsrgsaerit ndrrqqifes
      481 tlryevditd glnlallggv gtqttknqgf garsrqflfd tgwdnlgaga irvgnftnmy
      541 syanqdqlns vfgranfnyn nylfvsasvr aetysgfgpe nqtgvfpafs igsdftqlfd
      601 mglfsqfkpr vsfgvtgnlp psptlalgvf gngnridldg dplstddvyv givqnsnpnr
      661 flkwetkeef nvgidfgiwd nkvtgsmdyy trnisdllfn vpvgggpnif dpgrfntvgs
      721 twvnladlsn agfefsvavn glnlgeviwt psgnftiyqk tqinslsasg lgfdelrfat
      781 pgspgqnnnp iiynrvgqtl gdiygprleg isesgeyils ttnpdeferl gnglpkgefg
      841 fannfawrqf tlnfflrgvw ghdlynsyrg fyenadgasi twnsvvtdkt ptdpfitstp
      901 tfnssyveda sfvrldnmei gynfktnspn lgslrvyfag qnlftitnys gidpearvtd
      961 lengdgftts lspgierrnt yfqtrsftlg lslnfk
//
LOCUS       WP_092791975            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            hitonicola].
ACCESSION   WP_092791975
VERSION     WP_092791975.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus hitonicola
  ORGANISM  Algoriphagus hitonicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Algoriphagus hitonicola"
                     /db_xref="taxon:435880"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115562
     Region          25..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkallfvva lftmtlsyev saqqrvitgt visdedglgl pgatvlvkgt tvgtttdldg
       61 nysldvpags dvlifsfvgl eskeevignr tvinvtltad aaqlsevvvt aigierekka
      121 lgygvtsvgs eqlenrpeqd varvlqgkvp gvsitstngm sgsgtnmvir gyssatgsnq
      181 plfvvdgvpf ntstnaqngf ttggattssr fldidpnnie smsvlkglsa tvlygdqgrn
      241 gvilittksg askrkaaevt inqsvftnea aslptygqvy gngfqqapgf ffsnfgprmd
      301 qgltvnhpya tssvasirna fpeffnedgt pvqyeykaya dpsevffrkg lisntsiqva
      361 ggsdntsyna sfgytdeegf tpgnelkkyn fglginssvt dklsikssft faitdlqspp
      421 vnaafgsgps ggipsvfahv lytprsvdlg glpwenpvdr ssvyyrgdng ivnpnwlvrn
      481 ytntsdvqrf fnstsinydi nddffityri gldtytelqe arynrggpss slatqtgyyr
      541 stnitntiwn qdlvfnwnke fsddfgmtal lggnsrydvy sqngvasqgq lafglfrhsn
      601 fgqsssnday tgnnlnrtqe errmgvyanv tldyknylyl nlsarndwts tvepenrril
      661 ypgasisfip asafdwnsnv vndlklrlgy gtsagfpapy rtrnilaqsa rafsrdgsvt
      721 athsvsnllg npnlkpelhe etefgiegvm fnnkltfdls lyqkntrdli tqspidpstg
      781 ftstainigk irtrgvefqa tvtpvstasg fnwnstvnwg lyrsvtvelg ggleevliag
      841 fttlgnfaip gepfniikgi gfdrdeqtgq piilsnglqk paadlqilgd pnprwngswi
      901 nsfsykgftl sammeyrhkg vihsstvtat largvtkdpv idrelslimp gvkedgtpnd
      961 iqitasdyff ggyqgatdep nvfdgsmirl revslgyalp aslvsktpfk raslalsgtn
     1021 lwflalnfpp nmnydtdvlg tgvgnglgfd fvtgpssrrf ggtltlaf
//
LOCUS       WP_092793386             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus hitonicola].
ACCESSION   WP_092793386
VERSION     WP_092793386.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus hitonicola
  ORGANISM  Algoriphagus hitonicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Algoriphagus hitonicola"
                     /db_xref="taxon:435880"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40748
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,72,91,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtigllkepe gerrvallpe svkifidlkv kvrvetqage tafssdenyq avgaeicsrs
       61 etlqsdllls ihtpseeein qlkkgqvlvc qfqplsnkdl vdqllelnit sfsmdnvprt
      121 traqsmdvls smatvagyqa vltaanqspr ffpmfmtaag siipskvlvl gagvaglqai
      181 atakrlgavv eafdvraaae eevkslgakf vkvegakdea saggyaveqs eeykakqqel
      241 iqehakkani iictaqipgr kapvlitket veamapgsvi vdlaassggn celtednqtc
      301 ekygvkiign snlpssmpid askmygknmv nflklmitte gelnlnwedd ivantcvthq
      361 gnvmssrvks ilyptekvn
//
LOCUS       WP_092794032            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            hitonicola].
ACCESSION   WP_092794032
VERSION     WP_092794032.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus hitonicola
  ORGANISM  Algoriphagus hitonicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Algoriphagus hitonicola"
                     /db_xref="taxon:435880"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112875
     Region          26..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilsflwg lalillvsfe afsqnrvvtg tvtsssdglp lpgvtvldkt tqtgtttdvd
       61 gkysisattn svlvfsfigf epqeftvgnq svidvamged isdlsevvvt afgmerdqks
      121 lgysvtqvgg dkftesrain fgnalsgkva gvnvtppatg aagstrvvir ggssltgndq
      181 plyvvngipi esgnlgnagm wggndsgdgl nsinpddien isvlkgnaaa alygaraang
      241 vilittksga qrtgigvsvn snitfdrvwd qtdfqrqygp gidgrrpttq dealntgnng
      301 wgapydgvps vqfdgeqrpy aftgeelsdf fetsytwnns valdggnena nyrfsfsdld
      361 nkdivpnagf krrvvnanin gkhgkftlaa tgqysnqfak nrprlsdspg nanfsmlvrp
      421 gnlpldvmrg ttdkpgaled gtelryqsnv fqtnpywaay qffredetnr flgnmslkyd
      481 itdwlyvqgr igldfqsrvd rtsepygtay kplgdynlte rtirednadl figfnktfgd
      541 fdidgfiggn rmrrtaeslr gggndlvvpf fssvnnvrap sitygfseyg insyfgsanv
      601 gyknmiffna tarqdqfstl tpensklfyp slglsavisd mvtlpevitf akirgswgea
      661 gggapnpyal nltyglvgag hlganlgqin ngsipnsnlg pyrsseyefg adlrffdnrv
      721 gldiayynrt trndilatgi satsgfgstt vnigelnnrg iemllnvtpi aravrwdvsf
      781 nfannisevl slgtnaagep iqfinlgqsr lmrenirhiv gyplgmiagy khlqvdgqpv
      841 ydangfpvtt qgfetiaegr hpisaglsnt vtwkgfrlya lidirqgghm vsgtnyfayn
      901 nglhqetlig rdgnlsvsgv tangeantwt ipanpndpse ylidqywqry amvtenivyd
      961 asfaklrefs fgytfpstit sktpfnnlsl svvgrnlall wsnipnvdpe sayavdgnsq
     1021 gleffglptn rsfgfnlsan f
//
LOCUS       WP_092794471            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            hitonicola].
ACCESSION   WP_092794471
VERSION     WP_092794471.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus hitonicola
  ORGANISM  Algoriphagus hitonicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Algoriphagus hitonicola"
                     /db_xref="taxon:435880"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115267
     Region          33..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekayrfclk ilvifflagl apwsawaqsq lvgvvvdens apipgvsile kgtlsgtvtd
       61 ldgkftlevd agatlvfsyi gyltqeitvt edrildvqlf pavtdlegvv vtalgveknv
      121 kslgyavqev dgerfkkare pnlinsltgq iaglqvnntt alfqdpqisl rgarplivid
      181 gipstdndyw kvnaddvesi nvlkgatasa lygaigrnga lmittkrggq gtqveinsst
      241 lfqpnylvvp evqttygngd ngqyayidgs grgtegfgwi wgprlnqpdp stpsgfvevp
      301 qynsprdpnt geliplplis rgennirnff qrglistnni nitsgtengs frisgsnvyq
      361 kglvpnteln ntsfsvsggy kisdklstda sitynrqytd nfpetpygpe nylynlvlwt
      421 gvdvdvrdlr nywvegqegf qqkhfnntyy nnpyfqayey lrgyykdntf gqvkfdyqis
      481 peltltartg lnnyaldrtd kepksyvkyg rvsrgnfyiy nsaqinmntd lilnyskrfg
      541 enwglnanlg aanrfvrfrs esintdglai pnfynvanse qplsgsnslt kekinsayfs
      601 adidfmnavf ltltgrndwv stlpvannsf fypsvglatt vsdfltmpsf wdfakvrmsw
      661 sqvadgriss npyshiqays tginwngnps lffpgslvnp tirpetsdsy eigldnrflg
      721 grlgidltyf qirdynnlis vpvslasgfs srlengaefk rsgfelmfna lpiqtseltw
      781 evnlnfstyk riltesfdgt drfgnltvge rtdqlfsssq fqrtpegrli ignngfpird
      841 pyqrsmgfsn pdfifgvqnr vtykgislgf sfdgraggti ysltsekmww ggthpgtvnq
      901 frddanegqn tfvadgvvvt ggeveyddfg nilsdtrtya enerpinyia wnkttlnadl
      961 thyfdasfvk lrelsisyql pqqllqrtfl ntanvslvgr nlmlwsnven idpdsgvdnl
     1021 qtpsvrnigf ninlgf
//
LOCUS       WP_092794494            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            hitonicola].
ACCESSION   WP_092794494
VERSION     WP_092794494.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus hitonicola
  ORGANISM  Algoriphagus hitonicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Algoriphagus hitonicola"
                     /db_xref="taxon:435880"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117474
     Region          30..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mianqsiwkg iwafsmlfil nlswaqqvri tgkvsdanna plpgatvlvk gttrgtvsdv
       61 dgaysieasp eetlvfsfvg fetvekpign asiinvslte gfalnevvvt algveretka
      121 lgysvqevqg dqftearetn vinslsgrva gvqitngssg lggstrvtir gesslninan
      181 qplfvvdgvp isnnvvgssg sggqevdygn aageinpddv asmtvlkgpa aaalygsraa
      241 ngailittks gkgkkglgvs insnvtfdnp lvlpqwqdky gqgnngqfef vngagagiad
      301 gvdeswgpem dtgllipqfd sprsvagfrg gdlnasegst itptpwvsqp nnindffetg
      361 vtlsnnvsvs gsnenanirl swtnldqkgi vpntdlkrns ialngginvt eklsinsavn
      421 yqrtasgnrp sisygtenlm ylwvwygrqi ntrnlrdywm pglegtqqfn ynynyhdnpy
      481 ftvfentngq gknrifgnis anykftdkln lmvrtgldty nelrdrrraf stqrfprgny
      541 redavffseq ntdflltyse tskpvwtysi alggnqmrqe nrfqqtvapq llipgiynft
      601 ntavnlqvnq fnsekrinsl ygfgqigykn vlfldvtgrn dwsstlpves nsyfypsatm
      661 savlsdmltl prsisflkvr gayaevgndt dpysltnvfn pqvawgsiqa ktesnrlana
      721 nlkpeqtasf etgidirfle grlgldftyf dnrtrnqiip ieldiatgya sriinageiq
      781 nkgielvlng apvvsengln wnfmanftrt rgyvlelteg ldtytltern ganiqarige
      841 rmgniygvgf lrvedpqspf fgqivhnstg tplrdpelkl qgnynpdwml gfqnnfsyks
      901 lslgflfdyr hggivvsrtk vigstagqle etllgrengy dlsiegngiv slgvvqnadg
      961 syspntvkit srnwhnryye rnnveaakyd asflklrevt igyivpksfl grapiqdvki
     1021 sfvarnlalw tenphfdpet lsmaggtlqp gvenmsfpst rsvgfnlnvr f
//
LOCUS       WP_092802885             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Janthinobacterium].
ACCESSION   WP_092802885
VERSION     WP_092802885.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38574
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaesr pgetrvaatp etvkklaakh qvvvqagagv qasitdeaya aagaqigtae
       61 eaygcaivlk vrapdagera lmasgtvlig mlnpfdadni aamagaglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeek diakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvvkhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_092807633             369 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus globerulus].
ACCESSION   WP_092807633
VERSION     WP_092807633.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus globerulus
  ORGANISM  Rhodococcus globerulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Rhodococcus globerulus"
                     /db_xref="taxon:33008"
     Protein         1..369
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37811
     Region          13..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(25,80,99,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(54,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 metsksaqvr psvgvpress dgerrvalvp kivaaligkg vdvvvesgag lgalipdely
       61 taagakigdp wtadvvvkva ppssdeigki ssgakligfl nprnadnria elkaagiegy
      121 aveaiprisr aqvmdalssq anvsgykavl lassestrff pmlttaagtv kpatvlvlgv
      181 gvaglqalat akrlggratg ydvrpevadq vrsvgaqwld lgidaagegg yareltdder
      241 akqqqaleda ikgfdvvitt alvpgrpapr lvtaaavegm kpgsvvvdla getggncelt
      301 epgqtvvkhg vticsplnlp asmpehasel ysknisalie lmlvegalap dfsdevlaga
      361 cvtreekga
//
LOCUS       WP_092812227             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Roseivivax
            marinus].
ACCESSION   WP_092812227
VERSION     WP_092812227.1
KEYWORDS    RefSeq.
SOURCE      Roseivivax marinus
  ORGANISM  Roseivivax marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseivivax.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseivivax marinus"
                     /db_xref="taxon:1379903"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56000
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeil pgenrvamtp dsarmlqklg heclveagag ekagsldday reagvevvdg
       61 adalwsgadi iakvrpptee elnhldsskt lishfypgsn eelmklaadk gasviamdmi
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqedgsesgg yakpsspefr
      241 eaqlakfrel apdidivitt alipnreape lwtedmvkam kpgsvivdla aerggnckmt
      301 vkdekivtdn gvtivgytdf psrmatqsst lyatnirhlm tdltpkkdgk vdhdmeddvi
      361 rgatiahage vtfpppppkt kaiaaqkpkp kekektaeek raeemaafkq qtkqqvtlla
      421 vgavlmllvg miapasflqh fivfvlacfv gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgsf lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_092820281             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Acinetobacter].
ACCESSION   WP_092820281
VERSION     WP_092820281.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39877
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklisag htvvierrag vkaayidsay eqvgakitdd
       61 aytgsqiilk vrapqgeeiq klapntavia mfdpyrntel dqfaaqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptar dqveslggkw ldvpmsdeek qkaadaakng ygwmpgeqyi
      241 kdqavivdka vsnadivitt allpgrdapr liraetvakm kpgsiildma vesggnvegs
      301 kcgenvvtdn gvtilgipni pstvateasa lyarnvfnfl dtlfdaeknf ainpeeeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_092815672             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Afifella
            marina].
ACCESSION   WP_092815672
VERSION     WP_092815672.1
KEYWORDS    RefSeq.
SOURCE      Afifella marina
  ORGANISM  Afifella marina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Afifellaceae; Afifella.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Afifella marina"
                     /db_xref="taxon:1080"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39986
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,92,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlkepr ddeprvaatp esikkfktlg advvvesgag agssladevf aeagadiaqs
       61 rqaalqgadv vltvrrpeef sgfpegaavv slmdpyghee alkkmaeakl sgfalelipr
      121 itraqsmdvl ssqanlagyr avieaaeayg ralpmmmtaa gtvpaarvfv mgagvaglqa
      181 iatakrlgav vtatdvrpaa keqveslggk fiavedeefk aaetaggyak emsaeyrakq
      241 aelvrehiak qdivittali pgrpapklvd aemvksmkdg svvvdlaver ggnvegvead
      301 kqvvkdnvtl igivnmagqi aasasallar niyafvepmv dketkalsin redqivaatl
      361 lthggavvhp qfggepvnap nek
//
LOCUS       WP_092847771            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algibacter
            pectinivorans].
ACCESSION   WP_092847771
VERSION     WP_092847771.1
KEYWORDS    RefSeq.
SOURCE      Algibacter pectinivorans
  ORGANISM  Algibacter pectinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Algibacter.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Algibacter pectinivorans"
                     /db_xref="taxon:870482"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117081
     Region          25..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lllafvvqlt faqektisgt vsdasglplp gatvlvkgts sgtssdfdgn
       61 ysitarqgst lvfsfvgytt kevaigasnt vnvtlqedae sleevvvtaf gsdrnaketv
      121 yanqtvksdd llsvpsknal ealrgktagv nlstasgsvg sstrivlrga gsltgnnnal
      181 ividgvaidn tstsggagss ttgysdfgnr fndvnpddie svtilkgpsa tslygsrgas
      241 gvvlittktg kgkkmqvnyn gstsmetaiv slqrqskfgq gydnlhldsg enwswgpald
      301 gvvrpwtspi dsdgdgalea lirpysavqd qlqdffntgy titnninlsg stegftyyas
      361 ygntdqtgtl dntsynrnni tfnasaklsd rlksdfkvsy anvkqntaqe gsrafegnna
      421 yamavqspvn iplselrdyk spfhdingyw gsyssvnpyy ilneygnead idnvlanasl
      481 tysfldnlsv tgrfggnivn tqtdiwtptf spaeqivwtd nleqaardtk hsslgeyint
      541 nrkvenldat vmfnyntefs dnltltaaag ynffqrksqr ltgstvgglv vpdvynlans
      601 tqqanssmyr dkyriygvla natigykdaa flefsarndw sstlptenns flygavgasv
      661 iltdlfdikn dvlnyaklrg sygtsgkdad lyllnsyfvg npsiidlgdf alnfpkdgvp
      721 gftignrign pglkpelttt yevgtdlgff knkisvgyty yhsihddqlv tislprstgy
      781 tqtvsnigrm enkghelslt lkpikglvdg ldveffgtys knenevirit ddidelnigt
      841 fgfaagttvs ivakeglpfg tfkgndfkyn dqgqvivnad gfpeypaddv ylgnnqadyl
      901 lnfganisyk gfgfrilfdk kegglfasqt kyntnfngtn vnttvynrep fifpnsvvdn
      961 gdgtfsentt qiteqayftd ydapvstqli dasflklrev efsytfskdl lkntfftnar
     1021 islfgknlkf wlpdenkyad pevngistss sgsvsttgng qgiettqtpa ssslglnlql
     1081 sf
//
LOCUS       WP_092847934            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algibacter
            pectinivorans].
ACCESSION   WP_092847934
VERSION     WP_092847934.1
KEYWORDS    RefSeq.
SOURCE      Algibacter pectinivorans
  ORGANISM  Algibacter pectinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Algibacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Algibacter pectinivorans"
                     /db_xref="taxon:870482"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117148
     Region          21..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiiqlcml laligsthaq ktisgrvtda itnspiafvn iqngnngtit sedgtyqini
       61 tqntnkltfs ylgyktqiit ignqpiinva lsedasklge ivitalglsr dtkelgyavq
      121 ainskslnqv ktvnfldnlq gklagvtvtq gatgvgsssk itirgessfs nnnplfvvdg
      181 ipinnetvfn ftneaaagfq eidfgngame vnpddiesvt vlkganaaal ygtrasngvi
      241 viktkdgsnk kgfsvslsta itvdsafklp dfqntygqgq sgqfeyvdgl gggtsdnity
      301 swgprldvgn lipqfdspvq ladgsfvrga dtalynnlpi latpfnsnpn nlkdfyrtgv
      361 tttnniaisn gfdsgnyrls ftdlrsesii pgvnlnrqtv aaklnfkpss kteintsfny
      421 vnsssdnrps ngygsenvny slvawgprsl ninnlknywq pglegiqqys fnytffdnpy
      481 fillenrnaf nrdrifgnis fkqnitqhls islrtgmdys tetrklqrny ssnrfqngay
      541 aehdvlyrei ntdflvnyqn tfkdfsldis aggnrfnqta stkqsqtvnl aqpgifslnn
      601 aaspievfqf esekqinsly giaklgykny lylditgrnd wssalatpfs vgetsffyps
      661 istsfilsns anlpsafsfa klragiaqvg ndtsayqtsg afvsqttfng eptfsdqnfi
      721 pntnlkpeqt tsyefgadlr ffkdrlnfdf tyynsktkdq iislpvaiss gynqqvingg
      781 evntkgvelv lgitpiknsn lkwnttfnfa snrstitnlp qnngrltlaf sriydsanqt
      841 vwfqveeggr igdlygtgyl knennefiid dngrfiadnt lkkignynpd ftlgwnnnfs
      901 yknwnlnflf dwrqggeivs rtralgnvgg qlaetayrpe egiiaqgvnq tsglpntiav
      961 taesyyrqfy drnheennvy dasflklrqf aigynfklnd gflgiqngad lsisitgnnl
     1021 faitenphfd peqiavqgnn fvsgvedlsy atsrsfgfka ainf
//
LOCUS       WP_092849433             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Modicisalibacter xianhensis].
ACCESSION   WP_092849433
VERSION     WP_092849433.1
KEYWORDS    RefSeq.
SOURCE      Modicisalibacter xianhensis
  ORGANISM  Modicisalibacter xianhensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Modicisalibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Modicisalibacter xianhensis"
                     /db_xref="taxon:442341"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55836
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapketa rgearvaltp esarhiqklg hecfieagag eaagfkdevy qeagvtviqg
       61 aqalwdavdv vikvreptea evewlrqgqt lisffwpaqn ealleqcrak gakvvamdmv
      121 prisraqkmd alssmaniag yravieagnq fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtaaslg avvrafdvrp evaeqiesmg aeflfldfed sadgaesggy akpsspefre
      241 kqlalfreqa pdvdivitta lipgkpapkl wlkdmveamk pgsvivdlas ekggncdltv
      301 pderivteng vvvvgytdfp srmatqasll ystnirhmlt dltpekdgei vhnmeddvir
      361 gatvthegei tfpppppkvk aigsskpker pkeptpeekk aaehaafvsq tkrqvgllva
      421 ggvlmwllgl vapasfmqhf ivfvlscfvg fqviwnvshs lhtplmavtn aisgiivlga
      481 ilqigsgswl vgllagfsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_092850168             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            miluonense].
ACCESSION   WP_092850168
VERSION     WP_092850168.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium miluonense
  ORGANISM  Rhizobium miluonense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium miluonense"
                     /db_xref="taxon:411945"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40529
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msnlvfvake svaeetrvaa svetvkkmrs lgfdvviead agalsripda eyeaigarig
       61 svddaktadv ilkvrrptsa eiagyksgai viaimdpygn eaaleemara gltsfamelm
      121 pritraqsmd vlssqanlag yqavidaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg alvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemseeyqa
      241 kqaalvadhi akqdiiitta lipgrpaprl vsrnmlkamr agavavdlav erggniegae
      301 ygkvahvegv rvvgypnmag riaasasaly aknlvtflet mvdkdskslg lnradelika
      361 tmltddgevv hpnfvdpdqp tvnkgdl
//
LOCUS       WP_092852484            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algibacter
            pectinivorans].
ACCESSION   WP_092852484
VERSION     WP_092852484.1
KEYWORDS    RefSeq.
SOURCE      Algibacter pectinivorans
  ORGANISM  Algibacter pectinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Algibacter.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Algibacter pectinivorans"
                     /db_xref="taxon:870482"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117262
     Region          36..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkikrhga gsgivlmlai lfssfsaisl eaqeritgtv agadglplpg vnvlqkgtrk
       61 gavtdfdgny siqlvsgqkt lvfsylgfqt qevevsnkat vnvtleedva gldeiviigf
      121 qavkrekilg avetikseei qkaapvdplq giqgklsgvq vvsnngpgeg fdikirglst
      181 lsagatgply vvdgqqtfni dnidpndies levlkdgata aiygsqagng vviiktktgk
      241 vgklslditt vtgvnrligd lpaanaaqri eqerlqnttw gigggrdsls lvsrnsfdvq
      301 rlvtrpalrh qtnvalsggs ekakfywntg ffneegliin sehkrvntrl kvdvtpsdkf
      361 klgtlvnlsy eytnsistgp vlghllnrva ylplfepdgs ftpgspnkfs lnpiqnavlr
      421 kndrrryrgn vfnyaqfsit pelsirstlg vdffldrrdn fapaildprn fengihrgdq
      481 rqtltyqiqq dntlnylksf gnhdvsafag mqiqrrkvdn fnyaaqfnnd liqtwnnavn
      541 dpgvdtetgl dnntffvdke ggdrtqivtt gifslfggfn ydyankylfg atirrdgsss
      601 fgannkygyf psatagwrvs nenflknnsv iknllvrgsy gitgndriqp yryvstlgps
      661 diggfipltl gnadiqwees vsknfglels lfkgrrlnia ldvwekvtdg llveselpee
      721 sgfssvlenr gviknngvdf tiggtiikst dftwrsqfni svlknnveel avpirtgrfi
      781 teegrpvgni wgykntgvyq ydesnaytpe gerlfpnfda ngfflgsynr gngdaypada
      841 eirqlvhrss rnvlrggdyi wddvnndgfi dsedeqvlgn glptvyggfn heftyknwtf
      901 dtsfdysfgn eiyrrydhdr nslraavlsv spdrlqnawr eqgdiaqwpt lqpggarnqn
      961 rfdfsnstan ssfvsdgsfi kwryirvgyt fpkdvlesfn igmnrlslnl avnnimtwtn
     1021 yigynpefgs rgnpltpsed slrypndref lltlraqf
//
LOCUS       WP_092853222            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algibacter
            pectinivorans].
ACCESSION   WP_092853222
VERSION     WP_092853222.1
KEYWORDS    RefSeq.
SOURCE      Algibacter pectinivorans
  ORGANISM  Algibacter pectinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Algibacter.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Algibacter pectinivorans"
                     /db_xref="taxon:870482"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124280
     Region          58..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfqyllk ktlfimslfl tfsqsyglky vkhandidin ffekkwkesn vkflqqsieg
       61 vitdhnntpl igvsiiikgt akgtttdfdg kfsinakvgd vlllsylgfg dvnliidsrt
      121 fydikmnssa eelegveifs tgyqnvsker atgsfskidt kvlerkidqs iigkiageap
      181 gvqfdpfiqe knniglvirg rssinattep lvvvdgfaip ggfstinpnd vetitilkda
      241 aatsiwgira angvivittk kgennrklsi nlslnssvtl kqnvfkapya dpntqvdyqi
      301 glfnfeqysq srnlfdgtln efslfqtnsv retllrlqrg didiatadsr inalrnndgr
      361 eeysklflrq rlwnqynlsi sgggekynfn sslvynqnkg aivkdksdqf ilnvignykl
      421 tsklkarfss nisqtkneng igtgpvdyli nypiferild dngnylpmqg gvnvessqla
      481 qrqgypypwt fnlkqesdnv dntststdir iqtglnyeva kglkidlsyq ylwssffgrn
      541 llnenrfttr nlvnsfaqvd engevietpv pagslldist rsttdntfrg qlnystsfkd
      601 gihsidaiag yevrkqitef nrdrkfgynd qsliftqpnf ntlypspifg gqrlinsnsr
      661 ltfnenrfls yyvngaynfn krytisgsmr lddtnlfgas defrniplfs vglkwnvtke
      721 nffnsvffnn lnvratygsg gnvdrntspf lvarqgrdqg sflnnyltis nppnptlrle
      781 ktktlnlgvd fsmaknriyg sveyynrtse dllarrnisp tyglsssfln vaelynkgvd
      841 idlglriidt kdfkfdtril ysqnenkits idesnpgeif lftqydansf vvgdpidnfy
      901 sfryagldqq gnpsffnenn diievggdig aiealksegs rsptrtgslt ntvtyknlsl
      961 rvltvysggn rfrfernydp rffrtnvfsd yvsrwqqpgd elltdvprls spnetqtply
     1021 lyldesdrnt ddasyvrlaq vnlsykfpqn ltkklsmnsf tvslqadnlk vwnfnkwdvd
     1081 pvsrtipipp tftlnltttf
//
LOCUS       WP_092863592             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Albimonas
            pacifica].
ACCESSION   WP_092863592
VERSION     WP_092863592.1
KEYWORDS    RefSeq.
SOURCE      Albimonas pacifica
  ORGANISM  Albimonas pacifica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Albimonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Albimonas pacifica"
                     /db_xref="taxon:1114924"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55328
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigapaeif egekrvaltp esakrlqklg yeclvqsgag eaasfkdeay aeagvtvvet
       61 aadlwsqadv ivkvrapsde eiaaapegkt lisfiwpaqn eemlaalnak rmtvlamdmv
      121 prisraqkmd alssmanigg yravveaann fgrfftgqvt aagkvppaki lvvgagvagl
      181 aaigaaqamg avvrafdvrp evaeqiesmg aeflfldfed sqdgagtggy aapsspefre
      241 kqlelfraqa pevdivitta lipgrpapkl wtedmvlamk ngsvivdlaa erggncdltv
      301 pddkivteng vtiigytdlp srmatqssnl ygtniahmms dltpekdgkp vvnmdddvir
      361 gstvchqgei tfpppppkvk aiaaakpkek vkeptpeekk aaelaafkkq trsqvtllav
      421 gaalllgvgl vapasfmqhf ivfvlsvfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgswi vivlaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_092884473             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseicitreum antarcticum].
ACCESSION   WP_092884473
VERSION     WP_092884473.1
KEYWORDS    RefSeq.
SOURCE      Roseicitreum antarcticum
  ORGANISM  Roseicitreum antarcticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Roseicitreum.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Roseicitreum antarcticum"
                     /db_xref="taxon:564137"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55083
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkety qgearvamtp dsaaqlqklg hecliesgag vaagfaddly ksagvtvvdg
       61 akslwdaadv vikvrepska eaamvrssqt lisffwpaqn eemlnlfkdk gatavamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv livgagvagl
      181 aaigtatslg avtyafdvrp evaeqiesmg aefvflefee aaqdgaatgg yaapsspefr
      241 ekqlekfrem apeidivitt alipgrpapk lwtedmvrlm kpgsvivdla aekggncdlt
      301 vmdqkivtdn gvtivgytdf psrmaaqast lystnirhml tdltpnkdge ifhnmeddvi
      361 rgatvthnse itfppppprv kaiaaakpka peksagekaa eaaaamkkag rnqiamlvig
      421 gvlmlligtv apasflqhfi vfalacfvgf hviwgvahsl htplmavtna vssiiilgal
      481 lqigsssiiv tllsaiaili asinivggfm vtrrmlamfq ks
//
LOCUS       WP_092864034             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hyphomicrobium facile].
ACCESSION   WP_092864034
VERSION     WP_092864034.1
KEYWORDS    RefSeq.
SOURCE      Hyphomicrobium facile
  ORGANISM  Hyphomicrobium facile
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Hyphomicrobiaceae; Hyphomicrobium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Hyphomicrobium facile"
                     /db_xref="taxon:51670"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39557
     Region          2..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvtiavtsep adeprvavsp dtvkkfsalg arvrieqgag lrsrfsdday raqgaeivsr
       61 adalsgadil lavrrpsaed iralkpgaiv agmidpfger aglealagsg gtvfsmelmp
      121 rttraqsmdv lssqanlagy kavvdgaamf gqalplmmtp agtvpaaraf imgvgvaglq
      181 aiatarrlga qvtatdvrpa tkeqvqslga kfiaveddef kqaqtaagya kamsaeyqak
      241 qaelianhik nqdlvittal ipgrpapkli tramiesmkp gsvivdlaae rggnteltea
      301 gktietpngv kifgplnlag tiavnassly arnllafvet midkkektla vnwddelikg
      361 tlvakdgqlv hpnfatkas
//
LOCUS       WP_092895181            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092895181
VERSION     WP_092895181.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116072
     Region          25..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknyamtll fllgflasip lyaqqtikgk vtsqedgmpl pgvsivvqgs skgtvsdldg
       61 nysisvpgse svlvysfigy etqrkiagnt teiniqlaed vsqlgevvvt algitrders
      121 igyatqevkg enltytkeqn vlgslsgkia gvqvtgssga smggtqkiki rgvnsisggg
      181 eplmvvdgtp isnsnfsgss gqdygnlgqd inpedietin vlkgpaasal ygirgqygvi
      241 mittkkgkkg sdvkvelnsa vfvdnvsnlm pyqnlygggs sqtwrtlpng dkyvdmsvde
      301 swgpktdgtl vrqvmsfypq dptygqltpf vaypdnikdy yetgtnvnng vtitgggass
      361 nfrvslndtr iqgvepntsl krnnvgvslg vdltkklrls tnvnyaanqg rrpgqgsedg
      421 srylgqwfqr smdmkrlkdy kyddgtflnw nlrrpststg evtnfnplyw anpyflanen
      481 fsddnrdrff gdvglsyqis selkvsafvr sdmytqnins rasfggtgnp gysvgkyqnt
      541 emnyellaqy nkvwnkfsld anvggniydr dysylsmatv gglsspgfyn inasidrpvt
      601 ssyqqnkqik sayamvslgy nntyfldasl rndnsstlpv dnnsywypsl stsvvfsewi
      661 ksdvmtlgkl rlsyaqagsd lspysttsff nvgstytgss tvntlsvpdn lnnpnikpsf
      721 ahsyeagvdf kfyegrvgls ftyynqrnen qilnldisgt sgygsatina geivnrglei
      781 altatpfrsd nfnwdmsfni srnrnevvel ypgidvyqyg sttysstssy lnsyvgkpfg
      841 slvgqayqrd eatgkillgs nnlplytdat hdfgtvlpdf nggfqnvlny knfqlaamid
      901 fqaggqffsr skmlavrtgl dplsaaindk gmnvrdplad gggvkvegis aetgedvtay
      961 vdakayygvv arriyedwly dasyirlrev slsynfnksq fanlpvenvk valvgrnlgm
     1021 lfqnapkgin paelstgsqa igwyesgqlp svrsfgfnln vtf
//
LOCUS       WP_092896149             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus aquimarinus].
ACCESSION   WP_092896149
VERSION     WP_092896149.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40305
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvlketk tgekrvalsp dvikqlikke fsvaveqgag tgsnfsdedy keagavvgsi
       61 qdvfasdvll kvnlfskeev aqmqngsacm simyaynype ildemnkksi msfsmdavpr
      121 israqkmdcl ssqanlagyk svilganyle kifplmmtas gtitpakvli fgagvaglqa
      181 vatakrlgav vevsdvrpet keqveslggr fltvegadev kveggyasev saeflqkqke
      241 liqskikdsd lvittalvmg kkspilvtee mvksmkkgav ivdmavesgg nceisekdqi
      301 vqkygvtiig esnlpsllst nasqlyatni stlllhlatk dgfnldreee itkgvlitye
      361 gqvvheftnk ilnk
//
LOCUS       WP_092894654             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092894654
VERSION     WP_092894654.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108821
     Region          30..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnyllkqkt fllaialifc atlvanaqtr tvtgtvmdpt igesvpgatv lvkgttrgta
       61 tdldgkftld lqqgdqiliv sfvgyipqev eignkttfii nleediqsle eavvigygtq
      121 dkkeitsavv aikpedfnkg nvsnpaqllq gkvaglsitr pggnpnsgfn vrlrglstfg
      181 anssplivld gvigasmdnv dpndiqsidv lkdgsaaaiy gargssgvil itttkknpkd
      241 grvsvslnsf gtmdqatnli pilsaeefva rggtdfgsst dwrnelidda fsyttnasvs
      301 ggfnntnyla avnyrdnqgi vngvsnkrln trlnlsqgal dnrlrlnvnl sftnidresi
      361 ndaafryatl ynptapifen tqdaverfgg yfqrdlfdfy npvalanqqk fvsetksalt
      421 syraefdilr nltisaqysq drsntlsgdf wsrldynvgl gtggsaqrrt ndrvqkifes
      481 tlryeldlsd glnmtllggv atqstknqgf narvkqylfd lgwdnlgags irlgnstdla
      541 syanedqlns ifgranfnln nrfflsasvr aetysgfgan nqtgvfpavs lgsdftqifd
      601 mgifsqfkpr asfgitgnlp psptlalgvy gngnrvdldg dpltqsdvfv givqnsnpnr
      661 dlkwetkqem nfgldfgiwn nkvtgamdyy irnisdllfn vpvatgapnp fdpgrfntas
      721 stwvnladlr aagfefavta hdihlgnikw hpsvnftlyd kttieslsag dlgfdelrfa
      781 tpgspgqnnn pivynrvgqt lgdfygpvle gltedgkyil sttdpnefek lgnglpkgef
      841 gfannfeygg wnlsfffrga wghdlynsyr gfyenqdass ntwnsvitdk tqvvtstptf
      901 nssyienasf irldnmelgy nfktpsknln sfriyfaaqn lftitdytgv dpevritdse
      961 ngdgfttsls pglerrntyf qtrsftlgls lnfk
//
LOCUS       WP_092895717            1207 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092895717
VERSION     WP_092895717.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1207)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1207)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1207)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1207
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..1207
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133109
     Region          118..1174
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meitftkkhl lhlgrawlml mmllpnwvqa aelgqdkiil issnslplkq fisevesqse
       61 ykfiyadgih eqlsqkitvs tkatiqdllk evavtspfef kvmgenilir kpqteksfpv
      121 tgivldetdl plagatilvk gttngvitni dgkfsievpt kesvlifsyv gfetqefavq
      181 nqtffsvkll ptfadmegvv vtalgierde rslgysvael dgnafqngsq dnalksiagr
      241 vpgvsvsstg gagssvsmvi rgisslsgdn qplfvvdgvp iinslnnise igsenkvdyg
      301 naisdlnped iesmsilkgp saaalygsra gngvvlittk sgkkvndvtv tvssntllem
      361 pykylpfhsk fatgvrpytp dnnpypggql vieegssaga gpeldkgyta iqwnspldad
      421 gnriptplvs hpnnvsdfvr tgvtttngvs vannnefiny rigytnlsnw giipnsdfsr
      481 nnlsinttlk vnpkltlsss lninqtgsdn rpagnrgtnp leaaykvsph idinelksyw
      541 vpgqegiqqr sqaigdynnp yflayevnns ftrnrvfgni aldykfsdnf nvktsymldm
      601 yserreskip msytgdpngg yglvnldrme rnidilgtyt kdfnnfhmtl sgggnlrfnd
      661 nnsvqnstkp egsglivpgv ytlsntssen liytsstsqk avssvyglan fgfkdliyld
      721 vtarndwsst lpeanrsyfy pssslsliln emidmgnsid llklragwaq vgndtdpynl
      781 yqvlsnngew dgqtrltvpd nlktpdlkpe iatsyefgle lialqnrlkf dvtyfntdnk
      841 nqilpvtlps ssgftskyvn aglvnskgwe vmlgvtpirt ddltldlsfn yskyrstive
      901 ltdevdvfyl wsdsrggawt yvgdeigdiy drglvtvedk espyygypil dedgswnavn
      961 qataknkign fnpdflagmq vnlrykrlsl slnfdwrqgg dfvsqtyrys esdlktqrwl
     1021 dqmidpsgmq gkelrdylva nqgqfitdgi nvvggptaes ggypieynvt vndgvfnpgv
     1081 iaqyddqgnv tgyienlgee atkfipyadn ypwsffapat fdasylklre aainyqlpte
     1141 fvhklkmksi nvgvytsnli lwtkakvgid penafqpean gtfkqgiery nvnpwvipvg
     1201 fkinasf
//
LOCUS       WP_092896344            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092896344
VERSION     WP_092896344.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109267
     Region          26..1019
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvlsiafa lgfmlcavhl vqgqsrvlkg vvtaapdglp mpgvtildks sktgtttnve
       61 geyslsvgpn svlvfsfigy ssqqievgnr telnvlleed aselsevvvt algiskdket
      121 lgysvtqvgs eslttaretn vanslagrva glvvkgtnsg pggtskitlr glpsisgtgs
      181 plyvingipm dntqrgsagq wggadagdgi gnlspddiet mtvlkgqaas alygsrasng
      241 vilittkkga kggdwsltyt mnvmaenpvd ftdfqnvygq gvggmkptta tdaqtsgrla
      301 wgskmdgssv igfdgnqypy spsndryidf yrtgtnftnt vsiskglgsd gsfrmsvsnl
      361 daksivpnsg vdrlsinlnv eqnitdkftv tamvnytdqq stnvpnlsdg pknpnnflll
      421 apniqqsifa pgynpdngae tvfsddiyvt npyfisnqgv ndigrkrtis aistkysftk
      481 diyamirmgn dasnddffgv dpsglaysan lqgglsgrgq strsetnidg ilganfdlts
      541 klnldllaga nrrnnkfesv gvggsrfvip ylyspfnven fsrsygyner evqsayysvg
      601 igynniltlt ttgrydvyst lptdnnsifs psvaaafvfd qlidmpaldf gkfrasyavt
      661 sgepfdayqs tfyynsansy ngvpagsspt slpnlnlkpf ttselelgld lsffnnrlgf
      721 diayyeketh neimnanlsi tsgfnssvva tgstsnkgle vlvtgtpvqt pnffwktsfn
      781 lskvkneils tdpnnnpinl gqnrgtlgna itayvvgesg pqiraydyay ntdgsikvne
      841 aglpvrgeli nmgtvlptly ggwnnefnyk gvsfsflidy nygnkvlsat efysifrgln
      901 qvtlegresg vttggvtapa qayyqalaqn vtstsvvdgd fiklrqltlg ytfpakwfgn
      961 tpvlkglsas lvgrnlgfim rkaknidpea nfgsninytg ieggnlpstr sfgfnlnfkl
     1021 n
//
LOCUS       WP_092896408            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092896408
VERSION     WP_092896408.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120608
     Region          26..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilsiafa lvlmlgytat aqtqkrvlkg vvtskedglp mpgvtvldkt nqtgtttdld
       61 gkysisvgst svlvfsfigy aaqeylvgnr seinlslaed ssqldevvvt afgmekaqks
      121 lgyansiika delvktgtsn vasalygkaa gvkinagagg atsavniqir ginsitgksq
      181 plivldgvpi rneevtnnny wgdqrlrgng lldinpadve nisilkgasa aalygseavn
      241 gvvlittkkg kagkkgmqvd fntsysvdei aylpryqnvr gpgmpsqvqn lgqaedgfny
      301 tadgvrtvpn tttnygpvfd gkpmlawdgv arpyvaqedn yaalfnnpvs sqvnvsisna
      361 tdksdfrlsl trqdnealsl nsknskniin lnsgyqvskr lktdlminyi nqntknrpys
      421 idrminnfgg mmtrfdngaw yldkyqtsrg yryvtgngqs ltpdenitgn gfrgdiadyv
      481 wrvnenrste lsnrvigslt ntfqiteeln lrarvstdft srysenenst erplafgpsg
      541 sfgmqselfn ilygdlmlny kkaitdeitv gamigytart esfssigrst sgglstenlf
      601 dvvastnlpn nnsgrsyrti dafigtanfd fkntwfvegt irrdrvstmn pdnnafiyps
      661 vntalaisda fdlpefitfs klrgswgivg nypdiyrani aysqntlgvq qtgganvlyt
      721 tlsssfgndv ikpeqkhefe fgldtrffnn rfgidisyyn aqirdqilpl tlpsssgats
      781 vltnigtlrn agveiqltgd ivatpnfkwn aiinlarnvn kveqlangat ellhadydgn
      841 aaqlrsvvgr pmgdfyarpi aldangdkiv qpnglykidd qswiqvgnam pdatggiinn
      901 vsfknfslsa vmdfqiggsv mptginwmis rglteeslny mdeasgglay yknadgqgvg
      961 vshstaqgpn getvyhdgmv mdgvvadgsn nnnvisqayy ywntynwggp qysqsryely
     1021 iqdndyikmr elslayaipn hisskigasn vnisvygrnl fflyrnikdl dpevltggsr
     1081 wtqtltsagt npatrtygvm lrarf
//
LOCUS       WP_092897654            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092897654
VERSION     WP_092897654.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115832
     Region          29..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrykfyknlw fivfllcisv tvayaqevqi tgtvldetdm plpgvtillk gtttgtttdl
       61 dgkysisapr tstlvfsfig ydpleievgn qsvidltmnp nasdleevvv igygtakkrd
      121 itgavssvnp sklenenpns vqdilrgnaa glnvgistsa kgggslqvrg qtslnagnsp
      181 llvldgaiyy geladinpnd ienlevlkda saaavfgaka angvilittk kgtvgksiik
      241 fnanaglatm atypdvygpd efiswredvf ksinaggydp yefsdprklp sdvsledwma
      301 ydgssgdpvt vwlqrlnmqp eeiknylagn svdwrdkifq tgfrqdytvs lsgrtdniny
      361 ywsvgylnne giiigdeyet irtrinlegk vnkwltvgmn vqfatqdqsk vpvssglyrt
      421 lspwgseyne dgtykwrpnd eqsggthpfy drtyidrtdr dvninstlfa aiklpfgfnf
      481 rtnftprfey yeyfnhqsae hevwgasggi asrrqrkeyy wqidniltwq ktfaekhdfn
      541 atflvnaekf qswdntmtnn gfephdrlgy hniggginpi issndeystg dalmgrliys
      601 ydgkysttvs lrrdgysafg qsnpralfys aavgwvfsde nfvnidwldf gkmrfswgsn
      661 gnrdigryva lsdlntgkyf yqrpsgelyl vnqlyvnrmq nsnlqwerte sfnlgidfsi
      721 lktrltgtie mykmattdll vqrslpdflg fnyvwdnlgq vdnkgfeltl nstnfetknl
      781 twrttanfql nrneivslyg dldengveld dpsngwfigh aidqiwnykt dgiwqsdeae
      841 aaaeygvkpg dfkvvdvdgd gkftnadrqf qgyteprfrw slrneftlfk nldvsfmmys
      901 ywghegsfnq mknrdgfldr tssyvtpywt eenpnnewar lnssegsagg ysiyrkksfi
      961 rlenismgyn fpkqiiekak itnlrvygni rnvgffapew dfwdpensgp ipryftlgid
     1021 vtl
//
LOCUS       WP_092897994            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092897994
VERSION     WP_092897994.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119172
     Region          29..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskiifilml cgymqltann vfaqevsdis gevrsasdre plpgativik gsssatitda
       61 sgrfsfrtaa ervvlqvsyl gfvgldttla lpldrelylf lqadelvlse vevvstgyqe
      121 iprerasgsf aqvgqelvnr kvstnvmdrl qditpgvifn rsnasndpis irgrstifan
      181 tmplvvidnf pydgplenin pndvesftil rdaaaasiwg aragngvivi ttkqgkrntg
      241 prvslnsnvt vseepdllyt pqmssedlig lermlfvkgf yksseksink talspvvetl
      301 iaerdgviss qeadrriady tnhdvrnelq khyyrprlsq qyslgisggg erntytvsag
      361 ydgidesivg nsrnrltlna kntwhflkek leanvglyys rsdistatdi pptyaydyle
      421 gpdgsslpvt rgysrrfieg veqglldwnf ypleeigkld nksltadmrv nvglsykifd
      481 gfraslshqy wnnsfsqrnh rvessyfvrd linqytsrag dgslyrnipe ggildinsln
      541 gmshnfraql sydktlgagr ltalggyeak slenigdwtr yygyddengv srlvdnmsrf
      601 rryynnslas ipsyaghsgt kdnylswffn tsyvfhkkyv fngslrrdas nlfgvrsnqk
      661 avplwsvgas wviseegfwk ssglpflrlr ttygyngnvd rntsafttar yvsadafsli
      721 pnlpyafivn ppnpnlrwer igilnialdf etldgrirst veyyvkegkd ligdspvaps
      781 tgktlfrenf adtrtkgwdi eissanlqgr lewdtrfifs avnekviyyp ddirastylq
      841 gstrllpqeg kplyqllslp fagldpengn pliykdglps ddystilssl tvdeliyhgp
      901 srprfygslm ntvrwrnfsf sanmsyrlgy fyrretvnys niligrishs dyvlrwqqsg
      961 delvtdvpsm ptvnnfnrnt vmaygsnlve rgdhirlqdi rlsyslkrse lpclpfqsae
     1021 fytyadnlgi lwkfsndpld pdfrtqkplg svavglkvnf
//
LOCUS       WP_092898335             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092898335
VERSION     WP_092898335.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107010
     Region          24..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miykplltlv flilsigisq aqytvtgnvs dertgetlig asllikgtts gtitdldgnf
       61 tlpipnsngv elvissigyn sitlkvspsq ttlnitlkqd atnldevvvt glassvkrsn
      121 lanavstvsa rdltgtttiq tadgalygkv agatirsngg apgggmsiql rgissltgas
      181 qpliivdgvy innsfqstgr aavsgaggsn qddgsnrlad lnpadienie vlkgpsaaai
      241 ygtranagvi iittkrgveg rttvslsqdv gfanplnllg vdnwseekin fffpeqtraq
      301 elerfraaqa sntfidyedy fynnqatlln trinisggdd ktkffvsgnm tsedgtikrt
      361 gfdrysiran idhkiapwik lgvssnyins stdrgftgnq nnsgasigys iaytpnyydl
      421 rrnadgtypt npyfsenpva vtdfgennss vnrfiqaftl didilktdkh flkaqiaggl
      481 dflnnatevy lpeflqfqss qanpgdifvg rqeslntnfq aalvynwnvg rvnmnsqagm
      541 vrldfqnhsl fnrgrglvpg qknlkqaavq einsefesev qeagiflqqe mnfedkiigt
      601 lgirwdkssl ngnpneffaf prasmavnia nfdfwnssai tllkpriayg etagpvpfgs
      661 tytplggtni ggllgstvat signtaiipe taselefgvd vglfnnrfsl eatyyikntq
      721 nniqnlnlap stgvnttpsn eaelsnkgve lglsgtilek snirwfsrvl fwkntiemtr
      781 lgiptylsgg fgsglgtfly aegyspttiv gtpadpsvpg gftvwgdaqp dfnlsfsnsi
      841 slykgielsf lidwrkggsn inltsflndg ggttngwfdd dngdgipngr qrepepynna
      901 grwiqdasfv kvreiglyyt ipretitqwf ggtvqgikvg ssannafmft kypgydpets
      961 tfgaqavqnn vdiapyptsr riffhltldf
//
LOCUS       WP_092900064            1155 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092900064
VERSION     WP_092900064.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1155)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1155)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1155)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1155
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..1155
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126076
     Region          138..1154
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlikftryll vvgvtgvlal plsaegqnlt qfakgptltq kldtknlest lkelediysi
       61 siaypsslvd aqtkipaain skltaeenlq rilkgsqihf rkgagdfyml eqsyaapkap
      121 ssspnlsyqi pssqktervi sgvivdeeqi pipgasilik gtmngvvtdi dgkfsltlpd
      181 dspnailmis figfttqeik vgstsiftie lassdlalne vvvtafgler dkkalgystq
      241 svdgsaltes rptnvansls grvagvqvtg nsmpgsgahi virgsssvag nneplvvvdg
      301 vpleqtssrq ygnglseisp dnikemtilk gataaalygs raangvimvt tkngsgskgl
      361 giefnsnmtf dnplvkpdfq ntygggtgyr twyvdgrngf dadgirgtag vdeswgapmd
      421 grmvplwysa pekvallpqp nnyddfwetg qslsntials ggndqgnfrv sigrldqtsi
      481 madndyfrnn fkintsykfi pklqmsvnae yvksgsdnrg ftgsqdfiwa hrhtdytklk
      541 nwedyydtqk ltfregddyp yanwqheyfs npffnqkylp nsnekdrlvg sialnydise
      601 nfsilarsgt dywsdtrini nsaesfknnv krfgsysesv lnsqetnsdv iltfdkdllp
      661 rlslkiqaga nnrvnnykst svsvgqltid glynlgnyas pvtpsstirk qvvnsvfgsa
      721 qfgfnnylfl dvtgrndwss tlptsnnsff ypsvamsavl tdifdvqsgf lsfakirgsi
      781 aqvgndadpy llnqvysseg lwagttptys esseianrtl kpeittgkev gldlrffegr
      841 agidftyyhq stvnqilavs istasgyssq ilnageitnq gieltinatp intasgfswy
      901 talnfarnrn kvvelaegle nyilgtqnsl tsearvgqpy gslygrrylr spegelvynn
      961 glpvleegty tlgniqpdwi ggwtnsltyk glelntlvdv kmggdifdvg tglarktgqy
     1021 aetaigreeg vigqgvmnig tseapvyvpn dviasagtfw naqnprtyhe sgifdgtfvk
     1081 lrevslgyvf pkrflgnkfi qtmklsfvgr nlailyknhp hmdpevdmkg gngqgfaygq
     1141 mpttrnlgfn lnvtf
//
LOCUS       WP_092900231            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092900231
VERSION     WP_092900231.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117067
     Region          24..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktftvitl lmmllptvll aqvqvkgkvs dskgeglpgv tvlvkgtnkg tvadfegnyn
       61 imadesavlv ysfigfeaqe eaingrsiin itladdskal devvvtaigi kqqkkklgya
      121 tqevpmdvia eastlnlgna lsgqiagltv nnptgmfqsp sfslrgktpl ivldgvpvet
      181 dffdispeni esinvlkggs asalygargk ngailitrkn akkdgltvta ttnnmvtagf
      241 tvfpetqtay gngsngkyef wdgadggisd gdmiwgpkfe pgvlvpqwns pirnkntgev
      301 vewygsvtgt vyddkstyer vptewkrhdn lndfmrtgvv tkndisiayq gekaqlmfsa
      361 nyayqqgqvp ntsvntggfn fnssfklsek lqldatlgyn kvyspnypry gygpknhmyt
      421 iliwmgddvn gqdlrdhmyv pglegyrqan ynyawynnvy faanelnqvh nrnvmdgklk
      481 lkyqimpnly vqgrisarqr tlfedmqspk symnygdsrn gdykfwnddq lnldtdflaa
      541 ynkdfnekig ltvnagassf yrsykqayss sdglivpyvy slnntqgpvq asnyleekei
      601 rsvygsmgvd lwqsiflnvt arndwsstlp kannsyfyps asisaivsef mnlpkaidfi
      661 kvygswsevs sdlspysiys aynkgvtygs tpsvsypssl vnseimpqks ttfeaglsts
      721 fakkrltleg tyyrildenq iidlsiseas gyssrkvngn eyttngfelm mnyaaiqkdk
      781 fswniganwt kferkitgiy gdddnfgnlr vgdradsyya tvwqksadgq vildantglp
      841 trdpfltkig hldpswrfgi qnqfninkfr iamdvdgawg glirsltiek mwwggkhpns
      901 tqyrdeeyat gkpvyvpegv vvtggelvrd vdgnvlsdtr eytpnttavs wqtwsqtypy
      961 raqvtedenk tfanvydrsy lklrrlsvty dlmnimqskk iknldltlyg ynlfvlkklp
     1021 yldpdfgndn nlqdpssryv gmtlkavf
//
LOCUS       WP_092901343            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092901343
VERSION     WP_092901343.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111929
     Region          23..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilllgls lflvsavafa qgrkvtgivs sgedgqpipg atvlvkgtsv gtatdidgky
       61 altiptdgkv lvfsfigtnt qeiqigqqsv idvvlqpdvq slsevvitga agiesrriem
      121 gynatsietr dvaqgraanv aagltgkvag lqinttgsgv npnvrvilrg srsltgdnea
      181 livvdnvivp nsilgnlnpq diqeitvlng anaaalygsa asngaliivt kkgksgaprv
      241 tvghtvnleq vsfypqiqds fgsgyaggyp hdyvpyenqq ygprfdgsmv eigkpledgs
      301 iqtvpyantn skndfwetgv tnqtdlsvsg gddkstnffs aqyltndgtt pgdqytrasi
      361 rfnstrkftd klalnvstny vqnryditta tgsmydqilq tpahipltsy kdwrndpfan
      421 pngyyneyyd npyfqadnsr qnsgndyivg nvelkykplt wvdftyrvgi snrsyynknt
      481 tgkftftdyt kgissaktdi aggvsdgagy snqlisdfli nlkkpvgedl ffnlllgnql
      541 rknqsksvgv sanglvipgl ynvsnrvgea gasesnfess qigvfaqfkt aykdylflel
      601 tgrndwvstl skanrsffyp aanvsfvasd afpsikgkvi sqfkvrggis qvgqvnldpy
      661 qldptfspss gfpygslsgy sldnrlvaad lepeittsfe lgtdfilfdg kvngaftyyq
      721 setenqtist gvssatgfss ylqntgivan qgfetmlnvt afarnnfqin iganytfndn
      781 yvkeiaddld rlalssggna qvyaiegqpy pmligsvykr ddqgriivda nsgypsvaeg
      841 qvqlgntqpr hrlglnteil ykgfrlyala eyrggyniyy sgggsfdfsg sgitttyfnr
      901 erfvipnssy enpespgtyi entnvtvtdg gagfwtdgsf rrnvaenyli dgaywklrev
      961 aisydfpasl msrvgfiqga titaqgrnll iftpnsniyt dpdfnfsdgn avgivtlsat
     1021 pptrfyggsi tltf
//
LOCUS       WP_092901629            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            aquimarinus].
ACCESSION   WP_092901629
VERSION     WP_092901629.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus aquimarinus
  ORGANISM  Algoriphagus aquimarinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Algoriphagus aquimarinus"
                     /db_xref="taxon:237018"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119662
     Region          27..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllillms fwliglvhaq elnqmairgl vidqdsrlpl pgvnvlikgt ikgtitdekg
       61 efilpatsgk yllvlsfigy lkqeievdip qlspvkvlls vdeislasve vlstgiqeis
      121 aeratgsfsh lnnelisrrv stnlldrmed ltpglvfnrd radlakgesi sirgqsslfs
      181 dtqpliildn laydgaieni npndvesitv lkdaaaasiw gakagngviv ittkkgklgs
      241 plivnltsns tlgqsfnpfy apqmsvadfv eveqrlfhqg vydgdynayd qkklspvves
      301 lfqqingeit dsdlqnrlsg ykttdlrsyl aedfysnsfs qqialnlsgg setygyfvgl
      361 gydrirestv sdlsqritln lrqnwksvns klnmglqtyl vsagnstgfp vleglspydk
      421 lkdeagypls vmknynsrfi eslrdtdlln wdfiplnein assiqnrqle friapsisye
      481 llkglvfrmd yqywrshgsr kqinsldsyf srnlinlyst vsqngsvnrv ipvggindln
      541 fseayshtlr sqlnyqrqwg kdqdisailg felkdfqres sqdraygvdp itgipqpvdy
      601 lgyypllntg fpyqtpfmqn fgawtdrfls ayanagytlk nkylltgslr rdasnlygvs
      661 tnaravplws aglgwiisee swldkewisy lkfkvsygfn gntnpsataf ttaqyfsaat
      721 nslvgkpwls ilnppnpqlr werikivnlg aefefwkqrl tgslefyhkq gidlfgvlpt
      781 ypssgqsslt knyaatrtkg vdlainsrvl kgglswnasi iysyinervv dyqqkptatq
      841 aasyssglsg ispvpvegyp lfsifsfpfa gldpitgdpl gllegqpstd yteilnrttl
      901 edlqfegssi pthigglrns vtwkgfelss nvtfrlgyyf kkesveydql nrgqithady
      961 airwrnsgde littvpsdpl kqdprratfd qissrrvrkg dhirwqdikl syswskstia
     1021 slpfeqiriy syldnlgilw kaakdvkdpd frnyqaprty smglsitf
//
LOCUS       WP_092905343            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriella
            xinjiangensis].
ACCESSION   WP_092905343
VERSION     WP_092905343.1
KEYWORDS    RefSeq.
SOURCE      Algoriella xinjiangensis
  ORGANISM  Algoriella xinjiangensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Algoriella.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Algoriella xinjiangensis"
                     /db_xref="taxon:684065"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124878
     Region          22..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktfillpl faasiafsqe krvitgsvqd eetlmgiaga svkieaqsis tttdqkgiie
       61 svtvgtvtde hgnftlevpa ntqsvlvsyl gydsrliqls ngnntytigl fpaedtiape
      121 dnqlnevvvt gyqkiekrkl tsaiatvkme diqqagvasv dqllsgqvag vavttetgsp
      181 ggpskirirg taslsgpqdp lwvidglple gndvpnfsdk dnidqlqnfs iaglnpndie
      241 ditilkdaaa taiygaraan gvisittkrg kkgsmvvnfs antfvtarpd fdrlnllnas
      301 qkvdlelmla srsdltyrtd kgevmrilar ngqldalrng gfgsldavtq nqinglrgnt
      361 tdwgkllyrn ainqqyglsl sggnersdyy fslgyydeqg ttigtgfery nltlknnykl
      421 ndklnvgisi fatesdkesf vtdadasinp inysrnanpy lspynpdgsy rydqdidgye
      481 drfvpfnfie erentkynlk nrslkaildl dyqvakglkv tsqfgiqydn nktekyaaee
      541 tyftrkmreg tryyksgqyl yflpdgaikq nwdneyfqyn wklqatystt ingrheidlm
      601 agteirrten nttltrafgy dpitkratqi vfptssfasq kiyetyremp aevnayvstf
      661 atasytldkk ytvfgsvryd gtnlfgvnkk ykylpiwavs aswlvsresf menvdfisnl
      721 rlrasyglqg nidrntspff igeysdttil pgnnediinv ynppndklrw ekttntnvgm
      781 dlglfrnris famdayhrkg tdmismretp letgfeytmv nwgeltnkgf eiavttrnid
      841 kenfkwstti nfahnksrvd keqprenslt psreglpvna vfalktagmd engnpmfwkg
      901 kekisakeff alydlyadfm pgefvdsnls nedmrnlfty igdrdpkftg giinnikihn
      961 fdvtvsaafn ikqtvmrsps yrgmeldpgr nytqdifeag ttlpgitsps mdnnegwman
     1021 kwfagnhana ynlldiwake vsymrissir vgytfpkkyt dvigfksari niegrnlfvf
     1081 sngykgyfdp etygniyaqp iaksvtmgin vsf
//
LOCUS       WP_092906150            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriella
            xinjiangensis].
ACCESSION   WP_092906150
VERSION     WP_092906150.1
KEYWORDS    RefSeq.
SOURCE      Algoriella xinjiangensis
  ORGANISM  Algoriella xinjiangensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Algoriella.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Algoriella xinjiangensis"
                     /db_xref="taxon:684065"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119310
     Region          25..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrnlknlfv lgglllgasl yaqektvtgt vtdpdgfpva davvksssgk evytddkgvf
       61 sieansgdki tvefiglptq tftvgasssy nvslkqsevv elegavvtal gitrdkrslg
      121 yatqeisgdv vnqtpvsnfa damsgeiagl dikgsgsrgg stnmvirgts slvgdnnali
      181 vvdgipinns tyngttqqng gggfdyanaa adinpndiet invlkgaaaa alygsrgmng
      241 vvmittkkgt kkrgigtein ssitvgtvdk ttlpkyqkky gagyenngss tvnpyfnegp
      301 vgsnpndlyv mfsddasyga afdpnlmvyq wgsffegmpt ygqktpwvaa kndpnsvwks
      361 ittfqnsasf fgsnddgnfr lgftnfqdef glvnskqlrn sidfngsyki sdkltisakm
      421 nyvdnsakgr vgtgydgwnp mqqfrqwwqt nvdlneleqa yrvtqgknas wnigeidpnk
      481 kgylvplysd nfyftryeny qndsrkryng gvsldyklts wlsvlarygf dnytekreer
      541 laigsagspg fyrlrnydvs ennydvifnv tknlsedftl danvgwnlrv qdydsfvaqt
      601 ngglkipkly sllnsvnslt ssdigqsrfr kmvdgeyvra sigyknmlfl egsfrtdrss
      661 slwsksdkgn ryyypsgsfs fvfselmkss ivnfgklrln yaqvgndtap yrlwntydin
      721 asfsgvgsas npaantysnl kpekmeeyev glemglwknr vnfdvsyynr ttydlitdvd
      781 vststgasrq wtnmgdvrne gvearisfep ikndnftwkv ttnfaknvnk mlrfngeiey
      841 yqlaavqggi tigaqvgeav giirgrgyvy nengdrvvna ngryqlssst tilgnmnpdf
      901 tggvkntfty kntslsflid fqkggdvfsl dtyygyatgl ydnytsglnd lgnpirntia
      961 ngggvilpgv kadgtpndvr veastgnnnp wgyksnnnee yiydasfvkl rnvtfsydlp
     1021 qkflkntfin kftlsavgrn lwiihknvpy sdpeaglsag nvqgyqsgah ptyreiglnl
     1081 kvqf
//
LOCUS       WP_092906667            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriella
            xinjiangensis].
ACCESSION   WP_092906667
VERSION     WP_092906667.1
KEYWORDS    RefSeq.
SOURCE      Algoriella xinjiangensis
  ORGANISM  Algoriella xinjiangensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Algoriella.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Algoriella xinjiangensis"
                     /db_xref="taxon:684065"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112581
     Region          23..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrrltslgl laflglgtma faqvtgvvkd gngfpeadae vvvkgtdkva ytdengsfnv
       61 dakvgdtlvi ngkefkvtsn nlgalkysne telkealvtv afgkqrkeai vgavsvvdek
      121 ilekqqatnv isaiqgsvag vniisdggqp gttpsirirg issinassep livldgipfn
      181 gslsmisqdm iesinvlkda gstalygarg angvilietk kgrksaepri sftsqfgvad
      241 navkmykkvg aedymkyawe alknsstkga lagqdasdkl igflgynpyg siakpidang
      301 nlvpgaallw dtdwedliqn ktaarreysl nvdggndftt ynvgasylnq egsvitsrfe
      361 rttvkasvnt kannwlelga nmiagfsnen gptqsgssyq spiqwinsms niypvykrnv
      421 ngglayndlg eliydygqdp sqlvngtrpl lsnenayaal vegykvknkr tninvsgfak
      481 ikfnedlslr ssigyqsyly dnsqwssnly gnaagvggri eknrdtqitk nitnilnynk
      541 sfgdhtfsvd aimdlydyty ettgakgtgf lpgisviggt tmpesvsgsi ssernlayms
      601 rltydymgky fvegsyrkea ssrfsrdtrw gdfysvgasw iiskeeflkg nsvvsdlklr
      661 gsygevgnnq vlnagvqnyf pylqgyesgs sqldeagili gslvdpnikw ertgslnvgl
      721 dfgffknrit gyvnyfdrks idlimgkais psgggqasii tnigslknyg fevnlntinv
      781 rndnfewstn invgrtynev lklngsdqli mglnvlkvgg srydfylqey agvdaadgaa
      841 mwykndangn kvttkvyaea tryiqdksal pdfeggfsny fryknidlnv lfnfsvggyi
      901 ydssygglmn siktagyqls edikdrwqnp gditdvpkll asnndynsts trflfkndyl
      961 rlkalnlgyn fsdkavgqmg lkglriyfqg dnlltfqshk gldpeqsvgg ttfsrsyqqr
     1021 tytvgfnvkl
//
LOCUS       WP_092906838            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriella
            xinjiangensis].
ACCESSION   WP_092906838
VERSION     WP_092906838.1
KEYWORDS    RefSeq.
SOURCE      Algoriella xinjiangensis
  ORGANISM  Algoriella xinjiangensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Algoriella.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Algoriella xinjiangensis"
                     /db_xref="taxon:684065"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115768
     Region          23..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkrftslsv lslfmmgglt yaqvsgvlrd snnfpveeae vvvkstgvkv ytdgegnfnv
       61 dakvgdilki idsngkeniv kvtstnlgvv rfsksdadni elqtvnligg ikldpaqkvg
      121 sytivsrdnf estpvssvde vlngrvagln ystasgdpgs snmivirgvg silgtpnply
      181 vvdgivvgkg adnaslmesw nplssidpnm ienvtvlkda satalygarg angvimittk
      241 kgkfgqkprf nyssdmaiqd iafdkinmmn anqyhqyggq iyfnsqqalg ttfnsledat
      301 akfitdkdag wdgketdwrk avqrnqsfvn tynfsvaggt ngisyraglt yyknkpliqt
      361 tdfdrksail afdqkitenl kygfsinytg vkrktipdan asanpwlssl fipsskpiyn
      421 adgtynqtnl gevtegfnpi gnlnnnylkg kvdtylgsft aeykflrylt fntvfggqrq
      481 imdevvwwnp kygdgiaqng lmqtgdtriw dwnwtntlsf rkkfndihdf dfaigtdyqd
      541 heyklgqrqg rdfsepipdf qysdpdkfvd vttgagtfyk wrqdsyfskl syvynnkftf
      601 agqfrydrvs vlpkknrggl fwslggtwnv gkeeflkgss vvnnlilkas ygrlgnvpfa
      661 dmwgrqydyy slvssstttp ypygdnffsq isssgnanld weiskqldvg femslyknal
      721 disfsyydkq tegalfnavt ksesgnptsy ianvsdisnk gfevtltssp frkefkwdin
      781 gnfsrninki eklnieediy lisdmtalsa gkllgeyytw lwagpnndpn vgelgvgswy
      841 tdgtktattt dkskaekawl gksafpkylv glsntfsykg vslsvlftgq fdfyvhngyh
      901 sffyndgnfp grnqiadamd ywtpentdaa npkpqlnnpn nsrlesdrwm rkgdhirlke
      961 vklaysfgdk fkqqtgvknl vfyvkgfnmw tyafdkdlnf dpesienaws fegkgvfnyt
     1021 tpiikslsig msldf
//
LOCUS       WP_092908013             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriella
            xinjiangensis].
ACCESSION   WP_092908013
VERSION     WP_092908013.1
KEYWORDS    RefSeq.
SOURCE      Algoriella xinjiangensis
  ORGANISM  Algoriella xinjiangensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Algoriella.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Algoriella xinjiangensis"
                     /db_xref="taxon:684065"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108061
     Region          34..975
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkyffplfi lgslsinaqv tndsiqvead pfasdsiiln qavvigygsv kksdltsavs
       61 sanskdimqi asttamqslq gklagvniin tdtpggtptv lvrgmgtalg gkaplyvvdg
      121 livpnianin psdidkidvl kdaassaiyg vrgangvvvi ttkrgktgkl kvnydtyfgv
      181 rntmnmvema danqyityfn eqrkatggsl istnqkyntd wfdemlttgq iisnnvslsg
      241 agesinymfs vnnfeekgil egnnfkrtsi rsnndyklfd gklkikqsvs atfsreipkp
      301 ygafdvayrq splvpvkyen grwglpifnt ttgevtyvan agevtsnlns hgnpmatlfy
      361 dnqkinttti qgnieaelkl tkgltitsrt gatkywykyr eynpikekwi agnpirtase
      421 feglkaanpt sgtymnnsln lnnietfrws wenfvtfdrk fgdhsfnvva gvsaektgig
      481 efsnttvydv pdkeqywsvh hasgdyeasi dqnnytpvay asyfarlqyn yankyyvsgi
      541 irrdgssqfk nnqqywgtfp sasvawnisn eeflkdsnti sflklrggwg rlgnadvpyn
      601 yttittatgs dnanyvfgpg qdlvfgayvg spaydvswei veewstgldf elfkgkvtgn
      661 ldyynkttkn ailsinqils spydknfvdh aaevvnkgfe ialnynnets gglrysiggn
      721 fnynenevty vkpgyagmtg gslgngqiak rleagqplgs fwlyevegvw qtqtdidnna
      781 hlssarpghl rykdqngdgv iddrdkkfmg syipkfnygi ninldyknfd lnisgygagg
      841 nkiyngiknt rlggenitvd tfnnrwtgag tsntnpgser dqvassyyle kgdyfrlsni
      901 tlgynfrdki dfvknlrlyv saqnvfivtk ysgftpeltl nnekgkrydg spygttgmdf
      961 saypnvttfl vglnvef
//
LOCUS       WP_092941090             537 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paracidovorax wautersii].
ACCESSION   WP_092941090
VERSION     WP_092941090.1
KEYWORDS    RefSeq.
SOURCE      Paracidovorax wautersii
  ORGANISM  Paracidovorax wautersii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Paracidovorax.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Paracidovorax wautersii"
                     /db_xref="taxon:1177982"
     Protein         1..537
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55302
     Region          11..537
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqaspsptaq rigvpretfa gekrvatvpe vvqklvalgf svaveagage aahcsddayr
       61 aagaevlpda aalwaasdiv fkvrppsaae valmrpggll vgfvwpaqhp elmaqlaarq
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvrslg gefvkvdyee dgaggggyak
      241 vmsegfqaaq rrmyaeqard adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti lgftdlpsrl akqsstlyat nllrlaeelc kakdgvavvn
      361 meddairglt vvkageitwp applkaapap aaarpaaapv aekkagghgh gsagplpakt
      421 lailfavaav afwfigayap aaflghftvf vlacfigymv vwnvtpalht plmsvtnais
      481 siiaigalvq iappqaaang rpdglilwla faalvltavn mfggfavtrr mlamfqk
//
LOCUS       WP_092947278             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Roseateles
            sp. YR242].
ACCESSION   WP_092947278
VERSION     WP_092947278.1
KEYWORDS    RefSeq.
SOURCE      Roseateles sp. YR242
  ORGANISM  Roseateles sp. YR242
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Roseateles sp. YR242"
                     /db_xref="taxon:1855305"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38313
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpreta agetrvaatp etvkklvaqg hrvlveagag vqasatdeay vaagaevgss
       61 aqalgadlvl kvrppgpdew pafkrgaalv gmlnpfdrdg lqrladaglt afaleaaprt
      121 traqsmdvls sqaniagyka vmlaafhyqr lfpmlmtaag tikaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvafetaee reaaegvggy arpmppswla
      241 rqqlevakrv aqadvvitta lipgraapvl vteemvramk pgsvivdiaa paggncplte
      301 pgrtvvkhgv tlvgetnlpa lvaadassly arnvldflkl vltgeagvtl ppdddivtac
      361 lvahegrllr s
//
LOCUS       WP_092963624             532 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Agromyces
            sp. CF514].
ACCESSION   WP_092963624
VERSION     WP_092963624.1
KEYWORDS    RefSeq.
SOURCE      Agromyces sp. CF514
  ORGANISM  Agromyces sp. CF514
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Agromyces.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Agromyces sp. CF514"
                     /db_xref="taxon:1881031"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53720
     Region          3..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msrigivteh spesrvaatp atvkqlvalg yevsveagag arssfpdaay veagaeitsr
       61 atalgseivl lvnapteadi aalvpgstiv gllapafnpa llqaladhgv talamdavpr
      121 israqsmdvl ssmsnisgyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksiggt ylkvevaeqm qstdgyakat sedydrraae
      241 iyseqaadvd iiittalipg rpapklitaa dvasmrsgsv vvdmaagqgg nvagsvager
      301 vvtpngvtil gytdlasrlp tqasqlygtn vvnllklltp gkdgelvldf ddvvqrsvtv
      361 tqpgsvtwpp ppvqvsaapa aasaapveag akpakpartp mtpvkkvslv algiaalfav
      421 navappplpq hftvlvlsvv vgfyvigkva halhtplmsv tnaisgiivv gamvqitspe
      481 pvvqvlaava vllasinvfg gfavtrrmla mfarghasea aapgaaaagr nd
//
LOCUS       WP_092972454             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ralstonia
            sp. NFACC01].
ACCESSION   WP_092972454
VERSION     WP_092972454.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia sp. NFACC01
  ORGANISM  Ralstonia sp. NFACC01
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Ralstonia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Ralstonia sp. NFACC01"
                     /db_xref="taxon:1566294"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39282
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipqetr adetrvaatp etvkkyvalg hqvtvqsgag vaaaqpdday vaagakigta
       61 aealgaqivl kvrspeaael aqmqpgavlv gilnpfdden tarlaaanvt afaleaaprt
      121 traqsmdvls sqaniagyka vmvaanhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfltdee reiaqgvggy arpmppdwmr
      241 rqaelvhtra tqadivitta lipgrraptl lseatvqamk pgsvvvdlaa aqggncplte
      301 adrvvvkhgv tlvgytnlas mvaadasaly arnvldflkl iidkdgglni nreddivaac
      361 llsqagqvvr apaatsaak
//
LOCUS       WP_092981832            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Robiginitalea
            myxolifaciens].
ACCESSION   WP_092981832
VERSION     WP_092981832.1
KEYWORDS    RefSeq.
SOURCE      Robiginitalea myxolifaciens
  ORGANISM  Robiginitalea myxolifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Robiginitalea.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Robiginitalea myxolifaciens"
                     /db_xref="taxon:400055"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110801
     Region          24..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllksll ltgaflcfgl aqaqevsgtv sdatgplpga svvvkgtttg tqtdfdgnyt
       61 ldgvaedatl visyigyatq evavngqsti nvtlsedata ldevviigyg qttvkdatgs
      121 vtavtaedfn ggvitspeql iqgkaagvni qqvsgepgag iqinirgsns vrgnnnplfv
      181 vdgvplfgqg tdasgdtgqg gsetgnplnf lnpndiesis ilkdasatai ygsrgsngvv
      241 iittksgrta sggtiewssn lsistpvrqf dlldrnqflq avedyggnpd nvdfgantnw
      301 qdvimrtaas snhniaysrn ygsgnvratf gyqkqfgvve kseferitgr inlnqrlldd
      361 klilglqasv srvnreqppl aagagfrgdi lgaaysanpt wpanpgfddg ggllqpanyl
      421 aetqnltntn rflinasaey kltpelsakv nlgydksese ntsvlstnlq niqiaefagf
      481 gtyntrflen ktleatlnyt kqfdngnlta lagyayqdfr tsgrgvagrg fgtsdlnkmg
      541 edlrftanqa aaqlagssyq qyyfaanttg livnrlfpdv vagevnplnf qrkvialtad
      601 tgdntdelqs ffgrveyaha gkyiftatmr adgssrfgpe nqygyfpsga fawqiaeedf
      661 vgdavstlkl rlsagitgnq dglgygnfva rqrfaglgid nnnnvnpngl sivatdvpdl
      721 rweetlnfna gldfgfnldr fngsidvyrs ettdvllqtp paapstnpfq fgnvdasiin
      781 qgielslnyd fiqtedatfg asfniaynen eiqdfagsin tgeiagpgls gafaqrfeag
      841 qsifswymae ftgfdgdgnp tyedvdgngv gdpdsdkkfi gedalpdvtt glnlnfsykn
      901 wdasaffngq fgfsvynnta nalfnagqiv tsrnvtvaaa nagenggast avstrflekg
      961 dfvrfqnati gynvplsgdg tfktlrfslt gqnlalwtdy sgidpevtvq tgqlgsgvpt
     1021 rgidwsafpn pltvtfgina sf
//
LOCUS       WP_092983218            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Robiginitalea
            myxolifaciens].
ACCESSION   WP_092983218
VERSION     WP_092983218.1
KEYWORDS    RefSeq.
SOURCE      Robiginitalea myxolifaciens
  ORGANISM  Robiginitalea myxolifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Robiginitalea.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Robiginitalea myxolifaciens"
                     /db_xref="taxon:400055"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117028
     Region          27..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtnlngilt lllafvvqis faqdraisgt vtdadglplp gvnivvegtt tgtqsdfdgn
       61 yslqastgqv lvftylgmra errsvgagst invqmsedaq aleevvvtaq gikrekkalg
      121 yavsnvdeek ladrtegdig rvltgkasgv nitqqsgvsg satnivirgy qsfsqnnqpl
      181 fivdgvpfss dtnaqgdfad gnngssrfld ldpnniesvn vlkglsaatl ygeqgkngvi
      241 littkngslg gkpkkseiti asslffnela smpdyqdqyg ngfdqafgwf fsnwgpsfdr
      301 egragwgnaa nfpgiydlqn dgtilhpfst agastgipaa fpefqgrrya wkpynsvgqf
      361 frtgtvanis inangasedg kitynasygh lddegftpgn nlkrntigvg graqlsnkft
      421 isgtmnysrt dfrsppvarg dgsqvsgdga svfsnvfftp rsvdlvnipf qnpitggsvy
      481 yrqnnsiqhp lwtvanagtr qltnrafgrl saqydfsdnl nllyrfgydv ynerntqfqh
      541 kggidvstqf lsgvygswdn nntiwnhdvi lngsydltek ldltfnvggq arstyydrng
      601 vfssgqnvfg vlrhfnydlq neiqftqrnn lvgvygqvdl gyddflyltl ngrndwvsnq
      661 svenrslfyk gasfsfipts afeglssqgg inflklrggy gesagfatgy ptsvdlfldt
      721 qdfvnqdggf vvtntvsntv anpgikpery teieagiegr ffnfvtldls vyrritndli
      781 inrpldpstg gtaiqtnvge iegtgieadl glalintedf swnvnanfts gesvvndlgl
      841 dtdiivyagf tnlgnaaieg erlgvivgsr iqrdengnfv vdasgnyide evdengrlpi
      901 igdptpdfll nigsdlsykg fnfsflfnhq qggdiysett avllgrglie etvdrettfi
      961 lpgvstdgsp ntvainnsay yfsnvlfgpn elqiydattl rlqevslgys fpkkfldktp
     1021 fgslsvtvsg fnlwyeafnt pdganfdpni agvgvgngrg fdflngpssr rygvsvrasf
//
LOCUS       WP_092999323             430 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. NFR07].
ACCESSION   WP_092999323
VERSION     WP_092999323.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. NFR07
  ORGANISM  Rhizobium sp. NFR07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Rhizobium sp. NFR07"
                     /db_xref="taxon:1566262"
     Protein         1..430
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43828
     Region          14..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqktifvshe gsseprvsas pesvkrlagl gfsiivetga glssgipdgd feavgakigk
       61 agdaaeadiv lrvnrpgate lkaykpgtvv favmdpygne aalaamakag isafsmelmp
      121 ritraqsmdv lssqanlagy ravidasyey gralpmmmta agtvpaakvf vmgagvaglq
      181 aiatarrlga vltatdvrpa akeqvaslga kfvavedeef kaaetaagya kpmsaeyqak
      241 qaalvadhia kqdivittal ipgrpapklv sramlasmkp gsvavdlave rggniegsek
      301 gniatvegvs vigyanvagr iaasasalya rnlfafietm vdkttkefsl nledelvkat
      361 llthggsvih ptfaeaaaaa vvtaepavaa vkakpvaaaa gsvakpipkt rkkpaasssa
      421 epkkessdgq
//
LOCUS       WP_093010882             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Roseivivax
            halotolerans].
ACCESSION   WP_093010882
VERSION     WP_093010882.1
KEYWORDS    RefSeq.
SOURCE      Roseivivax halotolerans
  ORGANISM  Roseivivax halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseivivax.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseivivax halotolerans"
                     /db_xref="taxon:93684"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56096
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevm egearvamtp dsakmlqklg ydcaietgag dkagfpdaay eeagveiikt
       61 aaalykeadv iakvqpptdt evkrlsekkl lisffwpgqn edlmkaaadk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee dqedgsesgg yakpsspefr
      241 eaqlakfrel apdvdivitt alipnreape lwtedmvkam kpgsvivdla aekggncklt
      301 qkdkkivtdn gvtiigytdf psrmakqssl lyatnirhlm tdltpekdgq vnhnmeddvi
      361 rgatvaheke vtfpppppkt kaiaaqkpkp kekektpeek raeemaafqk qtqqqvallg
      421 vgavlilavg liapasfmqh fivfvlsvfv gfqviwgvsh slhtplmavt naissiiilg
      481 almqigsssf lvillaavsv fmaginivgg fmvtrrmlam fqks
//
LOCUS       WP_093012397             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingobium sp. YR768].
ACCESSION   WP_093012397
VERSION     WP_093012397.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. YR768
  ORGANISM  Sphingobium sp. YR768
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sphingobium sp. YR768"
                     /db_xref="taxon:1884365"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54703
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreva rdearvaltp dsalqlqklg haclvesgag iaagfgdday raagvtvmps
       61 aaalwaeadv vvkvrppead eaarltpgkt lisffypgqr geelaaisat ganvlamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqvt aagkvpparv lvigagvagl
      181 aaigaatslg aitlafdvrp evaeqiesmg aqfvyldfae eqqdgattgg yaapsspefr
      241 eaqlkkfrel apnvdivist alipgrdapv lwtkdmveam rpgsvivdla aerggncelt
      301 vadqkivspn gvtiigytdf psrmatqsst lyasnirhml adltpgkdga ivhdmeddvi
      361 rgatiafega vsfpppppki kaiaaqkpkp kaeeltpeqk rakdiaafka qtrsqvttli
      421 vaavlliavg avapasfmah ftvfvlacfv gfqviwnvsh alhtplmavt naisgiivvg
      481 amlqvgssns ivlalatisi liasinivgg flvtrrmlam fqrs
//
LOCUS       WP_093014458             552 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. OV700].
ACCESSION   WP_093014458
VERSION     WP_093014458.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. OV700
  ORGANISM  Variovorax sp. OV700
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Variovorax sp. OV700"
                     /db_xref="taxon:1882826"
     Protein         1..552
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57620
     Region          28..552
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mhietthepa agtngaiege aarkpavigv preifpgekr vatvpevvek liklgfsvvl
       61 qsgagdaahc sddsyraaga hivadaatlw assdivfkvc aptpeevalm kaggtlisfi
      121 wpaqkpelmq qlaerkvtvl aidslprtls raqkmdalts qagvagyrav ieaanafgrf
      181 fngqitaagk vppakvfiag agvaglaaig taaglgaivr andtraevad qvvslggefv
      241 kvdyeeegsg gggyakvmse gfqqaqremy akqarevdii ittalipgkp aprlitaemv
      301 ksmkpgsviv dmaaerggnc eltepgqsvv khgvtivgyt dlvsrlakqs stlyatnlfr
      361 lseelcktkd giinvnmedd airgltvike gsiswppppp kqaaapaqtk paaapvavkk
      421 ahghgapsep magnklailf gvsaalfwfv ganapaafla hftvfvlacf vgymvvwnvk
      481 palhtplmsv tnaissiiai galvqiappi agaanrpddw irwlaaagiv ltainmfggf
      541 avtqrmlamf rk
//
LOCUS       WP_093022953            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pustulibacterium marinum].
ACCESSION   WP_093022953
VERSION     WP_093022953.1
KEYWORDS    RefSeq.
SOURCE      Pustulibacterium marinum
  ORGANISM  Pustulibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pustulibacterium.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Pustulibacterium marinum"
                     /db_xref="taxon:1224947"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117293
     Region          25..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfsgllt lvlvfivqit faqqktitgt itdsdglplp gatvqikgts tgtqtdfdgn
       61 ysiqaatgdv lvisflgfkt tevsvgnqst lsltlesdvq aidevivvgy gtttkeaytg
      121 tatkieteni eaktvsnvsq alrgevagvn vvtgsgapgs datirirgfg svngnraply
      181 vvdgapyasd issinpadia smtvlkdaaa tsiygsrgan gvivittkqg kkgksvisvd
      241 yktsvntlml pqydvitspe qyietawssl ktkalvtgqs dpaawasanl ygdgtgegin
      301 sfyniwnveg sqlidpttgk vangvqrkyt ptswsdaafg tgyrseaniq fsgasdktky
      361 atsfgylndd gyainsnytr yttrlnlehk pkdwltvggn maftgskyin ssdsegssgs
      421 sanifaltnt tpaiydvylr dadgnlvedp ifggnqfdyg aetgrrawts tngiadsnyd
      481 lartdvatvl gnfnisadit dwltasvrys gqlqtseyas aanqfyggwa eaggylyrss
      541 skninqnflq mlrfnksfge hsieafvahe stenkyklms asatkaitpl stdlaqytta
      601 ygrassytqt wsidsyfgql nydyqqkyfl tgsvrrdgss rfkndkwgtf gsvglgwvms
      661 kedflsnasf ldylklkasy giigdqgtsl qygwqlwsin qtstgdysfs vsstfanpdl
      721 twetskiaqv gvestlfkni ldvnidyyik ntdnlffvqt lpvstgyssm qfndgqlrns
      781 glefdiyakv iqeqnftlgl gingeflsne itempgdyyt getkvldgqy seghslydfy
      841 mrewagvdpa tgagmwnmyy ndmngngvfd ssdeaiqsmt lyqnenpgan vqktttttys
      901 dattkyvgks aiptvrggfr lnagyknfnl taqfnyslgg ymydngyaql mdngdligsn
      961 nwhkdisnaw kepgdvtnvp rltsgldtdv qyssrstrfl tkadylalnn vnlgytfske
     1021 itdklklskl nlyvsgdnlm mlsrrdgfnp qtmfsasnsg iympmttfsf gakvqf
//
LOCUS       WP_093022947            1091 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pustulibacterium marinum].
ACCESSION   WP_093022947
VERSION     WP_093022947.1
KEYWORDS    RefSeq.
SOURCE      Pustulibacterium marinum
  ORGANISM  Pustulibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pustulibacterium.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Pustulibacterium marinum"
                     /db_xref="taxon:1224947"
     Protein         1..1091
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120385
     Region          25..1090
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgllt lllvlvvhit yaqdktitgt vkdsdgvplp gvtiqikvat tgtqtdfdgn
       61 ysitapegsv lvysyvgmtt vektvgesst idvtmkvnat elddvvvtal gikqevrklt
      121 yaaqdvkeee lnvtqnnnvn aaiagkiagv tvasqagskl gqsgairlrg aisatgtenp
      181 lyvvdgvvts peqidpenia sinvlkgpna talyglrgns gvlvittkkg ttnslkievf
      241 nsttfdkvay lpeyqnqygq gyngqdsfgt fqyeagfhpd ywasfdggrf ntesnadesw
      301 gprfdgqdyy pwytwfpdsp yfgqaqpwvs qednvkdfyd tgvtlkngft lsgggenftg
      361 rlnytrqdqn giipnstyak nlinasfdvd lndrltigmn lnysndkvvg dfadgysnnf
      421 sgsfnswfar dlemdklkel swlrsgqdgt gyatswnwwg pdyfpgtsgd naykkavfwf
      481 npyywaeqyk pedrntrlvg dihasykltd ninvnllasr tsrnydrvwk ipyeveyssa
      541 paayndyvns fgtrkytsee niikptidfd fdlsedfsld gvvgglfrvn kytntssqmt
      601 qngypgggdf vglvipdlyq ftnsrervnp tyemqkyrvn smfgrvnfsy knfltlsgdl
      661 rsdydsrydv fnsgdrqnds nrftfgsiga sfvfselidn adffdfgklf vsyaevgkei
      721 dayqvnppyr lssntygsnp lmyapssaig sgiepatsgs levgintaff qnrvrlnaty
      781 ynedrereil nldlptstgy ssivtnggli nregleitlg ltpvkttdft wdmninfstn
      841 ktmvkelegl dayaiassty syvtltnvvg eewgqlvgaa iardengtpi lnsngtyvse
      901 aghnygsilp dfnggifnsf sykgltlagt ltfqkggkff slseswgays glleetaatn
      961 dlgnnvrddv asgggvhsvg vdvdgntvdq yypaynwfgq yysnrlaepf vhdasylkln
     1021 elslsytlpk nligefmesa sigfvarnva llalskdnvh nwdpselsqv ygengqlpgt
     1081 rsygfnvkft f
//
LOCUS       WP_093026451             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pustulibacterium marinum].
ACCESSION   WP_093026451
VERSION     WP_093026451.1
KEYWORDS    RefSeq.
SOURCE      Pustulibacterium marinum
  ORGANISM  Pustulibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pustulibacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Pustulibacterium marinum"
                     /db_xref="taxon:1224947"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110389
     Region          37..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfflhsmgr haiflyflcf cfcfgspgaw aqstvslsgt vsdrdgpiyg atiqvkgsts
       61 gilsdengyy klpvmasdtl vfsylgyqsq eipvgglkli nvvliesvse ldavvvnagy
      121 ytvsekertg sitgisgeai eaqpvgnvfe tlqgrltgvs ivstggipgs rfdiqirgrn
      181 siaagneply vidgvpymse smeavfsaal tgggnplqal npadieriev lkdadataiy
      241 gsrgangvil ittkqgksgk sqlsvsvasg aakmtrfwdm lsteeylemr qeafantgtt
      301 ptnanapdll lwdqhrytdw qrkllgetae itqaqvslsg gndrtkyrlg tsfreqgsvf
      361 pgdfsnrkvs gnlsvqhese dgrfstqgtv lysrdvnkqp kndptynaly mppnapeiyl
      421 edgslnfens tfsnpyalil qsyqntqysf vgnlnvsyrl fqglklkvsg gynrmdgeqi
      481 gqtplaslnp avyttgeasf grrtfdswil epqlnymrsw nnsrlevlig gsfqenqfrl
      541 qefyakgytd dalldnmaaa psfqvrqfle tdyrymavfg rinynykhry ilnvtgrrdg
      601 ssrfgpgnqw gnfgavgaaw lfseenwfkd smlsfgklrs sygtsgndri sdygyldswt
      661 atyynyngqg glypsrlynp nygwevnrkf evalesgfwk driqfnvawy rnrsssqlig
      721 eplpattgfg siqnnldavv qntgwefelh stpvqgdvtw rnsllltvpk nklisfpdle
      781 lstyantyvv gqplditkvy nytgidpetg yytfedvngd gtitaaedkq tlrrsgqkyy
      841 gsfqntlsyk gwqleavlqf vkqtgysyfy dlggapgyir nqpnlvldhw qapgdtagvq
      901 ayttggvgan aynllqsssa aytdasyvrl qtvnfsyqfp krwldtvkls glrmyiqgqn
      961 lltftdyegw dpetqsvgsl ppltswmvgm qisf
//
LOCUS       WP_093026637             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pustulibacterium marinum].
ACCESSION   WP_093026637
VERSION     WP_093026637.1
KEYWORDS    RefSeq.
SOURCE      Pustulibacterium marinum
  ORGANISM  Pustulibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pustulibacterium.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Pustulibacterium marinum"
                     /db_xref="taxon:1224947"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110131
     Region          35..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfflhsmgr haiflyflcf clgsygafaq tsvnvsgtvs drdgpiygat iqvkgkslgt
       61 ssdvdgryml tvseidtlvf symgyesqsf lvgsrtvfdv vlleslrtld avvvnagyyt
      121 vsekertgsi asvraeaiek qpitnalsav qgrmtgvhit qntgvagggf siqirgvnsl
      181 rsegnaplyi idgmpvsatt psfnsagilp shemnplnal npndiqsiei lkdadataiy
      241 gargangvvl ittkkggvtg ktqftvnasq gwsqvasqme lmstsdyltm raqayandgi
      301 anypanaydv ngtwdanrht dwqkeligtt alnslvhlsv aggngqtrfm lsgshqeqtt
      361 vfsedfrykt nnvtgslehq ssdnrfqvsl tglfsdqtnn lirsditnqa lrlapnapal
      421 yqedgslnwe nntftnplaa nestyanttr tfttnanlqy alfpklllkv ntglnqqvfe
      481 ewslrpstmy npaygvtpas svatkgtsqr fsylvepqie yqitaskhrv qvllggtyqe
      541 rtsdvlglys ygfesnalih sleaasgvmv tddvrtsyry aalfgrinys hdgkyilnlt
      601 grrdgssrfg pnnrfanfga vgfawlfske dlvsdskwls fgklrgsygv tgsdalgdyq
      661 yldtytvsst gyqggsvlyp srlnnpyfsw ekttkfeval etgflkdrlr fnaawyqnrs
      721 gnqlvgiplp attgfssiqa nlpatvenrg wefelqampv tfeegqwhss vnlsiprnel
      781 vafpdlegst yansyvvgyp lsiqkvyqye gidpetglfq ftdfnedgvi sspadnqviq
      841 kigveyfgew nnqvqykhwd fsclfqfvkq vqrnynalma tpgtmnnqpi evnnvwsatn
      901 pdghympytt stggergrly syyrnstaai sdasfirlkn vqlsyhlpig kgmqdvriyl
      961 qgqnlwtltd yfgldpefva tgflpplkty algvqlkf
//
LOCUS       WP_093032062             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Thiocapsa
            roseopersicina].
ACCESSION   WP_093032062
VERSION     WP_093032062.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa roseopersicina
  ORGANISM  Thiocapsa roseopersicina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Thiocapsa roseopersicina"
                     /db_xref="taxon:1058"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38023
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigiplesa pgetrvasip evvkkligkg fevmveagag vragypdgey aaagaqltdr
       61 agafdvdlll kvrrpdaadv eavrpgglyv gllescgede ilsamlakgv rvlgmermpr
      121 tsraqsmdal ssqsniagyr atleaaaryg rflpmmmtsa gsakparlvv lgvgvaglqa
      181 iatarrlgad vyaydvrpet qeqirslgak pieldlgesg sgeggyakel seeakakqqa
      241 alsdqlakah viittalipc rpapvlvtee vvkrmrpgsv ivdlaaangg ncpltvagei
      301 verhgvtivg ltnfpalvpa dasafyarnl anlieimftp sesgpvlkdl aedditaaml
      361 vkpst
//
LOCUS       WP_093035047             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ruegeria
            marina].
ACCESSION   WP_093035047
VERSION     WP_093035047.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria marina
  ORGANISM  Ruegeria marina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Ruegeria marina"
                     /db_xref="taxon:639004"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55588
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif egenrvamtp esalqlqklg ydcaiesgag aaagfadaly eaagveivkt
       61 aaalwkeidi vakvrqptet elkrltkgkt lisffnpagn aegmelakak ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee qqqdgaatgg yasvsspefh
      241 aaqlkkfrel apemdivitt alipnrpapv lwtkdmvaam kpgsvivdla aerggnvegt
      301 vkdekvvten gvtiigytdf psrmaaqass lyatnirhmm tdltpdkdgk vnhnmeddvi
      361 rgatvtyege itfpppppki qaiaakpkek tkeltpeekr akevaafkaq tknqvtlltv
      421 ggllmllvgl vapasfmqhf ivfvlavfvg fqviwnvshs lhtplmaitn aissiiivga
      481 lmqigsgsfl villaglsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_093037600             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseovarius azorensis].
ACCESSION   WP_093037600
VERSION     WP_093037600.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius azorensis
  ORGANISM  Roseovarius azorensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseovarius azorensis"
                     /db_xref="taxon:1287727"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55680
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevl egenrvamtp esalqlqklg htcaiesgag eragfsdady eaagvevikt
       61 aaalwkgcdi iakvriptdt evkrlregqt lisffnpggn ekqlkmaaek gatviamesv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppaki lvigagvagl
      181 aaigtatslg aityafdvrp evaeqvesmg aqfvyldfee aaqdgaatgg yasvsspefr
      241 eaqlakfrel apdmdivitt alipnreape lwtedmvksm krgsvivdla aekggncklt
      301 vmdekivten gvtiigytdf psrmatqasm lyatnirhml tdltpgkdgv vnhnmeddvi
      361 rgatvthage vtfpppppkv aaiaaakpke kakdltpeer kaqematfka qtkqqvtllt
      421 vgavlllavg lvapasfmqh fivfvlavfv gfqviwnvsh slhtplmait naissiiilg
      481 almqigsgsf lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_093053955             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. YR634].
ACCESSION   WP_093053955
VERSION     WP_093053955.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. YR634
  ORGANISM  Variovorax sp. YR634
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax sp. YR634"
                     /db_xref="taxon:1884385"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38477
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etvkklvasg hsirvqsgag vaasvtdaay qaagaeitdq
       61 agafsadmvl kvrtptdaet allksgavvi gmlnpfdaag lqrlaaagvv gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmppswla
      241 rqqvevakrv aladvvista lipgraaptl itedmvksmk pgsvivdiaa gkgadgvggn
      301 cplseadrtv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvtqd gqvtkk
//
LOCUS       WP_093065611             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Thiothrix
            caldifontis].
ACCESSION   WP_093065611
VERSION     WP_093065611.1
KEYWORDS    RefSeq.
SOURCE      Thiothrix caldifontis
  ORGANISM  Thiothrix caldifontis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Thiotrichaceae; Thiothrix.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Thiothrix caldifontis"
                     /db_xref="taxon:525918"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39164
     Region          3..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msikvavpke taegerrvai essviakltk lgaevlveag agdaahipdt afsgativsa
       61 ahdlyqqadi vlkvqppsea eiaqlregsv ligtlqpyky periaalnak nitsfameli
      121 prisraqamd vlssqaavag ykaaimgadl aprffpmltt aagtirpskv iiigvgvagl
      181 qaiatarrlg avveaydvrs atkeqvqslg akfielgita egeggyarel taeekqkqqe
      241 elakhiatad vlittaavpg rpspkiipea tvegmksgav iidlaaeggg nctltqpgkt
      301 ivhkgvtiha plnvpsqvpv hasemyaknl lnflspmlkd gayapdfnde viagallthe
      361 gkimneairq lvega
//
LOCUS       WP_093075887             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudonocardia oroxyli].
ACCESSION   WP_093075887
VERSION     WP_093075887.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia oroxyli
  ORGANISM  Pseudonocardia oroxyli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Pseudonocardia oroxyli"
                     /db_xref="taxon:366584"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52783
     Region          12..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msdteetsgp alrvgvvaes tkgetrvals pettakvigl gyavavesga gahagfedaa
       61 yaeagaevva gpvwdadvvl mvnapqpdei pqlrsgatli amlaprfeee rtaaltaagv
      121 talsmdavpr israqsmdvl ssmaniagyr avieaahafg rfftgqvtaa gkvppakvlv
      181 agagvaglaa iaaanslgav vratdpraev adqvkslgge ylpveveqea stdgyakats
      241 eaydkraaei yseqaaecdi iittalipgr paptlitaad vasmrpgsvi vdmaaaqggn
      301 vegsvagevv ttehgvtiig ytdlaarlpa qasqlygtnv lnllklmtpg kdghlvldld
      361 dtvvrgitva hagetlwppp pvsvsaapaa qpaaapveke pekersplar alpgvlgava
      421 lflvtafapp elaghltvfv laivigfyvi gnvhhalhtp lmsvtnaisg iivvgailql
      481 gtggnglvia laavatllas inivggfavt rrmlqmftrs
//
LOCUS       WP_093076932             376 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Variovorax].
ACCESSION   WP_093076932
VERSION     WP_093076932.1
KEYWORDS    RefSeq.
SOURCE      Variovorax
  ORGANISM  Variovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax"
                     /db_xref="taxon:34072"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38419
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etvkklvasg hsirvqsgag vaasvtdaay qaagaeitdq
       61 agafsadmvl kvrtptdaet allksgavvi gmlnpfdaag lqrlaaagvv gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmppswla
      241 rqqvevakrv aladvvista lipgraaptl itedmvksmk pgsvivdiaa gkgaggvggn
      301 cplseadrtv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvtqd gqvtkk
//
LOCUS       WP_093083023             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingobium sp. AP50].
ACCESSION   WP_093083023
VERSION     WP_093083023.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium sp. AP50
  ORGANISM  Sphingobium sp. AP50
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sphingobium sp. AP50"
                     /db_xref="taxon:1884369"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54747
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreva rdearvaltp dsalqlqklg haclvesgag vaagfgdday raagvtvlps
       61 aealwaeadv vvkvrppead eaarltpgkt lisffypgqr geelaaisat ganvlamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqvt aagkvpparv lvigagvagl
      181 aaigaatslg aitlafdvrp evaeqiesmg aqfvyldfae eqqdgattgg yaapsspefr
      241 eaqlkkfrel apnvdivist alipgrdapv lwtkdmveam rpgsvivdla aerggncelt
      301 vadqkivspn gvtiigytdf psrmaaqsst lyasnirhml adltpgkdgv ivhnmeddvi
      361 rgatiafegt vsfpppppki kaiaaqkpkp kaeeltpeqk rakevaafka qtrsqittli
      421 agavllmavg avapasfmah ftvfvlacfv gfqviwnvsh alhtplmavt naisgivvvg
      481 amlqvgssst ivlvlatisi liasinivgg flvtrrmlam fqrs
//
LOCUS       WP_093092091             513 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Snodgrassella].
ACCESSION   WP_093092091
VERSION     WP_093092091.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella
  ORGANISM  Snodgrassella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Snodgrassella"
                     /db_xref="taxon:1193515"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54175
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg heviiehdag kaaslsdgly heagatvada
       61 ttvwqcplif kvnapnkdei aamnegtilv sfimpaqqpe lleqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flrldyqeee sssgdgyakt msaayieaem
      241 klfaeqarqv diiittaaip gkpapklitr emvdsmhegs vivdlaaatg gnceytepgk
      301 iittangvki igytdmanrl agqssqlygt nlvnlakllt pnqdgelaln fedviirnmt
      361 vthegnsmyp pppiqvsatp kaapkaaast ttaapavppn takkkliwaa iavilvlwvg
      421 avapvaflnh fmvfvlscvv gyfvvwnvnh alhtplmsvt naisgiivlg allqigqghg
      481 fvsllafiav aivsvnifgg favtrrmlnm frk
//
LOCUS       WP_093093029             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shimia
            aestuarii].
ACCESSION   WP_093093029
VERSION     WP_093093029.1
KEYWORDS    RefSeq.
SOURCE      Shimia aestuarii
  ORGANISM  Shimia aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Shimia aestuarii"
                     /db_xref="taxon:254406"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55484
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf agenrvamtp dsaiqlqklg yecaiesgag anagfsdaay eeagveiikt
       61 aaalwkasdi vakvrqpnet elkrltkgkt lisffnpagn eegmeaakak ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvqseefr
      241 naqlakfrel apevdivitt alipnreape lwtkdmvdam kpgsvivdla aekggncklt
      301 vadekivten gvtiigytdf psrmaaqsss lyatnirhmm adltpekdgq inhdmeddvi
      361 rgatvtfegd itfpppppkv qaiaaqkkpe vkeltpeekr aaevaafkaq tkqqvtllav
      421 ggalllgvgl vapasfmqhf ivfvlavfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_093095292             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093095292
VERSION     WP_093095292.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108202
     Region          27..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktllkkyl vtimvillsi pvfsqeknit gsvkneagea lagatirvkg tslavttdnl
       61 gafnlavpna atalevsfvg yqskevaiag ehidiqlqss sdqgldevvv igygtarkkd
      121 ltgslvtiqa knfnkglmta pdqliqgktp gvmvinntgq pggsatvrir gnssirasnn
      181 plfvldgvpm sgnsplpagr ggfssdrgnp ltylnpsdia smdilkdasa taiygsrgan
      241 gvviittkkg vagepvvqig asagvsgmrq ypdvldaarf realnyytps eaansdfggn
      301 edafkaitrq aitqnyygdv sggseygkyr lsagylnqng iirgsqlkky tgnftgnfnf
      361 lenkrlgldv slfltqldnr yapinamvga egnvisqamq wnptlpirde ngnltfvstt
      421 trnpltsida fkdqsttntm vanlspyyki tddleyrfiy svmrqtgare gmyraglidp
      481 saseveqafi snnaetnlqm thtlsynkqi npdwningli gyeflnynyk nnmtfgggfk
      541 ymgldyfdyl qystvatrdi ssyksptnel qsmflrggfn yknrylftgt vrrdgstkfg
      601 snnkyaifps lavawnvnee efmqsneifd qlklrlgwgk tgnqefpsga slnrfifgnq
      661 sisqanygnd dlrwetssti nvgldfailk nrlygsidyf nkkttdalfe qtlaqpspag
      721 liwvnldgei vnkglevalt gtivntndwt wdltgnatfl qnsvsglvgy yetgalrgqg
      781 ftgvlgqrmv ngqplnvwyl aqyegidpdt gmsmyrgqdg sissqndpai nkfysnspnp
      841 ttllgistnv sykkltlsan mngafghylf nntaatvlgl snlssrnige qffdtsvkes
      901 tsnssapstr flekgdylkl anlslsyslg nigktfknfn vsvtgqnlfi ftkytgfdpe
      961 vntdgstngi pslgieylpy pparnillgv nfsl
//
LOCUS       WP_093095247             982 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093095247
VERSION     WP_093095247.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 982)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 982)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 982)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..982
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110313
     Region          24..981
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkpnimlvi lfsciqvlfa qnkiqlngev vnttgeklsg vtislsnsnq kymtdengsf
       61 sfeyvpgtnl tinslgfatq qitltnqtsl kvvlieseen leqivvvgyg tqrkgettgs
      121 vasvksesfn qgavkdagql iqgkvaglri ttpsgdpngs tqinlrglns iqgavnplvi
      181 idgvpgdfns vapediesvd vmkdgsaaai ygtratggvi fittkqnrst dgrttieynn
      241 yaslqtlfrv pelmnaedyr rliaegqnyt dlghstnwvd evtqnpfshn hnlslfggna
      301 rtnftgtvnf rdwngvllks gqqrlnarad lnhemfdgkl rsriqiisns ikalqggssn
      361 ymwrqalirn ptdriyndeg kwqennaymy dnplgminet vndrifretr mngsldyrpi
      421 eslsfkamfs rvqdndltgt stsfnhvntt knnlngtasr ftqagvenlm eltgnfnksf
      481 gdhnfavlgg yswqrntfen fsaynfnfpt dqysynsles gmalkeglat mdsykqestl
      541 vgffgrltyn ykekymamls lrregsstfg ennkwgnfpa vsvgwdmake dflmdqtain
      601 qlklragygv tgtiagspyn sqisynytfd qgayingkwv pgfvparnfn pdlrwerkne
      661 fnvgvdysla nnriygsldy ynrrvkdlly wfevpvppyl tstmfinage msnsgfealv
      721 nadvlnkagg vqwktgvvfs tnknklinls ndrfgvtqef fdagytgepi qtfthrvevg
      781 rsigdfyvwk tvgldedgkw lvesqngeii piqdasvedr qyygngipdf nlgwnnnfqy
      841 knidltinwr gafghqilnm prmyyenpvn kaynvlktay dpidgkllnn dlvyvshyie
      901 dadyfkldnl tlgytfnpql ikgisnlriy vsglnlvtft kykgldpeat syegefqfap
      961 giehrdrypt trtytiglnv kf
//
LOCUS       WP_093095560             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093095560
VERSION     WP_093095560.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109121
     Region          25..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkhkllyvl lfwlslvqmt yaqttisgkv vdglsgsals nvsvrikdtr iggvtdnngn
       61 fsinapklpa tflftmvgfe dqevrvsaas nnlmikmqen mnntlnevvv tglassikrk
      121 nlanavssvn aaeltgvakp qttdgalygk vtganirsns gapgggmsiq lrglsslvga
      181 sqpliildgv yvnnttqstg ratvsgagns sqddgsnrla dinpdeieni eilkgpsaaa
      241 iygtranagv iiittkkgke grtkvsised fglttplkll gyddwseeki nyfyggttqs
      301 qtnrrnlele rfretkannn fvdyedyfyn hqhfssntrl nvsggtdktk ffvagginde
      361 nglikntgfq rytvranidq kitnaiqlsv nssyirsntd rgftgnqnrt gasigyaiaa
      421 tpnyydlrqr pdgtypdnpy ftenpialtd kstnnslvnr sissfnlgid lfkgessymk
      481 fvlnggldyl qnttnihlpe dlqyqrsian pgdimngkqe sfntnlqaal vynfnlkrvn
      541 mnsqvgmvrl dfkddllfvr gqglaplqkn vkqaavqtif nqffmrtqea giflqqeanf
      601 edkiigtlgv rfdksslngd psklfafpka slamnltsfd flkdhfisql kpriaygeta
      661 gpvafgatys slvgvniggl lgsslsttvg nvnilpetak elelgvdvgi lknrlsleat
      721 yyikntanni qplnlspssg ftstssnlae lsnkgielsl sgtpferenf kwnsrlmfwk
      781 nditisklgi ptyttggfgv sygtflmkeg eklgtivgtp qinpgeytvw gnsqpkfnms
      841 fnnnftiykn fdfsflfdwk kggynvnltn lnldeggnsk dwfgdrngdg ipngkqrepe
      901 pfnnagrfve dasyiklrev glyysmptev tqrlfknkvq rfragisgnn lvmitkysgy
      961 dpetstfgng lannidvgpy psarrfflnl sldf
//
LOCUS       WP_093095983            1222 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093095983
VERSION     WP_093095983.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1222)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1222)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1222)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1222
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1222
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=137445
     Region          136..1219
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlyflvhkkl grgkgidlkf lvkilkfiil lillmlysii vkaneqlisv kfqkaklntv
       61 lkaianqtdy qffyndrvnl itgpvtidie kgtvvqilel ilpkeklaye isenqitisi
      121 rrqntltsie prqeniqgtv rdtegkplpa asvsikgtnk ststdqngkf eisalptdii
      181 ivsflgykrq evsiagrkti nismqrdqqt levvdvaatg yqtidrrkft gaatkvkaed
      241 aqrfgvpdvs rmlegqvsgv svqnvsgtfg aapkirvrga tsitgdnkpl wvidgiiled
      301 vvnisndqls tgdantllgs svaginpddi esfeilkdaa atslygaram ngviiittkk
      361 gragtqavsy lgnyttylrp sysqfdivns ydqmsiysei arkgaidyal irnnmnsgif
      421 gnlsrglstw kedgtplien tpegreaflk ryiyqntdwf ktlfnnsllq ehsvsfsngs
      481 nkvqtyysts flqdngwaka ngvrrytani rgnynitdkl sigllttgsi rdqkapgtlg
      541 qdsnpvtgvv srnfdinpfs yamntsrvia pfdengnren vtmnyapfni lneldknime
      601 lkmidlkvqg elnyklpknv nynfigayry astgnehkin etsnlsnayr agtiygvegi
      661 ensiianqnr flyrdpanpd arpmsvlpyg giyitnenil ksfylrnsfn wnltsqkhyf
      721 tafatqeirf ldrmtkdmtg ygyqfdkggv pfidpniikm tvegnlpyyk mqvfsdrfva
      781 faangtysfd sryqftgtar ydgsnqlgrs rvarwlptwn lsgswnidqe nffknqtffn
      841 tltlrgtygl tasmgpatna slvlrsgsvn rpfiheqepv inidflenqd ltwekqyetn
      901 igldatfanr ryqivldlyk rdafdligpm risgiggeai kfanyadmks rgiellfkat
      961 vfdrknwgwk tqltnafydn eitsirnepn iwnlvnsvga akegyphrgl fsidfeklne
     1021 fngtpifvne nneisnnvfl qsiqtnylky egpvdptfng gfynnfnykn lnlsflvtys
     1081 agnkvrlnpi yknqyselda msydfldrfl apyenlspsi atsrtssrlp gdqvynayny
     1141 tdqrvadggf irmkqvtlgy qfpkkffgks ifnnlslnlv annlfliysd pklngqdpef
     1201 ygsggvalpi prqftlsika gl
//
LOCUS       WP_093096105             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_093096105
VERSION     WP_093096105.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38819
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag ikasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_093097227            1009 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093097227
VERSION     WP_093097227.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1009
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112557
     Region          49..1008
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktnskiyg vslkclclif ltlpnsssgv fagnkshlis mpasfqqqkr iqgtvrdemg
       61 kplsgatirt kltknavsst adgsfeieva kngdwisvhm lgyqtaeiqv sdrteinitl
      121 kttstsldav vvvgygtqkr dqittsvasv kaedfikgav qdpaqlirgk vaglnivtpd
      181 anpvgnsqin lrgittltag tsplviidgv pgslqsvapq diesidvlkd ggaaaiygtr
      241 gtngvilitt rkpdgnleps iminsyissq qinrrldfms pegyrelvaq kkagaydygh
      301 stnwldeisr naisqvhnls isggskntsy lanlnlrddq giilksdnqr iiprvevshq
      361 mfdgklklta nltgsqqkyf agadgssyrg dvyrnaityn ptdplkdedg nwtehtdktn
      421 yanplallme tkgknqnttl rslgsinyrp iqgldimamg sreifnsvrg yyetknhyst
      481 rrdskngfas rgttrreesl meltanyqrn fgnhdlkgll gyswretnhe dywmqnwdfp
      541 sddfsynnig aglalsrgea pqnsyqssnr ligyffrlny ayknryllma sirregsskf
      601 grnnkygnfp aisagwnikn egflmdnqvl stlklrasfg itgtepetpy lslnrlnfds
      661 nallngvwsq vvnvssnanp nlrwerkqet nlgldfgfwn nrltgsidly qrktndllfd
      721 ysvptppyly nriranaasm enkgvevqln yspimhekfq wnssinystn rnkllslsdk
      781 sfqlaagyfd agtteepiqq sltriqigqp ignfygyksv didengywii egkdgkpkpi
      841 adqkaedkqi ignglpkhyl nfnnnfkygn fdlgismrga fgfdilnlpq mfysapvmlt
      901 rgnilansyd kiygkrplad dqslnylsyy iekgdywkid nvtlgyrlnf nqskiksmrl
      961 ylsgsnlvti tnysgidpet pivgltpgvd erdrypssrt ftlgasltf
//
LOCUS       WP_093097321            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093097321
VERSION     WP_093097321.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115154
     Region          24..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrllsvil lcllfvgvan aqlrqvsgkv tsasdgnsls gvsirvdgtn tatqsdgdgn
       61 ytidvsrena tlvfsyigya tqrvavgnqs tvnvqltssd neleevivta lgvkrekrel
      121 gysaeqvdsk tvnkasavni anglqgkvsg lnvttsnsgv fedvrinlrg irsltgnnnp
      181 llvlngvqmd ikylsslnpn dvenvsvlkg aaaaaiygpd arngvilvnt ksgsertdin
      241 vshstqwqni sffpklqkqf gqgydgiidp venwswgpay dgqiadigpq lpdgsqqttp
      301 yvgtderekf ydtgvtnqtn vsinakdffl slensdikgi vpgdknrrng irlnakrefg
      361 mfraganfny sqqnyntfnq sgpedyftaq gtggndglfs qlintpahip ltkykdyknd
      421 kfatyenwft nyglnpyftl dnwrttgkkq dlitnidlgl kpfdwldfty rasltsrgia
      481 erdltvgtks tpfgqsrgkt pipssleeys ynqtiltsel fanvtkqind dfkfngilgt
      541 fvrqneyrat tvgagnlvip elynisirtg nltgnsdgyk trlfstygsa gfnyknwanl
      601 eftgrwdkts tlapgnnsyf ypgvnaavvv sdalditsdf fnylkirgaw tktansdisp
      661 yfleatfsqa ngfpfgvvsg ltannesyny nlkperintt eagfeagfwn nrltleatyf
      721 fskntdqiir vstseasgys rtntnaasfn skgvdfdfnl splikfndgg infrgnflwn
      781 dsevtsiyea qglnqkelai ggyiaagnya ivgepafvmr gtdyerddqg hiivseadgr
      841 pftsstnvnf grtlpkwiig lnpsvnyknf nlsalfeykg ghvtsffglg samawtgvse
      901 ataynnrepf ilpnsviedp nnpgsyipnt takigenepi ynyytgefgn tasnfivsan
      961 hwrfrelals ydipeawlsa rqktlkglsi afvgrnlalw lpkenkfmdp dfdsmasdyp
     1021 naygnvndts nppvrnfgft inarf
//
LOCUS       WP_093097376            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093097376
VERSION     WP_093097376.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117400
     Region          27..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrtiyfylv glffaigigq tqaqniikgk vlnelnqais gatvidkttq kqtqtnaage
       61 fsidssnpkt qikvrflgyq dqdlevgase sntiklvpsn dvleevvvta lgisrekkal
      121 gyavqevkst elqtrptnam aalsgkvagl qivssggnmg gstrtllrgi nsiagsnqpl
      181 yvvdgtpidn sdlnssstin gsagkdvgnm iqdlnpddie nisvlkgpsa aalygsrasn
      241 gvilittkra gkgeqvsidl ntglefeniv rlpkrqhlyg qgysqnfqtv niegqdykiv
      301 dyaadeswgp kldgtpvlqw ynlnpedaad ylnpspwiyp ehdvsyffnt glantnnlai
      361 agnsgntnyr fsytnknvkg tvpnstlgrn tlnfsggtkl gklsinssin yihntslgkp
      421 wtgasnrnii leafqwgavq vdykrlenyk rpdgtplawn rtgwqntpaa eatrfidnpy
      481 wsayesylee krdrfygnig aqyevtdwlq igakvhgdiy qfgtqdriav ysrsasqyee
      541 tsnklneyny eflatakknw dkislvanvg anlrdqnrkv dyaitqggli vpnyynlkna
      601 ssvkienfty nrriaslygs asfgyndllf ldatvrndws stlpshansf iypsftgsfv
      661 fsqlpviqnl dwlsfgkvrl gwaqvgndtd pyqlnkvydv eqsfdgkpsn klpstlnnad
      721 lkpeitsswe tglnlqffkn rlgfdvtyyh ntsrnqilpi pvssafgyea kvlnagkven
      781 kgievilnat pvrtedfewn ssinwarnrn kvlkldelvn tltlsstlin lvaregqpyg
      841 qllgydfvya dgqrvikedg tyqrtsqlvp lgsvlpdylf gfqnsfrykn fnfgflidgr
      901 vggsfysqty nvgmysgile rtaennvred giilegvkad vvfnadgtys tsnirpndtr
      961 itaqqwgrne ssgpttfsif dgtfvklrev tlgytiplnn pkvvkgvrls ayarnvwniy
     1021 tkskyidpef tnssgnvqgi eggniptplt ygfnvnlkf
//
LOCUS       WP_093098101            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093098101
VERSION     WP_093098101.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117712
     Region          26..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklqkliili lsifslqfay aqnqnlrgrv vdesnngiag vtvinaatnr aitatddngn
       61 fgvsiapnta lifkavgfnq rrvtvranqt tltvqmsstq dqveevvvrg yvarkkentt
      121 gssftlgekd irdvptanle qlmqgkvpgl nvqvntgapg frgstqirgl stlsttgsgs
      181 esilmptspl yvidgvpmda drasefglqq qgpgisplsl ippedvqsie ilkdaqatsl
      241 ygsqgaygvi iittkrgnsp vprinythst flktppklre tlggnlerqi kiwqiinnar
      301 tqaeidrimq tpmladslna ffnnstnwqs lyyqntfnqn hnlsldggne ilsyksnlgy
      361 ygetgviknt gfnrysanlr mdyrptkrfe ftgqvfaqlg kqnkgdgtgi lqtgvstggm
      421 nstllpppgf fsadndyisa irtkndnssk lirpyvegkf eiipglrlqs amsyefasnn
      481 edkftpaaaa gqfsevysfa gresnlynrn ilnytkdine dhnifinlfn evrhnqrqnt
      541 itkqartpnd qfegplgfdg yfsrgggvls nfrnekalsf alattysyks kyildlsyrl
      601 dgssangfkn lytknpavgf rwnahheewi ktlpwinlas lrftwgvnvm ptstleriyg
      661 kydisglynq ingiginyef ipnpnllpvt smqynlgvdl tflnnkieii ydtyykrven
      721 llfesflnnt sgfdklhsnd aglanyghei alnfrplsvn spfnwtlsin gaynqdvllq
      781 lpdnfrgqfi kwdgqadrlh mvnrvgtsal snyllenigv yatdadvpvd patglryrts
      841 dgtffqagdp iyvdrngdyi ldnrdyarag ntqplwtggv qntlnyknfq lsiyasytak
      901 rtilnyalaq rlnlyrdpfg gglvggksdg ataivpienl diwlkdgdia kypypydfsr
      961 ngsvqpfryd qtlweengsy fkinniifay vfdrdmlrrf kldrfriyas mdnvysfssy
     1021 sgpnpenvts lgrdasngyp vprtytlgfn lsf
//
LOCUS       WP_093098097             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093098097
VERSION     WP_093098097.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112308
     Region          65..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msvlwkfksl lifmsmsvgh ahshnvdfan lslqdttgtd sipaidtlae lkplyeldlp
       61 kfntlrnmkt nslitanslq qyikgelpgv yvsessgepg sniqmfvrgi skpilnnrdi
      121 yntqplvvld gvpligehpf afdvqnfdie rigtennllg nidfdniqsi rvlkdlsaia
      181 tygplaangv ieitsrkpeg dgdkriavns yigmsqrpsv ttingayena frkqfydlyt
      241 tngkynqddv ypiylsdsln ndyygpsnws dsyysnglnh ginanisggq pratfqfslg
      301 nvkttgvadd tkfdkynarf flnlrpfkwl nfetlfnasr lnrdrnrnlr nrfammgylp
      361 dlgaplapnk evydlylkef dksfdnnfsn ilegffrlqv nvgalkirsk favdynegyr
      421 dlfypstile ksnfasnyyg ynqrllvdnq vsydiendan yfyfeagntl mwdtykynya
      481 yaykgvndfi kinlldsdpn sgnylnptaf prqlvykfld rtkhnmvnfy gkasytynea
      541 ytaaltlryd assnaqpttr wflspilalg wnakndfmkd nesvslfnir asvgrighyn
      601 lydnygqgps ytaeigytgn aivpgyngfa alvrpynvgw vgydlpwsys dnlnlgfdlg
      661 fknrdiqvsf dayirdskdq limlpgkkdf gydyqyeagm dvrnmgidls asgnvvqndk
      721 itwntglvlg vntnkllalp nnldeievnd rllkvgerid afwlyenngm yqtdqevpqs
      781 ggqrmtyngi ilkagdpiws dtngdnqitk edkvlqgnii pklsgswnnm vayknfdlnl
      841 nfyfnlgrki vnqemsnrfn fienenassi nsikeitfwe krgdydkypl ynpwssvapf
      901 qtnqslfled gsflklrtvt lgynfkdiig drlgkkgdfy vylsannlft vskysgrdpe
      961 lvnymgydqg yslpiprtfa lgfklkl
//
LOCUS       WP_093098480            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093098480
VERSION     WP_093098480.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117148
     Region          64..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mswnkpndvp ninylkpmnl lklvlcsssi lfmanaeaap hylwktdkie snldysfglp
       61 qqttvkgvlv deqgapvpna silvkgtneg sksddqgrfs fqttkpkgvl vishmsyatt
      121 empintatqm rivlkensst dieevvvtsf gikrdrktlg ygvaevkade lsksptpdvt
      181 nalagrlsgv qvsgsgggfa gsnitirgfs tftgsnqply vvdgipldns gggnsvnsgv
      241 vnssrisdin pqdiesmsvl kgaaatvlyg sraasgvili ttkkakkgik nqisvgtntg
      301 vgmvsrmpaf qneyaqgsng nynnsvtgsw gpkiagqevt nwfgdkenlq aypdnindil
      361 qnsvssvndl sftgsgekyd yrvsygytve tgllpsnklt rnnisvnast dltdkfkvgt
      421 sfsyvnnvsn rtqagnqgan plwrgiytpr sydltnmpfk daegnqlwfa pedhpywsie
      481 nirnnnevnr fygninlkyd fldwltadlk vgadvfsmvs kgfdnkgirs ngntssagag
      541 gvqdrnvsmk ninsyftvta nkkvfenwnl iatvgneiia nnrntlqstg lgivlpnfdn
      601 qsnfltfnts gninqnrqvg vfadvvmdyk sylslnvkar ndfsstlskg nqsifypaaa
      661 vslvltdafp slksnvltma kvranvgevg kgtepyatnt yfgrasasdg fvstlvsfpy
      721 nglagytlnn sagnndlrpe ftreyelgld lslyngrisf egsvyerdtr nlifavpaps
      781 ssgftsmvtn agslstkgie lmlnlvpvqk enftwrsgfn ftkfksivee lapgvsnisi
      841 ggftspnirl vagqeygqiw snayqrddqg rmiinanglp kpttsvqkvg npnpkfnlgw
      901 tndfnykdft lsflvdfkyk gdvmsrtigd lriqgvaeet aeferidgsg nvtkpyifeg
      961 vlengspntt yvsaqqyysl qgkyvawegy vldgtfvklr eanisyklpt kwlegqnfik
     1021 gvnisvygrn lltyapnfph ldpeqnllgi snarglefgf sptprtiggs vrfsl
//
LOCUS       WP_093098783            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093098783
VERSION     WP_093098783.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119814
     Region          24..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrlitsla aslffstvlf aqtqlkgrvv desgapisgv tltlkngtat qtgangeftl
       61 sydqagqlnv salgysrkvi nlsnqttlei ildpstegld evvvtalgis rekkslpftv
      121 qevgakeltq agqlnvtsal sgkvagvqvn qfggtvgass rislrgnssv kadqqplivv
      181 dgvpisndtq rsgdntysgv dygsgindin pedietitvl kggsaalygm ragngvilit
      241 tksgkrgdkg iqlsydgnfs vdqaaylpkv qnlygqgyng dekhyndfqa sngkisyqdy
      301 aqtkgfayvd gtgqtgvwdg fdeswgprld vglnlpqfds pvnngvrtpt pwvsqkdnir
      361 dffqpgfsmn hnlsilaqsd ksstraslsf rdqngtvpnt dqkryslqln nntnisekvs
      421 fdvstnytrt esdnilnqgy dgnnpmngfi wsgrqinmqs lkdnwdqrde qgnytyynwn
      481 tnyhvnpyfn iyentnsykr drffgkssly yqpfeflkfe gragldyynl kafeknyyns
      541 afpyggfrdr ktdntelnld fiatfnkqfg dfnvlasaga nyrnlmwetn vmgadaltvl
      601 gvytianrvg davttmdhsh vrsnsvfata nlgwkdqiym dltarndwss tikddffyps
      661 ismswlptss fpslrnsvln fwkirggwae igagttayqn rayyypqnna fggvaqmfrs
      721 mvfpnanlrp eqirtweigt eigflddrih advvyyykst kdqilavtts nvvgfssmll
      781 nageienkgi evqlrgdvir keegfnwtty inyakdnskv ielypeldln vyqigwtwgi
      841 anvarkgerw gsligggydr vedgpmkgai kvnnrglvvn knaqiigntt pkflaswrnd
      901 frykdfsmgf mfdlrvggdi wsqtmshsyt agvaaitaen girekaivag rdvmtdekfv
      961 mqdangnwve ntietdaqtw fesggiaqty vfdgsflklr eaylsynvps rylqnmrgik
     1021 rvnlsligsn lallwthksn tmridpetgg vssdsrgvgf eqasvpssrs iglklgvtf
//
LOCUS       WP_093098818            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093098818
VERSION     WP_093098818.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115662
     Region          27..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlptclsia vaslcsiqml saqqlsiagk vtnaegepiv gasifvkgtq qgtssnesgl
       61 ftlnapssgt lliravgyap levpisgrtn isiqlqhdds eidevvvtal giqrsekslg
      121 ygaqsvnsat lnsnkqpnlv nalqgkiaga tisstggapg qganiqirgi nsidptrdnq
      181 plfvidgilm dnststqgga evrgmsnrsv dinpddieti nilkggaata lyglrgangv
      241 viittksgka gslkidyqgt vgfenvnkfp kmqdtytqgw kgvydkddfw pawgptiada
      301 ikvdpthptt lykpfeeafe tgnqfrnsls fsggsekfsf ltsvsqlkhn gvlpatdfkn
      361 yqarlntnft lseklkggss lavtnsggyr gnanryaeql iywtprynvr dylmdngtmk
      421 sygetdnpiy vahtnrfkdd vlrviggfdl tyspakwvdl myrvgidayr dnregtaigy
      481 qgladerlvy dngvegadgr gfynvynnnf raltstfiat fkhdfnddln atlrvgqdvy
      541 drfikrtate ggdltvynwf dlgnaniika atynekyrlm gffgelnlay kdylfltltg
      601 rnditstlsk nnrsffypsa tlsyvlsdqf smpeainfak lrlsyaqigk daapystsag
      661 fapytnlptg yigftrpsll gdpqlkpeft dtyevgmemk flnsrlgldv nfynsvskdq
      721 iiqvpvsstt gfvtasinag sirnrgleit lnttpvkkdn fswnsdinfs fnrnkilyir
      781 edlddeivvs seygylnstv smrirpgesy gtlygrtykr yytpdeiaqg ldktreydes
      841 rpmligangf pvlestsvpk klgnvqpswv ggwnntfnyk slslnvlvda rvgqyrynql
      901 gnfmaafgea dytenrndyk vfdgvladgs kntkevwlgq gkdpkngvdy gngyyrdnfr
      961 gnsqafveda swlrlrsvsi gyslpqqwle nkfvknarvs lignnlalwt kysgydpens
     1021 ttasgsnieg fagmtypavr sflfslnvgf
//
LOCUS       WP_093099456            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093099456
VERSION     WP_093099456.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122780
     Region          68..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqhktfknai pkfllrsssa vkpfinenyc lkeiflfpil ltigffllgn qlvaqehltm
       61 etkgklatgt vldavtgkpv qgvsirglev eaktdskgrf qlssdsserr islshvgyrd
      121 tailwdpsil smeimlvpva nmieqvevvs tgyqsiprer atgsfsfvds ktirrnpgms
      181 llsrlngvtn gllidrntgn pdglsvrgrs tifsstrpli vvdnfpyegd ldninpndiq
      241 svtvlkdata asiwgvrsgn gvivittkkp kdrlsvefss nflfrkrpdl sterwmsssd
      301 fidseiflfe kgyydrdinv pyqqispvve ilaqvrdgsl selqgnsqid gyrgqdvrad
      361 lekyfyrdlf qhqqqfsvss stpsfrnils ggidrsisdr vgsengrtsv rnasiwsllk
      421 drmtlnsevw yvqsssqvgn sqgytpkypy erladgngna leasygtstl rrsytdtags
      481 ghlldwkyrp ldelrgslss selsdkqlrf nfgikgklyr slslgisyln stnwqegsll
      541 ygkesfyvrn lvnqfssfdp vngtmvspip vggilsrngt rmgsrygraq adwnetiadr
      601 hsisgllgme frqdrrtfed hgllygydpv lenfstvdif tyfplyhkgt ysrianggsr
      661 tryvdnnrsf yglvsysyrg nlalnasfrk desnifgvka nqkgvplwsv gaaysfheai
      721 gwkpldmlkl ratygyngni dkntsaflts tlfrtlnpwg ypidrilnpp nstlrwervr
      781 nvnigldfsl fgdrfggsle yyskkgmdlm gnsplapqtg vtefygnvan tltdgvdlql
      841 ralwlerggf gfrsdlifna vsdrvtkylm dpganrdivf asgivplvgh pinslvlfrs
      901 sgldgngdpk gwsdggpste ysdilngldr tgitimgskv ptrfgslrnt vsyrgaelsf
      961 qvlykwgnfv rvnnsfssng lisgsyrfsd yasrwqeagd egstdvprfn ypmnanredf
     1021 yqssevlaip ggtvrlqdvr lsylvrpfeg rrnsalqlyv yasnlgllwk qndrglnpdl
     1081 isgyrvpsew sigmkfny
//
LOCUS       WP_093099541             983 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093099541
VERSION     WP_093099541.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..983
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109873
     Region          30..978
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkftsktiar safllliclv cttrafsqqr tingkvrtad nvplsnvsvl lkgtnigsqt
       61 nddgqfqisv pndgilifsi igyttqetdi kgkdylnvil epdnkaidev vvmgysqvek
      121 qhvassvasl dmestktrpi fkmeeafsgt vpgvtmlqgs nipgavpgti sirgistlqn
      181 adalvivdgm eqsitdldpn qiksitvlkd aastsmygsr gangviivet ergytgkfkv
      241 dlnawgafsn pidlpnwvna aeymklnnet rahqnqtllf tdedirkaes getrsvnwld
      301 eimtrkpfan nttanisggg gvgtfnlmlg higekglndi egtekfsarf ntniniadkf
      361 vlladfyahr lqvdrlmand nghglyqiaw rmnptqqify gdtdipehyi lhnnmnplas
      421 iakggiknyl hdrstinlrp ryninknlni egnvsymink sankaerrtf kfydgdgapv
      481 tiwnnsvtae qgvsssqlta ralanytkdl rdnkdklylt lgtemmsyty tdyreenkas
      541 ffgklnysfd nrylieltgr sdgsskfapg nkwgffpsaa iawnmhnesf fsslresgai
      601 nnlkirasyg lignenvapy lwqeivnnwg wtirvpnpdf swekqkqwni gmdltalnnr
      661 lsltaevydk fsydliynnf pvppltgsnt lesavnigev qnkgwelsak wsdrignlky
      721 nvgamlfdni nkvlkagynk gdtlifkgds dkiwyngaai dnyygfesng yfqnateven
      781 teaklpntlp gdirykdqng dgiindqdri ylgdpfphmn ysinlglnyk nwdfsvmgqg
      841 vgkrngrlvg megypvyvdg dsnslgtprk eyadnrwtes npnarfpriw sgnssnayls
      901 dvwlgdasyf rikmiqlgyt fpgigksikn irlyvnaqda ftftkwegle pergldkskt
      961 enqgngvypr matysfgvra tif
//
LOCUS       WP_093099331            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093099331
VERSION     WP_093099331.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121437
     Region          31..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnlfyhslr gslllailcc ihfaafsqta lkgtvtdplg nplegvtvsn qtqghvtktd
       61 eqggfsvqak vsdvisfssi gyqshkltle nlasvrisld psgedleevv vlgygsikks
      121 nltgsvsrld krvletgvrs npasalagti pglrvqqtsg rpgsvpnivl rggttygggg
      181 splvivdgli rsgfsdinqd diesidvlkd asataiygar asngvvlitt krgkdgvsni
      241 slkskigvns lnipfeflda edylywsrkg vqtsgmyqpn qlnqltsvgp fgtgnkykdd
      301 qgnildgnkv snavwstmfl ddsnrelleq gyqtmidpvt gkeliykdfd ytdyalrkna
      361 ltqdynlavq ggndkskyya slgkyyeqgv pigtnydrlt filngdykik pwitsnsgln
      421 fantkwrdai ngegnymtra lgapptmrgy nangdllvgr dwqdgnpavn ndrfirnnqn
      481 qkftmsqafv idlyeglslr tsgnwfinqt nnesfnrdyl aspgnwvrtr nssasydktl
      541 nqtynavlny kntfgekhnf damagweffd syntgfsasg sgapsddfmd lgltsteanr
      601 rgidsyhvrn ritsffgrln ydyderylmt ltlrrdgysn llnnrwgtfp gvslgwnlhn
      661 edffanimga dqvintlklr asygangnig sigaytlqgt ygtskydgnv gygmtslsip
      721 nlkweslitk evgletrlln rldlsvsyyh rttsdkiatl llpasagfts ittnngdmqn
      781 qgveidlnyq avrandftls fnwntaynen kilklpyngv ennrqngfqv ynpstmelkw
      841 vgglqegqdp nvayayealg iirnqqdldn yalqlkdlig artlvhpdvf namtaseksl
      901 hyplalgdvm wrdvnkdgii nsydrvymgn tvprwtggfg lystykdfsl sarfdyalgy
      961 vaydgprawf lgmmqgtfnt ttevldtytp entnakypty ywadqlfknn tsressmfyn
     1021 kgnylafrei slayrlprsf ankikmedls vsvtgqnlqy wtantlfsae sgsigqgggg
     1081 yplprtvifg lqltf
//
LOCUS       WP_093100529            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093100529
VERSION     WP_093100529.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111489
     Region          50..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikrfsspff plkrsqlvag aiilglslts gyaaahdlsk dkkeihafqq evegkvtsgg
       61 vvlpgvtvsv kedpsrstst taegefsita eigqtlvfsa lghekkevav tgatlnvels
      121 aseenidevv vtgystqkkg eisasivsld qkklkdsksp nvsnllqgkv agvdvvgtgr
      181 pgqqanvkir grsslssgtn plwvvdgvit hgvaninpnd ietisvlkda aattqygsrg
      241 tngvivvttk ralregegtf svnlssgvsk fnfgnfelmn sqelwdyyqt fpnqkdidpn
      301 vtkdvlnndy nwikngtqta pvndfsanym gktektsvfa sanyygekgs lkgydfermt
      361 grfnvehklt drltfkpkln aayttyldkq hslynmmfyl pwdnpynadg tiknpqdada
      421 nvlwlgrdht nylydlqyny gkgqtfdmqg nfdfsyrisd rftfesmnnl tyynqttmsy
      481 adpnsnagrn dkgtiyqfsd kritrffnqm lkynetfgkh svsgfaayey sdyvysslna
      541 kgkgiapgsq ilgnaasvld fggtkndysf qsgilqgtyg ydnrynlmas frvdgssrfg
      601 qnqqygafys vsgawninne affnvpainl lrlkasyggv gnvpidyyss fatyglnaqy
      661 ngepaaiqkn fqnanvswek sydanlglel gmfnrlnlsv dlynkntsgl lyyvefpsta
      721 gwdgywlnig glrnrgveva lsgsvfslen pfqwdlgvni ahnnnkitsl kdgqdipkgn
      781 mrfseghdvd swymrkwagv npengdplwe tideetgevs ttsnyndaal qfvgaatpkf
      841 qggfnsamny kgfnlnasfa yqnggvtyna arelfdsdga yasynqmilm dgwsrwsadn
      901 pnathpraey nntslsnkts srylestnfl rlrnvtlgyt fseslvsklk lkglnvylsg
      961 dnlwtstkfs gldpeaailg ndnsadkaag gdatsqypap krlifglnlt f
//
LOCUS       WP_093100608            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093100608
VERSION     WP_093100608.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119698
     Region          12..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlfslsslfa qqtvtgrvtd pngaglpgvs vsvvgtnkaa qsnmegnysi eanngqklrf
       61 tsvgyqtqev nvtsstlnvt mqedagnide vvvtamgikr apkelgyams tveakeltkt
      121 gspnfagaly gkapgvrisa apggatsgin inirgvnsit gnsqpliiid gvpmrtttfn
      181 nsnywgdqra rgngledlnp ediesitvlk gasaaalygs ealngvvmvt tksgkggegv
      241 aidfnatyth dqiaylprfq dvrgpgyttq yadagqgedm ffyygddlav dgvkrgllga
      301 tinfgpkfdg qpvvswdgkv rpyvaqnayg klfnnpnnti fnlalshtsd kantrfsltr
      361 qdnemtalss ynkkniasin stmkfwdklt tdivvnyvnq hthnrpfltd rlvnnftgmi
      421 stfdnpewyl drystslgyk yvtgsnqslt peenlrhngy kadvldfmwn nlarqydeys
      481 nrvigsftnt wqvtqdfsir grfsadmtnl ktddkqpnei pvafgqsgyy asnnttaniy
      541 ytdllasysk qitedvklga mlgytatkln ttnltantdg glsvrnwydi sasnnlsrgn
      601 stklnslrda tfgtinfnfk dfwfvegtlr reqisqmhpd nnvlyypsvn tsiilneafq
      661 mpeffnyakl rgsygivgky pdiylsalsy sqatlgnqgt gasvlytqip tssfgnekik
      721 penkheleig letrlfnnkl gldftyyngk ivdqilnytl pystgsnsil anvgtlrntg
      781 yefalngapi sndnfkwnsi lnfafnrnkv ealpggasql mladydgsaa rlvanvgqsm
      841 gdimvhpyvy dasgkkivnd nglyqldpde wvkagnampk vtggfintft yknitldali
      901 dfrwgghamp tginwmksrg lleetltamd aehgglsyyi kdgkgiattg nagpagekvf
      961 hdgmvmdgvl adgspntnii sqayyyaqty nwggpqysns nyglyvqknn yiklrelslg
     1021 yrlpasvaks lraknlqisa farnlffiyr smkdldpeqm tggsywvnnv tnagtspatr
     1081 tygfmlrasf
//
LOCUS       WP_093100888            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093100888
VERSION     WP_093100888.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119800
     Region          33..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkiilifa ivfistlely aqikpidgki fqdpdgspig satitssrnn tsvysdssgr
       61 fridvdhkad tlivshfgfe tkripidski typleiflei sttaiseivl ntgyqtlpke
      121 ratgsffqid nqalnkrvgg nildrlegls gsllidrrne eptiqirgis tlngdimkpl
      181 ivldnfpyeg dlsninpndi esitvlkdaa assiwgarag ngvivinskr tgtnqkplin
      241 fnsnltlspk pnlytadqig vgafvdleae lfdlgfydil fsdptyspmp qtaeileklr
      301 qglisrsesd rlinelkkkd lrsdmsryly rpavkqqyha gingtgkgir ylfstgfdsd
      361 lnslkgnsnq ritlrtnnsi ditdriefqi gsiyttnkst lnspggygsy mysttispya
      421 slvdeygkpa sldlfyrgef tdlalengll dwkyrplqel ynndkssknn dllinlglny
      481 kvldwlnvgv kyqnqkswia trwnngleny atrdiinrys qldgdrvisp iprksilhtt
      541 dventtqalr gqieiakdwa nlheinaiag geirqnnrkt tgdviygyde nllsiasinf
      601 aqqyptyeyl ygntfipngk nlnettnrfi slftniayty nkkytlsasa rrdasnlfgv
      661 ktnqkwvplw sigglwrvdq eswvdiptft slnlrvsygl sgnlspnass lariayydaa
      721 rspiglqsag ivsppnpnlr weqvktfnlg vdfgmlngrl tgsidvykkn sydllnskkf
      781 dpitgtmtai qnsaslaskg ldlvltsvnt ngeikwsssf llnfvsykvt enldpipleg
      841 lvssgntifp vigyspylla sykwaglnpe ngnprgyvng qisedyneiv knpieeqvvh
      901 gaalpplfgn lrnsfewnnf slsfnisyrl nyyfrkpslt ftgllqngsg ygygefenrw
      961 kypgderttn vpsflypady qrdnfyvnse invekadnik leevflqynl renavgikgi
     1021 kgiqlytyln nlnlflwkan kvnldpdrla nfrtpinmsl glkitfq
//
LOCUS       WP_093101052            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093101052
VERSION     WP_093101052.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117740
     Region          24..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkllslif vltcmisvaf aqdrqvsgkv tsvtdgapls gvsvalvgts iatqtdadgg
       61 ytitvadgkt vlnfsfvgyt skrvdvanqt tanvqlvede msldevvvvg ygsttkeaft
      121 gsakkvdgtk lqqkntsnvs qaiagevagl qvtnttgqpg tastvrirgf gsvngnrdpl
      181 yvvdgvpfsg nitsinnadi dnvtvlkdaa ataiygsrga ngvivittkt grgqssfiea
      241 dvnfgtnmsl lprydviksp eeyiglswea mynegvlage dgaayaneyl fsdrginpln
      301 nlwnvssvsd lidpvtrkvk nnvtrkfdpe nwedhafqna artdlnvrfg gatdktnyft
      361 sfgylgdkgy sinsdferft grvsldhkvt nwltvgmntn yskverntgg qsedsgsifw
      421 fvdnipsiyp lferdengnk iddnifggyv ydygtnsgrk fgsltnaiad atydikrhkr
      481 nelngrayvn fniidgltfe nslgiqyynn iyndrankfy gssasqngsl yqsrtelnyf
      541 nllnllryrk dfgdhsleal vaheavkwes nilnasgynl vdnnildfnn vivsnpvksy
      601 teayalesyf gqvnydyknk yylsgtvrrd gssrfkkdkw gtfgslgagw ivsnenfmqd
      661 qdifnflkyk vsygvlgeqa gvgyypgydl ysvdnlnnnp afsfvtkgne dltwetskmf
      721 qtgiefelgn yisgtveyyv kntdnlifdr gvgpsigypt ikvndgqlrn qgiefdlvgh
      781 ilkgqdyyld lgingesfkn kitkmpieps tnlpkeidiq gvygwskdhs lydfymrdfv
      841 gvdaetgesq fkvfytdnna ngqfdtgeqi tsmalfdnpe nkeikegttt vyseatqhyv
      901 gksaipklrg avnlragykg fdlsvqmlys lggyaydgay ailmnndvig gnnwhtdmfn
      961 rwqqpgditn vprlnndndv gvnssstrfl tsanylmlnn vrlgynfktn vldaigakal
     1021 giwvsadnla iasarkgfnp sthqagsssm yrysplstvs aglrvkf
//
LOCUS       WP_093101055            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093101055
VERSION     WP_093101055.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116168
     Region          24..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrllsvll lctmligvvh aqdrqvsgkv taasdgspia gasvrvvdln satqtdefgn
       61 ysisvpangk ltftyigyes qtitvgsqtt invrlvggen dleevvvtal giertrksig
      121 ysvqqvkged ltqarqadln talagkvsgi qirtgsgakf gtaairirgi nnltggnpiy
      181 vvdgvitgpe yvnnddiesl svlkgpaata lygqrgaega vviktksgka tpgigievnq
      241 atsfenvygl payqneyggg ynqefstfky dpsihadylk aldgakyynf sadeswghkl
      301 dgsmiapwya wdpthpkfgq laafspqpdn vksffetgit astnvavskr tddlnsrlsy
      361 tnlsrtgvmp nskqgkhwlg anaalnlsdk ltvstnlnfi fedrfntpid gyssgpqssf
      421 nqwfarnlnm ddlkdyqrpd gtyrswnmis ptntapkywd npythvyknt akdirkrlyg
      481 nvsavykfne hwkasaiarg nffngeqnsr iasntlsqde yyqylnnqqe lnfvgsldyt
      541 tkiqdfdiaa svfienrrnk rtytdartag glavpdlytl sasknrptln sflsdykvns
      601 lygyitlgfr dflfleanar ndwssslpkk nnsylyggls gsflfsefie sdwfsygklr
      661 asiarvgtdt dpfrvaqtys ignpygsspl ltvpnqlvnt elkptlsssi evgtelrffh
      721 drltfdynyy trsskdqiip ltvtsasgya ttainagqid nwghefslgg tpikndnfsw
      781 nlnanlgink nkvvelyedp vnnivvnnlr vtvdgtrnsf gfvgapliav narkgeafgm
      841 ltgsgfkrnd kgekivgadg fyvptsgdid lgsilpdftg gltsqfnykg itagfsldfq
      901 kggkymsiss mfgngsglye etagvndkgn pkrdpvdqgg gvlldgvked gsqndvyvdv
      961 qqlyqdklns gniwenwvyd asyvkmrein vgytfpdrmf gktpfkkvsl tliaqnpfli
     1021 yaknrnfdps ilegswfegg qlpntrtfgf nlrfsl
//
LOCUS       WP_093101237            1156 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093101237
VERSION     WP_093101237.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1156)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1156)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1156)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1156
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1156
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126802
     Region          74..1155
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrlilfsla lgltmptyas feankgival gnhaswtnas svlqntvtgt vsgpdgplag
       61 vtvsvvgssv kastdesgkf sisaavgstl rfsyvgyesk evtvagntmn vtlqsssdll
      121 devvvvgygt qkkgnltgav stisvkdnle grpiadvgrg iqgvtpgltv tvpsgevgsd
      181 prikirgava slqasgdpli lldnveipsi qyvnpddies itvlkdaass siygakaafg
      241 vilittktga kgekidisys nnfsfqnpfk qyemgrinal kytkdamerv gsnisgafyy
      301 vtpegyemak ewddkygstl gpndptvfgr dwivdptnts rkiglrtydp ydymvrewap
      361 titnnaslng svgrtkytat fghiaqsgml kagdsdkfkr anaavrvstd vsdyltlrag
      421 amfaqrqkly pyatnsttad pwyymyrwss vypmgldeng skirspwsey edaneasmkr
      481 nyinlnagat vnmtknwrld vdynftnedy dwfrpgtrft aanswiapiq rldangnqvy
      541 vdntgavvpa gspgaiaayd lntheytapg anpdhvyara ayeykhtfna fstynlnlen
      601 ghefkfmlgs nlvsdygkyn wtqktnlldl snpqfdlasg tvtgsggtyw tsqvgffgrv
      661 nyafknkyll eanarydgss kfvddliwrw ftsasagwva seenfmqwak palshlkfrg
      721 sygvignqav paslytpnmf pyetlwiggq nkyygvptpt fslrdiswed letidfgvda
      781 rflnnklglv fdyyvrntnn mfvglqgttw ttggaaplgn fgtlktkgye vavdynhrfn
      841 nglginvran fddaisrfyn vtsqrttgsy ydgaaygdiw gyetdrlyqm ddfvlgadgk
      901 pklinltedm tkyyangdgk anqlkdpngv yqprlentnt fnfgpgdvkf kdlngdgeid
      961 ngdgtvdnpg drkiignttp rynyglrlga dykgfdfsif fqgtgqramw gngalaiagy
     1021 ntadgampaa ivddywtpdn tgafypaafn nagsndannm qvqskylldl sytriknitf
     1081 gyvlpksfia paklsnvrvy valenfftwd klnglpidpe vvsgfsmfne snyntgrtgv
     1141 gtpsfksasf gvqlnf
//
LOCUS       WP_093101555            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093101555
VERSION     WP_093101555.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113685
     Region          24..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrllsmlv lcvlligssy aqnrqvtgkv tsasdgapis gvsvrvvgss vatqtsgdgt
       61 ysiavpdnng slsftyigyq tfqvsignra vinvelgsdd qtldevvvtg ylvqsrkdft
      121 gssakvgget vanrplqsft qgltgqatgv nivqpsgvln nppvvrvrgl sslslnsfpl
      181 vvvdgipist gdvsenssan nplgdinped iesidilkda astaiygsrg asgvliittk
      241 kgktgaakva ydgwfgtska vrlpeimnaa qyiahkngai anarelnpkl pvasfpvggg
      301 ffptldengn pidtrwydyv yrdgfshnhn lsvnggtekt kyffsgnlsd qdgilfnntf
      361 krkgvranle hrlndwiklg tnltftnsdn rspnsgsveg aafntsglgr iamvqapnvp
      421 aflpngdynv sgssigkgan vlapnypnpl pirdldknss etsrffanvs aevklldglt
      481 lnnnfnwdlr nttnqqfwnp ingdgysyng yaynnqaknn nwllfnalvy nkafgnhnlt
      541 vlggheaqst rtenwgavry dltdgffdqf qgnyltndag gngigelnld syfaslnyny
      601 ankyfftanf rrdglsslap gkkwgnfgga svgwtvseee ffkssslsnv fsnfrlrgsw
      661 grvgnsslsn lygsfdtydp aiygsvggmv fsqtgnkelt wetadqtnvg ldlgfwnnrv
      721 sleanyynkn hnglilavpq tpskgipgns ilmnigsmyn rgfefalnvr avekenfkwt
      781 tslnfstnkn evtaldnqgr pliattsgle ttsitevgks aaqiyavptv ginpengrri
      841 fvnlkgeqvq ylhnapdteg nynytymnge kansvagqav asgntlptyf ggfnnsfqyk
      901 sfdatlnftf sggnyiyngs raglrdqriw nnsvdmlnaw tptnkntdip raiygdnisn
      961 gsafaigsni ekgdfirlqt aslgyrlpgs vfgnsgissl riyaavnnaf litkytgvdp
     1021 eissngngnl nsgvernsmp ngrtftfgin lgf
//
LOCUS       WP_093101652            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium mizutaii].
ACCESSION   WP_093101652
VERSION     WP_093101652.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium mizutaii (Flavobacterium mizutaii)
  ORGANISM  Sphingobacterium mizutaii
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Sphingobacterium mizutaii"
                     /db_xref="taxon:1010"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116010
     Region          24..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkllsffv lfslsigllh aqnrqvsgrv tdattgapls gvsvklvgls tatqtddqgn
       61 ysltvnengr ltfsfigyes qtqsvsgksi lnisltsiad aldevvvvay gtvskkshvg
      121 ssaqvsskei enrpltnvss alvgsapgvq gtlsggapgs aanirirgfg sinasnnply
      181 vvdgipydga vsnvnpddve sisvlkdaat talygsrgan gvimittkkg kynsgnftan
      241 asagiirrgl peydridamq yypvmwqalk nslvtnglpd diarqiasgk ltsyngnnyt
      301 gifsqlgynp fnvdndaivd vngvlnpsak lkwaddldwe neilsggrkr qaygitydgg
      361 sekstyfanl gytndegyll ksslkrinar anittqatkw lrtglnlngn ynvnlfdnag
      421 dggtsfinpf fysrnvgpiy pvhlhdpvtg elildefger kfdfgdkrpf spgrhalyen
      481 tldeqrnvrs tlggrtfmei qilpqlkast nigldvqdsh eryydnpilg dgspagrayh
      541 ylyrttsytw nqileynqsf ndhnvglmvg henysykyny lsgsrsemiv dgitelpnfa
      601 tvlgtssyed nraiesyfsr lsydykgkyi ftgtlrrdgn srfhkdfrwa nfwsiggayn
      661 igeedfinkd kinmlkirss ygsvgndagi snyayqalyt lgvnnasnpg ftqsslpnds
      721 itwetaknfd vgvdfelfnr rvsgsveyfd rrttglifpv pmalmnggvv nsspyyhtid
      781 mnignlynrg vemsltghvv rkeglsystt lnlthlknqi tsmppgtpli tsgtkaysvg
      841 hsiydyylrd fygvdsengd alyrtnemta nakiigadtv tnvlseanlr figktaipdl
      901 ygsmshnlsy kgfdlnvlft fqlggyvyds qygslmssgn ygnakhvdvl nawqkpgdqt
      961 niprmdggnt snlsggssry ltkasylnln sitlgynlpk nmlntvavke ayiflsgenl
     1021 affnkrkgmn nlgafngvvd ntynfnrlft vgarikf
//
LOCUS       WP_093109933             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. CF079].
ACCESSION   WP_093109933
VERSION     WP_093109933.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. CF079
  ORGANISM  Variovorax sp. CF079
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Variovorax sp. CF079"
                     /db_xref="taxon:1882774"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38310
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeta pgetrvavta etakklvaqg htvriqsgag vvasvtdaay qavgaeitdg
       61 ngafgadivl kvrapsdaea vlmkpgtvvi gmlnpfdaag lqrlataglt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarivil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvsydtdee keaaqgvggy akpmpqswld
      241 rqkvevakrv aaadivitta lipgrpapvl vteemvkamk pgsvivdlaa pqggncplte
      301 adrtvikhgv tlvgetnlpa lvaadassly arnvldflkl ivnkegalni dleddivaac
      361 lmskdgqvtr k
//
LOCUS       WP_093112171            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salinimicrobium catena].
ACCESSION   WP_093112171
VERSION     WP_093112171.1
KEYWORDS    RefSeq.
SOURCE      Salinimicrobium catena
  ORGANISM  Salinimicrobium catena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salinimicrobium.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Salinimicrobium catena"
                     /db_xref="taxon:390640"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115221
     Region          25..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrlhvilt ffmalvvqit faqdrtvtgt vtdgdgmplp gvnvlvkgtt sgtqtdfdgn
       61 ysvqasmgdi lvfsyvgfet kqevvededv idvtmvvdaa qleevvvtgv agatsrkkls
      121 vtvgkvdasd levipstsaa salqgkvagv nvtnfgqpgs gstiqlrgat nlfggqepli
      181 lvdgvqvegg indinsddia sfeivkgasa salygsragn gvivittkrg kynadgpvvt
      241 lrndlglsel ankidlnksh ayqladdweq yqgqytrfag vtyaddysgv grvgvsgari
      301 pveddvadnp ygvyydnqdl ffgtgvdntt yasvsnasef tnvffsadrt enegifaetg
      361 gykrygvrln gdfqindwlk lstnnnyirs nnetpggtld gvifdlalts pdvnlnapnp
      421 dgqpyyfipd pwaattinpl yglatnrela trnrflgsyn lnieftdwln ldteyavest
      481 hwvnddynpy tafqvggmlg genvgfsysk gdfskessyt lsqkgqatln yvdsfgdlnv
      541 agklsylmed ihyeyyyglg qdfiyqgvis ldnfdsaltr vssnstdera qnafailgld
      601 ykdryivdam yridgsslfg enhrwndyyr vsgayrisqd fnipgitefk ihaalgtagq
      661 rpgfswqydm inlttgslat nriksnpdlk pstttelefg anleflqrft fegvyakset
      721 edqfmlvdif apanegknrq wqnvgtvefn tlelsltsai idkqdlgwdf girysrtrne
      781 itnlnvdpit vgpggtntpg vifrvkegee fgamygnafv tsleqmenql pegtsindfv
      841 vnrdgvvvrr davgtsdeaa iirrdengdv wygkigsqna dfqmgftsnl rykgfnfyml
      901 wdwknggdiy nrqgqwltrd nrhammdqag vpaaeqktqs yyqslyavng dyeywvedgs
      961 yvklreaslf ytlgkdqlag vangffdslr lgvtgrnllt ftdysgwdpe vqrydantqn
     1021 yyavdygvyp vsrgynlsvq lkf
//
LOCUS       WP_093112573             975 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salinimicrobium catena].
ACCESSION   WP_093112573
VERSION     WP_093112573.1
KEYWORDS    RefSeq.
SOURCE      Salinimicrobium catena
  ORGANISM  Salinimicrobium catena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salinimicrobium.
REFERENCE   1  (residues 1 to 975)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 975)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 975)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Salinimicrobium catena"
                     /db_xref="taxon:390640"
     Protein         1..975
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108101
     Region          24..974
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtfikstwl llfmmplsff aqstlsgivt erdtgmpipg anvvikgttn gtttnfdgey
       61 tltgvdlddv ivysyvglet qevpftgqet invalapdaa ileevvligy gstrrqdatg
      121 sveqisseef nqgaivspeq liqgksagvr itsgngapgg gteirirggs slsannspli
      181 vvdgipldqr gvqgvrnqln ainpneiadf vvlkdasata iygsrasngv ilittkkgkk
      241 nadlkfeydl kvsvgevvet vdildadqfr nliettpgtd vgllgtantd wqdeiyqtae
      301 gaihnltvsq gldnfyyrvn fnhtsqkgvl ktdlyqrnal ntafnydlld ndlkltltak
      361 gsvdqndfad eaaigaavnf dptkpvyden snyggfyewt nnngvalqqa trnplalllq
      421 rdaegktkri itnfnidydi plidelrfnl nagvdyaenn gftfrpttsa tvlqnipaee
      481 vywginrnql ldfyfnykpy vesistaidl taghsfqefy mssqqrytde avegnwvlnp
      541 lsinrnales yfarasfdid dkylisgsyr mdgssrfsed nrwssfpavs vgwkinnedf
      601 lkdsgilsel klragygvtg nqeigpnygy lgvytpsqrg asyqfgetfy ptlrpeeydk
      661 elkweelqty nvgmdfgffn drftgsvday hrttenllae vpvpaganls drlvtnvget
      721 vskgievgln gkliqtdkin wnlnynitfq dleitklslg ddpnffipqg gisggvgnmi
      781 qiwktdidpt tffvyrqvyd qngepiegay vdvngdntit eidrqpykka spdffmgltn
      841 nftykdfdfs ftwrgsfggy mynnmqsatg frgagtvtpq pyysnfnanv letdfnesqf
      901 fsdyyiqsad fvkldnvsvg ylipgekldf rasftasnvl titdydgldp eiaggidnnf
      961 yprprtytlg lnltf
//
LOCUS       WP_093113478            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salinimicrobium catena].
ACCESSION   WP_093113478
VERSION     WP_093113478.1
KEYWORDS    RefSeq.
SOURCE      Salinimicrobium catena
  ORGANISM  Salinimicrobium catena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salinimicrobium.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Salinimicrobium catena"
                     /db_xref="taxon:390640"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118580
     Region          26..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkakfsgilt lllalvvqit faqeqrtisg tvtddsgmpl pgvnvlvqgt trgvqtdfdg
       61 nysiqasage vlvfsflgmq treytvanvd tidvvlepdt aqleevvvta lgisrekrsi
      121 gyatqevage evstvktdnv innlsgkvsg vqikannnfg gsanflirgv ssltgnnqpl
      181 fvidgipisn ainntdaqrg gstgydygna asdinpedva sinvlkgaaa saiygsrgan
      241 gvviittksg qrgvakvtvs sgvtvgeidr stfleyqdgy gagygpyyga pnfdgyferf
      301 dvngdgtidd vvptyddasy gapldgrmvy qwdafvpdha nylqatpylp gettpadffe
      361 tsyqfnnsva vsggsekmty rlgytnfdqt gmlpnsnlnk nsfnlngdiq vtdnlkagas
      421 anfivqrtkg rnstgysdnl msqfrqwwqv nvdmdsqrei feqtgqnvsw nheggmggsy
      481 lqphywdnpy wtryknfqtd rrnrfygnlf atytvtdwld vtakgavdty kelreerrai
      541 gsvgapfgvl rdtessgydr kdvdfteyny dlmanidkdf gedvslagva ginlrretys
      601 yyhqstaggl iapgifalsn svntnpkpve vlqekevvgy ygqaslgyqn tayldgtyry
      661 dvssalppde ngygyfavss slifsnlfds nwfsfgklra gyaevgndlp annvydtyni
      721 lnnfgssalf sfpgtkqnqd lvpertkeie vgletrmwnn rvgldltwyk kntenqlmpv
      781 slstatgfsr rwvnagelqn kgvearlhlv pvtnddftwt vdfnwsknen lvvdlygdqe
      841 nlvlasyqgg vslnatvgqp yntlrgtgye ylngqrvvns sgyykavsdq vigdanpdwn
      901 ggisnklayk nlalsflidv qqggdvfsld lhygqgtglp dytgglnelg npvrdpvseg
      961 ggilnegvte dgqpnttrar adfyggayyw gnssrnpnqi nvydasyvkl relaltykmp
     1021 vkqwfgdmit agnvsligrn lwiidknvpf adpesglgag naqgylsgsy ptlktiglnv
     1081 qfef
//
LOCUS       WP_093116533             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Salinihabitans flavidus].
ACCESSION   WP_093116533
VERSION     WP_093116533.1
KEYWORDS    RefSeq.
SOURCE      Salinihabitans flavidus
  ORGANISM  Salinihabitans flavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salinihabitans.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Salinihabitans flavidus"
                     /db_xref="taxon:569882"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55816
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevl ngenrvamtp esaqqlqklg ydcaietgag lqagftdaay ekagveiikt
       61 aaqlwkaadi iakvriptet elkrltkskt lisffnpggn eeglelarsk gatviamemv
      121 prisraqkmd alssmaniag yravieagnn fdrfftgqit aagkvppakv lvvgagvagl
      181 aaigtatslg avtyafdvrp evaeqvesmg aefvyldfeg elddgsasgg yakpsspefr
      241 eaqlakfrel apemdivitt alipnreape lwtedmvksm krgsvivdla aekggncklt
      301 vadervvtdn gvtiigytdf psrmasqast lyatnirhmm tdltpekdgk pvhnmeddvi
      361 rgatvthkge itypppppkv qaiaaqpkke aakeltpeek kaqelgafra qtksqvtmlv
      421 vggavmlllg qvapasfmqh fivfvlacfv gfqviwgvsh slhtplmavt naisgiivlg
      481 ailqigsgnw ivvvlaavsv listinivgg flvtrrmlam fqks
//
LOCUS       WP_093117228             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thermoleophilum album].
ACCESSION   WP_093117228
VERSION     WP_093117228.1
KEYWORDS    RefSeq.
SOURCE      Thermoleophilum album
  ORGANISM  Thermoleophilum album
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia;
            Thermoleophilales; Thermoleophilaceae; Thermoleophilum.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Thermoleophilum album"
                     /db_xref="taxon:29539"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39360
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvsvpreta agerrvalvp dvvarltkgg levvvepgag aaahhsddey reagakveeg
       61 aglagdlvak vqppsidevs klregavlvg flqpftspdl vralaqrrvt alameaipri
      121 traqtmdals sqatvagyqa aliaarelpr ffpmlttaag tirpakvlvl gagvaglqai
      181 atarrlgaiv fgydvraavr eqieslgarf leidlgieda eaqggyarpl teeeearqrq
      241 lladaiagvd cvistaavpg rraplliied avermpagsv ivdlaaetgg nceltkaget
      301 veahgvkvig pvnlpasmpd hasqlyarnl qalielited gqlaldfdde ivagccithd
      361 gevvnervrq aigapas
//
LOCUS       WP_093127371             380 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Variovorax].
ACCESSION   WP_093127371
VERSION     WP_093127371.1
KEYWORDS    RefSeq.
SOURCE      unclassified Variovorax
  ORGANISM  unclassified Variovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="unclassified Variovorax"
                     /db_xref="taxon:663243"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38619
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etvkklvasg havrvasgag vaasvtdaay qaagaditdq
       61 agafsadmvl kvrtptdaes gllkpgavvi gmlnpfdaag lqrlaaagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadryqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmpaswla
      241 rqqvevakrv aladvvista lipgraaptl itedmvksmk pgsvivdiaa gkgadanggl
      301 tggncpisea dktvvkhgvt ivgetnlaal vaadasalya rnvldflkli vtkegalnid
      361 leddivaacr vtqggqvtkk
//
LOCUS       WP_093139333            1093 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacter
            litoralis].
ACCESSION   WP_093139333
VERSION     WP_093139333.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacter litoralis
  ORGANISM  Ulvibacter litoralis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacter.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Ulvibacter litoralis"
                     /db_xref="taxon:227084"
     Protein         1..1093
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117685
     Region          25..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfsgtlt llivlvvqit faqektitgt vsdnsglplp gvnivikgts ngtqsdfdgn
       61 yalkasvgqn lvftyvgfkt qertvtanss sisiameeda avleevvita iglekkkedd
      121 lssattiqae titksgeagv atalagktsg vniiksggdp gagvfiqirg antiqgddep
      181 lyvidgvlin nfnfgagvag vseqsrlndi ssediesvtv lkgasavaiy gtgaangviv
      241 vktksgkgkp gewsldyksg vyidkvnetw dlqdkygqgl ngvfndgggt stswgdlisa
      301 raggpdevnv gnqrfeaqdg tvyypiitkn sresflesnf davigqgitf ehdislkysg
      361 qsgstyisan nwdqkgivrn gsnyvrktlr fnnttnfsdk lsakiganyi ktdadaiqtg
      421 snlngfylgl lrtspdfdnr dykgtsfnaa gapsinamra yrgplgptsa ynnplwtmne
      481 qsntievdrf liapelsysf sdnvtvttry skdtyrdkrq vffpynsstd ignglgyfei
      541 derfvssqyl tafinsnhti sekfnlswil gasyennefe qlatsatnfs npyitlddli
      601 sienaaaani daidsydlek qvgayllvng eifnqvlfel tgrvdrsstl pdqtffypav
      661 slgwkfselv kgseflsfgk irgtygevav apqtysltng fgiggvnssw gdtlaggqyg
      721 staslddvqg nanlvvervk eyelgtdlkf fnnrlsmsft yydrktedvl leqavspssg
      781 fsnlnnnaat itnkgiefdl saaiiktedf kwsidlnysq ndnlvtspdg ngevlsflng
      841 fvgtssnvvd gqpfaallgn plardedgnl alndfgfpvv sedgeevigd pnpdwrggig
      901 tkinykgvel salfdfvqgm dvwngtkgvl nhfgvsevta nqvtvsaeea atilnfngva
      961 iadlpysqln edgsytvrgn lddfgagtvl ldqawylgta sgfngspeln iedasyvklr
     1021 evslgytfps kfiegigldn lsfsvsgrnl vtwtniegfd pdnnltgask grgleyftnp
     1081 stasyfftlr vgl
//
LOCUS       WP_093141488             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacter
            litoralis].
ACCESSION   WP_093141488
VERSION     WP_093141488.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacter litoralis
  ORGANISM  Ulvibacter litoralis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacter.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Ulvibacter litoralis"
                     /db_xref="taxon:227084"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107119
     Region          28..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqknstrrt flfllflfpc lvfaqtslkg kildkngdtv pfanviekgt tngtttdidg
       61 kftidvpnlp atlvfsslgy etveqvvnta apmtinfves aqaldevvvt glatsvkrsn
      121 sanavasisa edisgrtppq tldgalagkf agalvtkssg apgggisvkl rgvtsingns
      181 qplyivdgvy vnnssvsaag lnavsgaasg gnpssqdnps nriadinpdd iesievlkga
      241 saaaiygsra aagvilittk kgkrgetkvs lsqevgfntm lnplgqrtyt rdiaeaafgp
      301 gngalfaeaq angtltnfek eiygeegfin ntsvnvsggs entsfyagfs nseedgivkn
      361 tgynrksvrl nvehkfldkr akisvssnyi nsnadrgffn ndntgttigv sltstppwaq
      421 lfpdengnyp dnpyggsnpl qtrdlitnre tvnrfitgat ldfniydaen sslklqlrag
      481 vdyyqlvtka ifpkelqfqk isngglngls algsaenkda nysaflvhdf ntdndlaftt
      541 qvgitkqtfs vnivrniatn ligtetnldq sgnvsvsqnr leqedagffa qeeinyqnkf
      601 iatlgvrgdk ssnngdankl fyypkaslav nfhefdfwnn fetmnqfkir gaygeagnfa
      661 pngalftayg sslidglpgi vvpvtlgdpt ivperqkele fgvdagffnn rlnleatyyn
      721 knvddlvlla nnepssgfgs rwansgnlen rgielslnad vvrsdnfnws ttilyfknes
      781 eitrldvepf nlggfgqglg tfrieegesa tqivgnnadg dlvvlgnaep dfqmtftnnf
      841 nyknfdlsfl whwkkggdni nlsslltdfg qtsfdydgtn ldpsgamsng dyrvnaflsg
      901 natpfvedas ylrlreiglf ytvpskliks afkdyvsnfk igfsgnnlin ifdynsydpe
      961 vsnfgsngls sgvevtpfps skrylfhlav df
//
LOCUS       WP_093144113            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacter
            litoralis].
ACCESSION   WP_093144113
VERSION     WP_093144113.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacter litoralis
  ORGANISM  Ulvibacter litoralis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacter.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Ulvibacter litoralis"
                     /db_xref="taxon:227084"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115741
     Region          25..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqkfklmlv lfsvflaqas faqekqitgt vtdgsgvpll gvniiikgts qgtqtdfdgn
       61 yalqasegqt lvfsyvgyte netivgtnsn invtlqeges lnevvvtalg isrekqslgy
      121 stqelkseei ttnksgnvtn alsgkvaglq irrnnnfggs tnavirgnts ltgsnqalfv
      181 idgvpinntn tnsagqsqas ggyydygnaa sdinpddies invlkgaaas alygsraang
      241 vimittkkgk rssgmgitls tgvnvgfvdk stfadyqsdy gggygnywte edingdgiid
      301 qvanygddas ygpafdpslm vyqwdsfdpd lanyrtrtpy vaaengplsf fetpvtitns
      361 isfdkgfeeg sfrlsytkld qsglmpnsei nkhnfslsgv invtdkltat glanyiktdg
      421 lgrnstgygd nvisnfkqww nvatdiedqk sayfntrrnv twnpatsaag sapiywdnpy
      481 wtryenyqnd srnrfighfs lnyefadwvn atarvatdty selqeerrav gsvatpfgvt
      541 rgnvgsgylr rnitntetny dfmlnfnkdl sdkinlsgil gtnirrqeyq siavstaggl
      601 vvpglysiqn sagpvpnpte raekigvdgi yasasfgyas tlfvdvtarq dqsstlpadd
      661 ndyfypsvss sfvfskllnv daisfgklra nyaevgndap fdylydtyvi nadqgtsvan
      721 saknpnlrse rtksfelgle mkfansragf daayyktnsi dqivrvpvtt atgssskiln
      781 ageientgie lsafvipvkn dnftwrlnan wtqnknevls leegietlql gsfqggvtin
      841 aqvgqpygvi ygtdytylng qkvvdpdsgk yiatgtsnni igdtnpdwlm gisnnftykn
      901 lslgflidiq qggsifsldq yygqatgvya etsfindlgn pvrntladgg gfinegvnpd
      961 gstnttrlsa sgfspfgyas npnaafvyda syvklrevsl qynlpskfls ntfmtgltft
     1021 vtgnnlwiis kelphadpes glssgnlqgy stgslpttqd ygfnikaqf
//
LOCUS       WP_093144425            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacter
            litoralis].
ACCESSION   WP_093144425
VERSION     WP_093144425.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacter litoralis
  ORGANISM  Ulvibacter litoralis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacter.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Ulvibacter litoralis"
                     /db_xref="taxon:227084"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111708
     Region          37..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksyylwlv liffnmtavl aqektvtgtv tddtglplpg aniiikqtnt gtqsdfdgny
       61 tisvavgqtl sfsyvgfqnq evkvgaadki dislkpgall eevvvtgyst rnktvqssav
      121 vsisaseise lapttsvdnl lqgkaagvqv taangkpgqg afvrirgtgs ltaggasply
      181 ivdgapiree elgniatsdi etidilkdas mtarygsrga ngvvvittkr gkrnndakvs
      241 fssrygvtsr vdlnytmmda qqklqyetem yalgvggaaa lpgvttlpgs perqrlldns
      301 ldweelvlkd gyvqnnsvsi sggaekmdyf fsvghdkntg iidkidgfer lnarlnlnfd
      361 akdwltvgvn vgfarstsde prdrnnsqnp frhmldvnpy eteyildedn nvvldangsp
      421 vynttttgyp vrraletepa fdvenitlan veaiiklskn fsytfgmavn hlnrhtesys
      481 kpggvlddli gnadfpgrkt dsntqrldmt asnrltynls tdshnlnvlg lfeynfnein
      541 flyavsrgfs tpllttqsna gfvdpatttt rsrltlvsyg afadydfker ylasasirrd
      601 gsstfgddvk ygtfysgsig wnvakenffn vdsiddlklr asygtvgnrs gigryesqgl
      661 vefnpypggl gtvpsnfenp elqwettkts nfgvelsmfn rrlsfvadyf vrnttdllfa
      721 ipkadesgvd svtgndseik nagleialqa divrndnlkw tvggnilflt eseivtlpdg
      781 lpvdapntfn irweegakin ehylipyagv dpntgrplfy gadggvytad qmpegenrql
      841 qgkstiadke ggffnnivyk gfglrtdfvf kygnwinnyv ksnlvsdgla vdanqaveaf
      901 nywkepgdtd vqpspiyrnd agelasesdr flergdyirm rnatlsysfq kktlekspfs
      961 nlrvyiqgqn lltftkffgd pevglssget isfadsvapg eatlysypnt ksiqvgvdvs
     1021 f
//
LOCUS       WP_093144687             969 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacter
            litoralis].
ACCESSION   WP_093144687
VERSION     WP_093144687.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacter litoralis
  ORGANISM  Ulvibacter litoralis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacter.
REFERENCE   1  (residues 1 to 969)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 969)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 969)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..969
                     /organism="Ulvibacter litoralis"
                     /db_xref="taxon:227084"
     Protein         1..969
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107318
     Region          25..968
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqlfkkilf vvafiplalf sqnevqgtit ddstgmaipg vnvvikgttn gttsdfdgky
       61 tinnvktddl ivytyvgfaa qevkysgqtl iniqlvedas qleevlligy gstnkqdatg
      121 avqkvssevf nqgaivspdq llsgksagvr itssgggpge gseirirggs slagnnspli
      181 ildgipldqr slqgvrnpln ainpneieef vvlkdasata iygsrasngv ilittksgkk
      241 ntplvldygf qfsadqitdk vdvfdasefr qlvtdrggdl srlgrsntdw qdyiyrtang
      301 aihnltatqg fknftyriny nntnkegvll kdlyrrnaln lnltadlldn hlklvatakg
      361 sfednyyank gaignavnfd ptqpvygagn fegfyeytde tggplnlapk npfaqlqqdd
      421 nksrtkrtis nlnidykfhf lpelrfiana gidyseldgk qfisansatq qngqfknfys
      481 glnrntnldl vlnyknsies intkydilgg heyqefyiqs ylfnsqgsdv tlekndinrn
      541 slesyfgrvs fdisdkylis asyrrdgssr fspdarwgnf paasvgwkis nedflknskt
      601 istlklrggy gitgnqeint nygylgvytp gqpsasvefg gifvntlrpe efdenlkwee
      661 ttqynagldf gffedrlais vdgyyretkd llaripvaag snlsdilttn igesrsrgie
      721 vgidvdlars enfnwsinln gtlqdfeitk ldlsgsedff ipqgdisggv gnkiqlyrpg
      781 ydpstffvfr qvyddagnpi egayvdingd nqiteedkqa ykkatpdayy gfssnlsykn
      841 fdfaftlrgs lgnyvynnas agtgyyasmf dtlgdfyqng stdvvntnfe eaqyfsdyyi
      901 rradflkldn msigytiple kvtvrttltg tnlftlteye gldpeisngi dnnfyprprg
      961 fvlglnfty
//
LOCUS       WP_093145438             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacter
            litoralis].
ACCESSION   WP_093145438
VERSION     WP_093145438.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacter litoralis
  ORGANISM  Ulvibacter litoralis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacter.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Ulvibacter litoralis"
                     /db_xref="taxon:227084"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109162
     Region          33..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknyyrqslt lsvflillnt inspifsqns psktitgiit esdspldgvn ilvkntlrgs
       61 itdldgnysi taaatdtlvy tfvgfktqei avgnnasinv tmqpdattld qiiinagyyn
      121 vtdkektgsi sqlnakeiet qpvsnplstm qgrmagvnii qttgvpgggf svrirgrnsi
      181 ridgseplyv vdgvpyasqs lgssmvstvl ggtqsplngi spndiesiev lkdadatsiy
      241 gsrgangvvl ittkkgkpgk tsfqintgtg vgtitrkmel lnteqylamr reaftndgit
      301 nypfnaydln gtwsqnretd wqeeliggta yntnasasvq ggndntsfll rggyeeqttv
      361 fpgdykykkg stlvnlshkt pdnsfriqfn gnyvadnnnq pttnltream tlvpnapaly
      421 dsegnlnwen gtfnnplaal egeyisntnt ilansivsyt pykglevkan lgytkfqlee
      481 trtaphtiyn pafgldssys sstfnngern swlvepqisy tyalgkgkie alvggtiqke
      541 kttsllqvas nfptnsliyn paaaanlfis nnsdevynyr alfgrlnfnw ehkyivnata
      601 rrdgssrfgp gnqyanfgal gvawvfseet fvtkalpfls fgklrasygt tgndqignyg
      661 ylntyttegl syqgiqtlsp iqlfnpdygw etnkkletai evgfmedkit lsaswyrnrs
      721 snqlvgvplp gttgfsslqa nldatvenrg weveietvni qskklqwrtf lnltipknel
      781 isfpglsast yanqyvvgep lnivllynat gvnpqtgtyt fedidgdgii skpndlkssa
      841 nldpkyyggf rnalsygnfn ldflfqfvkq qgrnyhttia lpgtmgnqpv qvlehwqqpg
      901 dtasqqlfst gsnndayagy lnnydstssi sdasfirlkn iaasytipsl lsspfgcqis
      961 veaqnlltit kyegpdpetq iygnlpplkq inlgvqltf
//
LOCUS       WP_093147862             395 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Saccharopolyspora antimicrobica].
ACCESSION   WP_093147862
VERSION     WP_093147862.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora antimicrobica
  ORGANISM  Saccharopolyspora antimicrobica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Saccharopolyspora antimicrobica"
                     /db_xref="taxon:455193"
     Protein         1..395
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40787
     Region          35..386
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(47,102,121,314,340,342)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(76,154..155,164..165,168..169,172..173,175..176,
                     178..183,185,187..189,192,215..216,304..305,347..348,352,
                     355..356)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(149..150,154,157,160,201..204,224..226,254,265,
                     282..284,291,293)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(151..152,154,164,207..208,215,231..232,234..237)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(184..188,191,194,217,219)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqpshekppn arttpnattt enpgeaggag qrtsvgvpre svpgerrval vpgvverlca
       61 qglevrvepg agqaalipdd aftkagahlg dpwsadvvvk vnppspeeig kltrgstlig
      121 flapltdpdl aprlraagvt gfalesvpri sraqsmdals sqanvagyra vllaasectr
      181 ffpmlttaag tvkpasvlvl gvgvaglqal atakrlgart tgydvrpeva dqvrsvgakw
      241 ldlgisavge ggyareltee eraeqaqrls aaisgfdvvi ttalvpgrpa prlvpaeavr
      301 rmrpgsvivd lagaaggnce lsepgrtvvd heitiaapld lpasmpehas elyarnvral
      361 lelmlvdgrl apdftdevla aacitrsepg dghsg
//
LOCUS       WP_093161230             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aliiruegeria lutimaris].
ACCESSION   WP_093161230
VERSION     WP_093161230.1
KEYWORDS    RefSeq.
SOURCE      Aliiruegeria lutimaris
  ORGANISM  Aliiruegeria lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Aliiruegeria.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Aliiruegeria lutimaris"
                     /db_xref="taxon:571298"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55889
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigsprevf pgesrvamtp dsakqlqklg ydcviesgag iaagfsdaly aeagvevvns
       61 aeelfassdi iakvrppees eigllsadkt lisffypasn eplmeaakqk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvylefde eqtdgaatgg yaapsspefr
      241 eaqlakfrel apevdivitt alipnrdapv lwtkdmvemm kpgsvivdla aerggncelt
      301 vkdekivten gvtivgytdf psrmaaqsst lyatnirhmm tdltpekdgk vnhnmeddvi
      361 rgatithega itfpppppki qaiaaakpke pvkeltreek laiereefrk qtrsqailig
      421 vsaallllvg ayapasfmqh fivfvlavfv gfqviwnvah slhtplmavt naissiiivg
      481 almqigsgsf lvillaslsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_093166483             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. YR216].
ACCESSION   WP_093166483
VERSION     WP_093166483.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. YR216
  ORGANISM  Variovorax sp. YR216
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax sp. YR216"
                     /db_xref="taxon:1882828"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38921
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeta pgetrvavta etakklvaqg htvrvqsgag tiasvtdeay qaagaeitda
       61 agafgceivl kvrspderei slmkpatalv gmlnpfdaag lqrlasaglt sfaleaaprt
      121 traqsmdvls sqaniagyka vmmaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvggy arpmpqswld
      241 rqkvevakrv aladvvista lipgraaptl itedmvkamk pgsvivdiaa gkgpdgiggn
      301 cplseadktv ikhgvtlige tnlpalvaad asslyarnvl dflklvlpke ggikidledd
      361 ivaacrmtqd gqvtkk
//
LOCUS       WP_093183659             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sanguibacter gelidistatuariae].
ACCESSION   WP_093183659
VERSION     WP_093183659.1
KEYWORDS    RefSeq.
SOURCE      Sanguibacter gelidistatuariae
  ORGANISM  Sanguibacter gelidistatuariae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Sanguibacteraceae; Sanguibacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Sanguibacter gelidistatuariae"
                     /db_xref="taxon:1814289"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53294
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipretr agerlvaatp ttvaqlvklg ydvvieagag aqasfpdaay reagasvgda
       61 aeawssdvvt cvnapepdai aqlqpgativ smmapaahpe lvdafaergv salaldavpr
      121 israqaldvl stmsnvagyr avveaaesyg gmftgqvtaa gktapakvfv igggvaglaa
      181 igtagslgaq vrafdvrpea geqiesmgaq fvqaqaaqqe vsadgyaqem taeqerltsr
      241 tyaeesakad iiittalvrg saprtitaam vaamrpgsvi vdlaasgggn celtvpgski
      301 vtdngvtiig ytdltsrlpk htsqlfgtni vnlmklltpn adgqvvldme dvvqrgmtvt
      361 lageilwppp pvqvsaapaa atvavpvvdp avqaqqdkea ahrkgqrqlv gyglgavllg
      421 laitfspaaf agnftvfvla vfvgyyvisk vshslhtplm aqtnaisgii lvgallqigs
      481 dnwwvtalaf iaatvasini fggflvayrm ismfrkda
//
LOCUS       WP_093190531             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudovibrio sp. Tun.PSC04-5.I4].
ACCESSION   WP_093190531
VERSION     WP_093190531.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio sp. Tun.PSC04-5.I4
  ORGANISM  Pseudovibrio sp. Tun.PSC04-5.I4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Pseudovibrio sp. Tun.PSC04-5.I4"
                     /db_xref="taxon:1798213"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55148
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigaakevl ggerrvaltp asalqlqklg yecaietgag aaanfsdady teagvkvvtd
       61 aktlwetsdi iikvrppevs eldlthagqt visffwpaqn gellqkfadk kvnviamdmv
      121 prisraqkmd alssmaniag yravmeagnn fgrfftgqit aagkvppakv lvigggvagl
      181 aaigastslg aitlafdvrp evaeqvesmg aefvyldfke eqqdgaatgg yasvsspefr
      241 eaqlakfrel apdidilitt alipgrdape lwtedmvasm kpgsvivdla aekggncklt
      301 kmdekivtdn gvivigytdf psrmatqsst lystnirhmm tdltpekdgq aninmeddvi
      361 rgatatkdge itfpppkpki aaiaaqkpka pektaeekav daaaaakaag rkqigmlilg
      421 gavmaligay apvnfmqhfi vfvlavfigf qviwgvahsl htplmaitna isgiiilgal
      481 lqvgssswiv iilagisvli asinivggfm vtrrmlqmfn ks
//
LOCUS       WP_093196310            1159 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093196310
VERSION     WP_093196310.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1159)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1159)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1159)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1159
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1159
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127291
     Region          51..115
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          140..1158
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnsllclfs lllrtsltpl avgvvfqgvt hagpvgaqdi lnqsvnirva nqplrqvlse
       61 ieratnvrfs yrpkavqadq risltsqner ladvldrlft pikiryevag rqiiltpqav
      121 ntpgplssks ygetsqaeer pvsgkvtaen gealagvsvv lkgsirgvtt nasgefriai
      181 pdengtlvfs fvgyetqeit vgnrttltvs mkpglkalse vvvvgygtqt kanltgavas
      241 vggevlesrp lvnlaqglqg lvpnlninvn sgapgrgatf nvrgtgsing sdplvlvdgv
      301 qmdpnlinpq dvasvtvlkd aasaaiygvr gaygvilitt kmpkknaplr vsysgsvtmq
      361 tptrlpkyvn svdyirmhre adatgaktng aqatekftdl dvenaqkyfn dpahnlpvyi
      421 dpanpskyry vgntdwikeq yngwepmtdh tlslsggegk tsfsaslgyl nqkglievnk
      481 evykrynagl kinsdvnswl tlnfrlnlnr tdnnrptpan tggtaeswls ndlrpimpvy
      541 hpdgnfagqg sftnpialak lngryvttan dlwltggvtl rplpglqivs tytwngynan
      601 sirhwkeyne ygangvllgt fpwsrpsrvt eennndyyta vnayaeytkt ladkhnfkgm
      661 vgfnqelkqt ryysasaknl idqtmpainl nndpnptvgg srgewavsgt ffrlnydyag
      721 kylveingry dgtsrfprdn ryvflpsasv gwrvsdeaff aplrnaisdf klrasygklg
      781 nqatgslgny pylptmsagq vnyvmgsqlg igvgtpglvs snftwekvst ldfgvdfgff
      841 rnrltgsfdw ytretrdmiv gafplpgilg tsppsrnagn litkgwelsa nwrdrinsdw
      901 sydvtlslsd nktkitkydl nstktfggsn yyegqnlnei wgyetvgffq tddaaakadq
      961 kqlfsgtwla gdiqykdlng dgkitrgdnt vgnpgdqrii gnstpryvfg vnanlryknf
     1021 dfsfliqgvg krdmavggre fwgftsewnv pllhhlnywt pdninayypr qrfggggnfa
     1081 tqtkylqnaa yarlknislg yslpkavtdr lklqnvrvyv tgqnlfeits fykaldpetv
     1141 nqavyplnra vsagiqfgl
//
LOCUS       WP_093197121            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093197121
VERSION     WP_093197121.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113269
     Region          24..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktlhtyli lllfgsaava qrvqvsgtvt seadaspvpg vnvyvkgtsq gtvtdgkgqy
       61 sfaltssgnp vlvfssvgft tqevpvsgrt vidvrlkpyn talnevvvta lgisrekkal
      121 gyaaqsvssd elmqnrqtnm vnalqgkvag vtisgtggap gqgarilirg insidvgrdn
      181 qplfvvdgvl ldnststqgg detasrgmtn raadinpddi etinilkgga atalyglrga
      241 ngvvvittks gkagamrvny tgsygfdspn klpevqdkyt igwmgvydpk sfwpsfgptv
      301 eeavkidpth pkklynqfkd ayqtgsqfqn nisfsggsdr itylssvshl sqegiipftn
      361 ykkltlrlnt qakisdqfst svnlsfvnsg gdrynanrys ellsywspry dvrdyqkadg
      421 smnaysvdng npiyaamtnr fkdnvnrfig gagftytpls wltfnyragl dtysedrlft
      481 apgpmgiane ipfednglgf vkqhhanfra itstfsaaat hkfgqslntt lrlghdlydr
      541 kvrsfgidgt eltvynyfdl rnaktivasq ggedyrlmgl fgeltldykd ylfltltgrn
      601 ditsslqspn nsffypsasl gylfsqhlnl pqfitmgklr asyakigkda apystangya
      661 ayqslpsgmt gftrgsllgn pdlrpeftdt weagvelsfl kkrlgldftf ynsvskdqii
      721 qvnvssttgy vqaainsgqm rnrgvelvlr gtpiqsrdfs wdvslnfsan rnkvlsireg
      781 lteinyasey gyanstvtmk lvpgmaygnl ygrayqryyp taseeipgvl dknravviga
      841 ngfpvissaq kllgntqpkw laglnntlry knfsltalfd arvgqkrynq mgnffsafgi
      901 akytedrndv kvfdgvladg srntkavwlg qgvgpdgvny gngfyrnvhr gasenfieda
      961 swvrlrsvgl ayslpaallk gsfvknarls vtgnnlvlwt gysgydpeas tmssgsnvdg
     1021 fsgftypalr svlftvnvgf
//
LOCUS       WP_093197195            1177 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093197195
VERSION     WP_093197195.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1177)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1177)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1177)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1177
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1177
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129697
     Region          <73..108
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          145..1171
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmrrlppvra lslcvlvgit plmthaqlya lsaqkarvfa hevplrdvll qlkeryqvdi
       61 lfeenqqllv rgallrdatl eqnldhllas tglryrkvkk dtyilkqaap evsflaqrsn
      121 alppeatpir lsparteliv aippvkgkvt dratgqplvg vsvllkgtgq gtstnaagef
      181 tlslaesqgi llvssigyqt eeiplggrts laislaadtk algevvvtal gikreqkalg
      241 ysvaqidgae lsnvkspnml nalagkvagv nivststdag stalitirgq ssiskdnqpl
      301 fvvdgipvap slrtpnmaig rsvtdygspi gdinpddies vtilkgasaa alygsragsg
      361 vvlittktgs karkglgvtv nsttmfdkiw qypefqnqfg tgdfpgtant vqgsawgprl
      421 dvgmkkaqwn spldasgnri ptdwvsypnr isdffrvgtt ftnnlavtsn gekgsfrlsy
      481 tnlsnngvvp ntglkrnsld laanyklhdr vristnvgyt nnssanraaa yresvteily
      541 kmpanvdlrp lrnywkpgre gfeqftydpg nldnpylvay eetngyrrnr iignvqafvd
      601 itkdlslmvr tgmdfyaeeq dlkrpfsgkr tplggyylnn lfftehnsdf llsykktltp
      661 dwqfsasvga nrmdqqsrst attagslvlp giynfsnaaa gtvttlqnnt rkrinsiygt
      721 aevsyknmlf lnvtgrndws stlpsqnnsf fypsfslssv vtdmlkmqsn vltfakvran
      781 wsqvgsdtdp yqlyntllfd tdwgtvkrpn ldfalknsll kpeiatsyel gtdlrffrgg
      841 rigleftwyk tnnrnqiiki pttiaagsst rlvnagniqn egieigvrav pidavlrwei
      901 sanytrnink viklidglte ysmgsadgdn iryllkegtk igdmytpswi kvpdgpykgq
      961 plltsagllq rqttydylgn ynpdfsvgfn ntftyknltl nflidwrqgg kfysypmktm
     1021 ilqgtsaltl rgrdaetggl awtdgerrqr ndgmivqgyi angdgtyren tnilsasayy
     1081 dnlynkyyer ttydasfvkl reasltyqfg kkvlsrlpvy nlsvsligrn lfnwtacdng
     1141 fdpetsmsva edgfrrgvgh wtlpgvrsyg fklgfqf
//
LOCUS       WP_093197247            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093197247
VERSION     WP_093197247.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111522
     Region          31..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkyfmlrls avwliagflf vawpasaqsd irgrvtdaan qsslagvnir vkgtvrgtst
       61 daegrfqlsa assetlvfsi igyetkevtv gnqtdwsial qpaarslnev vvtalgierq
      121 trslgyatqq isgasltavk dpganlmnsl sgkvagavit ptatgpggav rvvlrgnrsi
      181 sgnnnalivv dgvpidntms teqggggsan tiatqpkgis sgysgsdgaa sinpqdvesv
      241 tvlkgpaaaa lygsraanga liittksgks galsvnyngs vaidepfllq kfqntygrgn
      301 ggkagaeaag swgaaaqtys nnvrdfyrtg ssltnsvdls ggnekirgyv sythnrnegi
      361 vprnglerst vnlrlnarpv erlttdvkit ymdqrirnkp rlgdtgipne animprdlsp
      421 aelakyetid atgkpvpvyw tnssiyrnpn wdvyrtslne drsrimmlgt akyqltdwls
      481 lqgrysldry ddnitasyyd gtvalpvqpg grylegfirr sernmdills gnnkitngln
      541 vsynvgastl hikgnntqal anglsipnqf nlnfattpaf snlpfekkmq svygnvqfdf
      601 rqllyldvsa rndwsstlpa phsyfypsvg lstvvsewlh mpswvsfgkv rasytqvgnd
      661 adpyllmqty sfsqgagngf vsrdnvkyis nlkpektrsy elgmewkfld grfgldatvy
      721 ksntinqlif iglpqatgys qqyinagniq nkgleisltg dlisrkdfrw tsalnfarni
      781 nkvlslspgi aqanlsssta lgsllvkpgq sygdiydyaw tkdangryvv nasglptvta
      841 lqklgnfnpd ftlgwnntln ykrfnlsfli dgrvggilvs gtdatlayfg vgdyttryre
      901 gglvlngvka dgsanttain aeqfwtsvsq ggrtgygqff afsttnfrlr elslgynlsl
      961 ktkairnarv sltarnllfl yrgksildip gigkrtipvd pesaigtsny qgiesgmlpl
     1021 trsiglnlsl sf
//
LOCUS       WP_093197491            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093197491
VERSION     WP_093197491.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117450
     Region          24..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnillaafa llsvlcipvs aqnrvvsgrv tsaddgapip gvnvtvkgtt rgistnsnge
       61 yqlsvadgat lafsaigfvr qevvvgnqak idvvlavsgs eltevvital nisrdkkain
      121 saiqtvssek lqiarnnnva dalagkvagv qvfsqsgakf gtpnirirgv nsltggdply
      181 vvdgtitdin yvnmddvesl nvlkgpaasa lygnrasagv vvittkkgkr qeglgidvnh
      241 sttfdrvsll ptyqneyggg ytqafdqfhy npavhpeswk afegqniidy sadeswgpkm
      301 dgtpyrpwys wipsdpefgk tvpfsphpna irdffntgtt vntnvafskg gdnynarvsy
      361 tnynvkgvip nttqkrdyls aklglnltpk ltvttninys tenttnrpad gyggqnqtig
      421 sfnqwwqrqn dmdhlrvykn pdgsyrswni tgpenttply wdnpytqvye ntnkekndrl
      481 fgdfgvnykf tdylsasvta rrdmytsqye rrvasftkgt pyfgartdvr rednyegllt
      541 ffkkfnkitv sanaggnirk nyrtylneet sgglaipnfy nisnsvnamt vsnlksqrev
      601 rsvygyvsld ygdflfleat arndwsstlp kgnnsyfyps vtggfifsef ihekrilsfg
      661 kirasyaevg sdidpyqilt tynvgskygs nttetlptql pnaalkpgls kgkeigvdlk
      721 flnnrlslef tayrqdntnq ilplavpgss gyssalinag nirsegielh igatpiktad
      781 ftwdldlnvd rsrskviqla aglktydllq sylgstsifs gvprfggttl gfiaregsdw
      841 gtivgkafqr fqavdgngkp vanpangkil vdadghpltk pnqdlatvlp kakggflssf
      901 tykgvtlrfn idwliggkfy sttrmfnags glsaetagln dkgkpkrdsp dngggvmikd
      961 avfadgtpnt kyvdtqtlye sdffdlnerw ifdktyvklr evnlgytlpk tflkrtpfrn
     1021 ayvalmvrnp fliyskvggg vdpsetqtyw geggqqipvr qmgfnvkfsl
//
LOCUS       WP_093200158            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093200158
VERSION     WP_093200158.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119398
     Region          23..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkflffcfl lvlscwtaqa qdrvitgkvt ssddgspipg vsiavkgttt gtntatdgtf
       61 rlrisndavl vftsigfdpq tievgntqtt levhlkpsvs alsevvvtal gvsrekkslg
      121 yasqeikgel vntakegnfi nslsgkvsgv eikrnnnlga ssnivvrgfk sltgnnqalf
      181 vvdgvpidns nsstndaatg rggydygnva sdinpddies invlkgaast alygsraang
      241 vimittkkgr knqglgvsms vgysvgspdq stlpkyqnny gggyglyyed ptsrflyrdl
      301 ndlfpdmasd gkkhlvvpts edaswgakfd pnlqvydwrs fdptsshyqk tspwtaaanv
      361 ptkflqdatt fngtvgidgg gengsfrvsy trfdqtgilp nsrlqknnfs fsgthdfnkk
      421 lsvstninft rqdakgrysn gysdnlmtsf rqwyqrnvdi vdlknafert gqnitwnwad
      481 ptdlkpiywn npywqryndy etdwrnrlfg nvaltykitd dinvmgrvtm dtynelqeer
      541 vavgsivnng taqyarfnrd fremnydlfv nysknitedf nikamlgnni rrtdvntmra
      601 atvgglvvpg iyalsnsasp msaptetava lyqqgvfgsv slgykntyyl dltarrdvss
      661 tlpvanntyf ypsaslsyif snhlsdkipa lsfgklrvny aevgntapaf slkntyvkpt
      721 nlnadnrdaf ggqtlfavss tlnnpnlrpe rtrsaeigle mkflknrigf dltayrtmsv
      781 dqimpvavsk atgydtkyvn agtiqnkgie lsafgtpvet kdfswrvlvn ftrnrnevvs
      841 lygdtpnlql asfgggvtln atrgqaygvl qgtaiklndn gqklvattgy ytqtdatsii
      901 gnvtpkwkmg vsntlnyksf sfsflidiqh ggsifsldry yglatglyke tdilndkgvs
      961 vrapisqggg wvfdgvqedg santvrvsge nygvfgyrrn pasvfvydag yvklrevtls
     1021 yklpatilgn trffksasis vvgrnlwiih knlpyadped gltsgnlsgw qsgaypslre
     1081 iggslrfsf
//
LOCUS       WP_093200503            1129 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093200503
VERSION     WP_093200503.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1129
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123305
     Region          33..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgpistfnvw lrkycllmaa vlfctyasaq qgrritgris vstdgspvqg asilvkgtri
       61 gtssdhngny altisgndpv lvisavgyka qevsvgnksv vdatleesse tlkeavvtal
      121 giqrdkrslg yavgevqgkd isrvaqenvl nslagkvagv qisstgpsgs svsmiirgak
      181 slssdnqplf vvdgvpinns lnnvgqigad nrvdygnams dinpedvesv silkgpsaaa
      241 lygsragngv vlittksgsk vqkmtvsvts ntvfdkpfkf lkmssrfatg vlpftpdsnp
      301 ypggvlqide gsaggvgpel dkgykaiqwd spvdangnki ptplvshpnn irdfvqtgit
      361 stngisiann ndkvtyrlsy anmssrgivp ssdlfkntla vsstlrvnkk ltvstnldfs
      421 rsnsnnrpaq ergtnplqwa yavgshidin klrnywvpgk eglqqlsqsi gnynnpffla
      481 nevknaftrd rvfgnvkaew qitpeiklmg ryaldtynet retkigysyt sepkgaygis
      541 alkryernad flatydkhfn dlsvlvsvgg nnrysessdi ttkskdktgl vipglytiqn
      601 iaqaniqytn yvykkaiysa ygtinlgyrd miyldltarn dwsstlpvnn rsyfypsasl
      661 svlinemvrm nnvnlfkvra gaaqvgndan pyslfatlqd agswngitrl tksggillpd
      721 lkpelatsye vgvdlnmfrn rlrfagtyyt sdnrnqiipt qlpsstgftt kninaglles
      781 rgielslggt vldqnglrwd lttnftknit rikeladglp yytlwtdakg gawtyvgdkv
      841 gdiydaqvit vtdknspyyg ypildndgsw qntsavnskn kignfnpdfm lglqnslsyk
      901 gftlnfsldw rkggqfvsqt yrymesdlrs qrfldnlinp ggrtgdqvan ylksnpeqli
      961 kihgnffpiv ggptadyggf pyefggksyp ygvfnpgvia kydgsgniig ytenlggtgt
     1021 kiipygdnyp wdftraatfd adfiklreis lgyelpskfv kaigiqsanf avysrniilw
     1081 tkakinidpe mafqpqtsaq agtqfkqgie rynvtpwvip vgfklgltf
//
LOCUS       WP_093200825            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093200825
VERSION     WP_093200825.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117845
     Region          23..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktilmvwat cvltwvnafa qdriitgkvt saddgaplvg vtvnlknttf gtitdasgny
       61 rikvpsgqka flrfsfvglv sqeieigtqs vvdvqlaads kslievvvtg tgtatskkkl
      121 giavesitae klpstptasi dqaligkipg aqissisgnp gdpvnivlrg intvqngtkp
      181 limvdgvqia atdlnsldls nvervevvqg aasaaiygaq gangviqift krgkagavai
      241 qfstsysanq finsghvkka dhhpyltdgs nniindkgqa igyndvgsid yisyqyggat
      301 ryaildprnv adkpynanlk yydhfkqmfq tgstvnnsls isgatdksdy alsvsnnhtv
      361 tpimkngyvd rtnvsanlgt elfknfrlss ntqliytknt ldpglganyg tgkggvgtvy
      421 sflntspffd lryrmadgsv payqtakmls inafnpyyqa eyasalnnkv dilqhfeady
      481 kpahflelna kyglnyrten arwtylnqsl nansnyyesw agnyasdnkg eidnfqytst
      541 fqnflatafi ktdferdfhl kvpiqtstqi tfdyrknkst dyrtyglglp lsppikvtst
      601 ssqavgldye epfitygyli nqkvdfgdfg gvtagfrsdw ssafgggskp ftfphfdgyi
      661 lpssfwngpv sgsvpyfklr aaygeagiqp gafdrypild qrnlgdgivy stqtssrnpn
      721 lqvevskefe agtdftvnvg kgsnwlntin gsfsywkrks enviysvsvp pstgatgqlt
      781 nainmssngv qfqlnfplyk srlfnwdftt nwshqlskid aisggadiil tssagstalv
      841 lapgqvigqi ygfkaltsld qkkedgsryi sesdvskyev vngrvvnktt kglqftenty
      901 sfgnpnpkfn asfinnlgfr dlvtlsfqld wvygshlynq tkewmyrdgi hgdfstpvti
      961 dgktaaytay ygsaysgswg slygagnnat kdyffedasf lrlrnvslgf elgkifrlpy
     1021 fkkcqlvltg rnlftvtkyt nfdpevssgt anssydrgvd nstlpniksy qvglnigf
//
LOCUS       WP_093201558            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093201558
VERSION     WP_093201558.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117114
     Region          26..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrrllwllt iligwsvtat aqsqlltgrv lsdddkvglp gasvslkgta igtttdaqga
       61 fklslpagga tlvitfigyi kqevaittqt tlevylkpea sqltevvvta lgiqrekkal
      121 gyaqqsiggk avsevrpsnv analsgkvag lriqagtgpg agstiqirga ssitnnnqpl
      181 ividgvpieq sfqkrlgggi gdinpenikd isvlkgpsas alygsraang vilittkdga
      241 gtkgigvevn tnytferpwi ipdfqntygg gngyrtwytd gwsgaitnpq eiqqyraayg
      301 pyapltgteg tdeswgapmd grlvrqwwtg tdvapltpnp nnykdfwqtg ttwsnniais
      361 ggndkgsfrl glgrldqkgi myyndyhrnn yklnaayhft pklsvnvsae yiqsgsgnrg
      421 ytggqefiws hrqtdwvklr nwrdyasvhi qkagdtdppn wqhtfftnpy ylqektpssd
      481 tkdrlvgnia mtykilpdls imlrsgtdlw tqtainvgnf ervrngsrsy gayseevlrr
      541 qetntdvllt yrkdisesfs vnatagallr tnyykrnytn vgqlvvdgvy nlansiatqn
      601 tvasrierke sqsvfgavnl gwqnmlfldv tarndwsstl psdnrsyfyp saalsavltd
      661 ivpslknstl sflkvrgsla qvgndtdpyr lnptftpgts wngslpeffe ptqkpnnrlk
      721 peittgkevg learffrgkl gldityyeql tkdqiipvql skatgynsai qnigkmqnrg
      781 ieitltgtpi klengftwdv avnfsrnrnk viellpgvln nlvinerrgl tlearagqpy
      841 gtlygygfer vqgsnpaaay ydgsgkyvgq lvmganglpi ksttqkilgn vqpdwmgglt
      901 ntfswkgvvl salidakigg dmydegtana rwtgqyaeta vgreegvigq gvnqvfksdg
      961 sytfkpnsti vsanqyygyn nprnyheaai fdasyvklre vslgyqipag flkkfrvqsa
     1021 kisvvgrnva mlfknhphad peidanggna qgfgygelps srsmgfnlsv gf
//
LOCUS       WP_093201765            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093201765
VERSION     WP_093201765.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115684
     Region          23..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqrllkwllp alllvqtgta faqqvsgtir asqdqqplvg vtvlvkgttr gtvsgadghy
       61 tvpakagdil rfsfigfkav eipvgaatvv dvalesedaa lqevvvtalg itkekkslgy
      121 avqelkskdi searegnlvn alsgkiagvn itnsqgnmgs srivirgets iagnnqplfv
      181 vdgipvdntq lgigsgrdfa naiadvnpdd iesisvlkgp naaalygsra sngviliktk
      241 sgksaarkgl gvtlnashti edllvlpdyq nvfgqgtggl fsykdgkggg lndgtdeswg
      301 prmdgrllpq ffskgeavpf vahpdnvknf fvkghttnlg lsvagsddkf dyrfsfnnsk
      361 qtgvipntgi tknsfavnas yrlndrltin tsanfirses dnlpglsgrg nsvmlqflwf
      421 grqvdtgllr nyrangendf nwnhsyysnp ylllyenttg qrrdrffgnv nlnyritdwl
      481 satvrtgndf ytdkrkfrvs ygtngtpygs ytedayvvse nntdfalnvk kklnedfeld
      541 glvggnvrtn fneqnyqqap rlavadlytl nnsrdplvsy nifskrriys ayasaqlgyr
      601 nfaflnatar ndwsstlpra snsyfypsvn asvvltdaln irtnwlsfak irggwaevgk
      661 dtdpyqlvnt ypfnqpfgsy plltvsdvll ntnlkpeitr ssevgvelaf lksrirldvs
      721 yyqtdsynqi lradvspstg ykqkllnagh innrgiealv natpvklang fqwdvtvnfs
      781 rniskviald kdgflndykl atsgvttlas vgkrygslyg taysrndkge iivganglpv
      841 kdanlqtlgy ytpkwmggit nsfsykgfnl svlidtkqgg qlysatnatg rytgvlastl
      901 pgrdaehggl syyypgnnas tapvqvanpt aatpngervy qdgmifngva adgsankviv
      961 paeryykavy snsagiqeas vfdasfiklr evrfsyalpk dwvrrvylqg vtvslvgrnl
     1021 aflqkntpni dpetafntgn gqgleslqlp ttrsygvnln vsf
//
LOCUS       WP_093201817            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093201817
VERSION     WP_093201817.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115559
     Region          21..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnklftlffl lagfwataqd rplsgvvtsa edgqplpgvs isvkgqtkga ttdaagafkl
       61 svpsgsvlvf syvgftsmev kvgnestlnv qmavsakslt evvvtalgie rdkkalgysv
      121 qelknseltq arptnlvnal sgkiagiqvt ssngqpgass rimirgansi ggnnqplfvv
      181 dgipidngsy ntaasasatn tnnvsvdygn gasainpddi dnisvlkgan aaalygsraa
      241 ngvilittks grgskgvgis vnsnitfdkp frlpewqngy gqgfskvnad gtygggvfey
      301 vdgkgggind gvdeswgpkm dgrliaqyns pidpatgkrv ptpwiahpdn vknfhrtgmt
      361 ttnnvaitgg sdkgdfrlsf tnlhqdgmyp ntnykrknla fnasyhltpk lnarasvnyi
      421 kdgsdnrqnl nlywiwfgrq vdladlnqev epgtdpsqwp vqrnwnsnyw nnpyyvlrhq
      481 tygndkdrvv gnvqmtyqvl pwlkvmgrsg tdfgldrrit krakgvglvn gefaednvyv
      541 qetntdflvt gdkhfgdfqa tvsvggnhry syfqrdylqa pelkipnlyn iansavrpnv
      601 ynrstkksvn slygsasfsy rdyyyldvta rndwsstlpa gnrsyfypsv sgsavlseal
      661 gfnsatvsyl karagwaqvg ndtdpyttqq vyqaedawgs vttfsennli ynsklkpeqt
      721 tafeagiear lfrnlinlev tyydkatsnq ilranvplss gyynsvinag kirnsgieve
      781 lsatpiklan gfrwdvtlny arnrsevvdl gglsnyqint gsllrnvile arpgspygnf
      841 ygtytrrapd gqmiidasgy pvmssdrrvi gnimpkwtgg fqtsvsykgi tlstlfdarf
      901 ggqifsqgin igrytgvlke tlpgresgni vapgvtetkn adgsftyapn tkavllpeny
      961 yhnfynrnnn enymfdasyv kwrelrvsyt lpqkwfgrtp frgvtlsavg rnlallyknv
     1021 phidpetsyy gdgnvqgfen gnlpsarsig fnlafgl
//
LOCUS       WP_093202752            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093202752
VERSION     WP_093202752.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115667
     Region          29..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlhtllrafr lvllvgavvs gsvswaqdrv vtgkvtdetg splpgvsvlv kgtsrgvsag
       61 adggyriqag sgqtlvfsmv gmttkevava aqtvidvvla stdsqlnevv vtalgikqek
      121 ralgysvgei kggdlvnaqr dnylvslqgr vaglnvttts gmpgsstsiq lrgaasiggn
      181 nqplfvvdgl pidnrttsgg vlysnranrd idylnkasni nfndiesmti lkgpeaaaly
      241 gidaaagaiv ittksgksgr tqidysnnfr fsevyrfpev qqvygrgtag ytdpnalsff
      301 gpkyaegskm ydnignffrt gftqthnlsf sggteratyn lstqyvgseg ivpttslknf
      361 nvkltsrikl sdkmslqpsl tyinvdnvkv mknnsgfvia llswpgndda snylnadgsr
      421 rillsairqg epdnpyfsiy knhleditnq traniqweyt pldwlkfnar fggdiystrs
      481 niflhpeswq agngagvtgg fssggsveda aensrllngn flatmnkkfg klnttlilgt
      541 aiddrdyrtn vmygqklyda nfnsvnntdp atqrdkysvs kqrtqgifgs lslnyedwly
      601 ltltgrndws stlpkknwsf fypsaalsyv ftdmpgikgn tgilnagkir laygqtgnpp
      661 ppyfvyprlv qqttygggyg ydfyggntdl qaergesfel gtelkffddr lgidaayyqk
      721 slsqqivqqr lsyatgfifg llnggsfqnk gveiqltgmp vktkdfrwnv tlnftklktv
      781 vsslpaqvpe yynsdtwlyg qarasafvnn lpsffdasnp ayrgfnwnyy qrgmgsatai
      841 ggysyqrnkn gdilinpatg lpiqnpnflp igdrnpdfti glqnsftyrn ltlsflldir
      901 kggdvfngte mylwrtglsk ktlnretpvv fkgvlrdgre dsdsptrnti qvnptlrsad
      961 yfnaipesef vekdinwvrl rdvtlryqvp ssvltrsklv ksasifvngt dlflltnytg
     1021 adpnvngtta asggvggggf dfgtvsmprg fafgislgf
//
LOCUS       WP_093203049            1166 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093203049
VERSION     WP_093203049.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1166)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1166)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1166)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1166
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1166
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130204
     Region          44..108
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          155..1165
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhtlllwvs aglafgyqag paqtfaraer tvqhseyapl thrslrevlk qvkseygvhi
       61 lfenrtvdhl svpagsirmt apvevvlenl lrpfgltfrk ikdrsyiivg eaknprtiag
      121 lprpalvtlp siasdapagt psvttiqlsp kdvpirgtvk dgatgeplpg anlqvkgttr
      181 gattdgtgsf ridvpdreav livssvgfet reilvgsqsi leinlkqidk alnevvvvgy
      241 geqkresitg aississkdl dkihggatvs sglagkipgv sfrmtdgrpg asaniqirnm
      301 gnplyvvdgi qkdagqfnni spndiesitv lkdasaaiyg vraangvivv ktkrgrtgsq
      361 ntinvdaytg fqnwtrfprt tnayewmlgk adaemnqygr tditpaelak wkqgteygyr
      421 sfdwydfivk knspqynvnl satggsdkin yyisathlfq nsvlgrefif krtniqsnvd
      481 aqitnslkvg vqingrietr dnpgvpgvdd ywaprfalfr nrpterpfan dnpnylndig
      541 hndtnwglln kkksgywted wrvlqanftg eytfpvkglt argvysyyia drlmngheyt
      601 ydaftyypdt qeykrtggst npwrergtrk vlenvlqgql nynntfgkhg igatfvaeri
      661 srreidvwvh svpqtnelpl lqfadmdtyn dtdvqtarag yigrfnynyd nkyflelagr
      721 rdasykfaps krwgffpsvs agwriteepf areilgagtv ltnlklrgsy galgdddvgi
      781 gdfdyvsgys ygsstvvmdg qvikgsrdrg vpitnitwft skildigadf sllngkvngs
      841 vdyfnrrrsg lrgrkydvlv pselgyslpd envnsdsqig gegslsytgk ahdvtysigg
      901 nlsfsrrkfl ssykprwnns ldhyrnsgeq rwndvfwgyh vtgqfqsqqq ineygvnvdg
      961 qgnktllpgd liyedtnkdg viddrdvrpi gnavgnnptl nyglnfqlaw kgidftadfs
     1021 ggagysymrn wemrwayqng gallrdfydd rwhredpfnl nspwiagkyp alrfndgghs
     1081 nnnkdsdfwl tnvrylrlrt leigyslpka llervkvkra riyfntynlf sidnlrkvgi
     1141 dpeisegngl aypqnkfvnv gvnlsl
//
LOCUS       WP_093202742            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093202742
VERSION     WP_093202742.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112794
     Region          28..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlhllltscr ckllilcllp mmaysqdril tgrvsdtkgq plpgvtiqvk gtprgtntna
       61 sgeyrlsvsp gvtlifsmig tqtqeielgs qtelnvtlen avtsldevvv tgstltssrr
      121 tlgnsiasik senltktgtn nlfgalqgkv agaqitqnsg dpsggisirl rgvkslqgns
      181 dplyvidgvv vsnssdnvsq iasatqagta atqgqnrmad inpndietin vingaaaaai
      241 ygsrasngvv littkrgksg kprvtfstsf nvnelrkkvf istygkqfgt adlrlhtiga
      301 apasapasdv vsivrdgtat nlyknlvdvk rydyqddifh tgygtdnyls isggtektqy
      361 faslsylkne giirgtdfkr yglrlrleqr ltdwakvslg lsytnsfshe mpngnvfysp
      421 insvnitnni ydisqrdaag nlkaveptri npltvietfk ftqavnrtvn nfqlnltplk
      481 glsvdwivgv daysqlgknf mppypyatea glpaerypkg faatannlvf linndvnaty
      541 srdltdwlsl natvgfnyqy qqkdqsvstg qnlspfietv sgasttitag ydlnrfaisg
      601 qfaqatfgyk nqlfltgair rdgstifsps etnqlypkvs gswvvsdagf wkqasldnvf
      661 sslklrasyg dagglsalgt ydrfwqfapt lflgantlvp narlansrvr permrelefg
      721 gdlsfwsdri slgltfykqk ikdlvvnrdl apsqggtsii dnvgemenkg vevtlgiqpv
      781 ktkdfewdvn fvysrnrnkv talgsptvsi snvagapvfl aqgyaapify gfyyarnpdg
      841 sllltpqglp qrergtapaa gqltgtpqrg adgqptgtfl nkiignpnpk wtgsfstslt
      901 ykqfglrvll davqgfqifn adkrtrnnvg igdlaeaemk gtaprgtvfs lvnieeyrvd
      961 dgsytklrev alsysfpklf kglermqlsl igrnlhvwtk ypgydpetna ggnsdllrgv
     1021 dfgnvpiprs yqvsltanf
//
LOCUS       WP_093203218             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas yamanorum].
ACCESSION   WP_093203218
VERSION     WP_093203218.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas yamanorum
  ORGANISM  Pseudomonas yamanorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas yamanorum"
                     /db_xref="taxon:515393"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38755
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 sdafgaelil kvvapnesel tliksgtvlv gmlnpfsnet itrlaehgvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv ticgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_093203729             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. YR750].
ACCESSION   WP_093203729
VERSION     WP_093203729.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. YR750
  ORGANISM  Variovorax sp. YR750
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax sp. YR750"
                     /db_xref="taxon:1884384"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38636
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etvkklvasg htvrvqsgag vaasvtdsay qaagaeitdq
       61 pgafsadmvl kvrtpteset sllksgavvi gmlnpfdaag lqrlaaagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf idvpyetqee kdaaegvggy arpmpaswlt
      241 rqqaevakrv aladvvista lipgraaptl itedmvksmk pgsvivdiaa gkgpdgvggn
      301 cplseadrtv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvtqd gqvtkk
//
LOCUS       WP_093203572            1159 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093203572
VERSION     WP_093203572.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1159)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1159)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1159)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1159
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1159
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125258
     Region          29..95
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          114..1158
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 malplrstvl lslfvltlpt hgqrlaigrd rsltevfdel ekryhvqfay qkrelrnkri
       61 dgafaltsas vegslsrllt plnlsfekig etyiiserrs agvakvtvdr evdiiikgkv
      121 aakdgtglpg vnirvkgtsr gtvtdaegry tlsvpsgqst lvfsfigyvs qevtlsgqtt
      181 ldvvldtemk qlnevvvtaa gierkatalg ysvstinsda laqknepdpi ralagkvagv
      241 niqggggvag gatnitirgn sslgnnnqpl yvvdgvpfdn stfapvggsg qrqtqssqst
      301 anrafdldpn niqsltvlkg aaaaalygsr aangaiiitt kasakksrkg teityntsys
      361 ieeiaglpey qqkygqgtng dyrsavygss gsayssrpti phplaragfs aadfpqfyea
      421 dgvtpvqvpy rsyagkaqrd ffrqgmvfen altvnsgsek gnftvglsrm tnkgmvpgnd
      481 inrtsinvgg narldnkfya rgtinyimtd qksppiggtg svmstmyylp tsynltdypf
      541 enpntganvy dyagvdnpyw svrhspstsn vdryygnfvl gfdplpwlni qntagfnayt
      601 drrvsvlgkg ssvyangtin tdniyrqeld ntllvtatks fwedfnvrai fgnnvnqrlt
      661 qrsafmgtdi itagindisn tstitlgglp nnrarlkqry yafftditld yknyaslnlv
      721 grndisstlp pqnrsylygg vngsliftea fhlagkklsf gkvrvgytrv gneaspyqts
      781 nvytsntssg dlgapfsngt vtnvstltls dilansvlkp efitefevgt elqffdnkls
      841 vdvtyynkrs tsqiftvksa pssgftdrii nlgqtsnrgf evavsgtpyv sasgfrwnin
      901 anftrnrnrv ddlggiaqlv ygsnvhiagq pygqiygtry ardnegnilv npqtgkpiaa
      961 atsgpignpn pnfivglsns fsfkrftldv lfdwkqggai ystnisnals rgvtrdtedr
     1021 etlwvgpgvl gnvntlqpil dgegkkipnn taltvidyff nggygpggig egyvfdatvf
     1081 rlreisfgys lpagllkhtp fgaaslsisg rnlwykapnt pkymnydpev stgaannqgf
     1141 dslgvptarr yginlrvsf
//
LOCUS       WP_093205811            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093205811
VERSION     WP_093205811.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119500
     Region          28..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqllqagic mlllcvsgfl fpgyaqqrtl sgkvlsaeds qplagvavrv kntnrgvntd
       61 adgryrltil sdkdivvftf vghepaeevv gnrtelsvsl ktdhkllnev vvtslgiqka
      121 krdlsyatqs ikaqdlikar epnpvnalvg kiaglnigas aellrapqvl lrggrplfvv
      181 dgvpiisdty ninpddiesy dvikgpsgsa lygsravngv iiittkkgsr dkrgvsvevn
      241 sstmveqgfl aipkvqdlyg pgdhgtysfv dgrgggkndg dydiwgpkfe gqlipqydsp
      301 vdpatgirkg tpwiargkdn ltrflrpgil stnsvsvsss sektdlrfgv tnqyqqgmip
      361 ntqlnsttfs atlgqnlsdk vrfesnfnfs rqasanypdv nygpnsliyn mviwggadwn
      421 vddmkqlwqp gkegiqqiya eyqrynnpwf vakewkrghy nnsyngyalm kfrlrddlel
      481 qartqvtgye lfrnekmpys attygreqak gdyredrrsl lenntdvlln ynktfrneis
      541 vravaglsgr ffryngnyas tdylnvpgvy sfdnslnavr ansfnsqmqv lsalysvdvn
      601 lgkyatvstt grwdknstlp ssknvffyps agvssvisdf vpmpqaisfv klrasyanvk
      661 daftqqniyt afsalsggnp lgygqtfasp ydgpsygttv aytisrpynn evaasysnsl
      721 ldpnlkpssr tsfeagldir flknrigldv syfsyldgpr ifgltlpeat gytslttngi
      781 ksqrrgleia ltgtalksar glnwdvtvnw stfqeylkei ygnqarlnqf ykigdrlday
      841 ygsafyrtke gqiindasgr pivnavsqfl gntnadfafg finkfsyrnf flnvqidgrv
      901 ggviedyiqk qtfrggrhie tvegkmgdar fqdykgvksw vgpgvvlteg siqpdvdgki
      961 tnydklsftp msdkyktylq dwisryyntn eaniisrsfv klrevtfgyq vpsrlltgrm
     1021 sflkgasvsf varnllyfaa kkdldveqfv nysntssdlq tpttrrygvn inltf
//
LOCUS       WP_093207265            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093207265
VERSION     WP_093207265.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120519
     Region          26..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkflltlii plvmisapvf aqsiggtvks vsdgspipgv svtvkgktlg altnsqgqyk
       61 laisgentli fsaigyktle vatagrttvd vtleeatssl nevvvtamgi akesrklgya
      121 ttqisakdit atsptnfasa lygkapgvti nanpggatsa vgiqirgvns igyqrqpllv
      181 vdgviirngd annegywnnq kiganglldi npeniqdini lkgaaasaly gsdanfgviv
      241 ittkngksik kgigvdvsls gnvekvstvp dfqtewgpgy ersvnmasfg addqgwihtt
      301 vngqsvkypn frsyaqfgpk mdgsdvywwd gqmrkyttqk nnwkqfyrtg sstiatvals
      361 natdrgsyrl sftrndyqgi qiggkqeknt fnlntkyfvt pkvtldvvmn yvnekvhnrp
      421 rqiyyltnnf ggffspadqm svffnkyqts kgykwvdyns nldveerlky nvrakdfldf
      481 lwnqlankyd etsnrfmpsa tlnynivkgl nlrgrmgidy tsfnqetker stqpisagas
      541 gsygtvsnns tytygdlllt yerqlsqkln atisvgyqar kekynfasas trdgltsenw
      601 fslsasktsp aqgstsveml lkdgmfgiln leynnflfve gtlrrersss lapgnntfvy
      661 pgvsssfels nafnlpaavs ysklrgawgv vgnppdryia nqvyssgsld gtpylfpats
      721 gfgnknlkne mkyefeigwe nrflkdragf dityysnkik dqittlgtps tigsssvlrn
      781 vgdmrnygie lslygtpvks shfswnarln famnrskvis ladglaqltl dnkdngslyv
      841 yakpgeaags iwgydhmkda kgnyvvgddg fyqidysklv kfgniqskfs gglmntftyk
      901 nfslgvltdf vwggqvisls rlygtgsgly knslfgrdae hggvayykda ttgkltgvga
      961 gvdngpkgek vyhdgiiaqg vttggeknat iveapqyyry hynwggypgs gsnitykdav
     1021 fdnnfiklre vslsytipsk alsklkiqnv tvsaygrnlf yfyksltgld peegvgtgwv
     1081 sratsvgagn aatrsiggsl rfsf
//
LOCUS       WP_093207330            1131 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            aquaeclarae].
ACCESSION   WP_093207330
VERSION     WP_093207330.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter aquaeclarae
  ORGANISM  Siphonobacter aquaeclarae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1131)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1131)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1131)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1131
                     /organism="Siphonobacter aquaeclarae"
                     /db_xref="taxon:563176"
     Protein         1..1131
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124710
     Region          63..115
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          161..1128
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdkpficfir rytllggall lllppplssq tvariafasq vshsqtlqpl gealdelkah
       61 yridliytdr lvaghkvasi sygrfqsaem alqellknld lrfqkvkdkt yiirrsrpvk
      121 kqnpaetpah eenersqadf tavplagltp ttsafgedqp irgqvvaaet ndplvgvsvl
      181 vkgttrgvnt dadgrfqlal pavpatlifs yvgyerqein itsqtnidvv lkpdqrslee
      241 vvvvgygtqk ktnltgavat vssedlirrp vgqtstalqg mmpgvtvtqr sgrpggdagt
      301 irvrgvgtlg ggqdplvlid giegsmnnid pnlietvtvl kdaasssiyg sraangvvli
      361 ttkrakggkl svnynnyfgw qsptnlphmv navdhmlltn eayvnvgrap lysddliqky
      421 rtegasnrdl ypdtdwqkav ltgsgfqqsh fltvkggtek frfltslgyl nqngiiqnss
      481 ftrytlrnnm dmqfskklsa radiqlvapt tiepgrssde vfhwmnripa nqiginsngt
      541 wgdgwngdnp iafsraggqm knnspyvlin aalvykpvdw itaevayapk yalsidknfn
      601 rniqtykpng alsflapaks tltegtsrsf yntlrgtvtl drtfgdhgvk vlagfsredf
      661 rndyvtayre gfllpdynvl nagaadiqrn tggasewalq sffgrinydy kqkylfeana
      721 rydgssrfvk gqrygffpsf sagwrvsqen fmqplsgvvn elklraswgq lgnqnigtyp
      781 fisslnfgsy algkqivnvv alntlantni twertemsdi gldltlfsrl sltadyylkr
      841 tkdilltldi paiiglgapn qnagvvdnkg welgltyrgk ardfrydigf nisdvrnkii
      901 dmrgvnltgv tvnregypis siyglqaegy fqsddevaah aqqfgtikpg dlkykdqngd
      961 giinaddyvv igstvprftf gstinlaykg fglnvvlqgv gkadgllyeq gimpfflggt
     1021 vqeqhknhwt penrnaafpr lafsesnnek issfwmknaa ylrlknvqfs ytlpqaltqr
     1081 agisslrlfa ngqniwtldr fwngydvesp vgtgrtypqv kmfsfgvdas f
//
LOCUS       WP_093218323             377 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Variovorax].
ACCESSION   WP_093218323
VERSION     WP_093218323.1
KEYWORDS    RefSeq.
SOURCE      unclassified Variovorax
  ORGANISM  unclassified Variovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="unclassified Variovorax"
                     /db_xref="taxon:663243"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38990
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpaest agetrvavtp etakklvagg hevrvqsgag lrssaldsay eavgaritne
       61 sgalgadlvl kvrtpfdnel almksgativ gmlnpfdaag lqrmasaglt afaleaaprt
      121 traqsmdvls sqaniagyka vmvaahhyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslggkf idvpyetaee keaaegvggy arpmppswle
      241 rqklevakrv aladvvista lipgraapvl itedmvksmk pgsvivdiaa gkgadgvggn
      301 cplteadktv vkhgvtlvge tnlaamvgad asalyarnvl dflklvlqke atavqvdmed
      361 divaaclmtq sgevkrk
//
LOCUS       WP_093228004             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas vancouverensis].
ACCESSION   WP_093228004
VERSION     WP_093228004.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas vancouverensis
  ORGANISM  Pseudomonas vancouverensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas vancouverensis"
                     /db_xref="taxon:95300"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38562
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag vsasivdsay vaagatigsa
       61 ndafgaelil kvvapadsel aliksgtvvv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag dvaadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_093232826             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium sp. NFACC03].
ACCESSION   WP_093232826
VERSION     WP_093232826.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium sp. NFACC03
  ORGANISM  Sinorhizobium sp. NFACC03
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Sinorhizobium sp. NFACC03"
                     /db_xref="taxon:1566295"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55155
     Region          1..527
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaplera anearvaltp dsavqlaklg yssiietgag vaagfsdday raagvevaps
       61 aealwdsadv vvkvrppeps evahlsadkt lisffypgqn aellelakak ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigvatslg aqtyafdvrp evaeqiesmg aefvyldfad gdgggqqdga atggyaapss
      241 pefrekqltk frelapqidi vittalipgr dapklwladm vaamkpgsvv vdlaaerggn
      301 cdltvadqri vsdngvvvig ytdfpsrmaa qastlyatni rhmltdltpg kdgklvhnme
      361 ddvirgatvt fegaityppp ppkiaaiaaq kpkekvkept peekraieta afkaqtksql
      421 allaagtall llvgafappa fmshfvvfvl acfvgfqviw nvshslhtpl mavtnavsgi
      481 vilgallqig sgnwlvvlla alsvliatin ivggflvtrr mlamfqks
//
LOCUS       WP_093237907             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            halocasei].
ACCESSION   WP_093237907
VERSION     WP_093237907.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus halocasei
  ORGANISM  Psychroflexus halocasei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Psychroflexus halocasei"
                     /db_xref="taxon:908615"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108019
     Region          34..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfsgflt lllvlavqis faqtktvtgt vtgedglpip gvnviekgts ngtqtdfdgn
       61 ysisvasgqt ivfsylgmkk qevvvnnqst initlledaa elaevvvtgy ssidrseygg
      121 sissvqsedl eqiplasfeq ilqgkaaglq itagsgqpgs sarvrirgng singengpmy
      181 ivdgieitpg dfanlnsndf ervdvlkdan atalygsrga ngvivvstkk gsfskgttfn
      241 yktsfgfsei geakfemmns sqllnfqrli grglgagktd aeiaelamvn tdwsdeffrt
      301 gtvsthelsm dggndktrff ssvqyldqeg lslrsglkrf slrnnlehrp dektqiglnt
      361 qmsyskssri dsessvtlqn pfaaaylgsp yhapydengd fntgggrvgp nalehllksg
      421 ndrnvvkiia sgfanrelfe nvtaginlgv dyqqsnviry tdpnshygrt tdpgqqgsyn
      481 esnrydanit sttnigyant fdekhnfsfd ayleyykrhv rssgftgygi nelivgypgg
      541 itagspsnel iptisggvle egifsyfgia dygydgrfgi nasvrrdsss lfadenkwat
      601 fwsvagrwnl heegfmdgad fvdnlklras ygtsgnkgai dpfqyatsyg qssydgqpgf
      661 vptnlgnsdl twetsnqlni gldfdlfdyr lygsveyynn lttelfidys lsatagatsi
      721 esnngemsnk gvdlslnydi vrsedkdgln islnvnanyn kntiedlgqv nefeqgtsii
      781 reglplgthy ivgwagvnpa ngqplyldkd gnvtnqysed nstanygsfn peytggfggt
      841 isykgfklst lftfqaeyyr fnnqtffqen pnfsqynlst kmldmwkqpg dvtevqsyly
      901 grefsskdie dasflkwrnl tlgytfsdkv iesigyisgl rvygmaqnls twtkftgfdp
      961 eddnniaqye yptpttitfg vdlkf
//
LOCUS       WP_093244386             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            halocasei].
ACCESSION   WP_093244386
VERSION     WP_093244386.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus halocasei
  ORGANISM  Psychroflexus halocasei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Psychroflexus halocasei"
                     /db_xref="taxon:908615"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111294
     Region          32..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyfythqcg fglillliff stttakaqnt yklsgqvtdt tgqaipgvhi qrinttngat
       61 tdfdgnynie vtgndrlsft ylgyqaqtia vnnrklinvq lspstealde vvinagyyrv
      121 kdrertgsie kvtsedielq pvtnpiealq grmagvevvq stgvpgaapt irirgqsslr
      181 tnfddngnlp lyiidgmpin sspidsqiql fegagvdpln tldltniesi evlkdadata
      241 iygsrgangv vlittksgqk nqgikvstkl ytgmsrvdnf lnllntqqyl kirkqafend
      301 gvepnaynaf dlvlwdenry tdwqkelfgk taelrsasfn isnanettsy iigasyqkqg
      361 tvfpgdfsye kktfnlnlnh qskdkkfkln lsanyglddn dlfnsstfvs talslapnap
      421 rlynddgsln wedstwsnpl atlqnegkls tnnlisnlgl tyrltpslsl kssfgythlt
      481 seeniqtpie sydpdmwdrv tnrsqysdir rnswivepqi hyrktwgqhh fntivgatfq
      541 enkntsltis grgyidrnli gnleaadqvs iikdrdltyk ysaifarlay dwkekyylnl
      601 tgrrdgssrf gpdkrfanfg aigaawifte enffdkhlnw lsfgkirgsy gttgndqigd
      661 yryldayeat pgpdglyptq ltnndfswet nkkleaalel sflnnrihte iawyrnrssn
      721 qlvgyplpai tgfskveanl patvenkgwe lglsakvfqk qsfqwntsln mtipssklva
      781 fpdieetaya ntyrvgeals ldilyefegv dpdtgyytvk dvnedgsydy ddrlitknlg
      841 rkffggvynk lnyknfslsf lfefvkqngr ktsslppgrl gnnlksvtey gssspedlqa
      901 psqsinafla fnryaynsdf sitdasfirl ktlslgyeis ndftknigls qfklfvhaqn
      961 lltitdyegl dpqspgskal pslqsltggl qltf
//
LOCUS       WP_093244562            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            halocasei].
ACCESSION   WP_093244562
VERSION     WP_093244562.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus halocasei
  ORGANISM  Psychroflexus halocasei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Psychroflexus halocasei"
                     /db_xref="taxon:908615"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117134
     Region          25..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkvkntvll lftllsagmf aqqvtvtgav kdadgiplpg vnilvkgtsn gtqtdfdgqf
       61 tiqaetgetl vfsylgmktq eigvsgdaei evvlesdank ldevvvtalg ikrekkslgy
      121 atqevggeev sdvatqnftn alsgkvaglk vkssgtmggs tnvvirgnas ltgnnqalfv
      181 vdgtpiinqn sntgdqqtgr ggydygnaas dinpdniesi nilrgaaata lygeraanga
      241 ivietkkgar nkgmgvsirs svtfadvnke tlpkyqkkyg agyaptydtg dgfwltdldg
      301 dgideettvf tadasygarf dpnrmiyqwn siypeldtyl qatpwtaakh tpndiwetgh
      361 ttinsvaldg gnedgnfris ytnlnqkgtl pnsrikrdni kfsgshdltd rltaaanvtf
      421 iktdgkgrfg tgydgqnlmq tfrqwhqmnv dlydqrdayf strknitwnp nsafnrtpiy
      481 tdnpywvrye nyqtdtrnry ygnvnlnyki sdvfsvlgrf tfdtyselqe erinvgsaav
      541 ssysrfdnrv aeynydliln fnkdltsdln ldgnigfnlr rneqtfiraa tngglnapgf
      601 yalsnskdpi nppleyeade mvdgifaras lgylstyyle atirrdrsst lpssdntyyy
      661 psvstsills niinedwlgf aklranfaqv gsatnpyevf ntyvvstpfn gqgsaslsst
      721 lnnlnlkset stsyevgles sfiddrvnfd isyyrtrted qitpvpista tgysrkllna
      781 geienkgvev lvglvpvrte dfswnmnvnw sknenevisl rdginnlqla sfqggvsina
      841 apgqpygair gtdyvydnqg nkivgadgyy evtsnnneii gniqpdwnag itntfkyknl
      901 sfsflidiqe ggdifsldtw ygmatglydv taglndlgne mrapiadggg vilpgvdasg
      961 nqntvripag stsdspygys ndanrghvyd asfiklrems ltyslddklv eklpftgasl
     1021 sligrnlwii dknmpysdpe aglssgniqg yqsgaypsar eygvnvklkf
//
LOCUS       WP_093246325             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. EL159].
ACCESSION   WP_093246325
VERSION     WP_093246325.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. EL159
  ORGANISM  Variovorax sp. EL159
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax sp. EL159"
                     /db_xref="taxon:1566270"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38517
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etvkklsasg htvrvqsgag vaasvtdaay qaagaeitdq
       61 agafgadmvl kvrtptdaea allksgavvi gmlnpfdatg lqrlasagvv gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadryqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmppswla
      241 rqqievakrv aladivista lipgraaptl itedmvkamk pgsvivdiaa gkgpdgvggn
      301 cplseadktv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvtqd gqvtrk
//
LOCUS       WP_093251726             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tessaracoccus oleiagri].
ACCESSION   WP_093251726
VERSION     WP_093251726.1
KEYWORDS    RefSeq.
SOURCE      Tessaracoccus oleiagri
  ORGANISM  Tessaracoccus oleiagri
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Tessaracoccus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Tessaracoccus oleiagri"
                     /db_xref="taxon:686624"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52758
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreig darvaatpks veglrslgyd vvvesgaglq asfedsayea agavvvadaw
       61 gadillavne pstsqiarlr pgatlitfla prqkpeltre laergvtams mdmvprtsra
      121 qsldalssla nisgyravve aahafgrfft gqvtaagkvp pakvlvagtg vaglaaigaa
      181 nslgaivrat dvrpetaeqv esmgakflhv aadqgvssdg yakeasadya araaelyaeq
      241 akdvdiiitt aaipgkpspk litadmvnsm ksgsvivdla aqgggncelt rpgesyvtdg
      301 gvtiigytdm asrlpgqasq lygtnlvnal qlmtpekdgq lvvdfedevv rtmtvahrge
      361 vtfppppiqv saapapakvd vaphpepvqk aprpwwhqva avaatsvvli alltvapssf
      421 valfgvfala civgyyvvwn vthalhtplm svtnaisgii ivgamtqlah ddwlvkalaf
      481 vavliasinv fggftvtyrm lnmfrka
//
LOCUS       WP_093251840             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rubrimonas
            cliftonensis].
ACCESSION   WP_093251840
VERSION     WP_093251840.1
KEYWORDS    RefSeq.
SOURCE      Rubrimonas cliftonensis
  ORGANISM  Rubrimonas cliftonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rubrimonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rubrimonas cliftonensis"
                     /db_xref="taxon:89524"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39578
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavpketr ayetrvaavp etvkkfialg aevtvqsgag daasipdaaf eavgasiaks
       61 faacvkdadl vlkiqrptda eiksfkkgqm lfssmypgld rpitdalaek gvevfamefm
      121 prisraqsmd vlssqanlag ykavleaanl ygkgmpqmmt aagtvapaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp ateeqvaslg akfiavknde flnaqtsagy akemsddykk
      241 qqaelvaghi akqdivvtta lipgrkapil vtkamvesmk pgsiivdlav eqggnvegae
      301 ldkivetpng vkivglpnma grlaadassl farnhlnfls pfikdgaltl deddelvkgi
      361 rltrdgalvh pfltkeg
//
LOCUS       WP_093255312             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Snoq117.2].
ACCESSION   WP_093255312
VERSION     WP_093255312.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Snoq117.2
  ORGANISM  Pseudomonas sp. Snoq117.2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas sp. Snoq117.2"
                     /db_xref="taxon:1500302"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38646
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpmetg agetrvaatp etlkkligqg hqvvvqqgag erasvpdaay aaigaqlgda
       61 aaalgadlvl kvaapnaael almkpgavli gmlnpfaqet leqlngrglt afaleaaprt
      121 sraqsldvls sqaniagyka vmlaadhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfeteee rqcaegvggy arpmpatwme
      241 rqakavhera kqadivitta lipgrraptl lheatvaemk pgsvvidlaa sqggncplte
      301 ldrvvvkhgv tlvgygnlaa rvpadasaly arnlldflkl vfkdgafhld laddivaacl
      361 mchggelrrk na
//
LOCUS       WP_093261550             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Saccharopolyspora shandongensis].
ACCESSION   WP_093261550
VERSION     WP_093261550.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora shandongensis
  ORGANISM  Saccharopolyspora shandongensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Saccharopolyspora shandongensis"
                     /db_xref="taxon:418495"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37545
     Region          11..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtspesgrts vgvpretmpg errvalvpgv verlcaqglg vvveagagqa alipdeafak
       61 agasigdpws advvikvnap teaeiarlsp gsaligflap ltdpdiadrl raagvqgfal
      121 esvprisraq smdalssqan vagyravlla asectrffpm lttaagtvkp asvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgakwldlg vsavgeggya reltddehae
      241 qthrlnsaia gfdvvittal vpgrpapklv paeavrrmrp gsvivdlaga aggncelsep
      301 grtvvgheit iaaplnlpas mpehaselya rnvqallelm lvdgrlapdl tdevlaaaci
      361 trpdpa
//
LOCUS       WP_093301530             376 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Variovorax].
ACCESSION   WP_093301530
VERSION     WP_093301530.1
KEYWORDS    RefSeq.
SOURCE      unclassified Variovorax
  ORGANISM  unclassified Variovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="unclassified Variovorax"
                     /db_xref="taxon:663243"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38606
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etvkklvasg htvrvqsgag vaasvtdgay qaagaeitdq
       61 pgafsadmvl kvrtpteset sllksgavvi gmlnpfdaag lqrlaaagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf idvpyetqee kdaaegvggy arpmpaswlt
      241 rqqaevakrv aladvvista lipgraaptl itedmvksmk pgsvivdiaa gkgpdgvggn
      301 cplseadrtv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvtqd gqvtkk
//
LOCUS       WP_093302118            1038 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter].
ACCESSION   WP_093302118
VERSION     WP_093302118.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter
  ORGANISM  Salegentibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Salegentibacter"
                     /db_xref="taxon:143222"
     Protein         1..1038
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113303
     Region          26..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkklflfas lllcsiqvll aqsqsvsgni vdaengmplp gvnvvekgts ngvssdfdgn
       61 ftieidegsi lqfsmlgyit qeiepegsei qielapdtea ldevvvtalg ikrekkslgy
      121 alqeiggesl tearennlan amtgkvaglq vvrgsngpas sskivlrgnn sltgdnqpli
      181 vvdgvpmdnf tgaanndfwn pspdmgnglg dlnpeniesm tvlkgasaaa lygsragngv
      241 ilittktgkt qeglgisyst nigfqsifss pdlqssfgqg angqydnqsg lswgpkiegq
      301 tvenaegeqe qlqaydnldn yfdnglnvnh slsfqqqvsd gtslfssvnh lddqslipga
      361 tlkrlnlmtr gvsvfgdkdn wksdvkvqyi rstaenrpln gvnvsnafst myllprsldv
      421 tkyerdtdef gnmrwyvpsn smnpywayrn nlnmdtrdrf mlngsirhdf ndwlyaeika
      481 gadlyttnte sklysgspls ptgryslgkn tfretnynal isgskddiig kwgaavtlgg
      541 nlmeqessli ssnagelevp nlfslnngia npgvsqgysn kkinslfgtf qvnydgflfv
      601 dvtgrndwss tlskanrsff ypsvstslvi sdmikntggt lpdwitfaki rasyaevgnd
      661 lpayqlfnfy nigkdpngnt tagrngtlyn pdvkselirs neigfdarff nnrfgidfsw
      721 yktnatrqli nlplnplsgy gsvkvnagdi enrgfelmln grildnpngf nwdmnlnfsr
      781 nvntvnrlad gvsqytlggf dnvsilaveg epygeiygtk yqrvedessp yfgqiivdee
      841 giplassdre rlgnqqpdfl lgfsnsfryk nlslsflvda riggeifsgt nraiqnagtg
      901 aqtvvngnre dlvidgvvad gegnfspntt gvspqlywmn ltersgnlgi neaniydatn
      961 vrlrsvnlry dlpnrwient ffnqayagis annvwmidsn lngvdpesvf atatnavgfe
     1021 nlasptirtv flnigvkf
//
LOCUS       WP_093302145             972 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter agarivorans].
ACCESSION   WP_093302145
VERSION     WP_093302145.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter agarivorans
  ORGANISM  Salegentibacter agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 972)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 972)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Salegentibacter agarivorans"
                     /db_xref="taxon:345907"
     Protein         1..972
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107528
     Region          24..971
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktlfkstlm lllmlpmsff aqetvsgvvs esatglpipg anvivkgttn gavtdfdgny
       61 tiqnvseddi lvfsflgfas qeipyegqat ldvqldedqa tleevvligy gstseqdatg
      121 svekisaesf nqgavvspeq lisgksagvr itpgsgepgg gseirirggs slsgnnspli
      181 vvdgvpldqr gvqgvrnqln sinpneiedf vilkdaaats iygsrasngv ilittktgkk
      241 esplalsydl kvsagriidk vdvlnadqfr tlinetpgtd psllgdantd wqdqiyqtav
      301 gaihnftatq gfenftyrin ynhtsqtgvl ktdvyernal nialnqdlfd nhlklsltsk
      361 givdenrfad qgaigsavgf dptqpvyneg syfdgyyeht lspeqqqiqa trnplalleq
      421 ldgrgvtkrn itnlnaeykf hflpelkfnv nagfdysend gynrrpltsa annqdipyfe
      481 dyggfnrntl ldfyfnyknd idfldteidl taghsyqeff itsqttetvs ndiqdfprdi
      541 nrnalesyfg rasfdianky lvsgsvrrdg ssrfggdnkw sifpalsvgw klhnenflad
      601 snvlnqlklr agygvtgnqe igpnygyfgt ynpsvggary qfgnqfyntl rpeaydsdlk
      661 weelqtynvg idygffnnri sgtieayyre tedllatvpv paganltdll vtnvgstvsk
      721 glefgingai iqqedfnwdl nynltfqdle itnltlgdnp nfqipqgeis ggvgnniqlw
      781 kegfdpttfn vfrqvyneng qpiegayvdv ngdneiteed rvaykkatpd yfmgltntmr
      841 yknldfsftf rgnfgnymyn ntqssngfvg agtvtpqpyy snfnsnvles nfnnnqffsd
      901 yyiqkadfvk ldnisvgylf pgedldirts ltatnvwtit dyegldpeia ngidnnfypr
      961 sttivlglnl sf
//
LOCUS       WP_093303323            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter agarivorans].
ACCESSION   WP_093303323
VERSION     WP_093303323.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter agarivorans
  ORGANISM  Salegentibacter agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Salegentibacter agarivorans"
                     /db_xref="taxon:345907"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118681
     Region          26..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknklhgilt lllafvvqft faqemtvtgt vvdedglplp gvnvivkgtn tgdqtdfdgq
       61 ysvstsrget lvfsyvgfgt eellvetsev idvvlrvdag sldevvvvgy gtstresftg
      121 takvvdgell nrknvsnvsq alagesagvr vinnsgqpgs sakvrirgig svngntdply
      181 vvdgvpftss spsalegesd tfnlnsinpe diesttilkd aaataiygsr gangvivint
      241 ktgragqsni evstktgvnf allpryntln speqyialgw egiynegvas gaedptayan
      301 enlfgdsgld prynmwnvad ggelinpdtr mvrdgvsrry npedwedygf qssirneanl
      361 kisggsektt yyssfgylkd vgyiidsdfe rytgrlnlth qvkdwlsgsm nmgyslsetn
      421 nngqsedsgs ifwfvdnipp iyplftrdae gnripepiyg gsqydygegr gfggltnsia
      481 dakysgsntm rhdlntsanl taditdwlsf ettfgaqyyn ssynslqnpf ygpsasqggs
      541 iyktktelft ynflqllrfq kdfgghsfna laahesnswe rqflfgnknq linpngtewn
      601 navvvssppg sytedytles yfgqlqynfd dtyflsgsvr rdgssrfvqe kwdtfgsvsg
      661 awvlsnesfl qdqsvfdflk lkasygtqge qagvgfypgy nrfdigslng mpsfsfntlg
      721 npdltwetst mmqaglefrf gtwldatfdy yrkntdnllf errvapstgv aiidvndgel
      781 lnagfefdlt ahiistqday fdvtlngeii knelltmpia petgepkvld qqgiygraeg
      841 ksiydfytrd fvgvdpedgq sqwrvfynda ngdgafqpge qvtnltdyla ttpdvsrgdl
      901 aegttknyae atqyftgesa ipdvrgafnl aagykgfsls aqflyqiggy sydgayatlm
      961 nndvvggnnw htdildrwqq pgditnvprl sndydpntna qstrfitkad flalnnvrlg
     1021 ysvpqsftes igvnslslfv sgdnlflmse rdgfnpsthi agssdtyrys plstvtggvr
     1081 inf
//
LOCUS       WP_093303270            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter agarivorans].
ACCESSION   WP_093303270
VERSION     WP_093303270.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter agarivorans
  ORGANISM  Salegentibacter agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Salegentibacter agarivorans"
                     /db_xref="taxon:345907"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110958
     Region          40..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnysrlkw valiilggif fflskaahaa ttnilfflqq evtgivsden gvpvpgvtvt
       61 vkntrrgavt kldgqyeita pangalvfsy igfktfevai dgrseiniql eediaslgev
      121 qinagyyntt arkrtgniar vsgeeiemqp ivsplealqg rmagveiqqr sgvpgsapii
      181 rirgqnslrn srddngnlpl yiidgvpvns splggsslng ttgidplntl nlsniesiev
      241 lkdadataiy gsrgangvil istksgksfe qktqvearly sgvgevsnkm ellnteqylq
      301 irnqafendg lepnqnnayd llvwdnylyt dwqeelyggt aeitdlnlsv sggnattsfr
      361 iggsyheegt vfpgdfkysk vtgglnlnhr skneklqlnl slnygvdnnn lfgsdsfisd
      421 altlppnapr lynddgslnw edltwdnpla nlqnssndqv nnlvtslgis yeilegltfk
      481 tnagytnlyr nqkgitkkes frpdirdsre hsssertnir kswiiepqlt ysakigagnl
      541 ealvgmtfqe sendnlrisg dgyvseslig nleaaesvev teyinimyky talfarlgyn
      601 wkekyfvnlt grrdgssrfa pnkrfanfaa lgtawifsee svvkenipfl sfgklrgsyg
      661 ttgsdqipdy gfldayeatp gpgglyptql tnpnfsween kkleaalelg flkdrinlgv
      721 swyrnrssnq lvgfplpstt gfpsiqanlp atvqntgwev efsslnistk dfrwqtsfnf
      781 tlpetklvef pnisqtsyen vyrvgyplni allynyegid petglyqvqd ingdgnfsye
      841 drtvieelgr qyyggisnnl syknfslqfl wqfvkqtgyd eyfsapgfis nqpenvfqgi
      901 adgelqqasq nftaaipysf arnsvhfisd asflrlktlg fsykipeell qnwkiegfrl
      961 flnaqnlltf teynglnpey pgggslpslr tvtgglqinf
//
LOCUS       WP_093303456            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter].
ACCESSION   WP_093303456
VERSION     WP_093303456.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter
  ORGANISM  Salegentibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Salegentibacter"
                     /db_xref="taxon:143222"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112396
     Region          29..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mniikfkvvf calfalmpfi gvaqtsedid veaivrgkeg kplvgatvtt eagntvvtds
       61 igsfslstgl ystlavaale ykpttvivtp fvdnislepa egyedvnvaf rkvekrnlis
      121 gvsfvdldel meknyntstl enmegfangf hgniwgmdey lvlidgvprd agsimpteid
      181 qisflkgvsa valygsraak gvvqittkrg kiqkqeidvr inagmfvpks ypkylgsaey
      241 mtlynearan dglsqrfdde tiyqhaagdn pyrypdvnyy ssdylqetyn rydataqisg
      301 gnetaqyytn lgfysagsll nfgeaennrt qrfnirgnvd iditetlyat vnasavyyng
      361 wgvntdywsg aanlrpnrfs pliptsmiee sdenslqyvn nssnlidgqy llggtqldqt
      421 npfaaiyagg snnytsrqfq fntgigadlg nlleglsfhs nfgvdystsy nqsynneyav
      481 yepswtnydg ddliasltqy gqdarsgvqn isdswyrqti sfsgqfnyet kieedhnvsa
      541 mliangfqqs iseeyhrtsn anlglyvgyd yldkyfvnfs galvhsaklp egnrqafspt
      601 ftlgwrlsee nflqnstvfd elkltasagi lhtdidiqdy ylyesiytqt dgawfnwrdg
      661 alsrstdsrr gqnddltfsk reeinlgvea slfdnlfqiq gsvfanrmtg givqasvlyp
      721 nyfetgwpns sfipyvnynd dervgfdfra dwnqqfgelk ttlgvvgtyy dtkatkraem
      781 yedeyqsreg npldgiwgle sdglfasaee ianspsqsyg qvapgdikyi dqngdgvidn
      841 qdevylgkag wfgppltlgv nftaewkdft ffalgigrfg ahgmknssyf wmdgedkysi
      901 vardrwtpet setatyprlt ttnsnnnfrn sdfwlystdr fdlakvqisy nfpkelfaqs
      961 fvqelgvyvn ganlltvspe reilelnvgs apqnrfynlg vkaif
//
LOCUS       WP_093304123            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter agarivorans].
ACCESSION   WP_093304123
VERSION     WP_093304123.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter agarivorans
  ORGANISM  Salegentibacter agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Salegentibacter agarivorans"
                     /db_xref="taxon:345907"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111001
     Region          1..>60
                     /region_name="PbpC"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein PbpC [Cell wall/membrane/envelope biogenesis];
                     COG4953"
                     /db_xref="CDD:443980"
     Region          40..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnysrlkw valiilggil mflsmvataa ttpppflqqq evsgivkdqn glpipgvtia
       61 lkntnrgtvt nldgeynita pangvlvfsf igyttveiei dgrkeiniql eediaalgev
      121 qinagyyntt drertgsisr vtsedieqqp vvsplealqg rmagveveqp ngvrgaassi
      181 rirgrnslrl ggdqplfiid gvpinansin sispftqnsg mdplstlnls niesievlkd
      241 adataiygsr gangvvlist krnkggdtqm eaklytgfsk vsnrmdlmnt aeylevrrta
      301 fendgattne yngrdllrwd qnqetdwqee llggtspitd lnlavsggne qtsfrlggsy
      361 rkegsvfpgt feynkvtanl slhhrskdnk faldlsanyg vdnnelffgs dfvrmavtlp
      421 pnapelyned gtlnwaensw inplnglfkp qnietnslls nlslkynfgk glefktnfgy
      481 snlqsgevtk nlinafnpvt wgyislfsyh tdtrrnswii epqisynkqf gdfninaitg
      541 ltfqenqnnf ltmdgtgygd dslvgnlsaa devratsdqe inyryaaifg rlgldwkdky
      601 ylnitgrkdg ssrfgpnkri anfgavgaaw ifseeafiqr nlpilsfgkl rgsygttgsd
      661 qipdygfmdt yeatdgpggl yptklynpnf sweinkklea alqlgllddr inleinwyrn
      721 rssnqltgyp lpaitgfssv qanlpatien sgweialntt niqneefswr tslnftlpkn
      781 klvefdnldl tpyrqtyrvg eplsialvyr yeginpetgr yevqdvnddg rldfsdrtgt
      841 afvgrkyygg vqntiriknf nlgflfeyin qnrrsylsei anspgtygnn stqildawtq
      901 pgdqtniqql ststsssaaf snamlsdemi tdasflrlkt lslsyqfses fveriglkel
      961 dlyihgqnlf tltdylgldp qggmavppmr titsglrltl
//
LOCUS       WP_093304250            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter agarivorans].
ACCESSION   WP_093304250
VERSION     WP_093304250.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter agarivorans
  ORGANISM  Salegentibacter agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Salegentibacter agarivorans"
                     /db_xref="taxon:345907"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117043
     Region          25..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfssilt lllvlavqit faqertitgt vvdedglplp gvtvlikgtn tgtqtdfdgn
       61 ysipatqgdv lvysfvgmet aeytvanndt idvtlstdsa qldevvvtal giqrekkslg
      121 yatqevqgae vsdvptqnfm nslsgkvagl sikssgtmgg stnivirgna sltgnnqalf
      181 vidgtpisnd tpntadqqag rggydygnaa sdinpndies invlkgaaat alygaraang
      241 aiiietkkgs kkqgigisin stfmttsvdd ntlpvyqdqy gagygpfydt pffntygnld
      301 lpdgfdpnip ftpftedasf gapfdgqlih qwnsiypqls tyqqatpwqa aqntpndiwe
      361 rgytainsva ldggsetstf rlgvtnlnnq gnlpnsrikr ntikfsgthe ftdkfsagan
      421 itytktdgkg rygtgydsen pmqsfrqwnq anvdvyaqrd ayletgqnit wnpnsplnrt
      481 piysdnpywt ryenfqtdtr nryfgnfnln yeindvfsvv grfsfdtfde lqeerrnvgs
      541 vgvsgysryn graaeynydl ilnfntdiid dlnldgnlgw nlrrndnssi rastngglna
      601 pdffalsnsv dpinppneyd atrmidgiya raslgyldty yvegtirrdr sstlpadnnt
      661 fyypsistsv llsnvveadw lsfakirany aevgndaapy svlntyvlst pfagagvagn
      721 qatlnnanlk pertksyevg leanfldrri gfdlsyynsq tedqitpvpv smasgftsvf
      781 fnagtvenkg feaslrlnpi rtedfnwnmn inwarnrsev lnlaqgidnl qlaglqggvs
      841 inatpgepyg tirgtdyiyd dsgnkvvgsn gyylttpnsn eiignilpew tggvqntfqy
      901 knlslgflid vqkggdifsl dtwygqatgv ydqsvgtndl gnpmrntlan gggivlpgvn
      961 engepnstra dfstyanpyg yardanaghv ydasfvklre anltyafgee midrlpftra
     1021 svsligrnlw iihknipysd pesglsagnv qgyqsgaypt freigaslkl nf
//
LOCUS       WP_093304279            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter agarivorans].
ACCESSION   WP_093304279
VERSION     WP_093304279.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter agarivorans
  ORGANISM  Salegentibacter agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Salegentibacter agarivorans"
                     /db_xref="taxon:345907"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113440
     Region          26..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkltimal laffqitgvl aqqtevtgtv tvasdgmplp gvnvlvkgtn dgtvtdmdgn
       61 yaievaadav lvfsslgfen qeqaiegrsv invamiedme gldevvvtsl gierekkalg
      121 yavqeiqged itktnqpniv salqgqtagv qitnsggapg qsariiirgv nsldpnadnq
      181 plfvidgvpv dnsttesgst prglsnraad inpndiesmn vlkgaaatal ygvraangav
      241 iittkkgkag dvrinvnssi gfeevnqype iqdvygqgfg gvydpnsfwp nwgpsideir
      301 eidpdaqind iwrdamrtgi qidnsfnisg gnekanfyas lnnldqegii pfsdwgrtsa
      361 rlngelkfsd qfkvagnmsy tisggnrvph drfmermvyn tpmqdindyi nedgtmksig
      421 tntnpiydar fstfedevnr iignlnftys pfewmdvnyl igtdfytdsr teitpgplgi
      481 egevplssqg fitetridsr dinsnlfitl kkqwddkwnt tlrvgndvfe rdyervdatg
      541 enfvipqfyd lsyasqisns qdkrkkrlvg lygdlmvdyd dmlflnitar ndwtstlpqg
      601 nnsffypsvn lgfafteafe mpevlsygkl rasyaevgkd tdpyrigqty tspgifplgg
      661 evgftrfsqf gdlglkpert tsielgtdlr ffgnrlgidf twyksnskdq iipvpvsess
      721 gfstfitnag eienqgvefi itgnpirted ftwnvtlnaa ynqnevvsir egieqiqvgs
      781 qygyagstvt mqliegeayg nifgssyery gadannlfln edlpkvigen gfpvrngnql
      841 ilgnttpkwi gglkndftyk nfdlsflidf rtgleqysqy dnffsafgia eytldrnetr
      901 vfegvladgt pntqevwlgq gegpdgrdyg agyyrnnyrt vsenfvhdas fiklrnislg
      961 ynfgdnvlda isfletarvs vaanniilyt pwdgfdpesf sagaggnatg ftglgypgvq
     1021 slfftlnlgl
//
LOCUS       WP_093316719            1163 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093316719
VERSION     WP_093316719.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1163
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129367
     Region          113..1162
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mndsfkrrwr dsrrirqmfd yvtllfrgsl iqnflvyfsv flartlspal slpkpclspt
       61 lalgkkrrli gpffgflisf hmilfcvcla harqqglgtp vatgvafqss yavtgkvmsv
      121 adrkplegat isvqgkqtkv ltnadgafri vtsdtsgvll vsfvgyqtae infnrreagp
      181 ftihlesngt qldevqvstg yqtlpkerat gsfaqpvkel ydgriatdvi tklegitpgl
      241 tfnrnttlan sgqldinirg rstihaddqp livvdnfpys gdinnlnpnd ienitilkda
      301 aaasiwgvra gngvivittk rgsfsqrlkv nananvtvge kpnlfynpyf lgssayidie
      361 emlfnlgafd gdidnkityp ilspviemla kkrvsevgne dverqiaylg nqdirtdvqr
      421 yllrpsvrqq ysfslnggge ktthlfsagy dnnssslian sdkritlssq nnfrlsknlt
      481 fdvglnyaqq mrqmdgtyny vtatdfpyqk lmdesgnlls vlrgssrsfi dqapsigfld
      541 wsytplhdlg mgkdrstgtd irvltglkys llkglsvdvk yqyqnyrfqk rnfqsedtyy
      601 trniinryat leddmvrkfn vplggilnts fdnqiahnvr gqlnydlqln rhqlfvvagl
      661 efnevlneat naalygydde latfkpvdni ttfplnpggn ssamipssvg iaasaarirs
      721 iygnaaytyn drytfsisar adgsnyfgvn anqktvplws vggkwdldke tfyrssflpy
      781 lklrltygsn gnldrsitgv ttfrylsnav wtghryadis nygnpdlgwe ktaitnlgid
      841 fslknhilsg sieyfikkgt dllgdrlfpn svglrslrgn yaasqgsgfd ivltsknltg
      901 rfvwssqlll sratdrvtry dvqlpatssm vasgttltyv igkpvysifs ykwagldpds
      961 gdpqgydqag giskdyasli npnlsdlvyh gsarptvfgg isntfsysrf slfvniaykf
     1021 gyyfrrptvs ysispttvsi salanadfln rwqnpgdeln tdvpsfsypf endrnsfysr
     1081 sevtvekgdh irlqdinlsy alnpafaswm amqecrffvy innigllwka nkvdldpdav
     1141 pasadytrvp tprsiafgik ltl
//
LOCUS       WP_093306498            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter agarivorans].
ACCESSION   WP_093306498
VERSION     WP_093306498.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter agarivorans
  ORGANISM  Salegentibacter agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Salegentibacter agarivorans"
                     /db_xref="taxon:345907"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113440
     Region          25..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkknliili lsvlawnsai aqeevtgvvr daqgplpgan vsikgtdtgs mtdmegnysi
       61 tvedenaili fsfigydake ikvngrsqid vtldssqesl qevvvtaqgi kksqkalgya
      121 iskvgseeie rrpeadlart lqgkvagvti tpangqtgsn spirirgnis ltgsnaplii
      181 vnnvpfngll rdidpnnieq inilkgfnas vlygsegrng viliqtksgs asvgeeqtsi
      241 systtvytni vsqlpefqnn ysnggegefs gtflsnwgpa fselgevphp ysplgdifpe
      301 yeglsipiea kpnnvknifr sgigtthsln fssskekvaf nlsagytdek giianndlkr
      361 fnlsiggnaq iteklnisat lnysnrkvnl vndedifnlv fylprwidlt elpyedpatg
      421 esvyyrndtn plwilnnsgn rievprtfgt fstdyqlndn inltyrvgld henpsqfdys
      481 nkggfdnnsy kygyldlssg ketvvdqtfl asfnydltea lnmeaqigan skltqyeise
      541 sfsdnqivyd ffrpsnfdat qaayttreen lagvfgqfqf afknylyatl sgrndwgstv
      601 esdyqslfyp gaslsfipts afdfggpiin ylklrgayat ssgypgayrt rgtlvtdprr
      661 faasdgsfpi tnrfstrfan pnlkpelhke feigietnlf rnrvtleasl ykrisedqiv
      721 gaplagssgf drqfinlgri dnegvevdlg idifetdyfs wnfrniftad eslvvkttpt
      781 gadinitedr favegrpfgv ikgdyalrdd egnllisgng sgtrvgevis ssnigladrv
      841 igdpnpdwrl tninriafkd fnfsvqweyr hggeihssav rnmlqrgvtr dtedrdhafv
      901 ipgyladddt gellldpngd kirntiqmns grlgysnyyt sndlatwdts ilrlreisvg
      961 yslrqskfkn ipferiditl sgrnlwyrap nfpkyvnydp endglegdst ipstrrialg
     1021 vsvnf
//
LOCUS       WP_093317416            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093317416
VERSION     WP_093317416.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119829
     Region          24..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrtitllv ssfflstvly aqtvlrgtvv dkekkpipgv sitlengkgt stgpngefsi
       61 tydgpsllnv saigyekqql piskqttlqi vlsdnaesld evvvtalgis rerkslgyal
      121 qevksedltk agqlsvtgsl sgkvagvqvn qfggtvgass risirgnssl ksdqqplivv
      181 dgvpingdsq rsgdntykgv dygsglndin pedietitvl kggsaalygm ragngvilit
      241 tksgknanng vsiaydgnft idraytypkl qnlygqghdg deyhyglded glsyqdyaaq
      301 ksfryvdgtg ndensvndgf deswgprldm glklpqfdsp vidgvrqatd wishpnnvre
      361 flrtgysmnh nvsllsrtdk sstrvsmsyr dqqgtvpntd qrryglqlnn ntnisdkvsy
      421 dvmgnysrte sdnllnqgyd gnnpingfiw sgrqvdmasl kanwdqrdek gdytyynwnq
      481 syhinpffnv ykntnsfqrd rffgktsmyy qpfeflkfeg rmgfdyygsk aleknyynts
      541 yregmfrdik qdntelnldf itsfnkqlkd fsvfamagvn yrdakwsrtm qgadaltvlg
      601 vytiankkgd aitemdhthv rsnsvyasgs lgwrdqlyld aslrndwsst vkddffypsi
      661 slswlpttsf pslsgtalsf wklraswaei gagtdayqnq lyyyaqtnsf ggvaqmyksm
      721 typnrnltpe ntatwevgte lgflnnrlha dftyyykktt dqilsvstsn vvgfnrmvln
      781 ageiqnkgve imvygdiikk etglnwrstv nfaknqskvi elypqlgvnd yqigwtwgia
      841 tmaragepwg mlvgpgydrv edgpmagaik vtsdglvrsk asqnlgninp dfllswrndf
      901 tvkdfsfgfm ldmrkggdiw sqtmshsyva gtaeitaeng vreraivagv dvmpeerfam
      961 qaadgswven tiatdaqtwy esggidqmyv fdgsflklre asitytvpqk ylqrfkgikr
     1021 anisligsnl allwvhksnt mrldpetggv ssdsrgvgfe qasvptsrsf glklgvtf
//
LOCUS       WP_093317624            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093317624
VERSION     WP_093317624.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112261
     Region          24..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrklllffm gmlfvsahvl aqqktiagkv tdsagqpipg vtvsvkgtsv rtqtnsegly
       61 niqtsqgetl lftyigsdpl eitvgsnsii naslqpsssn ldevvvtamg ikrevrslgy
      121 saqdiksdel lknkdpnivn slngkiagvn vtnsggapga sasivlrggt slerdnqplf
      181 vidgmpmdns tgqgdnsafd gsvnisttns nramdinped iesisvlkgp aaaalyglra
      241 aagaiiittk kgkegaatas vtsrfmsnwv nrlpdqqsly kqgsyyngnf tdqtalswgd
      301 kfetgetmyd nlgdffetah aydnsfnisg gtaknnffls asnlnqsgvv pttnfkrstv
      361 rfngeqkvgv ftfgvnasya vsksqktltg sglwgssgsg ymesilswpr nnnmknwlsa
      421 dgsnnlllpn valedntdnp ywiinknpqs drnnrfiata ytnvkitdwf datyrlgidn
      481 yttnfsslis pgssvklawq kgmlsetdra ynyinsnlml nfhktfndvw danvvlgttt
      541 edtkltsnsr raeqfeiptf idinnasnen kyysqsinrk rllgvygdfr lsyknmvylg
      601 ftgrndwsst lplqnrsffy paisgsfvft ellpkndvls fgkvrasyaq vgkdaaayqt
      661 atylfgpelt igggyrnyws rgndllkpet ttsiefgtdl rflkdrigld ftyyknksvd
      721 qiltprvsna tgyilssvnt gvlenrgiei tlnttpikrd nfqwdatinf shnngivkel
      781 pgslpilyvt dvqvgngkaa sfgngdfmgi sgskwqtdan gnilldwntg ypltstlttt
      841 yignrepdfi ggfnnnftfk nwnfsflfdf rkggdiynat eylmtvngis kltenrgntv
      901 tftgqslnpe tgqyeavsre viasekyyrd iyannvphfi envnwlrlrs islayslpqs
      961 llnkaswlkg atitatgtnl llftnysgmd petsaagagv vgsgsvgidy agvpatagfa
     1021 lglnvrf
//
LOCUS       WP_093317629            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093317629
VERSION     WP_093317629.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111546
     Region          25..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maksiyllli gclfccqiaq aqqttisgrv tdrntqealv gvsvkiknsn lgtstdvdgk
       61 ftlslnesvk qqeiifsytg yktetknial atgnnvlnce lsadlvglde vivtgtsagt
      121 trkqlgsyis sikgddltkg rsgnvlsslq gktagaqisq nsgdpaggis vrlrgissvn
      181 ssseplyivd giivnnnttr vtntqpgydg gnfvgsigqn rlvdinpadi erievlngaa
      241 aaaiygsran agvvqiftkr gslgapvvsf stnymnsnlr kkvavnqspv kfggsvdlet
      301 qdvlntaltt tspvnrydyq dyifrnasgt dnnvsvaggk ddtkyyvsas yfnnqgivrn
      361 tnfrrfslrt nidqkladwi sftaglnytn sgadekpdgn sfysplnsin iianyhdift
      421 rdadgnlksv gergrinpvs viedikqrqe vnrvlgnlgl kltpienlsl dftvgvdntg
      481 qtgttyippy tynanpdfwg gganlaptln gytstasnsa flinnefnat ftadisdlis
      541 stsqlgfsyq yekskynmln grglapfiet vnaasailpg mdarteysvs gayfqqnfky
      601 rdqlfltgai rvdessvfgk dnrrqvylkg sgsyvlssad fwknaamskw wdlfkvraay
      661 gqsgnltgig aydrynayss qtflsrvslf ssatlanenv kperqaelel gtdlsffsnr
      721 lglsfnwynk kvtdllisrv eaptvgfssf ldnvgslqnr gielvlngap vkntnfswnt
      781 sviysrnrnk aldvgglrlf ttnpgapvai idgqpigvfy gtffarnsdg slltnaqgip
      841 miergtqngi eitpqrdeng mptgtplrkv igdpnpdytl tfvndftykk lslhlqfdav
      901 rgvdvwnadw rtrqgvgngl maqqeqmgel prgyiagaya veewrvdngs yvklrevsls
      961 ynfgkvkffk dltinasgrn llsfdkykgy dpevnaggqs tilrgidfga ipiprtftlg
     1021 iqvkl
//
LOCUS       WP_093318898             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shimia
            haliotis].
ACCESSION   WP_093318898
VERSION     WP_093318898.1
KEYWORDS    RefSeq.
SOURCE      Shimia haliotis
  ORGANISM  Shimia haliotis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Shimia haliotis"
                     /db_xref="taxon:1280847"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55380
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf dgenrvamtp dsakqlmklg yecaieagag anagftdasy edagvevikt
       61 aaglwkacdi vakvrqpdat elkrltsdkt lisffnpagn eegmeaakak ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvqseefr
      241 naqlakfrel apevdivitt alipnreape lwtedmvamm kpgsvivdla aekggncklt
      301 vmdekivten gvtivgytdf psrmaaqast lyatnirhmm tdltpekdgq vnhdmeddvi
      361 rgatvtfegd itfpppppkv qaiaakpkev vpeltpeekr aaevaafkaq tkqqvmllgg
      421 ggalilllgl vapasfmqhf ivfvlacfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaaasvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_093319132            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093319132
VERSION     WP_093319132.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122728
     Region          83..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myltkqkksa gdpiavksgi laksdhhvfp kngmpwevik karypifltv lacsqihsla
       61 aepklnverp vyssvmlqdr imgkvvdgqn aplsgvsiav kgttlrtqtd engnfslggv
      121 pkngiivasy lgyatkeiat sgqtlltiql asrenaldev vvvaygsink alatgssgki
      181 saeliekrpi tnalssiags apgvqsttag gapgaspsir irgfgslsae ngalivldga
      241 afegdmagin pddiesisvl kdaattamyg srgangvvli ttkkgkidsk nlnvkaskgw
      301 isrglpeydr vtatqyyplm wetyrnslay gsariprdva gsiaagltte yngrrysgin
      361 sllgynpfnv pdnqivnang elnpnaqlly pddlnweeqs tqggkqrqny nlsysggsss
      421 sdyygsfgyt deegylvkss lkrytarlsv ntqpldffkt glnvsgnysk aqydnvgdgg
      481 tgyinpfyis rfigpiypvh lhdetgalvl dangqprydf gdnrpfapgr htiyenlmda
      541 qnqvrgqvna raygtvfivp glkattnisf dlldthnrty dnptlgdgap sgrayqyfyr
      601 ttsytfnqli eytksfgkhn lnvlagheny sykynnfngs rsgliaqgit eldnfatvlg
      661 lqsyehnati esylsrvnyd ydgkyifsgs lrrdgnskfa pgvrwanfws lsaawnidre
      721 dffdvdwvdq lkfrtsygtv gndrggdafg yypyqalyll grnnqseagf tqnslpneel
      781 twetaknfda gidfsffkgr lggsleffnr etsglifavp qpmsnggnyl gssegyfkin
      841 snignlynrg velqltgqiv ntgdfkysat lnwttfknei tkmpdnqpli qdgtkaysvg
      901 hsvydfymrr fygvdpdnge alyytnqqtn ntriigqdtv tnqiaeanyt ytgesaipdf
      961 hgamshnfsc knfslfvqft yqvggkvydn ayrslmhggt ygtamhvdal krwqnpgdit
     1021 dvprldngqv anyagisdrf ltdasyfqln tvslsysipk kwlnhlkaqn aniycsaenl
     1081 alwtkrkgmn tvgafngtvd ntynlnrivs vgvnltf
//
LOCUS       WP_093319616            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093319616
VERSION     WP_093319616.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119161
     Region          22..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkfniflf fllqvcavwg qqtikglvtd tenkpipdvt iyslkekkli ktnadgsfsl
       61 qlsdtdtlqi ssigykslri pvrkiegnlf kleklqmele avtvstgyyq iskerstgsf
      121 ayidsallnr svssdiisrl egvtngvnfd rrgsfyaddk psiqirglst ingntqpliv
      181 ldnfpydgdi ysinpndias vsilkdaaaa siwgaraang vivittkkgt rdrpasismn
      241 tnvsfsekpn lfynpnflss sgfiemeqal fergffnaae nssaqmpltp avelmikard
      301 gelsdellke slsqlglldv rkdatkhfyr egfmqqyaln ikgggkqfdy ylsggydrdi
      361 adikgndndr itlnaqnnft pianltvstg lyfiksstna ngmrlndirp ggrhiypyaq
      421 fadtqgnpla iidryrlgfv enaeqeglln wdyrplqela lnnqkrgsde ilintavryd
      481 ikpflnldlk yqyqringda ynlrsadsyy vrdlvnrftq adgtsvfpeg avlnqsyskq
      541 iahvgraqln fnkqlglqhe ltalagmemr qvnvtgqsfq llgydpevlt yqnmfdytrl
      601 ypqrpngtsr lpapssslqd lldryvsyya nasysyrsty altgsvrwda snlfgvkvnq
      661 rgvplwslgg swtlnqeplf qadwisllkl rltygfngnv dksstayvta aylndnltgl
      721 rraliqspgn lqlrwekvgv wnagldyalw nnrvrgsvef ynkratdllg dipldptvgf
      781 tgvyrvnyad mqtrgldlev ntsniqgtfs wqstlllslv kdkvinynae ditpvdlfta
      841 ssiprpmegl plyrvysypw lgldaetgdp lvmlngnisk dynayiqqvg mddlvyhgpa
      901 mptlfgslrn tfgwkgfsls atltwkagyy frrnsisyda lfnqsighld fygrwqrpgd
      961 elvtdvpslp etadvnrdlv ytrsevliek gdhirlqdln lsytlanpkk lglpisglsf
     1021 ycyarnlgil wranknrldp dfqtapyplt ktfslgvnit l
//
LOCUS       WP_093321651            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093321651
VERSION     WP_093321651.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107980
     Region          29..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkknfissl lcfilvlstl cvyaqnsnit gkvldeknep lpgasiqike lkksvgtntd
       61 gtfsvaglan grftlvasyi gyvqqekvvt vsgastsvvf tmqpdaqgld evvvvgygtq
      121 rksdltgava svgakdfnkg plvaadqliq gkvsgvqmin nsgqpggatt vrirgnsavt
      181 gsgqplyvvd gvaldgrsar pnqsggigts pagnplsfin padiasmeil kdasataiyg
      241 sraaygvvli ttkrgqsgal kvdvnssagi snimrkidil dgnqyrdaln kygfttgdfg
      301 snvdavdail rtaynqnhsl slsgggednk frasfgyqdq qgivrktgfk rysgafngnf
      361 kmleskklgl dvslmanqnn eniapivtda gatgslltha lawnptrplr nedgslaier
      421 gniinplams eayndrsnvs tilaslspyy kfndwleyrm llsvnyskge rrsstrsfin
      481 ipsiqaepan nfpggyasva nnelitkqlt htlsfnkeia sdlnlnavig yeymdfinrg
      541 tdmnargfgd ipvdytdvmq atapgnrnln sfndpttqlq syfgratfnf kdrylltatv
      601 ridgstrfge nnrygtfpsf agawnmkned fltdvtwlnq lklragwgkt gnqefpsgss
      661 qrrysigfgg ggqtrpinnn enldlrwqsd eqinvgadfg lfggrlsgsv dyfhkkttdl
      721 lfpqtpqypa spdasitwin lqgevinkgi elnlngvive ndnfrwdlga natfvnnkvr
      781 nlgeneiirt gslsgqglsd vtveviqndy plfafvtrey lgldnegfsq ytddgfvfyr
      841 vgnpnpkvll gistavdykk fsfsanlnga lgqdiynnta navlpisnlg srniaaelmn
      901 ssilespanp iaassryien gsylklanat lsyrvgdigs siknlgifvn gqnlfvitky
      961 kgfdpevnvs kavnnvpsag idnvtypsar tfnlgvnfsl
//
LOCUS       WP_093322934            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093322934
VERSION     WP_093322934.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117139
     Region          44..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmikgnikqr nrlsigdrts iflkvlilvg tmsfnpaflq gqekpvrgqv rdtenvpleg
       61 vtvqvkgtsi atatnangnf sinapsgavl afslighqtr eitlqnqavl nvqlspesrs
      121 mdevvvtalg ikkeskklgy saetvkrqdl lqnrtvnvme slegkvagld isppaagags
      181 stkirlrgqs afagaanspl ivinglpmdq garssngwep aydlgdnmqq inpddiesmt
      241 vlkgataaai ygsraangai iittkngqrd qgigieytsn ftvnsvldft dfqqefgqgq
      301 ggqrptdvgs aistgmlgwg srmdgepiin fdgimrpyss npnrikefyr dgavftntva
      361 lsggsdkgnf rasfsnadak gitpapdnry tkrifnlgln qdltkrlhfs fnvnytkenn
      421 enppqvgaqg pgapnfltrm stsiplaafr esavaengte rqtsgfqgtl lnpyfakgre
      481 filndrdrfl gtatlrydmt dwlyvqgryn ydysvsklef ntptgrgtst afnnngqgpg
      541 fngmyhieqa kgteintdfl igankefgdf svdlsvggni fkrdvgtfid evedftvrdl
      601 ysiqnginkt innytifrdq tnslyafaev gykgmlyvnl tgrkdwfsvl npdansefyp
      661 svsgsfifse lmkdqswlsy gklrgswaqv gsangippfs nhlfydilpn qlhgrtlgti
      721 lgtrspnall kpfsveerel gvelrffdsr vnldiaayek vttdqilpvq isnasgytdt
      781 qqnvgslqnr gmefmlevip mkrdnfrwts afnaslnttk vlsiapgter fvaqrfegne
      841 figslvyevg lplnqlsant ylrnengeil lndngrllqg pvvnfgsalp kwvggwtntf
      901 iyknlslsmh idfkaggkvl sssalnglrq ghtkaslvgr regengvvfd gvyqngetnt
      961 iavnpqdfyt dyrnlqiadp fifksdfikl rnialtynls dyvknkfgfi kgltltascr
     1021 nvailykdlp dydpeafass gdnrigyeqa tvpttrnyaf nlniif
//
LOCUS       WP_093320723            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093320723
VERSION     WP_093320723.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119868
     Region          25..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkyilifmy lccvltasaq ktlalkgfvi gqsnepiagv tvlikglkqq aqtdnngyfs
       61 wslpisdtae lvvskvgyks eivlitvntv fplsikltdh ftvleevvvs tgytsvpkdr
      121 atgsfsvidk elfnrqistd vitrldglap gilfdkrgge rqnfqirgis tlysnarpli
      181 ildnfpyegd inninpndie svtflkdaaa asiwgaragn gvlvittkka kfnapmqlnv
      241 tsnltiqdks dlfymplvss sdyidierfl feqgaydail sntadrpvit pvvellddvr
      301 agrleegrad ilinsyrdkd irkdyeryly rpaflqqhal qlsggndhhn yrlsfgydkn
      361 ltelkenend rltiraqnkf kplkqleiel gfvytasrqq dnnpgsvrmg ltdliypyak
      421 laddngtalp leqeyrkryl dtagsgklld wqyfplneiy eadnrirtnd lllnanvtyr
      481 inddlkvaal yqyenqgvln rgfkseemff trnlinkftt vdgnnikrnv plggildlnr
      541 qqlyshalrl qldynktwkd vhqltalggt evrdalsdse vsrtygyndq lmtggvvdll
      601 trfpvfggle wdqqipnlqs fgayrdrfls lyanasysfk skyifsgsar rdasnlfgts
      661 tnnkwkplws agfkyrlaee affpsqlvpk fdlsitygks gnvnngital ttiryqssps
      721 planlpfafv qgapnqelrw envsqlntei nfalknnrid gsvayyrkka tdlisgvaad
      781 pttgfssltm naasllttgl dvqvntlnmt nksfswatnw ifsrnkdkvl enyvsnlgss
      841 nyvtgsripp gnsyplnslf syawagldaa ngdpqgyldg qlskdyqail qspnidnlvf
      901 hgtqlprifg airnnvrwgn fslsvnvtyr fdyyfrrpti syssllssna smphadyykr
      961 wqqagdevht svpslaypas anrdrfyins evlvekgdhi rfqdanfsyr lpaatlrrtp
     1021 fksltitayv qnlgilwran regidpdyrq gplpksyalg ininl
//
LOCUS       WP_093321638             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093321638
VERSION     WP_093321638.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109159
     Region          29..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknymksvv lslllimiat lafsqtgsiq givydeknqt lpaasvlike lnesvgtddk
       61 grfsmssian gtytlvvsyi gyetkeqtva vsngtasavi ylqpsaegld evvvigygtq
      121 kkgeltgsvt tvgskdfqkg vitspdqlis gkaagvqitp vggrpgagst iriragasln
      181 asndplivid gvplssfkdg sgnnilpgts nplslinpnd ietftvlkda nataiygsra
      241 sngvilittk kgatgkpiit fstqnsvatv grtidvlspq qfrdyvtang sdsliaklgd
      301 antdwqkeif rtafatdnnl siggsykslp yrvafgylnq qgilkrddmn rtsaaislnp
      361 kffdnhlkvd lnlkgslqka nfgnqdaiya alqfdptkpv nqenefggyy ewmqgaiphp
      421 laprnpvgli dlkkdhgkvn rsfgnlqldy sfhflpelha nlnlgydisr gqggtevpaf
      481 aamnfttggr vtqfltdinn kvgefflnyn ktfddiksnv ditagygyyd yktttnnypt
      541 lradrsvltt ppfafdipqn rlisyygrii ytlddkyils gtartdgssr fspdnrwgff
      601 psagftwrmk keeflaeaea lsslnlrlsy gvtgqqdgia nysylanyyq svneaqyqfg
      661 nqfyptyspi aydqdirwes tttynggidy gfldgrings idvyykktkd llsvipipig
      721 tnfsnllltn vgnmenrgve fnvnlipikq edfswdvnfn ftynhnevtn ltavdnpnyf
      781 tqvgyieggt gqnvqahvvg yspftyrlyk qvydengkpl egvyadtngd givndldrql
      841 nksplpkyim gfstslhykk wtlstvlran ignyvydnvs snmanrnnil npvgivnnap
      901 vdflnsnftv nnalsdyyly nasflrmdnl gltynvgkls pnssaklsis gnvqnvftit
      961 nyhgidpeiq tgidnrfypr prtfvlglnv gf
//
LOCUS       WP_093323215            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093323215
VERSION     WP_093323215.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113561
     Region          26..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskkiiwtiw lwpllclyah aqttalrgav vaastgeglp gvsvqvigsn taaqtdaagk
       61 fslnvpsgsq lrfsyigyte qvivlqsnqs ylevrldeqe naldevvvta lniskekksl
      121 gysiqevkgt dlseakesnl vnslagkvag vqvtnsqgnm gssriiirge tsiagnnqpl
      181 fvidgtpvdn sqlgtsgnrd yanaisdins ediesmsvlk gpnaaalygs raaagvilit
      241 tksgskrkgl gisinsnntf ervavlpdyq nvfgqgadgk fsyvdgkggg indgvdeswg
      301 pkmdgrlipq fysngeavpf lphpdnvrsf fgtgrtlnng iaitdatdki dyrfsynnsn
      361 qtgivpnssi eknnfnlnts ykitpdltlt ananyvrtns gnlpgvggfr sngymlqftw
      421 fgrqvdvnrl knyrdadgnl vnwnnsyysn pyfiaeeniv qqqrdrifgn vglnykindf
      481 ltanfrsgnd yytdrrkiri aygtngtpfg syeedaytvn ennteftlny nqplsadfrl
      541 dilaggnirs qsrqrndqka prlavpdvyt lansrdalvs lgeysslkty slfssaqigf
      601 knyaflnlta rndwsstlpv dnlsyfypsv nasivlseaf alqsdvlsyw klrggwskvg
      661 kdtdpynlid syifsapysd spqltvndik knpdlkpett tsaeigtela lfdnrlrldv
      721 siydinsinq ilsvdvspst gykkqlvnag kinnkgievq lgltplrknd fqwdvnvnfs
      781 snksrvveld eagdlqsyti gssgsaqvla svgqpygmly gtaflrdgdg rivvdangip
      841 ttdpvnhyfg kftpdwlggi tnsfrykdfd lsflidikhg gkiysgtnat gtgtgvlast
      901 lpgrdaehgg lsytvgdvty ddgiivdgvn adgsenakiv saqqyykary rtnepnvfda
      961 syvklrevkl gyhlpnrwis kiglqsasfa lvarnlwiih knapnidpet afntgnaqgl
     1021 eslqlpttrs igfnlnvkf
//
LOCUS       WP_093324021            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093324021
VERSION     WP_093324021.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122513
     Region          26..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkelyskafa vvllciitfs sfaqttvsgi vsdaqgvlpg vtvrvkgttr asstdangrf
       61 siqtsagetl sfsmigyvvk dvpvgnqsil kvtletdena lqevvvtslg ikkeakslgy
      121 atstvsakel tktgspnfag alygkapgvr isaapggats gininirgtn sitgnsqplv
      181 iidgvpmrqt tfnnsdywgd qrargngled lnpediesis vlkgasaaal ygseamngvv
      241 lvttksgkgg kgysidfnat ytndriaylp rfqdvrgpgy ttayqndnqa edlfyyysdd
      301 laingvtrgl lpatvnfgpk fdgqdviswd gqvrpyvaqn ayskffnnpn ntifnlalgh
      361 tgensntrfs ltrqdnemts ldsynkknia nlntsfklwd klttdvvvny vnqhthnrpf
      421 ltdrminnft gmistfdnpe wylnkyktsl gykyvveapn vqsltpeenl ryngyktdvl
      481 dyiwntkake ydeysnrlig svtntyqvts dlslrarfsa ditslktedk qptekpivyd
      541 attgyfglgs qnaniyyvdl latyskqinp diklgvmggy tatksqdtyv qretagglsv
      601 rdwfdinasn ntiggstryn yrrnmlrdal fgtlnfnlke ywfvegtlrr eristmhpdn
      661 nvlyypsvns slvlseafdl peifsyaklr gswgivgnyp diyksalsyt qqtlgvqrqg
      721 gaaviynnvp tvdfgnenik perkkevefg letrlldsrl gfdityyngl iqdqilnytl
      781 pismgassif anvgalrnkg wefaitgapi qsenfrwnav lnfsmnkniv eelpggvsel
      841 lhrdydgqaa qlvskvgqpm gdimvhpiat dengnkivqd nglyqldadt wikagnampk
      901 avgglintft yknftldali dfrwgghamp tginwmtsrg lteeslnymd aehgglsyym
      961 dggrgiafdg avgpngqtvy hdgmlmdgvl sdgtpnnnii sqavyynnty nwggpqysss
     1021 ryelyvqknn yikmrelslg yriptslaak lgaknvqisa fgrnlfflyr sikdldpeqm
     1081 tggsnwinqv snagtspatr tfglmlrasf
//
LOCUS       WP_093325014            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093325014
VERSION     WP_093325014.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112031
     Region          22..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkriiqltcf ffltaiaiaq erniggivts kddgeplpgi siriagttqg tttdvngkfs
       61 lrapitstlt isgigyieqk vlignrniin ialetnaqnl devvvtsfgi qrdrktlgyg
      121 vseikadqla rapttdvtns lagkvagvqv sgagggfags nvtirgfttf tgsnqplyvv
      181 dgipldnsgg nnsvntgvvn ssrisdinpq dianvsilkg aaatvlygsr aasgailitt
      241 kkgqkgtrnq lsfssntavg tvsrfpdfqn eyaqgsngny innvsgswgp qimgqtvtnw
      301 fgeeetlqay pnnvrdvlqn sissqndlsf sgandkfdyr vaygfatetg lvpnnklyrn
      361 nlsvnagmqm tekfkistsf sisnntsdrt qsgnqganpl wrgiyaprsy dlthlpfeda
      421 agnqlwyaae dhpywsiehv knhrevnrfy gnlnmkydil swlqadlkig adiftsrlkg
      481 fddkgirsng ntssagaggl reqsnavrni nsyftltgnk rlndnfnlma tvgneiivny
      541 sndleaiglg ivvpgfdnlk nfitynpsga itkqrgigvf advvldyksf lsinakarnd
      601 fpstlltgnr sifypalais fvpteafpsl ksgilnnaki ranigevgkg adpyaigsyy
      661 graaasdglg stavnfpfng lagytfnnst gnpnltpeft reyelgteln lfnnrlaida
      721 sfyrrdtrnl ifsvpvpass gftslvtnag klstkgiell vtgipiqheh fsweaslnft
      781 kfksivkela pgvnnisigg ftspnvrlva geeygqiwsn ayvrddqgrm iigsnglpqv
      841 tsavqkvgnp npkftmgltn tfrykdfsfs flidfkykgd qlsrtigdlr ingvaaetae
      901 yprfnadgtp ntpyvfegvl adgtpntigv taqqyyglqg kyvawegyvl datylklrea
      961 nftyvlpssl fdnikfikgl qvsiygrnlf iyapnyphld peqnllgvsn arglefgiqp
     1021 tsriiggslr vqf
//
LOCUS       WP_093325082            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093325082
VERSION     WP_093325082.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113863
     Region          85..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpkklhvgwl yqmlaifscs lamifdkayg eplyagppdl ailmqdsivq dstaldsaki
       61 dtvyevklpl plkkvgrpaq nldatvddla rfpavslqqy lkgqaaglyv qepngepgsv
      121 qsmlirgasm pllsarelyq nqplivldgv qligehpfay diqqydfnri gtatnlltni
      181 dmaniasvev lkdlpavaiy gprgangvil lktkqagnrr aisfnaytgl vqrptvatmn
      241 gdyensfrqq fydrytpagr yteddvyply lsdslnadyy gpsnwtdsyy rnaliyavna
      301 siaggtdran frfalgnlkn kgvadntgld rysasftlnm kpikwmtfsa mfngnrierq
      361 rnrnlrdrfa lmnyipdlsa plapnkesyd rylknfensf ddnnsniveg fagllfdfgp
      421 ltfstkfsvd ynegyrdlfy prtllennsf asnyygysqr iqfdnlltyk vplnglhdls
      481 leagqfvqwd tykynyayay rgvndfikln llesdpgkde yltplafpre lvykfldrtk
      541 hnllafygra nysfdekykv slllrgdass naqptnrwlf tpvlaaewni kedlmtqqdf
      601 fdvfnlraga grtgrinafd nfaqgpqyta evgftgnvtt pgyngfavlt rpyssgwigy
      661 dlpwaysdql nlgldlgflq nriklqldgy irqdknmmla ipayaeygyn yaqqsgmevh
      721 nsgldigiqa tiiptdrpfs wttrlnvnln knklnalpgg ldeivlgnrk levgkpidqy
      781 wlfqnegiyl addevplvng qpmkfngtal kagdpkwvdt nndqvissed ktlvgnmlpk
      841 vaggftnqff yqkwsltadl yfnlgrkiln qemanrfdfi nregtntmda vkeitfwekr
      901 gdyskyplyn pwstvipyra eqdlflenga flkmrtlsls ydmsewlnkr tavvkklrvy
      961 vsghnlftlt pytgqdpelv nytgydtgyg lpiprtytlg vqvdl
//
LOCUS       WP_093325836            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093325836
VERSION     WP_093325836.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117959
     Region          28..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrflwilcl wycsaclsia yaqtekvtvs givtdeqnqs lpgvtvfsgs plraigstta
       61 kgsysvtidr gavivfrylg ylerrithng rqrtidikmq vdnnqlqevq vvvrgyvqrs
      121 kelstgssft isgkeiqevp vanveqllqg rvpglniqnn tgapgfrgst qvrglstmtv
      181 tgsgsesflq ptsplyvidg vpldadkase fgfqqqgpgm splslipqed iesieilkda
      241 qatsmygsra aygviiittk rgnspvprvr yignafmktp pmlretlggn lerqfkiqqi
      301 lgnaigmkdi yaisqtpfls dslnayynns tnwqdifyrt tynqthnvai dggnqklnyk
      361 anigyfgekg viqntgfqrf nlntrmefrp serfafsgtv ygqigkqnkg ngvgllqqgv
      421 anngqastll pgpsffqsss gvasslrtnn dnstrnlrtn idanfmvieg lrlttnlsyd
      481 fssnledtft paaannqfar vyafngrdyq lynrnsinys ktfnekhnff inafseiykk
      541 gtqnsitrqd kspndqfqgp wgfdawasrg ggvltnfkda rqasfagsls ydfmrkyiid
      601 lsyrldgdsg sgidnpyskn paiglrwnfn kekwfensew lnlgalrlsw gknivpstnl
      661 eviygkynig gmynnvqgig idyriipnpt lkpvtteqfn lgvdlslfgn kidliydtyy
      721 kdvsnllfer ylpntsafdi llsndasivn yghevsltir plpasskfnw sftingaynr
      781 dvltglpaey ngqfiqwadp ndayrqhiak rigrnalsny lrindgvysh hgdvpvdpvt
      841 gkryqtngry feagdpilrd lngdfilddf dyaltgnsqp lftggiystl sygqwsvaiy
      901 tsftakrtvl nnalsdrlsl mrdpfaldan agpravvpln sidmwmqpgd iskypyaydy
      961 trynsilpfr pdqtlweedg tylkinsvil symftkrfaq nlglnnikiy lstenlhtfs
     1021 rysgpnpenv tnmgrdvsgg ypvprtynig vnvdf
//
LOCUS       WP_093326282            1162 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093326282
VERSION     WP_093326282.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1162)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1162)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1162)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1162
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1162
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129421
     Region          122..1161
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkltrwcfkq qtllilvlvi nvwavystas artpeqvldk riqlsfskvn artllkeier
       61 kaavdfafte dirlenmvln nvhyqnskls dilsdlfkke hivfdeqggt islrrvqqgl
      121 lvkgqvrdan tnaiitganv qvkggsqktv tdngghyqlq vlgaesvlvf symgyrshet
      181 kvggqlqini tltednnpln evvvtalgis reaksigfsq qkvdgqtiqe shetnllntl
      241 ngrvagvrit nssggigssa niqirgqnfv sgynynnspl fvvdgvpisn nneqstrayt
      301 grqdfnnpnf tagegevdyg naageldpnd iesmtvlkgp naaalygsra angvvlittk
      361 sgkgtkgvgv sfnsqasaet plklpdyqye ygqgrdgeys yvdgmgggln dnvmenwgpr
      421 lngqlipqyd spvdpntger matpfvaypn qlkdffqtgt tftnnlaiag sneklnfrfs
      481 ytntsqrgiv pntdlkrnai glntgyaitp klkvdvnmny vnsgsdnras ygaknddaim
      541 kiflfmprnv dvnslrdywa dgpqrtqqrs piwglnssrl nnpyfvayen lngnnrdrvy
      601 gnvkftynfl pnlslmvrsg rdfyndkrtm rhavssaqyv ngyyqeddvy fletnhdall
      661 syntkinddf svnaslggnl msqeskrlga ivdrlsipnv ynltnnaspi vagnirqqkk
      721 inslygtaqi gykdalfldl tgrndwssal pkqnrsyfyp saslsvvase lfgwrseals
      781 ylklrsslss vrrdlepyqt mpnfqitqgw ngetvaihnn nypnpdikpe kvssyefgfd
      841 srffdnrvgi dftyyrsttt dliipvtlnp sagydtklmn vgkmknqgie lmvdltpikt
      901 nqfswnvnvn fglnrnkvvs laenigisri rqierwasle mrtentkgdg sfgslygdyl
      961 iyqndnlthr nglpqeengd wgylgnvnpd ytggvtnqfs yrnfdlsflf gfqkggvvhs
     1021 rtyieginsg slkeslvnrd engggtmvgg gtdidtgepn ttevtvrnyw rayynndria
     1081 tfdasyiklr evkityrlpe kllkrtpirq asfslvgrnl vlwsdvpnid pevsgydgqf
     1141 qgleafslps lrsygaalni nf
//
LOCUS       WP_093326453            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093326453
VERSION     WP_093326453.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119977
     Region          24..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkllsffl vcvallasay gqertirgki tdkgsgeplp gvsvmvtgta sgtttndegl
       61 ysisvpanaa slvysyigyv ketvtignqd qvdvelseda qalsevvvta lgiqrkrnel
      121 gyaaqevkse ditrtrdnnf tnslsgkvag ldikqsgtmg gstnvvmrgy ksltgnnqal
      181 fvidgvpvsn vntntdlqed adaqnqgrgg ydygnaaadi npddiesinv lkgaaasaly
      241 gsrasngvim ittkkgkknt tnitvnsgvt lgkidkstfa kyqkeygagy vnqyseegya
      301 spdgnfwyes vfgnadpali apftedasyg aafdpnllvy qwdafdetsp nygkatpwvg
      361 aqndpssfyk tgvnsmqsis idgggdvtty kvgytrndet gvlpnskitk nlfnlsgshq
      421 indkltvsat anfskidglg rfgtgydgrn pnqgfrqwwq tnvdikeler ayeregrnit
      481 wnwgdtgatg piysnnpywe ryknyqndtr nryfgsavvn wkplewmdvi grvtfdgsne
      541 fqeerlaigg tdipqyqryd rtyseanydl llnfnkeitt dltfkgllgs nlrrnylssi
      601 rartngglsy egiyslsnsi fpiepprerl erigvdgifa nanfgykety fiegsirrdq
      661 sttlptdnnv ywypsvagsf lfsnlmkdsn wlsygklrin yaevgndasa lslyntytin
      721 tpfngipmas iseelrnanl kpertksfev glemnfldsr lgfdasyyrs tsfdqimavt
      781 vssatgydrr wvnagslrnq gfelsafvvp vrtdnfswtm nvnfalnrnk mielyegnen
      841 lqlgtfqggi tlnatldqpy gtlrgvdyvy ldghygdpdy rvvgedglya tsgpdqvlgn
      901 inpdwlggiq nnfkykdfsl sflidikkgg slfsldqyyg matgiypeta glndlgnpkr
      961 tpisqgggvi lpgvnadgss nttrveaydn svtpygysnn pqagfiydag yiklrelait
     1021 yslpnrllan trffkgidfs lvgrnlwlih snvpyadpeg glssgnlqgi qsgvypavrn
     1081 ygfnvrmrf
//
LOCUS       WP_093326455            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093326455
VERSION     WP_093326455.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118720
     Region          24..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkllsffl vctmligtay aqertisgkv tslsdgeplp gvsvlvtgtt sgtttddkgl
       61 ftldvpsnas sitltyigfv kqtieignrn ridvvlaeda qalsevvvta lgisrqkksl
      121 gysvqeikge dvsqtkqtnf vnglngkvag vqvvggsgnm ggsakisirg issitgnnnp
      181 lfvvdgipmd nsnfapisat tgkpgtnqar gaggydygna iqdinpddie sysvlkgaaa
      241 talygsraln gvilittkkg stkkglgvsy nfnaqmdkvy klpdyqneyg ggawndeigg
      301 aqpfgrlytp ngtyddgdgk grydllvdya rdeswgpkyd pnllvrhyws fegdetgvsa
      361 pwvahpnnvr dffetgmtyt nnvaldgane qgsfriaytn lsqnfilpns dfeknnisfn
      421 gnynftprlh adlsanyagt katgrpgtgy dganvmqqfn nfgqrswdid hmrnyenpdg
      481 sqrtwnrvsa snpranytdn pywtryknyq ndgrdrfygv fgltyditde lkvsakamtd
      541 fytdirqeri afgsnavpfy shyerfnkee nfearitysk tfndfsvnam agvnrrenqy
      601 ringgqtvgg lnvkdffnlr nstsaallie qlfqnrmnsa fasasfgyke fiyldvtgrn
      661 dwsstlpann nsffypaasa sfvfselgsm rdsgwlnfgk lrfgaakvgn dtdpyrllni
      721 fepdqsigds psytrpvqln npnlkpetav eyeaglemrm fdnrfgfdfs ayhktakdqi
      781 iplaisptsg ytsriinagk mqnkglelai ygtpiktsgg ftwdatfnia rnvnkliely
      841 tdpvtgervt nltigtapfv atinaeeges ygsimgsnfv yddngekvvl pnglykvsng
      901 vekigsilpd ftggfmntfs ykafslgvnf dfqsggdvfs itnlfgkssg lfeetaangi
      961 rengiivpgv kedgtpndvs idaythfnan ggqriaaenv ydasyiylre vnlgynlpks
     1021 fverlrlqtv rvaltgrnlw lmksniphvd psamalstgn lqgiegvsmp strtfgfnln
     1081 vtf
//
LOCUS       WP_093326462            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093326462
VERSION     WP_093326462.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114581
     Region          24..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkllsffw vctmligiah aqertisgkv tdekggvlpg vsvlvsgttl gtqtnsegny
       61 slqigndaks itfryvgfvi qtiplssnnt lnvvlvenaa qldevvvtal gvvrekrslg
      121 ysvqnvksqd vvnsresnvv nalagkvagv qinssggqag ssarivirgn tsltgnnspl
      181 fvidgipmdn svnsgisest estlfngagg nramdidpni iedisilkga sasalygsrg
      241 afgvvlittk kgvrdlnrkw pkisfsssva fdnaitdgyq hsylqgtngl yknglplglg
      301 gyseadggat qttaswgphr dsvsqavids igipsiydpr kdfyrtgqvw nnsvslsggg
      361 ekssymltys nltqqgivpn ndfkrnsfta nftsqlsknf ssttsvsyts sinnrfsegn
      421 sarsflygln fapinfdikq aydqygnmsw sspadgttgf nnplwlvnnn sspsnvdrii
      481 asnemnlqlt dwlkltnrvg ldtytdemne ytnigtrgal pgrmyasllk ntqfnndlil
      541 saakdinedf sftalvgtny ndrkytrrtl rglnlsipgf ydisnaesvq afqdderrrl
      601 vglylagtld yknylflnvt arndwsstlp kgnnsffyps aslgfvftda lgwsndyfpy
      661 gkirvsyaqa gndaqpyrty qtfsqanpgd gtrgninfpf ngvnafrlns llandrltpe
      721 kvtekevgle lkffqnrlgl dmsyydkvsk sqildqeisg asgfasrvin agevsnkgle
      781 vvltgtplrt qdfswdvmvn farnryklks iaegvdnifl ggftspqira dkdygygviw
      841 gqgfmrneng diliddegyp lpaedlgpig nvmpdwtggi rntfnykgls lsalfdvrhg
      901 gdilnfdlyy stfygtagvt eqrntyttwq giresdgqpn ttpilqdqay fqnkftetye
      961 tivedagfik lreitlsyrl pqslikktpf eeisfsatgr nlwiksdfsy ldpegsllgn
     1021 gngqgfyhsv tpgtrgftfg lnvkf
//
LOCUS       WP_093326572            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093326572
VERSION     WP_093326572.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118504
     Region          37..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmktflrnvl ctfyffqwqi vamllffpma mfaqqtitvs gtvvsqgdnt plsgvavkek
       61 gttngvstnd kghfvlrnvk pnatltfsfi gfstqekaaq aqsplnivli adianldevv
      121 vvgygttrkr dltgavsqvn aekiqneapg qlsdvlrgnv agvnvgynrs akgggslqvr
      181 grtsfnasts plivldgaiy ygawedinpn dietvdvlkd assaavfgak satgvvivtt
      241 kkgkdgkpvi nynaniglat mavnervhda ntftswrtdv fksinpnaqa yrfddprtlp
      301 sdisvdtwmg ydgstgdpvr twlrrlnmqp veidnyiagk svdwydevfq kglrqdhnis
      361 vsgrnkdvgy ylgagylnne giikddqfkt lrtraniean itsflsvgmn tqftsrnesa
      421 iayswgeits lspwgsqyde ngnliwrpnt ensggvnpgy dashtdrlqr ittlnstvfa
      481 kvnlpfgitf qtnftpqlel yerynherss heswaafggr asrqqretyy wqldnilkwn
      541 ktfdevhrfd vtllanaeky qrwnntmtnd nfapnddlgy hgigsginpi vssndqystg
      601 dalmarlfys ykdrymftgt yrrdgysafg qsnpranfss aalgwvfsee pffkskwfny
      661 gklraswgtn gnrdmggdep myvaladltt gkylyvqpdg tviqvnqlwv nrlgnpnlrw
      721 ernrsvnlgl dfalfnnkld gslevyqmns sdllvqrslp tvtgfdwvmd nlgevrnrgl
      781 eitlnsnnmq renfswrtsa tfqlnrnsiq hvyrnldang relddvqnkw fighaidaiw
      841 dwkalgvyql geeetaakyg lrpgdykled vnndgrftna dkqflgytep rfrwslrndf
      901 qlyknfsfsf mmyslwghqe pfnwlksrng fpdrqnsyqf pywtpenqst ewarinsneg
      961 satgfnvyrk rsfirldnvs layslprdvi skykiqnlrl yvnvrnaamy apdweiwdpe
     1021 wndsntdegp gptpryftfg idlti
//
LOCUS       WP_093326939             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093326939
VERSION     WP_093326939.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110883
     Region          25..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrinyfilll isllsffrvq sqtatlrgkv idaanspvqg vsirikgist gtssnsegaf
       61 tintpsgatl vitalgyqsq eipftgqtql tiqleednqt lnevvvtalg ikrekrqlty
      121 stqevtgadi aktkepnvln sltgkvsgvq itsssgqpgs ssrivirgts slsgnneali
      181 vvdgvpinnd qtgnngngng isrfsdidpa iiesvnvlkg saasalygss aargvvivtt
      241 kngskdqkps inftsqyaid kaiypevqsl yaqgdrgiyw ngidndqkts liwgprldtl
      301 rvngnpvrnv npmdaffqtg ktytntisvq ggtdksnyfm sysyldqegt vpttdykrha
      361 afakfsnkif dkltanfqfn yvsttshrts egyglesplw tiytapfswd pspatnedgt
      421 qrvfrysrnn pfwaleniyn dtrgnrfipi atftynpadw ltiterlgad iyseqskyhe
      481 apsdvlatpg ilrdrnnnyr qfnhdfiaea rkqigddfev smlvgnnvfs tydqryqitg
      541 tggftvedfn nisntetqvs tedyrrfrrv sfyaqptvdy kkmltlsftg rmeqssvfdk
      601 enrtyfygsa sggfvfsell kdkmpwlsfg klrasyskvg ndnvgayatt tvysiadnfp
      661 fngipgflis gdlgnsnlkn ettteleigl etqflnnrig levnyfdrdh kdllsyvtla
      721 nstgyrnsyi nagsmynkgi eallniapvk kenfswdltf nftkiknrvt alyddaesvq
      781 igqtyafkgq pygtffasgy syndagqlli ddtglpvise skaigniqpd wlaglnnsit
      841 yknlnlsfff dmrkggdlmn sddrygffyg tskatenred rvvegvnint getntvtvsg
      901 qdyyqrlsni yesaiqdgty vklrnvslty nfpekyikrt pfkrasltat grnlwiyaph
      961 ftgsdpevss ygtgndalgl ygnsvptsrs ynftlsltf
//
LOCUS       WP_093327564            1129 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093327564
VERSION     WP_093327564.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1129
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125189
     Region          44..1128
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 marnrlkigv fflvfsslgv sslsyaegen tsvktvvger rvnitgtvkt akgeplpgvs
       61 iklkgskttt ttnadgvfrl nlptgneili fsyvgyktqe vpvngqrsln ivlqddnsal
      121 devvvvgygt qrardvtgai vsvdvkklad ipvasvsesl rgqipglnvs ggstrpgama
      181 tlsvrqqfnw gkdggndypl viiddviqvd aqtgkpsmer fnmldvseie sitvlkdasa
      241 aiygsrasqg aivvktkrgq vgaprisysg kfqtndavsh ekvmnarqyg efankfgral
      301 gwndnyfysd aelsqmesln ydwltndwra antmqhsldv sggseratyy tgasyytqga
      361 nlgsqdfkrw tfragtevkv asdlrlsatl aaantdldrs ftkinfsdgy atggeqndys
      421 vllhmpkyip wvyningvdq yvspalgpnk lgnvsgnnsl snwnyydmln ngskttnkdf
      481 nynanfslqy dvpflkglsf kfnygltqas gnteqvqmpl llararnint adnhlysntt
      541 qwddpllnra nsrvtydntt skneqlnffa nynqkfgdhd igamfsvekt tagwedryqi
      601 ydnptrgvyn gtsisagtln tsntityrte sgtlsylgrv nysyksryll qfvfrtdast
      661 kfapenywgf fpgvsagwvv sdenwftenv awmnylkvra svgitgnnnv npwkwarlyt
      721 aatdkgmafg nnggmyttgi tpdadpnrdl rwdrtvqrnl gldmsflksq lsmsldgyyn
      781 tttdmltdms gaigvpisvg gafaeqnyag vkawgtevsv twksnvnevn ysigmnfgln
      841 nykttryfdq pfdypadmtt rravgntgyg npvwgyktwk ntsggdgmlr tdadidaywn
      901 yltenasnsg iegaepnfmg itdksqmkkg mlvyedvrga ldpstqsygg pngviekdsr
      961 qdwevlkksn mnygittnls agwkgvsfqa qistswggan yldyvkqgts sthalwsqti
     1021 yltdmydpet npngkypnia yyddfggtns dffllptfrm fvrslsigyt lpkkwltkak
     1081 vdnvriflsg nnlwdfynpy pskyrnmyds pgtgyptlrt wslginlgl
//
LOCUS       WP_093328178             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassotalea agarivorans].
ACCESSION   WP_093328178
VERSION     WP_093328178.1
KEYWORDS    RefSeq.
SOURCE      Thalassotalea agarivorans
  ORGANISM  Thalassotalea agarivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Thalassotalea.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Thalassotalea agarivorans"
                     /db_xref="taxon:349064"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53945
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipkesl rgenrvaasp asvkaliklg fdvqvqkgag vkssiadqdy adagaklatk
       61 kavwqsdvvy kvnapteaei dsmkegatlt sfiapaqnae lleqlkakni ntlamemvpr
      121 mtrsqsmdal ssmaniagyr avieathhfg rfltgqitaa gnlppakvli igagvaglaa
      181 igtagslgav vrafdtrpev keqiesmgae fleldyeepe dtgsgdgyak emsqafidae
      241 malfaeqakd vdiiittami pgkpapklit admvrsmktg svivdlaaag ggnceltveg
      301 kaidaegvki lgytdlvsrl pnqssqlyan nlvnltklic pekdgaitld fedqvvrnmt
      361 vvkdgeitfp pppiqvsaaa pkpaakapek veekveeeqs stkkyvamav ggalfawlas
      421 vapasflshf tvfvlacvvg yhvvwnvtha lhtplmsvtn aisgiiivga llqvgsdsll
      481 iqvlagiail iasiniaggf fvtkrmlkmf rk
//
LOCUS       WP_093327770            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093327770
VERSION     WP_093327770.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111465
     Region          44..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkhskwial csipilgyvm atqdlyaaar ptpsvdhetp fqqrtvrgki snvdgtlpli
       61 gasikikdmp ggtstnqegl felalpqpqv tliissigyi tkevavtdqq nlnvqlqeda
      121 nnleevvvvg ygsldkrelt savssikqrd lvagtvspll aiqgkvpgln issnngsdpn
      181 anvsiqlrgv nsvkasqgpl vvidgvpggd insvakedie sinvlrdasa aaiygtrasg
      241 gvilvttkrp qigkaavnft seyfiesvrk rpdllsaeey lahglgqdng artdwydvvt
      301 nknpfshrqv vnvsggsena nvyttffkrd akgisigsqr geiggrvnsn fkffdgrael
      361 stnfsynqvd adfpgngapg dfrdennsly niaigldpti spydasdpsg ynvltggynt
      421 wnplaevmlr kkqnqyryll anatlkvnlt qdlyttamvg iknnsehptf frsaqhrvsr
      481 eqnvdgyakq eykrwqdriv ewtlnyskrf dehqisavag ysyqdfngqg fwaensnfpv
      541 dgleendmgs gtwladgrag lgswkdpwvk laaffgrvny sfkdryiita nlrhegsskf
      601 apgnrwgtfp gvsagwrlsq epfmrkltfi ddikiragyg etgnegfgae vstrvysadt
      661 wwpfagnwnr tfgvkhnqnp girwevkkey nvgmdftiln nklsgrfdyy krviddliye
      721 isvsqppaih dkttinvgsm enqgfefeln ynvvnkndwt yttsivashn ksnlrtlsgs
      781 qtfmdsknfp spgspgtavr lypgeaigqf yiwqfagftd dgqwllynkn nevipasdkk
      841 iedkrfigng ipklqlswnh sisyknwdas vylrswlgyd vfnmmkmyng ianvtgrnvl
      901 ksaydelanv kgekqlsdyw lengnflkvd aislgytfnk nwidpfknir vyatgrdlfv
      961 ftkysgldpe vninglepgf enldvyprtr tfmfglqasf
//
LOCUS       WP_093329209            1145 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093329209
VERSION     WP_093329209.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1145
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125793
     Region          75..125
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          134..1144
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkelnerv lykhsfvyff tkrnllsfry cvfltiflsl naiantdsqg ekidlvvqnv
       61 klknvfpile qrgkirlmys eesiafdkpv tikaketpvl qvlamllant nleymqmkdn
      121 lvivrnkanq psvtvsglvk gtdaqpltgv svivkgisgk gtrtgadgay tlsvpansvl
      181 vftyvgylsq eialggknri dvilqedaqq lgevivtalg ikrenkklgy aassvapeql
      241 tesrttnlgn slsgkvagln vspsptgpgg sskirlrgqs sfggnnspli vvngvpinna
      301 pqgganaagg gntgevntdl gdglqsinpd diasltvlkg aaaaalygfr akdgaiiitt
      361 ksggeqgegi gisystslqa dqpldytdfq yeygqgeygi rnatladarr tgvwsfgprf
      421 dglpimqhdg verpyapykd rikdfydigk tftnslavsg anekgnfrvs fantdansii
      481 pnsdynkkif nvglnynlnk dlsvqvnany snefnnnppv vnqqafnvnq tvytlansid
      541 mqwlknaykd pvtgneigps rftdrtnpyw ainerfetqk rdrlfgnvsm ryqftpwlwa
      601 qgrvgqdfft nvrhanrptg tamlpvaptg fngnyfqnts tfrernidfl iglnheigvw
      661 gvdatfggns mdqksermgt svtnffirdl ytvdngqikn piyafshkrv nsvfgtvdfs
      721 fneflflnlt grndwfstln pasnsafyps astsfvfsqi wkskptwlnf gkvrasyaev
      781 ggdtdpytna lyyniennlf ngvplgiits aispnanlrp ltvketelgi dfklfnnrla
      841 vdvaaynkit adeilnvdis nasgygqtlv nvgklrnrgv evslsvtpvk tehitwesvi
      901 nyaynktkvl qladnqtrfd vgtgeyigii shevglpmas vrgvdylrnt ngeiitsngl
      961 flpgniityg saipphtggw lntltykgir ffvqldfkag hkmisnsnfn wtrhglhqns
     1021 lvgreggvif dgvnsdgspn ttpveaelfy sqyrsgniat pfvydasfir artislgydl
     1081 skflrgtfik slnanlfvnn pfiiskkvdn ldpetqysas dlntgletha lpttrtygln
     1141 lnvnf
//
LOCUS       WP_093329373            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093329373
VERSION     WP_093329373.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116623
     Region          24..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkkirwlml silfitanaw aqekpiqgkv teeksgqalp gvtvtvkgts qrtqtnevgl
       61 yqvsakagnt lvfsyigmep lervvgngnm lnvvlkplss gldevvvtal gierqerslg
      121 ytaqkvtake lnynkqpnml nalqgkvagv tisstggspg qgariqirgi nsidptrdnq
      181 plfvidgvlm dnststqgeg adgrgmsnra vdinpddiet inilrggaat alyglrgang
      241 vvvittksgk sgsikidyqg tagfenvarf palqdtytqg wqgeydpesf wpswgptved
      301 araidpthpa klydhvkdaf ttgsqyknsl tfsggtekvt flsslsqlnq kgvlpttdfk
      361 nyqarlnttf kmsekftagv nmsvnnsggy rgnagryieq liywsprhdv ndyleengtm
      421 rsyggttnpr yatesnrfkd dvlrfigsan fsyrpvswln lsyragidty rdnrlgtalg
      481 frdlvgerlv ddngteaapg ygfvnvynqn frsinstfva sadhkfsddf satlrlghdl
      541 ydrymrrest egsdltvydw fslanaktlq setylekyrl mgifgelsfn yknylyltlt
      601 grndvtssla rpnnsffyps stlsyifsdh wklpeiinna kfrfsyarig kdadpystss
      661 glaiytdlpt gysgftrpgl lgdpelkpef tstwesglsm dffnsrlgfd fnyyhsvskd
      721 qiiripvsas igyvnaavna gsmrnqgiel sinaspikgn dfswdtrlnf sanrnkvlsl
      781 redferieaa nefgylssnv ymwlipgeay gdlygralrr yyspeeiaqg ldqsteidpd
      841 rplligedgf pildavankk klgnvqpdwi ggwsntfryk dlslsflida rvgqerynql
      901 anfysafgma kytenrndhm vfngvladgn pntkevwlgq gidpstgfny gdgyyriihr
      961 gvsenfveda swvrlrsvsi sysvpqkwiq nsivknvqls ltgnnlalwt nyagfdpest
     1021 ttnsgsnvda fagmtypavr sflftlnvgf
//
LOCUS       WP_093329217            1134 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093329217
VERSION     WP_093329217.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1134)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1134
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123615
     Region          73..125
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          131..1133
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskelnqkv fytycfahfi akrsvflfky ivlllitfsl peevyavsek idltarnvkl
       61 ktlfpvleqr gkirlmysee namldklvsi nvsdmpvlev ldqlfshtdl eykmlendlv
      121 vitkkdkqqt ievkgrisde ggqplagvsi ivkgtgkgts sneegqfilr spenavlvfs
      181 yigylsqele vksrqlidvt ltaeaeslge vvvtalginr ekkslsyavt qiggdqvtka
      241 reinlgnalt grvaglnatg tstgpggssr ivirgngsln gdnqplivvn gipidnsnqg
      301 aagsyggmdr gnglssinpd diesisvlkg gtaaalygsr aangvilitt ksgkgqqgvg
      361 veynttltme tprnlldwqy eygagsqgak pssqaeaiaf grmswgarld gsmvpqpnge
      421 eapyiaqrdn iknfyntgst fnntvalsgg neianfrfaa anldnkgivp nnalniksfn
      481 lsanatlakr iifegkaqys iekndnrpft adfqknpnag tqiiansidv rtlapgydan
      541 gnemvwsdyi yatnpyfavn kmtngdtrnr figmfstryn itdylyargr vgidqynfda
      601 fdlsepsgta fnnrgqmntd qnykqevnae ailgfdktlg dfsvnaligg nqmrnttkgv
      661 qltsgqfnvp fqyfigngsa qnftlnygkf ainsifasad igyksylylt lsarkdwfst
      721 lppeqnslly psvglsfvas eawkskpmwl dylkvraswa qvgggapapy sldltymnqp
      781 qqyitgatlm tvnsntipnk lkpytsttse agvearifnn klgvdltvyd rtttndivna
      841 svpyssgyqt valnvgeirn rgvelllsgt alrtgafswd laynmaynkn tvlkisddlq
      901 siqlpgattr tlnggiyhfe gqpfgmiagn raarnedgqi iynsatgipi qgpleilgkg
      961 vppltmgitn tfnyknfsln vlidgkfgak vyaatnaygt qfgldkrtve hniretgidl
     1021 sgvnqanepy tgnvsaqtyy stiwatltde fvtsadfikl rsitlgyslp nsllektpfe
     1081 altlsfvarn lfflynkarn idpeasyssg naqglenfgl ptvrsyglnl svkf
//
LOCUS       WP_093329456            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093329456
VERSION     WP_093329456.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118709
     Region          27..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkcflyvlis lcclhykvga qnrliygnvk gsdheqpleg atvrgmgsnl mvyadsngaf
       61 klalpadvds llisyvgykp iqiglqidlk lpldillera geeldevvvs tgyqqlpker
      121 atgsfvqvdn tllnrrvstg vidrledvts glqldrrgse vkidirsrgt imandqpliv
      181 ldnfpydgni eninpndies itvlkdaaaa siwgvragng vivintkkgg ykqklnmean
      241 anlqvvskpd fnrlpwmssa drlelegflf ekgyynaten snnklplspg velriaerdg
      301 lispqqlqae ldrlegydir kdyskylyqp avnqqyalnf rgggtgytyy lssgydknra
      361 alvgnsmerl tlraesniqv akplelnlgl iythterqrn glgmsvtqlp yarladnngm
      421 plpivkdyrf pfvqqatgng lldwtyrpll drdlqelgtn tadmrvntgl kytflpgftl
      481 eakyqyqran didtdlryge syyvrnlinr yssintdggv trpiplgdlm dradallash
      541 tfrgqlnyqk dwdhhqlvgl agyeyrtlkt drnsvrwygl dreiltynqq mdfntrfply
      601 hngsllripn tgsmggtfda aisyfsnaay tfqgrytfsg saridqsnlf gvsanqksvp
      661 lwsaglswli seepfykrew pylkarltyg yngnvdksis afttamyyna asitglryan
      721 ianpgnpelr wektgilnaa idfaafqhrl sgsieyyhkk gadligfapl dpttglksfk
      781 gnvgnirgqg vdimvnaeai rgkfnwrinl lynyavdevt rymepvtlvg nylgdasigr
      841 asnaitpieg mpvfsvygfa wagldpasgd plgflpsgei sndynqlart atfdqlifmg
      901 rarpphagsl rqtfsyanfs asmnlafkfg hyfrkptihy nqlfagvdap ghsdyalrwr
      961 qpgdeagtsv pslvypanaa rddfyqsavi nvlkgdlirl qdvtlnytct pnfggkplik
     1021 qldfymylsn lgllwtankk gldpdylelr ppftaafglk lsl
//
LOCUS       WP_093330815            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093330815
VERSION     WP_093330815.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112267
     Region          43..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meknkpfqiq lfilllvvlt islpirilaq nltsiagtir sqtdnttlpg vsvkvkgqtt
       61 gtssntegry rveaktgdil vfssvgyqtk elaigndaiv dvlliedaaq lnevvvtalg
      121 ierqtkslty atqelknedl ttvkdpsgnv mnslngkvag avvtpaatgp ggavrvvlrg
      181 nrsisgnnna livvdgvpid ntmsteqggg gsantvatqq kslssgysgs dggasinped
      241 vesitvlkgp aaaalygsra angalmittk kgkdgavkln ysggittdkp lllmdfqnty
      301 grgnggvagt daagswgava atypdnvrsf yntgttinns vnisggtakm qgyasytnna
      361 iagivptnhl drntlnlrln neilpglttd vkvtylnqki knkprlgdng vtnealimpr
      421 dmsseelknf esinaetlqp qplywtnssf fqnpywdvrr tslneernri mlvgsvkyql
      481 tdwlfaqgry sldryddkit gafhegtlpv ptlaggryqe nhvnrwerni dfllsgtnei
      541 gtdfgvnyni gaallnnsgy ntqslanglr ipnmfdlnfa stptfaniaa ekeiqsvygs
      601 atlnykqqlf ldvtarndws stlpaphsyf ypsfglsgll semikmpswv syakvrgayt
      661 qvgndadpyl lqqtysyspg agdgfvardq ikyiddlkpe ktkaweigte wrffegrlgl
      721 dasvyktntv nqlifiglpq psgynnqyvn vgdienkgle imltgnpvkk dnlswnttln
      781 falnrnkvls llpgieqanl spstnfgsll ikpggsygdi ygfkwaqdan gayqinnagl
      841 pvvqqlqnig nfnpdytisw lnqvdykqft lsfmidgrvg gtvisgtdal lgyfgladyt
      901 tknregglvl pgvlpdgspn niaisaeqlw tqvsqggtna ygdffaydat nfrlrelslg
      961 ytltlknspi ktarfsltgr nlfffyrgks kldipgigkr tlpvdpeaai gtsnfqgies
     1021 gilpstrsfg fnlnlsf
//
LOCUS       WP_093331464            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093331464
VERSION     WP_093331464.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116999
     Region          32..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlvqppthlq ktsalflllm ilfchysfgq tktisgkvtd sltnetipgv tvrnvtsgki
       61 astdqsgkfs lqvtqgdslr amfigyqand livgtqqell ivlapsqqgl nevvvtalgi
      121 kkekqavgys iqevkgpdlv karepsaisn lagrvsglti tpstnlfgdp gitlrgrsnv
      181 livvdgmpvn tdswnlspdd iesysvlkga naaalygnrg qngaivittk rakandkgfq
      241 vefnsstqlq tgynaipkmq teygpgsnye yafkdgrggg indndyniwg prfegqlitq
      301 ynsptdpetg elvplpwiar gkdnlknfle ngllstnnia istkgeqgdf rlsvsqmfqk
      361 gttpntklgg tnvnltggin agsklrfdas inynkqyspn ypnlsygphs piyiltlwgg
      421 adydindlrn ywqpgkenvq qfnreytiyd npwmtayenl rtydkddvyg hvmmnyklsd
      481 kltfnartsv stwnrnrtik ipisanlygy tiggsrvggy qetydtfwen nteasfkyqd
      541 rffdnigftg siygnlrtvg vkslfartdr gltvpgvydl snsvmptist ndrasrqvgs
      601 vygfvdldyk smlylsltgr vdksstmplk nntyfypsas lsavvsemvt lpkvissmkv
      661 rgayadvasd fvdedsqydi ykllpfysny grwdntytgv aytgvlpnad llaervktfe
      721 lglemrfldg rlgldaavfr nlegpsiiel ttsvtsgvsa rqingltllr kglelsidgt
      781 pisspnfswn vllnastnha wlhevdgvqn rygniyvger wdsyyvrdfq kdeqgklivg
      841 tnglpaynpy mtkighsdnn waismnntfr yktfslsfmf dgrfgglinn vqdakqwgsg
      901 thpesaneyr lkdwqnrdva dyqgsvmtdg lkivsgqlsa dqdgniiadt rvfapndipv
      961 lwqgwatnyy qsgpiaakkr tfvklrevvl synlpasmlq rtklfntasi slvgrnlfyf
     1021 tgkgtqnmdl dqftgsssdy qtpsvksfgv nlnatf
//
LOCUS       WP_093331478             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093331478
VERSION     WP_093331478.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109161
     Region          32..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvlkqfkng ilfafclfsg qqllaqqerp lvkglvqdtl gkaligvsvr ainqstqksf
       61 qastseqglf qfvsipsggp ydfvfsyigf mpdtlrnyqv vagkqitlnv klkeepmglg
      121 evvivgygts nkreitgsit svsseefntg vfstpsqllq gkvaglnitr sgnpnekpav
      181 vlrgpstlra gsqepfyvid gvpgasidli apddiesidv lkdaastaiy gsraangvim
      241 vttkkaksgs trlsystyva aeqisntidm lngeelrtyl sengktattd dgsntnwqde
      301 vsrtgishnh nlsfsgssqn ssygasvnyl nnqgiikgss lerfiargym eqrafndrlk
      361 lnlnitnsst nsqlvadevy snmliylptv avrqpdgsys edfsvtrgyl npvslidnne
      421 inqktklfla sggakvtile gldfttnvsy qderidsniy ynrlsglaqn vngrvirntv
      481 tntkkiiesf fnydrtfgeh glkllagysw qedrlgdgfq ttnqgfvtdd lsynnpglgn
      541 pdegvavdyg tkriqtlrli sfygrvnyqy qnkyllqasl rrdgssafga nnkwglfpaa
      601 sigwlidred fmqgapviss lklragygvs gnsagfdvft srflyagtgr fyydgkfina
      661 igpfqndnpd lkwertatin igldfglfnd vlsgsvdiyd krtsdllwty pvsatqyfvp
      721 rltanagemt nkgielslqa tpvnrngfsw ttainlahnk nemtslsndn felpliqtaf
      781 lggrgqsgna sqrvqegyal gsiytwryag knadgvsqfy dkegnltiap tsddfyyign
      841 aqpklvygwn ntfkykkfdl nfflrgvtgn kiingtladm napnnatqtn iprftldeqe
      901 pindnnayfl sdrfvesgay lrldnvtlgy tfktnnrtlr aylgannlfv itnyrgidpe
      961 vnmggiepgv dnrnyypktr sfmlglnvnf
//
LOCUS       WP_093332070            1165 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olivibacter
            domesticus].
ACCESSION   WP_093332070
VERSION     WP_093332070.1
KEYWORDS    RefSeq.
SOURCE      Olivibacter domesticus
  ORGANISM  Olivibacter domesticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Olivibacter.
REFERENCE   1  (residues 1 to 1165)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1165)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1165)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1165
                     /organism="Olivibacter domesticus"
                     /db_xref="taxon:407022"
     Protein         1..1165
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127398
     Region          68..>125
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cl21470"
                     /db_xref="CDD:473874"
     Region          182..1164
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkpyfymm fflslslsaa nlkshsnphi knsetlagtv ilqntvqdtt lmdsakanaa
       61 tdsterhgvv tdsagkplaq vsvkykgakd siltnaqgef tiktlgtgvl ifnlkgfqik
      121 eepinnltei ktklspveqv tatvnadsgt atrtdsaaqd tsarkaaqts pdtttkdstq
      181 ekitgtvkds kgpipgvsvt ikgkkegvit deqgkfsiaa pgnavlvfss lgydakeeft
      241 anrkiinisl eeesqklqev evvavgygtm drskltssvs sigsdqiend vlpsvtqaiq
      301 gkaggvqvtq ksgspgggln irvrgttsin assdplyvvd gipvnsttnf tggsnfnfgg
      361 gtqginilss inpsdvqsve vlkdaasssi ygaraangvv littkkgqpg tsvfnfnmye
      421 gfsevpkerw ydfmnteqyq dymrdyyrfk ldadgnpspv peqilanpgi ntnwqdemfr
      481 saptrnyels asggnektqy ytsigymkqg gvilnsnfsr lsarinldhq hseklrfsts
      541 inltraindr iqeenskega tkngvvsppn lpvynadgsy afdqvslsre npiamlqlpt
      601 nnaqtfrvla nvsaeyriip elalktsfgt dmsfidetff mppiglrsfa sqggigarrn
      661 trdqlwinet tlsfdktfgd hslnalagvs vqesrlefvd aqrsnfpsnd ieyissggvi
      721 tgansypeew aiasgftrvn ygykgkylft anfradgssr fgpnnrwgyf psfaaawras
      781 dedfiknika innlklrasw gitgnqnign yasyslysgg snylglpgfv pnvlgdknlk
      841 wettkqldig ldlglfgnri slladyyvkn tsdlligipv ltqsgflnrf tnfgeiqnkg
      901 fefelttqnl vgafkwtttl nmtfnknkiv elpvarilgg vgelnlaqag lplgtfygwk
      961 migvnpetgl idyedqngnp ttptnpddrq iigdpnpdff ggitnnfryk nfdlsimgqf
     1021 sygndifnyn langlegyna ssngfvdwtr rwrnpgditd mprpspgdln qgaisdrfvq
     1081 ngsffrirnv tlgysfpnem ieklnisklr vyatvqnayv ftkyrgydpe vssshggant
     1141 gliygydygs ypqpriftlg vnltf
//
LOCUS       WP_093335312             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudonocardia ammonioxydans].
ACCESSION   WP_093335312
VERSION     WP_093335312.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia ammonioxydans
  ORGANISM  Pseudonocardia ammonioxydans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudonocardia ammonioxydans"
                     /db_xref="taxon:260086"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38481
     Region          14..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(28,83,102,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(57,135..136,145..146,149..150,153..154,156..157,
                     159..164,166,168..170,173,196..197,285..286,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,135,138,141,182..185,205..207,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(132..133,135,145,188..189,196,212..213,215..218)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(165..169,172,175,198,200)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgdeagrddp qktvtigvpr etragerrva lvpkvlgkls argatvvvea gagagalipd
       61 eeytaagaei gdpwaadvva vvnapseeqi grlrsgqvli gflspltdpq ivqklrgagv
      121 tgfamesipr israqgmdal ssqanvagyk avlaaaehst rffpmlttaa gtvkpatalv
      181 lgvgvaglqa latakrlgar ttgydvrpev adqvrslgaq wldlgidaag eggyareltd
      241 deraqqqqal eeaitgfdvv vttalvpgrq aprlvsaaav egmrpgsviv dmageaggnc
      301 eltepgetvv rhdvtivspl nlpaampeha selyarnits llelmladge ltpdfsdevl
      361 arscvtreee gs
//
LOCUS       WP_093359981             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tropicimonas isoalkanivorans].
ACCESSION   WP_093359981
VERSION     WP_093359981.1
KEYWORDS    RefSeq.
SOURCE      Tropicimonas isoalkanivorans
  ORGANISM  Tropicimonas isoalkanivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Tropicimonas.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Tropicimonas isoalkanivorans"
                     /db_xref="taxon:441112"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55891
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf pgearvamtp dsalalqklg ydcaiesgag maagfsdavy kdagvevlet
       61 aealyeaadi iakvrppsee evarlsgdkt lisffypasn eplmeaakaq gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvfldfee esqdgaatgg yaapsspefr
      241 ekqlekfrel apeidivitt alipnrdapv lwtkdmveam kpgsvivdla aerggncelt
      301 vkdekivtdn gvtivgytdf psrmatqsss lyasnirhmm tdltpekdgk vnhnmeddvi
      361 rgatithage itfpppppkv qaiatqpkkd kpkeltreek qaqelaafkk qtrsqvtlla
      421 vgaivlllig lvapasfmqh fivfvlsifv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsf lvillaslsv fmaginifgg ffvtrrmlam fqks
//
LOCUS       WP_093363508            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093363508
VERSION     WP_093363508.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111294
     Region          39..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 menfgirkcs iyllllvcwv gisqaqdkpq pivnaslvgq iidahtkepi egvtvqleav
       61 thnvktdrdg nfqfvtgqkl pftlhlshvg yeskvlvaeh spitielipl delleevvvt
      121 gvsqgvsrkk lsfaltkvds elintvpald asttlrgkva glridqsggn agasvylrga
      181 ksvsgnvepl ivvdgfvtgl rladlnpndi esievvkgaa asalygtrge ggiiqvltks
      241 grsksrlsin vdnevgfsdi lllppttdkh hfkvnadgsf flvdgarvid yqengysvnl
      301 hpykdhydnt anllgrttyf tnaasvasng dkynlylsaq nqykggvspa vaadkrqnll
      361 lnvgyrpstk isadltaqyg yfdtpsravs srsegllyst llvephinls erdaegryvy
      421 lpkgtelsgq qwtnpfyrlt nqeynyiten lllggklkyn inqyfsaega vslqtrhynt
      481 evyhpigyqt itpdvelnng nyelttlres trngqlqlny nrtsgrldwg vtakyvyesa
      541 fgtgfggsgr nltapvksll vtepntrels sswektvnhg yflnakfgwd dkffidalgr
      601 ldqssrfgkd vgtaffprvs aayrltedvp lypltelkfr vaygkagslp pfgakdsrvt
      661 isnaggvsyt qndntdlkra iteeteigfd ailwnrlnvq fnyafsnstn dfisvpafap
      721 isgsaniydn lgavksnsle levngkvlek tkfawtvglt fskvrskits lgdvpeftqn
      781 gyrkavgast taiygysihs dlaqletnnd gfvvnagdgt kriddymvne fgvvvekaay
      841 gtakeapvfy vnpatgnaki igeanpnfni gfsnsfsygp lslyavidwq qggekfneta
      901 qyltyvyrsr fselssaagk plnfttqvfn asqvtdywie stthvalrel slsykiptqr
      961 lglskllqna sfslvgrnll iwtnyqgvnv dglgqdgfny psyrivsgkl tfnf
//
LOCUS       WP_093363682            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093363682
VERSION     WP_093363682.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116570
     Region          52..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrkihyill ialfltcqla ysqvqiqgqv tdnaqnplag atvtatgttt qsdaqgyfsi
       61 qiatlpanlt ftllgyqrqt ltvnsaspls vilqstdqei gevvvtalgi srekkalgya
      121 vqdiksselq trptnalsai sgkvaglqvv ssggnmggss rillrginsi sgnnqplyvi
      181 dgtpidntdp nssatvngsa gkdlgsmiqd lnpddienis vlkgpsaaal ygsraangvi
      241 littkkgakg ehidislntg ldfenvvrlp krqqlygqgy stifqtatin gteykivdya
      301 sdeswgpkld gtpvlqwysl dpedeenylk ltpwvypkhd vkhffntgla ntnnfsisss
      361 sgntnyrlsy tnknvggttp nsslnrntln lsgstrlgki qvsanvnyik nssvgkpwvg
      421 atnrgiilna fqwggvqvdf eklknykrad gtqiswnrts hqntaageat rfidnpywaa
      481 yesyveenrd rfygnfglty datdwlslta kahgdiyayd tqdriavysr sasqyeetsl
      541 klneynyefl atakknwdnl slvanvganl rdqqrrsdya itqgglilpn yynlknasnv
      601 linnytyhkr vsslyasasl gyndilfvdg tirndwsstl pvnnnsflyp svtgsfvfsq
      661 ldafrqidwl sfgkvrlgwa qvgndtdpyq lyktyvaqqa fegnpsyalp ttlnnaelkp
      721 eitsswetgi nlqffrnrlg ldvtyynnns rnqilpvpvs tafgyeykvl nagkinnkgi
      781 eitltgtpvr kdnfewnttv nwsknrntvv klddlvntlt lsdglvnlva regqtygqfl
      841 gydfvyapdg qrvvqddgty mrtsqlvplg svlpdflagf qnqfryknft lgflidsrfg
      901 gnffsqtykv amyagildkt aanniretgv vldgvtgdvq fhsdgtytvt ntatndknis
      961 alqwarneys gpttfsifda tfiklrevtf gyniplknts lvknlgvsvy grnlwniytk
     1021 skyidpevts sggnvqgieg gniptpvsyg fnvnvkf
//
LOCUS       WP_093363766            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093363766
VERSION     WP_093363766.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120752
     Region          25..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkryillvv yalaivatay gqvnikgsvl dslgngiakv svmeagyara vttdsegrfe
       61 iqtlqdkgsl lfkhvgyenv irnfdngtns ikvflipvis qieevtistg yqslpkerat
      121 gsfefmdrkm ldtrtgsnvl ellegltpgl qfdnrkgspt lnirglssln dvmtkplivl
      181 dnfpyqgdie hinpndiesv tllkdaaaas iwgaragngv ivittkrrkg qdrvaieyst
      241 nlnftekpnl lyypdmrssd fieaerflfe kghydaayng tartknntvf spvvellfke
      301 regqlnsgev eqaiarfnni dhryemmdif yrkpfrqqhf vgmgvhaqnf ssrfsigyda
      361 shgdqignks nrltlrsinr ldlstklsve gsisysgnta grygnlmshn yspgggksrl
      421 ypyaqyrnek geplpvpsgy nmeyvrslqg sqlldwmyyp vneigtvvse dsqkylqtql
      481 kldykplegl alsalynten qtsdgeslyr ehsfyirnlv nrftqvdgdk vtyvfplgam
      541 ksssrsilns ynirgqatyn kqfldlhdih allgaevsnr rrdtrgfwvh gfdeylltsq
      601 vvdpvntypi ydglssnsmi pqagannhsy didrfvsmff ntgytylnry gvsfsmrrda
      661 snlfgvktnd kwkplwsagv nwllhnekfi kdmdwisslk irmtyghsgn sggvantlpi
      721 ilhlkpeyga ltqlpraslt tlsnpnlrwe dvrmmnagid fslwngklhg sieaynkkst
      781 dllandlmdi ttgyqtitrn vgelkgkgid lrlssgygsg nlkgsttvnf santtevtkf
      841 ygtnfrgsvy aentgnsirp vlgkqlypvf sfkfsgldpe tgdprgildg eiskdytkll
      901 ndsiqylnyh gtalppyygs miqqltwkdi tlsflvaykf ghffqketir yndlfqswig
      961 hrdyadrwqq sgdeqrttvp smvypatanr drfyaaseph ilsgdiirlq dvgldyrlra
     1021 rygqrdvqln lffkinnvgl lwranskald pdydglppgr ryvfgisvnl
//
LOCUS       WP_093364492            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sediminis].
ACCESSION   WP_093364492
VERSION     WP_093364492.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sediminis
  ORGANISM  Psychroflexus sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Psychroflexus sediminis"
                     /db_xref="taxon:470826"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118191
     Region          25..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqnanwifl fifaiisqvg faqnqevtgt vvdntglplp gvnvieegta ngtqtnfdge
       61 ysiqvgeaav lvfsylgmke qripvnnras idvtlkpatg qldevvvtal gikrekkslg
      121 yatqqvdgne vsdvatqnft nalsgkvagl kvkssgtmgg stnvvirgna sltgsnqalf
      181 vvdgtpiinq ntntagqrag rggydygnaa adinpddiks invlrgaaas alygeraang
      241 viiietkrgq knkgigvsir ssvmfsnade ktlpnyqqky gagygpyyqs ddgyfnlydv
      301 ngdgtldett pftedasfga afdpdrmiyq wnsiypgldt yqqaspwdaa ehtpndiwet
      361 gytminsval dggtdkstyr igftnldqeg slpnssitrn ninlsathdf tdkfkvasnf
      421 nfiktdgkgr ygtgydalni mqsfrqwnqa nvdlykqrda yfatgrnitw npngpdnlsp
      481 iytdnpyftr yenyqtdtrn ryfgninlty qindvfsllg rftfdtysel qeerknvgsv
      541 gvsgysrfnn rvaeynydli lnfnknltdd lnldgnlgfn lrrneqtfir aatngglfet
      601 glyalsnsrn pinppieyea dqmvdglfar aslgylntyf leatvrrdrs stlpqsdnty
      661 iypsvstsvl lsniidqdwl nfakfranya qvgsatepyn vfntynmttp fdgqgiasnp
      721 stlnnlnlks etsksyevgl egsfldnrln ldfsyyrtrt edqitpvpis nasgylrkll
      781 nageienkgi evllsgtpvk lddfswnvsm nwsrnrnevi sltkgienlq laslqggvsi
      841 naapgepyga irgsdyvyde sgnkivnssg yyettssnnn iigniqpdwn agitntltyk
      901 nfrfsflldi qqggdifsld twygmatgvy dvtagindlg nemrapltng pdsggiilpg
      961 vnadgaqnet rvpfdtyanp ygyardankg hvydasfikl remsltydfg pealdklpft
     1021 naslsligrn lwiidknlpy sdpeaglssg niqgyqsgay pamkqygvnl kfnf
//
LOCUS       WP_093364506            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sediminis].
ACCESSION   WP_093364506
VERSION     WP_093364506.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sediminis
  ORGANISM  Psychroflexus sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Psychroflexus sediminis"
                     /db_xref="taxon:470826"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116053
     Region          25..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklngilt lllvlvvqls faqtktvtgt vtddsglplp ganvlvkgtv egtqtdfdgn
       61 ysievspdqq lvftyigfat ktvtvgdqev idvqmesges lsevvvvgfg tsrekkslgy
      121 avsevssegl eeraegdlgr vlngkvsgvv innssgvsgs atninirgyt singsnqplf
      181 ivdgvpisnd tnavgsfqdg nagssrsldl dpnsiknvsv lkgfaaatvy gsagkngvil
      241 ittkagsagd vkkkneisvs qgvffneias lpdyserfgn gfdgsfgnff snwgpgfyee
      301 gfggwaapss giaddgtysh pynranlanv fpqfqgerle wapqtdnvkd ffrtgivrnt
      361 svniastsed gkisynvnfg hlddegftpn nsttrtnfsv ggrallsnkf kinstinvsr
      421 tdfktppiar stgsgvsgag lsvfadvfyt prniplmelp fqnpvtgasv yyrndeaipn
      481 pnwvannsyv rqttsrmnss ntitydindn lnllyrvgld vysernetgt nigatagpil
      541 gaystytntn ivwdhnfqln gnyeftpdln inftagatsr ynkydrdgvs ssgqivfdvf
      601 rhfnfreqsp iqfqtfqniv glygvadley kdylylnlsa rndwvsnqvn nsqfypstsv
      661 sflptsafsd lrsknglnyl klragygtsa gfasgfptvn tlsldsrffq ppgasspvav
      721 nslsrvlane sirpelyeei evgfearald nrvswdfsyy ernttdliin rplaastgft
      781 stqfnigrie gygfesalgl rviqnegtgl nwdvninytk irsdvvdlgl etgdnpvdna
      841 ipysgfsnlg naaiegfpfs tmigstvard degnllvdsq gnyvfdqgpn vigdatpdfl
      901 mnyattlsyk nftfnalvsy qhggdiysqt igallargvt tdtdnrldtf ilpgvnqttg
      961 apndvqinns tyyfqntgfg pdelnvydgs firlaevsls ysfpkdwlea tpfgnlslsv
     1021 agynlyfnap ntpegtnfdp nivgtgvgng rgfdflngps gkrygftlra tf
//
LOCUS       WP_093364518            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093364518
VERSION     WP_093364518.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116285
     Region          24..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkllsfvl lftlfigaay aqnrqvsgrv tsasdgspla gvsvvvvgtt datqtdasgs
       61 ysinvsgnna tlafsyigya tqrvnvgsrs vvnaqligdd teldevvvva ygtstrsaft
      121 gsvatvkaet ienrpitsit kaldgaapgv vstlgsgqpg sdatvrvrgf gsinasanpl
      181 yvvdgipfng dlnsinpndi eslsvlkdaa astlygsraa ngvvmittkk gkegkvsvnf
      241 rtnvgiasra vkrydvmdtk eyletvfqay kndeiytkgt pegqagvnav nrlkgtvdpi
      301 fgvneqynpy nvpvdqlfdl stgkinsnaq lkwnenwlde vmasnpvrqe yqfdasggsd
      361 kiktmasina lkedgllktt sydrftgrvn telkpvdwfr ttmstnfars ttnsleatgs
      421 ttsnvwysse qmaplypiwe rdangdfvld vdgnrlfdyg ldrasgaqqn fnsiatlydd
      481 kyydirnnag argmiefntk dskygafqgf tlavnlgady rdnlytyyyn pyfgnaagsg
      541 rlnkqsrkvf sytfnqlltw drtfdkhnvn vllghenysy kfnhlsaqkt gfpfggiyel
      601 apgstiadad syenneties yfsrleynfd gkyylsssfr adgssrfykd nrwgnfwsig
      661 gawriseedf lkdvswlnsf tikssyggqg nndllfdgas ayyawqafyd ltwnnannng
      721 gkvssvenkr vtweknkafn vgfdgrfvdn rltvgfdwyt rkttdmllnr plalslgfdg
      781 fndnvgdmkn sgfdlslgyd virnseltwn itamgskvkn evlkltdgqn eiisgsniir
      841 vgealnsfym arsagvdpgt gdqlywvydn kddefdlskh yisndmgkaa asrvmlgnri
      901 pklygslsts vtyknfdfsa mttysiggki ydvvgysymt plyignnfsr emlrawkqpg
      961 dvtdiprvqk eatytltdrs lvdasyfsik niaigytfnv ksiglnsvrv faqgdnlalf
     1021 sarqglnpqn nftgttgyvy tpnrtisagv nlkf
//
LOCUS       WP_093364554            1164 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093364554
VERSION     WP_093364554.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..1164
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127723
     Region          50..1163
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrksllfsvm gmflassptf syemfagere stslsiegil pfsssvfqnt vsgtvtgssg
       61 piegvtvtvv ggtastqtda ngrytiqapl gstlrfssvg fatkevsvss nslsvtldsg
      121 dqsldevvvv gygtqrrgnl tgavssinvk enlegrpiad vgrgiqgttp gltitipsge
      181 igsdptikir gaiasvqgng nplilldnve ipsiqyvnpd dvesitvlkd aasasiygak
      241 aafgvilitt ktggtsekvt vnysnnfsfq npfkkyemgr lnalkytada mermgtnitg
      301 afyyltpesy ekavewdkky gssigkndpt vygrdwyvdp tntarklglr tydpydymir
      361 ewaptitnna svngsfgktk ftasfaqlsq sgmlkpgdsd rfkringglr lttelndnit
      421 lrggamfsqr nktypyatns atadmwyymy rwsslypmgn dehgnpirsp hsefdaanea
      481 smkrnyinmn vgttvklksn wkvdvdynft nedynwfrpg trftagdsws apaarmdasg
      541 npvyvdatga vvgagspgam paydliyrey tapggnpdhi yartantykh tlnafttydl
      601 nldgghdfkf mlgtnlvtdn arthwtqqtt llditnpqfd latgtitgsg sthwgaqlgy
      661 fgrlnyaykn kylveanlry dgssnfpsdl qwrwfpsfsa gwvaseesfm ewskpylshl
      721 kfrgswgsig nqavpsdlyv snmgssqssw ianggrvisl gspalrvpsv fwedletldi
      781 gvdarffnsk lgvvfdwyqk ttknmfspse gttwtlggaa pwgnfgqlqt rgfeiavdfn
      841 hrfenglgin lranlddaks vfsnytssrl vtanydgrvy gdiwgyetdr lfqyddfvld
      901 angnpqivkl tpemtkynts gggetylqkn gpngekpvyq awlestntfn fgpgdvkfkd
      961 lngdgeidgg dgtidnpgdr kiignftpry nygfrlgady kgfdfsmffq gvgqramwgn
     1021 galaiagynt adgampeaiv nnywtpetpn afypaafnna nsndannlrp qsrylldmsy
     1081 lriknitlgy slpksvlapv kvnnlrvyva lenfftwdkl nglpidpeee sgvsmfnatn
     1141 ynsgrtgvgt ptfksasfgl qlnf
//
LOCUS       WP_093364559            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093364559
VERSION     WP_093364559.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118064
     Region          46..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkailfsva lgmisyqgfa ldrhvdwrss salktevpkm feeqstirgv vrdangplag
       61 vtvsvigksi svqtdangaf sieaatgdrl rftslghaqq evtvtsgtvn vtlqaedtal
      121 devivtamgi trekkglgya vqdlgseelm knktanivns lagkiagvnv tqtsggagag
      181 asiilrggts lerdnqplfv vdgviydnst svngnslfdg gsstnstysn rvmdinpedi
      241 envsvlkgpa aaalygsraa agvvlittks gkegtasvsv nsrmisnwan rlpeyqnryk
      301 rgfyqqdgtl megdatttmg swgakfgpnd vmydnmgdff qsstswdnsv svsggskngn
      361 fylsasdfrq ngiipgteye kttvrfngqq nygilkvgan vayssadqls sltsgglygh
      421 ggagavqgaf iwprdmnmsh wlnedgskyr pfdweqvand fdnpywimnk mprtdntkrl
      481 tgsfkasvdi adwwdihytv gidrytqktn rftepgsgvn qiyqngllse ndtdfqylss
      541 nlmtnfkkkf gdfdmnllvg tmaemtdvey ngrkawnfii pgfyaytntt ltdraaaqqr
      601 tqkrmvgvyg eyrasyrdfa yvtvtgrndw tstlpihnrs yfypsvsgsf ifsefipenn
      661 ilsfgkvras warvgkdasp yvtntyvvtp aeytlynnga gvgvrndwlr gnrellpeit
      721 esqeygldvn lfgsklglef tyyknrsinq lmqprtsqat gyilmwtnag eivnnglels
      781 akvspikked frwdltlnas rnkgrvenll pgldvlyvtd vqvgnakaas fnggnfmais
      841 gskwlrspeg hlvlnpqsgm pqsdglvthe ignrepklfg glnnnfqykn wnlsflldyr
      901 igghvyngtd yymtamgmst rsmdrekltl tgvvktgena dktpiysdvq tfeyetgkmy
      961 qignqtrsge dvinsyyqsg gaynlesany mtdtnwlrlr tislayslpk ttlskvkaik
     1021 gltatvtgtn llvwtnykgm dpetsaagsg aigsssvgid yngvpatagv tfglnvtf
//
LOCUS       WP_093365479            1022 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093365479
VERSION     WP_093365479.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1022)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1022)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1022)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1022
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..1022
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112582
     Region          47..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikrftkpff igknvrlasv lmlgviahte lafgsgsiay ehvfyqqtvt grvtsstgav
       61 agvtvsvken pfvststddq gnftisanrg qtlvftavgy nrieqavtgn vlsvilqesd
      121 qsleevvvvg ygvqrkeslt gamqvvkgde lrditnpsve nmlngkvaga fvspgsgrpg
      181 sggavvirgq atlngttspl wvidgvivgs gagdlnpddi etmtvlkdaa staiygsqga
      241 ngvvvvttkr akagvtninv strmgfnqlt ngnlkvmnge elydyyaafa naneisfprw
      301 kpelrnsnfd wwdlatqsgf vqnhnvsiss gteklrsfls vgmydekgav kgydyrrynv
      361 rlnqeykpfe wltikpsivg arrgiedrey svtamysnlp wdspfdpdgn lvghrssswv
      421 nsastnylyd lqwnksaatn yelmgnldfv vqltdwltfn svnnyryiny gssgytdprs
      481 ngglsvqgri sdyrsevarr ytnqmltvnk twgahalyav ggyefndyqs knldvygtgf
      541 vpgfeildvv akpertkggi sewavqslls kvnytydnry mveaslrrdg asnfgdnaky
      601 gnffsisggw nihneswfka dyvdalklra sygssgnrps slypqydlya isaaasydgd
      661 pgalisqign rnltwektmt tgigvdaafl nnrirttvdf yskdtdnvly hvpisglsgv
      721 triwqnigem nnkgievsig gdiirtndwl wsldvnlghn vnkltnlfpt rnadgsysvk
      781 pvyigtgmni agsaqyvlep grpvdtyyvk ewagvnpdng apmwykvard adgnetsret
      841 tskyadatfe klgraapklf ggfatalqyk qfdlgatfsy slggklynys rqeydsdgty
      901 tdrnqmklmp gwsrwekpgd nathpiakyn nkdqgnlass ryiekndflr lrslslgynl
      961 klnqygvknl rvfftgenlc vitnysgvdp eipandgavl lstgpgvypa trkymfglnv
     1021 sf
//
LOCUS       WP_093365172            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093365172
VERSION     WP_093365172.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125036
     Region          125..1117
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqsltwvl alalctgtls fdtvkaksln ldqdknitel lkqlenrfdv rfnyesglkn
       61 lkiknnfdik nlrkgdiesf vkevtlnqiv iekvgnnayv iqkptaasvn qastlvntis
      121 ntvqqtlsgt vidantntpl sgvtvrvkgg sqstqtdang rfffegvpsn vtliissvgy
      181 nvveiaasnn qtirltaddq sleevvvtal gikreqkalg yavqdikgdq lqkvkgvdig
      241 ttltgrisgm rvtnstefnr mptiqlrgmn pilvidgiay enmdlrdipv dnieditvlk
      301 gatatalygs mgaggavmvt tkkglqqkgv eiavssnnmf fsgylalpev qssysagygg
      361 kyntddevwg dkldigriys qwnpltkqme dseltskgkn nfqnflepgf isnnsvsftn
      421 qgengsirts ishiynkgqy pntklnmtni svsgetkisd kislesrfgy nrryapndfg
      481 agyndqgyiy nilvwtgpey dltqykdywl vpnesqnwhy rawydnpyls aheklssdlv
      541 nklnaavtln yqvtdwgkfm lrsgydyygn treqtnpmgi ygtrggysgy hnrgkywtqk
      601 tdgfgttndl iftvnkdfgd ftidglagga ifyrrdnnit astvngisip gffslrnsvd
      661 pittsesktk emvnsvygrl slswrnaifv eatgrndwts alpketrsyf ypsvsgsvvv
      721 sdlvkdikpt wvsmfkvrgs wavtksvpsp yeirqnfgvn snvwdgmtta sypnsikdfs
      781 isptqrdlte vgvdislfnn rlygnytryy rllhnvttya tissatgfss rlintgeqtm
      841 tkgheitigg tamkkndfqw diisnlsqnl syyhkldpey sedalyvkvg ertdhyvtrd
      901 wertpdgaii hntagmpisa vhasrlfgys apkwfwgltn qfqykdfsls fsfdgrikgl
      961 sysnmnarlw qtgahpdsdt keryeevvng nrtfigqgvk ivsgsvsydk ygqivsddrv
     1021 faandqvvsy enywkraysg trniwdetfi klrevslsyn vpadiasklk akranigvtg
     1081 qnlflwtkey kfsdpdngse dlnspsmryl gfnlslsf
//
LOCUS       WP_093365658             310 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Sphingobacterium wenxiniae].
ACCESSION   WP_093365658
VERSION     WP_093365658.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..310
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35648
     Region          5..178
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiidlyskr qkrlrgevld iftydvlpnt lkvqivhiik dcfgyndhdf redlpsdiyq
       61 hirdilrrey gvfelrttts lyggeakdel ldffletddv ekaldviela ckviekiilp
      121 khhdfrhlyh skihpdqaiq dlnirfkeng igysyesghi iridstyths eitkptlnll
      181 nrgkfkgane eylkahehyk ngrnkeclte clkafestlk iicqekgwsf apnitakgli
      241 qicfdnglip tftqnqftsl rsllesgipt lrnnlgghgq gkipqkvdde mtryalnltg
      301 tniiflveqs
//
LOCUS       WP_093365665            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093365665
VERSION     WP_093365665.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125507
     Region          58..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfykggrg lcllqsdkhn hptkqttrlk slwlnaygll lifvsmfsls dawaqsgrtl
       61 sgvvrsaaeg qplqgvsirt dqrqaitdkd grfqiptsqq egsfevkhlg yktqqiafdt
      121 rftvfdiqle adesyieeve ivntgyqsip keratgsfvq vdnelfnrrv stnvldrlad
      181 vtpglifnng kgaaaqmrir gqntirsdas aliivdnfpy egdisninpn dvesitvlkd
      241 aaaasiwgar agngvivitt krnnitqqpk vtlnanttfg qrpdlhyqpl issadfidie
      301 qmlfekgfyt tyenslnkvp lnpavelfie krdnperaee idgkiallkt ydirsdyekf
      361 lyqsplmqqy alrmeggnsn nqyyasigfd knrtevirnn ndrysatlgn rivffgdklq
      421 lstqaafsqr kvenngfgsl tysshrgvps tplfpyarlv dedgnplavt kdyrvsyles
      481 vsndglldws yiplldrdnn dnttigkdlr ldagitykll davtlsaqyq ywsgstvtrg
      541 lnnldsyftr neinrltqrd pltgnlsyai pmgsildind gsthahnlrl qadfshrlqd
      601 vheinglggy eirdqqmvgv qsrlygyder vgvsqsvnyk grftsyfnpy ntyniipyvd
      661 reigtvdrfr svfgniayty drrytatgsl rfdesnlfgv ntnqkrvply svglgwnltn
      721 erflkvngid rlhlratygk sgnvnrsmta yttayynmqd yltglpmasi atprnpdlrw
      781 ekittynvgl dfsllksrif gsvefynkdg sdvisqmpsp gtsgiklltg nfsatntrgv
      841 evmintrpid kvirwsnqfh fntvrdkvtd yngpsftaln lmsnsdglta ypiegrplwa
      901 lysmpwggld sengdpigyl egqpskdyta imrtlsvdgl iyhgsvrptw ygsfrnmlew
      961 rrfmlsfnis yrggyyfkkp tasyydlltg isthgdfers wqkqgdeqht qvpsfqetin
     1021 tpraqvytys svlihradhi rlqdirveye lpleklrtdr nmrlrvygya nnlgllwkks
     1081 kteydpdyas vnylpvktfs iglnatl
//
LOCUS       WP_093367494            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093367494
VERSION     WP_093367494.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120175
     Region          55..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksyilsamf amafligaaq hriegtvrgq dsrsviaaav ingpdnrvls vsgtdgtfsf
       61 irpqgvdsvl ishlgyqakw fniadvntld vflsvnnnel eeieistgyf tvpknrstgs
      121 fesadnrlln qavstdilsr legvvgslnf drrtdghshs lklrlrglst insdetplii
      181 ldnfpfngsl esinpndven itvlkdaaat siwgaragng vivintkrak aneptkvman
      241 isyrvetkpd lnynpyfirs ssfipmeesl fergfytand pgqspqtpiv erlfdlkenr
      301 isfseyetlr nkmvgsdyrr dieryllrtg lnsqyfvslt sggeklstmv slgfdknkds
      361 qidneyqrat lslknsykln siidfstnvn yfhsrrwqga lnpndliprg kmalypyasl
      421 meagfpaaip knhrldyayn aqniglldwe ykplaekgmn rtlvempeyr vstalnikpi
      481 pafiltlmye kqagksntet lydknsyyvr neinrftqvd gshifpqgdi lrnltssrns
      541 dffrinasye qnilddheis llagtewnrr nekiipgtvl ygfdrdvgtg qtmfdytkry
      601 ptlpngtari tsppsyynef ddrflsyyfn gaylfrkkyn ittsvrkdms nlfgvqqnqk
      661 gvplwsvgga wdiakenffp wnsinsvrlr atygssgnld ktvtalttiy ystssltenr
      721 farietppnp nlrwervntl nlgtdlilqn nrirltvewy kkngkdlmgl reldptggyl
      781 nayrinyael ktygadislh akvvdkkfsw etslfaswvr driseyseep rpqtmvgais
      841 hplinrprya iysypwqgld nagnplvkvg davstdyvaf nsdlqledli yhgpasptff
      901 gnlrnrfsyg sfslavnlrw ksgfyyrsps isygdlfnsw kghrdfdnrw qkpgdekntd
      961 ipsmpegsfs ylrdvvylas ehhvkrgdni riqdmffeyn falgkragra klgntrifvh
     1021 atnigiiwka nndgldpdip fslipeqkni sfglqttf
//
LOCUS       WP_093367251             930 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium wenxiniae].
ACCESSION   WP_093367251
VERSION     WP_093367251.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium wenxiniae
  ORGANISM  Sphingobacterium wenxiniae
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 930)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Sphingobacterium wenxiniae"
                     /db_xref="taxon:683125"
     Protein         1..930
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101116
     Region          1..929
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvtsfgiqrd rktlgygise vkgddltkap ttevtnalag kvagvqvsga gggfagsnvt
       61 irgfstftgs nqplyvvdgi pldnsgggns vntgvvnssr isdinpqdie svnvlkgaaa
      121 tvlygsraas gvilittkkg kkgqrnqisf gtntavgsvs rmpdfqneys qgtngqynns
      181 vtgswgakia gqsvknwfge deilqaypdn isdimqnsvn svndvsftga sdrfdyrvsy
      241 gytletgllp kndikrnnis anvstqltdk fkigtsfsyv nnisnrtqgg nqganplwrg
      301 iytprsydlt nmpfedaegn qlwfapedhp ywsienvknr gevnrfygnl nlkydiltwl
      361 sadlkigadv fsmnskgfdn kgirsngnts sagaggvvdr smtmkninsy ftltanrals
      421 enwnllatlg nevisnnrnn lqstglgivl pdfdnqsnfl tfntlgeitr eraiglfgdv
      481 vldyktflsl nvkarndfss tlakgnrsif ypaaavsfvl teafpsmksn vlsmakirvn
      541 agevgkgtsp yatntyysra sasdgfvstl vsfpfnglag ytldngagnp llqpeftrey
      601 eigtelsfwn grlgfegsvy krdtrnlifa vpspatsgft slrtnagsls tkglemmltv
      661 vpvksdkvtw rsvfnftkfk siveelapgv nnisiggfts pnirlvagee ygqiwsnaye
      721 rndqgqmiin anglprptsn vqkvgnpnpk fnlgwsndis ykdfsfsfll dfkykgdims
      781 rtigdlriqg vaketaefar vdasgavttp ylfegvyqdg tpntthvtaq qyyslqgkyv
      841 awegyvldat flklreanit yrlpsrllsg qnliksvnis vygrnlltya pnfphldpeq
      901 nllgisnarg lefgfsptpr tiggsvrfsl
//
LOCUS       WP_093389067             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rugamonas
            rubra].
ACCESSION   WP_093389067
VERSION     WP_093389067.1
KEYWORDS    RefSeq.
SOURCE      Rugamonas rubra
  ORGANISM  Rugamonas rubra
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Rugamonas.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rugamonas rubra"
                     /db_xref="taxon:758825"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38794
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr sgetrvaatp etvkklaakh qiivqsgagl tasvtdeaya aagaqigtaa
       61 qafgadvvlk vrapnvdera lmtpgtvvvg mlnpfdadnn aamaaaglqa faleavprit
      121 raqsmdvlss qaniagykav mvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpfltdeer eiakgvggya rsmpadwmrr
      241 qaelvherak ladiiittal ipgrpapvli seetvkamkp gsvivdlavs qggncplsel
      301 nktvvkygvh ivgepdlatl vaadasalya rnvldflkli fdkedklvid redeilkaal
      361 mcaggevlrk
//
LOCUS       WP_093367760             971 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sediminis].
ACCESSION   WP_093367760
VERSION     WP_093367760.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sediminis
  ORGANISM  Psychroflexus sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 971)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 971)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Psychroflexus sediminis"
                     /db_xref="taxon:470826"
     Protein         1..971
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106497
     Region          23..970
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtikllgll lmllpisifa qstvsgtvvn dngmpipgvn ilvknttkgt ttdfdgnysi
       61 dlekgetlsf syigyrtqdi vfngnntrin vsmvedaeal kevvvvgygd qtvksisgsv
      121 asvtekdfnk gnivtsesli qgrvpglsit kgggpgsgse itirggssfn asnaplivld
      181 glplnnetaa gtrsilssin pndiesfsvl kdasasaiyg iraaggviii ntkkgrgeln
      241 vtldvqrnvt kidnsidvln asqfrtlvsd nfpdrldelg eantnwqdei yrdavssdin
      301 lsargalfge iptrlslnrs dqqglrrtsk fdrttaslsi nprlfddhlk vglnanysnv
      361 dnrfaagveg saiafdptqp vrdpgspygg ffefrdndgs assnvprnpv aellqtrnvs
      421 nadrffgnln ldykfhflpa lslvtnlgid rtesggafsr prtsalgvna eqgefignls
      481 rysqkrtnts adayfifddn ygdfgvklta gysyqkfese sfttgeildp naqgprttva
      541 ddvvfigyfg ranlsfkeky fingsirrdg vskfnpedri eyfpsvsgaw qiseedflkd
      601 sqvisnlkvr agwgqlgqqd issttdylsr yqrglsnqqy rfgpnaivpl qplytnpnis
      661 weilteinlg ldfaffddri sgsvdvfert addllsfvpv pdganfsnqg fqnigefvsk
      721 gveinldynv irqddlnwdv nynftafdre itrlafgqdi fvggisggtg ntiqvqrege
      781 wpnsfftyaq lydqsgqpie gayadingdg tiddrdryvs gngqadmlmg fqsnltyknf
      841 dfnfnlrasi ggeiynnvns sraqlgnldl aapnnlpvqv letgfartpd vilsdfyled
      901 asflrmdnit lgytlenfnk dstslrfwmg lqnafiitdy sgidpelgsg gidntiyprg
      961 rtyllgvnyn f
//
LOCUS       WP_093406025            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter flavus].
ACCESSION   WP_093406025
VERSION     WP_093406025.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter flavus
  ORGANISM  Salegentibacter flavus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Salegentibacter flavus"
                     /db_xref="taxon:287099"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111068
     Region          40..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnysrlkw valiilggii fflskaataa tttslslqqq evsgivkdqs glpipgvtvt
       61 vkntnrgtit nldgeynita padgtlvfsy igfktaeipv dnneeisvll eedvaslgev
      121 kinagyyntt erertgnisr vtaeeielqp ltsplqalqg rvaglevvdq sgvpgaapti
      181 rirgqnslrn sqndngnlpl yivdgmpins gpvnsinqft sgigtdplsg lnisniksie
      241 ilkdadatai ygsrgangvi littkggsfs gksdriearv ysgvsrvanf vnlletpryl
      301 evrrqafend gveptvsnak dlllwdtdrn tnwqevlfgr saptfnanln yagggeftsf
      361 nigasyfkqg svfpgdysfe kttanfalnh qsqnrkfrln lsvnyglndn slfsssnfvr
      421 talnlspnap rlynedgnln wedsswnnpl aalegegeak tnslvsnlgl qydltksltf
      481 kanlgynlln skenillpie tydpaiwnrv snrsqhsfvn riswiaepqf hykknkgyhn
      541 idalvgatfq ennndnlvin gtgysdkqli gnlnaadavs vnndrklvyk yqamfarlgy
      601 nwnrtyflnl tgrrdgssrf spenryanfg avgmawiftn nlffseklpf lsfgklrgsy
      661 gitgndqigd yryldtyest pgpgglyptq ltnpsftwet nkkiegalel gflkdrinln
      721 lswyrnrssn qlvgyalpai tgfntveanl patvqntgve ielstlnlkt dqfkwrssln
      781 ltlpsnklir fdnidqssya nayrvgkpld lgilyqfngi dpetgyfqvv dinqdgrndf
      841 ddrtairnlg rkffgginnq inykqfslnf lfefvkqkgs ryynnvpgfl gnvneesvnn
      901 ssedgntslq rptqsifgfi aynnanlsty gitdasyirl ktlslgfqlp ekvtgfipss
      961 evqlfvhaqn lftltnydgl dpqnpgslnl pplqsitggi qinf
//
LOCUS       WP_093404843            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter flavus].
ACCESSION   WP_093404843
VERSION     WP_093404843.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter flavus
  ORGANISM  Salegentibacter flavus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Salegentibacter flavus"
                     /db_xref="taxon:287099"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117311
     Region          25..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfssilt lllafvvqit faqeqtitgt vtdedglplp gvnvlvkgts agtqtdfdgn
       61 ysitadqgdv lvfsfvgltt aeypvgnntt idvvleadaa qleevvvtal giqrekkslg
      121 yatqevdgse vsdvptsnfm nslsgkvagl kvkssgtmgg ssdivirgns sltgnnqalf
      181 vidgtpisna tpntsdqarg rggydygnaa adinpddias mnvlkgaaat alygaraang
      241 viiietkkgq kgkgigisin stlmtsrade etlpkyqqqy gagygqyyas edgyfslydv
      301 dgdgnldett pftedasfga rfdpnrmiyq wnsiypqldt yqqatpwvag gntpndiwet
      361 gstainsval dggtdksnfr lgftnmmtdg nlpnatmkrn tlkfsaghdf tddfrvstnv
      421 tyiksdgkgr ygtgydseni mqsfrqwyqt nvdiyeqrda yfqtgenitw npnsptnltp
      481 iymdnpywtr yenfqtdtrn ryigninldy eindifsvmg rfsfdtyeel qeerrnvgss
      541 gvsgysrfnn rvaeynydai lnfnhdiatd lnldgnlgmn lrrnqnksir astngglnap
      601 gfyalsnsad plnppseyda tsmvdgiyar vgfgyqdtyf iegtirrdrs stlpkeentf
      661 yypsvstsii ltnalnadwl nfakfranya evgsdtnpyn vfntysisap fagqgiannn
      721 fslnnielvp eraksyevgl eadfldrrvg fdisyyntqt edqitpvpvs natgfgevwl
      781 nsgtienkgi evslnlnpir tedfnwnmni nwarnrsevl elapgidnle laslqggvsi
      841 naapdepyga irgrdyvydd ngnrivndag yylrsatsne iigniqpdwt ggvsntfqyk
      901 nlsldflidv qeggdifsld twygfatgly drsvgpndlg npirdavadg ggvilegvte
      961 ggqpnttrvr adyygtpfgy ardankghvy dasfvklrea sltyafgddv ierlpftras
     1021 isvvgrnlwi ihknipysdp eaglsagniq gyqsgaypaf keigasvkln f
//
LOCUS       WP_093407291            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter flavus].
ACCESSION   WP_093407291
VERSION     WP_093407291.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter flavus
  ORGANISM  Salegentibacter flavus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Salegentibacter flavus"
                     /db_xref="taxon:287099"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113142
     Region          25..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgkkllfllg lmffsfnqnl iaqeqtvtgt vtdsengipl pgvtvlekgt nngtstdfdg
       61 nysievpeda ilvfsmigfv nqeipvggqn tvnlslspdm ealdevvvts lgltrekksl
      121 gysvteldsd evntvkdynv asslvgkvag lvvnqasgvg sgsritirgn ntltgnnqal
      181 vvvdgipida sgnesggsiy nstvtgggit dinpadiesv svlkgpnaaa lygsraasgv
      241 ilittkrgkr gaglgisvns nisleetmfl pefqneygqg tngavysdld nfgssswgpr
      301 ldgsqqlyyt geeraytaqp dnvkdffetg vksintismd qggenhsvrf sytnnqttsv
      361 ipnselhshn lnlrgvidls dkltldskat yftqelenrv nvgtegvlay vyrmprnvai
      421 ddlkkykpsl wsnpemfpde ygaisfagqn ksmgnpywml nqdtnderrd rflgfsklny
      481 efndwlsafi riggdvtnvr seyiqdyghh ffydgrlnfs nrknveinsd flftankdls
      541 eklnlvanvg gslskrtfeg msvrgsqfrl ptrtflnntn vqtsthtplg tkkinslygs
      601 fsfsyddfmy ldltarndws stlseenrsf fypsvsysll idrfldpnnd vfdmlklras
      661 waevgndtgv yqlyqtfsvp tqgylgltvl egpsvklnpd lqpesvkste fgvefnmfqn
      721 rlygdfsvyq ivttdmifnv pvpfstgysy ykenvgevkn ngiefmvggi piktddfrwd
      781 vsvnfsrnen elvelidgld ytvlnslggl svraevgggi gdiygttwkt nengerlvna
      841 egfpvasndr ellgnaqpdf iggltntfry knwnlrflid grfggeiysa tssyldaagv
      901 serslqyrdq gvtidaineg tgeqndtqis aqqywssysg itsnyvydqt nvrlrefalt
      961 yrlpsemign tglnsasigl igrnlfflyk daedidpdas igtglsgqgi slnnaptirs
     1021 lglnininf
//
LOCUS       WP_093408557             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter flavus].
ACCESSION   WP_093408557
VERSION     WP_093408557.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter flavus
  ORGANISM  Salegentibacter flavus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Salegentibacter flavus"
                     /db_xref="taxon:287099"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108250
     Region          25..978
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktlfkstlm lllmlpmsff aqesvsgvvs esasglpvpg anvivkgttn gtvtdfdgny
       61 titnvqpgdv ivfsflgfat qeipydgqtt invqldedaa tleevvligy gstseqdatg
      121 svekvssesf nkgavvspeq llsgksagvr itpgggapge ggqirirggs slsgnndpli
      181 vvdgipldqr gvqgvrnqln sinpneiedf vilkdaaats iygsrasngv ilittktgkk
      241 nsplrleydl kvsagqiidk vdnldaqefr aliestpgtd pnllgeydtd wqdeiyqtsi
      301 gaihnltasq gfdnfsyrvn ynhtsqtgvl ktdvyernal nialnqdlfd nhlklalttk
      361 givdenrfad qgaigaavaf dptqpvyded lpfggyfehn tmsndqvipq lqatrnplal
      421 letldgrgkt mrnitnlnae ykfhflpelk fnvnagfdya eneghnyrpr yaagnglyiq
      481 greytqeysg inrntlldfy ftykteleal dtemdltagh syqefyienn neytvaddpg
      541 yrvepsvinr nalesyfara sfdiankyli sgsvrrdgss rfgadnkwst fpsasvgwki
      601 hneefllnsn tlsqlklrag ygvtgnqeig inygymgiys psvgparyqf gnqfyntlrp
      661 eefdadlkwe elqtynvgvd fgffnnrlsg tveayyrete dllatvpvpa ganlsdllvt
      721 nvgetvskgv evglngtliq kedfnwdmny nitfqdleit rlslgenpdf fipqggisgg
      781 vgnniqiwke gydpstffvf rqvyneagqp iegayadvng dneiteadkv pykkanpdyf
      841 mgftntlnyk nldfsftfrg sfgnymynnt qsgngfvtag tvtpqdyysn lnsnvlesnf
      901 vnnqlfsdyy iqkadfvkld nislgylfpg ekvdfrtslt atnlwtitdy dgldpeisng
      961 idnnfyprst svvlglnlif
//
LOCUS       WP_093408862            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter flavus].
ACCESSION   WP_093408862
VERSION     WP_093408862.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter flavus
  ORGANISM  Salegentibacter flavus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Salegentibacter flavus"
                     /db_xref="taxon:287099"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113824
     Region          25..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrlhvmlt lllafvvqis faqektvtgt vvdeeglplp gvnvieqgtn ngaqtdfdgv
       61 ysisveagdv lvfsyigyea reitvgaanv ydvelsvdaa aleevvvvay gsssleaftg
      121 sasvigseel sdrnvtspia aiegkatgvq ftsasgqpgs spgivirgvg tlsggaaplf
      181 ivdgmqyegd lntinqedia sftilkdaas tslygsraan gvvlittksg qkgevrtnvs
      241 sqfglvmqgi pnydevspge yyetmwealr nssagggdpa yasaniynql gynpfnvpnd
      301 qivgtdgrln pnadviyksl dwydvlqqtg vrqnynvnvs gggennkvff stsyldeegy
      361 vitsefnrlt trlngdfein dwittggsan ititesrgpa sagttsivnp fgfaknigsv
      421 ypvyvndldg nlvldaggnp vfdsgegfpd ynigsrpvsq grhalqelll ndelnrdnty
      481 gfryyadfri idglnfrvny grdinegink syenniigda qptgrygetr frrevenfnq
      541 iltysntfnd fhniditagh esfdrqfssn fgtaidqtae gifefanfat pvtlggsttn
      601 ktiegyflra nynfddkyyl sasarrdgss vfgsdsrwgn fysvgaswrm dkeefiqels
      661 finklklrgs fgqvgnddlg dfflsqprys ltsnagnpai iwtdignadl qwetvdswdv
      721 alefglfdnf vdgtieyykr nstdllynlp ialsnglnsy paniadmyns gwelglnfdl
      781 vnasdfnwdl tlqastfkne itsipdpfvn gskrwekgrs rydyfilhsa gvdpetgdql
      841 fykfeldddg nsvpvlgang eqettndwqd teraytgdss ipdllgsvan sfsykgfsld
      901 vlitygiggk fldygyaamm hsgnfgssyh pdildawrep gditnvprle sgnpdlvrsq
      961 strfltdasf wslrnvnlgy tfdsaitgnl gidnltlsvi genlylkser egldpqysls
     1021 gtpagndynp arlvslglni gf
//
LOCUS       WP_093423149             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tranquillimonas alkanivorans].
ACCESSION   WP_093423149
VERSION     WP_093423149.1
KEYWORDS    RefSeq.
SOURCE      Tranquillimonas alkanivorans
  ORGANISM  Tranquillimonas alkanivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Tranquillimonas.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Tranquillimonas alkanivorans"
                     /db_xref="taxon:441119"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55956
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpaevm pgearvamtp dsakalqklg ydcvieagag tragftdday reagvevveg
       61 adalwsaaei vakvrppted eakrlrqgql lisffypasn ealmelakdq gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvyldfee qtkdgsetgg yaapsspefr
      241 ekqlekfrel apemdivitt alipnrdapv lwtkdmveam kpgsvivdla aerggncelt
      301 rkdekfvtdn gvtivgytdf psrmatqsst lyatnirhmm tdltpekdgt vnhnmdddvi
      361 rgatiahage vtfpppppkv kaiaaapkkd kpkeltpeek raqeiaafka qtknqvallg
      421 vggvlmllvg lvappsflqh fivfvlavfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsw lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_093411617            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salegentibacter flavus].
ACCESSION   WP_093411617
VERSION     WP_093411617.1
KEYWORDS    RefSeq.
SOURCE      Salegentibacter flavus
  ORGANISM  Salegentibacter flavus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salegentibacter.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Salegentibacter flavus"
                     /db_xref="taxon:287099"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110844
     Region          43..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnykrlkm vvyvfvaill aiwafsataq aapikkyspq qeieisgtvk denglpiega
       61 tiaieglnrg titdmdgnft lfapsnavlv isylgyttqk ipidnekeih iileedvdal
      121 gevkinagyy ntterertgs isrvkgeeie lqpvvsplqa lqgrmagvei aargdlpgqa
      181 sririrgtns lrtegnfply iidgvpinst piesrsiags gtngfdplnt lnlsniesie
      241 vlkdadatai ygsrgangvi littksgiqk dfrleaavyt gasrlpnkme llnteeylqi
      301 rrqafendgv eptqfnaydl vlwdqnrftd wqdffyggta pvtdinlnas ggnattsfrl
      361 ggayhnqgsi ypgdynynkl ttslnlnhlt nderfginls vnygidnnil agstnvsspp
      421 fslppnapqv fnpdgslhwe ewaaagqnnp magffnrset qinnlissvg lnyriadgln
      481 lklnggytnl eskelvkipt rsfnpawnfe dnsqhlnisr kswiiepqih fnkslwdgel
      541 sailgttfqq nedenlelmg sgyisesqig nlnaaetits plhiktqyny naifgrlayn
      601 wdskyfinlt grrdgssrfg pgkqfanfga vgaawifsee afiknelpfl sfgklrgsyg
      661 ttgndqigdy gyleaydvtp gpgglyptql ynpdyswein kkleagiets ffndrislgs
      721 swyqnrssnq lvgfplpamt gfrsvqanlp atvensgwei elsslifnsr dfrwrtsmnl
      781 sipknrlvsy pdlesstyan ryrigeplni sllyryagld pntgfytved vnedgridsn
      841 drvdikdlsr qyfgginnsi sfknlslqfl wqfvkqegtl lnmdvgrign krhealaaln
      901 pnsryqmpsq siqaligyin vlntsffhsd asfirlktls ltydipktll aqvgvkkgsl
      961 slhgqnllti tdypgvdpel piggtsfggl rtftggikln f
//
LOCUS       WP_093416031             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_093416031
VERSION     WP_093416031.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38596
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag vnasvvdsay eaagavigsa
       61 sdafgadlil kvvapsdsel sliktgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvivahgv tiagptnlaa qvgadasaly arnlldflkl vftqegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_093429467             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_093429467
VERSION     WP_093429467.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38823
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_093430817             305 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Variovorax sp. 770b2].
ACCESSION   WP_093430817
VERSION     WP_093430817.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. 770b2
  ORGANISM  Variovorax sp. 770b2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Variovorax sp. 770b2"
                     /db_xref="taxon:1566271"
     Protein         1..305
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34755
     Region          4..168
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mvfdlyskrq krlrgespdf yiydeipfql kvqivflwel glgdideenp aaayklivqt
       61 lreeygnfsl akvpydatyf delrtfflse sdtervldai elsfkalssf grafnyrrnp
      121 qanelvekai sdlnirfkeh glgyqftnne iiridselih aevvkpvlrl lnqpyfkgae
      181 deylaahehy rhgntkealv eclksfesam mgickkrgwa ygekdtaktl idicmangli
      241 ptfwqsqlng lrsmlegavp tgrnrlaghg qgadptevpt hlvsymmhmt astlkflvea
      301 dtalr
//
LOCUS       WP_093436641             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. 770b2].
ACCESSION   WP_093436641
VERSION     WP_093436641.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. 770b2
  ORGANISM  Variovorax sp. 770b2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Variovorax sp. 770b2"
                     /db_xref="taxon:1566271"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38800
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeta agetrvavtp etvkklvasg hivrvqsggg vaasvtdaay qtagaeitdq
       61 agalsadmvl kvrtpsdaea almkagavvi gmlnpfdaag lqrlasagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmppswla
      241 rqqvevakrv aladivista lipgraaptl itedmvkamk pgsvivdiaa gkgpvnpdgg
      301 vggncplsea dktvvkhgvt ivgetnlaal vaadasalya rnvldflkli vtkegalkid
      361 leddivaacr mtqdgqvtkk
//
LOCUS       WP_093447457             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudooceanicola nitratireducens].
ACCESSION   WP_093447457
VERSION     WP_093447457.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola nitratireducens
  ORGANISM  Pseudooceanicola nitratireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudooceanicola nitratireducens"
                     /db_xref="taxon:517719"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55564
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egenrvamtp dsaaqlqklg hecyveagag aaagfadamy eaagvtvvkt
       61 aaalwkevdi iakvrqpnet elkrltadkt lisffnpagn eegmelaksk gatviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvkam kpgsvivdla aekggncklt
      301 vmdekivtdn gvtiigytdf psrmatqass lyatnirhmm tdltpekdgv vdhnmeddvi
      361 rgatvthkge itwpppppkv aaiaaqkpke kapeltpeek raaevaafka qtkqqvtllg
      421 vgavlllavg lvapasfmqh fivfvlsvfi gfqviwgvah slhtplmavt naissiiilg
      481 allqigsgsf lvillaglsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_093449341             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingomonas sp. YR710].
ACCESSION   WP_093449341
VERSION     WP_093449341.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. YR710
  ORGANISM  Sphingomonas sp. YR710
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Sphingomonas sp. YR710"
                     /db_xref="taxon:1882773"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38505
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlketa agerrvsatp etvkkfialg aevaveakag vtasvadray sdvgatvgtr
       61 eatlagadii lgvqgpdpet lsgyhpgawv vaglnpfger arvdayaaag lealamefmp
      121 ritraqsmdi lssqsnlagy kavldaasey grafpmmmta agtisaarvf vmgvgvaglq
      181 aiatarrlga qvsatdvrsa tkeqieslga kaifvenvkg iegegsggya temsdeykaa
      241 qaelvsshia kqdivittal ipgrpaprli tdaqiatmkp gsvivdlave aggnvegava
      301 gkvanvrgvk ivgytnvpsr lpadasalfs rnlynflsaf wdkeagrpml deeignairi
      361 tqggkvvnpr llg
//
LOCUS       WP_093466724             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. NFR16].
ACCESSION   WP_093466724
VERSION     WP_093466724.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. NFR16
  ORGANISM  Pseudomonas sp. NFR16
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. NFR16"
                     /db_xref="taxon:1566248"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38774
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklvgqg hkvtvqsgag itasvtdsay eaagastgsa
       61 ndafgaelil kvvapsdsel alikpgtvvi gmlnpfnnei iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee reaavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkapvl lsaetvsqmk pgsvvidlaa aqggncpltv
      301 adqvviehgv tivghtnlpa lvaadasaly arnlldflkl vftkegqfei nleddiiaac
      361 lmcrdgqivr kng
//
LOCUS       WP_093503954             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phytopseudomonas straminea].
ACCESSION   WP_093503954
VERSION     WP_093503954.1
KEYWORDS    RefSeq.
SOURCE      Phytopseudomonas straminea
  ORGANISM  Phytopseudomonas straminea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Phytopseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Phytopseudomonas straminea"
                     /db_xref="taxon:47882"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38440
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvplesq agetrvaatp etikkliglg hqvtvqsgag iaasitdaay taagasigda
       61 aaafgaelil kvvapsdael almksgavlv gmlnpfsnet iarlnaagvt afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag takaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaegvggy arpmptswme
      241 rqaravhert kqadivitta lipgrkaptl lheatvaemk pgsvvidlaa iqggncplte
      301 ldkvvvkhgv tlvghgnlpa lvaadasaly arnlldflkl vtkdgvfhld leddivaacl
      361 mctggeikrl nk
//
LOCUS       WP_093514283             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. NFPP28].
ACCESSION   WP_093514283
VERSION     WP_093514283.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. NFPP28
  ORGANISM  Pseudomonas sp. NFPP28
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. NFPP28"
                     /db_xref="taxon:1566231"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38800
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvarmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_093519486             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudovibrio ascidiaceicola].
ACCESSION   WP_093519486
VERSION     WP_093519486.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio ascidiaceicola
  ORGANISM  Pseudovibrio ascidiaceicola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Pseudovibrio ascidiaceicola"
                     /db_xref="taxon:285279"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55529
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigaakevl dgerrvaltp dsaqqlqklg yecaiesgag eaanfsdtdy tdagvkviad
       61 aktlwetadi vikvrppeas elklthegqt lisffwpaqn gellqqfadk kvnvlamdmv
      121 prisraqkmd alssmaniag yravmeagnn fprfftgqit aagkvppakv lvigagvagl
      181 aaigastslg aitlafdvrp evaeqvesmg aefvyldfee eqqdgastgg yasvsspefr
      241 eaqlakfrel apevdivitt alipgrdape lwtedmvqsm kpgsvivdla aekggncklt
      301 kmdekivtdn gvtvigytdf psrmatqsst lyatnirhmm fdltpekdgq aninmeddvi
      361 rgatatkdge itfpppkpki aaiaaqkpka pektpeelav eeaaaakaag rkqlglligg
      421 gavmaligay apesfmqhfi vfvlavfvgf qviwgvahsl htplmavtna isgiiilgal
      481 lqlgsgswiv wflagisvli asvnivggfm vtrrmlqmfn ks
//
LOCUS       WP_093570693             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium sp. 174MFSha1.1].
ACCESSION   WP_093570693
VERSION     WP_093570693.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. 174MFSha1.1
  ORGANISM  Methylobacterium sp. 174MFSha1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Methylobacterium sp. 174MFSha1.1"
                     /db_xref="taxon:1502749"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39305
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd paeprvaavp etvkkykalg aevtvqsgag lkagvpdaey eaagasiaad
       61 akaaadgadi vlkvrrpaed elpalkrgai viaimdpygh eaevkamada gvsaiamelm
      121 pritraqvmd vlssqanlag yravvdgaav ygralpmmmt aagtvpaari fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedde fkqaetaggy akemsaeykk
      241 kqaelvashi akqdivvtta lipgrpapkl vtadmvsamr pgsvlvdlav erggnvegvk
      301 adevveteng vkivgyanvp grlaatsssl yarnlyafve tlvdkgskal avkwddelvk
      361 atcltrdgav vhpnfqpkaa
//
LOCUS       WP_093578763             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus amargosae].
ACCESSION   WP_093578763
VERSION     WP_093578763.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus amargosae
  ORGANISM  Geodermatophilus amargosae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Geodermatophilus amargosae"
                     /db_xref="taxon:1296565"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51867
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpaetr rnetrvaatp tsvgavcalg hevlvqsgag eaasfpdeay vaagarmgsa
       61 adawgadvvl hvnaptgdei grlrpgavlv sllapalspd lvqalaargv talamdavpr
      121 israqsldvl ssmaniagyr aiveaahafg rfftgqvtaa gkvppakvfv agagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvgvpadeae aassgtgyas vtsedfnara
      241 avmyaeqard vdvvvttali pgrpaprllt eemvasmspg svvvdmaaaq ggnvagsvad
      301 evvvtpngvt iigytdlpar lpaqasqlfa tnlvnllkll tpgkdgrlvl dmddvvqram
      361 tvtrdgevlw ppppvavsaa pvaaapppap lpppakkapa pgrraalvgl aaavlfllaa
      421 fspdqlignl tvfalavvvg fyvighvhha lhtplmsvtn aisgiivvga llqlghvstv
      481 vtvlaflavl lasinvfggf avtrrmlgmf rra
//
LOCUS       WP_093600302             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Lentzea
            waywayandensis].
ACCESSION   WP_093600302
VERSION     WP_093600302.1
KEYWORDS    RefSeq.
SOURCE      Lentzea waywayandensis
  ORGANISM  Lentzea waywayandensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Lentzea.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Lentzea waywayandensis"
                     /db_xref="taxon:84724"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38362
     Region          1..358
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,284,310,312)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,274..275,317..318,322,
                     325..326)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,224,235,
                     252..254,261,263)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvgtpaesr paerrvacvp etvsslvdag ltvhvqenag rhahapdaay raagatvtpe
       61 dptpesdvvv svqpltidqa eklkpgavti sflqpqgere llevyarrnv tsfsfdllpr
      121 vtraqsadal ssqalvagyr avlvaaerlp rflpmfttaa gtvppakvlv lgagvaglqa
      181 iatarrlgav veaydvrkaa geevrslgak fleleletqs gvyasaqsee flerqrelig
      241 ehvaasdvvi ttaaipgrka pvlvttdmlk amtpgsvlvd laaesggnca asvvgqetwv
      301 gevlvhgaln lpssmpvhas klysrnvlnl lklmiadgsv rpdlsdevld gcclthdgqi
      361 rkelp
//
LOCUS       WP_093581461             509 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Streptomyces].
ACCESSION   WP_093581461
VERSION     WP_093581461.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51423
     Region          1..504
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvvredv agetrvaatp esvarllelg yevvvepgag ehagfpdaay aeagartgaa
       61 rgadvvlavr tppmdglrag vtlvglldpa heperlaela rrgitalame avprisraqs
      121 ldvlsstani agyravveaa halgrlfggq vtaagktppa tvlvagagva glaaigtaga
      181 lgavvratdp rpevaeqvrs lggeylpvap pgeegtgtgy aremdaeyra reaelyarec
      241 avadvvitta lvpgrpaprl ltadtvaamk pgsvivdmaa asggnvagtv pgervvtpgg
      301 vvilgytdla grlpgqasrl yannlvallt lltpdrdgtl vldtddivqr siavvragev
      361 hwppppvpvs atpappaeae rtapaeaapa ppprrgrrya laalaaalll lggatappaf
      421 lghltvfala vvigfyvign vhhalhtplm svtnaisgiv vvgallqigh gdtavtalaa
      481 laillacvni fggfavtrrm lgmffgsgs
//
LOCUS       WP_093621078             505 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinoplanes philippinensis].
ACCESSION   WP_093621078
VERSION     WP_093621078.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes philippinensis
  ORGANISM  Actinoplanes philippinensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Actinoplanes philippinensis"
                     /db_xref="taxon:35752"
     Protein         1..505
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51699
     Region          1..504
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigvlrdpd pgerrvaatp atveqlaklg yqvvvepgag agasfsdqay aeagatigdp
       61 lgadvvftin ppldrldrla egatligmln prlapelved larrpitals mdavprisra
      121 qsldvlssma niagyravve aahafgrfft gqvtaagkvp pakvlvagag vaglaaigaa
      181 gslgaivrat dprpevadqv rslggeylsv eaadvevsst gyakemsddy ndraarlyad
      241 qarevdivit talipgrpap rlitadmvat mrsgsvivdm aaanggnveg tvagevvvta
      301 ngvtiigytd lagrlpaqas qlygtnlvnl mklltpgkdg qlvldfddvv qravtvvrdg
      361 eltwppppva vsavpaavaa kpveavgkpv rkprdpllit gvaaaalfll taaapaalrg
      421 hltvfalaiv igyyvighvh halhtplmsv tnaisgiivv gallqlghgg avvtglsvva
      481 illasinvfg gfavtrrmla mfsrs
//
LOCUS       WP_093632744             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia aspalathi].
ACCESSION   WP_093632744
VERSION     WP_093632744.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia aspalathi
  ORGANISM  Paraburkholderia aspalathi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia aspalathi"
                     /db_xref="taxon:1324617"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39850
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaesr agetrvagtp etvkkltaqg htvlvqstag erahfpdsay alagatlves
       61 aeafaadlvl kvqtptetel qhmkrdamlv gmlnpfdvdq variraagls afalesiprt
      121 traqsmdvls sqaniagyka vllaaslyqr flpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpcetdee retaqgvggy arpmpvswia
      241 rqaalvhera kladivitta lipgrtaptl lneetvrqmk pgsviidlaa gkgasvgdrr
      301 ggncpltead avvlrhgvhi agytnlpamv atdasslyar nvfdflklvi dtdgkprida
      361 sddivaatll ghdasmlkta
//
LOCUS       WP_093637976             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia aspalathi].
ACCESSION   WP_093637976
VERSION     WP_093637976.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia aspalathi
  ORGANISM  Paraburkholderia aspalathi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia aspalathi"
                     /db_xref="taxon:1324617"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39502
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpterr ayetrvaatp etvkkyvaqg hrvtvqsgag itasyldgaf aaagaeivdt
       61 atafgadiil kvqsptetel pllrrgatli gildpfdkdn aaklaatgvt afaldsaprt
      121 traqsldvls sqaniagyka vllaaglypr fmpmlmtaag tvkaarilvl gagvaglqav
      181 atakrlgali easdvrpavk eqieslgakf ldvpyetdee reaasgvggy arpmppgwla
      241 rqanivhera kqadivitta lipgraaptl isvetvkamk agsviidlaa grgpefegrp
      301 ggncpltevd tvvtkhgvmi agytnlasmv psdasalyar nmldflklil tpagtlnidf
      361 sddiiaatll akdgeltrka
//
LOCUS       WP_093647589             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia aspalathi].
ACCESSION   WP_093647589
VERSION     WP_093647589.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia aspalathi
  ORGANISM  Paraburkholderia aspalathi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia aspalathi"
                     /db_xref="taxon:1324617"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39464
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msigvpaetr ahetrvaatp etvrkyvtqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatlv gmldpfnten ssklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvetvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvlkhgvqi vgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_093668099            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. MAR_2009_124].
ACCESSION   WP_093668099
VERSION     WP_093668099.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. MAR_2009_124
  ORGANISM  Tenacibaculum sp. MAR_2009_124
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Tenacibaculum sp. MAR_2009_124"
                     /db_xref="taxon:1250059"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113639
     Region          26..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyinivifg illltssqls aqqnfrgtvi ekttgygipg vnvvikgttk gtssdfdgnf
       61 qvgnvksgdv lvfsaigfiv qeytigaslk gtiqlqedsq qldevvvvgy gtttkkdatg
      121 svtsisskdf nktpvvgaeq llqgkvpgvr itsvggqpda apnirirgga slnannspli
      181 vidgvpidtt npagvsnplt lvnpndienf silkdasata iygsrasngv ilittkkgtn
      241 sgvkfnfssd vsigivgrtl dvmdgtqftk fiqtyhptqt nllgiddptt tatddlstpe
      301 iegrilsntn wqeaiyrtsv stnnnfsara flfdkvparf sfghtksegi vktndyerys
      361 lslrltpkfl ndqlkvdvna kgiyadknvi deggalggai nmdptkpiyd sstngfggfy
      421 qstrfndedp sqatkllldg qfnpvalllq rtrpervykl lgnveldytm pflselrgvl
      481 nlgletskte ikeefienai atrqfnasdt npetsavfnp ginytedqni tnttldaylv
      541 ynkqlegfls kvelqggysy qnfrnegske ifryntetgl reikpnpqnp tnryfnelnl
      601 qsffgranln fdnkylvtls lradgsslfr pskrwgyfpa aalawkieee dflknvdfvn
      661 tlklrlgwgk tgqqditgav gfypstplfs qgdassqyld gvniysaiaf nenltwekst
      721 tynlgvdfgf lndvisgsfd ifqrnttdll arvpvapgqg lgssfiknvg eteskgfela
      781 lnatpyendn frfdvntnva ynkteitslq ditrivssdg glpvgtgvnl ayspvglqah
      841 sawvfkqlyd ssgnpiwgah adlnddgiid nddrfyrplr pnwtygfgln fsyknwdlts
      901 nfrgqigglv ynakkltngw rdnaipinsn sltnvldfyn gasdvnfint ngnvrfsdyy
      961 ledasflrce nivlgyrfdq llkngmvrly gsvanpfiit nysgqdpenf nsidnnfypr
     1021 prtytigvnv df
//
LOCUS       WP_093668617            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. MAR_2009_124].
ACCESSION   WP_093668617
VERSION     WP_093668617.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. MAR_2009_124
  ORGANISM  Tenacibaculum sp. MAR_2009_124
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Tenacibaculum sp. MAR_2009_124"
                     /db_xref="taxon:1250059"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110833
     Region          25..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkskillll cfsfllvqfa naqektlsgv vtaksdgmpl pgvgvlikgt lkgvetdfdg
       61 kyqikastgd vlvfsyvgmk sqsitvinqq tinvaledan vldevvvtal gikkekkalg
      121 yavsnvkaed lqmakdpnvv nslqgrvagl einqasggvg sanrmvirgn nsltgnnqal
      181 yvvdgvpinn senegdvdew gngvsigngi adinpddies vsvlkganaa alygarasng
      241 vimittkkgk kgkmsigfns svtfeevafl pefqntygqg slgaiptdgs lrsfgswgpr
      301 ldgstqllwt gengryeanp nnvkdffsgg stvlnsfyve ggsekmtsri sytrsdiqgv
      361 vpnnelekna faayskldig kltvdlkgny inqkvnnrpy lsvwpdnvvn alysmprnvn
      421 ineleanpli vprsgsfnnp fssvntvgte drrnrvfgyv ranyqfsdnl tamvragsdy
      481 svqsflgwap inhptiaggq vsdntytnqe tnidflvtyn kelsedltat ivgggnrldy
      541 rgtvrggvgn glrvpgiyni lntesyvpnl gtgvytrrvn slystldldf rgylfaqita
      601 rndwssvlpa nnnsffypsv slsaivtdmf digsenlnyl klrgswaqvg sdgevgpygi
      661 hsryltepny lgngvlttps tkpnpnlvpq ttnsielgle gkffknrlgl dfsyyntqte
      721 dqiinlpapv esgytrflln egtlinkgie vglnydiikn ddvswnvgvn yshnrttved
      781 lssdfiplaa itgntpfril atnngrygdi vgfgykrndq gqilvgddgr plasddqqtf
      841 gnfnpdwlgg ftsnfrykdf sfrflisskv ggqilsrtdm ildvngnsmr tlegreggvv
      901 vpnsvvestg ainttavpaq eyyqtvager iiedyvfdad yiklkelaig ynlpqslisk
      961 lkissasiql igrnlfffhr etdsfdpevs gfntrnaqgv ellslpgtrs yglnlsvkf
//
LOCUS       WP_093668797            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. MAR_2009_124].
ACCESSION   WP_093668797
VERSION     WP_093668797.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. MAR_2009_124
  ORGANISM  Tenacibaculum sp. MAR_2009_124
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Tenacibaculum sp. MAR_2009_124"
                     /db_xref="taxon:1250059"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117675
     Region          25..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lflalivqit faqdktvsgs vsdesgplpg atvlkkgttn gtetdfdgny
       61 slkakagdil vfsfvgmktv erkvgtsnni nivlendssl leevvvvgyg tttkqsftgt
      121 akvvkaeale aksvsnvsqa lvgevagvnv intsgqpgta atirirgfgs vngnrdplyv
      181 vdgipfsgsi nsinpsdies ttvlkdasat aiygsrgang vimittktgk vgtssievdv
      241 ktgvnfqllp rydvitspne yielawhaig nrtldfdpnn dpvayannyl fssrginpdy
      301 nfyntnnvad iidpstgkvr pnvdrkytpe nwrdfafqss mrteanvkms ggnedtkyfs
      361 sfgylddkgf svnsgykrya trlsishkpk ewltakanvg ytlgkqitng qasdsgsvfw
      421 fvenipsiyp lflrdaqgni vedtkyggnq ydygargfgg mtnavgnahl nfvgndrhsl
      481 ngnfsfkvdl ldglefesqy gaqyysriad niqnpfygfa veqqgslfkr nssaltqnfl
      541 nifrynktfg dhtvsallah etnqrefqts aisknkvvnl fnglndpnny vvntspatgf
      601 rtktalesyf gqvtynyrrk yyltgslrrd gssrfftnkw gtfgsvgasw vlseedfvsk
      661 vgfidflklk asygivgdqa gaaiysgqdt ytignlggei slrpnaaqnp llswetskmf
      721 qtgleftlfn nkidasldyy vknvdnlife krlppssgna ildvndgllr nsgfefdits
      781 hiidkqnfkl dfgingemfs sdivdmpidp stgeqkildi atvsgidygr aagrglwdfy
      841 mrewagvdpn tgkatwsqyy hdannngtvd agegitslye yqqqnpnntv tktttttyad
      901 atqkyidksi iptvrgafrl nakihdfsis tlfgyslggy aydgvyaglm gtrqigssnw
      961 hadirdswkk pgdvtdipql isdrdlqsns issrfvtstd ylslnnvrig ytvprkfiea
     1021 sglgalslwv sgdnlfllts rdgfnpttse tgasstyryq plstltfgvr arf
//
LOCUS       WP_093668828            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. MAR_2009_124].
ACCESSION   WP_093668828
VERSION     WP_093668828.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. MAR_2009_124
  ORGANISM  Tenacibaculum sp. MAR_2009_124
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Tenacibaculum sp. MAR_2009_124"
                     /db_xref="taxon:1250059"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115538
     Region          25..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lffalfvqis faqektisgt vsdesgplpg vtvlkkgttq gtetdfdgky
       61 slnsksgdvl vfsfvgmttv ektvgasntm nvtmegdnil devvvtalgi kkdtravgya
      121 vqqvgaetin nsnandaisa ltgqasgvqv inasgsagag srivirgqts lngdnqalli
      181 vdgvrinnsq fntesrvagv agsnrgmdin padvesinvl kgaaaaalyg veggngvivi
      241 ttkkgksgki kvnlrsnvtf seanrfpklq ntfvqgsngv wsgpetgtsg swgpnkdnly
      301 wdgssydydk ngrivvgntt gslkkfqpyd vlevfqtgat fensvslsgg gekttfrmsy
      361 sdfkeegiip knefnrrtln fsgsakvndr lnvtlsgtyt nsdsyriqqg sntsgimlgl
      421 lrtpnsfdns ngfsnadnqv sayefedgsq rnyrggggyd npywvinntp ytdevnrfta
      481 slgidykvtd wmsfnanigl dtyadtrkqf fdigsrtspa gtiflddyny rhmdsyfnln
      541 gnfdvtedfn mgyilganiy seqytrnytq gddlgikgfd nitnastvia dhdlfrekni
      601 gfygqldfny krmlyltvtg rqdylstled pvnfnlddla lfypsanlgf vfseltgedn
      661 flnfgklrls waqvgagaps pyatstayet asfsdgwang ynfpysgnag fqidntlgnn
      721 nlvpstvtsy eigtdlrmfn nritldfayy nrlaedqila vpianstgyt ssflnsgele
      781 ttgyeatina kiidkedfkw nlginfdkse tivnkladgv enqfiggfvi ynipgerygq
      841 ifggsflrdd ngnilidddp nsanyglqia dpdlkvigdp tpdftlgfnn tftyknwsln
      901 fllewkegge mwngtewals ffgrseiten rgeqlviegv kqsdgspndi vatidqyyyq
      961 ssglsgfgsv deafiqdtsw irlrtlnlsy dltqdlnssy fdsiiltfsg nnlwldtpyr
     1021 gvdpetsltg agsnaqgvdy fnnpgtksfg fgvnvtf
//
LOCUS       WP_093669966            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. MAR_2009_124].
ACCESSION   WP_093669966
VERSION     WP_093669966.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. MAR_2009_124
  ORGANISM  Tenacibaculum sp. MAR_2009_124
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Tenacibaculum sp. MAR_2009_124"
                     /db_xref="taxon:1250059"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109933
     Region          24..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkngllkkli lltlllvgsi tyaqqisgkv tdsqgplpgv svlvkgttvg setdfdgnys
       61 leakkgdtlv fsfigyktke vvvgnsstvn avlddddqql devvvvgygt ttvkdatgav
      121 savkseefnk gvisspeqli qgktagvqmt aasgepgagi svrirgsnsi rsnnnplfvv
      181 dgiplssqgt tpasggvvdg gdtarnslsf inpndiesis ilkdasatai ygsraangvv
      241 iittksgksr qgkfefssnv sysspaneyd lfdaaqyrsq qlaitgnpvp sfddrgantn
      301 wqdvitrstf satnnlsysk nytggnvrat fshssqngvl enssqdrvtg rinashsffq
      361 dklkvtanls vaqvedeapq isggsgasgn ligaaysapp twpnsssfsi dgnrlnpani
      421 lenylgltet nryllngsve yqfsdelsak vnlgydqsda vatsavsany nnsgritgng
      481 qasrntleat skllegtlny kkeisdnlsi dalvgysfqd frrqgynaqa wgssttdler
      541 mnssldgsis ritnalgsts yqqfgydtng sflnslfpfd nsgtlnnang dyrslwldtf
      601 dntdelqgff grvnltlnnk flftatvrad gssrfggnnk ygyfpsgafa wkmheedfvg
      661 dnvstlklrl sagvtgnqag lghanylfrq rfggpgisdd gtvnrpglvt vsvqnpdlsw
      721 erltdynlgl dfgfnndrln gsvdlyrket rdllflspaa apadqpivfk nldqgvvvnq
      781 gvefslgydf iqqddmnfsv dfniaynnnv vedlqpgfta dlgplngpgl tgafaqrige
      841 gqslfsfyma eyaetngvpd fsaddkkfvg kdalpdittg lslnfnkgnf dvsayftgqf
      901 gfyvynntan aflnrptfgt srngtsdsvq lqsqevstly lesgdfvrlq slnigynipl
      961 keegplkslk lslsgqnlfl itgysgldpe vssntgafan gipsagidyt sfprprvfsf
     1021 gvnatf
//
LOCUS       WP_093670515            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. MAR_2009_124].
ACCESSION   WP_093670515
VERSION     WP_093670515.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. MAR_2009_124
  ORGANISM  Tenacibaculum sp. MAR_2009_124
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Tenacibaculum sp. MAR_2009_124"
                     /db_xref="taxon:1250059"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118530
     Region          22..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqillglil fivhnaysqq lvkgtvtskl dgtpipyinv tlkntktgtv tdldgsysik
       61 tsaledilvf ssigyitkev etrnktninv ilsesstgls evvitalnkk reskelgyai
      121 qsiqqkdise vkavnfldnl tgklagvsit sgsatgagss skivirgeqs ftnnnplfiv
      181 dgtpinnntv fnftneaaag fqevdfgnga mevnsddies vsvlkgasaa alygtrasng
      241 viiintkkak dkfsvslnss lfidtafqlp qfqnlygqgn sgnfefvdgl gagindnity
      301 swgprldqga lipqfdspvt lpngtvvrgg dtslynslpi tptpfvsnpd nlknfyqtgi
      361 ttinniaigs gfdkgnyrls ftdlnsesii pgvnlkrkti ttnlqflpsd kttvsahvny
      421 vnsnsdnrps ngygsenvny slvawgprsl nidnlrnywq pglegrqqya fnytffdnpy
      481 filhenrnef nrdrlfgnis lkqqitknls atlrtgmdys terrrflrnf stnrfrngay
      541 aehdvsyrei ntdfllnytk kitdfdfdvs lggnqlrqka ttkqtqttql aqpgifsfnn
      601 aaspietfdf ssekrinsly gllkvgyknt lfiditgrnd wssalatpfs aentsffyps
      661 astslilnnl fqlpkaisfa klrasiaqvg ndtnpyqtsr tflpttnvns qpsftsqnfi
      721 pnpnlkpekt tsfeigtdlr ffndklnfdi tyynaltedq ilslpipiss gfnqqvvngg
      781 kvrsegieiv mnstpvktgn fkwnttvnfs rnistieslp qnsgrvtlay srvynnpdqt
      841 vwfqveeggr igdfygtgyl knengdfvlt pegrfiadpt lkklgnynpd ftlgfnnefn
      901 yknwslsflf dwrqggelvs rtlslagvgg qleetayrpe egivaqgvvn tgtaqnpiyt
      961 qnttavtpes yyrqfydrnh eennvydasf lklrqfslgy tfhlknnafg fvkngakvnl
     1021 sligrnlfai sdiphfdpeq lavqgqgivg gvedmsyass rsfgfklgvn f
//
LOCUS       WP_093672623            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. MAR_2009_124].
ACCESSION   WP_093672623
VERSION     WP_093672623.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. MAR_2009_124
  ORGANISM  Tenacibaculum sp. MAR_2009_124
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Tenacibaculum sp. MAR_2009_124"
                     /db_xref="taxon:1250059"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119831
     Region          25..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfngilt lllalvvqis faqdrtisgt vsdesgplpg vtvlkkgttq gtetdfdgny
       61 slkaksgdvl vfsfvgmksa qktvnganqi nvlmendnll eevvvvgygt ttkkayagta
      121 atiqtenlea ksfsnvsqal agevagvtvi ntsgqpgsig tvrirgygsp lgnrsplyvv
      181 dgvpfagnfd lnsvnpadik tttvlkdata taiygsrgan gvvlittksg sksekgyiev
      241 dvktginqqi ipryevlssp eefiglvweg lynrgvfgdp aqpdpeafan ntlfgndgig
      301 qgynlwnvtd aaslidpttr tvrpgvqrlf tperygdiaf gtgirseanl rigggseksk
      361 yffsvgyldd sgytvnsdyr rystrlnvns dvkdwltvgv nmgysysest nngqiegsen
      421 vfefadkmap iypvfarypg tgdlipdpiy ggsqydygaq tsiinnfgfd rnrpnannln
      481 aigsavldfl gadthglngn vsanfkltdd ltfetqfggq ysyekrvdag nhvygtsegs
      541 ggtlgirdri rwsktflqll rfnksfgdhs fealaahetf ersfaqsnvs kqsvvvpgly
      601 vpnnylltts ptsgyqnasa iesyfgqvny nfankyfltg slrtdgssrf vkdkwgvfgs
      661 igaawiisee dfmsnsfvsf lklktsygvt gdqdgaetwr gyntfnadsv ggelalseri
      721 pgdenltwet skmfqvgies gfgqyldanf dfyrkntdnl ffnarrgpsv gfssirvndg
      781 eilnqgfefd ltghivnted fkldlsvnge mltnefvtmp ldastglpki ldagssedsg
      841 lfafaagrsm fdfylresag vdpadgtpmw yqyyddkndn gvldagegdf aieengints
      901 ttsslfeyqq rvsganikrt ttkvygdatq vfidksfipd lrgafrlsgk fknfdfstqf
      961 tysiggyafd aqyqelmtdr fgaastnyhv dirnrwsqpg dvtdvprlad gleqnstsdr
     1021 fitstdfial nnarigytvp ssfmpnsgid linlwvsgdn lfiesarkgf npsiretgns
     1081 grriyapatt itfgvrvkf
//
LOCUS       WP_093732652             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfitobacter litoralis].
ACCESSION   WP_093732652
VERSION     WP_093732652.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter litoralis
  ORGANISM  Sulfitobacter litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sulfitobacter litoralis"
                     /db_xref="taxon:335975"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55729
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpketf egenrvamtp esalqlqklg htclieagag eaagfsndky veagvevidt
       61 aaelwetadv vakvrvpsta emammrsdqt lisffspvad eakmkeaaek gttvvamemi
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee eqqdgsasgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvaam kpgsvivdla aekggncklt
      301 kmdekivten gvtiigytdf psrmatqast lfstnirhll tdltpekdgv inhnmeddvi
      361 rgatithdke vtfpppppkv aaiaaapkkd kpkeltpeek ranevaafkt qtrnqvglla
      421 iggvlllavg lvapasfmqh fivfvlsvfi gfqviwgvah slhtplmavt naissiiilg
      481 avmqigsgsf lviilaalsv fmcginifgg flvtrrmlam fqks
//
LOCUS       WP_093757129             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Tardiphaga
            sp. OK245].
ACCESSION   WP_093757129
VERSION     WP_093757129.1
KEYWORDS    RefSeq.
SOURCE      Tardiphaga sp. OK245
  ORGANISM  Tardiphaga sp. OK245
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Tardiphaga.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Tardiphaga sp. OK245"
                     /db_xref="taxon:1855306"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39229
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaisp dtvkkfktlg vdvaiepgag iksglpdsey tavgatisad
       61 avkdadivik vkrpevsela gykrgalvia imdpygndaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra vieaaesfgr afpmmmtaag tipaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf laveddefkn aqtaggyake mskeyqakqa
      241 tltaehikkq diiittalip grpaprlvta emvasmkpgs vlvdlaverg gnvegakpge
      301 vadvngikiv gytnvagrva asasslyarn lfsfietlvn ketkalavnw ddelvkatal
      361 tkdgavihpn flpkta
//
LOCUS       WP_093739481             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfitobacter delicatus].
ACCESSION   WP_093739481
VERSION     WP_093739481.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter delicatus
  ORGANISM  Sulfitobacter delicatus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sulfitobacter delicatus"
                     /db_xref="taxon:218672"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55271
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif egenrvamtp esalqlqklg htciietgag aaagfddaay eaagvevakt
       61 taalwkaadv vakvrppsed evkrlrsgqt lismfnpagn telmeaaaak gatvmamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee eqqdgsasgg yasvsspefr
      241 eaqlakfrel apdvdivitt alipnreape lwtedmvaam kpgsviidla aekggncklt
      301 kmdekvvten gvtiigytdf psrmatqast lystnirhlm tdltpnkdgv idhdmeddvi
      361 rgatitheka vtfpppppkv aaiaaapkke kvkektpeek radelaafka qtknqvtlla
      421 vgaalllgvg lvapasfmqh fivfvlavfv gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgsa lviilaalsv fmcginifgg flvtrrmlam fqks
//
LOCUS       WP_093785682             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinacidiphila guanduensis].
ACCESSION   WP_093785682
VERSION     WP_093785682.1
KEYWORDS    RefSeq.
SOURCE      Actinacidiphila guanduensis
  ORGANISM  Actinacidiphila guanduensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Actinacidiphila.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Actinacidiphila guanduensis"
                     /db_xref="taxon:310781"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52572
     Region          7..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msqsaqlvgv vsesrpgesr vaatpatvtq lrklgyevvv esgagrgasf sdeayaeaga
       61 avgeraaawg adivlavnpp saeeiglmre gallvallap atspdllqal aargvtalam
      121 davprisraq sldvlssman iagyravvea ahrfgrfftg qvtaagkvpp arvlvvgagv
      181 aglaaigaag slgavvvatd prpevadqvr slggeylavd saeaevsstg yakemsqdyn
      241 alaaalyare lpevdivitt alipgrpapr liteemvasm kpgsvvvdma aaqggnvagt
      301 vpgeavttan qvtligytdl agrlpaqssq lygtnlvnll klltpakdgq avldfedvvq
      361 rsitvvrdge ltwppppvqv saapapaaaa ppptpaaerk rpagpgrlyt avgavaaglf
      421 vlagfapaql ignltvfvls ivigyyvigh vhhalhtplm svtnaisgii vvgallqigh
      481 ahtavtvlsf vaillasinv fggfavtrrm lsmfskd
//
LOCUS       WP_093808459             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Stappia
            sp. ES.058].
ACCESSION   WP_093808459
VERSION     WP_093808459.1
KEYWORDS    RefSeq.
SOURCE      Stappia sp. ES.058
  ORGANISM  Stappia sp. ES.058
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Stappia sp. ES.058"
                     /db_xref="taxon:1881061"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39448
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavprese ageprvaatp dtvkrfvalg fdvavekgag alsripdadf eaagatlaad
       61 akatladadv vlkvrrpstd elgltkkgal viasmdpygh ddavkamaea giaafamefm
      121 pritraqsmd vlssqanlag yqavidasae ydrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedde fkqaetaggy akemsdeykk
      241 kqnelvathi akqdivitta lipgrpapkl idaamvasmk pgsvivdlav erggnvegsk
      301 pgkiaksgdv kiighlnvpg riaasastly aknlfafaet midkeakaia vnwddelvka
      361 tvltrdgqvv hpafapdtk
//
LOCUS       WP_093814461             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. TverLS-915].
ACCESSION   WP_093814461
VERSION     WP_093814461.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TverLS-915
  ORGANISM  Streptomyces sp. TverLS-915
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces sp. TverLS-915"
                     /db_xref="taxon:1839763"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51482
     Region          1..504
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvvredv agetrvaatp esvarlrelg yevvvepgag ehagfpdaay aeagartgaa
       61 rgadvvlavr tppmdglrag vtlvglldpa heperlaela rrgitalame avprisraqs
      121 ldvlsstani agyravveaa halgrlfggq vtaagktppa tvlvagagva glaaigtaga
      181 lgavvratdp rpevaeqvrs lggeylpvap pgeegtgtgy aremdaeyra reaelyarec
      241 avadvvitta lvpgrpaprl ltadtvaamk pgsvivdmaa asggnvagtv pgervvtpgg
      301 vvilgytdla grlpgqasrl yannlvallt lltpdrdgtl vldtddivqr siavvragev
      361 hwppppvpvs atpappaeae rtapaeaapa ppprrgrrya laalasalll lggatappaf
      421 lghltvfala vvigfyvign vhhalhtplm svtnaisgiv vvgallqigh gdtavtalaa
      481 laillacvni fggfavtrrm lgmffgsgs
//
LOCUS       WP_093822526            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093822526
VERSION     WP_093822526.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110323
     Region          53..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlfylsppf srrwsvlycf llainsltat genlsttspq tryvstnkpv aditisgrvt
       61 daatnealag csvllkgtqk gtttdakgey kitipdggqa vlvygfigfv seevqvggrs
      121 tinvalkasa selsqvvvig ygsttkrdmt gsvksiksad fnrgiinspe qliqgkvagv
      181 nvtsasgepg ssqsitirgp ggvrtgstpl fvldgipldn sstggttnpl tflnpqdies
      241 vdvlkdasat aiygargang vvlittkkgk agsatfnlss slgiskmarp lkvfsadefr
      301 tqvtalggil ddkgaatnwq keisqtaytq nhnlsfsgga ekltyygsfg vqdqqgilkn
      361 sslkrytgri nvsqrfledr ltvdvnltas qtnnqrppsg ssvgsgagvt vigsaisanp
      421 tyaaydangn pfqyqggtnp litlnlekdv ttinrvvgsi spsfkilpnl vyklnlgvdn
      481 sssvrdlqtl anavpqqdgr lesiyrtnrn tlienyftyt laksshnlta lvghsyqkff
      541 vqerdwsink fpitpvepiy npglgqdltl annrptgsal qnelqsffgr lnyqfndkyl
      601 ltatvradgs skfgannkyg vfpsisagwr lsdeaflksg pfsdlklrag wgqtgnqeip
      661 akitqalyta qvsgttsypl dnttsypagi sytrlanpdi qwevssqadv gldfalfkga
      721 lsgsvdyfnk vskkillevi padpiqpast ywtnvpnmsi snqgveidln yrylsqsgfr
      781 fdiggnltfi knivrnspys vitsgsaqgs gltsatvngy ineqpigtff lkdftgfddk
      841 gistyrdtdg dgivtdkdri aagsalptkq fnintslayk gfdlainfng vsgnkvydnt
      901 ansnfyklrl skglnttaea ikypnesinn sapvstrflk dgaffrlnnl algyslspkl
      961 igmnrwinai rfsvtgqnlf vitnydgydp evntdrtvng issygidyls ypkarsvvfg
     1021 lnltf
//
LOCUS       WP_093822915            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093822915
VERSION     WP_093822915.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114163
     Region          25..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkalillll ypflccclaf gqgnkvtgkv tgrdnqglpg vnvvvggtst gtatdaegny
       61 sinvpttgsl vfsyisyvsq tvavnnrsvi nvtlaedaka idevivtalg ikreaktlgy
      121 atatvnadqi svnrtnnfvs glqgkmagvn itsmgsgpag takirirgqs sfsgqnnpli
      181 vvngvpidns nyslggdygs ramnnsdggd glssinpddi etmtvlkggt aaalygsrak
      241 dgvvmittks rgagkgfgvt yntnftteta qdytdfqyey gqgeggirpt ttrpqsgvws
      301 fgekfqpgmt qtlfenqtyp yepvynrvkq fyrtgtnftn tvtlanngqn ggfslslsnt
      361 dnkgimennt fnrkvinlgf sqninskltv sgninysken nvnppqlnaq dfsvstvvft
      421 lansmpfqal rdnqvlpngd efsfarflvr nnpyysmnyh fenvlrdrif gnialkyqft
      481 dwlylqgria qdyyirnqdy nipngyapia kaptgyvngs ytqdvrqnte rnidfilggn
      541 ktfgkigvdv tlggntryar ndynsvtvqd fvqpglytva ngriknpiys lsekkinsly
      601 gsatvsyndy lfltatarnd wfstlapanr silypsltgs fvfsqafenl pawisfgkir
      661 aayaqvgsdn vnpysnalyy qvdnnsfpnp agqlvpvggi nvatvpnknl rplriqeaev
      721 glelklfnnk lgfdftyyhk ttndqilaaq isdassytnk linvgrsmnq glevalnfsp
      781 ivstnfrwdv nanasyntsk vlqlglspnd tvitvsggsg rvlnqvvgkp igqlytfmyl
      841 rdsqgrkvfd qnsgmplrnn tlvnvgnalp tyfggitntf tfkgislsvl idfklghkmi
      901 tgrninylrh glskrtlpgr dvgyvigdgv npngevnktr aavqpfyesl nplgihedfv
      961 nnagfwklrq itlgydftkl lppslfikgl klsavannvl iikkwtenmd peeanvssdn
     1021 svgldfwpgl pptrtmgfnl nvrf
//
LOCUS       WP_093823508            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093823508
VERSION     WP_093823508.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116453
     Region          24..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknlllsll lvcltcaftw aqerkitgkv tsvedggalp gvsvvvkgtt vgavtdgngs
       61 ysiavpakgs lvfsfigmat keiaigansv vdvkletdak qlseivvtgv gvatdkrkia
      121 isvesvsgkd lpqtpsasvd qaligkipga qitsrsgtpg advnillrgi ntinrgtqpm
      181 ilidgiqmga tslqtidlna iervevvqga aaatiygaqg angviqlftk kgkngqlnid
      241 fsssiavnty lnngglskak yhafatdasn niigssgkpi vydavngiys envqynstdp
      301 tatnskayda nlqyhdhfdy ffkpanttnn siaitggsqr adfgisvsns hqesnirdng
      361 yfdrsnlsan igaqlakglt lrsitqlayt kstlkssdrt ilfnllnayp ladfdlkttd
      421 gsiplnmnqt iginasnpsy rqaytrnndn kvdiiqnlnl nykfpkfvdl dlkyglnfqt
      481 qnrdleyanq annannkywl tqgttnyisl nnttntgelv kyawskmfqn flatatatfd
      541 fkedfhlnip iksttqalfd wrnskvkeyt sdaiglpaay apynaantts wrvyrdyvep
      601 fitygylvnq rfeigefagi sggfrsdyss afgqgskpft fprgdaylrl sslkfwensp
      661 innflpelkl raaygqagiq pqpfdryvti tpstvgntta fyyanqqsnp algvevseel
      721 evgtdmvfsl fkgsswlnai alsatywdrk tkdaiyqvdv apsvglgklt dnaftlgsng
      781 lqmslnstvy hstnlkwntt vnfgkqsski iavrgdapii vtsnagstny vlkagekigq
      841 lygyknlhsv derdpngnff ipqadqegyt vasngfvvnk ttkqpyftad kfsfgdpnpk
      901 fnmsfindit fknfltfgiq ldwvngnhly nqtkewmyrd gihsdyatpf tidgntgawt
      961 afyrgiyaqr tangtkdyfy edasflrlrn isvgvdfakl fkipavkrlq lvlsgrniwt
     1021 atkytgfdpe issgtsnsaw drgtdhstmp nfksyqasln fgf
//
LOCUS       WP_093824163            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093824163
VERSION     WP_093824163.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111842
     Region          22..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllfglvl lssisysyaq ersvtgkitt aadgaalpga niqikgttrg tnadadgnyr
       61 inipdnatli fsfigvesqq ipvgsqttin vslkadtkql nevvvtalga srekrtlgys
      121 vanvggdalt rsgepnviqg laaktagviv tsssgtpgas skivlrgpst ftgeqqpliv
      181 vdgvpinnet vttsagdypf nanlggvnns nraldlnpdd iasvtilkgp aaaalygara
      241 gngaiiyttk kgqkrsgigv tvgyrvelsq vnklpklqst yaqgsggkys tadvgpdqiy
      301 gtdddvsigt pnswgpkiss dptlqaydnp gnffktavsh ttnvalvggn ekanfrisyg
      361 nliqngiipn tdykrntlri tgeanmtdnl klggtvsyik sggikaqngs nvagvmlsll
      421 rapasydlrd yqfsngynrn yyapydnpny taynnpftdd inrvvgnvyl nyhhsshldl
      481 tykigvdays darrqvfsig sngddnaqry gqvnydnvts rdvysdlilr gehrfsekfg
      541 inytagqnit slnftdnyar grnlaipnfy nlgnaaelya snsgirkmtt avfgqldfdy
      601 anqlylsltg rnewsstfdr tvknnffyps aslswvftet alkntpisfg klrlayaesg
      661 ispaayrtrt yfskpsftdg ftnglnfpyg gvngysyyna ivgtpdlkpe rvkgleagin
      721 lkfwqnridl dvtayqqttv dilltkptap gsgftaaytn aaqlrnrgle vmlginaikt
      781 psfswdinin wsknvskvlq ladgvsevsl esafngiggy aivgqplgvl ygtkwqrnna
      841 gqliigsngl pllqeaqgni gnpypnwlsn irntftykgi tltalldirh ggaiwngtya
      901 rlqrigvtqe sadrertyvi pgvlasgean ttaipaltyf gqyqgdggga aeqfvenvnw
      961 frirevalsy rlklkkyvey vdfsvssrnl ylntnykgvd petsltgags nlqgfdyfnn
     1021 pgtrsyifgv nigf
//
LOCUS       WP_093824369            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093824369
VERSION     WP_093824369.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117068
     Region          59..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvhivqvcrp frtlarrfsv qllliifclp alsvqarsrp dkithpivll tddgpsadit
       61 vtgtvndvkt ntpipgvnvt ikgttrgatt dalgkyrivv anstdvlvfs figyvtreep
      121 vgnrteinvt iaddqkqlde vvvtalgvkr eerslgyavq kvsgntlqtv kglnaatslt
      181 grvaglwirn stefneaptl slrgetpllv idgvpygnmn ignipqddie sidvlkgpta
      241 aalygsrggs gavivttkrg agskgltvtv nsnnmvnagf lmlpeaqhsy saglggvydp
      301 tdyvwgqkld igkramqwnp ifkqmedqel tsrgrnnfnd flvpgvvsnn nisisqsgen
      361 gsfrvslthi ynkgqfpnlk snamnfsvsg emkignkftl qsqagynrkt apqisgagyt
      421 aqgyiynilv wmgseydlsq ykdnywlvpn eqqnwhykaw ydnpylmaye klngieqnkv
      481 ntnltatyev fpgakiivrp gfdaffnnet rrnppnilst rgwtanglys inqrngysfn
      541 gdalltynkt igkldidala ggtiytygnk elysstrggi vvpgyyslnn sierpdvivn
      601 pvynddpltp ygkkqvnsly gkvtlsymns lfldvtgrnd wsstmpqnsr syfypsvags
      661 vvlselvkmp tgldflklrg swtlsktdlr vfannqtyst ttadwdnlns aayplairns
      721 vvnpetnrtw eigtsayflg krfkldvayf nkynyniqrf asispgsgft stlintgety
      781 vrrgvevtvd atlikkgrfq wdatanysyn hryfknldpv ysannlwtkv ggrtdtytgr
      841 twitdpagnv vhqasglpla snynylygyt dpvalvgfan sirwnnfqig lrfdgriggf
      901 lnnyssykmw dtgshpdsdn qyrydevvng nksyvgqgvk viggtitydn lgqitsdtre
      961 fapndtkvsy qsyarsygdg trgvtnatfi klrevsigyt lpsafasrig arsasisltg
     1021 qnvwmwtkaf rfadpdkasd teltspsvry vganiqltf
//
LOCUS       WP_093824401            1133 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093824401
VERSION     WP_093824401.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1133)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1133)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1133)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1133
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123523
     Region          36..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpistfqli lrhsltiaml vgicfadala kgnpaktitg tvtlatnsqp iaganilikg
       61 tqigsvtdqk gnysisvnsn navlvfsfig hktqevtvgn qsvinvelve nnevlgevvv
      121 talgikrear slgyavgevq gkdlsrvaqe nvlnslagrv pgvqisstgp sgssvsmiir
      181 gakslntdnq plfvvdgvpi antlnnvsqi gsdnrvdygn aisdinpedv enisilkgps
      241 aaalygsrag ngvvlittks gsksqkisvs vtsntvfdqp ykylkmstgf atgilpftpt
      301 anpypggilq idegsaggvg peldkgynai qwnspvgtdg kqiptplvsh pnnikdfvrt
      361 gitstngvsi snnsekityr lsysnmssrg ivpnsdlfkn tlaistnvrv nnkltlstnl
      421 dfsrnnsnnr pagergtnpl qwayavgshi dinelrdywv pgkegiqqks qsignynnpy
      481 flayevnnsf vrdrlfgnmr aewqitpeik lmgryaldty teqretkiak sytgepngay
      541 glinlkryer nadflatytk rfnalsvvvs aggnnrysqs tdintsskdk agliipglft
      601 iqniattnin ysnylykkai ysayatanfg fkdmiyldlt arndwsstlp annrsyfyps
      661 aslsvllnei mhmpgsvdmf kvragaaqvg ndaspyslfp tladagawng vtrlsksgsi
      721 llpdlkpeia tsyevgidyn mfrnrlrfsg tyymsenrnq ilpsqtapss gfttkninag
      781 llesrgvels lggtiidkgg lrwdlttnft knttrikelt diipyytlwt dakggawtyv
      841 gdkvgdiyds eiitvtdqks pyygypildn ngswqsksat tsknkignfn pnfilgaqss
      901 lsykgftlnf sldwrsggdf vsqtyrymes dlrsqrfldn linpdgrtgd alrnylvena
      961 dqyikihgnf fpivggptaa yggypfefgg ktypygvfnp gvigqydaqg nltgytenlg
     1021 gtgtkiipyg dnypwdftra atfdasfvkl reislgydip akfvksiglq natfsvysrn
     1081 iilwtaakin vdpemafqpq ssaqagtqfk qgierynvtp wtipvgfrlg ltf
//
LOCUS       WP_093826188            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093826188
VERSION     WP_093826188.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115176
     Region          31..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhlvqrris mlgmlfwlti lltnavqaqd irvtgrvisg tdqkaipgat illrnstngt
       61 ttdadgnfsi laptngalvi saigftgqdi vlgnqtqltv tlqesaqnln eivvtalgik
      121 keskklgyat atvgteqlti nrttnlgnsl qgkvagvnvt aptggpggts kirirgqssf
      181 kgdnspliiv ngvpinnsnf ssrqgdtdgt anrsgsaadg gdglqsvnqd dietmtvlkg
      241 staaalygfr akdgaivitt ktgrrnagig vevnsnftad qaldytdfqy eygqgefgkr
      301 pttvgeaqss gvfsfgekid gkptyqfdgv mrpylaskdr ikkfyrtgst ftntvalsgg
      361 sdkggfrisf sntdanaiip nsdyhkkifn iglnynftpk fsaqinanys neynhnppqi
      421 glqdlnantt vyttantvdm ytlrdnryda ngnelatsrf tnrnnpywva ydraenvrrd
      481 rlfgnaslry qfndwlylqg rigqdyytrp ydfnrptgtr slsaaatgfn gyfyqevitf
      541 reknldfllg anhtfgnfgi dltlggnqlq qtytnnsasa tnfyirnlyt iqngqakdpq
      601 yaysrkqvns lyaasefsyk nflfvnvtar ndwfstlaqs sylypsvsgs lvlsdalkir
      661 ptwlnyakvr aayavvggdt dpyqnnlfys lnantlqgqg lgsittntsp nanlrplkik
      721 eaevglelra lnsrinldla vyqkntvdei lnvdistasg ydktkvnvgr lrnqgvemll
      781 tlvpiknnnf nwettfnlty nqskvlelan gqqrlkvgqg dffgelwhev glpmaslrgi
      841 aykrdpqgri itsggkpvag dittfgsaip kytggwlntf tykgfriftq idfkaghkll
      901 snsnlnflrh glsqaslvgr eggvlfegvn evknatgqve ytpnttrvea edfyssyrst
      961 nnteqfvyna sfvrwrslsi gydlsrfvnk tfikgltvsa ignnlllikk yvdnldpeav
     1021 agasdniqgi ethslpttrs ygvnvnlkf
//
LOCUS       WP_093826697            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093826697
VERSION     WP_093826697.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118037
     Region          24..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrillvsml lvcslwstaw aqerrvvgkv tsaedgsplp gvsvvvkgts kgtttdaggi
       61 ydislptask gavlvfsfvg vttqeirign esemnvslvs dsrqlsevvv tgvgvatdkr
      121 klgiavesvs sknlpqtpta sidqalvgki agaqissgng tpgapvnivl rgintinrgt
      181 apillidgvq vdastydtng nfnsnptsll ssidpntier vevvqgaaaa tlygaqgang
      241 viqvftkkgk sgklnvdiss sitrneylnv ggvaksqfng fitdaqnnvi gtsgkpltfd
      301 pntlvysenv qynpldvnnk adkpytanlk yqdhyayffr psntynnsva msggrdkfdf
      361 sisasnnrqe sniinnggyq rtnigtnlgf elakgltfrs ttqliytkst iksndrnily
      421 alnnarpfad fsaldpdgnp giyygdavgv nhnnpsywqr ytdnkdnkvd iiqnlnlnyk
      481 inqflmldak yginysrqei ittypnqvsn rnvqyyqgsn yqgnyatdas geidnyslnt
      541 tyqnflasaf ittdfqkdfk lnvpittstq vsfdyrnrls reyntyglsl psyepftaaq
      601 astfktfrdy tepfitygyl vnqqidfgdl agisggfrtd fssafgsgsk pftfprangy
      661 frpsalkfwe nsalanifpe lklraafgka giqpkpfdry qvlntrtlgn ansfytpasq
      721 pnpnldvevs seleigadlg ltplkgsdwl ssirlsasyw drstdnaifd vngapsagin
      781 svkdnafsla sngfqaslna siirtkdfsw nlttnfskqt skitavknna evvvlsnags
      841 tnyvlragek igqlygyvsi hqldardvng slyipqdqqs lytvasngfv vnkatkqpff
      901 sankysfgdp npkfnmsfin dftyknfltf gfqidwvhgs hvynqtkewm yrdgihadya
      961 npftiegqtg awtafyrgvy aqraangtkd yfyedasflr lrnvqigfdl sklvnapvlr
     1021 raqvvlsgrn lwtstkytgy dpeissgtgn sawdrgtdhn tmpnlrsyqa slnigf
//
LOCUS       WP_093826693            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093826693
VERSION     WP_093826693.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118873
     Region          24..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrillvsml licslwstaw aqdrrivgkv tsaedgsplp gvsvvlkgtt kgtttdvggi
       61 fdisvpqakg svlifsfvgv atqeipignq selnvslvsd srlltevvvt gsgvatskak
      121 lgiavesvsg knlpqtptas idqaligkip gaqissvsgn pgdpvnivlr gintvqggtk
      181 plimvdgvqi aatdinsldl snvervevvq gaasasiyga qgangviqvf tkkgkkgrva
      241 vnfstsysan efinsgnvrk adlhpyltda snnlidpsgk pltyneygsi egisykygga
      301 tryaildtrn vsntpynanl kyydqfkqvf qtgsttnnsi sisgaseksd faisaannht
      361 vsgvmkngyi drsnltanlg telfkgftlr sttqlvytkn tlhpglgapg gydygkgnsl
      421 gsigsvygff ntspffdlta kladgtypry qtadflsvna anpfyqqqyt sgldnkidvi
      481 qnfdanysin kflelnakyg lnyrtensrw tyfnqsanin styydtwssy fapdnkgeit
      541 nwqynttfqn flatayirtd fendfhiklp iqtstqisfd yrkkkyeeyd tyglglglap
      601 pfnisstssq gvasydnttk hngdyvepfv tygylvnqkv dfgdygglta gfrtdwssaf
      661 gagstpftfp hfdahiapfs fmknsgisnt lsyfklrgay geagiqpgaf drypvlgqqn
      721 lgsglvytip ttsnnanlkv evskelelgt dftiglgqgn wlnsingsft ywkrksenvi
      781 ytvsvqpslg stgqltnaid mssngiqfsl tlpvfnskgl kwdfttnfgh qiskidaisg
      841 gadiiltsga gdaalvltag qqigqvfgyk amtstaftrq dgsryitegd askytmvdgr
      901 vvdkatmaiq ftdekyplan pnpkfnasfi nsfsfkdflt lnfqfdwvyg shlynqtkew
      961 myrdgihgdf skpvtidgqt gaytaywasa yyalwgstrg agnnatkdff vedasflrlr
     1021 nislafdlgk vvklpyinrc qlvltgrnll tvtkytgfdp eissgasnss fdrgidhntl
     1081 pntksyqvgl nigf
//
LOCUS       WP_093826956            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093826956
VERSION     WP_093826956.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114673
     Region          23..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqpvlifll ligillrvqa qnrtitgrvs spenedmpgv svvikgtttg tvtiangtyq
       61 lavpakstlv fsfigyktme vapgdqttvd vklvadltnl devvvtanai vrekkelgya
      121 vstvggseli kardpnvlns magrvagvri sqqsgsvggs tkvmirgans lsssseplfv
      181 vdgvpisnss fngsetdivt ggvdvgnrag dlnpddiesm nvlkgaaasa lygsrarngv
      241 ivittkrgkv gskkmnisvn ssyrtdnvlr vpdtqteyaq gnlgvynprl gngwgpaiss
      301 vtgpvldytg atvqgltahp dnwknffvtg htvinsvsld gasdqgdyri gftnlnqtgt
      361 vpgsklgrnt fainagrkit dkltsrvwln yvrttsdgrp qqgsnttnil stilaglspt
      421 idindlrnnl fapatqsvpt gwtgdlarai dldgiqnnpy fvtafnkfsn svdrvyggts
      481 lsydvapwfn vtgrvgtdff tenrrsttrr gtrgrlngqf dtneiyerel qsdligtitr
      541 kisddwtfkg ivghqfnqrt irrsrvlsdg lnidqlytfa naqsnvasnf ysrreifgvy
      601 gdfsfdyrnf lflnvtgrnd wsstlpvnnn syfypsvsas filteafpnm givknnvlsy
      661 aklranyanv gsdedpyqla ftynpltqas diytfnilyp iggasafgat nvlpptnlrp
      721 qqqtsfefgt elkffggrlg ldltyyrnln ydqiisiavp qstgysarrl nvgeisntgv
      781 eamlsvtplk trsgfrwdat fnfnrnrnrv esladgltef vttsgdgfgi fvvakpgetf
      841 niqgvgwlrd pqgnivinps tglrtpgprr llgniypdwt lginnsfsfk gfdfnflidm
      901 rkggvinsqt vgivrsggla vetavnnrtp fidpgvirna dgtyrpndvp vasvqqywsq
      961 ldnsvspetn tfdgsytklr evriaynlpr tlvnktpfgs iafgvegrnl wiihsnvphi
     1021 dpeanvlgtg ligeglergs ipssrsigan lrftf
//
LOCUS       WP_093828695            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093828695
VERSION     WP_093828695.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121925
     Region          45..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtlflpsstl pqplrqrtar pvrtlrrlav aflfcllsgl tafaqtvsgr vvsgednqpl
       61 pgvsiivkgt ttgttsradg tysisvqsan tltfsfigye tqdvavgnri tidvslvvgs
      121 stlneivvta lgikkdirqt gvtvqtvdgt qllkarepnp insltgkvag ltigsssell
      181 grpnislrgn sdvlfvvdgi pitsdtwnvs addietytvl kgasasalyg frgkngaili
      241 ttkrgtkdkr gfsvevntsq madqgflaip kvqdeygpgd hgvyafgdgk gnglndgdyd
      301 iwgpalngql ipqydspvlp gqsftttfpn gktftsnrqp tpflprgkdn lsrfiqtgiq
      361 snnniavaas gekydmrfsl shnfqrglvp ntklnvtnfn vtggynfspk lrfeasmnyn
      421 rqytpnfpdv nygpnsliyn iiawggadwn iddmkqiwqp gkegsqqiya eyqrynnpwf
      481 lakywlrghy nsnlygytsl ryqltdaltv taktqlttys llrtekfpys atsygreear
      541 gdyredrrnl fdninqvlvq ynkkvtpdla inalvggear ifnynsdfas tnylnvpgvy
      601 nfanssnpvv asnfqsdmrv lsayysadft frdyatlttt gridklstlp kgnnayfyps
      661 valstvisdy vqlpaklgis flklrasyan vkdgltqsti gstpgasfpl gygvdynssy
      721 ggptyqnsav ytlplaynnk paayytntln npnlkpnsts qseigldirf lnnrlaldaa
      781 yyvsndgpri ftlpsseatg ytgrlvngis tqkkggeisl tgqairspkg fnwdvvanys
      841 tyterlkevy peggintlas nffvgsssdk rfinigdrtd gfyssafvrt pdgqlinddg
      901 grpiinpvsq flgyvnpkfv wginnrfsyk ninfsfqfdg rvggvigdyv rqktfqggrh
      961 ietiqgayga arpndvqgit sfvgqgvalt ggtinydvng nvlnygelky gpnttktfeq
     1021 dyiarafgst esflmdrsfa klreviigys lpqnllrhvg vkqasvslvg rnllyfaqyk
     1081 didldqyltg gisglqtptt rryginlnlv f
//
LOCUS       WP_093828875            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093828875
VERSION     WP_093828875.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113377
     Region          37..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkftqlmrg clsvvvaffc lltgnvgmad tvpladievt gvvtfkddgs plpgasvllk
       61 gspntgtitd angkfrinvp edatlvisyi gyiaqeikln krttltvald adaqqlsevv
      121 vtsfgiardr ktlgygvsel kteqltkapt tditnslagk vagvqvtgag ggfagsnvti
      181 rgfstftgsn qplyvvngip ldnsngggas ngtnsvntgv vnssrisdin pqdiesisvl
      241 kgaaatvlyg sraasgvili ttkkgkkgtn kqisfstnta vgtvsrfpkf qnqyaqgsng
      301 tyannvagsw gpliqgqtvt nwfgnqetlq aypdnvqdil qnsissqndl sfsgasdkyd
      361 yrvsygnaye talvpnnkls rnnltvnagt qltskfrint aftytnnvsd rtqsgnqgan
      421 plwrgiytpr sydltnapfq davggqlwfa aedqpywsin hiknhqevnr fygninlkyd
      481 itdwlqadlk vgsdvftytt kgfddkgvrs nantasagag gvldrtemtr nlnsyftvta
      541 nrkltsdlhl tatvgneiis nynsflqdig lgivvagfdn vknfltfnpt saitkqrtvg
      601 ffgdvvfdyk twlsvnakar ndfastlapg nqsifypava vsfvpteaft slkskvltsa
      661 kiranvgevg kgatpyvint yygkasasdg lgstavnfpf nglagytydn gtgnpnltpe
      721 ftrevelgae laffngrlsi dgsvyrrdsr nlifsvpvps tsgfsslvtn agklstkgie
      781 llvtgniiek enfswessln ftsfksivee lapgvtsisi ggftspnirl vpgeqygqiw
      841 sngyqrnaqg qmligsnglp kpttavqrvg npnpkytmgf sntfnykgls lsflfdfkyk
      901 gdqlsrtigd lringvsaet aelprfnadg tpnkayvfdg vlddgsknni gvtaqqyfsl
      961 qgkyvawegy vldatylklr eanltyklpt sivggskfik slqvsvygrn lfiyapnypd
     1021 ldpeqnllgv snarglefgi tptarliggs iraif
//
LOCUS       WP_093828972            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093828972
VERSION     WP_093828972.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116817
     Region          25..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqnrglllml ffalylpaql faqsrtikgi itsgddnsat pgvnvivkgt nvgastnaeg
       61 aysitvpenl vkngvlvfsf igmktaevpi gnqsaisikl qhdatsldev ivsalgfken
      121 adkrgatask idakdivrsg etgvingmsg kaagvqitks agdpgagsyi qirgqntitg
      181 stqplvivdg ipisnstlgd qaagvtqqsr lndinpedia smqilkgasa aalwgsraan
      241 gvivittkkg ansdkvnisy sstvsfdtpn llhplqsnyg qgsdgvynpt vanswgdkia
      301 nraggddiln mngarfesyt gktyypiltk nsketfndvr knsvfrtgty idnnlsisgg
      361 nekgnfylsi gdlrqkgiin gqsdynrttl rfnserrfnd viksstnaty arttsnriqr
      421 snsvnglyig ylrsapdfds rdykgnyfss ptasaipnrq rsyrnylgal anpiyndpmw
      481 aineltnfse vdrfimssel litpskwfdv tvrggidant dhritnypvn savnsglgsy
      541 eeaiykesem ngdvigrafg dfgknitstl ivgfnlndrk ylnlggtmnt fiipdapanf
      601 gnsltsndap yrttthrrma rlystlnvgf ynqlyvnasv aaesgstfgs qtkstfyyps
      661 adlawqftql pifhdnpvls fgklrasygt vgvqpdaykn attyvnasfa swanplsgsg
      721 ygngayvrna tqgdpflqpe rkteyevgtd lrflnnrlta gftyysneit nlllnvaaag
      781 stgytskytn agsmtnkgwe lemnfnilnk kgfnwnvfgn vsrninrvtn lagtdiitlg
      841 gfsstastva kvgyamssly ggtymrtesg alqlnangfp qvgtqfgvvg dpnpdyrggf
      901 gtnlsykkls lnilfetfqg gdfyngtrgt lynfgthadv gndvtltqdl knyagktiaa
      961 gstvrgniqd fgagpvlldq syytsigggf stlveqfitd aswtrlrevs vgysisspkf
     1021 raktklqsid itvtgrnpil wtkmvgidpe talngasnsr gqdyfnspnt ksllfsvkin
     1081 y
//
LOCUS       WP_093829285            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093829285
VERSION     WP_093829285.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117683
     Region          24..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksllmslf lvglhcslal aqgrkisgtv aadegidgfa gttvvvkgtt igtvtdvkga
       61 yslvvpesgt tlvfsavgmq tveeviggrs vidvklktdt kqlneviita lglkeerdkf
      121 assvstvsgk niaksgetsl ltglsgkasg vvitrnggdp gagayiqirg qntingnaqp
      181 lfivdgvpvs nssdnngsaa gnsivqqsri ndinpddies mevlkgasaa alwgtraang
      241 vivittkkgk dskgkvnitf kstvsfdrvn knhklqtnyg qgsgglyqqg srntfgdlis
      301 araggvdnfi tdptaagyqg fvtfpdgtkr yaiaagtaan phggknsrdt ydhtqdvfqt
      361 ghftdnainf sggnarsnfl lsysnlnqeg vikqfstyqr ntvrfnaasq ftewfrasan
      421 igytksyssr vqqgdnldgi ilggfrtpgd fnneyytgiy tnkagqtfnd ahvsfrnplg
      481 vdqntiyanp vwninnnrnt tdvdritgta eigitptswl sitgrtgidn ftdyrlerfa
      541 rnsgsygtgl lsknwitekq fntdvfanat htfnnnfsgs llvglnynsr rkeymsdqit
      601 nfivpnapdi ltnalnsnss isnynslirt yayygqaevq aynmlfltlt grtesastfg
      661 sktnssfffp saalawqfsk lkglenssvl sfgklrvtwg qvgiqpqpyq nfttfspaay
      721 tdayagglks asalygggyv rsttagndfl rperktetev gfdlrflnnk invsataydn
      781 stedvilsln vpnetgysir nvnaaklsnk gieleagadv lslgdfkwnl sanfslnrnk
      841 vvslagaaaq tlpdsyqqna sliegqpfgv fystdflkde sgkyqldang fpqggtgnei
      901 igdpnpkwrg glgstfsykg lslsvlfdrv agndfyngtr galysfgvha dqggtavapa
      961 ggikdvngnt iaagtsfqgq ikdfgagpva lnqawyqgrg tsfnsasykq fiedgsstrl
     1021 revtltyslr segfrrithl snvdfsltgr nlllwtnytg tdpevnitga glsrgqdwft
     1081 npntksllfs lrity
//
LOCUS       WP_093829546            1212 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093829546
VERSION     WP_093829546.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1212)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1212)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1212)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1212
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1212
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132773
     Region          61..113
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          157..1211
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mirlirttrf rlvglglllg yphvpygqvl ayhrdqites kqsatnrlrd vlldmqsryr
       61 inivfdekll egitvdtrkl spsmtitnrl ryllegsglr yvqtqkdtyl ivpdrpveka
      121 sdsksvpddk saaitplpgm pvsvnqptfv vdpsvrqtvs grvtdengag lpgvnvseqg
      181 ttngtttdae gkfrllvdgt nsvlvfsflg yqtltrsvgt gtafnvrlqp dvrslsevvv
      241 igygerqrkd ltgavsvvgg delvknkaln pelamqgrlp gvfvstpgga pnarptvrir
      301 gvntlgyndp lyvvdgvpit eygsgppqsg naaqatdlrg nvnilnminp ndiesisvlk
      361 dassaaiygv raangvvlit tkrgkvgrpr lelsasrgiq nlpkrydvld vpdyvalvre
      421 myannpaqaa nlpaiykdgn aaylgnlprt dwqsalinkn avtedysakv sggsesttyy
      481 vsggysrtes plqqnnfkry slalnltskv nrwlevgltn rlsyvdaldn tqsdlssawr
      541 yapwqpiyaq agfpaydgfa qtvnptfavn pafdptkisl gggpytitnt gllygtatrg
      601 nvlgqwdtrt nnysmlrtlg sayiqveplk glkikgtlsa dwyittrnqw qsvdsyrfss
      661 pftntfsatn gtskgqitqr ilrnynlvke fsvnynhafg ghsvdllfna mdqqygasst
      721 gaantqinyy npdalallnt apystgqiip ennalqgylg rlsynyksky yvdatvrrdg
      781 tsrfdkdyrw gtfpslavaw ritaepfmkn vtwlsdlkmr agvgeignqe ttqfaylslv
      841 nfnpdysygs gvngeaigsl qngirlanip vrnlswervq trnigfdasl lenritatie
      901 yydkktsgil qtvtlptsag iddgsaptnn iasvrnngfe fqlaytgkvg nnltynvsgn
      961 lttvrnqvtg lyrdlaftsg nnrteinqpi gylygykfgg ifqnqgeida ykatkptaaa
     1021 akdainsdrv vpgdayfqdt ngdgivnand rvylgktilg yyygfnlgaa ykgidvsiff
     1081 qgvgdvqain aerqagigmn seninywtdv rnrwtptnps ttlpravqgd pasnnrfsdr
     1141 fvenssfmrl knlqvgyalp rvlldrlsgl sgvriyvtgn nlltftgwkg ldpendaipp
     1201 arswilglnv nf
//
LOCUS       WP_093833247            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093833247
VERSION     WP_093833247.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116015
     Region          21..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvcllslvl flpifslaqq rvvkgkvsda agkealpgtt vtvkgstsgt vtdaqgtyql
       61 nipdknatlv fssvgfqsqd vvvgnqqtid vllipdtkql sevvvtaagi krdknalgys
      121 vstldankla qrsepdplra ltgkvagvnv qgsggaagga tnitirgnss lgnnnqplfv
      181 vdgvpfdnss fgstdgtvgg atttnrafdl dpnniltmtv lkgaaaaaly gsraangaii
      241 vttkagksqn rkgleitynv gystetvagl pdyqtkygqg tnfdyrsgvf gswgppyagy
      301 tsliptrsti phplttnnry pstvfpqfyq adgitpiqvp yqsysqdnak nffrtgnvfe
      361 nalsvstggd kgnftvglsr tvnqgvvpen qisrtgvnig gnaqlankfy vsgalnyvnt
      421 nqvspqltaa ngsgssimdi lmfvptsfdl tgfpntnpln gnnvydrvgt dnpywsvvns
      481 pttskvdryy gnvvlgvdpl pwlnvqntvg fnaytdrrtv vngkggdyfp ngnitndniy
      541 rqeldntlll tatkplseni glkvilgnnv nqriterqvv fgdgiifrgi nslnntsvti
      601 prvlpnnrnn fkqryfafft disldyknfa flnlvarndv sstlpesnrs ylyggasasl
      661 iftealkipk nvlsfgkfra gytrvgneat pyqtqtvyia npvlgagttt gaisspfsgq
      721 stltesdlla naalkpefit elelgtelqf fnnrlgfdit yykkistsqi ftvnavpssg
      781 ytqkvinlgk ssnegieigf natpvklkng ftwdissaft mnrnivldig slkelpyggf
      841 sdlgsvhiag qpygqirgst narddegnil vnpntgkpil sgkttaignp npdfiwgitn
      901 tfsykgitls alfdwkkggd mysftayell srgvtkdtee reaiiigpgv lgdvntlkpl
      961 lngdgkkipn nigigvadyy ftggfgpgga getnifdatv frlrevslgy lfpkkwlakt
     1021 pfgsaflsfs grnlwylapn fpkhlnfdpe vsslgagnsq gfdfigiptt rrmgvnlrfs
     1081 f
//
LOCUS       WP_093832196            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093832196
VERSION     WP_093832196.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112566
     Region          19..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlwltlllct navaqstrft ikghvtdpek qslpgttvav vgttlgtttd adgdytltvt
       61 lkpgpvtlaf saigyetlrq sitlgnadqv tanaalaaat tnldevvvtg stlsapkrel
      121 gnaistikas dlqqsgsgnl inslqgkvpg aqitqnsgdp aggisirlrg ikslvgssdp
      181 lyvvdgvivs nastnvsqla landagnanv gqnrlsdinp ddiatlnvin gaaaaaqygs
      241 raangvviit tkrgqsgkaq vtfstsfnin elrkgvpint ygkqfgfasl rlypigvvsd
      301 aqvaanpgtt ttgiyrdgtt sqlatnlvdv qrynyfdqif rtgygtdnnl sisggrdntq
      361 yyvsfgylkn qgiikdtdft rynlrarvdq rltnwakisv glsyansfsn ekangnvfys
      421 pinsvnitnn iyditkrdaa gnlqaveptr vnplstiedm kfsqsvsrti nslqlnltpl
      481 kglsidyivg vdaysqfgkn yirpypyqav aglpaarypg gfaatatnqv lqfnndlnaq
      541 yerqfsdkfk lnaaigysyq yyqadysins gqnlvpliet vsgasnttyq vrydldrfsl
      601 sgafaqatlg frnlafitga vrrdqsskfs ptqtnqyypk vsgsfivsdl efwknlsfsn
      661 afnslklras ygeagnlsgi gsyarfyqfs pvgflgkntv vpgtqlanpd vkpermaefe
      721 ggldlaflng riglgvtayq qkisdlvvnr tlapttggts ivnnvgamen kgfevvldvn
      781 piktknlnwd ftviynhnrn kvldlggqpi inpdassasg tpgnlivgqp vgvfygtgya
      841 rnadgslils psgfpqsera ssqdngsisy vparnsdgtl dvtkplanll ignpnpkwtg
      901 sfstnlaykk ltlhvlldmv qgvdvfnadk rtrqgvglgd yaeqelrgtl krgyifgvyn
      961 tqefrvdpgs ytklrevsls ytlpqfikgl srltvsavgr nlyswdkytg fdpetnaggn
     1021 ndllrgidfg nvpiprtyqf klaatf
//
LOCUS       WP_093834410            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            endophyticum].
ACCESSION   WP_093834410
VERSION     WP_093834410.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma endophyticum
  ORGANISM  Spirosoma endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Spirosoma endophyticum"
                     /db_xref="taxon:662367"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113187
     Region          54..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkdfhkiqgg khqyvvssln qfkhmksiyv ylsyllllcp ivavaqkkva ppmvikstvv
       61 dengapisda tvygnegtav sktdasgqfa itiptlgdll ieapgfesvv fkpgdysnqe
      121 rlsltkspfl fgqqdvvnva fskikkgnli navsilnpdd lrqfdntqsi ssalsglipg
      181 mlgssnirgi gspmfvvdgl prdvstlnls evaqisvlkd insailygnd aingvvlvtt
      241 krgqaykkqi natvfygisr psalpeylps adymelynea rlndglgiqy spaqiqnfrt
      301 gnpyrypsvd yysseylkkm rplsramvdf sggnnvatyy tnigwtqtgs lynfgegksm
      361 asnvfnvrgn idlkinpwik saldavfvln dnnmpqgsff anaatlrpnl yaplipisli
      421 dpenallkgr kndvdgtyli ggtaayltsp iasgysggqn rqlqrvfsfn nridfdlgrs
      481 ipglafhtnl sfdfltlydq fisnsyaaye ptwsdtqdri vslrkygedv rsgtqnvgna
      541 syrrrigfyg lldysknvdd vhqitgslla yltsdkvqgd iqgnknanlg lrlgygyknk
      601 ylvdfssafv nsvklpannr mafspslgla wvlssegfms svsfinylki rasagllnsd
      661 ngisgffnyd erytssgsys wyegtrsrgg viaqnggnan lafekrneln igfqsllfgn
      721 rlsldanvft slyydqiarp qtiypnyyst fipyrnfedn ayrgaelgls yrekwgdvkl
      781 vvganvlyad skvkkrdely atsnrnrtgq pvdarfglas dgfftsrsdi eshetqafgt
      841 vkpgdikykd qngdgiidan devrigrgqa pfsyglnlrl syknltlfar gngrmgadge
      901 isnnyfwvdg ddkystfvln rwteatqata tfprlssian tnnyrssdfw lyrdnfftvd
      961 rvqltyavpl kvsnklnvrg fsvfadasnl vmiskfrqfk elnigsepqy rsyslglnis
     1021 f
//
LOCUS       WP_093864604             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. TLI_053].
ACCESSION   WP_093864604
VERSION     WP_093864604.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TLI_053
  ORGANISM  Streptomyces sp. TLI_053
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Streptomyces sp. TLI_053"
                     /db_xref="taxon:1855352"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53194
     Region          13..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msaqdathhp prrigvvaes aagetrvaat pstvrgilal gyevvvesga gtasgftdea
       61 ytaagagvgd awaadvvlkv napstaevar lrdgatligl lapaqrpdll etlsarpvta
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvkslggeyl pvqaaqeast dgyakatsad
      241 ydraaaalyh eqardvdivi ttalipgraa prlltaedva amrpgsvvvd maaaqggnve
      301 gtvagrtvvt dngvtligyt dlaarlpaqa sqlfgtnlvn llklltpgkd gqlaldfedv
      361 vqravtvvra gevtwppppv avsaapapas apaapavvep arprlapaar fgligagmla
      421 lflliafapt qlaqnftvfa lavvigyyvi gkvhhalhtp lmsvtnaisg ivvigallqi
      481 ghgsttvtvl sfvailltsv nifggfavtr rmlsmfsssp err
//
LOCUS       WP_093868953            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. MAR_2010_89].
ACCESSION   WP_093868953
VERSION     WP_093868953.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. MAR_2010_89
  ORGANISM  Tenacibaculum sp. MAR_2010_89
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Tenacibaculum sp. MAR_2010_89"
                     /db_xref="taxon:1250198"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116148
     Region          26..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqsfkkalt flaffcfivs vsaqqrtitg tvsdeagqlp gvsvvikgtv kgtetdidgn
       61 ytvkantgdt lvymflgyen vekvvgqssi invkmtedan vldevvvsva yaakrkkdii
      121 gavsvvtake vgdlkvttvt ealqgtsgls lvntsgqpga sptirirgvg slqgnvdpli
      181 ivdgaqfagn lnsinfndve sysvlkdada vslygnrgan gviiiktksg adtngegiie
      241 vstsygfsdk atndysylns eqilttswqs irnarldagd tpavasnfat tnlisdlkan
      301 pysvsqpvgt dgniksnarl lyntnyydil tqnatrqdvs lvlrggsekt kyfisgafld
      361 sdgfslnstf rryngrinls sdvkswlsvg anafvtises nvptqsgslf anniqyarsi
      421 ssiyplykrn gdgtfilgan gekqydfaen rgffgnynpl aetygstnlf erntfnfspy
      481 vnfkfsdnln fksqlnytny lyeentfnnh fvgtpqdqvn nrssskrrnt tktwniintl
      541 sfnqtfnekh svtallgqem ydrtfnrlna tatgyvfsdl teldngatpt svgsitnknr
      601 lysffgrldy nfnekyyfgt gvrrdassif hkdnrwgtfw svaagwsiyd effrgsetvs
      661 slklrgsygt vgnqninqqf tyideyglgf nvlasgglap taignkdlkw ethnklnvgl
      721 dfalfnsriy gsveyydnrv tdllyfdtpa pslgsggtgp dddggsralg kwknfgemsn
      781 kgfefnvnsi niendnfkwt ssftistnkn riedlkqsen ngsfrweagr dryefymrew
      841 agvntktgap ewykdvtdas gkitgrekts kydeatryft gksalpdfeg rlgtkfeykg
      901 idlslnfnyk fgnyiyntdy aslmkarnlg eqlssnvlna wqkdgdvtdv pklttasdnf
      961 nsrstrwlqr gdfirlknis igynldqeml eklnirrlrv ylsadnywtw kresnlddpe
     1021 qsfngitnnr stvlktlslg vnisl
//
LOCUS       WP_093868923            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Tenacibaculum].
ACCESSION   WP_093868923
VERSION     WP_093868923.1
KEYWORDS    RefSeq.
SOURCE      unclassified Tenacibaculum
  ORGANISM  unclassified Tenacibaculum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="unclassified Tenacibaculum"
                     /db_xref="taxon:2635139"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114731
     Region          25..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lllalvvqis faqektisgt vsdesgplpg vsvlkkgstq gtetdfdgky
       61 sikakegdil vysfvgmktt ekivgassti nvtlendnvl nevvvtalgi kreakslgfa
      121 qqtvkgeqlt qtrevdinns iagkvagvqm lgapssgfgn alirlrgesd llyvvdgvki
      181 dnsgdinvdd veslnvlkgs gatalygpig kngvvvittk rakngktsfv idqalqvsnv
      241 yilpeyqney gggysqtfst lngqnipnya adeswgpkld grmvrhwdsw ipgssefgnl
      301 rpwsanpdnv rnffntgitn nttlsfskgg dgysvktilr nvdiegvlpn skrnlkqvsa
      361 sasfdvsdkl evytninyqy rttlndptgg ygsiasnfnq wfqrqldmnr lrdsyfqggk
      421 fytwnirsts nvnplywdsp yfetdqnikn qtknavygnv ginykitdni tlnteirrtv
      481 ntyksdarva fgglnqtsft erdrtisste ffamatynkd ltdnldltas vgtelrqwqd
      541 ryidgatsgg ltipgvytva sskdrptytn rewnrknrgl fataslgynd mlfldgtvrs
      601 dwnstanpnd nrvltyggsl sflfnkvinl eelsfgklrv gyaeapsfpn inatknvfqt
      661 gnslngvvpf fpsatqanag iqggirqefe igtelkffrn rlgldityfd rkdinlpidi
      721 plsgatgfna stvnsgkfss ngievaingt piknenftwd vglnfatlkr qvdelyvnpt
      781 tgeaittdvi dtswrgltie arvgeeygai ygrkirrdan gnmllsstgs iqfdqnqylg
      841 nllpdftggl tnsfnykgin lsfsldfqkg gkyfsvtqmf nnyaglgiat vgdnakgnpv
      901 rdplvdasga vasgtsinan nvsnttggvl vegvdatsgs aasyfvdsqt ywkrlfalhe
      961 rwiydasyvk lrqlslgytf pkkifentpi etitvnayan nlwliyssvd gvdpseienv
     1021 nnaglrweeg gqlpssrtfg mnikvkf
//
LOCUS       WP_093869143            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. MAR_2010_89].
ACCESSION   WP_093869143
VERSION     WP_093869143.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. MAR_2010_89
  ORGANISM  Tenacibaculum sp. MAR_2010_89
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Tenacibaculum sp. MAR_2010_89"
                     /db_xref="taxon:1250198"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111727
     Region          25..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknkilllf cfsflvtqla lgqektikgv vtskseggpl pgvgviikgt tkgvetdfdg
       61 kyqikasvgd vllftylgmk aqskavtnqs vtinialedd nvlnevvvta lgikkekkal
      121 tysaqevngd eltkvkqtnp inslsgksag vtitrsssgv ggtakvvlrg nssttnndpl
      181 yvidgvpmln sgngsngsep gtdifgsqtg nrdggdamsl inpddvesit vlkgasasal
      241 ygsqgangvi lvttkkgkeg rlsvnvsssf tvdnvmslpk lqseyqsasv gspiaengrv
      301 tdpkswgaka qglsndaksf fntgytains valtsgnakv qtyfsyantl aegvvpgnrl
      361 vrnnvtlret akflkdkini sasvnlsdqr iwnrptngly snaltgvylh pvgidrdiyk
      421 nkfeyfnqtt nmmdqyassf deniqqnpyw linrnpsqdi vqrvlanvsa kyqvtdnfsl
      481 qsrvsydksf ftfdkkqyag tdpvnsgdng ryvlektent qqyidliany skdfsedltf
      541 tgllgtsltk ysigdqilld sgrdgkglnf pnvftianfe ttnnirqsvg nrevqsvfgs
      601 anfgykkmlf ldvtgrtdws stlvntnsts ffypsigltg vlsemfempe sinfgklrvs
      661 yaevgkdipv yatlplnkin qtntgistap fapiegetle perqkafeig tewrflnnrl
      721 gfeltyystk tlnqiffiqa epnpngysqn ivnageisnk gielvlngkp irnenftwnt
      781 vlnfaqnknk vvsvhpslqd geaivtargv ngyefslieg edfgsikars lvrnqngvpv
      841 intsgalkst efktvahaqp dftlgwsnsf dyknftfsfl idgkfggdvv svteavndky
      901 gvsqatadar ntnggminvv neagvasqit aqdyynaigg rdgmlgeyvy datnvslrel
      961 sigyklpvkg effksvrlsl iannlfffyk eapfdpnisa stglglqgvd ifnqpstrsi
     1021 gfnvninf
//
LOCUS       WP_093871108            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. MAR_2010_89].
ACCESSION   WP_093871108
VERSION     WP_093871108.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. MAR_2010_89
  ORGANISM  Tenacibaculum sp. MAR_2010_89
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Tenacibaculum sp. MAR_2010_89"
                     /db_xref="taxon:1250198"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121117
     Region          26..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 manrklllti ftfivsisfy aqnasikgvv sdgtyplpga svkvvntakg sntdfdgnfk
       61 idnvkpgnlv vsisfigyet kiinitispg etknietvil kqlseqlnei vitalgikke
      121 ekslgysvst lkpkelneak etnlvnalng kiagvqitng ssgvgsssrv virgevslns
      181 skngplfvvd gisinnrtyl stmqntggse mqevdygnga aeinsddies isvlkgasat
      241 alygsrgang vilintksvr rnkrlqvsvn tgltmesvlr lpkyqnkygq gwagdfkyvd
      301 glnnslgsnd qedvswgpla ngqlitqfds ptinglragd ifargwvrda dgriispsta
      361 pndiiatpfe akpnnvkdff rtgytstiga svgfggeksd ilfslglldn qgiipntdlt
      421 rksfrvngsv dvtdkmklsl ktnyinsksn nrpssgygse samyiftwyg rtvntnslke
      481 ywqrgyegle qfnynyawhd npyfmlnent nsfdkhrilg nikleyqftd dlklqarsgm
      541 dyyadkresk raystqrflk gaykdervdf kevntdvlls ykkdlndsfg lsvdfggnim
      601 qqeanflynv anklvipeiy nlknsalplv tdqyklekei rsiygvvgls fdnklfldit
      661 arndwsstlp ednnsyfyps aslsaimsdi felpeafnff klraswakvg ndtepynlkt
      721 pyqyqlpyag nrtlsrgnvl lnenlkpeqi tsyevgtdir mfgnrlnldv tyyksisedq
      781 iisvpisntv gyqrqvingg kiqnqgieal vtvkpiktdn fqwassinft knvgkvlelp
      841 egtgdvlttn fasvysaegs kvfiqarkge rlgnmygrrf kryngkiiyk ngapivedel
      901 kllgnynpdf svgfnnsfny kgfsfsflvd wkqggtlisr tkqvgtyagn legsldrndy
      961 kdivpdgvke mpdgsyqplt sadaigwwsy ykplynrksn qetgivdaty vklrevkfgy
     1021 nvpnsfaekl gmeslrislv grnlalwtps snphfdpetl alqgsnivpg iedvsypssr
     1081 syginflfkf
//
LOCUS       WP_093873088             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. TLI_105].
ACCESSION   WP_093873088
VERSION     WP_093873088.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TLI_105
  ORGANISM  Streptomyces sp. TLI_105
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces sp. TLI_105"
                     /db_xref="taxon:1881019"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52241
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgvlkear agehrvsatp atiepirklg ydvvvdsgag vaagftdsay eaagarigda
       61 taadvvlgvn apspaqldgv rpeatvialf apafdpamve dlgrrpftal smdavprisr
      121 aqsmdvlssm aniagyravv eaahtfgrff tgqvtaagkv ppakvlvaga gvaglaaiga
      181 agslgaivra tdprpevadq vrslggeyls iespevevsk tgyakemgdd ykarevelya
      241 aqcrevdivi ttalipgrpa ptlitaemva smkpgsvivd maaanggnve gtvkgekvvt
      301 angvtiigyt dlagrlpaqa sqlygtnlvn llklmtpgkd gqlvldwddp vqrsitvvre
      361 gesawppppv qvsaapapap ataetkpakp kkepmtparr fggvavaala lflaagfapa
      421 allphvtvfv laivigyyvi ghvhhalhtp lmsvtnaisg iivvgallqi ghsstavtvl
      481 ssvaillasi nvfggfavtr rmlamfnrs
//
LOCUS       WP_093915922             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfitobacter marinus].
ACCESSION   WP_093915922
VERSION     WP_093915922.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter marinus
  ORGANISM  Sulfitobacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sulfitobacter marinus"
                     /db_xref="taxon:394264"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55340
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egerrvamtp esalqlqklg heclietgag lasgfddaay taagvkvvkt
       61 aaalwkaadv vakvrapdda emkklrsgqt lisffspvad eakmkaaaek gatvvamemi
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqvesmg aefvyldfee eqqdgsasgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvaam kpgsvivdla aekggncklt
      301 kmdekfvtdn gvtiigytdf psrmgaqast lyatnirhlm tdltpekdgv inhnmeddvi
      361 rgatiayane vtfpppppkv aaiaaapkka avkeltpeek raaetaafkk qtksqvtlla
      421 iggalllavg lvapasfmqh fivfvlsvfi gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgsf lviilaalsv fmcginifgg flvtrrmlam fqks
//
LOCUS       WP_093917801            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093917801
VERSION     WP_093917801.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115427
     Region          25..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkialllai fafglqsvla qtneitgtvt saedgssipg vsvsvkgttl gtitdfdgky
       61 tlkvpenatt lvfsfvgmqt qeapingatv nvqmeadvvg inevvvtalg iskerkslgf
      121 astsvsseef aeaktinpmn alqgkvagvd issapspggt qnviirgtss fssnqplyvv
      181 dgvpitnsqv qtgsslnwnt dfgsglnavn pddietmtil kgaaatalyg sraangvili
      241 ktksgkntgg kmrvsydgsi tvqnvgripe rqskfgqgws gdhaldengn wgpkydgqmr
      301 lwgfivnnsq llkpyafves rvrdfydygi syknavsvsg gnenttyfms vsnnntdgvl
      361 pedfdtykrt tlsskgshkw grlklsssin fsnektkavp sgqgnsvfrs lweiaedysi
      421 vdfkdyknpf fnldnyftpy glnpyyalfe ngseqkrnkf ygkvqadldi tnelsftyrf
      481 ggdfeatnte awvaivdipe dapsynaqsl dpgsysiakr aryetnhdaf lkynknfgek
      541 fslnaligan inergfqrvt geltaldvpg yynlsngtsd avasqyeskr rlwgafanae
      601 lgyndylylt vtarndwsst lppennsyfy pgvtgsvils elakesgmsl naidfaklrv
      661 aygwtgndag vydiypvfqk gfidnpgfpn vddlefplng inswmisnql gspdlapeit
      721 keyelglemn mfsnrlgfdv syynkltegl insqpldpss gytsivnnig dvrnkgfeil
      781 lfgspirtnn fewivsanys qndntvesla egeiflagyg gasivavegk emglfktfit
      841 qtteingeeh ivvdgngmpl stpdevvldk sinedfragl sntfkykgia lgatldlryg
      901 gyiysyqkdy mgwtgsglet tfndrnpfii pnsvalvnge yventtpvas adlhdfyseg
      961 gfnrtdeffi drsylklrev kltydlpkrf arklgvesvr asvvagnill wtpsenqyid
     1021 petttfgndl sakfgefgan ptnqnytfgl svtf
//
LOCUS       WP_093917799            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093917799
VERSION     WP_093917799.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115011
     Region          23..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkialllai faiglqslwa qtkeitgtvt ssedgssipg vsvsvknttl gtitdldgny
       61 vlkvpqdatt lvfsfvgmqt qeaeitgtti nvalesdvvg inevvvtalg tsrakkslgy
      121 asqgvsseel taansvspis slsgkvaglq isgqnfsgsq nilirgassf sqnnqplfvv
      181 dgvpisnenf nttstqnggg gydygsmtnd lnsydvasve vlkgsaasal ygsrgqngvi
      241 mittksgkag kksfsvevns gvnfetvsil pkqqkqyggg ygfetvsieg kdylipdyav
      301 deswgpkyeg qevlhwwgva dyeqgitstp qtapwvapkn dvksfyetgv syqnslnvvt
      361 tsdrsalrvg ytnvnmtgiv pnseqekhnf ningqsslfe diielnanln viktetmgrp
      421 qfgygdnsqs qkffqwgqrq ldfdklkdyi npdgtqrvwn rksltnpkpn ysdnpywtay
      481 knyqdddrtr ifgkaglkan itdylsasgn fyydtytfnq rervakgsqa lssylqinrq
      541 ateinlegkl efnrnfedfs vlamlgantr kndysrfege tngglvvdgl ynlnnsanqp
      601 llddfkreiq vnswfasasv gykdmlyldg tfrkdydstl ptgsneysys svsasflase
      661 llevdwldnl kvranygetg ngteayqvfn tylisdpfng spqftnddrl knqnlkpelt
      721 seiefgieaa flknrigfdi syynrdtknq ivpievsgas gyvervinag kinnkgveil
      781 lygtpvkikd fswditlnfa knqnevldlp egldkiqlar apfggayina vegatfqeif
      841 aydyvhdekg nkvvgedgiy ltsgeltsvg svlpdytagi hnsfkyknfd fsalidiseg
      901 gkyysitnmw gmysgmaegt avptsngnti redgiilpgv kedgspntts itaedwgvsh
      961 yhgngtpsat sifdasyikl revtlgytip kfvdiiesvr lsiygrnlav wgldnkgidp
     1021 etvvggsgni qgleggiipa trsfgfnlki nf
//
LOCUS       WP_093918018            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093918018
VERSION     WP_093918018.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113079
     Region          29..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktillmcl aligiiitps rasaqskait ghvmdaenqe plpgvsivik gttegtmttp
       61 egffkleasp gqtlqfsfig yatqeivvne sntinvnlkt dvqavdeimv taefgmkrvs
      121 rsigssvqni kakditdsgr esfisalqgr vaglnvsssg gtpgssttvv lrsitsisgn
      181 nqplyvvdgi pmnnstfnpg nladggasfs vrnldfasrg ndfnpedies mtvlkgaaaa
      241 alygsdasng aiiittkkgt agrarvsysn sfkwdkaygy pdlqtkyang argttnyyys
      301 grygglypqg melynniesv lrtgfssrqn vsieggsdka slrasasfld qegvvkttdy
      361 srmnvslsgk aklndwirfe gsmqfvsten tkvprgtsgp lymamrwpiv ddmsnymded
      421 gshmrmpnyy tdtdllnplf gmyknklyde sdrfissfva tispikdafl raqvgwdvgt
      481 styetsihpy yyndnggvgr ynlaksnfsy ptlnlltgyn ktikekfyis aqfgyhqien
      541 gvsrlatygs nyavidfqsi nnvdpstvas tkrtttrrvq alsgqvelay nnmafvtlra
      601 rndwsstlpv annsyfypai egafiatelp flkdnksvsy lklrgsvaqv gkdagpleid
      661 pqleateltg ggyqygytgp nknlrpemtt syeigfegrf andrintdft yfwthcedqi
      721 vkgfrlsyat gfvlnnmnvg tfdtwgwegh idadiiqtns glswnvgina shtksevvyl
      781 penvteyyna ytwnsgnirn gimvghpvtt ltgraysrnd agqilinptt glpiidetws
      841 vigdrepklr fgfttrfnyk gfslsallag rykatvvngt krtmmqrgts wesvdlresg
      901 pvvfdgvlrd gnentdtptk nnigvtydvy gssiytgqde dwlekdvnyl rlqelrlsyr
      961 ipskllrrtf israiihiag ndlatwtnys gidavgntvs aaaggtggeg ydvwsipnpr
     1021 gysiglnvtf
//
LOCUS       WP_093918200            1128 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093918200
VERSION     WP_093918200.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1128)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1128)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1128)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1128
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125347
     Region          41..105
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          118..1127
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikpdfrmr ppvlfillfl tllwtqpala qseglsvnls nqpikvvfns iqeqsdyrff
       61 ysddvidlne rysisfsnks iqealeilts ktqlsfkive eklivvsnqa iqssaflvkg
      121 rivsatdnep lpgvnvvlqg tttgkvcdfd gnyeievpne savlvfsfig fkkqvvpvna
      181 rpvvnvalee dvssieevvv talsierdkn slgysitqvs gddingakes npinslagkv
      241 sglqitkspt gvdgssrvvl rgvasmlgnn rplfvidgip mnagyggagr wggkdsgdal
      301 sdlnpedies msvlkgagaa aaygsrgang vilittkkgk nkkgigvsfs sgytaetpmv
      361 tpdfqyeytq gafgqyptla gnpakplady pwiwsygtki egqtetnwlg qeeqmtrqpn
      421 pydaffrtgs sfvntisfdg gnenttfras itnqdskgim pnndlsrqti nlrgfsklge
      481 klefdsklty irskvenrpy laedgsnivq sisilprnis lesmknntvd adgnmldwni
      541 dptfanpywv leniynadek nrlqgmfsvk wditdnfnal vrsgvdysna nskehenpgr
      601 psdgnpgkgs vaqtmgntme wntdflatys keyndfsfsl saggnyrynk ynsisqggrv
      661 mkvpglyhis nyesfgtsew fseksvysly slgqfsykny lyldvtarnd wsstlplsnn
      721 syfyhsenvs llfseafnln wdwldtgkir asfakvgndt gayeiaqyys iqqtqtdfpl
      781 agiggqlphf dlqpeetesw evgtnlsflk nrlvfdftyy ysvsdnqimn vdltpstgyg
      841 tkkmnagklq ntgyevqlna kpleskngln wdviltwskn kseveelygd meflplaeef
      901 hmmiqarpge aygmiyttdy krdafgnkli dkdgfaqage wkamgninpd wigginnris
      961 ykdlslnfli dvqmggdvys wgkaymglfg tsvetlegre ewnagtggfv edgvsesngq
     1021 pntvaidptm rwyniynrqi gtewiqdatn vrlrelvlay klpskwiakl pvenvnfslv
     1081 grnlfflyra mdhfdpetgf ssgntgngie hlslpsttsy gvnlkinf
//
LOCUS       WP_093919097             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sunxiuqinia elliptica].
ACCESSION   WP_093919097
VERSION     WP_093919097.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39982
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigllkesd sesrvaflpe vvaslikrkv svlvetgage salasdaaye eagasiaqrs
       61 evikqadfli giqapddklv aslsqekiwl sqynplwnie lvksfqskgl ttfsmdaipr
      121 strgqamdvl ssqatvagyk avleaalklp sffpmfmtaa gtirpatvlv lgagvaglqa
      181 iaiarklgaq vqafdvrsav keevmslgak fievegaqed saaggyaveq sedfkqkqqq
      241 ainehaakan vvictaqipg rkaplllpke avakmkpgsv iidlaastgg ncelskdnet
      301 vveygvsiig qsnypsqmpi daskmfgkni lnflellfne egefslnfdd aivkgtcith
      361 qgeivnervr siiqp
//
LOCUS       WP_093919551            1007 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093919551
VERSION     WP_093919551.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1007
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111447
     Region          27..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkmtkwall fsllfwsgig lthaqqktin gtvtdndknp lpgvnvveks tmngvitdvd
       61 ghyslavssg katlvfsfig mtaeevnvgd kttinvmmep dvigleevva igygsskkqa
      121 vtgsvskanl eayrevpvnn vletvkgivp glnvggtnra gqvaglsvrg qnstggnspl
      181 ivldgaiygg sigdissddi esltvlkdas aaavygsrsa ngvilietks grgingkpkf
      241 diklsygisn elerlevyda dgyiqrlldi raangletdp nniplylqde eqknyeatpd
      301 hrptltdpye mfrqnaynvr anvsvsnste nssyyisatm tdqkgvvlnd syknftgrvn
      361 issdltdwfn lgvkssysvr dfsgdspsiy rathfspwat vfnedgsykq fpqtttsfns
      421 pfweiatvdh dlqnnlngiv tgkisvpgvk glsytinysn slrwnernyf ynentingkg
      481 kngigqrsys rsvstlfdni vkynrtfaek hnvdvtllys rekyvyesma ayaedfdnti
      541 lldykledgk tqtastggge sfaigqmara tytfnnkysl tgtvrrdgys afsknnkwgi
      601 fssagfnwni skehfienid aindlalrvs ygsngnqsig lyqtlakvgt skylfagdps
      661 ytvtqsissf alndlgwett tglnlgldfg iinhringsv dlyktktsdl lfplslpras
      721 gkssitsnlg eiqnrgiein lhtlnlqkqd fewtsdfafs lnrnkvatiy gedndgdgie
      781 ddlissgyfi geplgtiyty kvigiyqqed mdngtimdgm rpgdykledi nedgkitsdq
      841 drqflgtske nfrwswtntf ryknfslmay lysiwggngy flsgnntpyy dgyanradln
      901 hpvydywtpt ntgamfprpd yssnaayrgt kyfdrsfikl qkvslsynlt dmvkpwgiqg
      961 mratvsadnl ftyaphwegl dpetgqgltd satpsirtyl fslsfnf
//
LOCUS       WP_093919897            1135 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093919897
VERSION     WP_093919897.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1135)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1135)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1135)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1135
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123838
     Region          40..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnntyslshs ipktlqflwl iipilltfel haqtatehiv sgtvtsandg qalpgvtvav
       61 kgtaigtvtn ldghyslvlp qpnatlnfsf igftpkevev ngqnqinlsl eeniealeev
      121 vvtalgikra ekslgfsvgq vegddltrva qenvlnsmag kvsgvtisst ggagstvsmv
      181 irgassmstd nqplfvvdgv pmastvnnvg gfgsdnrvdy gnaiadldpe sienvsilkg
      241 psaaalygtr agngvvlitt kkakadqgmt vqvtsntvfd ipsrflnvqs qfstgffsfr
      301 pedvgggilp eitagdatas gpendkgywa vqwdapldan gvpiptevis ypnnvrdfin
      361 dyaftttnsa aisnssgasn yrlgitnmth sglvpnsdln knsislaass kvrdnftvst
      421 dinftnswad nrpasnrgan pmqwaymhpa nidihklkdy gsgenvkrvs gnhenpyfla
      481 hevnnsfnry riygnliatw einsklsfma rytlnktdev reskiapgyl kepnngaygi
      541 gngnslernt dvlatykddw edfsltasag gnvlyskssv isnsskpgsg lnvpnlytvn
      601 ninsgalnys nsraekains vyamanlgwk drifidltar ndwsstlpge nrsyfypsas
      661 msimlnelvd lgpnvnllkl rggwaqvgnd tspyslyaty snqgqwgdai alakpsglls
      721 pqllpelats lefgtdirlf snrlrlegty ytvdnenqil giplaastga ssirinagll
      781 qskgwellig gtpiqnndwt wdlnlnfttn etrilelaed ldfvefwdna rvknigyvkn
      841 dalghdglvg nlysrkvqrv tdesspyygf pilgsgldae wmgeeayskv gnynpdfimg
      901 lqtslryknl slnmtfdwrs ggqyvsqtyr ylsenvitqt wldelvhpge lggaaseelk
      961 awvlehkdel llsdrlrpvg gptpeyggfp enfsgvtvyd atfapgvmgh ydengkfvle
     1021 qenlgnegtv flpyvvsypw digqanlfda dyvklreisl nyqvpdqlsr klgmqdvnls
     1081 lysrniilwt kdsklgvdpe rayqaegngr fsqgveryna dpwivpigfk lsftl
//
LOCUS       WP_093920032            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093920032
VERSION     WP_093920032.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125483
     Region          31..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrklkwlmk slftltvlfm gvgfviaqev kisgnvtsse dgaplpgvsv vqqgttngtv
       61 tdldgnyvvt vsqgsvvvfs figmethein adesktynlk mtpettglde vvvtalgikr
      121 qtkkigyaft evkgeeiasa ntvgtvqalq gksagvsiga sdgglfgnsk iqirgvsvln
      181 sdnnqpifvv dgvildnevs nahadwssns ndfgnqlknl npddyesvsv lkgaaataly
      241 gsrgingavv iktkdgqgqk glgvkvsqsv gidhafgqpd fqyvyapgam pgyidygnkd
      301 akgnyyrfdr nqvytngdgi itkqnfdwew mgygpkfdgr divdydgstt syspikdhml
      361 kayetgfnsn tsvaisggnd kstfylsdsy nhrtgvfpsn eftrnslrfa gthklsdwlq
      421 aeasisftts npknprnnla enfiggnwvn wydaekwnkr evyqaphggt pqsaysdani
      481 yvpgnstwfa ynmdvdsrke qvvrpivslt anitdwlsik aegnmnaynv saekkelgrg
      541 yaneggyykl hhikdvsqtg klvasinrql tddistnimf ggemwkqeks ytkvetdggl
      601 ivpgrfflgn skktlksegk iegtkqinsl yflanfgwrd qlflditgrn dwssalvytd
      661 gtgnnsyfyp svssswlfse tldtpnwlsf gklrvswaqv gndtspyyin pgykigkyel
      721 asggfvynna kstlsvdrni kpekknsfev gvdlrffsnr fgvdfayyne vinnqigevp
      781 ipeesgiknl ltnvgtlenk gielkvnvtp ikttnfewvs tfnywnnttt vtdlhddfga
      841 yrvlggivng gnfrvgsvaf eggeygvlms dilpkkyqse dpndprngmn vlvwsdsrrg
      901 affersneaq kvgkitpdfe gswdntfhyk gvtlsvllda rfgghvasya nrygtsygwl
      961 etslygrdpe yggvswesqy ddskgqtftd giipdgvfak gqeitspsge kvnvggmtyq
     1021 eafdagyvep thagfyhyft nswgqgvind swydelnyia lrnisigynl pksiaqkika
     1081 qniyvafnar nlgylyntmp nnmnpesfrg ttssgsflqr sivpntatyt mtlsvdf
//
LOCUS       WP_093920036            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093920036
VERSION     WP_093920036.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112469
     Region          31..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrrkkwlgk ylltllvlla gtgfiaaqtv tisgtvtsse dgaplpgvsv viegtttgti
       61 tnldgfytln vpsgsevafs figmqthrtt vsssatynlv mdpettglde vvvtalgisr
      121 ekkalgyavt evgsdeialv kdhnalnsla gkvagvvitq gtggpgsgsr vvirgnnsit
      181 gnnqplivvd gvpiddrgsn sggsvysstv tgggitdinp ddiasisvlk gpnaaalygs
      241 ragngvllit tktgkkgqgl gvsinsnitf dnpmelpdyq neygqgtqgn ipatvdelkq
      301 sagswgpkmd gssqlyytge erpyvaqssn vedffrtagk yinsvaldgg skdfsvrfsy
      361 tnnftesvlp nsklnshsfn lrgtanltdk fkvdakatyf iqdltnrvsq gsegvlayvl
      421 gmprnvdird letfqkpees lnsisysilg anpywilrhd entnrrerfi gftkvsydft
      481 dwlsafirig tdvanvkgns iskpghhfyt sgrmnvsqsr saetnadfll mfdkditqdf
      541 slaaqaggnh syrmydamti faedfkiptr vflnnartir ptntplqeke vnslyasasl
      601 syqdfvyldl tarndwssal skdnrsyfyp svsfsiltdh ffdpentvfn imklrtswaq
      661 vgndtgvyql ydyfniaqdg ylgrtqlsrp stkfnpdlkp enitsfevgl easllsnrly
      721 tdiswynikt edliynvpvp aatgysnfre nigementgi eilvggvpvq tsnfkwdvsf
      781 nfsknenklk dliegleshv lnttnsgnln iqatvnggfl diwgttwrrn sngdiwlnde
      841 gkprasadke klgnaqpdwi ggltnslsyk nlslrflida rvggeiysat eaaldgsgvt
      901 pktlqyreeg ivvdgvigde esgftantik isgqdywsay sgiasnyvfd qtnvrlremv
      961 lsykvprsvf dgtfiqsatv gligrnlffi ykdidhvdpe aslgtgnngq gilsynlptn
     1021 rsigvnlnik f
//
LOCUS       WP_093920313            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093920313
VERSION     WP_093920313.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111742
     Region          29..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfiqkhlvl lilflsllcs fntnaqeqit vegiitdaqt gesligatvi iknttsgvit
       61 nyeghykfgg lvpetilqys yigyesqelv vgsktiidiq lqpsskdlea vvvfgenqkd
      121 irtitgsvgk idtkvfsagt pagsfdqllq gqvaglaiqs sgepgekasi rirgnnslgi
      181 rakddaelvs anraneplyi lngspissdv fntinpddiv dirvlkdgls tveygtrgan
      241 gvieiktkrg ivgetqynvr yqhtvkpisg lggislmqss eklalerele ivsglgfiyt
      301 ptpsdseeea fiknkryrql eststnwlke lsriaqvkdl qlsisggadd tryylstsyy
      361 deqggfdnsw aerfttrfnl dhnfnddvsv gfdssvgrsk rskshsspas liytlqpyet
      421 ansddfiarn pitiggqyfe npfdelngry sdytswrvdl nsrlnwivse afnanasfgi
      481 tyndsennsv tlanklvqda gitkgkgafn kneskslasr lnlsldfrkr fndhsisvsg
      541 gteyihtknw gfgfnsigis dkvdpeigan pnatistakf ydallgfylr gnynfaskyn
      601 vtgsfrydgs silpedkrfv pawglgaswn iqkeswfeqf dvfdqfklra sygvnynsgg
      661 irqtlglpfy dftnndtylg drvinlvefw npdlkferar qwslaldfgl fdhsiygtie
      721 ayvkntddll aavdipasng ysdllrnigk lrnqgielql savtirtdhf rwttninfay
      781 ndneitdlyl qdeikvgseg yfkvgepins ayvkywagvn pengmplyyd enmnlvtggv
      841 apqmtgfgty thpvtggftn ifnyhdlevs tlftyawggv nynnlkarmi rnvkngevpy
      901 egfyndiwlk pgdvkplpyp kffsdtsvns lfvenasylr wkniiirynl seqlkikgit
      961 afkitaqann lltitgyegi dpeitgigqp lprsftlgvd vtf
//
LOCUS       WP_093920518            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093920518
VERSION     WP_093920518.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121679
     Region          107..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkfliillw giigtaspaf aqkisvnfdn lttrqavevl qakhnysfsm ntsgldmdkr
       61 ityqaknvel tevldkifee qgfkctvngq iitvlkndkl spaqekkklk gkvtdksgep
      121 ivgvtvvikg tttgiitnfd gffelevtsg qtlsvsfigy kkqeilvqdq eyiditleps
      181 vvdidevvvt algikreeka lsynvqkvnn kelttvknan fmnsltgkva gvqinssaag
      241 pgsavkvvmr gtksialsnn alyvidgvpm nnsvygkads gayssqpgte saadinpddi
      301 esmsvltgps aaalygyega ngvvlittkk gkagkttasy snsttfsspm mmpkfqntyg
      361 nlpgengswg getafrydpa nffntgvnlv ntvsistgnd ksqsyfsasa nnasgilsnn
      421 dydrynftyr ntttflddkf lldasvnyiv qesknmvsqg qyfnplpaly lfprgedfrd
      481 vqlyeryddn revnvqywpy gdqglslqnp fwimnrmnre ldrqrymlst slkynitnwl
      541 nvigrvnidn stskstdkry agtlaifagp kgryqlsqrd ekqtyadvia nidrtsglft
      601 fnvnlgasik drrmdshlie gdldkltnwf ttenmvrtvg vfkldddglk rqtqsvfana
      661 eigynrflfl tltgrndwds alawsesker sffypsvgls slvsevaklp dwftylkgrv
      721 aftsvgnsyd pyltrgfyiy deqtnsyeqs knkpnfnlkp eitnsfeagl nmkffdaals
      781 ldatyyrsnt snqthlatla dgeyekvyiq agnvinsgle lalgynkqwg nfewasnytf
      841 tynknkverl vsdflidgkq iematidkat lgsvgspllr lteggtmgdi ymtsdfkrdn
      901 ngyiyldpst qlpsmisles edykklgsll pkynmgwrns fsfkgvrlnv lvsgrfggla
      961 vsntqaildr ygvseysakl rseggvning tkvpaqdfln ivsegtgkad yyvydatnir
     1021 lqeisieyti pkkklnnvad vtlslvgnnl amlyckapfd pelvpsasnt fytgvdyfmq
     1081 pslknmgfsv klqf
//
LOCUS       WP_093921421            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sunxiuqinia
            elliptica].
ACCESSION   WP_093921421
VERSION     WP_093921421.1
KEYWORDS    RefSeq.
SOURCE      Sunxiuqinia elliptica
  ORGANISM  Sunxiuqinia elliptica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Sunxiuqinia.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Sunxiuqinia elliptica"
                     /db_xref="taxon:655355"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112645
     Region          31..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqikwfqr gfigvvlili sismafaqdv tikgtvtgae dgmpipgvsv vekgtvngti
       61 tdlqgmytlt apsgaivsft fvgmkaqevv lgtqaivdiq mapdavdvde vvvtalgikr
      121 eekslgygvs kvdseeiqss agsdvlssmq gkvaglelgs sqgglgssnr vvlrgnssis
      181 gnnqplyvvd gvpvnnstve vttgvwdrkd fgsgsmdinp ddienvtvlk gpnaaalygs
      241 raqngaiiit tksgkrgqgl gvelsssnmf dvvtdqflpk lqnkygqghy vdnvptystt
      301 atdnswglam agqslpswsg feenlnyspq pdnikdffet gfkttntial tkggensssr
      361 fsytnlygdg ivpgnvqhrh nfniraefkl adwlgvdtkv nylnqeiegg twlgegssna
      421 ifglfslprn tvlrelkkyn fnntpndpfv gtqmnpywts lhdnminkkd rligfakldf
      481 ditdnlsgfv rvgtdytdns veerynlghk qnssgqwiln qykrretnid gllsyrkqfg
      541 dldfganlgg nimknnsest ynrgddvisn gfwniqnyln knasyniyek qvnsayatln
      601 lgfrdylyld asfrndwsst lpqenwsyfy pavsasilin eiakltqinl lkvrlgyaev
      661 gndsdpyrla ttfginplln hngiplmdvd gtpgvpnlkp eqtasfefgm efraynnrlf
      721 adlnyysqst enqlfttrvs aatgyvnkyl nggevvnrgf elslggvpvk tgsfewettf
      781 tlaknkteik elaegidtqv ladlgnivgg vqiiakkgkd gygvimgmpd kvdgeyqlgn
      841 nnflpgekrv elgnftpdat fgwlntfsfk rfklrtlidg kiggdvmnat kgelsaagit
      901 entleyrdtg vevsgvnadg eqvtvemnaq dywgglanyg apwivdatnv rlrelslgyt
      961 frmnpdffik nlslnfnayn lffiyrdkda kdidpnqtwg tgnaqgynly nvpsttsygf
     1021 tvnvkf
//
LOCUS       WP_093924289             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfitobacter brevis].
ACCESSION   WP_093924289
VERSION     WP_093924289.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter brevis
  ORGANISM  Sulfitobacter brevis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sulfitobacter brevis"
                     /db_xref="taxon:74348"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55196
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtptetf egearvamtp dsalalqklg hecviesgag alagfddasy kaagvevvdt
       61 tealwsavdv iakvrapsea evarlrddqt lisffnpagn kelmeaaask gatliamdmv
      121 prisraqkmd alssmaniag yravieagnn fprfftgqit aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqvesmg aefvyldfee eqqdgsasgg yasvsspefr
      241 eaqlakfrel apdmdivitt alipnreape lwtedmvaam kpgsvivdla aekggncklt
      301 vpdekivtkn gvtivgytdf psrmatqast lyatnirhmm tdltpdkdgk inhnmeddvi
      361 rgatithagd vtfpppppkv aaiaaapkka pvkeltpdek raaetaafka atrsqvtllv
      421 vggaimllig afapasfmqh fivfalacfi gfqviwnvsh alhtplmavt naisgivilg
      481 allqvgsgsw lvvflsfvsi liasinvvgg flvtrrmlam fqks
//
LOCUS       WP_093926599             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfitobacter dubius].
ACCESSION   WP_093926599
VERSION     WP_093926599.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter dubius
  ORGANISM  Sulfitobacter dubius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sulfitobacter dubius"
                     /db_xref="taxon:218673"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55212
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif egenrvamtp esalqlqklg htcvietgag aaagfddaay eaagvevakt
       61 aaalwkaadv vakvrppsda evkrlrasqt lismfnpagn tdlmeaaakk gatvmamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee eqadgsasgg yasvsspefr
      241 eaqlakfrel apdvdivitt alipnreape lwtedmvaam kpgsvivdla aekggncklt
      301 kmdekivtdn gvtiigytdf psrmatqast lystnirhlm tdltpekdgv inhdmeddvi
      361 rgatitheka vtfpppppkv aaiaaapkke kvkektpeek radelaafka qtknqvtlla
      421 vgaavllgvg lvapasfmqh fivfvlavfv gfqviwgvah slhtplmavt naissiiilg
      481 almqigsnsa lviilaalsv fmcginifgg flvtrrmlam fqks
//
LOCUS       WP_093934746             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis thailandensis].
ACCESSION   WP_093934746
VERSION     WP_093934746.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis thailandensis
  ORGANISM  Amycolatopsis thailandensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Amycolatopsis thailandensis"
                     /db_xref="taxon:589330"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38403
     Region          8..354
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maaeneqltv gvvretgqge rrialvpkli ervsgrglrv vvepgagaga lladetfeqa
       61 gavigdpwda divvkvapps aaevaklkqg tiligflnpr gdpegiaale sagvrafave
      121 aiprisraqa mdalssqssv agyravllaa ekltrffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgaqttgydv rpevgeqvks lgakflelgi eavgeggyar elteeekaeq
      241 qrrlteaitk fdvvittalv pgrkaptlvt adavkgmpag gvvvdlages ggnceltkpg
      301 eevveydvti csplnlaaem pahsselyar nvtellellv dsegklaldf sdeivagacv
      361 agavaaeeee gge
//
LOCUS       WP_093952149             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis vastitatis].
ACCESSION   WP_093952149
VERSION     WP_093952149.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis vastitatis
  ORGANISM  Amycolatopsis vastitatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Amycolatopsis vastitatis"
                     /db_xref="taxon:1905142"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38295
     Region          10..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(24,79,98,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(53,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 madseqsqql tvgvvaesrp gerrvamvpk lvgrlaqrgl rvlvepgaga gahlsddayt
       61 qagaelgdaw gapivvkvna pspgeiakls rgtvlvgfld prgnpeglak leeaglrafa
      121 meaiprisra qamdalssqa siggyravll aaqklprffp mlttaagtvp pakvlvlgag
      181 vaglqalata krlgaqttgy dvrpevgeqv kslgaqfldl gieavgeggy areltpeere
      241 eqqrrlteai trfdvvitta lvpgrkaptl vtadavkgmp agsvvvdlag esggnceltk
      301 pgedvvehdv tissplnlpa empshasely arnvtellel lvtkegalel nfedeivaga
      361 cvagregsas
//
LOCUS       WP_093954858             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_093954858
VERSION     WP_093954858.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35891
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iinalgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaine lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlilndf acvvrechav frsvllrihe rkgivyheqd slntlmanlt argvisaeyv
      241 hkfhflsdvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 vap
//
LOCUS       WP_093964876             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ruegeria
            arenilitoris].
ACCESSION   WP_093964876
VERSION     WP_093964876.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria arenilitoris
  ORGANISM  Ruegeria arenilitoris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Ruegeria arenilitoris"
                     /db_xref="taxon:1173585"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55711
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeil kgenrvamtp esavqlqklg yecaiekgag aaagfsdeay eavgveivkt
       61 aaslwkssdi iakvrvptet emkrltkgkt lisffnpagn eegmelakak ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgsatgg yasvqseefr
      241 naqlakfrel apemdivitt alipnrpapk lwledmvkam kpgsvivdla aerggnvegt
      301 vpdekvvtdn gvtiigytdf psrmaaqsss lyatnirhmm tdltpdkdgq inhnmeddvi
      361 rgatatyege itfpppppkv qaiaakpkae vkeltpeekr aqeiaafkaq tkqqvtllgv
      421 ggalmllvgl vapasfmqhf ivfvlavfvg fqviwnvshs lhtplmaitn aissiiivga
      481 lmqigsgsfl villaalsif maginifggf lvtrrmlamf qks
//
LOCUS       WP_093966288             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actibacterium lipolyticum].
ACCESSION   WP_093966288
VERSION     WP_093966288.1
KEYWORDS    RefSeq.
SOURCE      Actibacterium lipolyticum
  ORGANISM  Actibacterium lipolyticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Actibacterium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Actibacterium lipolyticum"
                     /db_xref="taxon:1524263"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55555
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkevf egearvamtp esalqlqklg yecaieagag alagfsdaay eaagvevikt
       61 paalwkaadv vvkvrepnet eakrltkgqt lisffwpaqn ekmmelcksk ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfee qaqdgaatgg yaapsspefr
      241 ekqlekfrel apdmdivitt alipgrdapk lwledmvaam kpgsvvvdla aekggncdlt
      301 vkdekivsen gvtvvgytdf psrmaaqast lygnnirhmm sdltpekdgq vnhnmeddvi
      361 rgatvtyege itfpppppkv aaiaakpkek vkektpeeik aeeaaafqkq tktqvgllaa
      421 ggllllavgl vapasfmqhf ivfvlsvfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsvf mtginifggf lvtrrmlamf qks
//
LOCUS       WP_093975011             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Boseongicola aestuarii].
ACCESSION   WP_093975011
VERSION     WP_093975011.1
KEYWORDS    RefSeq.
SOURCE      Boseongicola aestuarii
  ORGANISM  Boseongicola aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Boseongicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Boseongicola aestuarii"
                     /db_xref="taxon:1470561"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55322
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkesa sgearvamtp asakdlqklg yecliqkgag eaagfsdaay kkagvsvvsg
       61 aalwkdadiv akvrpptdae akklsanqtl isffypasne tlmetakeqg asviamdmvp
      121 risraqkmda lssmaniagy ravieagnnf grfftgqvta agkvppakvl vvgagvagla
      181 aigtstslga itlafdvrpe vaeqiesmga efvyldfeee aqdgsatggy aavsspefae
      241 aqlkkfrela pdvdivitta lipnrdapil wtkdmvemmk pgsvivdlaa erggnceltv
      301 kdekivtknd vtivgytdfp srmaaqssll ysnnirhmmt dltpekdgqv vhnmeddvir
      361 gatithkgei twpppppktk aiaaqpkkdk pkeltpeekk aaeaaafkke tktqitalai
      421 ggalilavgl vapasfmqhf ivfvlsvfvg fnviwnvahs lhtplmavtn aissiiilga
      481 liqigsssti itilsmlavl maavnifggf lvtrrmlamf qks
//
LOCUS       WP_093976984            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093976984
VERSION     WP_093976984.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114242
     Region          25..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklsgilt lflalivqls faqektisgt vtdqdglplp gvnilvegtt tgtqtdfdgl
       61 ysidasvgqv lvfsyigqkn armtvgasnt invqmeedaq aleevvvtal gikrnprslg
      121 ysvksveaes itensepdli rslngkvpgv nvnvstgvag asnkisirgt tsfqggnqpl
      181 fvvdgtpysn tevetssqit ggggyetgis sldpndianv evlkgavaaa lygsravngv
      241 iiittksgks gglsnkkfev slntgvyfek ianlpeyqnt ygngtnfnyn nangswgarf
      301 dsletiptwp nllnafpdqf gptvpyvaqp nnvkdlfktg fvadnsvnis sakensnfsl
      361 tisnmdqqgy ipfnsykrtn isaggnfkle nglqvganls ysdsyqvgpf lgenqfvgaa
      421 ssfartlvlg rtwdlslpye dangapvipn ggwdhplwsw ehnqirtgvn rtvanvnfay
      481 dfnehinary qlginkydla rveitdkgsr aasgtgrvvt dnydseeies tfvvtfnydl
      541 aedlnmnllv gnnvnqrsdh rvgytgtnli adgiftvnnt anvvsdvdei srkrivgvfg
      601 dlglgykdyl flnatarndw sstlpktdns flypsvsssf ifteafglkn diisfgkirg
      661 gwanvsrdad pyqinkifsv gtvyagqpsv fvpstlgnps lspenteefe vgldlelfnn
      721 raildftwyk ktttdlisev nvptssgyts fltnigemen tgieigltli pirtenfrws
      781 tftsftkndn vvneliegld rfplnvneia fvdegepfgv fygtafardd egnylieegg
      841 ggilqalenk aigdpnadfk igftntfkyk tlslqaqldw keggdvfsst vesllgrgvt
      901 kdtedrertf iipgfygnpt tgeaildgsg nkipnttqit mnnlyfsptt nsntfginsv
      961 deatiydgtv frlreialay evpkkfldkt figamtfsiv gnnlwyyapn vpkytnfdpd
     1021 vtaygsgnlq gievssapss krfgfklnvt f
//
LOCUS       WP_093977103            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093977103
VERSION     WP_093977103.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119113
     Region          25..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskltwila pimgllmsfs yaqektisgt vtdqlglalp gvnilvegtt ngtqtdfdgn
       61 ytiqgsegqt llfsyigqms vtkvigesst invvmqedaq aleevvvtal gisrdkkslg
      121 yatqevqged lstvksgnfv nalsgkasgi qirknnnlgg stnvvirgna sltgsnqalf
      181 vidgvpvnnt ntnskyqgea sgnyydygnt asdinpddie svnvlkgaaa salygsraan
      241 gvimittkkg kdaagigvtv nsgitigsid kstfakyqdq ygagygayyd gpggywyeed
      301 itgdgnddqv vvytedgsyg apfdpnllvy qwdsfdpdsp nyrtatpwvn akngpisffe
      361 tpvtitnsvs farsyeddgs frlnytqfdq sglmpnssik khnfsmsgsf altdrltvtg
      421 yanyinqkal grnstgyndn iisnfkqwwq tnvdikdqkd iyfdtkrnvt wnpatseags
      481 apifwdnpyw tryenyqnds rnrfignvsl dykftdwlnf taraatdtys eiqeerrang
      541 svptsfgipd sagnrgnvds gygrrnlqvt etnydfminf qkdlsdqfnl kgilgtnirr
      601 sefesiysat sgglsvprly slqnstgpla lpvendekvg idgiyasasl gynsilfvda
      661 tirrdhsstl pednstfyyp siatsfvftn llnadfitfg klranyaevg nsapfdflyd
      721 tynvnippga pstsvdnekk npnlkpekte sfelglemkf lrnrlsfdva yyktnsvdqi
      781 fgvpvsratg fqkkilnage ienqgvelsl sgnpirtedf swtamvnwtr nrnevvsled
      841 gietlqlgdf qggvtlnaev gqpygviygt dytylngerv vdpadgqyik tstsdqkigd
      901 tnpdwlmgis nkfnyknfsl sflidiqqgg sifsldqyyg ratglyeeta findlgnpvr
      961 ntladgggfi negvnpdgat natrinanrf gafgyrrglp dkafvydasy vklrevaliy
     1021 nlpsrlladt fltnaslsli gsnlwiidkn iphedpeggl sagnlqgysv gslpttrdfg
     1081 vnlklqf
//
LOCUS       WP_093977652            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093977652
VERSION     WP_093977652.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116105
     Region          25..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnktsivmif affafimgys qvvftgtvld ennaplpgas vvikgsakgv atdfdgnfqi
       61 elnsasdill vsyigyipte latsgktsae ivllpdsekl nevvvtalgi traekkigya
      121 tqkmdveiie einapnvgnl ftgqvaglsv snptglfqkp sfslrgkspl ividgipvet
      181 dfydvsanni anvnvlkgtt asalygsrgr ngailittkn anvdgleisv shntmvsagf
      241 tvfpetqtey gngsngkyef wdgkdggisd gdmiwgpkfe pgvlvsqwns pildnvtget
      301 ipwwgdvygt qyddksrysr vptpweyhnn lkdfmgtgyi sstdfsissk sekgsfrlsg
      361 nysdqkdrvp nsglktgglt fksttnlsks ltldsklsyn kvyspnyprh gygpknhmyt
      421 iliwmgddvd gqdlkehmyv pgqegyrqan fnyawynnvy faanelnqky dadlinaqmv
      481 lkyniaegln lqgrgsaviq difedrqspk tylnygdare gdyktwnskr ltvdydilas
      541 ytksltedis fdvnagastf yrkyqqeyns tdglvvpfvy slnntsgnva attyvqerat
      601 nsvyatlgld lynavfltaa arndwsstlp kenrsyfyps vslstvvsnf vtmpeavdyl
      661 klygswaqvs sdlnpystes yytnsgvfgg niklqypngl vntniepess nsfelglssa
      721 flknrlaldl tyynvvdtnq iidlpisnts gfenrkvngn eyttnglevv lnakpiltdd
      781 fswnvtanws rkvqkiteiy gnnttynnlr lndradsyya tvwqksadgd lilganglpi
      841 rdnfpqllgh ndqdwtlglq nsfkyknltv nvgidggwgg lirsltvekm wwggkhpnst
      901 eyrdaeyaag vqvyvpegvq vtggdlvqdv ngdvisdtrt ytqnttavsw qtwsqnypyr
      961 aavtykesek fanifdrsff klrtlsfnyd ftelaningv knldvtlsgy nllvwkkadi
     1021 idpdfgndnn lqdpstryig igvnvkf
//
LOCUS       WP_093977902             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093977902
VERSION     WP_093977902.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106513
     Region          26..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqklikknm flfflmapll llaqdvvkgk vtdsslgdpl pgvnvvikgt ttgtttdfdg
       61 nyelsvdnfp silvfsslgy askemqvsgp stlnvaldes atgleevvvt glatsvkrsn
      121 aanavasvsa deltgrtppq tldgalagkf agaqitaasg apgggmsvkl rgvtsingqg
      181 qplyiidgvy vnnnsvyagg lneisnaagg gasstdsqdn asnriadinp ddiqnieilk
      241 gasasaiygs raaagviiit tkkgkagktk invsqalgwn eavnllgqrn wtaalaesvy
      301 gegalytaae sagrlrdyek viygekgfit ntnlsisggg ektsffgsft nneedgivkr
      361 tgaskqslrl nvdhritddi klsltgnylk ssadrgffnn dnsnttigvs llftrpwdyl
      421 lpdadgnypd hpanssnqih trdvmtnnes vsrliaggal dvnlfrnenq slkmilkagv
      481 dtytlkttvf fprelqfmsp avggvdglss dgttqnadan fsgflvhnfr tdnelsfttq
      541 agvtneqfsq ntvrvtstgl iaseqnvdqa anvkvdqfrl eqedagffvq eevnyqdkiv
      601 gtlgirgdks snngdanklf yypkaslaan ihnfdfwnie amnqlklraa ygeagnfapn
      661 galfttyins lisgnvgiit patlgdpsiq perqkefeig ldagffnnkv tleftwynkk
      721 vedlilqadn epssgytfrw anagalenkg aeiglnvnaf dsenfswdsg iiwfrnrsei
      781 teltvasfdt qgfgtglgtf rieegksatq ivgndengnv valgdaepdf qmsfnnnfky
      841 kdftlsffwh wkkggdnvnl srllsdfgnt sadydkmnld psgtlnngdy rksafgggfa
      901 dpfvedasyl klreiglyyn lpenalqklf ngnvsnvkvg lsghniinif dynsydpevs
      961 nfgstaagig ievapfpssk rfmfhlsigl
//
LOCUS       WP_093978139            1123 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093978139
VERSION     WP_093978139.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1123)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1123)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1123)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1123
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1123
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122967
     Region          68..1122
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkillnirgv rscpprdclk ikltillffl tlfniranvy sfdhlmpidl adrdrnelgv
       61 neivsqqiei sgtvkdvdge vlpganivlk gtskgvvsdf dgnftiavpn aqailvvsfi
      121 gmetkevvvg nntslevlld yaaekmdevv vtalgmkrek kalgyavavv eaealnqqpn
      181 tnvlsglsgk msgvqinemg gdinakmnvi irgqtsltsn nepllvidgs pvgntdamrd
      241 issldiasvs vlkgasaaal ygsragngvi littksgega kqgigvsftq sttlsvpysy
      301 felqntfttg qkgqfnessw qywygpragv evvqwntngq pqplvmydns lqdffqtgls
      361 tqtdasvsgn ydrgsfnfsi nhmksdgitp gmelkrlgfs latsykitdk vklttnitis
      421 kptsdnlplt nngsddiymd ifanpphvni ndlkdyweie gskqrragal pnnpwfsaye
      481 rdrtldqirg fgnvrldidi lpgltamgrv aysannekie siypwsydgf gssavkpfga
      541 yeqtkldere anvdflfsyd kkvgdfrinp svggnylnsr ntslygggdv ltlpalytls
      601 nvarpglgyn sgvfekeiys lyglaslsfk emvyldltar ndwsstlpke nrsyfypsas
      661 lsmlvsemtq mpswvslvkl rtgwaevgkd tdpysinpil nqtfwgndiq ysvpaslpnt
      721 alkpeiatsy evgtdlgfvn nrivfegtwy ktqnrnqiig vttspmsgfs satinagnve
      781 ntgielalnt vpvrtadfew nlgfnftkqe srlvelvegi drigvgnags ltqqtfvggi
      841 igdlystsvl rvesgeyegw pilnnngglt fqtdnalkpk vgkstndfnv gmntsvkykn
      901 ftlsanldwr qggnfysetm krtarsgwvd kwqgdagtfs gvlgsnsfdg drtalaneik
      961 snpdvyqadn iwiggrdaqt ggfeyngfnn gsfwpgvikn sdgtytenfg gpgtvlfday
     1021 kvvepggglw dvgssfmydl sfiklrnitl tydlpqkfas kisaqrvsfs vftknimlwn
     1081 aadigidpel ayyqnngsyd igkekwnalp wvapvgftin ltf
//
LOCUS       WP_093978271            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093978271
VERSION     WP_093978271.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115914
     Region          33..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnlfkkvrc salilmmllc tlfsaslygq dgfmvsgtvi ddlglplpga sivekgttng
       61 vvsdfdgnfs fevanpnatl tisyvgfetq elpingnsvl nvtmqatast ldevvlvgyg
      121 avkkkdltga isqvdadals dqstnsvtdv lrgnvaglsi glspspkgts qirirgnnsl
      181 sagssplivv dgmiyngdls diapsdidkl dvmkdassaa vygargasgv ilvttkrgts
      241 dkptinints vgiatdayke rpysaqgyad wrtdvfksin pqntiddpgr ydnpnnlpag
      301 vtldqwlayd gsagdptraw lnrigfqdve ignylagnsi nwydriiqtg frndintsis
      361 grngglnyyw slgrtsnegi yagekfealr srlnldakit dwltvgmntq fakrnegfia
      421 adrlqierss pwgsefdddg nirlspqddn gagavnafla qkfndridld htfnsrvyak
      481 vklplgfsye vgytsrlefq eyynhalaes penivgsaer tvtkinewql dnifrwdkti
      541 dkhsfnlmfl vygekfqsyl srsrantfep tdalgysame lgtvqtvdse detstgdavm
      601 trlnynydsr ylltltmrrd gysafggnnk rayfpsiaga wtisnesffn sefvnflklr
      661 lsygengnrd igrftalsrl nankylnvda ggnvitvptf dngtqentel rwertkatnl
      721 gldfslangv vegsieayqn itndlivtrq lpniigfdnv ttnlgeienk gleftlatqn
      781 ynrenfqwst sfnfslnrnk irklygdlde ngqeldditn qrfigeatdv iwgqeaigiw
      841 qtneaaeaae ygvfpgdwki rdvdnsgdft vednvfmghr tprfswamsn rfsllknidf
      901 sfevysnwgq krvfneaknr ngfidrtnsi qtpywtpdnp indyarlfss dgsssfsiwr
      961 dasfirlsni tlayrfpkpi lekislqslr iyanarnvav yaphwdfydp eptniegrns
     1021 dgdvdarqpt prfftigidl sl
//
LOCUS       WP_093978278            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093978278
VERSION     WP_093978278.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118874
     Region          48..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrktkllg llfsvgvaql lsanmlednl yaktvasinv dsnwqqlitg tvmdedgvpl
       61 sgasvlvkgt tngvvadfdg kfsievdses ilvvsyvgfe tkeikvglek dlkitlaagn
      121 aleevvital gikkekkrig yatqevkgvt lqkaitpnvl esmsgkvagl tvisngadff
      181 sdpsiflrge kpilvvdgvp mpdtdfwnis sddienitvl kgaaasalyg slgkfgalqi
      241 tmksgkgidg trvsvnsstt fqtgflripk aqtqygpgnt gryefgtgaa ggggvndfdy
      301 siwgpkfdgr likqsdspid pvtgeriptp wisrgpdnlg nfvetglvts nnvtlqsgse
      361 kgnyvisnsy khakgsipgq kldintlrlt gtlnvsdais vdaslqynyq ysdnrirgsy
      421 gptspiylls iwgganfdvr nlehvwvpgk egikqdfven wrynnpyala ynwkkpwtkn
      481 diltyakvnf kisdkinafl rstlstyslt dneeiskdiy nydipdrggr frynayryfe
      541 nntdflitys dnffnkdvsl eatlganqry lnrqeehast tqlivpevft lqnsvdqvtp
      601 tsykysqgvy sayavmdfsy rnrvffgmtg rvdksstlpe andtffypsv yssivlsdmi
      661 kmpsvisylk lrtayaqvgg dlgiyeatns ystgryrnlp tanfpatlen pdlrpsftns
      721 feygfemkil nsrlgidfsy yenqngpqif tqpfsaasay egvllngrtt errgmdfsit
      781 aipvrtknfn wsaiinfdks knyltslppl pdgtipeweg dfganfrnkv gtpigdyfyy
      841 vwerspdgql iiyenglpkr tdfkvntgnt qpdfiasinn sfsyknlsln flfdgrfggv
      901 tqdayerdlw ragghpdaih perelsniay vnggdaktmq iegvtivsge atydpdgnil
      961 tdtrvfepst ykvdyqswas rykadwpsvi kdktfiklre vvvtynlgkk lldktfmdsa
     1021 sfsvigrnlw ywtkddyygd ldtytltqgd tglqlpsqrs igfnlnvsf
//
LOCUS       WP_093978891            1130 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093978891
VERSION     WP_093978891.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1130
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123699
     Region          25..1126
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkfhyyll lasflfvqgi taqnktvsgt vkddvgtplp gvnvvekgtt ngtstdfdgn
       61 ysisisnsgt lvfsslgftt iersvsgvst invsmeedse qlgevvvtal gikreakaig
      121 yamtevqgee larinvvnpv qslqgkspgv sigasdgglf gnskiqirgv stlnssnnqp
      181 ifvidgvile natsgasadw nassndygni lknlnpddyk svsilkgaaa talygsrgin
      241 gvvlittkdg sgtrgigvsv rqsvgfdivy kgpalqneyg pgalagytdy gnqdgegnyy
      301 qwdtqqfyyn segqpslvnh pwgglsfgpk fdgrliedyd gnmvpylaqk nnmldayqtg
      361 intntsvals ggndkgnfyl sdsyndrtgt lpnnsftrns lmfrgsynla pwlrasasvs
      421 ftdsnshnpr ndisqsffdg tferiyntek ykqnqywqap hggvpnanyg deftnvpnrg
      481 lwfayennnn ynketvvrpi vtlaadvtdw ltitaegnmn hytteyenke lgsgyanegg
      541 yyelrhnkdv sktgkltfnf skditedlsg nlllggeiwe qeksytrswt dgglivpgrf
      601 ylgnslrtqr geggvsdtkq lnsayflanl sykdqlfldi tgrndwtsal vytdgtgnns
      661 yfypsvsgsw vfseatgtsn wftfgklras waqvgsdtsp ytinkgygqg sidnggnfvy
      721 tntvnttlvd rsikpelkds fevgadirff gnrlgfdvay ydetiseqig nvplpsesgy
      781 nnlltnigtl tnsgleltvm gtpikgnnfs wnttfnywnn ttkiddvhpd fgdykslggd
      841 isygnfrvgs vafeggeygi lysdsapkkf essdpnhpnn gmnqliwvds rrgayfersg
      901 eaeevgkvqp dfegswnnef nignfnmsil ldarygghma syssrygtay gytesslygr
      961 dpehggvtwt sgyadvqgtq fsdgvipdgv faegqmvtap ngtsvdvggm tyqqaydagh
     1021 vepthatyyt yrlnswgngv indnwfaevk yialrnislg ynlpkmaask mgarniylgi
     1081 narnvaylyn slpndinpes frgttssdsf rersfspyla sytfsiaidf
//
LOCUS       WP_093979252            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093979252
VERSION     WP_093979252.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112266
     Region          49..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkipistgr grlffalyiv csqfiintit asalepiplv afqdpqvlis gtitdsqgkk
       61 vpgvhivvqs tttgsisdvd gsytirakpe dslvfsamgf atltvpidgr teiniqlked
      121 vaqldeivln agyysvteke rtgniatika etiekqpvgn plaamqghls gvnivqstgv
      181 pgggfsievr grnfingvsd plfivdgvpy gsqslgsvdv sgqitggnts plnainpndi
      241 esievlkdad ataiygsraa ngvvlittkk gtvgktqfka nlsstlgqvs nfldlmnteq
      301 yleirregit ndgfgmfldd pafdfvwpdi kswdnsrytd wqkeliggts yrnnaqvsvs
      361 ggnaqtrfli sgayqkettv fpgdanykka tvhsninhrs endrlmlnls tiysnennil
      421 prtdftslay rlepnapevy daegnlnwen ntwdnplaal eeryeakint lianavisyt
      481 vlpnldlkss lgfnryrlds yrtlpssarn pqfgftpqny stittngaqr qswivepqln
      541 wkkewnkvnl dilvgttfqq ettqqfvqkg tgfpnnnllq nltaaeilev lqdadseyny
      601 naifgrlnln llgryilnft grrdgssrfg perqfgnfga lgvawlfsee aifnesslls
      661 fgkvrasygt tgsdnigdyr fldtynitgf dydgttvlqp tgifnpmfgw eankkleaal
      721 elgffndrlf intswyrnrs snqligipla attgfseltg nfdatvensg fevdvrtvnl
      781 qngnfkwttt fnitvpkskl lefdgletst fsdrfiigkp ltivklynal gvdpetgiyq
      841 fedynidgni ssledrqwve dfapkfyggf gntfsygnlt ldmffqfkkq kafneltfaa
      901 tpgyrgnapv slldrwqqpg dtnpiqmasg glafgedtgv lqqrsnaavs dasfirlrni
      961 slnykvpttd snlevnvylq gqnlltftny sgpdpeqpss trlpplrqlt lglqvaf
//
LOCUS       WP_093979308             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arenibacter algicola].
ACCESSION   WP_093979308
VERSION     WP_093979308.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39548
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigilketl dgerrvaitp niakqliasg fellaeegag eyssfidsdy knvgvavekr
       61 avifheaevl lkinpfdeed lklvdkgqil isklyhksnp dlikaiankg vsafsmdaip
      121 risraqdmdv lssqnnlagy kavilgafem tkifplmmts agtiaparvl iygigvaglq
      181 aiatakrlga iveatdirse tkeqaeslga kfisvdnege eteggyakea sadyqkrqke
      241 avnkslfkad lvittanipg rkapilitee qvmhmkngav iidlaaaqgg ncevseinkt
      301 ivkngvkvig tsidprsvst nasdlyakni ynyiihltdg tnfkwdlgee itdetlivqn
      361 gtirkn
//
LOCUS       WP_093979373             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093979373
VERSION     WP_093979373.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110663
     Region          2..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mltvsylgfk pqellvgnqt qvtitlapda tqlddvvlig yqkvfkrdvt savssiksdd
       61 iegipvldvs gliatqatgi qsvnmtgapa grgaliirgn tsiggdidad layssplyvi
      121 dgvqtsledl agygvsnvdf laslnpndia sidvlkdasa aaiygsrgan gviiietkkg
      181 valdkpefsf stslglqpkp dlvpmlvgaa erqakmgmiq rwwhtdelqs gqtpmvltds
      241 inpafnnnvd yqglfyktgi dqqydfsvrg gsektnyrvs lgydnqegvi kgtgvdrvtf
      301 ssnlnfkage kfrnqlitrf thtdlqtgqg npyqgsfnln sslpvdpagl qsslfyitde
      361 rvqslsgele gklnedrtvn ftisnfatyd llpslslnsq lsfvydsnkk nfyepstirt
      421 egdgfasyal ynrknltaet ylslfkniga nndhevtgvl gnrvdynkye dmamtafgfg
      481 sdaiqtinnr ytqdqisgyt disanalvsy fgrvsykykn rymiggnfsi dgssrfgkdv
      541 rwakfpslna gwvisdepfl kphissfidy lkirgswgin gkqfpenylr fgkynlgygg
      601 npywanqmnv ssyggvtgvi pnydqignas lsweeteqwn vgfdldmfnr rvslafdayn
      661 kntdklffdv afpaysgyns aptnvagvin ygwesmlryh vfprenylrm elsvgfaqnk
      721 nyvsklpngn qdyigsdygy vvgrplnlyk mfindyiidd ldqlpvnpft geplqgksaw
      781 anirpgfpiw qdlngdylln eehdlklttd yspipditgs fninlqykkw yfqaysqfsf
      841 gadikntvln symdsydrgg ddwarrglad lseytfweqp gdgaagvdfp aiypqsptlg
      901 afygfrdnqt lwiesgdywk vnnasigytf dqndnfmkni glsrlriyga mlnpyqwqrs
      961 kkvvdasmvd akghtygngy pqartitigi dtkf
//
LOCUS       WP_093979387            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093979387
VERSION     WP_093979387.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114112
     Region          22..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miqkllllct fmltwhgfaq nvsgnvkdes gmplpgvtvl ivgtntgttt dfdgnfiiaa
       61 kqgdivrfsy lgmksqditv rsnaelsivl sedasaldev vvtafgvekk qkslgysvtq
      121 vntedlnlag qsnpmeslqg rvagvqinrt sgssgggvdi lirgitsvnp srsnqplivv
      181 dgialnndtf sgevrpsags nsassseqfa fsnragdinp ediesfnvlk gaaatalygv
      241 rasngaiiit tkkgkqgkak invtasttfr diqttpslqt tyregfsgap rtlydpdset
      301 gfnrvqnats fyswgprysd dsytlsngtv vdltgdkfys pydifrtgfn sqvnvsisga
      361 nekldyflsm gkdqedgvlp ntdygknnfr fkagykisdq ltlnssiayt ksggrrangg
      421 dksvmsalsy fsgtfpindy mnadgterdy sfgiidnpry lmetsslidd vnrwignatl
      481 nwspkewvnv tyaaqidnys dqrnryvgad ldggsqvggf ilnqninftg lesnllvaft
      541 kdwsddfttd ltlghqisds kreyaqarge glnvpginei gntinyfldn svtqlrnvga
      601 fgelklgykd klfltvtgrn dwlstlpken rsffypsasl aydvsdvfgd ndvftfgklr
      661 aswaevgkgp gfgdvgqyfv vdgdfpfgsa ggyrrstllg dldivpernq stefgadlrf
      721 mkdrirldya yyktrvkdqi ftvgtayssg lsgitrnagd yevfghellv sadiirskdf
      781 rwelilnwst segkvleipe diesiifads gfagitseir agdkmgnlyg ykwryedgqr
      841 yldadgfpei vldervkvgn afpdfisslg snfkwkgigf nflleykegg dlydsglrns
      901 irngnplstl vrdeevvleg vmdngsggyt tnttpalidq nyyrnsnvyn raaevlvqda
      961 swvklrnvsl sydmdnkftr dlkmeklsls vsasnilvwt pfdgydpegn qysagsnvyg
     1021 ftglsvplsq sysfglnisf
//
LOCUS       WP_093979577            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093979577
VERSION     WP_093979577.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109869
     Region          23..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvkklllffv lvfgayplla qsktvtgtvt datdgsplpg vnvlvqgttt gsqtdfdgny
       61 sieaesgnvl vfsflgmktq svtvgasnti nvsmqedaeq lgevvvtalg ikreektlty
      121 aqqtvradel tatrdpnfmn sisgkaagve ikksssgagg stkivlrgnk slsgdssplf
      181 vidgipmann kggqpgmwgg vdagdglsai npddiesisi lkgsnaavly gsqgangvvv
      241 ittkagksgk ttvslnsgyt fehylelpdl qfkygangna keswsttpgd yqssyveeff
      301 qtghnfnntv tvsggndktt ayfsygnita sgitpenkyq knnftfkqst kmfndkvtvt
      361 ssvimaleet knrlpagyyl npltglymfp rqrnfydfkn nyevfdtdrn lytqnwfvvd
      421 hhqsnpywii nkepktdesk riigslsley diaeklklqv rgnydyaake feqqhaatsn
      481 stnvhpkgaw dyrkyedqlv ytdailsydt dlsdnfslng vlgasyqktv ygdgvsvntg
      541 tigllypnef tfqnlptnvq vsstydgsvi kqgafanlql gfkemlfldl sgrndwastl
      601 altgndsyfy psvgltgiis emftmpeavs fgklrasytq vgnevpfnri npqnrissng
      661 gvdrntvkpf fdakpeiits lefgadwrff qnrlgldity ysltskdqfi evpllqsese
      721 ggyttkfina geitnkgwei tlnatpvqtd dfqwvtafnf tnntneivdi gpdddkvinl
      781 gssegyqskl veggafndly vlkflrndqg qilfdagkpl rtattelvgn ldpdwtlgwn
      841 nnfsykrftl gmqingkfgg nvfsqtesml dgagvsqrta dardaggvtv ngvdqtsgaa
      901 ittvdaetwf raigdrngvg eayvydrtni rvnqlslgyn idvsklglpi taaslsfign
      961 nlfyiykdap fdpelamstn qnaqgldnfn lpstgtygfn lkvtf
//
LOCUS       WP_093979739            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093979739
VERSION     WP_093979739.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120073
     Region          43..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkitefslk gnivsmlrkt iyscfpliff flslhsteaq dqinvkgtvs dsqnvplpgv
       61 sivekgttng vttdfdgvys invpanailv ytyvgmssqe ialngrqsvd vrleesaesl
      121 devvvvgfgt qsrslmsssv skikqteiqn spavnpvqll qgkvaglsvn vdsgqpgsga
      181 avyirggtqt dprsgsnepl yiidgvfred lngvspsdiq sievlkdaas taiygaraan
      241 gvilvttvtg kgsgkgsini rystgvdqqa kdynwtsved ylrvsriaaq kgvslnspga
      301 rltnanfgys vqelsekgef gferialtyl deltslegqa yvdgllnngy rtmtdpvtgr
      361 elifidnkln eirvrsaith dinvgmsgss emgnynisag ylnqegvvig taatrfntlm
      421 ngtfkinddl svngqftyqf ndidqprstn ntinrssrlp htyriwnddg tpalgettss
      481 prnifhelyy qdderkqfrt sskigldwni vkglsfspsa svyrlesngn fferaspeis
      541 nramsrfndt qnqvmldgll kytntfkekh nldillgsqy vknhyenfsg sgsnaptdli
      601 stlnaseter ervssdistn klmsffgkld ynfsrkyllg fsirrdgssr fsennrfgif
      661 pavsagwnih qeefwksdli skvkfrgswg kagndnlals dtqggfssts yalgsavris
      721 klpnynlkwe tttqtnigld lgiandrfni lfdyynkvts drllnmplpa qtgfssirsn
      781 fgsltnqgve melsgtliak enfswnlaan laynksevte lpdnefdknr sggliiwden
      841 gnetrvggla egerpngvwa yemigvyatd eeaanapddq gmsgyyrsqy ggakkggdai
      901 wkdvngdnii dsrdqvfmgy idpnfrggmv ntisfkglsl rlvqdwatgh viwnnfrars
      961 nansrnnvvt ntdvlsdamw keqgdiatlp rydnasgadn gprnhhrqsn iytkkgdyls
     1021 frevslsylf pqdisgklgm sntslglefy nlgyitqydg ltpeqfdgtd egiyprpfqi
     1081 rlrltasf
//
LOCUS       WP_093979777            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093979777
VERSION     WP_093979777.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113497
     Region          49..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnleyrgv irlcllyicf lvpppyfahf phghcfnsfs tldtqqqyqi sgtvtdsygp
       61 mpgvhvlikg sntgtftdan geysllvnnk dtlvysylgy htrelavlgr tnldvemqse
      121 vtelqevevn agyytvkeke rtgsisrvta adielqpivs plealqgrma gvevvqnngi
      181 pgnaplirir gqnslrddgn fplyiidgmp instpidggn nfylsgvdpl stlnlsnies
      241 ievlkdadat aiygsrgang vvlvttkkgn yrrkteiear wysglgqvsn kedllsteqy
      301 lairktalqn dgrqpdefsd ydlllwnqhr ytdwqevlfg gtsqimdfnv aasggngtts
      361 frlggsyhne glvfpgdnsy hkvtaglnld hisennklhm nfsanygidq sdvpaydnsf
      421 vamsltlppn apklknedgs lhweeweysq wdnpyaaily rnssdvghnl ianlglsyql
      481 fhsltfktnm gynnltrdyk asfskdqysp eiregqnhss rerhadrksw iiepqflyra
      541 kmgkgtldgl igatfqqnds knlivtgegf vstaligdla aaqsvniinn eikrykynav
      601 farfgynhdq ryfinltgrr dgssrfgpnk rfanfwaigg awilsgenfv kqnlpfisfg
      661 kfrgsygitg sdqigdygym dayeatagpn giyptqltnp nysweenkkl ettlelgfln
      721 dritlgsswy rnrssnqlvg yplpsitgfs svqanlpatv qntgwefela tmnirsknfr
      781 wqtflnltip knkllsfpdi eqtsyaniyr ighplnirll yeyegvdpet glyrvndvne
      841 dgqydfndai vvkklgreyf ggltnkfsyk gmelrflwef vkqsaleret slpgykamqt
      901 aqffnewqyg qnnnvqtvse sfdagtayyn alfserfftd asflrlrtls lsydlpakpl
      961 kdiglkgcsl flqaqnlftl tdynslnven pgnatlpalk tltlgvqinl
//
LOCUS       WP_093980491            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arenibacter
            algicola].
ACCESSION   WP_093980491
VERSION     WP_093980491.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter algicola
  ORGANISM  Arenibacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Arenibacter algicola"
                     /db_xref="taxon:616991"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123843
     Region          27..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksslkflt fllfsmvsgi mlaqqgvtgv vssddgellp gvsvvvkgtt tgvtsdfdgi
       61 ysitvpnssa vlvfsylgme tkevavgnqt tlnvtmatss eqldevvvta lgisrekksl
      121 gysvsevggd aldnvpqenv lnalsgkvsg vninstggag stvninvrga aslssdnqpl
      181 fvidgspvin tanniteigr dnkvdygnai sdinaddias vtvlkgasaa alygsragng
      241 vilittksgk skkglgvtin tstvfdipsr fldthtrfat gsrpytednf pansygaiii
      301 getasawagp eldkgimaiq wpysaeeias gvpvprelks ynnpknffqt aitttnnisi
      361 qdsnekinyr lsysdlknkg nipntdlnkh sislnsalkl ndkftvstsl tytksgadnr
      421 pvgnrganam qavyelnphi dvrqmkdywl pgyegifqns pynfgddpte tewnnpyfla
      481 yennngfern rfygnvkgey kitddltgmv rynmdeinev retklskgyt gdmngaygin
      541 kiftnetnid flltyakrle gwdfsisagg nkrvlkgnnl lnstisrgsg lltpglftls
      601 niandnlvys ynsyekqvns lygmasigik dmfyvdvtgr ndwsstlpdn nnsyfypsvs
      661 tsllvnrllg fgngvslfkl ragyaevgnd tgaynlqptl gggtswgsgs llsvpstlln
      721 pdlkpesiss weagadlaff nnrlsmdfty ytadnenqif gialpissgy sskntnagll
      781 rstgieagln aniinsndwr wdmgfvfnrn rtkvielaeg mnsitfwtda rggaitwvge
      841 eignifdaal vrvddpnspy dgwpiiddsg fensdrtred adgnrvapii gnfnpdftlg
      901 mttsasyknw sismnfdwrk ggqfvsqthr ygesdlhtqr widklhnfnd itdvpaylre
      961 nadqflsedg efyvlvggpt aadggyplte ggitlndgvf mpgvqgeydd ngnfvataen
     1021 lggpgtvitr yqdhygwdft rnatfdsdfl klreisltys vpskhiqkig lqnlnislfs
     1081 rniilwtkad igidpemafq hesstqggsg iqfkqgierf nispftipvg fklnvsf
//
LOCUS       WP_093982125             467 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella algae].
ACCESSION   WP_093982125
VERSION     WP_093982125.1
KEYWORDS    RefSeq.
SOURCE      Shewanella algae
  ORGANISM  Shewanella algae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Shewanella algae"
                     /db_xref="taxon:38313"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51814
     Region          1..467
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvkklnqksf alsalvaasl maagafasdk teprnevykd kyknqyaswh dtaksseivd
       61 vlaedpnlvi mwagygfakd ynaprghiya vtdvrntlrt gapksaedgp mpmacwscks
      121 pdvprlieeq gedgyftgkw akggpevvna igcgdchekg spklrlgrpf aeramdtlgt
      181 pfdkasrkdk qsmvcgqchv eyyfekvegr kgfvkfpwdq gttvesmeay ydaiefadwt
      241 halsktpmlk aqhpgyetwq lgvhgknnvt cvdchmpkvt ndkgrkftdh kvgnpfdrfe
      301 etcaqchtqs kefmenltae rkakvnelkl kaedqivkah feaaaawkag ateaemkpil
      361 tdirhaqwrw dyaiashgva ahapdealrv lgtavdkaan arvklaqlla kkgivepval
      421 pdistkakaq aalgmdmkkm vsdkedfkkn vlpkwdaeak kreatyk
//
LOCUS       WP_093986151             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas fluvialis].
ACCESSION   WP_093986151
VERSION     WP_093986151.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluvialis
  ORGANISM  Pseudomonas fluvialis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas fluvialis"
                     /db_xref="taxon:1793966"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38753
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikkligqg hqvtvqagag vsasipdsay tavgatignd
       61 aaalgadlvl kvvapteael ahmksgavlv gmlnpfcnet iarmnargit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpqswme
      241 rqakavhera kqadivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvkhgv tlvghtnlaa lvpadasaly arnlldflkl vidkegqfhl nleddivkac
      361 lmceggnvvr tng
//
LOCUS       WP_093996043             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Octadecabacter ascidiaceicola].
ACCESSION   WP_093996043
VERSION     WP_093996043.1
KEYWORDS    RefSeq.
SOURCE      Octadecabacter ascidiaceicola
  ORGANISM  Octadecabacter ascidiaceicola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Octadecabacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Octadecabacter ascidiaceicola"
                     /db_xref="taxon:1655543"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55263
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgtpkelf egenrvamtp asalelqklg hscvietkag aaagfsdkdy kdagvevvkt
       61 aaalwkaadi vakvrvpddg emkrlsadqt lisffspvad eakmksaark gatvvamemi
      121 prisraqkmd alssmaniag yravieagnn fprfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvfldfee eqadgassgg yasvsspefa
      241 aaqlakfrei apdmdivitt alipnreape lwtedmvksm kpgsvivdla aekggncklt
      301 vkdekivtdn gvtiigytdf psrmaaqsst lyatnirhlm tdltpekdgv vnhdmeddvi
      361 rgatvaygke vtfpppppkv qaiaaqpkaa aveltpeekr avetaafkaq tkqqvtllgi
      421 gaavillagl wapasfmqhf ivfvlsifig fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl vvllaglavf mtginifggf lvtrrmlamf qks
//
LOCUS       WP_093991959             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Flavimaricola marinus].
ACCESSION   WP_093991959
VERSION     WP_093991959.1
KEYWORDS    RefSeq.
SOURCE      Flavimaricola marinus
  ORGANISM  Flavimaricola marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Flavimaricola.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Flavimaricola marinus"
                     /db_xref="taxon:1819565"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55539
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkevf egearvamtp asakdlqklg hscvietgag mlagfsdaay keagvevvkt
       61 aaalfkaaev ivkvrpptet evkrltegqt visffypgqn eklmaaanak gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvflefdd selpdgaatg gyappsspef
      241 qakqlakfre iapdmdivit talipgrpap klwtkdmvem mkpgsvvvdl aaerggncdl
      301 tvmdekivtd ngvtiigytd fpsrmaaqss tlysnnirhm ladltpekdg vidhnmeddv
      361 irgatvthkn eitfpppppk vqaiavqakk ekpkeltpee kraqdvaafk ketrnqvall
      421 svgavlllav glvapasfmq hfivfvlavf vgfqviwgva hslhtplmav tnaissiiil
      481 galtqigsgs alvvilaala vfmtginifg gflvtrrmla mfqks
//
LOCUS       WP_094005350             509 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Amycolatopsis].
ACCESSION   WP_094005350
VERSION     WP_094005350.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis
  ORGANISM  Amycolatopsis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Amycolatopsis"
                     /db_xref="taxon:1813"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52127
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mlvgvlkeat pgetrvaatp ataaqllklg yevvvdpgag elasfsdeay aeagasigna
       61 vqaeivlgvn apakeqldal kpgatlisll apalnqelvd dlanrpitam amdavprisr
      121 aqsldvlssm aniagyravv eaahtfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgavvra tdprpevadq vkslggeyls ieapdvevsa tgyakemsdd ykarerqlye
      241 eqcrdvdiii ttalipgrpa priitadmva smrpgsvivd maaanggnve gtvagkavtt
      301 dngvtilgyt dlpgrlpaqs sqlygtnlvn lmklvtpgkd gtpvfdlddi virsmtvvrd
      361 gellwppppa pvsaapaqaa pkaaaqepep akkklspaar igltavagal lfllvaaspp
      421 alqghltvfa mavvigfyvi ghvhhalhtp lmsvtnaisg iivvgallqv ghgggvvtwl
      481 afaaillasi nifggfavtr rmlsmfsrs
//
LOCUS       WP_094010764             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas soli].
ACCESSION   WP_094010764
VERSION     WP_094010764.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas soli
  ORGANISM  Pseudomonas soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas soli"
                     /db_xref="taxon:1306993"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38914
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvgqg hqvtvqrgag lkasipdsay eavganlgea
       61 adafgaqlvl kvvapsdqel tlinsgslla gmlnpfnnel iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa vqggncpltv
      301 adqvvmahgv tlvgptnlpa qvgadasaly arnlldfmkl lfdkdgnlvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_094028577             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium avium].
ACCESSION   WP_094028577
VERSION     WP_094028577.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37205
     Region          9..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtnaqanavk vgvvaesgad errvalvpka vaslvgsgla vvvesgager allpdalyte
       61 agadigdawa adfvvkvapp tadevaklhs gqtligflap rnadnsigal kqagvqafal
      121 eaiprisraq amdalssqgn vagykavlla asestrffpm lttaagtvkp asvlvlgvgv
      181 aglqalatak rlgartsgyd vrpevadqvr svgaqwldlg idaageggya relteeeraq
      241 qqkaleeaia gfdvvittal vpgrpaprlv taaavesmkp gsvvvdlage tggnceltep
      301 gktvvkhdvt iaaplnlpat mpehaselys knitalldll ikdgklapdf ddevvaaacv
      361 tresa
//
LOCUS       WP_094023511             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Maliponia
            aquimaris].
ACCESSION   WP_094023511
VERSION     WP_094023511.1
KEYWORDS    RefSeq.
SOURCE      Maliponia aquimaris
  ORGANISM  Maliponia aquimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Maliponia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Maliponia aquimaris"
                     /db_xref="taxon:1673631"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55773
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpmeve agenrvamtp dsarqlqklg yeclietgag kkagfsdady qaagvtvaes
       61 aadlwaqsdi iakvriptld eldhlspekt litffnpggn qegldkakek ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfke eqqdgaatgg yasvsspefr
      241 eaqlkkfrel apemdivitt alipnrpapk lwledmvkam kpgsviidla aerggnvegt
      301 vkdekvvten gvtiigytdf psrmasqast lyatnirhml tdltpakdgk vnhnmeddvi
      361 rgatvayqge itfpppppkv qaiaavkrek pkeltpeekr akeiaafkaq trqqvtllti
      421 gggllllvgl vapasfmqhf ivfvlsvfvg fqviwnvshs lhtplmaitn aissiiilga
      481 lmqigsgsgl vivlaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_094036194             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Antarctobacter heliothermus].
ACCESSION   WP_094036194
VERSION     WP_094036194.1
KEYWORDS    RefSeq.
SOURCE      Antarctobacter heliothermus
  ORGANISM  Antarctobacter heliothermus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Antarctobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Antarctobacter heliothermus"
                     /db_xref="taxon:74033"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55615
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpreve sgenrvamtp dsarqlqklg ydcmieagag akagfsdety rdagvevvds
       61 advlwagadi iakvriptld eldyltadkt litffnpggn eeglnkakek ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgsatgg yaavsspefr
      241 eaqlkkfrel apdidivitt alipnrpapk lwledmiaam kpgsvivdla aekggnaegt
      301 vmdekivten gvtiigytdf psrmatqast lystnirhml tdltpekdgq inhnmeddvi
      361 rgatvthqge itfpppppkv aaiaakpkek vkeltaaekr anevaafkaq tkqqvtllav
      421 ggglllavgl vapasfmqhf ivfvlsvfig fqviwnvshs lhtplmaitn aissiiilga
      481 lmqigsgsfl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_094039287             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Zobellella
            denitrificans].
ACCESSION   WP_094039287
VERSION     WP_094039287.1
KEYWORDS    RefSeq.
SOURCE      Zobellella denitrificans
  ORGANISM  Zobellella denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Zobellella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Zobellella denitrificans"
                     /db_xref="taxon:347534"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53526
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipretl sgetrvaatp ksveqlrklg fevcieqgag vkasfedaay qaagaklvga
       61 devwqsaiiy kvnaptadei erlqagttlv sfiwpaqnpe lveklkakgv tvmamdmvpr
      121 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvlv igagvaglaa
      181 igaagslgai vrafdtrpev keqinsmgae fleldyeeea dssdgyakem skafidaema
      241 lfmaqakevd iiittalipg kpapklitae mvaamnpgsv ivdlaaqngg nceltkpgel
      301 fvsdngvkii gytdlngrlp tqsstlyatn lvnlakllck ekdgnikvdf edvvlrnmtv
      361 vkdgevtfpp paisvsaapk akaaaqpaae phakkpsnlk yylggagvvl fawlsavapa
      421 eflshftvfv lacivgyyvi wnvshslhtp lmsvtnaisg iivvgalsqv gtggfvtfla
      481 fiavliasin vfggftvthr mlkmfrkg
//
LOCUS       WP_094064503             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas rhodesiae].
ACCESSION   WP_094064503
VERSION     WP_094064503.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas rhodesiae
  ORGANISM  Pseudomonas rhodesiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas rhodesiae"
                     /db_xref="taxon:76760"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38734
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag lkasvvdsay eaagatlgsa
       61 ndafgaelil kvvapsdnem aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetnee recavgvggy arpmptswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_094074456             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Labrenzia
            sp. VG12].
ACCESSION   WP_094074456
VERSION     WP_094074456.1
KEYWORDS    RefSeq.
SOURCE      Labrenzia sp. VG12
  ORGANISM  Labrenzia sp. VG12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Labrenzia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Labrenzia sp. VG12"
                     /db_xref="taxon:2021862"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55791
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigtpketf pgenrvamtp esakqlqklg yacivqsgag kaagfsdeay qeagveivkt
       61 apslwkkadi vtkvrqpddk elgyltegkt lisffnpggn etgmetaksa ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaasgg yasvsspefr
      241 eaqlakfrel apemdivitt alipnreapk lwledmvkam kpgsvivdla aekggnvdgt
      301 emdkkvvtdn gvtiigytdf psrmasqsst lyatnirhmm tdltpdkdgq lnhnmeddvi
      361 rgatvtykge itfpppppkv qaiaakskek pkeltpeekr aaevaafkaq tkqqvtllai
      421 ggllmflvgl vapasfmqhf ivfvlavfvg fqviwnvshs lhtplmaitn aissiiilga
      481 lmqigsgsfl villaalsif maginifggf lvtrrmlamf qks
//
LOCUS       WP_094078159             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Notoacmeibacter marinus].
ACCESSION   WP_094078159
VERSION     WP_094078159.1
KEYWORDS    RefSeq.
SOURCE      Notoacmeibacter marinus
  ORGANISM  Notoacmeibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Notoacmeibacteraceae; Notoacmeibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Notoacmeibacter marinus"
                     /db_xref="taxon:1876515"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55647
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mklgspkesa pgerrvaltp asakdlaklg heamvekgag alagfsdedy raagvevvds
       61 addlfrqadi iakvqppsde eiarlsddkt lvsffypaan perleavkat gasiiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvpparv lvigagvagl
      181 aaigastslg aityafdvrp evaeqiesmg aefvyldfse eqtdgaetgg yakpsspefq
      241 kaqlekfrel apdidivist alipgrdapv lwtadmveam kpgsvivdla aerggncelt
      301 vkdekivtdn gvtiigytdf psrmatqsss lyannirhlm tdltpdkdgv vnhnmdddvi
      361 rgatvahkge itfpppppkv kaiaaqkpke kpreltaeek ktaelaafka qtrqqvtlla
      421 igaalvlavg liapasfmqh fivfvlsvfi gfqviwnvsh slhtplmavt naissiiilg
      481 aliqigsfsi pikvlaaasi fmasvnifgg flvtrrmlam fqks
//
LOCUS       WP_094091176             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            clemsonensis].
ACCESSION   WP_094091176
VERSION     WP_094091176.1
KEYWORDS    RefSeq.
SOURCE      Legionella clemsonensis
  ORGANISM  Legionella clemsonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Legionella clemsonensis"
                     /db_xref="taxon:1867846"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40070
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mmisalnesn sdtrvaitpn avkhylkmgl dvtiesnagl asgfsdanyq eagativndr
       61 kimlhtaniv vcvnepnpke lagvrpgvll iahidnepsg nllpwackek isifsmnlip
      121 risraqsmds lssqanlagy ravleavshf kraipmmmta agmihpakvl ilgagvaglq
      181 aiatakrlga vvyafdvrra akeqveslga efievsaeqd aetsggyage tseeykrlqa
      241 elidqyarqs ditistalip gkpapvllak stiermkpgs vvvdlatarg gncevsekdk
      301 iityneitvi gysnmaglip ataselyatn linlirhvvp ssaelsfnae deiikqamlc
      361 hdgrhmpfke tqya
//
LOCUS       WP_094078852             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Janibacter
            indicus].
ACCESSION   WP_094078852
VERSION     WP_094078852.1
KEYWORDS    RefSeq.
SOURCE      Janibacter indicus
  ORGANISM  Janibacter indicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Janibacter indicus"
                     /db_xref="taxon:857417"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53440
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgvpkesk rgetrvaatp ktveqliklg ydvvveagag easaypdqay vdagaslesa
       61 eqvwasdiva kvnaptdeev prlrsgaila sllapalnpd kvealraqgv talamdavpr
      121 israqsldvl ssmaniagyr avvesahefg glftgqvtaa gkvppakvlv cgagvaglaa
      181 igaagslgai vrafdvrpev aeqvesmgae flqidveqev ssdgyaketg edfnrkaael
      241 yaeqakdvdi iittalipgr paprliteem vasmkpgsvi vdmaagsggn vagsvaderv
      301 vtdngvriig ytdlagrlpt qasqlygtni vnllklvtpd kdgqpvldme dtvvrgmtvt
      361 qgeetlwppp svqvsaaqst paaskvaeae adkkpekphd pnrkfwyigg aallflvaaa
      421 fmpaaflshf ivfalavvig fyvigsvhha lhtplmsvtn aisgiivvga llqvtspdia
      481 iqviaaaaif fasinvfggf tvtnrmlnmf rkg
//
LOCUS       WP_094098858             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            carolinensis].
ACCESSION   WP_094098858
VERSION     WP_094098858.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax carolinensis
  ORGANISM  Acidovorax carolinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Acidovorax carolinensis"
                     /db_xref="taxon:553814"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55515
     Region          11..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtspvpqpq rigvpretfp gekrvatvpd tvekliklgf vvavesgagd aanfsddayr
       61 aagakivgda aalwaasdiv fkvrppssde valmregttl idfiwpaqnp elmqqlaark
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rqmyasqakd sdiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltmpg qavvrhgvti vgytdlpsrl akqsstlyat nllrlteelc kakdgvavvn
      361 meddairglt vvkdgtitwp applkqapap apkaaaapva akksshgpga pmsaktltiv
      421 favlaalfwt igayapvafl ghftvfvlac figymvvwnv tpalhtplms vtnaissiia
      481 igalvqiapp dagingrpdg lilwlafaal vltavnmfgg favtrrmlam frk
//
LOCUS       WP_094124664             516 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Vibrio].
ACCESSION   WP_094124664
VERSION     WP_094124664.1
KEYWORDS    RefSeq.
SOURCE      unclassified Vibrio
  ORGANISM  unclassified Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="unclassified Vibrio"
                     /db_xref="taxon:2614977"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54214
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpketl tgetrvaasp ssvaqliklg fdvsietqag vlasfddaaf eaagativst
       61 qdvwnsdiil kvnapivdek qsidevalik egaslisfiw paqnpelmeq lsskkinvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv qsmgaeflev dfqetagsgd gyakemsydf
      241 nkkaaelyaa qakdvdiiit talipgrpap klitkemvds msagsvivdl aaanggncey
      301 tvadqvitta ngvkvvgytd mvgrlptqss qlystnivnl lkllckekng sinidfedvv
      361 lrgvtvvkeg eitwpappiq vsaqpqvkta ptrpepkkqe pvsatkkitg lvaavgafaw
      421 iasvapaafl shftvfvlac vvgyyvvwnv thalhtplms vtnaisgiiv vgallqigqg
      481 sgvvtflafi avliasinif ggftvtkrml emfrkd
//
LOCUS       WP_094132279             516 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Vibrio].
ACCESSION   WP_094132279
VERSION     WP_094132279.1
KEYWORDS    RefSeq.
SOURCE      unclassified Vibrio
  ORGANISM  unclassified Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="unclassified Vibrio"
                     /db_xref="taxon:2614977"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54256
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpketl tgetrvaasp ssvaqliklg fdvsietqag vlasfddaaf eaagativst
       61 qdvwnsdiil kvnapivdek qsidevalik egaslisfiw paqnpelmeq lsskkinvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv qsmgaeflev dfqetagsgd gyakemsddf
      241 nkkaaelyaa qakdvdiiit talipgrpap klitkemvds mnagsvivdl aaanggncey
      301 tvadqvitta ngvkvvgytd mvgrlptqss qlystnivnl lkllckekdg sinidfedvv
      361 lrgvtvvkeg eitwpappiq vyaqpqvkta ptrpepkkqe pvsatkkiag lvaavgafaw
      421 iasvapaafl shftvfvlac vvgyyvvwnv thalhtplms vtnaisgiiv vgallqigqg
      481 sgvvtflafi avlissinif ggftvtkrml emfrkd
//
LOCUS       WP_094127226             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio sp.
            V09_P4A23P171].
ACCESSION   WP_094127226
VERSION     WP_094127226.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. V09_P4A23P171
  ORGANISM  Vibrio sp. V09_P4A23P171
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Vibrio sp. V09_P4A23P171"
                     /db_xref="taxon:1938664"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54157
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpketl tgetrvaasp ssvaqliklg fdvsietqag vlasfddaaf eaagativst
       61 qdvwnsdiil kvnapivdek qsidevalik egaslisfiw paqnpelmeq lsskkinvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv qsmgaeflev dfqetagsgd gyakemsddf
      241 nkkaaelyaa qakdvdiiit talipgrpap klitkemvds msagsvivdl aaanggncey
      301 tvadqvitta ngvkvvgytd mvgrlptqss qlystnivnl lkllckekdg sinidfedvv
      361 lrgvtvvkeg eitwpappiq vsaqpqvkta ptrpeskkqe pvsatkkitg lvaavgafaw
      421 iasvapaafl shftvfvlac vvgyyvvwnv thalhtplms vtnaisgiiv vgallqigqg
      481 sgvvtflafi avliasinif ggftvtkrml emfrkd
//
LOCUS       WP_094134419            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094134419
VERSION     WP_094134419.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114775
     Region          25..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqls faqektvkgv vtdangpmpg vnvlvkgtqr gvstgfdgty
       61 sikasqgevl vfsfmgmgdv srtvgasasi svkmqddakq lgevvvtgal gikkkkdait
      121 svqqvvgsre ltqamnpnva rsltakvsgl qidnssggvn gntrivlrgp rsvsgnteal
      181 ividnaistg salaqlppdv vesvtvikga qgaalygdqg sngvilvvtk kgtaggklsi
      241 svnssiemeq isflpkkqsl ygqgwdgnhy svengawgpl ldgslqttgi neylkpysfv
      301 kdnmkayyqd gistqngvtl nfggedgyal lsanrsvqdf vvegdgsrrn sflfkggkki
      361 gkwkfdgsvr yvstqteqse adnalahllq sapnisvgdf entgiggwni yyknpfwerk
      421 nnrlnrssdf fdvsaslgya fnkhinvtyl anvqtqtsiq tthnaagfis gvsdegnysf
      481 gqksnfyrsn nhtmnfygdl llnfdyklfd kvsfkaavgs nmqdkyseri sqggenlqip
      541 gwyniqnvan idlakdlsnn mfrtrkvsgf gnvdlgyady lflnltgrrd atsvltssnn
      601 vynyysggls fvptkliegl kdkktlnylk lfvnyakvgn ssavnaydve klsplgygfp
      661 fsgltsysqf nsatnggikp efintveaga sfgfldnrlt ldatvyqskv tdlisekgis
      721 rasqgvanfk tnigdltnkg mefdlgfmpv ktenftwegr lsysayqtkl tkldgestei
      781 elynhandsn snvnsgtyai vgesfpsikg ttylrdvqgr vivdavtgmp kisvnrslig
      841 qvnpdyilgf snsftykglr lavvadyrtg nsfisgaksn lswtgnlees adydrtvgfi
      901 ypnsvlsttg lpnttvytgg dypgttaydn tinyyadysr lgeaqlldgt alkireisls
      961 ynlpkrfldk lklesvrfgv narnpfvffv dknnffkpsn nrnysdpeas nvnnanssvg
     1021 avrtsslsnt slnaggfsqt gqypstrtfg fsvnltf
//
LOCUS       WP_094138402            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094138402
VERSION     WP_094138402.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115598
     Region          25..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklklnrflv llfalisqla laqeknatgv vtdasglplp gvnvvvkgtt rgastsfdgt
       61 fkiqaqqgei lvfsfmgmnt verpatkgma vklndestkl advvvtalgi krekkslgya
      121 tqevkgddln kvnsgnvans isgkvagiei rrsgniggst sviirgsksi tgnnqalwvv
      181 dgvpvsndnt nskevakgns gydtgnpaad ispddiesin vlkgaaasal ygsrasagvi
      241 ivttkkgskn nkglgitiss gittgyvnnq tlpeyqteyg ggyggtsfgg asvqipagsg
      301 gfnkrvitkw dasfgapfdp nlnvfqwnsf spelptygka tpwvagknnp nsfykpstty
      361 nnsvslaggn engtfrisyt kfdqngfipn sqmkkdnini sgsynlspkt sisananyik
      421 tdilgqnevg ygdggnnifa sfrqwwqtna dmkdledayn ltgrnlswna ksrfdtspef
      481 hdnpyfvryn nyntvnrdrf fgnltfttql akwlsftgrg sadtylelde eriaptssrt
      541 tnrlgaysry nrnskeinld aflnfdtkiv sdltlkamlg gtarrnfvda iyattsggli
      601 vpgvynlgns igqvptptet llrkginsvy anatfgykdt yfvegsyrid qsstlpvena
      661 iynypsisgs wifsnnlkqv apwvsfgklr vnyaqtgsda dfavvkstya ktdtnfgsay
      721 lfstedwkkn sllkseltta keiglelalf kkrinldasa ytsdtkdqii pvsvsnasgy
      781 ykayvnggtv qnrgleasln vtaiktnnfs wntrinwarn iskvlslpdn tpnfeygfyq
      841 gisikaevgq plgvlrgsgy tyqngqrlvn sagnyvltqg avigninpew taginntfty
      901 knvslgvlid grkggnifsl dqyygqgsgl yantvgtndl gnpirnsvan gggqilegvq
      961 angstntvrq eyssdtqgyn sfphesfvyd asfiklrevt lgyklpskll kntsitnvmf
     1021 slnasnlwii ykklpyadpe sggtgntqgv qgavmpttrd isfnvkiql
//
LOCUS       WP_094138753            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094138753
VERSION     WP_094138753.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115005
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqls faqektvkgv vtdangpmpg vnvlvkgtqr gvstgfdgty
       61 sikasqgevl vfsfmgmgdv srtvgasasi svkmqddakq lgevvvtgal gikkkkdait
      121 svqqvvgsre ltqamnpnva rsltakvsgl qidnssggvn gntrivlrgp rsvsgnteal
      181 ividnaistg salaqlppdv vesvtvikga qgaalygdqg sngvilvvtk kgtaggklsi
      241 svnssiemeq isflpkkqsl ygqgwdgdha siengawgsl ldgslkvtgv ngdlkpysfv
      301 kdnmkayyqd gistqngvtl nfggedgyal lsanrsvqdf vvegdgsrrn sflfkggkki
      361 gkwkfdgsvr yvstqteqge adnalanllq sapnipvgdf entgifgwni yyknpfwerk
      421 nnrlnrssdf fdvsaslgya fnkhinvtyl anvqtqtsiq tthnaagfts gnsfdavpva
      481 ysfgqksnfy rsnnhtmnfy gdlllnfdyk lfdkvsfkaa lgsnmqdkys erisqggenl
      541 qipgwynlqn vanidlakdl snnmfrtrkv sgfgnvdlgy adylflnltg rrdatsvlts
      601 snnvynyysg glsfvptkli eglkdkktln ylklfvnyak vgnssavnay dveklsplgy
      661 gfpfsgltsy sqfnsatngg ikpefintve agasfgfldn rltldatvyq skvtdlisek
      721 gisrasqgva nfktnigdlt nkgmefdlgf mpvktenftw egrlsysayq tkltkldges
      781 teielynhan dsnsnvnsgt yaivgesfps ikgttylrdv qgrvivdavt gmpkisvnrs
      841 ligqvnpdyi lgfsnsftyk glrlavvady rtgnsfisgv khnlswignl eesadydrtv
      901 gfiypnsvls ttglpnttvy tggdypgtta ydntinyynd ysklgeaqll dgtalkirei
      961 slsynlpkrf ldklklesvr fgvnarnpfv ffvdknnffk psnnrnysdp easnvnnans
     1021 svgavrtssl sntslnaggf sqtgqypstr tfgfsvnltf
//
LOCUS       WP_094152951            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094152951
VERSION     WP_094152951.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115055
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqls faqektvkgv vtdangpmpg vnvlvkgtqr gvstgfdgty
       61 sikasqgevl vfsfmgmgdv srtvgasasi svkmqddakq lgevvvtgal gikkkkdait
      121 svqqvvgsre ltqamnpnva rsltakvsgl qidnssggvn gntrivlrgp rsvsgnteal
      181 ividnaistg salaqlppdv vesvtvikga qgaalygdqg sngvilvvtk kgtaggklsi
      241 svnssiemeq isflpkkqsl ygqgwdgdha siengawgsl ldgslkvtgv ngdlkpysfv
      301 kdnmkayyqd gistqngvtl nfggedgyal lsanrsvqdf vvegdgsrrn sflfkggkki
      361 gkwkfdgsvr yvstqteqse adnalanllq sapnipvgdf entgifgwni yyknpfwerk
      421 nnrlnrssdf fdvsaslgya fnkhinvtyl anvqtqtsiq tthnaagfts gnsfdavpva
      481 ysfgqksnfy rsnnhtmnfy gdlllnfdyk lfdkvsfkaa lgsnmqdkys erisqggenl
      541 qipgwynlqn vanidlakdl snnmfrtrkv sgfgnvdlgy adylflnltg rrdatsvlts
      601 snnvynyysg glsfvptkli eglkdkktln ylklfvnyak vgnssavnay dveklsplgy
      661 gfpfsgltsy sqfnsatngg ikpefintve agasfgfldn rltldatvyq skvtdlisek
      721 gisrasqgva nfktnigdlt nkgmefdlgf mpvktenftw egrlsysayq tkltkldges
      781 teielynhtn dsnsnvnsgt yaivgesfps ikgttylrdv qgrvivdavt gmpkisvnrs
      841 ligqvnpdyi lgfsnsftyk glrlavvady rtgnsfisgv khnlswvgnl eesadydrtv
      901 gfiypnsvls ttglpnttvy tggdytgtta ydntinyynd ysklgeaqll dgtalkirei
      961 slsynlpkrf ldklklesvr fgvnarnpfv ffvdknnffk psnnrnysdp easnvnnans
     1021 svgavrtssl sntslnaggf sqtgqypstr tfgfsvnltf
//
LOCUS       WP_094157710            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094157710
VERSION     WP_094157710.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115106
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqls faqektvkgv vtdangpmpg vnvlvkgtqr gvstgfdgty
       61 sikasqgevl vfsfmgmgdv srtvgasasi svkmqddakq lgevvvtgal gikkkkdait
      121 svqqvvgsre ltqamnpnva rsltakvsgl qidnssggvn gntrivlrgp rsvsgnteal
      181 ividnaistg salaqlppdv vesvtvikga qgaalygdqg sngvilvvtk kgtaggklsi
      241 svnssiemeq isflpkkqsl ygqgwdgdha siengawgsl ldgslkvtgv ngdlkpysfv
      301 kdnmkayyqd gistqngvtl nfggedgyvl lsanrsvqdf vvegdgsrrn sflfkggkki
      361 gkwkfdgsvr yvstqteqge adntlahllq sapnipvgdf entgifgwni yyknpfwerk
      421 nnrlnrssdf fdvsaslgya fnkhinvtyl anvqtqtsiq tthnaagfts gnsfdavpva
      481 ysfgqksnfy rsnnhtmnfy gdlllnfdyk lfdkvsfkaa lgsnmqdkys erisqggenl
      541 qipgwynlqn vanidlakdl snnmfrtrkv sgfgnvdlgy adylflnltg rrdatsvlts
      601 snnvynyysg glsfvptkli eglkdkktln ylklfvnyak vgnssavnay dveklsplgy
      661 gfpfsgltsy sqfnsatngg ikpefintve agasfgfldn rltldatvyq skvtdlisek
      721 gisrasqgva nfktnigdlt nkgmefdlgf mpvktenftw egrlsysayq tkltkldges
      781 teielynhtn dsnsnvnsgt yaivgesfps ikgttylrdv qgrvivdavt gmpkisvnrs
      841 ligqvnpdyi lgfsnsftyk glrlavvady rtgnsfisgv khnlswvgnl eesadydrtv
      901 gfiypnsvls ttglpnttvy tggdytgtta ydntinyynd ysklgeaqll dgtalkirei
      961 slsynlpkrf ldklklesvr fgvnarnpfv ffvdknnffk psnnrnysdp easnvnnans
     1021 svgavrtssl sntslnaggf sqtgqypstr tfgfsvnltf
//
LOCUS       WP_094158983             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Thiomonas
            delicata].
ACCESSION   WP_094158983
VERSION     WP_094158983.1
KEYWORDS    RefSeq.
SOURCE      Thiomonas delicata
  ORGANISM  Thiomonas delicata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Thiomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Thiomonas delicata"
                     /db_xref="taxon:364030"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38589
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpaesv agearvaatp etvkklvaqg hvvvvqagag vaagavdady eavgaqmvta
       61 aealgaelvl kvrrpqdael aqmqrgatvv gmlepfnaeg lqalaqaglt afaleaaprt
      121 traqsldvls sqaniagyka vllaanlypr fmpmlmtaag tvkaarlvil gagvaglqai
      181 atakrlgavv easdvrpaak eqveslgakf idvpfetdee reiaqgvggy arpmpkawld
      241 rqaalvaerv kqanivitta lipgrrapvl vseamvqgmr pgsvivdmaa aqggncplte
      301 adktvvrhgv tivgetnlpa mvaadassly arnvldflkl vldkdkgliv nmdddivaac
      361 lmtrdgevkr kaa
//
LOCUS       WP_094162796            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094162796
VERSION     WP_094162796.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115048
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqls faqektvkgv vtdangpmpg vnvlvkgtqr gvstgfdgty
       61 sikasqgevl vfsfmgmgdv srtvgasasi svkmqddakq lgevvvtgal gikkkkdait
      121 svqqvvgsre ltqamnpnva rsltakvsgl qidnssggvn gntrivlrgp rsvsgnteal
      181 ividnaistg salaqlppdv vesvtvikga qgaalygdqg sngvilvvtk kgtaggklsi
      241 svnssiemeq isflpkkqsl ygqgwdgdha siengawgsl ldgslkvtgv ngdlkpysfv
      301 kdnmkayyqd gistqngvtl nfggedgyal lsanrsvqdf vvegdgsrrn sflfkggkki
      361 gkwkfdgsvr yvstqteqge adntlahllq sapnipvgdf entgifgwni yyknpfwerk
      421 nnrlnrssdf fdvsaslgya fnkhinvtyl anvqtqtsiq tthnaagfts gnsfdavpva
      481 ysfgqksnfy rsnnhtmnfy gdlllnfdyk lfdkvsfkaa lgsnmqdkys erisqggenl
      541 qipgwynlqn vanidlakdl snnmfrtrkv sgfgnvdlgy adylflnltg rrdatsvlts
      601 snnvynyysg glsfvptkli eglkdkktln ylklfvnyak vgnssavnay dveklsplgy
      661 gfpfsgltsy sqfngatngg ikpefintve agasfgfldn rltldatvyq skvtdlisek
      721 gisrasqgva nfktnigdlt nkgmefdlgf mpvktenftw egrlsysayq tkltkldges
      781 teielynhtn dsnsnvnsgt yaivgesfps ikgttylrdv qgrvivdavt gmpkisvnrs
      841 ligqvnpdyi lgfsnsftyk glrlavvady rtgnsfisgv khnlswvgnl eesadydrtv
      901 gfiypnsvls ttglpnttvy tggdytgtta ydntinyynd ysklgeaqll dgtalkirei
      961 slsynlpkrf ldklklesvr fgvnarnpfv ffvdknnffk psnnrnysdp easnvnnans
     1021 svgavrtssl sntslnaggf sqtgqypstr tfgfsvnltf
//
LOCUS       WP_094162994             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_094162994
VERSION     WP_094162994.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36092
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efvkndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel vsymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_094165852             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio sp.
            V12_P9A6T4].
ACCESSION   WP_094165852
VERSION     WP_094165852.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. V12_P9A6T4
  ORGANISM  Vibrio sp. V12_P9A6T4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Vibrio sp. V12_P9A6T4"
                     /db_xref="taxon:1938667"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54195
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpketl tgetrvaasp ssvaqliklg fdvsietqag vlasfddaaf eaagativst
       61 qdvwnsdiil kvnapivdek qsidevalik egaslisfiw paqnpelmeq lsskkinvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv qsmgaeflev dfqetagsgd gyakemsddf
      241 nkkaaelyaa qakdvdiiit talipgrpap klitkemvds msagsvivdl aaanggncey
      301 tvadqvitta ngvkvvgytd mvgrlptqss qlystnivnl lkllckekdg sinidfedvv
      361 lrgvtvvkeg eitwpappiq vsvqpqvkta ptrpepkkqe pvsatkkitg lvaavgafaw
      421 iasvapaafl shftvfvlac vvgyyvvwnv thalhtplms vtnaisgiiv vgallqigqg
      481 sgvvtflafi avliasinif ggftvtkrml emfrkd
//
LOCUS       WP_094166452            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094166452
VERSION     WP_094166452.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115039
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqls faqektvkgv vtdangpmpg vnvlvkgtqr gvstgfdgty
       61 sikasqgevl vfsfmgmgdv srtvgasasi svkmqddakq lgevvvtgal gikkkkdait
      121 svqqvvgsre ltqamnpnva rsltakvsgl qidnssggvn gntrivlrgp rsvsgnteal
      181 ividnaistg salaqlppdv vesvtvikga qgaalygdqg sngvilvvtk kgtaggklsi
      241 svnssiemeq isflpkkqsl ygqgwdgdha siengawgsl ldgslkvtgv ngdlkpysfv
      301 kdnmkayyqd gistqngvtl nfggedgyal lsanrsvqdf vvegdgsrrn sflfkggkki
      361 gkwkfdgsvr yvstqteqse adnalanllq sapnipvgdf entgifgwni yfknpfwerk
      421 nnrlnrssdf fdvsaslgya fnkhinvtyl anvqtqtsiq tthnaagfts gnsfdavpva
      481 ysfgqksnfy rsnnhtmnfy gdlllnfdyk lfdkvsfkaa lgsnmqdkys erisqggenl
      541 qipgwyniqn vanidlakdl snnmfrtrkv sgfgnvdlgy adylflnltg rrdatsvlts
      601 snnvynyysg glsfvptkli eglkdkktln ylklfvnyak vgnssavnay dveklsplgy
      661 gfpfsgltsy sqfnsatngg ikpefintve agasfgfldn rltldatvyq skvtdlisek
      721 gisrasqgva nfktnigdlt nkgmefdlgf mpvktenftw egrlsysayq tkltkldges
      781 teielynhtn dsnsnvnsgt yaivgesfps ikgttylrdv qgrvivdavt gmpkisvnrs
      841 ligqvnpdyi lgfsnsftyk glrlavvady rtgnsfisgv khnlswvgnl eesadydrtv
      901 gfiypnsvls ttglpnttvy tggdytgtta ydntinyynd ysklgeaqll dgtalkirei
      961 slsynlpkrf ldklklesvr fgvnarnpfv ffvdknnffk psnnrnysdp easnvnnans
     1021 svgavrtssl sntslnaggf sqtgqypstr tfgfsvnltf
//
LOCUS       WP_094167422            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094167422
VERSION     WP_094167422.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115614
     Region          25..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklklnrflv llfalisqla laqeknatgv vtdasglplp gvnvvvkgtt rgastsfdgt
       61 fkiqaqqgei lvfsfmgmnt verpatkgma vklndestkl advvvtalgi krekkslgya
      121 tqevkgddln kvnsgnvans isgkvagiei rrsgniggst sviirgsksi tgnnqalwvv
      181 dgvpvsndnt nsrevakgns gydtgnpaad ispddiesin vlkgaaasal ygsrasagvi
      241 ivttkkgskn nkglgitiss gittgyvnnq tlpeyqteyg ggyggtsfgg asvqipagsg
      301 gfnkrvitkw dasfgapfdp nlnvfqwnsf spelptygka tpwvagknnp nsfykpctty
      361 nnsvslaggn engtfrisyt kfdqngfipn sqmkkdnini sgsynlspkt sisananyik
      421 tdilgqnevg ygdggnnifa sfrqwwqtna dmkdledayn ltgrnlswna ksrfdtspef
      481 hdnpyfvryn nyntvnrdrf fgnltfttql akwlsftgrg sadtylelde eriaptssrt
      541 tnrlgaysry nrnskeinld aflnfdtkia sdltlkamlg gtarrnfvda iyattsggli
      601 vpgvynlgns igqvptptet llrkginsvy anatfgykdt yfvegsyrid qsstlpvena
      661 iynypsisgs wifsnnlkqv apwvsfgklr vnyaqtgsda dfavvkstya ktdtnfgsay
      721 lfstedwkkn sllkseltta keiglelalf kkrinldasa ytsdtkdqii pvsvsnasgy
      781 ykayvnggtv qnrgleasln vtaiktnnfs wntrinwarn iskvlslpdn tpnfeygfyq
      841 gisikaevgq plgvlrgsgy tyqngqrlvn sagnyvltqg avigninpew taginntfty
      901 knvslgvlid grkggnifsl dqyygqgsgl yantvgtndl gnpirnsvan gggqilegvq
      961 angstntvrq eyssdtqgyn sfphesfvyd asfiklrevt lgyklpskll kntsitnvmf
     1021 slnasnlwii ykklpyadpe sggtgntqgv qgavmpttrd isfnvkiql
//
LOCUS       WP_094167627            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094167627
VERSION     WP_094167627.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114989
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqls faqektvkgv vtdangpmpg vnvlvkgtqr gvstgfdgay
       61 sikasqgevl vfsfmgmgdv srtvgasasi svkmqddakq lgevvvtgal gikkkkdait
      121 svqqvvgsre ltqamnpnva rsltakvsgl qidnssggvn gntrivlrgp rsvsgnteal
      181 ividnaistg salaqlppdv vesvtvikga qgaalygdqg sngvilvvtk kgtaggklsi
      241 svnssiemeq isflpkkqsl ygqgwdgdha siengawgsl ldgslkvtgv ngdlkpysfv
      301 kdnmkayyqd gistqngvtl nfggedgyal lsanrsvqdf vvegdgsrrn sflfkggkki
      361 gkwkfdgsvr yvstqteqge adntlahllq sapnipvgdf entgifgwni yyknpfwerk
      421 nnrlnrssdf fdvsaslgya fnkhinvtyl anvqtqtsiq tthnaagfts gnsfdavpva
      481 ysfgqksnfy rsnnhtmnfy gdlllnfdyk lfdkvsfkaa lgsnmqdkys erisqggenl
      541 qipgwynlqn vanidlakdl snnmfrtrkv sgfgnvdlgy adylflnltg rrdatsvlts
      601 snnvynyysg glsfvptkli eglkdkktln ylklfvnyak vgnssavnay dveklsplgy
      661 gfpfsgltsy sqfngatngg ikpefintve agasfgfldn rltldatvyq skvtdlisek
      721 gisrasqgva nfktnigdlt nkgmefdlgf mpvktenftw egrlsysayq tkltkldges
      781 teielynhan dsnsdvnsgt yaivgesfps ikgttylrdv qgrvivdavt gmpkisvnrs
      841 ligqvnpdyi lgfsnsftyk glrlavvady rtgnsfisgv khnlswvgnl eesadydrtv
      901 gfiypnsvls ttglpnttvy tggdytgtta ydntinyynd ysklgeaqll dgtalkirei
      961 slsynlpkrf ldklklesvr fgvnarnpfv ffvdknnffk psnnrnysdp easnvnnans
     1021 svgavrtssl sntslnaggf sqtgqypstr tfgfsvnltf
//
LOCUS       WP_094168331            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094168331
VERSION     WP_094168331.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115026
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqls faqektvkgv vtdangpmpg vnvlvkgtqr gvstgfdgty
       61 sikasqgevl vfsfmgmgdv srtvgasasi svkmqddakq lgevvvtgal gikkkkdait
      121 svqqvvgsre ltqamnpnva rsltakvsgl qidnssggvn gntrivlrgp rsvsgnteal
      181 ividnaistg salaqlppdv vesvtvikga qgaalygdqg sngvilvvtk kgtaggklsi
      241 svnssiemeq isflpkkqsl ygqgwdgdha siengawgsl ldgslkvtgv ngdlkpysfv
      301 kdnmkayyqd gistqngvtl nfggedgyal lsanrsvqdf vvegdgsrrn sflfkggkki
      361 gkwkfdgsvr yvstqteqse adnalanllq sapnipvgdf entgifgwni yyknpfwerk
      421 nnrlnrssdf fdvsaslgya fnkhinvtyl anvqtqtsiq tthnaagfts gnsfdavpva
      481 ysfgqksnfy rsnnhtmdfy gdlllnfdyk lfdkvsfkaa lgsnmqdkys erisqggenl
      541 qipgwynlqn vanidlakdl snnmfrtrkv sgfgnvdlgy adylflnltg rrdatsvlts
      601 snnvynyysg glsfvptkli eglkdkktln ylklfvnyak vgnssavnay dveklsplgy
      661 gfpfsgltsy sqfnsatngg ikpefintve agasfgfldn rltldatvyq skvtdlisek
      721 gisrasqgva nfktnigdlt nkgmefdlgf mpvktenftw egrlsysayq tkltkldges
      781 teielynhan dsnsnvnsgt yaivgesfps ikgttylrdv qgrvivdavt gmpkisvnrs
      841 ligqvnpdyi lgfsnsftyk glrlavvady rtgnsfisgv khnlswvgnl eesadydrtv
      901 gfiypnsvls ttglpnttvy tggdytgtta ydntinyynd ysklgeaqll dgtalkirei
      961 slsynlpkrf ldklklesvr fgvnarnpfv ffvdknnffk psnnrnysdp easnvnnans
     1021 svgavrtssl sntslnaggf sqtgqypstr tfgfsvnltf
//
LOCUS       WP_094178942             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            psychrophilum].
ACCESSION   WP_094178942
VERSION     WP_094178942.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108024
     Region          25..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift llvaltmqls faqektvkgv vtdangpmpg vnvlvkgtqr gvstgfdgty
       61 sikasqgevl vfsfmgmgdv srtvgasasi svkmqddakq lgevvvvgya kqekkkmiqs
      121 vsvvgaskir dtpiasfada lqgqasgvqv vnssgvlgsv pvvkirgvas isangrpliv
      181 mdgvplndal ltstqggqsl dplvdinqnd iesfsvlkda aataiygsrg sngvilittk
      241 sgkknqdakv evgfttsmtt atdvmsmmta dqyrafvikt npasnftned vglgsfnwid
      301 avsrkgistg vdvsvsggsd kttyslsgni sdqqgfiign glkkngfrln latdvkdwlr
      361 vgttigvses kmdrvgsens vaapftaayl qapnispyge dgkfqrtgfv snvvaiealn
      421 indansfrvn gnvfadlrlh knlnfktefg idrssldefe rqfeintagg farsyqavqq
      481 kivntntlny kktfalkhnf nilgglsven tgirdvtteg tgfasddlin vtsalnkttt
      541 dntttgsrlv glfsrlsydf sgkylvelsa rrdgssrfgs dfrygnfgav gvawvvseed
      601 flkesklvsn fklkanygia gndrigdyla rerteggvfp nyneatgiyt lrfanpnmkw
      661 ersksydlgl elgmfnnkfr vnvdyynktt nqlilrsnfs vadnngivgl tgnagsmenk
      721 gfdldvaldv frdskfkwts sfnfnnnknt ilelndaaat dldgnkfisg gssqraivgh
      781 svntffliry sgvnpqtgna ewldrngnat ttpkaddrvi vgdanpdftg gfnnnfkygn
      841 wdlnalinfs ygneimvdgl rftedarysn gfnkssdlln iwekpgdnas tpnitsptfr
      901 tfqqrstkql rdasfarlkg vtlgynlvfd ksssfaklvk svrlyataqn lytlkndnlr
      961 gidpevtstt anlgqgetff tppqtktfvf garltf
//
LOCUS       WP_094201907             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oceanimonas doudoroffii].
ACCESSION   WP_094201907
VERSION     WP_094201907.1
KEYWORDS    RefSeq.
SOURCE      Oceanimonas doudoroffii
  ORGANISM  Oceanimonas doudoroffii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Oceanimonas.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Oceanimonas doudoroffii"
                     /db_xref="taxon:84158"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53439
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipretl sgetrvaatp ksveqlrklg fdvcveqgag skasfedtaf aaagaqlvsa
       61 deawqsaiiy kvnaptaeei erlqvgttlv sfiwpaqnpe lveqlknkgv tvlamdmvpr
      121 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvlv igagvaglaa
      181 igaagslgai vrafdtrpev keqinsmgae fleldyeees dssdgyakem sqafidaema
      241 lfmeqakevd iivttalipg kpapklitad mvaamapgsv ivdlaaqngg nceltkpgel
      301 fvsdngvkii gytdlngrlp tqsstlyatn lvnlakllck ekdgninvdf ddvvlrnmtv
      361 trdgevtfpp paisvsaapk akaaaqpaae phakkpsnlk yylggagvll fawlaavapa
      421 eflshitvfv lacivgyyvi wnvshslhtp lmsvtnaisg iivvgalsqv gsggfvsfla
      481 fvavliasin vfggftvthr mlkmfrkg
//
LOCUS       WP_094250101             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_094250101
VERSION     WP_094250101.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53599
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta appkpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwv gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmtvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_094255167            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094255167
VERSION     WP_094255167.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115934
     Region          27..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlptclsia vaslctiqml saqqlsiagk vtnaegepiv gasifikgtq qgtasnengl
       61 fslnapsngi ltiravgyss ievpingktn lsvqlqhvds eidevvvtal giqrsekslg
      121 yaaqgvtnet lnsnkqpnlv nalqgkiaga tisstggapg qganiqirgi nsidptrdnn
      181 plfvidgilm dnstsvqgga evrgmsnrsv dinpddieti nilkggaata lyglrgangv
      241 viittksgka gtlridyqgt vgfenvnkfp kmqdtytqgw kgvynkddfw pawgptveea
      301 mkvdpthpst lykpfeeafd tgnqfrnsln isggsekftf ltslsqmkhn gvmpstdfkt
      361 yqarlntnfi isekfkggss lavsnsggyr gnanryaeql iywtprynir dylmdngtmk
      421 sygdtdnpiy vantnrlkdd vlrviggvdf tfspakwldl myragidayr dnregtaigy
      481 qgladerlvy dngvegadgr gfynvysnnf rainstfiat fkhdfnedfn aklrlgqdiy
      541 dryikrtstq ggdltvynwf dlgnaniika dsyiekyrlm glfaelemty kdflfltlts
      601 rqditsslap knrsfnypsa tvsyvfsdhi tlpevinfgk lrfsyaqigk dappystssg
      661 fgpysnlptg yigftrpall gnvdlkpeft dtyeagfelk ffqsrlgldf tlynsisrdq
      721 iiqvpvtsat gfvtasinag siqnrglelt lntvpvkkdn ftwnsninfs inrnkileir
      781 edlddeivvs seygylnstv smrirpgesy gtlygrtykr yytadeiaqg ldktreydes
      841 rplligangf pvlestsvpk klgnvqpswv ggwnntfnyk nlslnilvds rvgqsrynql
      901 gnfmaafgea dytedrndyk vfdgvladgs kntkevwlgq gkdpkngvdy gngyyrdnfr
      961 gnsqffveda swfrlrsvsi gyslpqqwld nkviknaris vignnlalwt kysgydpens
     1021 ttasgsnieg fagmtypavr sflfslnvgf
//
LOCUS       WP_094255186            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094255186
VERSION     WP_094255186.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111753
     Region          23..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myktlthlfl wlfaiqltyg qqrtikgtvv deqtksaivg atvrldaskk atstdesgkf
       61 sleapagpvn lsisvlgynt vkqtvsatds vinismspqt ariddvvvta lgvqrksksl
      121 tystqtvkge eltkvkdanp mnnltgkvsg mqinrsssgi ggsvnivlrg fksnrnnqpl
      181 yvidglpitn tggsgsegaf gggpdrgdil stlnaddils invlkgasas alygsqgang
      241 aimittkkga egnlkidvss sitadqafyl pklqyrygqt tqdseeswge kgsfqdpvdn
      301 ffntgttlin tislsggtek mqnyfsygnt snkgilptns fkqhsatfrn stnffdnklt
      361 fdgsmmysrq dihnrpssgl yfnpiaglyl fprgldfdky knnyeylspt rnlylqdwwn
      421 inadagltgt hhsqnpfwvl nrnptfqwrd niiaqgqlky ninewlsvsa rgtlnkrwdk
      481 werhvyagtq gvlsgekieg vlndngrytr dqtestslyg dllfignktf aedwdlnfta
      541 gtsindtrsn gwnldqlkla vankfllsni yrdapinvln esisrrqlqs lfastnlgyk
      601 dkifldltar ndwastlant pqekkgyfyw saglsavlsd mikmpsfity sklrltmaev
      661 gndvgiysti ptntlatgil nanvsgpyqg lplrpeisrs yevgyegrfw ndrinvdlal
      721 yktntkdqyf syeapvgqvy ttvflnagnv enkgieaalg idaikkdnft wntsvnftan
      781 rnkilelapk lgerysvggn fnvlrlngsf gdfwartflr dsngvmvvdd tgrpqigpeg
      841 yignnnpksi vgwnntinyg kfglsftida rfggqvisvt dgylnsfgvs eesaaardag
      901 gldipavkvd gtpwqgklpa qayysavgnr dgiiegqvyd atnirmreia ltyalpikwk
      961 gvnsasislt grnlfffhnd apydpelntt tgvgaqgyds fslpatrsyg lnlkvsf
//
LOCUS       WP_094255539            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094255539
VERSION     WP_094255539.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119258
     Region          58..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnknhyftkv rwskafihla llspsllfat atfgnegkie isrnyanitf nkslqtevsg
       61 tvkdkdgnpl sgvtvtvqne nkststdang kfsiavssss svlsfsfigy ttksvsasna
      121 knvildssed vldevvvvgy gtqkkshlts avsqvdpkvl qnrpsptitn mlqgaapglv
      181 vtrnsgrpgg qglnisvrge tsangsvspl vvidgvisse etfvalnpsd venisilkdg
      241 gataiygaas sggvilvttk kgksgkgris lssnlgiqrp gsmpdrlsli demnyvnlar
      301 knagiaeeyn eedlnyavng ptfvlgsndl wrtynqenil dqviqkkyni ynnniqftgg
      361 sekitymasl gnmaqngmfk vgddkfsrin aranisaqvt dylkldvgna finqktdnpq
      421 dggysidggg nsilrqfyss rmrfpiyned gtyyrsgtss afgyalmkdg gfnddlkrty
      481 fnnvtatvnn lvkglevrlm ysresidlqn rnfrrtvdyy sgptaksktq lnnpnsysit
      541 nyktlkqnvq alvdydltia enhnfhvlgg yqfydhdyqy itastknlyv ndspslnfts
      601 dplnkshnqg aqrekvqsff grfnynykek ylfeatfrsd essrlspdir rkvfpsysvg
      661 wnvakeewfq gatpfinelk priswgkvgs kigvgfydyi aqlstnsnll lndikqtyly
      721 qsaipaqait wetietrnlg ldfsllnrkl fgsfdyyqky nnnmlvslsl patlgiaipk
      781 sndgrlktwg weaslgyrdq vgdfnynvgv sladnknrli hyggannvvy tgsnklvegy
      841 amnsvwvykt dgyfqsegel qnapsyaqfi nkngvpglgd vkyidlngdg kitpggntlg
      901 dtgdliylgd tnpryqfgin aylgyknfdf sffiqgigkr llkpsneliq pqlyswylpm
      961 dfqmdywted nrnaafprpf legshnfqns dkwylsgaya rlknvqlgys lsktqfaklp
     1021 fervrlyvsa edlltvsklg vfkgaidpei rpedgkvspy pfattvsfgl nidl
//
LOCUS       WP_094255565            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094255565
VERSION     WP_094255565.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111452
     Region          50..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrfsrpff plkrshlvag aviiglslpg sssvanelnr devesyssqq evkgkvtsgg
       61 vvlpgvtvtv kedpskstst nasgefniaa engqtlvfta ighekkevai tgttvnveln
      121 sseenidevv vtgystqkkg disasivsld qkklkdtksp nvsnllqgkv agvdvvgtgr
      181 pgqqanvkir grsslssgtn plwvvdgvit hgvaninpnd iesisvlkda aattqygsrg
      241 tngvivvttk ralregegtf svnlssgisk fnfgnfdlmn sqeiwdyyqt fpnqddiddn
      301 vskdvlnndy nwlkngtqna pvndfsasym gktdktsvfa sanyygekgs ikgydferlt
      361 grfnvehklt drltfkpkln asyttytdkq hslynmmfyl pwdnpyntdg tiknpqapna
      421 tvawfgrdht nylydlqyny gkgqtldmqg nfdfsyrisd rftfesmnnl tyynqtamry
      481 adpnsnegrg nkgtiyqfsd kritrffnqm lkynetfgkh tvsgfaayey sdyvyssqna
      541 tgkgiapgse ilgnaasvld fggtkndysf qsgilqgtyg ydnrynvmas frvdgssrfg
      601 reqqygafys vsgawninne affnvpsinl lrlkasyggv gnvpvdyyss fatyglnaqy
      661 ngepaaiqqn fqnahvswek sydanlglel gmfnrlnlsv dlynkntsgl lyfvdfpsta
      721 gwdgywlnig glrnrgveva lsgsvfspgn pfqwdlgvni ahnnnritsl kddqdipkgn
      781 rrfsvghdvd swymrkwvgv npengaplwe svneetgevs ttsnyndaal qfvgaatpkf
      841 qggfnsamty kgfnlnanfa yqnggityna arelfdsdga yasynqlilk dgwsrwspen
      901 pnathpkaey nntslsnkts srylestnfl rlrnvtlgyt fseslvnklk lkglnvyvsg
      961 dnlwtstkfs gldpeaailg ndnavdkagg gdataqypap krlvfglnlt f
//
LOCUS       WP_094255641            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094255641
VERSION     WP_094255641.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112565
     Region          26..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msnfyskccs ltivmlisis tlfaqqtvtg kvtgpnganl pgvsvsvvgt dkvtqtnseg
       61 nfsieanngq kirfssmgyl tkeatvssts lninlqedas nidevvvtam gikrerkslg
      121 ysfqevkseq ltdaketnva nalvgkvsgl qvikgssgpa sstkitlrgn nsltgdnqpl
      181 iivdgvpmnn flgakggngk vnndfwnpgt dmgnglgdin pediesmsvl ksgaasalyg
      241 sragngaiii ttksgkaqkg tgitysstvg fetifmtpei qsafgqgsng vfdaistnnw
      301 geaidgnkyq aydninnffk tgfnhtqnva fqqqigetni yssatylndq skipgssler
      361 lnlmskvstt fgpnkrwste vkvqymnnda tnrpisgqnn snafatlfrm prsinilnyk
      421 npvdntgkmr wygttnsinp ywlaeynlnn dvrnrflsna nikykitdwl diegragldt
      481 yasrfenkty sgsplsstgl ystgktefae knftlalhar kdeingskwg vngsvfgqim
      541 rsdetflgvg vgelevpnff yvtngkgnpt pnqynnrkqi nslygtaeln ydgywflnvt
      601 grndwssals keyrsyfyps vstslvvsdl irksggnlps ainflklras yatvgndmgp
      661 yqifnaydig rdpngnttsg lgevfynpnv rseliktlef gfdtrlldsr lgidfawykn
      721 natnqlldip mnpmsgfrak kinagniqns gfeialdgqi lrsddglnwn ssvnfsknvn
      781 riieltpeie yynlggfdni avraisneif gqiigskflr vddqnsphyg klilngnglp
      841 qsvdgqvlgn qspkalagwt nsfsyknigl sfqidgrfgg effsgtnvnl qangtaaatv
      901 tdgkradfvv dgviqdgqny tqntksvtvq qywtqvattg nmgigeaniy datnirlrni
      961 tlsynlpssv lksnilqrar iaftvnnawm iksyangvdp esvfsinsna tgfenfatpt
     1021 srsyfvnltl gf
//
LOCUS       WP_094256023            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_094256023
VERSION     WP_094256023.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116413
     Region          26..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfqkliili lsiftlqiay aqnqairgrv vdesnngiag atilnaatnr aitassdngs
       61 falsvpantt lvfkavgfnq rrvtvkanqt tltvqlsste dqveevvvrg yvarkketst
      121 gasaslgqkd irdvpaanle qlmqgkvpgl nvqvntgapg frgstqirgl stlsttgsgs
      181 esilmptspl yvidgvpmda drasefglqq qgpgisplsl ippedvesie ilkdaqatsl
      241 ygsqgaygvi iittkrgnsp vprinytqst fmktppklre tlggnlerql kmwqiinnai
      301 tqgeldkime tpmladslna fynnstnwqa lyyqntfnqn hnvsldggne vlsykanigy
      361 ygetgviknt gfnryssnlr mdyrpnkrfd ftgqvfaqlg kqnkgdgtgi lqtgvstggm
      421 nstllpppgf fsadagyisa irtkndnssk lirpyvegkf evfpglriqs amsyefasnn
      481 edkftpaaaa gqfsevysfa gresnlynrn iinytkdine dhnifinlfn evrhnqrqnt
      541 itkqartpnd qfegplgydg yfsrgggvls nfrnekalsf alatsysyks ryivdlsyri
      601 dgssangfen lytknpavgf rwnahheewi ksipwinlas lrftwgvnvm ptstleriyg
      661 rydisglynq tqgiginysf ipnpslkptt smqynagldl nlfnnkvdlv ydtyykkvdn
      721 llfesfltns tgfdklysnd agvanyghel ainvrplsas spfswtfsln gaynrdvlll
      781 lpdnfrgqyi kwdgnadrlh mvnrvgtsal snyllqnvgv yatdadvpid patglryrta
      841 dgtffqagdp ifvdrngdyi ldnrdytrag ntqplwtggm qntlnyknfq fsvyasytak
      901 rtilnyaraq rmdlfrdpfg sqaivpieni siwmkdgdia kypypydfsr nnsvqpfryd
      961 qtlweengsy fkinniivay vfdmdflrry rldrfriyas mdnvytfssy sgpnpenvts
     1021 lgrdasngyp vprtytlgfn isf
//
LOCUS       WP_094256251            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094256251
VERSION     WP_094256251.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117413
     Region          69..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskikswsi pqnihninyl rpknllslml csgsmllcsa veasphhlwk adkietnyli
       61 pvhfeqqttv tgtvvndqgn pianasirvk gsnegsqtne rgefsfetaq srgtlvishm
      121 syqtlevpin atsamrivlq ddaanleevv vtsfgiqrdr ktlgygvgev kaddlakapt
      181 tdvtnalagr lagvqvsgag ggfagsniti rgfstftgsn qplyvvdgip ldnsgggnsv
      241 ntgvvnssri sdinpqdies msvlkgaaat vlygsraasg vilittkkak kgsrnqisvg
      301 tntavgmvsq mpefqneyaq gsngnynnsv tgswgpkiag qevtnwfgek enlqafpdni
      361 kdilknsvss vndlsftgsg ekfdyrvsyg ytletgllps nelkrnnisv nastqltdkf
      421 kigssfsyvn nvsertqggn qganplwrgi yaprsydltn mpfenaegnq lwfapedhpy
      481 wsiknvrnnn evnrfygnin lkydilpwla adlkvgadvf sltskgfdnk girsngntss
      541 agaggvqdrs vsmkninsyf tltanraise nwnliatvgn eviannrntl qstglgivlp
      601 nfdnqnnflt fntlgtiten rqigvfadvv ldyksylsln vkarndfsst lskgnrsify
      661 paaavsfvlt eafpelksnv ltmakiranv gevgkgtdpy atntyfgrss asdgfvstlv
      721 sfpfnglagy tlnnsagnek lqpeftreye lgaelslysg risfegsvyk rdtrnlifav
      781 papsssgfts vvtnagslst kgielmlnlv plksenfnwr sgftftkfks iveelapgvn
      841 nisiggftsp nvrlvageey gqlwsnayqr dnqgrmivna nglpkpttnv qkvgnpnpkf
      901 nlgwsndfsy kdfslsflfd fkykgdimsr tigdlriqgv aketagferi dgsgavttpy
      961 lfegvyedgs pnttqvtaqq yyslqgkyva wegyvldatf vklreanlsy rlparlfegq
     1021 kfikginisv ygrnlftyap nfphldpeqn llgisnargl efgfsptprt iggsvrfsl
//
LOCUS       WP_094257366            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094257366
VERSION     WP_094257366.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120807
     Region          31..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqvnkifqm lcilllvflg siaaaqqnde kiisgivqds ekrepisfvv ikkgsvqtst
       61 dtrglfsisa rigdtitfsr mgyhnenili sgniqnqyvi ilhpqvnqie dvvihsgyqt
      121 irqkdltgsv svisqkdler spsrnlldrm rdmvpglvfn khtslkeqnk sisirgqstl
      181 fanaeplivv dnfpyegdie qinpadvesi silkdaaaaa iwgaragngv ivittkkgtr
      241 dgksivdfsv nnswtnapdl nyqpqlsskd ylliekmlfe kgfyksaess inhapispgv
      301 elliahrdgk isseklqqel silegqdiya dlsrlvyrps wnqqyhgslr tgtkltstli
      361 smgydwqden liknnndrlt lslnqnisll kdrlqlkpsi sfsatsrssp nqilsemkfg
      421 ssniypyarl leydgspssi iknyreafts naqekglldw kyrpldeins vddlrrsqqi
      481 rlgiqtnfql dkhlsfelsy rykkdnikgq thygensyfa rnlinqyssi kdgkienpip
      541 kggimdrsye egrlhngrlq ikydrnwsls efkvlagtev sdshflrtqn rlygydgehe
      601 nslpvnyvvs ypvqsnpnsy qkipyqnfgr dltdrylsyy talnyqysdr yifngsmrwd
      661 rsnlfgvqsn qkgvplfsvs agwqlhnekf mqsllgiipl lkvrisyglt gnvdnslsaf
      721 ttsrlypsts fssglryayi vnpanpelrw ervkvtnlgl dlgllknkll fnldlyhkeg
      781 tdlignapft gssgvtkfyg ntgstrtsgg dlsvtgdfrl apvelrsffl fsyvrdkvts
      841 ykvkptilnl lsggyagvhp legkpltgmy alpwrgldpk dgrpigylng eetkdyaaiv
      901 qtstqedlvf lgtsrpkfsg sfrqeigfkn lnlslgiayr lgfwfrrssv nyntilggig
      961 ghgdfarrwq kpgdekttqv pslpeavnyn evsfyqyaqv lmepgdhirf qdislqynwk
     1021 pssvfhqvvf nlyvdnvgmi wkkttsnldp dytlaqpprt ysfgvklnf
//
LOCUS       WP_094256938             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094256938
VERSION     WP_094256938.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108425
     Region          27..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktllkkyl ltlivlmvsl atfaqeknis gtvtdeagsp lggatlrvkg ttvatstdnn
       61 gafsfnvpnd aktlevsyig fqskdvditg teiniqlqss tdqgldevvv igygtarkkd
      121 ltgslvtiqa knfnkglvta pdqliqgktp gvmvinntgq pggaatvrir gnssirssnn
      181 plfvldgvpm sgnsplpegr ggfssdrgnp ltylnpsdia smdilkdasa taiygsrgan
      241 gvviistkkg vagspvvsvg atagvsnire ypnildagrf realnyytps eastsdyggn
      301 enafkaitrq avtqnyyadv sggtehgkyr lsggylnqng iikgsqlkky tgnftgnfnf
      361 leskrlgldl slfltqldnr yapinvfaga egnlisqamq wnptlplidk dgkntfvstm
      421 trnpltslda fkdrattntm vanvspyyki tddleyrfiy simrqtggre gmyrsglidp
      481 saskneqafi snnnetnmqm thtlsynkqv nedwninall gyeylnynfk nnlsfgggfn
      541 ymgldyfdyl qyssistrdi lsyrsptnel qsmflrggfn yrnrylftat vrrdgstkfg
      601 snnkyaifps vaaawninee dfmkdneifd qlkirlgwgk tgnqefpsga slnrfvfgnq
      661 sisqvnygnd dlkwetsati nagidfsifd nrlygsidyf nkkttdalfe qtlaqpapsg
      721 riwvnldgei vnkgveialt gnivrgtdwn wdltgnltll knsvsglvgy yetgalrgqg
      781 ftgvlgqrmv ngqplnvwyl aqyegidpqt gmsmylgqdg sinstndpai nkfysnspnp
      841 ttlvglstnv sykkftfsan mngafghylf nntaatvlgl snlssrnigs qffdtsvkes
      901 tsnsaapstr flekgdylkm anltlsynvg nigntfknfn isltgqnlfi itkysgfdpe
      961 vntdgasngi pslgieylpy ppsrnillgv nfsl
//
LOCUS       WP_094257484            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094257484
VERSION     WP_094257484.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121540
     Region          31..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlyyhslr kvllmaficc lslaafsqta lkgtvtdpqg splvgvtvtn qtqgqvtktd
       61 eqgefsiqak vsdviafssl gyqphkqtle nlgslrisln ptgedleevv vlgygsikks
      121 nltgsvsrld krvletgvrs npasalagti pglrvqqtsg rpgsvpnivl rggttygggg
      181 splvivdgli rsgfsdinqd diesidvlkd asataiygar asngvvlitt krgkdgvsni
      241 slkskigvns lnipfeflda kdylywsrkg vetsgmyqpn qlnqltsvgp fgtgnkykda
      301 dgnildgnkv snavwstmfl ddsnrellnq gyqimidpvt gkeliykdfd ytdyalrkna
      361 mtqdynlavq ggnekskyya slgkyyeqgv pigtnydrit filngdykik pwitsnsgln
      421 fantkwrdai ngegnymtra lgapptmrgf nangdllvgr dwqdgnpavn ndrfirnnqn
      481 qkftmsqafv idlykglslr tsgnwfinqt nnesfnrdyl aspgnwvrtr nssasydkil
      541 nqtynavlny kttiaekhnv damagweffd syntgfsasg sgapsddfmd lgltsteanr
      601 rgidsyhvrn ritsffgrln ydydqrylmt ltlrrdgysn llnnrwgtfp gvslgwnlhn
      661 eeffassiga dnfintlklr asygangnig gigaytlqgt ygtskydgnv gyamtslsip
      721 nlkweslitk evgletrlfn rldlsvayyh rttsdkiatl llpasagfts ittnngdmqn
      781 qgveidlnyq airandftls fnwntaynkn kilklpyngv ennrqngfqv ynpstmelew
      841 vgglqegqdp nvayayealg iirtqqdldn yalqlkdlig frtlvhpdvf namtasekal
      901 hyplalgdvm wrdvnndgii nsydrvymgn tvprwtggfg lystykdfsl sarfdyalgy
      961 vaydgprawf lgmmqgtfnt ttevfdtytp entnakypty ywadqlfknn tsressmfyn
     1021 kgnylafrei slayrlprsl ankmkmedls vsvtgqnlhy wtantlfsae sgsigqgggg
     1081 yplprtvifg lqitf
//
LOCUS       WP_094257415             983 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094257415
VERSION     WP_094257415.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..983
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109819
     Region          30..978
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnltskttar sfllllfgvf wtisafsqqr tisgkvrtad nvplsnvsvl lkgtnigsqt
       61 nndgqfqinv pndgilifss igyltqetei kgknyiniil eaddkaidev vvmgysqvek
      121 qhvassvasm dmestktrpi fkmqeafsgt ipgvtmlqgs nipgavpgti sirgistlqn
      181 adalvivdgm eqsitdldpn qiksitvlkd aastsmygsr gangviivet ergytgkfkv
      241 dlnawgaysn pidlpnwvda aqymklnnet rthqnqtllf sdedirkaet getpsvnwld
      301 eimtrkpfan nttasisggg gvgtfnlmlg higekglndi egtekfsarf ntniniadkf
      361 vlladfyahr lqvdrlmand nghglyqiaw rmnptqqify dnmdipdhyi lhnnmnplas
      421 iakggtknyl ydrstinlrp ryninknlni egnvsymink sankeqrstf kffdgdgapv
      481 tiwknsvtae qgvsssqlta ralanytkdl rsnkdklylt lgtemmsyty tdyreenkas
      541 ffgklnysfd nrylieltgr sdgsskfapg nkwgffpsaa lawnlhnesf fssiresgai
      601 tnlkvrasyg lignenvdpy lwqeivnnwg wtirvpnpdf swekqkqwni gvdvtalknr
      661 lsltaevydk fsydliynnf pvppltgsnn lesavnigev qnkgwelsak wsdkignvsy
      721 nvgamlfdnv nkvlkagysk ndtlifkgds dkiwyngssi dnyygfesng yfqnadeven
      781 tsaklpntlp gdikykdqna dgiindqdri ylgdpfphmn ysinlglnyk kwdfsvmgqg
      841 vgkrngrlvg megypvyvdg gsnslgtprq eyadnrwtes nanarfpriw sgnssnayls
      901 dvwlsdasyf rikmiqlgyt fpgigksikn irlyvnaqda ftftkwegle pergldkskt
      961 enqgngvypr matysfgira tiy
//
LOCUS       WP_094257518            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094257518
VERSION     WP_094257518.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116968
     Region          24..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmrnlltiig flifhstlfa qsnvingsvv nadgapiqsi titekgtsnr tstdsqgkfs
       61 itlrnfpati vatgigykns eisitnlnpv sislqedgav vdevivvgyq qqstrkttss
      121 vqiisgkdie nmaapsfesl lqgrvsgvni qsftgepgar ntftvrgnst lspdlnseid
      181 lantmssply iidgmpmsvt dlatssatgt nyiaginind iesivvqkda aatavwgsrg
      241 angviliktk tgrsgkpqir lsyykgltqr pelqktllga terrtkldil nqyanhnqlg
      301 gltqpltdsl nssfnnatdw qslfyqsgni dnvdgsiagg seivnyrlsl gyyneegivr
      361 qtgfkryslr gnfgfklapf lrsdltfsts rmdrkrglgr ginqvvpidq gsmpssfvql
      421 sdldyafymg qydkllddnk tdilnifskt yvdivpglqy sfeaslqanf dsrdqfqpre
      481 lnqgvnfasa nknnafvynl anvlnyskvl nndhtftltg iqsfqyddyr ssyiygenlp
      541 tddihvvqgv aqknlaansn irksglvsfm gqfaydyksk yifnaswrad assrfgkntk
      601 wgyfpsgsla wvaseeeflk diswlnflkf rgswglsgsl pqdfyapfnv wdlntstydg
      661 gsvatpsfqk pltlpnltwn kseqvnlgfd lrlfndrltv tmdayrkitk dpilsfpfqf
      721 ytgytklsyn vpmtiynegf dvtiatrnma stspvqwntn lnltfnknti gslpfgdkgf
      781 yadsygynqs lfyrvgspiy qwaqmlyqgv ynqadqipvn pitgklltyf knnypvkpgy
      841 phwadvngdy dvwsdsdkga adgdlvptgn pnprltggly neinyknfsv gilgtftigr
      901 diintlksnq yngfggnvfn ftnrrlpdld gvdywtpeka qdpnyeanfp sispyqgyfy
      961 qffpfstmwn engsyfkvkt itlgyllpqd miksfrigls nvrfyamldn mltiqkarvp
     1021 daelvtpqge ysggayplpk kytlgveinf
//
LOCUS       WP_094257540            1163 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094257540
VERSION     WP_094257540.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1163
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127080
     Region          49..128
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cl21470"
                     /db_xref="CDD:473874"
     Region          179..1162
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtqilyrslf iactfmlfch qgrastnern hklelktklp sanidsldii gkitdstgta
       61 vegvviteqg ttnsvlsnen geykiaanpn gvlvflksgf atqeihvnnq kqldvkmlva
      121 tpeseaeetd sanvdssqvd stitetdssm vqvdssqnav atdstaqeat gtapsgqnti
      181 tgtvtgpsgp lpgitvkvvg snatastden gkfqiaadak nkirfssigy ktitqtvgnr
      241 kdiqvvmate tntiesvqvv avgygtmkra tlptavssig aneiedevlp svtqaiqgka
      301 ggvqvtqksg spgggisirv rgttsinass dplyvvdgip vnsttnftgg stfdfgggtq
      361 ginvlssinp sdvqsievlk daasssiygs raangvvlit tkkglagqsq fnfnmyegfs
      421 qvpkeryydf mntaqyqdym kdyyrilqee dpsktipdqi fsnpgintdw qeaifrtspt
      481 rnyelsasgg sdktqyytsv gymkqggvll ssdfdrlsgr lnlnhqhsdk lrfstsmnlt
      541 ratnhrvqee nskegstksg ifsppnipvy ddngnyyydq vrltrenpva mlelptnkaq
      601 tyrilanasa eyniipelll ktsfgtdlsf idetffmppt glrsytsqgg igasrstrdq
      661 lwinettltf dktfgdhyin alggfsvqgs rlefthaqrs gfpnndipyv tgggvitgan
      721 aypeewaias gfarasyvyk dryiinanvr mdgssrfgad nrwavfpsma aawriseedf
      781 lkdnatfsdl klraswgitg nqnignyasr slyssgnnym gqagfipnvl gdkglkwett
      841 rqwnvgvdag ffndrislla dyyykktsdl liglpiltss gfinrftnsg dienkgfefe
      901 lssknlvgef kwntslnmtf nrnkvlalpe glsemrggvg dlnraipgmp lgvfygwkal
      961 gvnpetgmid ylgrngeavt ptdyedhvmi gdpnpqffgg itnnfeyknf dlsilgqfsy
     1021 gndifnynla sglegfnpss nqfidfvdrw repgditdvp rpapgsldng avssrfvedg
     1081 sffrirnitl gyslptevae rikmkrlrfy vtvqnayvft kyrgydpevs sshggantgl
     1141 iygydygsyp qprifttgin ltf
//
LOCUS       WP_094257711            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094257711
VERSION     WP_094257711.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114367
     Region          25..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqqllsfll lfmvsigivn aqnlqvsgkv tsqedgspin gttitvigtn tstqtdesgs
       61 ytisapangs lrfsnigfvs qtvsinnnal invnlvadqa aldevvvtgy anikktefsg
      121 aasvismkei edkpvvnltq nlqgrvpgll ansgsgqpga sanvqirgtk siqgsgaqpl
      181 yiidgvpasa stvqninpnd fesmtvlkda saaalygarg gvgvivittk qgkkgtseis
      241 lrtqfgvtap pdfsrlnlmn tsellayeer vgaitgsqna afsnvpgwyy srknpananl
      301 saaqlaeydr kldstrnint dikdllfrng isqtyelnlr ggsenltyft slgymnqdgv
      361 dktsdferft trfnlgynkg kfsvqfnnsl gyslmrrasg dgfgnsplnp fqmiyrakpy
      421 dnpyladgtl nfggggtnln mktlanlvea nentrwteks wkinsglilg fkitdditir
      481 nttgidadng lyefyinpns yrgslqtfqh glareanrin aqiintssin ynktfnelhk
      541 idvgayfegi rvynkglgmm lynlnpslpw tgqganplpt ngaetmpqya tsarsgygir
      601 syfataaydy agkysitanl rrdgtsrivn idnreittws agatwniiqe nfmkdqtlft
      661 dlrlrasygq apnigsialn syglgfggle awtipnytss qvpgygtaay pgstlpgiap
      721 ttpgnpnlki etvnkanigl dfnmwtnrar fsfdvyseit ndlfvdqpls nttgfnsmai
      781 nagkmsnkgl egmisvdvfr tndidinvgl nhainvnkie dlgavtqyel gtylikeglp
      841 fgshytynyl gadpetgrpm yyaqdgttvv yelanagrfa tfgtykpkhv ggftfdfryk
      901 aftlstlfsy qfdvvrsnni rnwitdgtrg yigsvnqsre lldnqwekpg dqkffaspvy
      961 skgftnsdlq nakflrlrnl tlnynlpein vggvsyvkga nlyftaynla vwspwtgvdp
     1021 eddnnislne ypnpksfvfg infkf
//
LOCUS       WP_094257660            1158 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094257660
VERSION     WP_094257660.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1158
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127507
     Region          74..1157
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrlllfsla lgltmptyas fnankgvval gnhagwtkat svlqntvsgt vsgpdgplag
       61 vtvsvvgssv ktstdesgkf sisanvgsvl rfsfvgyesk evtvagntmn vtlssssdll
      121 devvvvgygt qrkgnltgav ssisvkdnle grpiadigrg iqgttpgltv tipsgevgsd
      181 pkikirgaia svasgsepli lldnveipsi qyvnpddies itvlkdaass siygakaafg
      241 vilittktga kgekldisys nnfsfqnpfk kyemgrlnal kytkdamerv gsnisgaffy
      301 vtpesyelak ewdakygstl gandptvfgr dwivdptnts rklglrtydp yeymvrewap
      361 titnnaslng tvgktrysat fghisqsgml kagdsdkfkr gnaavrvstd vndyltlrag
      421 aifaqrkkly pyatnsttad pwyymyrwss iypmgndehg spirspwsey saaneasmkr
      481 nyinlnagat vnmmknwkfd vdynftnedy nwfrpgtrft aadswiapvq rldaagnpvf
      541 vdangnvvas nttgaiqayd fntyqytagg anpdhvyars afdykhtlna fttynlnlde
      601 ghefkfilgs nlvssfgkyn wtqktnlldi tnpqfdlasg ivtgsggtyw dsqvgffgrv
      661 nyayknkylf eanarrdgss kfidrliwrw ftsgsagwvv seenfmewak palshfkira
      721 sygrignqav spslynptme ayetawigga nkfyavgspk fsvsdvtwey letkdlgvdl
      781 rflnnrlglv fdyyhrntin mfaplegttw tiggaapqgn ygelrtrgye ialdynhrfe
      841 nglgfnvran fddaisrfyn ytssrltsan ydgavygdiw gyetdrlyql ddfvlnsdgk
      901 pqlikltsdm tkyftngqge tyqlkdnngk pvyqsflent atfnfgpgdv kfkdlngdge
      961 idngdgtidn pgdrkiignf tprynyglrl gadykgfdfs iffqgvgqra lwgngglaia
     1021 gfntgdgamp saivdnywtp entgafypaa fnnagsntan nfqvqsryll dlsytrikni
     1081 tfgymfpksf iapaklnnlr vyvalenfft wdklnglpid pevengfsmf nesnynggrt
     1141 gvgtptfksa sfgiqlnf
//
LOCUS       WP_094257790            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_094257790
VERSION     WP_094257790.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116735
     Region          35..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiqkywki nllliflmsi niyvkaqeqn aeiigivvde fqkplkdvii tsvatkngts
       61 sdfdgnfvlk tysskqkvrf elegyhsiev dleperedlv illlkdnhel dkvidlgytt
      121 ttfrnltgav ssvsgseler hpvanlsqtf agrlaglttq etfselsrvn tdlfirgvsa
      181 arkgdplvii dgiptsynsg qsleyispne iesinilkda stqaiygiqg angvivvktk
      241 rgkkgdveik arldqsfqqv ttkplmlnsl qyaelsnqag vndglgafsq fsentinhyr
      301 sgdspelyps nnwydkyfkd fasmqrvgvn vtggndkity fsnlnfmhqg gyfntdtkey
      361 npnpknvwvn yrsnvdvqfn nylsgylrls gnvkrervpg ggsnegvygs mflmppttyg
      421 pltpeildpq tgevmipggq vvttdrinnp tygilnrsgy inhtvtniss qfglnldmsf
      481 lteglklsgv fayqtnsvgs lsntqsfery mrsenwdkle ftkkgeeqns plgfnkghsy
      541 yyhltykgql dysrsfgkhn ilasayglfq dltkantnap ellpykrlst gaqaeynydn
      601 rymlkavfgy sgseqysrah rylftpafga swiasnesfl egskdwlsll kfrgswgkta
      661 ndqsglqrya yldqivvhsg gplgylqylv venqtgnpni qaevstktnf gvdlglfnsi
      721 tfsgdifker menmivgavs tipsyqgipl snyprinegi fdnkgyelsl rydriinakt
      781 sfyvqgmfsk ndnkivswne aertadfayr kreegyslgq efgylvdysq gngffnsqae
      841 idasgltygf geirpgdlry qdlnsdgtid erdlgpigsg vipkvtysfa ggikyaafdm
      901 nfifqgigky sgimtgngiw etsngglyss lhqhawtaer yanneeitwp alsteksvnh
      961 egsdfvnfnk tylrlrnvel gytlqrdktr figfdqiriv lsgqnlftwd kmktkdfgpe
     1021 gpgymgfpvy rvysfgvnlm l
//
LOCUS       WP_094258497             612 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094258497
VERSION     WP_094258497.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..612
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=69188
     Region          <6..611
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpnfrarndd gsnfisgpla agaglynple ildkdsrnnn tqkaigsiyg eynilpnlki
       61 sskygidynn ieedyynnpn ygdgrnvggr syrdytryfn wvwtnlidyr wdidqakdwv
      121 anvkvgyeaq ksqsyyssva vykvplnpky tvpsvgatpi gasgsnddys fasflalgdf
      181 syknkyvlsw syrndgsssf geekqfgnfw saagswnmeq edfikdisfi nalklrgsyg
      241 vtgnagignn twrtlygytr ttynfvyngn igsgpiqygl rdltwertns fdvgldatfl
      301 dnrlsavfdf ynreskglly rvpiplstgf pdyvsnfagl rnrgieftan gtpvrtddfr
      361 ldlsfnisan kntttslvrd dlvespyrrk vgedyfsffl pqwagadpen gdpkwyides
      421 rtettndyrl akrvdlgkss mpkyfgsfgt nmnykgigld affyynfgnh iyqgfysyqn
      481 sggayygsyn qsamelerwq kpgdqsnvpk pvfggnrnsf aasdrllkdg sfirlrditl
      541 syslpssiin nwkvsnlrvy frgsnlwtwv kddtlpfdpe sgssevaggt qgitnfdvfi
      601 pktytfginv gf
//
LOCUS       WP_094258607            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094258607
VERSION     WP_094258607.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117775
     Region          26..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiffmiav lfsiaavays qqrgfrvvdg dskkgiiavv svgnnnlptd sngyfklsiv
       61 nrpvklriqa lnyipldtvl ndyngsvtfy lkpvvkeiee vvistgyqki kqeqltgsvq
      121 yigshvlenq vstdvlsrle aissglsvdr staqgritir glssingpkd vlivvdnfpy
      181 dgnlgninpn dvesitllkd aaassiwgsk agngvivitt kkgqfnqdlq iqssinnnvi
      241 skpdlyrlqs msssdyidve sflfsqgyyq sayddpakpg ltpvietlyn telsssekkd
      301 lldrwrhldv rdefkskvyg vglnqqynlq anggnrrynw latagydrnr dnldalyarl
      361 tlryaleinl aknlsvdmni thanaqsksg kqgyteital ngtlypyaql tdedgnampl
      421 vqnyrlsyls tldgrladwk yypltdylfn kdeinlnntg invgmnyrya gfdvqalyrm
      481 erqqttneni ydaqsyfard ivnsfaqpad dgsisylvpq ggimdvqngy llannlrlql
      541 nydkrfgshh fnalagaerr slrnesnsyr yfgletntln tglvdltkry phyitgsnsf
      601 ipgrqslglt rnnfvsfygn asysyrdtyf iyasarrdas nlfgvstnnk wkplwsvgla
      661 wnvdndlpwl kssaslklra sygfsgnadp srtglttity ntvspftqsn fasitrfynp
      721 dlrwetvgtl nigadfglfd rrisvsfdyy rkratdlfgf ypidytsgvg ptmvrniasm
      781 eghgidlrle srnlvgnglq wgtiinfstn rdkvtdyydv stkggdyigt gtitglvgkp
      841 vysvfsyryg gldqqgnplg ylnndlstdy veltgngssl tdlryhgsal ptvfgnftnr
      901 lsynrlslev alaykfgyyf rrssiqytnl vgsgrghsdy slrwqntgde mhtnvpsfqy
      961 pvndsrslfy qlsevlvepa dhlrlqyvsl syqlenkfkn lgirdmriml nasnlgllwt
     1021 snkkdldpdy dnvlqpskay alalqfkf
//
LOCUS       WP_094258712             982 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094258712
VERSION     WP_094258712.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 982)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 982)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 982)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..982
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111808
     Region          40..980
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnkiklsyl iiffllgasl pgmsstysly rfafqqelid ttelsekevs dfnrqrsivg
       61 vsdsinviel kkapftslad ivkgnlsgvn vqqpsgepgs yqnlvfrgik nkmfsnvdln
      121 anrmavfvng ipiaqdhsfa yeiqkydinr igpgtdllnt idirsiesie likdplklae
      181 igplaangai witttggksg freisidayt ginsiqsitp inaqyenlfr qpfyslygnt
      241 dlrqkypgyl adstnlnyyg psnwkdgyyk vallhnvnmg lrggtdranf gfygaytgda
      301 nssdetglqr ynalfninml pfkwfkisan inairterdr nknirdryae maylpdlstp
      361 ispsnnlysq fanhydaavd dnvtntvrgg ldlqfdilkn lqfnsnfsid ysegirdvfy
      421 pselmetinf vsnyfgysqr yifsnellyk kqvnedhlfs akggikyqdd lyrynyaray
      481 dgpndfikin vvsgdsqred ylkpiggiqv yrinnreiyr mfsvfgkfgy qykdfvnidg
      541 lirwdassna qpnsrwlftp slranwnvkn qlelenqfsv rasfakigip ewnsryamgp
      601 qysvqmgwkn epslvsyfgq agfsrpyqtg wigynldway tnqadltlen gflndriqtn
      661 lslyyqenkn qlmlvpvpqe ygyqgiykng mdvrntgvdi svsaqvmpke sdfqwrpsin
      721 lnfnknelta lpgglkelev gdrllrvgea vdkfwllnne giydnnsqip tgengkklny
      781 qgvelqagdp kwkdlngdnv inksdrslmg nsspklyggf tnnfkyknfd ltvqayfalg
      841 qkalnqrasn rydfintess rdinavkeif hwqqdvdisk yplynvwssv vpyrlnqdlf
      901 ledasflkir tvslgydfsn teflknnvkt lrraylyvmg nnlltvtkfs gsdpelinfn
      961 giydgsglal aptytlglkl df
//
LOCUS       WP_094258739            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094258739
VERSION     WP_094258739.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120278
     Region          50..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvfsdfhr gstrtystli lllglgispa iansysteva kkewpnqqki sisgviydeg
       61 tntrlsgvti lsegkvigts nangefsiqv esgkpvifqs lgyhsktqqw tsdsqsvrin
      121 lttsdesiee viitalgikr eekslgyavs qvtgkqmtda tpsnwvdamk gkvaglsitq
      181 assgplntar inlrgdrsld pknnealivv dgipmvngrf ssgvtdayga gssgpdkdip
      241 idfgnglgdi npddiesisv lkgaaataly gsragngali ittksgnknk kgigisinsn
      301 ssfqsilkwp dfqyeygqgn ldrnadgeqy ysygltqdgk ntgstssayg pkfngqeyfq
      361 ydpntetggt trtpwvaykg gvkdffnvge tymnsisldg gnevfssras lthtknswim
      421 pntgfqrlva ainssaklse klrinmkvny tnkssdnlpg tgynnqsiay fmifqnpsis
      481 ldwyrpmwkk drenieqihp fssyienpfi iayemtnslq shgidgmlqg qytfnpkwei
      541 mlrsgismrs dqrqqrrpwd tanfplgyyk qqdlfymesn tdallsfndk inedfsiras
      601 lggnlmrrdl keniglargl tspgvyklsn astspfadnt itqkeiqsif gmvnlgwrem
      661 ifvdltarnd wsstlpsnnr syfypsvsss fvlsemlemp ssisfaklrf swaqvgndad
      721 pyqtikyfns sifpgsaeap sllhnanlkp eisnsteagl nisffnnrlt advnyyfnrs
      781 rnqilrvprd vttgfsseii nggliqnrgw elslsgtpvr nenfqwnvsa nwaknnnkil
      841 elsegvetpq qiiassgsgv aeiiatvggs tgdlwgyglv rndqgqviyd aktglpvrpe
      901 dkvkignaya dwrggfhnef ryknlslsal idgqyggivy sqthhkmteq gklehtlrgr
      961 etgklvgegv iqnedgsfsp ntkevainty yadyyrranv etnsfdasyl klrevrfeya
     1021 lpktwvsrwk mnsasvaffg rdlfmisnfp mydpetaaln gatimpgvem gqmpstrtfg
     1081 mnlkvnf
//
LOCUS       WP_094258803            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094258803
VERSION     WP_094258803.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117148
     Region          27..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrtiyfylv glfialsigq vqaqhlikgk vidaqnqaie gatitekatq kqtqsnslge
       61 fsldastanp qltvrflgfq ektitvsssg fvqiqlspse dvleevvvta lgisrekkal
      121 gyavqevkst elqtrptnam aalsgkvagl qvvsaggnmg gstrtllrgi nsiagnnqpl
      181 yvvdgtpidn sdlnssstin gsagkdvgnm iqdlnpddie nisvlkgpsa aalygsrasn
      241 gvilittkra gkgeqvsidv nsglefeniv rlpkrqqlyg qgyspvfqtv qiegkeykiv
      301 dyaadeswgp kldgtavlqw ynlnpedaad ylnpspwlyp ehdvhyffnt glantnnvai
      361 sgnsgntnyr fsytnknvkg tvpnaslgrn tlnfsggtkl grlsinssin yihntslgkp
      421 wtgasnrnii leayqwgavq vdykrleqyk radgtplawn rtgwqntpaa eatrfidnpy
      481 wsayesylee krdrfygnig aqyevsdwlq igakvhgdiy qfgtqdriav ysrsasqyee
      541 tsnklneyny eflatakknw nnlslvanag anlrdqnrkv dyaitqggli vpnyynlkna
      601 stvkienyty nrriaslyas aslgyhdllf ldatvrndws stlpshansf iypsftgsfv
      661 fsqlpgfsaq dwlsfgkvrl gwaqvgndtd pyqlnkvydv eqsfdgkpsn klpstlnnad
      721 lkpeitsswe tglslqffrn rlgldityyh ntsrnqilpi pvsssfgyea kvlnagkven
      781 kgleiilngt pvrnenfewn sslnwsrnkn kvlkldelvn tltlssslin lvaregqpyg
      841 qllgydfvya dgqrvvkedg tylrtsqlvp lgsvlpdylf gfqnsfrykn lsfgflidgr
      901 vggsfysqty nvgmysgile rtaennvred glvldgvkad vvfnadgtyt tsnirendtr
      961 isaqqwgrne sngpttfsif dgtfvklrev tvgynfplnn pkvvkgvrls ayarnvwniy
     1021 tkskyidpef anssgnvqgi eggniptplt ygfnvnlkf
//
LOCUS       WP_094275175             369 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. OK302].
ACCESSION   WP_094275175
VERSION     WP_094275175.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. OK302
  ORGANISM  Rhodococcus sp. OK302
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Rhodococcus sp. OK302"
                     /db_xref="taxon:1882769"
     Protein         1..369
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37818
     Region          13..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(25,80,99,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(54,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 metsksaqvr psvgvpress dgerrvalvp kivstligkg vdvivesgag lgalipdely
       61 saagakigdp wtadvvvkva ppsseeiari ssgakligfl nprnadnria elkaagiegy
      121 aveaiprisr aqvmdalssq anvsgykavl laasestrff pmlttaagtv kpatvlvlgv
      181 gvaglqalat akrlggratg ydvrpevadq vrsvgaqwld lgidaagegg yareltdder
      241 akqqqaleda ikgfdvvitt alvpgrpapr lvtaaaasgm kpgsvivdla getggncelt
      301 epgqtvvkng vticsplnlp atmpehasel ysknisalie lmlvdgalap dfsdeviaga
      361 cvtreekga
//
LOCUS       WP_094279867            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094279867
VERSION     WP_094279867.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117492
     Region          69..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskikswsi pqnihninyl rpknllslml csgsmllcsa veasphhlwk adkietnyli
       61 pvhfeqqttv tgtvvndqgn pianasirvk gsnegsqtne rgefsfetaq srgtlvvshm
      121 syqtlevpin atsamrivlq ddaanleevv vtsfgiqrdr ktlgygvgev kaddlakapt
      181 tdvtnalagr lagvqvsgag ggfagsniti rgfstftgsn qplyvvdgip ldnsgggnsv
      241 ntgvvnssri sdinpqdies msvlkgaaat vlygsraasg vilittkkak kgsrnqisvg
      301 tntavgmvsq mpefqneyaq gsngnynnsv tgswgpkias qevtnwfgek enlqafpdni
      361 kdilknsvss vndlsftgsg ekfdyrvsyg ytletgllps nelkrnnisv nastqltdkf
      421 kigssfsyvn nvsertqggn qganplwrgi yaprsydltn mpfenaegnq lwfapedhpy
      481 wsiknvrnnn evnrfygnin lkydilpwla adlkvgadvf smtskgfdnk girsngntss
      541 agaggvqdrs vsmkninsyf tltanraise nwnliatvgn eviannrntl qstglgivlp
      601 nfdnqsnflt fntlgtiten rqigvfadvv ldyksylsln vkarndfsst lskgnrsify
      661 paaavsfvlt eafpelksnv ltmakiranv gevgkgtdpy atntyfgrss asdgfvstlv
      721 sfpfnglagy tlnnsagnek lqpeftreye lgaelslysg risfegsvyk rdtrnlifav
      781 papsssgfts vvtnagslst kgielmlnlv plksenfnwr sgftftkfks iveelapgvn
      841 nisiggftsp nvrlvageey gqlwsnayqr dnqgrmivna nglpkpttnv qkvgnpnpkf
      901 nlgwsndfsy kdfslsflfd fkykgdimsr tigdlriqgv aketaeferi dgsgavttpy
      961 lfegvyedgs pnttqvtaqq yyslqgkyva wegyvldatf vklreanlsy rlparlfegq
     1021 kfikginisv ygrnlftyap nfphldpeqn llgisnargl efgfsptprt iggsvrfsl
//
LOCUS       WP_094279231             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oceanimonas baumannii].
ACCESSION   WP_094279231
VERSION     WP_094279231.1
KEYWORDS    RefSeq.
SOURCE      Oceanimonas baumannii
  ORGANISM  Oceanimonas baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Oceanimonas.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Oceanimonas baumannii"
                     /db_xref="taxon:129578"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53486
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipretl sgetrvaatp ksveqlrklg fevsveqgag skasfedaay eaagaqlasq
       61 ddvwqaaiiy kvnaptadei erlqagttlv sfiwpaqnpe lveqlknkgv tvlamdmvpr
      121 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvlv igagvaglaa
      181 igaagslgai vrafdtrpev keqinsmgae fleldyeeds dssdgyakem sqafidaema
      241 lfmeqakevd iivttalipg kpapklitad mvaamapgsv ivdlaaqngg nceltkpgel
      301 fvsdngvkii gytdlngrlp tqsstlyatn lvnlakllck ekdgninvdf ddvvlrnmtv
      361 trdgevtfpp paisvsaapk akaaaqpaae thakkpsnlk yylggtgvll fawlaavapa
      421 eflshitvfv lacivgyyvi wnvshslhtp lmsvtnaisg iivvgalsqv gsggfvsfla
      481 fvavliasin vfggftvthr mlkmfrkg
//
LOCUS       WP_094279976             987 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_094279976
VERSION     WP_094279976.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112049
     Region          65..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msvlwkfksl lifmsmsvgh ahchnvdfan lslqdttetd svppldtlal lkplyeldlp
       61 kfnnirnmkt tslitanslq qyikgelpgv yvsesngepg sniqmfvrgi skpiltnrdi
      121 ynsqplvvld gipligehpf afdvqnydve rigtennlla nfdidniesi kvlkdlsava
      181 tygplaangv ieitsrkaag dgnkritvns yigmsqrptv ttingayena frkqfydlyt
      241 sngkfnqddv ypiylsdsln ndyygpsnws dsyysnglnh gvnanisggq pratfqfslg
      301 nvktsgvadd tkmdkynarf flnlrpfkwl nfetlfnasr vnrdrnrnlr nrfammgylp
      361 dlgaplapnk evydlyleef dksfdknfnn ilegffrfqi nagpiklssk fgvdynegyr
      421 dlfypstile nsnfasnyyg ynqrllvdnk lsydiendvn yfyfevgnsl iwdtykynya
      481 yaykgvndfi klnllesdpn ngnylnptaf prqlvykfld rtkhnmvnfy gkasytynks
      541 ytaaltmryd gssnaqpttr wffspilalg wdakndlaqd ndaismlnir asvgrighyn
      601 lydnysqgps ytaeigytgn rivpgynaia alvrpynvgw vgydlpwsys dninlgfdlg
      661 fdkrniqisl dayvrdtkdq limlpgkkdy gyayqyeagm dvrnmgidls asgnvvqndk
      721 vswntgivlg vnnnkllalp ngldqvevnd rllkvgerid afwlyqnngm yqtddqvpva
      781 ngqkmtyngi ilkagdpiws dtnadnqitk edkvlqgnil pklsgswnnm vtyknfdlnl
      841 nfyfslgrki vnqemsnrfn fienenassi nsikeitywe krgdyslypl ynpwssvtpf
      901 qtnqslfled gsflklrtvt lgynfkdivg nslgkngdly vylsannlft vskysgrdpe
      961 lvnylgydqg yslpiprtfa lgfklkl
//
LOCUS       WP_094280275            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094280275
VERSION     WP_094280275.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111449
     Region          50..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrfsrpff plkrshlvag aviiglslpg sssvanelnr devesyssqq evkgkvtsgg
       61 vvlpgvtvtv kedpskstst nasgefsiaa engqtlvfta ighekkevai tgttvnveln
      121 sseenidevv vtgystqkkg disasivsld qkklkdtksp nvsnllqgkv agvdvvgtgr
      181 pgqqanvkir grsslssgtn plwvvdgvit hgvaninpnd iesisvlkda aattqygsrg
      241 tngvivvttk ralregegtf svnlssgisk fnfgnfdlmn sqelwdyyqt fpnqddiddn
      301 vskdvlnndy nwlkngtqna pvndfsasym gktdktsvfa sanyygekgs ikgydferlt
      361 grfnvehklt drltfkpkln asyttytdkq hslynmmfyl pwdnpyntdg tiknpqapna
      421 tvawfgrdht nylydlqyny gkgqtldmqg nfdfsyrisd rftfesmnnl tyynqtamry
      481 adpnsnegrg nkgtiyqfsd kritrffnqm lkynetfgkh tvsgfaayey sdyvyssqna
      541 tgkgiapgse ilgnaasvld fggtkndysf qsgilqgtyg ydnrynvmas frvdgssrfg
      601 reqqygafys vsgawninne affnvpsinl lrlkasyggv gnvpvdyyss fatyglnaqy
      661 ngepaaiqkn fqnahvswek sydanlglel gmfnrlnlsv dlynkntsgl lyfvdfpsta
      721 gwdgywlnig glrnrgveva lsgsvfspgn pfqwdlgvni ahnnnritsl kddqdipkgn
      781 mrfsvghdvd swymrkwvgv npengaplwe svneetgevs ttsvyndatl qfvgaatpkf
      841 qggfnsamty kgfnlnanfa yqnggityna arelfdsdga yasynqmilk dgwsrwspen
      901 pnathpkaey nntslsnkts srylestnfl rlrnvtlgyt fseslvnklk lkglnvyvsg
      961 dnlwtstkfs gldpeaailg ndnavdkagg gdatsqypap krlvfglnlt f
//
LOCUS       WP_094280301            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094280301
VERSION     WP_094280301.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112610
     Region          26..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msnfyskccs ltivmlisis tlfaqqtvtg kvtgpnganl pgvsvsvvgt dkvtqtnseg
       61 nfsieanngq kirfssmgyl tkeamvssts lninlqedas nidevvvtam gikrerkslg
      121 ysfqevkseq ltdaketnva nalvgkvsgl qvikgssgpa sstkitlrgn nsltgdnqpl
      181 iivdgvpmnn flgakggngk vnndfwnpgt dmgnglgdin pediesmsvl ksgaasalyg
      241 sragngaiii ttksgkaqkg tgitysstvg fetifmtpei qsafgqgsng vfdaistnnw
      301 geaidgnkyq aydninnffk tgfnhtqnva fqqqigetni yssatylndq skipgssler
      361 lnlmskvstt fgpnkrwste vkvqymnnda tnrpisgqnn snafatlfrm prsinildyk
      421 npvdntgkmr wygttnsinp ywlaeynlnn dvrnrflsna nikykitdwl diegragldt
      481 yasrfenkty sgsplsstgl ystgktefae knftlalhar kdeingskwg vngsvfgqim
      541 rsdetflgvg vgelevpnff yvtngkgnpt pnqynnrkqi nslygtaeln ydgywflnit
      601 grndwssals keyrsyfyps vstslvvsdl irksggnlps ainflklras yatvgndmgp
      661 yqifnaydig rdpngnttsg lgevfynpnv rseliktlef gfdtrlldsr lgidfawykn
      721 natnqlldip mnpmsgfrak kinagniqns gfeialdgqi lrsddglnwn ssvnfsknvn
      781 riieltpeie yynlggfdni avraisneif gqiigskflr vddqnsphyg klilngnglp
      841 qsvdgqvlgn qspkalagwt nsfsyknigl sfqidgrfgg effsgtnvnl qangtaaatv
      901 tdgkradfvv dgviqdgqny tqntksvtvq qywtqvattg nmgigeaniy datnirlrni
      961 tlsynlpssv lksnilqrar iaftvnnawm iksyangvdp esvfsinsna tgfenfatpt
     1021 srsyfvnltl gf
//
LOCUS       WP_094280336            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094280336
VERSION     WP_094280336.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119272
     Region          58..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnknhyftkv rwskafihla llspsllfat atfgnegkie isrnyanitf nkslqtevsg
       61 tvkdkdgnpl sgvtvtvqne nkststdang kfsiavssss svlsfsfigy ttksvsasna
      121 knvildssed vldevvvvgy gtqkkshlts avsqvdpkvl qnrpsptitn mlqgaapglv
      181 vtrnsgrpgg qglnisvrge tsangsvspl vvidgvisse etfvalnpsd venisilkdg
      241 gataiygaas sggvilvttk kgksgkgris lssnlgiqrp gsmpdrlsli demnyvnlar
      301 knagiaeeyn eedlnyavng ptfvlgsndl wrtynqenil dqviqkkyni ynnniqftgg
      361 sekitymasl gnmaqngmfk vgddkfsrin aranisaqvt dylkldvgna finqktdnpq
      421 dggysidggg nsilrqfyss rmrfpiyned gtyyrsgtss afgyalmkdg gfnddlkrty
      481 fnnvtatvnn lvkglevrlm ysresidlqn rnfrrtvdyy sgptaksktq lnnpnsysit
      541 nyktlkqnvq alvdydltia enhnfhvlgg yqfydhdyqy itastknlyv ndspslnfts
      601 dplnkshnqg aqrekvqsff grfnynykek ylfeatfrsd essrlspdir rkvfpsyslg
      661 wnvakeewfq gatpfinelk priswgkvgs kigvgfydyi aqlstnsnll lndikqtyly
      721 qsaipaqait wetietrnlg ldfsllnrkl fgsfdyyqky nnnmlvslsl patlgiaipk
      781 sndgrlktwg weaslgyrdq vgdfnynvgv sladnknrli hyggannvvy tgsnklvegy
      841 amnsvwvykt dgyfqsegel qnapsyaqfi nkngvpglgd vkyidlngdg kitpggntlg
      901 dtgdliylgd tnpryqfgin aylgyknfdf sffiqgigkr llkpsneliq pqlyswylpm
      961 dfqmdywted nrnaafprpf legshnfqns dkwylsgaya rlknvqlgys lsktqfaklp
     1021 fervrlyvsa edlltvsklg vfkgaidpei rpedgkvspy pfattvsfgl nidl
//
LOCUS       WP_094280650             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094280650
VERSION     WP_094280650.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108347
     Region          30..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mirdfynwqf rliiififsf qivsgqqnlq lsgkvmdeag kelagatvrv kgtnkqvstn
       61 esgqyvldgl sagsmvveat yvgygsseqn vnltssqtld ftlssnasei gevvvigygs
      121 vekkhvtgav snvqskdfqk gaitspdqli qgkvsgvsit snggspgags tirvrggasl
      181 sasnnplivv dgnplsgagi tgsanplsli npndiesmti lkdanataiy gsrasngvii
      241 ittktgkigr pkltlstvns lstianqvdv ltadqvrsfv nergtaaqkg llgsantdwq
      301 sliyqnaftt dnnvtlaggl knmpyrfsig hleqsgilkn dmlrrgtlgv nisprffdnh
      361 lkldvnfkgt ltnqdfantg aigsaivfdp tqevydsssp yggffewqeg avpnslsprn
      421 pvsllenyan rgdskrsign aqldysfhfl pelhanvnvg ydiavgkgat sipdfaasnf
      481 ankgffqryk gkmnntfieg ylsyvkdies insnvnvtag ygyydnketq ynfesmnahn
      541 dvlttpnfpd nvqqnrllsy ygrliysfsd ryilsgtvra dgsskfspdg rwgifpsaaf
      601 twrikgenfl kdnnsisdlk lrlsygetgn kdgianygfi psyyystnes qyqvgnqfyh
      661 vyspiaydet lrwestttan igldygfwgg risgsidayq kktkdllati eipvgtnysn
      721 qlltnvgnme nrgvegsini qaiksenfnw dlgfnmtvnd skvtnltlsd npgyqlaagw
      781 itggtgnviq yhtvglapfq yfvykqvydq qgqpleavye dlngdgavtp adryyykkpa
      841 pdyfmgftts inykrltlnt vlrasfgnyv ydnissnfgv grnilnpsrf innattdvyn
      901 tnfnnnqyys dyyinnasfl rmdnlgliyn vghldkektv tmtvnanvqn vfivskykgv
      961 dpelfngidy tlyprprvys lglnfgf
//
LOCUS       WP_094280761            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094280761
VERSION     WP_094280761.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121553
     Region          31..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlyyhslr kvllmaficc lslaafsqta lkgtvtdpeg splvgvtvtn qtqgqvtktd
       61 eqgefsiqak vsdviafssl gyqphkqtle nlgslrisln ptgedleevv vlgygsikks
      121 nltgsvsrld krvletgvrs npasalagti pglrvqqtsg rpgsvpnivl rggttygggg
      181 splvivdgli rsgfsdinqd diesidvlkd asataiygar asngvvlitt krgkegvsni
      241 slkskigvns lnipfeflda kdylywsrkg vetsgmyqpn qlnqltsvgp fgtgnkykda
      301 dgnildgnkv snavwstmfl ddsnrellnq gyqimidpvt gkeliykdfd ytdyalrkna
      361 itqdynlavq ggnekskyya slgkyyeqgv pigtnydrlt filngdykik pwitsnsgln
      421 fantkwrdai ngegnymtra lgapptmrgf nangdllvgr dwqdgnpavn ndrfirnnqn
      481 qkftmsqafv idlykglslr tsgnwfinqt nnesfnrdyl aspgnwvrtr nssssydkil
      541 nqtynavlny kttiaekhnv damagweffd syntgfsasg sgapsddfmd lgltsteanr
      601 rgidsyhvrn ritsffgrln ydydqrylmt ltlrrdgysn llnnrwgtfp gvslgwnlhn
      661 eeffassiga dnfintlklr asygangnig gigaytlqgt ygtskydgnv gyamtslsip
      721 nlkweslitk evgletrlfn rldlsvayyh rttsdkiatl llpasagfts ittnngdmqn
      781 qgveidlnyq airandftls fnwntaynkn kilklpyngv ennrqngfqv ynpstmelew
      841 vgglqegqdp nvayayealg iirtqqdldn yalqlkdlig frtlvhpdvf namtasekal
      901 hyplalgdvm wrdvnndgii nsydrvymgn tvprwtggfg lystykdfsl sarfdyalgy
      961 vaydgprawf lgmmqgtfnt ttevfdtytp entnakypty ywadqlfknn tsressmfyn
     1021 kgnylafrei slayrlprsl ankmkmedls vsvtgqnlhy wtantlfsae sgsigqgggg
     1081 yplprtvifg lqltf
//
LOCUS       WP_094280799            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094280799
VERSION     WP_094280799.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111833
     Region          23..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myktlthlfl wlfaiqltya qqrtikgtvv deqtksaivg atvrldaskk atstdesgkf
       61 sleapagpvn lsisvlgynt vkqtvsatds vinismspqt ariddvvvta lgvqrksksl
      121 tystqtvkge eltkvkdanp mnnltgkvsg mqinrsssgi ggsvnivlrg fksnrnnqpl
      181 yvidglpitn tggsgsegaf gggpdrgdil stlnaddils invlkgasas alygsqgang
      241 aimittkkga egnlkidvss sitadqafyl pklqyrygqt tqdseeswge kgsfqdpvdn
      301 ffntgttlin tislsggtek mqnyfsygnt snkgilptns fkqhsatfrn stnffdnklt
      361 fdgsmmysrq dihnrpssgl yfnpiaglyl fprgldfdky knnyeylspt rnlylqdwwn
      421 inadagltgt hhsqnpfwvl nrnptfqwrd niiaqgqlky ninewlsvsa rgtlnkrwdk
      481 werhvyagtq gvlsgekieg vlndngrytr dqtestalyg dllfignktf aedwdlnfta
      541 gtsindtrsn gwnldqlkla vankfllsni yrdapinvln esisrrqlqs lfastnlgyk
      601 dkifldltar ndwastlant pqekkgyfyw saglsavlsd mikmpsfity sklrltmaev
      661 gndvgiysti ptntlatgil nanvsgpyqg lplrpeisrs yevgyegrfw ndrinfdlal
      721 yktntkdqyf syeapvgqvy ttvflnagnv enkgieaalg idaikkdnft wntsvnftan
      781 rnkilelapk lgerysvggn fnvlrlngsf gdfwartflr dsngvmvvdd tgrpqigpeg
      841 yignnnpksi vgwnntvnyg kfglsftida rfggqvisvt dgylnsfgvs eesaaardag
      901 gldipavkmd gtpwqgkipa qayysavgnr dgiiegqvyd atnirmreis ltyalpikwk
      961 gvnsasislt grnlfffhnd apydpelntt tgvgaqgyds fslpatrsyg lnlkvsf
//
LOCUS       WP_094280821            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094280821
VERSION     WP_094280821.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115916
     Region          27..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlptclsia vaslctiqml saqqlsiagk vtnaegepiv gasifikgtq qgtasnengl
       61 fslnapsngi ltiravgyss ievpingktn lsvqlqhvds eidevvvtal giqrsekslg
      121 yaaqgvtnet lnsnkqpnlv nalqgkiaga tisstggapg qganiqirgi nsidptrdnn
      181 plfvidgilm dnstsvqgga evrgmsnrsv dinpddieti nilkggaata lyglrgangv
      241 viittksgka gtlridyqgt vgfenvnkfp kmqdtytqgw kgvynkddfw pawgptveea
      301 mkvdpthpst lykpfeeafd tgnqfrnsln isggsekftf ltslsqmkhn gvmpstdfkt
      361 yqarlntnft isekfkggss lavsnsggyr gnanryaeql iywtprynir dylmdngtmk
      421 sygdtdnpiy vantnrlkdd vlrviggvdf tfspakwldl myragidayr dnregtaigy
      481 qgladerlvy dngvegadgr gfynvysnnf rainstfiat fkhdfnedfn aklrlgqdiy
      541 dryikrtstq ggdltvynwf dlgnaniika dsyiekyrlm gyfaelemty kdflfltlts
      601 rqditsslap knrsfnypsa tvsyvisdhi tlpevinfgk lrfsyaqigk dappystssg
      661 fgpysnlptg yigftrpall gnvelkpeft dtyeagfelk ffqsrlgldf tlynsisrdq
      721 iiqvpvtsat gfvtasinag siqnrglelt lntvpvkken ftwnsninfs inrnkileir
      781 edlddeivvs seygylnstv smrirpgesy gtlygrtykr yytadeiaqg ldktreydes
      841 rplligangf pvlestsvpk klgnvqpswv ggwnntfnyk nlslnilvda rvgqsrynql
      901 gnfmaafgea dytedrndyk vfdgvladgs kntkevwlgq gkdpkngvdy gngyyrdnfr
      961 gnsqffveda swlrlrsvsi gyslpqqwld nkviknaris vignnlalwt kysgydpens
     1021 ttasgsnieg fagmtypavr sflfslnvgf
//
LOCUS       WP_094281029            1158 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094281029
VERSION     WP_094281029.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1158
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127521
     Region          74..1157
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrlllfsla lgltmptyas fnankgvval gnhagwtkat svlqntvsgt vsgpdgplag
       61 vtvsvvgssv ktstdesgkf sisanvgsvl rfsfvgyesk evtvagntmn vtlssssdll
      121 devvvvgygt qrkgnltgav ssisvkdnle grpiadigrg iqgttpgltv tipsgevgsd
      181 pkikirgaia svasgsepli lldnveipsi qyvnpddies itvlkdaass siygakaafg
      241 vilittktga kgekldisys nnfsfqnpfk kyemgrlnal kytkdamerv gsnisgaffy
      301 vtpesyelak ewdakygstl gandptvfgr dwivdptnts rklglrtydp yeymvrewap
      361 titnnaslng tvgktrysat fghisqsgml kagdsdkfkr anaavrvstd vndyltlrag
      421 aifaqrkkly pyatnsttad pwyymyrwss iypmgndehg spirspwsey saaneasmkr
      481 nyinlnagat vnmmknwkfd vdynftnedy nwfrpgtrft aadswiapvq rldaagnpvf
      541 vdangnvvas nttgaiqayd fntyqytagg anpdhvyars afdykhtlna fttynlnlde
      601 ghefkfilgs nlvssfgkyn wtqktnlldi tnpqfdlasg ivtgsggtyw dsqvgffgrv
      661 nyayknkylf eanarrdgss kfidrliwrw ftsgsagwvv seenfmewak palshfkira
      721 sygrignqav spslynptme ayetawigga nkfyavgspk fsvsdvtwey letkdlgvdl
      781 rflnnrlglv fdyyhrntin mfaplegttw tiggaapqgn ygelrtrgye ialdynhrfe
      841 nglgfnvran fddaisrfyn ytssrltsan ydgavygdiw gyetdrlyql ddfvlnsdgk
      901 pqlikltsdm tkyftngqge tyqlkdnngk pvyqsflent atfnfgpgdv kfkdlngdge
      961 idngdgtidn pgdrkiignf tprynyglrl gadykgfdfs iffqgvgqra lwgngglaia
     1021 gfntgdgamp saivdnywtp entgafypaa fnnagsntan nfqvqsryll dlsytrikni
     1081 tfgymfpksf iapaklnnlr vyvalenfft wdklnglpid pevengfsmf nesnynggrt
     1141 gvgtptfksa sfgiqlnf
//
LOCUS       WP_094281064            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094281064
VERSION     WP_094281064.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114281
     Region          25..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqqllsfll lfmvsigivn aqnlqvsgkv tsqedgspin gttitvigtn tstqtdesgs
       61 ytisapangs lrfsnigfvs qtvsinnnal invnlvadqa aldevvvtgy anikktefsg
      121 aasvismkei edkpvanltq nlqgrvpgll ansgsgqpga sanvqirgtk siqgsgaqpl
      181 yiidgvpasa stvqninpnd fesmtvlkda saaalygarg gvgvivittk qgkkgtseis
      241 lrtqfgvtap pdfsrlnlmn tsellayeer vgaitgsqna afsnvpgwyy srknpananl
      301 saaqlaeydr kldstrnint dikdllfrng isqtyelnlr ggsenltyft slgymnqdgv
      361 dktsdferft trfnlgynkg kfsaqfnnsl gyslmrrasg dgfgnsplnp fqmiyrakpy
      421 dnpyladgtl nfggggtnln mktlanlvea nentrwteks wkinsglilg fkitdditir
      481 nttgidadng lyefyinpns yrgslqtfqh glareanrin aqiintssin ynktfnelhk
      541 idvgayfegi rvynkglgmm lynlnpslpw tgqganplpt ngaetmpqya tsarsgygir
      601 syfataaydy agkysitanl rrdgtsrivn idnreittws agatwniiqe nfmkdqtlft
      661 dlrlrasygq apnigsialn syglgfggle awtipnytss qvpgygtaay pgstlpgiap
      721 ttpgnpnlki etvnkanigl dfnmwtnrar fsfdvyseit ndlfvdqpls nttgfnsmai
      781 nagkmsnkgl egmisvdvfr tndidinvgl nhainvnkie dlgavtqyel gtylikvglp
      841 fgshytynyl gadpetgrpm yyaqdgttvv yelanagrfa tfgtykpkhv ggftfdfryk
      901 aftlstlfsy qfdvvrsnni rnwitdgtrg yigsvnqsre lldnqwekpg dqkffaspvy
      961 skgftnsdlq nakflrlrnl tlnynlpein vggvsyvkga nlyftaynla vwspwtgvdp
     1021 eddnnislne ypnpksfvfg infkf
//
LOCUS       WP_094281283            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094281283
VERSION     WP_094281283.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116968
     Region          24..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmrnlltiig flifhstlfa qsnvingsvv nadgapiqsi titekgtsnr tstdsqgkfs
       61 itlrnfpati vatgigykns eisitnlnpv sislqedgav vdevivvgyq qqstrkttss
      121 vqiisgkdie nmaapsfesl lqgrvsgvni qsftgepgar ntftvrgnst lspdlnseid
      181 lantmssply iidgmpmsvt dlatssatgt nyiaginind iesivvqkda aatavwgsrg
      241 angviiiktk tgrsgkpqir lsyykgltqr pelqktllga terrtkldil nqyanhnqlg
      301 gltqpltdsl nssfnnatdw qslfyqsgni dnvdgsiagg seivnyrlsl gyyneegivr
      361 qtgfkryslr gnfgfklapf lrsdltfsts rmdrkrglgr ginqvvpidq gsmpssfvql
      421 sdldyafymg qydkllddnk tdilnifskt yvdivpglqy sfeaslqanf dsrdqfqpre
      481 lnqgvnfasa nknnafvynl anvlnyskvl nndhtftltg iqsfqyddyr ssyiygenlp
      541 tddihvvqgv aqknlaansn irksglvsfm gqfaydyksk yifnaswrad assrfgkntk
      601 wgyfpsgsla wvaseeeflk dvswlnflkf rgswglsgsl pqdfyapfnv wdlntstydg
      661 gsvatpsfqk pltlpnltwn kseqvnlgfd lrlfndrltv tmdayrkitk dpilsfpfqf
      721 ytgytklsyn vpmtiynegf dvtiatrnma stspvqwntn lnltfnknti gslpfgdkgf
      781 yadsygynqs lfyrvgspiy qwaqmlyqgv ynqadqipvn pitgklltyf knnypvkpgy
      841 phwadvngdy dvwsdsdkga adgdlvptgn pnprltggly neinyknftv gilgtftigr
      901 diintlksnq yngfggnvfn ftnrrlpdld gvdywtpeka qdpnyeanfp sispyqgyfy
      961 qffpfstmwn engsyfkvkt itlgyllpqd miksfrigls nvrfyamldn mltiqkarvp
     1021 daelvtpqge ysggayplpk kytlgveinf
//
LOCUS       WP_094281313            1163 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094281313
VERSION     WP_094281313.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1163
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127076
     Region          49..128
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cl21470"
                     /db_xref="CDD:473874"
     Region          179..1162
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtqilyrslf iactfmlfch qgrastnern hklelktklp sanidsldii gkitdstgta
       61 vegvviteqg ttnsvlsnen geykiaanpn gvlvflksgf atqeihvnnq kqldvkilva
      121 tpeseaeetd sanvdssqvd stitetdssm vqvdssqnav atdstaqeat gtapsgqnti
      181 tgtvtgpsgp lpgitvkvvg snatastden gkfqiaadak nkirfssigy ktitqtvgnr
      241 kdiqvvmate tntiesvqvv avgygtmkra tlptavssig aneiedevlp svtqaiqgka
      301 ggvqvtqksg spgggisirv rgttsinass dplyvvdgip vnsttnftgg stfdfgggtq
      361 ginvlssinp sdvqsievlk daasssiygs raangvvlit tkkglagqsq fnfnmyegfs
      421 qvpkeryydf mntaqyqdym kdyyrilqee dpsktipdqi fsnpgintdw qeaifrtspt
      481 rnyelsasgg sdktqyytsv gymkqggvll ssdfdrlsgr lnlnhqhsdk lrfstsmnlt
      541 ratnhrvqee nskegstksg ifsppnipvy ddngnyyydq vrltrenpva mlelptnkaq
      601 tyrilanasa eyniipelll ktsfgtdlsf idetffmppt glrsytsqgg igasrstrdq
      661 lwinettltf dktfgdhyin alggfsvqgs rlefthaqrs gfpnndipyv tgggvitgan
      721 aypeewaias gfarasyvyk dryiinanvr mdgssrfgad nrwavfpsma aawriseeef
      781 lkdnatfsdl klraswgitg nqnignyasr slyssgnnym gqagfipnvl gdkglkwett
      841 rqwnvgvdag ffndrislla dyyykktsdl liglpiltss gfinrftnsg dienkgfefe
      901 lssknlvgef kwntslnmtf nrnkvlalpe glsemrggvg dlnraipgmp lgvfygwkal
      961 gvnpetgmid ylgrngeavt ptdyedhvmi gdpnpqffgg itnnfeyknf dlsilgqfsy
     1021 gndifnynla sglegfnpss nqfidfvdrw repgditdvp rpapgsldng avssrfvedg
     1081 sffrirnitl gyslptevae rikmkrlrfy vtvqnayvft kyrgydpevs sshggantgl
     1141 iygydygsyp qprifttgin ltf
//
LOCUS       WP_094281818             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_094281818
VERSION     WP_094281818.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53559
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaelta apskpvtvea knetfapqhp dqylswkgts
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_094282022             982 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094282022
VERSION     WP_094282022.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 982)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 982)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 982)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..982
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111839
     Region          40..980
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnkiklsyl iiffllgasl pgmsstysly rfafqqelid ttelsekevs dfnrqrsivg
       61 vsdsinviel kkapftslad ivkgnlsgvn vqqpsgepgs yqnlvfrgik nkmfsnvdln
      121 anrmavfvng ipitqdhsfa yeiqkydinr igpgtdllnt idirsiesie likdplklae
      181 igplaangai witttggksg freisidayt ginsiqsitp inaqyenlfr qpfyslygnt
      241 dlrqkypgyl adstnlnyyg psnwkdgyyk vallhnvnmg lrggtdranf gfygaytgda
      301 nssdetglqr ynalfninml pfkwfkisan inairterdr nknirdryae maylpdlstp
      361 ispsnnlysq fanhydaavd dnvtntvrgg ldlqfdilkd lqfnsnfsid ysegirdvfy
      421 pselmetinf vsnyfgysqr yifsnellyk kqvnedhlfs akggikyqdd lyrynyaray
      481 dgpndfikin vvsgdsqred ylkpiggiqv yrinnreiyr mfsvfgkfgy qykdfvnidg
      541 lirwdassna qpnsrwlftp slranwnvkn qlelenqfsv rasfakigip ewnsryamgp
      601 qysvqmgwkn epslvsyfgq agfsrpyqtg wigynldway tnqadltlen gflndriqtn
      661 lslyyqenkn qlmlvpvpqe ygyqgiykng mdvrntgvdi svsaqvmpke sdfqwrpsin
      721 lnfnknelta lpgglkelev gdrllrvgea vdkfwllnne giydnnsqip tgengkklny
      781 qgvelqagdp kwkdlngdnv inksdrslmg nsspklyggf tnnfkyknfd ltvqayfalg
      841 qkalnqrasn rydfintess rdinavkeif hwqqdvdisk yplynvwssv vpyrlnqdlf
      901 ledasflkir tvslgydfsn teflknnvkt lrraylyvmg nnlltvtkfs gsdpelinfn
      961 giydgsglal aptytlglkl df
//
LOCUS       WP_094282040            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_094282040
VERSION     WP_094282040.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120253
     Region          50..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvfsdfhr gstrtystli lllglgfsps lansypteva kkvwanqqki sisgviydeg
       61 tntrlsgvti lsegkviass nangefsiqv eagkpvifqs lgyhsktqqw tsdsqsvrin
      121 lttsdesiee vivtalgikr eekslgyavs qvtgkqmtda tpsnwvdamk gkvaglsitq
      181 assgplntar inlrgdrsld pknnealivv dgipmvngrf ssgvtdayga gssgpdkdip
      241 idfgnglgdi npddiesisv lkgaaataly gsragngali ittksgnknk kgigisinsn
      301 ssfqsilkwp dfqyeygqgn ldrnadgeqy ysygltedgk ntgstssayg pkfngqeyfq
      361 ydpntetggt trtpwvaykg gvkdffnvge tymnsisldg gnevfssras lthtknswim
      421 pntgfqrlva ainssaklse klrinmkvny tnkssdnlpg tgynnqsiay fmifqnpsis
      481 ldwyrpmwkk drenieqihp fssyienpfi iayemtnslq shgidgmlqg qytfnpkwei
      541 mlrsgismrs dqrqqrrpwd tanfplgyyk qqdlfymesn tdallsfndk inedfsiras
      601 lggnlmrrdl keniglargl tspgvyklsn astspfadnt itqkeiqsif gmvnlgwrem
      661 ifvdltarnd wsstlpsnnr syfypsvsss fvlsemlemp ssisfaklrf swaqvgndad
      721 pyqtikyfns sifpgsaeap sllhnanlkp eisnsteagl nisffnnrlt advnyyfnrs
      781 rnqilrvprd vttgfsseii nggliqnrgw elslsgtpvr nenfqwnvsa nwaknnnkil
      841 elsegvetpq qiiassgsgv aeiiatvggs tgdlwgyglv rndqgqviyd aktglpvrpe
      901 dkvkignaya dwrggfhnef ryknlslsal idgqyggivy sqthhkmteq gklehtlrgr
      961 etgklvgegv iqnedgsfsp ntkevainty yadyyrranv etnsfdasyl klrevrfeya
     1021 lpktwvsrwk mnsasvaffg rdlfmisnfp mydpetaaln gatimpgvem gqmpstrtfg
     1081 mnlkvnf
//
LOCUS       WP_094282175            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094282175
VERSION     WP_094282175.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114896
     Region          24..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrllsvil lcmlfigian aqqrqvsgkv tsasegspla gvsvrvdgtn tatqtdgngd
       61 ysiavskena vlvfsyigys sqrvnlgnqg tvniqltstd neleevivta lgvkrekrel
      121 gysaeqvdsk tinkasavni anglqgkvsg lnvttnnsgv fedvkinlrg irsltgnnnp
      181 llvldgiqmd ikylssinpn dvenisvlkg aaaaaiygpd arngvflvtt ksgnevtsvn
      241 lshstqwqni sffpklqkqf gqgadgeiip ienwswgpay dgsianigpe ledgtqqttp
      301 yvgtderqkf ydtgitnqtn lslnaknffl slenadikgi vpgdknrrng irlnskrefg
      361 ifraaanfny tqqnynvynq agqenyytaq ntggndglfs qlintpahip ltkykdyknd
      421 ifstydhwft dyginpyfsl gnwrrhgkkq dlltnielgl kptdwldfty rasltsrgia
      481 eryitegvke tpfgasrgkt aitsaleeyn ynqnvltsdl fasvntpine dlifkgilgt
      541 avrqneyrnt svgadnlvip elynigirtg iltgasngyk trlfsvygsa gfnyknwanl
      601 eftgrwdkts tlapgnnsyf ypgvngaivl tdaldmstdf fnylkvraaw tntansdisp
      661 yfleatysqa ngfplggitg ltannttyny nlkperintt eagfeagfwn nrltleatyf
      721 yskntdqiis vntseasgfa rtntnaasfd skgvdfdfnl splinfeggs vnfrgnflwn
      781 dskvtsvyea qglkqeelsi ggytiagnya ivgqpafvmr gtdyerddqg riivsaadgr
      841 pttastnvnf grtlpkwivg lnpsvnykgf nlsalfeykg ghvvsffglg admawtgvse
      901 ataynnrepf ilpnsviedp nnpgsyipnt eakigeneai ynyytgefqn tasnfivsan
      961 hwrlrevals yqvpetwlks rqkaikglsi alvgrnlalw lpkenvfmdp dfnnmidayp
     1021 naygnvnsts nppvrnfgft lnatf
//
LOCUS       WP_094282354            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094282354
VERSION     WP_094282354.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120751
     Region          28..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklinkifqm lclmflvsfa aaqqndekii sgivqdsekr episfvvikk gsvqtstdtr
       61 glfsisarlg dtitfsrmgy hnekivisrn iqnqyviilh pqvnqiedvv ihsgyqtirq
      121 knltgsvsvi sqkdlersps rnlldrmrdm vpglvfnkht slkeqnksis irgqstlfan
      181 aeplivvdnf pyegdieqin padvesisil kdaaaaaiwg aragngvivi ttkkgtrdgk
      241 sivdfsvnns wtnapdlnyq pqmsskdyll iekmlfekgf yksaessinh apispgvell
      301 iahrdgkiss eklqqelsil egqdiyadls rlvyrpswnq qyhgslrtgt qltstlismg
      361 ydrqdenlik nnndrltlsl nqnisllkdr lqlkpyisfs atsrsspnqi lsemkfgssn
      421 iypyarlles dgspssiikn yrdaftsnaq ekglldwkyr pldeinsvdd lrrsqqirlg
      481 iqtnfqldkh lsfelsyryk kdnikgqthy gensyfarnl inqyssikdg kienpipkgg
      541 imdrsyeegr lhngrlqiky drnwslsefk vlagtevsds hflrtqnrly gydgehensl
      601 pvnyvvsypv qsnpnsyqki pyqnfgrdlt drylsyyttl nyqysdryif ngsmrwdrsn
      661 lfgvqsnqkg vplfsvsagw qlhnekfmqs llgiipllkv risygltgnv dnslsaftts
      721 rlnpstsfss glryayivnp anpelrwerv kvtnlgldlg llknkllfnl dlyhkegtdl
      781 ignapftgss gvtkfygntg strtsgvdls vtgdfrlapv elrsfflfsy vrdkvtsykv
      841 kptilnllsg gyagvhpieg kpltgmyalp wrgldpkdgr pigylngeet kdypaivqts
      901 tqedlvflgt srpkysgsfr qeigfknlnl slgiayrlgy wfrrssvhyn tilggigghg
      961 dfarrwqkpg dekttqvpsl peavnynevs fyqyaqvlme pgdhirfqdi slqynwkpss
     1021 vfhqvvfnly vdnvgmiwkk ttsnldpdyt laqpprtysf gvklnf
//
LOCUS       WP_094282395             983 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_094282395
VERSION     WP_094282395.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..983
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109817
     Region          30..978
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnltskttar sfllllfgvf wtisafsqqr tisgkvrtad nvplsnvsvl lkgtnigsqt
       61 nndgqfqitv pndgilifss igyltqetei kgknyinvil etddkaidev vvmgysqvek
      121 qhvassvasm dmestktrpi fkmqeafsgt ipgvtmlqgs nipgavpgti sirgistlqn
      181 adalvivdgm eqsitdldpn qiksitvlkd aastsmygsr gangviivet ergytgkfkv
      241 dlnawgaysn pidlpnwvda aqymklnnet rthqnqtllf sdedirkaet getpsvnwld
      301 eimtrkpfan nttasisggg gvgtfnlmlg higekglndi egtekfsarf ntniniadkf
      361 vlladfyahr lqvdrlmand nghglyqiaw rmnptqqify dntdipdhyi lhnnmnplas
      421 iakggtknyl ydrstinlrp ryninknlni egnvsymink sankeqrstf kffdgdgapv
      481 tiwknsvtae qgvsssqlta ralanytkdl rsnkdklylt lgtemmsyty tdyreenkas
      541 ffgklnysfd nrylieltgr sdgsskfapg nkwgffpsaa lawnlhnesf fssiresgai
      601 tnlkvrasyg lignenvdpy lwqeivnnwg wtirvpnpdf swekqkqwni gvdvtalknr
      661 lsltaevydk fsydliynnf pvppltgsnn lesavnigev qnkgwelsak wsdkignvsy
      721 nvgamlfdnv nkvlkagysk ndtlifkgds dkiwyngssi dnyygfesng yfqnadeven
      781 tsaklpntlp gdikykdqna dgiindqdri ylgdpfphmn ysinlglnyk kwdfsvmgqg
      841 vgkrngrlvg megypvyvdg gsnslgtprq eyadnrwtes npnarfpriw sgnssnayls
      901 dvwlsdasyf rikmiqlgyt fpgigksikn irlyvnaqda ftftkwegle pergldkskt
      961 enqgngvypr matysfgira tiy
//
LOCUS       WP_094282427             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094282427
VERSION     WP_094282427.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108384
     Region          27..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktllkkyl ltlivlmvsl atfaqeknis gtvtdeagsp lggatlrvkg ttvatstdnn
       61 gafsftvpnd aktlevsyig fqskdvditg teiniqlqss tdqgldevvv igygtarkkd
      121 ltgslvtiqa knfnkglvta pdqliqgktp gvmvinntgq pggaatvrir gnssirssnn
      181 plfvldgvpm sgnsplpegr ggfssdrgnp ltylnpsdia smdilkdasa taiygsrgan
      241 gvviistkkg vagspvvsvg atagvsnire ypnildagrf realnyytps eastsdyggn
      301 enafkaitqq avtqnyyadv sggtehgkyr lsggylnqng iikgsqlkky tgnftgnfnf
      361 leskrlgldl slfltqldnr yapinvfaga egnlisqamq wnptlplidk dgkntfvstm
      421 trnpltslda fkdrattntm vanvspyyki tddleyrfiy simrqtggre gmyrsglidp
      481 saskneqafi snnnetnmqm thtlsynkqv nedwninall gyeylnynfk nnlsfgggfn
      541 ymgldyfdyl qyssistrdi lsyrsptnel qsmflrggfn yrnrylftat vrrdgstkfg
      601 snnkyaifps vaaawninee dfmkdneifd qlkirlgwgk tgnqefpsga slnrfvfgnq
      661 sisqvnygnd dlkwetsati nagidfsifd nrlygsidyf nkkttdalfe qtlaqpapsg
      721 riwvnldgei vnkgveialt gnivrgtdwn wdltgnltll knsvsglvgy yetgalrgqg
      781 ftgvlgqrmv ngqplnvwyl aqyegidpqt gmsmylgqdg sinstndpai nkfysnspnp
      841 ttlvglstnv sykkftfsan mngafghylf nntaatvlgl snlssrnigs qffdtsvkes
      901 tsnsaapstr flekgdylkm anltlsynvg nigntfknfn isltgqnlfi itkysgfdpe
      961 vntdgasngi pslgieylpy ppsrnillgv nfsl
//
LOCUS       WP_094282617            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium cellulitidis].
ACCESSION   WP_094282617
VERSION     WP_094282617.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium cellulitidis
  ORGANISM  Sphingobacterium cellulitidis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Sphingobacterium cellulitidis"
                     /db_xref="taxon:1768011"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117163
     Region          27..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrtiyfylv glfialsigq vqaqhiikgk vidaqnqaie gatitekatq kqtqsnslge
       61 fsldastanp qltvrflgfq ektitvsssg fvqiqlspse dvleevvvta lgisrekkal
      121 gyavqevkst elqtrptnam aalsgkvagl qvvsaggnmg gstrtllrgi nsiagnnqpl
      181 yvvdgtpidn sdlnssstin gsagkdvgnm iqdlnpddie nisvlkgpsa aalygsrasn
      241 gvilittkra gkgeqvsidv nsglefeniv rlpkrqqlyg qgyspvfqtv qiegkeykiv
      301 dyaadeswgp kldgtavlqw ynlnpedaad ylnpspwlyp ehdvhyffnt glantnnvai
      361 sgnsgntnyr fsytnknvkg tvpnaslgrn tlnfsggtkl grlsinssin yihntslgkp
      421 wtgasnrnii leayqwgavq vdykrleqyk radgtplawn rtgwqntpaa eatrfidnpy
      481 wsayesylee krdrfygnig aqyevtdwlq igakvhgdiy qfgtqdriav ysrsasqyee
      541 tsnklneyny eflatakknw nnlslvanag anlrdqnrkv dyaitqggli vpnyynlkna
      601 stvkienyty nrriaslyas aslgyhdllf ldatvrndws stlpshansf iypsftgsfl
      661 fsqlpgfsaq dwlsfgkvrl gwaqvgndtd pyqlnkvydv eqsfdgkpsn klpstlnnad
      721 lkpeitsswe tglslqffrn rlgldityyh ntsrnqilpi pvsssfgyea kvlnagkven
      781 kgleiilngt pvrnenfewn sslnwsrnkn kvlkldelvn tltlssslin lvaregqpyg
      841 qllgydfvya dgqrvvkedg tylrtsqlvp lgsvlpdylf gfqnsfrykn lsfgflidgr
      901 vggsfysqty nvgmysgile rtaennvred glvldgvkad vvfnadgtyt tsnirendtr
      961 isaqqwgrne sngpttfsif dgtfvklrev tvgynfplnt pkvvkgvrls ayarnvwniy
     1021 tkskyidpef anssgnvqgi eggniptplt ygfnvnlkf
//
LOCUS       WP_094291849             535 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            kalamii].
ACCESSION   WP_094291849
VERSION     WP_094291849.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax kalamii
  ORGANISM  Acidovorax kalamii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Acidovorax kalamii"
                     /db_xref="taxon:2004485"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55536
     Region          11..535
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtspvpqpq rigipretfp gekrvatvpd vveklvklgf tvavesgage aanfsddayr
       61 aagaevvdga aalwagsdiv fkvrppssge valmregttl idfiwpaqnp dlmqqlaakk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rkmyaeqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti vgytdlasrl akqsstlyat nllrlteelc kakdgvavvn
      361 meddairglt vvkdgaitwp applkqapap apkaaaapve qkkgghghgs saplpaktla
      421 ilfavaavaf wfigayapaa flghftvfvl acfigymvvw nvtpalhtpl msvtnaissi
      481 iaigalvqia ppeagvngrp dglilwlafa gtvltainmf ggfavtrrml amfrk
//
LOCUS       WP_094295237             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium neumannii].
ACCESSION   WP_094295237
VERSION     WP_094295237.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium neumannii
  ORGANISM  Mycobacterium neumannii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Mycobacterium neumannii"
                     /db_xref="taxon:2048551"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38199
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mteqthadva agaaptvgvv reseaderrv alvpkavasl vksgvavvve sgagerallp
       61 ddlytaagat fgdawrtdvv vkvapptaee vakltsgqtl igflaprndd nqiaalkaag
      121 vqafaveaip risraqvmda lssqanvagy kavllaases trffpmltta agtvkpasvl
      181 vlgvgvaglq alatakrlga rttgydvrpe vadqvrsvga qwlelgieaa geggyarels
      241 deeraqqqke leqaitgfdv vittalvpgr paprlvtaaa vegmkpgsvv vdlagetggn
      301 celtepgqtv vrhgvtiasp lnlpatmpeh aselysknlt sllellisdg klmpdfddev
      361 vaascvtrge n
//
LOCUS       WP_094300489             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_094300489
VERSION     WP_094300489.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53595
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfeg knkavkfpwd egmkvenmek
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkatlqnvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedla rkngllsq
//
LOCUS       WP_094327627             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nostoc sp.
            'Peltigera membranacea cyanobiont' 213].
ACCESSION   WP_094327627
VERSION     WP_094327627.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. 'Peltigera membranacea cyanobiont' 213
  ORGANISM  Nostoc sp. 'Peltigera membranacea cyanobiont' 213
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc; Nostoc cyanobionts.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Nostoc sp. 'Peltigera membranacea cyanobiont'
                     213"
                     /db_xref="taxon:2014530"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41484
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dtvarlvkqg levwvetgag ersffsdtdy eaagatiisd
       61 taklwgetdi llkvsppqer edgrsevdll kegavlvsfl nplgnpivaq qlanrkital
      121 smemiprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkldeetvaa ggyakeisea
      241 skqrtqevva ehvknsdvvi ttaqvpgrqa prlvteemva qmkpgsvivd laadqggnca
      301 ctepgkdivw ngvtiigpin lpssmpihas qlyaknvtsl mqllikdkvl qvdfsddivd
      361 aacvthagei rnqrvrdalq alstqqsavn
//
LOCUS       WP_094304673             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Enterobacteriaceae].
ACCESSION   WP_094304673
VERSION     WP_094304673.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53558
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg nnkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_094338668             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Shigella
            sonnei].
ACCESSION   WP_094338668
VERSION     WP_094338668.1
KEYWORDS    RefSeq.
SOURCE      Shigella sonnei
  ORGANISM  Shigella sonnei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Shigella sonnei"
                     /db_xref="taxon:624"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53524
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpvdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_094341764             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nostoc sp.
            'Peltigera membranacea cyanobiont' 232].
ACCESSION   WP_094341764
VERSION     WP_094341764.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. 'Peltigera membranacea cyanobiont' 232
  ORGANISM  Nostoc sp. 'Peltigera membranacea cyanobiont' 232
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc; Nostoc cyanobionts.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Nostoc sp. 'Peltigera membranacea cyanobiont'
                     232"
                     /db_xref="taxon:2014531"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41549
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dtvarlvkqg levwvetgag ersffsdpdy eaagatiird
       61 taklwgetdi llkvsppqer edgrsevdll kegavlvsfl nplgnpivaq qlanrkital
      121 smemiprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkldeetvaa ggyakeisea
      241 skqrtqevva ehvknsdvvi ttaqvpgrqa prlvteemva qmkpgsvivd laadqggnca
      301 ctepgkdivw ngvtiigpin lpssmpihas qlyaknvtsl mqllikdkvl qvdfsddivd
      361 aacvthagei rnqrvrdalq alstqqsavn
//
LOCUS       WP_094355954             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Enemella
            evansiae].
ACCESSION   WP_094355954
VERSION     WP_094355954.1
KEYWORDS    RefSeq.
SOURCE      Enemella evansiae
  ORGANISM  Enemella evansiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Enemella.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Enemella evansiae"
                     /db_xref="taxon:2016499"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53051
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpaelr pgetmvaatp ktvgqlialg hqvvfeagag raarlpdeqy aaagaelada
       61 devwrsdlvl kvraplpeel pqlregqlla clldparspe llaeladrge talsldavpr
      121 israqaldvl ssmaniagyr avieaansyg sllngqvtaa gkvpparvfv vgagvaglaa
      181 igtasslgaq vyafdvrpev aeqvesmgae fthlpgaqda eassdgyake ltadqeqrta
      241 elyadqsaaa divittalip grpaptlita amvaamkpgs vivdlaapng gnceltvrdq
      301 vvvsdngvii igytdlagrl ptqasqlfgt nlvnlvkllt pakdgqlvld lddpvqrsml
      361 vadrgevtwp pppvtvsakp apvpaakpah evepvrrgrg parvalgtlg vllavglaft
      421 psvfllyfti falavvvgyy visnvthalh tplmtetnai sgiiligall qigsdnlvvr
      481 ilafialtva sinifggflv anrmlamfsk d
//
LOCUS       WP_094358165             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium marinum].
ACCESSION   WP_094358165
VERSION     WP_094358165.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37158
     Region          7..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdpqttvgv vaestpderr valvpkavgs lvnsgvavvv esgagerall pddlyteaga
       61 tigdawaadv vvkvappsad evgklrsgqt ligflaprna dnsigalkqa gvqafaleai
      121 prisraqvmd alssqanvag ykavllaase strffpmltt aagtvkpatv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwlnigida ageggyarel tdeeraqqqk
      241 aletaisgfd vvittalvpg rpaprlvtaa aveamkpgsv vvdlagetgg nceltepgrv
      301 vvkrdvtias plnlpatmpe haselyskni talldllltd gklapdfdde viadscvtrg
      361 dd
//
LOCUS       WP_094365155             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Enemella
            dayhoffiae].
ACCESSION   WP_094365155
VERSION     WP_094365155.1
KEYWORDS    RefSeq.
SOURCE      Enemella dayhoffiae
  ORGANISM  Enemella dayhoffiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Enemella.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Enemella dayhoffiae"
                     /db_xref="taxon:2016507"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53398
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkelr pgetmvaatp ktvtqlvglg fevvvesgag alahlpdpay aaagafvgda
       61 aevwasdlvl kcyaplpeel drmrpglvla cmlaparspe lldalavrgv talaldavpr
      121 israqsldvl ssmaniagyr avveaaynfg sllngqvtaa gkvppanvfv vgagvaglaa
      181 igtansmgav vrafdvrpev aeqvesmgae fvhlpdaqda eassdgyare msddqerlvm
      241 rlyaeqsaga divittalip grpaprlita emvrsmrpgs vivdmaaang gnceltradq
      301 vvmsdngvii lghtdlagrl ptqasqlfgt nlvnlvklla pgkdgqlvld tddvvqrsml
      361 vtdagavtwp pppvqvsaap vpaaasatrs eaattqtaev avrgraartv slgvaaaala
      421 vglaftpqvf llhftvfala vvvgyyvisn vthalhtplm tetnaisgii lvgallqigs
      481 dnlavrilsf iavvvasini fggflvanrm ltmfrkd
//
LOCUS       WP_094350874             388 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Nostoc].
ACCESSION   WP_094350874
VERSION     WP_094350874.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nostoc
  ORGANISM  unclassified Nostoc
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="unclassified Nostoc"
                     /db_xref="taxon:2593658"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41006
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dtvarlvkqg levwveagag ersffsdpdy eaagatiisd
       61 taklwgetdi llkvsppqer edgrsevdll kegavlvsfl nplgnpvvaq qlanrkvtal
      121 smemiprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkldeetvaa ggyakeisea
      241 skqrtqevva ehvknsdvvi ttaqvpgrqa prlvteemva qmkpgsvivd laadqggnca
      301 ctepgkdivw ngvtiigpin lpssmpihas qlyaknvtsl mqllikdkal qvdfsddivd
      361 aacvthagei rnqrvrdalq alsgvgag
//
LOCUS       WP_094379660             956 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-92].
ACCESSION   WP_094379660
VERSION     WP_094379660.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-92
  ORGANISM  Prevotella sp. P5-92
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 956)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 956)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 956)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..956
                     /organism="Prevotella sp. P5-92"
                     /db_xref="taxon:2024222"
     Protein         1..956
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105622
     Region          50..955
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktknifmlt llagvalpam aqrdiadsva ykdqtvdiga nrlftreqst aavsvitnkd
       61 vnkrgarnig nnilgqgsgl vsldgsglfh aqnptfyirg lqtssgstpl ilvdgverai
      121 envvaedves vqilkdaaat aiygykgang vilvttkhgq yntksftfsy dhvfsfltnk
      181 pvmadaatya savneayrnq ggnaaysdav inaykngtnp lyypnvnwad etfrnvsnnd
      241 rlnlefkggt knfryftnvq lltnkgfvkn yendgystqn kytrgtlrsn mdidlspktk
      301 lhthlfgllt eqsqpgdqad lwsmiykvpa nafpvkvnda vwggnsvftt snpvaqsqga
      361 ayyknhqral yadlvleqdl saiteglsaq gqlgydtwsn vyenhsktyr ysnyqvtnng
      421 dviadgnatl asvegsdsnm gtasgndawi rrcifngsln ynrtfaekhd vygqlkydye
      481 fsdktgtntt vyrhnislfa hygydrryll dvalvesgss rlapgskwaf spnvsaawni
      541 sneafmndvt wvdflklras wgnkaldvlp gddvwtyynq fylmnantyp fdatytgtqw
      601 gntylstamt qslgheqasr fnvgidatlf gglnlsldyy yqhryniwys tagsytgvfg
      661 ltapyenvgv idskgfdisa dytkeinkdl tvslgasltl nksivkeqae apqlfantss
      721 tgerygqafg yvangffqks ddvngdgiis aaemqqkgyp vqsfttvypg dvkyvdltnd
      781 giidandrka igysttapdl yynfhlgaey kgfgldamfq gvgkwtgfmn tnglyrsava
      841 tntlsqylyd nswsaergnt enpafprlst tsnanndvns tlnmfdrsyl klryvelyyh
      901 lpkcvlekls vinnvklyvr gtdlftidnl eeadaaaygt tqpltrslql gaavtf
//
LOCUS       WP_094380705             965 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-92].
ACCESSION   WP_094380705
VERSION     WP_094380705.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-92
  ORGANISM  Prevotella sp. P5-92
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 965)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 965)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 965)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Prevotella sp. P5-92"
                     /db_xref="taxon:2024222"
     Protein         1..965
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107511
     Region          45..145
                     /region_name="Plug"
                     /note="TonB-dependent Receptor Plug Domain; pfam07715"
                     /db_xref="CDD:462243"
     Region          100..964
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkriktnifl lamvaaspla vnaqtsngds vqakkkvhva frdkdadqll ggvayvdmee
       61 lqkkdytmss ledlyalvgg wngsslwgmd tdqldtndns nlpvviidgv krpsnnvlps
      121 eieqvtflkg aqavalygpk aakgailitt krgkvdglqv einantgfhv akafpeyigs
      181 aeymtlynea randgldpry sqqdiynhaa glnpyrypnv nyysdeyvrk aynrseatae
      241 iqggsqrahf ytninyyrse dllnfgkate nytdrfsvrg nvdltlnkli kcfanasatf
      301 ynnhvnkgdf wgeaanmrpn fpenaaplip idmvdpyasn alailgksln lldgkyfpgg
      361 tktnqtnaia dcyfggkttg vsrqfqfdag liydlnkfvn glsfktqfai dyaasynlsy
      421 dnkyavfipt wsnyntndii vgltqqndei vsghmvmsns kyrqtiswng hfdydhtfgg
      481 khhvtgmllg nmytttssgt yhrytnfnvg llggydfmnr yfaevalvgv hssrlaegnr
      541 naispsftlg wniakesfmk dsfvddlmls asysdlnedi dvymgdqnyq yyylydaqwk
      601 tgggnfswne gnhsdityst igsnpaldfi hrkefsvslr gsffnklisa dltffnsdmd
      661 gfiiknpsmf pshlsgging stfkpainnn iqnrkgidfs vtaqkqlgkv hatlgvvgsy
      721 vktnykkfde ivefdnlrve ghaldairgy nclgfytydd fnkneetgkl tlkselptpk
      781 iggtiqpgdl kyedvngdgv ldtndrvdlg twssplhlgi nltlkykdft lfmlgngqfg
      841 getvnngpyy ymsgeskysv nargrwtpet advathprlt tlasannaaa stfwlistdr
      901 fnlrkvqlty dfpkeilnsk yvkalsiyls gsdlltiskh rkifetnvgh apqtrfynlg
      961 vkvtl
//
LOCUS       WP_094380794            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-92].
ACCESSION   WP_094380794
VERSION     WP_094380794.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-92
  ORGANISM  Prevotella sp. P5-92
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Prevotella sp. P5-92"
                     /db_xref="taxon:2024222"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115656
     Region          42..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkqvlicl llagmawtpa malaaadaak gtsivaapdn nvvkgtvtda dgpligatvk
       61 vagttsgtvt dfdgnfsiqc kpgatleisy vgyktisvka qngmkvmmea dgkvlsevvv
      121 talgvkrdrk algygleevk gedltkaket nvinslsgkv aglvvqntag gasgstrvll
      181 rgntemagnn qplyvvdgvp ldntnfgsag egggydlgdg isainpddie tmtvlkgpaa
      241 salygsrash gvilittkka ekdkisveyn gsftidsqla kwddiqqvyg mgyggklpts
      301 stsgtnsswg pkaddfvyky fdgeehafmm hpnnasnffr tgfttqnsai lsvnsgktgm
      361 rfsltdmrnk dilpntnmsr dnfnlrvnts agpvdfdfta nytredvknr palgdsqsnv
      421 gknlmtlagt ydqawlknyq dadgnyqnwn gndqynknpy wdlyknsnts kkdvfrftgk
      481 aiwnidehlk iqgtvgtdin nmtfqdyiak ttpgtpagkl tdqifnnrtl naeilalynn
      541 swgdfdvnat aggnifkvnn ktitniglnq qmdgivnimn yqeqnvresm yqkqinslya
      601 sasvgykhty ylegtvrgdk sstlpidnnt yvypsisgsl vfsefiknkn iinygkvras
      661 wakvgsdtdp yqlalnyatg kysysgytig misnatqpnk dlkptmtssy elglemkffh
      721 nrlsldltyy nqtskdqils lastttsgya yrlinagqiq nkgieialng rvlqikdfaw
      781 dagvnfsknt nkvkslvdgm dyfelakayw cgvsvgakvg enygairgkd fqrtddgqii
      841 idatsglplv dkevktigns swdwtggfys tftyknfrls agfdvkvgad iysmsmrsay
      901 qtgkasqtle grdewyasee areaagmtde qwrasgnckg fiapgviang dgtyrpndip
      961 vnpetywkai annvqsafvy dnsyvkcrei tfgynfpekm lgkwakalsv sfvarnpfiv
     1021 wknipnidpd ssyntsglgl eygslpsrks yginvnvkf
//
LOCUS       WP_094380827            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-92].
ACCESSION   WP_094380827
VERSION     WP_094380827.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-92
  ORGANISM  Prevotella sp. P5-92
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Prevotella sp. P5-92"
                     /db_xref="taxon:2024222"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123327
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrigtlls vlclfvtmav aqtkvsgkvf sqddgepvig asvmvegtkt gsitdidgqf
       61 tievpngkkl visyigmvtq tvkahngmtv ilapdaqtln dvvvtgmqkm dkrlftgatt
      121 kvtgekvkld gvadvsrale gkaagvsvqn vsgtfgtapr irvrgatsiy gsskplwvvd
      181 gvimedvtev dadalssgda atlissaiag lnaddiesfq ilkdgsatsi ygaramagvi
      241 vvttkkghsg snkisytgef tmrlkpsynn fnimnsqeqm gvyremekgg iinfastyra
      301 sdsgvygkmy hlinsydets gkfglantea arnaylreae yrntdwfdll fsnaisqnhs
      361 ismasgtdka qyytsfsimd dpgwyrqssv qrytgninal yniskkvtfn vignaayrkq
      421 rapgtlgqsl dpvsgevrrd fdinpysyal ntsrtldpne yyvrnyspfn ifhelnnnfm
      481 nfnvvdtklq gelkykpitk veisvlgayk fstttqehei hdyanqaway ramddatvrn
      541 anpwlytdpd kvnslpvsvl pvggfyretk yrmnswdfra tanyndvynd dhivnffggm
      601 evnnlerrrt ffhgvgiqyd mgmlpsydyq yfkqgqeegt qyfsvvdsyt rsaaffgtan
      661 yswkgrysvn gtvryegtnk lgrsrsarwl ptwnvsgawn mheepwfetl rpalsnftlr
      721 asysltadrg pssitnskvv itsynpwrps tgdsetglgi ndvenselty ekkhefniga
      781 nmgfldnrin veidwyrrnn ydligaittt gvggrvtkya nvasmrshgi elslstkniv
      841 tkdfkwntdf ifsktkntvt dfdsnvrvid mvtgtgftme gypvrslfsf dfqglnedgl
      901 ptfvnengqv ttsdiyfqey nekshlvyeg sidptitgsf gnvftyknfk lnvfmtyafg
      961 nvirldpvfk ssysdltamp kefknrwtvq gdeaitnvpv iadarllnnd nylsyaynay
     1021 nystervakg dfirmkeisl sydfpakliq plkltnlslk lqatnlfliy sdkklngqdp
     1081 effnsggvas pmpkqftltv rlgl
//
LOCUS       WP_094381466            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-92].
ACCESSION   WP_094381466
VERSION     WP_094381466.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-92
  ORGANISM  Prevotella sp. P5-92
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Prevotella sp. P5-92"
                     /db_xref="taxon:2024222"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122731
     Region          <29..94
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
     Region          108..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqckhlliv ivmllaalpv maqvgnitls fndeslpsal rklekasdyk isfayndvek
       61 yrvsgqvkns sfkavldfll kgkplsyefr gkfvdikagk pgmrrlsrev tgmvkdenge
      121 plpgatvtcl ggsggresst vvtdmnghfk lsaagdatkl evsyigftnk tialtsassy
      181 eiqmqpdska ieevvvtgvf trkantftga vttikgddlk rvgnanvlqs lknidpsfmq
      241 venlgmgsdp nslpdfqmrg astisgvqge yassanqplf ildgfetelt kimdldmnqv
      301 esvttlkdat akaiygskaa ngvivietkk pesgrlrvty tgnvslevpd ltsydltnaa
      361 ekleverlag lyysdnamsq itleknysqk lrevisgvnt dwlaqpvrtg vgtkhslyie
      421 ggdkamqygv nlsynniega mkgsdrstfs ggitlsyrvk nfifrdklti dynssndspy
      481 gsfsqyyrmn pysrlydang nyirsydytd nkgasaqysn plynttlnti nnntytnitn
      541 dfymewqile slkmtgrfgi vrktttadif kpanhtdfin ttdefrrgsy sqsngkhtdi
      601 sadlglqwsk qidkhlvfln gqlsmsdnsy ntvgimaegf pndfmddisf avqyakdskp
      661 tgtegvsrnc ggllsvnysf derylfdany rlmgsseaga knrwgsfwsv gggwnvhnek
      721 fmkaakwvnr lklrasygyt gsqgfssyda lptfvyysnl syngyigsyi kglaneylrw
      781 qekydtnigv dfnlfnnrls grfdyyiatt kgmvtnvtvp yttgfttyvd nlgetenkgf
      841 eaylnykvfd agrnyvnvfg svahnkntlk kisnslrawn eakdkdmian ettspsvkyy
      901 egcsmsaiwa vpslgidpqn gkeifvkkdg tvtydydiad qvvcgdtqpk fngnfginge
      961 ingwgwnvtm nyrwggqiyn qtlvdkvena qlqynvdrrv ltdrwqrpgd malykaitdq
     1021 sityptsrfv qdyntftlss ltfyydfrnc rwvkdsfler lkvsaytndl fvissvkter
     1081 gtsypyarsf slsaqvtf
//
LOCUS       WP_094382471            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094382471
VERSION     WP_094382471.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124605
     Region          117..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkercrrta iilvglllit smvsaqtgkr fsvtfknekl atalktiskk sgvnvtfaye
       61 dvekynvtka lknvdaneav ktvldgkplt fnvhngritv fraelakmae nmyhaegvvv
      121 dtdgqplpgv svksgdgqti cltdvdgkfr imiskgqsaq lmfsyigmes qtvtlsskns
      181 gkimrivmqe esgklgevvv tgifrkakds ytgalttids eqlqtfkgsn llqtlknida
      241 sinfpvnnla gsnpnvlpnm nirgssslpm sveefnsnaq qtvntpliil dgfeisltkl
      301 mdyndeqies inilkdaaat aiygsrgang vivvvtktpk egklrvtaka gidlqvpdls
      361 sydllnaaek lqlekqvgly tdeyepinqw kynnlysrrl kavldgtdid wihkpvrtgv
      421 gqryniqldg ganefrwats lgyndiegam kgssrktvng ditlmysvkn lifrnytsft
      481 snkskeseyg sfqdyvdqqp ynnpydengn vvktfsnffg tdevgnplyd atlntfnkne
      541 yinfldnfsv ewmiidglrf rgkigyqttr stsdlflpae hstfasssyn ttegllrkgr
      601 ytygtgrtdl fsanatlsyn ktfakkhqiy agldwslsee nytnytfvae gftnedmsfl
      661 gnatqyehas aptgskdvtr lvgvtgnvny tydnryyvdl syridgsskf gsndrfapfw
      721 svglgwnmhn ekwlkaiepi ntlrlrgsyg itgsqditte sintsynyas gsrylgwtsa
      781 smmglgnpdl twqktnelni giefglfnnr itgefdyytk kttdllsamd lplsvgfasy
      841 vanigemsnh gfeasvnayi irdykrkfnw mvgaqivydk nkitrlsdai kaqndkyleq
      901 nvevsnlfye gyplnsiyav qslgidpstg keifldregn vtstwnaadk vflgssqply
      961 rgnfrtmvmw nnftlnvsfg yhwggkmyns tlrdrvevss griaktnvdk rvlsdrwmnp
     1021 gdntffrgft yndtratsry vfddrvltlq svslqyrwnn dwlqrnsgle silfamnind
     1081 lfywssvkye rgtnypyarn iqgsvtftf
//
LOCUS       WP_094382752            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094382752
VERSION     WP_094382752.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123793
     Region          124..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtrtstikkv llaalllvsp svmpvltaav nsvqqkegep lvsafrkiek ttgyrisyaq
       61 sdvknlkaqg ntsskdihka ldtvignlpl aysvegkfvt vfpkkqkdtn seatpkvttl
      121 nkltvrgkvy dqdgegipgv svkvpsmqta ivtgangsft lylpqgrttk lqfsfigmkd
      181 atyifngkhd innlvinmkd dattinevvv tgiysrkkes ftgssqtyna eelklvgnqn
      241 liqslktldp aftvlennef gsdpnrlpdl eirgktsivg lketfgedpn qplfildgfe
      301 ttlqsimdls mdriasvtvl kdaastaiyg akaangvvvv etkapemgkl kfsysgnfnv
      361 swadltdynl mnaaeklefe rlagnftsni adyqefqeir ynkllsnvlk gvdtywlsep
      421 lrtglnqrhf isaqggneql ryslgvsynk idgvmkksgr dilsgnidvl yrvgkltfsn
      481 kmtvnvtkht nptvsfseya sanpyypkye edgtigkwle ykensmsttd asvivgnpmy
      541 ndqlnsydrg esfgvrnnfs meyrpwnffw irarlgltke tnesenfvsp entaydqvdv
      601 lkkgsysnqr sdgfsydgdv tatygqllak khqinavlga siressdqsk gfsavgfpeg
      661 nfttpgfanq ytesgkptyy dsknrtanfy fnggysfdnr ylldvnyrld gssvfgtnrk
      721 fsntwavgla wnihnekfmk dtelfqmlki rgsignpgnq nfgsyntltt ykfnnwmtnn
      781 fgtgllidai gdpdlawqkt idmnvgldvs llnrlhlnid vfhkntdpll asigipasvg
      841 vtsrlanigk qvtdgfngti rysfiyrpke rmnwttslsf shvrshyeni gstlaqynne
      901 nltknmtryy dggspsalwa vrsagidpat gkeifitksg nytfshsydd evevgdtrpd
      961 vegvfgnvfy ykgfsasiym ryslggdtfl stlydkveni sssalaknqd rralydrwqk
     1021 pgdiakfkgi srtestpmss rfvsvnnylt iesirvsyel pytlmkkmgl qgmtfsaymn
     1081 diarwatvke ergtsypfsr sismalslnf
//
LOCUS       WP_094383002            1143 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094383002
VERSION     WP_094383002.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..1143
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125018
     Region          26..93
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          104..1139
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrekrifgml iallvclttm aqgismkfkn eslpsvfkkl eratsykfvf aysdvdsytv
       61 tgevtessiy evmsyllkdk pleysvkgki invskssrks sqgkkirgvv ldaetgepii
      121 gatvrviggn mgvttdnngq ffldcspkni kinvsyvgme sqslaaseym niklkgslki
      181 lndvvvvgyg ttkrkdltgs vavvkpeeli napavtidda lagkaagvqv tkadgspgga
      241 vrirvrggss ltggvdplyi idgiptqien nyisstdind pnewanygeq dmgavsgsfm
      301 rglnslagln indietitim kdasataiyg skaangvvii ttkrgrhdqk pvfsfnyslg
      361 isspvkekvl ngeqylsale ssiktananl qknidlgdls lasagrkits nnellekvks
      421 vgnantdwld evlrtgtthn idfavsggsq ssryytsfsy nqqtgtligs dfrrltgnis
      481 mdndisskfr tfvklnlsys knnmssgiyy qalsappilp iynadgsyad ysaiggvgsa
      541 ymgfqnpvav ssstnlakty gfkgsiagey dilkelkfkt tisvnynnyn qlnyipsyvl
      601 tssyygaedn gggmgtqaqs tstnvfwent ltynkqfsdf hslnavighs weqdkndyfs
      661 atgkgypddn flnnlssasi aasvsgsnpl skssllsfyg rfnytildry lftftgrsdt
      721 sskfakahrt gffpsgafaw rlseekwlrd vkwideiklr asigktgtqn isdwmfltly
      781 spdaygnnsa lypsqlgndd irwesttqkd lgldysffng rlsgtiayyh kntdgallai
      841 tpapssgfss visnianvrn tgfefeinad firnktwkws galnishnes kvlkildeqf
      901 ssatdrkaln lgtslirege slgllcgrvv egliqnetel aeykskfayw kyfqqdlgig
      961 svkfaldetg yyyedvignc tpdfyggytn tlsyknwsll acftfsvgnd liyqkdvndm
     1021 cfsslsnrgv rvleassvdn ftgkplstys stmfltnlnv ydasylklqt lslaytfnrs
     1081 qlkplglnnl qlyatasnlf titgypgpdp avsdnpytis gggrdissyp tvksftfgvr
     1141 lgf
//
LOCUS       WP_094383073            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094383073
VERSION     WP_094383073.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117877
     Region          24..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrikmlfa tlflcmgmav aqtqvtgtvi sdedgepvig atilvvgtnv gtvtdtngkf
       61 kiacpegksv lsisfvgmep ievsaranmr iilksdskdl deivvvaygt akkqsitgav
      121 ssidakdiek rittsvtgal egsapgvqvn ntygepgsep iirirgigsi ngsntplyvv
      181 dgviysgnis dlnpndiqsi svlkdaasaa lygnraaagv viittkagrs sansqislki
      241 nqgfygrgik eysrlgvtdw messwkamkn yamtgslald eaaaaqyate hlatdviqnn
      301 ifdkdatelf dnggklianv kpgysdldwe dniertgsrq eynldgnyts dklsvysslg
      361 ylkengyvvg sdyerytgri nssytpnkwi tsglninati skrhfndsat gsyysnpfyv
      421 arymapvypy ymhnadgsiq kdefgepvwd ttspyldnrn iayelrkdkd esrrnvidat
      481 afatinlpyd fsltvkgnma hrtnnrtsyn npeigdgatn ngrltaysye ysnytmqell
      541 nwghdyglhh vdallgheny kyeskatygm ntnmavddif vmsnfltnsy fqgydneyat
      601 esymararyn fdqkyffdas wrrdgssrfh kdnrwgnffs vgaswnakke nflkdvkwid
      661 qarlrasyge vgndagvsyy ayqalyyidk nggnpalmkq slaandikwe ttqtfdiale
      721 grlfdrlnfs igyfdkrskd llfavrlpls agsfayneyd ynmtiyknig tisnrgfeia
      781 ldydifkgkn fswnvgadat flknkiitlp ngdnilsglh nytegrslyd fytyhfegvd
      841 qltgnslytl dpekeesaaa agelveingk kyttdtaygl rdfhetalpt vygsfhtnlt
      901 wkglsanilf tyslggkvyd asyqslmstn amssgsalhe dvlnswngvp sgitetsanr
      961 idtngipals ydrssynnnn sdrwltnasy lvcknislsy slpkslvsgw ncgitgiain
     1021 agvenlftlt arrgmnpqfn ftggsddtyv tsrvfnfgvt fnf
//
LOCUS       WP_094383652             899 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094383652
VERSION     WP_094383652.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 899)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 899)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 899)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..899
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..899
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98914
     Region          50..897
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 makskkdftl llialfcssf ahaqkqvpae wkdsidngsn iikivgnnsn kgaannaldv
       61 lsgqaagvnv tsngldrmam lnsvrvrgtt siiggndplv lidgvtsdvl tlstiypadi
      121 esfrilknaa etamygsrga sgvievktkk gtgrgfqisy egnvgfeqmy khlemlnaae
      181 yvatakalgi ycnnggfntd nykvitrtgm vsnhylafsg gtpqsnyras fgvmdhntii
      241 kkmdynvfva kvdvtqkafn drltgefgvf gssfknydif dtqmlfysaa cqnptfpagt
      301 dehgnwlkne sathvnppgi lleekndskd lnfdahikls ydfnknwrvs tfgsylygst
      361 engqfcptwv waqgnvyrge fkkeewlgnv sldfnkefgi hkvsagvsse yrklrktafw
      421 vyakgiptnd fhydnlgata arpyggtest yedqslasvm gsitynlldr ytlavnargd
      481 gssmvgdnnt wgffpsvsft wdmkkesfla nikplsmlkl rtglgqagnl ggisayttmn
      541 tvrqtgivpv kssptvtlgm vrnnnpdlkw etkttfnlga diglfanrlm ltaeyyyskt
      601 tdmlyayevp vppfayntll anigsmsnrg felglsvqpi skkdldlnin mnlsfqsnkl
      661 islsgdykgm smsaanitai gsldgagqng gdnnvvyqiv gqplgvfylp hckglvknen
      721 gsyfydiedl dhngnvdlsd ggdryiagqa tpkvilgsni sfryknyyis iqmngafghk
      781 ifngtglayt smacfpdynv lkdapkkniv dqrvsdywle kgdylnfehl tigynvplrs
      841 klirslrvsc nisnigtitg ykgltpmins yvvnstmgid dkrnyplyrt ysmglsvqf
//
LOCUS       WP_094385289             938 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094385289
VERSION     WP_094385289.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..938
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105531
     Region          33..935
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqiykgial catlattasg afaqtdeald afadtldnkv qvafrsvdkq dllngvsaid
       61 mkemaaknys sysldyienv vggvnnglwg ygdylvvvdg mvrdannvlp teieqitllk
      121 gsaavvlygp raakgvlqit tkrgqmgdlr invhanggmn tpkafpkylg saeymslynq
      181 ackndglmtp nytddeiyhf asgenpyryp nfdmydsdyr raastryegi levtggsgrv
      241 kyyttmgyyr endilkvgkt kdnytsrffv rgnmdvkfnd wltakadanv tfydsyaakt
      301 dwwsqaatlr phlvaplipi syieetdkns lgtvmnsnyl qngyffggtq tnptnpyada
      361 faagdnkfvs rqfqfntefd vnlgklvegl mfrakygidy astynqgysn kyatyspswt
      421 nyngkdmigs itqfgkdekt gsenisnsay rytynvsgqf dwtrtfdkrh nvfamllana
      481 wqtqrsghyh rttnanlglq lsynydhtyy idfsaampys tklpegkrsa isptvtlgwr
      541 isndllkdtf vddlmltasg giinqdidit adenedgyyl wkavvqqggw yswgdleggs
      601 vtefqrgdnm dlgfvkrkef svglrgslwn klitfdanff tskmdgglar vsslypnyft
      661 qvgyptssii pfvnynvdkr vgidfsvyan kkfgevdltl gvsgtwvkst adkrdeniey
      721 dylsavgksl nglwgletlg ifqtkdqida aptqtfgevr pgdlqykdqn ndgkiddndr
      781 vflgrwdnpf vgginltakw rnftlfamgn lylggygmkd nsywwmrgdg kyseaardyw
      841 ttentdaayp rltttngdnn yrnsdfwmyk kdcfnlarvq ltyalpeslf kdsfirgvdv
      901 fvggsnllti akereilemk vgsapqmrsy nigfkasf
//
LOCUS       WP_094385499            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094385499
VERSION     WP_094385499.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120778
     Region          44..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkttltkaa aitcmalita lpakaaedtt gegmnspaat afylkgkvld dtgepltgav
       61 vkikgtdtgv ltdlngnfsi pvtkqgrytl nitfvgmtal etaatttkai vvkmeadskv
      121 ldevvvsgfq tisrerntgs avivnsekln kiqattlssk legmtpglti yngdmsirgt
      181 ssfavsgtpl lvidgqpatg isidninpei idqvtvlkda aatslygvra sngvivittk
      241 naakdkldin vsanyylkpl pslsykhyas tsdiidleee fllsdpdyqa nplayfntlt
      301 nksnatfmtq vdmiyyrlak geidqagaks aidalrnydy rkeyrdklqq maitqdysvs
      361 vskggdkynf fasgrlrsng mytkfndnnt aqlylkndlq vapwfkltlg adlsvlksky
      421 tqasylgyan ampydrlynd dgslayrypy nqvlatsfdn aqglqpmgyn aveesgnnia
      481 ktdntymkyf aqtdfkivkg lglelkfqye krmidqeeyd eadsymmrsl vneftstntd
      541 gtytynipqg grlysvsany syynlrgqfn ynttiaskhd itallggeir ednyrswsse
      601 rfgyddqklt ysqvdwqtls rdgvvgqlys svrrraenls vseikhryvs ayfnagytyd
      661 qryafnasvr ieqadlfgtd pkyryrplws vgaswnanke efmkqfswin llklrltygi
      721 tgnvdqsssp yllagfattl hsgapvtmil tppnsslrwe ktstfnvgid yrflgklsgs
      781 idfyrryssd llvnksidps lgfngmakan ngemknvgve fvatydwlkh kqtslsttfs
      841 aaynsntiek vdyeptdaid miqspasnyr vgdtyksvya yryagltsdg npsvydesgn
      901 ivsispvrsa davvcvgqlt pkwsgalsmd fryknlglfl kavyytghsl rddvvtlyds
      961 yntirngaig edivnrwtpt ntdtdipamg lhsdtgerny hwkyadvnvv sasfikmrni
     1021 gvtydlpktw ltkigvkgar lklqvdnafr wtandkdidp eafnansgtr neavmpsyil
     1081 glniqf
//
LOCUS       WP_094385511            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094385511
VERSION     WP_094385511.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115946
     Region          59..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknikrkddi gnavtrlcll aalttfgats tqtfaqnaaq ngvqaknvvv vegvvyekat
       61 geilpgasia vyvkeklltg tsadidgkfk isvpagnfei kvsymgmvtq titsktkglg
      121 nlkvfldsdt qtiqdvvvtg yvnkrkesft gsvtqlkged lkmvsntnil taiaaltpgm
      181 avvqnssqgs npnhveelvl rgtssfsnsg qdvnqptiil dgteitmqel ydldmneven
      241 invlkdasat alygskaang vivitrkpik nstvrvqynf tgnlqfpmlg dynvlnaadk
      301 lkyeqlagly dakgavnsvt glpeqyeldr lyneryklva agqnsdwlsq parvafsqdh
      361 slrvyggasn mryelsgrfg dtrgvmkgdy rkrynigfkl dyfiknvvti snrttysevd
      421 tkntpygsfs qytrmnpydp mynedgsant nlswdmnnpl yeaqlgsysk agthsfnnst
      481 dvrwdinkqf rvtghlniqs slgwsdsfts pksqsyknep dltkrgqlvk adtrttsyda
      541 nivgtynkff adeslitasl gwevnhdksr tenteaigff ndqlsfigna sgypsdrqpy
      601 gsqaetatvg afltanysfr nryfvdgtwr mtgssqfgen nrwgnfwsag agwnilneef
      661 mksikkkidl mklrfsmgyt gkvsfspfqa mtmyqylnty eykngigavp ltigdvdlaw
      721 ertmnynigf dfsmfdrrln fvldayvrkt tdllldrsmp pstgvtqats nlgemenkgl
      781 efqvdgyifr skdfywklgt sgymnrnkit kinkaleein nkneenssls ltplpqyaeg
      841 esttalklvr sagidpatgr eiyikrngel tftydsadkv ligdtepryt gtvntnvywk
      901 gfnvyallnm rlgawlyntt rvskvegsnp kynadqrvfd drwkqpgdia lykniadssr
      961 peqtdrfaek entltlgtln isyefsdemc rrmyvrnlrc gvnftdilrl stvkiergtd
     1021 ylysqgfefy vnvtl
//
LOCUS       WP_094385866             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094385866
VERSION     WP_094385866.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111311
     Region          32..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqlrtknvm yrflmmlfmv cvtmtasaqk akitgtvrdp ggepligvsv rvdktgqgvv
       61 tdvdgnysie vsssgtlifs yvgfetasek ingrkvidvt lkeksdilne vvvigygtmd
      121 kkeltsaish vsekdfltvs sldpsmmiqg kvpgvsitnt gagdpnnqas iqirgvssrs
      181 aglgplivid gvpggnltni npndiasfdi lkdgaasaiy gtrgsngviv vttkkgskdg
      241 svhtsysgmm sfdvikkeld mmsaqdyrdv rlgwgdtgvd lggnvdwlda vsrtgvtmqh
      301 tltmsggndk nnyrisadyr dakgidlrse reeygarasv mhtskgglft ftanvaprii
      361 yrdnadwgvf kdaieanptt plmdpenpar yynfmgqvvg snpverqkle qdhadtklld
      421 wdatvklnll pllakegksn hrlttqlmfa dhqysndntw frpststiai nngregeasr
      481 syskerqqim ewltnysgsf gqhnvkamag ysyqysrysg fnaynkdfpn dglgadnlgs
      541 geyakeegei cmgsyqndsk liaffgrvsy dfagkymfta slrhegsskf ganhkwgnfp
      601 avsagwrisd ekfmkgvkwv ndlklradfg itgnqdfgsy lslntmtgfg yyfyngkyfq
      661 vwgpsknvnp dlrwekgknw nvgidfslfd nrlygsvnyf nrrqqdllgn ykvsvppylf
      721 detfvnvgtm kntgieidln fravntkdft ydinfvgttq snkfvdfsns qyvgqdyydv
      781 cgtedpypfy nlqriqkges lgnfymwrya ghttdgewlv ydkdgdiira sqasdadrtv
      841 vgngmpkftm stshnfrykd fdlslffrga fgfdifnihd fyygtrnftg nrlkkayakn
      901 fvvsstanpv vcdyflergd ylkldmitlg ytlkaencrf idrirlygtv knvftltkfs
      961 gvdpstyqvn gltpggqgsr tyfpstrqfi vgmqidf
//
LOCUS       WP_094386178            1180 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094386178
VERSION     WP_094386178.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1180)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1180)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1180)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1180
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..1180
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131950
     Region          28..96
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          111..1179
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkekqllim illfvalgir gqhqkvtlnf tstpvsqvlr tiskqtgldf vysnsqlesm
       61 gditikatke pigevlkrms astgftfkfd kntiivqqdn kktdvkidgy vvgvvtdadg
      121 nplpgvtvkf mennygttts sdgryhlnar gvskgsisfs figmknkvva ykgqsiinvv
      181 mdedshlidd vvvtgygtyn rgqyvgavsq vkaedikian essidqmlqg vipgvsvvnt
      241 tgkvggtpki rirgtstilg nqeplwvvdg viqtnptpip ndasplssdm demlqtagna
      301 iswlnpadie titvlkdasa taiygsqatn gvivvttkka kaqtgvsiny sgslsitqrp
      361 syglydlmns qqymefnqqm yhdrnaytye vlpigyaglv qklhnktitq eefnqefrnm
      421 eqmntdwfdl lfrtpvstqq nvsissgsek lqsrfslgvn sspgeakgnd mfqvtassnn
      481 tyrptknlsi dlsvngsyrk andfysgvsp ydyamntsra lplynedgsl yyypvygnis
      541 ysilnkhcyn ynilneldns gsqsavtsfq anlglrwkll knvefqgdas lslsssrmks
      601 wateftntvs qirgydmgev qanseeelss plpyggilns atqqnvnysf rgafvynntf
      661 aekhsvtfni gmqvtsykfd getmlhygyq kyrgetfatv palsdlhtvt gykpstdlhe
      721 lmrqgssitn tkqnqlseyf tavysfdnry vlnlngrlda snrfgqdenk rfnptlsfga
      781 kwrigeepwm dwasswydmf disfsygwrg nsvtevspyl iatdgglhty fkqyylkiks
      841 lpypdlgwek trdwnigadl sffdgrlsag fnyynkrsdv lssrevstey gvqsayvkgt
      901 imknygyefi isatpirtkd wtwsiafnts kdynrvenne ivnlpndylt gaaivegmpy
      961 gtiyafdfag ldpetgyptf ngldkeekpv dfreylveag ctepdvaggi stslryknih
     1021 lraqfamsig aqaylpqyfa ttgaprpeqn mptymldrwr qpgdelwtdi psiaagnpnd
     1081 initlkygsn geywsspyqm ynystariad tdfircrsls lqydlpkpal atlgmrnayi
     1141 tasltnpffi afdskwngrd petaswpark sftlalnitf
//
LOCUS       WP_094386222             958 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P2-180].
ACCESSION   WP_094386222
VERSION     WP_094386222.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P2-180
  ORGANISM  Prevotella sp. P2-180
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 958)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 958)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Prevotella sp. P2-180"
                     /db_xref="taxon:2024224"
     Protein         1..958
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105795
     Region          50..957
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkniimlt llagsclpam aqsdiidsva ykdqtvdiga nrlftreqst aavsvistkd
       61 vnkrgarnig nnilgqgngl vsldgsgiya sqnptfylrg lqslngntpl ilvdgverai
      121 envvaedves vqilkdaaat alygykgang vvlittkhgq yntksftfty dhvfsfltnk
      181 pemadaatya savneayrnq gstgnvaysd avinaykngt nplyypnvnw adetfrnvsn
      241 ndrfnlefkg gtknfryytn vqlltnkgfi knfqndgyst qdkytrgtlr snmdidlspk
      301 tklhthlygl lteqsqpgsq anlwsmiyqv panafpvkvn davwggntvy ttnnpvaqsq
      361 aaayyknhqr alyadvqlvq dlsaitegls aqgqigydtw snvyenhskt yrysyyevsn
      421 agdvisdgna slssvqgtds nmgtasgnns wirrcifngs inydrtfaek hnvygqlkyd
      481 yeyndqtgtn ttvyrhnisl fahygfanky lldvalvesg ssrlapgskw afspnvsaaw
      541 nisnesfmkd vkwvdflklr asfgnqsldv lpgsnvwtyy dqfylmngts ypfdatytgt
      601 qwgntylsta ptqslghers tkfnvgidat lfgslnvsld yfyqhrydiw cstagsynsv
      661 fglgapyenv gvvnsqgfei sadyskkins dltinvgasf tfnkntikeq aeapqlyant
      721 astghcygqa fgyvangffq ksddingdgi istsemtekg ypvqsfttvy pgdvkyvdlt
      781 geniidandr kaigysttap diyynfhlga eykgigldam fqgvgrwtgf mttnglyrsa
      841 vatntlsqyl yenswsaerg ntesalfprl sttsnanndl nstlnmfdrs yiklryvely
      901 ynlpksllnk lsvinnvkly vrgtdlftad hldkadaasy gvaqpltrsv qlgaaltf
//
LOCUS       WP_094387041            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-64].
ACCESSION   WP_094387041
VERSION     WP_094387041.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-64
  ORGANISM  Prevotella sp. P5-64
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Prevotella sp. P5-64"
                     /db_xref="taxon:2024226"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120844
     Region          115..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnskqskllg icllvtlmfs alsmsaqtvt ktfsneslrn vlkeverqtk msviykvdev
       61 nasqkvtatf hatpvrdvlt kvlgshlgfk idhkmitifk reakpaakds qapkktvkgq
      121 vldengepvi gatvrskatg aavvtdldgn ftisaeegsk ievsylgyqp ksvtakgdnl
      181 tvnisqdekt lnevvvtalg ikkeskalty nvqqlknsdi tgvkdanfmn alagkvagve
      241 inasaagigg gvkvvmrgnk singnnnaly vidgipmpsl qanqptdayh gdaqtgdaas
      301 mvnpddiesi svlsgaaasa lygsdaangv vmittkkgtv gkvrvsysnn tsffspfvtp
      361 efqntygqtg ngtfsswgsk latpssydpl dffqtgynvg nsvtfsvgse hsqtfvsast
      421 tnaegivenn emsrynftvr nttdflkdrl hldlsamyms vkeqnmisqg fyfnpivpvy
      481 lfpagddirk ytpfeqydpe rnfktqywpf gnqglsmmnp yweinrdiae nhkdrfilsa
      541 gltfdiakgi tlsgrakmdk tsgiyekrya astdplfage ygayyrtndn trqiygdail
      601 nidkyfgdfs ltanlgtsik dvetsytyvg gflnvannft lnavnransh mdadpalnyh
      661 hqvqsvfata qvgyksmvyl dltarndwds flgntqyrnk gffypsagvs ailtemipgl
      721 kskvlsflkl rgsysevgnt pekfyaltry tysnaapstt syypnnnlkp ertkawelgl
      781 qanlwqdkvn lnvslystrt tdqfflpels assgysklpi nggridnkgi easltlnqpl
      841 gpvkwsstft ytlnknkikq llapteltla ngnkvnvsld gmdmlnlgsv kvrlteggsm
      901 gdlyvtipkm dehgylivdy tsrniagvde gkyvyagnvn pkynmgwrns fswkgidlgf
      961 lisarvggrv ssitqgymdy fgaskttaea rdlggalvng yripaqdyys kigpsvgayy
     1021 iysatnvrls elsvgyslpi skwvpwienl rlaftgrnll mfyckapfdp eltastgtyf
     1081 tgidnfmmps lrnlgfsvkv df
//
LOCUS       WP_094387048            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-64].
ACCESSION   WP_094387048
VERSION     WP_094387048.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-64
  ORGANISM  Prevotella sp. P5-64
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Prevotella sp. P5-64"
                     /db_xref="taxon:2024226"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111101
     Region          24..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlsmffa clflsigmal aqtkvtgtvv ssednepvig asvkvvgtkt gvatdidgkf
       61 slvvnsknae lefssigmvt krlkasanmm vvldpdshvl eqvvvtgygq akkvgavvga
      121 igtvgseklg kivtpnftda lagqvsglsv lssagdpstt atirlrgvnf lqtsnqplfi
      181 ldgapisstf fstlnpedia nitvlkdaas tsiygaraan gvilitskqg rynesaqvsv
      241 kaqwgvsspt sdgaemmnse qyvqfrdiig qpvsdeirnl vknyglntnw ydevlsssap
      301 tydinatmqg gsqtvnyyms ynhhkqqglv eksamqrsvl narinarlnk ffkvgysani
      361 gvqdfeqnav wsamqsassi ytnnplvfar kalpfdvpyy ysfddsgkli kgakadylhy
      421 sgmktmeqds ryrrsfrkri tlntslnevl tpidgltlta qqslelvnqt ldnrnlpwet
      481 frtpmgdivg dgavgsmntg avqnrytssy qynlihtaey rkgfgdhnid vlvgeetrit
      541 kdwqfgafat ghadarlmni tsgtnvalsd ledaqtkvva nslfatleyn fkekyyfyss
      601 irrdgsskfa pdhrwgtfws lgvkwdakke sflkdvswln daslslnygt tgsdagpgay
      661 eyfglygqgs lyngqttlgi aqaanymltw ekvdklnfgi narvfdrlgv ninlyknkst
      721 dmimdvpysf ttgfsagvgn vgsmvnkgfe advdvdiikt rdmrwtfkan vgynkneite
      781 lfagrdnyti antgvryevg rsygefylpr ragvdprdga pmwydkdgni tktfseenct
      841 vwtgknryap wiggfgtnft wkgfaiiadf awqsgkyllm neevftanpa natswnqqtk
      901 mlniwtkpgq itdipaagyn vtmlddnlld nasflrmktl slqydlpkkw laplryvkgf
      961 kvfgiarnlf titsfsgydp epdinlvkfn ypntrqfvlg aevtf
//
LOCUS       WP_094387605            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-64].
ACCESSION   WP_094387605
VERSION     WP_094387605.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-64
  ORGANISM  Prevotella sp. P5-64
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Prevotella sp. P5-64"
                     /db_xref="taxon:2024226"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114304
     Region          40..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkivylfll lmlalaypsv smasptgmet atdqdgnnsi sgivtdqnge plagvtvlqr
       61 gtqnktitdl egrytirlka gsgrtlvfty igmvsqtipv kgsvarvmmk edatalqdvv
      121 vigaygtaqk rsdlvgsayq vnadqlkglp qqrldvmldg lipgvkidpn tadpgsprtr
      181 yevrvrgeas lnasneplwv vdgtpmytgd rtnlmpgtsy tvsplsflnp ediasvtvlk
      241 datatsiyga dgangvilvt tkkgrqgkmr itvntqygia hidestapkv lgakewlsla
      301 reayansgkd mrtfpfqdne lnqysttdtd wrdvfydtgt tfltnvgvsg gnqksdyyvs
      361 gqyyqndktv kgntqqrlsl atninlklnk rlkvgvdisa synnndlfal greyyellpi
      421 yspynadgtl rlynmevdgl nadgtphftk krfisnsvle reqndnnqkt wylrsnftlk
      481 yeilkgltyt gqfaydynst leetyssqkn wtgmdtdgtp igyarrssvd itnwntihrl
      541 nfnrtfgrhs vsalagfeag srdyttmyvt gsgfindnir dvsqanttkg ynsssrrrkv
      601 sllgqatysy dhryyltvna rkdgnsqfgs dvrwanfasv gaswnvhnek ffnipwvnvl
      661 klkasygang nsrlgsqesq gtyvysssys yngelggvlg tipnsrlswe ttymtnlglr
      721 lavlnridfe ieyyhnqtkn llsrlpisll tgdtrayrnv geivnkgiei nlttrnfvpk
      781 kdgdfawttd fnlahnqnrl tksyngtqvn fgeiswiegq dtktyymvrw agvdpldgsp
      841 mwydangnit kvydstnnrv rgksanptvt ggmtntlsyk nfslrfllny qfggyayssf
      901 asimnsdgyn vlsynqaieq rnywrnpgdi amntrpqagv stgssrtstr ylykkdlvrl
      961 qnvvftyqlp rslvngwkls nasvsliadn llayspysgs dhnsyktlms gyplertftl
     1021 slnvgf
//
LOCUS       WP_094387613             898 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-64].
ACCESSION   WP_094387613
VERSION     WP_094387613.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-64
  ORGANISM  Prevotella sp. P5-64
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Prevotella sp. P5-64"
                     /db_xref="taxon:2024226"
     Protein         1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98806
     Region          49..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mangkkttll llllfcssla haqkqvpier kdtianesni ikivgnhsnk gaannaldvl
       61 sgqaagvnvt sngldrmaml nsvrvrgtts iiggndplvl idgvtsdvft lstiypadie
      121 sfrilknate tamygsrgas gvievktkkg tgrgfqisye gnvgferryk hlemlnaaey
      181 vatakalgiy cnnggfntdn ykvitrtgmv nnhylafsgg tpqsnyrasf gvmdhntiik
      241 kmdynvfvak vdvtqkafnd rltgefgvfg ssfknhdifd tqmlfysaac qnptlpagtd
      301 engnwlknes athvnppgiv ldekndsrdl nfdahiklsy dfnpnwrist fasylygste
      361 ngmfcptwvw aqgnvyrgef kkeewlgnva lsfnkqigih risaeassey rkltktafwm
      421 yakgiptndf gynnlgatav rpyggtesty edqslasvmg svtyslldry llsvnargdg
      481 ssmvgddntw gffpsvsftw dmkkenflvn vkplsmlklr tglgqagnlg gisayttmnt
      541 vrqtgivpvk ssptvtlgmv rnnnpdlrwe tkttfnigad fgffanriml taeyyyskts
      601 dmlyayevpv ppfayntlla nigsmsnrgl elglsvqpis kkdmelninm nlsfqsnkli
      661 slsgdykgms mtaanvtaig sldgagqngg dnnvvyqivg qplgvfylph ckglvkneng
      721 syfydiedld hngkvdlsdg gdryiagqat pkvtlgsnis frykdiyval qmngafghni
      781 fngtglayts macfpdynvl kdapkknivd qrvsdywlek gdylnfehlt lgynvplksk
      841 fvrslrvscn isnlgtitgy rgltpminsy vvnstmgidd krnyplyrty slglsvqf
//
LOCUS       WP_094387937            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Prevotella].
ACCESSION   WP_094387937
VERSION     WP_094387937.1
KEYWORDS    RefSeq.
SOURCE      unclassified Prevotella
  ORGANISM  unclassified Prevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="unclassified Prevotella"
                     /db_xref="taxon:2638335"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111114
     Region          24..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlsmffa clflsigmal aqtkvtgtvv ssednepvig asvkvvgtkt gvatdidgkf
       61 slvvnsknae lefssigmvt krlkasanmm vvldpdshvl eqvvvtgygq akkvgavvga
      121 igtvgseklg kivtpnftda lagqvsglsv lssagdpstt atirlrgvnf lqtsnqplfi
      181 ldgapisssf fstlnpedia nitvlkdaas tsiygaraan gvilitskqg rynesaqvsv
      241 kaqwgvsspt sdgaemmnse qyvqfrdiig qpvsdeirnl vknyglntnw ydevlsssap
      301 tydinatmqg gsqtvnyyms ynhhkqqglv eksamqrsvl narinarlnk ffkvgysani
      361 gvqdfeqnav wsamqsassi ytnnplvfar kalpfdvpyy ysfddsgkli kgakadylhy
      421 sgmktmeqds ryrrsfrkri tlntslnevl tpidgltlta qqslelvnqt ldnrnlpwet
      481 frtpmgdivg dgavgsmntg avqnrytssy qynlihtaey rkgfgdhnid vlvgeetrit
      541 kdwqfgafat ghadarlmni tsgtnvalsd ledaqtkvva nslfatleyn fkekyyfyss
      601 irrdgsskfa pdhrwgtfws lgvkwdakke sflkdvswln daslslnygt tgsdagpgay
      661 eyfglygqgs lyngqttlgi aqaanymltw ekvdklnfgi narvfdrlgv ninlyknkst
      721 dmimdvpysf ttgfsagvgn vgsmvnkgfe advdvdiikt rdmrwtfkan vgynkneite
      781 lfagrdnyti antgvryevg rsygefylpr ragvdprdga pmwydkdgni tktfseenct
      841 vwtgknryap wiggfgtnft wkgfaiiadf awqngkyllm neevftanpa natswnqqtk
      901 mlniwtkpgq itdipaagyn vtmlddnlld nasflrmktl slqydlpkkw laplryvkgf
      961 kvfgiarnlf titsfsgydp epdinlvkfn ypntrqfvlg aevtf
//
LOCUS       WP_094387941            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P4-67].
ACCESSION   WP_094387941
VERSION     WP_094387941.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P4-67
  ORGANISM  Prevotella sp. P4-67
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Prevotella sp. P4-67"
                     /db_xref="taxon:2024227"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120854
     Region          115..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnskqskllg icllvtlmfs alsmsaqtvt ktfsneslrn vlkeverqtk msviykvdev
       61 nasqkvtatf hatpvrdvlt kvlgshlgfk idhkmitifk reakpaakdp qapkktvkgq
      121 vldengepvi gatvrskatg aavvtdldgn ftisaeegsk ievsylgyqp ksvtakgnnl
      181 tvnisqdekt lnevvvtalg ikkeskalty nvqqlknsdi tgvkdanfmn alagkvagve
      241 inasaagigg gvkvvmrgnk singnnnaly vidgipmpsl qanqptdayh gdaqtgdaas
      301 mvnpddiesi svlsgaaasa lygsdaangv vmittkkgtv gkvrvsysnn tsffspfvtp
      361 efqntygqtg tgtfsswgsk latpssydpl dffqtgynvg nsvtfsvgse hsqtfvsast
      421 tnaegivenn emsrynftir nttdflkdrl hldlsamyms vkeqnmisqg fyfnpivpvy
      481 lfpagddirk ytpfeqydpe rnfktqywpf gnqglsmmnp yweinrdiae nhkdrfilsa
      541 gltfdiakgi tlsgrakmdk tsgiyekrya astdplfage ygayyrtndn trqiygdail
      601 nidkyfgdfs ltanlgtsik dvetsytyvg gflnvannft lnavnransh mdadpalnyh
      661 hqvqsvfata qvgyksmvyl dltarndwds flgntqyrnk gffypsagvs ailtemipgl
      721 kskvlsflkl rgsysevgnt pekfyaltry tysnaapstt syypnnnlkp ertkawelgl
      781 qanlwqdkvn lnvslystrt tdqfflpels assgysklpi nggridnkgi easltlnqpl
      841 gpvkwsstft ytlnknkikq llapteltla ngnkvnvsld gmdmlnlgsv kvrlteggsm
      901 gdlyvtipkm dehgylivdy tsrniagvde gkyvyagnvn pkynmgwrns fswkgidlgf
      961 lisarvggrv ssitqgymdy fgaskttaea rdlggalvng yripaqdyys kigpsvgayy
     1021 iysatnvrls elsvgyslpi skwvpwienl rlaftgrnll mfyckapfdp eltastgtyf
     1081 tgidnfmmps lrnlgfsvkv df
//
LOCUS       WP_094389052            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P4-67].
ACCESSION   WP_094389052
VERSION     WP_094389052.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P4-67
  ORGANISM  Prevotella sp. P4-67
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Prevotella sp. P4-67"
                     /db_xref="taxon:2024227"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111924
     Region          45..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdrmqsnllr lffssalclg svsafavgap sekapfnkve qanektvggq vldengepvi
       61 gatvtvkgtk tavvtdidgk fsfkvpagst lvvtylgyad kevaatgtgm tinmaqdekt
      121 ldevvvtalg ikrsekalsy nvqqlgnedl ttvkstnfmn slagkvagvn inassagmgg
      181 atrvvmrgpk sinqsnsaly vvdgvpinnr nngtaegiya sqpggegiad inpediesis
      241 vlsgpaaaal ygsaaaqgvi mittkkgkeg rvsvvvsnst qfsdvfkmpe fqneyanrpg
      301 evrswgekgg seftgfdpen ffntgtniqn nvsltvgngk nqtyasvgtt nangimpnns
      361 ydrynftfrn stsflndklt ldfnlnyvkq sdmnlmaqgq yfnplvalyl fprgesfdai
      421 rtfevfdqsr giyvqnwnfg dalsmqnpyw ianrmnrttk khryminssl kyqifdwldv
      481 vgrirfdrat sksedkryas tinlfahsdy gfyaysnavd qsvygdvmfn vnksfdkfsi
      541 ganvggsfsr tqfdnngfqg glrapsnifs pnaidyanat ndnrpiyafn khninsvfan
      601 velgwrsmvy ltltgrndwd salagtknes ffypsvgtsa iisqmvklpe fidylkvrgs
      661 wasvgsaisp nitsqwrynf kpntqtyetv tykfpktfyp ertnsweagl tarffnnalt
      721 ldmtfyqsnt rkqtflrpit vsegydheyv qtgnvrnrgl elsigynhqf gklswssslt
      781 ysmnrnkivd lladpevtis ttglngvgvi lkkggtmgdv ysytdfardr egnialdasg
      841 nvirktlsnp kylgsvlpkg nigfsnefsw kginlgfllt arlggivmsq tqaimdyygv
      901 sktsaaaren ggipvntglv paekyyavvg gdnpiwseyt ysatnvrlqe ahisydvpkk
      961 wlagldlslg ltannlwmiy ckapfdpest astgtfyqal dyfmqpslrs lgfnvklkf
//
LOCUS       WP_094389213             898 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P4-67].
ACCESSION   WP_094389213
VERSION     WP_094389213.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P4-67
  ORGANISM  Prevotella sp. P4-67
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Prevotella sp. P4-67"
                     /db_xref="taxon:2024227"
     Protein         1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98778
     Region          49..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mangkkttll llllfcssla haqkqvpier kdtianesni ikivgnhsnk gaannaldvl
       61 sgqaagvnvt sngldrmaml nsvrvrgtts iiggndplvl idgvtsdvft lstiypadie
      121 sfrilknate tamygsrgas gvievktkkg tgrgfqisye gnvgferryk hlemlnaaey
      181 vatakalgiy cnnggfntdn ykvitrtgmv nnhylafsgg tpqsnyrasf gvmdhntiik
      241 kmdynvfvak vdvtqkafnd rltgefgvfg ssfknhdifd tqmlfysaac qnptlpagtd
      301 engnwlknes athvnppgiv ldekndsrdl nfdahiklsy dfnpnwrist fasylygste
      361 ngmfcptwvw aqgnvyrgef kkeewlgnva lsfnkqigih risaeassey rkltktafwm
      421 yakgiptndf gynnlgataa rpyggtesty edqslasvmg svtyslldry llsvnargdg
      481 ssmvgddntw gffpsvsftw dmkkenflvn vkplsmlklr tglgqagnlg gisayttmnt
      541 vrqtgivpvk ssptvtlgmv rnnnpdlrwe tkttfnigad fgffanriml taeyyyskts
      601 dmlyayevpv ppfayntlla nigsmsnrgl elglsvqpis kkdmelninm nlsfqsnkli
      661 slsgdykgms mtaanvtaig sldgagqngg dnnvvyqivg qplgvfylph ckglvkneng
      721 syfydiedld hngkvdlsdg gdryiagqat pkvtlgsnis frykdiyval qmngafghni
      781 fngtglayts macfpdynvl kdapkknivd qrvsdywlek gdylnfehlt lgynvplksk
      841 fvrslrvscn isnlgtitgy rgltpminsy vvnstmgidd krnyplyrty slglsvqf
//
LOCUS       WP_094389218            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Prevotella].
ACCESSION   WP_094389218
VERSION     WP_094389218.1
KEYWORDS    RefSeq.
SOURCE      unclassified Prevotella
  ORGANISM  unclassified Prevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="unclassified Prevotella"
                     /db_xref="taxon:2638335"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114276
     Region          40..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkivylfll lmlalaypsv smasptgmet gtdqdgnnsi sgivtdqnge plagvtvlqr
       61 gtqnktitdl egrytirlka gsgrtlvfty igmvsqtipv kgsvarvmmk edatalqdvv
      121 vigaygtaqk rsdlvgsayq vnadqlkglp qqrldvmldg lipgvkidpn tadpgsprtr
      181 yevrvrgeas lnasneplwv vdgtpmytgd rtnlmpgtsy tvsplsflnp ediasvtvlk
      241 datatsiyga dgangvilvt tkkgrqgkmr itvntqygia hidestapkv lgakewlsla
      301 reayansgkd mrtfpfqdne lnqysttdtd wrdvfydtgt tfltnvgvsg gnqksdyyvs
      361 gqyyqndktv kgntqqrlsl atninlklnk rlkvgvdisa synnndlfal greyyellpi
      421 yspynadgtl rlynmevdgl nadgtphftk krfisnsvle reqndnnqkt wylrsnftlk
      481 yeilkgltyt gqfaydynst leetyssqkn wtgmdsdgtp igyarrssvd itnwntihrl
      541 nfnrtfgrhs vsalagfeag srdyttmyvt gsgfindnir dvsqanttkg ynsssrrrkv
      601 sllgqatysy dhryyltvna rkdgnsqfgs dvrwanfasv gaswnvhnek ffnipwvnvl
      661 klkasygang nsrlgsqesq gtyvysssys yngelggvlg tipnsrlswe ttymtnlglr
      721 lavlnridfe ieyyhnqtkn llsrlpisll tgdtrayrnv geivnkgiei nlttrnfvpk
      781 kdgdfawttd fnlahnqnrl tksyngtqvn fgeiswiegq dtktyymvrw agvdpldgsp
      841 mwydangnit kvydstnnrv rgksanptvt ggmtntlsyk nfslrfllny qfggyayssf
      901 asimnsdgyn vlsynqaieq rnywrnpgdi amntrpqagv stgssrtstr ylykkdlvrl
      961 qnvvftyqlp rslvngwkls nasvsliadn llayspysgs dhnsyktlms gyplertftl
     1021 slnvgf
//
LOCUS       WP_094389706            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P4-119].
ACCESSION   WP_094389706
VERSION     WP_094389706.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P4-119
  ORGANISM  Prevotella sp. P4-119
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Prevotella sp. P4-119"
                     /db_xref="taxon:2024218"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123270
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmmfla glflslgmaf aqtkvtgtvi sqeddqpiig asvlvqgqrs gtvtdvdgkf
       61 tisvpsgkki tisyigmepq tvtpkngmtv tlrssaelqe vvvtgmqktd rrlftgsttk
      121 vdaekakldg vadisrsleg raagvsvqnv sgtfgtapki rvrgatsiyg ssrplwvvdg
      181 vimedvtevd adqlssgdae tlissaiagl naddiesfqi lkdgsatsiy garamsgviv
      241 vttkkgksgq trinytgeft mrlkpsysnf nimnsqeqmg iykeleangl isfgrtyras
      301 ssgvygkmyq lmntynpatg sfmlsqteea knaylreaem rntnwfdelf snaiqqnhsi
      361 smstgtdkaq yytsfsimdd pgwteqskvr rytasinamy nvnkkvtlnm ianasyrnqr
      421 apgttsqsvd avtgnvsrdf dinpysyain ssraldpnef ytrnyapfni hnelannfmn
      481 ldvvdlkyqa elkykpikkv eltvlgayky stttqaneih ensnmaqsfr amddatirdn
      541 npwlytdpdk pnskpvsvlp vggfyretky kmtswdfrat aqyndvfned hivnlyggme
      601 indtqrsrsy fngvgmqydm gylgsydylf fkqsaeqnam yyslsnsygr evsffataty
      661 swkgryving ttryegsnrl gksrsarwlp twnvsgawna heepwfqktf ktalthatlk
      721 asysltgdkp avtnsqaiiq sfnpwrpfas dkesglniyd fanpdltyek khelnigvdl
      781 gflnnrlnvq fdwyrrnnyd ligmrttngt kgtinefanv asmrshgeel sissknivsk
      841 dfkwntdfif shvktkitel dnrsrlidmv tgtgfakkgy ayrslfsfdf kglnangipq
      901 vvnesgevvt sdiyfqsrdi dylvyegptd ptitgslgns ftyknwhlni fatyafgnvv
      961 rldpafyasy sdldampkef knrwtvsgde nkttipaipd lrqlqadtql syafnaynrs
     1021 tdrvakgdfi rmkeisvsyd fpqtwlnalk lksasiklqg tnlfliysdk klngqdpeff
     1081 ntggvavpma rqftctvrvg l
//
LOCUS       WP_094390539            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Prevotella].
ACCESSION   WP_094390539
VERSION     WP_094390539.1
KEYWORDS    RefSeq.
SOURCE      unclassified Prevotella
  ORGANISM  unclassified Prevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="unclassified Prevotella"
                     /db_xref="taxon:2638335"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122958
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkllillv nifllcggvl aqtkvtgtvv sqedgepiig asiiiqgqrs gtvtdadgkf
       61 slsvpagkki svsyigmetq tlapkakmsi slrpsaelee vvvtgmqktd rrlftgatdr
      121 vnaedailng iadisrsleg rsagvsvqnv sgtfgtapki rvrgatsiyg sskplwvvdg
      181 vimedvtdid sdalssgdpe tlissaiagl nsddiesfqi lkdgsatsiy garamagviv
      241 vttkkgkagt ahinytgeft mrlkptygnf nilnsqdqmg iyrelydkgw lnlsntlngs
      301 dygvygkmye lintynpstg afalanttea knaylanaef rntdwfdelf stsiqqnhsv
      361 smsggtaksn yyasvsamtd pgwykqskvd rytlnmnvnh kildnlslni igsgsyrsqr
      421 apgtlsqdvd vvsgnvkrdf dinpysyaln tsraldpdty yhsnyaafni lheletnfid
      481 vnfldakfqa elkykpikdl eiavlgalky tttsqeykil dnsnqaeayr amdntiirda
      541 nkylytdkdv lysrpisvlp eggmykrtdn rmrdynfrat anyvhtfadi hyvnlfggme
      601 tteiqrsrsw fngwgmqyak geipyytyqf fkksleentd yyslsntnsr saaffanaty
      661 gydnryvlng tvryegsnam gksrsarwtp twniagswnv dqekffkawe ptishlklka
      721 sysltatppp tsytsstnvf kafnpyrift sdketgiqls dlenseltye kknefnfgve
      781 agflndrinv sfdiytrkny deigpvatqg iggqiirwan aadmkshgee lsisstnikl
      841 kdfswitslv yshtktkitn lasqdrvidm itnfggrrvg ypvrslfsip fagldenglp
      901 tfyneageit tdninfqerd kvdylkyegp tdptvqgslg nlfkykgftl nlfitysfgn
      961 vvrldpvfsa tyndlssmtk efknrwmvpg dekktnvpvi lsyaqytnns qlrygynayn
     1021 ysdvriakgd firmkeislq ydfpknwikp ltnlslklqa tnlfliyadk klngqdpeff
     1081 rsggvsapvp kqftatlkvg f
//
LOCUS       WP_094390584             932 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Prevotella].
ACCESSION   WP_094390584
VERSION     WP_094390584.1
KEYWORDS    RefSeq.
SOURCE      unclassified Prevotella
  ORGANISM  unclassified Prevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="unclassified Prevotella"
                     /db_xref="taxon:2638335"
     Protein         1..932
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104736
     Region          27..928
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrhiykglal caalvagstg vyaqeaetdt ldkvqvafra vdkqdlmggv svidmkemak
       61 knyatssiey ienvvggvng glwgygdylv vvdgmvrdan nvlpqeidqv tllkgsaavv
      121 lygpraakgv lqittkrgqm gdlrinahad msigtpisfp kylgsaeyms yynqarindg
      181 ydknysdeei ynfasgknpy rypnfdmyds qyrrdfttry egivevtggt ervkyyttlg
      241 yyrnnellkv gntkdnftsr ffvrgnmdvk fndwlsakad anvtfydafa aktdwwgqaa
      301 tlrphlvspl ipisfiestd kvslgsvmns nylqngfffg gtqsnptnpy adafaagdnk
      361 fvsrqfqfnt efdinlaalt qglmfrakyg idyastynqg ysnsyatfsp twtnyngpdm
      421 igsitqyged kktgqqyisd ssyrytynvs gqfdwartfd gvhnvfamal anawqtqrng
      481 hyhrttnanl glqlsynydh tyyfdfsaam pystklpagn raaisptvtl gwrptkdvlk
      541 dtfvddlmvn vsggiinqdi ditasdnedg yfmyktilqt ggwyswgdle ggaatefqrg
      601 dnydmgfvkr kefsvglrgs lldklitfdv nfftskmdgm ltratslfpn yftqtgypts
      661 siipyvnyni dkrigvdfsv ygnkkigevd lslgvsgtwy kstadkrden iefdylsaig
      721 rplnglwglk sdgffnsqee idaapeqtfg evkpgdikyv dmnndgkidd ndrvflgrwd
      781 tpfrmglnlt akwknftffa mgnlwlggha mksdsywwvr gtgkysevvr nawtpetaat
      841 atyprltttn gdnnfrysdf wmystdrfnl srvqityalp snlfegsfvr gidvyvggsn
      901 lltiakerki letniggapq mrsynigfra sf
//
LOCUS       WP_094398895            1189 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094398895
VERSION     WP_094398895.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1189)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1189)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1189)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1189
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..1189
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133017
     Region          117..1185
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdkrktyrmi fclclflffq vtdvlaqgkk islrcnnipl ptalnrveqq sgyfkihysy
       61 sdvsnyrvta dikdkeapea vmqllgglpf qmnvkgkfiq vkkgeavqlt hdanvakgkl
      121 mdtngeplig asvkvvgthn atvtdingcy elqdvsptdv leysyigmkp ykrkagskpv
      181 siilesdint isdvvvtgiq kmdkrlftgs ttwidaqdak ldgvpdisrs legraagvsv
      241 qnvtgtfgta priqvrgats iygnsqplwi vdgvvqdnvi evntdelssg naetllssai
      301 aglnaddies fqilrdgsat siygaramag vivintkkgh tgktninytg eftmrlkpsy
      361 dnfnimnsqe qmsvyqelqk kgylnpadvv nasksgvygt laklvasgev entdagrnaw
      421 lrqqeyrntd wfdllfsnsi mqnhsvsist gteksqhyas islmddpgwy kqsrvkryta
      481 nlnstfnfsq klkvqliana ssraqkapgt nnsemnivsg evtrdfdinp ysfalntsrv
      541 ldptesytrn yaafnifnel annyidlnth efkmqgqvty npieglelna vgavkrssfa
      601 sehnvtedsn eanayramdn tlirdtnpyl wtdptnpyav pvsvlpyggi yqrsdyrmts
      661 wdfrataayn kifadthimn lfaglesnel krdktwvrty griygfgnia nydptvfdkl
      721 kqeggdyftv skamertaaf fgnatysykg ryivngtlry egtntlgkdr tsrwlptwnv
      781 sgawnaheek wfdslkpwms hftlkgsysl tadrgpynis nssaiinslv twrpdgadqe
      841 talgitelgn seltyekkhe lsltadmgfl nnrinmevsw yrrnnydlig aitvqgvgge
      901 ldkfgniadm ksggfelsls tkniklkdfe wnttflyshq ynkvknlknt sriidlvhgn
      961 gfalegypvr sifsipfnkl ngegiptfnv aegkttidgi nfqeyadlsw lkyegssdpt
     1021 dygslentfk ykglrlsvfi vysfgnvvrl dpvfsntynd lvatprefnn rwssageenr
     1081 tsvpvipsvr qnflnpnlsi aynaynysse riakgdfvrm keisldytlp kkwlmplgin
     1141 svnlklqatn lfliyadkkl ngmdpeffnt ggvaspmpkq ytftvrlgf
//
LOCUS       WP_094398932            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094398932
VERSION     WP_094398932.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116106
     Region          51..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnktvkqtt slrrlflvgi lstglvplca tspyntasaq sgqaaeqsdi kivqgcvyek
       61 sngeilpgat isiyqgdklf tgtvsdvdgk fkisipngdf eirvsylglv tqtfsskskg
      121 ldklnvfles dsqtindvvv tgfvnknkes ftgsvtqikg adlkmvsntn iitaiaaltp
      181 gmaivqnnsq gsnpnhveel ilrgtssfsn sgqdvnqpti ildgseismq dlydldmnev
      241 esinvlkdas atalygskaa ngvivitrkp iknstvrvqy nftgdlqfpm lgdynvlnaa
      301 dklkyeqmag lydaqgaida ttglplqyel dnlynerykr vaagqnsdwl sqparvafsh
      361 dhslrvygga enlryelngr fadtrgvmkg dyrkrysigf kldyfikdai qisnrttyse
      421 istkdtpygs fsqytqmnpy drmynddgta ntdlawdlnn plyeaqlgsy skdgthtlnn
      481 ntdfrwdinr qfrltghlni vstlgwgdtf tspkslyykn etdltkkgql lktdtrstsy
      541 nanvvgtynk mfkdkslvsl sagweinhnk nrsetteaig ffndklsfig naagypsdrq
      601 psgsqgetat vgtfftgnys frnryfvdat wrttgssqfg ennrwgnfws agagwnvlne
      661 kfmkdikkhf dilkvrysmg ytgkvtfspy qamtmykyln tyeykngiga vpltvgnidl
      721 awertmnynv gldlsmfdhr lnivvdayir nttdllldks mppstgvtta tanlgemqnr
      781 glefqidgyi irtkdfywkl gtmgymnrnk itkinkalee innkneenss sslvplpqya
      841 egesttalkl vrsagidpat gkeiyikrng ektfvydsad kvligdtepr ytgtintniy
      901 wkgfslyalf nmrlgawiyn ttrvskvegs npkynadqrv fddrwkqpgd iakykdiads
      961 srpeqtdrfa ekentltlgs lnlsyefsdq tcrklslrnl rcglnftdil rlstvkierg
     1021 tdylysqgve mfvsltf
//
LOCUS       WP_094399262            1131 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094399262
VERSION     WP_094399262.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1131)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1131)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1131)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1131
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..1131
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126681
     Region          26..1130
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktnkikyll laafamvsaf asaqgirisg tvmapdgpvm mcnvterdan nrivsasqtd
       61 ingnfsmeik stanklqvsy igyktktvpi gdktvfdiem edqqtlkevv vvakkrfnhg
      121 glaipanevs vasqtfdmsn veglaftsad ealqgqiagl divansgnlg agtsmrlrgv
      181 tsingsaepl ivvddnifdn pdatfdfqna neetyaslls inpqdiadiq vlkdaaatai
      241 wgsrgangvi qirtkrgsrg atridyslrv qaswqpkgyn llngddytmm lkemyynpsq
      301 sassttnine inynkswaey enwnnntdwv davtqtgwsq yhyltiaggg ekanfrisag
      361 ydhqngtiik qsldrfstkl aldyfvsdri tfrvtfplty tsnnrnfddn ilgraqkvsp
      421 nmgiyrqnad gsntneyytm lptggdyags tapntsskel esirnlgnpv aianlawrhe
      481 ktyrispefk ldykllgtdd dktkldytgm vymdiyasst pkfwpgslft ktwtdsnynr
      541 nenneynslg fttrhtltft pafknkdwya tmfgrwemtt gnnnsqyqlr vntpndvnst
      601 svdggdlsdm ktgngqwrsm salfnghfsy ksryslgvsv radgttkfgd tkkwgyfpgi
      661 sarwnisdek fmkwankwls mlsfrpswgi vgnqpgseyl qyaryatgai ygqvgnndgt
      721 tylealqlnk lkwekttqtn lggdfgffng litgdfnyyy kktrdllmkd vripsttgfs
      781 tlawtnvgdm enkgwelnie ankfinigkf smsanfnisq nfnkilamde svlesinsdw
      841 daskrgsyln riqignplgs iyglrfkgvy qytyeylinm kernnwsged lrnyinnefl
      901 psgktapiai dnegkvlmss tgepvrqvyn fkdgsstykf qggdaiyedi nndgqinsld
      961 ivylgnsnpk vsggfgfnff wgsnwslkts fsyragvkvv nsakmgleqm fnaynqssav
     1021 nwrwrkngdv tnipramfdt gynflgsdry vedasfirms yiqlvynfnk kllkalgmrr
     1081 lqlsisgqnl fcwskysgtd pehsagawgi aydnsqtprs ksvtmninvg f
//
LOCUS       WP_094399270            1096 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094399270
VERSION     WP_094399270.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..1096
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121257
     Region          52..1095
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnnilcls vvlafgvsta afaqddvtyd dgaettvvkk kaqakrptyp tkdvkgtvid
       61 avtkaplagi qiqtlndrny aamtnekgef tikvptfata lyvhapqyls qqvaigdgev
      121 rvvliadkfk smyenttdvt asskstirtt vsqtvetdie nnlgadvhtv trsggpgyga
      181 amfvrglssl nanaqplivv dgvvkdmqtt rnslhygdyn nlllninped vekvtvlkng
      241 naiygakgan gvilietkrg rsmatridan igigvtlept lpdmmnasqy rlyasemlgt
      301 hpdinkydid rfnflnddpn gyyyktyhnd tdwtkevyht altenfninv qggdnvgmyn
      361 lslgytdgqs tarengfnrl svrfntdisv ignlstrfdm sftkvnrdvf dngapesfsa
      421 apvssptflg likapilnpy tynqngqlss tlaeednfvs lldnnltlgn ptallengna
      481 inknrvente fnaiiapkyq fndhfyiqet fsyglnrnsq ryyrptggmp tflidgigrv
      541 qnmamslfsk etsvmsdtrl qftkqlgahf ldvyggmrft sfsfdnnqpq gqyasaandk
      601 tpniskdmef kesygvddaw kniswyanvd ynyrnlyfaq vamslesssr fgenasglgl
      661 agvkwayfps vqlgwaisne kwfpqtnain ylllragydi tgnddinnya artsfsvvsy
      721 lnksaahlld nigndeitye ktgqlnlgfk sfllnnrlgi dfnyymrhtt nlltlksfdn
      781 pvaginnyws nggsmdnngf evtltakpvv skdfnievga svghytnkik slpnddkiyl
      841 ngkkdavgyt ssiygtdnia tivgqaagsf ygyktagvfa ddkeaaaagk dgylyltdnt
      901 gakqyfragd mhfvdingdg eiseadktii gnpnpdiygn ifasimwknf tlslgfnysl
      961 gndvfnysrs ileggnnfyn qttamtnrwr qegqqtdipr isfddamgns rfsdrwiedg
     1021 sylrlktlnl sykvpvnsew lqgltiwaea snlftlthyl gsdpefsasn svlyqgidpg
     1081 nialsraftf glkinl
//
LOCUS       WP_094399689            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094399689
VERSION     WP_094399689.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122052
     Region          62..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkstimnimq rhglrlslca malglstsaf aqtddeteev emsikqpkrq ravaddkytm
       61 mtisgtivdq vsnkplagiq lrmlgneryt amtgadgtfn ikvptfatsl yvhapgfmpq
      121 qvavnagddk qkvdikmlpd kyramytdht vytaqsgfea ssnsitiend ienklgadvr
      181 titrsaapgi gasmfvrgls slnanaqpli vidgveqdmq qnrlslhsnq vnnilanisp
      241 ddiasvrvlk natalygarg angvilidtk rgnsmatrid anisagvslv pqlptmmnas
      301 qyrnyateml gtvpenvnld tpisfrflnd dpnsyyyhty hndtdwsdyv yrtaltqnys
      361 invqggddig mynlsvgyik aestakkndf drmnvrfntd inilynlktk fdisisrtns
      421 svfddgaped ldagtitspt flslikapiv spyqynaiig gftsllsdyd diysqlgpny
      481 glanpvailq nsngdnknks entyfnvrie paytinpsls ltsmfsytld rnsqryhrpy
      541 ngvppfeiad lgtvtsmaas lfskeisvvs nthidwhhqy grhtigafgg fkytyfsfdd
      601 ndlkteytsa tndknpslsa gtgfqhingn ndvwknihwy anvdynymnr yfatvslsae
      661 ansrfgkkag gldlcgvswa lfpsvqlgwv mtnekwfpkt gainylrlna gfdmsgnddi
      721 snyaartsls avrfnynaig lqltnignde ikwetsrkfn vglqsflvnn rigvdfnfyi
      781 nktsdlltlk tfdnpiggin nywtnggelq ncgfeltftg kpvvsrlwni elgatvghys
      841 nevkklpdgd yttsiygdnn iltavgkpvg lfygyqtagv faddnearsa gkdgylymed
      901 nagqrnnfva gdvhfidrnn dgiindldkt vigdpnpdiy gnifatvsfr dftltmgwny
      961 slgndvynyq rsilnsgstf ynqqvaevsh wryegqqtaf prlaygdplg nnrfsdrwie
     1021 dgsylrlktl nlsykvpvpg swtwlqglti waqaenlltf tkycgsdpef signgvlyqg
     1081 idcgnlaqgr sfscgvkinl
//
LOCUS       WP_094399746            1133 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094399746
VERSION     WP_094399746.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1133)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1133)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1133)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..1133
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126968
     Region          24..1132
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msnkklllta clcaasltmm aqskrisgtv sdamgpvmma niteidannr ivsaaqtdfn
       61 gnfsmevksp knklrisfvg dktktitvgd kevfdivles dshtiqevvv kgtrmgsggl
      121 fipkrevsva qqtfdmssve gmaftsadea lqgeiagldi vsnsgnlgsg ttmrlrgvtt
      181 ingdaqpliv vddrifdnpd etfdfsnane eqyasllsvn vediasiqvl kdaaatavwg
      241 skgsngviqi ttkrgargkt rvnfsykftg twqpdgykll ngddytmlmk eefynpkqas
      301 nattniaeln ydqswseyen wnnntdwvka vkqfgqmhsy nvnltgggqk aqfrisagyd
      361 hqtgsiikqt ldrfstrlvl dynvsdrikf stnfaltytn nnqnysgllg iaqklapnms
      421 iyrqnadgsd tnefylmnpv apsgqspytg nyssselski rdlgnpiaia eqawkkdqty
      481 ritpnftlky ellgidadks rltftgrvdf diyahslpty ypaslttnkw tdtsynkatn
      541 tennrfqmsa raemtftpaf rnkdwfstml fryemttsks nnqyieeysl pdgidspttp
      601 galkdmssgn srsnsqywly nghisykery ildfslradg dskfgpknkw ayfpgvaary
      661 nvidesfmkp lrdkflsmla lraswgingk apnadylfys tyntnggsyg ngnnlftiat
      721 idglklddlr wekttsvnlg fnlgffndrv evdfdwynkd tqdllmtnvk ipsttgygtl
      781 syanvgkmnn qgwelnisgk kilqigkfsf daslnvaqnf neikemdqrv ldaintewsa
      841 ttrpasksst gytnriqvgn algsiygfry kgvyqygydy lenyqkehgl sateyeawin
      901 sqlaegktfp vvlgsdgkvl mtsqghpqhl vynysngsqt yvfrggdaiy edinndgqin
      961 aldivylgns lpkvqggfnf tfkygkwslk trfayrfgnk vvnlarmnle nmftpynqca
     1021 tvnyrwrkdg dvtpipramy nagynyqasd rfvengsfvr fnnlqlaynf dkkmikslgl
     1081 nqlqmylsvn nlycwtkysg tdpevsvqgw gvavddsqtp raksftvtln vgf
//
LOCUS       WP_094400569             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094400569
VERSION     WP_094400569.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110925
     Region          31..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 millkkipkc rflflalllt igatafaqkv kitgtvtdpg gepligvsvk tgnsgagait
       61 dvdgnysvev sptgtlvfsy vgfevrnepv knrrvinvtl kekndvlnev vvigygtmdk
      121 keltsaishv gekdfltiss ldpsmmiqgk vagvsitntg agdpnnqasi qirgvssrsa
      181 glgplividg vpggnltnin pndiasfdil kdgaasaiyg trgsngvivv ttkkgskdgr
      241 mhtsysgmfs wdvinkeldm msaqefrdvr lgwgdtgvdl ggnvdwldav srtgtaqqht
      301 ltlsggndks nyrvsadyrd akgidlrshr reygarasim httkgglfti taniapriiy
      361 rdqadwgvfk daieanpttp lmdpenptry ynfqgqvvgs npverqllek dhgdtklldw
      421 dgtvrlnllp llgndsdgnh rlstqvmfad hqydndnswf rpststicin ngregeasrs
      481 yskerqyvve wltnysgsfg shnvkgmagy syqyaqysgl daynkdfpnd glgydnlgsg
      541 eyakeegeid mgsyrndskl isffgrvsyd yagkymftas lrhegsskfg adnkwgnfpa
      601 vsagwrisee pfmknvkwvs dlklradygv tgnqdfgsyi slntmtgfgy yfyngkyfqv
      661 wgpsknvnpd lrwekgknwn igidfslfnn rvygsvnyfn rkqqdllgny kvsvppylfd
      721 etfvnvgtmk ntgieidvnf kavntkdfsy dlnfvgttmk nkfvdfsnsk yigqdyydma
      781 gtedpypfyn lqriqkgesl gnfymwryag hsadgewlvy dkdgdiiras qasdadrqvv
      841 gngmpkftms sshnfryknf dlslffrgaf gydifnihdf yygtrnftgn rldkaygknf
      901 vvsgsanpvv cdyflekgdy lkldmmtlgy tlnlkdcpyl drvrvygtmk niftitkfsg
      961 vdpssyqvng lypgaqgsrt yfpttrqfiv glqidf
//
LOCUS       WP_094401520             899 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094401520
VERSION     WP_094401520.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 899)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 899)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 899)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..899
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..899
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98817
     Region          50..897
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 makskkdftl llialfcssl ahaqkqvpae rkdsidngsn iikivgnhsn kgaannaldv
       61 lsgqaagvnv tsngldrmam lnsvrvrgtt siiggndplv lidgvtsdvl tlstiypadi
      121 esfrilknaa etamygsrga sgvievktkk gtgrgfqisy egnvgfeqmy khlemlnaae
      181 yvatakalgi ycnnggfntd nykvitrtgm vnnhylafsg gtpqsnyras fgvmdhntii
      241 kkmdynvfva kvdvtqkafn drltgefgvf gssfknhdif dtqmlfysaa cqnptfpagt
      301 dehgnwlkne sathinppgi lleekndskd lnfdahikls ydfnknwhvs tfgsylygst
      361 engqfcptwv waqgnvyrge fkkeewlgnv sldfnkefgi hkvsagvsse yrklrktafw
      421 vyakgiptnd fhydnlgata arpyggtest yedqslasvm gsitynlldr ytlavnargd
      481 gssmvgdnnt wgffpsvslt wdmkkesfla nikplsmlkl rtglgqagnl ggisayttmn
      541 tvrqtgivpv kssptvtlgm vrnnnpdlkw etkttfnlga diglfanrlm ltaeyyyskt
      601 tdmlyayevp vppfayntll anigsmsnrg felglsvqpi sqkdldlnin mnlsfqsnkl
      661 islsgdykgm smsaanitai gsldgagqng gdnnvvyqiv gqplgvfylp hckglvknen
      721 gsyfydiedl dhngkvdlsd ggdryiagqa tpkvilgsni sfryknyyvs iqmngafghk
      781 ifngtglayt smacfpdynv lkdapkkniv dqrvsdywle kgdylnfehl tigynvplrs
      841 klirslrvsc nisnigtitg ykgltpmins yvvnstmgid dkrnyplyrt yslglsvqf
//
LOCUS       WP_094401961             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Enemella
            evansiae].
ACCESSION   WP_094401961
VERSION     WP_094401961.1
KEYWORDS    RefSeq.
SOURCE      Enemella evansiae
  ORGANISM  Enemella evansiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Enemella.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Enemella evansiae"
                     /db_xref="taxon:2016499"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52922
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpaelr pgetmvaatp ktvgqlialg hqvvfeagag raarlpdeqy aaagaelada
       61 devwrsdlvl kvraplpeel pqlregqlla clldparspe llaelaarge talsldavpr
      121 israqaldvl ssmaniagyr avieaansyg sllngqvtaa gkvpparvfv vgagvaglaa
      181 igtasslgaq vyafdvrpev aeqvesmgae fthlpgaqda eassdgyake ltadqeqrta
      241 elyadqsaaa divittalip grpaptlita amvaamkpgs vivdlaapng gnceltvrdq
      301 vvvsdngvii igytdlagrl ptqasqlfgt nlvnlvkllt pakdgqlvld lddpvqrsml
      361 vadrgevtwp pppvtvsaap apvpaakpah evepvrrgrg parvalgtlg vllavglaft
      421 psafllyfti falavvvgyy visnvthalh tplmtetnai sgiiligall qigsdnlvvr
      481 ilafialtva sinifggflv anrmlamfsk d
//
LOCUS       WP_094402177            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094402177
VERSION     WP_094402177.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120714
     Region          47..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkryiiygls limfsaapaf aqdeadedap sakreqpakp rkqyptrvvk grvlnattnn
       61 pvsgamirta evdgystlsh sdgtyelkvp lfatslqvsa pdlnvakigl vrgeeqrdvl
      121 lypetfskey tdgtnvlase sttdfrysna vtiedevqkr lgadvrvinr ngtpgiggvm
      181 fmnginslni naqplivvdg vifdqqfgrt mlhegfyndi lsnispsdie kvtvlrngta
      241 lygakgangv ilietrrnhs matritasis agvtlepkfi dvmnasqfks yasdllsttn
      301 ttitnfkfln edpnyyyypq yhndtdwknl vyrtaitqny sinveggddv anynlslgyi
      361 snqsvlknng mdrlnirfnt dikltnefsv rfdasfanqt rnlrndgapa nydegtptst
      421 aflayakspm lspyayangi lsdsylditd esyldealae ypnynyklan pvavneygea
      481 enknrfensm initvtpkyq fnphlslseh fsynlvntne kfyipvngvp syyvssvnav
      541 renetrslfs kqnsvmsdtr vdwsnsygah avhvfggari nwesytlnsq wgyntgsdkt
      601 pfmssallna stvgsndswn svawyaqaey nylqryylqa nltaeassrf gadaenslka
      661 fdaawgifpg vqaswvvsne pwfakvrgid ylrlnvgydv sgnddidyfa arsyfsavkf
      721 ldaisgisfe nigntrlqwe ttkrfnvgfe tnlinnrlnl rfnyfnsktd hlltyqalgf
      781 ltgieknwgn ggslknegfd vtavgklvam ksfqwelgls vghyknkits laddatyfds
      841 svygatirte vgkpanmfyg yvtdgvfsts eeaaaaalyv lgdngvdkny fgagdmrfvd
      901 lngdhkideh drtfigdpnp diygnifttl aykrfrldvn fnyslgndvy nymrsqlegg
      961 srfmnqttal trrwqtegqv taipkatfqd pmgnsrfsdr wiedgsylrl ktvtlsyrlp
     1021 vnstllqgfe fwvqannllt fskylgsdpe fsmtsnvigq gidlgqlpqs rsfvagvkin
     1081 l
//
LOCUS       WP_094402184            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094402184
VERSION     WP_094402184.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123830
     Region          27..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnslrhivl sllcllamga taqitavhgt vsdefgeitg asvceidgsg riieatvtdi
       61 ngnfsmkirn pkdkirfsyv gckaqtlpid kdeyiitlks etnlkevtvv akrrlngggl
      121 aipereisya tqtistkefe glgmntidea lqgriagldi vsvsgnlgag ttmrlrgsss
      181 istltnanpl ivvngntwnv dmsnfdvsna ndeqfaqlln vnpediseit vlkdaaatai
      241 ygsqgangvi eiktkrgtrg aprltyslrl tgtyqpqgyk llsgddytml lkeayfnpeq
      301 sdvaanipei nydptfseye qynnntdwqd avtqvglrqn hylsvtggge katfrisggf
      361 dhetgsvikq qldrfstrvc ldyfvsdrik istnfsmtyt knqrnydnll alaykkmpnm
      421 siyeqdpitg edtdkyyqml qtapdvfkdd qrvyvnpvas anlaknddrt yditpefeln
      481 yhllgldees hqlnwqgrvy mnifneyvdm yypselvtts wkdgvnssya gstksvafnt
      541 kqtltyiphf nnkdhslmmm grfeltsgss sgqgtngngl psgvtspdag glitglsssy
      601 sqwrsmyytf sahyaykgry mldfsvradg ttkfgpdrrw gyfpavsarw niidepwmkg
      661 aqswlsmlsf rpswgkvgnq psqdylyesk ygstdkyldm samrpinikl tdlrwetkst
      721 wdigmdlglw ndkvvftlew ynaktsdmlm pnvripsnsg yytkayanvg smrnigwefn
      781 intnhliqag kfwadinatf annkneilem denvlktlnt efnfdgnrvt lqrvqlnnpf
      841 gaiygfrfkg vyqyqyetfa dmsdaeraef lasgktapva ltadgrvild dagdpvrmmy
      901 nytndgtgkn ykfkggdaiy edinndgnin aldivylgss lpkltggfgf nlnynrwkln
      961 aqfnyrlgnk ilnlarldte aminnnnqsq avnyrwrkeg ditnipramy gsdtnyntlv
     1021 sdrfvedgsf lrlnylqlsy sfdpkavkka iglnglrfya sannlfcltk ytgvdpeigy
     1081 gsygaatdtg qtprsksytl gitvdf
//
LOCUS       WP_094402955            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-122].
ACCESSION   WP_094402955
VERSION     WP_094402955.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-122
  ORGANISM  Prevotella sp. P3-122
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Prevotella sp. P3-122"
                     /db_xref="taxon:2024223"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122610
     Region          24..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrlsvila slflfvgmaf aqnkisgtvv saedgepvig asvmiqgtkv gtvtdvegkf
       61 tlssnranpm leisyigmvs qkvkgssnmv vtlqsdskti devvvtgmvk vdkrlfsgst
      121 skidaasakl dgvadisrsl egkaagvsvq nvsgtfgtap kirvrgatsi ygsskplwvv
      181 dgvimedvve vsadqlssgd antlissaia glnsddiesf eilkdgsats vygaramagv
      241 ivvttkkgka gqarisytge ytmrlkpsys tfnimnsqdq mgvyqelqqk gflnfaeisn
      301 aansgvygkm yellntydpa tgqfglantd earaaylrda eyrntnwfge lfsnsiqhnh
      361 svsitagtek aqyyasvsam ydpgwynksa verytanfna nyklskklna giignasyrk
      421 qeapgtisat tnpvtgevsr afdinpysys lnssraldpn tfytrnyspf nifhelenny
      481 idlnvvdfrm qaslsykpit kveltalgav kyaattsehn ikdnsnqaqa yramgnstir
      541 knnnylytdp ddiyalpvti lpnggildrt dnrmfgydfr asaayndvfn edhivnlyga
      601 meinsverhs twfrgwgmqy smgetpsway avfkksqeqg adyyslanth ersaafvgvg
      661 tyswkrrysi tgtyryegtn rmgksrsarw mptwnvsgaw nvheeswfnk lqpalsnltf
      721 klsysltadr gpssvtnsrv vimaenpwrp sagdnessly iaqlannelt yekkhelnfg
      781 idagflnnri nftfdiysrr nydligvint lgtggeprkf gnvakmksng veialntvni
      841 ktkdftwttd liyshmhnev telntlnrmy dyisgsgftm pgypqrslfs ipfmglnneg
      901 lptfldqdgn vsvtginmqe ydperlkflk yegpvdptdv gslgnvfryk gvtlnlfity
      961 sfgnvvrldp vfsssysdlt atpkefkdrw vkpgdenftn vpviaskqql nniaflsray
     1021 qaynysterv akgdfirmke islayefpks itqplrlsnl slklmatnlf liyadkklng
     1081 qdpeffnagg vanpmpkqft ltlklgi
//
LOCUS       WP_094409631             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Elstera
            cyanobacteriorum].
ACCESSION   WP_094409631
VERSION     WP_094409631.1
KEYWORDS    RefSeq.
SOURCE      Elstera cyanobacteriorum
  ORGANISM  Elstera cyanobacteriorum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Elstera.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Elstera cyanobacteriorum"
                     /db_xref="taxon:2022747"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39374
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,285..286,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkerr pferrvaatp etvkkfiglg asvtvetgag dgaffldday aaagatvaad
       61 aatalagadl vlkvrrplap gegevdelal lkpgqtvlgl ldpyggqaea laatgvnava
      121 mefvpritra qvmdvlssqa nlagykavie aasvyahgfp mmmtaagtvp pakvlvmgag
      181 vaglqaiata rrlggvvsat dvrpatkeqv eslgatfvav ideefqqaqt aggyakemsa
      241 aykekqaali aetikkqdiv ictalipgrk aptlvtaemv asmkpgsviv dlaveqggnc
      301 dlseyaqtvv khsvsiigha nmpsliatda salyarnlla yvtplidket kalvlneede
      361 ivkasliakg galvhpslvk paa
//
LOCUS       WP_094413582            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            cyanobacteriorum].
ACCESSION   WP_094413582
VERSION     WP_094413582.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium cyanobacteriorum
  ORGANISM  Flavobacterium cyanobacteriorum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Flavobacterium cyanobacteriorum"
                     /db_xref="taxon:2022802"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113048
     Region          25..1023
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskftwima lfmvltfnls faqektvtgt vsddagqplp gvsilvrgtn kstttdfdgn
       61 ysisvsvgqv lefsfvgfts qsatitaasg vinikleegq vigvivkday rtvserkatf
      121 atttisaeaf enrgnasiiq smqgqiagls igtgsgqpga dsaiilrgvg tingnfeplf
      181 ivdgvpvded gfrsinpndy asittlkdaa atsiygnrgs ngvivlttkr gsynqdlkfr
      241 ytsqfgynel qpvnidlmts rellqfqkrs gqglgstlsd aeidvlsrqa ntnwsdiffr
      301 kgttklhdls msvgsantnn ftsfsyfeqd gifintnlkr ftlrnnftgr sqdqkfeysl
      361 nfnanfsrqs gldgagtnsi ffapfraalq glpylspyda ngnitrdggi apgntdaita
      421 dnapyvllns slmntdiede fklitglnak ytfmknvtag mqlgldysqf kalerihpes
      481 ilgpfqangt nttqfgglqq estsrdfrfn slftlnynnt fadahtidlt gyveyiknhf
      541 dsfgfvqrgl dprlvgtgaa fidgetvegt lrpyiptvss gkaeeglfsy fanfdydykg
      601 kygfnatvrr dnsfrfiden kwatfyslgg rwnideesfm eklpfvdqlk lrasfgttgn
      661 qrinngsysa lnftrnlytq sggyngtpgt vpgqianpdl rwevteqtnv gldfglfgnr
      721 lsgtvdvyrk ftrdlfqstp isavnattdi dtntgalenk gvelflkyvi ydkngwnisv
      781 dantaynqnr mrdlpdsyng iiqptgsatt legyplntfy vvryagvnps ngnalfytrd
      841 ggltetirde drvntgkssl pvwtggfntr vsykgfefst qwsyvadiyr nnldyadlee
      901 tnlvndgtnr avsagtawqn pgditsvprv gnqynsvdyi nstdryleda sflrlrnvll
      961 gynfdkkile klpfsgvrly iqaenlvtft syrgwdaesn frttdrgqyp tpkiytlgav
     1021 vnf
//
LOCUS       WP_094416208             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodopirellula sp. MGV].
ACCESSION   WP_094416208
VERSION     WP_094416208.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula sp. MGV
  ORGANISM  Rhodopirellula sp. MGV
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Rhodopirellula sp. MGV"
                     /db_xref="taxon:2023130"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54108
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkvgipkevi dgerrvaatp dttrrliekl gfevlverna gaaasfpdaa yenagailcs
       61 dateiwgnae ivlkvrgpse helgqlrngq tvvgflapaq nedllhriae rganalaiea
      121 vprisraqkm dalssmania gyravveaag lfgrfftgqi taagkvppar vlvigagvag
      181 laaigtargl gaivrafdvr pevadqvksm gaeflylqfp sdenggtsgg yaktmskefi
      241 daemalfadq ardvdiiitt alipgkpapt littsmvesm rhgsvvvdla aeqggncevt
      301 vpgkviqheg vhvvgyydlp srlahtssql ygtnlfhlld emggaekfri dmddvvirsa
      361 tvvhqgqvtw ppppvavsaa apakpeegqq ktpaiakqrg vidvvltiag iallamlvmt
      421 qdrgvltdft vfvlacivgw qviwnvtpal htplmsvtna isgiiivggm vqagtdhpva
      481 svlgaiaifv atiniaggfl vtqrmlkmfr kldg
//
LOCUS       WP_094423091            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P4-51].
ACCESSION   WP_094423091
VERSION     WP_094423091.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P4-51
  ORGANISM  Prevotella sp. P4-51
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Prevotella sp. P4-51"
                     /db_xref="taxon:2024228"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120852
     Region          115..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnskqskllg icllvtlmfs alsmsaqtvt ktfsneslrn vlkeverqtk msviykvdev
       61 nasqkvtatf hatpvrdvlt kvlgshlgfk idhkmitifk reakpaakdp qapkktvkgq
      121 vldengepvi gatvrskatg aavvtdldgn ftisaeegsk ievsylgyqp ksvtakgdnl
      181 tvniaqdekt lnevvvtalg ikkeskalty nvqqlknsdi tgvkdanfmn alagkvagve
      241 inasaagigg gvkvvmrgnk singnnnaly vidgipmpsl qanqptdayh gdaqtgdaas
      301 mvnpddiesi svlsgaaasa lygsdaangv vmittkkgtv gkvrvsysnn tsffspfvtp
      361 efqntygqtg ngtfsswgsk latpssydpl dffqtgynvg nsvtfsvgse hsqtfvsast
      421 tnaegivenn emsrynftir nttdflkdrl hldlsamyms vkeqnmisqg fyfnpivpvy
      481 lfpagddirk ytpfeqydpe rnfktqywpf gnqglsmmnp yweinrdiae nhkdrfilsa
      541 gltfdiakgi tlsgrakmdk tsgiyekrya astdplfage ygayyrtndn trqiygdail
      601 nidkyfgdfs ltanlgtsik dvetsytyvg gflnvannft lnavnransh mdadpalnyh
      661 hqvqsvfata qvgyksmvyl dltarndwds flgntqyrnk gffypsagvs ailtemipgl
      721 kskvlsflkl rgsysevgnt pekfyaltry tysnaapstt syypnnnlkp ertkawelgl
      781 qanlwqdkvn lnvslystrt tdqfflpels assgysklpi nggridnkgi easltlnqpl
      841 gpvkwsstft ytlnknkikq llapteltla ngnkvnvsld gmdmlnlgsv kvrlteggsm
      901 gdlyvtipkm dehgylivdy tsrniagvde gkyvyagnvn pkynmgwrns fswkgidlgf
      961 lisarvggrv ssitqgymdy fgaskttaea rdlggalvng yripaqdyys kigpsvgayy
     1021 iysatnvrls elsvgyslpi skwvpwienl rlaftgrnll mfyckapfdp eltastgtyf
     1081 tgidnfmmps lrnlgfsvkv df
//
LOCUS       WP_094427480             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Enemella
            evansiae].
ACCESSION   WP_094427480
VERSION     WP_094427480.1
KEYWORDS    RefSeq.
SOURCE      Enemella evansiae
  ORGANISM  Enemella evansiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Enemella.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Enemella evansiae"
                     /db_xref="taxon:2016499"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52994
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpaelr pgetmvaatp ktvgqlialg hqvvfeagag raarlpdeqy aaagaelada
       61 devwrsdlvl kvraplpeel pqlregqlla clldparspe llaeladrge talsldavpr
      121 israqaldvl ssmaniagyr avieaansyg sllngqvtaa gkvpparvfv vgagvaglaa
      181 igtasslgaq vyafdvrpev aeqvesmgae fthlpgaqda eassdgyake ltadqeqrta
      241 elyadqsaaa divittalip grpaptlita amvaamkpgs vivdlaapng gnceltvrdq
      301 vvvsdngvii igytdlagrl ptqasqlfgt nlvnlvkllt pardgqlvld lddpvqrsml
      361 vadrgevtwp pppvtvsaap apvpaakpah evepvrrgrg parvalgtlg vllavglaft
      421 psafllyfti falavvvgyy visnvthalh tplmtetnai sgiiligall qigsdnlvvr
      481 ilafialtva sinifggflv anrmlamfsk d
//
LOCUS       WP_094434216            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Prevotellaceae].
ACCESSION   WP_094434216
VERSION     WP_094434216.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122915
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkllillv nifllcggvl aqtkvtgtvv sqedgepiig asiiiqgqrs gtvtdadgkf
       61 slsvpagkki svsyigmetq tlapkakmsi slrpsaelee vvvtgmqktd rrlftgatdr
      121 vnaedailng iadisrsleg rsagvsvqnv sgtfgtapki rvrgatsiyg sskplwvvdg
      181 vimedvtdid sdalssgdpe tlissaiagl nsddiesfqi lkdgsatsiy garamagviv
      241 vttkkgkagt ahinytgeft mrlkptygnf nilnsqdqmg iyrelydkgw lnlsntlngs
      301 dygvygkmye lintynpstg afalanttea knaylanaef rntdwfdelf stsiqqnhsv
      361 smsggtaksn yyasvsamtd pgwykqskvd rytlnmnvnh kildnlslni igsgsyrsqr
      421 apgtlsqdvd vvsgnvkrdf dinpysyaln tsraldpdty yhsnyaafni lheletnfid
      481 vnfldakfqa elkykpikdl eiavlgalky tttsqeykil dnsnqaeayr amdntiirda
      541 nkylytdkdv lyslpisvlp eggmykrtdn rmrdynfrat anyvhtfadi hyvnlfggme
      601 tteiqrsrsw fngwgmqyak geipyytyqf fkksleentd yyslsntnsr saaffanaty
      661 gydnryvlng tvryegsnam gksrsarwtp twniagswnv dqekffkawe ptishlklka
      721 sysltatppp tsytsstnvf kafnpyrift sdketgiqls dlenseltye kknefnfgve
      781 agflndrinv sfdiytrkny deigpvatqg iggqiirwan aadmkshgee lsisstnikl
      841 kdfswitslv yshtktkitn lasqdrvidm itnfggrrvg ypvrslfsip fagldenglp
      901 tfyneageit tdninfqerd kvdylkyegp tdptvqgslg nlfkykgftl nlfitysfgn
      961 vvrldpvfsa tyndlssmtk efknrwmvpg dekktnvpvi lsyaqytnns qlrygynayn
     1021 ysdvriakgd firmkeislq ydfpknwikp ltnlslklqa tnlfliyadk klngqdpeff
     1081 rsggvsapvp kqftatlkvg f
//
LOCUS       WP_094435195            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-50].
ACCESSION   WP_094435195
VERSION     WP_094435195.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-50
  ORGANISM  Prevotella sp. P5-50
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Prevotella sp. P5-50"
                     /db_xref="taxon:2024217"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123283
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmmfla glflslgmaf aqtkvtgtvi sqeddqpiig asvlvqgqrs gtvtdvdgkf
       61 tisvpsgkki tisyigmepq tvtpkngmtv tlrssaelqe vvvtgmqktd rrlftgsttk
      121 vdaekakldg vadisrsleg raagvsvqnv sgtfgtapki rvrgatsiyg ssrplwvvdg
      181 vimedvtevd adqlssgdae tlissaiagl naddiesfqi lkdgsatsiy garamsgviv
      241 vttkkgksgq trinytgeft mrlkpsysnf nimnsqeqmg iykeleangl isfgrtyras
      301 ssgvygkmyq lmntynpatg sfmlsqteea knaylreaem rntnwfdelf snaiqqnhsi
      361 smstgtdkaq yytsfsimdd pgwteqskvr rytasinamy nvnkkvtlnm ianasyrnqr
      421 apgttsqsvd avtgnvsrdf dinpysyain ssraldpnef ytrnyapfni hnelannfmn
      481 ldvvdlkyqa elkykpikkv eltvlgayky stttqaneih ensnmaqsfr amddatirdn
      541 npwlytdpdk pnskpvsvlp vggfyretky kmtswdfrat aqyndvfned hivnlyggme
      601 indtqrsrsy fngvgmqydm gylgsydylf fkqsaeqnam yyslsnsygr evsffataty
      661 swkgryving ttryegsnrl gksrsarwlp twnvsgawna heepwfqktf knalthatlk
      721 asysltgdkp avtnsqaiiq sfnpwrpfas dkesglniyd fanpdltyek khelnigvdl
      781 gflnnrlnvq fdwyrrnnyd ligmrttngt kgtinefanv asmrshgeel sissknivsk
      841 dfkwntdfif shvktkitel dnrsrlidmv tgtgfakkgy ayrslfsfdf kglnangipq
      901 vvnesgevvt sdiyfqsrdi dylvyegptd ptitgslgns ftyknwhlni fatyafgnvv
      961 rldpafyasy sdldampkef knrwtvsgde nkttipaipd lrqlqadtql syafnaynrs
     1021 tdrvakgdfi rmkeisvsyd fpqtwlnalk lksasiklqg tnlfliysdk klngqdpeff
     1081 ntggvavpma rqftctvrvg l
//
LOCUS       WP_094439271             536 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Alicycliphilus denitrificans].
ACCESSION   WP_094439271
VERSION     WP_094439271.1
KEYWORDS    RefSeq.
SOURCE      Alicycliphilus denitrificans
  ORGANISM  Alicycliphilus denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Alicycliphilus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Alicycliphilus denitrificans"
                     /db_xref="taxon:179636"
     Protein         1..536
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55552
     Region          11..536
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtsptppvq rigvpretfp gekrvatvpd vveklvklgf tvavesgagd aanfsddayr
       61 aagaevqpda aalwaasdiv lkvrppssee talmreggtl igfvwpaqnp dlmqqlaakk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rqmyatqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti igytdlasrl akqsstlyat nllrlteelc kakdghavvn
      361 meddairglt vikdgavtwp applkappap apkpaaaapv eqkkgghghg stgplpattl
      421 avifavaavl fwfigayapa aflghftvfv lacfigymvv wnvtpalhtp lmsvtnaiss
      481 iiaigalvqi appeagasgr pdglilwlaf aalvltavnm fggfavtrrm lamfrk
//
LOCUS       WP_094439353            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P4-98].
ACCESSION   WP_094439353
VERSION     WP_094439353.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P4-98
  ORGANISM  Prevotella sp. P4-98
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Prevotella sp. P4-98"
                     /db_xref="taxon:2024219"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123254
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmmfla glflslgmaf aqtkvtgtvi sqeddqpiig asvlvqgqrs gtvtdvdgkf
       61 tisvpsgkki tisyigmepq tvtpkngmtv tlrssaelqe vvvtgmqktd rrlftgsttk
      121 vdaekakldg vadisrsleg raagvsvqnv sgtfgtapki rvrgatsiyg ssrplwvvdg
      181 vimedvtevd adqlssgdae tlissaiagl naddiesfqi lkdgsatsiy garamsgviv
      241 vttkkgksgq trinytgeft mrlkpsysnf nimnsqeqmg iykeleangl isfgrtyras
      301 ssgvygkmyq lmntynpatg sfmlsqteea knaylreaem rntnwfdelf snaiqqnhsi
      361 smstgtdkaq yytsfsimdd pgwteqskvr rytasinamy nvnkkvtlnm ianasyrnqr
      421 apgttsqsvd avtgnvsrdf dinpysyain ssraldpnef ytrnyapfni hnelannfmn
      481 ldvvdlkyqa elkykpikkv eltvlgayky stttqaneih ensnmaqsfr amddatirdn
      541 npwlytdpdk pnskpvsvlp vggfyretky kmtswdfrat aqyndvfned hivnlyggme
      601 indtqrsrsy fngvgmqydm gylgsydylf fkqsaeqnam yyslsnsygr evsffataty
      661 swkgryving ttryegsnrl gksrsarwlp twnvsgawna heepwfqktf ktalthatlk
      721 asysltgdkp avtnsqaiiq sfnpwrpfas dkesglniyd fanpdltyek khelnigvdl
      781 gflnnrlnvq fdwyrrnnyd ligmrttngt kgtinefanv asmrshgeel sissknivsk
      841 dfkwntdfif shvktkitel dnrsrlidmv tgtgfakkgy ayrslfsfdf kglnangipq
      901 vvnesgevvt sdiyfqsrdi dylvyegptd ptitgslgns ftyknwhlni fatyafgnvv
      961 rldpafyasy sdldampkef knrwtvsgde nkttipaipd lrqlqadtkl syafnaynrs
     1021 tdrvakgdfi rmkeisvayd fpqtwlnalk lksasiklqg tnlfliysdk klngqdpeff
     1081 ntggvavpma rqftctvrvg l
//
LOCUS       WP_094440193            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P4-98].
ACCESSION   WP_094440193
VERSION     WP_094440193.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P4-98
  ORGANISM  Prevotella sp. P4-98
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Prevotella sp. P4-98"
                     /db_xref="taxon:2024219"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122956
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkllillv nifllcggvl aqtkvtgtvv sqedgepiig asiiiqgqrs gtvtdadgkf
       61 slsvpagkki svsyigmetq tlapkakmsi slrpsaelee vvvtgmqktd rrlftgatdr
      121 vnaedailng iadisrsleg rsagvsvqnv sgtfgtapki rvrgatsiyg sskplwvvdg
      181 vimedvtdid sdalssgdpe tlissaiagl nsddiesfqi lkdgsatsiy garamagviv
      241 vttkkgkagt ahinytgeft mrlkptygnf nilnsqdqmg iyrelydkgw lnlsntlngs
      301 dygvygkmye lintynpstg afalanttea knaylanaef rntdwfdelf stsiqqnhsv
      361 smsggtaksn yyasvsamtd pgwykqskvd rytlnmnvnh kildnlslni igsgsyrsqr
      421 apgtlsqdvd vvsgnvkrdf dinpysyaln tsraldpdty yhsnyaafni lheletnfid
      481 vnfldakfqa elkykpikdl eiavlgalky tttsqeykil dnsnqaeayr amdntiirda
      541 nkylytdkdv lyslpisvlp eggmykrtdn rmrdynfrat anyvhtfadi hyvnlfggme
      601 tteiqrsrsw fngwgmqyak geipyytyqf fkksleentd yyslsntnsr saaffanaty
      661 gydnryvlng tvryegsnam gksrsarwtp twniagswnv dqekffkawe ptishlklka
      721 sysltatppp tsytsstnvf kafnpyrift sdketgiqls dlenseltye kknefnfgve
      781 agflndrinv sfdiytrkny deigpvatqg iggqiirwan aadmkshgee lsisstnikl
      841 kdfswitslv yshtktkitn lasqdrvidm itnfggrrvg ypvrslfsip fagldenglp
      901 tfyneageit tdninfqerd kvdylkyegp tdptvqgslg nlfkykgftl nlfitysfgn
      961 vvrldpvfsa tyndlssmtk efknrwmvpg dekktnvpvi lsyaqytnnk qlrygynayn
     1021 ysdvriakgd firmkeislq ydfpknwikp ltnlslklqa tnlfliyadk klngqdpeff
     1081 rsggvsapvp kqftatlkvg f
//
LOCUS       WP_094440345             932 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P4-98].
ACCESSION   WP_094440345
VERSION     WP_094440345.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P4-98
  ORGANISM  Prevotella sp. P4-98
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Prevotella sp. P4-98"
                     /db_xref="taxon:2024219"
     Protein         1..932
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104780
     Region          27..928
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrhiykglal caslvagstg vyaqeaetdt ldkvqvafra vdkqdlmggv svidmkemak
       61 knyatssiey ienvvggvng glwgygdylv vvdgmvrdan nvlpqeidqv tllkgsaavv
      121 lygpraakgv lqittkrgqm gdlrinahad msigtpisfp kylgsaeyms yynqarindg
      181 ydknysdeei ynfasgknpy rypnfdmyds qyrrdfttry egivevtggt ervkyyttlg
      241 yyrnnellkv gntkdnftsr ffvrgnmdvk fndwlsakad anvtfydafa aktdwwgqaa
      301 tlrphlvspl ipisfiestd kislgsvmns nylqngfffg gtqsnptnpy adafaagdnk
      361 fvsrqfqfnt efdinlaalt qglmfrakyg idyastynqg ysnsyatfsp twtnyngpdm
      421 igsitqyged kktgqqyisd ssyrytynvs gqfdwartfd gvhnvfamal anawqtqrng
      481 hyhrttnanl glqlsynydh tyyfdfsaam pystklpagn raaisptvtl gwrptkdvlk
      541 dtfvddlmvn vsggiinqdi ditasdnedg yfmyktilqt ggwyswgdle ggaatefqrg
      601 dnydmgfvkr kefsvglrgs lldklitfdv nfftskmdgm ltratslfpn yftqtgypts
      661 siipyvnyni dkrigvdfsv ygnkkigevd lslgvsgtwy kstadkrden iefdylsaig
      721 rplnglwglk sdgffnsqee idaapeqtfg evkpgdikyv dmnndgkidd ndrvflgrwd
      781 tpfrmglnlt akwknftffa mgnlwlggha mksdsywwvr gtgkysevvr nawtpetaat
      841 atyprltttn gdnnfrysdf wmystdrfnl srvqityalp snlfegsfvr gidvyvggsn
      901 lltiakerki letkiggapq mrsynigfra sf
//
LOCUS       WP_094442261             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium sp. PC23-8].
ACCESSION   WP_094442261
VERSION     WP_094442261.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. PC23-8
  ORGANISM  Janthinobacterium sp. PC23-8
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium sp. PC23-8"
                     /db_xref="taxon:2012679"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38594
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaarh qivvqagagl hasipddaya aagaqiasaq
       61 eaygcaivlk vrapdaaera lmaagtvlig mlnpfdadni aamagaglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeer eiakgaggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvvkhgvh ivgepnlatl vaadasalya rnvldflkli idkddmllid redeiikasl
      361 vctggdvlrk
//
LOCUS       WP_094446234            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Prevotella].
ACCESSION   WP_094446234
VERSION     WP_094446234.1
KEYWORDS    RefSeq.
SOURCE      unclassified Prevotella
  ORGANISM  unclassified Prevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="unclassified Prevotella"
                     /db_xref="taxon:2638335"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123270
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmmfla glflslgmaf aqtkvtgtvi sqeddqpiig asvlvqgqrs gtvtdvdgkf
       61 tisvpsgkki tisyigmepq tvtpkngmtv tlrssaelqe vvvtgmqktd rrlftgsttk
      121 vdaekakldg vadisrsleg raagvsvqnv sgtfgtapki rvrgatsiyg ssrplwvvdg
      181 vimedvtevd adqlssgdae tlissaiagl naddiesfqi lkdgsatsiy garamsgviv
      241 vttkkgksgq trinytgeft mrlkpsysnf nimnsqeqmg iykeleangl isfgrtyras
      301 ssgvygkmyq lmntynpatg sfmlsqteea knaylreaem rntnwfdelf snaiqqnhsi
      361 smstgtdkaq yytsfsimdd pgwteqskvr rytasinamy nvnkkvslnm ianasyrnqr
      421 apgttsqsvd avtgnvsrdf dinpysyain ssraldpnef ytrnyapfni hnelannfmn
      481 ldvvdlkyqa elkykpikkv eltvlgayky stttqaneih ensnmaqsfr amddatirdn
      541 npwlytdpdk pnskpvsvlp vggfyretky kmtswdfrat aqyndvfned hivnlyggme
      601 indtqrsrsy fngvgmqydm gylgsydylf fkqsaeqnam yyslsnsygr evsffataty
      661 swkgryving ttryegsnrl gksrsarwlp twnvsgawna heepwfqktf ktalthatlk
      721 asysltgdkp avtnsqaiiq sfnpwrpfas dkesglniyd fanpdltyek khelnigvdl
      781 gflnnrlnvq fdwyrrnnyd ligmrttngt kgtinefanv asmrshgeel sisskniisk
      841 dfkwntdfif shvktkitel dnrsrlidmv tgtgfakkgy ayrslfsfdf kglnangipq
      901 vvnesgevvt sdiyfqsrdi dylvyegptd ptitgslgns ftyknwhlni fatyafgnvv
      961 rldpafyasy sdldampkef knrwtvsgde nkttipaipd lrqlqadtql syafnaynrs
     1021 tdrvakgdfi rmkeisvsyd fpqtwlnalk lksasiklqg tnlfliysdk klngqdpeff
     1081 ntggvavpma rqftctvrvg l
//
LOCUS       WP_094447875            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            bryantii].
ACCESSION   WP_094447875
VERSION     WP_094447875.1
KEYWORDS    RefSeq.
SOURCE      Segatella bryantii (Prevotella bryantii)
  ORGANISM  Segatella bryantii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Segatella bryantii"
                     /db_xref="taxon:77095"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122150
     Region          34..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mefkvkklqq lkrdlilltg llvqlsawaq diigtvrdah tgepiigavv svkgksankl
       61 tsvtdidgkf rlkvdntptv llisytgynp eevdvyeltn egidvnlsen lnhlqevvvv
      121 gygqqkksdl tgaltqinse tlterpvqnv lqalqgkasg vqvssnnrpg elgsvlirgs
      181 rslladnapl yvvdgipfta gslsdiapsd iesieilkda sataiygsrg angvilvntk
      241 kgakgkvtin ydgtfswstl hsltdwmsag elldykrqaa itggtyngsy gtapdpdrdk
      301 vlfigteewc drviksgyqy dangnvvlrd ateaekaagy adqvpvydss kllntdwadl
      361 atrtafsqnh qvslsagsdk sklyislgyl dqqvpmkdqd ytrvtanvng siqatqwlnv
      421 glnlnaaysl knygivqnss navakdsygl alntlpwvpa ynedgsylig stsgsaghni
      481 lsdidesene yryyatnlss yaeldfghiy aplqglkwrt nfgaqfrssr ygsyygenws
      541 npyeivhtaa gvaynqhses lswtlenlif yekditpdhh igltllqsae ryrteslnvr
      601 aygtvyptak wydvgdsddq qttygsgytn wtrasymarl nyafknryll tltgrkdgas
      661 vlaegnkwdf fpsaafawka seesflrdvk wldqlklrag ygvtgnssvs aystsgsvts
      721 efasipfgig gnvsnttgak pdvmpnynlk wertssfnlg vdfsvfrgrl ngsidfytsr
      781 tsdvimnrsi pvitgyaqir snvgetqnrg felalsstni qtrnftwqtd lsfstnheei
      841 vslvngkedm aannwfigea lnvyydykyd riwqnteeda llraaysang ltflagqyki
      901 kdqplilvde ntagaksfty ngttyyyenn gfgtfdeddk vvynkspkwe agltntfkyk
      961 nwtlstyiyg rfggwyyglt qtigrrvend twsetntdaa faqpttatrt tdydyvrnys
     1021 rsdmvlvkni glsytfkrrq lrslglgsae vyaqvlnpfi fggelvkagi npddvtgwts
     1081 sdhiggqtnn taitksfvlg vklgf
//
LOCUS       WP_094448187             956 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            bryantii].
ACCESSION   WP_094448187
VERSION     WP_094448187.1
KEYWORDS    RefSeq.
SOURCE      Segatella bryantii (Prevotella bryantii)
  ORGANISM  Segatella bryantii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 956)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 956)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 956)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..956
                     /organism="Segatella bryantii"
                     /db_xref="taxon:77095"
     Protein         1..956
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106198
     Region          50..955
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktknifmlt llagttlpam aqhdivdsva ykdqkvdiga nrlfsreqst gavsvisnkd
       61 vnkrgarnig nnilgsgsgl vsldgsglfh aqnptfyirg iqsssgstpl iivdgverai
      121 envvaedves vqilkdaaat alygykgang vlivttkhgd ynsksitfsy dhvfsylnnk
      181 pkmadaatya savneayrnq geasvysdav inaykngtnp lyypnvnwad etfrdvshnn
      241 rfnlefkggs nnfryytnvq lltnkgfvkn fendgystqn kytrgtlrsn mdidlgpktk
      301 lhthlygllt eqsqpgsqad lwsmiyqlpa nafpikatsa vwggntqytt nnpvaqsqaa
      361 ayyknhqral yadllleqdl ssiteglkgs aqlgydtwsn lyenhsktyr ysyyavnnng
      421 dvvpdgegal aavegsdsrm gtasnndswi rrcvwnlaln ydrtfaekhn vygqlkydye
      481 yndqtgtnts iyrhnislfg hygydnrylf dvafvesasn rlapgskwaf sptfsaawni
      541 sneafmknvk cidflklrvs wgnkqldvlp gdnvwtyynq fylmdaasyp fdatytgtqw
      601 gntylgtams lsqgheqssk fnlgldatlf gslnlsadvy yqnrydiwys tagsyssvfg
      661 ldapyenvgr itskgfefsa dyskklnknl tfsvggsltv nktivnrqae spqlfantss
      721 tgkrygqafg yiangffqks ddldgngiis eaemkqlgyp iqnantiypg dvkyvdltgd
      781 dkidsndrqa igysttapdl yynfhlgvey kgfgvdamfq gvgkwtgfkt tnglyrsava
      841 tntlsqylye nswsaergnt dqalfprlst vsnanndvns tlnmfdrsyl klryveayyy
      901 lpktvldktn fiknvklyvr gtdlfttdhl dqadaasygt tqpltkslql gaavtf
//
LOCUS       WP_094448227            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            bryantii].
ACCESSION   WP_094448227
VERSION     WP_094448227.1
KEYWORDS    RefSeq.
SOURCE      Segatella bryantii (Prevotella bryantii)
  ORGANISM  Segatella bryantii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Segatella bryantii"
                     /db_xref="taxon:77095"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123435
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlamffa slflfvgtvl aqnkvtgtvv sasdgepiig asiivqgtkt gavtdidgnf
       61 tlsvpsgkkl ivsylgmkti tvspkegmki slvaddktlg evvvtgmhki dkrlfsgast
      121 kvdaakakid gvadisrsle graagvsvqn vsgtfgaapk irvrgatsiy gsskplwvvd
      181 gvimedvtev nadqlssgda stvlssavag lnaddiesfq ilkdgsatsi ygaramagvi
      241 vittkkgrqg strinytgef tmrlrpsysq fnimdsqeqm gvykemesag llsysrtlra
      301 essgvygkmy qlmstynast gtfglantpe aratylqaae frntnwfdel fssaimqnhs
      361 ismstgtdka qyytsfsylt dpgwteaskm qrftaainad yklssklslg lrantsyrmq
      421 kapgttsqsv davtgkvsrd fdinpysyai nssrtldpna fyvrnyapfn ihhelannym
      481 dydivdlrfq aelkykpisk velslmgayk ystttqanti teysnmaqsf ramddatmid
      541 snpwlyqdpd qvntqkfsvl peggfyretk ykmngydfra svnyndvwne dhifnfyggm
      601 evnniernrs yfngvgmqyd mgylgaysyy yfkqaseqnd iyyylknfyn rkaaffgnvn
      661 ysykgrysln ltaryegsnr lgkatsarwl ptwnvsaawn lheekwferi epafshatlr
      721 asysltgddp svsnaeaiir stnvwrpfas dkesgleikd ianpdltyek khefnvgldl
      781 gflnnrlnvv fdwytrnnyd ligyqttngt kgairqlanv aamkshgeel tissknivtp
      841 kfqwntdfif shvktrvtel ddnsriidmi agdggvgftr kgdpyralys ldfrglnndg
      901 iptfineegn lttsdinfqs tnldyliyeg psdptvtgsf gnnftyknwh lnvfmtysfg
      961 nvvrladsfn yrysdldamp kdfknrwtqa gdekttnipa iadlrqiqnd lylkyaynay
     1021 nrstariakg dfirmkeisl sydfpksfae alriqnasik lqatnlfliy sdkklngqdp
     1081 effnaggvav pmprqftctl rlgl
//
LOCUS       WP_094448258            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            bryantii].
ACCESSION   WP_094448258
VERSION     WP_094448258.1
KEYWORDS    RefSeq.
SOURCE      Segatella bryantii (Prevotella bryantii)
  ORGANISM  Segatella bryantii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Segatella bryantii"
                     /db_xref="taxon:77095"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115598
     Region          26..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmtffa clflslgmal aqtqasgtvl ssedgepvvg aslkivgtki gavtdidghf
       61 svvvptgskl evsylgmitk vvsassnmti kldpdnkvld evvvtamgvs rdkkalgyaa
      121 qslnaselnk agtsslasam qgkltgvdir tssgapgasa qitirgarsf dgnntplyvv
      181 dgmpissqad ystgnsvtga dqasrtidin pediesinil kgqaasalyg irasngvvli
      241 ttkrghkqsn kpvitfstdl saqtvsrkfk hqdvyaqgns idaynpnssm twgpkisela
      301 ndptyggntn nkytngdlts hagqyynpky asagldgwtt pqtydnvsdf frtgftqnst
      361 fnisqmkndv sysfsisdty qngiipstgm trtgargavd wkvndqwktg fsanysavki
      421 tsapganngi mnvvysapae ynlkgtpysv pgdptsqvlf rsttfnnpyw wadndefsqh
      481 tnrvfgnaya eyrpkfnwdt dkynlvfreq agidvyttnn stvaeigsay nnkgevenyg
      541 vqvnifnnlf tanftakwga dkewdfgfll gnefnheskr ywdydgsgla fygqpvignt
      601 tsidihseyn hqertvgtfg qlslswknml fftttgrndi vstmprgnrs ffypsvslgw
      661 ifteipalks dflsygklrt syaqvgqagq fysnymyvps ygsgmyiytp isyplggata
      721 yspyyvkfde nlkpqntsnw emgldlgllk nrvkveytls yqdvkdqifd vptagstgyq
      781 ylrtnagrmt twahelsvka aiveskdwnv dlgvnftsvn nkvkelaegv esimlggfve
      841 pqiraqagyt ypniygyafk raedgqlllv dglpqatsas vnlgectpdf nmgfnlnvny
      901 krlnlaatld wqkggrmyng tiltmnyfga teeslpyheg tmvaegidea tgqkntvevs
      961 kqeyyqayne vteagifdts ylklrdltls ynlpkfagid msvyafarni llwskmpnld
     1021 pessqgngnm sgyferfsvp ntssfgggfr itf
//
LOCUS       WP_094448655             933 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            bryantii].
ACCESSION   WP_094448655
VERSION     WP_094448655.1
KEYWORDS    RefSeq.
SOURCE      Segatella bryantii (Prevotella bryantii)
  ORGANISM  Segatella bryantii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 933)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Segatella bryantii"
                     /db_xref="taxon:77095"
     Protein         1..933
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104771
     Region          35..932
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqpkkytks vmafslaaia svsanaqtva dtaevkvafg skaksellgg isavdmkdlt
       61 qknyntysld alqayaggyn gqlwnmgdal ilvdgvprda nnvnpseidq itflksasav
      121 vlygsraakg avlittkrgh tdglkvsvrg nvslftpkey ptflgaaqym slyneslvnd
      181 gdkpaftdtd iynfasgrnp yryhsndffs kdylkksytr yegqaefegg gkyahfyaqv
      241 gfyhqgdlin fgegkdnhtn rlnfrgnidl rlndwitgwv nssasfydlr gdrsnywsks
      301 atlrptskna lspllpismm npdvvdmmkm irnssnvidg qyliggtltd qsnpfadmya
      361 agyntytsrq lqfdagikfd lnkvlkglsf ttqvaidynt synasiqney ayyiptwsnq
      421 ngydeiisle kkmidkftan qnvsdshdkq tiffsgqfdw arqfnqhavg atllahayql
      481 sndgeyhhts nanlglnlny nyahryyadl smaavhsakl aeghrgaisp vgtlgwrlse
      541 ekfmegtkgw lddlkltasy gvvnedldle kyymyddift atgtwwgwse sanamqtsds
      601 qrgenvdlgf ikrkefrfgl dasfgkglvk lnanyfnvkf dglvitpean fpsyyhtywp
      661 vstflpnyny niqnrsgfdf tvdfhknlge vdlqagvtgm yvtnknsrvs elveydwqks
      721 egaridairg yqclgffade adiaanatvn dktkpgdlky kdqnedgkid skdrvvlghw
      781 npdfylgfhf takykgftff mnwtgdfggm glknneyawc ygerkysdma lgrwtpetan
      841 satyprltas nndlsfvdsd fwtyktsalr lnkvqftydf panmfagkwi nglsvyvsgn
      901 slltiakerk ymetsvgsap qtrsynlgvk vnf
//
LOCUS       WP_094448410            1091 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            bryantii].
ACCESSION   WP_094448410
VERSION     WP_094448410.1
KEYWORDS    RefSeq.
SOURCE      Segatella bryantii (Prevotella bryantii)
  ORGANISM  Segatella bryantii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Segatella bryantii"
                     /db_xref="taxon:77095"
     Protein         1..1091
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122430
     Region          44..1090
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrssnqyfht rkfvflmami aglpslpltt kaaetvqltn qaekisgqvl dqngdpviga
       61 tikvkgtttg tvtdldgnft inahsgstle vsyigyktmq vkaanhavik mqedsknlne
      121 vvvvgygtmr kkdltgsvvq idpnkiadqn pgsvqdilrg tpglqigfds sakgagasiq
      181 lrgqnslytd gshnspliil dgmqfngels einpddiaqi dvlkdassaa iygakaasgv
      241 liittkkgkv gkpvinvsmn laantkahyr kvfsasdymr yredwfkaqt ygydengnwg
      301 yygkdsgvpa gyydnvnnis qyglteeqwa tmgaktlqsg esiqslyarr mgldadaalv
      361 mqnylagksy nwedatfrtg fnqdydasvs gasdrvnyyl sfgylknqga iqgdnysayr
      421 anmkisadit nwlqiganvn fqdrtdtssp vplgtnywdn nqlrespyaq rynedgtenq
      481 yprsgnptng gynyhfdqqf iklnkgyttl ntifnakvtl pfgftyqfni aprlqwfydr
      541 yhmsaelpns dpatrgvnrn ssktydysln ntltwdrvfn kdhhvtvtlv qeaeenkyws
      601 dnisarnitp tdvlgyhyis gankaqssfs tndthstaaa ylgrlfygyk drymftgtvr
      661 rdgysafgqn npwatfwsmg gswvfseedf vkksmpwldy gklrvsygtn gnrslsntyl
      721 alsdlanggl yayykygsts qevinalsis rlgnpnlewe ktsswnigld fsvldqrltg
      781 sidwytkrth dmimgqrlpn ftgfssittn lgevtnsgie ltlnsrnidt enfkwntsvg
      841 fsynknkikh lyyeydeegk eiddtsngwf igkpigeiwy wktdgiwqvn eaeeaakvnq
      901 kpgdpkvvns yteddkinad gtrtpvyndn dreylgttqp pvywnmrndf tffkdftfsf
      961 smysymghks lsgewlnndn sgsmftntcn vydkeywtpd nptndyarln avgpsgvtgi
     1021 qklynrsfvr ldnitfgytl pkaltmkwgi qrvhvsagin nvftisswky gdpetggfsn
     1081 rqfqfglnvt l
//
LOCUS       WP_094448431            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            bryantii].
ACCESSION   WP_094448431
VERSION     WP_094448431.1
KEYWORDS    RefSeq.
SOURCE      Segatella bryantii (Prevotella bryantii)
  ORGANISM  Segatella bryantii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Segatella bryantii"
                     /db_xref="taxon:77095"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124264
     Region          50..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrdfwlnrpg allttcllvl psvssiagya aehhaslptv aqqkedlkhv tgtvtdenge
       61 pligaavnvp gspygtiada dghyefyvpk eckevqvsyv gmktaiiplr shendnhfvl
      121 tedksmlnev vvtgyqtlsk erttgafakv tstdlqdkrf sdlssllqge iagyntqnnq
      181 irgistmngv atplyvvdgf pientnysst gsitesipsl niddiesvtv lkdasaasiy
      241 garaangviv ittknarknk kvdvnfsmnl vwnpysydyd rltnssdivn leklwasdnp
      301 nlkgdgasay aqnlltnnvy qsqgirnilk yyagqisese mnsalarlsg lgyryykdve
      361 kyakrdafyq qyhlsvgkat dsnnfrasla yrtnkqhnky dkdnswtldi kdrltitpwl
      421 hftvgnyafi estqrqtfdp lsasytyepy dglknedgtn tvytqedrlt ssrlailnky
      481 glysmditpl deigrnldrt ktftdrvygk ldvdltswlk ynvmfqyeys mnrekllydk
      541 esyyvrnlvn qyatdngngv atynipygni yyranqnrqs yifrhqlnfd ktfggkhnvv
      601 alaghevrrs iidydnstly nydddmlsys lidqtalssi aglmggyglq egnfaymrnl
      661 dnryisfyan aaytyddkyv asasvrwdrs nlwgtnseyq nkpiwsmgla wnvdkedwfh
      721 vswvdrlklr fshgiagnia kdaapymtag yynnnnvggq ygsinsrpnp dlrwektttt
      781 digidfdllk grlygsieyy nkkgsdllan tmgvptegwg ystykinnge mrnrgfemtl
      841 ggdivrtkdf rldgsltysy nqnkvtyvnv tapvyylqld ypeaypvign synglygyhf
      901 aglseeglpq iydaegkavt yspgdlesih ylgsntptsl asiklgahyk gfslsvlaty
      961 mggykarntd lpmfsnnyns atgsyiasia pvnsdimnaw tpqntntdvp rvvygesplf
     1021 nydsrsiyyy sdanvydmsh welsnislsy tlprqwvhla hlsnvrlqld venvatiaks
     1081 ktahymlagn qapnyvfgly ldl
//
LOCUS       WP_094448530             903 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            bryantii].
ACCESSION   WP_094448530
VERSION     WP_094448530.1
KEYWORDS    RefSeq.
SOURCE      Segatella bryantii (Prevotella bryantii)
  ORGANISM  Segatella bryantii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Segatella bryantii"
                     /db_xref="taxon:77095"
     Protein         1..903
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100102
     Region          42..897
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhirytqts llvlaltafa tpakaqykki mpidsvapkh qigsvdvide krmnkglvtn
       61 tlqaisgqaa glnvqtgadr mailnsvrvr gttsltggna pliiidgvys disalnilyp
      121 adiesfsilk naaetapyga rgasgvivvt tkkgqskqfh isydgnigie svsdninmld
      181 assyvataqa lgkdyvdggy ntnfsdvltr tgfvqnhhia fsggsdtqny raslalmqen
      241 tviknngykn fvakidvkqk afddlltidl gvtgstqknn eiddiqklfy saaaqnptyp
      301 atmnasggwd rntnasqinn planlyrenk dkimnfnthm kftfqltpsl tailfgsysy
      361 tsdendnfkp twvwaqgqas ryeskredwl ghvmldyqht wgkhhleaka maeyqssntn
      421 gfgtlvkgfa nnvvsfydlq agylmpfggt tadyintslm sflgqvdyrl mdrytlsvna
      481 radgsslfad gnkwavfpsv slvwnmkqen fmkhidwlsq idvrtgygis gnlggveayn
      541 slsllnpsgl ipwkgsmvtt ynitnnanpn lkwesrgtfn igadmalwnn klvlkaeyyy
      601 sktwdmlyly dvpvppypfn kmlanlgtms nqglefgigy tpihkkdmel ninvnmawqk
      661 nkllslsgdy dgnyftapdr tsigqlngag fhggnnnivy qivgqplgvf ylphceglqt
      721 nadgttsyki adlnhddkvd isdgedryia gqatpkwtlg snisfrykqw dialqmngaf
      781 ghkiyngtsl tymnmssfpd ynvmhdaply riqdqtatdy wlesgdylnf ehltigwnvp
      841 vnqnrfissl rvalsinnlg tissysgltp minsfavnnt lgiddkrsyp pyrsysvsfa
      901 iqf
//
LOCUS       WP_094448260            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            bryantii].
ACCESSION   WP_094448260
VERSION     WP_094448260.1
KEYWORDS    RefSeq.
SOURCE      Segatella bryantii (Prevotella bryantii)
  ORGANISM  Segatella bryantii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Segatella bryantii"
                     /db_xref="taxon:77095"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117502
     Region          24..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlkmvla glvlsagmam aqtqisgtvi saedgqpvig asvkvvgtkm gtvtdidgnf
       61 slnapagskl eisyigmtsq tvtskggkln vnlqpdrqnl devvvvaygt akrqsitgai
      121 svvdgkkied rigtsvtgal egsapgiqvn nsygepgaep tihirgvgtl vnngtshnsd
      181 gvrnadqply ivdgtpyegk iselnaadie smsvlkdass aalygnraan gvvlittkha
      241 ksskptvtln inqgiyqrgi peyerlganq wmeaswkamk nyvmdvagys eaqaaayatn
      301 nlvgdfarkn iyneadnalf dengkligtl npnytdldwn divertgyrq eytatasass
      361 ekfnvytsvg ylnekgyiqn saferftgri narydatswl qvglnlsgvs snrdfnsnas
      421 gsayanpfnv arymapvysy ykhnadgtya ldangnkqwd tessylsnrn igyeirtdkd
      481 rtrrnaidat gfakiklpyg fgisltsnln tttsnrqeyn npnigdgaan ngrlseydyn
      541 yekktgqell twnhdfdkhn vdvmlghenn gwrrkshevm ntnaaidgll slsnfvtnss
      601 tegytyeykt esymgrvryn ydskyfadfs yrrdgsskfk dghrwgdffs fganwnmkke
      661 nfmkdvkwvd alrlrasyge vgndmavdyy gyqglyyitk ngdnpalvrq klaaddikwe
      721 ttqtvdfgve gtlfdrlnfs igyydkrskd llfevrmpls agsfpydsni anmtlyknig
      781 tlsnrgfefs fngdvvrgkn wtwnlaldat tlsnkvislp dhkdilhgqq nyseghsaye
      841 wytyhfegvd qmtgnslytl ntslestaaa dgalveingk kyttstayaa rvwagtalps
      901 vygsfasnls wkdlslnllf syslggktyd atyqslmsta sastasalhe dvlkswngvp
      961 agmtetsanr idpngipvln fnrstdtnat sdrwltsssy lilknitlgy nlpkalvskw
     1021 glqgvyakag venlsrkgln pqssftgstd dtyvsarvfn fslqftf
//
LOCUS       WP_094448855            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            bryantii].
ACCESSION   WP_094448855
VERSION     WP_094448855.1
KEYWORDS    RefSeq.
SOURCE      Segatella bryantii (Prevotella bryantii)
  ORGANISM  Segatella bryantii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Segatella bryantii"
                     /db_xref="taxon:77095"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117772
     Region          24..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlttila csflscgiam aqtqvqgtvi ssedglpvvg asvivagtkt gtltdvdgkf
       61 slsvpsgakl visylgmqqk tvnasgnlri sldpdnklln evvvtalgvs rekkalgyav
      121 sevagsdllk srgglsnpvn alqgkvagls issgagsmgg sskilirgnn slsgnnqplf
      181 vvdgvpiegt dynststarg aggydygnlv qdinpddien isvlkgaaat alygsraang
      241 vimittkhak gkdlqvdfts tvgfesvtkl pklqseyggg ygeddfgtai ingkeyttvd
      301 ysmdeswgpk ldgrqvlswy dlakweangk vgdpttsaws passdyrdff ntgvsftnni
      361 avsqaldngs frvsytntdl kgylpnssqy kntlnvtgnv tskdkklnif tnvnyfnnrt
      421 kgrqdtgygd nnimvkftqw gqrqlnmnel eeyymypdgt qatwnrnkvd dptpayhnnv
      481 ywsryktyen dvrnriygnl gfsyqilpel kfqykanldf yvdkqyerna vgsqeeskys
      541 eisrqqyein helmlqyaqk fkdfslsanv ganimkrhye ylygttkggl aiadfynlan
      601 sistptsenl krekgtnslf advtvgykdq lyleatlrgd kssalpssnn tyvypsvsas
      661 wlfsevlkek apwlsygkir agfsqvgndt dpyqiystyt qytnidsntp gyrlpntlnn
      721 adlkpestts feigleasfl nnrlgfdfty yhtntkdeil plsvsgttgy lykminsgei
      781 snsgiefalh atpiknrdfe wntnltlssn knkvksltdg vdyyriasap faaeigavvg
      841 eeygvirtkd flydseghkl vdpetgqyla tdsyvsvani fpdftggwnn tfryknfdas
      901 iqfdfskggh ffsttqmwgt ycgmfeetaa ngvrengiva qgyvaavdes gnliknadgt
      961 ykstgvntkt vdardyfeny ytgpgaqnvl rsdyiklrei nlgytfklnp nyfvkylrls
     1021 aygrnlavwg pdtkhfdpem ivtssgnvqg ieggatpmva sygftvnlkf
//
LOCUS       WP_094449207             932 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P3-120].
ACCESSION   WP_094449207
VERSION     WP_094449207.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P3-120
  ORGANISM  Prevotella sp. P3-120
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Prevotella sp. P3-120"
                     /db_xref="taxon:2024220"
     Protein         1..932
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104764
     Region          27..928
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrhiykglal caalvagstg vyaqeaetdt ldkvqvafra vdkqdlmggv svidmkemak
       61 knyatssiey ienvvggvng glwgygdylv vvdgmvrdan nvlpqeidqv tllkgsaavv
      121 lygpraakgv lqittkrgqm gdlrinahad msigtpisfp kylgsaeyms yynqarindg
      181 ydknysdeei ynfasgknpy rypnfdmyds qyrrdfttry egivevtggt ervkyyttlg
      241 yyrnnellkv gntkdnftsr ffvrgnmdvk fndwlsakad anvtfydafa aktdwwgqaa
      301 tlrphlvspl ipisfiestd kvslgsvmns nylqngfffg gtqsnptnpy adafaagdnk
      361 fvsrqfqfnt efdinlaalt qglmfrakyg idyastynqg ysnsyatfsp twtnyngpdm
      421 igsitqyged kktgqqyisd ssyrytynvs gqfdwartfd gvhnvfamal anawqtqrng
      481 hyhrttnanl glqlsynydh tyyfdfsaam pystklpagn raaisptvtl gwrptkdvlk
      541 dtfvddlmvn vsggiinqdi ditasdnedg yfmyktilqt ggwyswgdle ggaatefqrg
      601 dnydmgfvkr kefsvglrgs lldklitfdv nfftskmdgm ltratslfpn yftqtgypts
      661 siipyvnyni dkrigvdfsv ygnkkigevd lslgvsgtwy kstadkrden iefdylsaig
      721 rplnglwglk sdgffnsqee idaapeqtfg evrpgdikyv dmnndgkidd ndrvflgrwd
      781 tpfrmglnlt akwknftffa mgnlwlggha mksdsywwvr gtgkysevvr nawtpetaat
      841 atyprltttn gdnnfrysdf wmystdrfnl srvqityalp snlfegsfvr gidvyvggsn
      901 lltiakerki letniggapq mrsynigfra sf
//
LOCUS       WP_094456217             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Niveispirillum lacus].
ACCESSION   WP_094456217
VERSION     WP_094456217.1
KEYWORDS    RefSeq.
SOURCE      Niveispirillum lacus
  ORGANISM  Niveispirillum lacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Niveispirillum.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Niveispirillum lacus"
                     /db_xref="taxon:1981099"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40197
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,323,325)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,330..331,335,
                     338..339)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipkerr ahelrvaatp dtvrkyiglg fevvvetgag lgsaltdeay taagatiaad
       61 vastltgadi ilkvqrplaa gegevnelal ikegailiag lspygapdtv asyaaakida
      121 famefmprit raqsmdilss qsnlagyrav ieaanefgra fpmmmtaagt vpparalimg
      181 agvaglqaia takrlgavvs atdvrpatke qveslggtfv avmdeefqqa qtaggyakem
      241 skeyqakqaa liaetikkqd ivittalipg rkapvlvtdd mlktmkqgai lvdlaceqgg
      301 nvegavagqv vekygvkivg rinmpsriav dasalyaknl lnfitpfvdk dtkslkmnwe
      361 ddvvkgtglt rdgavvhpsf nkpaa
//
LOCUS       WP_094459328             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Enemella
            evansiae].
ACCESSION   WP_094459328
VERSION     WP_094459328.1
KEYWORDS    RefSeq.
SOURCE      Enemella evansiae
  ORGANISM  Enemella evansiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Enemella.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Enemella evansiae"
                     /db_xref="taxon:2016499"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52979
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpaelr pgetmvaatp ktvgqlialg hqvvfeagag raarlpdeqy aaagaelada
       61 devwrsdlvl kvraplpeel pqlregqlla clldparspe llaelaarge talsldavpr
      121 israqaldvl ssmaniagyr avieaansyg sllngqvtaa gkvpparvfv vgagvaglaa
      181 igtasslgaq vyafdvrpev aeqvesmgae fthlpgaqda eassdgyake ltadqeqrta
      241 elyadqsaaa divittalip grpaptlita amvaamkpgs vivdlaapng gnceltvrdq
      301 vvvsdngvii igytdlagrl ptqasqlfgt nlvnlvkllt pakdgqlvld lddpvqrsml
      361 vadrgevtwp pppvtvsakp apvpaakpah evepvrrgrg parvalgtlg vllavglaft
      421 psafllyfti falavvvgyy visnvthalh tplmtetnai sgiiligall qigsdnlvvr
      481 ilafialtva sinifggflv anrmlamfsk d
//
LOCUS       WP_094463302             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pannonibacter phragmitetus].
ACCESSION   WP_094463302
VERSION     WP_094463302.1
KEYWORDS    RefSeq.
SOURCE      Pannonibacter phragmitetus
  ORGANISM  Pannonibacter phragmitetus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pannonibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pannonibacter phragmitetus"
                     /db_xref="taxon:121719"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55209
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspreii dgearvamtp dsaaqlqklg yscviesgag kaagfsdeay rkagvevaas
       61 aadlfaaadi iakvrpplds evallgegkt lisffypaqn kellekakat ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv liigagvagl
      181 aaigtatslg avtyafdvrp evaeqiesmg aefvyldfad qvqdgaatgg yaapsspefr
      241 ekqlekfrel apdmdivitt alipgrdapk lwladmvaam kpgsviidla aerggncdlt
      301 vadqrvvsdn gvvvigytdf psrmaaqsst lyatnirhmm tdltpakdgq vvhnmeddvi
      361 rgatvtfkgd itfpppppkv qaiaaqkpke kareltpeek raqeaaafka qtrnqvalla
      421 gsgalillag lfapasfmsh fivfvlacfv gfqviwnvsh slhtplmait naissiiilg
      481 almqvgsgsf lvillgalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_094464111            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-126].
ACCESSION   WP_094464111
VERSION     WP_094464111.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-126
  ORGANISM  Prevotella sp. P5-126
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Prevotella sp. P5-126"
                     /db_xref="taxon:2024216"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122888
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkllillv nifllcggvl aqtkvtgtvv sqedgepiig asiiiqgqrs gtvtdadgkf
       61 slsvpagkki svsyigmetq tlapkakmsi slrpsaelee vvvtgmqktd rrlftgatdr
      121 vnaedailng iadisrsleg rsagvsvqnv sgtfgtapki rvrgatsiyg sskplwvvdg
      181 vimedvtdid sdalssgdpe tlissaiagl nsddiesfqi lkdgsatsiy garamagviv
      241 vttkkgkagt ahinytgeft mrlkptygnf nilnsqdqmg iyrelydkgw lnlsntlngs
      301 dygvygkmye lintynpstg afalanttea knaylanaef rntdwfdelf stsiqqnhsv
      361 smsggtaksn yyasvsamtd pgwykqskvd rytlnmnvnh kildnlslni igsgsyrsqr
      421 apgtlsqdvd vvsgnvkrdf dinpysyaln tsraldpdty yhsnyaafni lheletnfid
      481 vnfldakfqa elkykpikdl eiavlgalky tttsqeykil dssnqaeayr amdntiirda
      541 nkylytdkdv lyslpisvlp eggmykrtdn rmrdynfrat anyvhtfadi hyvnlfggme
      601 tteiqrsrsw fngwgmqyak geipyytyqf fkksleentd yyslsntnsr saaffanaty
      661 gydnryvlng tvryegsnam gksrsarwtp twniagswnv dqekffkawe ptishlklka
      721 sysltatppp tsytsstnvf kafnpyrift sdketgiqls dlenseltye kknefnfgve
      781 agflndrinv sfdiytrkny deigpvatqg iggqiirwan aadmkshgee lsisstnikl
      841 kdfswitslv yshtktkitn lasqdrvidm itnfggrrvg ypvrslfsip fagldenglp
      901 tfyneageit tdninfqerd kvdylkyegp tdptvqgslg nlfkykgftl nlfitysfgn
      961 vvrldpvfsa tyndlssmtk efknrwmvpg dekktnvpvi lsyaqytnns qlrygynayn
     1021 ysdvriakgd firmkeislq ydfpknwikp ltnlslklqa tnlfliyadk klngqdpeff
     1081 rsggvsapvp kqftatlkvg f
//
LOCUS       WP_094464355            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-126].
ACCESSION   WP_094464355
VERSION     WP_094464355.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-126
  ORGANISM  Prevotella sp. P5-126
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Prevotella sp. P5-126"
                     /db_xref="taxon:2024216"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123284
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmmfla glflslgmaf aqtkvtgtvi sqeddqpiig asvlvqgqrs gtvtdvdgkf
       61 tisvpsgkki tisyigmepq tvtpkngmtv tlrssaelqe vvvtgmqktd rrlftgsttk
      121 vdaekakldg vadisrsleg raagvsvqnv sgtfgtapki rvrgatsiyg ssrplwvvdg
      181 vimedvtevd adqlssgdae tlissaiagl naddiesfqi lkdgsatsiy garamsgviv
      241 vttkkgksgq trinytgeft mrlkpsysnf nimnsqeqmg iykeleangl isfgrtyras
      301 ssgvygkmyq lmntynpatg sfmlsqteea knaylreaem rntnwfdelf snaiqqnhsi
      361 smstgtdkaq yytsfsimdd pgwteqskvr rytasinamy nvnkkvtlnm ianasyrnqr
      421 apgttsqsvd avtgnvsrdf dinpysyain ssraldpnef ytrnyapfni hnelannfmn
      481 ldvvdlkyqa elkykpikkv eltvlgayky stttqaneih ensnmaqsfr amddatirdn
      541 npwlytdpdk pnskpvsvlp vggfyretky kmtswdfrat aqyndvfned hivnlyggme
      601 indtqrsrsy fngvgmqydm gylgsydylf fkqsaeqnam yyslsnsygr evsffataty
      661 swkgryving ttryegsnrl gksrsarwlp twnvsgawna heepwfqktf ktalthatlk
      721 asysltgdkp avtnsqaiiq sfnpwrpfas dkesglniyd fanpdltyek khelnigvdl
      781 gflnnrlnvq fdwyrrnnyd ligmrttngt kgtinefanv asmrshgeel sisskniisk
      841 dfkwntdfif shvktkitel dnrsrlidmv tgtgfakkgy ayrslfsfdf kglnangipq
      901 vvnesgevvt sdiyfqsrdi dylvyegptd ptitgslgns ftyknwhlni fatyafgnvv
      961 rldpafyasy sdldampkef knrwtvsgde nkttipaipd lrqlqadtql syafnaynrs
     1021 tdrvakgdfi rmkeisvsyd fpqtwlnalk lksasiklqg tnlfliysdk klngqdpeff
     1081 ntggvavpma rqftctvrvg l
//
LOCUS       WP_094466292            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-108].
ACCESSION   WP_094466292
VERSION     WP_094466292.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-108
  ORGANISM  Prevotella sp. P5-108
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Prevotella sp. P5-108"
                     /db_xref="taxon:2024225"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110081
     Region          29..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mclgsvsafv vgapsekapf nkveqanekt vggqvldeng epvigatvtv kgtktavvtd
       61 idgkfsfkvp agstlvvtyl gyadkevaat gtgmtinmaq dektldevvv talgikrsek
      121 alsynvqqlg neylttvkst nfmnslagkv agvninassa gmggatrvvm rgpksinqsn
      181 salyvvdgvp innrnngtae giyasqpgge giadinpedi esisvlsgpa aaalygsaaa
      241 qgvimittkk gkegrvsvvv snstqfsdvf kmpefqneya nrpgevrswg ekggseftgf
      301 dpenffntgt niqnnvsltv gngknqtyas vgttnangim pnnsydrynf tfrnstsfln
      361 dkltldfnln yvkqsdmnlm aqgqyfnplv alylfprges fdairtfevf dqsrgiyvqn
      421 wnfgdalsmq npywianrmn rttkkhrymi nsslkyqifd wldvvgrisf dratsksedk
      481 ryastinlfa hsdygfyays navdqsvygd vmfnvnksfd kfsiganvgg sfsrtqydnn
      541 gfqgglraps nifspnaidy anatndnrpi yafnkhnins vfanvelgwr smvyltltgr
      601 ndwdsalagt knesffypsv gtsaiisqmv rlpefidylk vrgswasvgs aispnitsqw
      661 rynfkpntqt yetvtykfpk tfypertnsw eagltarffn naltldmtfy qsntrkqtfl
      721 rpitvsegyd heyvqtgnvr nrglelsigy nhqfgklsws ssltysmnrn kivdlladpe
      781 vtisttglng vgvilkkggt mgdvysytdf ardregnial dasgnvirkt lsnpkylgsv
      841 lpkgnigfsn efswkginlg flltarlggi vmsqtqaimd yygvsktsaa arenggipvn
      901 tglvpaekyy avvggdnpiw seytysatnv rlqeahisyd vpnkwlagld lslgltannl
      961 wmiyckapfd pestastgtf yqaldyfmqp slrslgfnvk lkf
//
LOCUS       WP_094466252             898 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-108].
ACCESSION   WP_094466252
VERSION     WP_094466252.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-108
  ORGANISM  Prevotella sp. P5-108
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Prevotella sp. P5-108"
                     /db_xref="taxon:2024225"
     Protein         1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98775
     Region          49..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mangkkttll llllfcssla haqkqvpier kdtianesni ikivgnhsnk gaannaldvl
       61 sgqaagvnvt sngldrmaml nsvrvrgtts iiggndplvl idgvtsdvft lstiypadie
      121 sfrilknaae tamygsrgas gvievktkkg tgrgfqisye gnvgfeqmyk hlemlnaaey
      181 vatakalgiy cnnggfntdn ykvitrtgmv nnhylafsgg tpqsnyrasf gvmdhntiik
      241 kmdynvfvak vdvtqkafnd rltgefgvfg ysfknhdifd tqmlfysaac qnptfpagtd
      301 ehgnwlknes athvnppgil leekndskdl nfdahiklsy dfnpnwrist fasylygste
      361 ngmfcptwvw aqgnvyrgef kkeewlgnva lsfnkqigih risaeassey rkltktafwm
      421 yakgiptndf gynnlgataa rpyggtesty edqslasvmg svtyslldry llsvnargdg
      481 ssmvgddntw gffpsvsftw dmkkenflan vkplsmlklc tglgqagnlg gisayttmnt
      541 vrqtgivpvk ssptvtlgmv rnnnpdlrwe tkttfnigad fgffanriml taeyyyskts
      601 dmlyayevpv ppfayntlla nigsmsnrgl elglsvqpis kkdmelninm nlsfqsnkli
      661 slsgdykgms mtaanitaig sldgagqngg dnnvvyqivg qplgvfylph ckglvkneng
      721 syfydiedld hngkvdlsdg gdryiagqat pkvtlgsnis frykdiyval qmngafghni
      781 fngtglayts macfpdynvl kdapkknivd qrvsdywlek gdylnfehlt lgynvplksk
      841 fvrslrlscn isnlgtitgy rgltpminsy vvnstmgidd krnyplyrty slglsvqf
//
LOCUS       WP_094466348            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            P5-108].
ACCESSION   WP_094466348
VERSION     WP_094466348.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. P5-108
  ORGANISM  Prevotella sp. P5-108
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Prevotella sp. P5-108"
                     /db_xref="taxon:2024225"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120844
     Region          115..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnskqskllg icllvtlmfs alsmsaqtvt ktfsneslrn vlkeverqtk msviykvdev
       61 nasqkvtatf hatpvrdvlt kvlgshlgfk idhkmitifk reakpaakds qapkktvkgq
      121 vldengepvi gatvrskatg aavvtdldgn ftisaeegsk ievsylgyqp ksvtakgnnl
      181 tvnisqdekt lnevvvtalg ikkeskalty nvqqlknsdi tgvkdanfmn alagkvagve
      241 inasaagigg gvkvvmrgnk singnnnaly vidgipmpsl qanqptdayh gdaqtgdaas
      301 mvnpddiesi svlsgaaasa lygsdaangv vmittkkgtv gkvrvsysnn tsffspfvtp
      361 efqntygqtg tgtfsswgsk latpssydpl dffqtgynvg nsvtfsvgse hsqtfvsast
      421 tnaegivenn emsrynftir nttdflkdrl hldlsamyms vkeqnmisqg fyfnpivpvy
      481 lfpagddirk ytpfeqydpe rnfktqywpf gnqglsmmnp yweinrdiae nhkdrfilsa
      541 gltfdiakgi tlsgrakmdk tsgiyekrya astdplfage ygayyrtndn trqiygdail
      601 nidkyfgdfs ltanlgtsik dvetsytyvg gflnvannft lnavnransh mdadpalnyh
      661 hqvqsvfata qvgyksmvyl dltarndwds flgntqyrnk gffypsagvs ailtemipgl
      721 kskvlsflkl rgsysevgnt pekfyaltry tysnaapstt syypnnnlkp ertkawelgl
      781 qanlwqdkvn lnvslystrt tdqfflpels assgysklpi nggridnkgi easltlnqpl
      841 gpvkwsstft ytlnknkikq llapteltla ngnkvnvsld gmdmlnlgsv kvrlteggsm
      901 gdlyvtipkm dehgylivdy tsrniagvde gkyvyagnvn pkynmgwrns fswkgidlgf
      961 lisarvggrv ssitqgymdy fgaskttaea rdlggalvng yripaqdyys kigpsvgayy
     1021 iysatnvrls elsvgyslpi skwvpwienl rlaftgrnll mfyckapfdp eltastgtyf
     1081 tgidnfmmps lrnlgfsvkv df
//
LOCUS       WP_094469757             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas mandelii].
ACCESSION   WP_094469757
VERSION     WP_094469757.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mandelii
  ORGANISM  Pseudomonas mandelii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas mandelii"
                     /db_xref="taxon:75612"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38469
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag lnasivdsay etagaxigsa
       61 ndafgaelil kvvapsdsel tlirsgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlxl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_094481546             536 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodoferax
            sp. TH121].
ACCESSION   WP_094481546
VERSION     WP_094481546.1
KEYWORDS    RefSeq.
SOURCE      Rhodoferax sp. TH121
  ORGANISM  Rhodoferax sp. TH121
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Rhodoferax.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Rhodoferax sp. TH121"
                     /db_xref="taxon:2022803"
     Protein         1..536
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55365
     Region          12..536
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtsvatekg qrigipretf pgekrvatvp eavekliklg fkvsvesgag alancdddsy
       61 raagaevvat aaelwaqsdi vfkvrgpsva evgllreggt lisfiwpaqn pellqqlaak
      121 katvlaidal prtlsraqkm daltsmagvs gyravieaan afgrffngqi taagkvppak
      181 vfiagagvag laaigtaasl gaivrandtr aevadqvvsl ggefvkvdye eeggggggya
      241 kvmsegfqaa qramyaqqak evdiiittal ipgkpapkli taemvrsmkp gsvivdmaae
      301 qggnceltep gqavvkhgvt ivgytdlasr lakqsstlya tnlfrlaeel cktkdgivnv
      361 nmeddairgl tvikdgtvtw papapkapaa paaakaaapv vakkpahghg gagepmsaks
      421 llvlmavaav lfwvigsyap aaflghftvf vlacfvgymv vwnvkpalht plmsvtnais
      481 siiaigalvq vspvagavgr pdglitwlaa aaivltainm fggfavtqrm lamfrk
//
LOCUS       WP_094484439             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium sphagni].
ACCESSION   WP_094484439
VERSION     WP_094484439.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sphagni (Mycobacterium sphagni)
  ORGANISM  Mycolicibacterium sphagni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Mycolicibacterium sphagni"
                     /db_xref="taxon:1786"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38120
     Region          7..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdtkttvgv vaesgaderr valvpkavst lvnsgvavvv qagagerall pdelyteaga
       61 tigdawaadv vvkvapptad evarlksgqt ligflaprna dnqiaalkqh gvqafaveai
      121 prisraqvmd alssqanvag ykavvlaase strffpmltt aagtvkpasl lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwldlgida ageggyarel tdeeraqqqk
      241 tleaaiggfd vvittalvpg rpaprlvtaa avegmkpgsv vvdlagetgg nceltepgrt
      301 vvkhgvtias plnlpatmpe haselysknl tsllellitd galapdfsde vvsascvtre
      361 aapaakpsse eae
//
LOCUS       WP_094486764             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            aurantiibacter].
ACCESSION   WP_094486764
VERSION     WP_094486764.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium aurantiibacter
  ORGANISM  Flavobacterium aurantiibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Flavobacterium aurantiibacter"
                     /db_xref="taxon:2023067"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108699
     Region          25..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskftwfla liltlmlnvs faqektitgv vsnaglplpg asvtvkgttv gtstdldgky
       61 slkapvgati efsflsmktk sivvgasnvi nvsleedvnk ltevvitnsy nagqkrsdvv
      121 ssvstvsakq lennaftsfd qmlqgqvagl tvvsgsgqpg saakvrirgn ssitgnndpl
      181 yildgvpita ndyaalnpnd fenvnvlkda aataiygsrs sagvivitsk kgkynsptqy
      241 tyrgqsgite vsrarfnmmn ssqllnfqrl vsngrgatgg anggpmtdae iaeaskvntn
      301 wrdvffrtgf tqshelqirg gsentrffns lgyfeqdgva irsnlqrftf rsnldhkade
      361 nttmgstlsi gftkqdlids ensitlqnpy aaaylgspyd slydangdfa tgngfigana
      421 yenlvrnlry nnqlklvgsl yaerkfaknf tarfdlgidy sydqlirgsd pnsfygsttq
      481 pgnegfyget nsyiarfnnt fklnysntfa ekhsvdisgy fewlkthars gqffgyginp
      541 klvgypegit qgsaanglfa evggaesesg ilsyfmvgky gygerfnael slrrdasnrf
      601 adankwatfy avglnynfin enldgsdklf qslivrasyg ssgnqngign fqeegtwgtg
      661 gyggnpgiap ltfgnpalkw esgvkrnigv dysllknrlf gtveyydnyt dnlfisqtpp
      721 fesgkpqfde nagkmsnkgv diqlegilvk tndlsfslyg nfnynkntie dlgqvsefvq
      781 gtaiireglp fgshfavgwa gvnpangqpl yydlngnvtt qftednstan wgtyeppysg
      841 gfghklnykg lefsslftfa adymrynnqt ffqenpnfaq fnmstlmltm wqnpgditev
      901 qsfrynrefs skdiedasfl rlrnitiayn lpdkaikslk yissvriyaq gqnlatwtkf
      961 sgfdpeddnn iagyeyptpr iytfgvdvkf
//
LOCUS       WP_094486777            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            aurantiibacter].
ACCESSION   WP_094486777
VERSION     WP_094486777.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium aurantiibacter
  ORGANISM  Flavobacterium aurantiibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Flavobacterium aurantiibacter"
                     /db_xref="taxon:2023067"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114930
     Region          25..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkmkltsyla lllclvaeit faqqrtvtgv vsdskglpip gvsvvekgtt ngtqtdldgk
       61 ysintrnekt lvfsfigmkt kqvvvtgnvv nvsledesve legvvvtafg ikrnprdlgy
      121 avstvkaael tevsepdvtr alngkvpgvn invstgvaga anqitirgvn tlngdiqpli
      181 ivdgiaysnp evttssqttg gggyqsglss idpndiasmt vlksipaaal ygsravngvi
      241 vittksgsar gkrdkklgvt vssgtyfeni anlpeyqnky gagsnfnyas angswgprfg
      301 titeiptwap ilaafpdrfg ptvpyvakpn nvkdlfrtgt vndqsvnlsy gseegsfnlt
      361 lsdlnqngyi pyntfdrtai stggtfklkn gitvgsnmsy tkteqvggff genqfdgsss
      421 sfartmilar nwdfnlpykd pltgasvtpl egqfdhplws wendqiktet nrtvagfnla
      481 ysfnknisas yrlgynryel ermeirdins ranggvgslt tdefttadle qtllvnfdyq
      541 ltddialsai tgtnilnntt drivyqgndm ilpelfnmrn vetitnlids ktkrrnvgff
      601 gdltlsykny wfvnltgrnd isstlpknny syfypsfsts liltdalkie sdvlnfakir
      661 fgiaragrda aaeflnkpyv ignpfngtst irnpdflanp nvtpefttei elgtdleffk
      721 rkvildftvy qktttdlltp itvpgssgya efntnvsemv nkgieiglnv tplqsenfkw
      781 nvfttftkne nevteliegl erypidvnqv ayvakgqpfg vfygtrfard eegnflinpn
      841 gggiiqdptp giigdptpdf kmsfinslsy kgftlrtqfd wrqggdikss tiesllgrgv
      901 trdtenrert fiipgfygns dgtpildang nkipntvqlg mnelyfspng gntfainsvd
      961 easiydgtvf rlreasltyd vpkkwldktp fgaisfafig snlwyhapnv pkytnfdpev
     1021 tsfggtnlqg ievqsaptak rygfklnvtf
//
LOCUS       WP_094501444             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            qinghaiensis].
ACCESSION   WP_094501444
VERSION     WP_094501444.1
KEYWORDS    RefSeq.
SOURCE      Vibrio qinghaiensis
  ORGANISM  Vibrio qinghaiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Vibrio qinghaiensis"
                     /db_xref="taxon:2025808"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54137
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpketl tgetrvaasp ssvaqliklg fdvsietqag vlasfddaaf eaagativst
       61 qdvwnsdiil kvnapivdek qsidevalik egaslisfiw paqnpelmeq lsskkinvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv qsmgaeflev dfqetagsgd gyakemsddf
      241 nkkaaelyaa qakdvdiiit talipgrpap klitkemvds msagsvivdl aaanggncey
      301 tvadqvitta ngvkvvgytd mvgrlptqss qlystnivnl lkllckekdg sinidfedvv
      361 lrgvtvvkeg eitwpappiq vsaqpqvkta ptrpepkkqe pvsatkkiag lvaavgafaw
      421 iasvapaafl shftvfvlac vvgyyvvwnv thalhtplms vtnaisgiiv vgallqigqg
      481 sgvvtflafi avliasinif ggftvtkrml emfrkd
//
LOCUS       WP_094504939             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Brucella
            thiophenivorans].
ACCESSION   WP_094504939
VERSION     WP_094504939.1
KEYWORDS    RefSeq.
SOURCE      Brucella thiophenivorans (Ochrobactrum thiophenivorans)
  ORGANISM  Brucella thiophenivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Brucella thiophenivorans"
                     /db_xref="taxon:571255"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55777
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpleih agearvgltp dsaiqlqklg feclvekgag klagfsdeay raagvtvvdt
       61 adtlfsqadi vakvrppets eldrltagqt lisffypaqn tallkqakat ganviamdmv
      121 prisraqkmd alssmaniag yraiieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiqsmg aefvyldfke sqqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvmam kpgsvvvdla aerggncdlt
      301 vpdrkivtdn gvtvvgymdf psrmasqast lystnirhmm tdltptkdgi ifhnmeddvv
      361 rgatvtfege itfpppppki qaiaaqkpke kvkeptseer hirevaafks qtkkqgllla
      421 ggtalllivg mfaptsfmsh fvvfmlacfi gfqviwnvsh slhtplmavt naisgivilg
      481 allqigsgnw lvvllaalsv lvatinivgg flvtrrmlam fqks
//
LOCUS       WP_094505373             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Brucella
            thiophenivorans].
ACCESSION   WP_094505373
VERSION     WP_094505373.1
KEYWORDS    RefSeq.
SOURCE      Brucella thiophenivorans (Ochrobactrum thiophenivorans)
  ORGANISM  Brucella thiophenivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Brucella thiophenivorans"
                     /db_xref="taxon:571255"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44030
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifipke sdpnetrvaa saetvkkfta lgfdvvvekg ageksriidt efsgagarig
       61 taadsktadv ilkvrrpnda elkgyrsgaa lfamldpygh edavaalgka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaset ydrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfvavedee fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vtkemvaamr pgsvlidlav erggnvegai
      301 agqiaevngv kivghlnvpg riaatasqly arnlyaflet lvdkevkllk ldpeeelvka
      361 tllthggqvv hpafakadae rvivvekvak pkaapkpkap aaktarktpa kaaktsadgg
      421 ea
//
LOCUS       WP_094533600             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudanabaena sp. SR411].
ACCESSION   WP_094533600
VERSION     WP_094533600.1
KEYWORDS    RefSeq.
SOURCE      Pseudanabaena sp. SR411
  ORGANISM  Pseudanabaena sp. SR411
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Pseudanabaenales; Pseudanabaenaceae; Pseudanabaena.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Pseudanabaena sp. SR411"
                     /db_xref="taxon:1980935"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40369
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikeie fgerrvalip evvsrltksg levlieshag elsffadsty veagakiitd
       61 kstlineaei llkvgapree evsmfksgqi tigflnplgr pelirrlahq gvtamsmemi
      121 prssraqsmd alssqasiag ykavliaaaa lpkylpmltt aagtippakv vvlgagvagl
      181 qaiatarrlg aqveaydirp avreevqslg akfidvtlee dttaaggyak eiseaakqha
      241 qvilakhikd adivittaqv pgrkapvmvt damiaqmkrg siivdlageq ggncegtvag
      301 kdvichgati ispinlpasm pihasqkyak nllnllnhli kkgelnldfd ddiisstcit
      361 hageirnqrv kdalsqlvvs v
//
LOCUS       WP_094540190             441 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Brucella
            grignonensis].
ACCESSION   WP_094540190
VERSION     WP_094540190.1
KEYWORDS    RefSeq.
SOURCE      Brucella grignonensis (Ochrobactrum grignonense)
  ORGANISM  Brucella grignonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Brucella grignonensis"
                     /db_xref="taxon:94627"
     Protein         1..441
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45597
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifipke sdpnetrvaa saetvkkfia lgfdvvvekg ageksriidt efsgagarig
       61 ttadakaadv ilkvrrpnda elkgykpgaa lfamldpygq eaavaalaka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaadv ydrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedee fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgraaprl vskemvaamr pgsvlvdlav erggnvegav
      301 agqvadvngv kivghlnvpg riaatasqly arnlyaflet lvdkeakllk ldpqeelvka
      361 tllthegkvv hpafakaeae aalavvaekv akpkaapkvk apavkaeaak eaasatakpv
      421 akttrktpak aaktsadgge a
//
LOCUS       WP_094565285             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Herbaspirillum sp. meg3].
ACCESSION   WP_094565285
VERSION     WP_094565285.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum sp. meg3
  ORGANISM  Herbaspirillum sp. meg3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Herbaspirillum sp. meg3"
                     /db_xref="taxon:2025949"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38666
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlgipvesr dgetrvaatp etvkkliaak hevlvesgag ikssitdeay vaagaviaaa
       61 sdvyaadall kvrapsader arlksgtvvv gmlnpfdadn iaamaaaglt afaleaaprt
      121 traqsmdvls sqaniagyka vlmaantyqr fmpmlmtaag tvkaarmlim gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfitdee keiaqgvggy arpmpadwmr
      241 rqaelvhera kqadiiitta lipgrkapvl iseetvkamk pgsvildmav dqggncplse
      301 sgktvikhgv hiigegnlaa lvaadasaly srnvldflkl ivdgegklvi nreddivaat
      361 llcsggevlr k
//
LOCUS       WP_094569115            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter xinganensis].
ACCESSION   WP_094569115
VERSION     WP_094569115.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter xinganensis
  ORGANISM  Mucilaginibacter xinganensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Mucilaginibacter xinganensis"
                     /db_xref="taxon:1234841"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118565
     Region          24..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllvslc flvlcitqaf aqnrtitgtv tskedglplp gvsvtvpgtq vgtqtndygk
       61 ftikvpasak slafgfvgyk rvtatigatd vinatletna nelkevvvtg gygikqtars
      121 nsnsaqvvta telntvrqpn innalagkva giqvrsqsaa algrntevrl rgasgfgsgq
      181 galyvvdgti lpnaddinld dvesvtvlqg aaaaallgsq gangaivitt skakkngglg
      241 idlrlgatfd kayilpnyqn tygggnnpvf eqytwkagdp dhwkslsgky ypdysddssw
      301 gpklsgqeyi pwyawyagtk ytgktaswta qpnnaidfyq taplldnsit fnkagddysv
      361 klsygnvyqk giipnqdlkr ntlnlnynyd lnkhlslsan inyvnqkqtg tvqdgyanqt
      421 sgsftqwfhr dldmgimkel rglqygpgqy aswnhndpaa wnpanptnfy ggnywynyyt
      481 yqdlekdhyn rdrfygnial tykvnndlsf rltyrkqqnt twtenieste laqsqvqtgl
      541 kgsyftynsy snrenlefla tyskkikdfk idanfgtdkf nwtdkengaq tnngltipyl
      601 ytisnsvdpa siyntrlqer ynavlghlal gwkdlifldg slrndwfstl pqakndvlsk
      661 saglsfvfsd llksqdkwls ygkvratygq ipkalgtsne tfgayrypga sygvaaqkfn
      721 gqllmstpdq nvdplihgst vtqkelgldl rflndrigis gtywdgaetg ipssinvnga
      781 sgfssiltnf gnvtkkgfdi tfnaypvrvp nfawnvslty snllqdkvve isnkynvqqi
      841 ivayntfsql pylvqkagma wgqifgsgil rnsagvpild asgfyqrnps vyfgsvlpkh
      901 tggiqntfni ykdfsvnfni dyqfggkfas lsnafgafsg ttyrtaalnd kgnpvrdnva
      961 dgggvhqvgv dangkpvsmy vsaydyyhnn fnngtldefv ydltfiklre agisyripvk
     1021 klgignvikn asfqiqahdl wliyaksrdf dpsqisavqg esgqlpgtrg fgfnlkvgf
//
LOCUS       WP_094569542            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter xinganensis].
ACCESSION   WP_094569542
VERSION     WP_094569542.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter xinganensis
  ORGANISM  Mucilaginibacter xinganensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Mucilaginibacter xinganensis"
                     /db_xref="taxon:1234841"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122090
     Region          32..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiymqlkt vitvllfcla pvllfgqsri ggtvtdskkq plpgvsvvlk gtsrgtvtdi
       61 nghysltaek gqvftfkflg fvtkditise etnydvtlve dfktlnevvv talgvkretk
      121 rlgysvqeis gseltkarep navngltgki sglnvginqe ilaaptvllr gsplnfyvvd
      181 gipintdtqn ispddidtyt vlkgptaaai ygsrgingai littkrakkd skgftiefns
      241 stqfnkgfia ipkvqnsygg gdydkyafgd gagggvndgd ydvwgprlna glllpqydga
      301 ydptqtyttt fadgskfqgh ikptpwvarg vnnlqgflqt gvltsnnvsf sstseksnvr
      361 msitdghqtg itpntklntv nfnilasynf nkkfkvegnl nynrqftdni pdvsygpnsi
      421 iynidiwtga dwnindvrny wqpgkegiqs vfveykryhn pwfqsyewlr ghykndiygw
      481 aaftyspnkd fditlrsnvs tydvlrteke pfsahpygde hnhgnyredr rdqfdnntdl
      541 llkynfdnil ksgftvnala gstlrtmkyt slytstdqll ihdvytfqns inplkvynfa
      601 sdlitlsefa sadvtfkkyf tvtatarnek ssalqnqsyf ypsvsastpi sdyvklpdfi
      661 sffkvrasya nvkeggtspy igpagnaagy gstyqtnygg pgyissppay tlgkssdnvt
      721 vasaptyaid pslkpstrsn yeagadlrfl kdrlglsgty fiykdgpqif tasssetngs
      781 aqsfvtngfa tkrtgfefsl ngspivtpdl rwdvlvnvgs ykevydkfps qlngtfnqff
      841 higdrvdkly gaaeakapdg rvihdasglp mylpvaqylg nadpdfswgi nnkfrykqft
      901 lsfqfdgmfg gkiqdrvyrk lieggrgavt aegiigaarl yesqhwgdpg fkgavyadgt
      961 pmlghdgaal aagspaiqyd pktgvitnls qlkfvanttp vkyvqdyvss fyndpehtvi
     1021 sktyaklrev vigyslsknv vqklhlskvd fslvgrnlly ffhpgykdid vdqypgrdqn
     1081 gtpnreynlq tpttrsfgfn invvy
//
LOCUS       WP_094569832             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter xinganensis].
ACCESSION   WP_094569832
VERSION     WP_094569832.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter xinganensis
  ORGANISM  Mucilaginibacter xinganensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Mucilaginibacter xinganensis"
                     /db_xref="taxon:1234841"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106798
     Region          27..978
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklknllkls clvllcfvvl pamaqnktvt gkvtdakdgs plpgvtvslk gtttgtntda
       61 agafslsvpa sattleaafl gytkqevtit gsplniklvs sstslnevvv vgvgygsqrk
      121 kdvtgavesi sskdfnqgiv inplsqiqgk vaglnitqqg gnpnsqdagi sirgqtsitg
      181 nqsplfvidg vatsgnsqfq nlspddiesy dvlkdasats iygsrgangv iivttkkgrt
      241 grttvdysgy vgisnqakyy dllnaadysk aieaipgvtp styekggnvd wqraisrsav
      301 thsnniaisg gsngfnyrgs vnyqlqegti innqkkqlgl rfnaeqkald dklditlnfs
      361 nttvyrdqlt dggvianyif napptypiyn pdgsyntfvd fnlanplehl letysretsy
      421 qtlanttvny nllpslkvgv tgilihdntl thyfqpsfpg egninnaaqn synnntyean
      481 ahidfnksfg khnisatavy eyndfytesf sasgqnyttp elldnnlgsg dqsknvinss
      541 kddykiisfl arvnynydnr fyvtasirrd gsdkfganhq wgtfpavdla yrlkrdllqn
      601 vdwvddlklr lgygvvgnss alnvyqnvtl ygtgtryfdg saasnqypvs ytylqnanpd
      661 lqweerqgkn igldfslfnn rlsgdinyyn dktskmiyqy gvptppffvn tiyanigalt
      721 nkglevaltg qilrgsgltw tangqitfnk tkvvnlsgty qgfpvasdqi vtgsasgrgl
      781 ssspitylkp gqpadvfylt hytgvdangn elfdgktldq npnpnkyyid pnpkfnygis
      841 nsfgyknwnl sfflrgvygq kifnntlldy etitrlpsnn vtkaaltngi kdglhvsdlw
      901 lenasylrld naslgytfkn ikgisnmriy vagnnlfvit kykgldpefa pnshytdgng
      961 slqsypksrg fvlganvsfk
//
LOCUS       WP_094569850            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter xinganensis].
ACCESSION   WP_094569850
VERSION     WP_094569850.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter xinganensis
  ORGANISM  Mucilaginibacter xinganensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Mucilaginibacter xinganensis"
                     /db_xref="taxon:1234841"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116216
     Region          24..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilllnlc llliattqlf aqtqtvtgkv takedglplp gvsvsikgtt ngtqtdvngk
       61 yslavpsgaq ltfsflgyss qtlpisgnsl nvvlvassqq lgevvvtgal gisrtrnqqs
      121 yaaqqvngee vskqrstnfi sglsgkvsgl eirqnnalgg stnvvlrgtk sifgnnqalf
      181 vidgvpvdnt nsngsnqqqg gggydygspa sdinpddien vtvlkgagat alygsrgsng
      241 vilittkkak kglgvivnst vsfgsidkst faqyqkqyga gygpgfytgn ifgqtgvkva
      301 qtdadasngs afdpnlmvyq wnafdptsan ygkatpwvaa kndpttffek pvstnnsimi
      361 tnggengsfk lgytnsdeng vlpnsnlkkn lvdfaatyni tpkltvgasi nyyntngtgr
      421 ggtgydgtns dnrnvvsgfr qwwetnvdvq elkaayertk snitwnmada rhgntapayw
      481 nnpywvtdhn yetdsrnryl gnvnaaykat swltftgrvs ldtysalqee rydvgsiglp
      541 yysrtnqnys etnfdllanv dknlgndfnl kavlgtnirk nnfnsifast nggliipgly
      601 slsntlnspl spteiyqrre vdgvfggatl twknlltidg tirrdesstl psannkyyyp
      661 svsagfifse llkqytwlsy gklrasyaqv gadapiysvn dtytiippfg snpqtvanat
      721 knnnnlkpeq tkskeiglel sffnnrlgfd gsyyvtntfn eilpvnisga tgytaeylna
      781 gnvrnkgfel svngtpvrtk dfnwkinvnf trnrnevtsl fkdatgneaq nlqlgsfqng
      841 etlnaplhgs lgtirgtdyt yykngqpivg adgqyvltat anhdigntnp dwtgginnnf
      901 tykgfnlsfl idirkggsvf sndlayglad giypltaytn dlgnpvrspl ttgsnsggfi
      961 rpgvtadgqp ntvrvpggpy gsfgdgagll plkafvydas fiklreailg ytlpgsalgk
     1021 lgpvkevtfq ligrnlwiih knlpyadpee glsagnlqgi qegayptvrt isfnlklrf
//
LOCUS       WP_094570240             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter xinganensis].
ACCESSION   WP_094570240
VERSION     WP_094570240.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter xinganensis
  ORGANISM  Mucilaginibacter xinganensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Mucilaginibacter xinganensis"
                     /db_xref="taxon:1234841"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107868
     Region          29..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknyskkyv llcaflmmsv vafaqtggik gkvvdetsla lpgtsvtidg ttlgattdgn
       61 gdyaitglkp gnysvtakfl gyiaftktit vgnsvttadf tlkpqntsln evvvvgygtq
      121 rkkdltgsvv sisakdfnqg pittpealis gkvsgvqits nsgapgagst irirggasis
      181 asndplivid nvpvsnsgia gidnalatin pndiesfnil kdasataiyg srasngviii
      241 ttkkgksgkf avdfstlnsl skivkeapvl taaefrdvts saqaglttaq kglvgtsntd
      301 wqsliyhtaf stdnninfsg gikglpyrls igyldqdgil ktdnlkrttv alnlnhdflh
      361 qslkidfnvk gtytdrkfan qgaigaavgf dptqpvysgn snyggyfewl dasgngnpst
      421 laprnplgll nqynsngytk rtlgsltlny tfpflkelqa natfggditd gmgntyippt
      481 aasnfnqtyk gsysqyfsen ytytndyylk ytkdfksiks hldvqagysy qyfhfytkpe
      541 ntyaadktnv tsaaavsfpg qyyiespfgr vnftyddkyl ltatirddrs srfselrrng
      601 yfpslalawr lkeepffkam sslsdlklrv gygitgqqdi gplfpylavy dpsnssagyq
      661 fgsaftntlr adayntlikw eqtatsnigf dygflngrin gsidyyykkt kdllfdtpvp
      721 dgtnltnhvy anignlhsrg idlninvnai stkdiswnig ynvsfnritv dnisatkdpn
      781 qsiatggipg gvgntiqllk agytpyqfyv yqqvygksgm plegvyvdrn gdgsslndky
      841 lykhpnptvf mgfnsnlayk kwnlgftmra nldnyvynav qasngayagl kfqgylnnlp
      901 nsilktnfsq yqlysdyyve nasflrmdna nlsynfgkva glrslrvtan vqnvfvitny
      961 tgldpevssg idnniyprpr vyslgvnasf
//
LOCUS       WP_094570349            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter xinganensis].
ACCESSION   WP_094570349
VERSION     WP_094570349.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter xinganensis
  ORGANISM  Mucilaginibacter xinganensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Mucilaginibacter xinganensis"
                     /db_xref="taxon:1234841"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113580
     Region          26..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkiykllai llpfiivqtv aaqsvkisgl vtakadglpl pgvsvsvkgt ttgaltgadg
       61 kftiganvnd vlkltyigyv treitvkqde pnlqivlaea anslnevvit alniskdkks
      121 lgysvqglks kdiseaketn lvnalagkia gvqvtnsqgd mgssriiirg etsiagnnqp
      181 lfvvdgtivd nsqflgtngs rdfanaiadl npedieslsv lkgpnaaaly gyraaagvil
      241 iktktgkgak glgvninsnt sfstvqllpk yqnqygqgsn gkfsyvdgkg ggvndgvdes
      301 wgpaldgsli pqfnsngqpv pfvahpnnvr dffktgvtln nsvalsgste kadyrlsynn
      361 lhqtgiipnt sqgrnsfsln stfrlspklt vttianyikd dadnlpgagg kratstmlqf
      421 twfgrqvdis qlknykdang ntfnwnnsyy snpywlayen tvgqhknrii gsvelnykii
      481 dgltanfrtg tdyyndkrki kvaygtngtp fgsyeedayt vnetntegrl qytkklnndf
      541 sldvlgggni stilneendq vapklavagl ytlsnsrdpl vssnsygkyk tysyftsaqi
      601 gfrnyafinl tgrndwsstl paanlsyfyp svngslvlse algiksdilt yaklrggwsk
      661 vgkaalpyql nniynftapf ganpqqsaas idlnpnlkpe tttsaeagfe lgffqdrlhl
      721 dvsayntnsi nqilsvdvsp atgysqklin ggrinnkgle iqlggtpika ngftwdittn
      781 yslnrskvvs ldaegrlksy ilgsdrtvqv laavgqpygt lfgnayqrna ngqiivaang
      841 tpvinptkqy lgkftpkwqg sinnsftykg vnlsflidar iggsiysntn rtgtytgvla
      901 stlpgrgaan gglsyyypgn ntsaaavqvt gsapggvtvy ndgvifngvk adgsknttil
      961 paqsyykgft nvdeafvyda syiklrevkl gytlpskwvk gaglqsatis vvgrnlwiih
     1021 knapnidpet afnngngqgl edltlptvrn igfnvnlkf
//
LOCUS       WP_094571538            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter xinganensis].
ACCESSION   WP_094571538
VERSION     WP_094571538.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter xinganensis
  ORGANISM  Mucilaginibacter xinganensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Mucilaginibacter xinganensis"
                     /db_xref="taxon:1234841"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116436
     Region          26..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqllnsif flllvfacnh aysqtrtvtg tvvakddglp ipgatvvakg snngtqtnaq
       61 gkfsvavpag attltfsfis yktvslpipa sgvlnvtmvs dfkelnevvv tgsgvatskt
      121 rlgisveavs gkaltsspqa sidqglvgqi pgaqissvdg tpgartnill rgintvqgst
      181 apmilvdgie srttdlsqld pttvdhleiv qgaaassiyg aqgangviqi ftkkgkvgkt
      241 ridvissysa gnyinqgnvh qaklssfkvd angifidasg npivrdadgr yqgiqwayga
      301 dpgngnptam snplniahqq ygtnlkyydh laqlfktayt snnsvavsga ndktdynltv
      361 snnhqqsnir nngyndrtnl tlnlgtelfk gftlrsvtql iytkntlnpn ygignaggif
      421 dvlnaspyyd fnqknadgsy plslnsgtvs vngsnpnyyt qwanrvsnre dllqsimady
      481 kinkfitlsa kyglnyqhtd qniifknqsn tltaqdlgsy ygffaanpng eldkntsttv
      541 fqnfngsani ktdfqkdfhi nlpittstll aydyrknvdk qyntyglelp qyaiynfqqt
      601 atqavsydyt tpfitygfiv nqkidfgdyg gigggfrsdy ssafgggskp ftfpnvngyi
      661 rpssfdfwkn sslgnaipef klrggfgeag tqpmpfdryp tinpqnlgsa ltfnlptsla
      721 npdlkvevsk eyeigtdigi kgasgnwfse invsgtywnr kannviysin tapstggnki
      781 ltnaiglash gfqaslnigi lrskdfnwhf ttnfsnettt itstsgapii lstaagstqe
      841 sliagqkigq iygnkaltsv tetnsagvpy ilpadyskyt ivdgrvvnia tkaiqfgsea
      901 lplgdpnpkf nasfinnfty kalsfgfqfd wvygshlynq tkewqyrdgi sgdydkavni
      961 ggtsgaytay yrsayadiig arngarngtk dyfyegssfl rlrniylgyd fskliggkvf
     1021 kravltftgr niltftkytg fdpevssgas nspfdrgvdh dstpnsksyq vglnlgf
//
LOCUS       WP_094577967             442 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Brucella
            rhizosphaerae].
ACCESSION   WP_094577967
VERSION     WP_094577967.1
KEYWORDS    RefSeq.
SOURCE      Brucella rhizosphaerae (Ochrobactrum rhizosphaerae)
  ORGANISM  Brucella rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Brucella rhizosphaerae"
                     /db_xref="taxon:571254"
     Protein         1..442
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45950
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifipke sdpnetrvaa saetvkkfia lgfdvvvekg ageksriidt efsgagarig
       61 taadakaadv ilkvrrpnda elkgyksgta lfamldpygh edavaalgka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaset ydrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedee fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vtkemvaamr pgsvlidlav erggnvegai
      301 agqvaevngv kivghlnvpg riaatasqly arnlyaflet lvdkeakllk ldpeeelvka
      361 tllthqgkvv hpafakaeae vapvaamvek vakpktapkv kapavqaeaa ketapaaakp
      421 vrkttkkapa kaaktsadgg ea
//
LOCUS       WP_094578155             318 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Brucella rhizosphaerae].
ACCESSION   WP_094578155
VERSION     WP_094578155.1
KEYWORDS    RefSeq.
SOURCE      Brucella rhizosphaerae (Ochrobactrum rhizosphaerae)
  ORGANISM  Brucella rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Brucella rhizosphaerae"
                     /db_xref="taxon:571254"
     Protein         1..318
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36297
     Region          6..173
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maitklyser qkelrgedtd vyvydkvpda lrnqiwmive enlgdrnsyy nrhqqdvsaa
       61 ydyivdtlrr eygvfelspt mstadkfndl rsfllkepsv dkfidaveii ahiidsftsq
      121 fnyrglmdar eksnaaiaei nhrfkramig feyvgnevvr idsefvhvea vkpalvilrg
      181 rgysgaqqef lsafehyrhg rakealvdcl ksfestmkai cekrgwifsp kstakdliqi
      241 clenelvpky wqqhfsclra glesgiptar nrtsghgqgv qptevpeeia symlhmtast
      301 ilflarseer ipstetla
//
LOCUS       WP_094582640            1571 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides sp. CT06].
ACCESSION   WP_094582640
VERSION     WP_094582640.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides sp. CT06
  ORGANISM  Parabacteroides sp. CT06
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1571)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1571)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1571)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1571
                     /organism="Parabacteroides sp. CT06"
                     /db_xref="taxon:2025876"
     Protein         1..1571
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=178682
     Region          34..356
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
     Region          640..>723
                     /region_name="DUF302"
                     /note="Uncharacterized domain family DUF302; cd14797"
                     /db_xref="CDD:269820"
     Site            order(640,667,669,671,675,678,685,687,693,697,700,
                     704..705,707..711,713,715,717)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269820"
     Region          <715..1569
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkiaylll llmlipvgsf akekrtfeik dghfyvngkv tpilsgemhy priphqywrh
       61 rlrmmramgl ntvatyvfwn lhetepgkwd fegdknlaey iriageeglm vilrpgpyvc
      121 aewefggypw wlqnipgmei rrdnpeflkr tklyidklye qvgdlqvskg gpiimvqaen
      181 efgsyvaqrk dipleehrry nakikrqlad agfnvplfts dgswlfeggs tpgalptang
      241 esnvenlkkv vneyhggvgp ymvaefypgw lmhwaepfpd isdsgiarqt etylqndvsf
      301 nfymvhggtn fgftsganyd kkhdiqpdlt sydydapise agwvtpkfds irnvirkyvt
      361 ydvpeapapi plieipsisl tkvadvlala kegepvaspt pltfeqlnqg ygyvlysthf
      421 nqplkgrlei pglrdyatiy vdgervgeln rcfnqyamei dipfnatldi lvenmgriny
      481 geeivrntkg iissvkings eisdwkmykl pmdrmpalvs gepyvykngs pevaalgnkp
      541 vlyegtfhls dtgdtfidme dwgkgiifin ginigrywya gpqqtlyipg vwlnkgenki
      601 viyeqlnndr kssvrtvktp vltklkkiaa mekknrlmek tvspfsvdet mrrieeiiks
      661 qggsvfamfd hgrnasevgm klppnkvivf gspkvgtllm qqdpsislel plriilittk
      721 kgtksgqprl tydgyigvqk tgkkydvlns mdrlnldwea qknnivmrdi ggypsnpqfg
      781 tgdrpsipny ltqsgaqgst tidpsdydyp tttyapfsdt dwwdeldraa miqnhqigls
      841 ggtekgqynl sanyfkqdgt vidsyyqryq vrantsfnvr dwlrvgenlt yaftkdngls
      901 angaesnpys wtyraspwvp vydiagnfag skfsgtgnfq npvanqvrnk dnyytrnrif
      961 gnlwaeadif kdltfrtnfg idytnryyyr mekknpefse smgqnnfeeq sefnyrwvwt
     1021 ntltynktfn dihkltvllg teairdglgr kltgrrynyl fedntnswvl nmgennnqrl
     1081 anseykgefa lfglfgrvdy sfndkylftg iirrdgvsrf sksnrygvfp saslgwrisq
     1141 edfmestrdw lddlklrvgy gqtgnsevpr itnyamelat ypkrsdydln gqnnstttgf
     1201 ildkygnedt kwestemwnv gvdatflngk fnigaewywk kttdmlieaq ysafanpeik
     1261 kpyinfgdik ntgvdlnlny rdskgdwswd vslnlshykn evlrisesdd aslwgagtrl
     1321 dgnvtrttkg haisefygyk vngfyenvde vlalpplgqs glnaesakaw vgkfkfddvd
     1381 kdgklterdr tfigsphpdl iaglnatvtw knwdftmfwy stigndlfnn tkyftdfwmf
     1441 ngnksermrd qswtpgadns nailpildsn dgysgkfsns yyvenasflr lknvvlgytl
     1501 pksvlskvgi qnlrlyvqae nlltitgysg ldpeytnadm gkesggdlqr gvdmggwpst
     1561 mrflfgvnfa f
//
LOCUS       WP_094615592             372 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Rhodococcus (in: high G+C Gram-positive
            bacteria)].
ACCESSION   WP_094615592
VERSION     WP_094615592.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
  ORGANISM  unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="unclassified Rhodococcus (in: high G+C
                     Gram-positive bacteria)"
                     /db_xref="taxon:192944"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38068
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqstekg sgsttvvgvv resgegerrv alvpkivasl tgkgveivve sgaglgalip
       61 delyvaagat igdpwsadvv vkvappsdae iaklssgstl igflaprnae nsigalkaag
      121 vqafaveaip risraqvmda lssqanvagy ksvllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rptgydvrpe vadqvrsvga qwldlgidaa geggyarelt
      241 edermqqqka leeaikgfdv vittalvpgr paprlvtaaa vegmkpgsvv vdlagetggn
      301 celtepgetv vkhdvticsp lnlpasmpeh aselysknis allelmlvdg klapdfsdev
      361 lagacvtrek en
//
LOCUS       WP_094622262             513 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Rhodococcus (in: high G+C Gram-positive
            bacteria)].
ACCESSION   WP_094622262
VERSION     WP_094622262.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
  ORGANISM  unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="unclassified Rhodococcus (in: high G+C
                     Gram-positive bacteria)"
                     /db_xref="taxon:192944"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52824
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgvvaest pgetrvaatp asvrkllglg yevlveqgag erasfsdsay reagatvasg
       61 dvvwaaevvl kvdaptpvei drlsddattv sligpasnae lvaalaqrnl tvlamdavpr
      121 israqsmdvl ssmaniagyr svieaahefg rsftgqvtaa gkvpparvlv agagvaglaa
      181 vgtasslgai vratdprpev aeqvrsigge flevdvaqav stdgyakats edysrraaei
      241 yseqaadvdi iittalipgr saprlitead vasmksgsvv ldmaagqggn vagsvagerv
      301 vtdngvvilg ytdlarrlpt qasqlfgtnv vnlltlltpa kdgrlvidfd dvvqrgvtvv
      361 rdghttwppp ptavsaapla apaevvapqa qlprpiwhrw vwlaggvlaf flilgfapap
      421 lpqhltvlvl svivgyyvig nvahalhtpl mavtnaisgi ivvgaivqlg vggdstnagv
      481 irvlafvatl laainvfggf avtrrmlrmf skg
//
LOCUS       WP_094639619             378 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Rhodococcus (in: high G+C Gram-positive
            bacteria)].
ACCESSION   WP_094639619
VERSION     WP_094639619.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
  ORGANISM  unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="unclassified Rhodococcus (in: high G+C
                     Gram-positive bacteria)"
                     /db_xref="taxon:192944"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38950
     Region          12..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(25,80,99,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(54,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtadpritrh tkvgvlress dgerrvalvp kivgsligrg vavvvesgag lsalipdqly
       61 veagaeigdp wsadvvvkva pptdaeiakl spgttligfl aprnadnkie alaaagvqaf
      121 aieaiprisr aqvmdalssq anvagyksvi laasestrff pmlttaagtv kpatvlvlgv
      181 gvaglqalat akrlggrptg ydvrpevadq vrsvgaqwld lgidaagegg yarelteder
      241 aqqqkaleea ikgfdvvitt alvpgrpapr lvtaaavegm kpgsvvvdla getggncelt
      301 epgqtvvkhd vtiasplnlp stmpehasel ysknvsalle llldengala pdfsdeviaq
      361 scvtraepde qsetanag
//
LOCUS       WP_094657904             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. 06-418-5].
ACCESSION   WP_094657904
VERSION     WP_094657904.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. 06-418-5
  ORGANISM  Rhodococcus sp. 06-418-5
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Rhodococcus sp. 06-418-5"
                     /db_xref="taxon:2022507"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38920
     Region          12..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(25,80,99,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(54,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtadpritrh tkvgvlress dgerrvalvp kivgsligrg lavvvesgag lsalipdqly
       61 veagaeigdp wsadvvvkva pptdaeiakl spgttligfl aprnadnkie alaaagvqaf
      121 aveaiprisr aqvmdalssq anvagykavi laasestrff pmlttaagtv kpatvlvlgv
      181 gvaglqalat akrlggrptg ydvrpevadq vrsvgaqwld lgidaagegg yarelteder
      241 aqqqqaleea ikgfdvvitt alvpgrpapr lvtaaavegm kpgsvvvdla getggncelt
      301 epgqtvvkhd vtiasplnlp stmpehasel ysknvsalle llldengala pdfsdeviaq
      361 scvtraepde qsetgnag
//
LOCUS       WP_094675538             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. 06-235-1A].
ACCESSION   WP_094675538
VERSION     WP_094675538.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. 06-235-1A
  ORGANISM  Rhodococcus sp. 06-235-1A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Rhodococcus sp. 06-235-1A"
                     /db_xref="taxon:2022508"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38018
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqstekg sgsttvvgvv resgegerrv alvpkivasl tgkgvevvve sgaglgalip
       61 delyvaagat igdpwsadvv vkvappsdae iakltsgstl igflaprnae nsigalkaag
      121 vqafaveaip risraqvmda lssqanvagy kavllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rptgydvrpe vadqvrsvga qwldlgidaa geggyarelt
      241 edervqqqka leeaikgfdv vittalvpgr paprlvtaaa vegmkpgsvv vdlagetggn
      301 celtepgqtv vkhdvticsp lnlpasmpeh aselysknis allelmlvdg klapdfsdev
      361 lagacvtrek en
//
LOCUS       WP_094696224             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas sp. A35_P].
ACCESSION   WP_094696224
VERSION     WP_094696224.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas sp. A35_P
  ORGANISM  Aeromonas sp. A35_P
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas sp. A35_P"
                     /db_xref="taxon:1983805"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53371
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tglgtsgwaq aadetqpkgk vearselfak dhadqfsswk
       61 atgesrertd alaedpqmvv lwggyafakd ynkprghfya ltdvretlrt gapksaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy ftsptkavkf pwdkgttveq
      241 melyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg ivkqrkeavt eiklkvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakgisq eiaipdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeakvagrla
      481 q
//
LOCUS       WP_094702233             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. 15-649-2-2].
ACCESSION   WP_094702233
VERSION     WP_094702233.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. 15-649-2-2
  ORGANISM  Rhodococcus sp. 15-649-2-2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Rhodococcus sp. 15-649-2-2"
                     /db_xref="taxon:2023140"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38920
     Region          12..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(25,80,99,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(54,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtadpritrh tkvgvlress dgerrvalvp kivgsligrg vavvvesgag lsalipdqly
       61 veagaeigdp wsadvvvkva pptdaeiakl spgttligfl aprnadnkie alaaagvqaf
      121 aveaiprisr aqvmdalssq anvagykavi laasestrff pmlttaagtv kpatvlvlgv
      181 gvaglqalat akrlggrptg ydvrpevadq vrsvgaqwld lgidaagegg yarelteder
      241 aqqqqaleea ikgfdvvitt alvpgrpapr lvtaaavegm kpgsvvvdla getggncelt
      301 epgqtvvkhd vtiasplnlp stmpehasel ysknvsalle llldengala pdfsdeviaq
      361 scvtraepde qsetanag
//
LOCUS       WP_094712532             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Hahella
            sp. CCB-MM4].
ACCESSION   WP_094712532
VERSION     WP_094712532.1
KEYWORDS    RefSeq.
SOURCE      Hahella sp. CCB-MM4
  ORGANISM  Hahella sp. CCB-MM4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Hahella sp. CCB-MM4"
                     /db_xref="taxon:1926491"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53968
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipkehk phekrvaasp dsvkeliklg ftvvvenhag glssfhdday eaagakvvev
       61 kdvwqsdiil kvnepnenev elikpgatli sflwpavned likqlaekki tamamdsvpr
      121 israqsmdal ssmasivgyr avveashhfg rffsgqitaa gkvppakilv igagvaglaa
      181 igtagslgai vrafdtrpev keqitsmgae flevdieeet gsgdgyakem sqafidaema
      241 lfleqakdvd iiistasipg kpapklitee mvkamkpgsv ivdlaapngg nceltepges
      301 verygvtiag fvdlpsrlpa qssllyannl vnlmkllckt kdgiinvdfe diiirgvtvt
      361 kdgdvtwppp pvkvsaapkp kaaqpaaepa pkkempkelk hglmlgagvl flwlasvapm
      421 dflshftvfl lacivgyhvv wsvthalhtp lmsvtnaisg iivvgallqi sssstlvmll
      481 aaaatlvati nivggfvvtq rmlkmfrr
//
LOCUS       WP_094720972             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. 14-2470-1b].
ACCESSION   WP_094720972
VERSION     WP_094720972.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. 14-2470-1b
  ORGANISM  Rhodococcus sp. 14-2470-1b
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus sp. 14-2470-1b"
                     /db_xref="taxon:2023149"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37973
     Region          13..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 metsqstesr ttrvgvvres vdgerrvalv pkvvasligk gvevvvesga gsgalipdel
       61 yaaagatigd pwsadvvvkv apptdaeisk lssgstligf laprnadnki dalaaagvqa
      121 faveaipris raqvmdalss qanvagykav llaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrpt gydvrpevad qvrsvgaqwl dlgidaageg gyareltede
      241 raqqqqalee aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvvvdl agetggncel
      301 tepgqtvvkh dvtiasplnl patmpehase lysknvsall ellldengal tpdfsdevia
      361 qscvtrkaes
//
LOCUS       WP_094738637             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. 14-2483-1-1].
ACCESSION   WP_094738637
VERSION     WP_094738637.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. 14-2483-1-1
  ORGANISM  Rhodococcus sp. 14-2483-1-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Rhodococcus sp. 14-2483-1-1"
                     /db_xref="taxon:2023148"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38033
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqstekg sgsttvvgvv resgegerrv alvpkivasl tgkgveivve sgaglgalip
       61 delyvaagat igdpwsadvv vkvappsdae iakltsgstl igflaprnae nsigalkaag
      121 vqafaveaip risraqvmda lssqanvagy kavllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rptgydvrpe vadqvrsvga qwldlgidaa geggyarelt
      241 edervqqqea leeaikgfdv vittalvpgr paprlvtaaa vegmkpgsvv vdlagetggn
      301 celtepgqtv vkhdvticsp lnlpasmpeh aselysknis allelmlvdg klapdfsdev
      361 lagacvtrek en
//
LOCUS       WP_094764087             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Luteococcus japonicus].
ACCESSION   WP_094764087
VERSION     WP_094764087.1
KEYWORDS    RefSeq.
SOURCE      Luteococcus japonicus
  ORGANISM  Luteococcus japonicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Luteococcus.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Luteococcus japonicus"
                     /db_xref="taxon:33984"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53921
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresk pgenraaatp rtvqdliklg ydvvvehgag drssatdaaf eaagaqsvda
       61 qtvwtsdivl gvnepdesql smmrpgatli sflfprqnea ltqrlaqqgi tamsmdmvpr
      121 tsraqaldal ssmanisgyr avveashafg rfftgqvtaa gkvppakvlv agtgvaglaa
      181 igaansmgai vratdvrpet aeqvesmgat flhvkgpsqe istdgyakea sddfaaraae
      241 lyaeqcmdcd iiittaaipg rpspklitre mvasmkdgsv ivdlaalggg nceltrpgek
      301 yttdngvtii gytdlasrlp gqssqlygtn lvnalklmtp ekdgqfvvdf ddevvrtmtt
      361 vrngeitfpp ppiqvsaasa apataaavpa vveapkkpkp wwqpvvtigi aslaliallt
      421 vaptsfvslf gifalavvvg yyvvwnvtha lhtplmsvtn avsgiivvga itqlgsdnwa
      481 vkiisfvavl iasinvfggf tvthrmlqmf rkea
//
LOCUS       WP_094752342             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychromonas sp. CD1].
ACCESSION   WP_094752342
VERSION     WP_094752342.1
KEYWORDS    RefSeq.
SOURCE      Psychromonas sp. CD1
  ORGANISM  Psychromonas sp. CD1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Psychromonadaceae; Psychromonas.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Psychromonas sp. CD1"
                     /db_xref="taxon:1979839"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54434
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipkeiq enenrvaatp ktvellikqg fsflvennag anasfsdtaf keaganisad
       61 taqvwqsdii fkvnaptsse idlikegatl vsfiwpaqnp ellkqleakn isviamdsvp
      121 risraqalda lssmaniagy ravieaanef grfftgqita agkvppakvm iigagvagla
      181 aigtagslga ivrafdtrpe vkeqvesmga eflevnyqee eevstsgyak tmskgyqdaq
      241 almmaeqakd vdiiittali pgkpapklis kemiasmksg svivdlaaqa ggnaaftvkd
      301 evfvtdngvr iigytdlpsr latqssqlys nnlvnlmkll cknkdglidl dfedevirga
      361 tvikegkisw pappinvsat papkvapkva tvtpekksnk yikplavlif aclfgyvasi
      421 apsdflahft vfilaciigy gvvwnvahsl htplmsvtna isgiivigal lqvgsdnaiv
      481 tvlsiiatli asinivggft vthrmlkmfq kdk
//
LOCUS       WP_094766301            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            agarivorans].
ACCESSION   WP_094766301
VERSION     WP_094766301.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina agarivorans
  ORGANISM  Aquimarina agarivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Aquimarina agarivorans"
                     /db_xref="taxon:980584"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115323
     Region          33..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmknnfrlvd rlksmlfvsv lllgfgfmna qtktitgtvt gegyplpavs vlikgsssgt
       61 vsdfdgifil eaeegdvlvf dyvgfksqev vvgkentinv smkedvsvle evvvvgyqkq
      121 kkievtgais svkgdeltkq avgdpaealq gklagvniqa ssgspgaran vqirgansln
      181 gsdsdfnnpn aalqnpladg lsplwvvdgl pvtgdpnlsp seiesievlk dgasasiygi
      241 raaagvilvt tkrgvkgklk vdfntyssvn rltrrvsvln ssqalandrn iientggqvq
      301 tegiltrnpn afnfdtdwqd eilnqyaysn nanlrfsggv dflnyslnid ylnqegnivn
      361 snfertnikl ntgfnnggkf naftsfsisn snarvepwri lydaltapsy iqgpgdlana
      421 ntisldensa ntiaannvid klrqenrret lsgslygtfn ynwfegfntk lnlsfsrfdl
      481 kdrffdpaff flgldggvne gqiaqtiatl qerrglgkts lveffteyek dfsghklsgl
      541 vgvtsenrsw aqsgvsvrdf dtagfpnina akdksavqas gnltvnklrs lvgnmgygfk
      601 ekyllranvr rdqtsnftae nraetfggis lgwvpskesf iensdflsfi eslkfrasig
      661 wvgnqnveaf ianpgissgt niilgtrnve vvgisrtqig nldltwetsv senlgvdlll
      721 fggafnftge lyrvekdnll flantalssg fnptfpspta tvfsnvgalv negveltagy
      781 rdikgkfqwn lsgtftsnsn eitalagtts qinggqpapg tnqlqnfpvn fgregfpvgs
      841 fflldsdgli rnqteldeyq llggaipsna kigdlrfkdv dgdgsinvqn drtfkgsslp
      901 dfeiglnygm nyqnfdfsmq wfasfgakiy ngpkalayna qnhtdllfay radnqaseip
      961 inrqrarptn flsitdqfie dgdyirlrni qigynfpket lkkanlsklr iylaasnvlt
     1021 itdytgfdpe vggnglfsrg idrgytpvtg sgrlglelsf
//
LOCUS       WP_094766613            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudozobellia
            thermophila].
ACCESSION   WP_094766613
VERSION     WP_094766613.1
KEYWORDS    RefSeq.
SOURCE      Pseudozobellia thermophila
  ORGANISM  Pseudozobellia thermophila
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pseudozobellia.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Pseudozobellia thermophila"
                     /db_xref="taxon:192903"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120606
     Region          55..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnlktfraq lkciagllgi lgfltsgldt klyafaggdy pgepptdara vqdltitgtv
       61 taaedgmpip ganvivkgtt tgtttdfdgn ytievpssss vlvfssigfa tkeitvggnt
      121 tinvimdtdv atleevvvvg fgtqkkatlt gsvtqvkged imkgkgtsna alalqgevpg
      181 vvvtrtssrp gnegtdikir gdisvnnigp lilldgleip ewqlatlnan diesysvlkd
      241 gaaaiygtka aggvilvttk kgkqgkmqvn ykgetqmnip hdfpvanlqe waqmwlragd
      301 ndgisyvdad gvtqqaasny rfftrdelvs iidgtlpmap dsyfwlgkeh rfddvnqfda
      361 vygstlsqrh dlsvsggsen atyrssigya nerspiafvy dgakkynfrt nltyrmsdmv
      421 kteltvsydn rlvdeptqgv ghgvqdmylf plynpqgqyy difgannlla kldeggrtkt
      481 qeeifrlggv itldldkyik glsfkyngnf ssrnglrter ttsvtmydwd gnisytpttl
      541 ltsgvklyet dvmfqnhvlq anyqrsfgkh nlgllaglta eeeqtnkyyq srtnmasdel
      601 ddintgdvtt qinggshkns ngnwfysgss avglvsyigk lnydydgiyl lealgrrdgs
      661 srlhpdyrwk nffsasagir lsemefmkdg ffdnlklras ygetgsvtgi gaydyisnis
      721 vgttifgatp alantayias ltstertwer vattnfgidy amlnnrlsgs aeyfirennd
      781 mlipitypqv lgasapktns gdfktngwev slnwrdqvge lnynfgvmvw dsesevtrme
      841 gataialgvn dpiegkplna iytyktdgyl qteeevlayy nqygfvdpsn qlemkpgtvl
      901 pnyrsadrlv pgtvnridvs gdglineddl vyfgdanphm syginlgley kgfdfsaffq
      961 gvgkqnivre galaypfrsw wtnqnpsflg ktwtedtpna aypasfyngq rknwnyghin
     1021 dinvikasyl rakvltlgys lpqdvlaqsg lervrlsvtg ndlfvisnvk dgmdpemgss
     1081 anqgntvpyt stvllgievt f
//
LOCUS       WP_094766590             950 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudozobellia
            thermophila].
ACCESSION   WP_094766590
VERSION     WP_094766590.1
KEYWORDS    RefSeq.
SOURCE      Pseudozobellia thermophila
  ORGANISM  Pseudozobellia thermophila
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pseudozobellia.
REFERENCE   1  (residues 1 to 950)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 950)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 950)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Pseudozobellia thermophila"
                     /db_xref="taxon:192903"
     Protein         1..950
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106682
     Region          47..945
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miqlntlskl llcgcfcmvw clsikaqtid stdtivlsdp lnrlesnlee evnlgfevgt
       61 rrdivgasst vkpddflkfd ttqwvqdals grmtglqgss nirglgnali vvdgipgrdi
      121 nilnmeeiee itilkdanvs alygsmardg vivvttkrgs tkrefnisas tgvrlpirmp
      181 nylnsaeymq yfnearvndg lgelysaeqm enhrsgtnpy rypdvdfydk anfspltpya
      241 nvtadfaggs entkfyinlg fksdgsfqsi npenekgakr fnvrgnidfr vndwikssld
      301 vvaiidknkg slsnvyqdgs tfkpnlyspl ipissidfsa npqlrgivda ahqydgfllg
      361 gnqaysdnvp ianifaggyq tnmtrvsqvn nsidfdlnai teglsaksyv sfdfyniynl
      421 svqnkfavye ptwndegriv dlvnvkdtdl kdqvenvntd ffairygfyg lvnydkkwne
      481 dhginaslvg fanntyvrse kqsaknshva lslnynykdr llanfsgayv nsvklaeghr
      541 gkfapsvgfa yvlseepslk gsswlnyfkl rssigviysd lgiqdyflyd aiyeqngggy
      601 nwgdtngsgy ynastkilrg entgldfekr tdftlgfesl lfkkfwlegn vfqsimgdkv
      661 irastlypey ydsfrpytny nkdqysgfel gvnyyskagn stfdigarml ytrsertkvd
      721 evyqddyqyr kgtpvdaiwg leslglfqvd efnpdgslkn glptqygtvr pgdikykdqn
      781 gdgvvndqdm vqigrygapw sfgsditwsy kaftlfallt aqvggdgvls gdyyrpqgda
      841 kysevvkgrw teataesatf prlssigsan nfektstywl ysndnfriqr vqltydlpsq
      901 lisklkmkdi slftsvsnla efsknrkire lqlgynplfr yysfgarmkf
//
LOCUS       WP_094766795            1139 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudozobellia
            thermophila].
ACCESSION   WP_094766795
VERSION     WP_094766795.1
KEYWORDS    RefSeq.
SOURCE      Pseudozobellia thermophila
  ORGANISM  Pseudozobellia thermophila
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pseudozobellia.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1139)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1139)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Pseudozobellia thermophila"
                     /db_xref="taxon:192903"
     Protein         1..1139
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126021
     Region          54..1095
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkeiknngrp krlflkldyr tvflllcsvi iqqgafasks vhehtyttvp qtaitgtvtd
       61 esgvplpgat vlevgtsngv stdfdgnyti vpsgdspvle fsyigyatkt itvngqtsin
      121 vvlaedasel eevvvtglgi trakkaigya vatveaeslv eaaptnfata lygkapgvqi
      181 aatpggntsa vninirglns ingsnqplii kdgipirnqd vsnsnywsnq rvegnglldi
      241 npedienisi lkgasaaaly gseavngvvl ittkkgkgkg wsgefnsvys fdnvaympkw
      301 qnergpgypw yvatwgddvd edgfqwydtn gdgtpdtkgv igtnlnygpr fdgqpilawd
      361 gkvrpytaqn syeglfktah ntrfnvglsh vsdkantrfs ytrsdnqait pnssnynntf
      421 slnsnidwtd nfrtqvvvdy ynkkvhnrpy kidrivnnfg gmmnrfdnad wyedqyktsl
      481 gyryvtgsgq sltpdeniti pgyrgdildy fwrineydye easdrviaal tleydflndf
      541 tlrarashdf tseytedkrp teiplvynnt tgmfgmrqkk dnvkygelll tynkainddf
      601 svlarlgyna eertnrmtql qtvggltven wfdlsasrlq pttanlkgwn nrdnylrdgi
      661 fgtlnldykg flyvegtirr dristipaay ngftypsvng sfvvsqafel pqsidllkvr
      721 gswgvvgnap elyaaniayt qlgingseti yttlptqygn dqikpeekhe iefglelkml
      781 qnrigldvsy ydaeirdqil qytlprstga qsvlanigil gnkglevgln gspirtsdvd
      841 wslginfsrn vntvkkltdd sdqlvhqdqd gsavrlvsnv geamgdimvh plltdengnn
      901 vvsdnglylv dsdewvkagn vnpdfiggiw sslsvknfsl dfsidyswgg eimpkgyywm
      961 vgrglteesl afsdaarggi syypsqvgdd vqliqtsssq gpagesvynd giilegvktd
     1021 gtpndivvsn pdyfwtvynw ggpayspnar ydlfvrenny lkmreisigy sipkdvvekt
     1081 glssinlsvf grnlfylyrs ikevdgeavt vgtdwkenwy ngangwtskt vglqlrasf
//
LOCUS       WP_094766808            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudozobellia
            thermophila].
ACCESSION   WP_094766808
VERSION     WP_094766808.1
KEYWORDS    RefSeq.
SOURCE      Pseudozobellia thermophila
  ORGANISM  Pseudozobellia thermophila
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pseudozobellia.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Pseudozobellia thermophila"
                     /db_xref="taxon:192903"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116601
     Region          27..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkkfaslil msvfavlalh aqekdltvag vvtdmdgvpl pgvsivevgt vngtqtdfdg
       61 sysievavgs elrfsylgmk tetrtvqssn vlnikmqedl nqlsevivta lgiekskkal
      121 gysaqeidgd afsearetni asslagkvag vqvsniatga ggssrvvirg nssisgndap
      181 lyvvdgipid nqnidpadya aggvdygdgi sginpddves mtvlkgpnaa alygaraang
      241 vilittktgg skkkgigvtf nsnltsetia tmptyqnrfg igydpsfgas gttiidgkey
      301 evldpnqwqs wgpelngqiv adwedptktf amvpqpsdni rnffqsgfta tntvsfssgd
      361 ekanmrlsls nlgnegiipg stydrqtinf rgfanvtdrf sidakvnyih hkgvnrpgla
      421 asssnvmsvl iqmprhidld rlkdykdeng dpfnfttafe npywtinelq nederdrvig
      481 fvsmnykfnd wlnvrartgt dfytderfsr raigsrsart grvsnytwhv kennsdilft
      541 aeddlsenws gslsvgasrl ysktevtgal gqslrvpely hitnaeqitp rydkveremq
      601 svyaagqlay knylfldlta rndwssvlgi nnysffypsv stsfvftdal klnsnvfsfg
      661 klragyaevg ndsnpylttl gyvsntqtvn gqgqaaiqtq ipnpnlknel trsyefgtdm
      721 rffknrvgid ftyynsstkn qilpvnissg tgfnrmvina geiqnegvel lfnvtpiqlk
      781 nsfqwdltln yaknkskvvs ladgiethim sqdrwgtiea rpgedfgniv gfyykrneng
      841 eklldeygry qrdgnnvkil gniqpdwiag itnrfsykgf tlstlidikm ggellsgtky
      901 iqaargtgrf ttkglrqned gvwvgvadgv mendyyvddg ngnqvlhlaa gersdieldr
      961 vnlygmwtra diieefvlda syislreinl gysfseklla ktpftsaris lvgrnllylq
     1021 ehmdgigvtp eaafssesgs qgsesytlps trsvgvnlnv af
//
LOCUS       WP_094771395            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094771395
VERSION     WP_094771395.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117996
     Region          32..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmyenppkk nlfgilvlll llcqqlnaqq qrtitgivkd ekgkplsdls ivekgmgnas
       61 ksdadgkfsm klksanptlv fsyvgylkqe kllsagentl ritmqedgtg ldevvvmgyq
      121 dvqrrkttga iatvkgkdfe ntpyatfdam lqgrvagltv lstsgepgtn nivnirgtsn
      181 lgladnvlqa plyvidniiy dvsdiqaayg ntsplqainp ndiesvdilk dasasaiyga
      241 raangviiik tkrpahgkpe irisayngvs nrpamkpitv gaaerrmkmn llynggaydw
      301 fnngsisqml tdslnpsfnn nvdwqglflq saninnvnms igatmekfmy rfsaqryyeq
      361 gvmmgfenen ltprlmlqan ptdnfqfetn lfagftkakh gsgddqkypf stwgfpssfy
      421 eitdveeriy tgrydgmmdr dnsfslngnf aatlkkflin gltlrsqfsf nvnnntrdlf
      481 rpklltgnrn faqnwvnqnk rwewetyfny iksirnihnl savlgtgier ntsnnnymyg
      541 ysdngdyvkt vtgippgsdl yavtsisers rvsffgrfgy dykdkylvsa syrmdassry
      601 skdnrwgifp sisagwvlse epffqevknv vsffklrgsy gltgrdpgsv yaryntltfd
      661 asyngsvldn giegsllsyn gvrttypnyg spatsatikw erspqlnigf dmnllhdrlt
      721 vtsdfyirds kdlvydlmmp itsgyssisn nfisvrnsgv eltlvsrnma pgsafqwttn
      781 fniaynknyv tslpdggkei qvgppwmqra lnvgqpifpf kvwdvdgvya tnadvpidpl
      841 tgrriyhfnq svpyqagdpr rrdvngdyvi dyndkidmgn pnpdlvggfi nqfsyknfsl
      901 stlisfvvgr slwngylsdk lqdagsssly ntwgtnsaia gdfkssdfwm kegdqtkfpn
      961 lfrntvdnwh ianstfvena sfvrlkniql sytfpqamiq klklkmlriy gvvdnvaiks
     1021 wssvpdpeav qangystgng ypipkkwtig ldvtf
//
LOCUS       WP_094771009             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_094771009
VERSION     WP_094771009.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53588
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tsgihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_094771506            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094771506
VERSION     WP_094771506.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117930
     Region          24..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqfcitiil ftcmlgntll aqtkmvkgtv kgtdnkpisg vsirlespkr dlgksgsdgr
       61 fvisvpvdgv miftyqgygt vktkvtaakn eyniemdskn qeidevvvvg yqqrkretlt
      121 gsvvtisgke iqdipagnfv dllqgkvagm niqnntgspg mrgtiavrgi snfnvsgsgd
      181 nafltptspl fvidgvpidd nsgyeygfes agpgvspism ippedvedit vlkdaqatal
      241 ygsrgaygvi lvrtkrgnsk vpivqyqgqf flssvptlrk viggrderml rveqilrndt
      301 tlarafqrin dspmladsln pyynnstdwq syfyrntynq thnvnisgge rvfnykvnmn
      361 yydengiian tgfkrytvqs nmqyepndrf rmmanvnanv aenqmgsgna mmqtgvgksv
      421 nttslypaps lfsgsmgals alsvddqnkt gnyvaqvelq yepirglras stfnynytts
      481 tkdrytpell lgnssevygy ydnkskvynr nllswvkain ekhvinlygf temeisqssa
      541 dlniirgtan dqfqtgisyd trrtlgglln nlsnyrsvay agnasynyds kyiidltyrl
      601 dgtsvtggks pwssnpslgf rwnfkkekfm dkfdwwdtgf frgsvgrtis ptgtlsdlyg
      661 wykiddgryn nrpttsldlt napntelvpq tttqwsigte lgffnsalyv vyetyykqsd
      721 kilrkkpian hnafgnvltn esamvnmghe ltinfrprlq nrewelsgta tfamnkdyma
      781 slpdgarqll eadgsgynlp tyyrlgrnsq tfvlydykgv yksddevpvn pltglryrag
      841 gesaegkffr agdpiftdln gdyildendl vyvgnsqpkm tgglslfvrh kgwslrtqfs
      901 ytldrdilnt aladrfrnys tptgiyanpn dqpgayvpld aynvwrelgd nadypnvsdf
      961 trlslynpyr ynstmfledg syikfnsatl gynfdrkwiq rfgissarln ftanniytfs
     1021 hysgpdpeiv tgvgrdgsng ypskrtyslg invqf
//
LOCUS       WP_094771507             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094771507
VERSION     WP_094771507.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110728
     Region          58..975
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlfcflfl vpmlqkthar swdmwrmqqd tseisevdqq llrgrlksll qkksvkdsln
       61 fkqvetlplv sisevlkgqv sglyvqessg epgsiknmvi rglgsplfet kdainvqpav
      121 yingvpiare nnftysiqqy qfnrigpatd nfagidlsai esiqvikdpi elaklgplaa
      181 ngaiwiltkp gkegkreinf dayvgmatkp tvtpvnaqye nlfrssfysk yastfdrlay
      241 pgylsdstnv nyygpanwne eyykttpiyg gnlgirgggd ranfafmggy vknassadkt
      301 nferynalfn vnmapfkwfn fgttinasrs lrdrnkslrd rfgeasyvpd lsvpispnka
      361 myteylsmyd kaldnnsvnm lnllvnldly llpnlkfnss lgvdysegar qaffpsslme
      421 tnnymssyfg fnqrlvfnns vnynltvqek hkfnftlgsa ytqdlyrysy araydgpndf
      481 ikvnvvdgns nnagylkpvg glyvnrwsnr edfrlhslyl sgeyswnnkl dvnailrydg
      541 sstmqpdsrw iatpafaaky hfipeandgl wnhfdvkasw arigkpifts kyaigpnyta
      601 dlnwgseksl vsyngfavas rpysegwvgy dinwpytdha eltfdgslln krldfalsly
      661 qkkdvnqlin tpipaeygys gqiingmavq nrgidlnlga qvlhdpaslq wkssltlsfn
      721 qnkltalpeg reelvvgdrl lkvghaidqf wlyenegiyn eeseipvqng qklqfdgvnf
      781 avgdprwkdq ngdfqvnded rvmkgnampk ivgafqnqfn ykgfdlnfqw yfalghkamn
      841 qrasnkydfi ntentnsleg irevfhwqqd vdiskypiyn pwssivayrv dqdlflenas
      901 flklralsvg ydlahlnsik dkvktirray vyvsgtnllt iskfsgkdpe lvdfngyytg
      961 yglplspmis mgiklel
//
LOCUS       WP_094771687            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094771687
VERSION     WP_094771687.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119165
     Region          51..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnhyylshlk kallvcsilk csshslfasd lafntqvlpt ifeqesvsfq gkvvdgngrp
       61 lvdvsilngn ksigktdkdg afslhvtkgt vltfkslghr sheehvikps shieiklhtt
      121 eraleevvvt algikreeks lgysvstvkg eeltnavssn wmdalsgkva glnlmrsgag
      181 pvgstkiilr gennltgenq alivvdgvii nsgsgrrsgn vsdaiygtgg dnmpadygsg
      241 mddlnpedie svsvlkgpga aalygqkaan gaviittksg akrngkslgi tlnsntsfes
      301 vnrwpdlqye ygqgtggsdy ysygtsidgg stsgtssayg pkfdgqyffq ydpnlqavgt
      361 ertlwkpykn insffdvgkt ymntisidgg tektnarfsa tnvrntwivp ntgydrntva
      421 lsvnsrvsdk lsitskvsyn nrhsdnlpga gygnqslmyw fifwqpsadv nwlqdywvkg
      481 kedrkimypf ssypenpyai syefinrnnr ntftgnaqas yqfskefsaq irasidfsse
      541 drgqlrpyda gsklaegsyr tqeifsketn ldfllkydkk ihedwqitat ggggtlrnny
      601 rmtslasdgl tfpgvynhtn nkygiksvqd irnfeinsfy glitagfkdy lffdatgrmd
      661 wsstlatsiv pdknvgffyn sfnsslvlse vfslpktinf aklrasvawv gsgvdapymt
      721 qfgyvggnpl iggslqnpst lvnpyiepls trsiefgtdv rmfknrlnid vavyqgntsk
      781 qhlyrtidps sgysrylmnm gevrnrglei avntnqlvnk hgfnwsssit ysantnkims
      841 ipdssivlqy rsvgsgqivg lqggsmgdmy gigyqrapdg qviydektgv allteqvvyl
      901 gntiptgkls lgntfsyknf rlnvlfdtqw gavghslthy klaeqgktkn tlpgryngii
      961 gngvvsngdg tyrkndvvat nideyyrshy gqdnaegstf ptdfikfrea rldysfkkdv
     1021 lkrwgldrat iglygrnlfi wskwpafdpe fgtldggdiv kgfeiaqfps trtigfnlvl
     1081 gf
//
LOCUS       WP_094771754            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_094771754
VERSION     WP_094771754.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121374
     Region          28..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msyfytksag lalctlfsas tlfaqqsvtg kvtdatgpvs gvtvsvkgts rgtqtaadgs
       61 ftiqaaqget lrfsnigyka teiivgstkt invtltddas aldevvvtam gikrapkelg
      121 yamstvgaee ltktgspnfa galygkapgv risaapggat sgininirgt nsitgnsqpl
      181 viidgvpmrq ttfnnsdywg dqrargngle dlnpedieni tilkgasaaa lygseamngv
      241 vlvttksgkg skgfsvdfna tythdqiayl prfqdvrgpg yslayanggq aedkffyysq
      301 draingvtrg vlpatinfgp kfdgqptiaw dgtvrpyeaq nsynkffnnp nnttfnlalg
      361 httensntrf sitrqdnqmt sldsynkkni anlnssfklw nnfttdvvvn yinqhthnrp
      421 fltdrlinnf tgmistwdnp ewyldrykts qgykfvtgtn psltpeenlt yngyktdvld
      481 yiwntkarqy densnrligs ltntwqitkd fsvrgrfsad mtnnkiddkq pnerpislen
      541 tgyyslqnqs aniyytdlla sysksvtpdi klgamagyta tksqttnmns ytdgglsvrd
      601 wfdinasvnq arttnqklns lrdavfgtln fnfkdywfve gtlrrerisq mhpdnnvlyy
      661 psvnsslils eafdlpsafn yaklrgswgi vgnyptiyqs alsytqatlg nqgsgtavly
      721 tniptssfgn ekilpetkhe iefgletrlf nnrlgfdity yngkivdqil nytlpistgs
      781 tsilanvgtl rnkgwefait gtpiqngnfr wntvlnfsmn knvveelpgg atellhrdyd
      841 gaaaqliskv gqpmgdimth pialddsgnk ivqanglyki dadkwekkgn ampkavggfi
      901 ntftyksftl dalidfrlgg hvmptginwm ksrglleetl tnmdaehggl syyldgngkg
      961 vayngtsgpn gqkvyddgml tqgvladgst ntniisqayy yaqtynwggp qysnsnygly
     1021 vqknnyfkmr eislgyklps avaaklrakn vqisafgrnl fflyrsikdl dpeqmtggsn
     1081 winnvsnagt spatrtyglm vrasf
//
LOCUS       WP_094771758            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094771758
VERSION     WP_094771758.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118371
     Region          28..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msyfykksag lalctlfsas slfaqqsitg kvvdakgpvs gvtvsvkgts raaqtsangt
       61 ftiqaaqget lrftnvgyks seiivgstkt invtlnedas aleevvvtam gikrdakalg
      121 yavsniksee itkagntnfg salygkapgv kittapggsa savnvqirgi nslnyqrqpl
      181 yvvdgiiirn dqqngaggan nnnfnndqri rgngmldinp sdidnisilk gaaasalygs
      241 daasgvivit tkkgtkgrgl gvdfnyngsl eraaflpkfq neygpgydat inttngatae
      301 gwiadpksps grrpyfrsyg sfgpkftged vlwwdgqvrp yvarennyyd vfdkgynsta
      361 nvgisnqtek lnyrlsatrm dykstspgsk qnkntvnlns slklsdkist divanyintn
      421 thnrtyllgn vlgsfdgffs rtedmaamkn ayqtsdgyky skygtgrped fiytmrasnl
      481 ldyfwnqykn sydeienrll tsatlnwdiv nhlkfrgrig ndftsatstn kqynenatiy
      541 nasdrstggy attkgaysil ygdlmmtysn kinqdfdysa svgfqsrsen yddqysstea
      601 glvtenwfsi snslaqpltt nnrkemlkya yfgslnvgyk gyayldgtyr seysstlpsq
      661 nnnyqygsvs gsfifsdafn lksdkfaygk lrasygivgn daaiyeania ytqaplltvn
      721 gaipsltykn rygnldlkpe rkyemefgle lkflknrlgl dvsyynnyie nqilglttps
      781 stgatsqiln igkianngle lsingtpiqn dnftwtsrln ysfnnsrvke lmagvnelvf
      841 ysadanslki takageklgn iyvydiakdn ngnnlisdeg yyvidktkyk mvgnimpkai
      901 ggwtntftyk nfmldftady rfggkmvsen lkygmasgly entlpyretg vtlpgvnant
      961 gktndvhlsg aeyyfntfnw gddswsekga vydndfiklr elsigyripd sftkkikmnn
     1021 lrfsligrnl fyiyrtlenl dpeapvgnaw wsqgvdvgss aatrsfgfsl nanf
//
LOCUS       WP_094772290            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094772290
VERSION     WP_094772290.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117517
     Region          26..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkhttnfvv aaalclssst lyaqstikgk videhntaiq gatitdinsk kqiqtdlngl
       61 fefpsnentv tlqvqyigfe tktiqanisg lntiqltpts sqlnevvvta lgisrekksl
      121 gyavqevkgt elqtrptnal salsgkvagl qvttsggnmg gsshvllrgi nsisgnnqpl
      181 yvidgtpidn tdlnssstin gsagkdvgnm iqdinpddie nisvlkgpsa aalygsraan
      241 gvilittkra skgekvdisv ntgldfenit rlpkrqhlyg qgystsfqtq ningkdykiv
      301 dyasdeswgp kldgtpvlqw ynlnpedevn ylnpspwlyp kndvsyffkt giantnnfai
      361 agstgntnyr fsytnknvtg tvpnsslgrn tfnfsggtql gkikvtsnfn yirnssvgrp
      421 wtgasnrnii leafqwgavq vdykilenyk radgtplawn rtgwqnttaa eatrfidnpy
      481 wsayesymed srdrfygnig lqydvnnwls vgakvhgdiy sfqsqdriav ysrstsqyee
      541 msnklneyny eflatakknw dkfslianvg anlrdqqrkn dyaitqggli lpnyynlkna
      601 savkidnfky hrriasiygs fslgyndlly ldgtirndws stlpvennsf iypsltgsfv
      661 fsqlpafkql dwlsfgklrl gwaqvgndtd pyqlykvyda eqafegtpgy slpntkpnas
      721 lkpeitsswe tglnlqffkn rlgldvtyyn nnsrnqilav pvsssfgyan kifnagkinn
      781 kgievvlngt piktenfswd atinwaknkn kvikldeqvn tlslsntlve lvaregqsyg
      841 qflgydfvyt pdgervvqed gtfmktsqlv plgsilanyt fgfqnsfryk rfnlgflvag
      901 rvggkffsqt ykvgmysgil dktaannire tgitldgvka nvafnsdgty evtnirentt
      961 nitaqqwarn eyngptafsi fdatfiklre vtlgynfpit nskliknvav niygrnlwni
     1021 ytkskyidpe ftssggnvqg ieggniptpv tygfnvnlkf
//
LOCUS       WP_094772446            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_094772446
VERSION     WP_094772446.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119000
     Region          24..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktaiafla anllvssaiy aqtvlkgtvv gqdgkpipgv sislqdgtgt qtgpngdfsi
       61 sykqagtlsv saigyerkqi nlsnqtnlsi tlisntesld evvvtamgis rdkkslgyav
      121 qevkakeltd agqlsvtgal tgkvagvqvn qfggavgssa risirgntsl lndqqplivi
      181 dgvpitnnsq rsgdntyggv dygsglndin pediesmtvl kggsaalygm rggkgvimit
      241 tksgkranng vqisydanfs mdraatipky qnsygqgsrg deynyllses gltyqeyalk
      301 nsfsyvdgag ggvndgfdes wgprldaglm ipqfnspvvd gvrqstpwvs hknnvkdffq
      361 tgfsqnhnls llsksdrsst raslsfrdqk gtvpntdqkk ytaqlnneyk isdkltfdim
      421 snytrtesdn limqgydgan pmngliwfgr qvdmkdlkkn wnqrdeqgny tyynwnsnyh
      481 mnpyytmnes lnslqmnrif gksslyyqpf dflkfegrig vdyanakrfe rnyfnfdhln
      541 gsfsenknnr tefnadfian fnkqygdfnv lataganyrd yqmnfntlga tglnvlgvyt
      601 iankigpaet imdnehnrsn siygqasvgw rdqlyvdvta rndwsstltk sffypsvsms
      661 wipttsfesi kgdflsfmkl rlnisevgna tdpyrnrnyy yaqtdafndl aqmyksmtfa
      721 ienlvpesin twetgvelgm fnnrlhadft yyhknaknql lpvntsntvs ftrmflnagn
      781 ieskgielql rgdilkkeng lnwsatanfs kdnskviely paldlkdyqi gwtwgianma
      841 regqpwgtlv gpgydrveed gpmkgaikvt saglvqskaa qnignvvpdf laslrndfty
      901 kdfsfgfmld frkggdiwsq tmshgyttgv aeitaangir eravlagrdv mtnerfamsd
      961 gkggwienni ettaqdwyeg ggiaamyvfd gsflklreay ftynlpqhly srikgikran
     1021 lsvigsnlal lwvdksntmr idpesggvss dsrgvgfeqa tvpnsrsigl klgftf
//
LOCUS       WP_094773016            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094773016
VERSION     WP_094773016.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118754
     Region          24..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqtllsffv gsmiltsvaf aqdkkvtgrv vgadgnplvg vtivvqgsnl atqtdangny
       61 sfsvptgkii vfkslgyadk tiivkegtst lnvtledsnq nlnevvvtay gvqkkeaitg
      121 svvsvtskdi ekrpvssvta vlegiapgiq vnnsygepgs spnirirgfn singssapty
      181 ildgvvfagn iadlspdnie sisvlkdats aalygtrgan gvivitskka kkgssslnai
      241 vnqglytrai peydqldake ymgvawqgyr nqlltgdknl svadansqat kglipsilkl
      301 nifdksdael fdangnfnan anikgdyasd ldwfdqvsrt gyrqeylmng aggfekggyy
      361 fsvgyldeea yvttsdfkrl narlsgdisp kswikagmam nashqlsnnt tgegsgftnp
      421 wmfarniapi ypihlhdatt gaytldtqgn kiyddgadtr nqyvgrhviw enelntnask
      481 rntvntqayv dfnitkdlkf silgdvnlrf nearsynnai igdgagnngr gsrtiynykn
      541 ytvqqllnyt kslnslhnfd vmlghenygn dytylygykv nqtfagqidl infteitslt
      601 dyeyndrtes yfsrlrynyd ekyfvegsfr rdgssrvapd hrwgnfwslg gtwmlskenf
      661 ikdidwinal klrvatgvvg nlqslefydy qslynigqnn nvaalyrsnf enrelkwegn
      721 qssslalegr lfnrfnfnve yfnkqsrdli fdlnlplsvg sttttegkat vkknigdlvn
      781 kgleltfdvd likkqdlrwn fginatflkn eiktlpeqnr engilaapfk ymeghdvfdy
      841 ylfqyagvdm mtgqalyhan ttdydptstt gawvpfqkev ngelyttnss yakrefsgsa
      901 ipkvfgsfnt sldyknfsls glftyslggk gldysymslm svtstpgavh kdvlnswtea
      961 pagmtetsad rinkdatpqi nytnsqynna tstrflfdns yfvfknislg yrvpkktier
     1021 inlsslsvnf avenvatfta mrgyssqqaf dgtsrnqfvp artfslgini gl
//
LOCUS       WP_094773018            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094773018
VERSION     WP_094773018.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114711
     Region          24..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqtllsffv gsmiltsvaf aqdkkvsgrv tgadgkplag vtiavqgstl atqtdangny
       61 sfsvptgkvi vfrsigysdk tlivkegqsa fnvtlsnsdn eleevivtal gvkrekrelg
      121 ysaeqvsskt vnqasavnla nglqgkvagl nvtttsssvn edvkinlrgi rsltgkndpl
      181 lvldgvqmdi kylssinpnd venvsvlkgg aaaaiygpda rngvimvttk kstdtpsvnv
      241 shstqwqnvs ffpklqkqfg qgydgiidpv enwnwgpafd gstidigpkl pdgsqqttty
      301 sgtderqkfy ntgvtnqtgv sltakdffls ledavvkgiv pddknrrtgv rlnsqrefgi
      361 fragmnvnyt qqnydlynqt aqadyftaqn tggnsglfsq lintpadiil skykdyqndk
      421 fstyenwftn yglnpyfsig nwrkegkkqd lisnlelglk atdwlnftyr agltsrniae
      481 rnktvgvnps twavnrgkgp ipgaieeyny nqtiltseff adintkiddd ftfkgivgty
      541 vkqndwrttr vgadnlvvse lynlsnrigi lsgssngfrs rlfsvygsag lnyknwanve
      601 vtgrwdksst lamgnnsyfy pgvnaafilt daipeiksdv fnylkvrggw tktansdiep
      661 yflaatfsqp atsgfpfgsv sgltagntty dpnlkperit steagfeagl wnnrltleat
      721 yfynkntdqi isvniseasg ysrsyrnaas fnsygvdfgf nitpiikfnn ggvnlrgsfl
      781 wndskvtsid eslglnelsi ggyvaagnya ikglpafemr gtdykrddqg rvivdsktgr
      841 psvssdnvnf grtlpkwivn ltpsvnwknf nlsamfehkg ghvvsffglg sdmawtgvse
      901 atvynnrepf ilpnsviadp anpgkyient avkigeneei ynyytgefrn aasnfivsas
      961 qwrlrelsla ydvpsewlqa rqkvvkslsi alvgrnlalw lpkenkfmdp dfnsmtadyp
     1021 naygnvnana nppvrnygft inakf
//
LOCUS       WP_094773020            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094773020
VERSION     WP_094773020.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116566
     Region          24..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqtllsflv ggmilssvaf aqekkisgrv tsatgqavpg vtvvvqgtnq atqtdangny
       61 slnvpagkvv vfrsigfgek tiivnnnatv fnvsleddnn aleevvvtan aikrekrslg
      121 ysapvlksde ltegrnssai galagkvagv nitstsnspg sssrvvlrgg ssisgnnqal
      181 ivvdgtpidn ssviggassl ssvdfgnrgn dinpddiatv tvlkgpaaaa lygsrasnga
      241 liittksgkk gskneitfss tntmssilkl pefqneygqg ysgytkagdl vfvndpkenw
      301 swgapftgei qewgqaingv rqkkaysavk dnvkdffdlg lasdnnlsfs ggsdkstfyl
      361 glnalnsngv ypgkkdtynk ygvrfngste fsnkfsagvs fnysrinsnn vgggqgggsv
      421 ynnllqtprd mditgfkdls npynsygytd angvehndvy gyygaysnnp ywvlenynnf
      481 ndvnritgnf nvnykplewl tfqerigldn ytdrrrsesp kysflpadnt senysednik
      541 tdpgqyridq ynvneivhdf matathsfnd dweasfmlgn nirqrrtsns siatnssggl
      601 vvpgwynlan sngpldlied swsnrrligv ygdlnvsykn iaylqatarn dwsstlpkqn
      661 nsffypsvsg sfvlselftp elknnfnyak lranwaqvgs dtdpyqlltt fsrgeinggf
      721 gtttfpfgnv salmssstig nmelkpeitt sfeigaelgf fsnrlytdft yynnnsknqi
      781 lsipipastg ygfslvnagk vkntgveltl rgtpvktdnf twemfgtftk nnsevvelmd
      841 gveqvsvggf sgmnivaavg rpygefygvt natddqgrti vdqktglpvv ssspqylgty
      901 npdfqaslgt nltyknwsms alfdtkqggv fysrtkdilg fvgtsaetgg erfgqifpns
      961 vyldaagnsv vnttatydkv dyypnmeagv nivdatyvkl rnltvsykft kdqlkntpfg
     1021 aasigffgnn lfiwtpsenk yadpevnsag agnaqgfdft aqpslrnygi nvkvsf
//
LOCUS       WP_094773094            1131 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094773094
VERSION     WP_094773094.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1131)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1131)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1131)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1131
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1131
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123869
     Region          28..1130
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msyfykksag lalctlfsas slfaqqsitg kvtdakgpis gvtvavkgtt rvtqtdangq
       61 ftiqaaqget lrfsnvgfki selivgstkt inmtleedag aldevivtam gitkkqralg
      121 yaassvkpee iqranavnvv nalqgkvagv ninavgtsgv tssssitirg aksldknnsp
      181 ifvvdgivme nnitdtyggk dwgsqlknln pddyesidil kgaaatalyg srgangavvi
      241 tskggmarkg lgidfsqnyq iqkiyaphvk lqnifgagsv gngyegnflp sgnpntstsn
      301 fgpamegqlv dqyytdgekv pfspqkdnwk alyqdghysn tnfainggne ravfrisysh
      361 tdnkgvlknn sfkrdalslk ssgkindifs vdfginyaks aaenaydqgf yregqnlgll
      421 ttyymprsld lasfykqyrd pvtnavksqs vygtlanflh rldyynevrd eesiignval
      481 raqitenira saqanyttyn tlttnkqyga gpylgnggyy avngsrrnny nflfmldgsk
      541 dflngdlttn lkvasemygn ganenwgknt ngglvvpglf afsnsvntiy ptynytkgny
      601 kvlgvfavln layknqlfle msarndwnss llyptwitag tnnysvfyps anaswvftdt
      661 frdklpeafs fgklraswsr vgmgsaayat svgaggfnqs tiydqdknsi isanpnissi
      721 pntdlkpeiq qsielgtdir flkdrfgidf tyyktntfnq iltlgnvies gsstrrinag
      781 niqnqgielm ldvdaiknen lrwnvqfnyt vnrgkikklh pdikewqlms svdagpeiwa
      841 yeggdfgvit sgynntyasa palynnesnp ndpnngkril eyggktgspn payvyywste
      901 admgkperkv lgkiepdfig glntslyykn fdfyaqadgr iggqfyshty kyamgrgale
      961 eslygrdqah ggiartdykg ntvydgimld gvfkegtqap skldpsktva vggmtykeav
     1021 esglinpmma ssfyaynygw ganvedpimd nswimmreit igyklpaslt kkfkleyarl
     1081 gitgrnlfyi ynglkaglnp esiqsnnplt pyeyggvpys rsfsvslnvk f
//
LOCUS       WP_094773155            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094773155
VERSION     WP_094773155.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124398
     Region          25..1110
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkfllfiaf scfhlltfaq etvilkgkvl dsktqapisg atvfiestav gestgvsgqi
       61 qqsalgavtd htgsftltvp tdvkyftvsf vgyqnrqiqv akvfntiyle slenalqevi
      121 vtgynpiakk knttaytklk vddikqtgvs sidqllegqv aglqltnltg gpnsapqiri
      181 rgtvsingtq dplwvidglp iegtalpnsf dkdnlnslqn lpiaginpdd iaditvlkda
      241 aatsiygara angvivittk kgkrgptqva vsansfvtqk pdfdrlnlmn ssqkvdfela
      301 maqrndldyr agkgaiarll nqsneldlfr qsglsalsnn tqaaiqnlrn qnqnwgdelf
      361 raalnqqysa sisggsdnhd fylsggfyde qaatrgvgmr rysltlnnnf tisnklkagi
      421 nllgsttgrn nfiqdadaft npvnyirsvn pylskrdaqg kfvydpdidg yenayipfns
      481 ieerqntsyn ldnkalkaia nlsyqvlpsl llrtefglqf denrserfad kesyntrklr
      541 egtryydsva kknkyflpdg gtiqndnrsi fqynwksfaq ynltlndkhd fefmggtelr
      601 rsksvgiatk gfgynpktlt tqsilfpnat nidnplyrqy akvigetsya sfyanasyty
      661 nqkynvygsi rydgsnmfgv dpkyrflpiw sisgswnase edfikeqtwi snlkvrgsyg
      721 iqgnidrnty pfiignystg tvlpgnteet ivvttpandk lrwektkswn lgvdlavlkn
      781 rlqftvdyyn rkstdligts slplengfen vqrnwasvnn dgiefmissr nivrehftws
      841 tdfniahnrs kltrvisnpk aysvdvregd pinslyvlet agldkdglpq fyndkrevvs
      901 yedfyglydg wadflpgynv stsltektyq ekfkyqgsld pkfiggmtnr frlgafdlav
      961 savfnvdkwm rrtptynpsm vdrgfnytid vltavqggaa gipeigssns elndrwmays
     1021 wmmdndpvgs yknldiwskk msyvrinsir lgytlpksia skvqasnirf nvegrnllvf
     1081 gssykgyfdp etygnnyaqp isksisfgln asf
//
LOCUS       WP_094773172            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094773172
VERSION     WP_094773172.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109518
     Region          23..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkklllfcs gvmlstslwa qtktisgkvt nasdgtslsn vtvsikgkag stqtnpdgsf
       61 tikaepgdvl ifsaigskst qqtigsssti nmalsgseea lgevvvtamg ikqqarslgf
      121 avqnvsskei sesnqanvvn aiqgkvagvq vtnsggspga sanimirggs slsgnnqplf
      181 vvdgipidnt tpvsqgglga gtapasnrgv dinpediasi silkgpaaaa lygiraasga
      241 vvittkkgss gkglitygtt fsidnvnklp klqsiykqgl qgkydpqsyl swgpqfdqsd
      301 kiydnlgeff qtsvsqvhdl taggsterss fyasaslldq ngivknmdfd rksfrlnadh
      361 kifdnlkiga nmnyinsgrt yfsqgsangv mgaiywplnv dmkdyvnvdg tqkllsqnsd
      421 gavdnaywti nkkpitnkvn rfmavgdvsy dplswlnlty rigtdyyten fqsvtaptsq
      481 tsvtgylaes tatnqittst flanakrsyg dfnfnltvgh nlestyrqtt tstainfidp
      541 dfvginnsiq sdrtvsksin rrrimgvfgd lnmdwknivy lnfrgrndws stlpksnnsf
      601 fypsistsvv ltdlvkeing sestgvlsya kvrgawaqvg kdapahvlqt tlgtyindft
      661 inprgfitni tdyfgnpnlk peftnsyevg adlrfinnrv gldvtwyktk sddqilgtrt
      721 ppssgsflay lnggaienkg wegiiniqai kkenfqwsfd lnfsanrakv lslpgsldrv
      781 elsdawvtdn aaqaaaflng tvfgingnvw ktndqgqyll dnngrpqias smqlvgdrnp
      841 dwiagitntf kykdfglsfm wdfrqggdvf nataytlvns glspltqnrg nivipgiies
      901 tgqinnleip mnqdyyqtly aknsknfved gswvrlryvs lnykapsslv kklrlqnlqf
      961 tltgrnlllf tdysgvdpev sgsgagvggs gsfgfdnlgv patrgidlgl kfsf
//
LOCUS       WP_094773419             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094773419
VERSION     WP_094773419.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110179
     Region          41..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfkinnfkv atklllfstn fyaitsmasp mnqysnelqs vlsgsitdea gnplagatih
       61 vkgtpkstas dqngifklnn vkknevisih migfttqevr ynsettlnik misvaqslee
      121 avvvgygtid kkeltsavst ikqkdmvagt vspllaiqgk vpglsvistn gtdpnagisl
      181 qlrgvnsvna sqgplvvidg vpggdinsva kediesinvl rdasaaaiyg trasggvili
      241 ttkrpqigka qvnftseyfi etvrkkpevl saekfieygl gndlghktdw ydevtnnnpf
      301 shrqvvnisg gsenanvytt ftkrdatgma itskreeigg rinssfkffd gfaelntnvs
      361 yneakafgsn ndifnmamvl nptetpydvn dvsgfnvlvg gydywnpvae vklrsdlkqf
      421 kyllanstlk lnltehltts atigvknnse hgtyyrsaqh rlsrqdgvdg nasqyynkyn
      481 drvfewtvny nnrwadhavn avagysyqdf ngqgfsanns dfpvdgiken dmgtgsylve
      541 gragmgswrn pwvklaaffg rvnysyldry iltataryeg sskfapknrw gffpglsagw
      601 risqepflrd asfindlklr agygetgneg fdakvasrmy sadtwflqdg nwfrtygvmh
      661 nqnpdikwev kkeynlgldf silenklsgr idfykrkidd liydisvsqp paihdkttmn
      721 vgsmqntgye felnykavsn ehftystgiv ashnkstlnt lwgsqtftdr kdfpapgspg
      781 savrlypged igrfyiwkfa gftddgywql ydkdgnifdv rersktvgdk afvgnaiptl
      841 qlswnnqfsy knwdasiymr swighdvfnm inmyyslpnv kgqnvlaeay dkhknikgek
      901 elsdywlekg tflkvdalni gysfnnnvik pikslriyat ardlfvftny tgldpevnin
      961 glepgfeern vypktrtfmm glqinf
//
LOCUS       WP_094773691            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium faecium].
ACCESSION   WP_094773691
VERSION     WP_094773691.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium faecium
  ORGANISM  Sphingobacterium faecium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Sphingobacterium faecium"
                     /db_xref="taxon:34087"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111464
     Region          31..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfnkqnqfrk svlffalfta glsqvqaqqe qvkgatqden gkflsgvsik alhresgkaf
       61 ttsssekglf sfrnlpeggp yqfifssvgf rsdtlsgyrv qpgkplalsv kltptattld
      121 evvigygris rkdltssitt vkaedmnvgv mtspaqmlqg kvpgltistn nsnpnaapsv
      181 slrgastlrs geamepyyvi dgvpgaslal vapddiqsid vlrdasatai ygskaangvi
      241 ivttkrgkag qasisyngyl aidkiakrye mmtgeqyrqy iadnkfsmep tddlgantdw
      301 qrevartgis nnhnvsligg tettqysasl nsfknngvik gtdlgrqiar gfvqtnaldn
      361 rltasfnint sitkqndvla lgdglsvyda myyylpvspv rtesgawfek tdrsqyvnpv
      421 slieentnyt kskmiqahak vgykilpslt ynidlslqnr qynnaqyyss lsmaarnqng
      481 ksiraavede rkimemnlsf drtfgdvhkf salagyswee nnnndgfqlt tsdyyddgls
      541 yynpgmanvv dilgfgnyyl stlrmisvyg rvnyaydnky lfqatvrrdg ssafgannrw
      601 atfpsisgaw rlseesfird mnffddlklr agygvsgnsl gfdvftarqv ygatssfytd
      661 afgndlrtla alrnsnpdlr wertgmlnlg ldfaflhnrl sgtlefydkn ttdliydyav
      721 sttkylyrsl tanvgeinnk gieltlhavp vksthfnwnt givashnkni vtritnqefs
      781 tdyvdladlg gagqsnafqq rlqegapigq fytwewagyn dagistfyvr dvqtkqrtge
      841 ttitptnkdr titgsaqpkl tlgwnntlty knfaltgmfq gvfghkvmna trarhsnvvg
      901 nagqknllas vietekatdi nahylsdryl engnylrlan lglsynirni ggqlknikly
      961 atmnnvfvlt nykgidpevd lggltpgidn rqtyprtrti lfglnfnl
//
LOCUS       WP_094778048             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia ribeironis].
ACCESSION   WP_094778048
VERSION     WP_094778048.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia ribeironis
  ORGANISM  Paraburkholderia ribeironis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia ribeironis"
                     /db_xref="taxon:1247936"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39443
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqssag vgasftdeaf aaagaelvda
       61 asafgadlvl kvqsptdael pllkrgatlv gmldpfnadn sqklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atarrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswla
      241 rqatlvhera rqadvvista lipgraaptl isvdtvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvvrngvqi vgytnlasmv padasslyar nlldfvkliv tkegalnidl
      361 addivaatll ardgqvarka
//
LOCUS       WP_094787381             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Zooshikella ganghwensis].
ACCESSION   WP_094787381
VERSION     WP_094787381.1
KEYWORDS    RefSeq.
SOURCE      Zooshikella ganghwensis
  ORGANISM  Zooshikella ganghwensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Zooshikellaceae; Zooshikella.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Zooshikella ganghwensis"
                     /db_xref="taxon:202772"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54491
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipkeif anetrvaatp ktvqqliklg ftvcvaegag klasftdsay eeagasivsq
       61 keawqadiif kvnapqetpe deisylkpgq tlvsfiwpaq neslleklaa kginvlamda
      121 vprisraqal dalssmania gyravveash qfgrfftgqi taagkvpaak vlvigagvag
      181 laavgtassl gaivrafdtr pevkeqvesm ggeflelhve edgsstdgya kemseafika
      241 emelfsqqaa evdiiittal ipgkpapkli tadmvklmkp gsvvvdlaaa tggnceltqa
      301 dqlvttdndv riigytdlpg rlpnqssqly stnlvnltkl lcphqdgnis infddqvirs
      361 vtvvkegnis wppppvkvsa qpqpkaqeav apvekapepk sskrkhiala vgalvfgwia
      421 saapaaflsh ftvfvlaciv gyhviwnvth alhtplmsvt naisgiiivg allqvssdng
      481 lvwffsaiav liatinifgg ffvtqrmlkm frk
//
LOCUS       WP_094795734             534 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 7].
ACCESSION   WP_094795734
VERSION     WP_094795734.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 7
  ORGANISM  Bordetella genomosp. 7
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Bordetella genomosp. 7"
                     /db_xref="taxon:1416805"
     Protein         1..534
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55343
     Region          11..534
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqaqstpqaq rigipretfd gekrvasvpd avaklvklgf qvavesgage aanfsddayr
       61 eagaeiidga aalwsasdiv fkvrpptade vslmreggml vgfiwpaqnp elmqqlaark
      121 atvlaidslp rtlsraqkmd altsmagvsg yravieaana fgryfngqit aagkvppakv
      181 fvagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq ramyaeqvkd adivittali pgkpapklit admvrsmrpg svivdmageq
      301 ggnceltvpg eavvrhgvti igytdlasrl akqsstlyat nllrlaeelc kakdgvavvn
      361 meddairglt vinagevtwp applkpaatp pakpaaapaa kpgghghgat gplpakavag
      421 ifaaaavafw figsyapaaf lghftvfvla cfigymvvwn vtpalhtplm svtnaissii
      481 aigalvqias pdagqagrpd elirwlafia lvltavnmfg gfavtrrmla mfrk
//
LOCUS       WP_094802010             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 5].
ACCESSION   WP_094802010
VERSION     WP_094802010.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 5
  ORGANISM  Bordetella genomosp. 5
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella genomosp. 5"
                     /db_xref="taxon:1395608"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38682
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipketr dgetrvaatp etvkkyvasg havvvehgag qaahypdsaf etagarlada
       61 aqalgselvl kvrppdaael aqmrsgavla gmldpfdaeq lqrlaaaglt afaleaapri
      121 traqsldvls sqanlagyka vllaanqygr lfpmmmtaag tlkaarvvvl gagvaglqai
      181 atarrlgavv easdvrpaar eqieslgakf idvpyetdee reiaqgtggy arpmppawma
      241 rqaqrvaerc kdadiviata lipgrpapvl ltaetvasmk pgsvvvdlav erggncplsv
      301 kgeivqahgv tligltnlpg llptdasaly arnlldfvkl ivdaqgalai krddeivaac
      361 lmceggqvlr rt
//
LOCUS       WP_094809069             694 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094809069
VERSION     WP_094809069.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..694
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=75669
     Region          36..>693
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkhvptrrr lyeylqacti gfflllsltg qaqtsrtltg tvtdetgatl pgvsilrkgs
       61 qqgtttneeg kyrltfseeg atlifsyvgy tpqevavgag svldvvlkad skalsevvvv
      121 gygtqkkaev atavgsiegk tiadrgtvsp lqgaqgqiag vdisagsgra gasysvqirg
      181 qnslaggqpl yvvdgvivpd inflnpqdia kmdvlkdaas taiygsrgsn gvilvttkgg
      241 ssakgrttis ydgyvgirev armpnfmtgp ewweyrqntf ispeliagrt nydntigslg
      301 npvvqqrvan gdytnwrdlv lrtgtqmnhw ltisgasekn tvqyligagy qkekgnllqe
      361 sldrynfkas vdgrmndhws agmsvnfsls diergsddav rnafnmapif spydangnlm
      421 frpgqipvpn sttissftst vnplleipnt ennnrrlfgv gnlylqyaln dwlelrstfs
      481 psvnferngr ywgsltgvgd gllpdaqrsn aqslsyifdn iatirknfgd hrftftglfs
      541 mqkdrfegdg lrvndlpfns syynlgsstn rqsgtsyfrq vsilsymarv nyvfknryfa
      601 tlatrwdgss klaeghkwst fpslavgwql seenflksan fisdlklrvs agiagnnnni
      661 sayesqmnls dptfydyggt valgygpsrl pnpv
//
LOCUS       WP_094809046            1167 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094809046
VERSION     WP_094809046.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1167)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1167)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1167)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1167
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1167
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127861
     Region          <39..>149
                     /region_name="PRK10819"
                     /note="transport protein TonB; Provisional"
                     /db_xref="CDD:236768"
     Region          161..1166
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meplqplekv rpktgsfivc aslllgiilt deiqaqqtkp dplakpdtlv lpvpkadtip
       61 kprvrpdstp tprrviqqds lvipsntvpk paarpvrpns vktprrvtqs drlviptdti
      121 pkpanvpkpa htakpvtads lpvtppnaqv aadslpggrf vkgrvtdeks gglpgvgitv
      181 kntkiqtitn tdgsyqlkvp ndqailvfsf tgykaqeqlv nrrpvlnvrl vpdvkalnev
      241 vvvgygtqsk rdlatatsrv aateiktavv ntvdqalqgr vtgvqvtets gepgaatvvr
      301 irgnnslsgn neplyvidgf pmppyreasa nftgayaqng lyginpndie smevlkdaaa
      361 taiygsrgan gvilittktg krgegrvelv nrtsfgqisn pirmmnsrqy aeimnesyal
      421 tnreapfkdl napltntdwv kaitqpsfrq ditlgvsggs pkssyyisgn ylfergtiin
      481 sdnnraslra nintdvndwy tlrgqlsfvr qksnraitsg rawpnsggll dglkapptie
      541 lnylgfnssg ipgysgyyfa npyneltskt dvsqndysvi nlenwftiak glqfvvslgt
      601 nqnltrrqvf lppttaegya skgsgssgla ntysynvnay flyektfaek hylnttlgge
      661 ynsqifeqln tissgyaipa fgvdnigsaq nqsigsfket rtlqsafvrv nysfkskyvl
      721 ntslrldgas pfaqnkkygl fpavalawnl neegfmkdvk fvsnakfrvs ygetgsqaig
      781 pyssltqfys gfyqygqega igtslystti gnpnlswert rqlnagldfn sandrfvfsf
      841 dfynkrtlgl lqprtlpsqs gvstildnyg smenrgvevs vqaniiqkkn lvlssrlnls
      901 rnintlldlg erktpdyvni sgnllggtsg ilipgqqvgq fyglrvvgla qpsdfnnegs
      961 pqypyailtd qipgtwkyqd lnndgkidas drqvigksnp dfifgwtndf twknlsvtaf
     1021 ftgsvgndvl nltrfylnng lldyqgvifn qtedwyynrw tadrphnnvr ypstqrgiss
     1081 sdinsailed gsfvrlkmlt isygfpkigp vknprlfvtg tnlftltkyt gfdpevssfn
     1141 qsllqqgidy gaypaqksft iglscnf
//
LOCUS       WP_094809132            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094809132
VERSION     WP_094809132.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113203
     Region          22..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrlsilll llsslwataq drqltgvits sedgqplpgv sisikgtakg sttnaegayq
       61 lsvssgntlv fsyvgftske vvlgdestln iqlqmnassl sevvvtalgi trekkalgys
      121 vqeiggkqlt qaretnlvna lsgkiagvqv tnsngspgas srmlirgsss ignnnqplfv
      181 vdgvpidngn ynnnptavdy gngaaslnpd diesmsvlkg paaaalygsr gangvvlitl
      241 ksgkgsrgig vsvnsnttfd tpfrlpewqn eygqgakgqf rfvdgrgggv ndgvdeswgp
      301 rldgrlieqf dspvvngvrt ptpwvahpdn vnqffktgkt ytnnisltgg sdkgdfrlsl
      361 tdlnqsgilp ftnykrqtvs lnagwnltpk lniratgnyv kdgsdnrtnw glyfiwfgrq
      421 vdmenlqnyt apgsiyqnnw nynywtnpyy qlanskrene kdrlfgnisa tykftdwlsl
      481 martgtdfyt drrktknaar tsnlfdgyne eqifvqesns dfllnathkf gefdvtanig
      541 gnhrrnfyqr dymsaaelai prvwnmgnsr lrpvtensys kkvvnslyas anlgfrnylf
      601 ldltarndws salpasnrsy fypsaavsav ltdmfsvqss flsfakirgg iarvgndtdp
      661 yrllqafdya nawgsqaslk esnellnael kpeitssyei gtelkfwqnr igldvtyydk
      721 qsynqilkvd vsnasgfssk wlnagllqnr gveiqltgta vktnsfkwdi tlnwarnqnk
      781 vkelvdnltt ytlgtmrgmg iearvgqpyg tffgqgflrn pegkivydqs gypvidpvrr
      841 vlgnftprwi gglqntfayk nlslttlidm kqggdifsqt inigrytgvl kettvgretg
      901 ivgdgvvnvg taanpeyvpn tknisseewh hkyylltnne etifdgsyvk lrevrltyvf
      961 pgkvfkrlpf rditisavgr nlallhsnip hidpetsyyg dtnvqgieng qipttrsvgf
     1021 nislnl
//
LOCUS       WP_094809161            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094809161
VERSION     WP_094809161.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115884
     Region          23..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqlllkvllp vllwvqvqaa laqqvtgvvr stadqqplag vtvqikgttr gtvtnaegty
       61 tvtaqsgetl rfsfigykae elavpengvl nvnlnneesa lqevvvtalg iakekkslgy
      121 svqelkstei sqaretnlvn alsgkiagvn itnsqgnmgs srivirgets iagnnqplfv
      181 vdgipvdnsq fgstgtnrdy pnaiadinpd nietisvlkg pnaaalygsr aangvilikt
      241 kggkgnkglg vtlnaahtfe nllvlpdyqn vygqgtgglf sykdgkgggl ndgtdeswgp
      301 kmdgrllpqf fsrgeavpfv phpdnvknff ktghtnnigv siagsdakfd yrfsfnntrq
      361 tgvvpntdit knnfsvngty hlndrltint sanfirsesd nlsalggrgs svmlqflwfg
      421 rqvdtgllrd yrangendfn wnhsyysnpy lllyentnaq rrdrffgnvn lnykindwls
      481 amvrtgndfy tdrrkskisy gtngtpfgsy aedayvvnen ntdfalnfnr klsddfdleg
      541 lvggnirsnf yeqnyqqapr lavaglytln nsrdplvsnn vfrrrrvysa yasaqlgfrn
      601 yaflnltarn dwsstlppgs nsyfypsvna svvltdafni rtnwlsfaki rggwaevgnd
      661 tdpyqltnty pfnqpfgsnp lltvsdvlln rnlkpeitqs seiglelalf ksrvradfsy
      721 ynsdsynqil radvspttgy kqkllnaghi nnhgfeaqls gtpvqtsggf kwnvivnfsr
      781 niskvvsldd qgllnqyilg sngttqvlag vgqrygalyg safqrdasgn vvvgangfpl
      841 knanlqtlgy ytpkwiggit nafsykgwnl svlidtkqgg qiysatnatg rytgvlestl
      901 pgrdaehggl syyyagnnts stpvqvagpd akapngeriy sdgiifngvt adgqanktiv
      961 paeryykniy snsagvneas vfdasfiklr evrlsyalpq nlvkrlslqg vnisligrnl
     1021 aflqkkapni dpetafntgn gqgleslqlp ttrsygvnln isf
//
LOCUS       WP_094809764            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094809764
VERSION     WP_094809764.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113652
     Region          40..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrslskttl lvltclglwi ssaeiptygr ataftlpidr qitgtvtdek gapltgatia
       61 ikgttqgsit daegkftlsv pndqavlivs yvgynkkeit vgsqtvvnvs lapndgnlqe
      121 vvvtalgvsr esrtlgyavs tinaevmtka rennignsla grvagltvrg tsggpgstsk
      181 illrgmpsmn sggaplivin gvpmdntqrg sagewggadg gdglgnlnpd dienmtvlkg
      241 qsasalygar asngvilitt kkgrkgdfsi dynlnyamdq pmnftdfqyq ygqgenglkp
      301 ttvtgaketa rlswgakldg smitqfdgnq yaysaqrnni knfyrtgsnf tntvsiskgg
      361 dngsfrlsls nldnlailpn sgmnrktinl tvdqnitskl svsvlanyin ervhgkpqls
      421 dgplnanngm flasnidqri lapgfdpatg nevvfsedey vtnpyfvtsk yinnvdrqrl
      481 ismvstkyqf adwiyaqarv gydnandqvf rvtpwgtafs fkrdasgnll gsgqldeqsn
      541 arrmelnidg ligvnknltp dislnalvgg nirknrydkl lingnpfvlp nlyswrnvvs
      601 ynrevtyept evqsayysld lgyknflnlt ttgrydtyss lpadnrsift psvsgafvft
      661 dllkmnklsf gklrasyalt sgeparpyqt svyygvgnsl ngvatgnfst glpnlflkpf
      721 tksevevgle lkffsgrlgi daayftqeth neimnanysf atgytsglva tgstqnrgle
      781 lqltgtpikt skftwntsfn ltsvknkilk tdpsnspvvl gknratldna ttayvvglag
      841 pqiraydyky aadgqivvda agvpvkgdlk nwgtvlptlf ggwnndftlg nfnlaflidy
      901 nygnkilsat eyysyyrgln katlvgrean fittgvteeg vastaktslk ayyqgvanni
      961 tktsvidgdf ikfrqitlgy nlparllegl plikavnisl vgrnlfyimk kaknidpeas
     1021 fganlnyygi egtslpsart ygvnlnikfk
//
LOCUS       WP_094811614            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094811614
VERSION     WP_094811614.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115663
     Region          27..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqtsilffl llvlsiaspg wsqtpllqgt vtdeqgqflp gvnvllkgtt tgvvttangt
       61 falrpprplt padqlvfsfv gyataevaig sstqlnvrlk asplalqevv vtalgikree
      121 kslgyaaqsl senvvkdart nnwvnslagk vaglniqgtg agpmgsarit lrgesslnld
      181 nnqalivvdg vpvssritgt gynshlsads pvdygsslsd lnpddienvt vlkgpgatal
      241 ygsraaggal iittksgark dqgigvtvns nvsiegvnrw pdyqfeygeg rtstyfsyld
      301 spdgpntatt vaagrawgpr fngqsyyqyn paapngkpte rtpwipykdy isgffqtglt
      361 ysnslslegg tdkgsarfsl thlknkwiip ntgferinaa lsvnqkvsdr lkingrvnys
      421 nkksdnlpaa gynnqtlmyf lilgttpnir pewfkpywat gleqvqqrnp fnptpdnpyl
      481 imyemlnkmn khgvigtlsa tyqlsdhidl lvrsgldmsy efrsqqrpfs mtryprgmyr
      541 eqnvfsyesn tdfllsyknq lssrvhlnas aggnamrqly dfaglyadql aqpgiyqisn
      601 sldqavadpl ktrkainsly aaaqfsldek ifvdltgrnd wsstlpygnn sffypsvsss
      661 fllhellplp qsfsfaklra swaqvgndtr pyqtdryydk iygnsftnat tlfnanlkpe
      721 itssyefgld vrllnnrvgl dvayynnrsr nqilaipldp vsgytnalin aglinsrgle
      781 lkltgrplat sqwnwnstll wsrnrshvre laagitnqvi ynhntnvsie arvgglmgdm
      841 ygrgfqrspd gqiiyssvgl papldpenkk wgnafadwka swlnefsyrg vrlsvlldgq
      901 kggslfsqtn hknntlgktn vtlpgredgi igqgvvkqpd gsftpntvkv aassyydnyy
      961 aitnaetnif dasflkirev rlefnlpkrw lqrtglrqts lafygrdlfn ftkfpgfdpe
     1021 ggnlnggtlt pgvelaqfps trviganltl kl
//
LOCUS       WP_094811783            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094811783
VERSION     WP_094811783.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112765
     Region          24..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkillatvm llstlvmhay gqsrvvtgkv taledgsgli gvtvravgst avgtttnqdg
       61 syslnvpssv kslsfsfvgf ktsvldipan nvvnvslevn qsdlnevvvt aggltaqrre
      121 lgtqattikn teitqgkaan laaglsgkvp gllisavssg lnpnyrlvlr gnrsltgnnq
      181 alviidniis pnsilgnlnp ediediqvln gagaaalygs dasngalivt tkkgkagrte
      241 vkiahtttle kvsflpqlqk qfgsgttpdd vpsytpyenq qygpafdgsm vnigkplqdg
      301 siqsvpysyk gsredfwetg vqnqtdfsis sgdekstyyi sgqffdqkst vpydkyqrys
      361 vranstrkis dkltatfntn fianrydqss qaatvyqnll mspgqvdvtq ysdwrnnpfa
      421 npngyyneyy tnpyftlenn rvntrndyfq gnvelkwnpi kplsityrvg lstrnvsnks
      481 tvgkftftdy tksisgsskt dipgsvgdys gfntqlvndl iaqyntslgs nfslnvvagi
      541 ssrdnsskdv svgasglvis dlynvgnsln nptagesnfk arqlgvygdv rlgfkeylyl
      601 hvtgrndwrs vlakdnrsff ypaadlsfia sdaipalsqs nwlqslklrg gyskvgqvnl
      661 gnftnfgaya lattfsqayg ypyasgagft lgntlvasni kpemttgaev gfdfelkklg
      721 inggitlykt ntvdqtitvn vssasgfssl rtnvgevqnk glesylnitp irtasgfevs
      781 lganytynqn evisladqln elvlssvgta srvlakkgsp fpllqvttyn rdpqgriivd
      841 pttgypasng tfsdlgittp phvlglntgi kykglrlsal feyrnghyiy naistgydfs
      901 gagirtawyn rdrfvipnss yqtadgnyva nnniavrsgg adfwtdgtrn tsigenyans
      961 agfwklrelv vaynfpasil skanfikaat vsvqgrnlfi wvpktnlytd peysangtds
     1021 navgitnlgq tpparyfggt lsltf
//
LOCUS       WP_094812025             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 12].
ACCESSION   WP_094812025
VERSION     WP_094812025.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 12
  ORGANISM  Bordetella genomosp. 12
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella genomosp. 12"
                     /db_xref="taxon:463035"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38650
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipketr dgeprvaatp etvkkyvtag hrviveqqag aaaryadeey raagaelada
       61 asalsaevvl kvrapsstel qtlrpgtvlv gmldpfdaeg iarmaqaglt afaleaaprt
      121 traqsldvls sqanlagyka vllaadhsar lfpmmmtaag tvkaarvvvl gagvaglqai
      181 atarrlgavv easdvrpavr eqieslgakf idvpfetdee reiaqgtggy arpmpagwma
      241 rqaalvaqrc qqadvviata lipgrpapvl isaetvaamk pgavlvdlav erggncplse
      301 kgkivqkhgv tliglsnlpg mlatdasaly arnlldflkl itgdgatlti rrdddivaac
      361 lvceagqptr rs
//
LOCUS       WP_094812135             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094812135
VERSION     WP_094812135.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108717
     Region          40..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlsylhvsgp rrrwsglwll lpallfsysl valprpaavt vtgkvisntg gplpgvsile
       61 kgtnngtltd adgnykinvq gansvltfty ighvkqeitv gnqpvinvtl eesssalqev
      121 vvvgygtldk kevtsaithv sgkdlltvgv tnpisalqgk vsgltitntg ggdpnsmpsi
      181 qlrgvssrda glgplvvvng vpggvlenin qndiesidvl kggaasaiyg trgsngviii
      241 ttkkgsqgsr vdyngygafd faamplktls aneflaqnrg tdfgaqtdwl ksitrasafs
      301 hkhslsfsgg darnnyrata dyrdaqgldl rsgreeygar lmlnhtsann lytlslnvap
      361 ryfksnnady dsfdqaltln ptlpifdpqn ptrynriqsg fsspfnpver lrteqsgteg
      421 kildynasll vnilptlttq ltfgqftrdy fdfffrpsts tyaaqyqgsm nsasraynky
      481 dqrslewvgn yswtkgahdv kvlggysyqy fqssglsgen rqmpsdalty nnigtglyqq
      541 vegrngmgty kndsrliaff grinyalqdk ylfsaslrre gsskfgynhk wgnfpaasvg
      601 wrlsqetfmk tlswiddlkl radygvtgnq dfgnylsldt ysgygyypln gsqyqvwgps
      661 qntnydlrwe taenlnfgid fsifkerfsg sinyytrknk dllgfysvpl ppniqgstya
      721 nvgtmqnsgi elqlnaqvvs tsaftytmaf agatnsnkfv sfsnaayqgq nyidvvglps
      781 pgspgtaqrl qegqrigtfy mlhaagvgdd gkllvynqkg diipadkann ddkrvvgngl
      841 pkatlslnnt ftykkwdasv ffravvgykl fntqafytgt pgtqsnanvl tsaygggkya
      901 kltnqattvi lsdyfledgs flkldnvtlg ytpkvnlksi rsirlyaaar nlltftsftg
      961 gdpdryping lypginssrs yyptttqila giqlgl
//
LOCUS       WP_094813225            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094813225
VERSION     WP_094813225.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111676
     Region          22..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllfftfl mlfgwiaqaq drivtgtvta sedgapipgv tvvvkgsntg tntdakgtyr
       61 ltlpangttl vfsavgfgrk eeeingrtti dvvlqssves lnevvvtaqg ierdtrslgy
      121 atqnvngsal aqrsepnvln tlqgkvagvn itsssgapga stninirgit sfngsnqpli
      181 vvdgiifnnd vdnsqntlfg sqpssrlsdi spesiesinv lkgpaasvly gsrasagviv
      241 ittksgkgln gktevtfnss vnwqnvaylp klqnqygqgt qnnyvnnsta swgpafgtpg
      301 fetvqnfrge tvpyraypnn irdfyktgtm fqnalniagg dqnnnfaati sstiqngvvr
      361 esdfdrhsvq vggnsklkng iklggtityv ktaqkntlmg nggsafgqit riprsydlvn
      421 tpyldpltge dfyfvngqnh plwsiqntff nsnvdrvfgn lsvgyditnw lnvsyrvtad
      481 tytdnrkqiq rvgaarapqg qidedlrfrs elngdllina kkndlfvqgl nanlllgqnl
      541 nqrsyresgv iseslaipgf dnvgvgsvft ksyastnrrr lvghygqlsl dyksylflel
      601 sgrvdqsstl pkeqnayfyp saalsfvple afnvkteavs ylkvrgniar vgrdadpyrl
      661 qsfftsatfg nnvaditfpl nvggtslpgf qpdgrigstn lkpefvnsfe vglnvgffnn
      721 rlgvdftyfn trstsqifnv aisnssgydt rttnigemqn kgielqlsat pirtssfkwd
      781 vllnftrirn kvvaisegvn nsnitgdsfs giapsiavgy pygviigtan artesgellv
      841 npntglfvpg iagqvisnpq kdwvagltnn fsykgftlsa lvdvnkggql ysfsqvdmrn
      901 agqteitgvd rnqprilpgv ilnadgttrp nniqisaqsy wqslgglasq gavfdatayr
      961 lrevalnyal pssllsrtpf gnisigvsgr nlwmyapgfp sdpeintqga gniqgldlng
     1021 ipttrnygvn lrvtf
//
LOCUS       WP_094813321             604 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094813321
VERSION     WP_094813321.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..604
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=67363
     Region          <30..602
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtqlltagtr tmytttltsn lvlkhtmdyl tpglssrvsi ayddsytkgf aktvsipqfs
       61 amrnamdpan lvfiggqisp tttadnvgng swnklyleas lnysrsfgnh tvtglllgna
      121 qrftangqgy ntpsglmglv grvtydfker ylfefnmgyn gseqfapgrr fgyfpsvspg
      181 wilsnesffp kndvvtwvkf rgsygevgnd qlggrrylyl pntwayngrg yffgrsdgss
      241 anpyfsgaqe talgnpeitw erarktnlag efrflkdrls vttavfwekr nnilvslgti
      301 pgtygvpdwn vppanvgrvs nrgyeifgew ndkvgpiqyf vrgtfsyarn ridyqaeapy
      361 aypwmnstgy sigqykglrt dgfyntqeel snrpyntfgg nqaklgdlkf rdingdgiln
      421 nqdlvpigys nlprvaynfs vgfsykgfdi nalvigtrqg sfpqsgyils tpfaknvgav
      481 mqyaydgrwt pekyaagqpi syptisfsgg qannnqlsdf wlkpndftrl knlemgytfq
      541 qnnsflkath lqgvrlyvng nnlftwgshl idgidpeqad tgknsmgyly pltrtfniga
      601 siqf
//
LOCUS       WP_094814176            1176 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094814176
VERSION     WP_094814176.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1176)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1176)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1176)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1176
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126913
     Region          53..115
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          133..1172
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mglllrrkss glvgllitgi vcsaagqtpa yfaraeaere erprpatpat kgltevfqql
       61 ekkyhvqfay qkklvqdkri qatvgtgkrs leenlqqvls plnltyekig etyiiserir
      121 esveskktsk aeikvkgkvt akdgtelpgv nvrvkgtgig avtnaqgeyl itapsetsvl
      181 vfsfigyasq eldiagktti dvvlenetkq ltevvvtaag ierkanalgy svstlsttdl
      241 aqknepdpvr alagkvagvn vqggggvagg atnitirgns slgnnnqply vvdgvpfdns
      301 tfapvtgnnq tqsnqstasr afdidpnniq smtvlkgaaa aalygsraan gaiiittkas
      361 akksrkgtei tyntsysaet iaglpeyqql ygqgtngdyr savygssgsa ystratiphp
      421 laragfsaad fpqfyeadgv tpvqvpyrsy agknqrdffr tgsvyenalt vnsgsekgnf
      481 tvglsrttnq givpgneiar tsinvggnar ldnkfyvrgt inyvmtdqks ppiggsgsim
      541 stmyylptsy dltgypyenp ntganvydya gvdnpywsir hspatsnvdr yygnfvlgfd
      601 plswlniqnt agfnaytdrr vsvlgkgssv yangtintdn iyrqeldntl lvtitktikq
      661 dfslraifgn ninqrmtdrs afvgtniita ginninntst itlgtlpnnr amirqrfyaf
      721 ftditldykg faslnivgrn dvsstlppen rsylyggvng sfifteafgl nspilncgkv
      781 rvgytqvgne aqpyqtvnvf nanasagdld apfsnpvqsn vstmtlgdvl snarlkpefi
      841 tefeagtelq ffnnrlsidl tyyhkrstsq iftvksapst gftdriinlg qtsnkgielg
      901 isatpvslas gfrwninanf trnrnnvddl ggfaqlvygn nihiagqpyg qiygsryard
      961 negnilvnpq takpiaaats gpignpnpkf ivglnnsfsy kritfdvlfd wkqggaiyst
     1021 nignalsrgv trdtenretl wvgpgvlgnv ntlepildes gnkipnntal tvidyffsgg
     1081 ygpggigegy vfdatvfrlr elslgyqlps nilqktpfgs vsislsgrnl wykapntpky
     1141 mnydpevstg aannagfdsl gvpttrrfgv nlrasf
//
LOCUS       WP_094814664            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094814664
VERSION     WP_094814664.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110261
     Region          30..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrksvlpgkl lfyllfawta lagsvsaqvq lqgkvsdang sglpfitvkl ssastgtttn
       61 asgtyqftps lkpgrytlvf sgvgyksqqk sfdvnasqna vtldatleed vlgldevvvt
      121 gtmgatskre lgnsiatvga kdlqfsaaps ldaalqgkls gaqitqnsgn paggisirmr
      181 gpstivgssd plyivdgviv nndsrqlidl ggysqnrlvd inpadidrie vikgaaaaai
      241 ygsranngvv qiftkkgkeg kpsitfstqf rvsqlrkkma yneypfafan ttptdetqvp
      301 vtrydyqdki fqnafgteny lslsggtant kyfvsgsnyy nqgiikstdf nrngirlriq
      361 qkignkatis agsnyvysss keipnggise aygaltgfif snnsvnpepd pvtgvypsta
      421 pvsvvrrtnp leainrfkfg qrtsriisdf nfnlkpiegl nidytvgidn ytqsatayip
      481 pknttptydq glarradatv fqinndlnvs yntkvndwlt stsgiggtiq ydrtltfgat
      541 aqqlgafget inngtiiame frsersilga faqqsfgikd ryfitgaarv dassvygidn
      601 rwqffpkvsg syvvsnekfw segtlgrvin sfklraawgq sgnltaigay drftnyspvi
      661 yggqtgyisp aqfgnftvkp erqteteiga dlsllndrvs vefsyfnksv adlilnrtla
      721 pttgfnnrli nvgsmtnkgf evmvkavpvq tsgfrwittl tytsnkntvn gvegngvlpf
      781 aggfsqvaav ngyplgayys tffarnpdgs llltaptatn pnrypqrerg tqlangqytv
      841 qrdangqptg tilskvigdp npwgivgftn efeigkfnfr mqwdgmlgfe vfnftrrvge
      901 rdlyaslkgy epelrgdvpk gtsaalfsif enyiedgsfv klreisasyv ltpklwkmqn
      961 lrltligrnl lsidnysgwd petnaagqdn avrgfdfvev piprsflfgv svnf
//
LOCUS       WP_094814752            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094814752
VERSION     WP_094814752.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113809
     Region          23..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkrlllsif tlflfsgsla laqqirgkvt vegdntplpg vnvslkgtss gtvtnangey
       61 sinlssgrtv lvfsyigyvn qevdangrst vdvtlkadnk qfnevvvtal gisrdkkalg
      121 yaaqgvgsee lvqnhqpnlv nalqgkvagv tisstggapg qgarilirgi nsidvsrdnq
      181 plfvidgvll dnststlgnd aagrgmsnra adinpediet inilkggaat alyglrgang
      241 vvvittksgk agalranysg tygfenvnky pdvqdkytig wqgqydpnsf wpswgptvee
      301 arkidpthpa klynhfkday rtgqqfqnnl sfsggtdkin flssishlnq qgvipftnye
      361 klslrlnsni kfsdkfttgv nlnfinsggd rynagrynet lsywsprydv rdyltpdgtm
      421 kaysgdnanp mynamtnkfr dnvnrliggv nftyaplswl tftyragldt ysedrlqtap
      481 gpkgiageyi sgdnglgfvy qyhtnfrait stfaasathk fgdlnttlrl ghdlydrrir
      541 sfgaegrelt vydyfdlrna ktivpvqsae dyrlmglfge ltfdykdylf ltltgrndmt
      601 sslqspnnsf fypsaslgyv fsqhfnlpev lsmgklrasy aqigkdaapy statgyssyq
      661 nlpsgltgft rgallgnpnl rpeftdtyea glelgflnnr lgldftyyns lskdqiiqvn
      721 vssgtgyvra ainsgemrnr gvelilratp iktskfnwdi nlnfsanrnk iesirqdlte
      781 isyasefgya nstvtmklvp glaygnlygr ayqryypntg eeqpavldrd rpivigangf
      841 pvigtaqkll gntqpkwlgg lnntlrygnf tftalfdarv gqdrynqmgn ffsafgiaky
      901 tenrndtkvf egvlangtpn tkavwlgqgv gpdgvnygng fyrnvhrgvs elfiedaswv
      961 rlrsaslsys ipsswikssi vknarlsvtg nnlwlwtkyt gfdpeasttn sgsnvdgfsg
     1021 fsypavrsfl fslnvgf
//
LOCUS       WP_094815497            1143 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094815497
VERSION     WP_094815497.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1143
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126511
     Region          62..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          146..1142
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfftslht wglvvclalp gqpaspllsp tewqsslqlk ntsqrklkdv lhelkerfgv
       61 dilfgdqlvq gltvpktald pkasleenld rvlknsglhy rkakdgayli vgqrldktte
      121 relpqtsarp sspvasqqps levqdqvitg kvtdekgegl pgvnillkgt srgnttdaeg
      181 nfkltipesa dntlvfslvg ymsqevavgt rttidvqlkq diksleevvv igygtvkksd
      241 vtgavasids kniekvnrvd aasaiqgqvp gvmvqrtdnk pgsggfniri rgastihtte
      301 taanagytpg qnplfivdgi fvndisflnp adidrmdvlk dasataiygs rgtngvviiq
      361 tkkgesgklt vrynnyvgvk evyhlppiyn ttgyvdylkd vvvgnqyasg nynftrndvn
      421 lpnylnaeel knindgvstn widlitrkgf qtnhtldlsg gnkstvyaig fgytqdkgtt
      481 rgedfnrytl rgnlssdlts wlnlsynnyv tvatqnagsf eafrsayrlk pigraynedg
      541 slkflptake tqvtnplldi eneiretkyl nylgdiavrl klvpgmtfts kfspnikytr
      601 ygeyrgkytk ssvgnqsstr aqvenyldfs ytwdnivnyd tkinddnkin atfvysqyna
      661 qnesyslqvr nfssddylfy nlgagstvnn yssrylkqtl esftgrinys lkdkyiftvt
      721 grydgssila egnkwaffps aafawrmide gflksqnlfs daklrlsygk tgnngagggl
      781 splgslslls psytnindqs mstlfitgla nknltwehta einvgldfgl fknrltgsld
      841 vydrttnnii ffrplplatg fpgtydnigk asnrgvelgl navvidankf rwsvnlnfaa
      901 nrnkvlklng ssdeiifgsq gatlihkvgq pmgsfyyfka ngiwgtdqve earkygqkpg
      961 qvrvvdvdgd gqitesrdrm iignsapkwt ggmthsftyk nfdlsvfayt sqgamaasnf
     1021 hrsfafaydn eparlwngyr tdywtpdnqt snwfqpgngg tyssaykymd vsfvkvgymt
     1081 lgyrlpadll skarigslrv yatvqnpftf tkydgwdpen asrndwggaf msrtymagln
     1141 lsf
//
LOCUS       WP_094815879             962 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094815879
VERSION     WP_094815879.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 962)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..962
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105082
     Region          29..96
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          102..957
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mitrvpgllv alwisfgiwn qagaqqltlr lqqaslttif seiekqagvq fhydaqdipl
       61 krrfdfnssg plpvilrdla slsnlaflqk gnrilvrtqa qrrvsgrvid rsektplpgv
      121 svrsstgrvl avtdaegyyt gtvsatdlsq arlefrmvgm kpilspplgs satldvemep
      181 esrqmnelvi tnaytngtpk eevigsisqi nakelqpyrp iesfdkmleg laagvyvept
      241 tqlgtpvkin irgqgtltpv ggtrttstqp lfvidgipim eqergdaaqi fsgetlinpi
      301 aginpqdias isilkdasat aiyganaang viiittkags agrtaahvsv srgvstfinr
      361 mkllsgpeyf tlkreallns gftesqaadq agsstidtdw lglttrnasy tainadvsgg
      421 kegttyrfst gyryqqasal kndlqqlnls lkvnsilnrk lklgvtlspt iikksgldnf
      481 knnaylppnl spydaegnft tllgvpnpla vlaqneaftd alafngnanl hyavtpnlti
      541 sgtigtnfsq skdvsydsak natgstkggq lqifdrqtlg wlgylqgtya ktfqqnhsvq
      601 viagleaqdq rtvllagsgt nftydrirei sqatrqsass skqenatvsy yaqatydfkk
      661 kylltssira dqssmfgsdf nlalnsavgl swiiskepfl qnhpaftflk lrtsygstgn
      721 srigsyaarg lynfsygnyn gyvaavpets sapnpnlswe knlklnlgld ltlfdrlsit
      781 aeyyqntihd lisnvevple tgygsisynt akmrnqgfdl tlqthfiqsk hfkwrstltt
      841 gfnrnrilqy nqgftsvysd pasttseana airegystta iwgirwagvn petgneqfya
      901 pdgsvvdrtt irtyprssyf vlgdrlpkaq ggwvndlsyk qfsltlnily nlgenrmelr
      961 nl
//
LOCUS       WP_094817049            1179 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5385].
ACCESSION   WP_094817049
VERSION     WP_094817049.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5385
  ORGANISM  Siphonobacter sp. BAB-5385
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1179)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1179)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1179)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1179
                     /organism="Siphonobacter sp. BAB-5385"
                     /db_xref="taxon:1864822"
     Protein         1..1179
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130091
     Region          59..108
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          154..1178
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkritflyg lpafmylcgp pgvqaqeivr agqeqvreas asgqslehrl qevekqykvs
       61 ilynpelvsk krvkdfrkyt sleqtleqll kpygltfkkv sdsfyivsee kksntsavnl
      121 lpnkfvplen ltnlsrseri satsltmplm aaltvqgkvs dattgeplpg vnvvikntsq
      181 gvttnrsgey slpnvpenav lvfssigyqg qeitvqnrsq inisltsssq eldqvvvvgy
      241 sqqrrstltg svaqigadql kqapplnvsn vlagrlpgvi vtqpygqpga dnatinvrgi
      301 sttgsnaplv ivdgierpft aldpneietv svlkdasaaa vygaraangv ilittkrgkt
      361 gkptityetn fsqntntrfp kflsgpdymr wykraeeldn qylvsqgktp faltytdeei
      421 aslangtnqs eflgntdwvg mltnntsvsq yhnvsvnggt drvryfttlg ywnqngvikn
      481 tnykrynvrt nidadvndfi strldltvrm edrmnpalap tdqnyqnpfi laqrmqpnlp
      541 mfnpaglpvg gntdagvgnp ivavndignr naeattfngn lsmnvkipgv qglqarllvs
      601 ydktitevkt fvepamlavr nrnangwlwt parmsaynvn nliqdyshsy rttfqpsily
      661 drtfgknafn glllyeysgw gtngfgaqar nfpitdlldl nfgskaaedl raatgsstqy
      721 krggyvgrvn ytyddkylfe vaarydasvn fpestrwgff psaslgwvls kenfwqplnt
      781 pinffklrls agklgndvvg iyqylnsfql rttptvaign qvvstlynta panpritwee
      841 atmynggvev glwnsnlsle vdyfykvtsn iltgqsgvya psvggnfast vnagkvdnrg
      901 vdlqlayskk hnklsykiig nftyahnrvl rinesvnapa aqrrvghpvn tkfgflvdgl
      961 yqtqeevdrg psfpygpgap gyvkyvdlng dgkisfeqdv trigrsntpe imyglnlqag
     1021 ygpfdfsall qgaarsnvil agvynsgvqg ntvytqtfag ngnspyflve dswrpdnpna
     1081 kyprltanka gltnqngyqn sffvrdgsyl rlkslqigys lpkdflsrlk iqqwrfyaag
     1141 snlltfdkik yadpetpsvv qagfypqqrv fsigtnitf
//
LOCUS       WP_094822440             536 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 4].
ACCESSION   WP_094822440
VERSION     WP_094822440.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 4
  ORGANISM  Bordetella genomosp. 4
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Bordetella genomosp. 4"
                     /db_xref="taxon:463044"
     Protein         1..536
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55811
     Region          11..536
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqsdtisspq rigvpretfp gekrvatvpe aveklvklgf rvaveagage aanfsdesys
       61 aagaeivqda aalwaesdiv fktrppstee valmreggtl igfiwpaqnp dlmqqlaakk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaaslg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rqmyaqqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti igytdlasrl akqsstlyat nllrlteelc kakdghavin
      361 meddairglt vikdgaitwp applkpatpp ataakaaapv aekkgghghg ssgplpaktl
      421 aiifavaava fwfigayapa aflghftvfv lacfigymvv wnvtpalhtp lmsvtnaiss
      481 iiaigalvqi apptaglndr pdalihwlaf aaliltavnm fggfavtrrm lamfrk
//
LOCUS       WP_094827811             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 1].
ACCESSION   WP_094827811
VERSION     WP_094827811.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 1
  ORGANISM  Bordetella genomosp. 1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella genomosp. 1"
                     /db_xref="taxon:1395607"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38635
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipketr dgetrvaatp etvkkyvasg havivergag laahypdsay eaagatlada
       61 atafgqalvl kvrapdvael vhmragavla gmldpfdaaq lerlaaagit gfaleaapri
      121 traqsldvls sqanlagyka vllaanhygr lfpmmmtaag tlkaarvvvl gagvaglqai
      181 atarrlgavv easdvrpaar eqieslggkf idvpfetdee reiaqgtggy arpmppawma
      241 rqaqrvaerc readivitta lipgrpaptl vsaetvaamk pgsvivdlav erggncplsv
      301 kgeivqvhgv tligltnlpg llatdasaly arnlldfikl ivdaegtlai rrddeivaac
      361 lvveggqvlr rt
//
LOCUS       WP_094831677             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 1].
ACCESSION   WP_094831677
VERSION     WP_094831677.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 1
  ORGANISM  Bordetella genomosp. 1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella genomosp. 1"
                     /db_xref="taxon:1395607"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38576
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipketr dgetrvaatp etvkkyvasg havivergag laahypdsay eaagatlada
       61 atafgqalvl kvrapdaael ahmragavla gmldpfdtaq lehlaaagit gfaleaapri
      121 traqsldvls sqanlagyka vllaanhygr lfpmmmtaag tlkaarvvvl gagvaglqai
      181 atarrlgavv easdvrpaar eqieslggkf idvpfetdee reiaqgtggy arpmppawma
      241 rqaqrvaerc readivvtta lipgrpaptl vsaetvaamk pgsvivdlav erggncplsv
      301 kgeivqvhgv tligltnlpg llatdasaly arnlldfikl ivdaegtlai rrddeivaac
      361 lvveggqvlr rt
//
LOCUS       WP_094837449             536 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 4].
ACCESSION   WP_094837449
VERSION     WP_094837449.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 4
  ORGANISM  Bordetella genomosp. 4
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Bordetella genomosp. 4"
                     /db_xref="taxon:463044"
     Protein         1..536
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55821
     Region          11..536
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqsdtisspq rigvpreifp gekrvatvpe aveklvklgf rvaveagage aanfsdesys
       61 aagaeivqda aalwaesdiv fktrppstee valmreggtl igfiwpaqnp dlmqqlaakk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaaslg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rqmyaqqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti igytdlasrl akqsstlyat nllrlaeelc kakdghavin
      361 meddairglt vikdgaitwp applkpatpp attakpaapv aekkgghghg ssgplpaktl
      421 aiifavaava fwfigayapa aflghftvfv lacfigymvv wnvtpalhtp lmsvtnaiss
      481 iiaigalvqi apptagvndr pdalihwlaf aalvltavnm fggfavtrrm lamfrk
//
LOCUS       WP_094842741             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 11].
ACCESSION   WP_094842741
VERSION     WP_094842741.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 11
  ORGANISM  Bordetella genomosp. 11
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella genomosp. 11"
                     /db_xref="taxon:1416808"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38444
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipretl egetrvaatp etvkkyvagg ntvivergag saarytdeay eaagatlgsa
       61 tdslgadlvl svrmpdaagl aalkrgavla gmldpfdteg iarlaatgvt gfaleaapri
      121 traqsldvls sqanlagyka vllaahyygr lfpmmmtaag tlkaaravvl gagvaglqai
      181 atarrlgavv easdvrpaak eqveslgakf idvpfetdee reiaqgvggy arpmppawma
      241 rqaelvserc kqadivitta lipgrpaptl vsaetvqamk pgsvvvdlav erggncplse
      301 kgqvvekhgv tlvgltnlpa lvptdasaly arnladflkl ivdkdgalai qredeivaac
      361 lvcesgnavr rs
//
LOCUS       WP_094852939             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 10].
ACCESSION   WP_094852939
VERSION     WP_094852939.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 10
  ORGANISM  Bordetella genomosp. 10
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella genomosp. 10"
                     /db_xref="taxon:1416804"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38109
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvgvpretl pgetrvaatp etvkkyvtag havcvesgag taarypdeay tavgaglgsa
       61 aqalgaelvl kvrapagpel gllkpgavla gmldpydaag laalaatgvt gfaleaapri
      121 sraqsldvls sqanlagyka vllaahhygr ifpmmmtaag tlkaaravil gagvaglqai
      181 atarrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgtggy arpmpaswma
      241 rqaalvserc rqadivvtta lipgrpaptl iaaetvqamk pgsvvvdlav erggncplte
      301 kdrvvekhgv ilvglsnlpa llptdasaly arnlldflkl itakdgalai qredeivaac
      361 lvceggnvlr sa
//
LOCUS       WP_094848071             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 9].
ACCESSION   WP_094848071
VERSION     WP_094848071.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 9
  ORGANISM  Bordetella genomosp. 9
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella genomosp. 9"
                     /db_xref="taxon:1416803"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38480
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipretl egetrvaatp etvkkyvagg nsvivergag eaarypdqay eaagatpgsr
       61 adalgadlvl tvrmpdaggl aalkpgailv gmldpfdseg larlaatgvt gfaleaapri
      121 traqsldvls sqanlagyka vllaahyygr lfpmmmtaag tlkaaravvl gagvaglqai
      181 atarrlgavv easdvrpaak eqveslgakf idvpfetdee reiaqgvggy arpmpaawma
      241 rqatlvserc kqadivitta lipgrpaptl vsaetvqamk pgsvlvdlav erggncplse
      301 kgqvvekhgv tlvgltnlpa lvptdasaly arnvmdflkl lvdkdgapam qredeivaac
      361 lvceagnvvr rs
//
LOCUS       WP_094858660             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            genomosp. 5].
ACCESSION   WP_094858660
VERSION     WP_094858660.1
KEYWORDS    RefSeq.
SOURCE      Bordetella genomosp. 5
  ORGANISM  Bordetella genomosp. 5
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella genomosp. 5"
                     /db_xref="taxon:1395608"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38670
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipketr dgetrvaatp etvkkyvasg havvvehgag qaahypdsaf etagarlada
       61 aqalgselvl kvrapdaael armrsgavla gmldpfdaeq lqrlaaaglt afaleaapri
      121 traqsldvls sqanlagyka vllaanqygr lfpmmmtaag tlkaarvvvl gagvaglqai
      181 atarrlgavv easdvrpaar eqieslgakf idvpyetdee reiaqgtggy arpmppawma
      241 rqaqrvaerc kdadiviata lipgrpapvl ltaetvasmk pgsvvvdlav erggncplsv
      301 kgevvqahgv tligltnlpg llptdasaly arnlldfvkl ivdaqgalai krddeivaac
      361 lmceggqvlr rt
//
LOCUS       WP_094866548             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            vulnificus].
ACCESSION   WP_094866548
VERSION     WP_094866548.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54538
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprell agetrvaasp ssveqliklg fdvvvetqag alasfddsay esagakmvsk
       61 eeawnselil kvnapiidee ksideialik egatlvsfiw paqnpqlmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvfvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaeflsv dyqetagsgd gyakemsddf
      241 nkkaaelyaa qakdvdiiit talipgkpap klitkemvds mkagsvivdl aaanggncey
      301 tvanqvvtta ngvkvigytd mvgrlptqss qlyatnlvnl fkllckekdg ninidfedvv
      361 lrgvtvvkdg eitwpappiq vsaqpqakpk svekpapkvq epvspvkkla glavavgafa
      421 wiasvapaaf lthftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngavtflaf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_094866856             474 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            vulnificus].
ACCESSION   WP_094866856
VERSION     WP_094866856.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     gene            1..474
                     /gene="nrfA"
     Protein         1..474
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52947
     Region          1..474
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmass vsvtalvmta llnitavsae ekglvdprnd afeqnhpdqy qswkktsesv
       61 eiedalaedp nmvilwagyg fakdynkarg hfyalddvrq tlrtggpqda ksgpmpmacw
      121 sckspdvarv idergeegyf egkwarlgae ianpigcadc hdtrsekfkn gepelaltrp
      181 yverafqain kpfeqqsrld kqasvcaqch veyyftgptk avkfpwdmgt gvqqmeeyyd
      241 algfadwtha vskapmlkaq hpgfetwreg ihgknkvvcv dchmpkvkke dgtvytdhkv
      301 gnpfdrfedt caqchtqskd qlreivstrk aqvlnmklta ekqivaahfe agaawkagat
      361 edemkpilqd irhaqwrwdy aiashgvhmh apevalevlg tavdraadar tklvrllatk
      421 gitepvqipd isskaaaqka lgmdmekmna ekqhflktvv pdwdkaaaer esky
//
LOCUS       WP_094880855             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            885].
ACCESSION   WP_094880855
VERSION     WP_094880855.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. 885
  ORGANISM  Prevotella sp. 885
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Prevotella sp. 885"
                     /db_xref="taxon:2022527"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109716
     Region          25..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrlmtfla clflsiglam aqtrvtgtvt ssedgepimg atvkvvgnna vgtitdidgn
       61 fslelknana elefsyigmt tkkvkasakm tvildadshm lenviitgyg sakklgsvvg
      121 avstvsgekm ktvatpnftd alagqvsgls vltssgdpsa aasirlrgvn smnssneplf
      181 ildgapisss ffqtlnpsdi anitvlkdaa staiygsraa ngvivitsrn gkynesaqvv
      241 vkaqygistp tsdgvtmmss qqyvkfrdii gqpvsdairk aaqhintnwr demlsssapt
      301 sdinatmqgg gnsvnyylsf nhheqegliq ssgmqrntla arinarlnrf fkvgfnsnfg
      361 dqryvvnreq nsssgiysan plvfarqamp fdapyfyhyd engnivkdgk aygllytdmp
      421 tpeffdkyrk qdgeqvtlni ginevftpme gltftaqqsl ygydstsetg nipheemvtp
      481 mgqiiesqsg sladgfsryy aytlthtgew khnfgqhyvn llvgeetriq rsrsfsaytt
      541 gqtddrimll sagtkadpad mgdsrseava nsifgnveyn fkekyfvygs lrrdgsskfa
      601 pdhrwgtfws agakwnakke sflapvkwld nltlsvnygt tgndagasty gyfglyglgg
      661 mynghtsigi aqasnyqltw etvskfnvgl nmslfrrldl dfnfyrnkts dmlmsipysy
      721 ttglssgagn iggmtntgfe vsatvqliat kdinwtftan vgynknkite lfqgrdeyll
      781 antglnlkig haygefysvr nagvdprtge pqwldkdgni tkifneerda vftgknryap
      841 wiggfgtnft wkglsviadf awaadkwmmq nddyfiqnan fattwnqrve mlniwtkpgq
      901 vtdipaygyd iqfddkmiqn asflrmktlt vqydlpkkwl aptryikgvk vfgiarnlft
      961 itsfegydpe pdinvvqfny pntrqfmfga eltf
//
LOCUS       WP_094882393             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_094882393
VERSION     WP_094882393.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36014
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvrecytv frsvlirihe rksivyheqd slntlmanlm argiisaeya
      241 hkfhflsdvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 vap
//
LOCUS       WP_094882559             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_094882559
VERSION     WP_094882559.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53673
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvra hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdfik tvipqwedqa rkngllsq
//
LOCUS       WP_094887731             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_094887731
VERSION     WP_094887731.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53689
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfekas rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvra hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_094893408             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium amphicarpaeae].
ACCESSION   WP_094893408
VERSION     WP_094893408.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium amphicarpaeae
  ORGANISM  Bradyrhizobium amphicarpaeae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Bradyrhizobium amphicarpaeae"
                     /db_xref="taxon:1404768"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39384
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag lksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygneaa lktiadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa emvrsmkpgs vlvdlaverg gnvegarpge
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpkss
//
LOCUS       WP_094897459             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_094897459
VERSION     WP_094897459.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53684
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeded gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_094913545             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_094913545
VERSION     WP_094913545.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35911
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvrechaa frsvllrihe rkgivyheqd slntlisnlm argvisaeyv
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 vap
//
LOCUS       WP_094926724             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudonocardia sp. MH-G8].
ACCESSION   WP_094926724
VERSION     WP_094926724.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia sp. MH-G8
  ORGANISM  Pseudonocardia sp. MH-G8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Pseudonocardia sp. MH-G8"
                     /db_xref="taxon:1854588"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38032
     Region          13..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(25,80,99,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(54,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mntestvprr tavgvpresa agerrvalvp kvveklrsrg vevvveagag dgalipdalf
       61 tnagatvgdp wgcdvvvtvt pptseqigrl rsgatligfl apltspdtva alreagvqgf
      121 ameavprisr aqsmdalssq anvagykavl laaerstrff pmlttaagtv kpaqalilgv
      181 gvaglqalat akrlgarttg ydvrpevadq vrslgaqwld lgieavgegg yareltader
      241 aeqqkrleea itgfdvvitt anvpgrtapt lvtaaavegm ragsvvvdma gesggncelt
      301 epgevvvkhd vtiaaplnla atmpehasel yarnvsalle lmldesgala pdwddevlak
      361 scvtrgek
//
LOCUS       WP_094947064             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_094947064
VERSION     WP_094947064.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53682
     Region          21..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrvrr ffslifpfff itsvyaeqtp esaktvtvev knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_094946969             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_094946969
VERSION     WP_094946969.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35938
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhifrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlilndf acvvrechaa frsvilrihe rkgivyheqd slntlmanlm argvisaeyv
      241 hkfhflsdvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vap
//
LOCUS       WP_094963802             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_094963802
VERSION     WP_094963802.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35857
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlilndf scvvkechaa frsvllrihe rkgiayheqd slntlmanlm argvisaeya
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vap
//
LOCUS       WP_094964223             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_094964223
VERSION     WP_094964223.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35887
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn tcyylyspge ygfveydlme
      181 aynrlilndf scvvkechaa frsvllrihe rkgivyheqd slntlmsnlm argvisaeyv
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 vap
//
LOCUS       WP_094964425             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_094964425
VERSION     WP_094964425.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53659
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvra hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_094964433             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_094964433
VERSION     WP_094964433.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35884
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iinalgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehgl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechav frsvllrihe rkgivyheqd slntlmtnlm argvisaeyv
      241 hkfhflsdvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 vap
//
LOCUS       WP_094965172             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_094965172
VERSION     WP_094965172.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53656
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdfik tvvpqwedqa rkngllsq
//
LOCUS       WP_094968121             971 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Winogradskyella aurantia].
ACCESSION   WP_094968121
VERSION     WP_094968121.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella aurantia
  ORGANISM  Winogradskyella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 971)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 971)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Winogradskyella aurantia"
                     /db_xref="taxon:1915063"
     Protein         1..971
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106595
     Region          24..970
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktflnallv ilimvpatlm aqttvtgtvt dkanamplpg vnviikgtsr gtstdfdgnf
       61 slevsqgetl visylgytpq eilfsgqati dvalvedaaq ldevvligyg attkqdatga
      121 vekvgdedfn rgaivapqql iagkaagvrv ttgggaageg geirirggas igtefgatnd
      181 plividglpi dqrggaqgsr nalnainpad iedfvvlkda sataiygsra sngvilittk
      241 kgsanqplkl eygiqastrr itntvdnlsa aqyrqvaead gvdpsefgna ntnwqdeiyt
      301 tgigaihnit askgyenfsf rvnynhvsqe gpllgdlyer ngfntsfvhr fldndlkita
      361 iargiqdeyq yaedgaigaa vrfdptqpir npdgsfyqyg ttanlapanp lftlaetedr
      421 qtiqrfignf nidynfwflr dlklsvnggi dyaensgfrf apanpnnaga fnfngqsqgl
      481 nrntsldfll nyktfvesin tniditagha fqefyirtdi devsgpntti dtdinrnall
      541 syfarasfdi adrylisasf rrdgssrfse dnrfgnfpgv svgwklmnes wmqdsffsnl
      601 klragwgvtg qqeigqnygf qgiytpsrnd qaniqfgtti ngepifirtl rpegfdenik
      661 weettqynva ldygffnnrl sgtidfyyre tedllatvpv psgsnlrdli ttnvgeitsr
      721 gleltvngvi fqkenfgwdt nfnvtfqeqe vtrlslnndp nafflvggis ggvgnniqil
      781 rpgfdpttff vfrqvydneg npiegsyvdv ngdnqitead rqpykkatpd afigwtnnlr
      841 yknfdlnftf rgsfgnyvyn nnasdtgnln aitnqpgyla nghasvldtg ftnqnlfsdl
      901 yieradfvrl dnislgytip fekmtlrtsl tatnlfvite ysgldpeign giqnnfyprt
      961 rdvvlglnft f
//
LOCUS       WP_094969035            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Winogradskyella aurantia].
ACCESSION   WP_094969035
VERSION     WP_094969035.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella aurantia
  ORGANISM  Winogradskyella aurantia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Winogradskyella aurantia"
                     /db_xref="taxon:1915063"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112052
     Region          25..1023
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkltwllt lfmafvmqfs faqektvtgt vttasdglpl pganvivkgt sngqqtdfdg
       61 kfsikvnqgd ilvvsyvgmq tqevtvgtsn tynvslkedn aleevvvigr itqtreksnv
      121 ssvklseksi knrpnpsvvq tlngqvagvn ittntgqpga nstiqirgig singdteplf
      181 vidgvpvdqd nfrsinpqei asvevlkdag ataiygnrga ngvivlttkr gnfeqdlqvn
      241 yngflaystl qdndynvmss qellryerfr gqgagagnst svfnpgngsp mtdaqiaeap
      301 nfdwsefffr tgvtqnhtiq lssgsknfsq ftsfgyndtq gilqdsdlqr fnvrnnlsgk
      361 ssngkftynt nlsvnysksn epnaigtsgi nrnfiigafe svpyvtaady ttggdllspl
      421 sftntplfll drlrtytrfe eevkivggln mgyeitdwls anvtmggdyn nniltraegp
      481 tsfnallfgg aenptsgfqe qrstraftyn qitslnaska fgkhtvgaav yteyfkahfr
      541 qfgyfangln pstfspgdgs glvqqagglf ndeadaeiln aglfsvfgtv dydfdtrygf
      601 saslrrdass rfrdenqwgt fwsvsgrwni sneafmqgsi fnnlklrasy getgnqfitg
      661 tlfggldnte dfftstggyg nanslalaqi gvsdlrweti tqtnigidfg lwndrlrgnf
      721 dwyvketsdl yqegpvsata gitsldintg tlfnrgidys vfydvftpkt engflmtvgf
      781 lgnynetelq dlpnaegeii sggefsaglg rnggqlyeyy glryvgvnpa ngellyltad
      841 gnvteqpsvg edrvwlgkna ipewtgtfql dlefkgfflt nqwafatgvd ridndyaslv
      901 npddvgqfnl srdilrawsq pgditdqpsp taanrnsfas drfmrsadfl rlrfasfgyr
      961 fpksvldgtg ftnvsvfvna enaitftewr gydpetrsit naggttlrgy ptpktfsfgv
     1021 elgf
//
LOCUS       WP_094970596             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_094970596
VERSION     WP_094970596.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53473
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdggd gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_094976890             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium symbiodeficiens].
ACCESSION   WP_094976890
VERSION     WP_094976890.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium symbiodeficiens
  ORGANISM  Bradyrhizobium symbiodeficiens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium symbiodeficiens"
                     /db_xref="taxon:1404367"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39109
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag iksglpdsef taagatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygneaa lktiadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpaprlvsa emvksmkpgs vlvdlaverg gnvegarpge
      301 vaevdgikiv gytnvagrva asasslyarn lfnfietmid kgtkalavnw ddelvkatal
      361 tkdgavihpn fqpka
//
LOCUS       WP_094994130             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas lundensis].
ACCESSION   WP_094994130
VERSION     WP_094994130.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas lundensis
  ORGANISM  Pseudomonas lundensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas lundensis"
                     /db_xref="taxon:86185"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38821
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth tgetrvaatp etikkligqg hkvtvqrgag inasvidsay etagatigsa
       61 ndvfgaelil kvvapddsel alinsgtvli gmlnpfsnet iaklaghgit afsleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgi tivghtnlaa mvaadasaly arnlldflkl vftpegqfqi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_094995788            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            cobaltidurans].
ACCESSION   WP_094995788
VERSION     WP_094995788.1
KEYWORDS    RefSeq.
SOURCE      Maribacter cobaltidurans
  ORGANISM  Maribacter cobaltidurans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Maribacter cobaltidurans"
                     /db_xref="taxon:1178778"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117872
     Region          24..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkciwlfm lfltgmtway sqqktvtgnv vdeegvplpg vnilikgtts giqtdfdgny
       61 aievspgqvl vfsyigqrke ertvgsenvi nvtmvedaaq leevivtaqg ikrekkalgy
      121 aittlgedav qsrpeadiar vlngkvagvn ivgtgglags gtnitirgsv sitgnnqplf
      181 vvngipfntn tnaesnvttg ngsvsassrf ldidpnnian isilkglsat vlygdagrng
      241 vvlittktgq tdeiekgfei tasqsvfvnq ianlpeyqnt ygqggdnsvn vgfvgnwggr
      301 fdrnftvrhp yndarlansf pefqgvnipy epykdnikdf frqgmgttts inaskskedv
      361 synfnfghtd edgfvpgnni krvsfglggs mklsnkitis gafnfstsdf ttppvsadng
      421 tgnfsiftrt lfiprnfdlp nlpyqdping ssvyyrtdqe nplwlvdnaq esidvnrffn
      481 sistnydind nlaltyrlgy dtytekqqfy inkggvssil aqngflktta aintiwdhsl
      541 ilslkdvrfs eklglngtlg fnanserydk fgvastgqvv fgfidhnnfa tqsnadplgs
      601 sldfkqtent lglygqlqfd ydsflyvtla grndwtstie qsnrslfyps asmsivptsa
      661 fpemqsdfln flklrfgygt sagfpspynt rnilalgtsl ftdrggrtin vnsssalqtg
      721 ldvfpnpelk aelhrefelg letnlwknri nletsvfkrd skdqilskil dsstgfdrtt
      781 inagkintkg ievnlgitpf nnlegfrwts nwiffaaese vvdlpggddv fisgfsnngn
      841 yavegqplgv ikgsyalkdd egnylinptt gnifdssavg lddeiigdpn pdwkatsint
      901 fgykglslsa qleythggdf ssntianllr rgvtrdtenr egsfvtpgfy adpstaelll
      961 dangnkipnt iqqganevyf lnyldpsgqq ifdgsvwrlr evsltydlpr kflkdsfigs
     1021 lsfsvlgqnl wywapnvpky tnfdpevist gvgnglgldf qttptskkyg fsikatf
//
LOCUS       WP_094996014            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            cobaltidurans].
ACCESSION   WP_094996014
VERSION     WP_094996014.1
KEYWORDS    RefSeq.
SOURCE      Maribacter cobaltidurans
  ORGANISM  Maribacter cobaltidurans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Maribacter cobaltidurans"
                     /db_xref="taxon:1178778"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118761
     Region          25..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngllt lllalivhis yaqektvsgt vtdqsglplp gvnilvkgtt tgtqtdfdgn
       61 ynisasqget lvftyigqkt vsmvvgsdnt invqmeddat aleevvvtsl glkresrslg
      121 ysvakvdgdq iaqraetdav ramqgkmpgv nivgaggapg qstkinirgm ssltgntqpl
      181 fvvdgvpfdn svnsdqgaaq ntvfssrafd ldpnsiesis vlkgaaasal ygsratngvv
      241 littkgarqa srkgmevryn sslamtqisg ipdyqdvytq gsnqlynggf ignwgspfpe
      301 yvdsineeyg tnytpfysly pdgsnypagt asnpvsnrfp gvfpelmqdy vmpdgsvvsv
      361 sapykiephd iiggffrqgi tsdhsvsvsa ggeksnlnvg fsnmnqsgiv pnqgagrtnl
      421 yaggnarldn gltvsgtiny vnttqkspss gasafndyfg ggggsiysrl fylprnfdln
      481 glpwenpadg snifyraldn piwiannnly ksevnrvygn vsvgydindw lnvtlkggvn
      541 tyhekrrrne rpggianpdg yvrttdldnt ekdinllfni nkdfgekfnm tavigmngnq
      601 reytergvvg nqiistglnr fdatatlipt rdysrlrrly gvfadinfgy ndwlflnvvg
      661 rndwsstlpq gansyfypga sismmlsevi pmpgfinslk vraantkvgn dadpyrtstn
      721 yfiatpftsp vyglnniasr dnllgnaqlk pefttefeag lsavmfnsrl sldvtyfdrt
      781 steqiarasv arssgfadri vnvgelsnkg weigldvypv snenfkwnmy tafskvkslv
      841 vdagptgeif iggpgtslgt ihrngfpygq ifgtknarda egnllinket glpfasatsd
      901 iigdpnpdft lgvtnsftyk nftlralidw kqggdfysft aaslmlrgql ansvdrealr
      961 vvpgvygnvq tfepvldgng ntvqnttpit afdshftdgw gaygqdevni ydgttirlre
     1021 lglsyslpek flentpfgsl tfslsgrnlw wkapnvlegl nldpevlaet aasnvqgfey
     1081 gatpttktys fnlslsf
//
LOCUS       WP_094996790            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            cobaltidurans].
ACCESSION   WP_094996790
VERSION     WP_094996790.1
KEYWORDS    RefSeq.
SOURCE      Maribacter cobaltidurans
  ORGANISM  Maribacter cobaltidurans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Maribacter cobaltidurans"
                     /db_xref="taxon:1178778"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117607
     Region          21..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyimlvmtl fmtatgfcqn tvsgtvtdaa gnpipyvnvl lsgtnkgtit neegkfsint
       61 tdtkgvlefs vlgyqtqkvp indllyieva llesseqlde vvltalglkr etkelgyvvq
      121 sldaqgvtev ksvnfldnlt gklagvtisq gptgvgstsk itirgeasfs nnnplfivdg
      181 vpinnnsvfn ftneaaagfq eidfgngame vnpddiaevs vlkgpsaaal ygtrasngvi
      241 vietksgrns tglgisynts ffvdtafqlp dfqneygqgn agqfafvdgl gggtndlisy
      301 swgprldvgn lipqfdspvt lpdgtvvrgg dtalysglpi tptpfvshpd nlkdfyrtgt
      361 tlinniavas nfekgnyrls ftdlrsesii pgvnldrqti sarlgfrpte klsinssisy
      421 insksdnrps ngygsenvny slvgwgprsl nmeslrdywq pglegvqqys fnytyfdnpf
      481 fimyenrnsf nrdrvfgnis asyditehlt asirsgmdys selrqlrraf ssnrfqnggy
      541 aehdvfyrei ntdfllnyin rfndvsldvs vggnrldqka ftsqsqttsl aqprifrlsn
      601 aaspvevfef esnkrinsfy glvklgykdf lflditgrnd wssalatpfs vdntsffyps
      661 vsssfilsev vdvpqfisfa klraswaqvg ndtnpyqtts afvaqtpfng qptfsnqnti
      721 anpnlqpeqt ssfeigadlr ffgdqlhfdi syynaltknq iislpigiss gytkqvvnag
      781 svrskgleii tgispvvses fswnstlnfs tnraivedlp qedgrltlay sriydsqnqt
      841 vylqveeggr vgdlygtgyl knengdfilt degryipnnd lqklgnynpd fmlgfnnqfk
      901 yknwnlgfll dwrqggiivs rtralgnvgg qlaetsfrpe agivpvgvvn tgtddnpvyt
      961 pntvavsaes yyrqfydrnh eenntydasf lklrqfsigy tfkdlsvfnq darlnvslig
     1021 rnlfaltenp hfdpeqlavq gqgfiggved msyattrsig ikagfnf
//
LOCUS       WP_094997204            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            cobaltidurans].
ACCESSION   WP_094997204
VERSION     WP_094997204.1
KEYWORDS    RefSeq.
SOURCE      Maribacter cobaltidurans
  ORGANISM  Maribacter cobaltidurans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Maribacter cobaltidurans"
                     /db_xref="taxon:1178778"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112313
     Region          24..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllkslv vlgtflsfgi aqaqevsgtv sdasgplpga svlekgttng tqtdfdgnyt
       61 lsvgddaviv vsyigyktqe vsvngrstin ftleedaeal eevviigygt ttvkdatgsv
      121 savtsedfng gnisspeqli qgktagvniq qttgepgagi qinirgansv rannnplfvv
      181 dgvplfgent eavgsnaggt gsgqvgnpln flnpndiesm silkdasata iygsrgangv
      241 viittksgkg askgswefst nlsvaqpvrl fdlldrdefm aalplyqdgd vstndfgsst
      301 dwqevifrsa astnnnisys nnygsgnvra tfgyskqfgt iekseferit grlnlnqrfl
      361 ddkllftlqs sisrvnksqp plnsgagveg dilgaaysan ptwplsatfq ppgsvsrnpi
      421 nlllesqnit ntnrfllngs veykftpeis akvnagydks esenvsvqsa nminypgitd
      481 ngfgtfytld rdnktlettv nytkefensn ldvvvgyayq dfrtqgrntt grgfsttdln
      541 qmgddlvssv egaestidgs fqqfyyatnt tdlvvnrlfp tsgtdnipya fdrlvnavta
      601 dtfdntdelq sffgrinysl nskylftatm radgssrfgp enqygyfpsg afawqigeed
      661 figenvstlk lrlsagltgn qaglgygnfv arqrygdlss nndavvqqng laivatdnpe
      721 lkwestldfn vgldfgfnsd rlngsidvyr rdtkdlllrt ppafpaitpf qfgnvdasii
      781 nqgiefaigy dfiqqedlnf sanfniaynq neiqdfagai ntgpingpgl tgafaqrfea
      841 gqslfsyyma ifegfdstgn pvytdidgng vgdpdvdktf vgedalpdit sglslnlryk
      901 nwdlaayfsg qfgfsvynnt ansffnagql gtarnvtqnv lalgedpgas tavstrflek
      961 gdfvrfqnas igykvplsge galkslrfsl tgqnlflitd ysgidpevtv ntgnlnasei
     1021 psrgidfmtf pnprtftfgi nasf
//
LOCUS       WP_094999508             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_094999508
VERSION     WP_094999508.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38787
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth tgetrvaatp etikkligqg hkvtvqsgag vnasvidsay eaagatigna
       61 tdafgaelil kvvapsdsel aliktgtvli gmlnpfsnet iaklaergit afsleaaprt
      121 sraqsldvls sqaniagyka vliaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa mvaadasaly arnlldflkl vftsegqfqi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_095014160             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. NS1(2017)].
ACCESSION   WP_095014160
VERSION     WP_095014160.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. NS1(2017)
  ORGANISM  Pseudomonas sp. NS1(2017)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. NS1(2017)"
                     /db_xref="taxon:2025658"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38731
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvvdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avpadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095031300             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas fragi].
ACCESSION   WP_095031300
VERSION     WP_095031300.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fragi
  ORGANISM  Pseudomonas fragi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas fragi"
                     /db_xref="taxon:296"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38827
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth tgetrvaatp etikkligqg hkvtvqsgag vnasvidsay etagatigna
       61 tdafgaelil kvvapsdsel aliktgtvli gmlnpfsnet iaklaergit afsleaaprt
      121 sraqsldvls sqaniagyka vliaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa mvaadasaly arnlldflkl vftpegqfqi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_095036310             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_095036310
VERSION     WP_095036310.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38779
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth tgetrvaatp etikkligqg hkvtvqsgag vnasvidsay eaagatigna
       61 tdafgaelil kvvapsdsel aliktgtvli gmlnpfsnet iaklaergit afsleaaprt
      121 sraqsldvls sqaniagyka vliaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldflkl vftpegqfqi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_095059688             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_095059688
VERSION     WP_095059688.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38536
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagasigsa
       61 ndafgaelil kvvapsdsel aliksgtivv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaaavhera kqadivitta lipgrkaptl lsaetvsqmk pgsvvidlaa aqggncpltv
      301 adqvviengv tivgptnlag avaadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_095062113             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Kingella
            negevensis].
ACCESSION   WP_095062113
VERSION     WP_095062113.1
KEYWORDS    RefSeq.
SOURCE      Kingella negevensis
  ORGANISM  Kingella negevensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Kingella negevensis"
                     /db_xref="taxon:1522312"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54122
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mriaipkesl agetrvactp ttvaqlqklg fevavergag iaagltdaay eaagavlvda
       61 keawkapliy kvnaptdkes gslkagqtlv sflyprqnee lvqklnakkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvli igagvaglaa
      181 igtanslgai vkafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv mseefiaaem
      241 klfaeqarev diiittaaip gkpapklitk emvesmkags vivdlaaatg gnceltkpse
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeieln fddviirnmt
      361 vtrdgevtfp ppaiqvsaap qqankqpeki akselkptpl wlkfapavig salilwvgav
      421 apaaflnhfi vfvlscvigy yvvwnvshsl htplmavtna isgiivvgal lqigqghafv
      481 sflafvaill asinifggff vtrrmlnmfr kg
//
LOCUS       WP_095070645             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium taklimakanense].
ACCESSION   WP_095070645
VERSION     WP_095070645.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium taklimakanense
  ORGANISM  Chryseobacterium taklimakanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Chryseobacterium taklimakanense"
                     /db_xref="taxon:536441"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111200
     Region          34..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrklqtiit lvltgtvave maaqsrldti kerkidevvv talgikreqk algfsakkvd
       61 eetfekaqyn nwatamegkv aglkvltasa gpletarikl rgetsmsasd nfalividgi
      121 pvdqtltkgt gsaaygagag gdlpvdygni lnainpedie svtvlkgasa aalygergan
      181 gaimittksg kgkngklivg ynsnssfesv lkwpdwqyey gqgtqtrdks gryyysygas
      241 edgvntgsts safgprfegq yyfqydpeve gqsperrlwk pykdnvkgff nvgttfsnsi
      301 sleagwrkfn frtnlnytdn dwivpntgfe rftannsfgf nfnklkatak fifsnthsdn
      361 lpatgynnqs lnyfmifqnp nidlawyrpi wkkgkyqedq ihpfssfidn pymiayemtn
      421 ainknnmlgg itlnyqfnnn feimlrsgae ytvedraqkr pwssanyreg yyseqhindr
      481 vfnndlllsy nrefkdlnfk isaggsmrdt rsetertnav gliepgiytf enakalqvkp
      541 tkpynykvns myglinleyl kaiflditar ndwtstlprk nwsffypsvs tsvilsdlmd
      601 lnkgdllklr asyarsgfgt spyrltkyys psdyedsytm dallfnadlk pkintnleag
      661 ldvavlknrl nfnftfynny tenevfgipv lvesgysrkl insgkvrnrg velelagfpf
      721 kskaftwria anwsanknkv isipdefkde plgynyssvg gavyfnavvg gslgdmygyn
      781 lvrdplgnvv wgsdgltaks tqmakignaf plwkagiens fqiknvriqf sfdgqykgiv
      841 ysqthhkmte qgklahtlky rdsedgmmvg egvvqnadgs yspnttrilv skyysdyyrr
      901 anvetnsfda syiklrdari gyvfpktite smklremsis lygknlwmwt kfpifdpeaa
      961 tlddsditpg vdigalpstr tvglnfnvkf
//
LOCUS       WP_095071384            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium taklimakanense].
ACCESSION   WP_095071384
VERSION     WP_095071384.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium taklimakanense
  ORGANISM  Chryseobacterium taklimakanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Chryseobacterium taklimakanense"
                     /db_xref="taxon:536441"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113823
     Region          32..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttsvla vvlsssfvlv daqtrkdtat kttdiegvvv talgikreek slpyatqqvk
       61 aeelnvtnnv dvknaivgkv agvqlngqag sklgetgklr lrgavsmlsd adpiyvldgv
      121 ivdpntidmd nlesvnvlkg pnatalygqr aqygvvvmtl kkgarnrlnv elnsttnvdy
      181 vartmryqne ygqgydgeds fgtfkfnpvr hpaewaaleg mtykrgqnyl adeswgakfd
      241 grdylpwyaf wkdspyfgkt akweaqpnnv kdfydnaftf kntisvsggt sdftgrvsft
      301 nllqngitpy telrrnyfnt nanykfsekl nveaimnfsq grttgdfddg ysnqtsgtfn
      361 qwfgrdldit kmkelkdlet prgyhaswnw wgpdyyridg psayrtkpaf wynpytymer
      421 yrpyrdrktl mfsvapsyki tddltarvsy srvnnitnsr yympysltks asgteggymd
      481 flngfgltds dytedqyegr lsysnkfgni dlntfvggnl tnqrwtgvsq emdvfgklqy
      541 lltpdvwdfk naniapvpdp wdygkryksl fgnvsvgynd tfyvdasarn dinsaylngn
      601 nsfftyslga sillhnlwak ndvlnyfklr agiaqiasdi narqtnpefs fydkpltlgt
      661 ksyqmalqpt ryidpnlepa insnfevgad lkflknrltl sgtyydekrn deplpvtlps
      721 ssgalsifln sgdarrrgve lslsgdvlrs stglnwttsa nfamnkstie nvaegldnin
      781 ygfqpafgyv svlqmkgqew gqlvgngfar dangnkilns dglyviegnk nfgsilpkft
      841 ggwynsleyk gltlaasvdf qkggkffsls eqwgnsggll eptaamndrg hnvrdavadg
      901 ggvrvtgvde ngapvdtyve aydyftqfhg nrlaeqyihd asyiklreva lsytlpkalf
      961 tnttvqgitv gltarnpwli avskdnyhrq dpsemsqsyg edgqlpstkg yglnvkinf
//
LOCUS       WP_095072444            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            jejuense].
ACCESSION   WP_095072444
VERSION     WP_095072444.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum jejuense
  ORGANISM  Tenacibaculum jejuense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Tenacibaculum jejuense"
                     /db_xref="taxon:584609"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110980
     Region          21..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgrltivlv flvallyaqe tvkgtvldan tgevlpgvgi miknttkgts tdfdgkfslk
       61 vnkgqilqfs figfktqelv yngqgflkvl leednaqlee vivtslgikk ekralgyaat
      121 elkaneltkv ktpnvlnala gkvaglqvtg anngvassar vvirgensln insnqplfil
      181 dgvpvnnrif gvggnttdqa dlptdygngl selnaddfas vtilkgaaas alygsraang
      241 vvvittkkgs qydegiglei ssssmfssal rlpelqtqfg ggwagayasn fgtnfgpaln
      301 gaviphelsl gevvnrpfin rydlndffkq gvnldntvtl sggnekgdfl fsygntyneg
      361 ivpntnlrgn sfrinagykl sekltanvra nyvtrgsdnl tvagygnqgi myallwnyin
      421 vdlnelkdyw rvenqeqrrl ftwgdnpwfi aneninafdk nrfvgnvslt ydfndnlsll
      481 grvgidqsnd frwsrrsiga vrnpngmyre qeidfseina dflltykrnf genfttttsv
      541 ganrfdqqiq egflqgngls ipglynaqni nvtpvirsnl fkkrinsvya ftnlgykdyl
      601 fldlsvrndw sstlpsdnns yfypaasvsf ipssafelpe vidflklrfn vaevgkdtdp
      661 yslftayefg tlggtltnps qllnanlkpe rtistefgle gvflsnrvkl datyytstsr
      721 dqilnvgisg angfnsivan ageiknsgve lglgitpvrt dnmnwtinan ftknrsevvs
      781 llpnldtfii gqgpdgvtve arpggqmgdi ygdsfirndn gdiiyenglp ltgnrrkvgn
      841 ynpdwmlglg tsftykgfnl saqfdiregg eiysytnaig resgilantl swrdgivgeg
      901 vvrddsggfv pntqevtaea wayaiprsna eanifdasfv klrqlslgyt fsqpvveklk
      961 lqglsislvg snlflwtgvp nidpeaqgln ggtllpgfev tqlpstrsyg fkvnmkl
//
LOCUS       WP_095072601             951 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium taklimakanense].
ACCESSION   WP_095072601
VERSION     WP_095072601.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium taklimakanense
  ORGANISM  Chryseobacterium taklimakanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 951)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Chryseobacterium taklimakanense"
                     /db_xref="taxon:536441"
     Protein         1..951
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105651
     Region          33..950
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvatm galffmagna vfaqtiaqdt aktrdidevv ivgfgqkktv qevtgavstm
       61 ksekikdipv asvdkmlqgr vtgvqvgsss gqpggmasvr vrgvssingi vspiyvvdgv
      121 rvasgdlttg nttanilanm npddienvtv lkdavstavy gadagsgvii ittksgkrgk
      181 prfnlsmnag mndraveghk gmtmaqwrey lahavmntyn atpswgqtfn nigevytfle
      241 qggegadlqn ifttdvdtdw rkvtqktgyq qnidlnvsgg sdkityyssa nyftqesivr
      301 nssfdrlaft tkvgyqatdk lkintdfqis hsklrtlsqg gafanpilaq yfnrpsdpiy
      361 nedgswywap snsrlsngly nipylqrnny akggtlrafa nlgieyklfr dltykfvfsp
      421 eyinieedty wnplhgdgyt yggyqrtsnn ryfnfnvqni ldwnrrfdlh nvgatliqea
      481 wksdnkflaa tgitvgtptl qtlqnfvvpy gydgtkgvss rygyavtghy dydrlfildg
      541 sfrrdvlsqf vpekkagnfw slgvgvdlar lnyikemdai smmkfrasyg klgnqvsanp
      601 yalytytsny ndfaaggysg lynpnlswet vrpfnvgldl gfwnnrltlt aeyfnkkted
      661 liynlplsgs qgltsyvdni gnlvnkgmef slnadifkgd rdqfnwnlgf nlstldneit
      721 elyggdvnts tttlrvgegv rtwylkkwag vdpangdplw ylngidgett nnyalakqav
      781 qgsmlsnvyg gantalsykg fgldlqftyg fggkilddwa qymwsdgyyt dyypgygdim
      841 gnfwtpenpn aanpkpmyyy gnknsyrvss rvlydsdfir lsnakfsysf drqlltgtgl
      901 tgaqiyvman nawthvfder lkfdpeinla gssnlglpil ksfllgvnln f
//
LOCUS       WP_095072608             976 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium taklimakanense].
ACCESSION   WP_095072608
VERSION     WP_095072608.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium taklimakanense
  ORGANISM  Chryseobacterium taklimakanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Chryseobacterium taklimakanense"
                     /db_xref="taxon:536441"
     Protein         1..976
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106146
     Region          32..975
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msvklkvlsa galfflaqgi naqsdttkvr didevvvvgy gtqkkkdvta slssvkgaal
       61 adkpvqtfdq alagrstgvq itvpsgvlna apvfrirgvn sislssyplv ivdgvpsftg
      121 nnsstdaasn plasinpadi esveiakdaa ataiygsraa ngvvfittkk gkngkarvny
      181 snwlslsspy rlpqtlnaee yikyktmaaa nnpaasavnf tnidaagrti dtdwadivyr
      241 tgvsynhnin vsggmggtsy yfsagytdqe givqkndfkr isallnvdsk isrifslggk
      301 lsfsnernla aansgslagg afgtgglgrl qfvlpsilpv ynadgtynln gaaighspfm
      361 ngvgsnigyy npqflldnnr snsennrvqs nayfqakpfe wltartqfgi dylltdndlf
      421 wspkagdgfs yggyalgisd knktmlwtnt lqaekdfdrh nlnvlvgneq twgtyssfgi
      481 qrdkiadpey dvvqagfvnn npigmgksen ylvsffgran ynfddryyis gnirqdeysa
      541 lsvkkgrfwg vsagwevake pfwsqmgaen vfssfklrgs ygkvgniggi gdfrasylyg
      601 sglyggastl lfgqvgnpdl hwetskkldv gvsfamlknr ltgdityydn kiddlilfiq
      661 qspstglpts vpqnigsmyn kgwefdlkad vvrtadfswn sgfnislnen kvtalapdmp
      721 nlqtatsgle tvnrtmpgys igylfvvktn gvdpqtgkri fvnskgenvy yqyyapagty
      781 nwsltpdgtt rtnavsiadg ymayntqpkf yggfdntfry knfdlnamlt fqggnyvyyg
      841 snaglhdqrw wnnhvdvltd awmqpgdtgk kyakpvfndn vsngssmpld vnvfkgdfik
      901 lknltlgysl pketlsqyni nnirvyvsgq nlaiitkypg pdpevssngn iqtapgvdrn
      961 tvgnartvlf glnvgf
//
LOCUS       WP_095073013            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            jejuense].
ACCESSION   WP_095073013
VERSION     WP_095073013.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum jejuense
  ORGANISM  Tenacibaculum jejuense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Tenacibaculum jejuense"
                     /db_xref="taxon:584609"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117131
     Region          24..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklftlfsm fclsfislaq nvevkgkvld evtkepipgv fvllressvt aetefdgsys
       61 inaaigkvle fnypgyvkkt vvvtsslidv elkidteesf lneviiigyg ekrkelvsga
      121 ystikpeeie rnnpqrieqa lqgrtagvqv ssnsgspgss ynirirgvtt ngdnsplvlv
      181 dgvqigpdls iidpndieki dvikdastai ygvrgangvi littksgknn tetkftysts
      241 valqettkkl dllkgveyaa lvnetiaadg gtppfqlqni ntdtdwqdal fettpmtthh
      301 igatgggety nfnvsaslld qkgiiapgrs nyarwtlrsn lglnltdklk lntlilytns
      361 trraipegnr gsvlyyanna spltpifdgt dgtgpsrgfs yigteqgnei vnpfavidnt
      421 fnktrvnrft gkielvydfl knfeftsrns fnysnvysra yfplqyygen kvvntvrldp
      481 vsgqfnldrn gdgdrdlysr vnendqnffs fisenfvnyn ftigeyhnfq ttlgfsltte
      541 qsrgifgsgf ltandswena flfntqsfii ddddigtndi retvnsdsfs iedrytsifg
      601 rlqydfnery lfsailrrda strfgpnnrv aylpsfsagw vvhnedflsd tsisnlklrg
      661 swgivgndki gayrwlgflq gvngdatypf gdvlsfgnai gvlsnenlqw ettiqtnigf
      721 dlgfydnnln itfdyykkrt edllvvpeis gliggaapgs gapvvnagiv enkgvefdid
      781 ythyfsddis lalnynltti nnkvidvnna agfipgglfg lnqqpsrmqn glpigvfygl
      841 ktdgvfqtqa eidalavdrd gdgsldeyqp gaapgdlkyv dvdgngyief gsendltvlg
      901 dpipdftmgg gfnfkfynfd fgasfyaslg neivrsyerf ltysnklsly ngrwtgpgts
      961 neiprastna annqlfssfy vedgsflriq nvqlgytlns eqikgidfir lyfsvnnlyt
     1021 ftkyrgydpd isnasaigag vdlgqypqpr mfitgikvsf
//
LOCUS       WP_095073984             917 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium taklimakanense].
ACCESSION   WP_095073984
VERSION     WP_095073984.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium taklimakanense
  ORGANISM  Chryseobacterium taklimakanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Chryseobacterium taklimakanense"
                     /db_xref="taxon:536441"
     Protein         1..917
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101012
     Region          33..915
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnyrtvlki apafllagtm minaqqdstt rekkieevvl igygqrkksd ltgsivsvss
       61 kdfnggatsp eqliqgkapg vaitgnggap gsgssirirg gaslnansap lvvidgvpqd
      121 msknedgtsi rgasdplali npndiesvdi lkdasaaaiy gnrasngvil ittkkgaagk
      181 vkvnlstvas vstrmgnvdv lngdeyrtfv ntygpnaaka llgthntdwq dliyqeawgt
      241 dnnlavsggi kglpyrvslg yneqngivrt nefrrtslav nlspkflnnh lsinanfkgs
      301 ftdnrfpngg ainnaiyfdp tqpvymddpr fgnyfewlnn gslntvsnrn pvsllyntrn
      361 issvyrlmps iqldyklhfl pemrwnvnla ydyskgygsn qtspysgagn gsysyspyeq
      421 ekknklfety lnyvktissi ntnvdlmagh syqdfssasp agesllfntn tgetrltpfn
      481 ayedqltlls fygraiftia nkyiltgsir rdgssrfyng ttdnlwgnfp afafawkine
      541 egmfrdisnl stlklrlgyg ltgqqevagm ypaysrykis eetaqylfgn ifypmyrpeq
      601 ynpdltwekt ltknigldfg ffsnringsi dlfqkdtsdl iayvpvpagg lsnyntknvg
      661 dmtnkgieft lnltpvkndn ttwdinfnat hytseitsls davaadfkip vggisgavgq
      721 niqahsvgha pysfyvfrql ydnsgkpvpg ayvdtngdgv lndmdkyfyk sstpdallgf
      781 stkvtykkwd fstalravig nyvynnaasn sslaslttnd ylqniyrtaa dyrfgniqlw
      841 sdafvedasf lrmdnltvgh nfgevfgdrt nlrvygmaqn vfvisdysgv dpeifgnidn
      901 gfyqrpkvys lglnfqf
//
LOCUS       WP_095074039            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            jejuense].
ACCESSION   WP_095074039
VERSION     WP_095074039.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum jejuense
  ORGANISM  Tenacibaculum jejuense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Tenacibaculum jejuense"
                     /db_xref="taxon:584609"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114647
     Region          25..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lilallvhvs yaqdktisgk vtdgseplpg vsvikkgtki gtetdfdgky
       61 vikaktgdvl vfsfvgmksi ekvvgsgstv nailsedssv ldevvvtgva tgtsrkklgv
      121 svssvnaekl adlgtpsveq alqgkvagai iqsnsgqpgq qqdivlrsia slqgtnplvl
      181 idglavdtgs ssiggasnls srladidfsn varvevvtga sgatiygaqg angviniitk
      241 kgksgaprvt lntsvgfsnv isnedarrtr lhryqtdtng flvdgtgtrv tqlnaesqfl
      301 pvainivdvn gtqlgaegin nipyaeqtfd avdelfntaf nttygatvsg gsenitylas
      361 gsrtenesvl ingdyvryns rlklgiklsd klnfdtridy issrnttgtd tdaaadnnli
      421 ngvyqnlphv nlnvrnsdgd lvvapdatdp nstnpfffrd aqvrqdeisr titnftlnyd
      481 pfdflnvnlk ygfdtysqtf nffqnreddh qqadqitnns giltetntnf ffqnllanan
      541 lkfelkeglp lesttsitfd wrdeeassts vqgtdnpftg fgsftinqsk tktlnsigna
      601 tfvpfrtygi lvnqkldfyd glfgigggfr sdvssrfgnd vtgtfgrfng yfniadvies
      661 dplqqlkira awgqagiqpp fgsnleafdv vtigneapif sqttigntsl apavntelev
      721 gldysiktnn knwftnlrgs vnyftneteg aisiaelaps tgapqirtna ydlssdgfdf
      781 sldlgvyesd nfswnfgtrf tksttvldri angqalvvgd fftleegqei gsfsvfdivr
      841 sidqedsqgn liipaadann ftvastgyvv nkntgkpvft qektaggstq pdfvmsffnd
      901 fkinkffeis tqvdwfqgmd vynrakqwly nnglhqetsv pvtiedpsgv drtgafvsyy
      961 tglyntnvpt shfiedasfi rlrnvsfkfk lndlvkfknv qditltlsgr nlvtitdytg
     1021 ldpeaarnfg npfqrgfdef thpntksynl glkvtf
//
LOCUS       WP_095074045            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            jejuense].
ACCESSION   WP_095074045
VERSION     WP_095074045.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum jejuense
  ORGANISM  Tenacibaculum jejuense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Tenacibaculum jejuense"
                     /db_xref="taxon:584609"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113931
     Region          25..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lllalvvqis faqdrtisgt vsdetgplpg vsvlkkgtts gtetdfdgky
       61 sikaktgdvl vfsfvgmktv ekvvgssnni sftmegdnvl eevvvtgygt esretvsssv
      121 tvlsaedveg rptaslvqal qsqspglnis tgngqpggns villrginsl sgnseplfiv
      181 dgvpvdednf rsinqndias vsvlkdasat aiygnratgg vivittkkgk sgqklqirys
      241 grsgftfkpd pnfslansre ileieriagv gtgagnynpf vgsvtglpvr tpgspaiplt
      301 daqiatasqt ntdwtdillr vgnfnshdis lstgsdnits ytslgyfeqe gitlrsklqr
      361 mtvrnnttyk tdkftfnssi gigfsrsdia ggigtggtsg slsnpflgpf vskpylpayn
      421 adgslnvvgd tdpnnsggfl ntpyiiqnva rfdidrdtel ritgalsady nitdkfrahv
      481 gfgldmiees rfrleptnsi rgsrvsedvr gnpdaqftgr qrqdfardtr mitdlrlsyd
      541 dtigekhnys vlgitefnya efndfgfdqv gltpglegvg agfvagntte dpdgngepdf
      601 fyiptlfsrk fivsqfslig katydydkia gadftirrdg ssrfqgdnrf gifwsvggfv
      661 nltkslfdps dfvndiklrg sygitgndrl gggyyagldv pfdqfgavgg yngsvglapt
      721 qlgnrnikwe etakanigvd frllqnkltg sfdvyknitt dlfaqrpatn lstfsvindn
      781 vgtmqnqgie ailnykliqn entvwsvgvn gsynenlite lngieanang eiilddtqfs
      841 peavghafne yymvrwagvn pangsplyld rdgnlteqfs danrvftgks tipkyqggfn
      901 tsfyhkgfsl daqftfaaev yrnngtlgva edptllniin vtsdllgawq qpgditgipa
      961 lntgsirnla ttryledasy irlknvaigy eltnslikks pfssvklylq genlltwtkw
     1021 rgfdpefdpf qandffsfpn srivtlgvdl kl
//
LOCUS       WP_095074678             824 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            splanchnicus].
ACCESSION   WP_095074678
VERSION     WP_095074678.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter splanchnicus
  ORGANISM  Odoribacter splanchnicus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Odoribacter splanchnicus"
                     /db_xref="taxon:28118"
     Protein         1..824
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=94338
     Region          2..823
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfildgfeat aekvfdldmn rvasvtllkd aaakaiygsr aangvvviet iqpekgklkv
       61 sytgdltvta pdltsydlcd ateklevert agrynghfpv ddqwlaeeyn vlkkevergv
      121 ntywlakplh tgfghkhsly leggddylry gvdlsynkva gvmkgsdret vsgaitlsyr
      181 yksllfrnvl sttfnradds pygsfseytk lnpywtsede ngnvkqvlgs ysqrewqeat
      241 kyynplynam lgtknfakyt evtdnfyvew qmykdlkfig rfgytqkqds redfypgsht
      301 rfaewtgdry fqrgsyymkd gvtktlkvda tlnyskqwnk hllfanlnwn mqqnsydwhs
      361 meawgflnnk vdhvafakqy aengrpggde ettrevgvvg avnysydnry ladlsyrlsg
      421 ssiygsdnrw ggfwsagvgw nlhheaflke aewlrqfklr asvgytgsqn fnpyqamaty
      481 kyftdaeydn ivgaylmgma ndklkwqqtr dvnvgfdaql lkgmtvrfdy yvsntdnllv
      541 dfdlsgstgf ntfkenlgev qnrgfdatin wrvyentknd ayvtlfgsvs snkneikkis
      601 dalsksndeq iddegnpvst kpytrfeegq stsaiwavrs lgidpasgee mfiarngyrt
      661 yvwnvndqvv cgeanpkfqg nfgfnaewrg lavncsfayk aggeyynqts vdrvenvdvq
      721 wnvdrrvftg twkepgdrtf fkrvestptq typtsrfvek snelslssln vsydfkrlnv
      781 kryverlkia fymtdvfrvs tvkaergley pfartcsfsl qatf
//
LOCUS       WP_095082963             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sophorae].
ACCESSION   WP_095082963
VERSION     WP_095082963.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sophorae
  ORGANISM  Mesorhizobium sophorae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mesorhizobium sophorae"
                     /db_xref="taxon:1300294"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43847
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvvvetg agtrsripde efakagaaig
       61 kagdvakanv vlkvrrptdt elkgykpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedde fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmr pgsvlvdlav erggnvegae
      301 agkvvtrann vkivghlnvp grvaasasll yaknlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafakadq qphvepaaip attmvadasa kpaakkaapk kpaapkspss
      421 kskgia
//
LOCUS       WP_095083384             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Irchel s3h17].
ACCESSION   WP_095083384
VERSION     WP_095083384.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Irchel s3h17
  ORGANISM  Pseudomonas sp. Irchel s3h17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. Irchel s3h17"
                     /db_xref="taxon:2009182"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38704
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg htvtvqsgag vnasvvdsay eaagavigsa
       61 hdafgaelil kvvapsdtel tliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvivahgv tiagptnlaa qvgadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095093263             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Irchel 3A5].
ACCESSION   WP_095093263
VERSION     WP_095093263.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Irchel 3A5
  ORGANISM  Pseudomonas sp. Irchel 3A5
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. Irchel 3A5"
                     /db_xref="taxon:2008911"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38752
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgekrvaatp etikkliaqg hrvtvqsgag itasvtdsay qaagatigta
       61 adtlaaelvl kvcapndsel aqiksgaivv gmlnpfnset igkmaeqgvt afaleaaprt
      121 sraqsldvls sqaniagyka vllgahhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recavgvggy arpmpaswmq
      241 rqavavhera kqsdivitta lipgrkapvl lsaqtvaemk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tlvgytnlpa lvaadasaly arnlldfmkl lfdkdgqlhi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_095092278             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_095092278
VERSION     WP_095092278.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53600
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dvrtklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_095110353             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Irchel 3E20].
ACCESSION   WP_095110353
VERSION     WP_095110353.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Irchel 3E20
  ORGANISM  Pseudomonas sp. Irchel 3E20
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. Irchel 3E20"
                     /db_xref="taxon:2008983"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38638
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvldsay eaagatigsa
       61 neafgaelil kvvapddnel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvangv tivgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095113085             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Irchel 3H7].
ACCESSION   WP_095113085
VERSION     WP_095113085.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Irchel 3H7
  ORGANISM  Pseudomonas sp. Irchel 3H7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. Irchel 3H7"
                     /db_xref="taxon:2009042"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38824
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgekrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095116383             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_095116383
VERSION     WP_095116383.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38834
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqrgag lnasipdsay eaagaslgsa
       61 adaygaqlvl kvvapndqel alinsgslla gmlnpfnsel iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera rqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvrengv tivgptnlpa qlgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_095125109             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Irchel s3a12].
ACCESSION   WP_095125109
VERSION     WP_095125109.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Irchel s3a12
  ORGANISM  Pseudomonas sp. Irchel s3a12
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. Irchel s3a12"
                     /db_xref="taxon:2009047"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38837
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetlaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095119609             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_095119609
VERSION     WP_095119609.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38811
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095139706             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Irchel s3a10].
ACCESSION   WP_095139706
VERSION     WP_095139706.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Irchel s3a10
  ORGANISM  Pseudomonas sp. Irchel s3a10
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. Irchel s3a10"
                     /db_xref="taxon:2009045"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38802
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafaaelil kvvapsdael alikrgtvlv gmlnpfdnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095140489             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_095140489
VERSION     WP_095140489.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53598
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqlervdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_095141580             519 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Bacillaceae].
ACCESSION   WP_095141580
VERSION     WP_095141580.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55604
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkerv agerrvaatp ksviqlkklg fqvavetgag eaasftdeqy issgaeivea
       61 ddvfqcdliy kvnppteeev skikegatfv sflypaqnga lvkelsqkni nvlamdmvpr
      121 israqsmdal ssmaniggyr avtealhafg rffngqitaa gkvppakvlv igagvaglaa
      181 igmskslgai vrafdtrlev aeqiesmgge flklnfagee dgststgyak vmsdefiqae
      241 malfaeqake vdiiittalv qgkpapklit kamvdsmkpg svivdmaass ggnceytvpg
      301 emivtasgvk vigytdlpgr lpaqssemya tnlvnltkll ckekngeidi nfedvilrhm
      361 svvkegqitf ppppirvsat qtskketkqa epsetpvkek khhsllkmvf gglaivfflw
      421 lgqvsppefl shvtvfalai vvgyyvvwnv thalhtplms vtnaisgiii vgallqmnss
      481 ltsvkilsfl giliatinif ggftvtkrml emftkskev
//
LOCUS       WP_095147075             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_095147075
VERSION     WP_095147075.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38716
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg htvtvqsgag vnasvvdsay eaagavigsa
       61 hdafgaelil kvvapsdiel tliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvivahgv tiagptnlaa qvgadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095159014             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_095159014
VERSION     WP_095159014.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38669
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvgqg hqvtvqrgag lnasipdsay eaagavmgsa
       61 adafgaqlvl kvvapddsel gqiksgtvla gmlnpfnnel iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvqvngv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgalti nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_095163289            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flectobacillus
            sp. BAB-3569].
ACCESSION   WP_095163289
VERSION     WP_095163289.1
KEYWORDS    RefSeq.
SOURCE      Flectobacillus sp. BAB-3569
  ORGANISM  Flectobacillus sp. BAB-3569
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Flectobacillus.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Flectobacillus sp. BAB-3569"
                     /db_xref="taxon:1509483"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116148
     Region          24..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllllitv fflvqigntf aqdrqvtgkv tssedgaplp gvsisikgtp rgttsgadgs
       61 ykiavgkdav ltfsfvgfaa qtvtvggqsq invalkvnts qieevvvtal gakrseksla
      121 ysaqsvkdeq lntirqtnln nalagkvagi qvrsqstval grdasirirg agslsdkapl
      181 yildgnpvss sdvnlddves vtvlkgpsat alygqrgdag viimaskkgt mkkgvgieln
      241 qstfyesvyv lpryqnsyag gassdmikfn weagmpeewk alngkfyhdy sddaswgprm
      301 vgqeyipwys wypgtqytgk taslvaqpnn irdfyqgqfa tntnvnfska gdnystrisf
      361 taqnqnglmy kssgvkynis sqttvdlgkh ltataninls eytikgqfnd gyanqssgsf
      421 nawfhrdldl nklkelkdlt spegilaswn hnnpgayass plnfyganyw ynfysyfdkl
      481 disenrrrmf gdvnltykvn dnlkvagfvr fnqgntfges kvptilqtsa tqtgvragys
      541 tyqtygniin ngntpnemny elmatynkhi ndftidalag gnirhdsyrt msagtvnglv
      601 ipdyfalsns sstpslssyr sdkeirsmya rgsfgykdii flegsvrndr ssalpkdans
      661 ytypsigtsf ifgdlirntv palsfgkvra swaqvgsdlg pyslalnytl asakfgsssy
      721 mgtpntlvda nikpalsssy efgldlkflk dklglsvtyy nedkineiit vpisgtsgft
      781 sklinagkin rhglevslna tpvktkdvtw tttvnwaknt skvlalaegv daitvtsdaf
      841 gvgtvvhqvg eawgqirgga ytykdgkkvl tadgmyvvtp nsylgsvlpd ftggwfnqiq
      901 ykdfvlsani efskggkyfs lsdywggfsg lfertagvnd kgnpirdpia dgggvhvqgv
      961 tadgaavdky vdaytyfhqf atnklseehv ydldfiklre isigyripvk gskllqsatv
     1021 sivarnpwli ytknrdfdps emsqifgeng qfpgtrslgv niklgf
//
LOCUS       WP_095163408            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flectobacillus
            sp. BAB-3569].
ACCESSION   WP_095163408
VERSION     WP_095163408.1
KEYWORDS    RefSeq.
SOURCE      Flectobacillus sp. BAB-3569
  ORGANISM  Flectobacillus sp. BAB-3569
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Flectobacillus.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Flectobacillus sp. BAB-3569"
                     /db_xref="taxon:1509483"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115207
     Region          24..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksllltfl atllscaflq aqerkvvgkv tssedgatlp gvsitllgtt kgtqtdasgn
       61 fslpvngtna vlrfsfvgfe skdvpvgaqt tinvqlssdt kqlsevvvta qgivrekral
      121 gysittldkk vmedrpqadv grvlqgkipg vnitstsgvs gtgtnitirg yssitgsvqp
      181 lfvvdgvpfn sntnsrggft gggqssssrf ldidpnnven vtvlkglaat vtygdqgrng
      241 vilittkngt kkprqtefsv tqsvftntah lpryqntyvg gfqqnlgyff snwgpslaea
      301 nlypsqntna altthpyafl tnattraama dyvasvspyk meiypnnvkd ffrtglisnt
      361 slnisgggek vsynvsagyn aeqgfipeng lkrlniglgl naqltkklsa ttsfnfantd
      421 qyapplsagq gnnandfpsv lanvlftprq vdlmgwpyes pvdgssvyfr sgndipnprw
      481 ilanykttgv vnrffaattf nydlgkdlml lykigldtyd eqqeymlnkg gvalvnglyn
      541 tlnfkntiwd nslilsynkt lsdkltmsgk iggnmrndrf ssynitsqnq larnlfrhsn
      601 fidnvasnft seqtrlgvfg eitadynnyl flnlagrndw tstvekenrq ifypsaslsf
      661 vpttafegla nntinflkvr agigtsagfp npyqtrniln qnargwfttg piqthsvdnt
      721 lgnpnlkpel htetefgleg klfnnklsfd ltlyrrdtrn litsapldaa tgytsttinv
      781 gkirnqgiel slsgtpytrg dfgwettfnf srntpevldl ggtiqevqis gfgsalgnya
      841 ivgkpfniik gtgfrrddqg rllidasgnl qattspvilg dpnpafvtsl intfnykkfs
      901 lnvmvsyrhg gaiysstaga llgrglties gpetgydraq tfifpgvkad gspnttqita
      961 sdvyfnnvff fgdegrmydg stvrlqevsv syslpktflk rfgikgasls lsgnnlwyka
     1021 lnipkglnld tdnlglgvgn glgfdfltgp sarriggtlk lsf
//
LOCUS       WP_095163677            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flectobacillus
            sp. BAB-3569].
ACCESSION   WP_095163677
VERSION     WP_095163677.1
KEYWORDS    RefSeq.
SOURCE      Flectobacillus sp. BAB-3569
  ORGANISM  Flectobacillus sp. BAB-3569
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Flectobacillus.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Flectobacillus sp. BAB-3569"
                     /db_xref="taxon:1509483"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116022
     Region          51..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyiknpfaa ipkvtlmalt vygtmlahfd vvaqekkpte vvkvqvqynt qvsgviists
       61 tgkpvlgarv fyknmtstit gedgkfklti psssvavnve cpgfvsveip vakrsqfnvy
      121 lqdvlgtesn itlptgaise qrslgavass aaaeawsqlt esadtylqgr iaglnstrfs
      181 gstnigsfft irgynslqvs nrplivvdnv iydsgiygss lnsnyfdnpl syidirdisn
      241 isvlkdasaa alygtkgang vimittsrak elgtkidfal yggvnmapkg lpvmgvngyk
      301 sylsdllssq glnsnqisal pymndntsnp eyytyhnntd wqkkvyassp ltnmflkvtg
      361 gdniakyals vnylsnkngv igstlekyst rfnadmnlsr kltaaanlsf ayneaetkdf
      421 gfasktnpiy lalvkapflt dyrvssqgif spdyadhdif nvgnpivaak ntlggnkayr
      481 ffgvldfkya fnenlkvgtn iavtfdkike nrfipnyglv adtlkntlal nqlssqtkrl
      541 fnisnetfvs ydktfknvhe lsarlgvrfi ssrveqdkll aynsatdqli svgnglvlyn
      601 nieggigtyn wlntygsvny sysdkyflgl nigmdassrf gkeastfkvg gtpiaimpsl
      661 saawllsaep fladgpfdll klrgsigrvg nddignyssk qfyvgqnllg lqglvrgnia
      721 npslkwetva ksnlgldlav lkerislsvd ifqnktsdml vaevlpttag lgyaltnsga
      781 mttkgfeasi nfkvlnkssv kwdlgvnlah akstidqlpn gnadivtnig agnivtrvgd
      841 apnsffgtiy kgvyatdaea taeglqtrlp dgtlrafqgg darfadlngd kiiddkdrti
      901 lgnpnptiyg gitnrvvykn wtldalvsfv sgndvynytr rniesgdsyn nqsravegrw
      961 rgngqvtnip ratygdplqn srfssrwied gsyirlrsvg lsynfnvdkg ilkyltvyan
     1021 annvltftky lgydpefsat nsiigqgvdn tlepiqksfn lgvklgl
//
LOCUS       WP_095163681            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flectobacillus
            sp. BAB-3569].
ACCESSION   WP_095163681
VERSION     WP_095163681.1
KEYWORDS    RefSeq.
SOURCE      Flectobacillus sp. BAB-3569
  ORGANISM  Flectobacillus sp. BAB-3569
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Flectobacillus.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Flectobacillus sp. BAB-3569"
                     /db_xref="taxon:1509483"
     Protein         1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121349
     Region          29..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiltkilli cglvltgvsw shaqspnlft vrgkvveakd ssavidvtva eldkdnrivk
       61 gvttdvegnf virvsnqnnt lsfssigfkt qkvaikgrsn ikiwmesssa dldevvvtak
      121 ptdnglmtvs ernttiavak idakvledmq gtsidqmlqg rlagvditaa sgdpgtgmqi
      181 rirgtssins svdpmivvdg mpyetsipsd fnfgtademg yasllnlaps dikniavlkd
      241 aaatamwgsr aangvvvint krgaigtpkv tytfkgsisk qpnaipmlsg dqysmlipea
      301 ymnrngipln tqtikefqyd pndpywynny sqnvnwvdai tqlgysqdhn vsimgggeka
      361 kyyastgyfn qvgttigtgl drintrinld ynvsnrirfk tdlsfthsvn nrnyvssltg
      421 nrdlvrsvay skmpnmsiye yndlgqltgn yfspltniqg tftgltnaty npvamvksak
      481 niiiseriip hfqvqydlap gkwvatfdvq fdinnnktss flpqvatgqa ftssfvnvat
      541 dgdadgfavt tkstliytpk ikntkhdfts lwalntsdvk svwqesyvtn tassdltdas
      601 nparlttsrl asgvsqtrnv gllwnihygf ldryiidlgi rgdgnsrfgp ayryglfpsi
      661 sakwilsdep fmrpfenife hlgirasygq sgnaprydyl yygkyntlgw sylgdaavvp
      721 qtmqlnnlrw ekivgrnlgi niitskrklt ldaefyqnst kdlffenlqi paytgfsnvq
      781 mnvgtmenmg welnmmynpy ktkdwnvdfn fniarntnvi reisdlyprt ggnatlngay
      841 mtymqvnnpf gsfygyrylg vykdksatva kgksgepivt pdgqsvymrf nypntdytfq
      901 pgdamyedvn kdgninymdl vylgnsnpaf tggfggsvsy ksfkittffn frndydvvna
      961 trmnttnmfg fgnqstevla rwrkegdvsm vpralfnsgy nwlgssryve dasfvrfrta
     1021 tfsytfpknv lktlhftalr ayatvenlit wtkytgqdpe vqmrgsdpfr vatdnsmtpp
     1081 aktvtfgfaa tf
//
LOCUS       WP_095163948            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flectobacillus
            sp. BAB-3569].
ACCESSION   WP_095163948
VERSION     WP_095163948.1
KEYWORDS    RefSeq.
SOURCE      Flectobacillus sp. BAB-3569
  ORGANISM  Flectobacillus sp. BAB-3569
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Flectobacillus.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Flectobacillus sp. BAB-3569"
                     /db_xref="taxon:1509483"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120788
     Region          27..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkacrkiftt lfatlliltg qfvmaqqvvk gkvvdsnqsa lagvsilvkg ttkgtvtdgs
       61 gnytisvakn aslifqslgf atktvevsgr ttidvvlest sqdldevvvt algikreqka
      121 lgysigtvss keitasgntn fasalygkva gvkistapgg atsavnvqvr gvnslnyntq
      181 plyvvdgivi rdfnqagang lnnggywddq rirgngildi npadiaslsv lkgasataly
      241 gseasngviv ittksgvkgk glgvelnyty nqervaftpq yqnvygpgyd ratnlavgan
      301 eegfitnpgg skrvnfrayg qfgpkmdgrm mpwwdgtmqs ysakpnnfnd fyqtgynstv
      361 naafsnatdk gsyrfsytgt dyagimrgsn lkrntfnlns svklsnkvta dvvvsyinsk
      421 vhnrpeqinr vtanyggfys raedmnnfln hyqtsqgyky vpynvpernp seafkynirg
      481 gdimdllwna lrnsedenqd rvlssvtlny kinnefglrg rvgndftslg tevkkynefp
      541 alfnsgnstg eyrvasgrys ivygdamlty akklntdfdl sasagvqgrq ekyydqsvgt
      601 ngglvienwf smnnstnvln asasrremik faylgtlnaa yknmlfvegt arqeysstlp
      661 agnnsyfyts vnsgfvfsda fqmpnfmnyg kirasygvvg napplyvant tysqtilqta
      721 ygavpalras ssygndnikp eqkfenefgl etkffknklg fdvtyynsri kdqilqtsip
      781 tstgassvla nvgelrsfgw easiyatpik trdftwntri naainrtkve klakgipqlv
      841 aydadqsaik ivadegdylg niythvratd skgnfiised glytltsdyk kvgnvmpklv
      901 ggflnsfsyk nfsldinmdy riggqlvsnp llyatgagmf estmkyrdae ngglpyyvdg
      961 sgnnvllssh tatapnggkv yhdgvlldgv tasgekntki idaasyymnt ytwgssgwye
     1021 ngsvynnsyl kvreailsyt lpsavaqklr lqnvrvslig rnlfylyrtl knldpeapig
     1081 tswnrqgide gstaatrsfg valhasf
//
LOCUS       WP_095165179             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_095165179
VERSION     WP_095165179.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38638
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag isasvvdsay eaagavigsa
       61 ndafgaelil kvvapsdsel sliksgtvlv gmlnpfsnet iaklaergit afsleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvivahgv tiagptnlaa qvgadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095165413             314 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas sp. Irchel 3H3].
ACCESSION   WP_095165413
VERSION     WP_095165413.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Irchel 3H3
  ORGANISM  Pseudomonas sp. Irchel 3H3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Pseudomonas sp. Irchel 3H3"
                     /db_xref="taxon:2009038"
     Protein         1..314
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35258
     Region          5..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mpiydlyskr qrklrgevpd vyvydafpnt lraqlsymik dllgdqdnyh hhrlrtpkal
       61 ydeivvilkk eyglhslvtg yvnssftelh dfllqerdve rcldvvelcy slgdtfarky
      121 syaerknsne hvddclneln erfkeagcgy elidgkiiri dsqllhaevv kpaigflnge
      181 eyegprdefl gayehyrhgn qeealvdalk afestmkvil tangkaysag dtasklilac
      241 rdadlmpayn esqlqslvnv ltsgiptlrn kngghgqgea vrtvepeiva yglhlaasai
      301 vmlagleakr raah
//
LOCUS       WP_095165559            1151 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flectobacillus
            sp. BAB-3569].
ACCESSION   WP_095165559
VERSION     WP_095165559.1
KEYWORDS    RefSeq.
SOURCE      Flectobacillus sp. BAB-3569
  ORGANISM  Flectobacillus sp. BAB-3569
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Flectobacillus.
REFERENCE   1  (residues 1 to 1151)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1151)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1151)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1151
                     /organism="Flectobacillus sp. BAB-3569"
                     /db_xref="taxon:1509483"
     Protein         1..1151
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126872
     Region          48..113
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          125..1148
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkkrfslii rriisvptls lalglgichv qvsqaqevln tkvsvqaqnq slenvlsqie
       61 kqtgvrfvya gslisekdkv tfsaqnqnlk qvlngifsnr nidfsfsgnn qivlkaspks
      121 qdhttvsgki tdaqtgdalp gvnvsvkgts kgatsdangn fkisisdkda vllfsfvgfs
      181 sqevpikgrn hlnvqlsedn kylnevvvta lgikreekal gystqkldgs avtdapsnnf
      241 mnalsgkvag lnltktdgpm gssrvtlrge sildfnspga livvdgepin tsfqgvghga
      301 ylggdspidf gsaltdidpn niesinvlkg paasalygsr agngaiiitt ksaskdkkgl
      361 gvsfnsyvsv dqvnrwpdyq yqygqgtagq nyysygttad gagtqstssa wgpkfdgqsf
      421 yqynsprdan gvftertpwk pytdnrknff eqgvtlsnni sitnvkdksn trlslsqmkn
      481 nwilpntgye rislgfsnns qisaklstsa kvnyynkfsd nlpstgynnq simyfiafqn
      541 pnvnldwyqp ywlpgkegle qnhpfsslid npylivyeml nkssrhnvtg tmsatynilk
      601 gldltvrtgl dmgyefrsqq rpkntqkfqa gmyrqqnvfn lesnsdfllk yklplektwq
      661 vttslggnil kqsqkftnql adrlvipgvy nlanseqlpl tqsdraekri nslygfvnlg
      721 ykdfafldvt grndwsstlp kqnnsffyps atlslvlsqm tnmpnwisyg kirgayasvg
      781 ydarlgtynl ekiynsgtfp gelespnvia npnlkpqrnn sfeagtewrf fknrlsldat
      841 vyeqttidqi lyapvefasg yssslinmgk vvnkgveltl ngnpvknyag fswdvtvnws
      901 mnrnkvleln netgsvilak yvgsrvtvea regqplgtiy glgfkrspeg qivfdkdgyp
      961 vltdqfvnlg ntnpdwrgsi snnfkyknws lsvlldirqg grifsltnsi lgeqgkntat
     1021 lagrydgiig egvtlnadgq yvpnttkatn ivtyynkwyg rdnveantfd asfvklrear
     1081 laytipakil rktflrtasi giygrdlfvw stfpafdpet stldnatitp glevgqfpst
     1141 rtmganltis f
//
LOCUS       WP_095166491            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flectobacillus
            sp. BAB-3569].
ACCESSION   WP_095166491
VERSION     WP_095166491.1
KEYWORDS    RefSeq.
SOURCE      Flectobacillus sp. BAB-3569
  ORGANISM  Flectobacillus sp. BAB-3569
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Flectobacillus.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Flectobacillus sp. BAB-3569"
                     /db_xref="taxon:1509483"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111838
     Region          28..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlqkpfm vlvalmlmsi salaqtytik gkitsqstne alagtsviik gttlgtvada
       61 kgeytlranl kegsyelifr sigyknatkn itlgnsntln ldlalsddda faldevvftg
      121 stlssnkrel gntinsvkad alqktgttnl fsalqgkipg aqitqnsgdp sggisirlrg
      181 tkslrgssdp lyvidgvvvs nassnvsqia vdaqagvanl gtnrmadinp qdietinvln
      241 gaaaaavygs rasngvviit tkrgksgtpk vtfstsmnvn qlrkkvfvst ygkqfgfagl
      301 rlhtiggisa aqiaanpgvt ttnilrdgts tslatnlvdv trydyqdqif rtgvgtdnyl
      361 sitggnektq ylasvsymkn qgiikgadfq ryglkvrvdq hlnnwakvsa glnyintfsn
      421 ekpngnvfys pinsvnitnn iyditkrdaa gnllaveptr vnplstiedm dfsqatnrti
      481 adlqlnltpa rgltidwvmg idafsqlgkn tikpypyate aglplerypl gfaatassnt
      541 flfntdvnig ydknlsddvk mtltagfnhq ytqtdistnt gqnlapfiet vsgaasttvt
      601 atygldryav tgqffqatfg yknrafltga irrdgstifs pdqtnqlypk isgsyvllea
      661 qdgwingakl rasfgdaggl talgtydrfw qfspaaylgk stilpgrqla npsvkpermr
      721 elefggdfsl vknkvslglt yysqnitdlv vnrvlaassg gtsivnnvge mqnkgfevsl
      781 ganviktkdf swdanvvfss nrnkitklpg gnvaitnaag apifliegqp asvfygnpya
      841 rnadgslllt sqgfpqrerg tqtgilnytp qrnasgqptg afitsvignp npdwtgsfss
      901 nfqykklslr flldavqglq vfnadkrtrn nvgigdlaea elrgtaprgt vfalvpieey
      961 rvdngsfvkl revslgysfv kalagkydln vslvgrnlvs wdnyngfdpe tnaggnssll
     1021 rgvdfgnipi prtyqltisa nf
//
LOCUS       WP_095167861            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flectobacillus
            sp. BAB-3569].
ACCESSION   WP_095167861
VERSION     WP_095167861.1
KEYWORDS    RefSeq.
SOURCE      Flectobacillus sp. BAB-3569
  ORGANISM  Flectobacillus sp. BAB-3569
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Flectobacillus.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Flectobacillus sp. BAB-3569"
                     /db_xref="taxon:1509483"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111584
     Region          54..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikllrkpqf lrfppssfwl mvllsgypls httqaqntte ntqtsnatlr tilvtddnde
       61 vlenvnlkns rtgmfattss ngiatidaqi gdkigiycvg tflkeisikd iservvlssq
      121 npavarikpi rglfnqslqs eitagssqai ynkdiqkmpa tsilntlvgr lagtstfqfs
      181 gqpgsdgisf glrgqgplvi idgiprqlti fdleeiesit vhkdalsnam lgvrsnggal
      241 vintrkgsas nakmsftaqt aiqqplkfpk gldaynyakl ynearvndgl tpvysdaalq
      301 ayatnsdpyn ypnvnwrdat lepssrmdry tfsatggnnf skyfisfdhi nqtgllkknt
      361 ttpyntnnnf ksytirsnvd lqlnsklsgg iyllgrilng ndagagtsni lnsilntpnn
      421 aypvynpngs yggnqqfqnn ilaqtigsgy qqnfkrdmla dfylkrtlde iasgmwikav
      481 gsyyatlsen vvrnktfavf qrnvsatgqe tyqqfgvngd qsnynymdyq grsdylelsl
      541 gydktrgnhg vnavllanrq nsvsgsdlpy titglagrmg ynykqkyild lafglngsnr
      601 yptggttkyg ffpavglawn iskedflqsq awisylklya sygkngndnp gyfsyiqryf
      661 dntgavfgtg aggntgvtee planpnitfe ksnklniglt galfdnslgf tveyynmqyy
      721 dlliqrgrnt silgniypne nigknqytgi dlqlnwqkst sigdfyatan agfqnskviy
      781 idevtqpysw lyrtgqrvgq lfgyisegfy qttaelqsra ttvgyqpqlg dlkykdlnnd
      841 gvinqldvap igpqspyitf gstlgysrkg fdfsvlvqgv anrvivanan smlafqnggf
      901 gqafeqhldr wtptnpnasy prlwlgtntn nqlvstfwar sgdyvrlkni elgytlpskl
      961 cknikvqgir vfanatnlvt fnadkyldpe gfssnypiqr vfnfgvnlkl
//
LOCUS       WP_095168146            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flectobacillus
            sp. BAB-3569].
ACCESSION   WP_095168146
VERSION     WP_095168146.1
KEYWORDS    RefSeq.
SOURCE      Flectobacillus sp. BAB-3569
  ORGANISM  Flectobacillus sp. BAB-3569
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Flectobacillus.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Flectobacillus sp. BAB-3569"
                     /db_xref="taxon:1509483"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115242
     Region          26..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnrlrnflv lflfvltcgy aqaqttvkgv vsskedgtal pgvtvvlkgt tkgtttdkdg
       61 kfsiaaagng tlvissvgyt kqeisiqnrt tinvslegda qmlnevlivg ygtvnksthv
      121 gssaqiskdv iatkpvanvm nalvgaapgv qatlsggapg septirvrgf gslsasnnal
      181 yvvdgvpfng ststlnpddi esisvlkdaa ttaiygsrga ngvimittkk gkegrnnfni
      241 sasegviarg lqeyetvsaq qyyplmwevy rntltygslk vpqdvassia sglttsyggr
      301 aytgiynllg synpfnvspt qivdvngqln pnaqllyped lnwanamqqg gksrknytin
      361 ydggtsksdy fvslgytkeq gyllksdfer ftgrvsvntq atkwlktgln lngtysmanv
      421 dagsdggtsf inpfyisrfm apiypvykhd qttgayvlda ngnrvydmgd srpnssgrht
      481 iwenelnqrn qirgligart fatitilpfl kattnlsfdl qdthyrtydn ptigdgapag
      541 rsyhylyrtt nytwnqllef dkqigkhhvn vlgghenfty kynyltgsrs giivdgitel
      601 pnfatvlgvs syednyties yfaranydfd kkyilnasir rdgnsrfapg vrwanfwsvg
      661 gaynieredf fdvkwvdllk vrasygvvgn dgglgyypyq alytlgrnnn aepgftqasi
      721 pnpdltweta nnfdlgvdfs lfkgklsgsl eyfnretagl ifnvplplaa ggttgggfti
      781 pknignlynr gfefqltgdi intgdfkysa tlnattlknq itkmpdnqpl iisgskgysv
      841 ghsiydfylr qfygvdsetg nalyktnilt tngkvigadt vttvlaeanq ryngtssipd
      901 vygsinnnfs yknftlsvql tyqlggkvyd saygslmhgg tygtamhvda lrrwqkagdv
      961 tdvprfdngn itnqtggstr yltdasylml nnvtftykip snwlakigak nasvyfsgen
     1021 lgllsarkgm nvtgsfngtv dntynfnrvm sigarlgf
//
LOCUS       WP_095190293             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Irchel 3E19].
ACCESSION   WP_095190293
VERSION     WP_095190293.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Irchel 3E19
  ORGANISM  Pseudomonas sp. Irchel 3E19
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. Irchel 3E19"
                     /db_xref="taxon:2008981"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38809
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv ticgptnlag evaadasaly arnlldflkl vfakegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095194642             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Irchel 3A7].
ACCESSION   WP_095194642
VERSION     WP_095194642.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Irchel 3A7
  ORGANISM  Pseudomonas sp. Irchel 3A7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. Irchel 3A7"
                     /db_xref="taxon:2008913"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38505
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag vnasvvdsay eaagatigsa
       61 gdafgaelil kvvaptdsel aliksgtivv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlaa avaadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_095200827             428 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium carmichaelinearum].
ACCESSION   WP_095200827
VERSION     WP_095200827.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium carmichaelinearum
  ORGANISM  Mesorhizobium carmichaelinearum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Mesorhizobium carmichaelinearum"
                     /db_xref="taxon:1208188"
     Protein         1..428
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43945
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivetg agtrsripde efakagavig
       61 kaadvgkadv vlkvrrptea elkgykagaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedde fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 pgkvvttann vkivghlnvp grvaasasll yaknlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafakadq qphvepaaip attmvasaep aaakkaatkk taasqspssk
      421 spkskgta
//
LOCUS       WP_095231392             898 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides].
ACCESSION   WP_095231392
VERSION     WP_095231392.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98499
     Region          27..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgrvslclvi mfficsaqki daqvqnirek qdtisatksl ehirpenikk gplnnaldvl
       61 sgqsagvnvt tngtdrlaml nsirvrgtts imggndplvi idgvtsdiat lstiypadie
      121 sftilknate tamygsrgas gvieiktkkg tgrgfeisyd gnygfesmyk hlqmlngpey
      181 iataealgld ynnggyntnf hdvitrtgli hqhhlafsgg sensnyrasf gfmdhntivk
      241 vndyrnlvvk ldatqkafdg rlvgdfgvyg ysskihdifd trmlfysaaa qnptypagtd
      301 vngnwvknsa ashinhpgal lyekndseer nfnthlgmkf nildnlilsa fgsysysstg
      361 naqfcptwvw aqgnvyrgef kgedyftnvs lsynnawgds hldavvgaey lkqvrtglwv
      421 qakgittndf synnigatss rpfggtsssy edpslasimg svtysykdry siaaalrgdg
      481 ssmvsdnntf gffpsvslgw dvkkegflsd tdfitmlklr tgygrsgnlg gitsyttlnt
      541 vkengivsin gaptvtmgsi rntnpdlkwe trstfnigfd lgiwdnrlml tselyysktt
      601 dmlyeydvpv ptfafdklma nigsmsnqgv elgisvvpiq rkdmemninf nmsyqknkll
      661 slsgeyngmh mtasditpig slygagqngg dnnvvyqivg qplgvfylph ckglkenelg
      721 gysydiedln ddgeidfsdg gdryiagqat pkvtigsnis fryksfdiam qingafghki
      781 fngtglaytn msifpdynvl kgapekniid qnvsdywlek gdyvniehit igynipmksk
      841 avkslrlsag isnlatitgy sgltpminsy vvsntlgidd krtyplyrty slglsiqf
//
LOCUS       WP_095374707             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_095374707
VERSION     WP_095374707.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53567
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq inaekqdfik tviphweeqa rkngllsq
//
LOCUS       WP_095400239             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia ubonensis].
ACCESSION   WP_095400239
VERSION     WP_095400239.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39217
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ayetrvaatp etvkkyaaag hrvsvakgag vaasypdday aaagaeltdq
       61 saafdadivl kvqaptetei pslkrgsvli gmldpfngeq aaqlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaadlypr flpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmpaswlg
      241 rqaalvhera kqadiiitta lipgrpaptl isvetvqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qvivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegaltidl
      361 tddiiaatll crdgevark
//
LOCUS       WP_095415027             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thermogutta terrifontis].
ACCESSION   WP_095415027
VERSION     WP_095415027.1
KEYWORDS    RefSeq.
SOURCE      Thermogutta terrifontis
  ORGANISM  Thermogutta terrifontis
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Thermoguttaceae; Thermogutta.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Thermogutta terrifontis"
                     /db_xref="taxon:1331910"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40784
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,97,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigvlrerf pgekrvavvp anvpglvkag htvrvesgag eragfpdsey sargatitsl
       61 aevleaevll gvrwdippev rdeilagirp gqiligawdp lskkgdllpw vekgatifal
      121 ellpritraq smdilssmat lagyravlla altlpkifpm lmtaagtltp akvfvvgagv
      181 aglqaiatak rlgaavsayd vrpavkeqvq slgakfvele lptqaaedqr gyakelgeev
      241 yrrqrelmtq vvaqsdvvit tasvpgrrap vlitremvag mqpgsvivdl aaerggncel
      301 trpgetvveh gvtilgpvnl paeiphhasq mysknittff lyvckngqia ldsedeiird
      361 tlvarggqvv hamlrepagq psq
//
LOCUS       WP_095400808             534 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia ubonensis].
ACCESSION   WP_095400808
VERSION     WP_095400808.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..534
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55139
     Region          3..534
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlrigiple tttgerrvat vpevveklik lgfsvavqsg agaganfddd ayhaagaevv
       61 asaaelwsgs divfkvrpps sdevalmrdg gtligfvwpa qnpelmqqla arratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa nlgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvie elckakdgti nvdfdddair
      361 gltvikegni twppppikqa avaprpqaaa paaaaaaksk ghghsgepms akalaivfai
      421 galafllvgq yapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapplge laggagdrps glilglavga laltavnmfg gfavtrrmla mfrk
//
LOCUS       WP_095417459             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia aromaticivorans].
ACCESSION   WP_095417459
VERSION     WP_095417459.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia aromaticivorans
  ORGANISM  Paraburkholderia aromaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia aromaticivorans"
                     /db_xref="taxon:2026199"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39445
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvsqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatla gmldpfnten ssklaaagit afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvdtvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvirhgvti vgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_095435831             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. 11515TR].
ACCESSION   WP_095435831
VERSION     WP_095435831.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. 11515TR
  ORGANISM  Rhizobium sp. 11515TR
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium sp. 11515TR"
                     /db_xref="taxon:2028343"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40507
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msnlvfvake svaeetrvaa svetvkkmkn lgfdvvieag agtlsripdt eyeaigarig
       61 sikdakaadv ilkvrrptsk eisgyksgai viaimdpygn eaalaemara gltsfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg alvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vgrdmlkamr pgavavdlav erggniegae
      301 ygkiadvegv kvvgypnmag riaasasaly aknlvtflet mvdkdtksla lnrtdelika
      361 tmltdggevv npnfvdpdqp tikkgdl
//
LOCUS       WP_095439075            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_095439075
VERSION     WP_095439075.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118740
     Region          22..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllmfpai cfalpvmaqq iitgsvidet trlpvkgvtv aiqntktvtt tdqngkfsls
       61 tdekrislvi lgkgyeekvl slelplsepl riylsekvaq idevvlttgy hkipkerstg
      121 sfssvgktal ntqvstnild rlaatangiv isrgtsqgtp qvmvrglsti qgpkaplivv
      181 dnfpyegdis nlnpniveni tilkdaaaas iwgaraangv ivittkgaky nqpitvdfnt
      241 flttspkpdl nylkvissad fidveqelfk knfyntdins sshpvlspvv dllnkekkgl
      301 lshevvqqei erlkgidsre qfkrymyqpl enrqyslsma ggspqfswts slgyddntgn
      361 lgenyqrmnl rfqnnwqpik nltlntaiff thsatrngrs aygsiimktn avpymemada
      421 ngnalivsks feqgyksglg ngklldwnyy pltdwqhfsg tgrsteiiln aglnykilkg
      481 leadlkyqyq rttglsnsiy deesyyvrdy vnrftvinsn gsltynvpkg sildkttsql
      541 linnfrgqln fnrgfgkhqv saiaggeird ansqsaniry ygydpnnlsf gtvdfknkyq
      601 litggtsfid nlnalretnn rfisvyanaa ytfdnrytis gsarrdasnl fglktndqwn
      661 pfwsaglswn vsnekfypls wlpelklrgs ygyngninpa mvavttmail gvstytqeqm
      721 arfdnyynpq lrwetvrmin agldfatrnn risgsieyfr kkgenlfgqv pldytiglts
      781 liwnvagieg ngvdvelrti ninkvfrwqt tanfstykdk vtkyypssti arnfvlssvp
      841 isgieglpvy sifayrwsgl dpqngdprgy lngevskdya kmmgtdvkdl eyfgsaipta
      901 ygsftntfsy kqftldvgit yklgyyfrrp sinytslfkd wighsdyalr wkkpgdeaft
      961 dvpsnqyqtn snrdafyags aaliekgdhi rlqyinlgye iskkqwqqmp lkslqlyani
     1021 snlgilwqes ksgidpdfnl gsyvvkppvm ytlglkakf
//
LOCUS       WP_095447222             435 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ochrobactrum quorumnocens].
ACCESSION   WP_095447222
VERSION     WP_095447222.1
KEYWORDS    RefSeq.
SOURCE      Ochrobactrum quorumnocens
  ORGANISM  Ochrobactrum quorumnocens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Ochrobactrum.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Ochrobactrum quorumnocens"
                     /db_xref="taxon:271865"
     Protein         1..435
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45208
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifipke sdpnetrvaa saetvkkfia lgfdvvvekg ageksriidt efsgagarig
       61 tatdaktadv ilkvrrpnda elkgyksgaa lfamldpygh edavaalgka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidasst ydrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedde fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vtkemvaamr pgsvlidlav erggnvegai
      301 agqvaevngv kivghlnvpg riaatasqly arnlyaflet lvdkeakllk ldpeeelvka
      361 tllthqgkvv hpafakvdvv pvveaetvak pkaapktkpa avkaeaapaa vkparkttkk
      421 apakaaktsa dggea
//
LOCUS       WP_095457519             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            metoecus].
ACCESSION   WP_095457519
VERSION     WP_095457519.1
KEYWORDS    RefSeq.
SOURCE      Vibrio metoecus
  ORGANISM  Vibrio metoecus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio metoecus"
                     /db_xref="taxon:1481663"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53906
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprerl agetrvaasp ssveqliklg fevcieskag alasfddaay saagaqivss
       61 eeiwacplil kvnapleeem allqegttli sfiwpaqnpa lmeklaskki nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittangvkvi gytdmvgrlp tqssqlyatn lvnllkllsk ekdgnidinf edvvlrgvtv
      361 ikegevtwpa ppiqvsaqpq qkakaqpakv qkkepeptsp vkkvaglaig vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflaciaili asinifggft vtkrmlemfr kh
//
LOCUS       WP_095459531             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            metoecus].
ACCESSION   WP_095459531
VERSION     WP_095459531.1
KEYWORDS    RefSeq.
SOURCE      Vibrio metoecus
  ORGANISM  Vibrio metoecus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio metoecus"
                     /db_xref="taxon:1481663"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53927
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprerl agetrvaasp ssveqliklg fevcieskag alasfddaay saagakivss
       61 qetwacplil kvnapleeem allqegttli sfiwpaqnpa lmeklaskki nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittangvkvi gytdmvgrlp tqssqlyatn lvnllkllsk ekdgnidinf edvvlrgvtv
      361 ikegevtwpa ppiqvsaqpq qkakaqpakv qkkepeptsp vkkvaglaig vgffawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflaciaili asinifggft vtkrmlemfr kh
//
LOCUS       WP_095459923             264 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Vibrio metoecus].
ACCESSION   WP_095459923
VERSION     WP_095459923.1
KEYWORDS    RefSeq.
SOURCE      Vibrio metoecus
  ORGANISM  Vibrio metoecus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Vibrio metoecus"
                     /db_xref="taxon:1481663"
     Protein         <1..264
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          <1..263
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 vdiiittali pgkpapklit kemvdsmkag svivdlaaan ggnceytvkd qvittangvk
       61 vigytdmvgr lptqssqlya tnlvnllkll skekdgnidi nfedvvlrgv tvikegevtw
      121 pappiqvsaq pqqkakaqpa kvqkkepept spvkkvagla igvglfawva svapaaflgh
      181 ftvfvlacvv gyyvvwnvth alhtplmsvt naisgiivvg allqigqgsg ivtflaciai
      241 liasinifgg ftvtkrmlem frkh
//
LOCUS       WP_095467105             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_095467105
VERSION     WP_095467105.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53868
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kh
//
LOCUS       WP_095470670             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            metoecus].
ACCESSION   WP_095470670
VERSION     WP_095470670.1
KEYWORDS    RefSeq.
SOURCE      Vibrio metoecus
  ORGANISM  Vibrio metoecus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio metoecus"
                     /db_xref="taxon:1481663"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53907
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprerl agetrvaasp ssveqliklg fevcieskag alasfddaay saagaqivss
       61 qetwacplil kvnapleeem allqegttli sfiwpaqnpa lmeklaskki nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytikdqv
      301 ittangvkvi gytdmvgrlp tqssqlyatn lvnllkllsk ekdgnidinf edvvlrgvtv
      361 ikegevtwpa ppiqvsaqpq qkakaqpakv qkkepeptsp vkkvaglaig vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflaciaili asinifggft vtkrmlemfr kh
//
LOCUS       WP_095476505             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            metoecus].
ACCESSION   WP_095476505
VERSION     WP_095476505.1
KEYWORDS    RefSeq.
SOURCE      Vibrio metoecus
  ORGANISM  Vibrio metoecus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio metoecus"
                     /db_xref="taxon:1481663"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53921
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprerl agetrvaasp ssveqliklg fevcieskag alasfddaay saagaqivss
       61 qetwacplil kvnapleeem allqegttli sfiwpaqnpa lmeklaskki nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittangvkvi gytdmvgrlp tqssqlyatn lvnllkllsk ekdgnidinf edvvlrgvtv
      361 ikegevtwpa ppiqvsaqpq qkvkaqpakv qkkepeptsp vkkvaglaig vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflaciaili asinifggft vtkrmlemfr kh
//
LOCUS       WP_095484366             417 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Mesorhizobium].
ACCESSION   WP_095484366
VERSION     WP_095484366.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42871
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripde efakagavig
       61 kagdiakadv vlkvrrpsea elkayrrgta viaimdpygn daavdalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fraaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsviidlav erggnvegav
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafie tlvdkttkal ainrdddlvk
      361 atmltdggqv vhpafagkpa vmiasaepak paaakkpaat kkpaapkspa nkpkgia
//
LOCUS       WP_095493893             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium temperatum].
ACCESSION   WP_095493893
VERSION     WP_095493893.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium temperatum
  ORGANISM  Mesorhizobium temperatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mesorhizobium temperatum"
                     /db_xref="taxon:241416"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43302
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivegg agtasripde efakagavig
       61 ksgdvakadv vlkvrrpdga elkayrpgta viaimdpygn daavdalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vstamvasmk pgsvivdlav erggnvegav
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafle tlvdkttktl ainrddelvk
      361 atmltdggqv vhpafagkpa vmiasaapak paaakkpalp kkaaaskkaa tpkspanksk
      421 gia
//
LOCUS       WP_095502691             513 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Neisseria].
ACCESSION   WP_095502691
VERSION     WP_095502691.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54190
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl agetrvactp atvtqlqklg feivierdag laasldnaay eaagaimada
       61 dtvwqspliy kvnapteset grlnagqtlv sfiwpaqnpe lvqtlndkqv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgai vkafdtrlev aeqiesmggq flkldfpqea ggsgdgyakv mseefiaaem
      241 klfaeqakev diiittaaip gkpapklita emvqsmkpgs vivdlaaatg gnceltrpge
      301 lfitdngvki igytdmanrl agqssqlyat nlvnlaklls pnkdgeitld fddviirnmt
      361 vtrdgeitfp ppaiqvsaqp qakpsekaap makpepkpvp lwkklapavi gaililwiga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqghgf
      481 vsflafiavl ivsinifggf yvtrrmlnmf rkg
//
LOCUS       WP_095497104             463 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Paraferrimonas haliotis].
ACCESSION   WP_095497104
VERSION     WP_095497104.1
KEYWORDS    RefSeq.
SOURCE      Paraferrimonas haliotis
  ORGANISM  Paraferrimonas haliotis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Ferrimonadaceae; Paraferrimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Paraferrimonas haliotis"
                     /db_xref="taxon:2013866"
     gene            1..463
                     /gene="nrfA"
     Protein         1..463
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51322
     Region          1..460
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mktmqltmsa llsavifaag vsakpgtepr nemyekkfpk qynswkatae seeivdaleg
       61 dpnlvilwag ygfakdynka rghmyavtdl retlrtgapk taedgpmpma cwsckspdvp
      121 ryieengeka yftgkwakgg seivntigcg dchdkgspkl risrpyadra feaidmpfak
      181 asrkdkqtmv csqchveyyf ektadkkgfv kfpwdggttv eameayydal qfadwthgls
      241 kapmlkaqhp gfetwrdgih gknnvsctdc hmprvtdeng kkytdhkvgn pfdqfeftca
      301 rchdqskeml egvmqarhda vteiklkaek qlvaahfeaa aawkagatda emkdiltlir
      361 hsqwrwdyai ashgvsahap dealrilgta vskaadarvk lahllaskgq agpvklpdis
      421 tkakaqaalg mdmkkmnadk qeflkttvke wdkkaaarea kmk
//
LOCUS       WP_095497251             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraferrimonas haliotis].
ACCESSION   WP_095497251
VERSION     WP_095497251.1
KEYWORDS    RefSeq.
SOURCE      Paraferrimonas haliotis
  ORGANISM  Paraferrimonas haliotis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Ferrimonadaceae; Paraferrimonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Paraferrimonas haliotis"
                     /db_xref="taxon:2013866"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40981
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigllkein agekrvallp vnvaklvkkg lnvtveasag sasgfsdqdy qdagasiaer
       61 dqvmadaqvi icvsckdqqa eqvnsqlrkd qwliatmdpl araqqvaeya ntgvtalale
      121 lvpritraqs mdvlssmati agykavliaa ekaprlfpmm mtaagtlkpa rvfimgvgva
      181 glqacatakr lgavveaydi rpaareqiis vgarpvelnl edsatetkgg yateqtddfi
      241 arqqaamadv laqqdvvitt aaipgrpapk litaamvekm kpgtvivdla aetggncelt
      301 eldqviesng vtiigpsnma smaathasqm fatnienlln lmiedssltl dfedeiiket
      361 tvshqgeiis prlrdvlgln snnevsr
//
LOCUS       WP_095499838             463 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Paraferrimonas haliotis].
ACCESSION   WP_095499838
VERSION     WP_095499838.1
KEYWORDS    RefSeq.
SOURCE      Paraferrimonas haliotis
  ORGANISM  Paraferrimonas haliotis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Ferrimonadaceae; Paraferrimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Paraferrimonas haliotis"
                     /db_xref="taxon:2013866"
     gene            1..463
                     /gene="nrfA"
     Protein         1..463
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51332
     Region          1..460
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mktlqltmsa llsavifaag vsakpgtepr nemyekkfpk qynswkatae seeivdaleg
       61 dpnlvilwag ygfakdynka rghmyavtdl retlrtgapk taedgpmpma cwsckspdvp
      121 ryieengeka yftgkwakgg seivntigcg dchdkgspkl risrpyadra feaidmpfak
      181 asrkdkqtmv csqchveyyf ektadkkgfv kfpwdggttv eameayydal qfadwthgls
      241 kapmlkaqhp gfetwrdgih gknnvsctdc hmprvtdeng kkytdhkvgn pfdqfeftca
      301 rchdqskeml egvmqarhda vteiklkaek qlvaahfeaa aawkagatdv emkdiltlir
      361 hsqwrwdyai ashgvsahap dealrilgta vskaadarvk lahllaskgq agpvklpdis
      421 tkakaqaalg mdmkkmnadk qeflkttvke wdkkaaarea kmk
//
LOCUS       WP_095501368             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_095501368
VERSION     WP_095501368.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53599
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllnq
//
LOCUS       WP_095505652             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraferrimonas sedimenticola].
ACCESSION   WP_095505652
VERSION     WP_095505652.1
KEYWORDS    RefSeq.
SOURCE      Paraferrimonas sedimenticola
  ORGANISM  Paraferrimonas sedimenticola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Ferrimonadaceae; Paraferrimonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Paraferrimonas sedimenticola"
                     /db_xref="taxon:375674"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40821
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigllkein agekrvallp anvarlkekg leilveqgag lasaiadsdy teagaslvsr
       61 eqvfadaell lsvtikgdqa eqidaqiqsg qwllgmmdpl aqaqqvaqya dkgvtalale
      121 lvpritraqs mdvlssmati agykavliaa eraprlfpmm mtaagtlkpa rvfvmgagva
      181 glqacatakr lgavveaydi rpaareqils vgarpvelni edsateskgg yateqsddfi
      241 arqqaamadv laqqdvvitt aaipgrpapk litaemvkgm kpgtvivdla aetggncelt
      301 qldvevveng vtiigpsnmp smaathasqm fatnienlln lmvnegqvtl dfedeilkdt
      361 tvshegqiis prlrdvlgld kpteese
//
LOCUS       WP_095511233            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Rubrivirga
            marina].
ACCESSION   WP_095511233
VERSION     WP_095511233.1
KEYWORDS    RefSeq.
SOURCE      Rubrivirga marina
  ORGANISM  Rubrivirga marina
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rubricoccaceae; Rubrivirga.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Rubrivirga marina"
                     /db_xref="taxon:1196024"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106222
     Region          26..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mllstlrrat laalfvlpal aaaqgtvrgt vtdaetgasi pgatvfvaas nigtttdadg
       61 ayelalppgq rtltvsfvgy rsqelevpeg qttlnialep dllgleevvv tglgttirra
      121 nsansvetis arelaevstp qtldgalngk vtgavinsns gapggginir lrgittingn
      181 sqplyvvdgv iisndavsng inavtaaagg gnasnqdnpa nriadlaped iesieilkgp
      241 saaaiygara angvvvirtk rgssgrtdvs fsqsvgmtsi grrlgtrqft eataidqftt
      301 apdddatpee iaqynasveq irqlyragea agfydyeeal ygneglllts dlsvsggndr
      361 tqffvsgivk ddegiieqtg yekqsgrvnl thrlsnvfsv dananyirsv arrgitgndn
      421 sgttygigll atpnfvnlfp dangvypdnp fnssnflqtr dlstieeenn rflgsgqltv
      481 nlfttntqsl qlvgtggvdy yaldqvnlfp velqfedddg lpgtsilgrt tnlntnlqal
      541 avhgyapegr slsfttqlgf tafdqdfnnv ssvaqglipn qqnldqaaal qtnqgrlfqn
      601 dravfaqeev nwndaiigtl gvraeqssan gdvdtfyayp kaglavnltn lglfeggpvd
      661 lfklraafgq tgntapfgak fttygtlavg gniglsiggq rgladvvper aseieagldl
      721 tlldgrvnfe gtvyaktvdd llltrqvpls sgftvetfng gqlqnngiel glslipvdgp
      781 svrwisrtsf wanqaevtel nvppfqaagg gfgtglgsir ieegesptqi vgidggevvq
      841 lgdvspdfqm sffndvtiar rlrftafahw kqggdiinls ellgdlsgts pdydddadgd
      901 gtpdglqrll qfgssarpfv qdasyfrlre vrldydvapq ffgplggalq slrlgisatn
      961 lftitpyksy dpevsnfgnq pvasgvevap fpssrnvyfh vnlgl
//
LOCUS       WP_095506342             462 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Paraferrimonas sedimenticola].
ACCESSION   WP_095506342
VERSION     WP_095506342.1
KEYWORDS    RefSeq.
SOURCE      Paraferrimonas sedimenticola
  ORGANISM  Paraferrimonas sedimenticola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Ferrimonadaceae; Paraferrimonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Paraferrimonas sedimenticola"
                     /db_xref="taxon:375674"
     gene            1..462
                     /gene="nrfA"
     Protein         1..462
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=50999
     Region          1..459
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkamqvtlsv aiaatlcaal vqakpgtdpr nevyaekfsk qynswkates sseiedaleg
       61 dpnlvilwag ygfakdynka rghmyaltdv rqtlrtgapm spdegpmpma cwsckspdva
      121 rvieekgeag yfkgtwasqg hemnntigcg dchdkgspkl rvsrpfaarg feaagmpfdk
      181 asrkdkqtlv caqchveyyf ektegrkgfv kfpwdggtnv eameayfdai qfadwehgls
      241 kapmlkaqhp gfetwrmgih gkndvscsdc hmprveengk kftdhkvgnp fdrfeftcgk
      301 cheqskemlq avtkqrqeav aeiklraeeq lvaahfeaae awklgatdae mkdiltdirh
      361 sqwrwdyaia shgvaahapd ealrvlgtav skaadarvkl aqllaskgha gpvaipdist
      421 kakaqaalgm dmkkmeadke kflktvipqw eakaaereak mk
//
LOCUS       WP_095513338             981 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Rubrivirga sp.
            SAORIC476].
ACCESSION   WP_095513338
VERSION     WP_095513338.1
KEYWORDS    RefSeq.
SOURCE      Rubrivirga sp. SAORIC476
  ORGANISM  Rubrivirga sp. SAORIC476
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rubricoccaceae; Rubrivirga.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Rubrivirga sp. SAORIC476"
                     /db_xref="taxon:1961794"
     Protein         1..981
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104339
     Region          26..980
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhlstlraal lvalfafpal afaqgtvrgt vtdaetdqpl pgvtvfvqat ntgtttdvdg
       61 gyeltlppgq rrlqfsfvgy rdqeatvpeg qttfdvalep dllgldevvv tglgtsvrra
      121 nlansietis arelseisqp qtldgalngk vtgavinsns gapggginir lrgittingn
      181 sqplyvvdgv ivsndavsng vnvvtaaagg gnasnqdnpv nriadlaped iesieilkgp
      241 saaaiygara sngvvvittk sgtagrtevr lsqsvgvtqv qrllgtrqfd eatareayge
      301 igaelfrqan grtydyeeal fgndgllltt dlsvsggner tqfyvsgvvk ddegiiantg
      361 yekqsgrlnl thrlsqvfsa dvnanfirse targitgndn sgttfgigll stpnfvdlfp
      421 dengvypdnp fnsanflqtr dlatieetnn rflgsgrlta nlltsetqsl qligiggvdy
      481 yaldqinqfp velqfedddq lpgtstlgqt rnlntnlqvl avhgyaprdr nlsfttqvgy
      541 tafdqefdnv lnvaqglipn qtnldqastl qttqarlfqn dravfaqeev nwndavigtv
      601 gvraersssn gdveqfyayp kaglainltn lgllqggavd llkvraafgq tgntapfgak
      661 fttfgtlavg gniglsiggq rgladvvper ateieggidl tlldgrvsfe gtvytksidd
      721 liltrqvpys tgfafetfng gqlrnngiel glsvipvdgp tvqwvsrtsf wanraevtel
      781 tvppfqaagg gfgaslgsvr ieqgqsptqi vgdvngetvq lgdvspdfqm sffndvtimr
      841 rlrltafahw kkggdvinlt qlladllgts pdfdldddgd gipnieqrpa gaaafvqnas
      901 yfrlrevrvd ydvapsafgp fagtlrslrl gvsatnllti tpyksydpev snfgsqpvas
      961 gvevapfpss rnlyfhinlg l
//
LOCUS       WP_095514341             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rubrivirga
            sp. SAORIC476].
ACCESSION   WP_095514341
VERSION     WP_095514341.1
KEYWORDS    RefSeq.
SOURCE      Rubrivirga sp. SAORIC476
  ORGANISM  Rubrivirga sp. SAORIC476
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Rubricoccaceae; Rubrivirga.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Rubrivirga sp. SAORIC476"
                     /db_xref="taxon:1961794"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38739
     Region          1..357
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtlgvpreta pderrvaltp dairrlarag vevvvergag atafvsdaam eaagarlgdr
       61 tealgadvva tvkglppedv aqvregavvl gllrpldape alaplaerga taiamelvpr
      121 israqkmdal samstvagyr avllaaerlp kffpllttaa gtvrpakvlv lgagvaglqa
      181 latarrlgav tsaydvraaa reqvesvgad fveldlgagd aedasgyaka ltedqlvrqr
      241 aqladlvasv dvvittalip grpaplllte davaamppgs vivdlaapng gncaatvpge
      301 ttevsgvsil apldlaaemp lhasdmygrt vgalvldfmt ddgafrvdle deilagavvt
      361 hggvvvhprv lsllpeadsp
//
LOCUS       WP_095517374             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium wenxiniae].
ACCESSION   WP_095517374
VERSION     WP_095517374.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium wenxiniae
  ORGANISM  Mesorhizobium wenxiniae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mesorhizobium wenxiniae"
                     /db_xref="taxon:2014805"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43457
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtifipre ldaneprvaa spdtvkrlag lgfnvivesg agtasripde efgkagavig
       61 kaadvakadv vlkvrrpdea elkayrpgta viaimdpygn daavdalara gatafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttang vkiighlnvp grvaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafigkpa vmiasaepak paagekpaap kkaatsrkla apkslankpk
      421 gia
//
LOCUS       WP_095538322             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Vandammella animalimorsus].
ACCESSION   WP_095538322
VERSION     WP_095538322.1
KEYWORDS    RefSeq.
SOURCE      Vandammella animalimorsus
  ORGANISM  Vandammella animalimorsus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Vandammella.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Vandammella animalimorsus"
                     /db_xref="taxon:2029117"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38769
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpleta agetrvaatp etvkklvaqg hevlvqseag laaaatdeay raagaqivda
       61 aaalgaelvl kvrapsaqel palqpgavlv gmlnpfdaqg lqaladarlt afaleaaprt
      121 traqsmdvls sqaniagyka vimaadaypr ffpmlmtaag tvkaakvvvl gvgvaglqai
      181 atakrlgati easdvrpsvk eqveslgakf idvpyetdee reaaegvggy arpmpaswle
      241 rqkaevakrv aaadvvitta lipgraaptl vtedmvramk pgavivdiaa grgeggvggn
      301 cpltqadatv vrhgvtiigq tnlpalvaad asqlyarnvl dflklilpkd eglkidtedd
      361 ivaaclmard gqllrr
//
LOCUS       WP_095541153             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Vandammella animalimorsus].
ACCESSION   WP_095541153
VERSION     WP_095541153.1
KEYWORDS    RefSeq.
SOURCE      Vandammella animalimorsus
  ORGANISM  Vandammella animalimorsus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Vandammella.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Vandammella animalimorsus"
                     /db_xref="taxon:2029117"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38737
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpleta agetrvaatp etvkklvaqg hevlvqseag laaaatdeay raagaqivda
       61 aaalgaelvl kvrapsaqel palqpgavlv gmlnpfdaqg lqaladarlt afaleaaprt
      121 traqsmdvls sqaniagyka vimaadaypr ffpmlmtaag tvkaakvvvl gvgvaglqai
      181 atakrlgati easdvrpsvk eqveslgakf idvpyetdee reaaegvggy arpmpaswle
      241 rqkaevakrv aaadvvitta lipgraaptl vtedmvramk pgavivdiaa grgeggvggn
      301 cpltqadatv vrhgvtiigq tnlpalvaad asqlyarnvl dflklilpkd eglkidtedd
      361 ivaaclvard gqllrr
//
LOCUS       WP_095577990             369 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium marseillense].
ACCESSION   WP_095577990
VERSION     WP_095577990.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marseillense
  ORGANISM  Mycobacterium marseillense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Mycobacterium marseillense"
                     /db_xref="taxon:701042"
     Protein         1..369
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37737
     Region          9..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdaqtnavk vgvvsesgad errvalvpka vpslvgsgva vvvesgager allpdqlytq
       61 agatigdawa advvvkvapp tadevgklrs gqtligflap rnaensigal kqagvqafal
      121 eaiprisraq amdalssqgn vagykavlla aseatrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwldig idaageggya reltdeeraq
      241 qqqalekais gfdvvittal vpgrpaprlv taaaveamkp gsvvvdlage tggnceltep
      301 gktvvkhdvt iasplnlpat mpehaselys knisalldll ltdgklapdf ddeviagscv
      361 trdqgqkds
//
LOCUS       WP_095589956             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actibacterium ureilyticum].
ACCESSION   WP_095589956
VERSION     WP_095589956.1
KEYWORDS    RefSeq.
SOURCE      Actibacterium ureilyticum
  ORGANISM  Actibacterium ureilyticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Actibacterium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Actibacterium ureilyticum"
                     /db_xref="taxon:1590614"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55921
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapketf egearvamtp dsalqlqklg yecaietkag qlagfsdady ekagvevikt
       61 aaalwkecdi vtkvrqpdat emkrlregqt lisffnpggn eegmelaksk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg avtyafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apemdivitt alipnreape lwtedmvkam kpgsvivdla aekggncklt
      301 vkdekivtdn gvtiigytdf psrmaaqsst lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgatvtydhe itfpppppkv qaiaakpkae vkeltpeekr aaevaafkaq tkqqvtllav
      421 gaalllgvgl vapasfmqhf ivfvlavfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_095592860             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas dhakensis].
ACCESSION   WP_095592860
VERSION     WP_095592860.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53437
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tclgtsgwaq aadeaqpkgk vearselfak dhadqfsswk
       61 atgesrertd alaedpnmvv lwagyafakd ynkprghfya ltdvretlrt gapksaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy ftgptkavkf pwdkgttveq
      241 meqyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqnkemlqg vvkqrkdaih dlklrvekql vhahfeakta
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakglsq eiaipdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_095595828             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actibacterium pelagium].
ACCESSION   WP_095595828
VERSION     WP_095595828.1
KEYWORDS    RefSeq.
SOURCE      Actibacterium pelagium
  ORGANISM  Actibacterium pelagium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Actibacterium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Actibacterium pelagium"
                     /db_xref="taxon:2029103"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55569
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkevf egenrvamtp dsarqlqklg ydcaiesgag vaagftdaay keagvevikt
       61 aaalwkqvdi iakvrqpnat elkrltadkt lisffnpagn eegmeaakks gasviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvpparv lvvgagvagl
      181 aaigtstslg avtyafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvqseefr
      241 naqlakfrei apdidivitt alipnrpapk lwledmvaam kpgsvivdla aerggnvegt
      301 vpdekvvtdn gvtiigytdf psrmatqsst lyatnirhmm adltpekdgq vnhdmeddvi
      361 rgatvthqge itfpppppkv qaiaaksqek pkeltpeekr aqeiaafkaq tkqqvgllai
      421 ggaimlamgt vapasfmqhf ivfvlavfvg fqviwnvshs lhtplmavtn aissiiilga
      481 llqigsgsfl villaaisvf faginifggf lvtrrmlamf qks
//
LOCUS       WP_095600061             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. PIC25].
ACCESSION   WP_095600061
VERSION     WP_095600061.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. PIC25
  ORGANISM  Pseudomonas sp. PIC25
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. PIC25"
                     /db_xref="taxon:1958773"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39032
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth vgetrvaatp etvkkligqg hrvtvqsgag laaslpdaay qaigaeigsd
       61 adalgadlvl kvvapsetel aqmkpgavll gmlnpfdndn iarmaqrgii afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvqemk pgsvvidlaa aqggncplte
      301 adkvvvkhgv tlvghtnlaa lvpadasaly arnlldflkl vidkegqfhl nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_095605347             989 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fodinibius
            salipaludis].
ACCESSION   WP_095605347
VERSION     WP_095605347.1
KEYWORDS    RefSeq.
SOURCE      Fodinibius salipaludis
  ORGANISM  Fodinibius salipaludis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Fodinibius.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Fodinibius salipaludis"
                     /db_xref="taxon:2032627"
     Protein         1..989
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107741
     Region          44..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpniyrrif dkrgkrkvga ilailvmgvf lvftdsfaqg qdgvisgtvv eastgeplpg
       61 anvllqgtnk gasvdadgnf eitgleagey tlvirfigyk nyrqqitvvg qtnevnvele
      121 sesvgldevv vtatgemrsr evgtslsrvs sddfeagavs ntqdilngri tgatilansg
      181 npgaggtirl rgnnsisqnn npiiyvdgir isgddtpthq asrqssspln dinpndiesi
      241 dvvkgaaatt lygteasggv irittkqgqa gqtqwnagvt ggfnnmghfg pkednptglf
      301 mgecrgdnlv tydgtrfqea ncpdngswlq nglvqrynls vssgvedfty ylsgeyenee
      361 gvinngggtq glgfrgnfqf npidevsitf nssynndqtd wvpsgnngdg fvlnvtrgpg
      421 gnfsgasgce dpnaicvnng eilesknisd rehfinslvi etntlenlsn rltfgydyns
      481 selestqyfg ysrsplgqqs itdwqktvls feylgtfeqp inqdigltln wggqlfkeqt
      541 qttdlfsedf sgpqeptlts gartsisgds ritvttggff gqasfdlydk lfvetgvrvd
      601 ghsafgdnfg lqvypkvsas yvlsdygfwp tswwntmrlr aavgqagqap gafdavrtwr
      661 pvagedgqpg ftpnqignpd lgperstefe tgftasfldg rvttdftyyn qttsdalipv
      721 psvpsegfls sqvqnvgkvk nsgievdldl tvlqlqdvqw dmrfgfsken seavdlgntd
      781 eitvayfart yikegypvpg vfgakitnpd evadpeyeed hyfgpsypdk slslgttiql
      841 kdnlvldalg qfkyggymln atayqngrrg vwppcydlqq qdpssltasq rakcalnsgd
      901 vdprydhwie stdyfklrhv sltynlpqnw lvggvqsasl klaarnllti tdysgtdpei
      961 ddyrtslarr dyyamptyrs flatfnfsf
//
LOCUS       WP_095606318            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fodinibius
            salipaludis].
ACCESSION   WP_095606318
VERSION     WP_095606318.1
KEYWORDS    RefSeq.
SOURCE      Fodinibius salipaludis
  ORGANISM  Fodinibius salipaludis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Fodinibius.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Fodinibius salipaludis"
                     /db_xref="taxon:2032627"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121010
     Region          25..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvkkllslft lclifsataf aqsgtitgtv tdessgetlp svnvyvvelq rgaatnaqge
       61 ftiegveygt ytvrasfvgy ntfeqevtvd qstvtldiql assqmrldev vvtalgeevs
      121 qrqvsfstqe vgdeelnisq nsnvktslag kvsgvqivgq agsklgsfgd irirgaislt
      181 nelaeplyvl dgvpienpni idmnnvqevs vlkgpnatal ygqrgengvv iltsksgsgt
      241 gasveinsst tfdrvaylpn fqnqygkgyy asdgdpstsg gfatieaggt spfgapypsy
      301 ldeldgeryi aygyadeswg pefdgepyap wyswypdspy ygetqpwdas pnniknfydt
      361 gvtnkssiav nyntersntr ltftnlaqng iipsssldkk qlggnfsydv tddfnvgvkv
      421 nystqgvigd vrddgygnqt sgsfnswfar nlemdkmqel kdletpegyh aswnawgpgy
      481 mgfgggykkp afwynpytwm drydikrdtd nllmnvdlsy qltenielvg nasstsesyn
      541 rrfempyslt ksadqtgsfy nywvnsfgel sdeinehnfs srlkydadyg dfsvngfaga
      601 qmrieqykmf qadmgqtnit ygglnvpdly nfansreevi pvednwdkqv lsffgkatig
      661 yqdylfldat yrqdyssalp egnngygyps vglsfvftef mdndiltygk vragyaqvgn
      721 dvgaelinqt ynvrqipyrh avtgqpktll stsstlvdeg iepalnssfe vgadlefydn
      781 vfgldltyyn ekreneivta smssgtgytg lltnagaser egvevsfrat pvqnqdlrwd
      841 atvnwamnet ivtalpegvs syelgsnsaf gyislthrlg eewgqlrgpg iarndegqpi
      901 lnddglyvve qnkyfgsvlp dwtggiintv sykglqlsas idyqkggkff slteqwggys
      961 glteetagtn drggkirdyp segggvhvtg vdqqgnsvdt yvgaysyfsq fqantiaepf
     1021 indadfvklr elainytlpk qwtgnfinsa tigvvgrnlw miavadnnth nwdpselaet
     1081 ygengqlpgt rsygfnvkvt f
//
LOCUS       WP_095606022            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fodinibius
            salipaludis].
ACCESSION   WP_095606022
VERSION     WP_095606022.1
KEYWORDS    RefSeq.
SOURCE      Fodinibius salipaludis
  ORGANISM  Fodinibius salipaludis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Fodinibius.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Fodinibius salipaludis"
                     /db_xref="taxon:2032627"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118964
     Region          127..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkkrytvll slffvtamlv qgsiaqsnds eilslrnslq ydtsqsisle eilnnieedr
       61 nivflydvel iegktvslss ireperdlgl qlasilrpfd lsyerkggrs yiivskdkkq
      121 qalegilqgt vidgptgepm pgvnvfipel nigaasdaeg tfeisdvpeg tymlratfvg
      181 yetyeeeiei segdntieiv mnpsamqlde vvvsglassv krenlansvt kinadeltgn
      241 ttpatvdgal qgkvvgtnmt ssggapgggv diklrgistl gagssqplii vdgiyinnde
      301 letgvsavsa qqaasqddga nrladlnpde iesieilkgp saaaiygara nagvviietk
      361 rgsggatrvs fsqdvgyssi lnkigaasws edkidlvyga gssaaqsakq myndavangt
      421 lrdyeelifg regaqvntqi svsggdaqtq fyvsgafkde ngiientgfd ryslranidh
      481 qlnenidiss stnyintetn rgwtgnggvg svvqavaftp pfaqllpden gdypdnpffq
      541 mnplelieyg vnrqevnrfl qslsanfkly ssgahtlnfn ldggvdfmns ntmaymppfl
      601 qyqqsqanpg dvihsaekvl ninlqaflvy ntmvgsedsp wnlttqagyt tyhnerqlqq
      661 vrgrglvpgq tnvenaslqe iynqyfvdvt dvgyvaqqev nwddkvigtv garfdkstln
      721 adqdkyyffp kasmavnitn fefwsadile qfklraayge tgglpnfgvt fealnsglis
      781 gnlgtfrstr tidpnlepet aqelevgvdl glrggrasle atyyrknvsd lildqelpss
      841 sglqvmatna adlqnegiel alrtvpvqan kfswnstvnw wkntaeitnl kvpsfttggf
      901 gaalgtfyia egfspttivg tpfdteagrf tvygdsqpdy qmswtntinf lnnwefnffw
      961 hyshgqkvin lrrfladnag ttpdwnndsn gdgtpdgldr pgegagrfva dagylklrel
     1021 slyysvpasf lesytggtvk svrlgasgnn vllfsdypsy dpevsefgss aigtgvevaa
     1081 ypsarkimfh lkldf
//
LOCUS       WP_095606323             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Fodinibius
            salipaludis].
ACCESSION   WP_095606323
VERSION     WP_095606323.1
KEYWORDS    RefSeq.
SOURCE      Fodinibius salipaludis
  ORGANISM  Fodinibius salipaludis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Fodinibius.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Fodinibius salipaludis"
                     /db_xref="taxon:2032627"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40511
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miiaipketa erenrvalip dtisklveng hnvwvesdtg kassyldety qsagaeiitd
       61 rtklfadsdi lisiqtppee dlakmkpesi licflwalqn eetvsflqek kitalgmdai
      121 prisraqsmd alssmssiag yksaliaane ldrympmmmt aagtvapakv lvlgagvagl
      181 qaiatakrlg akveafdirp avkeqveslg atfvevpdld eeseteggya kelaedeqer
      241 qrqvihehaq qsdiiittal ipgkpaplli tkemvedmha gavivdlaae qggnceltdp
      301 getaikndvk vigplnipsq layhasqlys knmlsllnhl iqdgkaefdf edeitlntti
      361 thqgeiispm lkdn
//
LOCUS       WP_095606338            1007 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fodinibius
            salipaludis].
ACCESSION   WP_095606338
VERSION     WP_095606338.1
KEYWORDS    RefSeq.
SOURCE      Fodinibius salipaludis
  ORGANISM  Fodinibius salipaludis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Fodinibius.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Fodinibius salipaludis"
                     /db_xref="taxon:2032627"
     Protein         1..1007
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109113
     Region          25..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkntkyll gvvflllsqs avaqftvegt vidaqsgqal vgvniydpgs eqgtttnteg
       61 ffsleipaqs atlrityvgy nqknvevsad nneitielqk svanldevvv tglassvqre
      121 nlanavssvd seqltgttss qtlssslygk vaganitsnt gapgggmsvk lrgvttings
      181 seplyiidgi ylnndaiang snavtqaaag gsssnqdnpv nrvadlnpde iqsievlkga
      241 saaaiygqra sggvviittk rgsggkaqfs asqsigltti qkklgqrqft eataesafgp
      301 kgkalfneak ssnrfldyee lmygqegvls ktqisssfgn estsfyvsgm lqndegiikt
      361 tgyekqsira nvdhqftekf nvsvssnyih sesrrgltgn dntgttfgvs mvatpnfidl
      421 rpengvypah pfntanqlqt rdlfsnsenv nrvltsvkae ydifqkdgny lalqfqggvd
      481 ffsqnnklif psdlqferis aqpgtlvetn tnnlntntsl mlihtfslse natlvsqggy
      541 tsfnndqnti stvgrgilgt qtnvdqtvsv snnqtriyqr drgffiqeef nyndtyittv
      601 glrgdksdrn gnvneifyyp kasfawnisn mdfwegngpi dnlklrtayg qtgnlstfga
      661 kftslgpsni ggsggilitn trgtddiqpe rqkeleagfd isawggtanl svtvyqknis
      721 elllqrelep stgfsfesfn ggglrnrgie asldltpvrn nnlnwnstft fsknvsevtd
      781 lsvpafdvgg fgtslgvyrv eegksatqiv gldpvkdsng nfsgdittkk lgdgepnfql
      841 swynqlnilk nvdfsfmlhw kkggdvinlt ellsdlngtt adyddtdltf pdfvneaggi
      901 tddtkngvkr asllgvttrq fvqdgsylrm reiglyynvp tqmiegissa lrgirfgvsa
      961 tnlftispyr sydpevsnfg nqpiaqgiev tpypstkqyy fhfnidf
//
LOCUS       WP_095606727            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fodinibius
            salipaludis].
ACCESSION   WP_095606727
VERSION     WP_095606727.1
KEYWORDS    RefSeq.
SOURCE      Fodinibius salipaludis
  ORGANISM  Fodinibius salipaludis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Fodinibius.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Fodinibius salipaludis"
                     /db_xref="taxon:2032627"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119613
     Region          24..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkkllstlv ctflfagaal aqgtitgtvt dgqtgdtlpg vniqipsltm gaatnvdgnf
       61 tledvpagty tvqatfvgyq tfnqevavsa geettidiem qpdvvgledv vvtafgierd
      121 qralgygvse vasedlesrn qsdvgralsg qlpgvsisss ggvtgsgtdi nirgyssisg
      181 snqplfivdg vrfdggnnas sswadgggqq tnphrlldip psnikdvsvl kglsatvlyg
      241 edgrngviii ktksgsfged qepgfnvtln qsvyatqiss rpdyqdeygg gfdqnfgwfy
      301 snwgprfdtd npnlfgsdfr gfaddgtvli dhpltqhgat aqafpdlqna dyryeakpdp
      361 mgsffrdgla stssigingg tqdlrlnlny srneeqgftp nnklnrntfs igaeysvfsd
      421 ltaqttfnms ltdvqspata agggsgpaaa ggstsvfgdv fytprsidls ipyqnpqtgg
      481 sayyrsdnai phprwtannv ittnktdryy gktelnwqam drlnvvytmg ydsytesqay
      541 mqnaggirpe plnsgfyqti diarstwdht lnaqfdyqlt edftldgtvg gqyttesyqr
      601 qgvesqnqli fdffehsnft dqsstnfftg adfqrqenvq tagiygdfrl gyqdfvylnl
      661 sgrndwfstl epennsifyp svnlsyilsd hidinsdait fvklfggvat sagspdpyst
      721 rttlatdars fvnndgtvit tnatsnflgn qdlkpelhte yeagvdlrff enrlglqasa
      781 ytrsttdlit qapidpstgy sstfvnvgei enqgleltin akpitggefq wdvksnfyts
      841 rsevvslgag ldriqvgggf ttrgnfaieg epfqvmygtk ivrvteemkq ndpnfsdvev
      901 gtpiinsvgs yqeqddigki gnpnpdwels lsntfrykga slsfqmdyqq ggdmfstwis
      961 tllarglttt ttkvdrnntf ilpgvneqgq pnnvqispss vffdnfgfgt demrvydmth
     1021 irltnvrlgy dlpasvlest pfsqvtisvt gdnlwmyafn vpeasgfdpn vnsiggnsrg
     1081 feyltgpaar rfggsvtlrf
//
LOCUS       WP_095609856             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tamilnaduibacter salinus].
ACCESSION   WP_095609856
VERSION     WP_095609856.1
KEYWORDS    RefSeq.
SOURCE      Tamilnaduibacter salinus
  ORGANISM  Tamilnaduibacter salinus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Tamilnaduibacter.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Tamilnaduibacter salinus"
                     /db_xref="taxon:1484056"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41312
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligiprett pgenrvaiip sgipelleag feviiesgag taahfaddey rnngaiiadd
       61 aaslyrqasv vlkvrtpsed eaaqmrpdtt litimdpwfh qdrvrqlaer gvrtfaldfv
      121 prttraqsmd vlsamggitg yravlsgams lpryfpmlmt aagtihparv fvigagvagl
      181 maiatarrlg avveaydlrp evreqveslg adfveidvpd adngdggyag eqsdafydaq
      241 rqqlsdcvar adlvittaai pgrqaptlvt remihrmkrg svivdlaaer ggnvegtvln
      301 gktevdgvtl vghvdhpsrv pvhasqlltr nmvafiknmt edgqlapsde ddivcatrit
      361 dqgaithggl reaiaptttq qpeeata
//
LOCUS       WP_095620220             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            salipaludis].
ACCESSION   WP_095620220
VERSION     WP_095620220.1
KEYWORDS    RefSeq.
SOURCE      Halomonas salipaludis
  ORGANISM  Halomonas salipaludis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas salipaludis"
                     /db_xref="taxon:2032625"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55347
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapketf agearvaltp esaghihklg heclvergag laagfddday reagvtlvds
       61 aealwreaev vikvrepsra eadllregqt lisffwpaqq eallercras gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv liigagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfdd sadgsesggy akpsspefre
      241 kqlalfreqa pevdivitta lipgqpapkl wladmvaamk pgsviidlaa ekggncdltq
      301 pdqrvvsdng vvvvgytdfp srmatqasll yatnvrhmlt dltpekdgai vhdmeddvir
      361 gatvahqgev tfpppppkvk aiaaakpkpk ekaptpeekk aaelatfkaq tkrqltllga
      421 ggalmlllgq iapasfmqhl ivfvlacfvg fqviwnvshs lhtplmavtn aisgiiilga
      481 vlqigsgnwv vvllaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_095632670             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_095632670
VERSION     WP_095632670.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38563
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay aaagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag avaadasaly arnlldflkl vfnkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095639281             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            salipaludis].
ACCESSION   WP_095639281
VERSION     WP_095639281.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus salipaludis
  ORGANISM  Paracoccus salipaludis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Paracoccus salipaludis"
                     /db_xref="taxon:2032623"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55705
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigglketf dgearvavtp ssaghlqklg hevhvetgag aragfsdaay eragvtvhpn
       61 aaalteavdv vvkvrpptde elarmregqt lisffypgqn aellerardl gvnaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaatslg aqvyafdvrp evaeqiesmg aefvfldfqd sqdgaetggy akpsspefla
      241 kqlekfrela pemdivitta lipgrpapkl wtedmvrmmk pgsvivdlaa erggncdltv
      301 pdarivteng vtiigytdfp srmgaqasel ygnnirhmla dltpakdgtl vhdmeddvir
      361 gatvtrdhdv twpppppkvq aiaaakpkpk vkeptpeerr aaealafrrq trsqigmlvt
      421 ggvlmllvgl fapasflqhf ivfvlsvfig fqviwnvshs lhtplmaitn aissivilga
      481 llqigsgsal ivilaalavl mtavnifggf lvtrrmlamf qks
//
LOCUS       WP_095667887             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_095667887
VERSION     WP_095667887.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38718
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 sdafgaelil kvvapsdael alikrgavlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095670690             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila lacus].
ACCESSION   WP_095670690
VERSION     WP_095670690.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila lacus
  ORGANISM  Candidatus Planktophila lacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Candidatus Planktophila lacus"
                     /db_xref="taxon:1884913"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38681
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvavplevk agekrvalvp diinkltrlg yevviqsgag dnsqgtdaay aaagasvvkg
       61 dvlagadvvl svqpltpaqm atlksgaiti sflstvtavd sidaaikagv tafslelvpr
      121 israqsmdal tsqalcagyr avlvgaemsp rffpllmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlgav vsaydvrpss adevksmgat fiqlelesle gaggyaremt eeraakqrel
      241 ltpyiakshv vittaavpgr taprlmtqam idamepgtvi vdlaaetggn vegskpgevv
      301 vtsggvriwg gkdvpsqlpf hasslysrnv vnlltlmttg tkdgapvaln ldfadeiina
      361 savthggqrr dpsaggak
//
LOCUS       WP_095673119             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila sulfonica].
ACCESSION   WP_095673119
VERSION     WP_095673119.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila sulfonica
  ORGANISM  Candidatus Planktophila sulfonica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Candidatus Planktophila sulfonica"
                     /db_xref="taxon:1884904"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39125
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvavpreir dgekrvalvp dvinkltrlg yevviesgag vhsqatddlf taagatvksg
       61 nvisdadvvl svtsltpaqm gslkkgavti sflspvtavd sidaatsagv tafslelvpr
      121 israqsmdal tsqalcagyr aalvgaelsp rffpmlmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlggv vsaydvrpss adevksmgat finleleale gaggyaremt eeraakqrel
      241 ltpyiakshv vittaavpgr taprlmtaqm vdamdagtii vdlaaetggn vegskpgeiv
      301 vtakgvqiwg gkdvpsqlpf hasslysrnv vnlltlmttp skdgapvaln idftdeiidk
      361 satthggakh tpgasekgga n
//
LOCUS       WP_095674395             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila versatilis].
ACCESSION   WP_095674395
VERSION     WP_095674395.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila versatilis
  ORGANISM  Candidatus Planktophila versatilis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Candidatus Planktophila versatilis"
                     /db_xref="taxon:1884905"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39176
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvavpreir dgekrvalvp diinkltklg yevviesgag vhaqatdelf iaagatiksg
       61 nvigdadvvl cvtsltpaqi sslkkgavti sflspvtaid sidaavtagv tafslelvpr
      121 israqsmdal tsqalcagyr aalvgaelsp rffpmlmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlgav vsaydvrpss adevksmgat fidleleale gaggyaremt eeraakqrel
      241 ltpyiakshl vittaavpgr aaprlmtaam idameagtii vdlaaetggn aegskpgeiv
      301 ttakgvqiwg gkdvpsqlpf hasslysrnv vnlltlmtta akdgekvaln idftdeiidk
      361 aalthagakh tpgasekggs n
//
LOCUS       WP_095675754             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila dulcis].
ACCESSION   WP_095675754
VERSION     WP_095675754.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila dulcis
  ORGANISM  Candidatus Planktophila dulcis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Candidatus Planktophila dulcis"
                     /db_xref="taxon:1884914"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39155
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpreir dgekrvalvp dvinkltrlg yevvieagag vhsqatddly taagatvksg
       61 nvisdadvvl svtsltpaqm gslkkgavti sflspvtgtd sidaaasagv tafslelvpr
      121 israqsmdal tsqalcagyr aalvgaelsp rffpmlmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlggv vsaydvrpss adevksmgat finleleale gaggyaremt eeraakqrel
      241 ltpyiakshl vittaavpgr taprlmtaqm vdameagtii vdlaaetggn vegskpgeiv
      301 vtakgvqiwg gkdvpsqlpf hasslysrnv vnlltlmttp skdgapvsln idftdeiidk
      361 satthggakh tpgasekgga k
//
LOCUS       WP_095677072             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila lacus].
ACCESSION   WP_095677072
VERSION     WP_095677072.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila lacus
  ORGANISM  Candidatus Planktophila lacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Candidatus Planktophila lacus"
                     /db_xref="taxon:1884913"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38797
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvavplevk agekrvalvp diinkltrlg yevviqsgag dnsqgtdaay aaagasvvkd
       61 dvlagadvvl svqpltpaqm atlksgaiti sflstvtavd sidaaikagv tafslelvpr
      121 israqsmdal tsqalcagyr avlvgaemsp rffpllmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlgav vsaydvrpss adevksmgat fiqlelesle gaggyaremt eeraakqrel
      241 ltpyiakshv vittaavpgr taprlmtqam idamepgtvi vdlaaetggn vegskpgevv
      301 vtsggvriwg gkdvpsqlpf hasslysrnv vnlltlmttg tkddapvaln ldfadeiina
      361 savthggqrr dpsaggak
//
LOCUS       WP_095677991             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium sp. CCBAU 05631].
ACCESSION   WP_095677991
VERSION     WP_095677991.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium sp. CCBAU 05631
  ORGANISM  Sinorhizobium sp. CCBAU 05631
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium sp. CCBAU 05631"
                     /db_xref="taxon:794846"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39334
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msqivfiake sdsdeprvag svesvkklks lgfdvvveag agsrsrvpde efekagarig
       61 saadagsadv ilkvrrptae eiggyksgai vigimdpygn daaiaamaea gltafamelm
      121 pritraqsmd vlssqanlag yqavvdaahe ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg amvsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskdyqa
      241 kqaalvaehi akqdivvtta lipgrpaprl vtrqmldsmk pgsvvvdlav erggnvegae
      301 agrvveiggv kvvghlnvpg riaasaslly aknlvtflet mvskeekala vdmedelvka
      361 talthggavv hpafggangg dk
//
LOCUS       WP_095681021             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Nanopelagicus limnae].
ACCESSION   WP_095681021
VERSION     WP_095681021.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Nanopelagicus limnae
  ORGANISM  Candidatus Nanopelagicus limnae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Nanopelagicus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Candidatus Nanopelagicus limnae"
                     /db_xref="taxon:1884634"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38614
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpketk agelrvalvp diiskltkag levviesnag laaeysdkqf sdagaevksg
       61 dvlaasdvvl svqpltanqm ktlkkgsiti sflspstsqd sidaavsagv taislemvpr
      121 israqsmdal tsqalcagyk aslvaaelsp kffpllmtaa gtvtpakvvv lgagvaglqa
      181 iatakrlgav vsaydvrpas adevksmgak finleleale gaggyaremt eerankqrel
      241 ltpyiasadv littaavpgr taprlvtaqm vsqmipgsvv vdlasetggn vegsvagevi
      301 ttsggvkiwg gkdvpsqlaf hasmlfsrnv vnllllmtkt idgkptgdie pdfsdeiids
      361 atlthngarr ekgk
//
LOCUS       WP_095681645             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. CLI2509].
ACCESSION   WP_095681645
VERSION     WP_095681645.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. CLI2509
  ORGANISM  Streptomyces sp. CLI2509
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces sp. CLI2509"
                     /db_xref="taxon:1984801"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51247
     Region          1..504
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvvredv agetrvaatp esvarlrelg yevvvepgag ehagfpdaay aeagartgaa
       61 rgadvvlavr tppldglrag atlvglldpa heperlaela rrgitalame avprisraqs
      121 ldvlsstani agyravveaa halgrlfggq vtaagktppa tvlvagagva glaaigtaga
      181 lgavvratdp rpevaeqvrs lggeylpvap ageegagtgy aremgaeyra reaelyarec
      241 agadvvitta lvpgrpaprl ltagtvaamk pgsvivdmaa asggnvagtv pgervvtpgg
      301 vvilgytdla grlpgqasrl yannlvallt lltpdrdgtl vldtddivqh siavvragev
      361 hwppppvpvs atpappaeae rtapaeaapa ppprrgrrya laalaaalll lggatappaf
      421 lghltvfala vvigfymign vhhalhtplm svtnaisgiv vvgallqigh gdtavtvlaa
      481 laillacvni fggfavtrrm lgmffgsgs
//
LOCUS       WP_095685461             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila vernalis].
ACCESSION   WP_095685461
VERSION     WP_095685461.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila vernalis
  ORGANISM  Candidatus Planktophila vernalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Candidatus Planktophila vernalis"
                     /db_xref="taxon:1884907"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38640
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvvvpkeik dgekrvalvp dvinkltrlg fdvviesgag vhsqavdaey kaagatisdg
       61 evlstadavl svqpltpaqm gklkkgaiti sflspvtavd sidaaasagv tafslelvpr
      121 israqsmdal tsqalcagyr avlvgaelsp rffpmlmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlgav vsaydvrpas adevrsmgat fielelesle gsggyaremt edraakqrdl
      241 ltpyiakshi vittaavpgr qaprlmtqam vdsmgpgtvi vdlaaetggn vegskpgeiv
      301 itsggvkiwg gkdvpshlpf hasflysrnv vnlltlmtta akegeavafn lnfedeiing
      361 salthagsrr gdk
//
LOCUS       WP_095688460             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Nanopelagicus abundans].
ACCESSION   WP_095688460
VERSION     WP_095688460.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Nanopelagicus abundans
  ORGANISM  Candidatus Nanopelagicus abundans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Nanopelagicus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Candidatus Nanopelagicus abundans"
                     /db_xref="taxon:1884916"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38524
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpreik sgekrvalvp diiskltkag levviesgag vaaqysdkqf sdagaqvkst
       61 dviadadvvl svqplnpaqm kalkkgaiti sflsptgsad sieaaisagv taislemvpr
      121 israqsmdal tsqalcagyk aslvaaelsp kffpllmtaa gtitpakvvv lgagvaglqa
      181 iatakrlgav vsaydvrpas adevksmgak fitleleale gaggyaremt eerankqrel
      241 ltpyisaadv littaavpgr taprlvtaam ishmapgsvv vdlaaesggn vegsvageii
      301 ttsagvriwg akdvpsqlaf hasmlfsrnv vnllllmtks vdgkptgvie pdfsdeiids
      361 atlthnglkr ekgk
//
LOCUS       WP_095688854             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila lacus].
ACCESSION   WP_095688854
VERSION     WP_095688854.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila lacus
  ORGANISM  Candidatus Planktophila lacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Candidatus Planktophila lacus"
                     /db_xref="taxon:1884913"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38782
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvavplevk tgekrvalvp diinkltrlg yevviqsgag dnsqgtdaay aaagasvvkg
       61 dvlagadvvl svqpltpaqm atlksgavti sflsnvtavd sieaaikagv tafslelvpr
      121 israqsmdal tsqalcagyr avlvgaemsp rffpllmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlgav vsaydvrpss adevksmgat fiqlelesle gaggyaremt eeraakqrel
      241 ltpyiakshv vittaavpgr taprlmtqam idamepgtvi vdlaaetggn vegskpgevv
      301 vtsggvriwg gkdvpsqlpf hasslysrnv vnlltlmttg tkddapvaln ldfadeiina
      361 savthggqrr dpsaggak
//
LOCUS       WP_095692147             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila dulcis].
ACCESSION   WP_095692147
VERSION     WP_095692147.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila dulcis
  ORGANISM  Candidatus Planktophila dulcis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Candidatus Planktophila dulcis"
                     /db_xref="taxon:1884914"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39208
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpreir dgekrvalvp dvinkltrlg yevvieagag vhsqatddly taagakvksg
       61 nvisdadvvl svtsltpaqm gslkkgavti sflspvtgtd sidaaasagv tafslelvpr
      121 israqsmdal tsqalcagyr aalvgaelsp rffpmlmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlggv vsaydvrpss adevksmgat finleleale gaggyaremt eeraakqrel
      241 ltpyiakshl vittaavpgr taprlmtaqm vdameagtii vdlaaetggn vegskpgeiv
      301 vtakgvqiwg gkdvpsqlpf hasslysrnv vnlltlmttp skdgapvsln idftdeiidk
      361 sattyggakh tpgasekgga k
//
LOCUS       WP_095693312             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila versatilis].
ACCESSION   WP_095693312
VERSION     WP_095693312.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila versatilis
  ORGANISM  Candidatus Planktophila versatilis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Candidatus Planktophila versatilis"
                     /db_xref="taxon:1884905"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39192
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvavpreir dgekrvalvp diinkltklg yevviesgag vhaqatdelf iaagatiksg
       61 nvisdadvvl cvtsltpaqi sslkkgavti sflspvtaid sidaavtagv tafslelvpr
      121 israqsmdal tsqalcagyr aalvgaelsp rffpmlmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlgav vsaydvrpss adevksmgat fidleleale gaggyaremt eeraakqrel
      241 ltpyiakshl vittaavpgr aaprlmtaam idameagtii vdlaaetggn aegskpgeiv
      301 ttakgvqiwg gkdvpsqlpf hasslysrnv vnlltlmtsa akdgekvaln idftdeiidk
      361 aalthagakh tpgasekggs n
//
LOCUS       WP_095694272             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium sojae].
ACCESSION   WP_095694272
VERSION     WP_095694272.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium sojae (Ensifer sojae)
  ORGANISM  Sinorhizobium sojae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium sojae"
                     /db_xref="taxon:716925"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39858
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfiake sdpneprvag spetvkkirs fgfevvveag aglssripda eyekagarig
       61 takdaksadv vlkvrrptva eikgykagal viaimdphgn eeaiagmaka gltafamelm
      121 pritraqsmd vlssqanlag yqavidaahe ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg amvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemskeyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vtremlksmk pgsvvidlav erggnvegae
      301 agtvaevegv kvvghlnvpg riaasaslly aknlvtflet lvskeekrla lnmedelvka
      361 talshggtvv hpafdgakeg nk
//
LOCUS       WP_095694402             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium sojae].
ACCESSION   WP_095694402
VERSION     WP_095694402.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium sojae (Ensifer sojae)
  ORGANISM  Sinorhizobium sojae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium sojae"
                     /db_xref="taxon:716925"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39884
     Region          3..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnvtvyiare nspdeprvag spetvkkirs fgfevvveag aglssripda eyekagarig
       61 takdarnadv vlkvrrptva eikgykagal viaimdphgn eeaiagmaka gltafamelm
      121 pritraqsmd vlssqanlag yqavidaahe ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg amvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemskeyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vtremlksmk pgsvvidlav erggnvegae
      301 agtvaevegv kvvghlnvpg riaasaslly aknlvtflet lvskeekrla lnmedelvka
      361 talshggtvv hpafggakeg nk
//
LOCUS       WP_095695977             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila dulcis].
ACCESSION   WP_095695977
VERSION     WP_095695977.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila dulcis
  ORGANISM  Candidatus Planktophila dulcis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Candidatus Planktophila dulcis"
                     /db_xref="taxon:1884914"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39155
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpreir dgekrvalvp dvinkltrlg yevvieagag vhsqatddly taagatvksg
       61 nvisdadvvl svtsltpaqm gslkkgavti sflspvtgtd sidaagsagv tafslelvpr
      121 israqsmdal tsqalcagyr aalvgaelsp rffpmlmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlggv vsaydvrpss adevksmgat finleleale gaggyaremt eeraakqrel
      241 ltpyiakshl vittaavpgr taprlmtaqm vdameagtii vdlaaetggn vegskpgeiv
      301 itakgvqiwg gkdvpsqlpf hasslysrnv vnlltlmttp skdgapvsln idftdeiidk
      361 satthggakh tpgasekgga k
//
LOCUS       WP_095696744             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila versatilis].
ACCESSION   WP_095696744
VERSION     WP_095696744.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila versatilis
  ORGANISM  Candidatus Planktophila versatilis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Candidatus Planktophila versatilis"
                     /db_xref="taxon:1884905"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39162
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvavpreir dgekrvalvp diinkltklg yevviesgag vhaqatdelf iaagatiksg
       61 nvigdadvvl cvtsltpaqi sslkkgavti sflspvsaid sidaavtagv tafslelvpr
      121 israqsmdal tsqalcagyr aalvgaelsp rffpmlmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlgav vsaydvrpss adevksmgat fidleleale gaggyaremt eeraakqrel
      241 ltpyiakshl vittaavpgr aaprlmtaam idameagtii vdlaaetggn aegskpgeiv
      301 ttakgvqiwg gkdvpsqlpf hasslysrnv vnlltlmtta akdgekvaln idftdeiidk
      361 aalthagakh tpgasekggs n
//
LOCUS       WP_095698456             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Planktophila limnetica].
ACCESSION   WP_095698456
VERSION     WP_095698456.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Planktophila limnetica
  ORGANISM  Candidatus Planktophila limnetica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Candidatus
            Nanopelagicales; Candidatus Nanopelagicaceae; Candidatus
            Planktophila.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Candidatus Planktophila limnetica"
                     /db_xref="taxon:573600"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38587
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpkeir dgekrvalvp diinkltrlg yevsiesgag nhsqamdedf ksagasivng
       61 dvlkgadvvl svspltpaqm sslkkgalti sflspvtavd sidaaasagv tafslelvpr
      121 israqsmdal tsqalcagyr avlvgaemsp rffpllmtaa gtvtpaqvlv lgagvaglqa
      181 iatarrlgav vsaydvrpss adevksmgat fidleleale gaggyaremt peraakqrel
      241 ltpyiakshv vittaavpgr kapqlmtqam vdamgpgtii vdlaaetggn vegskpgevv
      301 vtkngvriwg gkdvpsqlpf hasslysrnv vnlltllttp aaegsalaln ldfddeiidg
      361 aavthagakr dggak
//
LOCUS       WP_095702331            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. MD40].
ACCESSION   WP_095702331
VERSION     WP_095702331.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. MD40
  ORGANISM  Mucilaginibacter sp. MD40
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Mucilaginibacter sp. MD40"
                     /db_xref="taxon:2029590"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116030
     Region          22..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrlllltfl lfnaaivaaq nrtvtgtvta aadkgilpgv svrvkeaqag tvtdangkyt
       61 isvpangatl vfsfvgfasq evpingrsti nvalgessqq lgevivtalg isrqekslgy
      121 aaqqikgenl tmtrqpdfnt alagkvagvq llggsgakfg astirirgin slqggnpiyv
      181 vngvvtdpna innddveslt vlkgpaatal ygqrasegav vitlkkgskk gigvtvnqtt
      241 tlervytlpk yqneygggts qdwnvynyqa gdpeylkgfn gikyydysvd eswgpkmdgt
      301 lyapwyfwdp snpgfgklkp fvaqpnnird fyqtgvttnn nvsfskggdd yntrisytnl
      361 nrtgvspntk qrrnnlsfng dvkltskltv saninvfqen lknvpaegyg tqtsgsfnqw
      421 fhrdiemnql knyrrpdgty ttwnitaptd ltpkfwdnpy teayvntaea nnnrlygnvt
      481 asynirkdlk fsiiargdyl nrdansrvgs ytinpdayne dsyqykeyny vasleydhmf
      541 gkdlsfraga faesredvtk ylssgtnggl svpelytvgn sldrpsttsi hstkvvnsay
      601 gytsfgykqf lyldlnirnd vssalptnhn sywyggasgs fvftesglip kndvltfgkl
      661 rasvakvgsd lppyqifqty tlsttpygss pvqfvpntlp nanlkptlst syelgtelhf
      721 lkgdrirfdf nyyhrntkdq ilnlpvngnt gysavainag siinrgieis lggtpvktsd
      781 itydlnfnia fnrnkvaaly pgfntlrtsp eggggstisg yqaagstgfg fvgspsfsvn
      841 svvgqpygql igsgflrdas gnvivdadgy perndnvnlg nilpkftggf tnnfnykgin
      901 fgfsidyqyg gkfvsvtqqn lagsglalst vgnnengvpr rndpsvgggs lvkgvhedgt
      961 pnttyvdtrt lneqyysqiw eqytydatyi klrevsigyn lpkswfgrip lqsarfsiva
     1021 qnpwliytka rvkgidpsql qtsfyeggql patrtigfnl nlnf
//
LOCUS       WP_095702747            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. MD40].
ACCESSION   WP_095702747
VERSION     WP_095702747.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. MD40
  ORGANISM  Mucilaginibacter sp. MD40
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Mucilaginibacter sp. MD40"
                     /db_xref="taxon:2029590"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114749
     Region          26..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkiykflla iwlpvlffqt anaqgikvsg tvtaqsdgqp lpgvsvavqg gntgtqtdvq
       61 grftltakvn dvlqisylgf vtqritvset qaplkivfve apnslnevvv talninkdkk
      121 slgysvqglk skdiseaket nlvnalagki agvqvtnsqg dmgssrivir getsisgnnq
      181 plfvvdgviv dnsqflgtng srdfqnaisd lntediesis vlkgpnaaal ygyraaagvi
      241 liktktgkga kglgitinsn tsfatlkvfp dyqnsygqgs ngrfsyvdgk gggindgvde
      301 swgprldgrl ipqfysngqa vpfvahpnnv rdffrtgvtl nngvalagss ekfdyrisyn
      361 nlhqtgvvpn sslgrnsfll natfrptpkl tvttianyik ddagnlpgay grratstmlq
      421 ftwfgrqvdi nqlknyrnad gstfnwnnsy ysnpyfiaye ntvsqfknrl igsvelnyki
      481 ikglsanlrt gtdfyndrrk ikvaygtsgt pfgsyeeday yvnetntegr lqytkklnkd
      541 fsldafvggn istvtneqnd qiapklavag lytlsnsrdp lvssnyygkl ktysyfasaq
      601 igfrdyafln vtgrndwsst lpaanlsyfy psvngslvls qaldiksdal sylklrggws
      661 kvgkattpyq lintynftap fngnpqqsaa nidlnpnlkp etttsgeagf eagffkdrvc
      721 ldvsvyntns tnqilsvdvs sstgytqkli nggrinnkgl eaqlsvtpvk ttnfswdvsv
      781 nyslnrskvv sldaegrlqs yvlgtnrtvq vlaavgkpyg tlfgtayqrd asgniiidns
      841 gvpvinpakq ylgkftpdfl ggitnsfnyk ginlsvlvda rfggsiysnt nrtgtytgvl
      901 astlpgrgae ngglsyyypa nntsasavqv atgasapnge tvyddgmvwk gvkadgtpnt
      961 kvipaqsyyk gftnvdeafv ysasyvklre vklgytfpas wvkgiglqsa tvsvvgrnlw
     1021 iihkkvpnid petafntgng qgledltlpt vrnigfnvnl kf
//
LOCUS       WP_095702942            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. MD40].
ACCESSION   WP_095702942
VERSION     WP_095702942.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. MD40
  ORGANISM  Mucilaginibacter sp. MD40
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Mucilaginibacter sp. MD40"
                     /db_xref="taxon:2029590"
     Protein         1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119949
     Region          29..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiylnlnr lvlliaaclf pvmlfaqski tgtvtdetkq plpgvsvmlk gssqgtttdv
       61 ygrfiinasp gqtlifkylg faeqeatvgt aknmiitlkg dnkalnevvv talgvkketr
      121 rvgysvqtvn geditlardp npitgltgkv aglsvgpsae llgapsvrlr gnaislyvvd
      181 gfpintdtyn ispddiesyt vlkgpaaaal ygnrasygai littkkgnkn kkgltvdvns
      241 stvindgfla fprvqhsfga gentyykfvd gkggapggvd gdydvwgpyf agqlieqyds
      301 pvingvrqat pytargannl knflrtgyqt nnnvalsang dnynirlsas qqhqssyipe
      361 qyldianani yasfspssrw kfegninfnr qttdnfpdvq ygpnsliyni avwtgadwdv
      421 napdikaiwq pgkvgvqsqf aeytryhnpw lmvkewtrgh yknnttgyls gnykinnnln
      481 vtlrsqidty dllrtekmpy sahpygregn mgdyredrrn lfdnntelmv nydytvakfl
      541 nlsgliggnm rnlsynsnwt stdylnvpgv ysfsnsmnpv qstsfrsdmr vlsayyslda
      601 slgkyatiss tgridkssaf qtpttyyyps vsvstvlsdy iqlpevisfl kgrasfsnir
      661 sdatattigp apfnsitvfd gstgaslytn plgygttyns pyngpsyaln tsfstskpyn
      721 sqtagfatdy lfqqgiktst rvnyeegfdi kffqnrlgls atafqyidgp qilanpista
      781 tgytveyvna lktkktgyeg slqgtpiknl ggfswnilan istfkdvyke lpagqgtynt
      841 ffkvgdrtdk lygsafvrtp dgqiindaag kplakpvaqy lgnmnakyaw svynklqykn
      901 fslgfqfdgs vggvivdymh nktmrggani etaegalgaa ryqdwanygk agytgsyvge
      961 gvqisnggvi nynsstgavi nyadlkyapn atktfvqdyv skyygvdean lmsktfsklr
     1021 evtlgfeipk qmlqktfiqk asvtvygrnl lyfykdkrfk dvdldqynya agltglqspt
     1081 vrsyglnlnv sf
//
LOCUS       WP_095703033            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. MD40].
ACCESSION   WP_095703033
VERSION     WP_095703033.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. MD40
  ORGANISM  Mucilaginibacter sp. MD40
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Mucilaginibacter sp. MD40"
                     /db_xref="taxon:2029590"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116184
     Region          24..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllvslc flslfvtqvy aqnrtitgtv vakddglpip gvtvkvkgtt igtqtspsgk
       61 yslsvpanst lvvsfigyna qeikvggssv vnvtlepsvn qigevlvtga lgikkakret
      121 afattnvsgk dinqtnvtnf angltakvag laiqtvdnsi dpnvtiklrg nrsiagnnna
      181 lividgipap ygainsinpd diaetqilkg agaaaiygse asngavlitt krgasngkpv
      241 isynnsfqlq qvgffpkfqn tygmyggegd pyidpltgga lyvpyenqly gpaydptgnt
      301 kvqvgypags atgptlvvpy kalkknpies ffntgiveqn evsvqqgdan nsfylsaqnv
      361 yskgvvpndk nlrtsvssrg artlgmfkad ysvsytktdv stygtgyngs ilytnlmqwp
      421 afldikqfrn snsgtfsnps dfydayainp ywivdnsryn tsrdvflsnl klsltptkwm
      481 dlayhvsynf ginqrrftrk qvtftpygvs dpygassvqa sfkntllapg qvedvyqfgd
      541 gtlngypggy arlqgdatvn lhhtffndfk tslllgntvw qqryktqtts snsllvpdvy
      601 nvafiggipt aseseskirq iaffadlnig yknyaffegt lrndrdsrlp sknrsfyyps
      661 gklsfvptda fsfmkdnkvl nylklygsls rvgnisigsy qinniygvts gfpygslggl
      721 sagttnyspd lkpeqiteie tgfeaalfns rlnvnatyyk qnsknqtlrv qtsaatgynf
      781 sllnvgevqs sgfefeangd iltkaannfg wrlggnfsin dskvislipg vntfdvltfg
      841 tasvsakvgq pfpllrgtdl nrdpqgrviv daktglpstn qapidfgrtt pkyilgvtsa
      901 wsykfvtlna vaeyrggyvi ynqvgstmnf ggssyvsasa grsrfifpns vintgtaanp
      961 vytpntsvsi qdgnygfwqs spyntanspl vssaafwklr evslnfdlsq fikrtgfikg
     1021 lnfaltgrnl alwkpksnpw tdpefadtsg ngvgttsaaq tpatriygad lkvtf
//
LOCUS       WP_095704604             751 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. MD40].
ACCESSION   WP_095704604
VERSION     WP_095704604.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. MD40
  ORGANISM  Mucilaginibacter sp. MD40
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 751)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Mucilaginibacter sp. MD40"
                     /db_xref="taxon:2029590"
     Protein         1..751
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=79973
     Region          62..>736
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfikhpkgv vnkyglstrk svlvmnltla ltvpvtlqsv asafpltkat vdinklvnfa
       61 aikgkvlden gaplpgvsvs vkgtsggtvt dasgnfsvna pdnatlvfsf igyqtqevav
      121 agrttinikm lpaakglnev vvtalgitke qkklgysvst vngdalnkak etnvvlslqg
      181 rvaglsvgas nggpgssarv llrgltsfta ggplyvingv pmdntqrgas gewggadygd
      241 gisninpddi esmtvlkgqs asalygtraa ngvilittks gkknsafgve fntniqfdkp
      301 vdntdfqqvy gqgilnaagv aakptslnea rnsgslawgt kmdgsmvpqi dgkdhpyspv
      361 snyidfyrta psftntaifs gggkesafrl slsdlransm vpnsyldrkt fnfngsqqvt
      421 pklnvnvvan yvlensknra glsdgpgnpn nvqflapnqd qatlapgvtp dgkeltftdd
      481 syvtnpyfaa ynfqkntqrn rlisalsaky dftnwlylqg rvgydvsndk rvdieptgtg
      541 yrgdngtmrq anaqitefnt dvllnakhsl vkdllnvdfs lggnirksna dgtfiegqgg
      601 fiipyfyslt nfgsrnsgpn tdiitskqvn sayysadfsi kdylvisttg rydyyssiak
      661 svgpgifsps vsgsflfsel hkmdgvdlgk vrlsfaqtsa dapayansvy ynlnnsingv
      721 ptagfssqlp nlflkpytlk eveangyikm l
//
LOCUS       WP_095705342            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. MD40].
ACCESSION   WP_095705342
VERSION     WP_095705342.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. MD40
  ORGANISM  Mucilaginibacter sp. MD40
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Mucilaginibacter sp. MD40"
                     /db_xref="taxon:2029590"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118717
     Region          25..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktiliivl avlclnfral aqstipikgr itdsidnkpl hgatvkikst sfststdeng
       61 nftinseksq gllivsfmgy ktveinfsqs digpfniala kdqstlkevs ivstgyqtip
      121 keratgsfti vnkdlynqqv tqdvlsrley iangvsvfrn sstktsqlmv rglstingpt
      181 aplivvdnfp ydgnitninp ndvasitilk daaaasiwgt ragngvivit tkkgtynqpl
      241 nieinsniti gekpdlnylt pmtssdyidf eknmynngyy kskisstsyp vlspviqllv
      301 ketngtissn qatdqinslr gldvrndfkk yiyqnlfnqq hyvninggnp dvkylfssgy
      361 dkdisnlsan ydklnlrsev afrpinnlqv ttgliytlsn nktgkpaygs inplapyqml
      421 adgngnalpi aqtysqlakd naastgrfld wnyypltdyq hnftavntqd ilgnfgaqyr
      481 ifkglnvdvk yqyekqqlks ntlydaqsyf arnlvntftq ltgtsvknvi pkggildqqn
      541 aaltsndlrg qinydrswdk nsitflagee lrqiennssi frsygynndi lsstgvdytn
      601 sypnyitkrn atipynnkys etlnrfvsfy angaytyadk ygisgsirrd asnvfgvetn
      661 dkwtplwssg lswnlskenf ynlsalpylk lratygysgn vdpsksavtt isyysansiy
      721 tnspysdvsn fynpdlrwek vrtfnvgldf kskndrisgs idyykknatd lyatvpldyt
      781 vglniatitk nvasmqgrgf dieinsvnln gpvkwltsln inyykdkvin yylssssgsy
      841 yvadyqnpvq gnpvwgvysy kwagldangn pqgylngkis edyasitgsg tkvsdlvyng
      901 prfpvfygsl gntlsfkgis ltarmtyefg nyfrrqsiny stlastgvgn adyakrwqnp
      961 gdenktnvps siyplvgard dfyngseilv dkgdcirlqy itvsynldkk qvywlpfkai
     1021 qlyinannlg ilwranhdgi dpdytytnsv mptpkniaig lranl
//
LOCUS       WP_095705574             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter sp. MD40].
ACCESSION   WP_095705574
VERSION     WP_095705574.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter sp. MD40
  ORGANISM  Mucilaginibacter sp. MD40
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Mucilaginibacter sp. MD40"
                     /db_xref="taxon:2029590"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108729
     Region          30..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktilfivl aalcfffnas aqinsrppni kitgkvtdeq glplpgatvk iqnessisit
       61 dkdgkftltn tpkngvitvs figfqttnip iplnldnefi iqlkadansl nevqvigygt
      121 ttkrlntgsv stitatdiek qpvtnilsal sgkaagvnvq stnglpggdv siqirgkgsl
      181 tagtnplyii dgvpfastsl vyntalaagi ngaisplnsl npndienisi lkdadataiy
      241 gsrgangvvl ittkkgksgk vktdinlyqg isqvanlpkl lnlqdyltir keafkndgli
      301 pssdptspsy apdltvwdpn kstdwakyil ggtghvtnfq anvsggseqt tfalgtnyrt
      361 etsvlpgnnr ytrggihmnv qhissnrkfn vlmstsytqd nnklvnpaia lssnillppn
      421 fpiyyqngnf nflnginpta svqntsdiqt nniitnavvs ykilpglqik tsagmnylnm
      481 nqvmvnpksa qdpstspqsf tyfgnnstks fivepqinys lkknksnfdv llggtfqkte
      541 nkseiiyatn fnsesqlenl asaatlrpsn syidykyvsi fgrvtynwde kylinasvrr
      601 dgssrfgpgn qfgnfgavga awifsnegwi ksnlnwlsfg kirssygitg ndqiadyqyl
      661 stykasnyvy qnitgltpar iandnfhwes nkkfeigldi glagdrvllt inrfqnrsgs
      721 qlvnyaipfi tgfdsyqanl paliqnqgwe veistrniqk pnftwstnfn ittsknilks
      781 fpnlatssya nvyiigesis raygfrfaga dpqtgaslyq vktggtsssp afenfyytmg
      841 dtnpsyyggm nnaiayknfq ldlfaqfsrq slpgslippg slsnnfavas nrwqtpgnst
      901 nipkattgtd dyyytlssan ffnasyirlk nvslsytfpe swtkyrkidr lriyaqgeni
      961 atwwsnntal ydpesgasan vpplriitig fqitl
//
LOCUS       WP_095715856             311 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Citrobacter sp. TSA-1].
ACCESSION   WP_095715856
VERSION     WP_095715856.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter sp. TSA-1
  ORGANISM  Citrobacter sp. TSA-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Citrobacter sp. TSA-1"
                     /db_xref="taxon:184912"
     Protein         1..311
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36065
     Region          5..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifelfskr qkklrgetld vyqyteipnp frvqvihiik dtigeesiyn desrsvyksi
       61 hqvlckeygv fslgghhqnh sesifnyflk eddyekcldi ielsfrvids yvrnnqwkfk
      121 gseqnaadai eelnirfqes glgyqfesge lirvdsqfmh sdvvkpvlql lgnkqdyqgv
      181 ndeflsaheh yrhqrykecl ndclksfesl mkaihkkhsw qfndndtakk linsclannl
      241 vpeylqnqfs sirillesgt ptirnkeggh gqgaeitkvp ehlasytlhl taanllflak
      301 cedhyskrtm r
//
LOCUS       WP_095717805             527 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Dietzia
            natronolimnaea].
ACCESSION   WP_095717805
VERSION     WP_095717805.1
KEYWORDS    RefSeq.
SOURCE      Dietzia natronolimnaea
  ORGANISM  Dietzia natronolimnaea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Dietzia natronolimnaea"
                     /db_xref="taxon:161920"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53785
     Region          17..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mspqtevpdp vaapsvigvv aesgpserrv aatpatvgkl iglgyrvvve sgagtraefs
       61 daayadagad lvdgdtawss dvvmkvavpt etevarlrpg atlvgllapa qnerllsvla
      121 ergvtalamd avprisraqs mdvlssmani agyravieaa hhfgrfftgq vtaagkvppa
      181 kvlvagagva glaaigaass lgaivratdp rpevadqvks iggeylpvev pdeekvvstd
      241 gyakatseay draaaalysa qaadvdivit talipgraap rlltaadvas mkrgsvivdm
      301 aaaqggnveg svadevvvte ngvtiigytd lagrlpaqas qlygtnlvnl tklvtpdkdg
      361 rwaldlddvv qrgvtvardg evlwppppvq vsaapaaaaa epleppaekk klsprarlgl
      421 iatgmallll ltavapgdip rhitvfvlai vigyyvignv hhalhtplms vtnaisgviv
      481 vgallqigid ntvgqvlati ailvasinvf ggfavtrrml gmfskga
//
LOCUS       WP_095730947             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. UFLA03-84].
ACCESSION   WP_095730947
VERSION     WP_095730947.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. UFLA03-84
  ORGANISM  Bradyrhizobium sp. UFLA03-84
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bradyrhizobium sp. UFLA03-84"
                     /db_xref="taxon:418599"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39054
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvavsp dtikkfkalg aevavepgag iksglpdsel taagatvsad
       61 alkdadiiik vkrpeasels kykrgalvia imdpygneaa lktmadagva afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegakpge
      301 vvetdgikiv gytnvagrva asasslyarn lfsfietmvd kakkelavnw ddelvkatal
      361 tkdgavihpn fqpk
//
LOCUS       WP_095752929             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. SA15].
ACCESSION   WP_095752929
VERSION     WP_095752929.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. SA15
  ORGANISM  Streptomyces sp. SA15
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces sp. SA15"
                     /db_xref="taxon:934019"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52831
     Region          13..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msaeepahhp pqrlgvvaes vpgetrvaat patvrlllgl gyevvvdqga geasgfadqv
       61 yvdagaevge awdadvvlkv napsgsetar lregatvval lapaqkpell qaladagvta
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvkslggeyl panvaqeasa dgyakatsad
      241 ydraaaelyh eqakdvdivi ttalipgrpa prlltaedva vmkpgsvivd maaaqggnve
      301 gtvagravvt engvtiigyt dlasrlpaqa sqlfgtnvvn llklltpgkd gqlaidfddv
      361 vqravtvvrd gavtwppppv avsaapaaqp saapakpepg qpklspvgrf aliglgmlam
      421 fllvafapaq laanftvfal avvigyyvig kvhhalhtpl msvtnaisgi vvigallqig
      481 hesrivttls fvailltsvn ifggfavtrr mlsmfskg
//
LOCUS       WP_095757719             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces xinghaiensis].
ACCESSION   WP_095757719
VERSION     WP_095757719.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces xinghaiensis
  ORGANISM  Streptomyces xinghaiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces xinghaiensis"
                     /db_xref="taxon:1038928"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53767
     Region          4..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mvqrlgvvae satgetrvaa tpdtvrrlms lgfdvlvesg agqrsdfade lyaeagakig
       61 sredawrsdv vlkvdpptad eigrlrddat ligmigpalr pelvetltqr sitvlamdav
      121 prisraqsld vlssmaniag yravieaahr fgrfftgqvt aagkvppakv lvagagvagl
      181 aaigaakglg aivratdprp evadqvrsmg geflaveveq easadgyaka tsedydrraa
      241 eiyteqaaev divittalip grpaprlita ehvasmrpgs vivdmaaaqg gnvagsvage
      301 vvvtdngvti igytdlpgrl paqasqlygt nlvnllkllt pgkdgqivld fddvvqrsmt
      361 vvragektwp pppvqvsavp aprqpdaaar paagsaagag gkqpmprnrk laiggltafg
      421 lflltafaps qlagnftvfv laivigyyvi gsvhhalhtp lmsvtnaisg iivvgallqi
      481 ghgntvvtvl sfaavllasi nifggfavtr rmlgmfskd
//
LOCUS       WP_095769374             425 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. WSM4313].
ACCESSION   WP_095769374
VERSION     WP_095769374.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. WSM4313
  ORGANISM  Mesorhizobium sp. WSM4313
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Mesorhizobium sp. WSM4313"
                     /db_xref="taxon:2029412"
     Protein         1..425
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43754
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqivfipre idpneprvaa spetvkrlag lgfdvivekg aglgsripdq dftaaggaig
       61 taadakkadv vlkvrrptdg elkgykpgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fvmgvgvagl
      181 qaiatarrlg aivtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl isaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng ikivghlnvp grvaasasll yaknlyafle tmvdktaktl aikrddelvk
      361 atmltdagqv vhpnfakaaq eprvepaavp aktmvadasn papkktaakn paaakspssk
      421 skgta
//
LOCUS       WP_095776996             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. WSM3868].
ACCESSION   WP_095776996
VERSION     WP_095776996.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. WSM3868
  ORGANISM  Mesorhizobium sp. WSM3868
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. WSM3868"
                     /db_xref="taxon:2029405"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43544
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldanepriaa spetvkrlag lgfevivekg aglgsritdq efataggtig
       61 tagdaknadv vlkvrrptda elkgyksgaa viaimdpygn daalaamasa gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatktl aikrddelvk
      361 atmltdagqi vhpsfakaag qprtepaaip atvlvadaad kkpaprrraa akspspkpeg
      421 ta
//
LOCUS       WP_095771598             434 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_095771598
VERSION     WP_095771598.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..434
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44679
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivetg agtrsripde efakagavig
       61 kaadvakadv vlkvrrpdet elksyksgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaaki fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegak
      301 pgqvvttang vkivghlnvp grvaasasll yaknlfafle tlvdkttktl aikrddelvk
      361 atmltdggkv vhpafakadq qphvepaaip attmvadasa apkkpaprkt asskssssks
      421 sspkssspks kgta
//
LOCUS       WP_095782245             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. WSM3862].
ACCESSION   WP_095782245
VERSION     WP_095782245.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. WSM3862
  ORGANISM  Mesorhizobium sp. WSM3862
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. WSM3862"
                     /db_xref="taxon:632858"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43645
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsritdq efataggtig
       61 tsgdaknadv vlkvrrptda elkgyksgaa viaimdpygn dpalaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatkgl aikrddelvk
      361 atmltdagqi vhpsfakaae tprtepaaip atvlvadtad kkpvprkraa akspspkpeg
      421 ta
//
LOCUS       WP_095789452             434 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. WSM4312].
ACCESSION   WP_095789452
VERSION     WP_095789452.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. WSM4312
  ORGANISM  Mesorhizobium sp. WSM4312
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Mesorhizobium sp. WSM4312"
                     /db_xref="taxon:2029411"
     Protein         1..434
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44689
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivetg agtrsripde efakagavig
       61 kaadvakadv vlkvrrpdet elksyksgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaaki fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegak
      301 pgqvvttang vkivghlnvp grvaasasll yaknlfafle tlvdkttktl aikrddelvk
      361 atmltdggkv vhpafakadq qphvepaaip attmvadasa apkkpaprkt asskssspks
      421 sspkssspks kgta
//
LOCUS       WP_095792049             434 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_095792049
VERSION     WP_095792049.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..434
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44729
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivetg agtrsripde efakagavig
       61 kavdvakadv vlkvrrpdet elksyksgaa viaimdpygn daavaalaka gviafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaaki fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegak
      301 pgqvvttang vkivghlnvp grvaasasll yaknlfafle tlvdkttktl aikrddelvk
      361 atmltdggkv vhpafakadq qphvepaaip attmvadasa apkkpaprkt asskssspks
      421 sspkssspks kgta
//
LOCUS       WP_095799175             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. WSM3866].
ACCESSION   WP_095799175
VERSION     WP_095799175.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. WSM3866
  ORGANISM  Mesorhizobium sp. WSM3866
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. WSM3866"
                     /db_xref="taxon:422271"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43719
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrmag lgfevivekg aglrsritdq efataggtig
       61 tagdaknadv vlkvrrptda elkgyksgaa viaimdpygn daalaamasa gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkvtktl aikrddelvk
      361 atmltdagqi vhpsfakaag qprtepaaip atvlvaeaad kkpaprrraa akspspkpeg
      421 ta
//
LOCUS       WP_095810373             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. WSM3860].
ACCESSION   WP_095810373
VERSION     WP_095810373.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. WSM3860
  ORGANISM  Mesorhizobium sp. WSM3860
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. WSM3860"
                     /db_xref="taxon:2029403"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43534
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsritdq efaaagaaig
       61 kaadasnadv vlkvrrptda elkgyksgaa vigimdpygn daalaamasa gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl isaamvasmk pgsvivdlav erggnvegam
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatktl aikrddelvk
      361 atmltdagqv vhpnfakaae tprtepaaip atvlvadaad kkpaprkraa akspspkpeg
      421 ta
//
LOCUS       WP_095806757             420 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_095806757
VERSION     WP_095806757.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..420
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43396
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre vdpneprvaa spetvkrlvg lgfdvvvekg aglgsrivdq dfaavggtig
       61 taadakkadv vlkvrrptdg eltgyksgaa viaimdpygn daalaamara gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegae
      301 agkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatkel aikrddelvk
      361 atmltdggkv vhpnfarave aprtepaaip attivadase kpaarkttak ksaakpkgta
//
LOCUS       WP_095817604             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. WSM3859].
ACCESSION   WP_095817604
VERSION     WP_095817604.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. WSM3859
  ORGANISM  Mesorhizobium sp. WSM3859
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mesorhizobium sp. WSM3859"
                     /db_xref="taxon:2029402"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43109
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqivfipre ldpseprvaa spetvkrlag lgfdvivekg aglgsripdq dfaavgaaig
       61 ktadaskadv vlkvrrptda elkgyksgaa viaimdpygn daavaamara gisafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegam
      301 pgkvvtteng vkivghlnmp grvaasasll yaknlyafle tmvdkatkql aikrddelvk
      361 atmltdggkv vhpnfakaae eprtepaavp attmvaeaad akpaarkkaa akpkgta
//
LOCUS       WP_095828151             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. WSM3879].
ACCESSION   WP_095828151
VERSION     WP_095828151.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. WSM3879
  ORGANISM  Mesorhizobium sp. WSM3879
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. WSM3879"
                     /db_xref="taxon:2029406"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43561
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsritdq efataggtig
       61 tagdaknadv vlkvrrptda elkgyksgaa viaimdpygn daalaamasa gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatktl aikrddelvk
      361 atmltdagqv vhpsfakaae tprtepaaip atvlvadaad kkpvprkraa akspspkpeg
      421 ta
//
LOCUS       WP_095824350             422 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_095824350
VERSION     WP_095824350.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43527
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsritdq efaaaggtig
       61 tagdaknadv vlkvrrptda elkgyksgaa viaimdpygn daalaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatktl aikrddelvk
      361 atmltdagqv vhpsfakaag qprtepaaip atvlvadaad kkpaprrraa akspspkpeg
      421 ta
//
LOCUS       WP_095831189             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. WSM3864].
ACCESSION   WP_095831189
VERSION     WP_095831189.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. WSM3864
  ORGANISM  Mesorhizobium sp. WSM3864
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. WSM3864"
                     /db_xref="taxon:2029404"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43531
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsritdq efataggtig
       61 tagdaknadv vlkvrrptda elkgyksgaa viaimdpygn daalaamasa gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatktl aikrddelvk
      361 atmltdagqi vhpsfaeaag qprtepaaip atvlvadaad kkpaprrraa akspspkpeg
      421 ta
//
LOCUS       WP_095836145            1136 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095836145
VERSION     WP_095836145.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1136
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126904
     Region          123..1135
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkkllilrg vgialclnaa vsaptiaqdm martvrtapr styqmeevfs rleqlhkvkf
       61 nynshvlagk tiseqqmrrl eqadlqtavp amlqqigltc ewiygnyyav ksfntvqqqq
      121 qqftvkgtvt dgsngaplpg vtiavkgktk gtatdaegry tlqglqtndq lvftligykt
      181 vtqpvngage invvlqqdvs glsevvvtal giqkekkslg yavqevkgnt mtqarepnlv
      241 nsltgrvagl tirtstdlfq nagislrgak plividgipd qladmwkinp ddvesisvlk
      301 gqsasalygs igkdgaimit tkrgkgkels vefnsstmfq psyiripkvq svygsgnkgk
      361 yayvdgsggg tegsgwiwgp kldqrdpatp sgywetpqyn spidpatgkl vplpwlsrgk
      421 dnvhnffrtg mittnnlsit ksndkgsfra sashiyqkgv vpntdlnnss fslagnydlt
      481 drlradaris ynrqytnnyp etgygpsnyl ynlvlwtgad vdirdlrnyw lpgkeglqqr
      541 hynlswynnp yfqayeylrg yykdntfgsl sldykfnkdl sakfrtgvnt ygltttskep
      601 ysyirysdks rgnfstgsdq yfdivsdlil kyehtfsknf sihaeggmsn yyrnqkyqts
      661 stdglsipgl ytlsnstnpl qgtnaleerr tnsfygfvdm efygafylsv tgrndkistl
      721 pvannsffyp svagslvvse lvkmprwlny lklrgswaev sagrleldny tynylpaydr
      781 gvkwnnipsl tfgstimnpn lkpqttqswe tglelklfdn rlgfdvtyfr ardfnnivdv
      841 plseasgygs rrengheylr kgieivvngt pvktgnfrwd vsanfssyrr ylhaifggkd
      901 qlnkirvner mdriftsvye kdpqgnivyq sngfpktdpf srfignddpd wiygventfr
      961 lgdfslrflv dgriggliys stnqkmwwgg thpgtvnsfr ddanagkaty vgagvvvtgg
     1021 eikydgngnv vadtrtfakn ekavnyidym intsnsannn ynyysetflk lrevnltwqv
     1081 pskwigktff rsasvalvgr nlllfsklpn vdpdpgsdnl qtpsmrsmgf nvnlkf
//
LOCUS       WP_095836683            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            sp. MD30].
ACCESSION   WP_095836683
VERSION     WP_095836683.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga sp. MD30
  ORGANISM  Chitinophaga sp. MD30
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Chitinophaga sp. MD30"
                     /db_xref="taxon:2033437"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115754
     Region          23..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkglfllls alflvgqvla qsrtingrvt saddgqpvig atvivkgtst gavtnpdgay
       61 siklpdgsaa vlvfksvglk eleakvgnsn tlnvvmyldv tklneqvita nairrdkssl
      121 gyaaptvkae eitqgratsa lsaltgkvag vnitntagap gsssrivlrg gssvagsnqa
      181 livvdgipvd nssvtggpnn lssidfgnrg ndinpddies mtvlkgpaaa alygsrasng
      241 aviittksgk kgakkseitv nstatfsnil klpdfqneyg qgsdgdydpk enfswgpkfd
      301 gqtkpwgqei dgerltkpys aqknnirkff elgrafnnnv svsgggektt yflalsslns
      361 dgvmpgssdt ynkygirfng saelsnnfkt avsinynkin snmvqggqgp gsvynnllqt
      421 prdipidqmg dlnnkfysyg syvdkngilr nnrygyygay ttspyyilqn yknlndvdrv
      481 fgnftltydp lkwlnvverv gadvyadrrr fkypkfnlsp adetsgnysq vsnqrnqvgs
      541 yeennfnvse ivhdlmitak kdfgkdfhas lmvgnnirqr qttslnsatn atgglvvpew
      601 ynlansngpv nstnnytirr lvglyselnv dyksmlflgv sarndwsstl pkannsffyp
      661 svnasfvfse lfqgtsfanv lnfgkvrasw aqvgadadpy lltttfnrti iqsgfgnttf
      721 pfngvpgltl ggtignpdlk peittafevg telnfldnri svdfsyyenk sknqilaipi
      781 aeasgftskv vnagtiqnkg velalrgvpv rtsyglniev ygtytrnvnk vlslldgisq
      841 islgglttms vvaavgqpyg sffstdvqrd dqgrvivdpn sglplktssg vflgsynpky
      901 qaswgtnity kgwslnvlfd tkqggkffsr tknitafngt saitggnrdp qifpnsvykd
      961 asgkivvntd knfspqayyn alpdgqnvvd asyvklreas lsyrlpkhtl nrtpfgditv
     1021 gifgnnlflw aakenkfadp evnsagagnl qgfdftaqps lrnfgvnvkv sf
//
LOCUS       WP_095837284            1254 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            pendula].
ACCESSION   WP_095837284
VERSION     WP_095837284.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga pendula
  ORGANISM  Chitinophaga pendula
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1254)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1254)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1254)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1254
                     /organism="Chitinophaga pendula"
                     /db_xref="taxon:2849666"
     Protein         1..1254
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=138019
     Region          148..1253
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlsaliplcr khyylwllcc mllsyrsafa gdevqweqgn nptltlgftn asvleafrqi
       61 tvvtgmqfsy nkedidtgrr irlvsqkrkl telldaigqq vhlkftqvnk tiavsvpepe
      121 qlpasaagpm ltplmatdtv pagvgnmtik grittarnep lpgvtvkvkg snagavtnge
      181 gyytlsnisr damliysfvg ylqqeervsg rqtidvqlqe dtrkinevvv talgikrqkk
      241 evgystekvt gveiaqaaap nivnalsgkm agvnvvqpgg veggktriti rgntsikgnn
      301 eplividglq fendggisns iesgkdwgsa innidpndie sidvlkgpta aalygargan
      361 gvimittkkg rnkkglgiey agefkltkan mfrdvqnefg mggpawgdve prllknsdge
      421 nvlpkfwgqs htgdgntats lgkratwenf swyysglswg prldgspvrw wdgqvrsfsp
      481 qpdnvslffk tgttikhnvs fsnagdfgsf rvslgrmdnd avvpnsnfsq tsvnigaslk
      541 issrlkadva mnylrydrkn sptlgsdans wgyqslygyp rewrpierdt yenpdgskna
      601 fnnypnmgky tsyadyigta gspgnfwwnt ynnntflgrd kifgtitlny eatswlnvmg
      661 rlgidrqfdl leyknkptsi ngitdgkygi nenklfvqnh eflvtahken ilpdfnvrls
      721 vggstwqrki nnfnastgnn nwsapwvyal nnvkdknale laditnlgyg lynkklnslm
      781 glldlsyrdm lflqlsarnd wastlpkgan sylypsatls wvfteleslk gmkglsfgkl
      841 rlaysnaard adpykvtpty gvgtsanqlv lslpvivpas nlknettrgm eagvqlgfld
      901 grlnldmayy rnrsynqllt snlplssgag qflfnsgvlq ntglevilda kildrkevsw
      961 nsglrlsnnk trvvaldpkv qylslgdlwg rygpsinvke gdtygtiygy dyqydasgrk
     1021 lvsddgtryl ttaekvpign anpkltggwt ntisyrgitl svltdfkwgg difagsyayg
     1081 vfsgqspttl aernggglpy tdadgvtrnv gvildgvtrd gkvndkvvhy lwkymgnigs
     1141 gwgnwsikek dpvtgaevnk eygflhkpai fdnswvklre vsisyqvpsk vvqrwkviqg
     1201 lsvyvtgrdl fyiyknlpdn inpegsisag naqgfewggy pnmrsfalgv rlsl
//
LOCUS       WP_095837612            1122 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095837612
VERSION     WP_095837612.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1122
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125140
     Region          31..1121
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrksqllvrt iilliavcls pwrleaqssq rivkgkvvda vsgkalpgvs vyassktigt
       61 ttsteniien isigaitdek gefslklpds lsvkqltvgf mgyetrlltl tasnhykial
      121 saagknlnef vftgyqtikr nkltgatdkv smekidvggv msveqmlqgq lsgvavtpqs
      181 gapgqaakir irgtsslqgt qdplwvidgl pvegtnlpsl ddakaidqly ttsiagynps
      241 diesitvlkd aaataiygar aangvivitt ksgkrneklt vtyrnnftft qkpdlgkldl
      301 mnsnqkvnle ldlftsdfsf ganngevsri lrkynvspqd lsggfgsina narneinalr
      361 nintnwndli frsaftqeht vsvsggsdrs tyyfsggyyd ekgatigtaa nrynitlktd
      421 ydltdklkfs agifanqrnq ssfnpnqggn tspvkysrla npytpvvdak gnyvydknig
      481 gdkniidfnl leernntsnt lktqsvntnf kldyeviprl hissqlgvqs diltgeqial
      541 entyyvrlla dqnmrfdpts gtqktiiprg gvinnnsrnt qqytlktmae ynftlnrkhd
      601 fnvmvgnelr rvkdkyittt gygydpktlt tipikfqndn dikalykdrt nyaenafvsf
      661 fgtgsytfdn rytlgasirf dgsdlfgvdp kykylplwsv sglwrvmeep fmknirfint
      721 lnvrasyglq gnidkntspf vvgiynnvni lpgdpvqtir vdnppnaklr wektisknig
      781 vdigvlnnrv nitadyydrh gkdlinvyal pletgfqsma inwaemrnrg vevslttrni
      841 vgknfrwttd fnfaynkntv lretlqdnsy fpsregqpvg tiwgidyagi dkngmimvny
      901 ngkveslsel lqlqddfagd pdlgglfpys kltntqqrdl lrsmgssdpl ytggfnnsfs
      961 ykrfdlsigl lfnlgqkvrv dpaynpffyd ratnapkail drwtpsnpng kypalfgdgp
     1021 gtneelkllg hwlqdkyyqy tslnlwirng gyirvrnitl gyrlseevcs rirlkglrit
     1081 aearnpfvfs rhydgfmdpe tmgniyaqpi pktftfglna tf
//
LOCUS       WP_095837330            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095837330
VERSION     WP_095837330.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120103
     Region          31..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqhylrnqik svgwllalcl sgtaayaqqa vtghvadads kqpvigatvk vkgtsrgtst
       61 dvsglfkita dpadtlivtf igytpvripv ngqhdieial ladkkaldev vvtalgirke
      121 vkrlgyavqe vkgsdlikar epnpinglvg kvagltvgas gellgapqvl lrgssinlfv
      181 vdgvpinsdt wnispddies ytvlkgatas alygsrglng aimittkkgs kdkrgfsvef
      241 nsstmfdrgf naipkvqdey gpgdhgkyaf vngkgagtnd gdydiwgpkf egqlipqyds
      301 pvdpvtgvrq gtpwiargkd nlkrflqtgv lstnsiavss hteksdlrfs lshsyqnsiv
      361 pknnlnitnf nisaghsfsd rlrldaylny nrqytpnfpd vqygpnsmiy nmviwsgadw
      421 nvddmrnywq pgkegiqslf aeyqryqnpw fmvnewkrgh yktdvngyak lsyklsnhld
      481 llartqvtsy dllrtekvpy sahpygmedg lgnyredkrt mfenntdlll tynntftgni
      541 slrasvggna rsfsykssfv ttdylnvpgl ytfsnslnpl kasnftsnml vlstygyadv
      601 tfnkyatlsl tgrvdklstl pkgndvyfyp svslstvvsd yvrlpevism lkfrgsyanv
      661 kggltsptig atpqgsypig ygaeyqssyd gpsfenfsgy svqpvydtki gakftrtian
      721 pqlkpfssta yeagmdirfl qnrigldvty fvtkngpriy slpvtdatgy ekilvngvvt
      781 rkkgweislt gsplrssngl nwdimanwst fkeryvsfyp gvntintyfk agdrvdgfyg
      841 stfvktpdgq liydfamqkn pdgtetrvst glplkspkdr flgytnpdwv wsinnsfryk
      901 qfnfsfqfdg rvggkminyi qqqtyrggrn iktvqgamge aryndykgvk swngggvwvs
      961 ngvpiqydnd gnvtnykdlv fspnttktfl qdyvsvyyst neanmisktf aklrevvigy
     1021 tlpqrmlgrs firqanisfv grnllyfaan kdldidqyag dqassslqtp atkrygvnin
     1081 ltf
//
LOCUS       WP_095837652            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095837652
VERSION     WP_095837652.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116100
     Region          25..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfarhaaal lfvilytqag faqsikiggv vtgktdaqpl pgviivvkgt sngtqsdadg
       61 kysikanssd tlrfsfigyn tievpvgkss qlnialesae sklqevvvta lgisrekksl
      121 gyamqelksk ditearetnl vnalsgkiag vnitnsqgnm gssrivirge tsisgnnqpl
      181 fvvdglpvdn sqlgvgsgrd fanaiadinp gdieslsvlk gpnaaalygs raangvivik
      241 tksgrgkqkg lgitvssnat vedllvlpsf qnvygqgsgg qfsyvdgkgg gindgvdesw
      301 gpkmdgrlik qffsngqpap wvphpnnvkd fyvtgytlnn glsiagsndk ldyrfsynnt
      361 kqkgilpntg isrnsfsfnt tyritpkltf ssnvnytrsv adnlpgvdgr rgnsvtlqfi
      421 wfgrqvdvnr lrdyknpdgt dynwnhsyys npywiqyent vgqqrnrifg ntrlsyqild
      481 wltanvrigl dyyndrrkyk iaygtngtpf gsytedaygi sevnteftln avkklsrdfn
      541 ldvlvggnir nnqteqnyqq aprlavkdvy tlnnsrdpvv ssnifgkrri ysgfasaqlg
      601 freyaflnlt arrdqsstlp rannayfyps anaslvlnea fhiqskaltl lklrggwaqv
      661 gndtdpyqli ntypfnqpfg eyplltvsdn flksdlkpei tssaeiglea gffnnrarid
      721 vtyynansrn qilladvsas tgylkkllna gqinnkgiei slggapvsta sgfrwdvnin
      781 yarnvskvve ldkdgflndy vlgtsgnvqv laskgkryga iygkayqrda sgqilvnpdg
      841 tpaiandrkv lgyytpkwtg sinnafsfkg vtlsflidtk qggsiwsgtn ytgiytgvla
      901 aslpgrdaen ggipyyyagn ntsstpvrlp nhnagapnge tvyhdgmifd gvtssgkknd
      961 vilpaqryyk svynsslnes svydasfikl revrigyalp kelvkrwgfq aidvtlvgrn
     1021 lwiidkkapn idpetafntg ngqgletlqi pttrsfglnl nvsf
//
LOCUS       WP_095837690            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095837690
VERSION     WP_095837690.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113073
     Region          31..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklflfiml laalpvlypq rglgqqkits vltgkileag srlplagasv silgksgasr
       61 adadgmfrls vegkaiimvs yvgyasksve lsegqatvei lltkkasdle dvvvigygkq
      121 kkkditsais sisgdeikqm pvttingalq sripgmqvqh tghepgagtn vkirginsit
      181 qgagpiyvvd gvittgdlre inpndvasid vlkdasaaai ygaraaegvv iittkkastg
      241 rasinydayy gvqkivkgyd fidniddyvh lrrlgwsded prawpigdsa adaklfhple
      301 lksianrkwy dwesvvtrpa pmqshtlsvs ngvgknklyl sgnylnqdgi irgsnftrys
      361 vkanveseln dkvkaginsn fshinnkvvs netyynavtm splfpiyndd gtpssnidps
      421 sgniqfnnpv tltespiqrv ddryianvyv eykvikdlqf rssfgvdiyk nqqfeyyprt
      481 tsngfskngv akaqnfgyrd mlwentltyd ynphqhhsfn flggftyqrr rqewnyeeas
      541 gfptdeltyk nmslasrrdn issdyfnwai qsllgrviyk ykdryilngt vrrdgssrfg
      601 sknkygvfps vsgawrlide pfigirtktv lsdaklrvsy gvignqeipw datffrmnaa
      661 aypfngstqt tgyqvngsvl gndalqwesq hqfnagvdla iindrirvsf dyynknvrnl
      721 llradlpvsq gfdtkwinva emntrgmdvs lkvspvktkn fdwqldinws kyrskvtsll
      781 pgrdslspyl kvgeapnsli vdyvydglyn agddfklnpg grpgdvrvkd mdgngvinqf
      841 drtivgrtvp kgwggiwnyv rfkqfslvvf anymygqdis nrayqdylys tdnrrrilks
      901 glnywtpeht qtdlprpnvf grsvrtlpag tssfivqkgd firirnitls ydftakmlsk
      961 lkvnslrvya qvmepflitk ykgidpeigv sqydvypryr tflagvqlsl
//
LOCUS       WP_095838101            1038 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095838101
VERSION     WP_095838101.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1038
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111850
     Region          46..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrlrltkv cvsaglafsl lcadsaymta aayaasssna nyfndisgtv kdsqgnplpg
       61 vtiviknskk gvksgadgrf vinanegdvl vfsfvgflsq evtvsgnnsl nivlqdnvkg
      121 lnelvvtalg irkaersvgy avskvsggef tkareisvan alvgkvagvn stapatgagg
      181 ssrvtirgnt slngdnqply vvngmplnne nmgnatkwgg sdlgdgissi npddiesmtv
      241 lkggaaaaly gqrgrngvil ittkggkark glgvelnsnv midkindftd wqdqygsgsr
      301 gikpttldqa rtnglqswga kldgsdvmlf ngqtgkytaq skdnlkdfyk tgvtytnsia
      361 fsggnenttf rlglgdlrss svypnskynr tnvnlsvgfk lsdkwsgdvn itysketgkn
      421 rpnlsdapgn gnygilflpp nikgsllapg ydavgneisa ssdvyttnpy faankfqnnt
      481 qkdrvlgvas lryqalswly iqgritndff afngtsitpt gtayfpdgri dlernyqfne
      541 tnmdllvgan keiakdlnlg vtlggnllkm qakdnrlaas alafrglysp atagvlrstq
      601 fqqprkdvqs lygsvelsyk stfyvsitdr ndwsstlpkg nnsynypsvn asyvfsehlk
      661 ssfldfgkir agyamvggda dvfktqlyyn tfgaigsaal gnlsnelpnp kleplkvkel
      721 elgaelkfln nrlgidftwy nkqtlndiva gtvsrasgfq talvnvgkid nkgvevlvtg
      781 vpvrtknfnw ttsvnfahnk ntvvqlaegq nfmltgeart engyiqqrvg qtyaqimafd
      841 ykrdakgtiv ldasglplqg nlismgtgiq pttggwsndv syknltlsfl idfksggkiy
      901 sgsnarayqn glhketlpgr dggvtvkgvd ekgvavektv naqdyynrlf qisslyvyda
      961 sfikfrsvsl tynfpasafn nkiqglslsl vgrnlfyfkk ntpnidpean ytntnaqgle
     1021 ygglpstrsf gvnlnvkf
//
LOCUS       WP_095838109            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095838109
VERSION     WP_095838109.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120303
     Region          29..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtlrrslll ftllyfccci talaqnktvv agivkdekgt plpgvtvkek gtangamtta
       61 egtykvsvap natlvlsfvg yvmqeipvng qstvnvtlle dkknlnevvv talgikreqr
      121 klgyavtelk gaevaktnsi npvaalqgkv agvdisgaag gpqaanrivl rgakslngkd
      181 qpifvidgvi fenevsaadv nfgnvlknfn pddfesvtvl kgaaatalyg sraingaili
      241 ttkkgttrkg lgvnlsqtvq fehayrqpia lqnsygagrf gtfkpnttne ldwvgglsfg
      301 pkmdgkmvkl pngeevaysp kssnaldgyq lgkyfntnvs meggndkatf rfsysrldnn
      361 svspdnkfsr nsfalkstaq iskvfsldgg vnyatsiarn pnrqggdytn lnigrkwiyv
      421 fprnydpdyw ekryltpana radlaqnpga dywfalknyt werderllsa nlaltatttd
      481 wlkfivkgnf sneqntdrrk evgtlanfsg pdglfalqtv nrsqhtftgm amltpklgge
      541 fegslnlgve twnsgigtqm enrtqgglri pkmfaisnsv nnpvsketpl lrkrinsaff
      601 aaslayknaf flditgrndw ssaltykngt gtnsyfypsf sgaweftqsl knsipsfisy
      661 gklrasyamv ggdtdpfein pgyltegfwn ssstgqglpq inmfnqntlp nlhlkpsisr
      721 sfevgadirf fnnrigidva wyksnitnqi iklptsmetg vkeryinags mqntgievai
      781 nasaiqhknf twditlngsr nrnkikslap gvnqielnnd qdvrvlaavg qaygvivtdy
      841 gftpyqakda sgnpvahpnn gkpvisatgs elpykynrgy qvvgnitpdf nlglsnnfty
      901 knwslgflvq ariggdifsa shqfgtgrgt vestmhgrda anggitytda ngktrddgmi
      961 pdgvfqdgyk iskngqeinl ggmtyreayd kgyvtpmtpy gyygmqgdwg igirstsvfd
     1021 asyvalrevs lgytlpsnvt qrwkmnslrv mlvgrnlgyl ynnlpdrlnp esirnnstsa
     1081 fseygavpfv rnmaftvqvg f
//
LOCUS       WP_095838289            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095838289
VERSION     WP_095838289.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124094
     Region          133..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktikstgir lvmvagmlcg agvhagyggg kayhedqpat vplvsfisrl egkfdirfsy
       61 dtrllkgkqi pspdvdeftl snmevmlkry isplgllckr idnklyiisa iqqpaittsg
      121 kvqlavaeqv qavrgvvkds sgnvlagvvv klkgtsrgai tdgqgvfvid nvqegdvllf
      181 slmgftnrev vyqgqrditv vmkestvslg qvvvtalgik reekslgyav qqvkgdkvqt
      241 vkgvdigtsl tgqvsglvik nsteffarpt ielrgegall vidgvpygnm tlrdiptddi
      301 aaidvlkgpt asalygsraa ggvllvttkk ggepglsinv nsntmvqtgf laipkpqtsy
      361 grgqygkidn dyvwgpkldi ggtardwnpe tkqfedkrpl esvgrnnlkn flelgvvtnn
      421 ninvsqsgkl gsfraslnhi ynkgqfpnak lnmfnftlgg elkasekfkl eahmglsrre
      481 spqvwgagyg nqgyiyqltm wtgpeydirq yrdywkvpnk tqnwmytnwy dnpyliayek
      541 lngiqqhtin asltanykfs ndlnllvrtg ydvynnketf qnptanifst rggwnargry
      601 sinnawgwsi nndailsytk kvgdwsfdam gggtiyywvd eglnastkng lvsptfysla
      661 asvepptisq sytsrqvnsl ygrlaigwkn aifidatgrk dwnssqpens rayfypslgt
      721 svvlseltkm pdvldmwkir gawatfktpa dvyainrlys tttsawntln aasypsnllg
      781 tdllpssqrt weigtaaylf kkrlhidvay fnkyyynqqr svsipgssgf sstlvntnet
      841 yvrkgveitl ggtvirkkgf ewttmvnwsn qhryyvnids vysaknpwtk khermdtytg
      901 rywltdpsgn iihvngypvs sdydkkygys dpvfsfgfin nfrigqfnvg inidgrvggl
      961 lynytydkmw dtgtnpesdn syrydevvkg lannyvgkgv kvisgsvtyd nfgnitsdtr
     1021 qygpndtkvs yqdyaqkfrg gdngiqkktf vkvreisvgy sfpgkllsrt gikqasvavt
     1081 aqnlflftgf kfsdpdvdae nlnspsqrll ginfrigf
//
LOCUS       WP_095838355            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095838355
VERSION     WP_095838355.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112261
     Region          24..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkhllkvll ilvlmgqplf aqnrevsgtv teksggapmp gvivrvkgak sgtstnaegk
       61 yhlqvpgqha vlifsfvgyt qvehvvsgdv ldvslvadnk qlseivvtaq glkrsarelg
      121 ysvakidnas ltqgkvvnla tglaskvsgl qvnlpnngvn peprivlrgn rsltgnnqal
      181 ivvdgvpvps avlsnlnpnd ienvnvlkga naanlygseg vngvlmittk kgktgrpvvr
      241 ysnttqfetv smlpdmqykf gggsdgvhdp ientswgapf dgtlkqvgpt ladgskwmlp
      301 yvglkdekrk fwdrgltvqn dvavsagsdn sefylsfqda nikgvipkdk nrrtgarlna
      361 srkmgiftag fnagytvtkt ntttaniydn llnipqnvpi tqlsdwrnnk waatdgyfng
      421 yyrnpwwlid nqradrmtnl fngnldlglq plswlnfvyr vglyneaytq ksfrakvnpt
      481 tayqrptadn gyvkdeaytr rrinsdilvt adhkfgdfst kltlgntird nydnyssiea
      541 nglvapdvyn vnnrtgeatv dqyyrdtrlt alfgdlsvgf rnylflgvta rnewvsilss
      601 knrsyfypga slsfvftdai qalqgnrtls fgkvtlsank tgnvnldpyq litpfingtg
      661 fpfgtlpgqt ldnrfrsqel kpefvnsvea tlqlgffqdr lsteisvykt tskgqiipiq
      721 tsfatgyssv lvnsgevsik giefdvkgtp vknknvtwtv gvngtylqnk visiyggeng
      781 tsevpiggya nsayiyavig qqyptlkvka yqrdpqgriv vdgatgypkv analkpvgqt
      841 npnfmmgfnt svkykgftlg iqldyrtgnv fynqlgrgmd fnglgsrnae ynrepfvipn
      901 svievspgkf epntniktts ggfdywysqy sqinenyvad atflklreas ltydlpatll
      961 rrqnivkaas vtisgrnllm wlpkeniwtd pefnftsgna igvvddkiap ptriygasvn
     1021 itf
//
LOCUS       WP_095838363            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095838363
VERSION     WP_095838363.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107554
     Region          26..965
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mllfrstlma lvlitcafal yaqqsltgkv tdavsgkglp gvtirvpnts kgtitdvngq
       61 fnlatpagts qliltftgyk tktvavgnsn tlnitmeedy akldevvvtg lattvkrsnl
      121 anavatisak dlagtapaqt fdaalsgkip galitansga pgggisvklr gitsifsnsq
      181 plyvvdgvfv snvsipagln ditgaatagn pqnqdnpssr iadlnpqdiq nieilkgasa
      241 aalygskaaa gviiittkrg kagktqfsvn qetglvkvrk llgvrqftpe taadlagaas
      301 stdpavqaar arnrqdflaa qaagkiydye keiygqtgll lntslsasgg sekttfffsa
      361 nrrsedgiik rtgylnnslr lnidhkvsdr vslgftsnyi nsssdrglsn ndnngvslgv
      421 alastpgfve lhptanglyp rnrfaasnpl etrdkmtnne ntnrfitsin fdakvqqsnk
      481 sntrlivrgg vdffnlktaa ifprslqfme ntlqgasiqg ntnntntnla gfivnvfsps
      541 eklnltstig atletgnldn ivvastklvg tqtnvdqaga snprqfrqky rdngifiqee
      601 ltlldaitat aglrfdrstn ngdfkkyyly pkgalswnia kmdfwhskqi nslklrvayg
      661 qsgnvspyga kftslvgsnt ggfpgslvdn qlgnpnilpe kqteleagvd isildgrvsl
      721 eatfynkkif dlllrratpg stgyttqwvn ggdlrnrgve lglslipvnt knvkwtanin
      781 wwknqsritr leipafslga fgnslgtffi eegksatqik gtvkdkvglq tlgnaepdfq
      841 msfmnevtlw rnltfrflvh wkkggdninl tellsdlggt tpdydddkng ngikdglert
      901 nagdasifvq dasyvrirei giyynlplhn tkyiralrfg isannwftft dyksydpess
      961 nfgsntlstg tsrgssgist gvevmpfpas krasfhvgid f
//
LOCUS       WP_095838507            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095838507
VERSION     WP_095838507.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118839
     Region          23..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktyllmlll slwtisassq ellrgivtdd tkvplpgati rikgtttgtv tqpdgsfsir
       61 vndpkqttvl vnyinyltqe iplegrlqln vslvrdpvkl kdvvvtsalg ltrkaksvvy
      121 ssqsvdptrl teardvnian tlagkvaglq vttsgqpggs srviirgdns itgnnqplwv
      181 idgvpidnps gdgrgdnldy gngvsdlnpd diesievlkg pnaaalygsk aangailits
      241 kkgrgrgdrs lgvsvnqnmm wntisefpay qnvygegnaf rlvqnanniv pgtnainmgt
      301 ntrswgvpml gqpyndysgk phgylpqpnn vrdlyrsslt nitnvaiaks dsvsafrlsy
      361 tytrandvle nqnirnkhnl nltasrglgk kvnvdtrlly tydnmrnrty rnmdpqspmn
      421 ayiyllrsid iaslhpyrdd ngdayaygaq gdgyenpyws inenenqdlh hrviggvttt
      481 idllpdlkfr aqiagdlafg ngyqyrekga rqnkngfysn fnqqnqywni eglllynkql
      541 kpdfsltasl gtnfnfgnsl frqasvasli nhdmpsians naypratesl vrrkvnsvfa
      601 attlgykdfl fldvtgrndw sstlptgnas ffypsvggsf vftqflesis nivnygklrv
      661 swaqvgndap ayylqsnyqy gglflgtpwl dyenllknkn lkpeqttsre vgldlslfkd
      721 risinatvyk sntinqimra qvaretgfte qilnageiqn sgielslkat pvrtnkftwd
      781 llanwatnns kvvsltpgvn ryvlgswwmm ssnaevgqpy gvlrgnvayr nqgkliinpa
      841 ngqpyydena ylgnfrpdwi gsfgstfryk gfdlsflvtv kwggdiysvs nhkanvtgnt
      901 iaslegrdaf lfsslvlges gdeqkgvgly gnpyldarnk gmrhpgyypl ldasgkpild
      961 kngryqpgap nahwispqgy wqtmdfdmeh nlfnatsirv selvlgyslp lsrntrrffq
     1021 garlalvgrn lwtilkhtpk gidpeaants gnaqgieqgg sfpyaqygfd lkfnf
//
LOCUS       WP_095838844            1145 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095838844
VERSION     WP_095838844.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1145
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126112
     Region          115..1141
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhhsrilcll cllcirgltl narqqpsplh ekvslevdnq pllriihlle qqtsasfayp
       61 ndillnrppc sihrrhvplh eilqllfppq tytlrvigrq iiikqvtpqp aaasqvngtv
      121 rdassglplp gatisagnia atvtdtlgmf slrvplgtpv scayigyhta trnatqepll
      181 femspgvqpm ntvvvtalgl nrsqrslgya ladidgrdit tarevnplnn lsaqvagldi
      241 yrvnsgvgga tkvtlrgpki iggnnqplfv idgvpidnss pgqaakfggy dlgdgsaain
      301 pdeiatisvl kggaaaalyg srasngvili ttkkgssqgl qvtlsantvv eqlnnnddfq
      361 eeygsgrdgi lprdvaiard asqtswgprl hpdslvwlwn grkvpyrkaq ktsrhffrqg
      421 ltttnavtaa agnqhlqtrl tythinnkdi iprsnqqrhn isvrttaqpn khwladirmg
      481 yaneqvvnrp alsdysnnig yvlstvapni dldwlksykd pvtgnyinwn dnvyqvnpyw
      541 aineqpndsk qdritgfvll khqwtpdlyl qgrigidytq fhfrefmeys tpfnpsgmlt
      601 lknrrlrein nelllhygkq ighwqltana glnrmdyien vlnttgrdin irgikslynf
      661 ktvlsqells rkrinsayaa fnisyqnwlf lditgrkdws ssltkghrgy fypsasvsfv
      721 fsdllpasnv lsfgkwrcsl aqtgtdaidp yqltlsygnd pelpgvggfi iggvavdkip
      781 atdlrpgtsr sieaglqlnf wkdrisldls yyhtntidqv lnvvvspasg yttavinagk
      841 venrgveayl slkpvatpnf kwelrlnaaq nrnrvnalns llsgyhmlsg arwgnasiva
      901 kegaaygmim grkllrdpqg rlildaaglp gfenadtplg ngyynwtagi tnqltyknls
      961 lsilldikqg gniysmtnfi ahargrakgt vpgrdgwans ekeriaagks paewiptggl
     1021 qvkgvrqtgv dangkpvyns fstfvnpqty wqritdnipe pfvydasfvk irqltldyhc
     1081 ppaicrqlal keltvsliar npftlykavp nidpessynn gdgqgleygs lptrrsygin
     1141 lcvkf
//
LOCUS       WP_095838640            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095838640
VERSION     WP_095838640.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116374
     Region          23..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkrllalll laglpmylwa qqrqisgavn dekgqalpgv sireagtsng tttsnqgkft
       61 lrlkndkakl vvsfigyltq titadekdqy tiilktdaqs lkdvvvigyq evkrktttaa
      121 vasvkgkdie nlpspsfdql lqgrvaglnv qnftgepgvr gsfvirgnts isrnidraqa
      181 lssplfvidg ipvslddaas fdntgtnyia ginpndiesi dvlkdasaaa iygsrgangv
      241 viiktkrgkp grpqinfsty agisekpkfe hfitgteerr mkleyllara pydraanlpr
      301 iltdslnpaf naatdwqdlf yrtamvqnad isvsgasdni nyrvsgnyfn eqgvlkgtgf
      361 krytvstaig mkmspkvsvd alfrlsrgdr srgrgqlpwe naiplrngqf lsslfqlsei
      421 drmnyvgale sgrdknindd itgsitfnyd fnkhlrfssi gsiqasvnsr difrpgilaa
      481 tgmsyaqssk siyqnlnldn tlsyttnvan dnhhlnvllg htinsikney tgvgggaisn
      541 dnvkvvqgid pnfyvlrdpy gslitgsdfk ssgllsffar inydykeryl fsvawradas
      601 srfgkdsrwg yfpsvsagwn imdepfaegl krfadafkir gsygitgtlp sgyylpfnty
      661 sinqggyggs qaityngvna vtpnfsggva qngltweqsi qsnlgidaaf fenrlvitad
      721 vynrgkskil fdlklpstgg ydkvntnavs vrntgwevni fgrlmnsknp fqwntriims
      781 anknqivalp ngnrdlvved pntgmiyllt kgrpiyefyl mqskgvysnd kdipfnpltg
      841 dkltywggsh tvqpgdyiwv dqnndfdvwd wndrvrsgnp npritggftn tfmykgfsle
      901 vfmtfllgrd ifnkyvsdrl qgfqsnlsti alidpnrlqt wqkqgdlaky aelnpygany
      961 yqflpfssay iengnyarik yinlsytlpr rlldrlklrn lqiysvidnl ytfqkssvpd
     1021 aeavnelgvy sgtgypiprk ftlginvgf
//
LOCUS       WP_095839431             989 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095839431
VERSION     WP_095839431.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..989
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108836
     Region          30..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkttlflfk vcaqssvwll lalsiyaqsk vitgkvtdsq dnsplpgvtv qvkngktgtq
       61 tgadgsyrlt vpadgntiif sfvgyqqler avasagtinv alvadvkslq dvvvvgygtq
      121 kksevtsavt svkaedfrqg garnaldliq gkvaglaitr tsgtnpnsgv aiqlrgatsl
      181 tgsisplivi dgipggnldl lqqddvasid vlkdgsaaai ygtqanggvi littkrgrsg
      241 pmkvdyasyi rkeyvqrrpk fltgeefaak iasgeikttd rgnrtdfldl linhanltqn
      301 hnlafsggnd kstyrvslyy qdlqgiaken arqqyggrvs itsrglqdrl slqlnlttnf
      361 nkanmlgggg wegyltanpt tspynpdgsw lferngtnel arlsqetnrr qqqttsgdak
      421 lgleiikglk asifasvqrd swldgayrlq ksesskenyd ssgyasqnte lkvnyavept
      481 leyvttiakd hnltaitgys yrygveqgfn annwgflndv fqenkldags kltegkagmn
      541 sykndntlia ffgrvnyayk nkymaqvifr regssrfgan nkwgnfpavs agwnikeerf
      601 mnmvpvvdal klrvgygitg nsgianyasl vtmgtggnyi ypdgfwrqty gpnrnpnpdl
      661 rwekkkewni gvdfslfkgr lsgaidvykr ttedlletft sqqppfires iyvnvgsisa
      721 rgveltlsgi pvtnknftwn vdlaastnnt rldkfsndly kldfktygdi ggagalgnai
      781 rtnegerlgn fygkrfagft ddgkwlfykk dgskvtfdki nsqqdhvvlg naipkfyasl
      841 tntfhyknld lrifmrgkfg ykilntmela ygnkvavpnn vlrtaftkha klndtyqysd
      901 yylekgdhvk ideitlgynf sfkntpiirn lrvyvtggnl ftitgysgnd pdfirdtgln
      961 pgidalntad nrspyistrs fmiglnvgf
//
LOCUS       WP_095839745            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095839745
VERSION     WP_095839745.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117108
     Region          24..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksiyaifmv chllcplmll aqsrtitgkv saaeggtplp gvtiqvkgtn egtttdaqgn
       61 yritvqqada qlifrfigyl avslpaagqt vinvslkpdt rnleqvvvta lgivrrersv
      121 gyatqqvkge nltltkeqnv igslsgkiag vqvtgssgas mggtqkikir gvnsingadq
      181 plividgtpv snsnfsaern gpdlgnlaqd inpddiasis vlkgpaasal yglrgqfgvv
      241 mittkkgsrk gdkkvsvdfs safsleragn fmplqntygg ggsqtfstin vngvqqpfvs
      301 gtdeswgpkm dgrpvrhmys wfpadpdygk ltpfsphpdn ikdfyrtgyt fnnnisisgg
      361 genssfrlsy nntriegvep ntwlkrnnlg fngslnitps lqvntslnya nnnaqrpsqg
      421 yyegsrnfvq wfqrsldmkk lrqykyadgr fyhwnlndpt qpgflesvsd wnnpyfeaye
      481 npahdsrdrf fgnvgliydp lpglklsgfv rgdmyiqqld kreaiggrrl nsystgkyqn
      541 kemnyeflaq ynrewgdisl nanlganllt qrysylsaat qgglsvpnff nisaskerps
      601 itdylrrkei ysyfgsatvg ykdiyyldat lrndrssalp kgnnsywyas gaasivfsel
      661 lkweplsfgk lrvslaqags dldayrisqt ynlrapigtt ypmsvpdtln npnikpaigt
      721 sfeagvelrf lnnrvgldvt yynqqnkdqv irldvsgtsg fsyywvnagn iqnkgievsl
      781 ngqpvksrlf nwttvfnisr ntslikslyp ginnlildqn tysrvsvfln atvngtfgtl
      841 ignayqrdpk tskilldaqn lplfeqnhdf gsvlprfigg wqntfrignf digamidfqs
      901 ggrffswsrm lavksgqaee taamndrgkn vrdpvaeggg vkvngisaat gqevttyvda
      961 kayfrsrlgt svyeewlyda syikmrelra gytfrkeqfk glpfsslnia fiarnpfmiy
     1021 qkapkgldps elsagsapis wletgqlitt rsfgvnlnvs f
//
LOCUS       WP_095840017            1198 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095840017
VERSION     WP_095840017.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1198)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1198
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134290
     Region          119..1197
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfevrykkkr pksrllllll tvcclqaman plseeqlrte kleailrkme qkfnvvfvyd
       61 aaviskemnv elnleklsmt dalkvlanrg issrimgdkv iltrpaqpea apqqqvvalk
      121 grvsvrseng disfmpgisi hekgtqngta tnnkgefsik vsagatvvfs mvgfksqeik
      181 vtssrdnmsv mleenittln qvvvngyqti drklftgaat alkasdvrrd gitdvsrmle
      241 grvagvsiqn vsgtfgaapk irvrgatsit gdnkplwvvd giiledvvnv sneqlstgda
      301 ttligssvag lnpddiesfq ilkdaaatal ygaramngvv vittkkgrvg kplisytgny
      361 stylkpkysd fnimnsadqm saylemerkg wlnyadvsrr anggvftkrs dlihkgqlln
      421 tpeskgdylk ryaaantdwf dilfrnsfmq ehslsissgt ektqlyfsts flndngwtig
      481 dnvkrftgna ranfnvnerl nfglitqasi rdqrapgtvg rvsnpvegky ardfdinpfs
      541 yalntsrtmt aydengnley frrnyapfni inelrnntld ltmidlklqg easykilpnl
      601 kysflgalry aktnrehkvk enanmamayr aaddatirar nkflyrnpdd peaepvvvlp
      661 yggfyntndd ylvsynlrns lewnktynnt hifhvlatqe lryadrqnkf sygygyqfdk
      721 ggvpyvdpnv ikqgvegnfd fygmswrydr flaymtnaay sykgkynlng tvrydgsnll
      781 gkartarwlp twnisgswnl dteefmkhqs tinrltlrat ygltasmgra tnsslvlign
      841 rtkrpylsev esvinirdle nseltwekqy etnvgvdvgf fnermnltld lynrdgfdli
      901 slmrtsgigg qfeksanyad mkskgievti ggniiqhkdy gwrtqltfay nknkitnlrn
      961 npniwdlvga dggplqgrpy rglysvqfsg ldpltgapyf ineagdkshn vylqsqdiky
     1021 lkyegpvdpt ttggffnsfr yknftlsall tfsagnkirl npvfdesysd ltamprefrd
     1081 rwmatgdekl tnipaildqr anaalngfyt ynvynysser iadggfvrlk qvsltynlpv
     1141 rylsaigann lslsavannp wliyadkkln gqdpeffgsg gvalpipkqy tvslkvgf
//
LOCUS       WP_095840056            1158 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            sp. MD30].
ACCESSION   WP_095840056
VERSION     WP_095840056.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga sp. MD30
  ORGANISM  Chitinophaga sp. MD30
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Chitinophaga sp. MD30"
                     /db_xref="taxon:2033437"
     Protein         1..1158
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128726
     Region          123..1156
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrpiltslwl lciallafni pvsgqqkdvi vslvmdkaty rqvferitaq tglqfsysdr
       61 fnpdeqvrga lvmgniklrq alyllikkqr kldfeisgnt iyidkkpvpa vsvpvvqree
      121 llvitgivtd stgmalpgat irvisdnsgk gvttdidgqf risgisksar lgvsytgyqt
      181 altdiptsgy lhvrlshkrv gmgeieivst gyqsipkera tgsfvginng lfnrqvstsi
      241 vdrlegivsg llfakagtlt gndavmsirg rstlfaatap lvildnfpyd gdlrninpnd
      301 iqsvsilkda aaasiwgara gngvivfttk rgklqqpvqv tfnsnltige kpnlhsvpql
      361 tsaetidlek qlfdkgvydg tisvpylpis pavaifsdlk ngkitagead rlinqlkevd
      421 vrkdqkkyfy ntsvnqqysi gvsggtaihn yyasvgydrn nnsmvnnkye rftinvnntn
      481 yflknrlevs tgilltkskt tsgnsylpgs pyekvvspeg kalavnttsy rksfldtvga
      541 gklldwtykp vderdfgate dvtdyrlnfg akyyvtpdln ialsyqygrg nyyvlipngl
      601 ntfytrnlin sftqidpftg nitrpiplgd inqygntvsn vhngriqany sktihtdhyi
      661 tglvgfevrd tksdanssta yginkrngsa gpvdyvntyp dyvtglmnni pgsfsyqtlv
      721 drflsyffnm sytyknkyil sgsvrrdesn lfgvntnrkg vplwsagvsw eisqedfyss
      781 hilpflkvrv tngyngnidr slsafttaql vpgavnqfls pfseirnpvn pnlrwekvhi
      841 vnlgvdfafk nnvlggtiey yskkgtdlla ntltppqagi tmskgnyakm ltqgvditll
      901 arildkrfkw nsvlltsfvk drilkydvkq ttnyryiaan yndpmegkpy saifaykwvg
      961 ldkegdpqgy lndkvskdwa glrsstdrtd mtyigpgsps vfgafrnsfs fgplhlscni
     1021 vyrlgyyyrk pvmnnaalis ssmigyrqpd ynkrwqqpgd elhtsvpvir ypgddardef
     1081 ykyasvnvek gdhirlqdiq lsyrvntqrl kginalniya yisnlgilwr anksgidpdi
     1141 ltsiapgkty slgikldm
//
LOCUS       WP_095840419            1125 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095840419
VERSION     WP_095840419.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1125
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125018
     Region          38..1124
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnesvcyrkk yvlkwlplll aiiscciqpa iaqqqetitv agkvrirtrd akeetvpgis
       61 vvekgtkngt vtgvtgefsi rvknnatlvi tmvgyktrev pvtgatssfs llldedisgl
      121 kevvvtgfqq idktkfagaa vklkaddikm dgiadvsrml egraagvsvq nvsgtfgsap
      181 klrirgatsl tgtnrplwvv dgivledvid vtneqlssgd aatllassva glntndiadi
      241 yvlkdaaats lygaramngv vvintkkgrs gklqinyagt fssqlrpsyn nfnimnsdeq
      301 msvfseiyrk gyfnlgrign esdkgvfgkm ydmmqqvdpa tgkftlentp earraylery
      361 arantdwfrl lfnnsfiqeh tislsggtdk mqsyfsasfl ndngwtiadk vsrytfnaqt
      421 nynissklsa gfiasgsvrk qqapgslnrt adavygrmsr dfdinpynfs lstsramtay
      481 dqngnleyft rnfapfniin elqnnrvdls vvdvklqgnl gysitkhlry dflgairyak
      541 ttqedivnen snranayran ynatiaranr flyenpdfpn dlprvvmpsg gfynrnensl
      601 tnydfrnnit ytqsfgkhdl nvlvgqqvry adrqnafntg ygyqydyggi pivdyrivkq
      661 nvekglqyyg mnrlydrfvg fyttvdytfn kkynfkgavr ydgsnqlgks ptarwlptws
      721 vsgawnvdqe pfmkdiksis flklrgsygl taamgrasns sielrtvntv rrfsdeiesg
      781 ivirnlenad ltweknyaan lgvdasffds rlnvtldvyn kkgfdliadi rlagiggetq
      841 ktanyadlks sgfevtvgge ivrkkiwgws snvtmgynkn ritnakntpi ifnqvraegg
      901 nqegypvnsl fsldfkglep ntgvplfvne ggevgrdvnl qdretkylky egpvdptvtg
      961 gwannfryka ftlnvlftfq agnkirlnpv fkptysdlda lpkefidrwt lpgdeqktnv
     1021 psiidalnyn rigsaypynn ynyssarvad ggfvrlknia ltyalpaaii artglnnlsl
     1081 tasasniwll yadkklkgqd pefynaggva qplqrqvava lkigl
//
LOCUS       WP_095840469            1122 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            sp. MD30].
ACCESSION   WP_095840469
VERSION     WP_095840469.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga sp. MD30
  ORGANISM  Chitinophaga sp. MD30
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Chitinophaga sp. MD30"
                     /db_xref="taxon:2033437"
     Protein         1..1122
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124849
     Region          157..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkctlllag vlsvlcpdnt apaaaplsap arvvhtqprs iplpvllkti qqrhkvsfiy
       61 eesllkgkac tcdaartrre eveqyvaaii apmhlklkrf ndytyaiisa dtpddtalpa
      121 epipssgrsh qldkvsntaq agtyhvssad alqqrvvisg rivaeenedp lpgaivmveg
      181 tnfgttadee grftlrvpta rillikhigy epkeltlgdk rtdliirltg ksktltdvvv
      241 tgiykrpven ftgsakiita eelqrispqn ilaaiavldp afqmpeninl gsdpnrlpdv
      301 qlrgqnnfpv qsgrssnasl rsmygdkpna pmfvldgfev siqrifdldm nrvsritilk
      361 daaataiygs rasngvivid trqpkegavr vsyrgglqve apdlngydll nakeklqlek
      421 dagryistrf qgdqlnldee ynrrlkavts gvntywlsqp lqtgvgsths lyleggdnav
      481 rygvnlgyqn nvgvmkgsgr qnlsggvtln yrsnkllfgn dlsitsnkat nspygsfsay
      541 akmnpynkaf dlnahplryl dtswigytyn ylenpiynat igsrnnsqyl lftnnfrfew
      601 salswlrfng sfsftkstde sndfkpaaht sfdnvdfsqk gsfqkingks anynatlgfd
      661 irkmfgksll yvtgggnlne iknestgvta vgfpnakmdn iifasgyaan tkptgiqgis
      721 rlaslrmnin ysydnrylad fsssidassq fgtnkslapf wsfglgwnih reaflhnnrl
      781 inflklrasi gttgdqrfpp ymaittytya ndryylnqls aylmgygnpa lgwqkgfkrn
      841 igvdatlwqn rwslsadyyd nstndlildi stppslgfsg fkenvgslrn kgwqvstnvv
      901 liqrtrqeff wrigvsayhn tnkidkisnt lkklnsdndk fgndtekkqq lyprlrfeeg
      961 qsltalwgvq smgidpangq elfrrrdgty tytwdpndki vlgdtepkvs gtistgvdfk
     1021 gfsiniyimy rlgaqiynqt lvdrvenadi tynvdrrvse qrwrkpgdhs mykgitsspp
     1081 vayhnrylhl ptpppascrq kihwiaaayp patasringl kg
//
LOCUS       WP_095840736            1121 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095840736
VERSION     WP_095840736.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1121)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1121)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1121)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1121
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1121
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123543
     Region          136..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvlkkitgn drrerrvatr kyqrlrkimw isclsmqvyt aaygqqvtir kqqvavidal
       61 nsvkqqtgyy yvgqvellka tqpvdlqlvn aslettlqai fkdqpltwsl rdktiivkrk
      121 qdavfqstnv dkftsingei rntqgtplpg asillqgtqk gtaadanghf hldnitfpai
      181 leihytgyls kivrishsen iqvilepaeq qmnavivtgy sqkkiseltg slstvkgedl
      241 rnvttssviq qlqgklagli vsspggdpaa spnmsvrgvg slggntatqp lvvidgliqd
      301 agtaaninpn dvesvtllkd aasaalygsr aangvllint kkggspdgkp qinfeavysr
      361 eqptfgkfrm mnaderytlm eqaysndyrk qnptatpeav nnylsavmpd kaaalanntn
      421 wlregyrigq lqrynlsing gtnrfkyyag gsyhhevpva itdkfdkyql rvntvyspsd
      481 rftittafng tytkaissgl snyrgnlygm mpwdnpykad gtyrvggpne pnwysgtdty
      541 nplydaslqd aynhayiaga dvklqyrvtp wlslstanrl tynggrsgfy tdprdsasgy
      601 pggyysqnrs qqvnyitsni asfnkrfglh eikglagmef ndvrfentsv svrnitpgkr
      661 sittgtvdrv sesiseiafl sylseinysf ldryflsgsf rrdgsskfgs nnkfgnfysi
      721 gaawnisdet flannrtitq lrlrfshgts gnadpvgays iygvynyttg ggdnyngaqg
      781 iipgaqgdnp dlhwevqrmn nlglniglwd ririnidlyd kannsllrsv paaitsgiss
      841 vvknigkisn rgmeieitst nttgkvkwnt slnlafnrnk vlyltgvptv fpttgtnnll
      901 apgyavgsyw gvvytgadeq tglptyekev dgkrsrttdi kqatlrylgs qqpdcsggit
      961 ntitykdvtl silldfvsgl rltndlrgdi ygpneldgas vttnnvalpp gqrrwehpgd
     1021 vafapaatlv gyadargwft trflenasyl rirnvrlnyn tpkrwlsrih aqqlsvfvsg
     1081 dylytftgft gldpenggrn fenaskyiin rkltagvnlt f
//
LOCUS       WP_095840900             377 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Chitinophaga].
ACCESSION   WP_095840900
VERSION     WP_095840900.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40221
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miagilqekn gesrvslvpe vvkqlssqgi tiwveqdagr lawyndeayt qagavikpre
       61 iilqqaqlil siqvpdrstw eqlpagavii gvyqplyhag lmqqwaahgl tvfsldsipr
      121 ttraqsmdvl ssqaniagyk avllaasnys ryfpmfmtaa gsiapakvlv lgagvaglqa
      181 vatarrlgav vevfdtrpav keevmslgak fievegaada skaggyaveq svdylrrqea
      241 kiaestakad ivittaqipg kqapvlittd mlermrpgav ivdlaaatgg ntavsrnnet
      301 vihngvtvig hsslaatmpa dasklyarnv snflqllwkd nqlslnfedd ivrgacivhn
      361 gdilmerlkt vtlpgnv
//
LOCUS       WP_095841024            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095841024
VERSION     WP_095841024.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120417
     Region          28..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrclciils mlsmlyavss raqeiphisg tvkdtkgtpl pgisvrikgs ntgsitdpdg
       61 syllrkvptd avllfqgigy itreipaagk keinvalstd ekqlgeivvt gfgekrekkq
      121 lgyavtevkg ddirktnain piaalqgvvp glqvspgtgg pqatprflir gsasldpfkn
      181 qplivvdgiv mddqvvlpnr ggeqdfgnil kninnddias isvlkggavt alygnraang
      241 vimittkkgf sqkglgvsls htqswdqayk lmafqnqfgs gqttedfvaa gpdgipginp
      301 atygygfgpr ldgrqvrdin grivantpks dvlgiyqtgr yintnvgveg gnerttfrfs
      361 fsntdskgvt prnefkrnsf slrathkmgn avlldgnvay vrsntlnpnr asggnniiyn
      421 fsfgapanyd tdywmknyid ptkggrnttd pvsgiwytll edrqeqiedn frgnitarvt
      481 ltpwltfean psvnlfstsf ssktlgrdag fgggaytaet rrviqsrlkg nfnlsrqind
      541 felfgqfgae mnnsnrtgvr sytrsglkip rvyrisnsvd lpgaeeltpn eyrivsgffq
      601 asatwkgmlt lnvygrndwn stllypggag tysyfypgad vawvfteafk lpqfinygkl
      661 rtsyvyagng tdiyrtntgi fratdgyrdr dgntiqryey esrnlgnlnl iperseklet
      721 glemkffsnr lgfdftyykq ntknqiiplq vpresgvena linagnvqnq gielavygtp
      781 vkakkfswdv ylnytrnrnk ilslapgvtv vglesedgvr svayvggdyg tmiaaygfar
      841 yqardaqgka iesplngkrv lsstggflra anyaaglere vtlgstlpkf lgsirntfny
      901 gslslsfmld arfgglvysp synygsqlgq tvntlpgrtk dlggleyvna agakrddgii
      961 pdgvyadgtt itgldgnryn vsgmtyreay dkgyvrpira layynnsfnw fggireqsvf
     1021 enswvsvrdv svgydlptsi tsraklnalr ltlgarnlgf lykslpidln pddltssgsg
     1081 aafmgggtpy irsffvtvna nf
//
LOCUS       WP_095841217            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chitinophaga].
ACCESSION   WP_095841217
VERSION     WP_095841217.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117506
     Region          23..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkallffti flvsvslayg qqrqvsgkvt gsdgapipfa tvqikgtnsg ttadadgrfv
       61 lkvstgtvlk vsalgmedke itvgsgniva valnvsdvnl kevtvtgafg ikkaqrntsy
      121 ssqvigteql nvipqtnvnn alagkvagvq fqgqspmkld aqgflrirgg lglkdvdpiy
      181 vvdgtivgaf einpndiadv tilkganata llggrarnga imittkkgsk ggfgievnqg
      241 itfdkvyilp kyqnqyaggg vsslipfkye agmpdewkal dgksyldhtd daswgprieg
      301 qeyapwyawi pgtqytgkte rlqaqpnnvr dfyqtgitsn tnvaltkgge qynmrisytn
      361 qsvkgmlpgt sskrnalsfn gsydlnphft tganvnyttt nirgefdday snqsagnfsq
      421 wfhreldmsk lrelrglrnp tgtlagwngn npdsyldlgp tdywknnywy npyayfdnid
      481 ynqtrnrlfg dafltykfnd alslrgtirk dllttnrenk iksiiersgg qtgklasydt
      541 rlesydetny eliatynkki tdfdinvtag gniftreekt alqktsngli ipdlfaitns
      601 kdqpslenir rsyktnslfa sgefgykrii ninaavradw ystlpssgnr lispsvggtf
      661 ifselthnal pwlsfgkvfa swgkkpldlg fheanfsykl dqfqwgsniv mrtpnsfpds
      721 tlkgslitty eagfdvrfld nrfglnalyy nednnnaplp vtvggaggft trvvnaarvk
      781 rtgielllta kilqskdftw dvsksfsyll snkvvslynn vdriqldata fgtrfarafq
      841 qkgenwgqli gagikrnadg qplldpvlgt yvtdsekkwg sivpritggl tntfsykdft
      901 lafsvdyqvg gkffsltenf stfsglldvt astndkgknv rddvangggv hvtgvstadg
      961 ktpvdlyipa kryyqqyynn qiaepfihdl tfvklreisl gynlplrkwg vtnwvkgmyv
     1021 svlarnpwli yreaknfdps eisnnagesg qfpgtrslgf nvkfsf
//
LOCUS       WP_095865761             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhodococcus].
ACCESSION   WP_095865761
VERSION     WP_095865761.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37849
     Region          13..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqsasta rptigvvres ndgerrvalv pkivasliak gvdvvvesga glgalipdel
       61 ytgagakiad pwsadvivkv appsdeevgr lhagqtligf laprnqdnqv aalkaagvaa
      121 faveaipris raqvmdalss qanvsgyksv llaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrat gydvrpevad qvrsvgaqwl dlgidaageg gyarelteae
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvvvdl agetggncel
      301 tepgqtvvkh gvticsplnl pasmpehase lysknisall elmlvdgala pdfsdevlaa
      361 scvtreegvs
//
LOCUS       WP_095865848             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. ACS1].
ACCESSION   WP_095865848
VERSION     WP_095865848.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. ACS1
  ORGANISM  Rhodococcus sp. ACS1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhodococcus sp. ACS1"
                     /db_xref="taxon:2028570"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39163
     Region          16..378
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(28,83,102,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(57,135..136,145..146,149..150,153..154,156..157,
                     159..164,166,168..170,173,196..197,285..286,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,135,138,141,182..185,205..207,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(132..133,135,145,188..189,196,212..213,215..218)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(165..169,172,175,198,200)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mksnevssgs sqrclvgvpr essdgerrva lvpkivsali gkgvdvvves gagmgalipd
       61 elytaagaki gdpwtadvvv kvappstdei srisagtrli gflnprnadn riaeleaagi
      121 egyameaipr israqvmdal ssqanvsgyk avllaasest rffpmlttaa gtvkpatvlv
      181 lgvgvaglqa latakrlggr atgydvrpev adqvrsvgaq wldlgidaag eggyarelte
      241 derakqqral edaikgfdvv ittalvpgrp aprlvtaaav egmkpgsvvv dlagetggnc
      301 eltepgqtvv khgvticspl nlpasmpehg selyaknisa lielmlldgg agegtgkvpv
      361 lapdfsdevl agacvtreek ga
//
LOCUS       WP_095869319             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. ACPA1].
ACCESSION   WP_095869319
VERSION     WP_095869319.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. ACPA1
  ORGANISM  Rhodococcus sp. ACPA1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus sp. ACPA1"
                     /db_xref="taxon:2028572"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38129
     Region          13..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqsasta rptvgvvres rvderrvalv pkivasliat gvdvvvesga glgalipdel
       61 ytevgakiad pwsadvvvkv appsdeevgr lhagqtligf laprnqdnqv aalksagvqa
      121 faveaipris raqvmdalss qanvsgyksv llaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrat gydvrpevad qvrsvgaqwl dlgidaageg gyarelteae
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvvvdl agetggncel
      301 tepgqtvvrh gvticsplnl pasmpehase lysknisall elmlvdgala pdfsdevlaa
      361 scvtrdlegh
//
LOCUS       WP_095882151             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Alloyangia
            mangrovi].
ACCESSION   WP_095882151
VERSION     WP_095882151.1
KEYWORDS    RefSeq.
SOURCE      Alloyangia mangrovi
  ORGANISM  Alloyangia mangrovi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Alloyangia.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Alloyangia mangrovi"
                     /db_xref="taxon:1779329"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55597
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpteif egearvamtp dsalqlqklg ydcliqsgag akagfadaay eaagvtvvad
       61 aaalwaqadi iakvrppsee evahltpekl lisffypasn ealmkqaadl gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aqfvyldfee eqadgassgg yasvsspefr
      241 eaqlakfrel apemdivitt alipnreape lwtedmvkam kpgsvivdla aerggncklt
      301 vmdqkivtdn gvtiigytdf psrmatqssa lyatnirhmm sdltpgktdg tvvhnmdddv
      361 irgatiahak dvtfpppppk tkaiaaqkpk ektpeltpeq kraqevaafk aqtkqqvtll
      421 gvgavlllav glvapasfmq hfivfvlsvf vgfqviwnvs hslhtplmav tnaissiiil
      481 galmqigsgn wlviilaals vfmaginifg gflvtrrmla mfqks
//
LOCUS       WP_095893250            1121 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Capnocytophaga].
ACCESSION   WP_095893250
VERSION     WP_095893250.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga
  ORGANISM  Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1121)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1121)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1121)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1121
                     /organism="Capnocytophaga"
                     /db_xref="taxon:1016"
     Protein         1..1121
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124458
     Region          26..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgkflkhil imslcfflqg vfaqekevsg vvtssddgmp ipavsvivkg tnrgvatdfd
       61 gkytikaneg eilqfislgf ttvekkvtgg gksliinalm keeanqleev vvtgyggtre
      121 kakltnsiat vkaevlekgs fsnpaqalsg avaglrvaqt sgkpgsiptl ilrggtnlng
      181 sgsplvivdg qvrgglndln pndiesmdll kdagataiyg aranngvilv ttkrgkvgss
      241 smnlrikhsf dymnrqhefl dardylhwqr tavyntsriy qladgtwkgy snanslnnvg
      301 pygignlhfh prtgelidpn vysqavwspm llerlsdsqk qtllgegwqt mmdpvtgkei
      361 ifsnfdrsst afrpfaltrd ytfsmtggne kgkyyaslgy fnqeglpvkn wykrlngtln
      421 aeyqlrpwlk sissfsiaha twnnningmg ddryfgrmls apptqkeyvd gqlvlgrdvq
      481 dgnpwiydgk firknntdkf nlgqsfkvdl lkglsftlng yvmfdegvye sfdkdyldrp
      541 nsinktrsss asfgrtirqt yngilnykvs lgshnldama gyeyydnyhm gfsatgegap
      601 tddfmdlslt lseegkrrid snhsnnriks yfgrlnydyd gkyilsltlr sdgysslidn
      661 rwgtfpgvsg gwvitkedfv sdsfknilsf aklrasfgln gnasgigpyd lqgsyrtgky
      721 kgetgfhlgd lpntglrwek srtfevgadl mflenrlstn itfydrlted kyaniglphs
      781 sgitairtnn gafrnrgief eanfkainke kmkwdiglni thnkntvikl pnnglernrq
      841 gafevydgtt gnkiwvggyq egqtpgdlyv yealgiykne eeirqlannl idesiggygs
      901 dnkklygpaa wealseaeks askvkhlpiq pgdviwkdvn gdgkidqfdk vkvgnifpkf
      961 tgginttfsy enirlsarmd yalgfkqlis eigslpwfma naqgsfntvt evkdswtpen
     1021 pnakypryvw adqlgkrnyt rdtsmfvyeg sylafreisl ayafdsdlck slslnglevs
     1081 ltgqnlgylt qskayspeal grtannyplp rtviiglnlt f
//
LOCUS       WP_095893563            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sp. H2931].
ACCESSION   WP_095893563
VERSION     WP_095893563.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. H2931
  ORGANISM  Capnocytophaga sp. H2931
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Capnocytophaga sp. H2931"
                     /db_xref="taxon:1945657"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120844
     Region          24..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrgkliwtls lfffalqfvf aqektitgmv kdesgqpllg vtvtikgttr gvatdfdgny
       61 sikakagevl hfvalgmkpi drpvsasttk idvimeeeah eleevvivay gtakkqslvg
      121 sqamvsakql etrpitnlta alsgiapgvq vttssgqpgs ssdirirgfg sinagsdpiy
      181 vldgsiyrga isdipshdie nisvlkdaas tslygssagn gvvlittkkg sskakntpii
      241 tytnnigfsk egqehyetvg amdyyplrwq qwfneykysr kytdeqaaaa ankdvldafr
      301 yqpyagiksy yqydstnnmw nltttptstd sypalvladg klnpeitgll wnddldweka
      361 lyrtgvrneh nlsvnyatdk lksymsvgyi deqgyriksd yqrisgrlnl dydvrkwlsv
      421 gsnlaytnrk snsptatggq lsntfsfirt iapiypihrh nddgsymidn kgnkvfdysk
      481 drpfrpnfnp illseldlla sdnnsfvsrs yaeikvipel kfrasyshdl lqyttreryn
      541 nvlgdqpdgl feiynyknst ttfiqsleyd kmfnkhhfnv llghesfdyk rysntsskkg
      601 vvfpgvdels nykdpaslts vtdrytkegy fgrinynysd lynlslsyrr dgtsrfhpdh
      661 rwgdfwsaga gwhvknqllk evkwidrlkl rasigqtgnd avssyyayqt tysivrnged
      721 lglrignyan pnlvwekqqs tdialefgff drleaslelf dkrskdlifs fplptstgvg
      781 sidknigqir nygieadltf hifksrnfrw ninvngtvlk nkvlelpehn rkegiesgyh
      841 kylegssiyd yylrkwagvn pddgfamyvi daerypdkad pnspnfegid ktgerakytr
      901 nadiakkefa gsaipdlygg istnlswkgf glnmhfsyqi ggkgfdggya slmgrslsgg
      961 nalhvdmkka wtkegqvtdv prldsghygq fdshsadrfl vsrtalmlkn vsltytlpsd
     1021 lvkkldvsni rigvsgenlf lwskrkgfnp msnyggvtgl nsynyakivt csflisl
//
LOCUS       WP_095893569            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sp. H2931].
ACCESSION   WP_095893569
VERSION     WP_095893569.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. H2931
  ORGANISM  Capnocytophaga sp. H2931
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Capnocytophaga sp. H2931"
                     /db_xref="taxon:1945657"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114480
     Region          24..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkliwtms lfffalqftf aqektitgtv kdesghpllg vtvtvkgttk gvatdfdgny
       61 sikakvgdil hfiglglrsv dksvqasttk idvvmeeeve qleevvvtam gvsrdekslg
      121 yatqkvdgdq lskagqqnai salsgnvagv qvtasssmgg stritirgig svtgdnrpli
      181 vvdgipmnns nynssslggr dygdasadin pddiesvtvl kggpatalyg srggngvivy
      241 ttksgkkgkt svdvksgitf estyiapilq nrygggssdk fqtvningkd ynvaeystde
      301 swgpkfdnqp ylpwyafdke afpndylkev pwkasendvd sffrtgvtts nsvsitrsiq
      361 atnlrlsast aktegivpns hlkkstlsfn fgsklsekfk vdgglnyvft ngfnrqdqgy
      421 ndnsvaqkfy qwgqrqldmk klrdyknpit geqrswnrva wddptplysd npywiayent
      481 aedkrhrffg nvgvtynitd klyavgnvyg dvysfaikeh vaigsqaqsy ftsinrnssd
      541 fnyearlhfd pkignnfsin sfvgvsrrea rynyvhgttv gglvkpnfyn lanstaiprg
      601 snyeswrrtn svygmvslgf kemlfveatg rndwfstvsk pvfypsvtgs fvfssvakad
      661 wlsfgkvrlg waqvgndtgp yrlethpvvs dsflgasrya npttentpnl lpelkttqev
      721 glelklfrnr vgldityydt kikdlilplt tdpstgyayk ylnagsmqnq gievslsatp
      781 vktddfswdv twnfaknnnk llelhpqmkv yqlasffsst ilnavegety gqlyttnykf
      841 hegtgqpivg snglyvkgnv eslgsiipdy nmglnntfry knfdlsvlfd fqkggkyfst
      901 nhmfgmysgm lketaegdir eagvvlsgvt adgqpnttka dvaawgashy tgvraqsvfd
      961 atylklrnis lsytvdlpkn khikelvlsa ygrnlwttgl dykgfdpeqa sygsgnvqgi
     1021 dtgslpstrt ygmsvqikl
//
LOCUS       WP_095893646            1120 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sp. H2931].
ACCESSION   WP_095893646
VERSION     WP_095893646.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. H2931
  ORGANISM  Capnocytophaga sp. H2931
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1120)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1120)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1120)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Capnocytophaga sp. H2931"
                     /db_xref="taxon:1945657"
     Protein         1..1120
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126722
     Region          25..1119
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqsmikkll ytifllcsqw amaqqeikgt vvdnqgmpll gatvivkern vgvttdidgk
       61 fttkaengqt lvvsyigfqt qrvkitastm hivlkedvqe ldavvvtgyq kiksrvftga
      121 sasvkmeqvk mdgvadvsrm legrvaglsi qnvtgtfgsa prinirggas iignvqplwv
      181 idgavyedlv sltldqlvsg davtlissai aglnaadied iqvlkdasat svygaralng
      241 vivvttktak rdtpnritys yeqsfrqips ykdydllnsq etmsvyqela nkgyfslrda
      301 lygrrsgiyy qwykgistin pntgtyyyen tedakraffk ereyvntnwf nhlftinpiq
      361 qhtltfsggg kntttyaslg lfndkgwtit drvqritanl kstffitddf kttlsvqgnm
      421 rnqkapgtft qrknttigsf erdfdinpfs yalgtsrtlr prtndgkley yrnnwaafni
      481 lneyennyld inlldfkiqa easykinkdl eatallstrq astssahfik epsnvvqafr
      541 anetpwvaqq niylikdkdn plsqpkiglt hggifnktet tlksyqarma ldynkslgeh
      601 dikafgfaem ryadrtvnpf qgygiqydkg nqiftnplif qklidegndy fawlerydrg
      661 ltfslsgtyg ykgkyifntv lnyegsntag knsrsrwlpt wnvggkwnid qedfmkdqky
      721 fstlafrlsy gltakmneqa insnavyknv ilnrfhfkdr enalrilhle nrdltwekmy
      781 elnlgidagf fnnrlnatid iyqrnsfdli dlirtsgvgg qyykyanfgd mrtrgvelal
      841 nskniltddf kwttnftisy mnqkitrlln tpntfdmvag agrgnivgfp kgslfsfnyq
      901 glnnyglptf dfglyplndr aygniagadf ldaqysksyl iyhgsiepnv ngglsntfsy
      961 knwefsffvt aqagnkirln psfdpafadl nvfsteyydr wiapgdewrt evpalpsqdl
     1021 irligqenie kayntynysq nrvadgsfvr mknislgynv pesavkrykm kslnvrgqit
     1081 npfliysdsr lkgqdpeyyr sggvslptpk qftltvnvgf
//
LOCUS       WP_095893693            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Capnocytophaga].
ACCESSION   WP_095893693
VERSION     WP_095893693.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga
  ORGANISM  Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Capnocytophaga"
                     /db_xref="taxon:1016"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114201
     Region          26..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfltlfa fvfswcltls aqmvsvkgtv tdegkvplpg vsvliknttr gvatdfdgky
       61 eikanrgdvl vfsylgfvtq ekiigggnsl tinvllveea eqlgevvvta lgikrekksl
      121 gyalqevkgd alveaketnl anafsgkvag lqivrgsngp aasskivlrg nnsltgdnqp
      181 livvdgvpmd nftgasnndf wnptndmgng lgdlnpndie smsvlkgpaa aalygsragn
      241 gvilittksg kareglgity sssigfenvf mkpdvqnvfg qgadgnydpl sasswgpkie
      301 gqmvedwkga riplrvhdnv egflntgvdv qhsvsfqqqv tngtsiyssl thvdnqssip
      361 gatlerlnli sraisrfgkd ekwttdfkvq yinskvknrp iggqrdinvf nsmlnlpvtv
      421 dvtefsraid dygnhiwynt sglnpfwlak yntnedsrdr fmmngsvkyq ftdwlnaevk
      481 ggtdlyttnv enktygkssl tttgryslgk dtfnetnlsf lfsaqkndlf gkvgmaatfg
      541 gnlmkrhssg lsidagelev pnlfvvtnsk gnpgvsqhyr mhkinsfygt yqinynqyaf
      601 lditgrndws stlskanrsf fypsvstslv fsemlekeyd ikpewfnygk irasyavvgn
      661 dmgpyqlynf ykigkdpngn ttattndvly nsnvknelik sweigvdakf fnnrlgidls
      721 fyksnatnql lniplnsmsg ykamkvnagd ienkgfelml tgqpirgekf swdmvvnask
      781 nintvnslve gsepvtqygl gtfdniqila msgerygviy gtkfvrvedi asphygriiv
      841 dehgapkgtg ekyilgnqqp dfllgftntf tyknlslsil vdgrfggkif sgtnhglkts
      901 grsaatvvng eradivyngv vesgngyqen tkaispqdfw vnrmasrtgn lgiteenlfd
      961 atnirirnlq lnyrlpddwv kglgaqsakv gmsvnnvvml ksylngvdpe svfatgtnav
     1021 gyenfssptm rsyyfnvtvs f
//
LOCUS       WP_095894429            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sp. H2931].
ACCESSION   WP_095894429
VERSION     WP_095894429.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. H2931
  ORGANISM  Capnocytophaga sp. H2931
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Capnocytophaga sp. H2931"
                     /db_xref="taxon:1945657"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113964
     Region          25..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkflvtfv ltmvfcfhwl yaqnrtvsgv vtdesgipls gvsvlvkgtt rgvstdfdgk
       61 yniqaqaeei lifssmgfvt qekkanvtkl nvmlkedaee leevvvtalg ikrsekalgy
      121 alqeidgtkl leardanvtn alsgkvsglq ivkgaggmag sskivlrgqn sltgdnqpli
      181 vvdgvpidnk asgaadiwgn sgmdmgngls dinpediesl tvlkgasaaa lygsragngv
      241 ilittksgke kkglgitfst tlatedifvk palqntyaqg vdnlydpkta rnwgpriegq
      301 tvtnwnnkqv kleaydnmnn ffrtgitatq vlsfqqqink tsvygsvnym dntsmvpetd
      361 mnrtsmalrt ttnlgasdrw kvdfkinyvn tqahnrpiqg lnqsnvfktl tifprtldir
      421 efnppivngq qvwydtqtlp ddnpwwtlky ntnndvrnry isfgavtyef tnwlrgevkg
      481 gldyyntkmy qrkhsgslsv pkngqyaeas kefseknlsf lliaeksdll kdlngtltfg
      541 gnlmsqhise mnaksgdlli pnifslnngk ekptvtslit qrkmnslygs aqigwknsly
      601 ldatfrndws stmskvnrsy fypslsfsgv iselielpew vtfakvrasy aevgndlepy
      661 mlynsysvak dywgvptist neilydhsvr selvksyeag ldlrlfnnrv rldaavyktn
      721 amrqllrlpm detsgykfki inagnienkg velslgvgil qnpeglnwdt tvnfsknenq
      781 iidlypgvas yelltvdeim vlaevgkeyg aiygsairrv ndansphngk miltaeglpq
      841 rdavalhylg nqqpdyllgf snsfswkgin ldflvdarvg gkmfsmtrnl ltgygmaaet
      901 avdgkrdsfv vegvianssg gydvntkqvt pqrywgalaq nnigiteanm ydatsvrlrt
      961 lslgytfgkk hlesigiqnl kcsftannlw lihtnipgid pesvsgtgtn vtalefgapp
     1021 tsrtftfnit igl
//
LOCUS       WP_095894996            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            stomatis].
ACCESSION   WP_095894996
VERSION     WP_095894996.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga stomatis
  ORGANISM  Capnocytophaga stomatis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Capnocytophaga stomatis"
                     /db_xref="taxon:1848904"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113126
     Region          48..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 minllrksgr agtrwillal ltqgfwtvsa sekieatstd ilvqqqtkkv sgtvtdasgv
       61 plpgvsvlvk gtsvgvatdf dgnfeinvpe dktdlvfsyi gfkeqtikvs ksqsglkivl
      121 qeevmelegt vvtalgikrq ekalsynvqq vksddltkvk etnivnslng kvagvniqrs
      181 ssgvggatkv vmrglksldg nngvlyvidg vpmfnrqkdg agafgrpagg esiadlnped
      241 vesinvltgp saaalygsea angvilintk kgkegkmevn lsssvelvtp tllpdlqdty
      301 gsvgqkswga kldapsgynp akffntgtni tnavtlstgt kqnqtfvsma qtnsggvipn
      361 ndyyrynvnv rntssflndk lhldvsgsfi rqgnrnmisg ggyfnplval ylmprsvdyr
      421 dveiyeryna ergiyekyqp ypeqvgsyfs enpywvvnre lflfnkkrym msaslkydil
      481 dwlnitgrvr ldndygvnee kfyasttnfl vgwatelgph nkgrysinns kdeqtyadim
      541 lnanksfged fsltanlgas yndrystsvg gsgilinvpn lfsaanfasq hsgvgqsygr
      601 nknvaifasa elgykgmlyl sltgrndwss qlvnskepsf fypsvglsgv itemtklpdf
      661 vdylkvrgsy tevgspiskt gltpgtiths lnssglianr vypypefkae rtrslefgln
      721 gkffnnslsl dltlyksntf nqffeqelsa ssayskfylq agnvenrgve lalgfnkela
      781 kdfnwstslt ysrnvneike lvrgyknpft geifdikevr kggsilregg smadivvkgv
      841 llrdvngdli eeaaqfkfdt tqeirlgrst pdfqlgwkhs faykgfdlnv lfngsfggvv
      901 lsgtqpylda ygvskisada rdaggvwvng kqydtekyyn tiqnlpgyys ydatsvrlqe
      961 aslnytldgk visdkikrit fgiigtnlwm iynkapfdpq ltfgvgtyas telfmtpamk
     1021 tygaslkiqf
//
LOCUS       WP_095894941            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            stomatis].
ACCESSION   WP_095894941
VERSION     WP_095894941.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga stomatis
  ORGANISM  Capnocytophaga stomatis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Capnocytophaga stomatis"
                     /db_xref="taxon:1848904"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113582
     Region          23..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrrvlcllv lfiasfplfa qvktvtgtvt deagsplpgv svliqgtkkg tstdfdgnyt
       61 lqvneggvle fsyigfttqt kkvtgggnsl kinvvmkeqa eqlgevvvta lgikrekksl
      121 gyalqevkge alveareani anafsgkvag lqivrgsngp agsskivlrg nnsltgdnqp
      181 lvvvdgvpmd nftgasnndf wnpsndmgng lgdlnpndie smsvlkgpaa aalygsragn
      241 gvilittktg kareglgity sssvgfenvf mrpnvqdifg qgedgvydpi sfsswgpkie
      301 gqtitnwdkk kiplrsydnv nsflntgidi qhsvsfqqql kngtslytsl thvdnestip
      361 gstlerlnli travsrfgkd nkwttdfkvq yinskvnnrp ingsrkdnpf stlinlpstv
      421 dvsefssgin sngyhiwfhp kdglnpywat kynlnsdsrd rfllngsvky eftdwlnaev
      481 kvgtdlyttn lenktygkgp ltatgrysig kntfnetnms fllsanksnl fgkvgmaatf
      541 ggnlmsrkht gmgitvgele vpnlfsvnns vgtpsvsqdy kqhkinsfyg tyqisydsya
      601 yldftgrndw sstlskanrs ffypsvsasv vftelldkef sakpswfdyg kirasyaavg
      661 ndmgpyqlyn yyvigsdpng nttgstnsvl fnpnvkneli kswevgletk mfnnrvgvdl
      721 sfyksnatnq llniplnsms grtakkinag dienkgfelm ltgqpirnen fmwdmnlnvs
      781 knintvnelt egitqyalgg fenvkilast gerygaiygs kfsrvedtas phygriivda
      841 ngipeaaegs fylgnqqpdv mvgftntfty knlslsvlid grfggkifsg tnyglkasgr
      901 sdvtvvngdr adiiyngvvs dgqggyaent kavspqifwt tlagksnrnl gitednlyda
      961 tnvrirniql nyklpdswak afraqnakvg fsmnnvvmlk shlngvdpes vyatgsnavg
     1021 feyfsaptmr syyfnltisf
//
LOCUS       WP_095894993            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            stomatis].
ACCESSION   WP_095894993
VERSION     WP_095894993.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga stomatis
  ORGANISM  Capnocytophaga stomatis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Capnocytophaga stomatis"
                     /db_xref="taxon:1848904"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113749
     Region          48..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 minllrksgr tgtrwillal ltqgfwtvsa sekieatstn ilvqqqtkkv sgtvadasgv
       61 plpgvsvlvk gtsvgvatdf dgnfeinvpe dktdlvfsyi gfkeqtvkvt ksqsglkivl
      121 qeevmelegt vvtalgikrq ekalsynvqq vkseeltrvk danfvnslng kvagvniqks
      181 ssgvggqtkv vmrgaksilg gnnvlyvidg vpmgentnre rgdqrfgtpa ssegiadfns
      241 ediesisvlt gpsaaalyga aaangvilin tkkgkegkmk vnlsssvefs nplilpefqn
      301 tygtsdsffs wgnkldtpss ldpkkffnvg ttynnalnfs vgnkqnqtfv sassitsegi
      361 vsnnqyrrhn vlirntssfl ddkleldvsa syvrqfeknm isfgeyfnpi vgvylfprge
      421 nfewmksfel ydiekgynai qnripgdlgk dvqnpywimy rnirpkvrdr ymfsgqlkyn
      481 ilknlniagr vrldntysks edkryagtlg afakekgrya ysqgtfkqky adlimnynts
      541 faddfnlvvn agtsfedydn kgksyrgeik hiankffian tdtstavvsd eggndrrrni
      601 avfasaelgw ksalyltltg rndwasqlvn sdeesifyps vgvsavitel lspetknkly
      661 pylgfakvra sftevgspis vtgitpgtit kkieggsika ndfypltapl kaertrsyev
      721 gistkwlknr lsldvtayks ntynqlllag lpkssgyqtm yvqagnvenk gleialgynq
      781 evtdfnfgtn vtatanqnki irlasgipnp fdasspidit emtvgnfylr eggsigdiya
      841 ndwikrdqyg lvdissgtia teatepymlg svnpdwllgw qgnlgyknls lnflfkarlg
      901 gvvvsktqqa ldyygvskas adardlgyaq lgsfkvdpra yynaintlda yytysatnvr
      961 lqevsltysf pkqalgktfs dlsislignn lwmiynkapf dpelasttgt fgqgydyfml
     1021 pslrsyglsi kmgf
//
LOCUS       WP_095896005            1096 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            stomatis].
ACCESSION   WP_095896005
VERSION     WP_095896005.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga stomatis
  ORGANISM  Capnocytophaga stomatis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Capnocytophaga stomatis"
                     /db_xref="taxon:1848904"
     Protein         1..1096
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123146
     Region          20..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkglvllff lltafgwaqk nvegvvkdhq gmpiigvnvv vkgtkkgvst gfegtfgltt
       61 nvgdvlvfsa igyktqevki tkkgsfisvv meedlmemee vvvtgyqtvd ptkvataytk
      121 idtksferrg tadvisgieg lsaalvlstn pnnptgskef sirgistlsg dtrplivldg
      181 fqyggrledi npyevesitl lkdaasasiy gakssngviv ittrkgragk tqvrytsnlt
      241 fqdkmdvnym lnrvsssklv diehqyaken dnniinyrhl letndpymsy yvgntnrvyh
      301 lyglkkygyi teqdfdsqla qlrlydntkd ierlylqnpi tnqqnisvsg gsesfkfrss
      361 lnytnslkdv knnatqriif dfvsnlkfsp kvnldfqtsl tsnddsykli dyeniglsss
      421 ddifrvasyd rlfdengnpl svfrpadgsg tnsgglfggk dpyeiqrlva aglldetyyp
      481 andfgkysln etnwsahvqg llniditpdl takiggqirk gafkttriaa tdswfmksli
      541 nnttplyysg dtrslnvpyg drikesrges inylfrtqle yqktfgehni hlfagaemqe
      601 tksestqidr lgydpksnly lptdydrlrn dinsvyhpng sisgginfse gfgysqnryv
      661 agyanftymy tnkyvlsgsi rmdqsnlfgt dpryrykpfw slagrwrlge edffknknir
      721 advrlsygin gniankygpf diarkifdyr agniltlgiq nlkvnnlrwe rsettnfgtd
      781 lsffdnrlel vldyyykrti dalakvdsdp tfgsnlvyrn daslinngye vmltsrnirt
      841 pntlwetqlf frynkskite asfdtsqgka yrfagqvlni kgsepnslyv fdyegvsdtg
      901 egqirkadgn ivkvdysydp pglfnyddlk pvgtvvpkyv asvnnnfsyk giglsflfvy
      961 qgghimmkds yngsttayti tlmnkdaert wqkpgdeavt diprfssaly sgiikgstkn
     1021 vlpadfirlr dvvlsytvpt sllgglkiqe ltfnvraanl wmwtknnegi dpetqglgfr
     1081 tarlpksytm ginlif
//
LOCUS       WP_095896058            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            stomatis].
ACCESSION   WP_095896058
VERSION     WP_095896058.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga stomatis
  ORGANISM  Capnocytophaga stomatis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Capnocytophaga stomatis"
                     /db_xref="taxon:1848904"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112540
     Region          30..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mevnnkktlk wfglvlffcv fiqtalaqnr litgkvvdef giplhnisvt vkntmrgvet
       61 dyngmyriea kdgdvlifyi lgmekqehkv kpgiqtidve mvleineled vvvvgygsak
      121 kvstlvgsvv kidrtqvsnk psanlldalq gkvaglsifs nsgepygmgs irlhgigsly
      181 gggdplfild gspvskkvvi mmnpsdfesv svlkdasats iygtraangv iyittrngkn
      241 rqtpvisiss qygfsslasr kffddimnvd eyayylvdkg ymtqeevdal lrenpystrw
      301 drvyfrnnvp nqqidvsasg ggektnyyvs gsffnqeglm yrsgfkrytg rinlrtsltd
      361 wldlnlsvsa nygeymqnpy vggmnasygs lsilsppiyt pvdgngkryd yipglevphp
      421 nyiadnhpak tknmnfipqi sfivnpienl tiksqigvey insigydfiy psyiqrdnei
      481 slssskqkah tsrtsgenii ktftntaeyv hningnnrft fllgqesvsy dnshflaisk
      541 gqtsdratml shgtsdkdvg dgrsvstyns ffiradyghn nkyffdisar rdgssrfgkn
      601 nryanfwsvg mlwklkeekf lknsswiddl dlkfsvgtsg nsnalsdyas lslvlnnqsy
      661 kdlpgyllsg agnpdiqwqk qlkttlavtl gmfkradltv evydrvindm lgfvprpsfs
      721 gsegivengg kfqnrgidat lavsvvkgkd fyvtpflsln ynqekilelh nnlpyiigeq
      781 tpvsfvvgep llyfypifwr vnpedgysqw ylpgkdliht nidansvtnt fdaialrqnt
      841 gikrnppfng gfgldaaykn lslrvafafs sgkytinsdr yftenpvgti sfpdsnqsrr
      901 vldnwkkpgd vatfpayehg lpfteydsrl iedasfirmk dltlsyslpq kvlnqigffk
      961 dirvfgtgrn lltftkysgl dpefdtsags aganpgtkey tfgieikf
//
LOCUS       WP_095896133            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            stomatis].
ACCESSION   WP_095896133
VERSION     WP_095896133.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga stomatis
  ORGANISM  Capnocytophaga stomatis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Capnocytophaga stomatis"
                     /db_xref="taxon:1848904"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115239
     Region          24..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkekliwtvs lfflalqfaf aqdktitgtv kdvsgvplpg vtvmvkgsar gvstdfdgny
       61 sikakngdil hflgiglksv dkavsastsk idvtmeeeae qleevvvtam gvsrdekslg
      121 yatqkvegdr lskagqqnai salsgnvagv qvtasssmgg stritirgvg svtgdnrpli
      181 vvdgipmnns nynnernlgs dlggrdygda sadinpddie svtvlkggpa talygsrggn
      241 gvivyttksg krgktsvdvk sgitfestyi apilqnkygg gsstsfpeve ingrkysiaq
      301 yrvdeswgpk fenqlylpwy afdkenfpdd ylkevpwkas endvdsffrt gittsnsvav
      361 trsvqatnlr lsastsktdg ivpnshlkks tlsfnfnskl sekfkvdggl nyvltngfnr
      421 qdqgyndnsv sqkfyqwgqr qldmkklrdy klstgeqrtw nrtawddptp kysdnpywia
      481 yentsedkrh rffgnvglty niadnlyavg nvygdvysfh vkeqvavgsq aesyfkdivr
      541 nssdfnyear lhfdpkmgdn fslnsfvgvs rrearynyvn getvggllkp nyynlansie
      601 tpkatnyesw rrtnsvygmv slgfkemlfv eatgrndwfs tvskpvfyps vtgtfifssv
      661 ikpewlsfgk vrlgwaqvgn dtgpyrlety ptvsnpflgs prysnpntan npnllpevkt
      721 tqevglelkl fknrvgldvt yydtrtkdli lplttdpstg yaykyinags mqnqgievsl
      781 satpvktdnf swdvtwnfak nnnkllelhp qmkvyqlssf fsstilnave gepygqlytt
      841 nyrfhegtgq pivgsnglya kgkveslgsv ipdynmglnn afryknfdls vlfdfqkggk
      901 yfstnhmfgm ysgmlketae gdireqgivl sgvtadgqpn tiaakatdwa ashysgvraq
      961 svfdatylkl rnvslsytvn lpknkhvkel vfsaygrnlw ttgldykgid peqasygsgn
     1021 vqgietgslp strtygmsvq ikl
//
LOCUS       WP_095896646             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            stomatis].
ACCESSION   WP_095896646
VERSION     WP_095896646.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga stomatis
  ORGANISM  Capnocytophaga stomatis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Capnocytophaga stomatis"
                     /db_xref="taxon:1848904"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110006
     Region          25..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmklrlilif vlflgalhss faqkimvsgt vkdengvali gatvaikgtr igvatdfdgv
       61 ytigldagqt lifsfigtqt qehkitksnn alhivlqyea ealddvvvvg ygsakkigtt
      121 igsvakvagk dlaesptpnv ldalqgkvag ltinatsgkp gsapivllhg lgtlsdvnas
      181 gkdglgstpl yvvdglpvdd glvaslnpdd fesvtvlkda satsiygara aygviyvttk
      241 kggfeqptev svssqigfsq issykfydnl ltsseyvdym ldlghlpnkd vadifrqqyk
      301 gntrwdkiyf kpnsltaqnn vsvmgggkkv syyfsgsnfk qggnrygsdy eryslranid
      361 srikdwlsag lslsvghsis tsnggnrgny ggvmalpiye aydeegrlvd yvttiygnrf
      421 ylpqytaskl lsnggntniv pnfyvtlkpi dnlifktqag lqysvsvgen kilpsydqsg
      481 gigqvsrtfg ehinktltnt leykfrigdk sfftallgqe svsndskgfs asssgqvadg
      541 lttllqgkke prvgdsrdvs tynsffsrvd ysydgryfid fsgrrdgsst fgrnnryanf
      601 wsaglmwnak neaflkdvsw ldelrfkist gtagskggag sygsysrldf gqyreqasyh
      661 lsnlgnpdlr wekqdkttig mnlglfnrvk levdlyqrvi rdmyytlplp misgfgrypt
      721 nlaklqnrga dvtlyldvik dtknklyvsp yvnfnyndmr ilelfvgnqq ipedeystgy
      781 evgsqlmifa pifkrvnpdn gdpewyvpge dkmktttddt qittkfdrvt lnqntgktay
      841 apwnggfgln asykglslqm gfafsygkyq anqdryhtes ssafaynvsr eslnywkqpg
      901 dnvslprkel qfvqydsrll edasfirlkn invgyslpke vmetipffth lrffatgrnl
      961 ltftnytgad pefgillsqg gypntrqytf gvefkf
//
LOCUS       WP_095896737            1120 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            stomatis].
ACCESSION   WP_095896737
VERSION     WP_095896737.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga stomatis
  ORGANISM  Capnocytophaga stomatis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1120)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1120)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1120)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Capnocytophaga stomatis"
                     /db_xref="taxon:1848904"
     Protein         1..1120
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126799
     Region          25..1119
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqsmikkll ytifllcsqw aiaqqevtgt vvdnqgmpll gatvivkern vgvttdidgk
       61 fttkaengqt lvvsyigfqt qrvkitastm hivlkedvqe ldavvvtgyq kiksrvftga
      121 sasvkmeqvk mdgvadvsrm legrvaglsi qnvtgtfgsa prinirggas iignvqplwv
      181 idgavyedlv sltldqlvsg davtlissai aglnaadied iqvlkdasat svygaralng
      241 vivvttktak rdtpnritys yeqsfrqips ykdydllnsq etmsvyqela nkgyfslrda
      301 lygrrsgiyy qwykgistin pntgtyyyen tedakraffk ereyvntnwf nhlftinpiq
      361 qhtltfsggg kntttyaslg lfndkgwtit drvqritanl kstffitddf kttlsvqgnm
      421 rnqkapgtft qrknttigsf erdfdinpfs yalgtsrtlr prtndgkley yrnnwaafni
      481 lneyennyld inlldfkiqa easykinkdl eatallstrq astssahfik epsnvvqafr
      541 anetpwvaqq niylikdkdn plsqpkiglt hggifnktet tlksyqarma ldynkslgeh
      601 dikafgfaem ryadrtvnpf qgygiqydkg nqiftnplif qklidegndy fawlerydrg
      661 ltfslsgtyg ykgkyifntv lnyegsntag knsrsrwlpt wnvggkwnid qedfmkdqky
      721 fstlafrlsy gltakmneqa insnavyknv ilnrfhfkdr enalrilhle nrdltwekmy
      781 elnlgidagf fnnrlsatid iyqrnsfdli dlirtsgvgg qyykyanfgd mrtrgvelal
      841 nskniltddf kwttnftisy mnqkitrlln tpntfdmvag agrgnivgfp kgslfsfnyq
      901 glnnyglptf dfglyplndr aygnivgadf ldaqysksyl iyhgsiepnv ngglsntfhy
      961 knwefsffvt aqagnkirln psfdptfadl nvfsteyynr wvapgdewrt evpalpsqdl
     1021 irligeenie kayntynysq nrvadgsfvr mknislgynv penvikrykm kslnvrgqit
     1081 npfliysdsr lkgqdpeyyr sggvslptpk qftltvnvgf
//
LOCUS       WP_095897269            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            cynodegmi].
ACCESSION   WP_095897269
VERSION     WP_095897269.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga cynodegmi
  ORGANISM  Capnocytophaga cynodegmi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Capnocytophaga cynodegmi"
                     /db_xref="taxon:28189"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114174
     Region          29..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmktkrilll sfvlglffss imaqtkvsvt gtvtdekamp lpgvsiiikg takgvssdfd
       61 gkytieavqn eilefssigf vsqqrvvgan skqiinvilk eetqqldevv vtalgikrse
      121 kslsyatqsv sgkeltdvps snvlntlagk tagmtvtgsg sglgssvkiv lrgnrsiqgn
      181 nqplyvvdgt pintasfsst gaewgfgggv dtgdgmagin pediesinvl kgataaalyg
      241 sqaangvili ttkrgksekm avsvtssvqa dipyltyefq dryamgtngv nqqtrdawga
      301 arttedlsnd fvrdffntgf mmqngisasg gsntsknfls yqntsasgim pmnefkkhnl
      361 sirsttnlfn nfvevdgsia ltkqdtehap tapgryynpi vglysfpaga svfnqyrday
      421 eisnpnrngl mtmnwineed vyknpywlin rhnysfgvek viaklntkln ftpwlnlqlr
      481 gsydrtatig erkihsgvvt iagangrydy nttddallya dallsanksf ehfsvsatlg
      541 ssitdrkyeg kdvlignlvi pnlfdlrnyt gidggitptr thrqlqsvfg tvslgydemv
      601 fldvtgrndw sstlpannrs yfypslgtsi vftemlnkse akpiwldfgk lrfswtqvgn
      661 dmpwgltepy drlkkggviv antvkpfddl kpersnslea ginlrmfagr ltldaavyqt
      721 itenqyfeva ntsgsgyssy yinagkirnr glettlsfip iqtkdfswtg tinytlnenf
      781 vmtlpsqyad kgfdlngnty firlyegqew gsmyqkrlkr ddkgnilltq tidngvdkgi
      841 qlqqsddyeh igninpkfll gfkneftykn lslsflidgr fggnvisttq hyldsygrte
      901 rtadardngg vpikgiltqt vktngnadvv ttsdfdglvn aqtyykiaps getsvysatn
      961 vrlrelslsy slpksiidrl kpienirlsl igrnlmffyr dapydpeitl stsingasnt
     1021 dnfsipasrs igfsvninl
//
LOCUS       WP_095897788             959 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095897788
VERSION     WP_095897788.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..959
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106867
     Region          24..957
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkiqllli lllltsgalq aqmktitgev fdenneplpl veviikntns skttkgvstd
       61 idgkfelkar vgdilefnff gyetqrrkve gknktinfrv vlkeqklevf tiinippetm
      121 algiqkvpyr ltylqqavss kdltqvkqvn fvnsldgrva glhiqrsatg iggatkatmr
      181 garslfgdnn mlyvvdgmpi anqaergfgg ngrdtsegis dlnpediaev vvlqgaqata
      241 lygasaangv llirtkkand nqlninlsss vefvnkltkp efqetygnel gqytslstra
      301 lpkgtnfnin dfyrtghiyq nslnvsggfn feggnnktya svaslqsggi vpnsvynryn
      361 aylqnstsll kkklnidlsg nyirqyernq vasgiafnpi vglylyprge qfaqeryfer
      421 ydavagydkq ywiagsgtpd tpanlgeniq npywiayrnl rpatknrymf sakanykimd
      481 nlevaarfrm dntsstmddk ryastlpaya aangyyahwk etfkqqyadv ivhynerfsd
      541 fgldahigas yegydtqvdg yrgnlinvnn ftqsniaapt aishplwgkr sntaffamae
      601 idwknklylt lsgradkpsd fpytsestvf spsiglaipl ynfininkdi lsygklrggy
      661 sqvaapmsya glgvaetsra wigdsytlpn ypadlqlert tsyevgldtr wfnnlslnat
      721 fyhtrtnnql vpilwqqvge vqnqgveval gytyseynra lkgetqlias tnkneilslp
      781 seiangmytl reggeigdiy dsngnklgst npdwllgwkg klsyknfdld flfkarlggi
      841 vlseteryfd rygvskasad nranfvpfia nrtdadyhys atnirlqeaa ltyhfregfi
      901 vkglkdlsvs lvgsnllmly nkapfdpeiv psvgtygsgy dkfmlpsvrs yglnvkmqf
//
LOCUS       WP_095897980            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095897980
VERSION     WP_095897980.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115109
     Region          27..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkesmllf vlllcctvam aqtrvsvigs vtgndglplp gvsvvvkgtt rgvstdfdgk
       61 yeiqvtpnev lefssigyas qlkkidtkkg tftlnivlke eaqqlgevvv talgikreqk
      121 alsynvqqvn veeltkvkda nfinsltgkv agvtinrsss gvggatkvvm rgaksieksn
      181 nalyvvdgvp mlsttstqgs grfnsqgtte siadinpddi esmtvltgas aaalygsaaa
      241 ngailittkk gkegkmniql ssntefgnpf vlpefqntyg sdgkvtswga klpddasryd
      301 vkdffrtatt ltnsvalsgg teknqtyfsa astnaeglvp nnqynrynft vrntthllnd
      361 rlridasasy ilqnhlnmin qgeymnplvs aylmprgygl qrarqferyn ptthiyeqvw
      421 gdltagpdgt fngsfagdys lqnpywvayr nlreskrery llslgvtldl kkwsptekwd
      481 isgrvrtdnt nftstdkrya stlslldmsk tgyfgiargy ekqtyldvlt nlnknfeweg
      541 vgrfslvani gaslqdtryd elgykgplrk dgipnvfnaf nidqgavktr pyqsgyteqt
      601 qsifgslevg ynswlyltlt grndwasqla nspqssffyp svglsgvltd llspetkakw
      661 yntlsfakmr vafssvaspf drelttptft fnedtkvwka vsyfpigelr pertdsyevg
      721 iatkwlkgtl sldatvyqtn tynqtikaei spstgfdgiy lqtgdvrnrg levglgydlk
      781 ikdkinwnsy ftmsynenki mslvedyinp vtgqregrsy lekggiggar yilktggtlg
      841 dvyatndfkr nadgnllvds ngkvnveeyg nrdnyvklgt vlpkynlgwr ndfnignigf
      901 gamfagrigg vaismtqaal dhygvskesa earnaggvnl dgykvpaqsy feergkgrva
      961 qyytysatnf rlqeayvsyh lprklvndki dvtlsivgrn lamlyckapf dpeavsstgn
     1021 yaqgldyfml pslrsygfsi kanf
//
LOCUS       WP_095898057            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095898057
VERSION     WP_095898057.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113210
     Region          24..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklfyvfl fvlffsavat aqertitgtv rdanglemlg vavvvkgenh gtqtdmegry
       61 sikvapgktl efsflgmktq shkvgtssri dvvlqeeave igevvvlgvv kkkaaestgn
      121 tvqlsskdis tpsaisvdqa lqgktpgvvi naasgtpgae qtvmirgvgs mnssnkplyv
      181 idgvpvisen ltedkntvss mstlasinne diesltvlkd aaatalygar gsngvivitt
      241 ksgkrgktkf nvntsvgfqn dayfkrsplt gdqryhllkq glanqfasng aaydtaidfa
      301 htnglringa enfnsalnnn nwseliknkn avmtsadisa sggdekgtyy vslgynrtes
      361 tvktsdpfkr vsglirinrd lndklkleas vngswvsqnp iteqgayftn pyvtkilmsp
      421 wvspynadgs ynvttfnryt glynylylqe hdvsknntlr glinfkvdye llknlvfstr
      481 anvdyissdy knyqnrvhsn asknngsshr imthhatwvy qntlsynfnv aekhkfglta
      541 lyeyqkykkn ylegygtnia adgltnlasv tkqktisstf edwanvsllg mlnysyaeky
      601 ildasirreg ssrfaeknry gnfwslglay nlhkefdvla kvfndlklra sygltgnsgv
      661 dlnqyqvlla ydenydenga aypktlgnna ltweknrtfd vglnfalfnq rlrgsvayyd
      721 kytydlllnv plsrttgfee qainagamsn kgieaslgvd iirnenftwn lsaniatvkn
      781 rveelakdgt gadvdptags ehkqtkvget yaywymptwa gvnvntglpe wydkegkkts
      841 dynlaerrfq giaipkysgg lsthlqykgv fldasvyftg ghkvyeeysr fylrtnsfvt
      901 vnyngdaell nawqkagdvt dvpkmsysgn dnfhsvssrh lydgtfarlk ditlgyevps
      961 kylegtgfdg vtftvrgtnl ytwvkdsglk ldpevgnknn rmgyttlttp pvksvvfgvn
     1021 lkf
//
LOCUS       WP_095898156            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095898156
VERSION     WP_095898156.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110331
     Region          24..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkismllf vfalfsgalm aqtkvtgtvt ggdgmplpsv svvikgttrg vstdfdgkye
       61 iqananetle fislgyatqq kkvtqakghl tlnivmqeea lqlggvvvta lgikrqekal
      121 synvqqvkse eltkvkdvnv vnslngkvag vniqrsssgv ggstkvvmrg lksldgnngv
      181 lyvidgvplf nkqsdgggsn fgkpgggegi adinpddies invltgpsaa alygseaang
      241 vilintkkgk egktevnvss sveiltpiql pefqntygsn gdkswgakla tpsnvdpkkf
      301 fnvghnimns vtfstgnaqn qtfvsaaqtn aeglipnnay yrynigvrnt anfakdklhl
      361 dvsgnfvrqg srnmiagggy fnplvglylm prgidyrdvk ayerynpstq iyeryqpfse
      421 radsyfsenp ywvanrelfl nnkkrymmsa slkydildwm nvtgrvrldn dygtseekly
      481 asttnflvgw ktelgsynkg ryainetkde qtyadimlni nknlgqkfsl tanvgssynd
      541 rlsnnlsagg ylkeianlfs ianfdgqvga sgqgysrakn vavfasaelg yrgmlylsat
      601 grndwssqlv nsaepsffyp svglsgvise mvklpsfiny lkvrgsytev gspisktgit
      661 pgtithqlts tglvtnkvyp ypdfkaerta sweaglntkl fdnslsvdlt lyksntynqf
      721 feqqlssssi ytsfylqagd venrgielav nynkeflnkq lawnttltys rnvneikklv
      781 rgyrnpftgd lfditevrkg gtvlreggsl sdiivkgvls rdvngnlien asgfqydetq
      841 eiklgrstpd fqmgwrntls yknidlsfli ngsfggivls gtqpyldayg vskasadard
      901 aggvlvngkl ynpekyynti knldgyysyd atnvrlqevs ltysldgshf wdkvkrvtig
      961 vigtnlwmiy nkapfdpqlt fgvgtyaake lfmtpsaasy gaslkiqf
//
LOCUS       WP_095898232            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095898232
VERSION     WP_095898232.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114544
     Region          24..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklnlfytwi ffltasfamv aqnievtgtv kdekgepllg vlvlikgtqr gaatnmdgky
       61 eiqtkvgevl qysflgmktv ekkitastkr vdivlkddvq eleemvvtgy gapkiasrtv
      121 aqvaqvsskd lnnapvasvs dalqgrlagv vvssssgrpg snseiiihgy nnfqavqrge
      181 ntheplyimd gvavsssvms dfnpndieti tvlkdaasts vygaraangv ilittkkgrr
      241 nertsitvsh qlgfsaltsa srkffdnmmt preymdfwle kdptsiisaa gmsrmgstre
      301 vaeaaankil qenpyntrwd kiyfrdfvpm srtdvslsgg testsyylsl gyfnqegssn
      361 psvdykrytl ntnidtrvtk wlkvglslsa ghserdgssg ditarvtalp fysptypdgs
      421 rkdyitsitr nssmgfyhpe yyaekhprts vsddflpsgy itiepiknli fktqggiqyg
      481 ysdseakelp sflnyrqrvp aptsnpftrf stdrslrktl tntleyrfwl gnkkehsfnf
      541 ligqesient aknvtvtayg qaadglstlm qgnknkvied dksantfnsy lgrfeysynn
      601 ryfldlsgrr dgssgfgagh rygnfwavgv mwklkqekfl kevkwlsdln lrfstglsgn
      661 sigggykhlt sikvddfyee kvgysvfalg npylhweeqr kttvglnivi drgtsfniey
      721 ydretydmls srslnstsgq nqffdnaggm rnrgidftfs svvyrsknnd lsirpyfnvn
      781 ynkqevtslf gnkisdvgvs gvgykigrpl ewgavirkgv npttgeteyy vpgedrmeqv
      841 tddnkitnay dankliqttg kkmqapingg fgwsinyktf tvdmafsfsl grymmnydvs
      901 ytenparfgy snlsrnvfdy wkkpgdetrh pkitsnafvy gldsrllqda syvrmksigl
      961 syrlpkevid qvkffegvrf hatarniftf tkyegpdpes ssaislggyp psrqftlgid
     1021 lnf
//
LOCUS       WP_095898308             917 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095898308
VERSION     WP_095898308.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..917
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101647
     Region          38..916
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkykhnilfc glvgcmlwag avqaqsplni peelstlsts svkgeqllkm pttnftnslf
       61 gvlpgltvlq gggmdnasln irglgsynyp svtyfidgyq sdfillspse iesitvlkda
      121 aalapfgmkg ahgivwittk rgaegkpvvg vdfqtgvqmp tvlskplsat eyaqlyneay
      181 sndagawtsf ynipndvkyn tdwydkvlkk salfdrqdvs irggsattky fvllghagns
      241 glyaskndds hssgrfdqyl vkanldfsml kifegnvnin griedrkspn yneyklwqnl
      301 asypniiypa qnpngsfpgt aihpdnpyas iralgikqlh drtlganfnl kekldfitpg
      361 lyiqqgvsls swtrgtrivs rdytrmfngv aqtthrdsny kvdddwgtnq wnrlqlllga
      421 gyarefgqnt fqtavnylqy vyniddnlng kaglnnnyay qniggrvfyd wnkrvsaefg
      481 fafggsdnyk kgnqfgfyha lsaayqvfne qhpsantnin rlklrasvgs tgndvynegr
      541 ylyeryygsy ggggfatgnd dpswhsaigl kyvpnerifa ekaykynigv eakffnkwdv
      601 midaflnkhe giitpdysis sifgatppyk nigkvtnrgf evstlysnaa gkltysigan
      661 asyaknkidy maeydatses saqtgrpigt rfgyeaagfy dindfdsngn llpslpkpsf
      721 gnvapgdvky rdlngdnrid padkteigks ylptltyagt lnlgyegfdl gvlvqgvqgr
      781 evnllddarq ktvafenngn vyaiaknrwa yypaqgidtr ssaqyprlsl lsnnnntqps
      841 tlwikkanyl rvryielgys ipkrmldeig vsklriyvna anpftfssll tdydldpevl
      901 sgypalksvt mgvslkf
//
LOCUS       WP_095898387            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095898387
VERSION     WP_095898387.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124303
     Region          25..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkeklmyall cavlfvgvaf aqehtvtgvv kddagtplpg asvvvkgtsh gvatdfdgky
       61 sikvpnskav lvfsslgmkp tersvgnnka invtleveaq qltgvvvtgy qefdrskftg
      121 naqtlkadni kmdgvvdvgr miegraagvn vqnisgtfgt spkitirggs sifgdtkplw
      181 vvdgavqeev vnlsfeqlas gdastlvssa isginandie sieilkdasa lslygaraln
      241 gaviittksg kknvktqvny qleesvrmip nynqydimns qesmgvyrel eekgyfslss
      301 ytqaryggay nimyraidty npatgrfgle nseaariafl rkyeyantdw fktlfrpslt
      361 qnhtvslsgg genatvyasv gffvdpgwti adrvhrvtgn lkttynlspk vkigvltqgs
      421 irtqrapgtf nrsantvngg ydrdfdinpf syalnttral rpygddgkye yysynyapmn
      481 ilnelannym dlnvleykiq gdleiklakg lkynflgsvr hvkssnehsm ressnvvgay
      541 ranrttviak anpflfedpa npdkipqvvl pnggiyklte nnlqsyyfrn aleykhlfke
      601 khdlklflgq eyrhtdrdnq tfngygyqfe rggtaftdyr viqksiqens pyfekgfske
      661 rgiafflqgt ytydnryvfa gtanyegsnq lgrsrsarwl ptwnvsgrwn asnesflkdn
      721 tkisnlafrv sygliaglga asnalavfkn gvanrynigd reniieiddl qnmdltwekv
      781 yetnvgmelg lfknrvnlsl dlyqknskdl idyvrtsgig gqfvklanna smvtkgiela
      841 ldtkniktdn fswntginfa yfnqeithlt yrpnvynlvr evggnvvgga rntlysydfr
      901 glndkglplf nllngstnfd didfqqidni lsylkkegav epnitaglsn tfryknwels
      961 alitaqagnk irkpdqydss yddlsvfpke mknrwvhpgd ekttnipgip drrtvyeigs
     1021 ntlrrvynay nystervvdg sfvrmknisl syafpkevle qlkvsnltlr lqaanpfliy
     1081 sdknlngqdp effrsggvay pvtaqytfti nlgi
//
LOCUS       WP_095898601            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095898601
VERSION     WP_095898601.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125671
     Region          22..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnklsyiflf llaslsasaq tftlkgtvke tngtpllgat ivvkeshigt stdmeghfsi
       61 kaqvgqtlev syvgmktqrf kikgeslqiv lqeeaqaleg vvltgyqkiq nrvftgaaas
      121 vkmdnikmeg vadisrmleg rvaglsiqnv tgsfgsapri nirggasiig nvqplwvidg
      181 aiyedlvsls ldqlvsgdav tlvssaiagl natdiediqv lkdasatsmy garalngviv
      241 ittksgkrdt pnritysyeq sfrtipsykd fdllnsqetm sllqemnskg yfnlqntlyg
      301 rrsgiyyqwy kgvstinpnt gnyyypntpa tqaafmrere yantdwfkhl fsinpirsht
      361 itfngggkns tsyaslgyyh dsgwtitdnv kritanlknt fyindqlkat ftavgnlrsq
      421 kapgtfaqrk ntavgaferd fdinpfsyal gtsrtlrpkd aqgnleyyrn nwapfnilee
      481 yrnnymkidv ldfkiqaeas yklnphlevt alvsarqaqt qsshyitens nvikafrane
      541 tpqvandniy llknkdnpla ppqialtngg ifnktetslk symgrlavdy hrtlhehhdl
      601 kafgfaeiry adrtvtpfqg ygiqydrgnq vftnplifqk llnegnnyfa ltekydrgit
      661 fsasgtygyk gkyianavln yegsntagra trsrwlptwn vgakwnidre dffnsknist
      721 lalrasyglt akmneqains ysvfqnyvqn ryrfsdrena lrllhlenrd ltwekmyeln
      781 lgvdagffnn rismsvdiyq rnsfdlidli rtsgiggeyy kyanfgdmrt rgielslntk
      841 niqqqdfqwa ttisfsymnq kitrllntpn tfdmvsgtgr gnivgypkgs lfsfnyqgvn
      901 hqglptfdfg lyplnnrana nvvgadfldt qysksyliyh gsvepnviag fsntftyknw
      961 easffisaqa gnkirlnptf dpafgdlnvf skeyynrwlh pydelrtevp slpsqslinl
     1021 igkenieray ntynysqnrv adgsfvrmks islgyrvpkk alerygmssl tvraqatnpf
     1081 liysdsklng qdpeyyksgg vslptpkqyt lafqigf
//
LOCUS       WP_095899085            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095899085
VERSION     WP_095899085.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113016
     Region          6..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msaqqieisg tvkdnkgepl lgvfilvkgt qrgattdfdg hyslkanvgd vlkfsflgmk
       61 tvekkltagt kelnitmqed vqqlegtvvv gyggkkvasr tvasvatvkg kdiaetpnas
      121 aidalqgkva glvistdsgr pganssvlih glntffsvfd etivseplyi idgavvtsdi
      181 mtmynpadie sitvlkdaas tsiygaraan gvilittkrg krnerthiai nhqlgfsmrt
      241 nvtrkffenm atpeeymdfw ilkepsalts lgrrlgytet tpreiadril aenpyntrwd
      301 kvffhdfapv srtdvsisgg snttsyflsl gyldqqgika rsdykrynln anldtqiaew
      361 lkaglsisla htdmqsvsgg ggaetdilsl piysptqtdg krknyipsit ghqngfyhpd
      421 ylaekypadr ysdnimpigy lqiepvknlt fktqlgiqyn vdedysrgpl psfieyrydt
      481 dsnktvgqte rqmskylqrt ytnlleyrwn ikeshnfdfl lgqesvesvm rsfsasskgq
      541 psdrltmlsh gpkeptvrds qsetgfnsff srleysyknr yfldlsarrd gssafgannr
      601 yanfwaigam wkvkeekflq nvnwltsldl rfstgisgns sigdyrnrtl ispsntykek
      661 sgyflsmlgn pdimweeqqk ttlglhisiv kgtninlefy ernthktlaq gyinsasgft
      721 siphnigdmq nrgidftfst iafrsknnnw nirpyfnmny nqqkvtslyl nkeffansfs
      781 yagyrlneal qwtmpifkgi nkdgnaewyl pnetnymiqq kddskttyqf dekqlmqttg
      841 kkmyapvngg fgvavtyrnv sldlafsysl gkwlinedky ytlnqgsfga knfskdllny
      901 wkqegddtel prlnsayymr kdtrllenas ymrlksvsis yalpqelidq mkffsgvrly
      961 asarniftit kysgadpefs ntlsrggypp trqftmgvel kf
//
LOCUS       WP_095899351             976 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095899351
VERSION     WP_095899351.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..976
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110584
     Region          51..961
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvlnlktll llcifvllaq waaaqtrtat ttqtttqttt taqapmntnt rgatsisgst
       61 kplwvlngvv legsidlkpe dlvsedakml iaaaipglta esiesfkvlk dasataiygq
      121 raiggvvait tkrgttggss itytnestfr fiptygeyni mnsqdqmsvi qelirgghfk
      181 senqsitenk gvigrmydlf yvldrngnsv vpnteagrta ylqaaerrnt nwfnklfqts
      241 imqnhtlsfs sgtekstyya slsalfdpgw tkgdklsqys gnlnanynls pkfklnvisd
      301 lsyqkqttpk qdiydyavth srsmdskeyy vndfapynif neidnaykni nianlrlqte
      361 ltykitkkve atmmgairyy tnqqnteyke nsnyalsyra mpnslvrsyn prlyddpndp
      421 ydlpsvvlpe ggirerrdrt itsnhfratl ryndsfkggl hnvslyagae mdnykstddk
      481 nqnygvlfss gnysyytylf fkklqeenst yysiynttnn yqafftngsy tfgnryting
      541 tlrydasnkf aesryirwmp twnvgvnwnv tnekffdklk plshlsfkas fgvtaispsv
      601 snslsqiytn mpwrnsskre iglnivdnan hdltyeknqe lnlgtqfglf nnrinisaew
      661 fnrrsydlig nivtqgvggt itkkgnmael rihgvelgle ttnfktkdfs wktsfiysrs
      721 kneitklltn ptvrnmigys sssksvggfa kegyplrsif svpfnglndk glptfldang
      781 nstvsgirfd nrnvdfleys gtliptdkgs fsnyftykgi slgvvftysy gnvvrlrklt
      841 nsyndfwvap relnnrwqyp gdehrtnipv lyttymydly ggynniiqay ntydysnvri
      901 akgdnirlke isigytfdrd flkrnklrql smklqgtnla llyadkklng ddpdylangy
      961 spiaakrlif tlrvgl
//
LOCUS       WP_095899847            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095899847
VERSION     WP_095899847.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123166
     Region          20..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkglvlffv lltavvwgqk dvtgvvkdqq gvpvigvnvv ikgtskgvst dfegnfvlsa
       61 kegnvlvfsa igyktqekkv lkngafisvv meedlmeige vvvtgyqtvd ptkvatsytk
      121 idiknferrg tpdvisgieg lsaslvlsnn pnnptgskef sirgvstlsg dsrplivldg
      181 fqyggrledi npyevesitl lkdaasasiy gakssngviv ittrkgkegk tqvrytsnlt
      241 fqdkmdlgyi mnrvsssklv diqhqyaken hnfvqnyqkl feanspyasy yaansnrvyy
      301 lyglkkygyi teqdfdeqia qlrlydntkd ierlylqspi tnqqnisvsg gseafkyrts
      361 lnythslkgv knnenqrvif dfisnlkfsp kvnldfqtsl tsnnnsykli edqqkslers
      421 difkigsydr ffdekgnpls vfkpggnvgt nsgglfggkd pyeiqrlvaa glldetyypa
      481 ldfgkytakd ndwtahvqgl lnielteglv akvggqlrkk afninntsaa dswymkslin
      541 nttplsfsgn ardliipyga rfretrgesi dylfrtqlef nrtfgehnih lfagaeaqed
      601 kiqltridrl gydpksnlyl ptdyktlrdd innvyhpnkr iasgihfdeg feefqnryia
      661 aysnfsylyt dkyvlsgsir idqsnlfgtd pkyrykpfws lagrwrlgee aflkdknmkl
      721 dlrasygvng niankygpfd iaekrfeyra gdilalnitn ykinnlrwer setanfgadl
      781 sffnnrlelv ldyyrknttd alakvdsdpt fgsnfvyrnd aslinngyev mltsrnirtp
      841 dvlwetqlff rynkskitea sfdtstgrph nfsgkvhnmk gnepnslyvf eyagvsdtge
      901 gqirkadgsl vkveysystp rlfnyddlka agtvipkyta smnnnftykg lglsflfvyq
      961 gghvmlkdsy ngsptqngvt lmhkdteraw qkpgdesftd ipklssalys siisgstknv
     1021 lpadfirlrd vvlsytlpts llgglkvkel tinmragnlw lwtknkegid petqglgirt
     1081 pllpksytmg vnlif
//
LOCUS       WP_095900088            1133 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095900088
VERSION     WP_095900088.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1133)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1133)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1133)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1133
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123812
     Region          25..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkllvalm lvmgvfmqsv laqvrmvsgq vtdesgmplp gvsvvvknts kgvstdfdgk
       61 yslqanqgdv lefsyigfat qtkkvtgskm dvvlkeeteq lgevvvtalg vnkqarsvgy
      121 attkvdvaei grlnvvnpvn alqgkvagva intvgssgvt sssgitirga ksidknnspi
      181 fvidgmiiqe avtgalsgtd wgsqlknlnp adyesitvlk gaaatalygs rgangaiviv
      241 skggkfgkqg lgiemshsve mgdiykspia lqnvygagyp hngyeggflg dgsltrvals
      301 fgpkmegqlv nqymphgkat pfvphpnnwr alyqspiniq hniainggge tssfrlsysy
      361 adnngvfarn nfnrntlafk glmklnnvfs veagvnyafs saqnggnqga wnyggnlpmm
      421 styytprnfd matyqaiyrd pvthavetns pwgtlrgylh drdlnlrkry enslltnltl
      481 raeiapwlta svkgnynyyg istldktygt gvdygptrtg sysrggnnsg synilgmlqs
      541 ndnkfniage eftfdaivaa elygnleshs wskstkgglv vpgvfafsns aetiipnfty
      601 tprnnqtfgl sgilnfgwrd qlfleitgrn dwlstltypt ymnlgknnys vfypsvnasy
      661 vftesfnmpe wfsfgkiras iaevglgtsa yattrgfgvf sqssqfdpnr nsvlvanpnl
      721 gtawnadlkp eiqrsievgt dlrffnerln ldftyyktnt rnqilsigav aeagatsqli
      781 nagniqnqgi evqlegtpir tkdfrwtlga nftknkgkvv klhdnvkewk lldgydagpe
      841 iwayeggdyg vittiynsas gsaiyrfnnp dnandprngk pvityigryg spnpvyaygy
      901 vtnqdkgkpe rvvlgkvead fylslntsfs yknfdfyalv dgrfggnffs hthkyatgrg
      961 saestlrgrd refggiprkn ykgetvydai mldavfdega kvpsasdpsk qievggktya
     1021 ealeagimpm matsyymfny gwggpnelni qdntwlmlre itlgyrlped ickkfganyl
     1081 rlgvtarnlg ylmnkltdgl npesvssnnp ltpmdiggap fhrtysfnlt lrf
//
LOCUS       WP_095900185            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095900185
VERSION     WP_095900185.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123561
     Region          22..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllkgll flmpvvmlaq ekisgtvkdt egepmlgvsi iikntnkgtt tdfdgnfeiv
       61 anasdilvfn yigyaqkevl igkkkhldvv lsedtqelke vvvtgyqktd rklfagaatk
      121 vsaedtkidg ivdvgkmieg rvsgvsvqnv sgsfgaapki rirgassiyg dtkplwvvdg
      181 vvledvvdvn pdqlssgdis tlisssvagl naedidsfqi lkdasataly garamngviv
      241 ittkngsrdr vsidvkseyt mrskpsyndy dilnsqdqms vfremerkgw lshadmmssr
      301 dggvyfqmyn aintyqngsy gllntpqara eylktyekin tdwfkllfqn nlqqnhsvsf
      361 kggsqksqfy astsflhdtg wtisdkvnry tinakgtfdi sdkftlgist kgsyreqrap
      421 gtfsrqpsqv nggytrefdi npfsyalnts rtispyetda ktyryhrmny apfnilneyn
      481 nnyidldvld lniqanldyk inpnwsysfv gniryvkntt ehkikadanv akayrandda
      541 tiedqnnylw kdpenpssrp ivvlpkggfy nrednllknf ylrniieykn ialedhrfna
      601 ilgqevrasd rkgasfdgyg iqydkgntvf tdpniikklt qagfpyfavs nsydrfvaff
      661 angaysfnsk yifnatarld gsnrlgsstd arwlptwnvs grwnakdesf lqnvdwlsnl
      721 niratyglta smgpatnsra vlrstltiap ypdeiqngll vrslqnselt wekqyeanag
      781 fdigvfnnrf sisadfyhrk gfdliaairt sgiggelikl anyadmvskg vefslnsrni
      841 dtpsfkwttd vtfaynenei trlysepnvf sltrsegaak lggpvrglys ipfaglsneg
      901 iptfydkegk asydiffqdr nvnhlkyegs idpkitggvs nrftfdnfsl nlfftyqlgn
      961 vvrlypsfqa rysdlnamps dlkdrwlhsg deahtnvpti lskplydkyg nnilstynay
     1021 nfstervakg dfvrlkevsl tykvpndfak klgvagasfk vsgtnlflly sdkalkgqdp
     1081 effgsggval piarqyswsl ninl
//
LOCUS       WP_095900820             967 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095900820
VERSION     WP_095900820.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 967)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 967)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 967)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..967
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107859
     Region          24..965
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkiqllli llfltsgalq aqmktitgev fdenneplps veviikstns sknpknvstd
       61 idgkfelkar vgdilefnff gyetqrrkve gknktinfrv vlkeqklevf tiinippetm
      121 algiqkvpyr ltylqqavss kdltqvkqvn fvnsldgrva glhiqrsatg iggatkatmr
      181 garslfgdnn mlyvvdgmpi anqaergfgg ngrdtsegis dlnpediaev vvlqgaqata
      241 lygasaangv llirtkkand nqlninlsss vefvnkltkp efqetygnel gqytslstra
      301 lpkgtnfnin dfyrtghiyq nslnvsggfn feggnnktya svaslqsggi vpnsvynryn
      361 aylqnstsll kkklnidlsg nyirqyernq vasgiafnpi vglylyprge qfaqeryfer
      421 ydavagydkq ywiagsgtpd tpanlgeniq npywiayrnl rpatknrymf sakanykimd
      481 nlevaarfrm dntsstmddk cyastlpaya aangyyahwk etfkqqyadv ivhynerfsd
      541 fgldahigas yegydtqvdg yrgnlinvnn ftqsniaapt aishplwgkr sntaffamae
      601 idwknklylt lsgradkpsd fpytsestvf spsiglaipl ynfininkdi lsygklrggy
      661 sqvaapmsya glgvaetsra wigdsytlpn ypadlqlert tsyevgldtr wfnnlslnat
      721 fyhtrtnnql vpilwqqage vqnqgveval gytyskyigy tyskynrafk getqliastn
      781 knkilslpre iangmytlre ggeigdiyds ngnklgstnp dwllgwkgkl syknfdldfl
      841 fkarlggivl seteryfdry gvskasadnr anyvpfvanr taadyqysat nirlqeaalt
      901 yhfregfivk glkdlsvslv gsnllmlynk apfdpeivps vgtygsgydk fmlpsvrsyg
      961 lnvkmqf
//
LOCUS       WP_095900983            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095900983
VERSION     WP_095900983.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115095
     Region          27..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkesmllf vlllcctvam aqtrvsvigs vtgndglplp gvsvvvkgtt rgvstdfdgk
       61 yeiqvtpnev lefssigyas qlkkidtkkg tftlnivlke eaqqlgeviv talgikreqk
      121 alsynvqqvn aeeltkvkda nfinsltgkv agvtinrsss gvggatkvvm rgaksieksn
      181 nalyvvdgvp mlsttstqgs grfnsqgtte siadinpddi esmtvltgas aaalygsaaa
      241 ngailittkk gkegkmniql ssntefanpf llpefqnsyg sdgkvtswga klpsdasryd
      301 vkdffrtatt ltnsvalsgg teknqtyfsa astnaeglvp nnqynrynft vrntthllnd
      361 rlridasasy ilqnhlnmin qgeymnplvs aylmprgygl qrarqferyn ptthiyeqvw
      421 gdltagpdgt fngsfagdys lqnpywvayr nlreskrery llslgvtldl kkwsptekwd
      481 isgrvrtdnt nftstdkrya stlslldmsk tgyfgiargy ekqtyldvlt nlnknfeweg
      541 igrfslvani gaslqdtryd elgykgplrk dgipnvfnaf nidqgavktr pyqsgyteqt
      601 qsifgslevg ynswlyltlt grndwasqla nspqssffyp svglsgvltd llspetkakw
      661 yntlsfakmr vafssvaspf drelttptft fnedtkvwka vsyfpigelr pertdsyevg
      721 iatkwlkgtl sldatvyqtn tynqtikaei spstgfdgiy lqtgdvrnrg levglgydlk
      781 ikdkinwnsy ftmsynenki mslvedyinp vtgqregrsy lekggiggar yilktggtlg
      841 dvyatndfkr nadgnllvds ngkvnveeyg nrdnyvklgt vlpkynlgwr ndfnignigf
      901 gamfagrigg vaismtqaal dhygvskesa earnaggvnl dgykvpaqsy feergkgrva
      961 qyytysatnf rlqeayvsyh lprklvndki dvtlsivgrn lamlyckapf dpeavsstgn
     1021 yaqgldyfml pslrsygfsi kanf
//
LOCUS       WP_095901127            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095901127
VERSION     WP_095901127.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110356
     Region          24..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkismllf vfalfsgalm aqtkvtgtvt ggdgmplpsv svvikgttrg vstdfdgkye
       61 iqananetle fislgyatqq kkvtqskgtl tlnivmqeea lqlggvvvta lgikrqekal
      121 synvqqvkse eltkvkdvnv vnslngkvag vniqrsssgv ggstkvvmrg lksldgnngv
      181 lyvidgvplf nkqsdgggsn fgkpgggegi adinpddies invltgpsaa alygseaang
      241 vilintkkgk egktevnvss sveiltpiql pefqntygsn gdkswgakla tpsnvdpkkf
      301 fnvghnimns vtfstgnaqn qtfvsaaqtn aeglipnnay yrynigvrnt anfakdklhl
      361 dvsgnfvrqg srnmiagggy fnplvglylm prgidyrdvk ayerynpstq iyeryqpfse
      421 radsyfsenp ywvanrelfl nnkkrymmsa slkydildwm nitgrvrldn dygtseekly
      481 asttnflvgw ktelgsynkg ryainetkde qtyadimlni nknlgekfsl tanvgssynd
      541 rlsnnlsagg ylkeianlfs ianfdgqvga sgqgysrakn vavfasaelg yrgmlylsat
      601 grndwssqlv nsaepsffyp svglsgvise mvklpsfiny lkvrgsytev gspisktgit
      661 pgtithklts tgletnkvyp ypdfkaerta sweaglntkl fdnslsvdlt lyksntynqf
      721 feqqlssssi ytsfylqagd venrgielav nynkeflnkq lawnttltys rnvneikklv
      781 rgyrnpftgd lfditevrkg gtvlreggsl sdiivkgvls rdvngnlien asgfqydetq
      841 eiklgrstpd fqmgwrntls yknidlsfli ngsfggivls gtqpyldayg vskasadard
      901 aggvlvngkl ynpekyynti knldgyysyd atnvrlqevs ltysldgshf wdkvkrvtig
      961 vigtnlwmiy nkapfdpqlt fgvgtyaake lfmtpsaasy gaslkiqf
//
LOCUS       WP_095901192            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095901192
VERSION     WP_095901192.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114171
     Region          24..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklnlfytwi ffltasfamv aqnievtgtv kdekgepllg vlvlikgtqr gaatdmdgky
       61 tiqtkvgdvl qysflgmktt ekkitasskq ldivlkddvq eleemvvtgy gapklasrtv
      121 aqvaqvqgkd vsaapvasvs dalqgrlagv vvtsdsgrpg snsdilihgy nnfqgalrge
      181 rtqeplyimd giavsssvms rfnpndiesi tvlkdaasts iygaraangv ilittkkgrn
      241 nertsvtish qlgftaltna srkffddmmt preymdfwie knpeavnlav gkfssskdva
      301 rqsadkilad npyntrwdkv ffrdfvplir tdvsisggtn nstyylsfgh fsqegstapr
      361 sdyrrytvng sintqitkwl ktgfsfaagh tereggstln tpkvialply sptyedgrrk
      421 nyipgitsrs agfyhpdyya ethpsnsfsd dflpsgfvsi epiknlifkt qggiqygyge
      481 selkelpsfi dykffddpnp ytsvsnsrtl rktitntley rfllgenkkh sfnvllgqes
      541 vensskqldv ttfgqpsegl tmlrhgskdk riedqktvst fnsyfgrvey syntryfvdl
      601 smrrdgssaf gknnhygnfw aigamwklkq enflkdvkwl sdlnlrfstg lsgnalggyk
      661 hittikpdnf yqgktaytvg slgnpdlrwe eqrkttvgln ividrgtsfn ieyydretyd
      721 missrelnst sgqnqffdna ggmrnrgidf tfssvvyrsk nedlsirpyf nvnynkqeit
      781 alfgnktsnv vpsseigykl gralewaavi pkgvnpttgq meyyipgddr meqvtddnrv
      841 tttydssklg qttgkkmqap inggfgwnin yktfsldmaf sfslekykwn ydmkytenpd
      901 qfgdhnlsrk ildywknpgd ntrhpkintt tfvnssdarm iqdasfmrlk nitlsyslpk
      961 evinqikffe gvrlyvtarn iftltkyega dpeytnpiss ggyppsrqft lgvdvnf
//
LOCUS       WP_095901382            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095901382
VERSION     WP_095901382.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124277
     Region          25..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkeklmyall cavlfvgvaf aqehtvtgvv kddagtplpg asvvvkgtsh gvatdfdgky
       61 sikvpnnkav lvfsslgmkp iersvgnnka invtleveaq qltgvvltgy qefdrskftg
      121 naqtlkadni kmdgvvdvgr miegraagvn vqnisgtfgt spkitirggs sifgdtkplw
      181 vvdgavqeev vnlsfeqlas gdastlvssa isginandie sieilkdasa lslygaraln
      241 gaviittksg kknvktqvny qleesvrmip nynqydimns qesmgvyrel eekgyfslss
      301 ytqaryggay nimyraidty npatgrfale nseaarlafl rkyeyantdw fktlfrpslt
      361 qnhtvslsgg genatvyasv gffvdpgwtv adrvhrvtgn lkttynlspk vkigvltqgs
      421 irtqkapgty nrtantvsgg ydrdfdinpf syalntsral rpygddgkye yysynyapmn
      481 ilnelannym dlnvleykiq gdleiklakg lkynflgsvr hvkssnehsm rensnvvgay
      541 ranrttviak anpflfkdpa npdmipqval pnggiyklte nnlqsyyfrn aleykrlfke
      601 khdlkvflgq eyrhtdrdns yfngygyqfe rggtaftdyr viqkaiqdns pyfgrsftke
      661 rgiafflqgt ytydnryvfa gtanyegsnq lgrsrsarwl ptwnvsgrwn asnesflkdn
      721 tkisnlafrv sygliaglgs asnalaifkn evanrynlsd rentiyieal qnseltwekv
      781 yeanvgmelg lfknrvnlsl dlyqknskdl idyvrtsgvg gqlvklanna smvtkgiela
      841 ldtkniktdn fswntginfa yfnqeithlt yrpnvynlvr evggnvvgga rntlysydfk
      901 glndkglplf nllngstkfe dinfqqidni lsylkkegpv epnitaglsn tfryknwels
      961 alitvaagnk irkpdqysvd yndlsvfpke mrnrwinpgd ekvtnipaia dkrtvnevgr
     1021 atlrrvynay nystervvdg sfvrmksigl syafpkevld qlkvsnltlr lqatnpfliy
     1081 adknlngqdp effrtggvay pvntqytfti nlgi
//
LOCUS       WP_095901323             917 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095901323
VERSION     WP_095901323.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..917
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101717
     Region          38..916
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkykhnilfc slvgcmlwag amqaqsplnv peelstlsts svkgeqllkm pttnftnslf
       61 gllpgltvlq gggmdnasln irglgsynyp svtyfidgyq sdfillspse iesitvlkda
      121 aalapfgmkg ahgivwittk rgtegkpvvg vdfqtgvqmp tvlskplsat eyaqlyneay
      181 sndagawtsf ynipndvkyn tdwydkvlkk salfdrqdvs irggsantky fvllghagns
      241 glyaskndds hssgrfdqyl vkanldfsml kifegnvnin griedhkspn yneyklwqnl
      301 asypniiypa qnpngsfpgt aihpdnpyas iralgikqlh drtlganfnl kekldfitpg
      361 lyiqqgvsls swtrgtrivs rdysrmfngv aqtthrdsny kvnddwgtnq wnrlqfllga
      421 gyarefgqnt fqtvvnylqy vyniddnlng kaglnnnyay qniggrvfyd wnkrvsaefg
      481 fafggsdnyk kgnrfgfyha lsvayqvfne qhpsananin rlklrasvgs tgndvynegr
      541 ylyeryygsy ggggfatgnd apswhsaigl kyvpnehifa ekaykynigv etkffnkwdv
      601 mieaflnkhe giitpdysis svfgatppyk nigkvtnqgf evstlysnaa gkltysigan
      661 asyaknkidy maeydatses saqtgrpigt rfgyeaagfy dindfdsngn llpslpkpsf
      721 gnvapgdvky rdlngdnrid padkteigks ylptltyagt lnlgyegfdl gvlvqgvqgr
      781 evnllddarq ktvafenngn vyaiaknrwa yypaqgidtr ssaqyprlsl lsnnnntqps
      841 tlwikkanyv rvryielgys vpkrmldeig vsklriyvna anpftfssll tdydldpevl
      901 sgypalksvt mgvslkf
//
LOCUS       WP_095901554            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095901554
VERSION     WP_095901554.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125642
     Region          22..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnklsyiflf llvslsasaq tftlkgtvke tngtpllgat ivvkeshigt stdmeghfni
       61 kaqvgqtlev syvgmktqrf kikgenlqiv lqeeaqaleg vvltgyqkiq nrvftgaaas
      121 vkmdnikmeg vadisrmleg rvaglsiqnv tgsfgsapri nirggasiig nvqplwvidg
      181 aiyedlvsls ldqlvsgdav tlvssaiagl natdiediqv lkdasatsmy garalngviv
      241 istksgkrdt pnritysyeq sfrtipsykd fdllnsqetm sllqemnskg yfnlqntlyg
      301 rrsgiyyqwy kgvstinpnt gnyyypntpa aqaafmkere yantdwfkhl fsinpirsht
      361 itfsgggkns tsyaslgyyy dsgwtitdnv kritanlknt fyindqlkat ftavgnlrsq
      421 kapgtfaqrk ntavgaferd fdinpfsyal gtsrtlrpkd aqgnleyyrn nwapfnilee
      481 yrnnyikidv ldfkvqaeas yklnphlevt alvsarqaqt qsshyitens nvikafrane
      541 tpqvandniy llknkdnpla ppqialtngg ifnktetslk symgrlavdy hrtlhehhdl
      601 ktfgfaeiry adrtvtpfqg ygiqydrgnq vftnplifqk llnegnnyfa ltekydrgit
      661 fsasgtygyk gkyianavln yegsntagrg trsrwlptwn vgakwnidre dffnsknist
      721 lalrasyglt akmneqains ysvfqnyvqn ryrfsdrena lrllhlenrd ltwekmyeln
      781 lgvdagffnn rismsvdvyq rnsfdlidli rtsgiggeyy kyanfgdmrt rgielslntk
      841 niqqkdfqwa ttisfsymnq kitrllntpn tfdmvsgtgr gnivgypkgs lfsfnyqgvn
      901 hqglptfdfg lyplnnrpna nvvgadfldt qysksyliyh gsvepnviag lsntftyknw
      961 easffisaqa gnkirlnptf dpafgdlnvf skeyynrwlh pydelrtevp slpsqslinl
     1021 igkenieray ntynysqnrv adgsfvrmks islgyrvpkk alerygmssl tvraqatnpf
     1081 liysdsklng qdpeyyksgg vslptpkqyt lafqigf
//
LOCUS       WP_095902317             976 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095902317
VERSION     WP_095902317.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..976
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110541
     Region          51..961
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvlnlktll llcifvllaq waaaqtqtat ttqtttqttt taqapmntnt rgatsisgst
       61 kplwvlngvv legsidlkpe dlvsedakml iaaaipglta esiesfkvlk dasataiygq
      121 raiggvvait tkrgttggss itytnestfr fiptygeyni mnsqdqmsvi qelirgghfk
      181 senqsitenk gvigrmydlf yvldrngnsv vpnteagrta ylqaaerrnt nwfnklfqts
      241 imqnhtlsfs sgtekstyya slsalfdpgw tkgdklsqys gnlnanynls pkfklnvisd
      301 lsyqkqttpk qdiydyavth srsmdskdyy vndfapynif neidnaykni nianlrlqte
      361 ltykitkkve atmmgairyy tnqqnteyke nsnyalsyra mpnslvrsyn prlyddpndp
      421 ydlpsvvlpe ggirerrdrt itsnhfratl ryndsfkggl hnvslyagae mdnykstddk
      481 nqnygvlfss gnysyytylf fkklqeenst yysiynttnn yqafftngsy tfgnryting
      541 tlrydasnkf aesryirwmp twnvgvnwnv tnekffdklk plshlsfkas fgvtaispsv
      601 snslsqiytn mpwrnsskre iglnivdnan hdltyeknqe lnlgtqfglf nnrinisaew
      661 fnrrsydlig nivtqgvggt itkkgnmael rihgvelgle ttnfktkdfs wktsfiysrs
      721 kneitklltn ptvrnmigys sssksvggfa kegyplrsif svpfnglndk glptfldang
      781 nstvsgirfd nrnvdfleys gtliptdkgs fsnyftykgi slgvvftysy gnvvrlrklt
      841 nsyndfwvap relnnrwqyp gdehrtnipv lyttymydly ggynniiqay ntydysnvri
      901 akgdnirlke isigytfdrd flkrnklrql smklqgtnla llyadkklng ddpdylangy
      961 spiaakrlif tlrvgl
//
LOCUS       WP_095902449            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_095902449
VERSION     WP_095902449.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113017
     Region          6..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msaqqieisg tvkdnkgepl lgvfilvkgt qrgattdfdg hyslkanvgd vlkfsflgmk
       61 tvekkltagt kelnitmqed vqqlegtvvv gyggkkvasr tvasvatvkg kdiaetpnas
      121 aidalqgkva glvistdsgr pganssvlih glntffsvfd etivseplyi idgavvtsdi
      181 mtmynpadie svtvlkdaas tsiygaraan gvilittkrg krnerthisi nhqlgfsmrt
      241 nvtrkffenm atpeeymdfw ilkepnalts lgrrlgytet tpreiadril aenpyntrwd
      301 kvffhdfapv srtdasisgg snttsyflsl gyldqqgika rsdykrynln anldtqiaew
      361 lkaglsisla htdmqsvsgg ggaetdilsl piysptqtdg krknyipsit ghqngfyhpd
      421 ylaekypadr ysdnimpigy lqiepvknlt fktqlgiqyn vdedysrgpl psfieyrydt
      481 dsnktvgqte rqmskylqrt ytnlleyrwn ikeshnfdfl lgqesvesvm rsfsasskgq
      541 psdrltmlsh gpkeptvrds qsetgfnsff srleysyknr yfldlsarrd gssafgannr
      601 yanfwaigam wklkeekflq nvnwltsldl rfstgisgns sigdyrnrtl itpsntykek
      661 sgyflsmlgn pdimweeqqk ttlglhisiv kgtninlefy ernthktlaq gyinsasgft
      721 siphnigdmq nrgidftfst iafrsknnnw nirpyfnmny nqqkvtslyl nkeffansfs
      781 yagyrlneal qwtmpifkgi nkdgnaewyl pnetnymiqq kddskttyqf dekqlmqttg
      841 kkmyapvngg fgvavtyrnv sldlafsysl gkwlinedky ytlnqgsfga knfskdllny
      901 wkqegddtel prlnsayymr kdtrllenas ymrlksasis yaipqelidq mkffsgvriy
      961 asarniftlt kysgadpefs ntlsrggypp trqftmgvel kf
//
LOCUS       WP_095909719            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            gingivalis].
ACCESSION   WP_095909719
VERSION     WP_095909719.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga gingivalis
  ORGANISM  Capnocytophaga gingivalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Capnocytophaga gingivalis"
                     /db_xref="taxon:1017"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112615
     Region          24..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktnvvyfml ffigvlqvsf aqkktltgvv rdenqepmlg vsviikgtse gvstdengvy
       61 tlkvkdgdev evsamgyktq vhkvtaktkk wdvllaldve eipefvfvgf gqkqavkeat
      121 gsigkvdnls nsasasvdka ltgkvagvqg gvttgqpgga anirirgias vngrtnpiyi
      181 idgvrvnqgs ltsgatssni lanlndddie sitvlkdavs taaygadaga gviiittksg
      241 kkgeakynfn sevgvvsral kgeenlstsq wlgllydayl ntkegtrlfp nndkaallaa
      301 leagtlstaa tgrslqalyk nrnistdwrk esensmalvq klngsvsggt dridyysslg
      361 yykqdgivkq tgfhrvtnsn kityrandrl tlatdiqlsy sqtmtmpsgg dyanpilgqy
      421 llrptdrayk tdgslnyggr ggklsngfyn vvalqnlnyi qsqttrafgn fqadykilkn
      481 ltykfvfape yvdimedkyl tplhgdgkde gglsnwyasr yfsfnvqnil sydfkykekn
      541 nfyvnliqea yksdvrrlsa sasnvgpsgl ttlsnfikpr dasgtkavss rggyaltfhy
      601 dydklflldl sgrqdrvsnf weenktgyfg svgvgvdfar lealkkskal sqlklsasyg
      661 svgnmvdvfp yatysyllny neqvggnvng venrdlrwet lsplnvgldi gflkdritls
      721 aayfykktsd mifavplsra qgssggsvyk nigemvnkgl eltfnakvve negdgfnwsv
      781 ggnfttlkne vtklygdkqe iisgsriirk geavnsfwmk kwagvdpdng dplwyvngeg
      841 gettkdynka gyalqgspmp tfyggfdtkl syknftlsld ftysggnrii dvfasyvnsd
      901 gglllnypgy rsqignywtp enknardpkp vlnegnknat gfstryqykg dfvrlqtlrf
      961 syklkpewle gtylrglefy vlgnnvwthn fdknfkgdpd lnisgetsfa lpslrtysfg
     1021 vnvnl
//
LOCUS       WP_095909819            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            gingivalis].
ACCESSION   WP_095909819
VERSION     WP_095909819.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga gingivalis
  ORGANISM  Capnocytophaga gingivalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Capnocytophaga gingivalis"
                     /db_xref="taxon:1017"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113702
     Region          24..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkklflwi cfvfttmtfa qqnlsgsvkd vtgkpvagas vtvfgttrtt ktspegayti
       61 kakegeviqf saagyknvem kvgisttmda ilqpvsaqeg geagalgikr dknavgyatq
      121 ktdadqglsg nvagvqtstt ssmggntnvt irgvgsitgs nqplividgv pmatvggtds
      181 kfgdaagdin pediesvtvl sggaatalyg srggngviiy ttksgkagkt tidvkssvsv
      241 erayiapklq nqygggrkpt fetytkdgke ynvpayetde swgpkydgtp ylpwyaydek
      301 ylpehylkpv pwqapkndvd klyrtgfnia nsvsvsravg gtnlrfslgn nevtgivpnt
      361 klqktnvsfs fnsklsnklk seggfnyiit srdnpensyt mknpiskvly awtqrqldmk
      421 nlenyykapd gthrtwnrks vtdgtpryad npywtmyent sndkrhrffg nigftynftd
      481 nlywvgkiyg diyslntear vavgskeqss yettnytnsd fnyetrlhyt pnlgkdftlt
      541 gfvglarreg ryhwvkgktn gglvlpdfyn lensaetpss tnyrnwrrtn sifgmasfgy
      601 kgmvfveatg rkdyfstvse pvfypsvtgs fvftsawksk pswlsygkvr vawaqagndt
      661 spyqlltypt iglpfngspn ylhpytqnnp dlvpeiketk eaglelrlfk drlsanvsvy
      721 dilsknliip lpvdgangyv ykmvnsgems nkgievslsa tpvqvgkfsw nvswnfaknn
      781 nkllklypgt trykitndss glvslyaieg qaygqlfgrd fvyddkgnrl vdsqgkylts
      841 epkalgtiip dytmglrnsf kygpvslsfl fdfqkggkyf anaymlgmyt gmlretvdng
      901 mrdeverngk keqrgivapg vfapgtpkag qpndkiltpk eygslyyrgv dsqnifdaty
      961 fklrsvtlsy dvpltekkhi kgvnisifgn nlwttglswd gmdpeiaasn kgigesslps
     1021 trsfgmslgl kl
//
LOCUS       WP_095909821            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            gingivalis].
ACCESSION   WP_095909821
VERSION     WP_095909821.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga gingivalis
  ORGANISM  Capnocytophaga gingivalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Capnocytophaga gingivalis"
                     /db_xref="taxon:1017"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113067
     Region          22..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnfkklwlyl fiafsattfa qqkisgsvkd stgkplpeas vivvgtqrna ktnaegayti
       61 sakenevlhf sasgykstev kvgvsttidv vlpqaeaaae egalgikrdk navgytaqka
      121 gasdnlsgsv agvqtnttss mggntnvtir gvgtitgsnq plividgvpm atvggtdskf
      181 gdaagdinpe diesvtvlsg gaatalygsr ggngvilytt ksgkagktsi dvksgvtfek
      241 iyiapklqne ygggdsqrfe tvningrqyk iaryavdqsw gpkfenqqyl pwyafdkeyl
      301 pekylktvpw kapdndvdkf yttgvgisns isvsrslsgt nlrfslgnne vtgivpttkl
      361 qktnfsfnfn sklssklkse ggvnyvlter dnpdfsntvn nplaivhytw sqrqldmrnl
      421 eryyeneagd qrpwnrttwn naepkfvdnp ywelnkntnn dkrhrffgni gftyefssql
      481 ywvgkiygdi ysltkedrka vgsfgtpyyt ktvynnsdfn yetrlhytpk lsknftltgf
      541 iglsrrngky gwssgktvgg lvspnfynla nsketpqasd yaswrrtnsv fgmfsfgykg
      601 mafveltgrq dwfstvskpv fypsvtgsfv ftsalkkkps wlsygkvrva waqagndtnp
      661 yelvtyptvh npfggapdys rpdvsnnpel vpeiketkea glelrlfkdr lsanvsvydi
      721 lskdliiplp vdaangfisk rvnsgkmsnk gievslsatp vkvgkfswnv swnfaknkne
      781 liklapgikr ykvtsdrygl vslyaiegea fgqlygrdfk yddkgnkiiq angkyapsel
      841 kslgsiipdy tmglsntlky shlsvsfkfd fqkggkyfsa ahmvgmstgm lrettengir
      901 dlitrngrve ergivldgvl angqrntkvl spkrygegfy rggidtqnif datylklrnv
      961 sisydvplpe kknikglnit lfgnnlwttg ldwdgmdpet aasnkgigev slpttrsfgm
     1021 siglkl
//
LOCUS       WP_095909823            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            gingivalis].
ACCESSION   WP_095909823
VERSION     WP_095909823.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga gingivalis
  ORGANISM  Capnocytophaga gingivalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Capnocytophaga gingivalis"
                     /db_xref="taxon:1017"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113162
     Region          24..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkkllllc flvfttmafa qqsvkgsvkd stgkpvagai vqvvgasrsa ttnsegayai
       61 qaqaeetlrf saqgyqnvei kvglssvvna vllpmenkqe agalgiernk davgyntqnt
      121 eggqnlsgav agaqtsssss mggntniilr gvgtvtgsnq plividgvpm atvgdgkntg
      181 dalsdinped iesqsvlsgg aatalygsrg gngvilittk sgkggktsie vksgvtfeta
      241 yiapvlqney gggdsqqfer atingqqynl aryavdqswg pkydsskmyl pwyafdqkyl
      301 pqhylkpvpw vapqkgiekf yrtgvgmsns fsvtrslsgt nlrfslgnnq vngivpntdl
      361 hktnlafsfs adlskklkse ggfnyvitsr tnpdfantvn ndlanvfyaw shrqldvekm
      421 ekyyidpagg qrtwnrtawd neepkfannp ywevyknynn dkrhrffgnl gltyhfkenl
      481 ylvgkvygdi yyytkenrna vgaygvpsyq ktvynntdfn yetrlhytpk lgenfsltgf
      541 igmsrresry awssgktvgg lvvpnlynms nskqvpqasd ysswqrtnsv ygmasfgfkn
      601 mafvevtgrq dwfstvskpv fypsvtgsfv ftsawkskps wlsygkarva waqagndtgp
      661 yrlmnyplvn tpfrgspdyi rsntsnnpdl vpeiketkea glelrffkdr vsinasiydi
      721 lskdliiplp idaangynwk yvnsgemsnk gvevtlsvtp iqtekfnwnl swnfsknknk
      781 leklapgirt yrvnwdkygq vslyaiegrp fgelygrdfv yddkgnrivq sngkyatsel
      841 kalgniipdy tmgltnsfry grlnfsfvfd fqkggnyfsa ahmtgmstgm lretvaggir
      901 eydptgpknq kgivlpgvtr sgavntkrid pqtygegffq gavdkqnifd atylklrsvs
      961 lsydvplpst kyiknvnvsf fgnnlwttgl dwdgmdpeta asnqgigeis lpttrsfgms
     1021 vglkl
//
LOCUS       WP_095909826            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            gingivalis].
ACCESSION   WP_095909826
VERSION     WP_095909826.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga gingivalis
  ORGANISM  Capnocytophaga gingivalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Capnocytophaga gingivalis"
                     /db_xref="taxon:1017"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114199
     Region          22..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkklfllc slvfttmafa qqtikgsvkd skgkpvtgat vlvigtsrsa ttnsdggysi
       61 eaqaeetlqf aaqgyqnvqk kvglettidi vlplateenk kvgalgverd anaagytdtt
      121 leggedlkgk tagltatssg gmqgskmelr gkgsvtgsnq plividgvpm vdmgskygds
      181 aseinkddie svtvltggaa talygsrggn gvilyttksg kggktaidin ssvsfdrayi
      241 spklqneygg gssldftqql ingttynlpq yevdeswgpk ydgtpylpwy afdkkylpeh
      301 ylkpvpwqap kndidkffrt gmninnsasi trsisgtnlr fslgntettg ivpttelrrt
      361 slafsftsel skklkaeggl nysitvrenp nytyadandn ggfsvvlygy tqrqldmenl
      421 rrfykspige qrtwnrtswe npkpnfadnl ywmlyentqn dkrhrffgnl gltynftdkl
      481 flvgkmygdi yalttesrta vgshdtsqys ryiydnssfn yetrlhynpd lgenftltgf
      541 vgvaraqnky eyvgaetqgg livpnyysaa nskerpkgit ysswtrtnsv ygmasfgykg
      601 tafvevtgrn dwfstvstsi fypsvtasyv fsnsfknlps wftygklrag waqvgndasa
      661 yvlktypsvy qafkgaqyyl vptekknpel rpeiketkea gidlqffngr lslgfsyydi
      721 lskdlilsmp vdaangytyk kvnsgemvnr gfeitlsatp vqtdkfswtl dwnlsrnrnk
      781 llklapglsr ykvtweyygn velyavegrp fgeiyggnyv yddkgnrlvd eegnyfispk
      841 kevlgninpd fttgltntlt ygnlslsftf dyshggsyya gpyalgmyag tiretvengm
      901 rerdpngpng qkgivldgvv ghkqadgsiv stgvkntkai spkqhgttfy kgidaqavfd
      961 atflklrsvs lsydvpltet ryikglnftl sgynlwtgal awdgmdpeta mynqgmgnss
     1021 lptirsyals vglkl
//
LOCUS       WP_095909871            1122 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            gingivalis].
ACCESSION   WP_095909871
VERSION     WP_095909871.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga gingivalis
  ORGANISM  Capnocytophaga gingivalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Capnocytophaga gingivalis"
                     /db_xref="taxon:1017"
     Protein         1..1122
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126052
     Region          26..1121
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkwlyvll gflcltatgl yaqestitgi vrdeegkpll gvsvvvkgtt rgvdtdldgk
       61 ysikvpdeka vlvfsmlgsk pvervvgnhk elnvtlkedv teltglvfng yqeidkklft
      121 gnsqtlkidn ikqdgvvdvg rmlegrsagv nvqnlsgtfg tspkitirgg ssifgdtkpl
      181 wvvdgavqee vvnlsfeqla sgdastliss aisglnandi esieilkdas alslygaral
      241 ngaviittks gkrnvktqls yqleesvrmi pnyaqfdlmn sqetmsvyre leqkgyldra
      301 tytaaqqggv yqimyrntdt ydpatgrfll qnspearnaf lrkyeyantd wfktlfrpsl
      361 tqnhtlslsg ggenttiyss lgffvdpgwt iadrvhritg nikttydlss kvkigilaqg
      421 airnqkapgt fsrssnqvtg eyerdfdinp fsyalnttra lrpyddegny dyyrmnyapm
      481 nilkelknny idlkmmeykl qsdleikftp alkykflgsv ryaqstqeht itegsnvvga
      541 yrandnmiig ernpflyrnp ddpsalpqvv lpnggiykle qnnlqsyylr naleynkafk
      601 dqdeqdkhtl klflgqefry tdrdnqsfdg ygyqfnrggv vftdpriiek viadnaqyfd
      661 rstgrergva ffsqasygfr nryilsgtln yegsnqlgrs rkarwlptwn isgrwnvtne
      721 hflpathals nlsfrlsygl iaglnnigna lpimastitp rfrnqdnerl irilslqnsd
      781 ltwekvyetn fgtdigflsn sislsvdlyq knskdlldiv rtsgmggemn kyandasmtt
      841 rgvelvldtr nfktedftws tsvnfayfkq eitslanasn svfnlvretg gnvlgnprnt
      901 lysydfagln sqgmplfnlk ggsrdykdid fqdrdnilsy lkkegavdpn itgglsntfr
      961 yknwelnfli tmqagnkirk aplykgagyd dlsvfprefk nrwvapgdea ltqipgivsq
     1021 rtlneenkay israysaynh starvvdgsf vrmksislsy tfdkevlenl nlgnltlrlq
     1081 asnpfliyah kdlngqdpef frsggvaypi tpqytftinl gi
//
LOCUS       WP_095910328            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            gingivalis].
ACCESSION   WP_095910328
VERSION     WP_095910328.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga gingivalis
  ORGANISM  Capnocytophaga gingivalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Capnocytophaga gingivalis"
                     /db_xref="taxon:1017"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117817
     Region          24..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrikisicll fsllgmihtf aqeksisgtv knsqglpqqg vvvslkgdss rttqtdakgg
       61 ytilakstdi lvfsslgmat iertvgeatt idvvmsssta katptpsttg eavartnvrg
      121 pssiygeskp lwvvdgiild dgvelspdal sssdaktlia salgglssdd idtfrvlkda
      181 satsiygpra iagvvvvntr kgskgtnsis ytnestfrli psynnfnimn sqdqmdvfme
      241 mmrrgnityk emgnrrhyge igrmyallnt atpsgyglan tneakeaflr aaemrntdwf
      301 srlfqtnilq shsvsistgt dkasyyasvg iindpgwmrf snynrytani nanyklsksv
      361 sfnliangsy renktpgsvd gvsgkvssaf slnpysyaln asrtmdpeat yryrfaplni
      421 feemennytn thigdikiqg qlswkispkv tavglaairy qnisqelnqt ersnlarayr
      481 amdnvtmitn ntylyedpyd dfdvkrtvlp eggirekses ilngkdfrgt idyrdafsgg
      541 ihkiqvlgga etsdiyrnkd wnqnlgllye lgdmsyfsye afkqmqenkt nyytltrttt
      601 rnvaffsnam ysykdkyifn gtlrtdasnk fgashyirwm ptwnlaltwn isqekffpkl
      661 kpisalsfkg sfgmtpesps vsnslakiig erpwrsadrf qetalrisea anhdltyekk
      721 eelnlgvqmg lfknrinlal dwytrnnydl igrvpsqgln gtvirsgnva amrssgvdls
      781 lqtknltigd fswvttfvya rndnkitkly veatiedmvk gtgfskegyp vgsifsipfr
      841 glnseglptf adsngnttid glrldqrdnl dflkysgttr ptdvgslgnl fkykgislni
      901 lltysfgnvl rlpasfkhsy indsptspsd mvampkefkn rwmqpgdenr tnipaiasay
      961 qlyaiptley aytaynysdv riakgdfirl keislaydfd ketlrdmkik rlsfklqgtn
     1021 lfllyadkkl ngadpefsas ssfiptpkql tfsirvgl
//
LOCUS       WP_095910945            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            gingivalis].
ACCESSION   WP_095910945
VERSION     WP_095910945.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga gingivalis
  ORGANISM  Capnocytophaga gingivalis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Capnocytophaga gingivalis"
                     /db_xref="taxon:1017"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112775
     Region          25..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklrifyvfa llfiaiqgal aqkvtvtgtv kdgqgdpimg tyilikgtsk gattndkgay
       61 tieanvgdil yysflgmkqv ekkvtqkssv invvlqddvq eidtglvftg ygapkvaskt
      121 vasvetiqgk emaetptana mdalagrvsg mvvttdsgrp gttskvlihg fnnfqaalrg
      181 nasrqdplfi vdgvqvdddi mssinpndie sitvlkdaas tsiygaraan gvilittkrg
      241 kynqpasisi shqvgfnait sasrkffdnm mspreymdfw aqrdpgairs aagvsgdtda
      301 aiekilkenp yntrwdkiff rdfvptsrtd vsvsggtenm ayyfslghlk qegstapsld
      361 yhrynlnssi dtrinkwlka gvslsmsyte seggrssvvg grvlalplyt pynpdgsrkn
      421 firgitgrat gfyhpeydae khpygsygid vmpigyltve piknlvfktq agiqyssges
      481 qskqlhsftd ykfgyemtpy tqlseskayk ktftntleyk fllgdshhft allgqesien
      541 isktltnntg gqpsdglsml vhgnkdlsia dnkmvsafns ffsrleydyq grffldlsgr
      601 rdgssnfgrn nryanfwavg amwklkkenf lkevkwltdl nlrfstglsg ntgglnysnl
      661 nvispmalyq gqtgytlsrl gnpdirweeq tktsvglnvv flyntslnve yynrrtydal
      721 syrdnnsssg ytqlygntgg mqnqgidlsi ssrvyynean nlsirpyfnf nynqqkivei
      781 fdgrqslvna rdkigfkvgk aleytavlhk gvnpdtglie wykpgedkme kqtddsqitt
      841 eynlnlgqtt gkkmhapvng gfgwditygg fsldmnfsfs igrwvenrdm iyienpntfa
      901 ngnlsrnvfd ywkqpgdvtr hpkiteatfv qgsdsrliqn adfirlkgit lsyrlpkevi
      961 eqvgffqgvr lygtarnvft itkyegadpe ftqpisiggy ppsrqftfgv elkf
//
LOCUS       WP_095911774             947 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sp. H4358].
ACCESSION   WP_095911774
VERSION     WP_095911774.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. H4358
  ORGANISM  Capnocytophaga sp. H4358
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 947)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 947)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 947)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..947
                     /organism="Capnocytophaga sp. H4358"
                     /db_xref="taxon:1945658"
     Protein         1..947
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104141
     Region          2..946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miinvllkee aeqleevvvt algikrqeks lsyatqtvsg keltdvpssn vlntlagkta
       61 gmsvsgsgsg vgssvkivlr gnrsiqgnnq plyvvdgtpi ssgafsgsai gdgygggidt
      121 gdgmaginpe diesinvlkg ataaalygsq aangvilitt krgnsekiav svtssvqadv
      181 pyltykfqdr ytmgvdgvsq ssmdawgapr tnqdlsndfv knffntgfms qngvsvsggn
      241 kvtknflsyq nttatgimpn ntfdkhnlsl rsttslfddf ievdgsvalt hqdtgnapaa
      301 pgqyfnpilg lylfpagtta fnsyrdvyev pdpsrnglmt mnwanqidvy knpywlinrh
      361 nysynvekai vklntkfnft swlnlqlrgs ydktatlger kvhagmttlt gkggrydhkt
      421 qnyalmyada lltanksyek fsisatlgts isdtkettne iqihnlaian lfdlrnyigi
      481 eggsdnkrth rqlqsvfgtv slgynemlyl dvtgrndwss tlpannrsyf ypsvgtsfvf
      541 temldqneak pewldfgklr fswtqvgndm pwgltepydk lqkggviean tvkpfddlkp
      601 ersnsleagv nlrflggrft fdaavyktvt enqyfkvdnt sgsgysqyyi nagevenkgf
      661 eltlgftpik tndfqwngyl nystnkntvl slpsqyldkg feissvgyrf rlkegeewgr
      721 myekrlkrdn qgnilltqti engvdkgiql qqsddfeyig nvnpkfligf knefsyknfs
      781 lgllidgrfg gnvisstqni ldrfgrsqrs aeardnggip ltgtlvtttk vtgspdvvtq
      841 tafnqkidaq tyykvapage tsvysatnvr lrelslsytl pkslveriky vesvrlslig
      901 rnlgffynea pydpeitlst ssnglsnadl fsmpasrsig fsmninf
//
LOCUS       WP_095911971            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Capnocytophaga].
ACCESSION   WP_095911971
VERSION     WP_095911971.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga
  ORGANISM  Capnocytophaga
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Capnocytophaga"
                     /db_xref="taxon:1016"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119272
     Region          24..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkliwtms lfffalqftf aqektitgtv kdesghpllg vtvtvkgttk gvatdfdgny
       61 sikakvgdil hfiglglrsv dksvqasttk idvvmeeeve qleevvvtay gtqnkssiag
      121 svqtikaeql skvqsanvmq slagkaagvq ikntsgqpga gsevrfrgig sisasnsply
      181 vvdgipfhgd iasisaqdie sitflkdasa nalygsrgan gvivvttkkg sgnkvrvtye
      241 tkvgvntrav pdydvitdpr eyyqlefqrr klgswvknns ltevqaaqna atslvpsigy
      301 nifnvpnnqv idpatglvnp naqilyqddw ykalfgtgfk tehfvnltrg gektntylsl
      361 gylnedgyvl nsgfdrvavr tnvdykltdn ikvgtnlnya ytfqkspqeg knsttfsnlf
      421 swtrnaapif piyardrygn mrydakgnii ydfgkgqtqn fdgsatkrvy ienmnpyatt
      481 lkntqtnerh slgarafasi dflkdfnfty niaydlfadn rlrygwevgg dsapyggsit
      541 ngvrfqstlt nqqllswkke fgahsidlmv ghessdfqsk mlagnktnvv vsdkvfisna
      601 tkfgslngyn dtyqtegyls klnygyadky fvnasyrrda ssvfhpdnrw gdfygfgvaw
      661 nvtkesffph sntlnnlklk asygeqgndn ilypdyvsfd hrthfsfrrn ykpyltqydi
      721 tpdaegnasv reaylgnkdl rwevsknfnv gfetklfnrv nleaeyfvrk vsdmlynepq
      781 qpssgnptis rnigdmenrg fevsldidvi ktqnsnlnlw anathyknki trlpapftdg
      841 yyryvegksa ytyyvrefvg vdeadgtglw nkgdvdtngi atgekttvkv hsqatqylsd
      901 ktahpdlygg fglsfsyknw sfstgfayqi ggyiydsvyn glfvqnegfg nsghnfhkda
      961 yktwnfnnrn aqfprmttad sqqfgvsdlf ltkadylswe dislsyklai keiqsigles
     1021 vtltatgsnl wvwskrqgld prmvslgtgn ttniyslyrt isfgltakf
//
LOCUS       WP_095912056            1120 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sp. H4358].
ACCESSION   WP_095912056
VERSION     WP_095912056.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. H4358
  ORGANISM  Capnocytophaga sp. H4358
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1120)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1120)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1120)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Capnocytophaga sp. H4358"
                     /db_xref="taxon:1945658"
     Protein         1..1120
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126675
     Region          25..1119
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqsmikkll ytifllcsqw aiaqqevtgt vvdnqgmpll gatvivkern vgvttdidgk
       61 fttkaengqt lvvsyigfqt qrvkitastm hivlkedvqe ldavvvtgyq kiksrvftga
      121 sasvkmeqvk mdgvadvsrm legrvaglsi qnvtgtfgsa prinirggas iignvqplwv
      181 idgavyedlv sltldqlvsg davtlissai aglnaadied iqvlkdasat svygaralng
      241 vivvttktak rdtpnritys yeqsfrqips ykdydllnsq etmsvyqela nkgyfslrda
      301 lygrrsgiyy qwykgistin pntgtyyyen tedakraffk ereyvntnwf nhlftinpiq
      361 qhtltfsggg kntttyaslg lfndkgwtii drvqritanl kstffitddf kttlsvqgnm
      421 rnqkapgtft qrknttigsf erdfdinpfs yalgtsrtlr prtndgkley yrnnwaafni
      481 lneyennyld inlldfkiqa easykinkdl eatallstrq astssahfik epsnvvqafr
      541 anetpwvaqq niylikdkdn plsqpkiglt hggifnktet tlksyqarma ldynkslgeh
      601 dikafgfaem ryadrtvnpf qgygiqydkg nqiftnplif qklidegndy fawlerydrg
      661 ltfslsgtyg ykgkyifntv lnyegsntag knsrsrwlpt wnvggkwnid qedfmkdqky
      721 fstlafrlsy gltakmneqa insnavyknv ilnrfhfkdr enalrilhle nrdltwekmy
      781 elnlgidagf fnnrlnatid iyqrnsfdli dlirtsgvgg qyykyanfgd mrtrgvelal
      841 nskniltddf kwttnftisy mnqkitrlln tpntfdmvag agrgnivgfp kgslfsfnyq
      901 glnnyglptf dfglyplndr aygniagadf ldaqysksyl iyhgsiepnv ngglsntfsy
      961 knwefsffvt aqagnkirln psfdpafadl nvfsteyydr wiapgdewrt evpalpsqdl
     1021 irligqenie kayntynysq nrvadgsfvr mknislgynv pesavkrykm kslnvrgqit
     1081 npfliysdsr lkgqdpeyyr sggvslptpk qftltvnvgf
//
LOCUS       WP_095912671            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sp. H4358].
ACCESSION   WP_095912671
VERSION     WP_095912671.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sp. H4358
  ORGANISM  Capnocytophaga sp. H4358
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Capnocytophaga sp. H4358"
                     /db_xref="taxon:1945658"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113932
     Region          25..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkflvtfv ltmvfcfhwl yaqnrtvsgv vtdesgipls gvsvlvkgtt rgvstdfdgk
       61 yniqaqaeei lifssmgfvt qekkanvtkl nvmlkedaee leevvvtalg ikrsekalgy
      121 alqeidgtkl leardanvtn alsgkvsglq ivkgaggmag sskivlrgqn sltgdnqpli
      181 vvdgvpidnk asgaadiwgn sgmdmgngls dinpediesl tvlkgasaaa lygsragngv
      241 ilittksgke kkglgitfst tlatedifvk palqnayaqg vdnlydpkta rnwgpriegq
      301 tvtnwnnkqv kleaydnmnn ffrtgitatq alsfqqqink tsvygsvnym dntsmvpetd
      361 mnrtsmalrt ttnlgasdrw kvdfkinyvn tqahnrpiqg lnqsnvfktl tifprtldir
      421 efnppivngq qvwydtqtlp ddnpwwtlky ntnndvrnry isfgavtyef tnwlrgevkg
      481 gldyyntkmy qrkhsgslsv pkngqyaeas kefseknlsf lliaeksdll kdlngtltfg
      541 gnlmsqhise mnaksgdlli pnifslnngk ekptvtslit qrkmnslygs aqigwknsly
      601 ldatfrndws stmskvnrsy fypslsfsgv iselielpew vtfakvrasy aevgndlepy
      661 mlynsysvak dywgvptist neilydhsvr selvksyeag ldlrlfnnrv rldaavyktn
      721 amrqllrlpm detsgykfki inagnienkg velslgvgil qnpeglnwdt tvnfsknenq
      781 iidlypgvas yelltvdeim vlaevgkeyg aiygsairrv ndansphngk miltaeglpq
      841 rdavalhylg nqqpdyllgf snsfswkgin ldflvdarvg gkmfsmtrnl ltgygmaaet
      901 avdgkrdsfv vegvianssg gydvntkqvt pqrywgalaq nnigiteanm ydatsvrlrt
      961 lslgytfgkk ylesigiqnl kcsftannlw lihtnipgid pesvsgtgtn vtalefgapp
     1021 tsrtftfnit igl
//
LOCUS       WP_095912953             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            leadbetteri].
ACCESSION   WP_095912953
VERSION     WP_095912953.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga leadbetteri
  ORGANISM  Capnocytophaga leadbetteri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Capnocytophaga leadbetteri"
                     /db_xref="taxon:327575"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111271
     Region          60..970
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntlklskll ffgwlatvgq afaqqpkktl ssvangtqtv tktttqtttt aqtpmntntr
       61 gatsisgstk plwvlngvvl qgtvdlkped lvsddakmli aaaipgltae siesfkvlkd
      121 asataiygqr aiggvvaitt krgstggssi tytnestfrf iptygeynim nsqdqmsviq
      181 elirgghfks enqsitqnkg iigrmydlfy vldrngnsvv pnteagrtay lqaaerrntn
      241 wfnelfqtsi mqnhtlsfss gtekssyyas lsglfdpgwt kgdqlsqysg nlnanynlss
      301 kfklnvisdl syrkettpkq diydyavths rsmdpkeyyv ndfapynifn eidnayknin
      361 ianlrlqael tyritkkvea tmmgairyyi nqqntefken snyaqsyram pnslvrtynp
      421 rlyddpndpy dlpsivlpeg girerrdrtt ignsfratlr yndsfkeglh nvslfagvem
      481 dnykntddkn hnygvlfgsg nysyytylff kklqeenssy ysiyntinnn qafftngsyt
      541 fgnrytingt lrydasnkfa esryirwmpt wnvgvnwsvs nekffprlkp lshlsfkasf
      601 gitaispsvs nslsqiytnm pwrnsskrei glnivdnanh dltyeknqel nlgtqfglfn
      661 nrinvsaewf nrrsydlign ivtqgvggti tkkgnmaelr irgvelglet tniktkdfsw
      721 ktsfiysrsk neitklltnp tvrnmigyss ssksvagfak egyplrsifs vpfnglndkg
      781 lptfldsdgn stvsgirfdn rnvdfleysg tliptdkgsf snsfsykglt lgvvftysyg
      841 nvvrlrkltn syndfwvapr elnnrwqypg deqrtnipvl yttymydlyg gynniiqayn
      901 tydysnvrva kgdnirlkei sigytfgrdf lkrnklrqls vklqgtnlal lyadkklngd
      961 dpdylangys piaakrlift lrvgl
//
LOCUS       WP_095913257            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            leadbetteri].
ACCESSION   WP_095913257
VERSION     WP_095913257.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga leadbetteri
  ORGANISM  Capnocytophaga leadbetteri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Capnocytophaga leadbetteri"
                     /db_xref="taxon:327575"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114135
     Region          26..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkftivlc flfasignlf aqnlevsgvv kddkgepllg vfvlikgtqr gastdldghy
       61 tlhtkvgdvl lfsflgmksv ekkvtanskv lnvtmvedvq elegtvvmgy sgkkvasrtv
      121 asvatvqgke iadipggnvi dalqgkvagm vvttdsgtpg sassvlihgf nsfasmlesk
      181 dqqlkanspl yivdgvpvds svmtilnpad fesvsilkda astsiygara angvilittk
      241 rgkrnertni tinhqlgvta ltnvtrkyld klatpreymd fwllkspsei vaagnrlgyt
      301 etdpaavanr iladypyntr wdkvflrdfv ptsrtdiaas ggnehttyyv slgylnqegm
      361 rksskfnryn aslnvdtqva dwlkgglsfs yahsdndiyt npfeseaeil alpfysptdk
      421 ngktkdfina ingarngfyh pdyiaknyln kgfvddimpi gyltiepvkn ltlktqagiq
      481 ytisegeikg pmpsfinykt gsqavgrver dmqksiqkty tnllqykfdl aqkhlfdvll
      541 gqesientgy gfsassqgqp sealmmlahg nqeknvrdnk svstfnsffs rleysynnry
      601 fldlsarrdg ssafiknhry qnfwavgamw kakeekflqk vdwltdlnfr fstgiagsar
      661 igdyrnmila eadnsvtyng qlsfrlaqvl gnpnlvweeq rkstfgvnfv laagntsfni
      721 eyydrhtynt lstrelntif gygripdnig dmqnrgidfs fattayrdrd krisvrpyln
      781 mnynsqkitn isygkpyaln resymgykvg kaaewvlpif kgidnngnaq wyeagddkle
      841 tqmddskvtk tynpvalaqs tgkkryapin ggfgcdatyk dfslsvtfay sigkynvned
      901 katllnpgyf gvkniskdlf nywkqpgddt eiprldsdvl mwkdsrilek adylrmknin
      961 lsynlpqtti dqlkivkair lsvsaqnift ltkfsgvdpd ytrgiiggyp ptrqytfgve
     1021 lkf
//
LOCUS       WP_095913491            1009 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            leadbetteri].
ACCESSION   WP_095913491
VERSION     WP_095913491.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga leadbetteri
  ORGANISM  Capnocytophaga leadbetteri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Capnocytophaga leadbetteri"
                     /db_xref="taxon:327575"
     Protein         1..1009
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111004
     Region          27..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkismllf vfalfssalf aqtkvsvtgt vtgndglplp gvsvvikgtt rgvstdfdgk
       61 yeiqaagnev lefsslgyts qskkvdkssg kltlnvvlke eaqqlgevvv talgikreqk
      121 alsynvqqvk seeltkvkdv nvvnslngkv agvniqrssa gvggatkvvm rglksidgnn
      181 gvlyvidgvp lynkqndsag amsrpgggeg iadfnpedie sinvltgpsa aalygseaan
      241 gvilintkkg kegktevsis ssievmtpim lpefqntygs igdkswgpkl atpstfeprk
      301 ffntgtnmmn svtfstgnaq nqtfvsaaqt eaeglipnna yyrynvgvrn takfakdklh
      361 ldvsgnfirq gnrnmiaggg yfnplvglyl mprsldyrdv eayerynpar giyekyqpys
      421 eqadsyfsen pywvanrelf lnnkkrymms aslkyeilsw lnisgrvrld ndygtkeekl
      481 yasttnflvg wkpefgphdk gyysvgnskd eqtyadimln mnknfgedfs ltanlgssyn
      541 drystslsag gylfrlpnvf saanfnpqig gsgqgysrak nvavfgsael gykgmlylsv
      601 tgrndwssql vnsaepsffy psvglsgvis qmvklpqfin ylkvrgsyte vgspisktgi
      661 tpgtithnlt ssglttnkvy pypefkaert asweaglntk lfdntlsvdl tlyksntfnq
      721 ffeqelssss iyssfylqag nvenrgvels vnynkeffnk elnwnstlty srnvneikel
      781 vrgyrnpftg qlfditevrk gstvlreggs msditvrgvl srnkngelie eaaqyqydqt
      841 qeiklgrstp dfqmgwrntl sfrnidfsfl fngsfggivl sgtqpylday gvskasaear
      901 daggvmvngk lydaqkyynt ikklpgyysy datnvrlqev slsysldgkh fcdkvkrvtl
      961 gvigtnlwmi ynkapfdpql tfgvgtyaat effmtpsaat ygaslkiqf
//
LOCUS       WP_095914085            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            leadbetteri].
ACCESSION   WP_095914085
VERSION     WP_095914085.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga leadbetteri
  ORGANISM  Capnocytophaga leadbetteri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Capnocytophaga leadbetteri"
                     /db_xref="taxon:327575"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123809
     Region          25..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqkltyvll wvlsavglsy aqeltitgvv kdsdgtplps asvvvkgtsh gvatdldgky
       61 sikvpnnktv lvfsslgakt vertvgankv invtlqdeaq qlegvvvtgy qefdrskftg
      121 naqtlkadni kmdgvvdvgr miegraagvn vqnisgtfgt spkitirggs sifgdtkplw
      181 vvdgavqeev vpltfeqlas gdastlvssa isginandie sieilkdasa lslygaraln
      241 gaviittkgg krnmktqvny qleesvrmvp tysqydimns qetmdvyqel erkgyfslss
      301 htqgryggvy nimyraidty dpatgkflle nsdaaraafl rkyeyantdw fktlfrpslt
      361 qnhtvslsgg genasiygsi gffadpgwti adrvhrvtgn lktsytlspn vkigiltqgs
      421 irtqkapgtf arkentvsgg ydrdfdinpf syalntsrtl rpyddngnle yyrynyakmn
      481 ilnelannyi dlnvielklq gdleiklakg lkynflgsvr hvksssehsi tedsnvsnay
      541 raaettivrq qnpflftdpn dpeaiakvvm peggifklse nnlqsyyfrn alefkrllkd
      601 vhdikiflgq eyrhtdrdnn nftgygyqfn rggtvftdyr avqkaidesn pyygksytke
      661 rgiaffsqgt ytydnryvla gtlnyegtnq lgrsrsarwl ptwnisgrwn asnekflenn
      721 stisnlafra sygliaglsp asnalpifrn avmeryrsgd kesairissl qnseltwekv
      781 yesnlglelg lfknrlnlsa diyqknskdl idyvntsgig gqriklanna smvtkgiela
      841 ldtkniktdn fswstginfa yfnqeitkls depnvynlvr dlggnvlgga rntlysydfi
      901 glsdkgmplf nllngstayq dinfqsitni lsylkkegav epnitgglsn tfryknwels
      961 alitvqagnk irkapqysvd yndlsvfpke mrnrwvaagd eqttnipaip skrtitelge
     1021 ntlrrvynay nyssarvvdg sfvrmksisl sytfgkevld alrvsnfslr lqatnpfliy
     1081 adkdlngqdp effrsggvay pvtsqytfti nlgi
//
LOCUS       WP_095914154            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            leadbetteri].
ACCESSION   WP_095914154
VERSION     WP_095914154.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga leadbetteri
  ORGANISM  Capnocytophaga leadbetteri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Capnocytophaga leadbetteri"
                     /db_xref="taxon:327575"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114285
     Region          26..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklkqlftw gffflaifsv saqnvqlsgt vkdeagtpll gvfimikgtq rgattdtdgk
       61 ytlnanvgdv ldftflgmkt vqkkvtantk kldvvmkddv qeleemvvtg ygapklasrt
      121 vaqvaqvqgk dvsaapvasv sdalqgrlag vvvtsdsgrp gsnsdilihg ynnfqgalrg
      181 ertqeplyim dgiavgsnvm srfnpndies itvlkdaast siygaraang vilittkkgr
      241 nnertnvtis hqlgftaltn asrkffddmm tpreymdfwi ekdpqavnla agkftsnkdv
      301 arqsadkila anpyntrwdk vffrdfvpli rtdvsisggt nnssyylsfg hfsqegstsp
      361 rsdyrrytvn gsintqitnw lkagfsfaag htereggssl nmpkvialpl ysptyedgrr
      421 knyipgitsr sagfyhpdyy aethptesfn ddflpsgfvt iepiknlifk tqggvqygyg
      481 eseqrelpsf idykfyddpn pytfvsnnrt lrktltntle yrfllgeakk hsfnvllgqe
      541 svenstkqld aatygqpaeg ltmlrhgskn kriedqksvs tfnsyfgrle ysyntryfvd
      601 lsmrrdgssa fgknnhygnf waigamwklk qenflkevkw lsdlnlrfst glsgnalggy
      661 nhittvkpdn fyqsktaytv gklgnpdlrw eeqrkttvgl nlvvdrgtsf nieyydrety
      721 dmissrdlns ttgqvqfydn aggmrnrgvd ftfssvvyrs knqdltirpy fnvnynkqev
      781 talfgnktsn vipsseigyk lgralewaav ipkgvnpdtg qmeyyipgdd rmeqvtddnr
      841 vsttydsskl gqttgkkmqa pinggfgwnv syktfsldma fsfslekykw nydmkytenp
      901 dqfgdhnlsr kildywknpg dntrhpkint ttfvnssdar miqdasfmrl knitlsyslp
      961 kevikqikff egvrlyatar niftltkyeg adpeytnpis sggyppsrqf tlgvdvnf
//
LOCUS       WP_095914209            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            leadbetteri].
ACCESSION   WP_095914209
VERSION     WP_095914209.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga leadbetteri
  ORGANISM  Capnocytophaga leadbetteri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Capnocytophaga leadbetteri"
                     /db_xref="taxon:327575"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120105
     Region          25..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklnrlvyal llalivhgfs laqerevkgt vrdsngleml gvavvvkgea hgtetnldgk
       61 ytirvadgkt lefsflgmkt krfkvngqsr idvvmeeeaq eigevevvgy vtvkkdqyvg
      121 taatidkesl krksvsnvsk aiagevagvr vinssgqpgt eatirvrgfg svngnrsply
      181 vvdgvpyega vssinpddie smvvlkdats tsvygsrgan gvvlittkkg rvdtsriqve
      241 skigfnmrll pryetitspe ryaelgweal rqsgaltqak npaaftragy aspadyaskn
      301 lfgklgiapk ynmwnvagan linpatgkvn dgvtrkydpe dwgdyafqta vrseynvsms
      361 ggsgkttyyt gfgylkddgy ainsgferyt grlnlgyqpk swlkgefnls yahtktkang
      421 qssdsnslfw ftdnipsiyp lflrdsngdk vddphyggyq ydfgkgrgfg altnavaqat
      481 ydkkdrtrnn vlgnvflrad ivkgltfetr lggeyfnnay nnytnpyygs sasqngslsk
      541 tryellnytf lqmlrysqqf gkhnlqafva hesttfdyyi lsggksglvd pkgtelenai
      601 klnsftsyih nyrlesyfsq llydyegkyl fsgslrrdgt srflnhkwgt fasvglgwvv
      661 skenflkeke wlpyfklkts ygtvgdqevg sgnasyysgy dvydlgsfmg lpsavfnrig
      721 ypdltwekak ifqvgaeftf lksraielql dyyhkttdnl vfdsrlapss gnglwkvndg
      781 klvnsgfefn lqthvvntkn wrvdvgvnge llnnkltqmp ydksikgeki idisgifgrs
      841 kghslydiyt qeyrgvnpqt gaaqwtmhya dnnnngtydn gdeaiaslhe yqakypnani
      901 kekltedysq atqkyigksa ipdvrgafnf nvgykglsls aqllyslggy aydgvyaalm
      961 gnekigsnnw hkdienhwkq agdatdvprl tsnygndgqa nntssrfltk tdylalnnvt
     1021 laysldkkvc qtigfegltf tlagdnlwla tarkgfnptt sesgnsaryt ysplstftlg
     1081 vkatf
//
LOCUS       WP_095914492            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            leadbetteri].
ACCESSION   WP_095914492
VERSION     WP_095914492.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga leadbetteri
  ORGANISM  Capnocytophaga leadbetteri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Capnocytophaga leadbetteri"
                     /db_xref="taxon:327575"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115875
     Region          26..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdnthkialf ifcwlfpfwl iaqevtikgt vkdedglelp gaaivikgta kgmatdwngn
       61 femkahqgdi lvfstigyap kevkvgkert lhivlsadvq qlegtevvav aygttdkksf
      121 tgsmatikad aiqakqttdv aktlegavag vqistssgqp gssssirirg igsinassdp
      181 liildgvpfe gtlnainnsd iesvnvlkda sssalygarg angvvlittk sgskgrlsis
      241 vdsklgfnyr gipeydliss pseyyetlwa slynqnlysq rqadalarsn asqslinnvg
      301 agyniynvad devvlptgkl npaatikysd aatfnqweka lfntrvrkeh nlsmtkgteh
      361 nsfyfsfgyl gdegynmnsy fnrystrfay kgditswlka nassmityte kqgstedsgy
      421 dnpfawtrti apiypiyehd angnrlntyd ygatrkfndn tnpvatqren lnysrdyyfn
      481 qalsldaqlh knltfsvngn fyanfydvny fttplggagk nyggaatkyk sdnivltfnq
      541 llrysknwdn ygiealfghe syqkrfgtie gskknfvdpr nsefnnaavl saltsytnry
      601 fvegyfgqln anyqqkyyls aslrrdgssv fapenrwgtf wsvgaswlls eekflekvdf
      661 vdlvklklsy gvqgndelyl pgggrsyvpy mtlysvstng ntpglvasyk gnrnitwees
      721 gnlnagvela ffrnrltlea dyfvkktndl lfnmplpast gftseprnva dmlnkgvefs
      781 lavtpvrtdk vqwtvsvngl hykneitrlp delrekgltr gyqtlkeggs iydfymvkwg
      841 gvnptngdaq fyiknattge yelkgsenyk sdskqyvgss ipdlqggfgt tlsaynfdla
      901 vqfsyqlggk fydyqyaglm hsgdlgrtwh adirnrwtpd nttsdiprle fanqkllsls
      961 drfmvssdyl slrnisvgyt ftrqmveklg ltklryylta dnvylwsyrk gldprtslsg
     1021 sntaavyspi rtvsmgltlt f
//
LOCUS       WP_095916379            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095916379
VERSION     WP_095916379.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114042
     Region          49..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 midllsrsns rgklgkflli alacglwada vyakaeitsv revveqqtkk vsgtvtdesg
       61 qplpgvsvfv kgtqrgittd fdgnyqiqas qgevlvfsyv gfvtqekivs stgnelvini
      121 slkeetqqle qvvvtalgik rqekalsynv qqvkseeltr vkdanfvnsl ngkvagvniq
      181 ksssgvggqt kvvmrgaksi lggnnvlyvi dgvpmgentn rergdqkfgt passegiadf
      241 nsediesisv ltgpsaaaly gaaaangvil intkkgkegk mkvnlsssve fsnplilpef
      301 qntygtsdlf fswgdkldtp ssldpkkffn vgttynnaln fsvgnkqnqt fvsaasitse
      361 givsnnqyrr hnvlirntss flddkleldv sasyvrqfek nmisfgeyfn pivgvylfpr
      421 genfdwmksf elydmekgyn aiqnripgdl gkdiqnpywi myrnvrpkvr drymfsgqlk
      481 ynifknlnia grvrldntys ksedkryagt lgafakekgr yaysqgtfkq kyadlimnyn
      541 tsfaddfnlv vnagtsfedy dnkgksyrge ikhiankffi sntdastavv sdeggndrrr
      601 niavfasael gwksalyltl tgrndwasql vnsdeesify psvgvsavit ellspetknk
      661 lypylgfaki rasftevgsp isvtgitpgt itkkieggsi kandfyplta plkaertrsf
      721 evgistkwlk nrlsldvtay ksntynqlll aglpkssgyq tmyvqagnve nkglevalgy
      781 nqevadfnfg tsltatanqn kiirlasgip npfdasspid ikemtvgnfy lreggsigdi
      841 yannwikrdk yglvdissgt iateatepym lgsvnpdwll gwqgnlgykn lslnflfkar
      901 lggvvvsktq qildyygvsk asadardlgy aqlgsfkvnp rayynainal dayytysatn
      961 vrlqevslty sfpkqalgkt fsdlsislig nnlwmiynka pfdpeltstt gtfgqgydyf
     1021 mlpslrsygl svkigf
//
LOCUS       WP_095917078            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095917078
VERSION     WP_095917078.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124697
     Region          25..1134
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkllvalm lvmgvfmqsv iaqvrtvsgq vtdesgmplp gvsvvvknts kgvstdfdgk
       61 yslqanqgdv lefsyigfat qtkkvmgggn sliinavlke eteqlgevvv talgvnkqar
      121 svgyattkvd vaeigrlnvv npvnalqgkv agvainntga sgvtssagit irgaksldkn
      181 nspifvvdgm iiqenlvgal ggtdwgsqlk nlnpadyesi tvlkgaaata lygsrganga
      241 ivivskggky gkqglgvefs qsiemsniya ppmklqnlyg agspfngyeg gflgdgslen
      301 tpssfgpkme gqlinqymps geqtpfvahp dnwrvlyrnp fnqtynvain gggenssfrl
      361 sysymdnngs fkrnnfnrnt vsfkglmkln nifsmeagvn yafseaknap nqyggywdqn
      421 qallttlrip rnfdmktyea tyrdpitqav etdtpwssir nylhirdlnl nqrnenslla
      481 nltlranias wltasvkgny nyysystmsk sygtgafygp tktgeysrgg kidgsynflg
      541 mlqsnnnkin iageeitlda ivaaelygnl eshswskstk gglvvpglfa fsnsaetiip
      601 sfgytpannk vfgvsgilnl gwrdqlflev tgrndwlssl typnymiggk nnysvfypsv
      661 nsswvftetf qmpdwfsfgk vraswaevgm gtgayasskg ygifkqesqf danrnsvlva
      721 rpnlgtawnn dlkpeiqrsi elgtdlrffn drlnidfayy ktntrnqils vgtsiesgas
      781 tqlinagniq nqgielqieg tpirtnnfrw tigtnitknk gkivelhpnv kewqimgqtd
      841 agaeiwayeg gdygvltsay naqfgsaiyr fnnpddtndp rngkpviyya gaggtpnray
      901 ayiyrtntqk nikdrvvlgk veadfylnin tsfsyknfdl yalidgrfgg qfysnanrya
      961 tssgalestl qgrdaehggl prvnykgetv ydaimldavf dqdvkaplas dpsqridvgg
     1021 ltykealdrg iapmmasthy yynyrwgapv dlniqentwl mlreisvgyr fddevckkig
     1081 mnylrvglta rnlgllmskl qdglnpesla nnnplqpvvy ggvpysrtfs fnltarf
//
LOCUS       WP_095917369            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095917369
VERSION     WP_095917369.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113492
     Region          24..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlkltwmvm lfftalqlsf aqektvkgtv kdasgvelpg vavqikgeqr gtetdfdgny
       61 slqvapgkil vfsylgmknv ektvgnsnti nvvmeedthq lgevvvtgam glqrkpkels
      121 ysvssvkskd ltaansanta tamigkvsgl qinvvnngvs pstrvvlrgn rsllnnneal
      181 ivvdgfpaqr gvldrinped ieettvlkga nasalygsea angvliittk kgrsklnvtl
      241 nstlemeevs ympkfqdqfg sggfpdgtkv glenvawgpr fdgelidase kyengdvwmi
      301 pyspikdnhk sffskgltfr ngvtisagdd ksdllfsfdf irkngvvpkd eygrnnvrln
      361 agrklgkfef kgnfsfynsn tnivssaagk qdrpiywnvi ntplhipikq mknwkdgyyt
      421 rkevsfyrfy enpyylidne rdegkyneft figdvkynft dwlsatyrag ytfdnyvfkr
      481 kkaaytmafi vpdayhnadt yeastsdrit isnrfnsdfi lsfdknigel fniqanlgqs
      541 trmdnenrin lsgenlivpd fynvstrtge lkgsqytkny rkvgvfadvt fgikkwlfln
      601 asarndwsss lsadnrsyfy pgggvsvvls daipqlvtdn glsylklsgn itqsgndpsa
      661 yanqaifeva sgfphgsiag ltqgsrevst dlrpeftlak eaglefglfk nrvtgnvtly
      721 qtntydqiip vnisyasgas siltnlgele nkgievdlnt tllkatdfkw digvnysgyt
      781 skvlelspgv eelsiggyad asivakkgaa ypqikvsaye rddmgrvivd dtgdpiksse
      841 mkyagkttpd yvvglnssit yknfklyvta dyragsvfyn tlaggmeftg lsphsvtagr
      901 kpfvfpnssy sdgkggyian tdrltsnggn afwdkysdvk enyvydgsfi kireislsyd
      961 fntdvlkkig innlsmavya rnpfmftpkd nvltdpefny stgniigigt daqtpptrly
     1021 gfkltanf
//
LOCUS       WP_095917381            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095917381
VERSION     WP_095917381.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123570
     Region          22..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllkgll flmpvvmlaq ekisgtvkdt egepmlgvsi iikntnkgtt tdfdgnfeiv
       61 anasdilvfn yigyaqkevl igkkkhldvv lsedtqelke vvvtgyqktd rklfagaatk
      121 vsaedtkidg ivdvgkmieg rvsgvsvqnv sgsfgaapki rirgassiyg dtkplwvvdg
      181 vvledvvdvn pdqlssgdis tlisssvagl naedidsfqi lkdasataly garamngviv
      241 ittkngsrdr vsidakseyt mrskpsyndy dilnsqdqms vfremerkgw lshadmmssr
      301 dggvyfqmyn aintyqngsy gllntpqara eylktyekin tdwfkllfqn nlqqnhsvsf
      361 kggsqksqfy astsflhdtg wtisdkvnry tinakgtfdi sdkftlgist kgsyreqrap
      421 gtfsrqpsqv nggytrefdi npfsyalnts rtinpyetda ktyryhrmny apfnilneyn
      481 nnyidldvld lniqanldyk inpnwsysfv gniryvkntt ehkikadanv akayrandda
      541 tiedqnnylw kdpenpssrp ivvlpkggfy nrednllknf ylrniieykn ialedhrfna
      601 ilgqevrasd rkgasfdgyg iqydkgntvf tdpniikklt qagfpyfavs nsydrfvaff
      661 angaysfnsk yifnatarld gsnrlgssad arwlptwnvs grwnakdesf lqnvdwlsnl
      721 niratyglta smgpatnsra vlrstltiap ypdeiqngll vrslqnselt wekqyeanag
      781 fdigvfnnrf sisadfyhrk gfdliaairt sgiggelikl anyadmvskg vefslnsrni
      841 dtpsfkwttd vtfaynenei trlysepnvf sltrsegaak lggpvrglys ipfaglsneg
      901 iptfydkegk asydiffqdr nvnhlkyegs idpkitggls nrftfdnfsl nlfftyqlgn
      961 vvrlypsfqa rysdlnamps dlkdrwlysg deahtnvpti lskplydkyg nnilstynay
     1021 nfstervakg dfvrlkevsl tykvpndfak klgvagasfk vsgtnlflly sdkalkgqdp
     1081 effgsggval piarqyswsl ninl
//
LOCUS       WP_095917700            1119 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095917700
VERSION     WP_095917700.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1119
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126405
     Region          24..1118
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfiqhfict ivlfagvayg qneriitgnv tsssdkmplp gasvfipskv vtsetavkgi
       61 lesvgigvva dfdgnftisv pqgtkqlavs figfetkiit lseaknhyni aleeetnalq
      121 evvvtgyqki ekrkltsavv kvdskdiiqa gvasidqllq gqvagmvttv gsgapgelak
      181 irirgtasls gsqdplwvvd glplegneap dltkgnidel knysiaginp ddiqditilk
      241 daaataiyga raangvivvt tkkgkkgnmk inisantfvt qrpdfdklnl mnanekvdfe
      301 lylasrkdlt yrndkgaiar ilkqdnaydt yqnqgfsalp tqtqqainal rdgnahwdkl
      361 lyrnafnkqy tasisggndq ndyyfslgyy deegtttgtg fqrynlslnn tfritdkfki
      421 gtsvlasqtd kesylsdtdr ftnpsnysrd vnpyffpyde kghfafdkdi qgysdryvpf
      481 nllqerqnta ytlknlslka ildleykiwn nltfvsqfgl qrdqdktekf anketyftrk
      541 yressryyds strtykyflp eggiiqnwnt dffqynwknt lqyalnfnnl heidllvgse
      601 lrynqvigvh tkgfgfnekn lttqgivfnn sdnansslyr tylkndnena fvsfyatgsy
      661 tynrkytifg slrsdgsnlf gvdpkyrylp lwslsgswlv seesflkdnt fvpylrlras
      721 ygfqgnidkn tspfvvgnyq nhtflpgynq stinvtsppn nklrwekten ynvgfdagff
      781 nnrirlagdw yerkstdlig lralplengf nsttvnwaqv snkgyeisls tqniktdkfd
      841 wkttisfshn kshvdriqvk endrmpsreg lpvnaifalk tngldanglp qfvdkegkst
      901 siiehfklyd pwelflpgem teskltpkei relytfmgdr dpkfsggiin tfrygnidlt
      961 inanfnleqt mvrtapynpa qidrglnysr dvlnawtpdn qqthmpriig qstltgddwm
     1021 aykwlsgsda tygmntiasl dtwvkqmsyl rissirlgyt lpqefskrig fdnfrlsieg
     1081 rnlmvfstdy sgffdpetyg niyaqplaks ltvglnlsf
//
LOCUS       WP_095918213            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095918213
VERSION     WP_095918213.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123122
     Region          20..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkglvlffv lltavvwgqk nvtgvvkdqq gvpvigvnvv ikgtskgvst dfegnfvlsa
       61 kegnvlvfsa igyktqekkv mkngafisvv meedlmeige vvvtgyqtvd ptkvatsytk
      121 idiknferrg tpdvisgieg lsaslvlsnn pndptgskef sirgvstlsg ssrplivldg
      181 fqyegkledi npyevesitl lkdaasasiy gakssngviv intykgkegk tqvrytsnlt
      241 fqdkrdldyv mnrvsssklv diqhqyaqsi dpyvknyrnl vetndptasy nagttnrvyy
      301 lyglkkygyi tdqefnnqld llksydntkd ierlylqspi tnqqnisvsg gseafkyrts
      361 lnythstkdi knnenqrfif dfvsnlkfss kvnldfqmgl isnnnsykli edgqrilegs
      421 difqlssydr lfdangssls vfkpnlnvgt nsgglfggkd pyeierlvaa glldetyypa
      481 ldfgkytlke adwtahvqgl lnvelteglv akiggqlrkk vekrsnmaar dswymkslin
      541 nttplsfsgd vkdltipyga rlregrgetl nylfrtqley kktfgehnlh lfagaeiqed
      601 kleltkvdrl gydpksniyi ntnykklkdd iedvyhpdrn iaggipfdeg fqetqnryva
      661 aysnftylyt dkyvvsgsir mdqsnlfgtd pkyrykpfws lagrwrlgee aflkdknmkl
      721 dlrvsygvng niankygpfd iaekgfeyra gnisalkien lkinnlrwer setanfgadl
      781 sffdnrlglv ldyyrknttd alaeiesdpt ygsnfidrnd aslinngyev mltsqnirsk
      841 dvlwetqlff rynkskvtqa sfntnkgkay kyagqvlnik dsepnslyvf dyggvsdtgd
      901 aqirkadgsl vkvqnnyqap nlfnyddlkp agtvlpkyva sinnnfsykg irlsflflyq
      961 gghimlkdsy ngspignyiv linkdteraw qkpgdesftd ipklnsviys siikgstknv
     1021 lpadfirlrd vvlsytlpts llgnlkikel tlnmragnlw lwtknkegid petqglgvrt
     1081 aripksytmg inlif
//
LOCUS       WP_095918829            1133 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095918829
VERSION     WP_095918829.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1133)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1133)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1133)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1133
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123432
     Region          25..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkllvalm lvmgvfmqsv laqvrtvsgq vtdesgmplp gvsvvvknts kgvstdfdgk
       61 yslqanqgdv lefsyigfat qtkkvtgskm dvvlkeeteq lgevvvtalg vnkqarsvgy
      121 attkvdvaei grlnvvnpvn alqgkvagva intvgssgvt sssgitirga ksidknnspi
      181 fvidgmiiqe avtgalqgtd wgsqlknlnp adyesitvlk gaaatalygs rgangaiviv
      241 skggkfgkqg lgiemshsve mgdiykspia lqnvygagsp lngyeggflg dgslqgtats
      301 fgpkmegqmi nqympdgklt pfvahpnswr alyqtpvnvq hniainggge tssfrlsysy
      361 adnngvfarn nfnrntlafk glmklnnvff veagvnyafs saqnggnqga wnyggnlpmm
      421 styytprnfd matyqaiyrd pvthavetds pwstlrgylh drdlnlrkry enslltnltl
      481 raeiapwlta sikgnynyys istldktygt gvdygptrtg gysrggsnsg synilgmlqs
      541 ndnkfniage eftfdaivaa elygnleshs wskstkgglv vpgvfafsns aetiipnfty
      601 tprnnqtfgl sgilnfgwrd qlfleitgrn dwlstltypt ymnlgknnys vfypsvnasy
      661 vftesfnmpe wfsfgkiras iaevglgtsa yattrgfgvf sqssqfdpnr nsvlvanpnl
      721 gtawnadlkp eiqrsievgt dlrffnerln ldftyyktnt rnqilsigav aeagatnqli
      781 nagniqnqgv evqlegtpir tkdfrwtlga nftknkgkvv klhdnvkewk lldvydagpe
      841 iwayeggdyg vittsygsga gaaiyrfnnp dnaadprngk pvikyvgagg npnkayvydy
      901 vrntdkgisd rvvlgkvead fylslntsfs yknfdfyali dgrfggnffs htrkyavstg
      961 atvsslegra qeyggvartn ykgemvydai mldavfdega taplasdpsk ridvagktya
     1021 ealqegiapm mgstywlysh rwgapnelni qdntwlmlre itlgyrlped ickkfganyl
     1081 rlgvtarnlg ylmnkltdgl npesvssnnp ltpmdiggap fhrtysfnlt lrf
//
LOCUS       WP_095919756            1120 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095919756
VERSION     WP_095919756.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1120)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1120)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1120)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1120
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126640
     Region          27..1119
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqsmikkll ysvlllcsqw alaqtdikgt vtdakgepll gatvilkern vgvttdmegk
       61 ftirgeqgqt levsyvgfqm kkvkitsnnl kitlqeeteq lgevvvtgyq kiksrvftga
      121 sasvkmneik mdgvadvsrm legrvaglsi qnvtgtfgsa prinirggas iignvqplwv
      181 idgavyedlv slsldqlvsg davtlissai aglnatdiqd iqvlkdasat svygaralng
      241 vivittksgk rdtpnritys yeqsfrqvps yreydllnsq etmsvyqela nkgyfglrda
      301 lygrrsgiyy qwykgistin pntgtyyyen teegkraffk ereytntdwf nhlftlnpiq
      361 nhtitfsggg kntttyasig fyndggwtit dnvqritanl kntfyindkf kttlsaqgnm
      421 rqqkapgtft qrknttlgsf erdfdinpfs yalstsrtlr prgsngeley yrnnwapfni
      481 lneyqnnyln inlldfkiqg easykfnndl eatvllstrq aftatshfik egsnvvqafr
      541 anetpwvaqq niylikdkdn pllqpkvglt hggifnktet tlksyqarfa ldynkqlgeh
      601 dikgfgfaei rsadrsvnpf qgygiqydkg nqiftnplif qkllnegtdy fslleryerg
      661 vtfslsgtyg yqgkyifntv lnyegsntag rnsrsqwlpt wniggkwnid qesfmkdqny
      721 fstlafrasy gltakmneqa insnavyknq ilnrfrfedr enalrilhle nrdltwekmy
      781 elnigidagf fnnrlnatid vyqrnsfdli dlirtsgvgg qyykyanfgd mrtrgvelal
      841 nskniltddf kwttnftisy mnqeitrlln tpntfdmvag agrgnivgfp kgslfsfnyq
      901 glnsyglptf dfglyplnnr aygnisgadf ldaqysktyl iyhgsiepnv nsglsntlqy
      961 knwelsffit aqagnkirln psfdpafadl nvfsteyynr wiapgdewrm evpalpsqdl
     1021 irligeenie rayntynysq nrvadgsfvr mknislgynv pehyakkfgl stinvrgqvt
     1081 npfliysdkr lkgqdpeyyr sggvslptpk qftltvnvgf
//
LOCUS       WP_095919951            1119 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095919951
VERSION     WP_095919951.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1119
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126378
     Region          24..1118
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfiqhfict ivlfagvayg qneriitgnv tsssdkmplp gasvfipskv vtsetavkgi
       61 lesvgigvva dfdgnftisv pqgtkqlavs figfetkiit lskaknhyni aleeetnalq
      121 evvvtgyqki ekrkltsavv kvdskdiiqa gvasvdqllq gqvagmvttv gsgapgelak
      181 irirgtasls gsqdplwvvd glplegneap dltkgnidel knysiaginp ddiqditilk
      241 daaataiyga raangvivvt tkkgkkgnmk inisantfvt qrpnfdklnl mnanekvdfe
      301 lylasrkdlt yrnnkgaiar ilkqdnaydt yqnqgfsals aktqqainal rqdnahwdkl
      361 lyrnafnqqy tasisggndq ndyyfslgyy deegtttgtg fqrynlslsn tfritdkfki
      421 gtsvlasqtd kesylsdtdr ftnpsnysrd vnpyffpyde kghfafdkdi qgysdryvpf
      481 nllqerqnta ytlknlslka ildleykiwn nltfvsqfgl qrdqdktekf anketyftrk
      541 yressryyds strtykyflp eggiiqnwnt dffqynwknt lqyalnfnnl heidllvgse
      601 lrynqvigvh tkgfgfnekn lttqgivfnn sdnansslyr tylkndnena fvsfyatgsy
      661 tynrkytifg slrsdgsnlf gvdpkyrylp lwslsgswlv seesflkdnt fvpylrlras
      721 ygfqgnidkn tspfvvgnyq nhtflpgynq stinvtsppn nklrwekten ynvgfdagff
      781 nnrirlagdw yerkstdlig lralplengf nsttvnwaqv snkgyeisls tqniktdnfd
      841 wkttisfshn kshvdriqvk endrmpsreg lpvnavfalk tngldanglp qfidkegkst
      901 siiehfklyd pwelflpgem teskltpkei relytfmgdr dpkfsggiin tfrygnidlt
      961 inanfnleqt mvrtapynpa qidrglnysr dvlnawtpdn qqthmpriig qstltgddwm
     1021 aykwlsgsda tygmntiasl dtwvkqmsyl rissirlgyt lpqefskrig fdnfrlsieg
     1081 rnlmvfstdy sgffdpetyg niyaqplaks ltvglnlsf
//
LOCUS       WP_095920196            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canimorsus].
ACCESSION   WP_095920196
VERSION     WP_095920196.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canimorsus
  ORGANISM  Capnocytophaga canimorsus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Capnocytophaga canimorsus"
                     /db_xref="taxon:28188"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114042
     Region          49..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 midllsrsns kgklgkflli alacglwada vyakaeitsv revveqqtkk vsgtvtdesg
       61 qplpgvsvfi kgtqrgittd fdgnyqiqas qgevlvfsyv gfvtqekivs stgnelvini
      121 slkeetqqle qvvvtalgik rqekalsynv qqvkseeltr vkdanfvnsl ngkvagvniq
      181 ksssgvggqt kvvmrgaksi lggnnvlyvi dgvpmgentn rergdqkfgt passegiadf
      241 nsediesisv ltgpsaaaly gaaaangvil intkkgkegk mkvnlsssve fsnplilpef
      301 qntygtsdlf fswgdkldtp ssldpkkffn vgttynnaln fsvgnkqnqt fvsaasitse
      361 givsnnqyrr hnvlirntss flddkleldv sasyvrqfek nmisfgeyfn pivgvylfpr
      421 genfewmksf elydmekgyn aiqnripgdl gkdiqnpywi myrnvrpkvr drymfsgqlk
      481 ynifknlnia grvrldntys ksedkryagt lgafakekgr yaysqgtfkq kyadlimnyn
      541 tsfaddfnlv vnagtsfedy dnkgksyrge ikhiankffi sntdastavv sdeggndrrr
      601 niavfasael gwksalyltl tgrndwasql vnsdeesify psvgvsavit ellspetknk
      661 lypylgfaki rasftevgsp isvtgitpgt itkkieggsi kandfyplta plkaertrsf
      721 evgistkwlk nrlsldvtay ksntynqlll aglpkssgyq tmyvqagnve nkglevalgy
      781 nqevadfnfg tsltatanqn kiirlasgip npfdasspid ikemtvgnfy lreggsigdi
      841 yannwikrdk yglvdissgt iateatepym lgsvnpdwll gwqgnlgykn lslnflfkar
      901 lggvvvsktq qildyygvsk asadardlgy aqlgsfkvnp rayynainal dayytysatn
      961 vrlqevslty sfpkqalgkt fsdlsislig nnlwmiynka pfdpeltstt gtfgqgydyf
     1021 mlpslrsygl svkigf
//
LOCUS       WP_095927757            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN2].
ACCESSION   WP_095927757
VERSION     WP_095927757.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN2
  ORGANISM  Flavobacterium sp. ACN2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Flavobacterium sp. ACN2"
                     /db_xref="taxon:1975676"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109586
     Region          25..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfifsfla llllptymmg qaqaikgkvv dsngmgipga iiasadarat adadfdgnft
       61 inakpgdilk vsmlgfdsvs vpataapmsi tlkeagdtal kevvvigygt rkkidntsav
      121 ssikseeitk mkvinasqai qgkaagvqva tsdapgstps ivirgvgtal ggrnplyvvd
      181 gmptdninni nsnditsyev lkdasalaiy gtrgangvim ittktgkgkl tvdidsyagf
      241 rsplkkvkma nadqyiqynn aafisqfpag rfsqnqpynt nwfdeitrtg vytqnnvsls
      301 gsgenikyff svgnyeeegi lkgteygrtt frsnneykis eklkisqnfs vssikntpqp
      361 msaftsayrq splvpvrfpn gkygvpfiqn gvisqtgdsf nsvgnpvval dynneqqktv
      421 tlqgglrldw dimkslkfts qfngeyftyk qynfvdnlgl wlaadpsrve asydkkslnt
      481 ntltrntddy fnwnlsnyft ynkvfaeihd vevtagiean vigtrsktta dirnvnpnsn
      541 ywgldginya qnggvttyka vndnqarlas yfarfqykll drylltgtvr rdgssnysnd
      601 yrwgtfpsvg igwivtkesf lsdiknldll kvrgswgklg nqkvplniqs ftsgvdyngg
      661 sgttinsqid pslsweivee asagidvelf nsrlkgsfdv yskntnnail nvtpystsgi
      721 tvespthvge vsnkgyeial rwddkitdnl sywvggnfsh nknelaslkn vrlatinggs
      781 lgngqvtkil dntsvgqplg sfymyeyagv dpangqmlyy tadgnkvaqg aldqtkdrky
      841 vgsvlptsty gvtlglnykn idfsvdgygt ggakvyngkk aqrfygenve tsllndmwtp
      901 tntsgsnpap fnqvpvasty ylesgdffri nnitlgyklp lkeegfinyc riyvnamnpf
      961 isqkfsgfsp evlgdgelvk gtqgvelday palktfvvga nlkf
//
LOCUS       WP_095929166            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN2].
ACCESSION   WP_095929166
VERSION     WP_095929166.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN2
  ORGANISM  Flavobacterium sp. ACN2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Flavobacterium sp. ACN2"
                     /db_xref="taxon:1975676"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115828
     Region          32..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiklkryaw lciflisigv kaqetkpliq sklegtvvda vtkepiigas vtiqgtthgv
       61 itdtdgkfyf qtgqkfpyvl lvsylgykkq evvvnkndit idlteeqnal sevvvtalgi
      121 skekkslgyt tqsvkgkela ttketnflna lsgkvagvri tnsqgdmgss riiirgetsi
      181 agnnqplfvv dgvpvdnsql nfggatrdfr naiadlnpqd ietltvlkgp naaalygsra
      241 ahgvvlittk sgkgqkggfg vtfntgltvs qvatlpsfqn tfgqgsngrf syvdgkgggv
      301 ndgvdeswgp rmdgrlipqf yskgeavpfi ahpnnvkdff ntgltydnsv siakandksd
      361 frlgvnnqkq lgtvpnsein ktnfsintny qisesvkvgv nanyiatnap qlpggpsggr
      421 aagvmlqflw fgrqvdinel ekdrntnwnn syysnpywna yynttsqqrn rligdihlda
      481 klaeglnfrf rtgvdyyndr rkytikygtn gtpfgsyaed aytvneqnte gifqytkqln
      541 ddftvdalag fnirnhsdan nyqkaprlav pdlytltnsr dpltssnsls rlrvysayas
      601 aqfgfrnyaf lnvtarndws stlpssnrsy fypsingsvv ltdalnikss tldflklrgg
      661 wsevgndadp yqlatvynfq tafdgnpiqt ssqrklnenl kpettrstei ggeasfwknr
      721 lhfdiayynt nsfdqileik ttaasgytsq linagkinnq gieiqldanp vqtenfkwnv
      781 avnysknksk veildyagdi knytigssgg vdvlasvgqa ygalygtaye rdasgnivvg
      841 anglpkadpt kkvlghytpd ylagltntlt yknlelsflv dasvggelfs gtnrtgnytg
      901 vlaqtlpgrg aengglsyyy pgnntanpkt lvtggaapgg atiyddgmif ggvfadgtpn
      961 nkvisaqeyy kasyniseay iysstfvkmr eikltynfnk klikklgleg asvtaagrnl
     1021 ffiykdapni dpetafntgn aqgleslalp ttrnfslnln vkf
//
LOCUS       WP_095928750            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_095928750
VERSION     WP_095928750.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118375
     Region          25..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklklngflv llvalitqlt faqertvsgi vsdnagmplp gvsvlvkgtk sgtqtdfdgk
       61 fsikatssev lvftyigmkt qevaassttl svkltsntte lesvvvtalg ikrekkalgy
      121 stqelkgedl vggttganfl ndlsgksagv yirkntnfgg stnvvsrgvk nltgnnqmli
      181 vidgmpinns nvnssngsqt agarntydyg nagmdinpdd ietlnilkga aasalygfqa
      241 gngvimittk kgkaqkgmgv tissefgvgs vdkntfpvyq nkygqgygpt yktdgtpngi
      301 pvgptgaffv mdkngnqvvs ttddasygva fdpnlsvltw esytpyssky gqkspwvaak
      361 ngpitffeta qtfnnsisfe ggsdksnfvi nynnykengi lpnselrknn asikfnhklt
      421 dklsasvfan ylaqttqgrn ttgyggdnva glfrqwwgtn vdiqsqkevf qnsggqnisw
      481 nmadpangnt spkywdnpyf tryknyqtde rnrfigygql dykftdwlna tgkistdsys
      541 elreerkavg slagtfginr lavgsgyqky tgmfseqnyq ftlnfnkkln ddfsltglvg
      601 ynalrtrrts tlastdggli ipgiyalsns vnaspfpiev edntavnsvy asasvgfrdf
      661 lylegtvrnd afsqlpqddn dvntfsvsgs yvftkhinap wlsfgklras yaenpqgsid
      721 syalqdvftk fnpfgsnqly srpniannpe lhpvktksqe lglemqfldr rigfdvsvyk
      781 slsedqifpv dystatgnss ryvnagsven kgvevifnvt pvktndfqwd invnwsknen
      841 tvvdltpgvd vltigtfqgg vsivgtkgha ygdilgkdfi ysadgqkvtk ngvylqtatt
      901 nnvignvtpd wiggvrnkft ykqislgfli dvqkggdifs ldqyygqssg lftstagnne
      961 lgnpvrntla ngggvilpgv nedgtpnatr tpspevagsi ygyntnpqka fvydasyvkl
     1021 revsitysfp kqfiakagln dlrlslvgsn lwiisknlpd adpesgissg nlssgysggs
     1081 lpttrnigcn ltlkf
//
LOCUS       WP_095929280            1241 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN2].
ACCESSION   WP_095929280
VERSION     WP_095929280.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN2
  ORGANISM  Flavobacterium sp. ACN2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1241)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1241)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1241)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1241
                     /organism="Flavobacterium sp. ACN2"
                     /db_xref="taxon:1975676"
     Protein         1..1241
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=137932
     Region          144..1240
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkpvvkqrl lhqimkitlf qfvlalvfss vtlannvngq kkldtkvtit vdnltldnal
       61 skieksahvk fsynsrlpql gekvsieanq etlssvlsri lvpfnitfse vsnqivlqkn
      121 tintfsygnn hdslfeiltf gpiikgkvtd qsgsplpgat vmakgtktav ltdfdgnfti
      181 empanvdrll isyvgmetke igidntsptv vlteagqnlk evvvttgyek tskrtftgai
      241 skisgtelki dgvvdvsrmi egkaagvtvq nvtgtfgtap kitvrgsssi fgdtkplwvi
      301 dgvvqediin msfadlasgn setllsssva glsandiqsi eilkdasats iygsrslngv
      361 vvvttkqgrr dsplkisygl eqtvrtvpny sqfdilnsqe smsifkemea kgyldlpttv
      421 ngryggayni lgraintynp etgnylvnnd pvsrnnflkk yeqantdwfs vlfrpsitqn
      481 hslsfsgggk nntfyaslgy ytdpgwtiad dvkqissnik gtfyvndkln itlstlasir
      541 dqgapgsyes ekdvvfgkvt rdfdinpfny vlntsrtlrp yddngnleyy rnnwakmniv
      601 nelannfmei evkdirfqld ldykinphlt ynltgsarya ntsrehkile gsnvvgayra
      661 gtaigedgvn tlvrdqnifl yqdpndltap kesvlpnggf lrkftndmts ynlrnsvsyr
      721 nifsdkheve glfgtemrvv drtsdqftaa glqydrglta ftdpriieki inagdsyygf
      781 neekertvgf fgkvgytydr rytasvtgry dgsnrqgdsd ssrwlptytf sgkwnvaees
      841 fmkdvqsvnt lavrasyglt atagpatnsl aiyksaitdr fglddresgi rieelqngnl
      901 twekqfetni gldlgmfnnr vqlttdvyrr kafdlvdyvi tsgiggqrir qgnnadmetk
      961 glevgittkn ingkdfkwst nlnfsvyhqe itklqntpta fdlvdsnggn tvghprnsly
     1021 syqftglnnq glptfilqdg aennitdanf qdnlnvtkyl kyegsiepnk sfgfantfty
     1081 knlslyiffv gsggnkvrln pvydstyddl tvftkdftnr winpgdenyt nvpviadrrl
     1141 nanyggdrtl arayntynys dvriadgdfv rlknislswe fpadfkkkig vstftlkgsa
     1201 vnpwlvysdk rlngqdpefr nsggvafpvt tqytftlnls l
//
LOCUS       WP_095929394            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN2].
ACCESSION   WP_095929394
VERSION     WP_095929394.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN2
  ORGANISM  Flavobacterium sp. ACN2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Flavobacterium sp. ACN2"
                     /db_xref="taxon:1975676"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118078
     Region          25..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkfkgfai lvflltaqlf faqektisgi vsdgsgpipg anvmvkgtsn gvqtdfdgky
       61 kikaktgdvl vfsymgmkdq svtvgnsssi nikmqeggeq leevvvqvay gtqkkqeitg
      121 avskidskml etsqasnavq sltgkvagvq isansgqpgd apqvrfrgig sisssnaply
      181 vvdgipfngd insistqdie sisflkdass nalygsrgan gviivttkkg kkgqltvtye
      241 tkigvnsrav peydmikspa dyykavynrv kngliyqgqt panasniaaq nliegdtysl
      301 gynnynvann qvinpatgei nadakllyhd nwskalfrda irqeqylsls gstdnlnsyl
      361 sigylsddgy tinsnfervt lranvdynvs skvkigtnvn yahsnqnapi sktssstysn
      421 lfswarniap iytiwqrdds gnmiynqdgt ksydfnqkgd rpygsnlnpy attllniksn
      481 eenkfgaray asveflkdfn frynigydfl sgyyltsttg eggddmgvng rigtatkney
      541 tltnqqllsw kktlgehtld vlighessdf tskmlagqks nvvisnlpii snatkygyld
      601 gyndlykveg yfsrlnynyk nkyfvnasfr rdgssvfape nrwgnfygfg aawsvikesf
      661 fpktkwitdf rikgsygeqg ndninypvts qishrsyfgs lrnyyayetq yeivpdsdgn
      721 asvlnvfead ksvkwekskn lnigfdinlf drisieaeyf ernvsdliyn fpialstgts
      781 fvsknigdmg nkgieinlgv dvvknknvdf niwanatryr nkitslpkaf tdgiyrfevg
      841 apaysyflre fagvdkangd alwykdekdt ngnltgnkvt tnvfgdatty lskkdanpdv
      901 yggfgtllry knitfqasfa yqfggymydg vyqsamysgs dnigqnyhkd vtkawtidnp
      961 tsniprvdhi siyqmgnsdy fliksdyisl qdvsigynyn dtwlkdlgiq stkftlmgsn
     1021 lalwskrtgm dprlnrlger vnngqslnvy gvmrsvsfgl tvnf
//
LOCUS       WP_095930346            1130 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN2].
ACCESSION   WP_095930346
VERSION     WP_095930346.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN2
  ORGANISM  Flavobacterium sp. ACN2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Flavobacterium sp. ACN2"
                     /db_xref="taxon:1975676"
     Protein         1..1130
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125388
     Region          28..1129
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqalikrcs fllfalmsvl syaqnqvtvt gtvtdnlggl lpgvnvteks tknsvttdyn
       61 gkyqikvksg gtlvfsfigm kkieiplnnr sivnakmedd fnqlenivvv gygsqkkkel
      121 tgaiatikad dlmdlpvtnl sdalkglvpg vtvtsgtgrp gdagsvqirq tfslskdggf
      181 stpliiiddm iqvdpsngkp tleqfnrldp seiesitvlk dgsaaiygsr asqgaivvkt
      241 krgkagkakf synsqfaind avshskvlda yefgvfsnrf fksrvaapav idpatiysda
      301 eleqmkglny nwlkeawkpa iqqkhsfnvs ggtedityfa gatyltqdan lgnqkydkwn
      361 frtginakia knldfsasvs gnvgtvdksf tkassnisdg syasaaggeq adygfllhmp
      421 qhvpwqttvd gnqyyvspfp nsnknfgsan annniagwny fanlnngshq vtddntfnvn
      481 aslnyklaav kglsfkvtys rnqssayteq iqlpydlvri rdyqlqdkhl asaanpsfyn
      541 attnptgsyi letnvrnsrv yynntdgkst qgdfminydr tfgdhqigam vggeasevyn
      601 tftrlayeqt gkdylgdyrt agqlslsnsq atkveggtls yfgrlnysfk qkylfqfilr
      661 sdastkfape nywgtfpsvq vgwvmskenw fekglpwvdf fkirysigkt gkdniqpwrw
      721 eqyydlivdk gfqfgpgtat ggggfngngl tprvnpnrnv twdttiknnv gldinllknr
      781 lnftydfyyd kntdmltdms savgvpisvg gayaeqnygq idawghefsi nwsdkiksnm
      841 syniginfsy nnneikkypd qgnlvpssnt trvgyssfnp vwgfavwkgt stgdgilrtd
      901 edianywayl teratavggv pryfdinsvs gmrkgslayq dvagqlnpdg tlapadgqim
      961 kendyvklan ssrtygfttn lgfkydgfsl rtqiatswgg anfvdlvnqg tssannmwsr
     1021 esfwrdmyda ednpngkypn vaqwtymssp sdfwqlntfr cfvrnlslny dipkkvfadt
     1081 kiaaitlgvt gnnlwdlynp ypdhyrnmyd nssvnyptlr twslnfnvsf
//
LOCUS       WP_095930525            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN2].
ACCESSION   WP_095930525
VERSION     WP_095930525.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN2
  ORGANISM  Flavobacterium sp. ACN2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Flavobacterium sp. ACN2"
                     /db_xref="taxon:1975676"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109113
     Region          22..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiflifmi vftaqvslaq vknvkgvitd sdgmplpgas vavqggqkgt ttdfdglyti
       61 evqkgqslvf tyvgletqtv vvgdastvnv kmvqgasnsl nevvvtslgi kkarksltya
      121 aqelkgeelt rvkdpnlint vagkiagvav tksssgaggs tkvvirgnss fvnnqplyvi
      181 dgiplynqgt gqpngtfgdl aggnrdggdi vslinpddye gmtvlkgaaa svlygsqgan
      241 gvillnskkg kagvesfnin svttfdsaay lpefqsdyts adgdprswgd kkkvegdikd
      301 ffetgvtqit smsfskateg nstsltyant dasgiipgnh lkknnfgirq tskflndrls
      361 vavtgnyvaq tinnrptngl yfnpisgvys hprafslndl ktyevfdpvr nmnvqnypgf
      421 aavnesnenp ywqinrqksv dtnnffngai aldykvaewf hlasrysynr sesnfqkemy
      481 assatslvha tgryinanti gtqnyadllg lfntkmgenf sfngtfgasi nntkvtgltv
      541 dsgiggglny aniftlgnfv nnngnvqtga erevqsvfaa ttfgykdylf ldlaarndws
      601 stlvntndss ffypsvgvtg ilsdmftlpe vfnfgkvrat yaqvgndiag sitsptstiv
      661 agsivnppvg pmpgqtlkpe lksevelgte wrmfdnrlgf efsfydsktk nqfiqvpapa
      721 tnpfgytnya inagsisnkg felvlyadiv rgekfnwdtr inysqnksrv ndipaeegtg
      781 griiltdpgs nsyryslieg rpfgviegkn lkrddqgril vnddntiqrt dweevgnanp
      841 dfmlgwsntf kfgsftanil idgrfggevl sltqaindyn gvskatgdar naggvkingv
      901 rasdgtpvtt mdafdyyngt agrngasgey vysatnvnvr eisigytfkk dklpyvqsat
      961 isliarnlff lykdapfdpn valstgeglq gvdvfglpst rniglnlnlt f
//
LOCUS       WP_095931256            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN2].
ACCESSION   WP_095931256
VERSION     WP_095931256.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN2
  ORGANISM  Flavobacterium sp. ACN2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Flavobacterium sp. ACN2"
                     /db_xref="taxon:1975676"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112208
     Region          23..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrilavlgv illsslsaaa qnrlitgivt daenkgvvaa sievqgkpfs avtdaegrfk
       61 mnvpegkitl nissigfqsk qvvlqeketr vavtlaentq elkdvvvtsf gvkkqkkslg
      121 yavgelkgdd ltknkeinlg nalqgkiagv nvsapvtgps gssrvvirga tsasglnqpl
      181 yvvdgipidn tqqgnagmwg gadkgdgmss fnpddiasls vlkgsaasal ygyrgsngvi
      241 littkkgkng tgigvdfstn ssfntpasll kwqdqygaga pnasgvptrf nnlqelrdsy
      301 yfawgdkydg tpslsldgkt rpyqaygkdn venfyrtgys fsntlaisgg nestnfrlsf
      361 gntkdesilp ettfgrnnva lslnsapnkr isiesnaqyi sekshnrpyl ndsprnpsfp
      421 ttfmtpgtdi rwlsnpydan ggeedflgan vyhtnpyfat ksplnddlrk rfigsakvny
      481 nitdkiyaka vigiddinye yteieptgin yspggsienr ietrsevnas gflgykgdia
      541 kdlsldafig anrqhnrysg ikmkgnnfiv pfkyfygntq pdkteklfse sevnslfysa
      601 dlgykdylfl sltgredwfs tldpsnnstf ypsvsssfiy seviglpewi sygkiragwg
      661 nvggalpeay alaltyttpd gqtdslgqpi lgvngetipn rtlkpynvst iefgfentff
      721 nnrvstdltf yskkttndit dadvsqasgy rttkinvgei lnkgvefain vkavktenfs
      781 wnvgynfayn dsevlnlsdk ittktlegnr dgranvvlek gqpfgvikay dylrdangni
      841 vldtngkflr gnliiagqgv aptsmglsnd fsyknftlsv fvdakfggei ysatnqlgtr
      901 yglseitlpg retgvavsgt dvngnpvntt vsaydywrsy sdvtsnfvyd adfvklrais
      961 faynfpkayl qktpfqsvsl afsahnlwti ydkvpnidpe snysnsnaqg merasmpltr
     1021 nygfalnvkf
//
LOCUS       WP_095939676             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. HAR-UPW-AIA-41].
ACCESSION   WP_095939676
VERSION     WP_095939676.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. HAR-UPW-AIA-41
  ORGANISM  Pseudomonas sp. HAR-UPW-AIA-41
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. HAR-UPW-AIA-41"
                     /db_xref="taxon:1985301"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38935
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikkligqg hqvtvqsgag vkaslpdhvy evvganigda
       61 atvfgadlvl kvvapddael almksgavlv gmlnpfcnet iarmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vmlganhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpaswmq
      241 rqagavhera kqadivitta lipgrkaptl lheatveemk pgsvvidlaa aqggncplte
      301 vdqvvvkhgv tivgysnlaa mvpadasaly arnlldflkl vidkeghfhl nleddivaac
      361 lmcrdgnvvr tng
//
LOCUS       WP_095931503            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN2].
ACCESSION   WP_095931503
VERSION     WP_095931503.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN2
  ORGANISM  Flavobacterium sp. ACN2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Flavobacterium sp. ACN2"
                     /db_xref="taxon:1975676"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117079
     Region          27..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv lllvlvaqlt faqeravsgt vsdntgmplp gvsvlvkgsk tgtqtdfdgk
       61 ysikasssqv lvfsyigmkt qevaasssvv nvklsgdaqe leavvvttal gikrekkslg
      121 yssqkldekt vnstptnnfl nnlsgkvagl evktnsnfgg stnivlrgsk sltgnnqalm
      181 vvdgvaisnd nlnsasaksg rqgfdfgnsa sdidpnnies itvlkgaaat alygsqaang
      241 aimittkkgk knsalgvsfs sttsmgsydk dtfikyqkgy gangysgpnd sfytadangd
      301 gipdqvvdmt adssfgnafd pslnvfqwta fapgnanygk atpwvaaand pgkffqksfs
      361 tvnniglsgg dekgsynfsy tnnnesgilp nsrlnrniln gsftrnlsdk iktsafftfs
      421 dqstvgrnst gygdniltgf rqwwqtnvdi rdlkqaydvn gqnvtwnmnd plngnfspay
      481 wnnpyfdryk nyssddrtrv laganisydi tknfnvlgrv tvdtsndrqe lrkekgshae
      541 efglqaldet sgyelytrsf lqttydfiat ydlkisekis akllggstfi kshtdsfdgs
      601 ttgglvapgl ftlansmsfv apleqeinyn klglytqgsi dynriifveg syrrdqstal
      661 pqnnnkydyw slgtsfivse likqdwlnnl klranyavvg ndpvagrlgw kinngliggn
      721 lmfannstfv nfkdlrsekl kswefgvesa mfknrlsfdv svyqsnttdq ifnvpqstst
      781 gfassqvnag elqnngievs lfgspvktkd fewqvgvnws rnrnkvvsln agrdnlqlas
      841 wqngvslnat vgqpygtmrg tdyvydangn ktvdedgyyl latdkvigni qadwigglsn
      901 rfnykdfsln flidmkkggs vysldqaygq ytglypetag lndlgnplrn siangggiil
      961 dgvyedgtpn qsripanmvg agfgvevepn kkfiydasyv klrevgftyn vpskfldktm
     1021 aksisfsllg nnlwiihknl pyadpeagqs sgniqgfqsg vmpttkvysf nikatf
//
LOCUS       WP_095944674             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. ACN8].
ACCESSION   WP_095944674
VERSION     WP_095944674.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. ACN8
  ORGANISM  Pseudomonas sp. ACN8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. ACN8"
                     /db_xref="taxon:1920428"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39051
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigipleta vgetrvavtp etarklkiqg htlrlqsgag vaasapdeay vavgveivdr
       61 itafgcdlvl kvrspqpdel alfkpgatlv gmlnpfdkeg lqqlairqlt afaleaaprt
      121 sraqsldvls sqaniagyka vllaaqhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaaavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv tivgptnlas avaadasaly arnlldfltl vftpegqfqi nlednivaac
      361 lmcrdaqvir kna
//
LOCUS       WP_095949749             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            boronicumulans].
ACCESSION   WP_095949749
VERSION     WP_095949749.1
KEYWORDS    RefSeq.
SOURCE      Variovorax boronicumulans
  ORGANISM  Variovorax boronicumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax boronicumulans"
                     /db_xref="taxon:436515"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38399
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeta agetrvavtp etvkklvasg htvrvqagag iaasvtdaay qtagaeitda
       61 agalsadmvl kvrtpsdaea aqlkagavvi gmlnpfdaag lqrlaaagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadryqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf idvpyetqee kdaaegvggy arpmpaswlt
      241 rqqaevakrv aladvvista lipgraaptl vtedmvksmk pgsvivdiaa gkgadgiggn
      301 cplseadktv vkhgvtivge tnlaalvaad asalyarnvl dflklvvtke galkidledd
      361 ivaacritqd gqvtrk
//
LOCUS       WP_095951401            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095951401
VERSION     WP_095951401.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115667
     Region          32..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklnryiw lcvflisvgv kaqetkpliq sklegtvvda vtkepvigas inikgtthgv
       61 qtdfdgkfyf qtgqkfpytl ivsylgykka evvvdknavv ielteeqnql sevvvtalgi
      121 skekkslgyt tqalknkdia etketnflns lsgklagvri tnsqgdmgss riiirgetsi
      181 agnnqplfvv dgvpvdnsql gsvggatrdf knaiadlnpn dietltvlkg pnaaalygsr
      241 aahgvvlitt ksgksqkglg itlnsgitis qvatlpsfqn tfgqgsngrf sfvdgkgggv
      301 ndgvdeswgp rmdgrlipqf fsngeavpfv ahpnnvkdff ntgvtydnsi svarsdeksd
      361 frlgvnnqkq lgtvpnsevn ktnftintny qisknvkvgv tgnyittnap alpggpsgnr
      421 aagvmlqflw fgrqvdinql qsnrdvnwnn syysnpywna yynttsqqrn riigdihlda
      481 klaeglnfkf rtgvdyyndr rkytikygtn gtpfgsyaed aytvneqnte giftytknln
      541 ddfsldalag fnirnhsdan nyqkaprlav pdlytltnsr dpltssnyls rlrvysayas
      601 aqlgyknyay lnltarndws stlpssnrsy fypsvngsfi lseafklksn tldflklrgg
      661 wsevgndadp yqlatvynfq tafdgnpiqt ssqkklnenl kpettrstev gleasfwknr
      721 lhfdvayynt nsfdqileik ttassgynsq linagkinnn gieiqldgsp iqtenfkwni
      781 ganysrnrsk veildyakqi qnytigssgg vdvlasvgqa ygalygtayl rdasgnivvg
      841 anglpkadpt kkvlghytpd ylagvtntlt yknlelsflv dasvggeifs gtnrtgtytg
      901 vlastlpgrg aengglnyyl ngttktlvtg tppagttvyd dgmifngvyd ngnpntqvis
      961 aqeyykasyn iseayiysst fvkmreikla ynfnksfakk lglegasita vgrnlffiyk
     1021 dapnidpeta fntgnaqgle slslpttrnf slnvnlrf
//
LOCUS       WP_095951419            1185 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095951419
VERSION     WP_095951419.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1185)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1185)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1185)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1185
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..1185
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132382
     Region          132..1184
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkhnseky fsgrnhyyly lllmrsvtaf iwismcslya npslgqnkih vrfkntplid
       61 vfsilekqtn yvffynddvl ksantitldk datleeilnn alknnnltyd iidkqvvvkr
      121 nkkkpeqldy eltgtvtdkk gaplvgvnvt lkgkqlwdit rtkgdfriyv spndtivfss
      181 lgyktltvpv nnkrtisatl iadvlelhsv eiqasngyta lpkervtgsf evigakelae
      241 vptvdiasrl egkmagvnvd prsgnitirg tnsysgsppl ividgfpqsd ndfkfsrrgv
      301 pgssilsyln pddvesitvl kdaaaasiwg sraangvivv ttkkgkkddp tinfstatti
      361 gekidlgklr vmntaqyidy ekdlvaggfa addfnnwqak npsaaqqimf rqqrgeisln
      421 erdqllnqls qndnlgqinr yllknsattq ydlsvsggsd kstyylslgy nkdqaamign
      481 esksynvtln nsfqlksflk lntgvnyvss syqtntvane alsnvsttal rpydmiaden
      541 gngidryiif rpeiakgfed kgylpwtyny ldeinysnvv tkganirlna sltatvndwl
      601 nfeasgmytk isnktrslse ldsyysrnai neatsvntag klvygipvga ylynsnaend
      661 sqsmrfqmni nknfnenngl hflagsevre erregsgqrf ygydtdtnsg ssvnptvyyt
      721 tiygwqtyig tsdnsiskfr drylsyyslg sydfmnkyhi sgsvrfddyn llgasrknra
      781 lplwsvgtkw dinkefflrd vswldnlstr vtygkagsap gggfgsnsai igvgsidynt
      841 qlptsyislp enaeikwett ttlnfgldyg ifnnrlrgsv dlyykksndi ltnvpynpty
      901 gwsylnynta tldghgvdvn iggiiinkaf kwisnfnfay ntnevsdsrf katttnqyin
      961 sgqiegkplt slyaykwagl datgqstifk ndgttitpsq gisavapedl kymgttvapy
     1021 fggfmnnlsy nnftlgaqit yfmghvfrns vlqnyptysg vqygavakde lvadrwrqag
     1081 deaftnvpgl tnisynslnr yqmadinvlp adnirlqqis fgynvpskfl dktfikslsf
     1141 nfaarnlgll wvkndqnidp qylsnnnynt lapqrnytlq fncsf
//
LOCUS       WP_095952259            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095952259
VERSION     WP_095952259.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115427
     Region          25..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkikgili lvfilttqlf faqertisgi vsdasgpvpg vnvlvkgtnl gvqsdlngky
       61 sikakngdil tfsymgmkdl nltvpsgsil nakmqeqgee lkeivvvtal gvkknarsig
      121 yatqqvkasd itrgnnnsls galqgklagv qitpssgapg assqivirga rsftgnnspl
      181 yvidgmpvas qpdfstgngv sgsdianrav didpneiesi nvlkgqaasa lyglrasngv
      241 ivittkngkn saqngkpiit fntstsfeti skkpntqney aqgsngvfnp nastnwgpki
      301 selpndpiyg gnvanalngg vlqpdkyyvp qrakagldpw vnpraynnvn dffntgitin
      361 nslnisqate ktnysfgigt skqdgiipet gmsrytakav vdtklnnewk tgfsfnyiqt
      421 kinkstsand gaivgvfaap rsydlkgigy anpanpydqi yyrpsvfnnp ywaannnefs
      481 ektnrafgnt yiqyspivsl egnhkltvky qvgidswttn yrnifefgnk ldlsgqsssa
      541 hlfgttndvi nslftlnynl nitkdlnlnv lvgneynhqn tkeydemgta fnfgglptig
      601 nartiaaeey rrqirtvgff nnielsfknm lflsgtirkd iasnmprgnr dfiypsaslg
      661 fvvteleglk ensfisyakl rgsiaqvgqa gnyignyyts psygggfwsg qpiqyplggi
      721 ssyipnnvqy dpnlkpqntk syefgvdlkf fnnrvgidyt fskqnstdqi fsvplagstg
      781 asslvtnggk mrndvheltv mlnpvrakdf nwtlnanfsk idsyvealan gvdniflggf
      841 vtpqlrasvg drfpviygtg yardaqnnii vnaeglpvad gelkvlgeva pkftlggstq
      901 ftykrismga vvdwknggki ysgsnnlmny ygidartadr tsefvfpgvk engtpndivr
      961 ggvsdpnaqq qlqavlngia esavfdasfv klrevtlgyq fpkllnnsvd lrtsvfarni
     1021 llwskmpnld peatqgnnnf sggfeqwsmp qtksigfgmn ftf
//
LOCUS       WP_095952366            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095952366
VERSION     WP_095952366.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113965
     Region          27..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv lllvlvaqls faqeravsgt vsdnagmplp gvsvlvkgtk agtqtdfdgk
       61 fsikaspsqi lvfsyigmkt qeiaatsttv nvkladasve lesvvitaal gikrekksis
      121 yaaqdlkgsi ineggtnnav salsgnvagl qvtspstmgg strvvlrgvg svtgenrpli
      181 vvdgipldng nynstttqrg aggrdygdas adinpddies vtvlkggpaa alygsragng
      241 ailyttksak ksggkaeiaf ntgitfenvy impnlqheyg ggssstfqqq vingqtynia
      301 dyatdeswgp kydpnlkylp wnafdpefsn dylkekswin pkndvrsffn tgitrtnsis
      361 fakntqdsgv rfaftnqkte givpnssltk ntftvnantk msdklkvesm vtyvqtrgfn
      421 rpevgygdng lgqkffqwgq rqldydelkd yklstgeqrs wnrkawndat pnysdnpywi
      481 inentsndtr nriygngkit ynitpdlyav gnvyadiynl giqervaigs qalssftsss
      541 rtltdfnyeg rlhydkkfgk fslasfagan rrnsfltrvs gntvgglvlp gqynlsnsas
      601 paqstnedir drtnsvygfv slgyddflfl eatdrqdwfs tvyksvnyas vtgsfifsel
      661 tdiswlnygk vrggwaqagn attayrlqny adiaipfqgt prysqpgtag npflkpelkt
      721 tkevglelsl fdrrlgvdvt yydvvttdli tpiqvdpstg fnfalfnagk lqnkgieatv
      781 tvnpvrtqdf rwditwnfsk ndnklrelip gvneltiana pfqarllavv gqqygqiygt
      841 dftydangnk vvdaegayip saqkslgtit pdynmglrnn fkyknlnfgf lidmqeggsy
      901 fstshmwgsy sgmlehtatp glrengvvvd avyengaqnt svlpgqawaq qhygldamnv
      961 fdasyvklre vtlgytlpkr iigpfadirf slfarnlftw gldwkgmdpe masygsgntq
     1021 gleggslpst rtygmnlelk f
//
LOCUS       WP_095954261            1198 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095954261
VERSION     WP_095954261.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1198)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..1198
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133657
     Region          39..>114
                     /region_name="PRK06196"
                     /note="oxidoreductase; Provisional"
                     /db_xref="CDD:235736"
     Region          137..1197
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknlsakdc gvksalwdkf leimkkslil siflfnival aysqkkvtin arnqsvssvl
       61 ktitkktnve ffysddifda qrrvdisvnn advmavikel igdnyraefa nnklivialn
      121 pkiktiatss vieervkikg vvtnskkefl igatvwvkgt kdgavtnfdg syeimakkgd
      181 vlifeylgyk ktevtvtdsl iinpilledv saldevkivs tgyqnidker stgsfvtita
      241 kdlekvpvnn vlhrlegqva glqldiqdsd ntfvyqnkfg snqgkfsynv airgkstfds
      301 fgtntmpliv ldgtpteldi rtinpndiek itflkdaasa siygaraang vmvintkkgk
      361 qgqtrinfsq nygfsnkptl sklplmnssq vlnleqefvd knlvtdpasv tymlttpvsq
      421 gmdlmfqykr gqitqaqrda gldvlrgrnt ygqaeqyllq astsqnydls fsgaendysy
      481 fmsgsyskee tqskgtdgqr ltllsnqdfk lfnyvkmtts lrgsifkynd nglglsplgt
      541 spttllpynq ivgddgnsvd yyrryyaaqt ipleqkgylp wtynyideln nmdrtmdeqn
      601 fgatisatfp llkgldavgt ysvetstsss dniynentyy ardminsats inssgdlvyg
      661 iplggifqnn tfgktsstmr gqlnydgiig edhlinamgg iearetgetq dsrtlygyns
      721 ktqtsvdlps tqyvdvngyn ytltngnvhk dshrrflsyy anagytfknk ytltgsarld
      781 dynnfgvske lrrtplwstg akwnikeesf lkevnlvnsl alrasygysg ninlnvfpft
      841 nislsdldtf sqqpyafisq panpnlrwek tailnfgldf silnsrlngt veyykkdskd
      901 livefpvspf ygvsnnalvq naatlaghgi dlslngtilk akdfswnsal vvsfnktevt
      961 dsrfqnfsqy lngsggtppi egyalnsvfa frsagldatg rtqvydkdgn ivnsftslkd
     1021 iadmkymgtn ipsyygsfsq tfnykklsly ilatykfdyv lfkptyggyv nrqgrfnqyd
     1081 lntdidqrwr npgdeattsv pgiqgstgls yvryvqgedq imqgdhirfr elslkydmts
     1141 linrgivrga sisftarnlg ffwrknkdgl dpdflpytgv nmklpamamy sigfnvnf
//
LOCUS       WP_095954370            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095954370
VERSION     WP_095954370.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108960
     Region          22..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiflifmi vftaqvslaq vksvkgvitd sdglplpgas vavqggqkga ttdfdglyti
       61 eaqkgqtlvf tyvgletqti vvgdaatinv klvqgasnal nevvvtslgi kksrkslaya
      121 aqelkgeelt rvkdanlint vagkiagvav trsssgaggt tkvvirgnss fvnnqplyvi
      181 dgiplyngga gqpngtfgdl nggnkdggdv vslinpddye gmtvlkgaaa svlygsqgan
      241 gvillsskkv kagsesfnvn svttfesaay lpefqsdyts nagdprswga kqkvegdkdi
      301 kdffevgntq itsmtfskat egastalsya ntdsngivpg nhlkknnfgi rqtskyfkdk
      361 lsvavtanyv tqtinnrptn glyfnpiagv yshpraftln dlkefevfdp vknmmqqnyp
      421 gfaavnesne npywqinrqk svdtnnfftg sialdykiae wfhltsrysy nrnesnfqkg
      481 mygssasslv hptgryinan ligtqnyadl ialfntkind nfsfngtlgt sinhsratgl
      541 tvdsgigggl vydniftlgn fvnnngnvqt gaerevqsvf aaatlgyndy lfldlagrnd
      601 wsstlantdt pgyfypsvga tailsemaam pefisygkvr atfaqvgndi astitsptsg
      661 ivagnivnpp vgpkpgtslk nelksewefg tewrmfnnrl gfevsyytsd tknqflqvpa
      721 estnpngytn yainagsisn kgfevvlfad iirgekfnwe srinysqnks rvndipsest
      781 ggrivltdpg snsyryslie grpfgviegy dfkrdaqgri lvnddntlqr tdwteignan
      841 pdfmlgwsnt fkigaftani lldgrfggev lsltqaindf ngvskatgda rnagvvning
      901 vkasdgtavt smdpyeyysn tagrngvssq yiydatnvsv reisigytfn katlpfvqta
      961 sisliarnlf fiykdapfdp nvalstgegl qgvdvfgmps trsiglnlnl tf
//
LOCUS       WP_095954504            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095954504
VERSION     WP_095954504.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123656
     Region          31..1110
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqalikrcs fllftlmsvl syaqnssnqv tvtgtvtdnv sgllpgvnvt ekstkntvtt
       61 dfngkyqitv kpgatlvfsf igmkkseipv ngrttvdakl aedsnvlddi vvvaygtqkk
      121 nnvtgaivtl kpeefqdlpv snlsealrgl tpgvsvsgga grpgeaatlq irqtfgfskd
      181 gnsniplvvi ddmvqidpqn gkptletfnq ldpseiesmt ilkdgsaaiy gsrasqgaii
      241 vktkrgksgk pkftyysqfs indavshskt mnayehgiwk nrflnsnlea dqskyfsaae
      301 leqmkglnyd wlkeawkpat qqrqslsasg gtekatyfag ityfdqgpnl geqdykkwnf
      361 rtgtnikisq dlefsasvsa ittdvnksfs kasanlndss fgslaggeqa dyayllhmpk
      421 yipwqttvng kdywmspfpr tdrnlgsans nttiagwnyf agldagkqie eqfsynvnls
      481 leyklpfvkg lsvkgsfars qsssyteqyq lpydlaritn hhladnhlen pnsiyaidtn
      541 irgsrvyytt dmdkliqanf fatyartfgn hnvsamfgye qseawnknvr layegtskdy
      601 lgnsttagpi stnsqavkve sgtqsylgrv nysfkdkylv efifrsdast kfapnnywgf
      661 fpgaqlgwvv tkedwftenv swisnlklry sigktgkdni dywrwlqfye plpdkgaqfg
      721 snggllgggi tprpnpnenv hwdttiknnv gidigvlknr lqltadfyyd kstemligla
      781 geagtpitvg ggfaevnyaa idawgtefsl nwndkikdnf synvgvnfgf snnevkkypd
      841 lartdantni ttvgastffp vwgfntwkqt stgdgilrtd edvanywnyl terataaggv
      901 psymginnvt amrkgmlaye dtagvynast gtqagadgri mrnedyvkma nnnrtygftt
      961 nmgfkyksvy fktqiqtswg gynaldlvkq gtssahndwa hesfwtdmyd atdnpngkyp
     1021 nmaqqdyifa psdfwqmntf rcvirnmtfg felpkeamkq lniqkatlgi tgnnlwdlyn
     1081 pypdhyrnmy ddsasryptl rtwsinlnvs f
//
LOCUS       WP_095954745            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095954745
VERSION     WP_095954745.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109078
     Region          25..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfifsfla llllpsymmg qaqaikgkvv dssgmgvpga iisapeskts adadfdgnft
       61 inakvgetik ismlgfdavs vpatagmmsi tlkesgdtal kevvvigygt rkkidntsav
      121 sslkseeitk mkvsnatqai qgkaagvqvt asntpggtps vvirgvgtal ggrnplyvvd
      181 gmptdninni ntnditsyev lkdasalaiy gtrgangvim ittkagkgkl tvdidsysgf
      241 ktalkkvkma nseefarysn aafndpnkfs lnqpvntnwy daitrtgtfs enniaisgss
      301 esvkyflsaa nyeekgilng tdysrtsirn nneykisdkl klsqnfsvts ikntpkplsa
      361 fttayrqspi ipvrfadgky gvpfvnngva aetgsqfnsv gnpvsavdyn dekqqtvilq
      421 gglkldydit kslkftsqfn gefytykqyn yvdnlalwla adpnrvasay dtsslntntl
      481 trnrdqyfnw nlsnyftynk vfaeihdvev tagietnvig trekltvtrk nveansnywa
      541 ldnvqyapsv vgyndvalsq rklssyfarf qyklmdkyll tgtvrrdgss qfsdgnrwgt
      601 fpslgagwiv skedflkdsk iinllkirgs wgklgnqnvp lnnqtftsgl nygpdsgqgi
      661 svdssidpnl swevveelsa gfdvelfnnr lkgsfdvydk ntdnailyvi pfstsgltqr
      721 tathvgevsn kgyeislrwd dkinddlsyw vggnfshnqn klsslnnpsi aqivggnlgn
      781 gqntkllydt svgqplgsff myeyagvdpa ngqmlyynas gdkvaqgaln evndkkyvgs
      841 vlptlnygvt lglnyknidf svdgygtgga kvyngkkaqr fsgenieasl trdfwtptnt
      901 tasnpapfny vpvastyyle sadffrinni tvgyklplke dgfisfcrly vnavnpfitq
      961 kfsgfspeal gdgelvtgtq gveldaypsl rsfviganlk f
//
LOCUS       WP_095955173            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095955173
VERSION     WP_095955173.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111716
     Region          24..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkhlilll fifgilasys qnnvvkgvvt dgsgntlpga nilvqgtkdq tstgtdgtfs
       61 ikanqgavll vsyigfntke iivngvnlki visesaqtln nvtivgsmgi vrnksslgya
      121 vqevkgkeia etqrpnfata lqgrvagltv tstsgapgas aaiqlrgvns lsgsnsplyv
      181 vdglpvsnet mdqgltisna pnrtqdytnr gadinpddie svvilkgpea aalygmqagn
      241 gaivittkkg kkgvgrltys tntrfdnlyr fpeiqkvyqr gsdgvnnpdy rrqfgtayep
      301 gtkfynnven ffrtgvstnh nlsfeagtet tsyrlsianl eqegvvpntg ysrltanlna
      361 saklssklrs eatfnftksd nqkaakgags avqipgvtna gyllslltwp snddasvyln
      421 pdgtrrkits galdnetdnp ywdvnknlse dfnnrfitnv gliydptswl nltgrvgwdv
      481 nsgqgyraih pesaagiasg gyiesyysnt snlnttllvt akksfgkfnt klmvgnsvnd
      541 ndyrilsttg srffdpnfys inntdattqr sqeriiqsri igffsemsld ydkivyltlt
      601 gredwtsvlp dpffypsvst sfvftnlngl kdkeilsygk lrasyaeaan ipspysaepv
      661 ftpqlttdgg yaygvtganp nlkpefrksf elgtelkffk nrvgldvavy stktidpilk
      721 nmrlsygtgf vvtsanfgdl qnqgleitls gspiqkdnfs wnvsanfskt qskllnlpsv
      781 vseyyvsdtw lygnvrggvt vgnplttltg ndylrnnage plidpntgfa lkdpnfkivg
      841 drnpdfmlgl qntfvyknls lsflldirkg gdiynatefy lyqnglstkt ldrdqtrivk
      901 gvlrdglens atptqnnipv rpsvqneyyr tgaidadfie kdinwlrmrd itlsyqmpse
      961 ilkktfinnl slyltmtdlf iitnytgadp svngtnastg gaggtgfdfg vvstprginl
     1021 glkigl
//
LOCUS       WP_095955153             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095955153
VERSION     WP_095955153.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110266
     Region          39..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnftnhsvlq sfgnkllekk lgftiffllm flnsiaqtki qgsikdingg pisgvsimek
       61 ntsnnavlsd fdgnfqitlq kpnsklvvsy vgfisqevtv tnnkvdivll esveqlsdvv
      121 vvgygtqkks rvtsaiasik ekdftrgair dasdlikgkv agltissgsg dpsaapnisl
      181 rgisslksgs aplvlingvp ggidtvspne iasievlkda saaaiygtrg angvilittk
      241 tvnkemqpti tystfttvsn fakkadflda aglrslisqg vkvpftdega ttdwldqisr
      301 ssfaqnhnld lkggtaktny avnlnyvdqt gvfngtfnke yrfsfdvnhr mfndklkinl
      361 nllngtqkmg ihpdiagyay rqamirnpta pvykpdgtya etnrfqyynp vailnetdqd
      421 rqstwqrfta nltldllpgw dvsallaknk nsgldgyses kkhysnting rngvasrntg
      481 qtdrdfveft skynkkfdkh eftllggysy qytvnegfsa snfdfptdaf synnlgagna
      541 lsdgkasmgs yknddkligf fgrvnynfnn kydllfsirr egsskfgqnh kwgnfpavsa
      601 gwsinkesfl sdvsavnnlk lragygvtgv iptdsylsqt lynydgyffn dgkwvkglvp
      661 asnpnpdlrw ektaevnvgi dfgflnnris gsfdvyskkt sdmlwdysvp tppylyssit
      721 anvgkmenkg fevllniipv ksenfmwnss mtfshnknkl tslsndlysi drnfintgdt
      781 gdpisftthr levgqaigny wglksvditd dgkwiietad gtrktltpdl yndsnkqylg
      841 ngipnyvagw tntftykkfd lsivmtgafd fqilnsqrmf yenptinynm lssafdkvyd
      901 kavlnynqty vsyyleqgdy vkvdnvtlsy nfdvkpytfi sgmrvyasan nlavitkykg
      961 ldpeiardnv lsqgvdnrdk ypttrgftlg lnvtf
//
LOCUS       WP_095955253            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ACN6].
ACCESSION   WP_095955253
VERSION     WP_095955253.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ACN6
  ORGANISM  Flavobacterium sp. ACN6
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Flavobacterium sp. ACN6"
                     /db_xref="taxon:1920426"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111001
     Region          25..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miknvlkllf viclfgfqsl eaqttvkgti tdastgipip ganiivkgtk tsassdfdgk
       61 ysitvpnqaa vlvftyvgsa tkeiavgtqt tlnvalgadt qqlgevvvta lgikrekkai
      121 tysaqnvsvd elsearslnv anslsgkvag lnfsttsngv gsssritlrg nrslngnnqp
      181 lyvvdgvpis ngttnsnpdi dtggttqpdg isninpedia smtvlkgpsa aalygsrasn
      241 gvivittksg kagktsvsls snfmassayn lmnlqneygq gtngayvans ssswggrldg
      301 sqvsnwqlvr npnyagpatq syspqpnnvi dfyktgynla ntltvtsgne kaqgyfsytn
      361 traegivggn qmdrhnlnlr ltskisdklt ldvktnyivq didnllrtge esigtsayll
      421 prsiayndyk nfeyfdaagq rqvnyfldet gapggnpfws alrddartdk rnrfiglasl
      481 kyeftktlsl qgragldqmt nknvrnryat nafnsnmgsy sesyetvsel nvdallsyne
      541 kfgdwavgln aganalqqns salnsggvls krnffalsnv qtvqsqstas dkrinsvyaf
      601 gqlgfrnylf ldvtarndws stipndyfyp sfglsavlsd mftlpevisf akirgsyaqv
      661 gndtdpyqtq qrfsyiggng gmlygqstka npnlkpeiss stefgadvrf fnnrlgldft
      721 yftsltnnqi fyintpessg ysraivnggd ienkgieltl tatpiqtenf twditanyas
      781 ykskvksife grdelvlgeg rlvrskvvag geygdlyikg fqrdpngnii vnsaglplat
      841 ngfdvragnf npdwtagfkn nfkyknfsls flvdfrigge visytqarqa glgvsditla
      901 greggivvdg vvaagngtyt pnttsitaeq ywtsigqrtp iaepfvydat nirlrelvfg
      961 yslpkrilgd sgfssidfsl vgrnlfffln kaehfdpeag agtgnlqgie sfnipstrdy
     1021 gvnvkfgf
//
LOCUS       WP_095963107             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas ogarae].
ACCESSION   WP_095963107
VERSION     WP_095963107.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas ogarae
  ORGANISM  Pseudomonas ogarae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas ogarae"
                     /db_xref="taxon:1114970"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38940
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigipreta sgesrvsatp etirkivnqg hrvmvqscag vragvtnkvy eaagatigsa
       61 sdafgaelil kvvapsdsel tlikrgtvlv gmlnpfnnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvviangv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_095971538             369 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhodococcus].
ACCESSION   WP_095971538
VERSION     WP_095971538.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..369
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37909
     Region          13..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(25,80,99,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(54,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 metsksaqvr psvgvpress dgerrvalvp kivsaligkg vdvvvesgag lgalipdely
       61 taagakigdp wtadvvvkva ppsteeiari stgakligfl nprnadnria elkaagiegy
      121 aveaiprisr aqvmdalssq anvsgykavl laasestrff pmlttaagtv kpatvlvlgv
      181 gvaglqalat akrlggratg ydvrpevadq vrsvgaqwld lgidaagegg yareltdeer
      241 akqqqaleda ikgfdvvitt alvpgrpapr lvtaaavegm kpgsvvvdla getggncelt
      301 epgqtvvkhg vticsplnlp asmpehasel ysknisalie lmlvegalap dfsdevlaga
      361 cvtreekga
//
LOCUS       WP_096002683             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_096002683
VERSION     WP_096002683.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36112
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkyits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel vsymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_096037654             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096037654
VERSION     WP_096037654.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53544
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qdnirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096049105             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas mosselii].
ACCESSION   WP_096049105
VERSION     WP_096049105.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mosselii
  ORGANISM  Pseudomonas mosselii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas mosselii"
                     /db_xref="taxon:78327"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38913
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvgqg hqvtvqrgag lnasipdsay eavgatlgea
       61 tdvfgaqlvl kvvapndqel alinsgslla gmlnpfnnel igkmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvthngv tlvgptnlpa qvgadasaly arnlldfmkl lfdkdgnlvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_096064839             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychrobacter sp. FDAARGOS_221].
ACCESSION   WP_096064839
VERSION     WP_096064839.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp. FDAARGOS_221
  ORGANISM  Psychrobacter sp. FDAARGOS_221
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Psychrobacter sp. FDAARGOS_221"
                     /db_xref="taxon:1975705"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40079
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,126,129,132,173..176,196..198,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigtiqakq efegrvaitp dsvkklvklg heviiesgag qhayyddnay lnagakvase
       61 sdvlrqaqii cvvqnltaeq iaqlgnnsiv igmldlyrnd qldnyakqgt tafamellpr
      121 tlsraqnmdv lssqanlagy kavlmaandy arpfpmfmts agtvkpakvv vlgvgvaglq
      181 aiatakrlga vveasdlrps vkeqveslgg kwldvpmsde ekekakstgg yawvpseqym
      241 kdqaavvdka vsnadivitt aqipgrnapr lvhkttldkm kagsvlidma assggnvegt
      301 vagetvvtdn qvrivgaani patlaaqssd lyannlvnfi ttlfdkendn alhinledei
      361 qgalavthgg evrlqrr
//
LOCUS       WP_096070151             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_096070151
VERSION     WP_096070151.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38606
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen ivrmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_096071612             321 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Clostridium perfringens].
ACCESSION   WP_096071612
VERSION     WP_096071612.1
KEYWORDS    RefSeq.
SOURCE      Clostridium perfringens
  ORGANISM  Clostridium perfringens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Clostridium perfringens"
                     /db_xref="taxon:1502"
     Protein         1..321
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=37236
     Region          4..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mitniyskrl ekvdmtnniy eyelipdklr iqiifivrda fgnlnsvwet vkeqlcreyg
       61 leclvnyyve ddqkeceafl ktvknvnnfl dmvelifdii qnkmgpvirn nnytlknnpd
      121 glrilpedav velnhrfken nfgyefiegr iirmdrkfth nelvrpalnl lfeeefksan
      181 defliahtyy kegcskenpn edfknaiinc nkafestmki iceknkerlt nynikhtand
      241 lindlvkadi ipahlshsfh giknilkglk sslesglpvi rnkvghgkgt eeewvseefv
      301 tyainlaatn ivllvniykn l
//
LOCUS       WP_096074520             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_096074520
VERSION     WP_096074520.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38625
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqc hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_096084109             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_096084109
VERSION     WP_096084109.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38449
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaaxl aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_096088344            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_096088344
VERSION     WP_096088344.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125510
     Region          22..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkllyillf llaslsasaq tftlkgtvke tngtpllgat ivvkeshigt stdmeghfsi
       61 kaqvgqtlev syvgmktqri kikgeslqii lqeeaqaleg vvltgyqkiq nrvftgaaas
      121 vkmdnikmeg vadisrmleg rvaglsiqnv tgsfgsapri nirggasiig nvqplwvidg
      181 aiyedlvsls ldqlvsgdav tlvssaiagl natdiediqv lkdasatsmy garalngviv
      241 ittksgkrdt pnritysyeq sfrtipsykd fdllnsqetm sllqemnskg yfnlqntlyg
      301 rrsgiyyqwy kgvstinpnt gnyyypntpa aqaafmkere yantdwfkhl fsinpirsht
      361 itfsgggkns tsyaslgyyh dsgwtitdnv kritanlknt fyindqlkat ftavgnlrsq
      421 kapgtfaqrk ntavgaferd fdinpfsyal gtsrtlrpkd aqgnleyyrn nwapfnilee
      481 yrnnymkidv ldfkvqaeas yklnphlevt alvsarqaqt qsshyitens nvikafrane
      541 tpqvandniy llknkdnpla ppqialtngg ifnktetslk symgrlavdy hrtlredhdl
      601 kafgfaeiry adrtvtpfqg ygiqydrgnq vftnplifqk llnegnnyfa ltekydrgit
      661 fsasgtygyk gkyianavln yegsntagrg trsrwlptwn vgakwnidre dffnsknist
      721 lalrasyglt akmneqains ysvfqnyvqn ryrfsdrena lrlqhlenrd ltwekmyeln
      781 lgvdagffnn rismsvdvyq rnsfdlidli rtsgiggeyy kyanfgdmrt rgielslntk
      841 niqqqdfqwa ttisfsymnq kitrllntpn tfdmvsgtgr gnivgypkgs lfsfnyqgvn
      901 hqglptfdfg lyplnnrana nvvgadfldt qysksyliyh gsvepnviag lsntftyknw
      961 easffisaqa gnkirlnptf dpafgdlnvf skeyynrwlh pydelrtevp slpsqslinl
     1021 igkenieray ntynysqnrv adgsfvrmks islgyrvpkk alerygmssl tvraqatnpf
     1081 liysdsklng qdpeyyksgg vslptpkqyt lsfqigf
//
LOCUS       WP_096088503            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_096088503
VERSION     WP_096088503.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124414
     Region          25..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkeklmyall cavlfvgvaf aqehtvtgvv kddagtplpg asvvvkgtsh gvatdfdgky
       61 sikvpnnkav lvfsslgmkp iersvgnnka invtleveaq qltgvvvtgy qefdrskftg
      121 naqtlkadni kmdgvvdvgr miegraagvn vqnisgtfgt spkitirggs sifgdtkplw
      181 vvdgavqeev vnlsfeqlas gdastlvssa isginandie sieilkdasa lslygaraln
      241 gaviittksg krnvktqvny qleesvrmip nynqydimns qesmgvyrel eekgyfslss
      301 ytqaryggay nimyraidty npatgrfale nseaarlafl rkyeyantdw fktlfrpslt
      361 qnhtvslsgg genatvyasv gffvdpgwti adrvhrvtgn lkttynlspk vkigvltqgs
      421 irtqkapgty nrtantvsgg ydrdfdinpf syalntsral rpygddgkye yysynyapmn
      481 ilnelannym dlnvleykiq gdlevklakg lkynflgsvr hvkssnehsm kedsnvvgay
      541 ranrttviak anpflfkdpa npdkipqvvl pnggiyklte nnlqsyyfrn aleykhlfke
      601 khdlkvflgq eyrhtdrdnq tfngygyqfe rggtaftdyr iiqkaiqens pyfekgfske
      661 rgiafflqgt ytydnryvfa gtanyegsnq lgrsrsarwl ptwnvsgrwn asnesflkdn
      721 tkisnlafrv sygliaglga asnalavfkn gvanrynigd reniiqiddl qnmdltwekv
      781 yetnvgmelg lfknrvnlsl dlyqknskdl idyvrtsgig gqfvklanna smvtkgiela
      841 ldtkniktdn fswntginfa yfnqeithlt yrpnvynlvr evggnvvgga rntlysydfr
      901 glndkglplf nllngstdys kidfqqidni lsylkkegpv epnitaglsn tfryknwels
      961 alitaqagnk irkpdqydsn yndlsvfpke mrnrwinpgd ekitnipsip drrtvyevgs
     1021 ntlrrvynay nystervvdg sfvrmknisl syafpkevle qlkvsnltlr lqaanpfliy
     1081 sdknlngqdp effrsggvay pvtaqytfti nlgi
//
LOCUS       WP_096088562             917 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_096088562
VERSION     WP_096088562.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..917
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101788
     Region          38..916
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkykhnilfc slvgcmlwag avqaqsplnv peelstlsts svkgeqllkm pttnftnslf
       61 gvlpgltvlq gggmdnasln irglgsynyp svtyfidgyq sdfillspse iesitvlkda
      121 aalapfgmkg ahgivwittk rgaegkpvvr vdfqtgvqmp tvlskplsat eyaqlyneay
      181 sndagawtsf ynipndvkyn tdwydkvfkk salfdrqdvs irggsattky fvllghagns
      241 glyaskndds hssgrfdqyl vkanldfsml kifegnvnin griedrkspn yneyklwqnl
      301 asypniiypa qnpngsfpgt aihpdnpyas iralgiktlh drtlganfnl kekldfitpg
      361 lyiqqgvsls swtrgtrivs rdytrmfngv aqtthrdsny kvnddwgtnq wnrlqlllga
      421 gyarefgqnt fqtavnylqy vyniddnlng kaglnnnyay qniggrvfyd wnkrvsaefg
      481 fafggsdnyk kgnrfgfyha lsaayqvfne qhpsananin rlklrasvgs tgndvynegr
      541 ylyeryygsy ggggfatgnd dpswhsaigl kyvpnehifa ekaykynigv eakffnkwdv
      601 mieaflnkhe giitpdysis sifgatppyk nigkvtnrgf evstlysnaa gkltysvgan
      661 asyaknkidy maeydatsen saqtgrpigt rfgyeaagfy dindfdsngn llpslpkpsf
      721 gnvapgdvky rdlngdnrid padkteigks ylptltyagt lnlgyegfdl gvliqavqgr
      781 evnllddarq ktvafenngn vyaiaknrwa yypaqgidtr ssaqyprlsl lsnnnntqps
      841 slwikkanyl rvryielgys ipkrmldeig vsklriyvna anpftfssll tdydldpevl
      901 sgypalksvt mgvslkf
//
LOCUS       WP_096088634            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_096088634
VERSION     WP_096088634.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114497
     Region          24..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklnlfytwi ffltasfamv aqnievtgtv kdekgepllg vlvlikgtqr gaatnmdgky
       61 eiqtkvgdvl qysflgmktv ekkitasskr vdivlkddvq eleemvvtgy gapkiasrtv
      121 aqvaqvsskd lnnapvasvs dalqgrlagv vvssssgrpg snseiiihgy nnfqavqrge
      181 ntheplyimd gvavsssvms dfnpndieti tvlkdaasts vygaraangv ilittkkgrr
      241 nertsitvsh qlgfsaltsa srkffdnmmt preymdfwle kdptsiisaa gmsrmgstre
      301 vaeaaankil qenpyntrwd kiyfrdfvpm srtdvslsgg testsyylsl gyfnqegssn
      361 psvdykrytl ntnidtrvtk wlkvglslsa ghserdgssg ditarvtalp fysptypdgs
      421 rkdyitsitr nssmgfyhpe yyaekhprts vsddflpsgy itiepiknli fktqggiqys
      481 ysdseakelp sflnyrqrvp aptsnpftrf stdrslrktl tntleyrfwl gnkkehsfnf
      541 ligqesient aknvtvtayg qaadglstlm qgnknkvied dksantfnsy lgrfeysynn
      601 ryfldlsgrr dgssgfgagh rygnfwavgv mwklkqekfl kevkwlsdln lrfstglsgn
      661 sigggykhlt sikvddfyee kvgysvfalg npnlhweeqr kttvglnivi drgtsfniey
      721 ydretydmls srslnstsgq nqffdnaggm rnrgidftfs svvyrsknnd lsirpyfnvn
      781 ynkqevtslf gnkisdvgvs gvgykigrpl ewgavirkgv npttgeteyy vpgedrmeqv
      841 tddnkitnay dankliqttg kkmqapingg fgwsinyktf tvdmafsfsl grymmnydvs
      901 ytenparfgy snlsrnvfdy wkkpgdetrh pkitsnafvy gldsrllqda syvrmksigl
      961 syrlpkevid qvkffegvrf hatarniftf tkyegpdpes ssaislggyp psrqftlgid
     1021 lnf
//
LOCUS       WP_096088674            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_096088674
VERSION     WP_096088674.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113019
     Region          6..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msaqqieisg tvkdnkgepl lgvfilvkgt qrgattdfdg hyslkanvgd vlkfsflgmk
       61 tvekkltagt kelnitmqed vqqlegtvvv gyggkkvasr tvasvatvkg kdiaetpnas
      121 aidalqgkva glvistdsgr pganssvlih glntffsvfd etivseplyi idgavvtsdi
      181 mtmynpadie sitvlkdaas tsiygaraan gvilittkrg krnerthiai nhqlgfsmrt
      241 nvtrkffenm atpeeymdfw ilkepnalts lgrrlgytet tpreiadril aenphntrwd
      301 rvffrdfapv srtdisvsgg snvssyflsl gyldqqgika rsdykrynln anldtqiaew
      361 lkaglsisla htdmqsvsgg ggaetdilsl piysptqtdg krknyipsit ghqngfyhpd
      421 ylaekypadr ysdnimpigy lqiepvknlt fktqlgiqyn vdedysrgpl psfieyrydt
      481 dsnktvgqte rqmskylqrt ytnlleykwn ikdihnfdfl lgqesvesvm rsfsasskgq
      541 psdrltmlsh gpkeptvrds qsetgfnsff trleysyknr yfldlsarrd gssafgannr
      601 yanfwaigam wklkeekflq nvnwltsldl rfstgisgns sigdyrnrtl ispsntykek
      661 sgyflsmlgn pdimweeqqk ttlglhisiv kgtninlefy ernthktlaq gyinsasgft
      721 siphnigdmq nrgidftfst iafrsknnnw nirpyfnmny nqqkvtslyl nkeffansfs
      781 yagyrlneal qwtmpifkgi skdgnaewyl pnetnymiqq kddskttyqf dekqlmqttg
      841 kkmyapvngg fgvaityrnv sldlafsysl gkwlinedky ytlnqgsfga knfskdllny
      901 wkqegddtel prlnsayymr kdtrllenas ymrlksasis yaipqelidq mkffsgvriy
      961 asarniftlt kysgadpefs ntlsrggypp trqftmgvel kf
//
LOCUS       WP_096089243            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_096089243
VERSION     WP_096089243.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115169
     Region          27..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkesmllf vlllcctvam aqtrvsvigf vtgndglplp gvsvvvkgtt rgvstdfdgk
       61 yeiqvtpnev lefssigyas qlkkidtkkg tftlnivlke eaqqlgevvv talgikreqk
      121 alsynvqqvn veeltkvkda nfinsltgkv agvtinrsss gvggatkvvm rgaksieksn
      181 nalyvvdgvp mlsttstqgs grfnsqgtte siadinpddi esmtvltgas aaalygsaaa
      241 ngailittkk gkegkmniql ssntefgnpf vlpefqntyg sdgkvtswga klpddasryd
      301 vkdffrtatt ltnsvalsgg teknqtyfsa astnaeglvp nnqynrynft vrntthllnd
      361 rlridasasy ilqnhlnmin qgeymnplvs aylmprgygl qrarqferyn ptthiyeqvw
      421 gdltagpdgt fngsfagdys lqnpywvayr nlreskrery llslgvtldl kkwsptekwd
      481 isgrvrtdnt nftstdkrya stlslldmsk tgyfgiargy ekqtyldvlt nlnknfeweg
      541 vgrfslvani gaslqdtryd elgykgplrk dgipnvfnaf nidqgavktr pyqsgyteqt
      601 qsifgslevg ynswlyltlt grndwasqla nspqssffyp svglsgvltd llspetkakw
      661 yntlsfakmr vafssvaspf drelttptft fnedtkvwka vsyfpigelr pertdsyevg
      721 iatkwlkgtl sldatvyqtn tynqtikaei spstgfdgiy lqtgdvrnrg levglgydlk
      781 ikdkinwnsy ftmsynenki mslvedyinp vtgqregrsy lekggiggar yilktggtlg
      841 dvyatndfkr nadgnllvds ngkvnveeyg nrdnyvklgt vlpkynlgwr ndfnignigf
      901 gamfagrigg vaismtqaal dhygvskesa earnaggvnl dgykvpaqsy feergkgrva
      961 qyytysatnf rlqeayvsyh lprklvndki dvtlsivgrn lamlyckapf dpeavsstgn
     1021 yaqgldyfml pslrsygfsi kanf
//
LOCUS       WP_096088900             976 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_096088900
VERSION     WP_096088900.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..976
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110555
     Region          51..961
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvlnlktll llcifvllaq waaaqtqtat ttqtttqttt taqapmntnt rgatsisgst
       61 kplwvlngvv legsidlkpe dlvsedakml iaaaipglta esiesfkvlk dasataiygq
      121 raiggvvait tkrgttggss itytnestfr fiptygeyni mnsqdqmsvi qelirgghfk
      181 senqsitenk gvigrmydlf yvldrngnsv vpnteagrta ylqaaerrnt nwfnklfqts
      241 imqnhtlsfs sgtekstyya slsalfdpgw tkgdklsqys gnlnanynls pkfklnvisd
      301 lsyqkqttpk qdiydyavth srsmdskeyy vndfapynif neidnaykni nianlrlqte
      361 ltykitkkve atmmgairyy tnqqnteyke nsnyalsyra mpnslvrsyn prlyddpndp
      421 ydlpsvvlpe ggirerrdrt itsnhfratl ryndsfkggl hnvslyagae mdnykstddk
      481 nqnygvlfss gnysyytylf fkklqeenst yysiynttnn yqafftngsy tfgnryting
      541 tlrydasnkf aesryirwmp twnvgvnwnv tnekffdklk plshlsfkas fgvtaispsv
      601 snslsqiytn mpwrnsskre iglnivdnan hdltyeknqe lnlgtqfglf nnrinisaew
      661 fnrrsydlig nivtqgvggt itkkgnmael rihgvelgle ttnfktkdfs wktsfiysrs
      721 kneitklltn ptvrnmigys sssksvggfa kegyplrsif svpfnglndk glptfldang
      781 nstvsgirfd nrnvdfleys gtliptdkgs fsnyftykgi slgvvftysy gnvvrlrklt
      841 nsyndfwvap relnnrwqyp gdehrtnipv lyttymydly ggynniiqay ntydysnvri
      901 akgdnirlke isigytfdrd flkrnklrql smklqgtnla llyadkklng ddpdylangy
      961 spiaakrlif tlrvgl
//
LOCUS       WP_096089299            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            sputigena].
ACCESSION   WP_096089299
VERSION     WP_096089299.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga sputigena
  ORGANISM  Capnocytophaga sputigena
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Capnocytophaga sputigena"
                     /db_xref="taxon:1019"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113248
     Region          24..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklfyvfl fvlffsavat aqertitgtv rdanglemlg vavvvkgenh gtqtdlnghy
       61 sikvaqgktl efsflgmktq thrvgtssri dvvlqeeave igevvvlgvv kkkaaestgn
      121 tvqlsskdis tpsaisvdqa lqgktpgvvi naasgtpgae qtvmirgvgs mnssnkplyv
      181 idgvpvisen ltedkntvss mstlasinne diesltvlkd aaatalygar gsngvivitt
      241 ksgkrgktkf nvntsvgfqn dayfkrsplt gdqryhllkq glanqfasng atydtaidfa
      301 htnglringa enfnsalnnn nwseliknkn avmtsadisa sggdekgtyy vslgynrtes
      361 tvktsdpfkr vsglirinrd lndklkleas vngswvsqnp iteqgayftn pyvtkilmsp
      421 wvspynadgs ynvttfnryt glynylylqe hdvsknntlr glinfkvdye llknlvfstr
      481 anvdyissdy knyqnrvhsn asknngsshr imthhatwvy qntlsynfnv aekhkfglta
      541 lyeyqkykkn ylegygtnia adgltnlasv tkqktisstf edwanvsllg mlnysyaeky
      601 ildasirreg ssrfaeknry gnfwslglay nlhkefeala kvfndlklra sygltgnsgv
      661 dlnqyqvlla ydenydenga aypktlgnda ltweknrtfd vglnfalfnq rlrgsvayyd
      721 kytydlllnv plsrttgfee qainagamsn kgieaslgvd iirnenftwn lsaniatvkn
      781 rveelakdgt gadvdptags ehkqtkvget yaywymptwa gvnvntglpe wydkegkkts
      841 dynlaerrfq giaipkysgg lsthlqykgv fldasvyftg ghkvyeeysr fylrtnsfvt
      901 vnyngdaell nawqkagdvt dvpkmsysgn dnfhsvssrh lydgtfarlk ditlgyevps
      961 kylegtgfdg vtftvrgtnl ytwvkdsglk ldpevgnknn rmgyttlttp pvksvvfgvn
     1021 lkf
//
LOCUS       WP_096099415             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Enterobacteriaceae].
ACCESSION   WP_096099415
VERSION     WP_096099415.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53590
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apaktvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg kkkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096100678             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_096100678
VERSION     WP_096100678.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53788
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 aavwaypliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkqge
      301 lfvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_096102819             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas congelans].
ACCESSION   WP_096102819
VERSION     WP_096102819.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38838
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag ihasvpdsay eaagavigdt
       61 netyaaelil kvvapddeal sliksgsvvi gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 apakrlgavv easdvrpvvk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_096108587             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_096108587
VERSION     WP_096108587.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53870
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_096119609             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas salmonicida].
ACCESSION   WP_096119609
VERSION     WP_096119609.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53275
     Region          2..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrlt rlgfaalllt tcfgasglaq adevtpkgki earselfakd hvdqfsswkg
       61 tsesatrtda laedpqmvvl wggypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eqyydeigfa dwthtlskap mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqskemlqgi vqqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaqmk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llatkgishe ialpdistke kaqaalgmdm kqmnadkaqf lkttvpvwda eakaagrlaq
//
LOCUS       WP_096112615             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_096112615
VERSION     WP_096112615.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53755
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwvcpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_096122988             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_096122988
VERSION     WP_096122988.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53750
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsedel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaas aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_096127287             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_096127287
VERSION     WP_096127287.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38817
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lhasvpdsay eaagavigds
       61 netyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtdlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_096131296             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas congelans].
ACCESSION   WP_096131296
VERSION     WP_096131296.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35767
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maihdlyskr lkrkrgetpe iytydsipqe livqmfhifd dgignviytg rndiltvwes
       61 ivstlnreyg sftlarfshs kysthydefy hfmfsehnvd rlidgielal gamnttarea
      121 yyggrnnnde kidelieean qrlkehgvgy rfaenvivri dsefihaevt kpalsllqge
      181 wcagaeeefy rahehyrhgn fketlneclk sfesilksvc rkrgweisdk atassliqtc
      241 ldnglipsfw qshfsslksl lesgiptgrn kmsghgqgat ptevpryivs ymlnmtaacl
      301 lficeaeaef eql
//
LOCUS       WP_096131339             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas congelans].
ACCESSION   WP_096131339
VERSION     WP_096131339.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38810
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag ihasvpdsay eatgavigdt
       61 netyaaelil kvvapddeal sliksgsvvi gmlnpfnnel igkmaahgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa alggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_096133881             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_096133881
VERSION     WP_096133881.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38850
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lhasvpdsay eaagavvgdt
       61 netyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nfeddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_096137500             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_096137500
VERSION     WP_096137500.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38890
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag ihasvpdsty eaagavigdt
       61 netyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvtqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_096139839             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas congelans].
ACCESSION   WP_096139839
VERSION     WP_096139839.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas congelans
  ORGANISM  Pseudomonas congelans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas congelans"
                     /db_xref="taxon:200452"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38810
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag ihasvpdsay eaagavigdt
       61 netyaaelil kvvapddeal sliksgsvvi gmlnpfnnel igkmsahgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfnkdgafsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_096164942             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096164942
VERSION     WP_096164942.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53598
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqlindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096169861             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096169861
VERSION     WP_096169861.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53558
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa darsklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096174369             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cohaesibacter sp. ES.047].
ACCESSION   WP_096174369
VERSION     WP_096174369.1
KEYWORDS    RefSeq.
SOURCE      Cohaesibacter sp. ES.047
  ORGANISM  Cohaesibacter sp. ES.047
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Cohaesibacteraceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cohaesibacter sp. ES.047"
                     /db_xref="taxon:1798205"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55494
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkelf agenrvamtp ssammlqklg ydcvletgag ekagfndqvy veagveivns
       61 adalweavdi vakvrqpepe elkylakgkt lisffnpagn eegmeaakts ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv livgagvagl
      181 aaigtsvalg avtyafdvrp evaeqvesmg aefvyldfee eqqdgsssgg yasvqseefr
      241 naqlakfrei agemdivitt alipnrpapk lwladmvaam rpgsvivdla aerggnaegt
      301 vkdekvvtdn gvtivgytdf psrmaaqsse lystnirhmm tdltpekdgq vnhnmdddvi
      361 rgatvtfege itfpppppki qaiaaqpkke tkeltpeeqk eaeaaaarka grqqigllvv
      421 gaalmglvgl yapaafmghf ivfvlavfvg fqviwgvshs lhtplmavtn aisgiivvga
      481 llqigssswi vlllagisil iasinivggf mvtrrmlqmf qks
//
LOCUS       WP_096176981             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096176981
VERSION     WP_096176981.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53652
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfaphhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdred gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglk mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096215907             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096215907
VERSION     WP_096215907.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53630
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaareme aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096238109             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium svalbardensis].
ACCESSION   WP_096238109
VERSION     WP_096238109.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium svalbardensis
  ORGANISM  Janthinobacterium svalbardensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium svalbardensis"
                     /db_xref="taxon:368607"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38738
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qiivqagagl qasipdeaya aagaqigsaq
       61 eayacaivlk vrapdapera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpflteeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvikhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagseilrk
//
LOCUS       WP_096251631             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096251631
VERSION     WP_096251631.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53628
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdalt edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqlindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096252619             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096252619
VERSION     WP_096252619.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53603
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edqrlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096260390             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096260390
VERSION     WP_096260390.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53554
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaeikpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096277344             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Halomonas].
ACCESSION   WP_096277344
VERSION     WP_096277344.1
KEYWORDS    RefSeq.
SOURCE      Halomonas
  ORGANISM  Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas"
                     /db_xref="taxon:2745"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55519
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkesa rgearvaltp esakqiqklg heclvetgag laagfnddty rdagvtvvdg
       61 pealwrdaev vikvrepsde eaerlregqt liaffwpaqn eallekckaq gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aefvfldfed sqdgsesggy aspsspefre
      241 kqlecfreqa ldvdivitta lipgkpapkl wlddmvaamk pgsviidlaa ekggncdltk
      301 pdervvsdng vivigytdfp srmatqssll yatnirhmlt dltpekegvi nhnmdddvir
      361 gatvthqgei tfpppppkvk aigaakpkkk ekeptpeekk aaeiagfkaq ttrqvgllai
      421 ggalmlllgq vapvsfmqhf ivfvlacfig fqviwkvshs lhtplmavtn aisgiiilga
      481 ilqigsgsav vsvlaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_096283746             369 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium ahvazicum].
ACCESSION   WP_096283746
VERSION     WP_096283746.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium ahvazicum
  ORGANISM  Mycobacterium ahvazicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            simiae complex.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Mycobacterium ahvazicum"
                     /db_xref="taxon:1964395"
     Protein         1..369
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37745
     Region          9..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdaqlepvk vgvvaesgtd errvalvpka vaslvssgva vvvesgagar allpdelyte
       61 agatigdaws advvvkvapp tsdevgklrs gqtligflap rsaensigal kaagvqafal
      121 eaiprisraq amdalssqgn vsgykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwltlg ekdlaaageg gyareltdee
      241 raqqqqalek aisgfdvvit talvpgrpap rlvtaaavea mkpgsvvvdl agetggncel
      301 tepgqtvvkh dvtiasplnl patmpehase lfsknitall dllitdgkla pdfgdeviad
      361 scvtrkeds
//
LOCUS       WP_096292743             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas ureae].
ACCESSION   WP_096292743
VERSION     WP_096292743.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas ureae
  ORGANISM  Nitrosomonas ureae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas ureae"
                     /db_xref="taxon:44577"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39347
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir sgetrvaatp etvkkytakg vhkvlvqlga gagasipdsa yqeagamivt
       61 dvaelyaqsq ivlkvrgpes nelammrkda vllgllsphq edgvnalaqh gltafamekl
      121 prisraqnmd vlssqaniag ykavivaani yqkffpmlmt aagtvkaarv lvlgagvagl
      181 qaiatakrlg avveafdvrp avkeqveslg akfvevplsd eekaqaetag gyaaemsddy
      241 krrqgelvhe raisadiiit talipgrpap vlikestvqa mkqgsvivdm aveaggncpl
      301 selnknvikh gvhligianl pglvaadast lyarnlmnfl nlmldqenda lkidrsdeii
      361 agtllcaggd vvgkp
//
LOCUS       WP_096295689             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            weixii].
ACCESSION   WP_096295689
VERSION     WP_096295689.1
KEYWORDS    RefSeq.
SOURCE      Neisseria weixii
  ORGANISM  Neisseria weixii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria weixii"
                     /db_xref="taxon:1853276"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53861
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl agetrvactp atvaqlqklg fevvvehdag laasldnaay eaagavvada
       61 htvwqspliy kvnapaesei gllnagqtlv sflwpaqnse lvqkladkkv dvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvli igagvaglaa
      181 igtanslgav vkafdtrlev aeqiesmggq flkldfpqea gdsgdgyakv mseefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkags vivdlaaatg gnceltkpge
      301 lfitdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeiald fedviirnmt
      361 vtregeitfp ppaiqvsaap qqtpsekaap aakpepkpvp awkklapavi gavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwdvshs lhtplmsvtn aisgiivvga llqigqghgf
      481 vsllafiavl iasinifggf yvtrrmlnmf rkg
//
LOCUS       WP_096300058             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            sp. hl-4].
ACCESSION   WP_096300058
VERSION     WP_096300058.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. hl-4
  ORGANISM  Halomonas sp. hl-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas sp. hl-4"
                     /db_xref="taxon:1761789"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55346
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkesa rgearvaltp esaqhiqklg heclieagag eaagfndday rnagvsvvds
       61 aealwrdaev vikvrepsda evtllregqt liaffwpaqn ealleackaq gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflflefde tqdgaesggy aapsspefre
      241 kqlacfreqa pdvdivitta lipgkpapkl wledmvaamk pgsviidlaa ekggncdltk
      301 pdervvtdng vvvvgytdfp srmatqssll yatnirhmlt dltpekdgvi nhnmdddvir
      361 gatvthqgev tfpppppkvk aigaakpkkk ekeptpeekk aaehaafkaq tkrqvgllai
      421 ggalmlllgq vaptsfmqhf ivfvlacfig fqviwnvshs lhtplmavtn aisgiiilga
      481 ilqigtssvi vgilaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_096302476             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Jatrophihabitans sp. GAS493].
ACCESSION   WP_096302476
VERSION     WP_096302476.1
KEYWORDS    RefSeq.
SOURCE      Jatrophihabitans sp. GAS493
  ORGANISM  Jatrophihabitans sp. GAS493
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Jatrophihabitantales; Jatrophihabitantaceae; Jatrophihabitans.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Jatrophihabitans sp. GAS493"
                     /db_xref="taxon:1907575"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52831
     Region          5..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 malhigvvke sasgetrvas tpttvkqlla lgytvsvetg agerssfpds ayteagaqia
       61 ptaatwradv vlkvnapsea elpllaegat lvslispaln pelverlsgr pitvlamdav
      121 prisraqsld vlssmaniag yravieaahv fgrfftgqvt aagkvppakv lvagagvagl
      181 aaigaasslg aivratdprp evadqvkslg geflavevae qqvstdgyak atsedydrra
      241 aeiyseqald vdiiittali pgrpapkllt aadvasmksg svivdmaaiq ggnvagslag
      301 evvvtdngvt iigytdlagr lpaqasqlyg tnlvnlmkll tpskdgelvl dfddvvqrni
      361 tvvrngektw ppppvavsaa paatakpvaa vthepkapis tsrrytivgi gaailfllta
      421 fsppqlignf tvfvlaivig yyvighvhha lhtplmsvtn aisgiivvga llqighadva
      481 itilsfvail lasinifggf avtrrmlsmf skg
//
LOCUS       WP_096307151             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096307151
VERSION     WP_096307151.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53571
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta appkpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqtdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096308572             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096308572
VERSION     WP_096308572.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53361
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakxvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg kxkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096310624             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096310624
VERSION     WP_096310624.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53568
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfygkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw aagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096312635             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium pallens].
ACCESSION   WP_096312635
VERSION     WP_096312635.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium pallens (Mycobacterium pallens)
  ORGANISM  Mycolicibacterium pallens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Mycolicibacterium pallens"
                     /db_xref="taxon:370524"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52355
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgetrvaatp qtvgqliklg yevlvesgag vaasfsdeaf veagaavgtt
       61 aealgadivl kvnaptsaei aalrdgatli slispalkpe lveelstrpi tvlamdavpr
      121 israqsldvl ssmaniagyr avveaahtfg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaagslgai vratdprpev adqvkslgge ylsiespeae vsatgyakem gddykareaq
      241 lyaeqsedvd iiittalipg rpapriitad mvasmksgsv ivdmaaangg nvegtvkdqa
      301 vltdngvtii gytdlagrlp aqasqlygtn lvnllklltp ekdgtlvldf ddvvqrsvtv
      361 vrdgettwpp ppvqvsaapa paataapavq qtkqpmtmgr rlgitfgaaa llfllialsp
      421 aalqvhltvf alaivigyyv ighvhhalht plmsvtnais giivvgallq ighgdvivtt
      481 laavaillas inifggfavt rrmlamfsrs
//
LOCUS       WP_096319263             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096319263
VERSION     WP_096319263.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53425
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkxpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096322439             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096322439
VERSION     WP_096322439.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53459
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknxv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiz ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096349281            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096349281
VERSION     WP_096349281.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113205
     Region          19..1023
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkilyiilfi ispltafcqt vtgnvqdqeg kplagitvsv kdtkiatatn ekgqfrlvve
       61 dpaavirfts enmetheirl agqkaltvvl kqktnsldev hiiaygtstq rntvgsitkv
      121 sgadisaqpv tnplaglegr vpgmvvssts gipgasftlq irgqnavnps lsgnivapls
      181 qplfiidgvp yapqngninq fpslaspgsn nvynnkyggi spfdginpsd iesvevlrda
      241 dataiygsrg gngviiittk kgqagktqfn lnivdgesvv ghtmpmmnts qylamrkqaf
      301 andgltpnni qydqayapdl tlfdttrntd wkkyffgnta hnlnvnssls ggtantqfrl
      361 gagfnrdtyi fpgdyadsra sfsanvhhis dnkrltvdft atysyeknns sgnpnlllay
      421 tlepdypsll dskgnlvwny ngvpldgapg gwnalsylke lytiqntsln snlligykii
      481 dgltfrtslg ystynsqeyy gdpvaaqnpe yspvastrfg nnnfmtwile pqleykrtfk
      541 kasfnlligg tiqkntnyqt etdgsgyvnd vliqsisgsp vqyatdsyse ykyiaafgrf
      601 nfkwdgkyiv ditgnrdgss rfgpnkqfgn fgsvggawlf neenffknkf sfitygklrv
      661 sygitgsdqi anyqflsrwn pttynyggni gytpqnlynp dfswattrkl efglelgfvq
      721 drillnstwy rnrsgnqlvt ynlpaqtgfs svlenenavv qntgfeftlq stilktkalt
      781 wtsafnitfp knkllsfpgl aessysttyr igqpisivnv yryagvnpgt gyfqfynasg
      841 qitedpvqrg ggslndqnya vnldpkfygg wqnsfsykqf qlnifleyrk qtgvnylqsv
      901 ysylpgnefn qpvallnaws kpgqvtnfem lssqysqaan eanyflqssg iysdasylrl
      961 ktlsfsyslp qpvvkklnlq nirfyvsaqn lftitnykgn dpetqnfygv pplktivcgl
     1021 qltf
//
LOCUS       WP_096349950            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096349950
VERSION     WP_096349950.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120203
     Region          29..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiyqtikt vvtvllfcva pyalmaqtki sgtvtddthq plpgvnirva gtktgsitdv
       61 ngrysiavnk gqtlkfsfig yeelsvqvad qttidvtlkv sakglnevvv talgvkketr
      121 rigyatqsvn gddlttardp npingligkv aglqvgatse ilgvpnvtir gntvslfiid
      181 glpfnsdtyd ispddietyt vlkgpaaaal ygsraqfgai iittkkgdkn kkgitvdins
      241 stvlnkgfia fprvqhsfgp gentfyefvd gkggapggvd sdydiwgpyf ngqlipqyds
      301 pvvngvrqgt pwtalgannl anflqtgyqt nndvaitang dnynirfsas qehqqsyips
      361 qyldiananv yasfnassrl kfeasldfnr qstddfpdvq ygpnsiiynm aiwtgadwsv
      421 nspdikaiwq pgkvgvasef eeytryhnpy fltkiwtrgh hkndvygylg gtyklndnln
      481 valksqisty nllrtedmpy sahpygregn mgdyredrrd lfdnntlltl nynytvakfl
      541 nlsglvgsnl rsfkynsswv stnylnvpgv ysfsnsenal qatsfnsaql qlsefaslda
      601 sfgkyatlsg tirneyssaf qqpttylyps lslatvisdy ikmpdfitfl karasyanir
      661 sdatsptigp apyssitafg gstgpslfdn plgygstyns pyngptyaln tsystakpyn
      721 sqtagygpdn lyangiktst rvnyeegfdi kflqnrlgls gtafqyidgp qilanaista
      781 sgytieyina lktkttgyel svtgtpikdl ggfgwdvlan fstykqifdq lppgqstynt
      841 ffhqgdrtda vygsafvrtp tgqiifgsng ealvnpvaqn lghatpdfnw sfynkfhyks
      901 vslgfqfdga vggvisdymh nktmrggana ltaegalgaa ryqdwknfpl nnitpnpnyt
      961 gsyvapgvvi sngvapnyds htgkvlnysa lqygtnttpv fvqefaseyy gvteanlmsk
     1021 tyaklrevtl dydlpkrwlq ntfitkaslt iygrnllyfy knpefkdvdl dqyanssagg
     1081 tglqspsvrs yglniklsf
//
LOCUS       WP_096350198            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096350198
VERSION     WP_096350198.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115066
     Region          44..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlncysqkyl tgiimlmllv fnisfavaqq dttvkatvhp gwasgivlde ysqplkgvni
       61 rikgnavftt sdaagqfqid aapgttlvfs ytghlvrelt ikdnskitvk lddnylrnpq
      121 nidvlygtqk keselgaist vytnqltttp aslfvyafpg qlagvytqqq sgftsfhtas
      181 isspsvigqn lvntasnnns tsdnsemmvt vrgqtpitvi dgvqreissi dpesiesisv
      241 lkdglstilm gvnssrpivl vttkrgevgk pritftaetg lqkslglptp lpayqyayli
      301 netltsdskl pqysaadfna yrdhtdptgh pdvnwfktil tdyapmtqyk lnvnggsnia
      361 kysislgyfd qagifntase vpyntnndls ryiinsdvgv qvnknlnvdl qlfgrvqttt
      421 epggnngggy tsvlnslynt pnnaypvrnp dgsfggsiig gntgpysnnl lsqteysgyi
      481 qnltddilan ldlnynlnsv lkgltaklkg nlsyqsital nrslqnpsfi lnkdstysqy
      541 gaivaqsnvf ntvytsrqsf gqaalnyerq fgknqvnaia lydskslvtn ydlpevvtdi
      601 alkgtynydg kyfaeaavnr sgnnryppgh qfgtfyaagl gwqmgkesfi kdnfswidsw
      661 kwrgtyartg ngniaqqasl yyayqqtysn nnfnkqyqig tgyvtnyywy edalanpyit
      721 wesadkidfg mdislfkdkf litadyyhdk ysnvlglrgn siallgapyp leniginlyq
      781 gaelsltyqd htgnfnyfvt gninlqaski vyqdelnspy pwtrqtgnpv ngviygytaq
      841 glyqtaqdaa tsphiagyvp qagdikykdl ngdgvinqfd esaiggtkpi vfyglnpgfs
      901 ykgfslsvii qgvtnrqiyv gynniatqfg ldystinqqa ytgatgrwtp etasiatlpr
      961 lavsaynnng ltssfyvrsg nylriknaev gytfpvsvtq klrlaglrvf vngenlatla
     1021 glkgidpeet smtaypvqrv inagitvkl
//
LOCUS       WP_096350630            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096350630
VERSION     WP_096350630.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118713
     Region          8..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhaqnlpvrg ivldnnnqpl pgvsifikgt drgtltgveg rftlsvdkgq tlvfksigfi
       61 tqeivvnetn lsvqlfqdnk alnevvital gvkkefqklg ysqsqisgde lttardanpl
      121 nsmagkvagl tigasseffg aptvvlrgsk dilyvidgep vesntydfnq ddvdtytvlk
      181 gpnaaalygs rgingaiiit tkhgtkdkkg wqidinstle aekgflvlpk dqyeygrgtk
      241 fayaygnqly dnnqrlpewg prfdgvfqtt qfdspyntvt gvrtptpwaa rginnfnnfv
      301 qtgytstnsv slsasgsnyd mrlsyghtyq qgdfpntkln idnfkisagy ditpklrldg
      361 dlnlnlqysp nipdvsygpn syayeffvyg ssdydinalk niyqgpqgvp nlvqyaqeyg
      421 rennpwfqak kwlkgrdnqv vngslrltyk fnndlsvalr ssldtyneln tedvpsstnl
      481 nqylpwyyfg wygdyrqdqr nllenntdvt vnynkkirnf nisalagane rsfrylsnwa
      541 ttkdlslpnv ynldnstnpi lsynfnskmq vnsayysvdl gyknyinint tgrvdnistl
      601 pssnntyfyp svsvssvvnd yvklpefisf fkvrgsfadv kgaltnpyip sayaavtgns
      661 igsllgyste hftpyngpny vnsssvsptt yyngspsvnl sntianasik pydvksyefg
      721 adlkfignrl glnatyfttt ngpnifslpv assttfssqi vngvttkkkg velelvgspl
      781 rskdglnwdv ninysnyket lasiyggetg lyqnnhlyhi gdrldaiygt kfvrdgsgni
      841 insggapiqa pgqsnnaqlg llgyadpsfa fgitnhftyq nwslsfqfdg riggktydyt
      901 yyhamnggta vesasgayga arlaewnsta egtksatpay vgpgvtlvsg tptygpggvi
      961 tnlsqltfap nttavtvqgy issglggnfd eyymisrsya klreatigys lpskllqgtf
     1021 ikkasfsivg rnllyfaark didldqyasg ydassrtlvg gsggsdlasp tarryglnih
     1081 ltf
//
LOCUS       WP_096351528            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096351528
VERSION     WP_096351528.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110496
     Region          27..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqfknllkvs llalfcffmv pamaqnktit gkvtdskdgs pligasisak gstagaitdi
       61 ngafkltvpa stttlvvsyi gyvskdvlvt sdvvnvtlda nnnalnevlv vgygtvrkkd
      121 atgavvkvns adfvqgvttd plqqlqgkaa gvvvattngd pnggltvrir gtvsltggnd
      181 plyvidgveg adpralspnd vesfdilkda ssaaiygsra aggvimittk qgkagkaqvs
      241 fntyvasesy ehlmdfanas qylsmfqsfy ghpmatfnpa spsttsnqga ntnwykallr
      301 tglthnenls vaggtdkshy rasvtytdqq gialaserkd lnarfnfdqk tlddkllitm
      361 nlqathtnan ytdgnafsda afvpsvisey dplnpghyqy inntdetnpv phltditntg
      421 ainkmsgnlr ldytlakglv ispfangslg nasynlylpp snllsavndq lnytlnqttv
      481 pgelltdgdv dksstadysv tygiyanykt tfgksrlnll ggyegnqfnn tglrvaahnf
      541 nditnypnen igaanlvtnk dinsydngft lqsyfgraey nfndkyyitg nvrydysnkl
      601 glnnqsevfp svdaawvvsn edflkqttwl tslkirggwg kvgdqsaisp yasqflfgst
      661 gnlyydgatg twltsnfstq nqnndlkwet vttvdlgvdf slfqgrltgn vdyyskttnn
      721 llfdytvptg gqyfvgtila nvgtmtnkgf efslngaiak skdfswnlga nvsinrnkiv
      781 slsgalnntq fnvtqsqvgs tgglgisgav sqigylkvgy pigtlllpey agqdgsgkql
      841 fyynkngsrq ttsnigdlnm addgtgdrrf yttdpkftyg isnnftykhf dlviflrgqy
      901 gskgfnqndm nftslqklgt yavlasaakd hitsssepss yflestsflk vqnatlgytf
      961 klsenkyidk lhiyvagnnl ytftsykgid aelttaggqt gidqaiaypr trelsfgvnl
     1021 tlk
//
LOCUS       WP_096351775            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096351775
VERSION     WP_096351775.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116213
     Region          25..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtknllmilc illltgnqlf aqnltvtgkv tgkddglplp gvsvsvkgsp sigtqtdvng
       61 kysltvpaga tlsfsfigys tqflpvnggv lnvvlapasq qlgevvvtga lgitrtrnqq
      121 syaaqqvsgd evskqrsdnf idglsgkvsg leikqnnalg gstnvvlrgv ksitgdnqal
      181 fvidgvpvgn entngsnqqq ggggydygsp asdlnpddie sitvlkgaga salygsrgsn
      241 gvilittkka kkglgivins tvsvgeidks tfpqyqkqyg agyaqyfnsg nifgnanaqv
      301 aptaddasng tafnpnlkiy qwdafdptsp nygkatpwva akndpstffv kpvstnqsim
      361 itsggetgtf klgytksien gvipnskldk nqvdfggtyn itpkltvgae infyntngtg
      421 rggtgydgsn sdnrnvmtnf rqwwetnvdv qelkaayert qsnvtwnmad pidgntnpay
      481 wnnpywvtdh nyetdtrnry lgninltykp tswlnitgrt sldsyseldq erydvgsigv
      541 pyysrynhsy setnydllan vdknisndfn lkallggnir rdyensifas tnggliipgl
      601 yslsntvnap lspteydatk evdgifagat ltwkkmltld gtirrdksst lpaannsyyy
      661 psvsagfvfs ellknytwls ygkiranyaq vgsdaplytv ndtysivppf ganpqtlvnt
      721 tknnpdlkpe qtkskeigie maflksrlgf dasyystntf neilpvnvsg atgynfkyln
      781 agsvenkgve lslngtpvlt nsfswkinvn ftaaknrvts lytdatgkea snlelasfqn
      841 geslnaplgq pfgtirgtdy vynskgqkiv gadgqylits tsnnnigntn pdwtgginns
      901 ftyknfslsf lidirhggsv fsndlaygla dgiypltayt ndlgkpvrnt ladgggfirp
      961 gvyangqpnt trvtaynygd fgdgagllpl safvydasyv klrealigyt mpqnvisklg
     1021 pikevtfqli grnlwiihkn lpyadpeegl sagnlqgiqe gayptvrtis fnlklrf
//
LOCUS       WP_096353424            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096353424
VERSION     WP_096353424.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110782
     Region          29..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknyfkkyv llfvlitmsf mafaqtggit gkvvdeknqp lpgssvtidg ttvgastdvn
       61 ggftithlka gtytvtakfl gyiaskktvt vegsvvtvnf alqpdntsln evvvigygtv
      121 kskditgsva tvtakdfdgg aittpeqliq gkvagvsits nsgapgagst itirggasin
      181 ggndplivid gvplapdgia gaanpldmin pndiesfsil kdasaaaiyg nrasngviii
      241 ttkkgqsgkp vinfstqvsd atlpkeapvl taqqfrdyin shdtttagiy rnlmgtastd
      301 wqkqiyqksi stddnlsisg ttgklpyrvs vgytdnqgil kttslnryta svnlsptlft
      361 dhlkvnfnfk gaqvkqrfan eggvisdavd fnptvpvygs gsqyapyggy wqwtdanntp
      421 sglkslapln plgvleqndn estvyraias laldyklhff pdlhanvnls ydgsrgsgfd
      481 nipanaatni dsykdasgny hsgseskyks vlenklfegf lsynknvksi kstfnliagy
      541 siqdfkstsy snfyagntnt kfadgtidpr saatypfyin enimtsfygr liynydekyy
      601 ltasvrddns tkfapssrtg ifpsvalawr isnedflkgs nvlsnlklrl eygitgnqeg
      661 vgdydylaqy slsnstaqyp fggtyyqmyr pgayfpgrtw ettastnigl dygflrdrit
      721 gtidyyynkt knllevisqs agtnfsnvit gnvgnmendg lelgitgkii aqkdiswsan
      781 fnvsfnhnki tnltaipnpn ypgqavggvs ggtgnnveid qpgyarntff vyqqvygsng
      841 kpldgvfvdr nhdgvinnqd lyhdhspdpk qiyglssdfn yrkwnlgfva ranvgnyiyn
      901 nvasatgiqr nimnplgiln ngsndvlnsg ltgngsndll sdyyiqnasf lrmdnmhlgy
      961 nfgsfaswvs afkvsfnvqn vfiitdykgv dpelgyvgag gggidnnfyp rprtysigln
     1021 lsvr
//
LOCUS       WP_096353280            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096353280
VERSION     WP_096353280.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112816
     Region          37..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqktlyyksf ifilknvclt avfvlllign amaqagqvik gtvtdaetke qlagvtvsvk
       61 ggtnkvatdv ngayaitvpp gsvlvfytig ydrieftvtn qtsidvklkq sttqlkdvmv
      121 talgitkekr aigysvsevk gasitevren sfvnslegrv agvnvsgvat gpngasnvii
      181 rgitnmtgnn qplyvlngip lvnnnyattd vgggyggkdg gdgigdinpd dietisilkg
      241 aaatalygyr gsngvvlitt kkgksgeglg veinsnyvse nvidetnfqt qygqgyngak
      301 pvnaadalgs messwgapld gtktfqfdgv krpyseaakg nlgrfyhags nftntvafsk
      361 gfgddgatrf svsdlydqsy vpnaglkrlt fnqttnlkla ksltldlssq yvseytqnap
      421 nvsdavgnln wgpmfvppni nittlagpfg ngtmangnel npfadpyttn pyfaayqlqg
      481 aihrnrftgs anakytfdng ifiglavadd ytsdrntnie pigtgylvde gvngdmyeqn
      541 vkqtelnidl ttgkkikfsk nfstnllfgv nyrksvqeyf tasgqnfaip llynignlen
      601 ltdnyslnne efesvyasad lsykdflylt vtgrndwyst lapgkinyly pslsgsfvfs
      661 ellhipaldl gkirlsyadv ggaadnpyqt lqtyaiagtl titngifpig tagngqvpns
      721 alkpssrrei eaglemdffk nrlkfdlavy qkkviddivp vtidytsgyn sallnvgtlr
      781 ynglelaigg tpvksrditw didfnasytk gkvislggqp qitlgyeaqd wgsaaytqqi
      841 vgkepmqiia ldpardsqgk iiidpalgap dpslaqpkdy gsaenpwtgg innsfhfgpv
      901 nlsflidgkf ggklfsntnl iayqqglskl tlpgrdllyg tnqqyasgyy gdwqaadqgm
      961 fvydasfikf rqltlgydfp vkklfnnkih glklsfvchn vftitkhtpn idpestysas
     1021 iytqgleapa vpysrtigln lnikl
//
LOCUS       WP_096353917            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096353917
VERSION     WP_096353917.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109883
     Region          25..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfnlkklllf lllvvsccnl faqgrvlkgk vtekdgsalp gvvieikgnt ksavasgpdg
       61 ffsinisgaa tlvahsigyt aqtinvtasq nnltivmqvd nqqlgeivit gyakqkkgnl
      121 tsaisvvsad klkdvtsddi gamlqgkvag lqvvnssgap gsaseirlrg vssvnasqsp
      181 lfvvdgiigg nydpndvesv tvlkdagata iygsqanggv iivttkkakg dktqyefsat
      241 tgfktpdfgt mvmmnssely qnqkqlfrdy ipgaannsyv idlvqfqsqr pasilntntn
      301 wlttlfksap iqnyhfstsg ktakneyyfg atfyneggtf mntdfkrvnl rtndvyhftd
      361 kitmtnsinv sgtlgksydy ndiyyaylnl pwdnpydanh naiyvdgnst fkwwsrdktn
      421 pintiqnsnh pyknfdvnyd lgldlpitpw lsfntsnrls ayygysstyy spavegfyhg
      481 tgylnnqssf syggistnll kfnfqfgksa lngiagvefe gsendymgas gkglplglav
      541 ldvvsntqtv ngyyntpsiv sylsqvnysy lgryflsgsf rtdgssafpp snryasfpsi
      601 sagwlasned flkdshtidn lklrvsygit gtqdigagry lglyslntqy nssvgatpyq
      661 lespnltwes khqldagfdi glfhrinitv dayhnitknl llqvaqplsv gfetkwenkg
      721 qvlnnglefa insvniksan fqwttdfnis fnnnklqgfp stvvstgass vsqiyrndgn
      781 lyefympkwe gvnpqtgapq wevetkdskg nvtsksvtsn yalatleeqg salpkyqggf
      841 nnefkykkff lrvntyfvyg nkiynanlse vqndgsepyl nqivapkgti vwthpgqiat
      901 dpspqnntns tspstrylkd gsylsirnia lgyslpksfv qrlklsdvnv svsadnvytf
      961 thylgqdpat titpgnfitp gvadfkypdn rqfllninik f
//
LOCUS       WP_096353989            1022 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096353989
VERSION     WP_096353989.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1022)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1022)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1022)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1022
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1022
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112329
     Region          26..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktilyivl aalclnfrak aqavtkltgr vidsaqntpl hgatikikst gtttstnekg
       61 dftlytkess gkltisylgy ktteisfnpt dkdpfairla edknllkevs vvstgyqnip
      121 keratgsfvl adsallnrsv stnildrlns vtsgvlfnns snlqfgqsai eirgratlfs
      181 npspliiidn fpydgdpgni npndiesiti lkdaaaasaw gsrsgngviv ittkkghlns
      241 apqvsfnant tvgarpdlyy lpqltsaqyi gveqylfnqg aydnaistgy qalspaveif
      301 saarngtisk sdslseintl ksydsraqll kyfyrpsvnq qyqasvsggs atqkyffsag
      361 ydknlnntvn ssydritlna antwyflknk lelftnivyt gsttksgpal astdypydqi
      421 adangnplai antlsipygs tagngallnw lykplqelen gysgttsslt dyrinvslsy
      481 qiikglkasg lynyekgind vnnlnelqsy ytrnlintft nidpvsgavt ypvpmgailn
      541 tsltnissnn grfqlnydhh wgknavsaia gtevkdyttf nnaytlygyn petatdqnqa
      601 vdftaynpyf ygyntaqipa ntsetgttnr ffsvyfngsy tyddkyilsl sarkdesnlf
      661 gvsanqkgvp lgsaglawii dkesfyaidw lpqlklraty gytgnvntsi saylaavggn
      721 iaqtynayas tivnppnpsl rwevdrntdl gmdfgtkdnr isgsidywlk agldligssp
      781 iapqtgisly tgnsantitk gidlqinsin lkgkfkwttt flynycqnkv tqykvsngtn
      841 lnvvsanynn plqgypyyai fsfkyaglnk sgdpqgylng kistdytsim natnrtelvy
      901 ngsatptsfg slrntfnykt fdlsfnityk lgyyfrrasl nngtlysagp nsyqmadfds
      961 rwqkpgdelh tnvpalvypd niyrddlyty snilvvnaah irlqdlrlgy tipkrpichs
     1021 et
//
LOCUS       WP_096355825             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Variibacter gotjawalensis].
ACCESSION   WP_096355825
VERSION     WP_096355825.1
KEYWORDS    RefSeq.
SOURCE      Variibacter gotjawalensis
  ORGANISM  Variibacter gotjawalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Variibacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Variibacter gotjawalensis"
                     /db_xref="taxon:1333996"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39480
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiplesd ggeprvaatp etikklkalg aaeiavepga gvksgirdsd yeaagatisa
       61 datrdadvvl kvrrpsaeel trykrgaavf aimdpygnep alqamadagv safamelmpr
      121 itraqvmdvl ssqanlagyr avidataeyg ralpmmmtaa gtvpaarifi mgvgvaglqa
      181 iatarrlgav vtatdvrpat keqveslgak flavedeefk naqtaggyak emskeyqakq
      241 aalvaehikk qdivittali pgrpapklvs aamvdsmrpg svlidlaver ggnvegakag
      301 eiveingvki vghnnvagrl aatasslyar nlyafleilv nkeskalain wddeivkata
      361 ltrdgavvhp nfqpksaa
//
LOCUS       WP_096356159            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gotjawali].
ACCESSION   WP_096356159
VERSION     WP_096356159.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gotjawali
  ORGANISM  Mucilaginibacter gotjawali
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Mucilaginibacter gotjawali"
                     /db_xref="taxon:1550579"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114598
     Region          24..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllvslc flmlcitqvf aqnrtvtgtv tasddgqpip gvtvklkgts igtqtsvagk
       61 ytlsvpagat lvftfvgytp lelpvgtaav lnaklvpasr qltevvvtsf giqrqaaslg
      121 ysttkvtgad intakpisva ngltgkvsgl qvntvnagif aptritlrgn rsllgnnqpl
      181 ivvdgsiyys distlnpedi qstdvlkgss asavygsdas ngvivittkh garatsvtls
      241 stadietvsy lpkfqnqfgs nggelyvndf ndlrtyipye nqsygplfng kmvplgrplp
      301 dgsvemvpya avknqkrdff ntgltthqnf sydsgdengs fhmsaqdins tsvtphdigr
      361 rdifriggdk kygifsatys atytyvnknv tnsggvyddl lesplhvpva dlknvdskyg
      421 npdtyyndyy yspgqiiaqt ryldienhin anvaltlkpw kwvsltyrss leniqarsev
      481 kdagitysdf sksndtiyys nsqgtgivka edsgtkysan dappsygldd fnnllftsdf
      541 lasfntkfak dfsfngtagi ayienkitnt pinqgalvtl pyntqnfsgt psvggqysye
      601 arkigyfaeg tfgykdfayv hgsfrtdlds rlskanhyip yydidgslvl semfkgmtdn
      661 gvlnfakvry ahsltgnvsp langsqyiaf gayrtdptlg aaygfpyass giagyslntt
      721 ianpnikpek vtedevgldl gflndrinla asyyqsktkd givfanvsga sgfttallna
      781 antsnkglel dlsgtviktg ninwkigvnw thqssnvesi vsgvnalpig naawavvghs
      841 ypelegydwt rdpangkviv dpntglptra sklsilgqsv psdligfstt fkyksfsfqm
      901 tadyrggyvi ynsnlgttld hsgtsitsai agrqrfvfpn seylvngayv pntnvevqdg
      961 nfnfwptlyq sidanyvtsa aawklreval syslpkqlis dikfvkavti tvsgrnllmf
     1021 vpstnkftdp efsndtgngv gttslnqlpp trifsttlsv tl
//
LOCUS       WP_096363647             377 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Thiohalobacter].
ACCESSION   WP_096363647
VERSION     WP_096363647.1
KEYWORDS    RefSeq.
SOURCE      Thiohalobacter
  ORGANISM  Thiohalobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiohalobacterales; Thiohalobacteraceae.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Thiohalobacter"
                     /db_xref="taxon:1273155"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40531
     Region          3..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpirvavpke tlegecrval dpvvakrfaa lgcevrmehd agagahyvdd dyedvgfvtd
       61 kaellasadv vlkvqppted eikqmaegsi vvgfmspyrf pdrvklmrdr kitsfameli
      121 prisraqsmd alssqaavag ykaaimaadr tgrffpmltt aagtirpakv lvigagvagl
      181 qaiatakrlg avveaydvrs atreqvqslg akyietgvaa egeggyarel teeekrkqle
      241 vlakhitqad avittaaipg kpspkiisqe mvdnmkvgsv iidlaaeggg ncevtkpged
      301 yvygcvrvyg pfnvpamlpv hasdmyaknl lnfltpmiee gelkldwedq vihdsalthd
      361 geirheptra lvegdas
//
LOCUS       WP_096372024             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium ulcerans].
ACCESSION   WP_096372024
VERSION     WP_096372024.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium ulcerans
  ORGANISM  Mycobacterium ulcerans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Mycobacterium ulcerans"
                     /db_xref="taxon:1809"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37091
     Region          7..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdpqttvgv vaestpderr valvpkavgs lvnsgvavvv esgagerall pddlyteaga
       61 tigdawaadv vvkvappsad evgklrsgqt ligflaprna dnsigalkqa gvqafaleai
      121 prisraqvmd alssqanvag ykavllaase strffpiltt aagtvkpatv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwlnigida ageggyarel tdeeraqqqk
      241 aleaaisgfd vvittalvpg rpaprlvtaa aveamkpgsv vvdlagetgg nceltepgrv
      301 vvkhdvtias plnlpatmpe haselyskni talldllltd gklapdfdde viadscvtrg
      361 dd
//
LOCUS       WP_096375915             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas chlororaphis].
ACCESSION   WP_096375915
VERSION     WP_096375915.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38702
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapcdsel aliksgtvlv gmlnpfsnet iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvvdlaa vqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_096407243             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Halorhodospira halochloris].
ACCESSION   WP_096407243
VERSION     WP_096407243.1
KEYWORDS    RefSeq.
SOURCE      Halorhodospira halochloris
  ORGANISM  Halorhodospira halochloris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Halorhodospira.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Halorhodospira halochloris"
                     /db_xref="taxon:1052"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39957
     Region          3..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maikvavqke trpgekrval vpgtlkqfgk lgvelmlekg agsnagfdda dyesagvriv
       61 dnksdllaea dvllgvqplt akeagqlnkg svlvafmsph egderisnlc knkvtsfame
      121 lvpritraqs idalssqaaa agykaaliaa ersprffpml ttaagtirpa kavvvgagva
      181 glqaiatcrr lgaqvegydv rpetkeqves lgakfidtgv eavgeggyar eltaeeqkqq
      241 aevlanhian ahvvittaav pgrkapqiid katvermqrg svivdmaaet ggncavtqag
      301 kdvthkgviv agpknlpasl avhtsemysk nlynllslmi adgqlqldwe dqviadtclt
      361 hdgkvrhept rerleggks
//
LOCUS       WP_096422920             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microcella
            alkaliphila].
ACCESSION   WP_096422920
VERSION     WP_096422920.1
KEYWORDS    RefSeq.
SOURCE      Microcella alkaliphila
  ORGANISM  Microcella alkaliphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microcella.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Microcella alkaliphila"
                     /db_xref="taxon:279828"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38867
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqiairrepi egerrvaatp atvatyvreg yqvvverdag aasgypdqay aaagatlada
       61 vdlgaadvla hvrpldpati aaltpgavav gfaapagele avaaladrgv tafalelvpr
      121 israqsmdal tsqaliagyr cvleaatrfp rflplymtaa gtippakvlv lgagvaglqa
      181 iatakrlgak vsaydvrsas adevrsmggt fihldldena daaggyakel aadraarqre
      241 llsphvqaad iiittaatpg rpaprlitad mltgmtpgsv ivdlaaesgg nvegsiagvd
      301 taiavdggai tlvgmkdaas tmafdasrll aqniaqligl mtvdgaltpd fddevvagac
      361 lthdgvvrhe ptaqavaern gar
//
LOCUS       WP_096428366            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            antarcticum].
ACCESSION   WP_096428366
VERSION     WP_096428366.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum antarcticum
  ORGANISM  Labilibaculum antarcticum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Labilibaculum antarcticum"
                     /db_xref="taxon:1717717"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114764
     Region          24..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslvsmli lciiglqsvl aqsrevsgvv tsaddglsip gvsvivkgtt igtttdfdgn
       61 fslnvpedgk ilvfsfvgmk mqeheitsst invvmesesi gmdevivtam gvtrekkalg
      121 yaatsiggde igksqvvnpm nalqgkvagv distapgpga tqnvmirgas sfgnsqplyi
      181 vdgvpitnvq nqsgnalnsq vdfgsginai npddiadmtv lkgaaataly gsraangvim
      241 ittksgkntd gkmrvsysgs ttfsrvgrlp dvqkqfgqgw sgeraldeng nwgpaydgkd
      301 rvwgnivdns qqvkpyvfle drvrdfyevg knlknsvsls ggnetttfll slsqnsvdgv
      361 mptdsdsydr ytiatkgshk agkltisanv nfstektkav asgqgtsvfr slyespndvs
      421 ivdqkdynnk fnnldnyltp ygvnpyyvln enaaeqnkkk lfgkfqldyd ftddlrlsyr
      481 fggdyevalg ethtaiigft pgspndgssv anpgnftesr teriqinhdv mmtykknlne
      541 dftlnaiagm nvnersmtyl dgsinsidip dfynlansfs psvsthessk rrligvyanv
      601 dfsyrnyayl tltarndwss tlpleqndyf ypgitgsfli tdflkyndid tgilnfakvr
      661 aaygmtgnda eayavydryv safsnnpgyp niddltfpig gvnsysasnr lgnpdlknel
      721 tkefelgfea qffnsrlgfd vsyynrlteg lianlpkdps sgyttqvanl gdvrneglei
      781 avnftpvrta nfswdvaynv slnentiesl dveevyldgf ggasivaveg ksmgqfkias
      841 vkkvdidgvm htvvdgsgnp qpttetefig kdvdadfrmg ltntftykgf slgttldlsy
      901 ggymysytkd ylhwtgsspe svlndrktfl vpnsvvsdgq ggwventtav dptglhkfyg
      961 dgggfdgded aiidrsylkl rnvnlsyalp ksfcsklhvs slslslsasn illwtpnena
     1021 yidpetttfg ndigakfgey gagpsnefyt fglnftl
//
LOCUS       WP_096427889            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            antarcticum].
ACCESSION   WP_096427889
VERSION     WP_096427889.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum antarcticum
  ORGANISM  Labilibaculum antarcticum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Labilibaculum antarcticum"
                     /db_xref="taxon:1717717"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115849
     Region          24..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkmiglfvl lifmglqvvt aqskqitgti tsaedglgmp gvsvvlkgtt igastdidgr
       61 ysleakstdi llisfvgmit qeikvgdktv invvmetesi gmdevvvtal gvtrekkslg
      121 yavtevsges isegkesniv nslsgkvagv sirqantmgg sanilirgsa slmgnnqalf
      181 vvdgvpmdns ntntadqssg rggydygnaa sdinpddves vsilkgaaas alygsraang
      241 vvlittkkgk krngfgvtvn sgitfntink etmpeyqyey gagyspdwsf sgsdglngni
      301 vvntnddasw gpafdpnlqv vhwdaldpna dnygetrpwv apkstvydff etgvkytnsv
      361 altggndfgs frlsftnsde sgilpnssik knsmsiksdy klteklkasa sanyvntkgk
      421 grfgtgyddn npmqnfaqwf qtnldfdrlk knyergdggm ltwnasnptd lapayannpy
      481 wtryknyedd ernrlfgyia ldyelndmfs ltyrtsidfy qerqneriav gsntqskfss
      541 fdrtysewns dlmlkfkkrv ndfslnglvg vnyldrniqt isgetsgglv vpglytvans
      601 vvaksptetl lekntksgyg sfsvgyknfa yfegsfrvdq tstlptnent yfypavsgsl
      661 ilselgaikd lsflsfaklr anyaevgndt npynirsays qyvnwgnkas fsvngtlknp
      721 elksertesv elgleanffn nrfgfdlaly ksnsfdqimd vnvstasgys rafvnsgeie
      781 nkgielgini spvkssdfnw dmninwaknk nevislyngv dniqilsawd itmnatvgea
      841 ygvlkgtdfv ytngkktvda ngyytktaed dkvigniqad wtggitntfs ykgitlralv
      901 diqkggdiys vdrkyglatg lfketgglns kgnpkrdavs dgggilhaea vnidgtpntt
      961 faranswggd qyygrtptar yiydasyvkl revalsytip ksilsqtfft kavvsavgrn
     1021 lwiihkntpg fdpetgqssg neqgiangsy pttrtygfnv tlgf
//
LOCUS       WP_096431944             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudothioclava arenosa].
ACCESSION   WP_096431944
VERSION     WP_096431944.1
KEYWORDS    RefSeq.
SOURCE      Pseudothioclava arenosa
  ORGANISM  Pseudothioclava arenosa
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudothioclava.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudothioclava arenosa"
                     /db_xref="taxon:1795308"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55877
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egearvamtp dsalqlqklg hecyiesgag hlaglddsay ekagvtvikt
       61 aaalfkevdf vvkvrpptdt elkrlkegqt lisffypaqn telleqakat gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigastslg aityafdvrp evaeqiesmg aefvyldfae eqtdgaatgg yaapsspefr
      241 eaqlkkfrel apevdivitt alipgrdapi lwtkdmveam kpgsvivdla aerggncelt
      301 kmdekvvtan rvtiigytdf psrmaaqssq lystnirhmm hdltpgkdgv vnhnmeddvi
      361 rgatvahhge itfpppppki kaiaaqkpke kakeltpeei kardraafqk qtrnqvallg
      421 iggalllgvg lvapasfmah fivfvlscfv gfqviwnvsh slhtplmavt naissiiilg
      481 allqigsgsw lvialaglsv fmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_096433252            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            antarcticum].
ACCESSION   WP_096433252
VERSION     WP_096433252.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum antarcticum
  ORGANISM  Labilibaculum antarcticum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Labilibaculum antarcticum"
                     /db_xref="taxon:1717717"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113833
     Region          60..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkcylrnlh sglsnplgtg skigifallc ammvlpfsan anvnsltedy ssvsatqqlv
       61 tgavtedsgi slpgvsvvve gttigtvtdi dgkfeitvpd assvlvfsfv gmqtqeitvg
      121 sqsvinivma tdalqvgevi vtalgikrek kalgysvqdv kaeeltqggn sdlvsslagk
      181 vagvqinqsg ggvggasrie irgasslsgn naplwvvdgv pfddgnsrda svwggtsrag
      241 gafdlnpedi esvsilkgpn aaalygergg ngvvlvttkr gtrgkglgis ysggftmsea
      301 aymldlqdqy gqgtngeysn sstsswgsem qgqmleswtg emlpyeaqkd rlkdftrtgt
      361 sqkhniaftg gneegayrvs lgkdimngiy edhkvekltf dlradydvns wlnvdtkvsy
      421 fqtegnerpe igtysyvsyf ntmpmnirnq dltpgydiis gqhveklytt ananyrnpyf
      481 lqaqttnyde knrtfgyvaa nikinsdlka kfkygmdfyd fssvegylfa dnvdasrpny
      541 nptqsnfkee nyefllsynk einedftigv nlgandmrrv skglsansgr lssegdffla
      601 agsnikases asesevrsvy gfgqvayknm vfldltarnd wssaltaada kydnsyfyps
      661 lslsgivsem tdlpdwvsfa kvrgswakvg katepyntsq sftlesgnyn ltrgnvsdqs
      721 vvdglkpeis tsweigadlr llnnrigidf tyyneetknq ilpvpgvqss gyntilinag
      781 litnkgielm lttvpvktkd ltvgldfnfa mnesvmesla egvpeysfgm nvmaipgekl
      841 gvirgsvydr dangsliide nglmvvaqgd dhvlgniqpd wtgsinlsvd ykglfltalv
      901 siqeggdils ssersavsag taarttendr maffvdgvta aggannvivs aeeywrqlak
      961 vdeefmydas hmklrevaig ynipksllsk iphnpvksar fslvgrnlly fykntpgtap
     1021 dasaystefa aqaydfspvp sartygfsln vgf
//
LOCUS       WP_096436504             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium shigaense].
ACCESSION   WP_096436504
VERSION     WP_096436504.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium shigaense
  ORGANISM  Mycobacterium shigaense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            simiae complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Mycobacterium shigaense"
                     /db_xref="taxon:722731"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37553
     Region          9..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtepqanair vgvvaesgtd errvalvpka vaslvnsgva vvvesgager allpdelytq
       61 agatigdaws advvvkvapp tadevgklhs gqtligflap rnaenvigal tqagvqafal
      121 eaiprisraq amdalssqgn vsgykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwldig idaageggya relteseraq
      241 qqqalekais gfdvvittal vpgrpaprlv taaavqamkp gsvvvdlage tggnceltep
      301 grtvvkhdvt iaspfnlpat mpehaselys knitalldll iadgklapdf ddevvaescv
      361 trgkds
//
LOCUS       WP_096452915             428 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. 113-1-2].
ACCESSION   WP_096452915
VERSION     WP_096452915.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. 113-1-2
  ORGANISM  Mesorhizobium sp. 113-1-2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Mesorhizobium sp. 113-1-2"
                     /db_xref="taxon:2744515"
     Protein         1..428
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43993
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivetg agtrsripde efakagavig
       61 kadavakadv vlkvrrptea elkgykagaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedde fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 pgkvvttann vkivghlnvp grvaasasll yaknlfafle tlvdkttktf ainrdddlvk
      361 atmltdggkv vhpafakadq qphvepaaip attmvasaep aaakkaatkk taasqspssk
      421 spkskgta
//
LOCUS       WP_096457140             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfurifustis variabilis].
ACCESSION   WP_096457140
VERSION     WP_096457140.1
KEYWORDS    RefSeq.
SOURCE      Sulfurifustis variabilis
  ORGANISM  Sulfurifustis variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Acidiferrobacterales; Acidiferrobacteraceae; Sulfurifustis.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Sulfurifustis variabilis"
                     /db_xref="taxon:1675686"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41086
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipreta vgetrvagtp etvkklralg ldvvvereag lashftdaay rdagaelvsa
       61 setlaadivf kvhkptfeqi rgmrrgatli clldmcyddg tfdtlaaqgv dsfalemmpr
      121 israqtmdvl ssqaniagyr avleaarlyg rffplmmtsa gsakparvvv lgagvaglqa
      181 iatarrlgaq vwaydvrpev keqvqslgar fieldvgesg aghggyakpl seeaqrkeqa
      241 llteelkkad iivstalipc rpapvlited airgmhegav vvdmaaasgg ncpltepdri
      301 vtrhgvilcg itnfpalmps dasnffarnv ynflefmlep gaegvrfkdf laddvtsmtl
      361 itfqgtvrfe ttkmakkrpa gasa
//
LOCUS       WP_096472478             379 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia cepacia complex].
ACCESSION   WP_096472478
VERSION     WP_096472478.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39189
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiakgag iaasypdeay aaagaeltdq
       61 saafdadvvl kvqapidtel pllkrgsvlv gmlepfngeq aaklaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetaqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qvivhngvti agytnlasmv asdasalyar nlldfmkliv akdgtlnidl
      361 tddivaatll crdgevtrk
//
LOCUS       WP_096478285             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            phaseoli].
ACCESSION   WP_096478285
VERSION     WP_096478285.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium phaseoli
  ORGANISM  Rhizobium phaseoli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium phaseoli"
                     /db_xref="taxon:396"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55453
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkely vdekrvaltp esalqlqklg hqclveagag lasglsdeay raagvevvat
       61 aqdlwqaadi ivkvrppqqe eltplpsgkt ilsfvhpaqn adllesarvr kvnliamdmv
      121 prisraqkmd alssmaniag yravieagns fgrfftgqvt aagkvapakv lvigagvagl
      181 aaigtstalg aityafdvrp evaeqiesmg aefvfldfad qqqdgaasgg yatpsspefr
      241 gaqlskfrel apqidivist alipgrdapr lwladmvaam kpgsvivdla aerggncelt
      301 iadqkvvtpn gvtiigytdf psrmaeqast lysnnirhli adltpskngc lvhdmeddvi
      361 rgatvthegk ityppppprv qaiaaqkpre karepspeek rsqelaafrr qtrdqgllla
      421 ggtallllvg amapasfmeh fvvfvlacfi gfqviwnvsh slhtplmavt navsgivivg
      481 almqigsgns iviglaavav lvatvnivgg flvtrrmlsm frks
//
LOCUS       WP_096478283             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            phaseoli].
ACCESSION   WP_096478283
VERSION     WP_096478283.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium phaseoli
  ORGANISM  Rhizobium phaseoli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium phaseoli"
                     /db_xref="taxon:396"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55144
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgspreta pgelrvaltp eaalqlqklg yecvieagag kaagfsdeay rdvdvtvvds
       61 aallyetsdv iakvrppeat evdrlaagkt lisffypaqn kdlleqarss gatviamdmv
      121 prisraqkmd alssmaniag yravieasnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfge eqqdgaatgg yaapsspefr
      241 ekqlakfrel apqidivitt alipgreapk lwladmvaam kpgsvvidla aerggncdlt
      301 vpdqrtvsdn gvivigytdf psrmaaqast lyatnirhmi sdltpakdgv ivhnmeddvi
      361 rgatiakdge stypppppki qaiaaqkrke kmkeptaaek raaeaaafka qaksqgillv
      421 vgtallllvg ayapasfmsh fvvfvlacfv gfqviwnvsh slhtplmavt navsgivilg
      481 allqigsgng lvvtlaalsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_096480487             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas frederiksbergensis].
ACCESSION   WP_096480487
VERSION     WP_096480487.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas frederiksbergensis
  ORGANISM  Pseudomonas frederiksbergensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas frederiksbergensis"
                     /db_xref="taxon:104087"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38778
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvidsay eaagatigsa
       61 sdafgaelil kvvapsdsel tliksgtvlv gmlnpfnnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv ticgptnlvg evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_096485745             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylorubrum populi].
ACCESSION   WP_096485745
VERSION     WP_096485745.1
KEYWORDS    RefSeq.
SOURCE      Methylorubrum populi
  ORGANISM  Methylorubrum populi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylorubrum.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Methylorubrum populi"
                     /db_xref="taxon:223967"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39446
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavltetd pieprvaavp etvkkfiglg sdvvvqsgag akagvpdsey eaagakiags
       61 aeealsgadl ilkvrrpnad elakiqkgat vvaimdpygh edalkaaaea gvntfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrslpmmmt aagtvpaari fimgvgvagl
      181 qaiatarrmg avvtatdvrp atkeqveslg akfvavedde fkqaetsggy akemsaeyqk
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 ageivtvgng vkivghvnvp grlaatassl yarnlyafve tmidkeakal avkwddelvk
      361 atnltrdgqv vhpnfqpka
//
LOCUS       WP_096504793             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacteroides stephanolepidis].
ACCESSION   WP_096504793
VERSION     WP_096504793.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides stephanolepidis
  ORGANISM  Mycobacteroides stephanolepidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Mycobacteroides stephanolepidis"
                     /db_xref="taxon:1520670"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37218
     Region          6..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdqpvtigv vresgederr valvpkaiag ligkgvnvvi esgagerall pdelyteaga
       61 tvgdawsadv vvkvappspa evaslregqt ligflaprna dnsigalksa gvqafaveai
      121 prisraqvmd alssqanvag yksvlvaase strffpmltt aagtvkpalv lvlgvgvagl
      181 qalatakrlg grttgydvrp evadqvrsvg aqwldlgida ageggyarel teeerqkqqq
      241 aleeaikgfd vvittalvpg rpaprlvtaa avegmkpgsv vvdlagetgg nceltepgqt
      301 vvkhgvtias plnlpatmpe haselyakni tsvlellikd galapdfdde ivagscvtre
      361 vs
//
LOCUS       WP_096505943             532 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. IDO3].
ACCESSION   WP_096505943
VERSION     WP_096505943.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. IDO3
  ORGANISM  Burkholderia sp. IDO3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia sp. IDO3"
                     /db_xref="taxon:1705310"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55009
     Region          3..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple iatgerrvat vpevveklik lgfsvavqsg ageganfddd ayraagaria
       61 ataaelwags divlkvrpps teevasmreg gtligfvwpa qnpelmaqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq ardadiivtt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl ygtnllrvve elckgkdgti nvdfdddair
      361 gltvikegnv twppppikqa vvapkpaata paaapakskg hghsgepmsa kalaivfaig
      421 avafllvgqf apasflshft vfvlacfvgy mviwnvtpsl htplmsvtna issiiaigal
      481 vqvappldel anagdrpsgl ilglavgalt ltavnmfggf avtrrmlamf rk
//
LOCUS       WP_096511162            1158 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Filimonas
            lacunae].
ACCESSION   WP_096511162
VERSION     WP_096511162.1
KEYWORDS    RefSeq.
SOURCE      Filimonas lacunae
  ORGANISM  Filimonas lacunae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Filimonas.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Filimonas lacunae"
                     /db_xref="taxon:477680"
     Protein         1..1158
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125907
     Region          129..1157
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdirfnrylf laafllpqlk aitadarapk hfappsqkmv alaealhqiq gtfhvnfnys
       61 satiankfvp aekipvkggf tedklsallq plglvaekld atdyaikpav ttqkqsytfn
      121 vaasrashvv kgvvtndkee llagvavtar pggktvltna tgafsieveg ddvvlvfssa
      181 gyltqelkag nnatlnvqlq adiknldnvv vtalgikrqe kalgysiati dgskvntvke
      241 vnvvnalsgk vagvdiravs sdpgssvlit irgsssissg sqplfvvdgv pissgnrtpa
      301 tpvgqvtvdy gspisdinpd diasisvlkg asaaalygsr agngvvlitt ksgsgkskkg
      361 lnvqanfnam ydkawqfpef qnefgagdvt sstdptntls taswgprldq gtkyvqwnsp
      421 tdvngnlvpt dwvsypnrvk dffetgstyt tnvavsgnnf rlsytnlqnk gispntdlqr
      481 ntvnlaagye lspkikvttn vayannhskn rptfnrgsas yiiytmpgni npallknywq
      541 kdkeglaqfs qdqgstdnpy fvayeltngy nrnrltgniq lnidllknls lmvrsgvdfy
      601 setdeskraf savqnpnggy sigslfqmer ntdflltykk nlkkdwsffv saggnrmdan
      661 nnsqsqaagt lvmpgvynia naaagvvtnn ssrstrrins iygmgelsys nyaflnltar
      721 ndwsstlpsn hnsyfypsas lsfivsdmlh lnsktvsfak vrmnwskvgk dtdpynlynn
      781 ftfaspdwgs vkmatfsatl knnnlkpeia tsyeagtdlk ffnnrlgiea tyystssrnq
      841 ivpiptsmss gystkiintg eirnsgweig vngtpvtgaf twnisanftr nrnkvvslsk
      901 dlssysmgsa egvqyqimeg tqmgdmygnt wktvpdgphk geelldntgh sqaatglvki
      961 gnynpdfmag ftnaftykqf slntlldwrq ggqffsyvfm nllsdgrtvn tlygrdaahg
     1021 gvswndngve rndgmiengy isdgnggyvk ntnvtdpesy ygdyywkmhq rntfsatyvk
     1081 lreasltytf tkkqlsrlpf tnlsvaligr nlfsytaagk gydpetamti ksgsivpgta
     1141 swslpytrsy gvklsvnf
//
LOCUS       WP_096514027             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_096514027
VERSION     WP_096514027.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38635
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvidsay eaagatigsa
       61 ndafgaelil kvvapsnsel alikrgtivv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivgptnlaa avaadasaly arnlldfmkl lfdkdgqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_096527592             529 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Nitrosoglobus terrae].
ACCESSION   WP_096527592
VERSION     WP_096527592.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Nitrosoglobus terrae
  ORGANISM  Candidatus Nitrosoglobus terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Candidatus Nitrosoglobus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Candidatus Nitrosoglobus terrae"
                     /db_xref="taxon:1630141"
     Protein         1..529
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56746
     Region          1..529
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipkelh lgekrvaatp dtaehlqklg fsvaleskag lsanfsdeay rqvgvkiien
       61 tpslwetsdi ilkvrppgky skpaidelal lregaylisf iwptqnknll eqlatkkatv
      121 lamdsvpris raqkldplss maniagyrav ieasyhfgrf ftgqitaagk ippakilvig
      181 agvaglsaig tavglggivr afdtrpevke qvqsigaefl vlnfkeessg kggyakemsk
      241 efiqaemalf aqqaaevdii ittalipgkk apiliteemv ksmrrgsviv dlaaeqggnc
      301 altkpdeatt khgvtilgyt dllsrlptqa sqlygtnlrh lleelcpnkd giihlnmkde
      361 iirsltvakd geitwppppl skpavpapkp lqqqaesipt qgqaiaatpk kkwqlskavk
      421 ialsmslsgl slwglgavap psfmphfmvf vlacfvgyqv iwnvtpslht plmsvtnais
      481 siiiigalvq vakpgillgi latiailits vniaggflvt qrmlrmfrk
//
LOCUS       WP_096550900             302 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Ureibacillus thermosphaericus].
ACCESSION   WP_096550900
VERSION     WP_096550900.1
KEYWORDS    RefSeq.
SOURCE      Ureibacillus thermosphaericus
  ORGANISM  Ureibacillus thermosphaericus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Ureibacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Ureibacillus thermosphaericus"
                     /db_xref="taxon:51173"
     Protein         1..302
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34993
     Region          5..164
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
     Region          <234..295
                     /region_name="Abi_C"
                     /note="Abortive infection C-terminus; pfam14355"
                     /db_xref="CDD:433897"
ORIGIN      
        1 mgildifskr nrkdmdpifk yddfpkefrv qvihiwsdai gaepysesmr lwaqihkllc
       61 keygvfelsd rggdnpfikc qyfilnelki ervldiielt frvidvaire leykwremgv
      121 vqtpddaile lnqrfrehgl gyqyvkgniv rvdsdyiyre avepaiqrlf degfegasde
      181 fmkahehfrk gndkeaiiea mkafesvmkt ilvrkkwsyd grdtasklin alfengivdk
      241 slqthltslk ttleglstir nrtsghgqge kkkevprhlv ayalhlcatn ilflidcyka
      301 sk
//
LOCUS       WP_096569215             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphaerospermopsis kisseleviana].
ACCESSION   WP_096569215
VERSION     WP_096569215.1
KEYWORDS    RefSeq.
SOURCE      Sphaerospermopsis kisseleviana
  ORGANISM  Sphaerospermopsis kisseleviana
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Aphanizomenonaceae; Sphaerospermopsis.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Sphaerospermopsis kisseleviana"
                     /db_xref="taxon:289435"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40795
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeie vcerrvslip divaklikqg leiyvetgag ekafftdady eaagakiisd
       61 patlwgeadi mlkvsppqer edgrseidll ktgsvlisfl nplgnpqiaq klaqrqital
      121 smeliprttr aqsmdalssq aslsgyktvl laaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkleeetvaa ggyakeised
      241 skkrtqelva ehvknsdvvi ttaqvpgrka pilvteemvk amkpgsvivd laaeqggnca
      301 ctapgkdivw ngvtiigpin lpssmpvhas qlysknital mqllikdktl qvnfaddivd
      361 aacvtyggei rnqrvkdalq avvv
//
LOCUS       WP_096573350             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tolypothrix tenuis].
ACCESSION   WP_096573350
VERSION     WP_096573350.1
KEYWORDS    RefSeq.
SOURCE      Tolypothrix tenuis
  ORGANISM  Tolypothrix tenuis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Tolypothrichaceae; Tolypothrix.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Tolypothrix tenuis"
                     /db_xref="taxon:457083"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40987
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vgerrvalip dvvaklvkqg levwvetgag ersffsdsay eaagakiigd
       61 patlwgeadi llkvsppqer edgrseidfl kagsvlisfl nplgnpaive klanrqvtal
      121 smeliprttr aqsmdalssq aslagyksvl iaaaalpkyf pmlttaagti apakifimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vqleeetvaa ggyakeisea
      241 skqrtqevvt ehvknadvvi ttaqvpgkka pllvteemvk qmkpgsvivd laaeqggnca
      301 ctdpgkdivw ngitiigpin lpssmpvhas qlyaknltsl mqlliskeka lqvdfaddiv
      361 daacvtyage irnkrvseel aalkvrg
//
LOCUS       WP_096588985             301 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Calothrix sp. NIES-2098].
ACCESSION   WP_096588985
VERSION     WP_096588985.1
KEYWORDS    RefSeq.
SOURCE      Calothrix sp. NIES-2098
  ORGANISM  Calothrix sp. NIES-2098
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Calotrichaceae; Calothrix.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Calothrix sp. NIES-2098"
                     /db_xref="taxon:1954171"
     Protein         1..301
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34878
     Region          5..164
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mkvydifskr qkrlrgefpd vyqyvdipqp lrvqifyiln dviaapidlh fmkgfseiys
       61 rlyreygklq qaivgkdiin lflfntqvte hildfielsf qlidttyrrs itvnenfski
      121 tadeaiaeln frfrehgvgy qyesgkmirv dsqiihteav kpvlhllsdt rfqganeefl
      181 kahehyrhgr ykeclveclk afestmktif dsqgwsyqst dtakklidic fqnnlipayl
      241 qtqftslrsn lesgiptirn knaghgqgsq litipqhfaa yqlhmtasti lflleaertl
      301 p
//
LOCUS       WP_096594179             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Calothrix
            sp. NIES-2098].
ACCESSION   WP_096594179
VERSION     WP_096594179.1
KEYWORDS    RefSeq.
SOURCE      Calothrix sp. NIES-2098
  ORGANISM  Calothrix sp. NIES-2098
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Calotrichaceae; Calothrix.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Calothrix sp. NIES-2098"
                     /db_xref="taxon:1954171"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41410
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vgerrvalip divarlvkqg leiwvetgag ersffsdsay eaagakiiad
       61 patlwgeadi llkvsppqer edgrseidfl kagsvlisfl nplgnplvvq qlanrqvtal
      121 smemiprttr aqsmdalssq aslagyksvl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkleeetvaa ggyakeisea
      241 skqrtqevva ehiknadvvi ttaqvpgkka pllvteemvk qmkpgsvivd laaeqggnca
      301 ctdpgkdivw ngitiigpin lpssmpvhas qlyaknltsl mqllinkdka lqvdfaddii
      361 daacvshage irnqrvqeal qalstqigkh
//
LOCUS       WP_096604574             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Calothrix
            sp. NIES-2100].
ACCESSION   WP_096604574
VERSION     WP_096604574.1
KEYWORDS    RefSeq.
SOURCE      Calothrix sp. NIES-2100
  ORGANISM  Calothrix sp. NIES-2100
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Calotrichaceae; Calothrix.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Calothrix sp. NIES-2100"
                     /db_xref="taxon:1954172"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40978
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vgerrvalip divarlvkqg leiwvetgag ersffsdsay eaagakiiad
       61 taklwgeadi llkvgspqer engrseidfl kvgavlisfl nplgnplvvq qlaarqital
      121 smemiprttr aqsmdalssq aslagyksvl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkleeetvaa ggyakeisea
      241 skqrtqelvs ehvknadvvi ttaqvpgkka pllvteemvk qmkpgsvivd laaeqggnca
      301 ctspgrdivy ngitiigpin lpssmpvhas qlyaknltsl mqllinkeka lhvdfsddiv
      361 daacvthage irnqrvseal aalkvkg
//
LOCUS       WP_096619614             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Enterovibrio altilux].
ACCESSION   WP_096619614
VERSION     WP_096619614.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Enterovibrio altilux
  ORGANISM  Candidatus Enterovibrio altilux
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Enterovibrio.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Candidatus Enterovibrio altilux"
                     /db_xref="taxon:1927128"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55334
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil ayetrvaatp ktveqlinmg fdvviesnag llasfdnaaf ekagarvvda
       61 eavwqsniif kvnapiklek tneferlkeg mtlisfiwpa qnavlmeqla akninvlamd
      121 avprisraqa mdalssmani agyravveaa hefgrfftgq itaagrvppa kvfvmgagva
      181 glaaigtass lgaivsafdv rhevkeqves mgayflpvsf teeassgdgy akeisdnfnr
      241 kvaelcfeqa kdvdiiitta lipghpaprl itkkmvnsmk sgsvivdlaa anggnceyte
      301 adkiiltdng vkvigytdmv srlptqssql ygtnlvnlmk llckkksgdi nidfedlilr
      361 gvtvikegev twpaplmpis aqsqvksksv tkeakvkkpm scvkrvtmls vavgvfgwla
      421 svapvaflsh ftvfvltcii gyyvvwnvnh alhtplmsvt naisgiiivg allqigqgng
      481 ivsflafiav liasinifgg ftvtqrmlem frrdk
//
LOCUS       WP_096623808             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Calothrix
            sp. NIES-3974].
ACCESSION   WP_096623808
VERSION     WP_096623808.1
KEYWORDS    RefSeq.
SOURCE      Calothrix sp. NIES-3974
  ORGANISM  Calothrix sp. NIES-3974
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Calotrichaceae; Calothrix.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Calothrix sp. NIES-3974"
                     /db_xref="taxon:2005462"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40608
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaiakeie vgerrvalvp dtvsrlvkqg levwvetgag erayfddaay adsgaqiiks
       61 keqlwgeadi vlkvnppglt eegnseldll ksgsvlisfl nplgkpeial klaergvtgl
      121 smemipritr sqsmdalssq asiagykavl vaaamlpkyf pmlttaagtv ppakvlviga
      181 gvaglqaiat arrlgavvea fdvrpvvkeq vqslgakfid iqidentdag ggyakqvget
      241 tqetirqaia phvksadvvi ttaqipgkpa plmiceqtvm gmkpgavivd laaenggnca
      301 ltekgrdvvk hgitiiaptn lpastpihas qlysknlasl lqllikdqql nldfgdeiin
      361 aicithagei rsdrirnllt vkqv
//
LOCUS       WP_096629050             310 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salinivibrio sp. YCSC6].
ACCESSION   WP_096629050
VERSION     WP_096629050.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. YCSC6
  ORGANISM  Salinivibrio sp. YCSC6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Salinivibrio sp. YCSC6"
                     /db_xref="taxon:2003370"
     Protein         1..310
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35890
     Region          5..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 malfelfskr qkklrgeapd iyqydkleqn frvqvvhivq dtigsessyh tvtnavyqei
       61 hkilckeygv fslkkdansh fesvfnffln ekdhekcldv ievtfqfidt vvrerewefn
      121 naigvsqkpe daidelnarf kesgigyqfe sgnliridsq yvhseivkpa lfflgkdrqy
      181 agvsdeflsa hehyrhkryk eclndclksf eslmkaihek hkwpfnrndt akklihscls
      241 nklvpdylqn qfsslrvlle sgiptirnke gghgqggeit svpehlasyt lhltatnllf
      301 likceekyrg
//
LOCUS       WP_096667993             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Dolichospermum compactum].
ACCESSION   WP_096667993
VERSION     WP_096667993.1
KEYWORDS    RefSeq.
SOURCE      Dolichospermum compactum
  ORGANISM  Dolichospermum compactum
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Aphanizomenonaceae; Dolichospermum.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Dolichospermum compactum"
                     /db_xref="taxon:136073"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40562
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeie vcerrvalip dtvaklvkqg ldvwveagag ekaffsdady eaagakiign
       61 saqlwseadi llkvsppqtr edgrteiell ksgsvlisfl nplgnpviaq qlanrqital
      121 smeliprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkleeetvaa ggyakeised
      241 skkrtqelva shvknsdivi ttaqvpgrqa prlvteemva qmkpgsvivd laaeqggnca
      301 cteagkdiiw ngvtiigpin lpssmpvhas qlyaknvtsl mqllikdkal einfgddivd
      361 aacvthggei rnqrvkdalq avav
//
LOCUS       WP_096667564             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polaromonas sp. AET17H-212].
ACCESSION   WP_096667564
VERSION     WP_096667564.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. AET17H-212
  ORGANISM  Polaromonas sp. AET17H-212
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Polaromonas sp. AET17H-212"
                     /db_xref="taxon:1977061"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38254
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpaeit agetrvavtp etakklksqg htvciqsgag vaasvpdeay vaagaeitda
       61 agayasdivl kvrcpldsei glakagtvlv gmlnpfdpag lqrlaaaqlt afaleaaprt
      121 sraqsmdvls sqaniagyka vmmaansyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslggkf idvpyetdee reaavgvggy akpmppswle
      241 rqkaevakrv aladvvitta lipgraapvl vtedmvkamk pgsvivdlaa pqggncplte
      301 pgktvvkhgv tligetnvpa lvaadasaly arnlldflkl viskegtlni dleddivaac
      361 lmtqggevkr k
//
LOCUS       WP_096672052             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter meluiroseus].
ACCESSION   WP_096672052
VERSION     WP_096672052.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter meluiroseus
  ORGANISM  Polynucleobacter meluiroseus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Polynucleobacter meluiroseus"
                     /db_xref="taxon:1938814"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39589
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpletr pdetrvaatp etvkklisqg hqvliqkdag vkasqpdaay eavgasivda
       61 aqafsaeivl kvrapeahel kqipsgsvli gmldpfdqhn idamaaqgit afsleaaprt
      121 traqsmdvls sqaniagyka vlvaaneyqr fmpmlmtaag tvkaarilil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpyetdee reiakgaggy arpmpeawmk
      241 rqaalvaera qqadivitta lipgrkppvl lqsdtvarmk pgsvvidlaa grgdngsgnc
      301 plteadkive kngvkiigyt nlasmvaada salyarnlid fmklivnaea kllipadddi
      361 vtaclmcrdg qavrkn
//
LOCUS       WP_096684838            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Ichthyobacterium seriolicida].
ACCESSION   WP_096684838
VERSION     WP_096684838.1
KEYWORDS    RefSeq.
SOURCE      Ichthyobacterium seriolicida
  ORGANISM  Ichthyobacterium seriolicida
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Ichthyobacteriaceae; Ichthyobacterium.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Ichthyobacterium seriolicida"
                     /db_xref="taxon:242600"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118293
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnssllmfl tiiltlqisf aqlrisgtvn skeeneifpl tgasivikgt nkgvssdlng
       61 dfsidaekgd vlefsfigmk tvlfnveksd vitidmipds dlldevvvma ygsekskrel
      121 vgavgtvgke vienqqvtsv agalqgsvpg ltmitsggqp gsnptirirg iasinasadp
      181 lyvvdgvplt gnintissdq iesmtvlkda assavygsra angvilittk kgtynsppkv
      241 sintviggat pavkgfefls vkdymelswe glrnsylytq dktgslivnp kitprqaaqk
      301 atdnliselg ynpygvnnpv glngkvlpnl kqplwetdwe kafyrgislr kdvslsvsgg
      361 nndskyfvsa nyldtdgpvk tsnferfatk fnlssrvkdw lnftvlssfs gshsnvplqs
      421 ggkvtnpmsw vnrissiypl yarndkgkii kddngnpqyd ysnrkggvna qrpeslttgn
      481 vnpagqfend vniikrrqst lngimdarly eglhfkqnvs ftnftfmnhy yghykygdss
      541 ieggivseyr diystwnsis sleyqktfgl hnfdakvine fmyftlnkik akgkkllpev
      601 kvldgavips niggsegreg lmsyvamagy dydkkyylts sfrmdgssrf hkdtrwgnfy
      661 sigaswivsn edfmeplkev lsftkvnlsy gelgnnkild snddiyffpy vntvfeasng
      721 nnmgyllskl vndkitwekv lsfnvglnlv ffddrieldv dyyrkvtkdl llykplppsi
      781 gwttilvneg gllnygfegv irsknistdd fkwntsmnfs fdrntitelt qkevikgtkk
      841 wmvgksiydf fireyagvdp kdgmaqwykd ekdktgkktg krvltkkyse adkyyqgssl
      901 pdiiggfnny isygdfdldi llnfsfggmv ydysyssltd gmkklgkqqs vdikkrwtkp
      961 sdktdfplll snsinragdd ssrylfkndy irlkavtlgy nipnsvldki nlsklkvylq
     1021 gdnlltyqsh kgidpeqsfn gltdsrsrsl rtfslgvkie f
//
LOCUS       WP_096685237            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Ichthyobacterium seriolicida].
ACCESSION   WP_096685237
VERSION     WP_096685237.1
KEYWORDS    RefSeq.
SOURCE      Ichthyobacterium seriolicida
  ORGANISM  Ichthyobacterium seriolicida
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Ichthyobacteriaceae; Ichthyobacterium.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Ichthyobacterium seriolicida"
                     /db_xref="taxon:242600"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118709
     Region          26..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnsinkllpi vigiiffqis haqemkisgt itsddngetl savsikikgk nfgtssdfdg
       61 eysidanrgd vlefsfigmk tkyvkvegsn ridvimnsdt qllddvvvta lgikkekksl
      121 gysvqkvsgd dvnvvksgni tnslsgkiag vkinrtnnmg gstnviirgn sslsgdnqal
      181 fvvdgvpisn ysknanttkh taidygnias dinpediksv evlkgaaasv lygsqaangv
      241 imittkkggd igtksanvif ksstsfgfld qstfpeyqke ygggsngeds wvdfpiglnt
      301 veknagvpfn tqasfgpkys dkkkvynwwa aysesgkdky rkkgvwkyae ndpltyfetp
      361 vtlsntisvs gsnesasyrl sytnhnekgs epngsinkdn fslsssykfs nklssnvsvs
      421 nilqkaigrs rmgrddnnmt mfrqlwatnv dlkqqreaye knkkniswnf ilngdkphps
      481 ywnniyfery enyptdyrnr wlgnasldyk fidlkglkvs glvrasidty ymyydmriqk
      541 gsrsmqlavi ndlvtsgyyr adshfklfnh dailnidadi npdlsfvgli gttvkrehts
      601 ftrahtnggl giaghyflrn smksilppke ydtilgtnsl yssasldykk yayvdlsvra
      661 dqsstlpqgs nlyvypsmst sviltelidi phvsfgklrv nvaqvgasae fdkivdtymf
      721 eaenggavsg vhhtkknpel kpesttsyev gldlklldnk igldmafyyn ltkdqisnvt
      781 ttsstgytsk mvnggklsnk gleialsskd islglvswns svnwsmnrse vlslakgvkk
      841 eklhkrkigt nvsihstkgs pygliygtdf eyhksgakiv dkttgkykvs essskvignq
      901 npdwllgfsn sfsyegfvfs flidcqkggd ifsvdmlygl gnglyketsf tnengknird
      961 kvadgggiln pgvyedgtkn ttrmevtqgs lggslpdkaf vydasyiklr emsisydlpl
     1021 gteyfkkitl glvgsnlwil yknlpyadpe asmgagnaqg fsvgslptfr elavniklnf
//
LOCUS       WP_096685538             622 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Ichthyobacterium seriolicida].
ACCESSION   WP_096685538
VERSION     WP_096685538.1
KEYWORDS    RefSeq.
SOURCE      Ichthyobacterium seriolicida
  ORGANISM  Ichthyobacterium seriolicida
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Ichthyobacteriaceae; Ichthyobacterium.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Ichthyobacterium seriolicida"
                     /db_xref="taxon:242600"
     Protein         1..622
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=67995
     Region          25..>576
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnssllmfl ttiltlqisf aqlrisgtvn skedntispl tgvsivikgg nkgvssdlng
       61 efsidaekgd vlefsfmgmk tvlfnveksd vitidmipds dlldevvvma ygsekskrel
      121 vgavgtvgkk vienqqvtsv aralqgsvpg ltmitsggqp gsnptirirg iasinasasp
      181 lyvvdgvplt gnintissdq iesmtvlkda assavygsra angvilittk kgtynsppkv
      241 sintviggai pavkgfefls vkdymelswe glrnsylytr dktgslivnp kttprqaaqn
      301 atdnlisklg ynpygvnnpv gpngkvlptl nkplwetdwe kafyrkmplr kdvslsvsgg
      361 gddskyfvsa nyldtdgpvk tsnferfatr lnlssrvndw lnftvlssfs gshsnvprqs
      421 gskianpmlw vnrvssiypl yarndkgeii eddngnpqyd ysnrrgkgan aqrprslttn
      481 nknpagqfen ddvihkrrhs tlngimdlrl yeglhfkqnv sftnytlmeh dydhykygda
      541 srvggritee rhihskwnsi ssleyqknfg lhnfdakvin efmhftlnki taegerllpe
      601 vkvlngavip sgiggavkae ka
//
LOCUS       WP_096687163             969 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Ichthyobacterium seriolicida].
ACCESSION   WP_096687163
VERSION     WP_096687163.1
KEYWORDS    RefSeq.
SOURCE      Ichthyobacterium seriolicida
  ORGANISM  Ichthyobacterium seriolicida
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Ichthyobacteriaceae; Ichthyobacterium.
REFERENCE   1  (residues 1 to 969)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 969)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 969)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..969
                     /organism="Ichthyobacterium seriolicida"
                     /db_xref="taxon:242600"
     Protein         1..969
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110082
     Region          24..967
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mridlgktil vflslhvnlc faqfslsgtv lskedelplp gveisiegtd kntstnfdge
       61 ysieahigdv lkfsflglqt vrkkvvgkee idiyleinkv drdkiidvgy gtqdeifisd
      121 aidkmplkei ypiplgnllm gkipgalvnq qneivdsdin itvrglssvt rnilrpmyvi
      181 dgiemptyyn vdplsfinqn diesitvlkd asskaiygvk gsngvvilnt krgsdknkfs
      241 lslykglsip trklnllngp kykelllesl knagyselga ekimndslsl yqgdrqwkni
      301 dnnwqdlafq mgytrdanfs fyggnevfks yvslgyndkk gilvgdklsk ytfsfnmkyn
      361 lnekinfgii snafnnnydy lsadknlnks ldilkeipvs psyltngein kntymknkfl
      421 ledkipnnrn tsynlygktf vnyfifpelt lrselgynly nsidgafmsk ylhkynrfsy
      481 sannyitikq eipvvgkikl mfgtsfrrnn idsslenske vlakkddini sdnknvfdal
      541 kysvnssyls yfirlnyils dkyfikmslt gdsdsyldng ynhntffsvs sgwiisrekf
      601 mepmssvvsn lklrtswgii gnspyenaft klfssyhded kspisvfkel lvfnlqlekt
      661 qeynigldys lyedrltgsl dlykkitngv flnsqydkfk digisnqgie fslntksivl
      721 edlsflwntn fsisvninki rslgggadiv idnnilrqgs ainsfylkey agvnpnngka
      781 myykntlknn geldktkten yqeaekrifg slfpsafiwl nntikyigfd lsfafqatvg
      841 gkryskhrei hesgfskglh nqssemlkrw qkkgdnsntp kliygidngs npstrfless
      901 dhlhlkelvl gyslsdivle kigmshfriy lsalniptlt nyksydresi sidplaqsmi
      961 ismglnmrf
//
LOCUS       WP_096696529             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polaromonas sp. AER18D-145].
ACCESSION   WP_096696529
VERSION     WP_096696529.1
KEYWORDS    RefSeq.
SOURCE      Polaromonas sp. AER18D-145
  ORGANISM  Polaromonas sp. AER18D-145
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Polaromonas sp. AER18D-145"
                     /db_xref="taxon:1977060"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38226
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpaeit agetrvavtp etakklksqg htvciqsgag vaasvpdeay vaagaeitda
       61 agayasdivl kvrcpldsei glaqagtvlv gmlnpfdpag lqrlagaqlt sfaleaaprt
      121 sraqsmdvls sqaniagyka vmmaadsyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslggkf idvpyetdee reaavgvggy akpmppswle
      241 rqkaevakrv aladvvitta lipgraapvl vtedmvkamk pgsvivdlaa pqggncplte
      301 pgktvvkhgv tligetnvpa lvaadasaly arnlldflkl viskegalni dleddivaac
      361 lmtqggevkr k
//
LOCUS       WP_096701873             529 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Magnetospirillum sp. 15-1].
ACCESSION   WP_096701873
VERSION     WP_096701873.1
KEYWORDS    RefSeq.
SOURCE      Magnetospirillum sp. 15-1
  ORGANISM  Magnetospirillum sp. 15-1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Magnetospirillum.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Magnetospirillum sp. 15-1"
                     /db_xref="taxon:1979370"
     Protein         1..529
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55357
     Region          3..529
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msltigvpre tfpnekrvat vpdvveklik lgfsvvvetg agalanfdde syvaagasia
       61 ksaaelwtaa dmvfkvraps mdevalikeg ttligfiwpa qnpelmqala arkitvlamd
      121 cvprqlsraq kmdalssman iagyravvea anqfgrfftg qitaagkvpp akvfvagagv
      181 aglaalgtav slgaivrand traevadqvk smgaefvkvd yeeegsgggg yakvmsegfq
      241 aaqremyaqq arevdiiitt alipgkpapr litaemvssm ragsvivdma aeqggncelt
      301 vpgevvvrhg vtiigyadlp srlskqastl yatnllrlte elcktkdgvi dvnmgddair
      361 gltvikegei twpppplvlp appapkaasa apvaakksgh ghgagepmsp ksltitfgig
      421 alafwfvgan apeaflghft vfvlacfvgy mvvwnvtpal htplmsvtna issiivigal
      481 vqispplgeg isrpgfwigl lavisiilts inmfggfavt krmlamfrk
//
LOCUS       WP_096721077             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia acidicola].
ACCESSION   WP_096721077
VERSION     WP_096721077.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia acidicola
  ORGANISM  Paraburkholderia acidicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia acidicola"
                     /db_xref="taxon:1912599"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39406
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvaqg hrvtvqsgag ngasfpdeaf taagaeivdv
       61 aaafgadlvl kvqspteael pqlkrgavlv gmldpfnadn aaklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgsvi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswlt
      241 rqsalvhera kqadivista lipgrpaptl isvetvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvtkhgvqi vgytnlasmv aadasslyar nlldflkliv tkegtlnidl
      361 addivaatll ardgavtrkp
//
LOCUS       WP_096707950             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phaeobacter gallaeciensis].
ACCESSION   WP_096707950
VERSION     WP_096707950.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter gallaeciensis
  ORGANISM  Phaeobacter gallaeciensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Phaeobacter gallaeciensis"
                     /db_xref="taxon:60890"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55578
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egearvamtp dsavqlqklg yicaietgag aaagfadaty eavgveivkt
       61 paalwkasdi vakvrqptet elkrmtagkt lisffnpggn eagmelarsk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigastslg aityafdvrp evaeqvesmg aefvyldfee sqqdgaatgg yaavsspefr
      241 eaqlakfrel apdvdivitt alipnreapk lwledmvaam kpgsviidla aekggnvegt
      301 vmdekvvten gvtiigytdf psrmaaqast lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgatvtfeke itfpppppkv qaiaaqpkke vkeltpeekr eqeieafkqq tkqqvtllgv
      421 ggalvllvgl fapasfmqhf ivfalacfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl viflaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_096753814             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Citrobacter koseri].
ACCESSION   WP_096753814
VERSION     WP_096753814.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter koseri
  ORGANISM  Citrobacter koseri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter koseri"
                     /db_xref="taxon:545"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53504
     Region          5..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 martilrarr ffslilpfff issvyaeqts vpaktvtvea knetfapqhp dqylswkats
       61 eqstredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnalgc adchntasdd fakgkpaltl
      181 srpyaerame tigkpfdkas rfdqqsmvcg qchveyyfdg knkavkfpwd egtkvedmek
      241 yydaiafsdw tnplsktpml kaqhpeyetw svgihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gateaemkpi lddirhaqwr wdlaiashgi hmhapdeglr mlggamdkaa dartklvcll
      421 gskgitheip lpdistkeka qkaiglnmqq inaekqdfik tvipqwedqa rkngllsq
//
LOCUS       WP_096758690             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Citrobacter].
ACCESSION   WP_096758690
VERSION     WP_096758690.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53509
     Region          10..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 martkspvlr ffslilpflf isavhaeqtp vpaktvtvea knetfapqhp dqylswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntasad fakgkpeltl
      181 srpyaerame sigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmek
      241 yydaiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegkiytd
      301 hkignpfdnf pqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gateaemkpi ledirhaqwr wdlsiashgi hmhapeeglr mlgsamdkaa dartklvrll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdfik tvipqwedqa rkngllsq
//
LOCUS       WP_096763700             382 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium].
ACCESSION   WP_096763700
VERSION     WP_096763700.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38907
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgniifvase vtdgetrvaa saetvkkmks fgfdvvveag agaasripdr efeaagarig
       61 sladaasadv vlkvrrpsas eiagyksgav viaimdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqg
      241 kqaalvaehi tkqdivitta lipgraaprl vsramlasmk pgavavdlav erggniegvv
      301 ageiadvegv svigfanmpg rvaasasaly aknlvtflet mvnketgsvv vnvddelvka
      361 tmltyagdvv hpafggakkg dm
//
LOCUS       WP_096765349             511 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Snodgrassella].
ACCESSION   WP_096765349
VERSION     WP_096765349.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella
  ORGANISM  Snodgrassella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Snodgrassella"
                     /db_xref="taxon:1193515"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54002
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg hevviehdag kaaslsdgly qeagatvada
       61 dtvwqcplif kvnapnkeei asmqsgtilv sfimpaqqse lvqqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flqldyqeee sssgdgyakt msaayieaem
      241 klfaeqarqv diiittaaip gkpapklitr emvdsmregs vivdlaaatg gnceytepgk
      301 iittangvki igytdmanrl agqssqlygt nlvnlarllt pnkdgelaln fedviirnmt
      361 vthegnsmyp pppiqvsaap kaepkvaapa pvataqpasa nkkiiwaaia vilmlwigav
      421 apvaflnhfm vfvlacvvgy fvvwnvnhal htplmsvtna isgiivvgal lqigqghgfv
      481 sllafiavai vsvnifggfa vtrrmlnmfr k
//
LOCUS       WP_096786150             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodobacter sp. CZR27].
ACCESSION   WP_096786150
VERSION     WP_096786150.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacter sp. CZR27
  ORGANISM  Rhodobacter sp. CZR27
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Rhodobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rhodobacter sp. CZR27"
                     /db_xref="taxon:2033869"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55435
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreif egearvamtp dsalqlqklg hhcvietgag mkagfsdeay aaagvevlps
       61 akavfdtadv vvkvrgpepa eaqmlrsgqt lisffwpaqn aellelckak gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtavslg aityafdvrp evaeqiesmg aefvflefee aqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrpapkl wtedmvssmk rgsvivdlaa erggncdltv
      301 pdqkvvspng vtiigytdfp srmaaqastl ystnirhmlt dltpkkdgvi dhnmdddvir
      361 gatvthagai tfpppppkvq aiaaakprek vkeltpeekr aaehkafrkq tisqvtmlav
      421 gtalllfvgn yappsfmahf ivfalacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 llqigsgnwl vvmlaavsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_096770604             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sophoriradicis].
ACCESSION   WP_096770604
VERSION     WP_096770604.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sophoriradicis
  ORGANISM  Rhizobium sophoriradicis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium sophoriradicis"
                     /db_xref="taxon:1535245"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38822
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgniifvase vtdgetrvaa saetvkkmks fgfdvvveag agaasripdg efeaagarig
       61 sladaasadv vlkvrrpsas eiagyksgav viaimdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqg
      241 kqaalvaehi tkqdivitta lipgraaprl vsramlasmk pgavavdlav erggniegvi
      301 ageiadvegv svigfanmpg rvaasasaly aknlvtflet mvnketgsvv vnvddelvka
      361 tmltyagdvv hpafggakkg dm
//
LOCUS       WP_096790229             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phaeobacter piscinae].
ACCESSION   WP_096790229
VERSION     WP_096790229.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter piscinae
  ORGANISM  Phaeobacter piscinae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Phaeobacter piscinae"
                     /db_xref="taxon:1580596"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55448
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf dgearvamtp dsavqlqklg ytcaietgag aaagfadaty eavgveivkt
       61 paalwkaadi vakvrqptet elkrmtagkt lisffnpggn eagmelarsk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigastslg aityafdvrp evaeqvesmg aefvyldfee sqqdgaatgg yaavsspefr
      241 eaqlakfrel apdvdivitt alipnreapk lwledmvaam kpgsviidla aekggnvegt
      301 vmdekvvten gvtiigytdf psrmaaqast lyatnirhmm tdltpekdgq inhnmeddvi
      361 rgatvtfeke itfpppppkv qaiaaqpkke vkeltpeekr aqeveafkqq tknqvtllav
      421 ggalvllvgl fapasfmqhf ivfalacfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl viflaavsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_096792378             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudoalteromonas sp. 1_2015MBL_MicDiv].
ACCESSION   WP_096792378
VERSION     WP_096792378.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. 1_2015MBL_MicDiv
  ORGANISM  Pseudoalteromonas sp. 1_2015MBL_MicDiv
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Pseudoalteromonas sp. 1_2015MBL_MicDiv"
                     /db_xref="taxon:1720343"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53950
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkeir tgerrvattp davskliklg fnvaieagag maanytdday iaagcevvns
       61 aqdiwaqsdi vlkvqapevd entllksgqi licflwpaqn peilkdltqr gitaiaidsi
      121 prisraqkmd arssmanisg yraiveaaqh fgrfftgqit aagrvapakv lvigagvagl
      181 aaigaaksmg aivrsfdtra evkeqiesmd aeflmldfkd edgsgeggya kvmsdefiea
      241 emalfaaqak dvdiivttal ipgkpapkli tsemvasmns gsvivdlaae qggnceltvp
      301 gkvavchgvs iigytdlpsr latqssqlys nnlynllaem tpekdgelfv dmtndvvlga
      361 tictegkttw pppattlsat pkkvaatpis tptivekkks vfgpiigaai galallglgg
      421 vapadfmshf tvfvlacfvg ymviwsvspa lhtplmsvtn aissiiviga liqisstddt
      481 ikwfavftvl iasinivggf avthrmlkmf rk
//
LOCUS       WP_096797300             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_096797300
VERSION     WP_096797300.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38760
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 nnafgaelil kvvapsdael alikrgtvlv gmlnpfnndt iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_096805481             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Celeribacter ethanolicus].
ACCESSION   WP_096805481
VERSION     WP_096805481.1
KEYWORDS    RefSeq.
SOURCE      Celeribacter ethanolicus
  ORGANISM  Celeribacter ethanolicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Celeribacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Celeribacter ethanolicus"
                     /db_xref="taxon:1758178"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55802
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgvpkevf egearvaltp esakqlqklg ydcaieagag aaagfsdkvy aeagvevieg
       61 akalwdacdi vakvrqpdet emgylregqt lisffnpggn aegmekaket ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgsatgg yasvqseefr
      241 naqlakfrel apemdivitt alipnrpapv lwtkdmveam kpgsvivdla aerggnvegt
      301 mkdervvtdn gvviigytdf psrmatqast lyatnirhmm tdltpekdgk lvhnmeddvi
      361 rgatvtydha itfpppppkv aaiaakpkek vkeltpeekr aaevaafkkq trnqvtliav
      421 gailllgvgl vapasfmqhf ivfvlsvfig fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgswl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_096831171             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Tychonema
            bourrellyi].
ACCESSION   WP_096831171
VERSION     WP_096831171.1
KEYWORDS    RefSeq.
SOURCE      Tychonema bourrellyi
  ORGANISM  Tychonema bourrellyi
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae; Tychonema.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Tychonema bourrellyi"
                     /db_xref="taxon:54313"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40206
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklaiakeie agerrvalvp davaklvkqg vevwveagag aksffsdlay eaagakvvad
       61 tatlwgeadv vvkigelqes evhqlreggv figflnplgn palvqrladr hvtafsmemi
      121 prtsraqsmd alssqanvag ykavliaaaa lpkyfpmltt aagtirpakv lvmgvgvagl
      181 qaiatarrlg avveafdirp etkeqvqslg akfidvelke etvaaggyak elseaakeht
      241 rqvltqhvga sdavittaqv pgrkapilvt remvsqmkpg avivdlaaeq ggncecteag
      301 kdvewngvnv igpinlpgsm pvhasetysk nvssllqlml kdkelnlnfe ddiiagscva
      361 rdgeisnqrv rdalaaqasv vs
//
LOCUS       WP_096839146             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096839146
VERSION     WP_096839146.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53588
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml ksqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096842419             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096842419
VERSION     WP_096842419.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53531
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc gdchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096839861             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_096839861
VERSION     WP_096839861.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36050
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygifslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel asymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_096873101             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phaeobacter piscinae].
ACCESSION   WP_096873101
VERSION     WP_096873101.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter piscinae
  ORGANISM  Phaeobacter piscinae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Phaeobacter piscinae"
                     /db_xref="taxon:1580596"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55570
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf dgearvamtp dsavqlqklg ytcaietgag aaagfadaty eavgveivkt
       61 paalwkaadi vakvrqptet elkrmtvgkt lisffnpggn eagmelarsk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigastslg aityafdvrp evaeqvesmg aefvyldfee sqqdgaatgg yaavsspefr
      241 eaqlakfrel apdvdivitt alipnreapk lwledmvaam kpgsviidla aekggnvegt
      301 vmdekvvten gvtiigytdf psrmaaqast lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgatvtfeke itfpppppkv qaiaaqpkke vkeltpeekr eqeveafkqq tknqvtllav
      421 ggalvlfvgl fapasfmqhf ivfalacfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl viflaavsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_096876155             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylomonas koyamae].
ACCESSION   WP_096876155
VERSION     WP_096876155.1
KEYWORDS    RefSeq.
SOURCE      Methylomonas koyamae
  ORGANISM  Methylomonas koyamae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylomonas.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Methylomonas koyamae"
                     /db_xref="taxon:702114"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54617
     Region          1..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkevy dgekrvattp eaaekiiklg fevllesgag adanisdday caagvqivet
       61 aqelwqksdi vmkvrapqqh pqlgvdeadl lrdgqhlisf iwpaqnealm qklaaknatv
      121 lamdsvprms raqkmdalss maniagyrai veaaqhfgrf ftgqitaagk ippakvlvig
      181 agvaglaaig aakgmgaivr afdtrpevke qiesmdaefl mldfkedgsg sggyakvmsa
      241 efiaaemalf aqqakevdii vttalipgkp apelitaemv asmkpgsviv dlaaeqggnc
      301 alteknqvvv khgvtiigyt nlpsrlanqs sqlyatnlrh lltdlcpnkd gtlnvnfdde
      361 virgatvike gkitwppppp qlsaapkaaa aasaavatep kkpllpepir qflpmvlagl
      421 alfgvgavap asflahftvf vlacfvgymv iwnvtpslht plmsvtnais giivigalvq
      481 vsstteivag lsglailias iniaggflvt rrmlamfrk
//
LOCUS       WP_096883278             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Dermabacter jinjuensis].
ACCESSION   WP_096883278
VERSION     WP_096883278.1
KEYWORDS    RefSeq.
SOURCE      Dermabacter jinjuensis
  ORGANISM  Dermabacter jinjuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Dermabacter.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Dermabacter jinjuensis"
                     /db_xref="taxon:1667168"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53682
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipretl edqplvaatp dtvrklrklg ydvavergag erasyldaay adagaeivge
       61 evwqsdivtt ldtppremre rmlagavlis rmapgrnpel idelkehrlt alamdavpri
      121 sraqsmdvls smaniagyra vieaasnfgr lftgqvtaag kvppanvyvi gagvaglaai
      181 gtansmgaiv katdlrpeaa eqvesmgaef vpieakteks edgyakemta dqakaaaqly
      241 srqsaeadiv ittanipgrk apvlltaadv qnmkpgsviv dmaaanggnc eltrpgevyq
      301 tengvtivgh tdlagrlpgq asqlygqniv nlmklvtpqk ngvmmldfed tivrgitvtf
      361 ahdgqadvlw ppppvkvsaa papapeaapa paeapeakks hagtiaaiig gilgvalvla
      421 spfqvaeqym vlmlaivvgy yvitsvthsl htplmsetna isgiilvgai lqvgsaniav
      481 ailsfiaivi asinifggft vthrmlsmfs reg
//
LOCUS       WP_096888530             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096888530
VERSION     WP_096888530.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53630
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd ddmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096915107             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096915107
VERSION     WP_096915107.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53602
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqtiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096918001             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_096918001
VERSION     WP_096918001.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36073
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fhilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel vsymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_096940900             207 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Escherichia coli].
ACCESSION   WP_096940900
VERSION     WP_096940900.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>207
                     /product="STM4504/CBY_0614 family protein"
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkyits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykecl
//
LOCUS       WP_096942618             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_096942618
VERSION     WP_096942618.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36084
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkyits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel asymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_096950361             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096950361
VERSION     WP_096950361.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53575
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgmamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096953879             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_096953879
VERSION     WP_096953879.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36050
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshiak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel asymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_096959347             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_096959347
VERSION     WP_096959347.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36037
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvae
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel asymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_096960454             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096960454
VERSION     WP_096960454.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53559
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ievedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq inaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096960656             218 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Escherichia coli].
ACCESSION   WP_096960656
VERSION     WP_096960656.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>218
                     /product="STM4504/CBY_0614 family protein"
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesim
//
LOCUS       WP_096965311             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_096965311
VERSION     WP_096965311.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36008
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseevir vdsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel asymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_096960827             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_096960827
VERSION     WP_096960827.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53500
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpgltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqqvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_096994421             471 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            thalassae].
ACCESSION   WP_096994421
VERSION     WP_096994421.1
KEYWORDS    RefSeq.
SOURCE      Vibrio thalassae
  ORGANISM  Vibrio thalassae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Vibrio thalassae"
                     /db_xref="taxon:1243014"
     gene            1..471
                     /gene="nrfA"
     Protein         1..471
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52257
     Region          3..471
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnkhwilssv aaiallgals asavaapeeg lidprnqaye kdhpdqyktw ketseseeie
       61 dalahdpnmv ilwagygfak dynkarghfy alddvrqtlr tggptdpksg pmpmacwsck
      121 spdvgrvide rgedgyfegk warlgaeisn pigcadchdt rsdafkngep alaiakpyve
      181 rafeaigkkf deqsrldqqa svcaqchvey yftgptkavk fpwdmgttvg emetyydaln
      241 fkdwqhavsk apmlkaqhpg yetwrdgihg kngvvcvdch mpkvtkedgt vftdhkvgnp
      301 fdrfedtcan chtqtkeqlq givstrkaqv lnmkltaekq ivaahfeaga awdagateee
      361 mkpilmdirh aqwrwdyaia shgvhmhape valeilgtsv dkaadarakl irllakkgit
      421 dpveipdist kekaqaalgm dmdkmnaekq hfletvvpew dkeaaareak y
//
LOCUS       WP_096994093             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            thalassae].
ACCESSION   WP_096994093
VERSION     WP_096994093.1
KEYWORDS    RefSeq.
SOURCE      Vibrio thalassae
  ORGANISM  Vibrio thalassae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio thalassae"
                     /db_xref="taxon:1243014"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54073
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaatp ksveqllklg fdvsiepqag llasfddsay eaagatitss
       61 kevweadlvl kvnaptdeei allkdgaslv sfvwpaqnpe lmeklsskni nvmamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrsfdvrpev keqvesmgae flevdyqens gsgdgyakem sdefnkkaae
      241 lymqqakdvd iiittalipg rpapklvtke mvdamkpgsv ivdlaaangg nceytvadqv
      301 vmtengvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgninidf edvvlrgvtv
      361 vkegevtwpa ppiqvsaqpa pakaevkkpa ekveeptspv kklvglvaav gvfgwvasva
      421 paaflshftv fvlacvvgyy vvwnvthalh tplmsvtnai sgiivvgall qigqgsgvvt
      481 flsfiavlia sinifggftv tkrmlemfrk dk
//
LOCUS       WP_096981225             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_096981225
VERSION     WP_096981225.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36092
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimra ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel vsymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_097023953             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chromohalobacter canadensis].
ACCESSION   WP_097023953
VERSION     WP_097023953.1
KEYWORDS    RefSeq.
SOURCE      Chromohalobacter canadensis
  ORGANISM  Chromohalobacter canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Chromohalobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Chromohalobacter canadensis"
                     /db_xref="taxon:141389"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55454
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigaprera qgearvaltp esakhiqklg hdcvvesgag raagfddday rdagvevidg
       61 gaalwsaadv vikvrepdee evgylrkgqt liaffwpaqn edllerckat gatvmamdmv
      121 prisraqkmd alsstaniag yravieagnh fgrfftgqvt aagkvppakv lvvgagvagl
      181 saigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgsgsggy aapsspefre
      241 kqlalfreqa pevdivitta lipgkpapkl wledmvhamk pgsvivdlaa ekggncdltv
      301 pderivtdng vvvvgytdfp srmatqasll yatnirhmlt dltpekdgvi vhdmeddvir
      361 gvtvahqgei tfpppppkvk aigqsapkek pkeptpeekk aaehaafldq tkrqigmlva
      421 ggvvmgllgl vapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgiivlga
      481 vlqigsgswl vgllasisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_097030752             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cereibacter ovatus].
ACCESSION   WP_097030752
VERSION     WP_097030752.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter ovatus
  ORGANISM  Cereibacter ovatus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cereibacter ovatus"
                     /db_xref="taxon:439529"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55382
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreif egearvamtp dsalqlqklg hhcviesgag mkagfsdeay kaagvevvas
       61 aralfdaadv vvkvrgpeta eagmlrsgqt lisffwpaqn aelldlckar gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvylefee sqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrpapkl wtedmvsamk rgsvivdlaa erggncdltv
      301 pdqkvvspng vtivgytdfp srmaaqastl yatnirhmlt dltpkkdgvl vhnmeddvir
      361 gatvthdgai tfpppppkva aiaaakprek vkeltpeekr aaehkafrkq tlsqvtmltv
      421 gtalllfvgn yappsfmahf ivfalacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 llqigsgnwl vvilaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_097043894            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pacifica].
ACCESSION   WP_097043894
VERSION     WP_097043894.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pacifica
  ORGANISM  Flagellimonas pacifica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Flagellimonas pacifica"
                     /db_xref="taxon:1247520"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111110
     Region          24..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllksfl llgaflcfgi akaqtvsgtv sdangplpga svlvkgttng tqtdfdgnyt
       61 lnnvdngsvi vfsyigfstq evnfngqasi nvtlqedaqa ldevviigyg tttikdatgs
      121 vtavtaddfn ggvisspeql iqgktagvni sqssgepgag isvnirgsns vrannnplfv
      181 vdgiplsgdn tspagdsglg atavrnplnf lnpsdiesis ilkdasatai ygsrgangvv
      241 iittktgkgs qggvfefsss lsiaspakdy dlldrdtfls gvtqfggnas avdfgantnw
      301 qdfisrraas tnnnlsysnn ygkgnvratl gyskqfgvvk ktdleritgr vnarhrffdd
      361 kltvglsati srtndetapf satagfrgdv lgavysanpt wptnpnftdg gtqilpanll
      421 qysqlqtftd rilvngsley tftpelsakv nlgydtsese aisalsgdiq nlsgiedigf
      481 gafntleken rllevtvnyk kefenskfdv lvgysfqdfq trgkntngrg fttanlnqig
      541 ddlkntvnti qgvipgsfqq fyygvntplv lanrlfptdv agdpvtfngd rpvraivadf
      601 fdntdelqsf fgrvnysiad kylftatvra dgssrfgpen qygyfpsaaf awqlaeedfv
      661 gdnvstlklr lsagvtgnqd glgygnfvar qrfsdltiqd nmevnqnglv ivatdvpdlk
      721 weptlnlnvg ldfgfgddrf sgsldvyrne ttdvllrtpp aapaidpfqf gnqdasiink
      781 gvelglsydw iqtqdvnfst sfnvaynene vldfassint geingqglsg afaqrfeagh
      841 slfsyymaif egfdsdgfpi ytdvdgngtg dpigdqtfig edalpdittg lslnlnvknw
      901 dlsayfagqf gfsvynntan gfftagsinn arnvtqnvlt sgeaggasad vstrflekgd
      961 fvrmqnatlg ynwpvsgegl lkslrlsvtg qnlflitdys gidpevtvat gdlgsgvptr
     1021 gidwaafpap rtitfginas f
//
LOCUS       WP_097044606            1093 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pacifica].
ACCESSION   WP_097044606
VERSION     WP_097044606.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pacifica
  ORGANISM  Flagellimonas pacifica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Flagellimonas pacifica"
                     /db_xref="taxon:1247520"
     Protein         1..1093
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119427
     Region          25..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlvafll afsasvmgys qtvftgkvvd ennvplpgas vvvkgssvgi atdfdgnfqv
       61 elsqsgdile vsyigylsqd fdtsgktsat ivlqpdsqkl nevvvtalni trdekslgya
      121 vekvggeevs qststnlvst lsgraagvqv vtngtgpgqs ssvvirgyss lqgnnqplfv
      181 vdgvpinnst dtrtntlgga snmnidygng aaevnpedve sisvlkgana talygsraan
      241 gaviittksg rshrgmgisv nskmtfesil kgpeyqrvyg qgknfdfqfa dgygsgtfdg
      301 vdeswgplmd gtlraqhdsp tanglrggdv hgldfvlgss gvdltrrgai tptpfvdpgd
      361 pvenfavtgr tftnnisffg gndkgnyrvs ytnldnegil pntdirrnsf alsgsydltd
      421 rltvsskiny vrtdsdnrhv ngygtesvmy lfvwwgqqvd vrglknywqd glegfqqfny
      481 nynyhdnpyf tmfentnala kdriignisa syklsddfkf mvrggrdffs eyrfikrays
      541 tqrfpngqyr edkinfqetn ldflltfnkd itddfsvnan iggnrmvqkn hfnalmankl
      601 llpgiysfnn adgplvqris rpekqinsvy gfaqlgwknq ifldltarnd wsstlpkenn
      661 syfypsasls vvlsdmlgvt nndflsfakl rggwakvgnd tdpyglnnff algtpvgdnp
      721 taapsnnlan adlkpeiqts yevgtdlrff knrlgldfty yntisknqil didlattsgk
      781 tsrtinagki knygielmld atpvstdnfs wnttfnfgln rneileladg vdkysyggng
      841 itliaekggs lgdmwgtglv kvedensqfh gevvfneglv qqdntlrklg nfnpdftlgw
      901 nntinyknfs lnflfdwrqg gellsrtrli aatsgnvvet lwgrspefgg ahpgiadsgl
      961 dyggansdgv igdgvkqlad gsytandviv panayhnnry rrgnetegmy datfiklrea
     1021 risyslpskv lerlgvqdft fsligtnlwl wakefnhgdp ellsfgggsy vpgvenatvp
     1081 ttrsigmavn lkl
//
LOCUS       WP_097046793            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pacifica].
ACCESSION   WP_097046793
VERSION     WP_097046793.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pacifica
  ORGANISM  Flagellimonas pacifica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Flagellimonas pacifica"
                     /db_xref="taxon:1247520"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118998
     Region          141..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkntlcknyf tlkidlkmki talflfvalf qlhannaysq kskismnmed atiasifdei
       61 ekntdynily knsvldfdkr itvnvdkvki dtlmdlilkd tkvsfevrrk livlveinek
      121 pvfepsprll snsprpsqqt itvtglvtdq gnvplggvsv vvkgttkgvs tnfdgeyeiq
      181 asegdilvfs yigfakheve vtqktainvt mkpdlmdlne vvvtatgirr kvemgnsian
      241 lnvsddvkqr pisnvsdllq gqaagvqiss sggstgfgsr irirgsnsas lsnepviyvd
      301 gvlinneans isfetggqsp srlndinped iesieiikgp saatlygsia angvirittk
      361 kgkqgeprws aflesgived vttypknyqa ldaqgnpgfn feaaegtfvp stvnsfqpln
      421 dsrtspfrtg qsygaglsvs ggsevltyfl sgsltdgkgv lpvnniqrmn frgnfgaqvt
      481 drlkvnfttg ytnsdlelpl ndnfalalms qglngtssid inngwgeftp delftidtrq
      541 rinrftsgle vlwqpsqkln irvaggldlt srwdsqffpt geapdflnyd egarfsnrfn
      601 dfvytldavg syktditeni nsrtslgfqf lqnlsegtfa tglqlvagsn siagaavtqs
      661 neetietrtv gvfleeqigf kdklfvtgav radrgssfga sfnsvfypkv saswliseed
      721 ffnketkygl sslrlrgawg asgvqpgtnd alrffnpiaa tldgqsvtgv sigsvgnadl
      781 speqstelef gfdakllsdk iglemtyfnk rtedalifrq lplslgvgeg rfenlgsvkn
      841 sgieiglntr ivetdkfffg ldivgsfidn elielgegiq pvifeqqrhv egyplggywd
      901 etytfndang dgfigqnevq igeisylgtp fattdisftp ilsffenqfv lkgllnfrgg
      961 qklynntgaw rngnsnnrel ndpnaslsdq aravaskflg tnagyiedas fwrlreislt
     1021 ynapgsfsdk lgfdrisltl sgqnlgvwtd ytgldpeiss egqanfttee flsqppvrsw
     1081 karlnltf
//
LOCUS       WP_097046950            1022 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pacifica].
ACCESSION   WP_097046950
VERSION     WP_097046950.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pacifica
  ORGANISM  Flagellimonas pacifica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1022)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1022)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1022)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1022
                     /organism="Flagellimonas pacifica"
                     /db_xref="taxon:1247520"
     Protein         1..1022
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112804
     Region          25..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkklfgtl vfvllsiasv qsqektitgt ildqtgtplp gvniivqgta ngtqsdfdgn
       61 yaitasigqt lvftylgqrt tqrevgaqnv invqmeedaq aleevvvtgs asgkslkels
      121 falgqvknel lenvpatsaa aalqgkvsgv sisspggqpg snvsiqlrta nslstgqdpl
      181 vivdgvileg gladintedi drieiakgaa gaslygsraa ngviqiftkr gkgnnkinvt
      241 yrselgvkei tskydlatth rfkltadgsa fdltsgsrev dddglsdnry pignifnyqd
      301 eifttgvfnt hyasisggde ktrylfsyqr lqdegiyvlv ddyrrdnfrl nldnnlsdki
      361 svktslfysn snrdaainsg ttvgilfpal itepiydwna vneedgspyn fdsntfdpni
      421 knplytlann dksekrnrvl gnvaldyrvt pwlklngsys ydfenntfqd yipkgylsdd
      481 pdgqaqnigf iqrsnfngra qntrfnalfs pfsvdsdynl alrfsylher yesefnnseg
      541 ynlavsgirs ldnitdspsv ssqaqeiltd syfviadfdy kdkyifsgva rregsslfgp
      601 ntrwanyfrt slayrvtedi qipgvqelkl rasygtagir psyemrfetf llrngsptra
      661 tignndlrpa ktgelelgln mnfldrfsfe fnyvkakted qilrvplsaa agfsaqwrna
      721 geidattyea slnaniiksd nvswdlgivw dkseqkvsql dvpayltgpg tqettlfrie
      781 egqnfgvmyg ndfitslsdl pagsnasdfv vnsagfvvdq atgetpvrra dasgneffvi
      841 gditpdfrmg inttfnyknv slyalfdwkq ggdiynktkq wlyrdgrhtd itsglpynfy
      901 qglynvnlps safvedgsfv klrelslyyt lkgeslgsva nfidtmkfgf vgrnlltftn
      961 ysgfdpeith qsesnranlt trdtdgignd pntpggdpni fkvdnfpypt tktysfsvql
     1021 tf
//
LOCUS       WP_097044751            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pacifica].
ACCESSION   WP_097044751
VERSION     WP_097044751.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pacifica
  ORGANISM  Flagellimonas pacifica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Flagellimonas pacifica"
                     /db_xref="taxon:1247520"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113241
     Region          25..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkklhyflm ivsllciqgi saqgktvsgt vtdadtgdpl pgmnvvekgt rngtstdfdg
       61 nytisvsdds ailvfsalgy tskevavggq svvnvtlgen telldevvvt algltrerks
      121 lgysvteldg davslikdsn vastlagkva gvvvskstsg vgggtrvvir gnnslngnnq
      181 plyvvdgvpi dngtnatagt gefnvpdlgn gisdinsddi esisvlkgpn aaalygsraa
      241 ngaiiittkk gstsrglgvn ytasvtfedp lvlpdyqney grgtdgnfpt inpsdalsvq
      301 lnavrgagsw gprfdgsqql ayngeqrays aqpnnvrdff rtgtslvnti alnggnenas
      361 vrfsytnsdl esmlpnsnvk rnnfnlrgfv qlsdklslda katyflqeak nrpnqgtegv
      421 maylwpmarn vsnadlqvfq ntenpidpdn pfnvigpgsl ganpywilqn dfngdkrkrf
      481 iglvkldykf tdwlsafarv gtdavtqdte aytavghhff prgrisfgkn dntetnydfl
      541 lmfnkdvsek lnitanaggn lrhstriesr tsgedfkipg ryflnntdgs litasqsdli
      601 ekrvnslygs asfgydnmvy ldltarndws salaqenrsf fyssanisil ldqilnlqgt
      661 avdmlklras iasvgndtda rqivnlftva gngylgntqi nrpnikfses lrpeditttt
      721 igaefrlfgn rlygdvsyyd istkdlifdv pvdpgtgfds frenvgeisn kgieillggt
      781 piqtdnftwd isanisknen klvdliegqe nfqfsssngg ivdvraqvge gygdiytttw
      841 lrndageliv saegrpratt erekfgnyqp dysggitntf tyknftlntl vdfrvggevf
      901 sftdsaldas gvskrslefr dggilvegvv dngdgtfspn tttisaqdyw gavsnigsey
      961 vfdqtnfrlr elsisyqfpn kllkdtfvqn aslsfigrnl ffiykkadnf dpessystsn
     1021 fgqgvlfyal ptsrslglsl nvnf
//
LOCUS       WP_097047023            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pacifica].
ACCESSION   WP_097047023
VERSION     WP_097047023.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pacifica
  ORGANISM  Flagellimonas pacifica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Flagellimonas pacifica"
                     /db_xref="taxon:1247520"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116826
     Region          25..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngllt lllafvvqis faqdktitgn vtdangfplp gvnivvegta ngtqtdfdgn
       61 yaisasqgqa llftyigqkd arrvvgaenv invqmeedaq aleevvvtal gvkkeaqslg
      121 ysiakvdgde vaeqpssdig rllqgkaagv nitasnglsg sstniiirgy tsitgsnqpl
      181 fvvdgipfgs dtnnneaffd nstessrfld ldpnniadin vlkglsatal ygnrgrngvi
      241 littknaqgg dfegkttvsv ssstffsnph lpdyqndygg gfdqefgwyf snwgprfgdt
      301 npniwtgyln eirggrvfln hpfatntvda yitgfedlaa sqyeykayqs vpaffrtgvy
      361 tsqsigingg ngttsynaty srtedksfvp gntlfknnlg vggstrlgkl mvnaslnysv
      421 tdlksppiaa srgsgvegdg aslfgdlmyt prsvdlmgip yqradggsly yretnsiqnp
      481 lwtvdnsktg qkvdrffgnv amtyelsenl nvsyrygldi ynentfygqn kggidgnalg
      541 lyrtqkirnq itdhnlsiny dkdlsesfnl klvggfnans vlferdgles tnqiaygilk
      601 hwnftnasss nsfnainfqr qtqnntfgly adaslgykdf lylngsvrnd wtstlekdnn
      661 rilypsasls fvptnaiegl rsdgnglnyl kirvgygssa gfpdvystrn tlsltgrsfv
      721 daagnvvssn ttddflgnps lkpetvseie fgidarflnn riglntsifk ketkdlitdk
      781 dldpstgytl ttinggdmei kgieadldmh liksidngfn wnanvnfyad eslvtrlpeg
      841 idqiiignff vadaknaaiv gqpfgvligd kiqrddagnr vvtastgnyv nntedvpigd
      901 pnpdwtasld ndfsfkgftl gaslgyrhgg difsktavtl lsrgiidfpf drlgtyvlpg
      961 vnedgspntt qigatdiafs nwlgqdelev wdgttirlre vrlgysvssk mlektpfssl
     1021 sfkitgsnlw ykavnfpkgv nfdtntlsng vgnnigleyf sgpsskrygf sikatf
//
LOCUS       WP_097056201             971 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salinimicrobium sediminis].
ACCESSION   WP_097056201
VERSION     WP_097056201.1
KEYWORDS    RefSeq.
SOURCE      Salinimicrobium sediminis
  ORGANISM  Salinimicrobium sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salinimicrobium.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 971)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 971)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Salinimicrobium sediminis"
                     /db_xref="taxon:1343891"
     Protein         1..971
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107787
     Region          24..970
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtlikstll llfmmpmsff aqstvsglit eadtgmpipg anvviqgttt gtttnfdgey
       61 tlegvnlddv ivvsyvgfts qeipytgqqt invelspdta vleevvlvgy gsvrrqdatg
      121 avsqvstedf negsivtagq litgkvagvn vtsgggapge gqniiirgqg slslnsspli
      181 vvdgvpidnd niggsrnvld finpndiesm svlkdassta iygsraangv ilittkkgkg
      241 mdfkfnysav ttvyeptdfv dmldadqfrt linevgsdaa idrlgesntn wqdeiyttaf
      301 gvdhnfsttg niggfmpvra slgytdqdgi lkrdnftrst asinlrpnfl dghltlelng
      361 rgmytentfa nrdaigasvd fdptqsiyde dspfggyftw lnsegvknnl sptnplalin
      421 lkddnsevrr fignakvdyd lhfmpdltat vnvgldktns hgrtrtsiem pssdldwnga
      481 ntrytneatn slfdayltyq kefsnnsina vagysyqkfe netynfdsea qedgndyefi
      541 dkwrsvllsy fgrinfnfdq rylltatlra dassklnpnd rwgyfpsvav awnihnenlf
      601 tdsstfdelk lrvgygeign vnglgdynfl tkytgsrsna tyqfgsgyfq tyrpeefnen
      661 lrwevgktfn agldyslfdy rvtgsfnayi kktedlisfv tvdpftnfsn gidknigdme
      721 nkgiefdini lpvetedfkw sigyniaynv neitnlpdqv evgginggtg nniqlhkegy
      781 spfsywvykq vyneegypie gvyvdrngdn iindsdryiy kdpyadiimg lntnlnyknl
      841 dfsvvtrani gnyaynnmas sksyeirase nsiltnlhsd yyntrflslt etnlqsdyyi
      901 qeasffkidn itlgytlpev iknstlrifg saqnvltitd ydgldpeidg gidnnfyprp
      961 rsfaiganln f
//
LOCUS       WP_097056526            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salinimicrobium sediminis].
ACCESSION   WP_097056526
VERSION     WP_097056526.1
KEYWORDS    RefSeq.
SOURCE      Salinimicrobium sediminis
  ORGANISM  Salinimicrobium sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salinimicrobium.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Salinimicrobium sediminis"
                     /db_xref="taxon:1343891"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117344
     Region          27..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lllalvvqfa faqqqmtvsg tvtdsngmpl pgvnvlvkgt tqgvqtdfdg
       61 nysievdqge vlvfsylgmk tteypvtnvd tidvvleqda aqleevvvta lgisrekrsl
      121 gyateevaga evntakegnf inslsgkvsg ldikksstlg gssniiirgy tsltgnnqpl
      181 fvvdgvpisn antntanqqt grggydygna amdinpddva svnvlkgaaa salygsraan
      241 gviiittksg qknenigvti ssgvtfskmd ddtfveyqke ygagygefye tgyfdswdvd
      301 gdgtddlvvp ftedasfggr fdpnllvfqw dalypespny lqatpwvaae ngpesifrtg
      361 vtfnnsvald ggtdkstyrl gytlydqegi lpnsrirrnt vdikathdft ekltagvtat
      421 ftntngkgry gtgysgtnif qsmrqwnqan vdfeaqrray fntgrnitwn yadaengdfs
      481 piytdnpywq lyenyqtder nrlygnfnin yeltdwlsat grvsmdyygd freerrnvgs
      541 ngvshyqryd gtykeinydf llnfdydlne dinlagilga tarrldnaqm ragttgglvi
      601 pglfalsnsq nlltppneav telhtngyfa sasfgyrdfl yldatgrvde vsslpeednt
      661 yfypsistsv vfsqlldtdw lsfgkfrany aevgnyappl svqdvyaspt nfttplysvs
      721 stannpnlkn ettkswevgl emeffqrrlg fdvaayqsns vdqlmpvtit aatgytsrwv
      781 nageienkgi elslhgspir tedfewrvna nwyknesevi slygdnknlq maslqggvti
      841 natvgqpygt iwgtnytfln gervinptng rfvvdgtpqv igdinpdwka gisnslsykd
      901 lsfsflidiq kggdifsldt wygyatgvpa ntaglnelgn plrdpvadgg glllegvnpd
      961 gspnttrtqm snyanaigyg yapnayhtyd asfvklremt lsyslpesit drismaditl
     1021 savgrnlwii dknipysdpe aglssgniqg yqsgaiptar eygfnvrlqf
//
LOCUS       WP_097070403             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodobacter maris].
ACCESSION   WP_097070403
VERSION     WP_097070403.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacter maris
  ORGANISM  Rhodobacter maris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Rhodobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhodobacter maris"
                     /db_xref="taxon:446682"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55555
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egearvaltp dsavqlqklg hecyveagag haagfedsay eaagvtvvkg
       61 aatlfdtvdf ivkvrppvda emarlkpgkt lisffypgqn kalleaakat ganvvamdmv
      121 prisraqkmd alssmanisg yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigastalg aityafdvrp evaeqiesmg aefvyldfee tqqdgaatgg yaapsspefr
      241 eaqlkkfrel apemdivitt alipgrdapi lwtkdmvaam krgsvivdla aerggncelt
      301 kkdekvvten gvtvigytdf psrmaqqssq lyatnirhmm tdltpgkdgv vvhnmeddvi
      361 rgatvayqge itfpppppkv aaiaaqkpke kpkaltpeei raaekaafrk qtrdqlimlg
      421 aggafllgig lvapasfmah fivfalscfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqvgstny lvvllsavsv flaginifgg fmvtrrmlam fqks
//
LOCUS       WP_097056566            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Salinimicrobium sediminis].
ACCESSION   WP_097056566
VERSION     WP_097056566.1
KEYWORDS    RefSeq.
SOURCE      Salinimicrobium sediminis
  ORGANISM  Salinimicrobium sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Salinimicrobium.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Salinimicrobium sediminis"
                     /db_xref="taxon:1343891"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113485
     Region          25..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkitlftf miailqfmnv qaqervisgt vttadqgmpl pgvnviiegt rtgtvtdfdg
       61 nysinaeagd vlsfssmgyq tvkrtvgaed einvameadl qaldevvvts fgieretkal
      121 gyavqelsse divqsnqqnv vsalqgqaag vqitnaggap gqssriiirg insldpnadn
      181 qplfvidgvp vdnsttesag tprglsnraa dlnpndiesl nvlkgaaata lygvraanga
      241 viittkkgks gamrinlnss vgfeeinryp dvqevygqgf sgeyeadsfw pnwgpsmeei
      301 nqidpdvrfy diwrdafrtg vqfdntlsis gggenatfyg slgnldhkgi mpfsdwgrts
      361 aklsgevkms dkfrfsgnin ytisggnrvp hdrfmermmy wapnhdvtdy inpdgtmkty
      421 gntnplydar fstfedevnr tigslnfvys pvewldvnyi igtdyysdsr teitpgplgi
      481 ageiplsstg fitetritsr dinsnlfltf nntwsekist tlrvgndife rdyeridatg
      541 enfviprfyd lsytsqisns qhkrkkrlvg lygdllvdyd dmlflnitar ndwtstlpig
      601 nnsffypsvn lsyvftenie vpdflsfgkl raswaevgkd tdpyqigqty tspsvyplng
      661 qvgftrfsrf gdpelkpert tsiefgtdlr flenrlgldf twyksnskdq iipvpvseaa
      721 gfstfvtnag eienkgvefv lrgspimted fswevsfnas ynknkvvnir egideivvgs
      781 qfgyagstvt mkliegeayg nifgssyary gadpnsifln edlpiiigan gfpvrngsql
      841 vlgnttpkwf gglrnefnyk gfdlsflvdf rtgleqysqy dnfmaafgia eytlarndtr
      901 vfegvledgs pnaqavwlgq gvgpdgrdyg agfyrntyrt vsenfvhdas fiklrnislg
      961 ynfqsnilea lpfesarisv aanniilytp wdgfdpesfs agaggnavgf tglgypgvqs
     1021 yfvtlnlsl
//
LOCUS       WP_097066763             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosovibrio sp. Nv4].
ACCESSION   WP_097066763
VERSION     WP_097066763.1
KEYWORDS    RefSeq.
SOURCE      Nitrosovibrio sp. Nv4
  ORGANISM  Nitrosovibrio sp. Nv4
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosovibrio.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosovibrio sp. Nv4"
                     /db_xref="taxon:1945880"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39221
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaeir ggetrvaatp etvkkftang lnvvliqsga gagasipdea yqaagasiva
       61 naaelygqsq ivlkvrgpes gelalmrkda vllgllsphq aegiealarh gitafsmekl
      121 prisraqsmd vlssqaniag ykavlmaanv yqkffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avieafdvrp vakeqveslg akfvevplse eekaqaetag gyaremsddy
      241 krrqgelvhq raaaadiiit talipgrpap vlikeetvqa mkpgsvivdm aveaggncpl
      301 seldkivvkh gvhligianl pglvaadssa lyarnlmnfl nlmldaksge fkvnredeii
      361 agtlvcadge iirka
//
LOCUS       WP_097077631             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter puyangensis].
ACCESSION   WP_097077631
VERSION     WP_097077631.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter puyangensis
  ORGANISM  Acinetobacter puyangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter puyangensis"
                     /db_xref="taxon:1096779"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39675
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetl tgehrvaatp etvkkltsag htvvvergag vkaayidsay eqagakitdn
       61 ayqgsqivlk vraphgdeis qleaksivva tfdpyrnpel drfasqnvsa falellprtl
      121 sraqnmdvls sqanlsgyka vllaaneyqr lfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak eqveslggkw ldvpmsaeeq qraddaakng ygwtpgeqyi
      241 qdqaaivdka vsnadivvtt allpgrnapr lihaatvakm kpgsvildma vesggnvegs
      301 kvgetvsten gvkilgvpni pstvateasa lfarnvlnfi etlfdenkvl klnqddeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_097089764             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_097089764
VERSION     WP_097089764.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38900
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletf pgetrvaatp etikkllshg hrvtvergag hsasvtdaay eaagaqlgsa
       61 adafgaevvl kviapseael lsihpgcvli gmlnpfdndn iarmaargvt afsleaaprt
      121 sraqsldvls sqaniagyra vllatqyypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpfetdee recaqgvggy arpmpaswmq
      241 rqaqavhera lqadiiitta lipgrkaptl lsaetvaqmk pgavivdlaa vqggncpltq
      301 adtvvvengv tivgpsnlaa qvaadasaly srnlldftrl ifdtqgnlni nleddivaac
      361 lmcrdgqavr kna
//
LOCUS       WP_097103057             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium/Agrobacterium group].
ACCESSION   WP_097103057
VERSION     WP_097103057.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium/Agrobacterium group
  ORGANISM  Rhizobium/Agrobacterium group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium/Agrobacterium group"
                     /db_xref="taxon:227290"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55702
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely dgearvgmtp dsaqglqklg ydciletgag kaagfsdday raagvtivds
       61 adalytgadi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qsqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvaam kpgsviidla aerggncdlt
      301 vpdqrvvsdn gvivigytdf psrmatqast lystnirhmm tdltpakdgk vvhnmeddvi
      361 rgatvtyqgd itfpppppki qaiaaqkpke rakeltpeek hakeraefka qtksqvgllv
      421 igtavlllvg lyapasfmsh fivfvlacfi gfsviwnvsh slhtplmavt naisgiviig
      481 allqigsgnw lvvilaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_097105998             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Hoeflea
            halophila].
ACCESSION   WP_097105998
VERSION     WP_097105998.1
KEYWORDS    RefSeq.
SOURCE      Hoeflea halophila
  ORGANISM  Hoeflea halophila
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Hoeflea.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Hoeflea halophila"
                     /db_xref="taxon:714899"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39388
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgatvfvake sdslesrvaa spetvkkmta lgldvivqkg ageksriada dfaaagakag
       61 taadakkadv vlrvrrpset eikslksgai vlaqmdpysn eqalaalaka gvtsfamelm
      121 pritraqsmd vlssqanlag yqaviegahv fdrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedde fkaaetsggy akemskeyqa
      241 kqaalvadhi skqdivitta lipgrpapkl isrdmlksmr lgsvavdlav erggniegsk
      301 agetvivdgv tvigilnmpg kiaasaslly aknlltfldt midkeaktvs vnmedelvka
      361 talthggavv hpafggetsk gaa
//
LOCUS       WP_097117327             209 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_097117327
VERSION     WP_097117327.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..209
                     /product="STM4504/CBY_0614 family protein"
     Region          <5..73
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 krkhidtiel afnyidtylr tyevtlglep dkaiselnni fhehslkyry engrivrlrr
       61 ikrlknicyy lyspgeygfv eydlmeaynr lmlndfacvv kechavfrsv llriherkgi
      121 vyheqdslnt lmtnlmargv isaeyahkfh flsnvlesei flpmapeksh hhyammlris
      181 eelacsiyyl tersiffltq raeedsvap
//
LOCUS       WP_097124543            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097124543
VERSION     WP_097124543.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118541
     Region          23..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkciltqlv lclfaiplla qnrtisgkvt saedgsvlpg vtilikgttq gtttnadgsf
       61 qitadkgatl qasfigfatq svklenqttv nltmkpdasq lqeivvtaqg irksqreigy
      121 aiskvetedv tvgrspqlaq alsgkvtgla vynvnnsvdp avkvvlrgyr sltgnnealv
      181 vldgmqttss vlaiinpndi esvsilkggq aatlygsagi ngaliittkk gkqgklkvsy
      241 snstnfeqis fmpqlqdkfg sgshyyqsfg tagysndylt rmaanwrsye nqqygdqfdg
      301 sirmqgrtte dggqyllpys aipnarrkaf dtgvsmnnqa sfqggdetgt fymsienqki
      361 agivpndkse rtgtrlsatr dygkltaafn agytqaaydr tsadfyndil nqpanlplsd
      421 lrdwqnnkfa npngfyndyy nnpyfnadnn rmkykdanln gnvnlnfkpt swlmiterag
      481 imnnsrtgkn ttgkflysdw aksksfipap ffreddgtgi yraitdnlga vldysstenv
      541 vnnefqvhlt kdfgpfsnkl ilgnsiyqrt tkniaigsss ivvpdvynvs nrqgelvgge
      601 attqerrfgy yadftsnykn flifngtfry datsrfykqd ratntymypy ygaavsfiat
      661 dafpnirsqf lnyakirvna nknandnipl ygldlaynng anfpygntvg ltvgnvlpdp
      721 nlkpetvyst eiggefqlln nrinidvsay tqsskgqvit vkvpnstgfs nllinvgetk
      781 nwgyeaefky liarggkfsw dasvrysynd nkvidlypgi nefqyggfsy antnvikdqr
      841 fpilktdgyq yaadgsgrvl vnattgyplr qttlsprggv lprhiaglgs kieygnfgft
      901 fnfeyrggnv mfsdlgrqmt ftgtgkwted raphiypnsa ylapdgttiv pntsvnvrea
      961 eyglwvdnyr lisenfvtpa wfiklrdvnl ayrlpqsvla ktkflsaasi slygrnlfti
     1021 vdklnyytdp efsyqgnqap gstgtpttns aigiginttg qtppvrqygv ninltf
//
LOCUS       WP_097125371            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097125371
VERSION     WP_097125371.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109086
     Region          26..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrklllfvw lffsitslvf aqeqavtgkv tdgegtpipg asvvlkgrav gtntdatgsf
       61 klnapangtl ifsfigfttq evaignrsvv nvqladgnqq ldevivtgla tsvkrsnsan
      121 avaslsakql tgvttpvttd gamqgklaga niqangsvpg ggfnvqlrgv stlgssasqp
      181 lyivdgvyid ngqyssgrse ankagagsst asqdnngnrl adlnpddies mevlkgssaa
      241 aiygtranag viiittkrgk ggrtnvsfgq dlgvsnaysy yggadwtadk ltnhfsaadv
      301 sklqaakqng tytdwerviy getgsiknth lsvtggnekt kfyvngsasn etgiikntgf
      361 trysiranid hklnnwidfg istnyvnsnn drgwtgndns ninygyslpy tkpytnlypd
      421 atgvypdnda svgenplair drainnqkvn rfiqgfnanf rlinnattsl tikvnggldy
      481 qsgfatiwlp tdlqsqrqea npgfaqdtrt evynsniqva gvlthaamgg klnltssagv
      541 vrlhrdfnyn yvrgqklpvg vsnparggvq siaaeyqrnt dvgifaqqea nyddkvigtv
      601 girfdksdln gnnfdkyyaf pkaslavnlt rfgnwaaass gaisalkpri aygataglps
      661 wgtpysqlgs tgigglsglq pstvlgnnqi kperateley gldfglfnnr itgeftlynk
      721 kvfdliqplt tapttgvtst ninaadlvnr gleltigaev irskavtwfv qpifwfnrse
      781 itrldiperl tggfgatfgq wrvkqgyspt qivgqprtlp ttdpgyassw tsygdqqpky
      841 efslnqrvtf lknfefsall hyrhkftvvs lqrvlwdegg ntsdwnstsl gltdggkapg
      901 tgeqvapngi arqnvnglda ngvpregynp siasflkmre vslyyrvpka vlgsafrnvi
      961 qgvrigvsgt nllrwtdyka gydpensnfg slalgsgvdi gsaplarrmm vhiaidl
//
LOCUS       WP_097125421            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097125421
VERSION     WP_097125421.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117921
     Region          24..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkficlsll ligafsmtaw aqdrrvigkv tsaedgsplp gvsvvlkgtt kgtstdaggi
       61 fdisvpsarg ttlvfsfvgv atqeipvgnq selnvsmasd srlltevvvt gsgvatskak
      121 lgiavesvsa kdlpqtptas idqalvgkip gaqisstsgn pgdpvnillr ginsvqggtk
      181 plimvdgvqi astdinsldl snidrvevvq gaasasiyga qgangviqvf tkkgkkgrta
      241 infstsysan eflntgnvhk aqlhpyltda snnivdtqgn ildytqygai egisyqygga
      301 tryaiqdirn vadkpynanl kyydhfkqvf qtgsttnnti nisgaseksd fniaaannht
      361 tspiltkeng sidrsnlsan vgtelfkgft lrsttqlvyt kntlkpglga sygplnggng
      421 qvgsvysfln tspffdltrk ladgtypvyp tadflsvnag npyyqatytd ainnkidvlq
      481 nfnanykvnk fleldakygi nyrnetarwt yfnqsqnass eyyqswssny apdnkgeidn
      541 fqynntfqnf lgtafirtdf qddfhsklpi qtstqisfdy rknksnrydt yglslstapp
      601 ynvaatssqa vaydivtpfi tygylvnqki dfgdyggita gfrsdwsssf gggstpftfp
      661 hfdahvaplt ffknsglnnt lpyfklraay geagiqpgaf drypvlsqrn lgtglvytvp
      721 tttqnpnlkv evskefevgt dftlggnagr swlnslsgsf tywkrssenv iytvsvppsl
      781 gstgqltnai nmssngvqfs ltlpvynsrg lkwdfttnfg hqismidais ggadiillsn
      841 agstalvlta gqpigqvygy ktltsldftn qegvkyitda nranftmvgk yvvdkttyqp
      901 qftnetyplm npnpkfnasf inglsfknyl tlnvqfdwvy gshlynqtke wmyrdgihgd
      961 fsnpitidgk tgaftayyag ayyglwgstr gagnnatkdf fvedasfvrl rnislafdla
     1021 kvvqlpyfnr aqivftgrnl ltftkytgyd peissgtsns sfdrgvdhst lpniksyqvg
     1081 lnigf
//
LOCUS       WP_097125684             966 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097125684
VERSION     WP_097125684.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 966)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 966)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 966)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..966
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..966
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107125
     Region          58..963
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhivfttki calltlstlg amaqtnpnve arssaesnqp svaaadtnrq eivpagiedr
       61 aslvnvafrt vsrkdlpggv sainlpallq knyttgaldn lsafvggfng nniwgmgeyl
      121 vlidgvprsa ttdihpteie qitvlkgvaa lalygsraak gviqittkrg vanekrinvr
      181 vntglhvpkg ypnylgsaey mtlynearqn dgltplynqe tiwnhyagtn pyrypdvnyy
      241 speylrkayn rtdaiteisg gnsrarfytn igfthsnsll kigeaqndnn trlnvrgnid
      301 vrlndnitts idasaifgnn rfahgnywtn aatlrpyrfs plipvsmiee sdqpsqlqiq
      361 nsnylidgky llggtqqhlt npfadmyaag ynkgttrqfq ftnvinvdlr kalpglsfas
      421 rigvdystsy nlafnnqyai yaptwnnyag ddlissmqkf gedrkngaqn vsnswrqqtl
      481 ffsgqfnylt kindvhnisa ilvgtghqrs etsayhatqs hvnlglqlgy nyrqkyyldf
      541 sgavlhsakl apgnrqafsp tlsagwrise epflagssiv snlkltasag ilhtdldipg
      601 yylykgifth adgtwyswrd gtltrttdsr rgenndlffa qrkeisvgvd gsffqqlisl
      661 nanffisrmn givtqaatiy pnyfvtgfpq ssfipyvnyn ndqrtgldfn lslnkqlgqv
      721 awtvgmagtv ysskatkrae nyenayqnrv gkpldaifgl qsnglfvdqn diaanatqsf
      781 gqvkpgdiky idqngdnlid srdevylgra gwngspfsfg vhatarwknl tvfaiatgnq
      841 gaysqknssy fwirgddkys aavrdrwtpe taatatyprl tslnndnnir tsdfwlyrnn
      901 rinlakvqvt ytlpgrllpa kfirdlnlya sgsdlltiak erqimemnig gapqtrffnl
      961 glnaaf
//
LOCUS       WP_097126720            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097126720
VERSION     WP_097126720.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114692
     Region          25..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklvlvfll ligalcrsea qtqlisgkvt spenegipgv nvlvkgattg tvtkadgtyq
       61 itvptnaktl vysfigyktv dipldgrttv dvklvadltn ldevvvtana ivrekkelgy
      121 avstvggsel vkardpnvln smagrvagvr isqqsgsvgg strvmirgan slsssseplf
      181 vvdgvpisns sfngsetdiv tggvdvgnra gdlnpddies mnvlkgaaas alygsrarng
      241 vivittkrgk agskkmnisv nssyrtdnvl rvpdtqsqyg pgtrgvynpr lgngwgpeis
      301 sitgpvldyt gatvqrltay pdnwknffvt gqtainslsm dgasdqgdyr igftnlnqtg
      361 tvpgsklgrn tfainagrki tdkltsrvwl nyvrttsdgr pqqgsnttni lstilaglsp
      421 tidindlknn lfapatqtvp agwtgnlara idldgiqnnp yfvtafnkfs nsvdrvyggt
      481 slsydvapwf nvtgrvgtdf fsetrrsttr rgtrgrlngq fdtneiyere lqsdligtit
      541 rrlsddwtfk givghqfnqr tirrsrvlsd glnidqlytf anaqsnvasn fysrreifga
      601 ygdfsfdyrn flflnvtgrn dwsstlpvnn nsyfypsvsg sfilteafpn lgivkrdils
      661 yaklranyan vgsdedpyql aftynpltqa sdiytfnily piggasafga tnvlpptnlr
      721 pqqqtsyefg telkffggrl gldltyyrnl nydqiisiav pqstgysarr lnvgeisntg
      781 veamltvtpl ktssgfrwda afnfnrnrnr vesladglte fvttsgdgfg ifvvarpget
      841 fniqgvgwlr dpqgnivinp ttglrtagpr rllgniypdw tmginnsfsy kgidfnflvd
      901 vrkggvinsq tvgivrsggm aaetavnnrt pfidpgvirn pdgtyrpndv pvasvqqywn
      961 qldnsvspet ntfdgsytkl revriaynlp ralvsktpfg siafgvegrn lwiihsnvph
     1021 idpeanvlgt gligeglerg sipssrsiga nlrftf
//
LOCUS       WP_097126925            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097126925
VERSION     WP_097126925.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119685
     Region          62..110
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          156..1117
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlssftgllg lvvcltlpgq satalpysip qpvhstgrtt dsmnrlltda lndlkqlygv
       61 dilygdqlvr gvmvpailid qkanlednlk vllkntglqf rkvkngayli tgqradkkls
      121 asiksvpesl pptssaeiil seaaektyav avdraingqv ldelgvglpg vsvvlkgtqr
      181 gtvtdkdgly rlsvpdgaat ltfsfvgyis qevpfanqsa invtlkpeak sleevvvvgy
      241 gtvrkkdltg aitsvtakdf nkgnftspdq liqgkvsgvq iinnsgqpgg aatvkirgns
      301 aitgtgqply vvdgvpldnr sarpglnang lgntpggnpl nflnpadias idvlkdasat
      361 aiygsraayg vviintkrgq agqakidigm ntgvasifrk invlnaeqyr eaikyygvsa
      421 andrggnadg fgsilrkgvq qnytlaisgg netgkyrisa gylnqegiin rtgfkkytan
      481 fsgnlkfles krlglditvn ssqyieniap itndagsngs ligqalqwnp tdslrkangs
      541 lnikagavin plamselysd vskvttilas ispyykftdw leyrmlysvn ysaggrrasi
      601 nqdinnsatl gkgwasisnn elstqqftht lnfnkdiapd lnlnalvgfe ymsfankgaa
      661 msalgpasgf gnygldytdy iqysnttgrv lssfvdpsad lqsyfgraiv nykdrylvta
      721 tlrsdgsskf gannkygyfp sfsaswnisn ekffqlnait slklrggwgk tgnqefpsgs
      781 sqarysftdn gglgqtnnpn pdlkwqsdkq ynfgfdlavl gnritatvdy fnktttdllf
      841 psppiqpapp gsvirwinld grienkglev aidgniikks nfswdlgvna tfiknsvsgl
      901 tapiltgaln gpglsgvtve virnglpina fftrrylgmn estglanyed agntffyvgn
      961 pnpkallgls ttlrykklsl ianmngafgm diynntnnav isvglinggr niglslyqqp
     1021 vkesianpvt pssrflergd ylkmnnatls yalgniarvi rganvyvtgq nlfvitkytg
     1081 fdpevnvnka vnsvpsvgid yaaypsarti tfgvnfsl
//
LOCUS       WP_097127043            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097127043
VERSION     WP_097127043.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113846
     Region          25..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklllgsll llllshfpam aqevvvsgrv tssddgsslp gvsvqvkgls rggttdaqgn
       61 ykvsvpangr lvfsyigyks qefpvgnrtt lnvvlqadat nlgevvvtal gierdtrsls
      121 yatqqvngdr isqrgepnvl nalqgkvsgv qitgasgeag astninirgi qsftgnnqpl
      181 fvvdgipisn svdrtnlgpn gtlggpqssn raldiapeni eslnvlkgpa aaalygsraa
      241 sgvivittks gknakkktei tvnsgltfqn vyglpnfqng fgqglnnifq snsvaswgpa
      301 ygspatleng fftrnattpt qldstalfpg galpaykays nyraypdnik nffnqgrils
      361 nsvniggasg ssnynfsvan taqdgivrns kfnrtnvsfg gntvlsntfh vgasinysnt
      421 dqsnsltgng gsafgqlvsv prsydlpnlp fqdvngrsvf agtpgsnenp iwglennrtt
      481 snvdrligni nigvdlvkgv nlfyragidt ytdrrkqifa psaarllvgg vgediyywqe
      541 lnsdliltgq kndilpglni egrlgfnvnq rksqnvtang qsltlpnfyn lsnatvfsnn
      601 tgesntlrrl agyygqasfs frnyaflelt grfdksstlp lsnntyfypa vsanvilsdi
      661 fpiksstlsy lkvrgsaatv gkdadpyqlq svyvttsrgn nvsniafpin gqnafsisnr
      721 igpgdnlkpe fttsyeggln lglfdnrfsi dltyynsvst dmivnvgmaa stgyttrttn
      781 vgkmtnkgie alltvtpirv kdfrwdvtvn ytrnvnevvd iapgvesfsi pgsaftgsvp
      841 sivkgqpygv ilgnkkptnp dgqwiinpnt glwnpevsnq nisnpnplwi gsiqntlkyk
      901 gialgvlfdt qqggqlvqfs sgsyksngtl dvtgvnrqap riipgvfeis nadgtktytp
      961 nniqvdaqsy wrafglqsdl nvfsatrysl reatlsydlp aslisktpfg gislsvvgrn
     1021 lwyfapgspi dpevntqgag nirglelqsa pntrnygvnl rftf
//
LOCUS       WP_097127040            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097127040
VERSION     WP_097127040.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112486
     Region          24..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkillgswl lsllfclpvl aqdiavsgrv tssddgstlp gvsvqvkgtt rgaitdadgn
       61 yrisvpvnar lvfsfigytg qeiavgnktt invtlvagsq sldeivvtaq gierdkrslg
      121 yatqeiggni laqrsepnll nalqgkvagv nisgssgvpg astninirgi tsfngsnqpl
      181 ivvdgiifsn dvnltqntlf gtqpsnrlad inpesiesvn vlkgpaaavl ygsrasagai
      241 vittksgrnq nnktevtvns synvqdvygi pkfqndygqg annlltptsn nswgppfvgg
      301 ptsvtnnqnq vvpyqaypnn vrdfyrqgsi lqnsvniasg datrnyiisi gntlqsgivq
      361 ntkfnrtnvs lggesklkng lkvsgtgtyv qtvsravpgg ngasafgqit riprsydlan
      421 epyqgvdgrs iyftpttnnp qwsvnnerld sqvdrffgnf qlsydvaswl nvayrvtgdt
      481 ytdrrklilp igsgrapsgq vqqdnffrne lngdllitar kdnlfmegln anlllgnnln
      541 qrktqesaad atsltlpgfy ninsgtvftg tfesstlrrl vgyygqlsln ynnylflels
      601 gradqsstlp kanntyfypg asvsfvptda fkinsdvlsy akvrasiakv grdadpyqls
      661 tvynkssygn nvanivypla pnntpgfsid trigsnnlkp efvtsyefgi nlgffknrls
      721 idatyfdsks tqqifnvavs nssgfdtrtt nvgelqnrgv elilnatpvr iggfkwdatl
      781 nytlirnkvv siapnvkssn isgnsfigia psiyegypyg vivstansrv qntdpnglyy
      841 datgqfagqy lvngstgqfa pglanavisn pqpnyiaglt ntfsykgval svlvdtrqgg
      901 qifsfnavda rqngsmyvtg idrdqprilp gviqntdgtf rpnniqlpaq tywsalggla
      961 seaavydatv yrlrevalny tlpktllgkt pfgtisvgvs grnlffyapn fpadpevntq
     1021 gagniqgldl ngppntrnfg gnirltf
//
LOCUS       WP_097127461            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097127461
VERSION     WP_097127461.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121838
     Region          33..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlsvtyprk yryyvvliic wltsvgawaq tttlsgsvrd vrtnellpgv nitvrgtnrg
       61 tvtnqdgqfs lpvkkgdvlv vslismstqe vvienqttld vkltesaksl devvvvgygq
      121 qsrktltgav stidqtvfks vprtnvgtal qgtapglrvq qttgqpgatp tivfrggtdf
      181 ngsgsplvvl dgvivpslfg inmedvesid llkdaasaai ygarasngvi lvttkkgkkg
      241 rtsvtysfkr annyirrnpl eymsasdyil wnrrgiasry aaaqadnnta emnnarnqlt
      301 gawgwgvnsg wtapdgkyst qlvsnsnrnl ltdpqyslli dknpfnanqt dsllyrstsq
      361 rqledlilqq gvlnehylnv sggndqgnfa lgvgsirdag tligsslsrm nmnfngglnv
      421 gknlvvslnm sgysakttps fisadasggl qggvvqrfag iaptvrltnd qtgailpgvd
      481 avwlgnpayf kdkffnqtle qryagglnle ytilpglkal asasgfyryt taesftkayv
      541 ngtggalvnt rnasftnqra sqytynaflq ynkdfgkhtv salaggeffe srvydygata
      601 nlaatdfipw lsastaavgv ptssfsswqr lasvigrvny tfantyllnv nlrydgtskl
      661 itnqygffpg vslgwnmhya dffansflrr yvstlkpris fgengsinpl nsagqpligd
      721 yatipqygsv gtysgqpgfa asgitntnlk werantlnfg vdvgllnnrv tviadyfvrn
      781 vydkitslti pgwtgfssyv tnlgqlqnrg ielevranvl kptsadgvsw tvsanlfhvk
      841 nfakklpnng ldlnrqgavq ifdpaqnklv wvgglqegkr vgldeiyapi ydgiytsqaq
      901 lderanllnt ylpytnkrik llgdarwrdt dkndtldyrd nvfvgrttpt iqggfssnls
      961 wkgfnlygqf dyslgfvivn qsylrgmsqv qgsqngpvdi tktwspenpt gtlpryywan
     1021 ygrnyftdag gnttapanfw qkgdylamre vtlsydmpak llervarnrv kslrvfltgs
     1081 nlvyitgyng tfpevggndv grfplprtat lgatisl
//
LOCUS       WP_097127574            1200 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097127574
VERSION     WP_097127574.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1200)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1200)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1200)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1200
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1200
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131802
     Region          126..1199
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhftqslsr avvlllvgvs isvcafaqqs rvpladaldq iakkykakfa yehgivqgkt
       61 anrseasnak nleealkavl ypnnllflyv sernytivtr dtktdvtvti ergvtpaddr
      121 anetfitgkv vdesggpmpg atiktnssnq tyitnsngdf smfvtpntte vsvfyigyep
      181 sfqkinpntk nlrmvlkpss nqleevsvvs tgyqkisker atgsatvvta keiekvpvpn
      241 llyrletmvp gvkitlnsgd nsfvygntms singgtrtrg tsdynmsirg rsslpgpqsa
      301 esfplividg aisendisti npddvesvtf lkdaaaasiw gvragngvmv intkrgknnq
      361 vpainfsmna avsnhpnlkd lplmnaaqti afeqeivnkn litapsnatp lgqpvaavtd
      421 ltfklragti tqsdynaaia rystmdnraq vedyllqrsn nqvynfsisg gnnysnyfys
      481 asyanekpya vgnsgkrltv tlnntfklfk vatlstnvkg aflnyknngm alnalyapsa
      541 ttfmpydqlv ddngnrvsys rryysgwlnt lypkgflnwg ynaldeiena dntqkdnnys
      601 vnlnlsvpif kgltanayya nefgfsnarr yyneqsffyr dfvngytpnp ttgtavnsig
      661 lskgagilnt qnttsnnytv rgqlnydntf gtdhqvtaia gseiretnag qstgtlygyn
      721 mgtggsrpvd fftpyatvtg fssslggsyp tlqnkkrrfl syysnaayty kskytlsgsv
      781 ryddynnfgl drsfratply sfgakwdahk esflkniswi snlslratyg vngnistqlf
      841 pftwisvspa dlitglpnas iiapanpelr wektyvrnla ldfgflnnri sgsvdvyhkd
      901 gkdlyynfpi ngtygvttlt rnsttmtgkg vdlalsgvly ttkdwevssr inyayntnnv
      961 ndtrfivtsg fyanpaygsv lagypsdkmf vyrnagldaa gltlvydekg nkvsanqnvt
     1021 niaalkyagr sapshfgsfv qsvrykdftf taiasyqfgs vflkptassy sssrlgvryd
     1081 lhedvakrwq kagdeattnv pgmagtfapt sllryqqsdi nvlkgdyvrl relslsyrip
     1141 tqkitdkikg atfgfnvrnl gliwtankeg ldpdvlpnls sntlglpatv synfslnlnf
//
LOCUS       WP_097127648            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097127648
VERSION     WP_097127648.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116149
     Region          24..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msrililsfl lvssiwstaw aqerrvvgkv tsaedgsalp gvsvvikgst kgtttdasgi
       61 ydltvpggkg iilvysfvgv ttqevklgse sqvnvslvsd srqlsevvvt gvgiatsktk
      121 lgiavesvsa kdlpaaptas idqalvgkia gaqivsangt pgskanillr gintinrgts
      181 pivlmdgvqv gstdinsldl stierveviq gaaagtlyga qgangviqlf skrgkdgpaq
      241 isfsnsyasn syinkggvaq adkhafvtda snnvigvsgk slafdqatst wsenvqynal
      301 dvnsqaskpy dqnlkfydyy kmffrpseti nnslnisggs gkadysitas nsyqstilkn
      361 ngafnrsnlv snigmtlakn ltlrsvsqlv ytkntintnd ravwydinnt rpfnnydytd
      421 pdgnyaayfg sasgvngynp nyrlqyrnhv dnkvdviqsv eldykpikyl dlnaryglny
      481 tqegerytyg nqtlnrniva ngagyattln asdakgeist ydyktvfqnf lasafiktdf
      541 qedfklnipi rtstqisfdy rknnykefdt yalgvptynp ytaaqastyr vsldnstpfv
      601 tygylinqhi eygellgvta gfrsdyssaf grgstpftfp hadgyvrpss ltfwqnsalg
      661 tyvpefklra aygqagiqpr pfdryvtlgt rtfgannvfy ntvtqsnpdl gvevskelel
      721 gtdftvkgsn gdwlrklnfs fsywdrstdn aiynvnsaps tgigtvkdna fslsskgtqf
      781 slnatvyrgr sftwnfttnf ghqssqidav kgnqqivvts sagstnyvlk agqkigqlfg
      841 flaihsldqv lpdgnpaiae sakgnyevas ngyvvnkttk qplfssaqys fgdpnptfvs
      901 sfindisfrd ivtlnfqfdw tqgshiynqt kewmyrdgih kdytnpitin gqtgawtafy
      961 rgvyqagann gtkdyfyeda sfvrlrnial gveltklikl pmrrlqvvfs grnvltftky
     1021 tgfdpevssg qttgnessaw drgtdhnttp nnrsyqvsln fgf
//
LOCUS       WP_097127641            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097127641
VERSION     WP_097127641.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118516
     Region          24..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkillmsll lvcsfwlpaw aqertitgkv taaedgtplp gvsvvlkgla rgtntdangs
       61 yslnapakgg tlvfsfvgsa tqeieignrs vidvklanda kqlgevvvta lgqqrdkkal
      121 ayavsnvkgd vlqqrsepdp lralsgkvpg vnitagngap gagtritirg nnsftgnnqp
      181 lfvvdgipfd nsvntpqngs qgynqntvtt nraydidpnn ieamtvlkga aasalygsra
      241 angvivittk sgsksarkgl einfnssysv envstvpdyq dtytqgsnqt ynggfignwg
      301 tvfpsevdri naglgferys kvvdpdypag tiphplvdat vpygaarfqt afpellqang
      361 rgiavplqpy diiggffktg kvmengiqin stgdktslna svsrtknegi ipnsftdrtt
      421 lsfggnatls ntinvagsva ytntnqqspq sgagyyadyg glasagsiys rlfylprnyd
      481 lngypfenpv dgsnvfyral dnplwtakyn lynsavnriy gnmtlsydit pwlnftargg
      541 intysetrkn vlrpggsfap lgsvsrqdlt ktevdftfla taqhdfseki nakllvgfnp
      601 nqrtytesai agapvidpni ltiggtlnqn aadyrnqrrl ygifseltvg ygnflfltas
      661 vrndqsstlp asnnsyyypa vsgsfvftdv lnlpkniinl gklranyakv gkdadpyqvf
      721 taynlgrtfy ngtaistatl psqlnnlnlk peftsevelg telqffnnri gidaayfdrv
      781 stdlivtrel prtsgfanei tnagkisnkg wevgltlvpl rmangltwts yfaytsiksk
      841 vedagpggei figgtgltsl gtifrnglpy gqiigsknar desgnllinp stglpiraaq
      901 ssiigdpntk fqvgwtntvn fknfslsvll dykaggslfs staaslllrg qlknsedreg
      961 mrvipgvlgd patykplvgd ngqpikntia mtafqyhftd gygaygadev niydatvvrl
     1021 reislgysvp kdflkryakv lgslrlsvsg rnlwfyapnm lkglnfdpev lsnfadsniq
     1081 gfdlgaspst rrfginlnas f
//
LOCUS       WP_097127959             944 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097127959
VERSION     WP_097127959.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..944
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103962
     Region          72..942
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msvfirtlrv ftccvlllly hastlhaqqv vdttskkqdt lqlidkklkk liffntptnl
       61 stsssasisg seltstlvas ypialagrlt glttsqnngq pfnegyalrl rgqsplifid
      121 giprsvseig ieeiesitvl kdavslamlg vrgangaisv itkkgissgq kisftsqfgi
      181 qqpiqnlvsk qldafnyanl ynealvndgl svanngfsqt ainayqtgsd plrypnvnwt
      241 devlrkssav aryslntsgg ndfvrffvnl ehftqdgllk trddintkys tnanfvgyfi
      301 rsnvdvkltd nlsaglyvqg riltdnspgn sgtesifnsl ratpnsaypv fnangtyggs
      361 pqfqnnivaq gvsagysstn trtvlsdfyl kynlddltkg lwvkarasff snlsenyirt
      421 kgyavfeqig gfgtntpvyr qynnntdqtn tnnigfqnrs dfqelslgyq rdfgahgiea
      481 vvlanrdnli sgsnlpytiq gisghvsyny nkkylaevsf sqnganrypn nggfrygffp
      541 alglgwnihe edflkgnkll sllklygsyg kvgrdngayy tyqqvyngap aaifgssagv
      601 vttigesfla npavtwehak mlnvgidaaf ldnrlglnie yyrnnyadls ivrgsnntll
      661 gisypaenig kqnyygwetq lnwterkkdw gysvrlnasl qnskliynae aaqrhswmqr
      721 tghpvgqsyg yiaeglfrsq qeitgaatie gytpqpgdir yrdlnndgii nqydqttigs
      781 qkpslflgar fgfniggldv salfqgvinq evylsgnsyw efqggtaqay qnhlnrwtpa
      841 taataeyprl ttnsgprnga vnnfvassfw lrngdflklr nvelgytlpt nltqkigvks
      901 trlfanglnl wtlssktfng adpenfngsy piervfslgl niql
//
LOCUS       WP_097127792            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097127792
VERSION     WP_097127792.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123934
     Region          40..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpfstfqli lrqtltiall mgvcalhtla vgsatgkppr titgsvtlgt nnqsvagvni
       61 lvkgtqlgtv tdqrgnyait vstdnavlvy sfigyktqei tvgnrsvidv alvennevlg
      121 evvvtalgik rearslgyav gevqgkdlsr vaqenvlnsl agrvpgvqis stgpsgssvs
      181 miirgaksln tdnqplfvvd gvpvanslnn vsqigndnrv dygnaisdin pddvenisil
      241 kgpsaaalyg sraangvvli ttksgsksqk mtvsvssntv fdqpyrylkm gsqfatgilp
      301 ftpennpypg gilqidessa ggvgpeldkg ynaiqwnspt gpdgkkiptp lvshpnnird
      361 fvrtgitstn gvsiannsek vtyrlsysnm nsrgivpnsd lfkntlaint svrvndkltl
      421 stnldfsrsn snnrpagerg tnplqwaygv gshidinelr dywvpgkegl qqksqsigny
      481 nnpyflayev nnsfvrdrvf gnlkaewqlt peiklmgrya ldtyseqret kiaksytgep
      541 ngayglinlk ryernadfla tytkrfnals vvvsaggnnr ysqssdlsts srngaglvip
      601 glytiqniap nnlqynnyly kkaiysvygm anlgfkdmiy ldltarndws stlpvdnrsy
      661 fypsaslsvl lnemihmpns vdlfklrggi aqvgndanpy slfatlgdag awngvtrlsk
      721 sggillpnlk peiatsyevg idynmfrnrl rfsgtyytse nrnqilpsqi apssgfttks
      781 inagllesrg velslggtlv ekgglrwdlt tnytknttri kelaesipyy tlwtdakgga
      841 wtyvgdkvgd iydaeiitvt dknspyfgyp ildndgswqs rsastsknki gnfnpnfilg
      901 aqsslsykgf tlnlsldwrs ggdfvsqtyr ymesdlrsqr fldnlinpgg rtgdalrnwl
      961 venadqyiki qgnnfpivgg ptsayggypf efggktyayg vfnpgvlaqy ddkgniigyt
     1021 enlggadtki ipygdnypws ftraatfdas fvklreislg ydlpakfvks iglqnasfsv
     1081 ysrniilwta akinvdpema fqpqsspqag tqfkqgiery nvtpwvipvg fklgltf
//
LOCUS       WP_097127981            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097127981
VERSION     WP_097127981.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113853
     Region          25..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meklvrmclv ltfllcssla maqqieisgt vttdgegtal pgvnvsvkgt tvgtltneng
       61 qysiratpgn silvfsyigy esqevpvgsr tsisvalkad nkmlnevvvt algisrdkka
      121 lgyatqsvna eqivqnrqtn lvnalqgkva gvtisstgga pgqgarilir ginsidasrd
      181 nqplfvvdgv lfdnststgt snsgaefrgl snraadinpd dvetinilkg gaatalyglr
      241 gangvvvitt ksgkagalra nysgtygfen vnkypevqdk ytigysgvyn pqdffpswgp
      301 tvaeaikidp thpqklynhf rdafytgkqf qnnlsfsggn dkitylssig hvtqdgvipf
      361 tnynklsvrl ntnvkfsdkf stsanlnfin sggdrynadr yneslsywsp rydvrdylna
      421 dgsyktygng npiygamtnk lrdnvnrlvg glnftynpls wltlnyragl dtysedrkrt
      481 apgpagiane rifednglgf vyqyntsfra itstfaasan tklgsdinat lrvghdlydr
      541 rirgfgaegt eltvynyfdl rnaktivptq saedyrlmgi fgeltmdykd ylfltltgrn
      601 ditsslmapn nsffypsvsl gylfsqqfql pqfislgklr asyakigkda spystvtgys
      661 sytqlpsgtt gftrgsllgd ptlrpeftdt fegglemnfl nnrfgldfty ynsiskdqii
      721 rvdvtsstgy vnaainsgsm rnrgielilr atpvrtgkfn wdvnfnfsan rnkilsireg
      781 lteinyasqs gyanstvtmk lvpgyaygnl ygrsykryfa npteetveld rsrpvvigan
      841 gfpvinttqk llgnsqpkwi ggitntlryg dfsltalfda rvgqyrynql gnffsafgia
      901 kytedrndtk vfegvladgt pntkavwlgq gkgpdgvdyg ngfyrnvhrg ssenfiedgs
      961 wvrlrsvgls yslpttllkk sfvknarlgv tgnnvwlwtk ftgydpetss tnsgsnvdgf
     1021 tgftypavrs flftlnvgf
//
LOCUS       WP_097128088            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097128088
VERSION     WP_097128088.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115678
     Region          21..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkerlfallf llpflsfaqq rvvrgkvsda ngkeslpgtt vtvkggtagt vtdaqgtyql
       61 tipdksatlv fssvgfqlqe vavgnqqvid valiadtkql sevvvtaagi krdknalgys
      121 vstldankla qrsepdplra ltgkvagvnv qgsggaagga tnitirgnss lgnnnqplfv
      181 vdgvpfdnss fggtdgtvgg stvtnrafdl dpnniltmtv lkgaaaaaly gsraangaii
      241 vttkagksts rkgleityst gystetvagl pdyqtkygqg tnfdyrsgvf gswgppyagy
      301 tsliptrati phplttnnry pstvfpqfyq adgttpiqvp yqsysqgnak nffrtgnvfe
      361 nalsvstggs kgnftvglsr tgnqgvvpen qitrtgvnig gnaqldnkfy vsgalnyvnt
      421 eqvspqvtaa ngsgssimdi lmfvptsfdl tgypntnpln gnnvydrvgt dnpywsvkns
      481 pttskvdryy gnvvigvdpl pwlnvqntvg fnaytdrrvv vngkggdyfp ngnitndniy
      541 rqeldntllv tatkplseni glkvilgnnv nqrvterqvv fgdgiifrgi nslnntsvti
      601 prvlpnnrnn fkqryfafft disldyknfa flnlvarndv sstlpasnrs ylyggasasl
      661 iftealkipk nvlsfgklra gytrvgneat pyqtqtvyia npvlgvgsgt gsisspfsgq
      721 stlsesdlla nselkpefit elevgtelqf fnnrigldit yynkistsqi ftvnatpssg
      781 ytqrvinlgr ssnegieigl tatpvklkng fswdissaft mnrnivldig alkelpyggf
      841 sdlgsvhiag qpygqirgst yardevgnil vnpntgkpil sgktaaignp npdfilgvtn
      901 tfsykgltls alfdwkkggd mysftayell srgatrdtee reailvgpgv lgdvntlkpl
      961 ldgegkkipn nigiavadyy ftggfgpgga getnifdatv frlrevslgy qfpkkwlakt
     1021 pfggaflsvs grnlwylapn fpkylnfdpe vsslgagnsq gfdfigiptt rrlgvnlrfs
     1081 f
//
LOCUS       WP_097128094            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097128094
VERSION     WP_097128094.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115453
     Region          45..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkngkanrf lkgralpkyv vifsvflill sysslaqnnp linskltgkv idartkepla
       61 gavvqiegvt nqtqtdadgq fnlvtgqsfp ynlivsylgy ekqkvtvngs pitvelkeia
      121 nelsgvvvtg yntqkkqdft gsaarvsakq ianrpaqsfd qliggqaagv nivqpsgvln
      181 aapvfrirgi nsissgiypl ividgvpsft gqqggnvgnn plsnlnpgdi esidvlkdas
      241 ataiygsraa ngvvvvttkk grsgktkvny dawvnvstpa nlpelldasq yvaikneamv
      301 nagrqpgfal qtrsdgstvn tdwydvayhn gvsqnhnvsf sgateatnyf islaygkqng
      361 ilrtndqdqk tarinlehkl fnnitlgthi gynntlgrgp atgslpgqyi gtdalsrmty
      421 vlppnvavyn edgsyniqdk qrvgyganna naasagyvgn inaynlqlil dldkyssesn
      481 sllgdvyaew eilkglkfkt tyglnklfie nlsfqngihg dagpanggat ntnrrlnrsd
      541 wvntlsynrt flekhnlnal vgyeeivttv dswgaqrlgl sdpfftsyqg gfttitpsgn
      601 sqsrngfisy fanlnysfas kyllsysfrr dgysglpkdn rfgnfnggsv gwvvseedff
      661 knsplasvfd rfkikasyge vgninigdfp slglfsaaty ngiptlgfsq agnsqlqwet
      721 skksnvgvvl sflkerltfe adyynnkvdg lildakqaps kgipgniisa nvgslynkgf
      781 elaltaaiiq kddfkwnanf nistvknrvt alsngadiys psnfgiqnmt regysigaiw
      841 avptngvnsa ngnrifinrd grevqynhia tnkwtyldgt vapaidnyld griqgsslpt
      901 yygglnnnfs ykrfdldfgi ifsggnklyn gtkanlldqr yfnngtfvld rwttagqvtd
      961 ipklyfsdnv stgfsitnsa mvedgsflkl knlalgyrip aqtlfngkis slriyaqatn
     1021 lftitkytgs dpeisingns iasgkdhnav vnartfalgl nlqf
//
LOCUS       WP_097128129            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097128129
VERSION     WP_097128129.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109017
     Region          24..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkhilycim mvlvaagplw aqdrqlsgtv rddrgqglpg vnvqlkgstr gtttaadgtf
       61 rlgvsgsgtl vfssigftsq estfsagtsq vtiqlvtddr llnevvvtal gieksaktlt
      121 yaaqqidgak ltqvrdanfv ntlsgkiagl qvvqgaggvg saarvtlrgn rslngtnnal
      181 ivvdgvvfdn snggqvssdf ggyngsdgaa ninpddiesv nvlkgaagsv lygsraangv
      241 miittkrgka grisvdvnsg vvsespmllp efqntytqga ggksnttasg swgaagktyp
      301 nnvrdffrng vstnnsigvs ggtekmqtyf sythnynqgl ipnnnltrht fnlrvsnqis
      361 krfstegkit yvlqdignki kvgeesgivm niykiprsvd lesiktyett dgvptywtss
      421 siymnpywti nrtinsekrn ritllgqany kltdwltltg risvdkyfdr nlrsfynrtl
      481 lfagnggtys afdtenleqn idlfaqgnnq itkdikvnyt vgaqlskrfn qtigatangl
      541 qipnkfdlgf aralqpisgl sqrqvngafa satfslrdyl ildltarndw sstlpaphsy
      601 fypsvgvtai lsdmmklpdv isfakvraay trvgndaspy llqqtysfaq ggtngfiqrd
      661 atqaipdlkp eltnslelgl dwrfvqnrfg idltyyktnt inqlltlgla pasgfsaqyv
      721 nsgnienhgi emaltgkils graltwdmtl nfsrnvnkii slhpdikkaa laggfgrtss
      781 pvvaeggsyg dietqrwstd aqgryivdan gkpvvttgqv avgnfnpkfm mgfqnsfsyk
      841 gftlgvlfdg rfggvitsgs eanlafdgna ayttafregg wvlpgvtaag etntkainae
      901 tfwttvsggr yswgefftyd atnvrmrelt lgynfnlpgn ffvkrarlta varnlfflyr
      961 gkaildlpgv ptrqlsfdpd islgagnfqg veygnvpasr svgvnlqlsf
//
LOCUS       WP_097128152            1143 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097128152
VERSION     WP_097128152.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1143
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124692
     Region          49..117
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          137..1139
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskrvlyqkt lqkimrigiy qaflsvafat fsyavevsgq kvleqkvtlq lsnadvekvl
       61 dkletvtnvk fmynpqifgn dakatykfrn eplsdvlnki lypyqvtyev lqdriilrri
      121 essselrtpv qpeapkrkva givldengag lpgvsvvike aqkgtttgad grfsldipde
      181 navlvfsfvg ykrqevtvgn qsnlsvtlap eastlgevvv talgiarekk alayavsevk
      241 gseltqaren nvanaltgki agvnatgmat gpggssriii rgngslngnn qplyvingmp
      301 mdnstpggtt adgngmnvdr gdgigginpd diesisvlkg gpaaalygar asngvilitt
      361 kkgraqkgvg veinsnttfe diavipnwqy eygqgldgrk pttvteakst grlsygarmd
      421 glptiqvdgq lhpyspqknn lknfyrtgan yinslaftgg netvnfrlgl nntqsnsivp
      481 nssftrrian lnlnaflgkk lsvetvfqyn veegtnrpkv gyadfnphwa tylianvvdi
      541 rslapgydpv tgkemewnpv paapnpyfvi nkfknndtkh rfisqgsiry dildnlfikg
      601 svsqdfysfs seyvqptnna yqplgtyear ktsssetngm ltlnynttff kdltfsalag
      661 mnaqrsifdq ttiagseftv pyfysytnla tstttptylk sainsvfgsa dfgyknvayl
      721 tlsgrqdwfs vlnpksnsif ypsvggsfil sdafqlpkav sfaklraswa qvggatvnay
      781 qiyqyysmqq gghngrpvqv lsssqvpnpd lkpltsttye ggieakflnn rlgidltlyn
      841 rkttddivtt nialssgyts allnvgalsn kgvellltgt pvskgpfswd vsynmaynks
      901 kieqlatgit gidvgagvgg glvrnvldrp ygtvwgynkk tdangnvvfn tasgyavrgd
      961 lqeigqgtpp ltmgitnnfr yrnfslnilv dgkfgsivys nlyqyayrfg lpqetlpgre
     1021 tgvtvtgvtp egapytkkws keevdtyydn dknytamfmf nndfvklrqv ilsynlpvak
     1081 lpflklqsat isfvarnlai lykdkknqyf dpesgytstn aqgleafgvp rtrslgvnlm
     1141 vkf
//
LOCUS       WP_097128170            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097128170
VERSION     WP_097128170.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113943
     Region          25..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkaliflcc lllscglaya qtnritgkvt gtdkqplpgv nvlvsgtsig tatdasgnya
       61 inapanasli fsyisyvsqt ipvnnrsvvn velaedakai devvvtalgi kreaktlgya
      121 tatvnaeqin vnrtpnfmsg lqgkmagvni tsmgtgpagt akirirgqss fsgqnnpliv
      181 vngvpidnsn falggdfgnr asnssdggdg lssinpddie emtvlkgata aalygsrakd
      241 gvvmittksk gsgkgfgvty ntnfttdtpl dftdfqyeyg qgeggrrptt anptsgvwsf
      301 gekfqpgmtq tlfdnetwpy epvrnrvrqf yrvgtnftnt vtvsnsgqng gfslsfgntd
      361 nkgimenntf nrkvinlgft qnitskltal gninyslenn vnppqlntqd lsvstviftl
      421 ansmpfqalr enqtlpngde fvfsrflvrn npyysmsrkf envnrsrlfg nvalkyqfad
      481 wlyvqarlaq dfyvrnqeyn ipngyapiar apvgfvngsy tqdvrqnter nldlilgmnk
      541 tfgsigvdvt lggnhryarn dynsvtvqdf vqpglytvmn grikdplysl aekkinsvfg
      601 aatvsykdfl flsatarndw fstlapsnrs ilypsvtssf vfsqafdnmp awlsfgklra
      661 ayaqvgsdnv dpysnalyfs vdnnsfpnps galvpvggin atvvpnknlr plriqeaevg
      721 lelklfanki gldftyyhkt tddqilaaqv sdassytskl invgrsmnkg lemlltfspv
      781 rtpafrwdvs anvsyntskv lklglspndt vitvssgggr tlnqvvgkpi gqlytftylr
      841 daqgrqvfda nsgmplrnnt lknvgnalpn yfggitntft yrgivlsali dfklghklia
      901 grninymrhg lskrtlpgrd vgyvigngvn pngeinqtra avqpfyesin plginedfvf
      961 nagfwklrqi slgydfdkil pqrfflkglr lnavannvli ikkwtenmdp eevlvssdna
     1021 vgldfwpglp ptrsigfnln arf
//
LOCUS       WP_097128211            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097128211
VERSION     WP_097128211.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121253
     Region          33..102
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          115..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkllsklst fflvlvcfyf pswananslq kidlnaqnks lktiieslek qsnyyfiydn
       61 ellnsnknls vnfdnltfee tvkllsskin vnykivdktv tlysknssvp qqevtitgfv
      121 klknkdnnip fpvngvsvlv kgtnrgtttd fkgqfslkis gpvtlvisyl gyekkemavn
      181 aatkidlvlq elegtlnevv vsaygikesk enqigsaytv takdlekrpa lridallegl
      241 vpglefniqd qnngsarprf strvrgessa pygvmsnepl wildgipvnt ggttnsiagp
      301 etsispltyi npediesitv lkdasataiy gssgsngvil vrtkkgngtp ivkytyrtti
      361 dqiasyntfn vlngdqyrrv vnemglgdki agygdvstnw ldtyyeqgkv nthnlslsgs
      421 nestnyyisg sfydqqltsl tnetkryslr sqintdvskr lsfnfvfggs fnvndmwsvg
      481 snyytelpvv spynpdgsya lydylenrlf pslaeayqne ngqstlqafs qiqatfrilp
      541 gldfttrsgv dfssinelry sslqnltgkq fngylyknqa rmynwtsnat lnytkqlydg
      601 tlsallgfea nnsnssfira safnfpndyv relsmaiaen trssgntnet aslsnfgrls
      661 ylwkdkynvs vsfrrdgdsd fgedvkwatf yalgaawtvs neefwknnvp kdinflkfkl
      721 sygtagngrf ngnyakglyt fsegngyggv vgaimsrgrn tglkwettyk fntgidfglf
      781 nrinvgleyy rdithdlisd atvslttgqr siyrnsgklq nsgfeatiss tnierggftw
      841 stnfnlalnr nkvlslptdi gqsnltsimq vggdsralyl vrwagvdpst gdpmwydang
      901 nitkvydlnn rvvmgrvtpn fyggitnsfn ykgfnlsfll lysqggssls ellntaghdg
      961 lnilstnlst dlldhwrypg dlsvnprltq vstssnrnst rylidrsniq lknisleyrl
     1021 pddfvkkgfl kraavyimad nvamwtpyrt skrnnlgngq yetiklntya nsfrgapgqa
     1081 sysagvnltf
//
LOCUS       WP_097128506            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097128506
VERSION     WP_097128506.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119018
     Region          69..1095
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnktttqkag vllhvsecen ilqsqlsvig ilkklflrnv svmtflfvai fqflllqnat
       61 aqnasqnvti kgtvlddgdn ngvpgvsiid nnrkmlgltd akgdftisia kgttvsfsmi
      121 gyaaisktft dgqtgvnirl ksstnelntv vvtalgikrd qkalgyattt vdgeqltnai
      181 annwtsalsg kvaglnliks gggpagsnki ilrgenslag esealividg vitsgssgrr
      241 stgsgsgayl sgdsptdfgn sladinpddi esvsvlkgpa atalygsrgg ngaviittks
      301 gkvnqkgigv sfnsnssfet isrwpdyqne ygqgatgqdl yysylatadg astrstssaw
      361 gpkfdgqsyf qydpvtktts atrlpwvayp nnhkdffqta ntfinsvald ggtdkttarl
      421 svtnlqnrwi ipntgmtrnt islsvssklt nklqiaskvn ytnkysdnlp stgynnqsim
      481 yfirgltpnm nmdwfkeywm pgqegimqnr pfsslldnpy lianemlnks nrnnvvgnvs
      541 atynflknls lmvrtsvdls yegrsqqrpf ntnkyangmy rtqnifsqei nsdfllrynd
      601 kvgskfdytv tlggsrmknr ytvdelradq llypgifsfa nskntlitlp nrqnyavnsf
      661 yalgtasydn flfldltarn dwastlatpt gtdnvsffyp saslsavlsd kikfpkqisy
      721 lklrasvagv gsgstkpyqt ayaytptgfp gslvnptvia ntelrplkts svelgldlkl
      781 fknrlgidfa vyqnntkdqi ipsridassg yssvilnige vrnkglevql nasplksksg
      841 lninlfgtfa tnrnkvisls dsvgslvlss gprgtiearv ggamgdiygl gyerspdgqi
      901 vykdgipvlg qttqylgnst aryksslgtt isykrfslnl lfdaqfggka yslthavlae
      961 egklqktvpg ryngivgngv mlkdgvyvpn tivatniqay ynghfnrdnv esnlfstdfi
     1021 kfrearldya ltpkftsklg lqkatigiyg rdllmftdwp afdpefgtig adgdisagfe
     1081 saqfpstrtf ginltiaf
//
LOCUS       WP_097128705            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097128705
VERSION     WP_097128705.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119159
     Region          40..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknrlfnlm lmvllaivfn afcvkdaaak nhrltaqqqf svvgtvtddn nfktagatil
       61 nkktkqavvs nvdggysvra sngdtiqvrm tgyatqtfva rdtrkrvdis lrediqmlka
      121 vevrtaldir rgekelgysv tqvsgddink aketnimnsl sgkvaglvin sgaggpagss
      181 rvvirgatsi tgnnqplyvi dgipmdnsny gqvgsdqfgg gvdmgdaisa inpddvetit
      241 vlkgpaatal ygslagngvi littkkgtnn kelgidfnst ntietqltry ddvqylygqg
      301 rsqlipsdqa qafnslfvnf garldpnvty vgfdgvtrpy alvedniqnf frtgssfnnt
      361 valsssteks sfrfsaadlr yqdivpksdi rrntytftgr skfgnkltfd vratylnedv
      421 nnraglgdsp snigmnfngl annidqalfa tnyknaqgdy ldwgggqyrl npywvinemy
      481 nkthkdrftg alnatyqftk afslnakaat ditfldyesy rprttpgalg gqldqvnqry
      541 ttnqvevlas ytkqvskdfn vsarlggsin drirkgtnss fsnmivldai satsyldkvv
      601 ipndiprqir svyglatvgy knylfldmsv rrdqsstlpe snnsytypsa alsfvftdaf
      661 kiksdilsfg klrfnvaevg sdtdpflldr yytlnqltfn gslngkissr vippldlkpt
      721 rtrsyeigtn mkffknkinf datyynsdsr dqinivpapi ssgypqqlin agvisnqgie
      781 llisgsplss kskvkwdmsv nfarnvskik slsdrvgdhl slsearwagl rvvarpgeqy
      841 gtlmgydflr dpngnvvlna tnllpiidpn mkvlgkgvfd wtggftsrvs yknfsvnaai
      901 dvkygadlfs mtnlfmharg salatlegra ewilseeqrl gekktaaqwq aegrvrgyvp
      961 kgvvntgtat npvytentra idptnywqtf itdgsniatp fiykatyvkl reltltytlt
     1021 pafskqlglk gaslglvarn pfilykdvpn vdpdsnynns ngqgleygsl ptrrgfgfnl
     1081 nvkf
//
LOCUS       WP_097128756            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097128756
VERSION     WP_097128756.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117898
     Region          46..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrtysllfq dvgkrtaall iyltlfsyst lfaqvtptkt pkiigtvtgv vsgdgaaipg
       61 atvknknanl tvvadangvy kigitgandi ltfsylgyqn adrvvgtlkq isvtlisvan
      121 elkdvvivgy gsqkkrdvtg aivsisaedi ekkaptnvye alqgqaagvq vttgsgqpge
      181 sasvvirgis tmnndgvgpl wvvdgvpttn vdalnpydie smevlkdaas aaiygsrsan
      241 gviiittkkg spkapvielr ylhslnnlth tmpqmnskqy rsmqkgltey ingegatlvp
      301 tavknvmaaq iadslnflln adndyqalvf staqkdqidm sfgggsdklk yfigagylne
      361 egiisntsfn ristrlnady iatskltlgs rltlsygkkm gvdeggflns llsrkpnlal
      421 yypdgtiigt lwganpiald vqtnftniyn asffqfaeyk fnkdlkfttn vsgtlslyry
      481 nfmrptllsd gylnnfgsht stlnynwlne nyfnytksin nthnftgllg fsmqswrtei
      541 dsysgrnsat davytqnafa anfdltrtgt tetahtlasl ftrftynyks rylftanvra
      601 dgssrfakdk kigyfpsasa awrfsdepfm kwtkklkitd akfrlsygvt gnesigdyes
      661 iltygiggiy dgvagvtaar igvndlgwee taqtnvgldl nfnnnrivft adyynkatsn
      721 llaayeipke wgfntvrkni gsivnkglef slsgdvikkk fvtwnigani tfnknkvtei
      781 aggipyifnd twwisqgkpl gdfygytsng ifaydqsnaf tnnweqltpv fqtdasgqmi
      841 kdgngkyilq nyllgnavyt gtvnqkklad gtpfrggdvn wqespedvng vitdkdrtvi
      901 gnaqpdfigg fntnlryksl slfvsayfsi ggeiynfaky nlvqgsmngl stvppvdfln
      961 nfwvkqgddv tyarpysdrf qnaravnsmy ledasyvkir tirltyalpa kwvskvklrg
     1021 lsvysyvnna ftftgysgyd pefsaysala lgmdvnrypr krefgmglnv nf
//
LOCUS       WP_097128876            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097128876
VERSION     WP_097128876.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115012
     Region          31..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mehnlrtris acilavwvtf lishtalaqd rrvtgrviag kdqqpipgvt ilvrntqlgt
       61 ttdangsfnl nvpanatlvf saigfagqtl tignqtqltv tlqeadqnls evvvtalgik
      121 keakrlgyat aivnpeqvtt nrtvnfinal qgkiagvnis slgtgaagts kirirgqssf
      181 sgqnsplivv ngvpidntnf gqnngntggd nsignrdrny sdggdglssi npddiegmtv
      241 lkggtaaaly gsrakdgail ittktkgtgq gigvtfnsnf ttdrpldftd yqyeygqgey
      301 gtrptaanst sgvwsfgekf agqtqvlfgg vtvpyapvrn rintfyrdgs twtnsisvss
      361 gsekggfnls ianldnkgit rnntfnrktm nlgfsynlsp rltvtgtiny sneynknppq
      421 iaqqdnstpt viytlansmp ldvleanqin patgnefvys rfmnrtnpyf vlnnkfenir
      481 rdrlfgnlta rynvtdwlyv qgrvgqdyws rdqdynfptg qaslaaapag fvngayvqda
      541 rrfreinadf liganhkfga fgidltvggn qlyrrsdlns vqvtdfivrg lyvpqngrvk
      601 dptyglserk vnslytaaef sfkdvlflng tvrndwfstl spanrsilyp sltgsfvfsq
      661 afdnlpsfin fgkiraayae vgsdgdvapy snnlfysvna nlfpnpaglg qpvgnitsst
      721 vpsatlkpsr taetevglel klfnnrvgld mavyrkitsd qivqaqssda sgytstlinn
      781 gqsqnqgiev llnlspirtk dfswditlng aynktkllkl ltdklgeqiv vgngiyvgdl
      841 rqvvgeelgq lysfgyvrna agqivhggdg lpvrtpapis fgsalpkytg gitntvnykg
      901 lnlsflidfk lggkmisgtn lnafrhglqk etlvgrgetd nkmvgvgvnd kgevnavraf
      961 vqdyysvgrs kslgeqvvyd aglwklrqis lgydftkmlp ktlfikgirl savannvaii
     1021 kkwvpnidpe qfgfssdnli glestglptt rsigfnlnvk f
//
LOCUS       WP_097129091            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097129091
VERSION     WP_097129091.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117230
     Region          25..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrkftltll gflllavfty aqkavkgkvt dvtngqgipg asvsvkgqag ntvvtnndgs
       61 ftinvpsdns llvvtyigyt tkevsvgtqs tinialness qtlegvvvta lgikrseksi
      121 gystqqingd nltltkeqnv igslagkvag aqvtgssggs mggtqkikir gvnsvtgggq
      181 plmvidgtpi sntnfsgsng ngvdygnvgq dinpedvesi svlkgpaasa lyglrgqygv
      241 llittkkgam ganridvsln saftiekvgn fmplqdiygv gnnqtfqtfs ngekyvngnd
      301 eswgpkmdgt pvrmyysfyp qdaefgkltp flpqpnnikd ffetgtntnn gisisgsgqn
      361 snfrlgynnt yingtypnsw lkrnnvsfag slkltdkltv gtnanyanns aqrpvqgyqg
      421 sftganqwfq rnidinrlrn ykyadgtvln wnvnpslsgt tlgtivtnrp sdwnnpffda
      481 yenlnldsrd rifgdinlty qvlpelklsg fvrtdrftqn inrrnalggr ldesfstgky
      541 qsadnnyefl aqylkkvndf dfnlnvganl ltqsynylta atagglsspg fysieasidr
      601 ptsfsylrek evrsmyamgs vgykdtyfld asvrndissa lpkdnnsywy psvsgsfifs
      661 nllksnvlsf gklrssfaia gadlaayetv mgyvtgnvyk tttntvttgf vpdklknpsi
      721 epsfansfei gtdlkflknr igidftyykq rnknqiidls vsggsgftsf vvnagdiqnq
      781 gievslnanp vasklfqwnt ilnfarnksr inelypginv yqldanvyss qtvylnatvg
      841 kefgslvgpg yardasgqll lgadnmpvqe lnkdfgsvvp eftggfvnnf kigkfdvaam
      901 idfqkggqff swskmlavks gqaaetvvln dkgmnvrepl angggvrmtg vyapgtmiti
      961 agvptnvggq nfdgyvdarv yfrnkigtqi yeewlydasy iklrevsvgy tfdkdlikkl
     1021 pvksvrlsai arnplmiwqk apkgldpsel ssgsasiswi ekgelqtvrs ygvnlnvif
//
LOCUS       WP_097129273            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097129273
VERSION     WP_097129273.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110171
     Region          54..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmnksykinr sgdnvgqvga rqpqsikqna fsgilsmlvm vlllsqstaw aqertvtgkv
       61 tdptgavlpg vsiqvkgtqr gtntngegvy titnvpdnat lvlsfigytt qevavgnrtt
      121 vdvqladdtk alqevvvvgy gtqrakdvtg svatlgpkdf nkgviaspeq llqgrvagvq
      181 itpasgepga anniqirgav slrggntply vidgvpldgg dfssgtpdfg tgsttarnpl
      241 sflnpsdien isvlkdasaa aiygargang vvlittrkgr agapqfnfsa sgavssslkr
      301 ydllsatdfl agvqaaggdp tlstvnagan tnwqneilrt svsqiynasf gggtndtryl
      361 fslgyqdqqg lvkgtgqqrv tgrinasqdl fnkkltlavn attssvtdqy amtgnqagal
      421 gnlfgamiga nptypvfsnt sdtasyyqla ggsyrnpram ldyyhdrgvt nrtlanisat
      481 wnilaglslk anfgidnsts trstsidsrl ngqftvplgs vtnqvyadpt tglggaayin
      541 slnrlsklve ytanynrdlg pgkleavagf ayqtfgtrts yvaasrfpfd eseisytdni
      601 gaantltgta igggssraqn dlqsffgran ynfkekyllt atvrvdgssr fgvnnkygtf
      661 psvagawris qesfipknif ddlkiranyg ivgnqdftgg askiiytyns sgsqiqqnnp
      721 npdlkweqnt ttgagidfsv lkgqlsgsid yyhragtntl lqvfyaqpap vnykwinlpg
      781 qivsqgieln liyqvfqkpq fgweavfnlt tldikaqgig tdqavgaisg qglsgayaer
      841 itsgyppfaf fipkftgfda ngystyaddg rstyqgspfa klrlgltnnf tfgawtaslf
      901 vngqfggkiy nntanalfak galknarnvt ydvansneng lnpasvstrf leksdyvrit
      961 nltisrrfdl peggfaksls lsltgqnlfi ftgytglnpd vntvtfngng ngipslgidy
     1021 tpyptprtvt lglnvgf
//
LOCUS       WP_097129263            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097129263
VERSION     WP_097129263.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115893
     Region          34..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhflpnekr rhlalvtafw lltmlvgwaq npgrtitgki lsktdgkglp ganvlvkgss
       61 vgavtdaegs faisaqpnat ltvsyigfvs qemaignqte vvislaedas qlsevvvtal
      121 gisrdkkalg yslqelkgne ltqarptnlv nalsgkiagi qvtatnglpg assrilirga
      181 nsiggnnqpl fvvdgipidn gsynvtpgst ggnvnnvttd ygngassinp ddidnisvlk
      241 ganaaalygs raangvilit tkrgsasknv gvtvntnttf enplrlpdfq neygqglkgq
      301 fsyvdgmggg vndgvdeswg pkldgrlipq fnspigadgk rtatpwiarp dnvknfydtg
      361 vttsnsialt ggnekgdfrl gytnlyqkgm lpntnykrqn lsfnagwnft pkftvrtsin
      421 yikdgsdnrq nlnlywiwfg rqvdledlka npvqpdtdps qwpvqrnwns nywnnpayal
      481 kylkyandkd rlignitaty kltdwltltg rtgtdfsndr rttkqaknvg vpngsyaedi
      541 vyvsetnsdf lltadkrfse lhvvasvggn trrnytqrdy myaseltipn lynignaksr
      601 ptvynritdk rvnslygsas lsfrdylfvd ltarndwsst lpagnrsyfy psisasaivt
      661 dmlgltsnvl tyaklrggfa qvgndtdpyn ltqvfsneta wgntttfsen nliynknlkp
      721 elttaiefgv etrlfrnaln feftyydknt knqilqanva qssgyynsvi nagqirnsgf
      781 eielsgapvk naggfrwdvg infarnrsev vdlgglstyq intgsllrnv ilearpgdpy
      841 gnfygtyyrr dpsgnlifns qgypimasdr kvvgnimpkw tggfqntfsy kwvslsslid
      901 vryggnvfsq ginigrytgv laetvpgreg nivgkgvvet anadgsfsya snttavasad
      961 dyyhnfynrn vnenyifdas yvklrevrlg ftlpqrwlgk tpfrsatfal vgrnlallyk
     1021 niphidpets yygdgnvqgf engntpsars mgfnlnfgl
//
LOCUS       WP_097129724            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097129724
VERSION     WP_097129724.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119973
     Region          39..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          116..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msitflqvfi vlslfgtala tptrgqdvln kkisidqsdv tmgnvlkkle sdyninfvys
       61 pqvidpnkkv rvfsqlrpls elldqlfvsm gltyeasdnv iairkvrdan saskainitg
      121 kvvdeetgtp vpgvtvrvkg stagtftnae gvyvinvpde nativfsilg ydtqekvvgs
      181 qkvinvilks srselnqvvv vgygtqkrqn vtgavasanl esfkdapntn faqslqgsvp
      241 glnvgpvtta gstptitirg qntingnqnv liildgvqyy nslgsinpdd iasidilkda
      301 sstavygaqa angvmlittr kgskntppri nfstsyatqe psvdlrpmgr eeyldkvrnl
      361 yynraflapg ytvpdpsfni anyvdisqrv ltsgqpntlv dtdfdwweag tkrgfindnq
      421 lsisgggdkv syllsgaytn qagfivndlf krksirsnie sqifpwakvg lqafgsfvnn
      481 dgqeptlnel miqsplnspy nadgtlrpqp fnttgtnpfl sydvddkerh ntlfanvytq
      541 idfpfvkgls yklnvgvnyr tdlrynanqy ganltgeayk nneqysdyti dniltynrsf
      601 nkhsitatal ygaverqsdy fqaratgftr mnlgynnlnl galqftnsna wqealnyqma
      661 rvnyafdgry lltatirrdg fsgfaannkf atfpslslgw vlneenfaks lkwlnyaklr
      721 vgygvsgnlt sryfsldrvt sdpayvfgdg gttqygqfva tlpnpdlrwe rtteynvgld
      781 ftvlnnritg sfdyynrrtk dllfpveipt vtgydrintn vgevankgfe lsltskniqs
      841 sngfnwsttv avsrnvnkvv allgtgdlvs snlfigqpiy pvfdyrtngi yqlnevpppg
      901 fftgnirved ingdglintn dreilgatqp ayrfsvlntf kykklsltvf vnsiqggsng
      961 ylgnntqtrr lddnnvrwnh isgtdfwsps npngrypsft lapaiapalf ydrsfvrlqd
     1021 vtlsyqidgk ifqkagiknl nvfasgknly twtnwqgwdp eignggmtts grpllkgysl
     1081 glnvtf
//
LOCUS       WP_097130831            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097130831
VERSION     WP_097130831.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110548
     Region          34..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksklrraip glflflgiwi saaaspvfav dsevtgrvsd ekgndvvgas vtikgtnrgt
       61 ntdasgkyri vvpdgsavlv fsyigynkqe vtvgnrsvvd vklepgsavl devvvtalgi
      121 skearkvgya vttinseaft karetnvgns lagrvaglnv kgtsggpggt akilmrgmps
      181 insggapliv ingvpmdntq rgsagewgga dggdgignln pddietmtvl kgqsasalyg
      241 tratngvili ttkrgkkgdy aieynanlta dspvnftdfq yeygqgtggv kpttvsaaqq
      301 tgrqswgakl dgsqitqfdg kqyaysaqkd niknfyrtgt nftntvsvtk ggdngsfrls
      361 lsnldtksil pssglgrktf nltadqnits klsvsllany idekvtakpq lsdgpmnann
      421 glflatnidq rilapgyntt tgreiifsdd eyvtnpyfvt nqyvndvsrk rlismiatky
      481 qfadwiyaqa rvgydnandr ifrvtpygta ysqdakggld eqsnaqttel nidgligvnk
      541 aitpdfsida ivggnirknd yekigigggp fvlpylysfn nvvnfnrsya faksevqsay
      601 ysvdfsykgf lnisttgryd tysslpssnr siftpsvtga fifsefvksp alsfgklras
      661 yavtsgepga pygtsvyygv gsaingvptg nfssslpnlf lkpftkseve vglelkffgn
      721 rlgfdlayyd qktrneilpa nyspatgyts gvvatgstqn rglevlingt pvktaklawn
      781 vsfnltsvkn kilqtdannn plglgsnrat lgnattnfvv gesgpqiray dykyasngqi
      841 ivdasglpvr gdlinmgtvl ptlygglnne fsfgnfnlaf lvdynygnki lsatenyayr
      901 rglhkatlvg reggittgvv eggaantvta taqnyytala nnvtklsvvd gdfikmrqlt
      961 fgynipasvl tkvplirsvn isfvarnlfy imkkttnidp eatfganlry agiegtslps
     1021 srnygvnlni rfk
//
LOCUS       WP_097130839            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097130839
VERSION     WP_097130839.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120593
     Region          22..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 makslqrlii llwvistpvf aqtisgrvta gndgqplpgv silvkgttsg titdtdgkyt
       61 iaaakakvlv fsfigykske vlidnkttvd vlldedasmi nevvvtalgi pkeeralgya
      121 tvvvkndali ktatpnfata lygkapgvti natpggatsg vsisirglss itgntqpliv
      181 mdgipirnge arntdywgdq rirgnglldl npadienisi lkgasaaaly gseavngvvl
      241 vttktgkgrk glgvdfsasy svdkiaylpr yqnvrgpgyf qnyanggqda ngfisydtdg
      301 dgkgdtrgll gatvnfgpkf dgqpvmafdg virpyvasnn syanlfqnan ssninlaisk
      361 atdnstirfs ytrqdngmis ygakneknim nlnasfkvnk klttdlmvny vnqythnrpf
      421 kvdrminnft gmmnrfesad wyfnkyqtsq gykyvtgtnq sltpneniir ngfkgdigdy
      481 vwstrantyd eysnrviasi tqhwqildnl klrgrigtdl tseriedkqr ssiplafgys
      541 gsfamnnnly snvygdvllt ytkklnpdvt vmasggytan kmlntyvgrs tngglstenf
      601 fdisasvnts ggsnsrdksi rdaflgtvnf dyknfffieg tlrrdrtstl apgnnafvyp
      661 slnssfvfsd lfrlpaviny aklrgswgiv gnyppiysan naynqgnlsi qqtggssvly
      721 tnissdygnd kirpeqkhey efgleaklfr nrlgidlsyy naqivdqilp ltiaatsgar
      781 silanigtlr nqgvelglnf savksadlng lnwditlnla knsnkveklt nnstellhad
      841 ydgnaaqlrs vvgqpmgdiy vhgilkdang rnvvgpngiy qldganwika gnampkltgg
      901 flnsvgykgf nldvvvdfry ggsimptgin wltsrgltee sltamdaesg glryykdang
      961 kgiqttgsag pngevvyndg mlmdgvlptg eantnvisqa vyynstynwg gpqysssrye
     1021 lyvkentyvk mreislgyri pasltrkigt qnltlsvfgr nlffiyrtik dldaeqtnss
     1081 trwaeninna gnnpsfrtmg vmlrasf
//
LOCUS       WP_097131467            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097131467
VERSION     WP_097131467.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116548
     Region          23..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkflltqfv lclfalplla qdiaisgkvt ssedgsvlpg vnitvkgtsr gtstnaegtf
       61 qlnapansrl vfsfigfttq eiaignrtni svnlapdasq lqevvvtalg isrdkkalny
      121 avqdlkadkl nfardqnvgn alagkiagvq vlgqsgakfg npnirirgvn slsggdplyv
      181 vdgtptdisq vnmddvenlt vlkgpsatal ygnrasagvi vittkrakag etrldinhst
      241 tldmvallpk yqneygggys qawetfqfdp sihpaawssf ngqkildysa deswgprldg
      301 sphrsafswq qgpefgqltp fspqpnnvrd ffekpisnnt niafsrgtea fqsrisythi
      361 inngiipnss qsrdyisskn aikfaeklta nlninytstn tknqpadryg ssggtgvsnn
      421 lfgvsnstln gynqtigmfn qwfqrqlrme dlrnyknpdg tfrswniggp leaapkywds
      481 pytqayentn tnrsdrlfgd igltyqftpa lkasatvrrd qnayyqqgrv aigtlneggk
      541 ggfstlntns rennyellvn ynenfkdlsv vanaggniry nrtdglfqat vgglsapgfy
      601 niaasidrpl annylyerqv nsvfgnvsvg frdfvfveas irndwsstlp kannaylyps
      661 vsagviltel lpksqvlsya kvragyaqvg tdvdpyrtal aysagqpygn sstaflpgtl
      721 pnanlkpgls ssyeggidlk flnnriglef tayqnnnnnq iiplpvaats gytnavvnag
      781 lirtsglelh iyanpirsan gfnwefdina drnrsqviel asgltnyqid gpqwrtltln
      841 artgtdgspr dwgtlvgqgi qkdangrpmv ygsganagly ikqdnvelgs vlpkfkggwl
      901 ntfsyknvtl rvntdfvvgg kffsttkmfn aysglaaeta glnelgnplr ddpasgggvl
      961 ldgvteegkq ntvrvdaqnl yenwlfalne rwiydktyvk lrevafgynl pkqllgkwlk
     1021 sanisliarn pvliysaigg gidiseseti wyeggqlppv rsfgvnvrlg l
//
LOCUS       WP_097131469            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097131469
VERSION     WP_097131469.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117595
     Region          26..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkaltgswf llllfympvl aqetaitgrv tssddgsalp gvsvvvkgtt rgtttdangt
       61 yqintgattt ltfsfvgfkp qdvavgnrat vnvvlaadas tlnevvvtgf girrnereig
      121 tsvtkinntl inqaapvnla ngltgkvagl qinavsngvg tnpritirgn rsflgnnqal
      181 lvvdgaltdv sflsainpnd iesssilkgp saaalygsda angvlvittr rgttnnkpqi
      241 sytnntqles vsympdlqrl ygsnggegap fldangqrly vpyenqqfgp lyngslqplg
      301 ygvqiinpdg siridtlkvp ysstgkdprr affstgvtqq hdlayrvgda enyfglsvqr
      361 vdqkgivpnd kysrtnftvn ggrtidrfta nakmqftyen tdqengdfgq grplywnlln
      421 qpahaplndp rikdinspyg dvngyfnayy pnpwwqvtgd nsravtnkys iqgtadigyk
      481 ftdwlnvtyr vsgqvsntqf kshlaavsfs syalgdpwga gniasslkqv ngnvsdysrt
      541 tsrvtgdlli tvaptfgdft tklilgqqar vdnsryistt atslvvpgty nianrlgnvl
      601 asensfqsrl lgyfydftag frnfafinat grydntslla pgnrsyfypg vnasviltea
      661 ipalkgsnal tylklrggia ragnisvgpy qlqnvfnpga gfpygsqpgf slstqqndpn
      721 lkpefttnke vgvefglfdr vnaeivyytm etinqtvpiq vsratgygsa lintgsmlnn
      781 glevelktlr pivntggftw nintnftyln ntvtsvypgl drinitqang aqssnvfaav
      841 nytypalfgt diarvqntda naayydptgq fvgqavinpa tgypildanf kylgntqpky
      901 rfglnntfaf kgltlnalve yrggnviynq lgnaleftga girttyngrq nfifpnsvla
      961 ttnpdgttay apntsvstrd gnlefwtnsg yhnavssyvt saafwklrev alsynfptql
     1021 fsnikfirsl tlgltgrnll mlrpktnvft dpefsldnsn aqgvtneyqt pptrqygfrl
     1081 svgf
//
LOCUS       WP_097131627            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097131627
VERSION     WP_097131627.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117382
     Region          27..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkmkqlliif llalglsvna qqlvlfkgtv ssstngeaia gaklklagve qviitnsdgg
       61 fevrlvrgsy tlkvshvgyt vldtlvklpn aeyaisltpa vkqldevvin tgyqktsvek
      121 ltgayqhisa kvleeqvgfd llprleavan alsidresne rgrinirgvs tingakqvlv
      181 vldnfpyegd ieninpndve sisilkdaaa tsiwgsragn gvvvittkkg kynqglkisg
      241 nfnttikerp nlsrlpqlns sdyidaelfl fnagrylndy nnvarpavtp vvdlmysnls
      301 aaektaklde wrkqdvrddf nrymyrngyt sqyfvqatag gkgygwslsa ghdrvtstld
      361 asnrrtslry alnvdlipsl klnfglalsd nnaesgksgy gnitsvggvl ypyaafadad
      421 ghalaipkty rvshlatlds rlldwkyypl nddshgvlrs krndmdvnvg lnyhwagfta
      481 svlgrferqw gstnqlygle sfytrnlins fsqlsgtnml ykvpfggidd raannlqasd
      541 lraqlaydks vkshafrmml gaerrellnn serfrnygyd eslmsttqvd yvnpypnfit
      601 gatarvpylq slgatnnryv svygnlgydy adkyllyasa rrdatnffgv ntnnkwrplw
      661 svgagwivsk esfyrwtvve ylklrisygh sgnanptqtg vttimygsvs pytlspdani
      721 dkvanpelrw ekvtttnigl dfkllagrls gsidyyqkkg tdlfgvfpid yttgvgnsil
      781 rnvasmlgrg tdlqlnsvnl ngsfkwetql nlsnnkdkvt dyyfepsnsy eyvrpgrani
      841 sgivgrpvys mlsfesagld angnpvgyln gersldyini tqkgtaldql rfhgaalptw
      901 fgnlqqrfny kgfglqlsls fkaghyfrrs sinytnfins gqghsdfsqr wqnpgdeakt
      961 nvpafiypnn asrdvfyasq sslvaradhv rlqyvnlsyt lpkmllkgyv kqasvycnma
     1021 nlgmvwrank lgldpeingl tnfpaertls fgarlsf
//
LOCUS       WP_097131829            1169 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097131829
VERSION     WP_097131829.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1169)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1169)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1169)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1169
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1169
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128763
     Region          44..109
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          163..1168
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrilfytt lwlssfsgiq egvaqltfas ihrrkegtpt qetntslivl lkkleltykt
       61 sfvyqkelle nktfsgavne ndkleqvldr vltpaklrfq klkgggytil prkigknssa
      121 eteplkasgt qplepeadke lainsltarv dmqafstakp adivvkgrvt dndkgdpipg
      181 asivlkgank gtntdangqy sisvpnanav lvfsfvgfek qevtvgnrtq vnitlkndlk
      241 elnevvvvgf gtqkkinatg aistigtkel iqspvanisn slvgrlpglf atqsggepgn
      301 dgskirirgv gtfsgstdpl tlvdgiqvdn ynnidpneie svtilkdass tavygirgan
      361 gvliittkrg kvgppkvsyt fnqgfnsftd lrqmmnsgdy athfndalka dtyvngttyt
      421 prytdqdiel yrngqdpifh pnvnwfdvmf kkvskqsqhn vnisggqnkv ryfvsagyfs
      481 qeglfkdtkd vvdafspqsl fqrynlrsnf nfdvtsrlrm tldlssqtev rsgnngsste
      541 rvvgdiaras plstpgvvdg kvvniltgsq nnpyasllyp nlagglkrsy rnylngnfrm
      601 dydlgfltng lsvhgnvamq tyndqqivnt ktlitylavk lpdgsvnyvp stteaqfgfs
      661 qsgnynrrit aeagvdykqs fgvhnvtgll lynqqktfdp alaflvpkgy qsfvgratyd
      721 yngrylaevn vgyngtenfa pgkrfglfpa yslgwvasqe pffpksgfvt flkvrgsyge
      781 vgndniggtr flyretsyss vpnmyyfgnv gstysgftgi regatgnpnv tweravkqni
      841 glelwflkdk ikftgdvfse krsdilatpq tissitglsq pasnlgrmen kgyegdityi
      901 dkvgglgyri sanfsfarnk vtfrdevpnq fayqnrtgqr lgqnfgliae glfnsweevn
      961 ntsrpvyays nnkiqpgdik yvdyngdgiv nnfdavpigf snlpektfga siglnykgfd
     1021 lsvlfqgvgn vshyytrfqr gtgygqappe gspsymnesw tqerydaglp irfprfsvna
     1081 npngegssyw ladasyvrik naeigyrlse gllkrlhiga criyvnannl ftwksmypgi
     1141 dpentstgdt ntepyplvrt intgvnlsf
//
LOCUS       WP_097131889             836 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Spirosoma fluviale].
ACCESSION   WP_097131889
VERSION     WP_097131889.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 836)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 836)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..>836
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          53..>828
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkhlppqgl lgrpfsvvit qlllallcis ftyakkplgv kaptdrpsmt adrtlsgrvt
       61 dekdealpgv svilkgtqrg tvtdadgryk veiptggatl vfsfvgylpq evrianqtsv
      121 dislkadskv ldeivvigyg takksdltga vtsvkeaqlq erptsslnqa lsgrmpgvqv
      181 ntnsgrpggr ttvrirgfss inssnnplyv vdgvmlpqgt gdqfsnpidy inpndivnve
      241 vlkdasstai ygargangvi lvstrkgkag esrvtydgqf svntigpnkp kvlnakeyla
      301 tedlayanma kydpvgwaag kwsyldpkvr raafsaarpg vfdanlnply dtdwfkessq
      361 ntlsqnhqlg fsggnertqy slslnyrddq gliktsymkr ysgrfsiddq vkswlkiggt
      421 lsynnqsenl vdvndavarq ivedfpflpv typttgvfae nrdypfaegt mssvhrlmdr
      481 ryiqntqttl gslftnitlg kglemrtvlg aniqtqeinq sqtrtlnigg ngnasannnk
      541 tsfwslehyl tynkqfgqdh sftgllglsw qetntfgiga svsgfatdyf gfnnlgagat
      601 npsvssgasr fafnsyfgri nygyknkylf tatgradgss kfgenfkfaf fpsaalawrv
      661 seedflkgnp visnlkvras ygltgnseip pyqslsllss nystiyndgr vggtgisrla
      721 npdlrwekta qtdvglevsf lkgritlead yyyrlttdml ldapvpqssg yatirrnvgs
      781 menkgfefgl ntininrgtf swntnfnisl nqnkvlslat psdifnvggp nftnpt
//
LOCUS       WP_097131833             967 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097131833
VERSION     WP_097131833.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 967)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 967)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 967)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..967
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104757
     Region          44..965
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtytipvf lvlllgvfgn vhaqqrtgql ptldsvavfp alavtnigfg nlptqrvtsa
       61 lstvygsdle knfslnlgnt lygrlaglsv tqggsepgas tpnlfvrgvn tfgaagnapl
      121 yiidgyisng agpsnafmql vpeeietitv lkdasataiy garaangvvl vttkagkagp
      181 lrisfttrqg fnqaqyvpkf lnaynysvly nealsndglp trytpadlda yqngtdpvfh
      241 pdvnwynqvl rptapvssyn ltfgggdkfv ryfvnlnait sqglfkkfgd mndessnsny
      301 akynfrtnld vnltqrlsae fkiagsfeqs nnpnnyttgs tfgllaqlpp nafpvynpng
      361 sfggnalyan pvgnmlatgf ftnnsrtvls slklteqldm iakglsasvs vsinnyfesg
      421 srkskqypry sisrgvagdt iyspavgqlt slagaeetld qyrslifqsf lnykrtvgkn
      481 disamlmfns dnvtvfgpan dlstptanst dpykhnngaa rftytynnky laevsagymg
      541 sdifapgqry gffpaasvgw vlsgekflsn nktidflklr gsyglvgndn ivtqglssry
      601 aytatfgggg yffgtgntav ggfaenaian pnvtwekeks lnigvdatlf knfdlsvdvf
      661 nrdrydivva sasttplfsg ivtpnlnqgk annkgfdval rynatqkkdf qffvesnfsy
      721 fknkvvfnae aiqlnsrlya agnaigqpig lkaigfysle diaqrqldpk nvpgvlsevi
      781 kagdikyqdi ggpdgkpdgi idandrmpig npglpnlslg lhtgfrykgf dadlvfqavt
      841 gntvylggny fqafqgngqv apialnrwtp qtaatadypr lsskdnlnny qfstfwqrng
      901 sfvklrsaei gyslptalsd rvrlktvrff vngtnlfsld rvpygdpetl tgypvtrtvt
      961 lglkvql
//
LOCUS       WP_097131918            1167 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            fluviale].
ACCESSION   WP_097131918
VERSION     WP_097131918.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1167)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1167)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1167)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1167
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..1167
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127089
     Region          71..121
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          157..1164
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknqyillsm llggvyvlpq psvaqlltra qpayesnaqa tspaetpagq rtrrnrslkk
       61 alfelerrfn vnfaydeqvv anrqtdadld glsleqalsq liesqglryr kvnanlfaiq
      121 pvpakkvglv spaespapal asvsnaltnv teapqlkrit gqitdennqg lpganviekg
      181 tttgattdsn gnfvlnvsda attltissvg yvsqdvaigt ntvvnvklvp ddrtlnevvv
      241 igyqtvrkrd vtgandviss tqankvtans laesiqglsp gvtvrntgvp gqqasiqirg
      301 vasflntdpl yiidgmiada nptinnddie siqvlkdasa aaiygsraan gviiittkqg
      361 kegpirvsfs akygtqqvyk rwdvmdaanf aatqrtqyqn agqtppasva tatfnpnint
      421 dwqdqvlqtg nlqdynltls ggtktgtyli sgsyfgnkgy vigsgfdras lrintksqig
      481 rftfgenall tnsniqnfpa gnpiydmagm lpvipvqdps yidagnpggy gigrnpdavt
      541 yafnpvavrn lasnksnfak lvgnayldvk ladwltyran aglevsfdyt qnlrrlgiyq
      601 ysaspvptsv gedrsrylsl lfehtlnfnk vfgmhningv vgisqqtsrr ditsgsrtnl
      661 gfaggqyfnt inaatgisns aggtpddyri lgyigrvnyt yndrylltlt grvdqdsrfg
      721 anyrtgffps iaaawrisee kffnvdwisd lklnasygkl givvptlgsf pytafinnnp
      781 rtifgvdqtp yvgayqaqla npdlrweerl qqnygvsasf lrnrittein vynslsndai
      841 lnlavpgylg nlrgnpyvnt asirnrgvef satyrnneha vkwdvsgnft tiknrvenvg
      901 nqgqeinyiq sgntrsqvgq avgqwyvlkt agifqnqeei nnyrgpngnl iqpdakpgdi
      961 ryvdqltvdt nndgipdqgd gqitqnndrq fvgspwpklq agaqanvsyg qfslnlqltg
     1021 vfgytvyndv rrgldsyqlt nfrsdispwt ttntnttdpr lglesgdqgi isnnfgytdr
     1081 wlenasyvrv rnveigftlp ktllntlkir narvyvsgqn lftitkytgl dpdvtgpagt
     1141 tgiqergvdn ghwpsprvvs vgvncdf
//
LOCUS       WP_097132002            1210 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097132002
VERSION     WP_097132002.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1210)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1210)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1210)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1210
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1210
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133436
     Region          134..1209
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikdqkepw hsalatnplv rimkltmiim tvflmqlsaa glaqnvtfkk nnsslkefft
       61 eirkqtgyhv vwqegkvnda ikinaafqat pleqaleqtl saknlayeiv nktvvvkpke
      121 kglldriksy faritvsgkv ldtetnlpmp gvtvkitgtn ksavtdvngl fkiddveena
      181 slslssvgya srsmavqenm lirlspvtqe ldgvvistgy qeikkgtttg aanvitskei
      241 eetpsinlme rlegkipgvq fdirkntiqv rgtssytgks plvvidgfpa vnqdlttvtn
      301 sviesrpnnr nqpetsgnai lstfnpadie sitflkdaaa saiwgakaan gvivittkrg
      361 kkgtssvnfs attglsaaak lsdlnsmtna qyieleqelv dknfiqdpva nliasptngw
      421 rtgpvteaqe wmfrakrnpa lipqrdaalk elasrsnhdq irdyllqtam qqqynlsfag
      481 gkgnssyyis gnytkdrpvf ksneaekysv lsnltnnfln nrlivttgln ynyskskvnt
      541 aaisalsegs lglapyelmv dangnrirkg vvfttrtsds ltrvrnllpw tynaidelay
      601 gntvntgnvi rinssvkgii tnwlnftvsg qlqksieeqv nlknensyyt rnlintgtsq
      661 qnvallgtvy gfpkggiyqa grvnrndygl raqfdvkkdf gadhhfdmiv gseireekas
      721 gseqmlygyn eelstsinvn tvgnaaryyn iygnqvsigq pnnlisrnir rylsyygngs
      781 ysylgkyhat asarfddvnv lgvsrkarat plwsaglrwd vskedfmsdi rwvsglslrs
      841 sigvsgnipe qssnfttirl glvdgytqlp yanigfpvnq dlgweitkmt nigldvalfn
      901 nrvsfnfdyy kknvsdllia lpinstygwq sltynagtlk ahgvdlgita ellrtkdfkw
      961 naifnygynt nevtesriqp qtitglaltn gyavdniwvy rwagldnlgr gqifdangii
     1021 ksstdntirt edrvaagrtv aphfggftnt fsykgwtlma ratynlghkf liqnisqgly
     1081 ptnggysgii gnnaaivnrw rnpgdeaftd vpglsnvnvn sitryinsdl nirdagqirl
     1141 qqvsltyalp nsmlkglpfi kgvnlgatvs nlgliwvank egidpeyqmt smfnnlpptr
     1201 nyvfnlnltl
//
LOCUS       WP_097132239             836 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Spirosoma fluviale].
ACCESSION   WP_097132239
VERSION     WP_097132239.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma fluviale
  ORGANISM  Spirosoma fluviale
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 836)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 836)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Spirosoma fluviale"
                     /db_xref="taxon:1597977"
     Protein         1..>836
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          53..>828
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 makllppkll sdrlirvsst qlllaalcvs ftyagkpvnp klpvhqsvkl adrtltgrvt
       61 dekseglpgv svilkgtqrg tvtdadgqyk levpdgsstl vfsfvgylpq evnvgsqtai
      121 nvslktdskv ldeivvigyg ttrksdltga vtgvkeaqlq erpatslnqa lsgrmpgvqv
      181 ntnsgrpggr ttvrirgfss inssnnplyv vdgvmlpqgt gdqfsnpidy inpndivsve
      241 vlkdasstai ygargangvi lvstrkgkag esrvtydgqf svntigpnkp kvlnakeyla
      301 tedlayanma kydpvgwaag kwsyldpkvr raafsaahpg vfdanlnply dtdwfkesaq
      361 nklsqnhqlg fsggnertqy slslnyrddq gliktsymkr ysgrfsiddq vkswlkiggt
      421 lsynnqsenl vdvndavarq ivedfpflpv rypdtgvfae nrdypfaegs mssvhrlidr
      481 kyiqntqttl gslftnitfg kglemrtvlg aniqtqeinq sqtrtlnign ngnasvnnnr
      541 qnfwslenyl tynkqfgqdh sftgllglsw qetntfgiga svsgfatdyf gfnnlgagai
      601 npgvssgasr fafnsyfgri nygyknkylf tatgradgss kfgenhkfaf fpsaalawrv
      661 seedflkgnp visnlkvrts ygltgnseip pysslsllss nystiyndtr vsgtginrla
      721 npdlrwekta qtdiglevgf lkgritlead yyyrlttdml ldapvpqssg yatirrnvgs
      781 menkgfefgl ntininrgtf swntsfnisl nqnkvlslat psdifnvggp nftnpt
//
LOCUS       WP_097132425            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097132425
VERSION     WP_097132425.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119717
     Region          113..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqinpkill vftlllfyht lpalaqsknp kvtvnvyqkp lnvvlkdiek qtgltfnydk
       61 nevdlsqllt lnttdnlkev ltllsgrsgl dfnmagnnia irkgirkaap qtrlitgvvt
      121 srqdgspipg vnifkkgtrq gaitdvngef tfklvgdidr ttiefiyigm ltkevtvgkq
      181 sflkvemdnd ifgmdevvvt ssytkekrre dvvgsisqls skqlqtyrpi esfdkliegm
      241 vagvyvettt elntpvkini rgqgslpsia gsrgtstqpl yvvdgipaye qqrgneasvf
      301 ngegylnpms ninpddirsi silkdatasa lygadaangv iiittkagea gktklnvgyd
      361 tgisrfiney kwlsgpqyys llreayingg rsvtdatqfa gssttdtdwf dltnrtpiyq
      421 nlnldvsggt gkttyrlssg yrnqkssslg sdlqkvylrl rvdqqindkf kvgfnlspty
      481 tqenklstfg gvilppniaa vaadgtyqdi qgvpnplail sqnqnsnkgv qlmgnlngsy
      541 qitkeiavsa tigadnyqnk qtqflsaqna tgrnvngrlt iydrnylsyt afvqatydkt
      601 fkdahtlnfl igtqlsdkkt dllrgsgsgf sfdryrvlnm atnqssasst nsdanvsyys
      661 qlgydfkkky yaningridk ssifggdkqv alngaiglaw iisnedflkn nsvinhlklr
      721 ttfgstgnsr igtyaargly sfgtqsgngy ngnvasypdv sgapnpdlgw eknfkfntal
      781 dftlfnkvqv taeyynntiv dlissvavpl etgyanisan tgkmrnqgfe lsintpvisk
      841 qnfnwftsfn lgtntnklis fnngfaslya tatdaaalkv gnstnaiygy rwagvnpqdg
      901 semfydnngv irnaseinal pigntmvlgd rlpdfqggfi ntfnlydfnf sfnilysyga
      961 dlfvsyades dgrnlqnrnq svnlvdrwqr pgdvtdiprl linrnivsns srymydasyl
     1021 klsnvtvgyt lpkklasrlt ldraylfana tnlfyvykda gtkgrngvae rrfvtpetsa
     1081 ftfgvkigl
//
LOCUS       WP_097133523            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097133523
VERSION     WP_097133523.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111599
     Region          23..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfv llfvcvagya qaqtvtgkvt saddnlpipg vsvkvkgasg gvatdakgsf
       61 tiiaakgttl ifssigfatq evtvgsgpvn vqlasdskql seivvtamgl srqssavgys
      121 ttkvdpnkll qksepdmlks lqgkvagvdi rtsqgtpgaa triqirgnss ffgdnqpliv
      181 vdgipysndq ittssqtsgg gayssglgnl dpndiasmqi lkgsaagaly gsrasngvil
      241 ittksgsgsy qnqpvsatfk ssasvenvan lpsyqnsyga gsnftysnsn gswgpafsal
      301 ttiptwpaya nyfgtatipy qaypnnvkdl frtgsvfens isitgggans svaltasrls
      361 qdgyvdnagy nrtslgaggk tttkfglslg anlsytksnq nggvfgenqv dgaasqfart
      421 lflarnwdln lpyennetpn gggqfdnprw sarhntvdtq eerfitnfna dikvykwita
      481 vfrmggnihs lnrrqitdig sraaeglgrl vtdnyrkqei estvllnfdp kidndftltg
      541 tlgfnsnsrk tsrqlntgnr fitpgiftlk ntsqqefsnd nisnrrlyga fgeatvgykn
      601 yafltftgrn dwsstlpasn rsyfypsvsg sfvfsealkm dskildygki ragyakvgrd
      661 aspysladvf vigtnfmgqs tasidgtsnd pllkpeftke leigtnlsfl ksrltldlaw
      721 ydkkstnlia pistpassgf dsyytnfgai snkgvevelt gipvksnnfs wsitgvftkn
      781 knivteltng vtrlplagvl ttiapyaevg mpygylrgsr slrdaagnll idsstgmlie
      841 dteqgmvgnp npdyklgitn afkyknftlg vlfdmtkggd lysvtissll grgvttdted
      901 rlkswvipgv ygdpntkapi ldgngntipn itrittndly fgntfavnss tewnvydatv
      961 yrlrevtlgy tfpksmfrkl pigslnlsls arnlwyiapn vpkgsnfdpe tnsfgatnvq
     1021 gielsaaptt rrygvnlsvt f
//
LOCUS       WP_097133565            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097133565
VERSION     WP_097133565.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111925
     Region          36..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskfyiswrv ksralfltpi llllfftana qtnryvitgk vtedaskspi pgagvkvqgt
       61 nfavaantdg syslvanlap gnyqiavtfi gyktstkqvt lgsntnvtad fslaqdamgl
      121 devivtgtsq gttrkqlgny itsvkgddln kapsgnvlss mqgkvagaqi tqnsgdpagg
      181 msvklrgiss anssteplyi idgvivnnst trvtnttgny dganfvgsig qnrmvdinpa
      241 diervevlng asaaaiygsr anagviqift kkgvagktqv sfntnfvise lrkkievnqs
      301 pvkfggsvds ftqdviqtva papgatpvll tnttavtryd yqdyifrtgv gtdnnlsisg
      361 ggentkvyts fgyfnnqgii kntdfrkynf rtnldqklnn waslsaglny vksaanekpd
      421 gnsffspmns vtiignfhdi wrrdangnlm avgergrvnp vsviedikqr qevdriians
      481 tlklnpvknl tidftlgvdn ssqngttyip pytynvnpdf fgggalmtat qngytsaatn
      541 kalmfnnein atyqakisdl lssvtqvgys yqyekgqyal lqgrglapki stingaatpl
      601 psaegrtels isgayiqqnf kykdhlfvtg alrmdessvf gkdnrnqlyv kaslsyvlss
      661 adywkttsfs swwntfklra aygqsgnltg igayerinay ngqafvgnts lfspfqlane
      721 nvkperqdel evgadlgffn nrlnlsvnyy nkkvkdllls qviaptegyt sflnnigslk
      781 ntgfefvlgg tplktenfsw ttsaifnrnr neaynigamr llstnpgapv aiidgkplgv
      841 fygtyfarna dgslvtnaag ipqqakaang dplrkvlgdp npdfnwsfvn dfnykrfglr
      901 iqldgvqggd vwnadwrtrq gvgngkvaeq eqmgllprgy vagvyaieew riddgsfvkl
      961 reislsynig kvksisnmtv vlsgrnlisw dnykgydpel nsagqstilr nidfgsvpip
     1021 rtfslglqvk f
//
LOCUS       WP_097133802            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            xixiisoli].
ACCESSION   WP_097133802
VERSION     WP_097133802.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter xixiisoli
  ORGANISM  Pedobacter xixiisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Pedobacter xixiisoli"
                     /db_xref="taxon:1476464"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112020
     Region          25..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkllmlfl aafllaiqam aqqvtvtgki tssedgqpip gatvkvkgts vatqantngi
       61 ytikantgdv lqfaylgmit keqtvgastn initlvtdsk alnevvvtal gqkvnkralg
      121 tsqqevkged iaqtqrenfv nalqgrvagv evtstsgvpg asssitirgv ssisgsnqpl
      181 mivdglpidn ktlntsafvs esssntsqan rnadftnrsa dinpediesl vvlkgpeaaa
      241 lygidaanga ivittkrgkp gtgtidysns fridaprgkp evqkefgisg attgsflyfg
      301 neylpgttfy dnidgffqta ltqkhnlsms ggsekisyrf stsytdqngv ipnslydrin
      361 itgatratin dwlkadlsln ytysnneqar kgaggpligl lvwpqtdnak dyltsigtrr
      421 rvttlgagei dnpyfsvnkn rissknnrii snlgltitpf swgffetrig idnytnenti
      481 frhpesasgf syggildvan dvtrninmqn lfnikkqelv eglsfdatig qsfqdlrsni
      541 nslygeglld pnfisvnnts irnarstltr rrlvsffsra tlnyndylyv tgtirndrts
      601 tipidrysfw ypsvsssfvf tdvpafkdal skiftsgrfr aayaqvgkda rpyaylpyle
      661 ykptvgggyg ysfygpnpdl kpefaksyef glelaffkdr lgldvtyynk ktvdqivndi
      721 rgsystgyil fnlnggstqn kgveislrgt pvknknfswd ilanfekakg tvlalpnslp
      781 esyvsdtwly gnvrngntpg estrsltglf ylrnnegqil idpttglplr sttfvsggyd
      841 rqpdfslgit ntftyksfsl sflvdirkgg dilnatnhyl stkglgmntl drsepriing
      901 virdglensa nptknnlivv prfqtgyytd mseelfiekd vnwvrlrdvt lnyrlpstll
      961 kkqkfvksas vfvtgtdlfl itnytgmdpi vngnsaavgg sggvgidfgn fpmpmginfg
     1021 vrigl
//
LOCUS       WP_097146557             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudooceanicola antarcticus].
ACCESSION   WP_097146557
VERSION     WP_097146557.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola antarcticus
  ORGANISM  Pseudooceanicola antarcticus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudooceanicola antarcticus"
                     /db_xref="taxon:1247613"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55438
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpsevf egearvamtp dsaqqlqklg hecliqsgag lkagfidaay taagvtvlet
       61 aeelyeaadi vakvrqpsee evallrdgqt lisflnpggn aelldrikgq gatavamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvigagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yaavsspefr
      241 eaqlakfrei apdidivitt alipnreapk lwlkdmiasm kpgsvivdla aekggnaegt
      301 vadekvvten gvtivgytdf psrmatqass lyatnirhlm adltpekdgv vnhdmeddvi
      361 rsatvtrage itfpppplkv qaiaaqkpkp kapeltpeek raqevaafkk qtrnqvtlla
      421 vmaalilgvg liapssfmqh fivfvlsvfv gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgsf lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_097137110             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            subbaraonis].
ACCESSION   WP_097137110
VERSION     WP_097137110.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium subbaraonis
  ORGANISM  Rhizobium subbaraonis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Rhizobium subbaraonis"
                     /db_xref="taxon:908946"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39814
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgeivfvsre idpaenrvaa svetvkkmks lgfdviveag aglasriadg eyeaagarig
       61 maadaksadv vlkvrrpadk eikgykagai viaimdpygn dkalaamaka glttfamelm
      121 pritraqsmd vlssqanlag yqavidaace ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemskeyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vtrdmlksmk agsiavdlav erggnvegve
      301 agkvaevegv kvigylnvpg riaasaslly aknlvtflet lvgketrala vnpddelvka
      361 tmltrdgavv hpnfataqmk gea
//
LOCUS       WP_097154647             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cohaesibacter gelatinilyticus].
ACCESSION   WP_097154647
VERSION     WP_097154647.1
KEYWORDS    RefSeq.
SOURCE      Cohaesibacter gelatinilyticus
  ORGANISM  Cohaesibacter gelatinilyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Cohaesibacteraceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cohaesibacter gelatinilyticus"
                     /db_xref="taxon:372072"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55639
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtprevf ggearvgmtp svakhlqklg yecaieigag qaagfsdady eaagveiiat
       61 aaalwkasdi iakvrqpnvt etkrlnknkt lisffnpagn eegmeiaksk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvigagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yaavsspefr
      241 eaqlakfrel apeidivitt alipnreape lwtedmvasm ktgsvivdla aekggncklt
      301 vadekivten gvtiigytdf psrmanqsse lyasnirhml tdltpekdgq vvhdmeddvi
      361 rgatvtyqge itfpppppki aaiaaqpkke vkeltpeekr aaevaefkaq trsqvtllgv
      421 gtalmllvga vapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgswl viilaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_097172452             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. AN5].
ACCESSION   WP_097172452
VERSION     WP_097172452.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. AN5
  ORGANISM  Rhizobium sp. AN5
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. AN5"
                     /db_xref="taxon:1855304"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55701
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely dgearvgmtp dsaqglqklg ynciletgag kaagfsdday raagvtivds
       61 adalytgadi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qsqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvaam kpgsviidla aerggncdlt
      301 vpdqrvvsdn gvivigytdf psrmatqast lystnirhmm tdltpakdgk vvhnmeddvi
      361 rgatvtyqgd itfpppppki qaiaaqkpke rakeltpeek hakeraefka qtksqvgllv
      421 igtavlllvg lyapasfmsh fivfvlacfi gfsviwnvsh slhtplmavt naisgivilg
      481 allqigsgnw lvvllaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_097183631             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus haudaquaticus].
ACCESSION   WP_097183631
VERSION     WP_097183631.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus haudaquaticus
  ORGANISM  Blastococcus haudaquaticus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Blastococcus haudaquaticus"
                     /db_xref="taxon:1938745"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52308
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpretr aretrvaatp atvkklvalg yevvlesgag aaasfpddaf aeagatvgta
       61 ddawqadvvl rvnapaveei prlrdgatlv sllspglnpd lvdalaarpi talamdavpr
      121 israqsmdvl ssmaniagyr avieaahvfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvavpageae vsadgyarem gedfnrraaq
      241 myaeqapdvd iiittalipg rpaprlitee mvasmrsgsv ivdmaaaqgg nvagsvadei
      301 vvtgngvsii gytdlpgrlp aqasqlygqn lvslltlltp akdgqlvldf ddvvqraitv
      361 vragektwpp ppvqvsaapa pvaaaavepa ppkappppgr rfalvglgaa vlfaitafsp
      421 neliqhvtvf alavvvgfyv ighvhhalht plmsvtnais giivvgallq ighddrlvta
      481 lafiailvas invfggfavt rrmlgmftr
//
LOCUS       WP_097191221             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Caballeronia arationis].
ACCESSION   WP_097191221
VERSION     WP_097191221.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia arationis
  ORGANISM  Caballeronia arationis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Caballeronia arationis"
                     /db_xref="taxon:1777142"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39570
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpaesr srkslvaatp etvkmlvaqg rtvtvesgag ecahytdday rkagaqigda
       61 asafgaqivl kvaspnesel slmkpgsvla gmldpfdten tarlaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vlvaaehypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpfetdee reaaegvggy arpmppswla
      241 rqaaqvhera kladivista lipgrpaptl lsvetvkhmk pgsvivdlaa grgvefegrk
      301 ggncpltetd qvvqkygvti ighthlaslv aadasalyar nlldflklii tkegtlnidl
      361 addivaatlq crdgqvtrpa
//
LOCUS       WP_097192811             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas lundensis].
ACCESSION   WP_097192811
VERSION     WP_097192811.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas lundensis
  ORGANISM  Pseudomonas lundensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas lundensis"
                     /db_xref="taxon:86185"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38756
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth qgetrvaatp etikkligqg hkvtvqsgag inasvidsay etagatigsa
       61 gdalgaelil kvvapndnel alinrgavli gmlnpfsdet iaklashgit afsleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgi tivghtnlaa mvaadasaly arnlldflkl vftpegqfqi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_097195550             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus aggregatus].
ACCESSION   WP_097195550
VERSION     WP_097195550.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus aggregatus
  ORGANISM  Blastococcus aggregatus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Blastococcus aggregatus"
                     /db_xref="taxon:38502"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53230
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mhigvprenr pretrvaatp ttvtqlvglg ydvvveagag aassfpdeaf aaagarigta
       61 deawqadvvl rvtapsveei arlrdgatli gmiapafnpd lvaalaarri tvlsmdavpr
      121 israqsldvl ssmaniagyr avveaahvfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvavkageqe vssdgyarem gedfnrraae
      241 myaeqakdvd ivvttalipg rpaprlitee mvasmrsgsv ivdmaaaqgg nvagsvpdei
      301 vvtpngvsii gytdlpgrlp aqasqlygtn lvnllklltp gkdgvlvldl ddvvqraitv
      361 vregetlwpp ppvqvsaapa paaavaprpa apppeppkpg rrlalvglga allfvlagfs
      421 pgelvqhltv falavvvgfy visgvhhalh tplmsvtnai sgiivvgall qighddalvt
      481 alafvailva sinvfggfav trrmlgmftr gpstgsaar
//
LOCUS       WP_097203934             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus sabuli].
ACCESSION   WP_097203934
VERSION     WP_097203934.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus sabuli
  ORGANISM  Geodermatophilus sabuli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Geodermatophilus sabuli"
                     /db_xref="taxon:1564158"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52980
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mmigvpaesg sretrvaatp atvtkllalg ydvlveagag qassfldeay agagarigta
       61 teawgadvvl rvgapsvhem grlregatli sqlapafnpd rvdalaarpi talamdavpr
      121 israqsldvl ssmaniagyr avieaahvfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgav vratdvrpev aeqvrslgge yvavpageqq vstdgyarem gedfnrraaq
      241 myaeqatdvd iiittalipg rpapllitke mvasmksgsv ivdmaaaqgg nvagsvpdei
      301 vvtengvsii gytdlpgrlp aqasqlygtn lvslltlltp eedgrlvldf ddvvqramtv
      361 vregektwpp ppvqvsaapv avaaetvevr qpkappppsr rfavvgiaaa llfgitafsp
      421 neliqhftvf alavvvgyyv ighvhhalht plmsvtnais giivvgallq ighddpvvts
      481 latvaillas invfggfavt rrmlamftrg par
//
LOCUS       WP_097203990             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus sabuli].
ACCESSION   WP_097203990
VERSION     WP_097203990.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus sabuli
  ORGANISM  Geodermatophilus sabuli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Geodermatophilus sabuli"
                     /db_xref="taxon:1564158"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52486
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mliavlkear pgetrvaatp ttvaqllklg yevvvepaag eassfsdeay vaagakvadw
       61 sdgdvvfgvn apsaeqldrl kpgatlvsll apgltpdlva dlarrpitam amdavprisr
      121 aqsldvlssm aniagyravv eaahvfgrff tgqvtaagkv ppakvlvaga gvaglsaiga
      181 agslgavvra tdprpevadq vrslggeyls iespevevsa tgyakemged ykarevqlya
      241 aqcadvdivi ttalipgrpa prlvtadmva smksgsvivd maaqnggnve gtvkdqavrt
      301 angvtiigyt dlagrlpaqa sqlygtnlvn lmklmtpekd grlvldfddv vqrsmtvvrn
      361 geltwppppv qvsaappaaa aaappvtsha kqpvspqrry avvgvaaavl fvlaalspqa
      421 llghltvfvl aivigyyvig hvhhalhtpl msvtnaisgi ivvgallqig qggsnsalit
      481 glatvavlva sinvfggfav trrmlamfsr s
//
LOCUS       WP_097205905             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus sabuli].
ACCESSION   WP_097205905
VERSION     WP_097205905.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus sabuli
  ORGANISM  Geodermatophilus sabuli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Geodermatophilus sabuli"
                     /db_xref="taxon:1564158"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52786
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpretr pgetrvaatp atvrqllglg ydvvvesgag vaasspdaay adagarigta
       61 aeawtadlvl hvakptpaei ellrdgavlv stlspaldpe lvrtlaarpv talamdavpr
      121 israqsldvl ssmaniagyr avieaahafg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igtasslgav vratdvrpev aeqiaslgge yvgvpadeqs aggtgyagvt sedydrraar
      241 myaeqvrdvd ivittalipg rpaprliaee mvasmrpgsv ivdmaaaqgg nvagsvpdqv
      301 vttpggvsii gytdlpgrlp gqasqlfgtn lvnlvklltp akdgqlvldl ddvvqramtv
      361 vrdgevlwpp ppvqvsaapa appalrpaah ppaarrpasp vrtaavvgta avllflataf
      421 spnqlignlt vfalaivvgf yvignvhhal htplmsvtna isgiivvgal lqlghtstlv
      481 tvlafvavlv asinvfggfa vtrrmlgmfa aggptrtrp
//
LOCUS       WP_097213751             371 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Rhodococcus (in: high G+C Gram-positive
            bacteria)].
ACCESSION   WP_097213751
VERSION     WP_097213751.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
  ORGANISM  unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="unclassified Rhodococcus (in: high G+C
                     Gram-positive bacteria)"
                     /db_xref="taxon:192944"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38423
     Region          13..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqsskqp rptvgvvret ndgerrvalv pkvvatlrgk gldvivesga glgalmpdel
       61 yeeagatigd awsadvvlkv aapnaketar lragqkligf laprtnetgi aaladagvea
      121 yaveaipris raqvmdalss qanvagyksv vlaasestry fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrvt gydvrpevad qvrsvgaqwl dlgidaageg gyareltede
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvivdl agetggncei
      301 tepgqtvvkh gvticsplnl patmpehsse lysknlyali elmldesgal apdfddevla
      361 aacvtrkeak p
//
LOCUS       WP_097221661             519 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Streptomyces].
ACCESSION   WP_097221661
VERSION     WP_097221661.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53251
     Region          11..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mvpaephpqg igipaestag etrvaatpat vgrlvalgyd vtvepgagas srfsdaayee
       61 agarlgdpwq advllkvnap sseeigrlrd gatlialisp alnpelveel arrpitvlam
      121 davprisraq sldvlssman iagyravvea ahafgrfftg qvtaagkvpp akvlvagagv
      181 aglaavgaar slgavvratd prpevaeqvr slggefltvt aeqevstdgy akatsddynr
      241 laaqlyaeqa advdiiitta lipgrpaprl itaedvarmk pgsvivdmaa sqggnvegtv
      301 agkavvtdnd vtiigytdlp grlpaqasql ygtnivnllk lltpgkdgrl vldfddvvqr
      361 sitvvregek twppppvqvs aapapggaak epepapaatp aksarpawss yalvgvgala
      421 lflvtalsps ellghftvfv laivigfyvi gnvhhalhtp lmsvtnaisg ivvvgallqi
      481 gqgdtavtvl sfaaillasi nifggfavtr rmlgmfskg
//
LOCUS       WP_097247128             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            amikacinitolerans].
ACCESSION   WP_097247128
VERSION     WP_097247128.1
KEYWORDS    RefSeq.
SOURCE      Nocardia amikacinitolerans
  ORGANISM  Nocardia amikacinitolerans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Nocardia amikacinitolerans"
                     /db_xref="taxon:756689"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38038
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mettqnvgds sprgarvgvv resnagerrv alvpkiipal lkqgvevvve agaglgalip
       61 deayvaagat igdpwsaevv vkvappsdae vaklsggqtl igflaprnae nqiaalksag
      121 vqafaveaip risraqvmda lssqanvagy kavllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rttgydvrpe vadqvrsvga qwldlgidaa geggyarelt
      241 eeekakqqqa ledaikgfdv vittalvpgr paprlvtaaa vegmkpgsvi vdlagetggn
      301 celtepgqtv vkhgvtiasp lnlpatmpeh aselysknia allelmlvdg kvapdfedqv
      361 ladscvtrev n
//
LOCUS       WP_097281471             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Caenispirillum bisanense].
ACCESSION   WP_097281471
VERSION     WP_097281471.1
KEYWORDS    RefSeq.
SOURCE      Caenispirillum bisanense
  ORGANISM  Caenispirillum bisanense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Novispirillaceae; Caenispirillum.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Caenispirillum bisanense"
                     /db_xref="taxon:414052"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40667
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipkerr agehrvaasp dtvkklvglg fdvvvetgag dgaaftdaaf teagakiaps
       61 aaeavgdadv ifkvqrplta eegtdevgqy kegailvgsl kaltepalve alaarkitsf
      121 amelmpritr aqsmdilssq nnlagykavi eaaatfnram pmmmtaagtv pparvlifga
      181 gvaglqavat akrlgavvfa tdvrpatkeq vqslggkfvv vdeamekeae taggyakemp
      241 peyfekqkki vgehltkadm vittalipgr kaptlitaaq vetmkpgsvi vdlaaeaggn
      301 celtepdqvv vkhgvtligh tnmparlasd asllfaknll nfltpqvdkd kkalainwdd
      361 dlikgtlvtr dgqivhpmlk kaeaeggq
//
LOCUS       WP_097291602             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097291602
VERSION     WP_097291602.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53606
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltf
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097293950             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097293950
VERSION     WP_097293950.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53588
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edpwlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq inaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097297074             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097297074
VERSION     WP_097297074.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53573
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgkndv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097306301             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas chlororaphis].
ACCESSION   WP_097306301
VERSION     WP_097306301.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38617
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaaip etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_097309333             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097309333
VERSION     WP_097309333.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53586
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr welaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097310414             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097310414
VERSION     WP_097310414.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53572
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr welaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq inaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097313332             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097313332
VERSION     WP_097313332.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53575
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik mvipqweeqa rkngllsq
//
LOCUS       WP_097324347             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Escherichia].
ACCESSION   WP_097324347
VERSION     WP_097324347.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53602
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkatlqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097330920             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097330920
VERSION     WP_097330920.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53586
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnklgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097340461             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097340461
VERSION     WP_097340461.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53585
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw nnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097341710             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097341710
VERSION     WP_097341710.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53519
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva eckqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097343740             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097343740
VERSION     WP_097343740.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53618
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkncllsq
//
LOCUS       WP_097353072             195 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: cytochrome c nitrite reductase pentaheme subunit
            [Vibrio].
ACCESSION   WP_097353072
VERSION     WP_097353072.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03146.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     gene            1..195
                     /gene="nrfB"
     Protein         1..195
                     /product="cytochrome c nitrite reductase pentaheme
                     subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=21724
     Region          7..194
                     /region_name="PRK11659"
                     /note="cytochrome c nitrite reductase pentaheme subunit;
                     Provisional"
                     /db_xref="CDD:183264"
ORIGIN      
        1 mgniklaivi mlksilafsf ygysfsaiad tsvateatds srfqvelird rdykcvqchk
       61 dsketlsgsh gedahkilgr evnctechnn igpdhregap lvtkyssaqs kqgsekvfmd
      121 tsailkansa ctdchqpqyl redswthdvh aknltcsnch dvhankakvl glerkekikm
      181 cvdchsdfnq keeer
//
LOCUS       WP_097353073             474 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Vibrio].
ACCESSION   WP_097353073
VERSION     WP_097353073.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     gene            1..474
                     /gene="nrfA"
     Protein         1..474
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52960
     Region          1..474
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmass vsvtalvmta llnitavsae ekglvdprnd afeqnhpdqy qswkktsesv
       61 eiedalaedp nmvilwagyg fakdynkarg hfyalddvrq tlrtggpqda ksgpmpmacw
      121 sckspdvarv idergedgyf egkwarlgae ianpigcadc hdtrsekfkn gepelaltrp
      181 yverafqain kpfeqqsrld kqasvcaqch veyyftgptk avkfpwdmgt gvqqmeeyyd
      241 algfadwtha vskapmlkaq hpgfetwreg ihgknkvvcv dchmpkvkke dgtvytdhkv
      301 gnpfdrfedt caqchtqskd qlreivstrk aqvlnmklta ekqivaahfe agaawkagat
      361 edemkpilqd irhaqwrwdy aiashgvhmh apevalevlg tavdraadar tklvrllakk
      421 gitepvqipd isskaaaqka lgmdmekmna ekqhflktvv pdwdkaaaer esky
//
LOCUS       WP_097357333             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Enterovibrio escicola].
ACCESSION   WP_097357333
VERSION     WP_097357333.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Enterovibrio escicola
  ORGANISM  Candidatus Enterovibrio escicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Enterovibrio.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Candidatus Enterovibrio escicola"
                     /db_xref="taxon:1927127"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55421
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkerv ahetrvaatp ktveqliqmg fdvvveynag qlasfdneaf eqagatvgdt
       61 dlvwqseiii kvnapikcde scvdelelik egttlvsfiw paqnetlmgk lsakkinvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvfvvgvg
      181 vaglaaigta gslgaivraf dvrpevkeqv esmggqflqv afekqmgsgd cstkeisddf
      241 nrkvaelyae qakqvdiiit tallegrpap klittemvda mqpgsvivdl asanggncey
      301 tvadkvvvtd ngvkiigytd mvgrmptqss qlyscnvvnl mkllckekdg nihidfadvv
      361 lrgltvvrdg kvtwpappiq vsmqpqvehq vesavnpvke sispmkrlva lvlgmggftw
      421 aasfapvafl shvtvfvlac vvgyyvvwnv ahalhtplms vtnaisgiiv vgailqitqg
      481 nvvvsflafi ailitsinif ggftvtkrml emfrkdk
//
LOCUS       WP_097361079             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_097361079
VERSION     WP_097361079.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53512
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knetfvpqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetg sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcatchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_097363095             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_097363095
VERSION     WP_097363095.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35903
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iinmlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnlfhehgl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechaa frsvllrihe rkgivyheqd slntlmanlm argvisaeyt
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 vsp
//
LOCUS       WP_097366663             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_097366663
VERSION     WP_097366663.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53669
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhvqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekldflk tvvpqwedqa rkngllsq
//
LOCUS       WP_097370838             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            parahaemolyticus].
ACCESSION   WP_097370838
VERSION     WP_097370838.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54703
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvviesqag vlasfddaay eavgakvvss
       61 devwasglil kvnapivdee kgideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaefltv dfqedsgsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgrpap klitkemvds mkagsvivdl aaanggncey
      301 tvkdqvimtd ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvikeg eitwpappiq vsaqpqakqa qpvkkepkve eptsptkkli glvaavgafa
      421 wiasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvsflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_097373089             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pacificitalea manganoxidans].
ACCESSION   WP_097373089
VERSION     WP_097373089.1
KEYWORDS    RefSeq.
SOURCE      Pacificitalea manganoxidans
  ORGANISM  Pacificitalea manganoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pacificitalea.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pacificitalea manganoxidans"
                     /db_xref="taxon:1411902"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55471
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf sgesrvamtp dsarmlqklg yacaiesgag aaagfndaay eaagvevmad
       61 aaalwaasdv vakvrppset evgylrdgql lisffypgsn etlleeckat gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg amtyafdvrp evaeqiesmg aefvyldfee kaadgaetgg yaapsspefr
      241 ekqlekfrel apemdivitt alipnrdapv lwtrdmvelm kpgsvivdla aerggncelt
      301 vkdekivtdn gvtivgytdf psrmatqsst lyatnirhmm tdltpekdga vdhdmdddvi
      361 rgatvthage itfpppppkv kaiaaqkpke kakeltpeer raaeiaafka qtkshvtllv
      421 agavlialvg ayapasfmsh fivfvlacfi gfqviwnvsh slhtplmavt naisgiiilg
      481 avlqigsgsf lvtllsfvsv liasinivgg flvtrrmlam fqks
//
LOCUS       WP_097376366             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_097376366
VERSION     WP_097376366.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35931
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrinrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechav frsvllrihe rkgivyheqd slntlmtnlm argvisaeya
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vap
//
LOCUS       WP_097377175             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_097377175
VERSION     WP_097377175.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53698
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqheged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkeva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rksgllsq
//
LOCUS       WP_097408905             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097408905
VERSION     WP_097408905.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53561
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafsvtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097418244             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097418244
VERSION     WP_097418244.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53608
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apaktvtmea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097420918             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097420918
VERSION     WP_097420918.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53602
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rknsllsq
//
LOCUS       WP_097424590             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097424590
VERSION     WP_097424590.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53538
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipffl ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097419123             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097419123
VERSION     WP_097419123.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53587
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarql
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097426515             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097426515
VERSION     WP_097426515.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53598
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rknglliq
//
LOCUS       WP_097431755             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097431755
VERSION     WP_097431755.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53646
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedsplpm
      121 acwsckspdv arliqkdged dyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq inaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097440651            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sediminicola
            luteus].
ACCESSION   WP_097440651
VERSION     WP_097440651.1
KEYWORDS    RefSeq.
SOURCE      Sediminicola luteus
  ORGANISM  Sediminicola luteus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Sediminicola.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Sediminicola luteus"
                     /db_xref="taxon:319238"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117252
     Region          25..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklrgilt llvalvvhis faqektisgt vtdqdglplp gvnivvegtt sgtqtdfdgn
       61 ysisassgqs llftyigqkd vrqtvgasst invqmetdaq nleevvvtaq gikrekkalg
      121 yavssvgsed leqkadadva rvlsgkaagv nitaaggmsg satnvvirgl ssfsgsnqal
      181 fvvdgvpfss dtndggtngd ggnfitgntg ssrfldldpn niekievlkg laaatlygsq
      241 grngvilvtt kagsgksgtk kteitvsqsy fvnefaslpd yqdkygngfd qsfgwffsnw
      301 gpsfeeggva gwgrqpaide ngtlahpyst triqktkdgf pelqdarydw kpyesleeyf
      361 kpggvsstni ninggtsdgn tnynvnfgyl dddsfvpgns vnrtnlsvgg rsklsnkftv
      421 qaamnfsrtd yktppvalsr gngtqglslf gnvfftprsv dlmglpfenp idgssvyyrn
      481 gndiinprwt eknvtyrqlt nrvywnasln yeinenlsat yragmdfyne rnengsnkgg
      541 vefdqaifgf yetydnnnti wdhyiaingn ydlsekigmt fnaggtsrsd ffdqqgvrsd
      601 gqivfgvkrh fnyenqnaiq fsrrrnivgl lgqvtfdydn mlfltastrt dwvsnltsen
      661 nsltypsasl sfiptaafeg lrsqnginfl klragigtsa nfptgyptvg fveqntrvgq
      721 vanpvtthqi asfkanedlk pellteyevg fesklldnrv sldftyfnrt ttdlivtqpl
      781 apstgftstq snvgeiqgdg ieidlgvdwf rnpegfswnt ranfstynpe vtkqdediii
      841 yagstalfig anaaiegqpl gaivgtafer dengvpyvne sgnyisvevd rdgntpvvgd
      901 pnpdfvsnfi nsmsyknwnl gfqinwtkgg dmvsnttaal lgrglikete drentfilpg
      961 trkatgqpnd iqinnstyyf snllfgplea kvydasvvrl neislgytfp akmlentpfg
     1021 slsitaqgfn mwydayntpd ganfdpnvqg agvgnsqgfd nlngpsgrry glsvkatf
//
LOCUS       WP_097440657            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sediminicola
            luteus].
ACCESSION   WP_097440657
VERSION     WP_097440657.1
KEYWORDS    RefSeq.
SOURCE      Sediminicola luteus
  ORGANISM  Sediminicola luteus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Sediminicola.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Sediminicola luteus"
                     /db_xref="taxon:319238"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120682
     Region          25..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklkgvlt llvafvvhit faqqktvsgt videyglplp gvniviegtt qgtqtdfdgn
       61 ysisastgqt llftyigqkd krvtvgssnr mdvtmetdte tleevvvvgy gqttkkafag
      121 tatvvkaevl eaknfsnvtq altgevagvt vintsgqpgt vatvrvrgyg spngnraply
      181 vvdgipfagt fdlnsvnpad iesttvlkda tataiygsrg angvilintk rgrsempfve
      241 vdvktginrq lipryevldn peeyvgyvwe glynrgvvtg nadpvdfann tllgdngign
      301 gynmwnvntg gelidpetrt vrpgvqrlft peryadeafg tgfrnevnlr aggstdksny
      361 ytsigylnde gysinsdykr ytarinlssq ikpwlkigsn lnfvhsestn ngqiigsenl
      421 fefadkmapi ypvfarhpet gqllpdnvyg gyqydygspt gtqngfersr pnanllnpig
      481 savydydgrk tngingnlka dfkftdylka eisyggqwsl qrrqdmtnnv wgsgantngs
      541 lsvedrirys ttflqllrfn ksfgdhnlev laahetferg fsysdqyked vivpglynls
      601 nyslfpsaps gyednsgies yfgqvnynfn gkyfltgslr tdgssrfvnk kwgtfgsiga
      661 swviseenfm kdtffnylka kasygvtgdq dgvdtysgft ifnanyvggl alsenrpgdp
      721 nltwetsrqf qaglemtign fldinldyyk kdtdntffdr rvgpsagfss irvndgevrn
      781 egfefdinar ivntedfkln faingemlnn emlvmpldps tgipkviden sstdgnyafs
      841 vgrstfdfym rdwagvdaad gapmwyqyyd drnnngqmds gegdfstfpn gdesttssly
      901 eyeqavgdan iqrtvtktya datqvyldks fipdlrgafr iggafknfdf stqftyslgg
      961 yaydaqyael msdrfgaagn nfhkdirnrw qkpgditnvp llsdnavvng tstssrfits
     1021 tdylalnnar igytfdgksl egtglhnlnf wvsgdnifiq tarkgfnpsv revgssarri
     1081 yapastftlg vrakf
//
LOCUS       WP_097441479            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sediminicola
            luteus].
ACCESSION   WP_097441479
VERSION     WP_097441479.1
KEYWORDS    RefSeq.
SOURCE      Sediminicola luteus
  ORGANISM  Sediminicola luteus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Sediminicola.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Sediminicola luteus"
                     /db_xref="taxon:319238"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110333
     Region          24..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllksfl mvgaflcfgl ikaqtvsgtv sdangplpga svlvkgtttg tqtdfdgnyt
       61 legvssdatl vfsyvgfksq eiavagqsti nvtleedaet ldevviigyg tttvkdatga
      121 vaavtsedfn gglistpeql iqgktagvqi gqasgepgag vsirirgsns irsnnnplfv
      181 vdgvpltges ttpgggdvin gpntarnpls flnpsdiesm silkdasata iygsrgangv
      241 vivttksgks grggvwefds slsiaspane ydlfdgptfi qrtadlrspe iaaasnfgnn
      301 tdwqdyitrt ttsqtqnlsy snnygkgnvr gtfsygkqfg viqkssqeri tgrinaahrf
      361 lddklrlnlq asisrindea ppvsaesgss gnligaaysa nptwpsnpgf flegnqinpa
      421 nylanfqaet htnrelinfs teydftpelt gkvnlgydhs daeaitavsg ninnfnrvsg
      481 ngqsayntle atsklleatl nykkqfdnss idaivgytfq dfrreginsq gwgspttdln
      541 rmgelleeti rgaqgaidgs yqqfgydsgs tfvnrlfpid ntgtidnnfk rgydaawgdt
      601 fdntdelqsf farvnydlsn kylftatira dgssrfgenn qygyfpsaaf awkmheedfm
      661 gdafstfklr vgagitgnqe glgyaqylkr qryaqpgitd sgtiarpgle tvavqnpdlk
      721 westldlnfg idfgvnadrl sgsvdlyrke tsdllfrqaa aapaadpfvf knledgvvin
      781 qgvelslnyd fiqqedvtfs aafniayndn kveglngtta dfgalrgpgl sdafaqrlge
      841 gislfsfyma eyaedasgnp dfdpsdkkfv gedalpdvts glslnlrvkn wdasayfngq
      901 fgfsvynnta naflnlptfn ttrnatdeal nnksqevstl ylekgdfvrl qnasigynvp
      961 lsgegalksl risatgqnlf litdysgldp evnsstgdlg sgipsagidy tsfprprvft
     1021 lglnarf
//
LOCUS       WP_097441537            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sediminicola
            luteus].
ACCESSION   WP_097441537
VERSION     WP_097441537.1
KEYWORDS    RefSeq.
SOURCE      Sediminicola luteus
  ORGANISM  Sediminicola luteus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Sediminicola.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Sediminicola luteus"
                     /db_xref="taxon:319238"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112177
     Region          26..1012
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkmrqtylil lvfffmgftt lvaqetltgt vtdadglpll gvnvvekgts ngnvtdfdgr
       61 fslkvdqlpt tlffsyvgfk taeinatnns piqvvleeda qmidevvvta lnierdktsl
      121 gysldvvdse qvtvakenni vnslsgkvsg lqitqttggv nkesrvilrg issltgnntp
      181 llvvdgfpmn gsfsdinpdd vesisvlkga gasaaygsrg angvilvttk ksaqkdkigi
      241 siassigfed imltpdfqne fgtgafsefa pinsdgrpvl dypfswswgp kmegqtytnw
      301 lgnedtftvq gnpfeefyrt gvsaintvtl egggdkstmr ftytdqrtkg iipnndlkkh
      361 tfnlrstskl tdklsmdsrv tyilntvrns palaengdnt almlslmprd iklsdlkant
      421 edangnelkw lndntfnnpy wtlahvnnqn kldrlqgfls ltydispaft ltgksgidil
      481 gqdytyhads gssvysngrg eyrhntneti ewnsdfllsy kktldrlnlg fsvggnylmr
      541 kynrlntygk nekapdlyri snygvvttdd weskkgiysw yllgqadygg yayldatfrn
      601 disstlpken rsyfyysvng sllfskllgl egstfssgki rgsvatvgnd tdpyqlltty
      661 nfdnrtylpy amasspnglp nsdlkpente swevgtdlaf fdnrlsiggt yyesvtdnqi
      721 mpvtisrfsg yhtkrinags iknsgfelav ngtvlqnedf swelganitk nkslvqslhp
      781 dlenlvlgkl rtvtvearpg splgeiwgfd ylrdnfgrrl indqgfaqkg erkklgdinp
      841 dfyggittaf kyknwslral vsyqqggefy twgrgyrlff gtdaqsavgr vdgviedgin
      901 entgfentqs inpmlqhftn vftndistdl ildatnvkmr emvlayevpr sflantgidr
      961 vtlsawgrnl fffynaagdi dpessyssgs vgngfehssl pstrtfgmdl kldf
//
LOCUS       WP_097442330            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sediminicola
            luteus].
ACCESSION   WP_097442330
VERSION     WP_097442330.1
KEYWORDS    RefSeq.
SOURCE      Sediminicola luteus
  ORGANISM  Sediminicola luteus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Sediminicola.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Sediminicola luteus"
                     /db_xref="taxon:319238"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117113
     Region          24..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkskltlil alfaiitgys qqnitgtvld enniplpgat ivvkgsssgt stdfdgnfti
       61 evpandavll vsyvgytdqe vptagksniq vvlqpasqel devvvtalgi kretkklgya
      121 iqevsgdeit qakevnvvns lagkmagvqv tggnsgiggt sniiirgess ftnnsplfvv
      181 dgipinndvs snsgdgnmev dfgngamdin pddvesmtvl kgpsatalyg srggngvili
      241 ttksgtksrg igvsvtnntt fetiltmpky qdvygqgsng qfafgdggqn rsltggvndh
      301 vdeswgpamn gqlipqhdsp ttsgfragdv nlrprnadgt fadeiiatpf spqpgniedf
      361 frtgftmsnn valsggnedg nfrvsftdlq sesivpnsnf krrtyaings ynltdwlkvs
      421 gsmnyvnsgs rnrpnnsygt enimylwiwf grhidmnslk dywqpglegi qqfnynynyh
      481 dnpyftvhen tngfnkdrli gnmradmklg dkfnlmvrtg ldysneidkr kraystqrfp
      541 ngqyredyiy gfeqntdfll syntdinedl elgasvganh rsnknsyqri sanslsvpgv
      601 ynfdnaaepl sstdwdskkk vnsvyafanl ayknmlfldl tarndwsstl pkenwsyfyp
      661 svnasailsd mfempeaisf aklragwasv gndtdpyrla ptygfgtpfn gnsrvyspse
      721 lpnenlkpel tdsfeigadl rffqsrlnld iavykartkn qlislpvstt sgfssrfvna
      781 gelenkglei tlgakpvvtd nfmwqtninf tmnrgkvnel iddldfyrta snylivgaei
      841 gerigsvygt gfekvddkns pyhgqwiide nsglpirsse lrnlgnynpd fmlgfqnnfk
      901 yknfdlsvlf dwrqggvfhs rtvaiggttg mldftvpgre sgivaegvid ngdgtytpnt
      961 qnvaasnyys hvykrsnees smfdatyvkl reirlgynfp rkilektpiq aasialvgrn
     1021 lalwtenphv dpetisfsga tivpgvedma lpstrsfgln lnvqf
//
LOCUS       WP_097442347            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sediminicola
            luteus].
ACCESSION   WP_097442347
VERSION     WP_097442347.1
KEYWORDS    RefSeq.
SOURCE      Sediminicola luteus
  ORGANISM  Sediminicola luteus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Sediminicola.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Sediminicola luteus"
                     /db_xref="taxon:319238"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120370
     Region          25..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkllsflv fvsmlsvstg yaqsknvsgt vsdesgvplp gvsvvvkgqa rgastdfdgn
       61 fsidnvastd vlvfsfigfa dqevtvgsqs sftitlaesa ealdevvlta lgiekqaksi
      121 gyaqetvkge elagrqennv idalkgrvag vqitnndagg ggsvnivirg gtnilpgrsd
      181 qplivvdgvp iqnddtdqdr gsrrdwgsgi navnpadies mevlkganaa alygsrgang
      241 vilittkkgr dnggigityd fnarfediat trdvqnvygi gyngwdkanp fptndngnla
      301 mpgvsywgsg aswgpemdgt pveyydgvvr pfspqpnnlk epygigetyv hsvsmqgane
      361 kgsfrasftd nksermepnn hydrfnasfn adynlsskvt agltfnyani dnlnprvlgd
      421 ndqgwgkall ynwarservq lrmdnyltpe gtldpdyryg rsggivwnll qrkemreidr
      481 yfgaftlnwq ftdwlnlmvr tgidnaneqr tmkqppqnpd gldlkystgl skdnsrnsef
      541 lltgnhqltd dlgltanfgg sqyyrkkygl ysrddrywnn pnlyaldnaq qfvngdrnra
      601 inripneefw ekkinslygt ldfnfkdylf lqvtgrndws stlpddansy fypsfnssfv
      661 ftdafqdafa gmewlnygkv rgtwaqgavd dspyqtvpty nigsrfgepa sfvpgeipat
      721 nlkpqktdtw eagldlgmfn nrvnfnftyy nklsenqims gplawstgfn srrfntgsmr
      781 nsgveitvda tpistndfnw nvlfsfsknk nevvnlddsg aietlritgl wgsngpsiea
      841 qpgqpygqim gwdfiyddat gkplvdedgy lyttntrval gnvtpdflsg lintftykdf
      901 tfnmimdaki ggdtyfsskg vadgfgqsae slrgrdtqyg glswtdgngn artdgmieda
      961 ivspdapvyn petdsydfst sgentsiipa rhywavrssg wgagaptths vhenswirlt
     1021 elslgynvpr kflesffiqn lsfnvfarnv gylyktapdn lnphstingg klsgiefggs
     1081 pitrtigfga kvsf
//
LOCUS       WP_097442352            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Sediminicola
            luteus].
ACCESSION   WP_097442352
VERSION     WP_097442352.1
KEYWORDS    RefSeq.
SOURCE      Sediminicola luteus
  ORGANISM  Sediminicola luteus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Sediminicola.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Sediminicola luteus"
                     /db_xref="taxon:319238"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112010
     Region          25..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkllsflv fvsmlssgta faqnktvsgt vsdesgmplp gvsivvkgqt kgtstdfdgn
       61 ftledvassd vlvfsfigfa dkevavggqs ninvtlseda ealdevvvta lgvrketkal
      121 gysltevgge eiatvkqtna inslqgkiag vnitqnstga agssrviirg assfgnnqpl
      181 yvidgipmgn dtngsagmwg gsdggdgiss lnpddiesis vlkggaatal ygsrggngvi
      241 vvttksgkdk qgfgvefsss vtfdmidnsi qdfqteygqg rrgavpanqe daldigtsaw
      301 gprldgsnvi qydgqsrpys ytgnnldkfy rtgttfinsl afsnagenst lrfsasdltn
      361 edivpnagln rksfslnssh kmmdkltldi nakyiredvk nrprlsdspg nanfsvallp
      421 pnvdvrdlqp gadedgmerg fsnniystnp yfaaynfrnq dytnriitsa alrydindwl
      481 ylfgragidh strkstsvtp ygtayqregs mnenerrytq vdadimfgvt rdltdklavd
      541 affganknsi esenlnlsgg rfivpgledi sntrdqgrsr syskrkigsl ygsvelswdr
      601 wayltitgrn dwfstlsypg ketpnddfyp svsgsvvlse vvdlpetinf lklrggysqv
      661 aggadqayql alnytifgqg hlgqslgrid ngsipnanlv awnkdefeig ldlrmlnnrl
      721 sfdlayynne ssnqivnvaa sptsgyggat anigvianng fewlisatpi rnenfswtts
      781 ingsynnsei kstndvdgei glgqartrnv eikqivgesf gvikgrafqr dgqgrivyei
      841 dgdgvplaqe adewqilgeg vpplnmgwtn tfnykdfsls flidgkfggq ifagtnaity
      901 gnglhketln gregglqvtg vtadgaeftt tvapedlqty ygrindfaep fvedadfikf
      961 rqftlgynvp sryleniflk svnvsvigqn lfylmrkvdn inpeaaynng naqgleyfgv
     1021 pptrnfgfal nvkf
//
LOCUS       WP_097461840             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mangrovitalea sediminis].
ACCESSION   WP_097461840
VERSION     WP_097461840.1
KEYWORDS    RefSeq.
SOURCE      Mangrovitalea sediminis
  ORGANISM  Mangrovitalea sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Mangrovitalea.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Mangrovitalea sediminis"
                     /db_xref="taxon:1982043"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41736
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mivgipkeif sdearvavip sgvadlvkkg fdvvvqagag drshigddef raagaslaad
       61 akslyeqadl vlkvrvpted vengyheadl iregaslicm mdayysldvv qklaarkvrs
      121 falefiprit raqsmdvlss maaisgyrgv lagamslpqy fpmlmtaagt itpakvfiig
      181 agvaglmais tarrlgavve aydtrsaare qveslgakfv efdlpaqddk atggyakaqs
      241 eefyrrqreq maqkvaqsnl ivttalipgr eapklitadm lhlmkkgsvi vdlaaerggn
      301 vegtvrnekv ykdgvtiigy cdhpsrvpvh asqlysknit tflynmskdg elelnledei
      361 vsstmltadg dvvhaalker lqpqeagn
//
LOCUS       WP_097467847             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097467847
VERSION     WP_097467847.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53618
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knsedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc tdchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097475961             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097475961
VERSION     WP_097475961.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53515
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw aagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097476823             460 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097476823
VERSION     WP_097476823.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..460
                     /gene="nrfA"
     Protein         1..460
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51338
     Region          4..460
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtftsvhaeq taapakpvtv eaknetfapq hpdqylswka tseqservda laedprlvil
       61 wagypfsrdy nkprghafav tdvretlrtg apknaedgpl pmacwscksp dvarliqkdg
      121 edgyfhgkwa rggpeivnnl gcadchntas pefakgkpel tlsrpyaara meaigkpfek
      181 agrfdqqsmv cgqchveyyf dgknkavkfp wddgmkvenm eqyydkiafs dwtnslsktp
      241 mlkaqhpeye twtagihgkn nvtcidchmp kvqnaegkly tdhkignpfd nfaqtcanch
      301 tqdkaalqkv vaerkqsind lkikvedqlv hahfeakaal dagateaemk piqddirhaq
      361 wrwdlaiash gihmhapeeg lrmlgtamdk aadartklar llatkgithe iqipdistke
      421 kaqqaiglnm eqikaekqdf iktvipqwee qarkngllsq
//
LOCUS       WP_097444368             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097444368
VERSION     WP_097444368.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53626
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta appkpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwv gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097486280             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097486280
VERSION     WP_097486280.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53532
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgkttv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqwdeqa rkngllsq
//
LOCUS       WP_097492981             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097492981
VERSION     WP_097492981.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53556
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdapa edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097490443             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097490443
VERSION     WP_097490443.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53514
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wglaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097508268             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097508268
VERSION     WP_097508268.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53572
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvlpqweeqa rkngllsq
//
LOCUS       WP_097486055             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097486055
VERSION     WP_097486055.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53583
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqpindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheie ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097531052             546 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tannerella
            forsythia].
ACCESSION   WP_097531052
VERSION     WP_097531052.1
KEYWORDS    RefSeq.
SOURCE      Tannerella forsythia
  ORGANISM  Tannerella forsythia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Tannerella.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Tannerella forsythia"
                     /db_xref="taxon:28112"
     Protein         1..546
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=61455
     Region          <3..545
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfnntyetnn irdyqienti nydktlfedk lklnvllghs fqrwdyedsy vqgekfpsdd
       61 lrwlvsagei nkgrsyiksm alesyftrlq lnwgdkyhlm asirrdassk fndknrtgyf
      121 paisagwtvs neeffnvsfv sdlklrasyg ytgnqsgvsy asgqnligag qnydlqpgla
      181 ttdiynpdlt wekgrsanig fdinlfsrvn vsfdyydkkt esllnrinvp qetgfktmla
      241 nvgnisnkgf eisfdanivd rrdfkwnaga nfsynknkvl sigteagrys tgfvsiiqeg
      301 eslgsfslye akgvakekfe ykdkdgkvtk tvlpgdmiyv dqnqdgkidd kdkkvfsggi
      361 apvygglftr lnykgfdlsi sghysigkki yafykkdaln ggavgapsys nnmykeilsy
      421 wtpentstmi prphmaaeis awntehssrf lenadylris ditlgydlks ikalkfgfin
      481 slrvyvqarn wftftkystg dpetsyvdqs aensqdksdg mkvqagvdlg gipntksfvv
      541 glnisf
//
LOCUS       WP_097531053            1022 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tannerella
            forsythia].
ACCESSION   WP_097531053
VERSION     WP_097531053.1
KEYWORDS    RefSeq.
SOURCE      Tannerella forsythia
  ORGANISM  Tannerella forsythia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Tannerella.
REFERENCE   1  (residues 1 to 1022)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1022)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1022)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1022
                     /organism="Tannerella forsythia"
                     /db_xref="taxon:28112"
     Protein         1..1022
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111863
     Region          23..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgvpvsilha ekfagvtvit qqkeikgtvk drsgepiiga nvyvkgttng vvtgvdgdfs
       61 iqvsssdilv isfigfknve vpvkdqlvih vslaedsell devvvtalgi krekkalgya
      121 mqeikteglt enrsvsvanm lqgkvagvqi nqsatgvggs trvvlrgtts lsgnnqplwv
      181 vdgipisddv nqkadqwggr daeggasein pediesisvl kganaaamyg sraqngaiiv
      241 ttkkgqsgdl rieyngnltf saaydafkyq ntygqgsagk ydpaavggsw gpkmegqmvq
      301 nwrktlygqv dapdyalesq gnyidkfyrt gvnytnsiia sggtekmqsr fsftdsrneg
      361 itpnhslnrq yydlssqwss ryidlsakvn fmrqkalnrp rlgeygvmqq fvfmprnvrl
      421 qdledciinn nvanwsgtst tifnpyalvk pengakeqrn rllgkvqava kitdylrltg
      481 rvgldwynde stsqtsynyt itetgyhkgm inyeefnadl ilnfdkhfgd fsvlanfgaa
      541 ttsrklssln gssgyytlpg laalangnnq ttsenyskkr vnsvlgnati gyksmayldv
      601 tarndwsstl padnrsyfyp svslsgilse mfhlpepvsy wkvrgswaqv gndtepyklv
      661 ntyelnktng niinanssst fplfdlkpen ttswelgtel rvfnnrlgld ltyyssnttn
      721 qilsvtmpgs sgyttklina gkmtskgwei mltgtpvltk dfswdvtlnw gqnrtecvel
      781 adgltqfvig etrmgkvvar egsrygdivs taykrdangn iivneksglp qkesnqvlgn
      841 mtpdwtgsfa slltwkgfsl nalidvnygg sflsatssya dfygnserag qrdnasadfp
      901 tghiivdgvn engkknttki gleeyyqglg gsyglgeahl ysktyvklre vaigytlpka
      961 wlsglpvssv kisavgrdlf ylykkapmnp efafsradya qafeyaampp trtlgfslnv
     1021 kf
//
LOCUS       WP_097531088            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tannerella
            forsythia].
ACCESSION   WP_097531088
VERSION     WP_097531088.1
KEYWORDS    RefSeq.
SOURCE      Tannerella forsythia
  ORGANISM  Tannerella forsythia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Tannerella.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Tannerella forsythia"
                     /db_xref="taxon:28112"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116222
     Region          24..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrklklfla lffigagavm aqaqvrgtvt dengepviga svvvkgttvg tvtdmdgkfa
       61 lpevpssakt lmisyigmvt qevaiapnlq vvlkgdtral eevvvtamgv trekkalgya
      121 atsikgdeia nakavnpmna lqgkvagvdi stapgpgatq nviirgassf gnnqplyivd
      181 gipitnaqnr sgnnlnsqvd fgsginalnp ddiadmtvlk gaaatalygs raangvimit
      241 tksgkntegk vqivydggyt isrvgrlpee qsqfgqgwsg nraldengnw gapydgkerv
      301 wgriieneqq vkpyvflknr vrdfydlgqn yknslslsgg taktnyflsl sqnssdgvvp
      361 tdhdsykryt iaargshqak nltvsssvnf stektkavps gqgtslhrsl yeiasdisiv
      421 dfkdykskfn nldnyftpyg lnpyyvlned gatqnkhkvf gkfqldyevi kglnftyrfg
      481 gdlevstses htapvkftpg apndgsstan agryeewrre rvqinhdama tyktkwesgl
      541 slnaiaglnv nerkynwlsg ainsidvpgf ynlrnsrsps vsnqrkeqrr lvglylnadl
      601 gykdfaylml tarndwsstl pqnnnsyfyp gatfsflitd flqsrdiktr fvnfakfrva
      661 ygmtgndadi yyvydryvaa tiqnpgypkv ddlsfplngv nsysvsnqlg npelkpeltk
      721 efeiglearf fenrlgfdfs yydrytegli dvipkdpssg ytsqisnlgd vrnrgfeltv
      781 nvtpvkikdf swdiswnyst nknkvenldv devflggfgg agiyavkgep lgqfkltgvk
      841 katidgkeyt ivdgkgnpqp tatteyfgkd inekyrmglt ntftwkglsl fatfdyrngg
      901 yiysntkkym hwtgsapetv lndrkpfmvp nsvidngdgt yrentipvdp talhtfysdr
      961 gglmgqqsav isrsylklrd agiayripvg fcsklhlasa risfnvsnil lwtprenpyi
     1021 dpetttfgnd vsakfgefna npsnqlytfg ltlaf
//
LOCUS       WP_097531441            1141 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tannerella
            forsythia].
ACCESSION   WP_097531441
VERSION     WP_097531441.1
KEYWORDS    RefSeq.
SOURCE      Tannerella forsythia
  ORGANISM  Tannerella forsythia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Tannerella.
REFERENCE   1  (residues 1 to 1141)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1141)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1141)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1141
                     /organism="Tannerella forsythia"
                     /db_xref="taxon:28112"
     Protein         1..1141
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124877
     Region          29..1139
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkklfear glltlllcis tlslsaqtit vrgtvtdrnn epltgatvvv egstsqgtvt
       61 didgnytlag vsskaslefs yvgmkvqkia vngqttinvt leedsevlge vvvtalgvtk
      121 qarsvgyatt kvstseieri nvinpinalq gkvagvnint agasgvtsss sitirgaksi
      181 dknnspifvi dgmiiqepik galdgtdwgs qlknlnpsdy esvtvlkgaa atalygsrga
      241 ngaivivskg gkygkqglgv eisqtlettd iykspikfqn iygagtpnng yeggfladgs
      301 lqktsisfgp rmdgslvdqy mpngektpfv phpnnwksly qsglnsttnv aingggekss
      361 frlsysytdn ngvfkrnefk rhsvafkglt dlnqifsiev gvnyafsqaq nganqggwnw
      421 ggnlgmmsty ytprnmdmka yesmyrnpen havetnspwe tlrgylhdrd mnlyqrsens
      481 llsnltlrak iaswltaslk anynyygwty lvnkygtgan ygptgsgeyg regetsgsyn
      541 flgmlqstnn kiqignqefv ldaivagely gdigknwwkk ftaggldvpg ifafsnskns
      601 iipefsynsk gtnrtfglsa ivnlswkeql yleltgrndw lstltypiym eagmnnysvf
      661 ypsvnlswvf tetfempkwf sfgkfrasia qvgmgtipya ttngygvfeq kaqldaqrgs
      721 vlnavpkigt awnkdlkpei qqsielgadl rffderlnld fayyktntrn qilkvpavle
      781 sgaseqlina gniqnqgvei slegtplrtk dfrwtigsnf tlnrgkiiel hpnvkewqlm
      841 gqydggpeiw ayeggrfgvi ttpygsgtga alyrfnnkkd pndprngkpv ityigsygkp
      901 nsvpaygyvt nidkgikdrv eigkveadfl lsintsfsyk nfdvyalidg rvggnffsnt
      961 ykyassrgtl esslygrdqe hgglprvnyk getvydgypl dgvfdegvka plasdpskti
     1021 dvsgltykea lekgirpmpa gmyymanlgw gmpaelglqe ntwfalrevt lgyrlpehic
     1081 kkiganyfrv gltarnlgyl inklkdglnp asissnnplq pidiggvpfa rtyalnltir
     1141 f
//
LOCUS       WP_097537904             382 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Sinorhizobium].
ACCESSION   WP_097537904
VERSION     WP_097537904.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39378
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msqivfiake sdsdeprvag svesvkklks lgfdvvveag agsrsrvpde efekagarig
       61 saadagsadv ilkvrrptae eiggyksgai viaimdpygn dtaiaamaea gltafamelm
      121 pritraqsmd vlssqanlag yqavvdaahe ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg amvsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskdyqa
      241 kqaalvaehi akqdivvtta lipgrpaprl vtrqmldsmk pgsvvvdlav erggnvegae
      301 agrvveiggv kvvghlnvpg riaasaslly aknlvtflet mvskeekala vdmedelvka
      361 talthggavv hpafggangg dk
//
LOCUS       WP_097531550             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tannerella
            forsythia].
ACCESSION   WP_097531550
VERSION     WP_097531550.1
KEYWORDS    RefSeq.
SOURCE      Tannerella forsythia
  ORGANISM  Tannerella forsythia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Tannerella.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Tannerella forsythia"
                     /db_xref="taxon:28112"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111386
     Region          30..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkrkslklm kwamfiwlwt fpvsvfaqqi tvrgnvkdvk gepligvsvl isgtslgtit
       61 dvdgnftlnn vasdgklhvs yvgmqsetip vnnrtvievv mkediaalhe vvvvgygtqe
      121 rrnltsavtt vtskdflqga annplqmidg kipgvtisny aisdpnrnpm dnfqvrgsts
      181 fkggsaplvv vdgmpgadlr qianqdiesi tvlkdgsaaa iygsraangv llittkkgka
      241 gkasisydty iehdrvyrkp dvlsaeeflq nkrdedrgar tnwydelirk nnfghthhis
      301 lsgggenaiy risadykdkn aidiasarre ygvranfnht tlegllniig nlsyrttked
      361 ytdynafsqa vklnptipvm dpkdpgkytf lkgydtwnpv drlknrdnfg kndystidft
      421 arlnilsnln telkvarqgr flkryewyps thqesisnsr kgrarleser wedytlewit
      481 nyyttiqdvh niklmggysy qefnwekyga enmdfpsdal kynnlgtgqw ntkegrlgmw
      541 sekekeknia flgrlnydyk dvlllmaslr yegsskfgkd hkwglfpals aawrlsslpi
      601 fqqteivddl klrlsygetg rssfpryrsl slysgfgkyl drngqwiqvw gpgnnsnasl
      661 hwekqisynl gvdyallgqr lsgsldfflr kgndliyeyd vsvppylhdk mytnvistst
      721 rgvelmlnyn aiqtktfnyt tnlnvswakt qidswsndef kgedrdvydl pspgnpgraq
      781 ilgegmeigt frggryagvn ekgeimiwke givggekkla sqkndkdrvp lghgmprwem
      841 swghtvtykn fdlslffrgk fdykilnlyq myygltaqpk vnlirdaytr naeikgekqi
      901 vdyflengdy fkldnitlgy tpkvnckyis nlriyatarn vftltkysgi dpagvnivgl
      961 epgignldvy psttnlsfgi qisy
//
LOCUS       WP_097540200             525 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Sinorhizobium].
ACCESSION   WP_097540200
VERSION     WP_097540200.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium
  ORGANISM  Sinorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Sinorhizobium"
                     /db_xref="taxon:28105"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55476
     Region          4..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mvvigvlkes leresrvamt pesaiqvqkl ghsvvieaga gkaagfsdsa yraagvtvld
       61 iveelfaaad vvakvrpper sefaqlrcgq tlisffypaq nkelleqard kgvnvlamdm
      121 vprisraqkm dalssmania gyravieagn nfgrfftgqv taagkvppak vlvigagvag
      181 laaigvatsl gaqtyafdvr pevaeqiesm gaefvyldfd gaqqdgavtg gyaapsspef
      241 rekqlakfre lapeidivis talipgrdap klwladmvaa mkagsvvvdl aaerggncdl
      301 tvpdqkivsp ngvtiigytd fpsrmaaqss alyatnirhm ladltpgkdg kivhnmeddv
      361 ircstvafeg aitypppppk iaaiatqtrq kkvkeptpee kratesaafk aqtksqlsll
      421 avgtgllllv gafaptafms hfvvfvlacf vgfqviwnvs hslhtplmav tnavsgivil
      481 gallqigsgn wlvvllaals vliatinivg gflvtrrmla mfqks
//
LOCUS       WP_097545357             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            anhuiense].
ACCESSION   WP_097545357
VERSION     WP_097545357.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium anhuiense
  ORGANISM  Rhizobium anhuiense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium anhuiense"
                     /db_xref="taxon:1184720"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55506
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mfigsprerf egearvamtp dsatqlqklg yhcaietgag klagfsdday ravgvtvvds
       61 idalyasvdv iaqvrppean dlarlsaskt lisffypaqn kelleqaktt ganvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsislg aityafdvrp evaeqiesmg aefvfldfke qqqdgaatgg yaspsspefr
      241 eaqlkkfrei apdidivvst alipgrdapk lwladmvaam kpgsvvvdla aerggncdlt
      301 vpdqkivsen gvtvigytdf psrmasqast lystnirhmm tdltpkkdgv lvhnmeddvi
      361 rgatvafqge itypppppki qaiaarkrqe kpkeltpeer raaeasafks atrqqvgllv
      421 vggvlmalig ayapsafmgh fivfalscfv gfqviwgvsh slhtplmavt naisgiiiig
      481 allqvtaggw lvtalaavsv aiatinivgg fmvtqrmlnm fqks
//
LOCUS       WP_097553391            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            branchiophilum].
ACCESSION   WP_097553391
VERSION     WP_097553391.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium branchiophilum
  ORGANISM  Flavobacterium branchiophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Flavobacterium branchiophilum"
                     /db_xref="taxon:55197"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117250
     Region          25..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwiyt lllalamqfs faqektvtgv vsdatgalpg anvtlkstkk gvqtdldgkf
       61 sikasqgdal iisyagfetk tvqigaasny nvklqenakv ledvvvvgqs qskdkkklty
      121 qvsslsskei egkpqadvir slqgkvsgvq itntggmags tsnfvfrgvk sftgssqplf
      181 iidgvpfdts ksditgsfnq ggasssnrfl dldpsnieni sflkglaasv tygsagrngv
      241 vlittkggkk kqkmkvdyms svyfsevanl peytnkyggg sdltigtgti gnwgaafdss
      301 vlashvydqp hlnasfpeyi gvktpwvaap nnvkdffrkg lgtqhslsls ggtenvvynf
      361 ngsytdedgi vannnvtkyn fggkfgfdis dkfkinssft ffntqyttpp vsaangagai
      421 svfsrliylp rnydlmnlpy qnpvtgasvy yrndlenprw llnnskltqn vdrffgviep
      481 kyalsskidv kyrlgfdryt dsqdfyvnrg avttpynlgy lrsiaginti idqnlifthk
      541 tikisedftl dpllgvsarr dsytqkgiss qgqiqfgatd hsyfssqvnn dvfagdldip
      601 lqwtnllgay atldfsykny ltfnlsgrnd wgsmietntr slfypsasfa flpsnlftel
      661 kdlhidflkl rgayatsagf pqlyrsrnfn efnsniytnt ssipgvssqr rlgnpnlkpe
      721 lhkefevgae lemfkrrvkl dvsmyfrqsk nqivsraldp gtgytsitdn agridnkgie
      781 anltvipfkt ddfewdvtgi fyrnvskvve lpagqeriti sgfsngisna aivgepygvl
      841 fgsyaltdan gnflinpgdg tiisstdvgl pnkvigdpnp dytlsvnntf nykgfnlsil
      901 meftkggdfy sntienllrr gvtrdtengr eqshiipgyy anpnngaill dannnqipnn
      961 iqisannvyf lntldaesqn vydatrlrlr elsfgyvfpa kyfkntglsg lsinfvgsnl
     1021 wlkafnipky tnvdpdlist gqgnglgldf qtapqsrrfg mnikinf
//
LOCUS       WP_097553583            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            branchiophilum].
ACCESSION   WP_097553583
VERSION     WP_097553583.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium branchiophilum
  ORGANISM  Flavobacterium branchiophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Flavobacterium branchiophilum"
                     /db_xref="taxon:55197"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118616
     Region          25..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklklkgila lflvlitqlt faqdrtvsgv vsdasglpip tanvkvkgtt ngvqtdfdgk
       61 ykikanasdv lvfsyvgmka qevkatstti nvklasdane lnqvvvtamg ikrekkslgy
      121 atqtvssedl nrpnaanfts nlagkvsglq ikagsnfggs vdvvlrgyrs itgdnqalfv
      181 vdgvpminnn nntadqrlsg rpgydfgnti sdinpndiae vnvlkgaaat alygsraqng
      241 aiiittkrgk ktndlgiefs ssiatatidk ttfaeyqdky gqgygyyyga aanaqfsnyn
      301 pttgavddsv ndqlmaptte dgsygapfnp nlnvwqytsf ipesanygka tpwinakngp
      361 vtffqtgyal tnnlsfskan dvssfrlsym nsnttdvlpn sslkknsftg nasyklsdkl
      421 tanfygtyvv qntlgrnstg yngnimsnfr qwwatnvdiq eqrdlynatg knytwniqsp
      481 tdlrpaywdn pyfqryenya tddrnrfagn gslnyefnkh fnitlrvgtd gynqrmedrk
      541 avssnpelmg fgltsiaqps gyavmnikaq etnydilasy ktdlstnvnl savvggnint
      601 lyrytnsqst sgglfipnly tisnsasspa lpsitettkt irgifaqtni gfyntyyldg
      661 tirrdessal pkgnndyiyy sgsvsaiisn wsflkefkpl nfakvrasya evgsdtganq
      721 lqnqyfteta vnsplyyynt taknanlkpq rskqtefgin lqfmknrfgl dfawfkndaf
      781 dqilnlpvsf atgslnqvkn vgnlsttgle vslnlnpint enfkwdinvn wsnpvtkvte
      841 lapgvenitl gsfqggvsin asvnelygti kgtdfiytng qrtvgangry litsstnnvi
      901 gnmqakwfgg linkftyknm tlgvqvdwre ggsvfsldqy yglatglype tavnndlgnp
      961 irnslatggg vilpgvyang tvnstrvsgt nyglygyrya pasnfvydas fvklrevsft
     1021 yafpskslak sikglsmsii gnnlwiihkn lpyadpeagl ssgnvqgyqs gvmpstrnvs
     1081 fnvkinl
//
LOCUS       WP_097553603            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            branchiophilum].
ACCESSION   WP_097553603
VERSION     WP_097553603.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium branchiophilum
  ORGANISM  Flavobacterium branchiophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Flavobacterium branchiophilum"
                     /db_xref="taxon:55197"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112535
     Region          27..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtifrklli lslllpfsvl aqnvlngtvl dkkskqpipg vnvvvqgssk gvstdfdgnf
       61 klpnvkkgdk ivfsfigykn tivayeaqvs lqvmleedan elkevvvqtg ygavkkkdat
      121 gsvtlvtskd fnkgaivsvd qllagkaagv ritnsggapd adpnirirgg aslsaenkpl
      181 iiidgvaisn dnpagvsnpl slinpndies fsilkdasat aiygirasng viiittkkgs
      241 sgaaqfnyss nisvgnvtkk vdvmtgadya rfigeyfpsr vnslgiqdps nptkrilydt
      301 dwqdqifrts istdhnfsar anlykkipfr asigynrteg liktsdyqrf nysikltpkl
      361 wddhlkvdin akgtltdkna vdeggaiaga inmdptkpvl dpysnkfggy yqntilngny
      421 drldgssnpl alleqrtrpe rvirilanae leykmhflpe lraivnfgid asrskiveqy
      481 tnnaiasyqf nqnnsnhntn yvfnpgvnyv enqsvtnksm dsyfaytkal ngfvtkvdaq
      541 agyayqdfri dgtkelyryn tttglresyv dnvanptnry fsptnlqsff grgnidilnk
      601 ylftatmrad atsyfkkenr wgyfpavgia wkvkeesflk dlsfvqdlki rlgwgktgqn
      661 sisgivgyfp srplfvvgts asqylpginl ysakaynadl twektttyna gidfeffkkg
      721 ivsgsfdiyk rettdllsqy tlppgqgltd qfignvgste gkgfelnlni klvqqdqlni
      781 gingnvayny tkvtdlngvs qvnspnggip tgtgayiafn apgqqahsaw vyqqlydang
      841 aaiigayadl ngdhqidnnd ryykamrpnw tfgfgtsiny kkwdlsanfr gqiggqtydt
      901 rqitngfieh atigtsqaln nvlnfyngsa nmllnnlnqn maysdymlqd atflrcdnia
      961 lgykfakfik ssslrvygav nnafivtkyk gqdpenfnai dtnfyprprt ytfglsldf
//
LOCUS       WP_097559233            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tannerella
            forsythia].
ACCESSION   WP_097559233
VERSION     WP_097559233.1
KEYWORDS    RefSeq.
SOURCE      Tannerella forsythia
  ORGANISM  Tannerella forsythia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Tannerella.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Tannerella forsythia"
                     /db_xref="taxon:28112"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124736
     Region          23..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkgflyvfl cfilstaada anrvvtgvvl agddnqplvg vsiqvpsdel kkagissntl
       61 gtitdvngnf sisvpdevrr lvftyigyqe eslllqdgrn dyrivlqsgt hmladvvvtg
      121 yqtverrrlt aavskidvse avigaaksid qalagqiagv svtnttgspg aparirirgt
      181 aslngtqdpl wvmdgmpleg tdiprisssn dndiinmgqt aiagispndi esitilkdaa
      241 ataiygaraa ngvivittkr grsgkpvinf ntrltympnl ntsrlnllrs eekvdlelel
      301 mkepddevff spvpvyatkg gvaailtryn lleayrkngw ngltpeaqqa innlktvhtd
      361 wndilyrdaf tqeynlslsg gaekityyns lgymkengnv pavsmdrfnl tsktdyrlsk
      421 vlklgfslfv nrrknntfvt dtygfsnpny ysrianpyfa pfsadsryly dydiatgntr
      481 dlkqgfnife eranssdevt ttainsifda elrfgdhwkl ssqvgvqweq yeqqryvgqe
      541 tfsmrnarin shywdnaskt nkyllpeggm hkttdrtmsq imwktlgeyk ntfadshdvq
      601 amigseirkn rydnhsvngy gynprtlttk plifrdeaqa rayplytkny qenafasffa
      661 ngsyslmkry ilgasvrmdg sdlfgvdkky rylpiysvsg lwrlsneafl qsydridnla
      721 lrlsyglqgn idkntspfli gryenisilp gvteenitis dapnsklrwe ktasynlgvd
      781 fsaieqrinl sidyyyrkgt dligtrmlpl engftsmsin wasmenrgie vnlqtrnimt
      841 kdfswytsfn faynrnkvlr qmvpdnqttp glegypvgai falevksidp qtgriyianp
      901 egkavtleel ygasdptgtg fyefkttpvq ertfykyigs sdapytgglm ntftyhnwel
      961 svnfayhlga yvrtspsyki vgqdpghnvn rdilerwspa nptgtlpall trktfpadys
     1021 lidnrgdiyr nlsiwvkkqn yirlqnirla yrmpavflhp lhisgatlal egrnllvfgs
     1081 syknymdpes mgnlyatpip ksitfnfnld f
//
LOCUS       WP_097559727            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tannerella
            forsythia].
ACCESSION   WP_097559727
VERSION     WP_097559727.1
KEYWORDS    RefSeq.
SOURCE      Tannerella forsythia
  ORGANISM  Tannerella forsythia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Tannerella.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Tannerella forsythia"
                     /db_xref="taxon:28112"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114130
     Region          29..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkklfear glltlllcis tlslsaqtit vrgtvtdrnn epltgatvvv egstsqgtvt
       61 didgnytlag vnskaslefs yvgmkvqkia vngrttinvt leedsevlge vvvtalgikr
      121 dkkalgyaiq evkgddivsa rennianals gkisglqvik ssngpgassk ivirgnnsvt
      181 nlnqplivvd gvpidnftga dnndywnpta dlgnglgdin pediesmtvl kggsaaalyg
      241 sragngvili ttksgrkaeg lgitisssvs terafiqpkl qntfgqgsng ayneesgssw
      301 gakiegqeyt kwdgskgtmq aydnvasyfn kpglnlteni sfsqqynnvs vftslnrldd
      361 ksripganls rtnltarais kfgndkwtld tkvqyiktna enrpvsgnnn rnpfltiynl
      421 prsldirdfs npldevgkmv wyvkssamnp ywlskyqlnh dirervimlg llkyeftdwl
      481 naeikggtdm yftefenkty gkspltatgr ygfgeekffe nnfsillsaq kdnifskwgg
      541 aatlggnlme qkktgvhanp dellvpdlft fgnaknklea krifshrkin slygtaqiny
      601 ggyffidgtf rndwsstlhp dnrsffypsi stslvisdmi neegkgmpvw fdfakirasf
      661 aqvgndldpy qlyntywigk dpennatagt ngtlfdssvr selisswevg telrlfdnrl
      721 gldfawyktn arrqllnlpm dpfsgfgdkk inagniqntg ielmvnvrpv qtrdfawniq
      781 anisknsnti keliddvkly qlggydnlkv yatvggnyge iygttfkrvt dknsphfgki
      841 ivdgdglpig dseikkvgdq qasalagvtn slafkgfsfs flidsriggd ifsatnhtlq
      901 asgasdvtap gglretfvvd gvvddgkgny tvndkavtpq nywgrvtgat gnlgiseani
      961 ydatnirlrn iqlnydfaks mlkntpfqkv rlgvsvnnvw mimshlngid pesvfatstn
     1021 avgfegyapp tsrsylfnvt fgf
//
LOCUS       WP_097560763            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tannerella
            forsythia].
ACCESSION   WP_097560763
VERSION     WP_097560763.1
KEYWORDS    RefSeq.
SOURCE      Tannerella forsythia
  ORGANISM  Tannerella forsythia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Tannerella.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Tannerella forsythia"
                     /db_xref="taxon:28112"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113542
     Region          31..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mirkctmgrk mklllsvlll svgvamaqtr itgnvtdekg epvigasilv kgtdqgtvtd
       61 ldgnfslsvs sssgknylii symgmktqev eakpnlaivl kedatalgev eitaefgmkr
      121 varavgssvq nvkasdiies grdnfisalq grvagmtvss sggapgasnt vvlrsltsis
      181 gnnqplyvvd gipmnnstfd ptsvgggfsp rnldfasrgn dfnpediesm tvlkgaaaaa
      241 lygsdasnga iiittkkgrk gkgrvaysnt frwdkaygyp diqtkyangs ygttnyfytk
      301 hfgglypegm plydnfnsvl qtgfsnkhni sveagsdkat lragasylnq tgvikttdys
      361 rfnlslsgka eitswlkfeg smqysstqnt kvprgvdgpl flamkwplvd nmseylaadg
      421 ahmrypryyt dtdllnplfg lyknkfydes drfisnasvt itpiknaffr aqvgwdvgmq
      481 tfetskhpyy yktnngdgty vltksnfsdp tlnllagynd kylddkftfs vqfgyhqlqn
      541 gitrlstngs kfiipdfqsi nncepatvss tkrttkrriq alstqaefgy dnmafltfra
      601 rndwsstlpk annsyfypav egafiltelp flkenkminy lkirgsvarv gkdagpleid
      661 pqleatkltg ggfkygftgp nkklkpemtt sreigfegrf wddrivadft yfathcsdqi
      721 vkgfrlsyat gfvlnnmnvg tfdtwgwdsh vdvdiirgad nlrwnmgvnl shasskvvsl
      781 penvseyynw mtwssgnirn gimmghpitt ltgkayqrnk agqvlidptt glpmvdskws
      841 vlgdrepklr fgitsslsyk gfrlsamfsg rykatvvngt krsmmqngts wesvdlrerg
      901 pvifngvlkd gkensdnptk ntiavdystf gssvynggde dwleknvhyl rlselrlmyr
      961 ipsqwlrktk visdasihlt gndlftwtny sgidavgntv saaaggtgge gydvwsipnp
     1021 rgmsigfnlt fn
//
LOCUS       WP_097574486             431 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sanjuanii].
ACCESSION   WP_097574486
VERSION     WP_097574486.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sanjuanii
  ORGANISM  Mesorhizobium sanjuanii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Mesorhizobium sanjuanii"
                     /db_xref="taxon:2037900"
     Protein         1..431
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44196
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
     Region          <398..428
                     /region_name="COG1754"
                     /note="Uncharacterized C-terminal domain of topoisomerase
                     IA [Function unknown]"
                     /db_xref="CDD:441360"
ORIGIN      
        1 mgqmvfipre ldaneprvaa spdtvkrlag lgldvtvesg agtasripde efakagaaig
       61 kaadaakadv vlkvrrptda elkgyrsgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgevvttang vkivghlnvp grvaasasll yarnlfafle tlvdkttkql ainrddelvk
      361 atmltdggkv vhaafakatl dphvepaaip attmvadasv kkaaprktad kkaaagksta
      421 qksaakpkgi a
//
LOCUS       WP_097567523             309 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Enterobacteriaceae].
ACCESSION   WP_097567523
VERSION     WP_097567523.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35521
     Region          5..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifdlfskr qkrlrgevpd vyqytnlpnn frvqvihivk etigedygrg sdpgdiykvi
       61 ndtlcreygv fklrdypksn feavydffln ekdiekcldv ielsfkvidg yvrenhwrfh
      121 gheqkcdsai eelnirfkes gigfqfesge lvrvdsqfih sdavkpalqi lgrskafega
      181 ndeflsaheh yrhqrfkecl ndclksfesl mkaihkkrsw eygstdtakk lissclsngl
      241 vpdymqnqfs slrillesgv ptirnkeggh gqgdevtnvp ehlasytlhl tasnllflak
      301 cdenftkkk
//
LOCUS       WP_097580417             385 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium].
ACCESSION   WP_097580417
VERSION     WP_097580417.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39306
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare iageetrvaa saetvkkmks fgfdvvveag agtasripdg efeaagarig
       61 sfadaasadl vlkvrrpneq eissyksgaa viaimdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemsadyqg
      241 kqaalvaehi akqdivitta lipgraaprl vsramlasmk pgavavdlav erggniegvv
      301 agevadvdgv kvigfanmpg rvaasasaly aknlvtflet mvnketgsvv vnlddelvka
      361 tmltfagdvv hpafggakkg ttdgq
//
LOCUS       WP_097581364             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. H4].
ACCESSION   WP_097581364
VERSION     WP_097581364.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. H4
  ORGANISM  Rhizobium sp. H4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. H4"
                     /db_xref="taxon:2035449"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55165
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligsprerl egearvamtp dsatqlqklg yqcaietgag klagfsdday raagvtvvds
       61 aetlfasadv iakvrppess evarlssgkt lisffypaqn kdlldqakst ganviamdmv
      121 prisraqkmd alssmaniag yralieagnn fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsvslg aityafdvrp evaeqiesmg aefvfldfde qqqdgaatgg yaapsspefr
      241 aaqlkkfrei aadidivitt alipgrdapk lwladmvatm kpgsvvvdla aerggncdlt
      301 vpdqkiisdn gvtiigytdf psrmaaqsst lystnirhmm tdltpnkdgv ivhnmeddvi
      361 rgatialmge itypppppki qaiaaqkpke kpkeltpeek kaaeaagfks atrnqvgllv
      421 vggllmllig afappvfmgh fivfalacfv gfqviwgvsh slhtplmait naisgiiiig
      481 avlqitaggw lvtalaaisv aiatinivgg fmvtrrmlnm fqks
//
LOCUS       WP_097586816             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium fredii].
ACCESSION   WP_097586816
VERSION     WP_097586816.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium fredii (Rhizobium fredii)
  ORGANISM  Sinorhizobium fredii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium fredii"
                     /db_xref="taxon:380"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39268
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msqivfitke sdpseprvag svesvkklks lgfdvvveag aghgsrvpda efekagarig
       61 saadaksadv ilkvrrpttv emagyrsgai viaimdpygn deaiaamaga gltafamelm
      121 pritraqsmd vlssqanlag yqavidaahe ydralpmmmt aagtvpaaki fvmgagvagl
      181 qaiatarrlg amvtatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskdyqa
      241 kqaalvaehi akqdivvtta lipgrpaprl vtramldamk pgsvvvdlav erggnvegae
      301 agkvveaggv kivghlnvpg riaasaslly aknlvtflet mvsketkala lnmedelvka
      361 talthggavv hpafggangg dk
//
LOCUS       WP_097590222             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. J15].
ACCESSION   WP_097590222
VERSION     WP_097590222.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. J15
  ORGANISM  Rhizobium sp. J15
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium sp. J15"
                     /db_xref="taxon:2035450"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39047
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgniifvare vtdgetrvaa saetvkkmkg fgfdvvvetg agaasripda efeaagarig
       61 sfadaasadv vlkvrrpsps eiagyksgav viaimdpysn deaiaalaga glsafamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvsslg akfiavedee fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vsramlasmk pgavavdlav erggniegav
      301 agevadvegv qvigfanmpg rvaasasaly aknlvtflet mvnkesksvv vnlddelvka
      361 tmltyagdvv hpafggakkg dm
//
LOCUS       WP_097592123             311 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Rhizobium sp. J15].
ACCESSION   WP_097592123
VERSION     WP_097592123.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. J15
  ORGANISM  Rhizobium sp. J15
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Rhizobium sp. J15"
                     /db_xref="taxon:2035450"
     Protein         1..311
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35029
     Region          5..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mavyelyskr qqrlsgaepd vyrydvipqk lrvqiihild kalgsredad ssrgriehty
       61 rlivstirqe lgvfrlppas regnpytelr dfflgateae tcldvielaf raidrltrti
      121 dysntrgyne radeaiddln irfkqnavgy qyidgeivrv dselihaeav kpalrllntk
      181 eyagphqefl sayehyregk nkealndclk afestmkaic dkrgwtykpg dtakalidvl
      241 yaeglvppfw qthfgalral lessiptgrn kqsghgqgat ptavpdhmaa ymlhmtastl
      301 vflttaeqsl p
//
LOCUS       WP_097593404             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. J15].
ACCESSION   WP_097593404
VERSION     WP_097593404.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. J15
  ORGANISM  Rhizobium sp. J15
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rhizobium sp. J15"
                     /db_xref="taxon:2035450"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55265
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalrerl dgearvaltp dsasqlmklg hdifvetgag lmagisdeay rnagvavvps
       61 pqalaaaaev ivkvrpptde eiallspekt lisffhpaan kellerarhs gstvvamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqit aagkvppakv lvigagvagl
      181 aaigtsvslg aitfafdvrp evaeqiesmg aqfvyldfde qhdgavtggy aapsspefrq
      241 kqlskfrela pdmdivitta llpgrdapil wladmvaamk pgsvivdlaa erggnceltv
      301 adqkvvsdng vniigytdfp srmaaqsssl ystnirhmia dltpgkdgvi vhnmdddvir
      361 gatvtfrgdi tfpppppkvq aiaaqkpkek akeltreekr aaemasfrsa trtqvgllla
      421 ggfltalvga yappafmahf ivfvlacfvg fqviwgvsha lhtplmaitn aisgiivlga
      481 llqmgspgwl vpllgsvsvl iatinivggf mvtrrmlmmf qks
//
LOCUS       WP_097593601             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. J15].
ACCESSION   WP_097593601
VERSION     WP_097593601.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. J15
  ORGANISM  Rhizobium sp. J15
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rhizobium sp. J15"
                     /db_xref="taxon:2035450"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55213
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligalkeiw egearvavtp esalqlrklg yecvvetgag eaagfsddty raagvvvvet
       61 atalyeaada ivkvrppets evqrlragqt lisffypaqn aelleearar ganviamdmv
      121 prisraqkmd alssmaniag yravieagsn fgrfftgqvt aagkmppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfde qqdgaatggy aapsspefre
      241 kqlqkfrela peidivitta lipgrdapkl wladmvammk pgsvivdlaa erggncdltv
      301 adsrvvsdng vivigytdfp srmaaqastl yannirhmma dltpakdgvi vhnmeddvir
      361 gatvtfagai typppppkiq aiaaqkpkek akeptleekr aaetaafrvq tknqgmllas
      421 gtallllaga fapasfmshf ivfvlacfvg fqviwnvshs lhtplmavtn avsgivilga
      481 llqigsgsal vttlaalsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_097593617             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. J15].
ACCESSION   WP_097593617
VERSION     WP_097593617.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. J15
  ORGANISM  Rhizobium sp. J15
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. J15"
                     /db_xref="taxon:2035450"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55826
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeih adekrvaltp esalhlqklg yeclvetgag ltsgvsdday rtagvailpt
       61 aqdlwqaadv vvkvrppqqe elalltqgkt ilsfvhpaqn vdllekacmr qinliamdmv
      121 prisraqkmd alssmaniag yravieagns fgrfftgqvt aagkvapakv lvigagvagl
      181 aaigtstalg aityafdvrp evaeqiesmg aqfvfldfan eqqdgaasgg yatpsspefl
      241 naqlskfrel apqidivist alipgrdapr lwladmvatm kpgsvivdla aerggnceft
      301 iadqklvtan gvtiigytdf psrmaeqast lysnnirhlm tdltpnrdgr lvhnmeddvi
      361 rgatvthegr ityppppprv qaiaaqkpre rsrelspeek rsqeliafrk qtkaqallla
      421 ggtmllllvg amapasfmgh ftvfvlacfi gfqviwnvsh slhtplmavt navsgivivg
      481 allqigssng iviglaaisi lvatinivgg flvtqrmlsm frks
//
LOCUS       WP_097595174             382 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium].
ACCESSION   WP_097595174
VERSION     WP_097595174.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38984
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare tegeetrvaa saetvkkmks fgfdvvveag agaasripdg efeaagarig
       61 sfadaasadv vlkvcrpsgs eisgyksgav viaimdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaagv ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgraaprl vsramlagmk sgavavdlav erggniegvv
      301 ageiadvegv rvigfanmpg rvaasasaly aknlvtflet mvnketsrvv vnlddelvka
      361 tmltyagdvv hpafggakkg di
//
LOCUS       WP_097595893             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            anhuiense].
ACCESSION   WP_097595893
VERSION     WP_097595893.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium anhuiense
  ORGANISM  Rhizobium anhuiense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rhizobium anhuiense"
                     /db_xref="taxon:1184720"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55218
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigslketv eqearvaltp dsarqliklg heclvesgag aksgfsdeay rsagavvvqd
       61 aaelsaasdv lvkvrppqpe eldrlaagqt lisffhpsqn gpllqqavek gvntiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvpparv lvigagvagl
      181 aaigtatslg aitlafdvrp evaeqiasmg aefvyldfee qqdgsatggy aapslpefre
      241 rqlakfrela pevdivitta lipgrdapkl wladmvaamk pgcvivdlaa erggncdltr
      301 aderviadng vivigytdfp srmaaqsssl yamnirhmla dltpgkdgll vhnmdddvir
      361 gatvafnggl tfpppppkiq aiaaqkprek akeptaeerr akeiaafkaq tksqgfllvg
      421 gtaflfilga fapasfmshf vvfalacfvg fqviwnvshs lhtplmavtn avsgivilga
      481 llqvgssdwl vttlaaisva iatinivggf lvtrrmlamf qrs
//
LOCUS       WP_097597220             382 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium].
ACCESSION   WP_097597220
VERSION     WP_097597220.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39048
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare ttegetrvaa saetvkkmkg fgfdvvveag agaasripda efeavgarig
       61 sfadaasadv vlkvrrpsps eiagyksgav viaimdpygn deaiaalasa glstfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vsramlssmk pgavavdlav erggniegvv
      301 agevadvdgv svigfanmpg rvaasasaly aknlvtflet mvnketkavv vnlddelvka
      361 tmltyagdvv hpafggakkg dm
//
LOCUS       WP_097599405             311 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Rhizobium sp. L9].
ACCESSION   WP_097599405
VERSION     WP_097599405.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. L9
  ORGANISM  Rhizobium sp. L9
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Rhizobium sp. L9"
                     /db_xref="taxon:1340738"
     Protein         1..311
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34990
     Region          5..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mavyelysrr qqrlsgaepd vyrydviper lrvqiihild ralgsredaa ssrgqventy
       61 rlivstlrqe lgvfllppsn regnpytelr dfflgassae tcldvielaf ravdrltrti
      121 dysntrgyne radeaiddln irfkenavgy qyidgeivrv dselihaeav kpalrllntk
      181 dyagphqefl sayehyregk nkealndclk afestmkaic dkrgwtykpg dtakplidvi
      241 yanglvppfw qnqfaslrgl lessipparn kqsghgqgav pttvpnhmaa ymlhmtastl
      301 vflttaeqsl p
//
LOCUS       WP_097600929             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium].
ACCESSION   WP_097600929
VERSION     WP_097600929.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55386
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalrerl dgearvaltp dsasqlsklg heaivetgag lmsgisdeay rqvgvtvves
       61 pqacaeaadv ivkvrpptdd evallspekt lisffypasn ggllerarts gatfiamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqit aagkvppakv liigagvagl
      181 aaigasvslg aityafdvrp evaeqiesmg aqfvyldfde qqidgaatgg yaapsspefr
      241 qkqlskfrel apdidivitt allpgrdapi lwladmvaam rpgsvivdla aerggncelt
      301 vvdqkvvsdn gvtiigytdf psrmaaqsss lystnirhmi adltpckdgv ivhnmdddvi
      361 rgatvtfrgd itfpppppkv qaiaaqkpke ktreltteek raaemasfrs atrtqvgllf
      421 aggllmslvg ayappafmah fivfvlacfv gfqviwgvsh alhtplmait naisgiivlg
      481 allqigspgw lvpllgslsv liatinivgg fmvtrrmlmm fqks
//
LOCUS       WP_097603583             527 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            phaseoli].
ACCESSION   WP_097603583
VERSION     WP_097603583.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium phaseoli
  ORGANISM  Rhizobium phaseoli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Rhizobium phaseoli"
                     /db_xref="taxon:396"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55758
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkely vdekrvaltp esalqlqklg hqclveagag lasglsdeay raagvevvat
       61 aqdlwqaadi ivkvrppqqe eltplpsgkt ilsfvhpaqn adllesarvr kvnliamdmv
      121 prisraqkmd alssmaniag yravieagns fgrfftgqvt aagkvapakv lvigagvagl
      181 aaigtstalg aityafdvrp evaeqiesmg aefvfldfad qqqdgaasgg yatpsspefr
      241 gaqlskfrel apqidivist alipgrdapr lwladmvaam kpgsvivdla aerggncelt
      301 iadqkvvtpn gvtiigytdf psrmaeqast lysnnirhli adltpskngc lvhdmeddvi
      361 rgatvthegk ityppppprv qaiaaqkpre karepspeek rsqelaafrr qtrdqgllla
      421 ggtallllvg amapasfmeh fvvfvlacfi gfqviwnvsh slhtplmavt navsgivivg
      481 almqigsgns ivigraavav lvatvnivgg flvtrrmlsm frkssss
//
LOCUS       WP_097603907             381 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Rhizobium].
ACCESSION   WP_097603907
VERSION     WP_097603907.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38918
     Region          4..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare nagetrvaas petvkkmksf gfdvvveaga gaasripdge feaagarigs
       61 fadaasadvv lkvrrpneee issyksgaav iaimdpygnd eaiaalasag lsafamelmp
      121 ritraqsmdv lssqanlagy qavieaaavy drampmmmta agtvpaakvf vmgagvaglq
      181 aiatarrlga avsatdvrpa akeqvaslga kfiaveddef kaaetaggya kemsadyqgk
      241 qaalvaehia kqdivittal ipgraaprlv sramlasmkp gavavdlave rggniegvva
      301 gevadvdgvk vigfanmpgr vaasasalya knlvtfletm vnketgsviv nlddelvkat
      361 mltyagdvvh pafggakkgd n
//
LOCUS       WP_097607308             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. M10].
ACCESSION   WP_097607308
VERSION     WP_097607308.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. M10
  ORGANISM  Rhizobium sp. M10
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. M10"
                     /db_xref="taxon:1324586"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55192
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligsprerl egearvamtp dsatqlqklg yqcaietgag kpagfsdday raagvtvvds
       61 aetlfasadv iakvrppess dvarlssgkt lisffypaqn kdlldqakst ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsvslg aityafdvrp evaeqiesmg aefvfldfde qqqdgaaagg yaapsspefr
      241 aaqlkkfrei atdidivitt alipgrdapk lwladmvatm kpgsvivdla aerggncdlt
      301 vpdqkivsdn gvtiigytdf psrmaaqast lystnirhmm tdltpnkdgv ivhnmeddvi
      361 rgatialkge itypppppki qaiaaqkpke kpkeltpeek kaaeaagfrs atrnqvgfli
      421 iggllmllig afappvfmgh fivfalacfv gfqviwgvsh slhtplmait naisgiiiig
      481 avlqitaggw lvtalaaisv aiatinivgg fmvtrrmlnm fqks
//
LOCUS       WP_097613390             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            chutanense].
ACCESSION   WP_097613390
VERSION     WP_097613390.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium chutanense
  ORGANISM  Rhizobium chutanense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium chutanense"
                     /db_xref="taxon:2035448"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39129
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare iageetrvaa saetvkkmks fgfdvvveag agaasripda efeavgarig
       61 sfadaaaadv vlkvrrpsps eisgyksgav viaimdpygn deaiaalasa gvsafamelm
      121 pritraqsmd vlssqanlag yqavieaagv ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vsramlssmk pgavavdlav erggniegvv
      301 ageiadvegv rvigfanmpg rvaasasaly aknlvtflet mvnketktvv vnlddelvka
      361 tmltyagdvv hpafggakkg dm
//
LOCUS       WP_097618208             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. L43].
ACCESSION   WP_097618208
VERSION     WP_097618208.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. L43
  ORGANISM  Rhizobium sp. L43
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium sp. L43"
                     /db_xref="taxon:2035452"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39043
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare iageetrvaa saetvkkmks fgfdvvveag agaasripdg efeaagarvg
       61 sfadaasadv vlkvrrpsps eiagyrsgav viaimdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaagv ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgraaprl vsramlaamk pgavavdlav erggniegvv
      301 ageiadvegv rvigfanmpg rvaasasaly aknlvtflet mvnketktiv anlddelvka
      361 tmltyagdvv hpafggakkg dm
//
LOCUS       WP_097615749             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            chutanense].
ACCESSION   WP_097615749
VERSION     WP_097615749.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium chutanense
  ORGANISM  Rhizobium chutanense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium chutanense"
                     /db_xref="taxon:2035448"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55263
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligtpretr egearvgmtp dtaqalqklg hgcaietgag nragfsdday raagvtivpd
       61 aatlytvadv iakvrppepa everlragqt lisffypgqn gellelarsk gvnviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigvatslg aqtyafdvrp evaeqiesmg aefvyldfag dqqdgaatgg yaapsspefr
      241 ekqlarfrel apqidivitt alipgrdapk lwladmvaam nsgsvivdla aerggncdlt
      301 vadqrvvsdn gviiigytdf psrmaaqsst lyatnirhmi adltpgkdgk ivhnmeddvi
      361 rgatvtfdga itypppppki aaiavqkpke kvkeptpeek raaeaatfka qtrsqfafla
      421 igtallllvg afapssfmnh fvvfvlacfv gfqviwnvsh slhtplmavt navsgivvlg
      481 allqigsgnw lvmvlaalsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_097620187             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. L43].
ACCESSION   WP_097620187
VERSION     WP_097620187.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. L43
  ORGANISM  Rhizobium sp. L43
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. L43"
                     /db_xref="taxon:2035452"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55507
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mfigsprerl dgearvamtp dsatqlqklg yqcavetgag klagfsdday raagvtvvds
       61 vdalyasvdv iaqvrppeps diarlssskt lisyfypaqn kelleqaktt ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkippakv lvigagvagl
      181 aavgtsvslg aityafdvrp evaeqiesmg aefvfldfke rqqdgaatgg yaspsspefr
      241 eaqlkkfrei apdidivvst alipgrdapk lwladmvaam kpgsvivdla aerggncdrt
      301 vpdqkivsen gvtvigytdf psrmasqast lystnirhmm adltpkkdgv lvhnmeddvi
      361 rgatvafqge itypppppki qaiaaqkrqe kpkeltpeer raaeasafks atrqqvgllv
      421 iggvlmalig ayapsafmgh fivfalscfv gfqviwgvsh slhtplmavt naisgiiiig
      481 allqvtaggw lvtalaavsv aiatinivgg fmvtrrmlnm fqks
//
LOCUS       WP_097643469             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Viridilinea mediisalina].
ACCESSION   WP_097643469
VERSION     WP_097643469.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Viridilinea mediisalina
  ORGANISM  Candidatus Viridilinea mediisalina
            Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales;
            Chloroflexineae; Oscillochloridaceae; Candidatus Viridilinea.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Candidatus Viridilinea mediisalina"
                     /db_xref="taxon:2024553"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40975
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,98,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mivgvpreta pgeqrvalvp ndvsflqklg levqieagag vaagfpdafy vergvtvaas
       61 rqglfaaadm lfqvratgaa qgdadlallr sgqlvigfld pfwqpqwiaa laqrgvnaia
      121 lelvprisra qsmdalssma tivgykatll aamhlprifp mlmtaagtit parifvigag
      181 vaglqacaqa krmgarveay dvrvavkeqv esvgakfvel pletgdsedk ggyakaqged
      241 fyrrqrqlmg evvarndvvi ttaaipgkrs pvlvtgemvq gmqpgsvvvd laaehggnce
      301 ltradelvqv hgvtilgptn laatvpnhas qlysrnlini irlavkdgkl nlttddeiir
      361 esmvahagev cnarvqelle aksavtts
//
LOCUS       WP_097628716             382 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium].
ACCESSION   WP_097628716
VERSION     WP_097628716.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38938
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare iageetrvaa saetvkkmks fgfdvvveag agaasrvpdg efeaagarig
       61 ssadaasadv vlkvrrptaq eisgyksgav viaimdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgraaprl vsramlaamk pgavavdlav erggniegvv
      301 ageiadvdgv kvigfanmpg rvaasasaly aknlvtflet mvnkegrsvv vnlddelvka
      361 tmltyagdvv hpafggakkg dl
//
LOCUS       WP_097651640             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Chloroploca asiatica].
ACCESSION   WP_097651640
VERSION     WP_097651640.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Chloroploca asiatica
  ORGANISM  Candidatus Chloroploca asiatica
            Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales;
            Chloroflexineae; Oscillochloridaceae; Candidatus Chloroploca.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Candidatus Chloroploca asiatica"
                     /db_xref="taxon:1506545"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40819
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mivgipaelv sgedrvaivp advpalmkmg lqvvveagag mragfpdaay vergartvas
       61 rtevyaqadi vlkvraagad pghadkeram lrpqqlliaf leplweprla aslaergvta
      121 iamelipris raqsmdalss matvagykav liaaasmprm fpmlmtaagt vtparvfvig
      181 agvaglqaca takrlgarve aydvraavke qvesvgakfv elpleagsse dkggyakalg
      241 ddfyqrqrkl maevvarndl vittaaipgk pspvlitaem vagmqpgsli vdlaaerggn
      301 caltrsdqii vahnvtiigp gnlpatvpnh asqlysrnli nllrlmvkdg kltvnmddei
      361 irestvvhdg kvvsarindl igagtpvass
//
LOCUS       WP_097659816             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. Y36].
ACCESSION   WP_097659816
VERSION     WP_097659816.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. Y36
  ORGANISM  Bradyrhizobium sp. Y36
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium sp. Y36"
                     /db_xref="taxon:2035447"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39215
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag lksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneaa lktiadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa dmvksmkpgs vlvdlaverg gnvegakage
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_097666269             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. M1].
ACCESSION   WP_097666269
VERSION     WP_097666269.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. M1
  ORGANISM  Rhizobium sp. M1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. M1"
                     /db_xref="taxon:2035453"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55462
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigatkeva knearvaltp eaalqlkklg ygcvieagag rqagfsdeay raadvtivat
       61 atevyetadv likvrppeaa eldrlgsgkt lisffypgqn nalleqarss ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aiayafdvrp evaeqiesmg aefvyldfde vqqdgaasgg yaapsspefr
      241 ekqlakfrkl apeidivitt alipgrdapk lwladmvamm kpgsvvvdla aerggncelt
      301 vadervvsdn gvivigytdf psrmaaqast lyatnirhml adltpgkdgq lvhnmeddvi
      361 rgatvtyqge itypppppki qaiaaqkpre kpkeltpeer rakeaaafka qtkkqgvlla
      421 agaallllvg ayapatfmnh fvvfvlscfi gfqviwnvsh slhtplmavt navsgiviig
      481 aflqigsghw lvvvlaalsl liatinivgg flvtrrmiam fqks
//
LOCUS       WP_097666768             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. M1].
ACCESSION   WP_097666768
VERSION     WP_097666768.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. M1
  ORGANISM  Rhizobium sp. M1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. M1"
                     /db_xref="taxon:2035453"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55174
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligsprerl egearvamtp dsatqlqklg yqcaietgag kpagfsdday raagvtvvds
       61 aetlfasadv iakvrppess dvarlssgkt lisffypaqn kdlldqakst ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsvslg aityafdvrp evaeqiesmg aefvfldfde qqqdgaatgg yaapsspefr
      241 aaqlkkfrei atdidivitt alipgrdapk lwladmvatm kpgsvivdla aerggncdlt
      301 vpdqkivsdn gvtiigytdf psrmaaqast lystnirhmm tdltpnkdgv ivhnmeddvi
      361 rgatialkge itypppppki qaiaaqkpke kpkeltpeek kaaeaagfrs atrnqvglli
      421 vggllmllig afappvfmgh fivfalacfv gfqviwgvsh slhtplmait naisgiiiig
      481 avlqitaggw lvtalaaisv aiatinivgg fmvtrrmlnm fqks
//
LOCUS       WP_097677765             932 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            congonensis].
ACCESSION   WP_097677765
VERSION     WP_097677765.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides congonensis
  ORGANISM  Bacteroides congonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Bacteroides congonensis"
                     /db_xref="taxon:1871006"
     Protein         1..932
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103078
     Region          4..930
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhfsqaitla naqplkivmg edtqtldevv vtalgikrat kalsynvqev kgdeitavkd
       61 anfmnslagk vagvqissga tgaggaarvv mrgmksltkd nnalyvidgv pifntgksgg
      121 eglfgdmggs davadlnpdd iasismmtgp saaalygssa angvvlittk kgqtekttit
      181 vsnsttfska yimpdmqnry gtssglfswg eltdrrydps nffetgtnvi nsvalstgns
      241 knqtylsast tnsggilpnn synrynftar nttnflndrl tldigaqyii qnnknmvsqg
      301 qyynplpaly lfprgdnfde irlyeryntn ygymeqywpy gdaslslqnp ywvqnriirt
      361 sdkkrymlna slkwkvtdwi nivgrvnldn sdyrnkneks astlttfcgv sggfedamrq
      421 erslyadvla nidktfgdfh ltanvgasiy htsmdqlyfa gdlvipnffq vnninfssny
      481 kpdptgykde iqsifasael swknqlyltl tgrndwdskl afskqksffy psvglsalls
      541 emvelpelit yakvrgsytv vassfdrflt npgyeynsqt hnwanptvyp menmkpektk
      601 sweiglnlkf wenrfsldat yyrsntlnqt fkvdipsssg ykqaivqagd vqnqgielal
      661 gfsdkwagfg wssnatftln rnkvkrlasg svnpvtgeai qmdemnvgwl gkenvaprvi
      721 lteggsmtdi yvynqltkdn ngnikvdqng nlgitssntp vkvgnldadf nlgwinhfty
      781 kgidlgvvls arvgglaysa tqgildyygv sevsasvrdn ggtpinngkv daqkyyqtis
      841 tgeggygryy lysatnvrlq elslnytlpr kwfknvanvt lgvvgrnlwm iyckapfdpe
      901 lsastssnyy mnvdyfmqps lrnfgfnvkv qf
//
LOCUS       WP_097697500             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097697500
VERSION     WP_097697500.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53559
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea kketfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097715440             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097715440
VERSION     WP_097715440.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53560
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqstndlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097735543             234 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Escherichia coli].
ACCESSION   WP_097735543
VERSION     WP_097735543.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>234
                     /product="STM4504/CBY_0614 family protein"
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndt
//
LOCUS       WP_097742487             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097742487
VERSION     WP_097742487.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53607
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta tpakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag cfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqe rkngllsq
//
LOCUS       WP_097749256             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Enterobacteriaceae].
ACCESSION   WP_097749256
VERSION     WP_097749256.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53519
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa ckngllsq
//
LOCUS       WP_097749964             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097749964
VERSION     WP_097749964.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53590
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipyff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntsspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqwdeqa rkngllsq
//
LOCUS       WP_097755264             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097755264
VERSION     WP_097755264.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53602
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartkltrll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097760348             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_097760348
VERSION     WP_097760348.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53586
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq ekaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_097802866             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pelagimonas varians].
ACCESSION   WP_097802866
VERSION     WP_097802866.1
KEYWORDS    RefSeq.
SOURCE      Pelagimonas varians
  ORGANISM  Pelagimonas varians
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Pelagimonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Pelagimonas varians"
                     /db_xref="taxon:696760"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54770
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpleve agenrvamtp dsarqlqklg ydcvieagag akagfsdady taagvevvtg
       61 adalwsasdi iakvripqea elgrltadkt litffnpggn eagleqakat ggsviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yaavsspefr
      241 eaqlakfrel apevdivitt alipnrpapk lwtadmiaam kpgsvivdla aekggnaegt
      301 vmdekvvten gvtiigytdf psrmaaqast lystnirhmm tdltpekdgq inhnmeddvi
      361 rgatvahaga itfpppppkv aaiaakpkev vpeltpeekr aaetaafkaq tknqvtllav
      421 ggalllavgl vapasfmqhf ivfvlsvfig fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgswl viilaslsif maginifggf lvtrrmlamf qks
//
LOCUS       WP_097788346             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            beimenensis].
ACCESSION   WP_097788346
VERSION     WP_097788346.1
KEYWORDS    RefSeq.
SOURCE      Halomonas beimenensis
  ORGANISM  Halomonas beimenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas beimenensis"
                     /db_xref="taxon:475662"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55157
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkera pgearvaltp esaqqiqklg heclveagag eaagfddaay rdagvtvveg
       61 akalwdaadv vvkvrepsee eagylrrdqt lisffwpaqn eallercrdt ganviamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgsgtggy aapsspefre
      241 kqlalfreqa pdvdivitta lipgrpapkl wledmvkamk pgsvivdlaa ekggncdltv
      301 pderivtdng vivvgytdfp srmatqasll yatnirhmls dlspekdgti dhnmdddvir
      361 gatvtyqgdi tfpppppkvq aiaaakpkpk epeptpeekk aaehaafvaq tkrqatllgv
      421 ggalmlllgq vapasfmqhf ivfalacfvg fqviwgvshs lhtplmavtn aisgiivlga
      481 vlqigsgsal vgllaaisvl iatinivggf qvtrrmlamf qks
//
LOCUS       WP_097827613             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acidipropionibacterium jensenii].
ACCESSION   WP_097827613
VERSION     WP_097827613.1
KEYWORDS    RefSeq.
SOURCE      Acidipropionibacterium jensenii
  ORGANISM  Acidipropionibacterium jensenii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Acidipropionibacterium.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Acidipropionibacterium jensenii"
                     /db_xref="taxon:1749"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53549
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresl agenrvaatp vtvprlvtlg ydvtvergag erasfpdaay eeagstlgsg
       61 gdawgadlvl avnpptdqei almhsgtvlv tflaprqdta ltdklaaagi tgmsmdmvpr
      121 israqsmdal ssmanisgyr avveaafayg rtfggqvtaa gkvppakvfv igtgvaglaa
      181 lgaansmgae vfatdvrpet aeqvesmgar flhvrtaqtd qgvssdgyak etsddynara
      241 aelymeqakv cdviittaai pgrtspklit aemvaamkpg siivdlaalg ggncvlthpg
      301 ekyvtdngvt iigytdlasr lagqssqlyg tnlvnlvkla tpekdgqfvi dfedevirtm
      361 tvcrdgevtf ppppvqvaaa papvakapae pvkvekqprp wtqtyamvgg lailliallt
      421 fapsyflglf gtfavavvvg yyvvwnvsha lhtplmsvtn avsgiimvga itqlgseswt
      481 iriiaavtvl iasinvfggf lvtarmlkmf rka
//
LOCUS       WP_097927709             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Bacillus toyonensis].
ACCESSION   WP_097927709
VERSION     WP_097927709.1
KEYWORDS    RefSeq.
SOURCE      Bacillus toyonensis
  ORGANISM  Bacillus toyonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Bacillus toyonensis"
                     /db_xref="taxon:155322"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34854
     Region          3..163
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
     Region          <252..290
                     /region_name="Abi_C"
                     /note="Abortive infection C-terminus; pfam14355"
                     /db_xref="CDD:433897"
ORIGIN      
        1 myetfskrek krmgqvkdvy iydkipdrlr vqvihiwgqa igesdftwgt inqimskelg
       61 efnlteenck pkkhcidfll sckdiyaidi ielsfcilke qyekgaisid pflldllkig
      121 qsfdeaikel nhwfkdnsig yefingeiir idqtymheev vkpainllfe edfegaaeef
      181 lnahkayrkd dyktalveal ksfestmkti cdkrnltynk asdtarklit ilfenniipg
      241 ylnnhftslr ttlesglptv rnkqaghgqg sesvkvdpyf veyainlaat niillvkayk
      301 esk
//
LOCUS       WP_097928669             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Monaibacterium marinum].
ACCESSION   WP_097928669
VERSION     WP_097928669.1
KEYWORDS    RefSeq.
SOURCE      Monaibacterium marinum
  ORGANISM  Monaibacterium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Monaibacterium.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Monaibacterium marinum"
                     /db_xref="taxon:1690039"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54469
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaiketw pgearvamtp qsvvalaklg htcvieagag aaarfndady taagaevvad
       61 aaavyaaadv iskvrapada eighiragqt iisfiwpaqn pelletlqgk gatviamdmv
      121 prisraqkmd alssmanigg yravveasnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigaatsmg aityafdvrp evaeqiesmg aefvyldfde eqtdgaetgg yaapsspefr
      241 ekqlakfrel apevdivitt alipgrdapi lwtkdmveam kpgsvivdla aerggncelt
      301 venekiesan gvtiigytdl psrmatqsst lyatnirhmm ddltpandgv ivqnmeddvi
      361 rgatvvhdna itfpppppkt kaiaaakpka pektpeekaa eeaaaarksg qmqmatligg
      421 gllvlllggv apasfmshfi vfvlacfigy qviwsvtaal htplmavtna issiiiigam
      481 lqigsgegwa vvlaaiavli asinivggfm vtrrmlamfq ks
//
LOCUS       WP_097933827             286 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Mycolicibacterium diernhoferi].
ACCESSION   WP_097933827
VERSION     WP_097933827.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium diernhoferi (Mycobacterium diernhoferi)
  ORGANISM  Mycolicibacterium diernhoferi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Mycolicibacterium diernhoferi"
                     /db_xref="taxon:1801"
     Protein         1..>286
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..>286
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgipresl pgetrvaatp qsvgqiiklg ytvvvesgag aassfsdaay veagatigsp
       61 wnadvvlkvn apddseiaav rdgatvvgli spalrpdlve klssrpitvl amdavprisr
      121 aqsldvlssm aniagyravv eaahafgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivka tdprpevadq vaslggeyvs vdpaaaevsa tgyakemddd ykareaalya
      241 elaadvdiii ttalipgrpa priitaemva smkpgsvivd maaang
//
LOCUS       WP_097934266             248 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Mycolicibacterium diernhoferi].
ACCESSION   WP_097934266
VERSION     WP_097934266.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium diernhoferi (Mycobacterium diernhoferi)
  ORGANISM  Mycolicibacterium diernhoferi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Mycolicibacterium diernhoferi"
                     /db_xref="taxon:1801"
     Protein         <1..>248
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          <1..247
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 priitaemva smkpgsvivd maaanggnve gtvkdeailt dngvriigyt dlagrlpaqa
       61 sqlygtnlvn llklltpekd gvltldfddv vqrsitvvrd gqstwppppv qvsaapaaat
      121 aaaapvvkep kkpmstarrl gltfaaaaal fafiaispaa lqvhlvvfal aivigyyvig
      181 nvhhalhtpl msvtnaisgi ivvgallqig qgdtaitala fvaillasin vfggfavtrr
      241 mlamfsrs
//
LOCUS       WP_098000209             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium duvalii].
ACCESSION   WP_098000209
VERSION     WP_098000209.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium duvalii (Mycobacterium duvalii)
  ORGANISM  Mycolicibacterium duvalii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Mycolicibacterium duvalii"
                     /db_xref="taxon:39688"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52276
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigiprese lgetrvaatp qtvgqlvklg yhvlvesgag aaasfsdaay aeagadigst
       61 yqvlgadvvl kvnapspgei aglrdgatli slispalrpe lveqlatrpi tvlamdavpr
      121 israqsldvl ssmaniagyr avveaahtfg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaagslgai vratdprpev adqvkslgge ylavdpaqae vsatgyakem gedykareaa
      241 lyaeqckdvd iiittalipg kpapriitae mvasmtpgsv ivdmaaangg nvegtvkdea
      301 vvtdngvtil gytdlagrlp atasqlyatn lvnllklltp ekdglltldf edvvqrsvtv
      361 vrdgtvtwpp ppvqvsaapa aaaaaapveh kpakepmtra rklgltfaaa aavfaliaas
      421 paalqvhltv falaivigyy vignvhhalh tplmsvtnai sgiivvgall qighhdtvit
      481 alafgailva sinifggfav trrmlamfsr s
//
LOCUS       WP_097940318             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium agri].
ACCESSION   WP_097940318
VERSION     WP_097940318.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium agri (Mycobacterium agri)
  ORGANISM  Mycolicibacterium agri
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Mycolicibacterium agri"
                     /db_xref="taxon:36811"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52802
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgetrvaatp qtigqliklg yevvvesgag aassfsdeay tdagasvgsa
       61 eqvwgadvvl kvnapddaei aklrdgatli slispafkpe lveklatrpi tvlamdavpr
      121 israqsldvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igtagslgav vratdprpev adqvkslgge ylsiespeae vsatgyakem sddykareaq
      241 lyaeqakdvd iiittalipg kpapriitad mvasmkpgsv ivdmaaangg nvegtvkdel
      301 vvtdngvkii gytdlagrlp atasqlygtn lvnllklltp ekdgklmldw ddvvqrsvtv
      361 vrdgeitwpp ppvqvsaapa aaaatapkve epakkplttg rrlgltfaaa avlftlials
      421 psalqvhltv falaivigyy vignvhhalh tplmsvtnai sgiivvgall qighgpvivt
      481 vlatlatlla sinvfggfav trrmlamfsr s
//
LOCUS       WP_098028235            1009 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            cynodegmi].
ACCESSION   WP_098028235
VERSION     WP_098028235.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga cynodegmi
  ORGANISM  Capnocytophaga cynodegmi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Capnocytophaga cynodegmi"
                     /db_xref="taxon:28189"
     Protein         1..1009
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113136
     Region          30..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mehknktafk wllvvivlsl gignlfaqtk ivtgrvtdat givlpgvsvi ikntkkgvet
       61 dfygqfqiea qegdilvfsy lgmdtqekkv tstdsnfsiv lkesinqldd vvvvgygsak
      121 kistiagsiv kvegekltnk psasvldalq gkvaglsifs tsgepygmgs irlhgmgsty
      181 ggadnplfil dgspvskdvv vllnpsdfqs vsvlkdasat siygtraang vvyittksgk
      241 tresatvtis sqygfsslas rkffdgmmnp eeyasflvek gektreeade llkefpnkvr
      301 wdrvyfkdnv pdqqinisfm gggsntryya sggyyeqegl myrsgfkryt arfnlnsnin
      361 nwlktelsls sgyaeymqnp naggginsfy gslsvltppi yspvdengnr ydyipviglp
      421 hphylaennp slskntnftp qanititpiq nlilksqfgl qyfnvrseet llpsyverak
      481 reyffrgeaf asrtiverli ktftntaeyk wnvndsntlt fllgqeside nygfvsastq
      541 gqtsdkatll ihgdknkeig errseigyns ffgridyqlk dkyffdisar rdgssrfgan
      601 nqyanfwafg alwkigeenf lkkhswidnl dlkfsigtsg nsdvisdyas lalvrnnsyy
      661 kdktgyllsd pgnpdlqwqk qlkttigfnv alfkkislgv dfyerkttdm lghiyrpsfs
      721 gtigimengg sfrnrgvdvs fsanlfanek nkfyvtpfis lnynqekils lhegrpyiig
      781 esspvsqivg qpllyvypif khvnpetgrs ewyvpgedit qrvkddskvt ttfdehdlrq
      841 ntgikrnppf nggfglnagy kafslqmsfs fssgkymina dryytenpin ttlhpdnnqs
      901 rtifdnwkkp gdiarfpsye hgnlftqyds rliedasfir mkditlsytl peeaikqirf
      961 fkqirffgtg rnlltftkyt gldpefdvdi ssganpstkq ytfgievqf
//
LOCUS       WP_098028694            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            cynodegmi].
ACCESSION   WP_098028694
VERSION     WP_098028694.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga cynodegmi
  ORGANISM  Capnocytophaga cynodegmi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Capnocytophaga cynodegmi"
                     /db_xref="taxon:28189"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116651
     Region          24..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkekliwtvs ffflalqial aqektitgvv kdeqgeplpg itvtikgttk gvatdfdgny
       61 kikakvgdil hfigiglksv drlvsastsk fdvvmhlete eleevvvvay gtadkksltg
      121 svalvsaeki sqqqttdvak alegavagvt istesgqpgk eskirirgig sinasndpli
      181 vldgvpysge lssinnndie slsvlkdass salygargan gvviittkkg kkgalsvtld
      241 skvgfnsrgv peydvmtsps eyyetiwesi ynkaiytdgk tdaearalas sadegglyqs
      301 lgyniynvan dqivdpvtgk inpnasikys daanfnnwtk alfntqtrke hnltvtrgge
      361 kgtfyfslgy lgdegyslns sferystrfs yngellpwln vnastmisft eakkgtegga
      421 ysnpfgwtrn iapiypvyvh dadgnlvynk gervydfgei rngvnlgray ggstnpvatq
      481 dkdidsdiny ylnqtlgfdv slaknlifta tgnfygnfye ynyfktpigg agktyngige
      541 kqrvnsrtit ltqllkynkt fgnykadill ghesysriln rvageksnyv dpsntewnna
      601 akitelysyn hkhavdgyfg qlnlsygeky flsgslrrdg ssvfapenrw gtfwsagfsw
      661 rvdqekflkd vswldalklk vsygvqgndh lllpnsasrs wtpyltlyti tsdgnnpgls
      721 asykgrrevt weenanlnag ievslfqnrl sfdfdyfrkk tnnllfnlpv pettgfstep
      781 wnignmenkg iefsvvgtpi ktknvvwtln vnglhyknkv lslpekfake gitrnthqki
      841 fegggiydfy mvkwggvnpe ngdaqywiad gkggyelkps kdyesthskq kvgsaipdlq
      901 ggfgttlnvy gfdlgvnfsy klggkildse ysglmhigny gdnwhrdiln rwtptnrntd
      961 tprleaenqd inqsssrflt dasyialrni nvgynfspsv ledlkikklr vymaadnval
     1021 wskrkgldpr qsiagfnnda tyspirtvsa gllltl
//
LOCUS       WP_098028754             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            cynodegmi].
ACCESSION   WP_098028754
VERSION     WP_098028754.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga cynodegmi
  ORGANISM  Capnocytophaga cynodegmi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Capnocytophaga cynodegmi"
                     /db_xref="taxon:28189"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110555
     Region          27..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrekvltlfv flmgvfsysl laqtssvkgv vtdsegvplp gvsvvvknss rgistdfdgn
       61 feiraeqgdv lvfsslgfat qektvgkdks ktmkvilqee aqaieevvvv gygsgrkvgt
      121 ivgsvakvgg kelsqrpsgn avdalqgkva glqiftssge psalssirlh gvgslgssss
      181 plfvvdgvpv sqeavrslnq sdfesvsilk dasatsiygs raangvvyit tkrgktgkge
      241 imlstqygfs nlanreffdn mmnadelskf wvetgyrtqk qvdelrakyp sdtrwdetyf
      301 qkntptqqad lsisggtdkt ryyvsggyfk qkgimyrsgf erytfrsnvd trvndwmklg
      361 inasvnyydy itnaytsndp ngglsflapp fyspidekgq rydyipgwnr yhpeylaekn
      421 psnytglgvi ptgfieitpi knltfktqgg feftngiysf nrlpsyagdp kngiarrrss
      481 rdlrktltnt leykfdlskn hfmvllghev vsqddrsfqa egrkliddnl lllrhsttdk
      541 eitenrsfni tesifgriey dydrkyffdf slrrdgsskf spnnkygtfw avgamwkmkk
      601 ekflsdisai nnldlkfsag tsgnsaigdy thqaltsanq yggstswair aagnpnltwe
      661 nqakytlsvd aslfnrasls lefynrittd mlmdiptayt tgfssikqnv gklqnlglgm
      721 slsvdvyknk shkahfspyv tfsynrekvl eifqnreswy rsgygygyvv gqpvkffypv
      781 fkginsengn pewylpseni aeetrdearv ansfnserlt qntginryap inggfgfsaa
      841 ykalslqvdf sfsqgkylin ndryfsenpt sfqgynqskv vqdywkkpgd qsrfpkwgtr
      901 ftefdtrlle dasfirmknv tlaytlpnei lkqvgffnei rfyttgrnll twtkytgpdp
      961 eidsnralga npntrqyvfg vevkf
//
LOCUS       WP_098029375            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            cynodegmi].
ACCESSION   WP_098029375
VERSION     WP_098029375.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga cynodegmi
  ORGANISM  Capnocytophaga cynodegmi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Capnocytophaga cynodegmi"
                     /db_xref="taxon:28189"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114572
     Region          25..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkllmmfv lvmgvfthpl laqtrtvmgt vtdeagipls gvgimikntt qgvttdfdgk
       61 ysiqakqgdv lvfsyigfst qekvvksssn sltmnivlke dtqqlgevvv talgikrsek
      121 algyalqevd gskllesrda nvtnalsgkv sglqivkgag gmagsskiil rgqnsltgdn
      181 qplvvidgvp idnkasgaad iwgnsgmdmg nglqdinped iesvsvlkga saaalygsra
      241 gngvilittk sgkqqqglgi tisstiated ifvrpklqns faqgrdeiyd pkttlnwgpk
      301 iegqivtnwd nkqvkldtyd nignffrtgi tstqaitfqq qiektsvyas lnymdnssiv
      361 petelnrtsa tlrtstnlgk sdrwkldfki nyvntvannr piqglnqsnv yktlnifpqt
      421 ldirefnppi vnekqvwydt qtlpddnpww tlkynrnndv rnryisfasl syeftnwlkg
      481 evkggmdyyn tkmfhrkhsg slsvpkngfy segskefiek nlsflfiaqk ndllkdlsgs
      541 ltfggnlmsq qtsemsassg dlllpnifsl nngkekpvvn sllterkmns lygsaqigwk
      601 nslyldatfr ndwsstmsve nrsyfypsvs fsgvfsells lpewitfakl rasyaevgnd
      661 lephmlynsy svskdfwgtp tistkeilyd ssvrselvks yeagidlrff nnrlkldaav
      721 yqtnstrqll rlpmdetsgy kfriinagni enkgvevslg vgilnnpkgl nwdtsvnfsk
      781 nknkiidlyt dvnsydlltv deitvlaekd keygaiygsk irrvndvnsp hhgkmilnse
      841 glpqrdqval hylghqqpdf mlgvsnsfsw kgfnldflvd arvggkifsm trnlltgygm
      901 aaetapggar epfvvegvia nasggydvnt kevtpqrywg alaqnnigit eaniydatsv
      961 rlrtltlgyn inkkhlermh iqslkcsfta nnlwlihtdi pgidpesvsg tgtnvtalef
     1021 gappttrsft fnitigl
//
LOCUS       WP_098028817            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            cynodegmi].
ACCESSION   WP_098028817
VERSION     WP_098028817.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga cynodegmi
  ORGANISM  Capnocytophaga cynodegmi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Capnocytophaga cynodegmi"
                     /db_xref="taxon:28189"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123204
     Region          20..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkglvlffv lltavvwgqk dvtgvvkdqq gvpiigvnvv ikgtskgvst dfegnfvlsa
       61 kegnvlvfsa igyktqekkv mkngafisvv meedlmeige vvvtgyqtvd ptkvatsytk
      121 idiknferrg tpdvisgieg lsaslvlsnn pnnptgskef sirgvstlsg ssrplivldg
      181 fqyegkledi npyevesitl lkdaasasiy gakssngviv intykgkegk tqvrytsnlt
      241 fqdkrdldyv mnrvsssklv diqhqyaqsi dpyvknyrnl letndptasy nagttnrvyy
      301 lyglkkygyi tdqefnnqld llksydntkd ierlylqspi tnqqnisvsg gseafkyrts
      361 lncthstkdi knnetqrfif dfvsnlkfss kvnldfqmgl isnnnsykli edgqrilegs
      421 difhlssydr lfdangnsls vfkpkldvgt nsgglfggkd pyeierlvaa glldetyypa
      481 ldfgkyttke ndwtahiqgl lnvelteglv akiggqlrkk vekrsnmaar dswymkslin
      541 nttplsfsgd vkdltipyga rlregrgetl nylfrtqley kktfgehnlh lfagaeiqed
      601 kleltkvdrl gydpksniyi ntnykklqdd iedvyhpdrn iasgipfdeg fqetqnryva
      661 aysnftylyt dkyvvsgsir mdqsnlfgtd pkyrykpfws lagrwrlgee aflkdknmkl
      721 dlrvsygvng niankygpfd iaekgfeyra gnisalkien lkinnlrwer setanfgadl
      781 sffdnrlglv ldyyrknttd alaeiesdpt ygsnfidrnd aslinngyev mltsqnirsk
      841 dvlwetqlff rynkskvtqa sfntnkgkay kyagqvlnik dsepnslyvf dyggvsdtgd
      901 aqirkadgsl vkvqnnyqap nlfnyddlkp agtvlpkyva sinnnfsykg irlsflflyq
      961 gghimlkdsy ngspignyiv linkdteraw qkpgdesftd ipklnsviys siikgstknv
     1021 lpadfirlrd vvlsytlpts llgnlkikel tlnmragnlw lwtknkegid petqglgvrt
     1081 aripksytmg inlif
//
LOCUS       WP_098029427            1139 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            cynodegmi].
ACCESSION   WP_098029427
VERSION     WP_098029427.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga cynodegmi
  ORGANISM  Capnocytophaga cynodegmi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1139)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1139)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Capnocytophaga cynodegmi"
                     /db_xref="taxon:28189"
     Protein         1..1139
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125498
     Region          23..1135
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrvlcllv llvvsfplfa qvktvtgtvt deagsplpgv svliqgtkkg tstdfdgnyt
       61 lqvneggvle fsyigfttqt kkvtgagnsl kinvvmkeea qqlgevvvta lgikretkkl
      121 gyamtemkge elakvntvnp vsalqgesag vsigssdggl fgnakiqvrg vsslnsnnnq
      181 pifvidgvil enntsgasad wesnandfgn ilknlnpddy ksvsvlkgaa atalygsrgi
      241 ngvvlietkn gsgakglgvs vkhslgvdhv yatpelqtey gqgimagyid ygktdangry
      301 frfdteqfyy dangnpsrvn hpkeglgygp rfnentmivd ydgklvpyrp yknnllkayn
      361 lgvsnttsvs ltggnekgnf ylsdsynqrt gvlpnngfsr nsllfsgayn latwlkaeas
      421 vsytssegkn prsdlatnfl tgvwtneydv ekykqnqywq akhgglpnsn ygdeyayvpg
      481 ngiwfaynkn nqvrnenvvr pivklsaeil kglnvrlegn lnyytikqen kelgngyane
      541 ggyyalyhyr dvsqtgkisl dytkditqgl sayvvvggei wnqeksetrv rtdgglvvpg
      601 ryylknskkt piadagrvfg tkqinslyfl tsfslkdqlf lditgrndws salvytdgtg
      661 nysyfypsvs sswvfsqtlg lpswvsfgkl raswaqvgsd tdpysinkgy slgsyemngg
      721 nniylnevst tlvdrsikpe rknsyevgld arffnnrlgf dvayydeyit nqigdiplpn
      781 asgyrnlltn igtlrnygfe lkvdakpirt dnfvwdvsfn ywrnrtqvtd lhkdygaykv
      841 lggtpaygnf rigsvafegg eygvlmsdsa pkkfqakdan gnniddprng mpvlkwtnng
      901 rtayyersge veeigkmqpd fegslkntft ykgvslsvml darfggymas fsnrygtang
      961 flntslkard ahhggitwts qypdtkgkvf sdgiivdgvf apgtnvqtpa gttqdvgglt
     1021 yreamdkgyi epshasthty fknswgqgvv nddwfhevny valrnislgy tlpsevskkl
     1081 kmrnlylgvn lrnlgylyns lpnklnpesf rgttstesff ersfipytas ytfsvaidf
//
LOCUS       WP_098031948             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AR29].
ACCESSION   WP_098031948
VERSION     WP_098031948.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AR29
  ORGANISM  Bacteroides sp. AR29
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Bacteroides sp. AR29"
                     /db_xref="taxon:93975"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108797
     Region          33..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkslkrcl kkrmilllgf lmmtgvavaq qlqvqgkvtd atgegligas vlvkgttsgv
       61 itdidgnyvl lnvnpdaili fsyvgyqtqe lnvsgrnkid vvlhddqqvl eevvvvgygs
      121 lskkevsssi vqvdkknfnl gamnnpmemv sgkvaglnvn tqaaanpnss sslqvrgats
      181 vsasnspliv idgvaggdir niaaqdiesi tvlkdagsaa iygtrgangv ilvttkrgsg
      241 eagktvvtyd syiafnvakp spdilsadef rrsrrgtdyg adtdwyglit rdvaydtnqy
      301 isidgstkng fygasfnyks angldivsgr eefggrfsme qrvlenrlqf ngslsarrvn
      361 etwgndgffd raltmnptmp vynadgsyyq ptsptgatnp vaelalrdnn gqrmyllgta
      421 eaklnilqte khllnttlsy slhyndmkqq yyassagses ywngykgrae mkyqkwytnr
      481 lewlgnyaln lgdhnikavv gytyeksiwe qiggsnndfs fdntkywdlg sgsylkdgla
      541 slysgrsest ligffgrlny nwkdmlfasa slryegsskf ganqkwgyfp aaslawemme
      601 mgfmkntrkv ltslkprvsf gitgrsdfda ykslstyntn gsylfdgrwv tgyapssnan
      661 pdlaweksva inlgvdfvlw nrlrgsveyf drsskdllyt ytapqppfvy stilvnvgtt
      721 kntgievsld gdiltktavk wtsginysyg ktkltklsnd iykasyldly lkpgtgssey
      781 ffrvqeggei gqfygyeyag vdengnmlil ndkdeqipis qadakykryi gngapkhfls
      841 wsnnltwrnf dlsvffrgtf gfdvfnmrky gmglqgcgtd nvlrsayled knirtgggvi
      901 ssyfledgsf iklvnvtlgy nftpknrkll dnmriylsak nlftltgysg ndpsiidvng
      961 iqpgvdsnsa yptatqlslg vtlrfk
//
LOCUS       WP_098032302            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_098032302
VERSION     WP_098032302.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122912
     Region          24..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrvlivll clvgvlssaf aaekkvqgvv issednlpli gasvyvtaed lkkagsaqtt
       61 mgvitdvdgq fsiaipagit rffcsyvgyd vlevklvpgk ehyeitlhas sqmldavvvt
      121 gyqtverrkl taavskldis detigavksi dqalagqiag lsvsptsgap gapakirirg
      181 taslngtqdp lwvldgiple gtdvpepdel nditnmkqss iaglnpadie nitilkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs srftytptls ldrlnllnsa ekvglemdmi
      301 rnnyspdnhk ggvynilsny nelsafqngg wdalssdtqa ainrlksvnt nwgdilfrda
      361 fsqeynlsls ggtervtyyt sfgyykedgn vdgvgmdrfn lvgktsykvn silkvgasmf
      421 anrrkntnyl tdaygmsnpv fysrkanpyf elydkngnyn ydydiqnntd kdlgfnifee
      481 rqntsnesvv nsfssifdae lrfndkwklt sqfgyqlekt sreeiadwes yamryyykls
      541 eysqggetkh flpeggmqks yensnsqitw kamgeyrdsf ndihelevma gtelrktwye
      601 tlfsagygfd rktlttkpvi fpnesyatsf plhqttyken ayvsfystas ysllnrytvg
      661 gsirfdgsdl fgvdkkyryl plysvsalwr lsqepfmqqa kwvdnlvfra syglqgnidk
      721 ntspfllgty rsesilpgvs edviiinsap nkklrwektq svnagfdfsv lnqainlsvd
      781 yyyrkgtdli alrmlpletg ftsmnvnwas menkgveisl strnittknf swytnfnfay
      841 ngnkvlqeni peqqttpgre gypvgaifal ktagvnketg nmmfynpege kvtlkelyrl
      901 kdewgigias sdvtaaeert fysyigssda pytgglintf syknwelnvn fsltfggyvr
      961 tqpsydiinp dygknynadv lnrwtpenpn aelpafmlsa snpeeyswyd sktiwrdldi
     1021 wvkklnyvrl qnlrlgyrip elltkrlgmn satvsiegrn lfvfgsgynn ymdpesmynp
     1081 yatpvpksvt fslnlnf
//
LOCUS       WP_098032541            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_098032541
VERSION     WP_098032541.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117225
     Region          42..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkkckntl lcgtltlclw ggfsqvraas fenfaieqqs nkvtgivnde fgpvigasvv
       61 ekgtsngvvt dldgkfslnv kpgatliisf vgykqqevka gnaplnivle edskmlsevv
      121 vtalgikrer kalgygvaev qgealtkake tnvinsmagr vpglvvtqta ggasgssrvi
      181 lrgstemtgn nqplyvidgv pldntnfgsa gtyggfdlgd gissvnpddi esmsvlkgpa
      241 asalygsras hgvilittkk ankdkvsvey ngtltfdtql akwddvqqvy gmgangtypi
      301 navsntnmsw gakadgtnml kyfdgverpy livpdntsqf frtgftatns aiigvnngkt
      361 girftytdmr nkdivpkthm srdifnlran tsagkfdldf svnytredvk nrpalgdsks
      421 nigknlmtla ttydqawlks yqdangeyan wngmdpynvn pywdvyknsn sskkdqfrfn
      481 gkvvwnitqh lkvqgtagae lnwftfedyk apttpgyesg ylqnnnfrnr mynfellaly
      541 nnswgnfdfn atlggnlykv nnqtivttak dmkirdvval msfnevsvep ysyrkqinsi
      601 ygavnlgwkh mlyfdatlrg dqsstlpisn nmyiypsfsg sfvfsellkl gdklpygkvr
      661 mswaqvgsdt dpyqlglvyt kskfaypgyt igyisngtip nkdlkptktn sfemglelkf
      721 lknrigldft yysqlsknqi mgmassstsg ygyrlinage ienkgveial ntrpiqtkdf
      781 swdlnfnfsk nsnkvkklvd dmdmfeleka twldvqvaak vgenfgsivg pdfqrnengd
      841 ilidpstglp mydksnhvlg naswdwtggv ytnfsyknis lsavfdvkvg adlysmsara
      901 ahetgksmat legreawyks eearqaagya kdspdwiptg gfiapgvidn gdgtyrendi
      961 vinpekywms vcrnapsmfi ydnsyvkcre itlsytlpka wlknvvdglt isfvarnpfi
     1021 vwknipnidp dsnynnttgm gmeygslpsr ksygfnvnvk f
//
LOCUS       WP_098032794             938 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AR29].
ACCESSION   WP_098032794
VERSION     WP_098032794.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AR29
  ORGANISM  Bacteroides sp. AR29
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Bacteroides sp. AR29"
                     /db_xref="taxon:93975"
     Protein         1..938
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104054
     Region          2..937
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 misfvgmqtq evtikphvkv ilksdselle evvvtgygtf kkasftgaas tvntstledv
       61 pvlsvadkls gnvagvtfgs sssnpgsvss irvrgmgsin agnnplyvid gtpvtsgdls
      121 eftysdagtd ilsslntndi esitvikdaa aaslygsraa ngvvvittks gkqgktnvsf
      181 rsdwgfsnma idyrpmldgd srrellwtgl knyglysgnm sdadaatfad qniedfaskp
      241 stgwtdwkdl lfrngshqny qlsvsggndr tkfytsaayt nqegiiykqg lerftgnanl
      301 thkfgdfevq vtsqfskvrq nktneatsyd gpvanyaffq spsstpyned gtlnngcgif
      361 gvnplyereh ssdvytlmka fntikltyni wdklnlseki aydyaqgtnd vlwdrhsnng
      421 apggvmqriv nrndqlntqt qlsyinsfgl hnidallgfe tqdteyafny magqdypgdl
      481 yeltnagsts aetnrqsyrm tsflgranyn yadryylgls yrtdgssrla renrwgsfws
      541 vsgawrfide sflnpvksvl tdgklrvsyg vngtqpsdyy aymnlykygi iyngqsgmsi
      601 vgianpdlkw eknktwnigl dlsfidrisv tfdyyqrkts dliydlpvsq vggyydgnyg
      661 yttpqnigsl knsgfeltit stnfrnkdft wttslnmahn snkltkldgq qneivsgpli
      721 hrvgepyysy yvyeyagvda etgkemfyln dgtenarktt tniseankti vgkhqasieg
      781 gltnnlkwkf idlgftftys lggdafdyst wqhsnggshl yggavptyyd iskmwtgpgd
      841 tnatlpkfey gsaaslssrw lmptdylrlk nltlgvsipq nyinklglsk ariyfsgsnl
      901 ltwkskdlfv dpemrvdglc tfetpalrty tfgielnf
//
LOCUS       WP_098032799             898 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AR29].
ACCESSION   WP_098032799
VERSION     WP_098032799.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AR29
  ORGANISM  Bacteroides sp. AR29
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Bacteroides sp. AR29"
                     /db_xref="taxon:93975"
     Protein         1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98450
     Region          27..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgrvslclvi mfficsaqki daqvqnirek qdtisatksl ehtrpenikk gplnnaldvl
       61 sgqsagvnvt tngtdrlaml nsirvrgtts imggndplvi ingvtsdiat lstiypadie
      121 sftilknate tamygsrgas gvieiktkkg tgrgfeisyd gnygfesmyk hlqmlngpey
      181 iataealgld ynnggyntnf hdvitrtgli hqhhlafsgg sensnyrasf gfmdhntivk
      241 vndyrnlvvk ldatqkafdg rlvgdfgvyg ysskihdifd trmlfysaaa qnptypagtd
      301 vngnwvknsa ashinhpgal lyekndseer nfnthlglkf nildnlilsa fgsysysstg
      361 naqfcptwvw aqgnvyrgef kgedyftnvs lsynnawgds hldavvgaey lkqvrtglwv
      421 qakgittndf synnigatss rpfggtsssy edpslasimg svtysykdry siaaalrgdg
      481 ssmvsdnntf gffpsvslgw dvkkegflsd tdfitilklr tgygrsgnlg gitsyttlnt
      541 vkengivsin gaptvtmgsi rntnpdlkwe trstfnigfd lgiwdnrlml tselyysktt
      601 dmlyeydvpv ptfafdklma nigsmsnqgv elgisvvpiq rkdmemninf nmsyqknkll
      661 slsgeyngmh mtasditpig slygagqngg dnnvvyqivg qplgvfylph ckglkenelg
      721 gysydiedln ddgeidfsdg gdryiagqat pkvtigsnis fryksfdiam qingafghki
      781 fngtglaytn msifpdynvl kgapekniid qnvsdywlek gdyvniehit igynipmksk
      841 avkslrlsag isnlatitgy sgltpminsy vvsntlgidd krtyplyrty slglsiqf
//
LOCUS       WP_098032896             994 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_098032896
VERSION     WP_098032896.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109969
     Region          2..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 misyigmqtq evaikpsvkv tmrsnaeald evvvvaygta kkesltgsis vvdnkkiekr
       61 ittsvtgale gaapgvqvnn tygepgsaps irirgfgtlv sgasdplyvv dgvpfdgnma
      121 elnsndiesm silkdaasaa lygnraangv viittksgrn thkpsitlqm nqgmynrgip
      181 eydrldadrw meatwmakkn ammsnagmsa sdaaayatgh vvsesigrni ynaagdklfd
      241 nngkliatrl agyddldwqn aiertghrqe ynlsaatsge kynvyssigy lnekgyvkat
      301 gyerfsgrin ttytpnkwfk ggvnltgswt krdynsnasg nyyanpfyit rymapvyplf
      361 mhnadgtyql dadgnkiydt tssylsnrni ayemlynkqe svrnvlggqa fatislpygl
      421 sltvkgdlnn stsnnkkydn peigdgatng grltsyayqy ktvtlqeils wnyqfnqvhn
      481 veamvaheny swerkytsgm ntgmavdgnl tmgnflnnsy fsgsddedkt esylarvkyn
      541 ydnryfvegs frrdgssrfh kdnrwgnfys vgaswnmkqe aflqdvdwvd alklrasyge
      601 vgnnmgvsly ghmalytidk nggeaalvkq slsapdikwe ttqtvdvave grlfnrlnfq
      661 igyfdkrskd llfevrlpls agsypwvddt apmnltqykn igtvsnrgwe islnvdvinn
      721 ndwkwnigad atflknkivk lpdgkdilhg mqnyseghsi yewytyhfeg vdqmtgtsly
      781 tldpdkkaaa qeagalttin gtdyatatsy akrdwagsal ptvygsissa lswknwdlnm
      841 lftyslggkt ydgsyaslmg vsesgaagsa yhkdilnswk evpagmtets anridpngtp
      901 radfykssdl natsdrwlts ssyfvfknln lsyslpkrwl ksvgieglsl tagvenlftl
      961 tsrkglnpqy sfnggsddty vtarvynfgl tvkf
//
LOCUS       WP_098061419            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Longimonas
            halophila].
ACCESSION   WP_098061419
VERSION     WP_098061419.1
KEYWORDS    RefSeq.
SOURCE      Longimonas halophila
  ORGANISM  Longimonas halophila
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salisaetaceae; Longimonas.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Longimonas halophila"
                     /db_xref="taxon:1469170"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115615
     Region          28..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrtafftvf ifallgagna awaqdgnitg tvldseteet vpganvvide lqqgtatdaq
       61 gafelsgiap gdytltvsyl gyettstpvt veagetteve imispgavel gdvvvtalgi
      121 erderslgya vqevsgeela gtaetnfvsn lqgriagadi stsnsmggsa rivlrgarsv
      181 sgnnqplivi dgtpldnssf tsagqagggg gydygnaaqm inpdnvesvs ilkgpnaaal
      241 ygsraangvi eittksgesi adgvigvdir tsastkqvyg lpdyqntygg gswrpfsmnd
      301 qgqyivdfgt dqswgprldg rpvrqwysyd dvngllgett pweanpnnve dyfntgtvfn
      361 tsvafsqgge nfnyrasvkn vmeegvypns sldrssvsfn gsldlsekls tnlqatytnt
      421 qgqgrpgtgy dgrnvfqqfn hfgqrqldlg ensymrdyer pdgsqrgwnw tggeegarag
      481 dliyfdnpyw tqfnnfqede ndrifggvgl sydvnddlql stsartdlyt drrqervavg
      541 stiqdqyree irqvreinar vqadystqlt dqfsldayag sdyrynsydl signtqggls
      601 lpgvytlens isrpaitdff eerkligayg nvtfgyndlv yvdgslrndw sstlpegens
      661 ylypsvkgsf ifsdlstfdn vnflsngkvr lgwaqvgndt dpyqlrpayd ldvpfrgnpv
      721 qsvpgqlnnp dlkpeittsv eaglelglfe drlaldlavy rdvsrdqilg vevsrasgyq
      781 sllvnageie nqgvelalsg spivnddmrw dvtvnwatns nevieldesl glesytiggt
      841 pfgpdvvarv gepygtlfgv gyqyddegni ilnssgipet sapkslgsyt pdwtaglqts
      901 fsyksidvsa slngqkggni ysvtnmfgmy sglveetveg dvrevgfvpd gvyendagel
      961 vewtgrvdpn afsisgffgn neantfdath iklqsvsvry tlpemwfnrt pirtlsvavq
     1021 gtnlatlykk tphfdpatal satnlqgvea gqippqrtyg islnmql
//
LOCUS       WP_098061496            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Longimonas
            halophila].
ACCESSION   WP_098061496
VERSION     WP_098061496.1
KEYWORDS    RefSeq.
SOURCE      Longimonas halophila
  ORGANISM  Longimonas halophila
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salisaetaceae; Longimonas.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Longimonas halophila"
                     /db_xref="taxon:1469170"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108691
     Region          31..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhdrylmrha wawlilfall gapmlataqt tvegtvidae desplpgvnv tvqntqigal
       61 tnadgqftie lpegrrtlvf sfvgfatqei dvtegetsie vsmepdvmgl devvvtglas
      121 sikrenlana vtkidaedia gnvdpstldg amqgklagvn itsqsgapgg ginvqmrgis
      181 tlgagssqpl yiidgvyvnn sqistgrssa dgagegnqdn sanrladlnp deiqsievlk
      241 gpsaaaiygq ranagvviit tkrgeagdtr vnfsqelgav salnllgvas wsedkidliy
      301 gegtdaaare rarfnqaqqn gnlfdyeeel ygnvglarnt qleisggdeq tqffvagglk
      361 eedgiientg farktvrani dhrlsdrvrl tsssnyiysd sdrgftgnqn stggsvgytl
      421 aytptyaqlq pdedgnfpdn pyfaenplrl vneatnnqev srflqsfsln adllqsenas
      481 lsldlkggld ylnsnstvyf ppffqfqqaq sdpgdviqgk ednfntnmqg flvynqtles
      541 gagpfslttq ggftrftqde nrqlvrgrgl apgqlnplng qtqeifsqqf vkivdigyvg
      601 qqevnwddrl igtvgarfdr stlnanqeef yfypkgslai nlhnfdfwgf dsinqmklrt
      661 aygetgglpq fgatfsalns vniggglgst istrgidpdl dpersrelel gadisaldgr
      721 laleatyyrk tvddiildre npvstgitti atnagtlrnt gielglsvlp vdrenfswfs
      781 rtlfwqndse mtdltipaft tggfgaalgt yyigegfspt tivgtpatpd sevpftvygd
      841 aqpdfqmsfs nsftlfqdle lsflfhwsrg geninlsrfl sdiggttddw nedhdgdgvp
      901 ngldrtdmfg pgaaqfveea syvklreasi yytlpssvld tafngalrnv klglsgsnll
      961 lfsdydsydp evsvfgtqav aqsvevtpyp ssrrltfhlr ley
//
LOCUS       WP_098061598             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Longimonas
            halophila].
ACCESSION   WP_098061598
VERSION     WP_098061598.1
KEYWORDS    RefSeq.
SOURCE      Longimonas halophila
  ORGANISM  Longimonas halophila
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salisaetaceae; Longimonas.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Longimonas halophila"
                     /db_xref="taxon:1469170"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39962
     Region          5..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,76,95,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(47,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpaslgvpra aatdetraal tpdvverlqd thgveirvas gvgtdayhtd ddyeaagatv
       61 vsdddawgad ivltlapppp errtalsdeq avlgllqpld apqvladiak qgatalpmel
      121 vprisraqsm dvlsamssla gyraaleaal rlpkffplms taagtirpas vlvvgagvag
      181 lqaiatakrl gakvrgydir datreeiesl gasfveleld tslsegddgy akeleqakqe
      241 rqpellrphi aksdvvitta lipgrpaplv ineaavkdma pgsvvvdlaa pnggncalte
      301 pgetvtrhdv himgptnlpa tmpvhaself antvralldy llnddgtlal dlddevadam
      361 cavhngtirn ervrslldts aa
//
LOCUS       WP_098065507             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_098065507
VERSION     WP_098065507.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35926
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tflrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlilndf scvvrechaa frsvllrihe rkgivyheqd slntlmanlm argvisaeyv
      241 hkfhflsdvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vap
//
LOCUS       WP_098074331            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Longibacter
            salinarum].
ACCESSION   WP_098074331
VERSION     WP_098074331.1
KEYWORDS    RefSeq.
SOURCE      Longibacter salinarum
  ORGANISM  Longibacter salinarum
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salisaetaceae; Longibacter.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Longibacter salinarum"
                     /db_xref="taxon:1850348"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110480
     Region          42..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvlvtkraa acglllcglc vaflstsara ahegasrtsd titisgivid enadplpgvn
       61 vrikqtgrgt attsdgtfsi tigerqsrtl vfsfvgyetv ertfdesrtd vvvemevdqq
      121 elsevvvtgy giektrtelv gsvteisgee leplrpeasf qtllsgkiag lkvnnpsgge
      181 agkpisvkir gqgslptpql rrstssqply iidgvplydi qseqfnqaag reellnplas
      241 inaddiesis vlkdasaaai yganaangvi lietkdgatd gfdvearvss gmsnsinevm
      301 llnseqyvrl yqetlindga tpeeaaqevg sdsvytnwde vlkrramftn atlsfsggte
      361 tlsarvslny ndqetisrgn sfqkygfrsr idyqlgdlar vnlsngvtgi ekvslgsfsn
      421 vplppnispy dadggfndat ifqdrpnpla vivqndndhn slsttnslqv tvepinnlnl
      481 ralggidyyq nrnfiyrskk natgndsggg ltivnrrnrk witnltgdys frlgeahafs
      541 tlggveaqek ntkvlrgsgs nflndnlrvl qaagdredrd aassddnvtt lstfgeisyn
      601 yngkfntsln arrdassifg gdvrnanfas lgvsyvlsee rffrdlsfld flkikssfgs
      661 tgnsrigsya arglysvssq nayagqiglv pstpqntrlt weknykfnag idatlfgrld
      721 vlveyyrnei vdaissiavp hesgftigdv naadmrntgi evtlgysifq dgdftwdvda
      781 naatnrnvvt elkledadis tvsgigyrvg edvrtiygvk yagvdpenge alfelpdgtv
      841 tddysvasri enrqrigdgn pnvfggfsst vsyrnlslrl vgeysfgsdi lvsnlyatdg
      901 rqisfnnqsv nqldrwqepg dqtdvprlse nappysvtdr yvynldyvkl anmtlryslp
      961 qslaervgve ragafinasn igyiyfgdap dgrngaaeyr yrfpeartit agidvti
//
LOCUS       WP_098074412            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Longibacter
            salinarum].
ACCESSION   WP_098074412
VERSION     WP_098074412.1
KEYWORDS    RefSeq.
SOURCE      Longibacter salinarum
  ORGANISM  Longibacter salinarum
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salisaetaceae; Longibacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Longibacter salinarum"
                     /db_xref="taxon:1850348"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114341
     Region          32..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmtrvwtlsl llstlllmit wtpapaqaqs dreisgqvtd avtgetlpgv nvfvpstkqg
       61 tatgidgtyt ltvseeadsl sfsyvgyetm tvplagrtei dvalapatle agelvvtalg
      121 ieresrtigy svqevegsdl sqtaelnvin slqgqlagvq vqpsgtgpgg ssrivirgir
      181 flgssnqpli vldgipiqgg grqqtgsfgg fdygggigdi dpnsiasltv lrggnaaaly
      241 gsrgangaiv ietkkgtqet evtvssqtta geplvlpdlq neygrgnngt ltqgsdgipv
      301 vpagdiswgp rmegqdvrdw tgsvqpyspq pnnvedlfdt systnnsisf atgnetatar
      361 atisnvqsag tlpgneldrt nislassadl sdrftvdgrv gyvaqsafnr vnvakspdnp
      421 iynayyfprn lrlsdledfr tsdgdprlwl desaadfstr nnpywtvnln tnederrrvl
      481 gymrlkydfa dwlngfirgg tdyntlrrev rvasgtsykv aqcgsdgsrr cgeylaeqtm
      541 sqettfdall dgereltddv tgrlgvggew rfergettgt sgsglsipnf ftagnltspt
      601 ptygfsekev rslyalftir yrdylfldlt arnewsstlp ednnsyfyps atagfifsdi
      661 wgpswlsfgk frasvaqvgs dtfpyrtmle ydvqgqghag qsfgsvqval pgvdlkpemt
      721 ttteagldle fvdgrfalss tyyltntrnq ildlpippas gwrsgiinag kvrnegvelr
      781 feaaavdgdd fqwdidvnws tnaseivklt ddidtyelss dlgvtieare gepfgqiygt
      841 ayqrtddgrr ivdqnglpvg issdslallg nfqadwvggv sntfrykgig lsvlldvkkg
      901 gdifslsnav aaqqgtaaft vdgreafyng nggivaegvv ntgtasnpty eentqavdpq
      961 aywsrvggeg giteefvyda syvklrqvtl syrlpsgwiq parlqsarvs vfgrnlaylf
     1021 kntpgfdpes tystslsnqg reafaypptr sigfslnltl
//
LOCUS       WP_098074716            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Longibacter
            salinarum].
ACCESSION   WP_098074716
VERSION     WP_098074716.1
KEYWORDS    RefSeq.
SOURCE      Longibacter salinarum
  ORGANISM  Longibacter salinarum
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salisaetaceae; Longibacter.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Longibacter salinarum"
                     /db_xref="taxon:1850348"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117480
     Region          27..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrklltaaf vlslvapgwa laqdtgtiqg vvtdstagas ipganvvirs ismgaatgad
       61 gsyeissvpa geysvtasfv gyvaksqeva veagetvtld falapqtvem gdvvvtalgv
      121 erdrrsvgas vqqvtgeela qvenenfvss lagrvsgasi ktsstmggsa nitlrgfnsl
      181 tgdnqplivi dgipidnstq rtdvgqergf ggfdygnaas iinpnniqsl svlkgpaaaa
      241 lygsrgangv iqittksged sdglgvsfss gvqvqrayqf mdyqnsyggg aagstfrtlq
      301 gndfvldgss dqyvadyatd eswgprldgr nvrqwyswdd vndlngvatp weahpdnvkd
      361 flqtgtrysn dlavsdgaes ynyrlymgnv nmkgvmpnse mdryrfgvng tvdvseslta
      421 navaeynyqe aqgrsgtgyg faenafaqfn tfgqrqldlg pdsymrdylr pgrqqrgwnw
      481 agvqgaqqgt fqytdnpyvg ryenlqtdds qrffgkaqln ydiaegigss fmvtndhrte
      541 rrgervslvs seqssytedv ieaqeintel kfdyetqfan dfdldafvag rirwetfern
      601 rqatsnglaa pqlytvensv grpeitdyfq qnavyssygs vnvgyndlvy mtgtlrndws
      661 stlpednnsy lypsiqtsfv fsslealedq dvlsygklra swarvgddtg pyqldvvypv
      721 eipyagqsiq rvdrvlnnan lepeittgve vgldleffnn raslattyyr dvtrnqilst
      781 dvspasgfgg tvvnagevln tgveaqlgvt pvrteevnwd invnwalnnn eivelaegin
      841 tyvigdgvfa pptvaqvges ygtvfgssfi rdangqivyn rsgvpvasge skslgsflpd
      901 wtagastnls ykgaslsvlv egqkggkiws lsnafgtysg llqetvegnq retgvipsgv
      961 vlpsgvdrad aattegipfg eavgrisaag fwknqffgpl gdnflydasy iklqevvlay
     1021 nfpsrwfant piqrlnvavt grnlailykk apnidpsltm stgnfqgfea gqippqrqlg
     1081 mrfnltf
//
LOCUS       WP_098075396             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Longibacter salinarum].
ACCESSION   WP_098075396
VERSION     WP_098075396.1
KEYWORDS    RefSeq.
SOURCE      Longibacter salinarum
  ORGANISM  Longibacter salinarum
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salisaetaceae; Longibacter.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Longibacter salinarum"
                     /db_xref="taxon:1850348"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40565
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maltigipre tesgetrval ipkiadrmlk svdgleilve sgagerafhs drsfedagcq
       61 ivdrdtvfga dliakvapps ddeiaamheg qviagflspl drpslarala drgvtslsme
      121 lvprisraqk mdalsamssl ggyratilaa drlpkffpll ttaagtirpa qvlvlgagva
      181 glqaiatakr lgakvfgydi rdatreeies lgakfvelel dmgdqedegg yakelqkekq
      241 erqpellqph iadadvvist alipgrpapl lireeaveam kpgsviidla apnggncayt
      301 eagetvvehd vsvigptnlp admpvhasql yaktitslie efvedgaftp dfddeifdga
      361 clthdgevhn ervrgmlsqe a
//
LOCUS       WP_098078113             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Longibacter
            salinarum].
ACCESSION   WP_098078113
VERSION     WP_098078113.1
KEYWORDS    RefSeq.
SOURCE      Longibacter salinarum
  ORGANISM  Longibacter salinarum
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salisaetaceae; Longibacter.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Longibacter salinarum"
                     /db_xref="taxon:1850348"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107878
     Region          20..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlvlllivsl gfipaahaqf tvegtvtdan ngdpipgani vlvgtsigva tdpqgefsie
       61 vpgeegtlrv sfvgyqtler dvtpetgrve ialqpdiagl eevvvtglat svkrrnlana
      121 vtkidaeeia grvdpttvdn alqgkipgvn itaqsgapgg gnnvqlrgis tlgagssqpl
      181 yiidgvyvnn sqittgrstl ddaggpsqdn vsnrladlsp ediesvevlk gpsaaaiygq
      241 ranagvviiq tkrgqagrts vsfsqdvgav salnllgtas wsedkialfe epgtqsfqde
      301 iarfregnst dyedevygnt glttntqlsv sggddqtqff vsgnlkdeeg iientgfvrr
      361 slranldhrl hervrltsqs nyvytdndrg ftgnqnstgg svgytlayvr syadlfqned
      421 gsfpdnpyfa enplrvidga tnnqevsrfv qsfsaeadli rsnstslrlr gqggfdylns
      481 nstvyfppff qfqqaganpg dvirgkqddf ntnlqavlvf nqatslgggd lnlttqtgfs
      541 rftqdtnrql vrgrglppeq tnpvnasvqe ivnqlpndvy ntvkvrdigf fgqqdanwrd
      601 riigsagvrl drstlnasqd eyyvypkasl avnvhefdig lpsflsqlkl rsafgqtggl
      661 pqygvtfesl asqnidgnla stidtrgvdp tlkperaeef efgtdisafe nrvslelthy
      721 rktvsdlild renavstgit eiavnagtlr nvgwevgltl apiqterfaw tsrnlfwant
      781 seitelnidr fttggfgaal gtyliqegys pttivgtpal ddgdtpftvy gdaqpdfqms
      841 fsnqftlfrd felgflfhwk kggeninltr fltdsggtts dwnedhdndg vpngrdradm
      901 fgpgaaqfie gssyvklrea slyynipssf lertfgnvls rarvgvsgnn lllfsdyssy
      961 dpevsvfgtq aiaqsvevsp ypssrritfh lrlty
//
LOCUS       WP_098086618             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            sp. FDAARGOS_372].
ACCESSION   WP_098086618
VERSION     WP_098086618.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. FDAARGOS_372
  ORGANISM  Nocardia sp. FDAARGOS_372
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Nocardia sp. FDAARGOS_372"
                     /db_xref="taxon:2018066"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38322
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mettqnvgds sprgarvgvv retnagerrv alvpkiipal lkqgvevvve sgaghgtlip
       61 dqayveagav igdpwsadvv vkvappsdae vaklskgqtl igflaprnae nqiqalksag
      121 vqafaveaip risraqvmda lssqanvagy kavllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rttgydvrpe vadqvrsvga qwldlgidaa geggyarelt
      241 deekakqqqa ledaikgfdv vittalvpgr paprlvtaaa vegmkpgsvi vdlagetggn
      301 celtepgktv vkhdvtiasp lnlpatmpeh aselysknia allelmlvdg alapdfsdqv
      361 ladscvtrev da
//
LOCUS       WP_098097407             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_098097407
VERSION     WP_098097407.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36000
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyie tylrtyevtl
      121 glepdkaisd lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechav frsvllrihe rkgivyheqd slntlmtnlm argvisaeya
      241 hkfhflsnvl eseiflpmaq ekshhhyamm hriseelacs iyyltersif fltqraeeds
      301 vap
//
LOCUS       WP_098097917             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_098097917
VERSION     WP_098097917.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53639
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaitvtvea knetfvpqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_098115260             306 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Bacillus wiedmannii].
ACCESSION   WP_098115260
VERSION     WP_098115260.1
KEYWORDS    RefSeq.
SOURCE      Bacillus wiedmannii
  ORGANISM  Bacillus wiedmannii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Bacillus wiedmannii"
                     /db_xref="taxon:1890302"
     Protein         1..306
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35450
     Region          3..163
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
     Region          <248..296
                     /region_name="Abi_C"
                     /note="Abortive infection C-terminus; pfam14355"
                     /db_xref="CDD:433897"
ORIGIN      
        1 myetfskrek krmgqvmdvy iynkipdrlr vqvihiweqs iggsddtwat inqtmskelg
       61 kfsltneycq phehcknfll sckdvhaidl ielsfyvlkd hykigkiphd pfaislmgie
      121 qsfeeaikel nywfkdnsig fefingeiir idqthmheev vkpaitllfe eefegaaeef
      181 lnahksyrkg dyknalveal ksfestmkti cdkkeytynk srdtaqrlit vlfdnnlipe
      241 ymrnhftslr ntleaglptv rnkqaghgqg aesvkvepyf veyainlaat nivflinayk
      301 eskenv
//
LOCUS       WP_098124152             302 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Bacillus cereus
            group].
ACCESSION   WP_098124152
VERSION     WP_098124152.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus group
  ORGANISM  Bacillus cereus group
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Bacillus cereus group"
                     /db_xref="taxon:86661"
     Protein         1..302
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34823
     Region          3..162
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
     Region          <246..295
                     /region_name="Abi_C"
                     /note="Abortive infection C-terminus; pfam14355"
                     /db_xref="CDD:433897"
ORIGIN      
        1 myetfskrak krtgqikdvy tynivpdrlr mqvihiweqa igefnepiwd vvnktmskel
       61 glynltsvkl qssfqrcavf lqtctdteai dfielsfiiy kkdyetygwn qsnnygladq
      121 sfdeaieeln ywfkdnnlgy eftngeliri dqthmheevv kpaitllfee efegpaeefl
      181 nahkayrkgd yknalvealk sfestmktic dkkgytynkg sdtaqklitv lfdnnlipey
      241 mrnhfsglra tleaglptvr nkqaghgqgs esikvepyfv eyainlaatn ivflinafke
      301 sk
//
LOCUS       WP_098192083            1116 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098192083
VERSION     WP_098192083.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1116
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125000
     Region          132..1115
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkriksistk lvmvlamscc lpkyfisraq asghseqpnt vslvsfisal eskfdirfsy
       61 ntnlvkgkef iapklndftl snvddklnea implglmckr innklyiiky drkatekmmq
      121 lqtelnlpaa iikgvvkdsl gnplpgvivk lkgtsrgttt dasgafsldq vkdgdvlifs
      181 ligyatieva ikgqtnlniv lkestvsldq vvvtalgikr qekalgyavq rvggeqvqtv
      241 kgvdiatsmt gqvsglvikn steffakpti elrgesallv idgvpygnmt lrdvptddie
      301 sidvlkgpta salygsrasg gvilvttkkg ssgglavnin sntmlqtgfl aipetqhsyg
      361 rgqngqidnd yvwgpkldig ltardwnpet mqfeddrplk slgannlknf melglvtnnn
      421 isvsqatdkg sfrvglnhiy nkgqfpnaka nmfnftasgt ikasdkfsle shvgiskrys
      481 pqiwgsgygn qgyiyqltmw tgpeydirqy knywkvpykt qnwmytnwyd npyliayekl
      541 dgikqntvna smtanynfte dlnllvrlgy dvytnqeewt npaaniystr ggwnakgrys
      601 inktwgwstn ddvmlnykkk lkdwtveama ggtiyywvde alsastrngl tsptfyslng
      661 sveaptisps nysrqvnsly grvalswknt vfidatgrnd wnsaqpkeer affypsigss
      721 vimseffkmp raidmwklrg swatfktpag vyetnrlyst ttaawnslna ayypsnllgg
      781 ilapssqrtw eigtalyllq krfsvdfayf nkyyynqkas psipsssgfs stivntdety
      841 vrkgieltvg akviqnrhfe wntmvnwsnq hryyvdldst ytperpwikr narkdvytdn
      901 ywlrdpdgnv ihnngmpvrs dyakvygytd pkfsfgfint fkvynftigl nidgrigglm
      961 ynyindkmyd tgshpdtdne frydevvngl tnyvgkgvkv vsgsvtfdnf gnivsdtrky
     1021 adndvevsyq dytqkfrggd ygamkksfvk vrefsigysf pakmlaksgi knasvaftaq
     1081 nlflftkfky sdpdvddenl nspsqrmigl nfkvgf
//
LOCUS       WP_098192192            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098192192
VERSION     WP_098192192.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113588
     Region          23..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkallfftm lmvsislaya qerqvsgkiv gsdgipvsfg tvqikgttrg ttadqlgvyn
       61 lrakvgdili iravgylqke vsvpatgeld itlesstktl devvigaggv aarkreigyn
      121 stivgseqli qarpvnvass lagkvaglqv taisggvnpt vkltlrgnrs llgnnnalvv
      181 ldnvivpsdi lgnlnpddie dinvlngsna aaiygsdasn gaviittkkg kngqniikfa
      241 qtltaekvsf ypklqnefgs gstgnnqvyt pyenqqygpr fdgsmvqigr plrdgtiqtv
      301 kysptddkkt fwetglnsqs dlslssgdek gstyfavqyv kvngttpkde ynrfglrang
      361 trnvlenvkv gysvyytqnr yditsatssi ydqllntpaq ipltkyqdwr ndpfanpqgy
      421 yndyyanpyf tidnnrsktr ndylvgnael kwnplkwmta vyrvglatrn yssksytgrf
      481 ifeddyyltg skasipgsvs dgtgyttqlt sdfqlqfnht vkdfdfnlil ghfarnntak
      541 nvgvgssgni ikdlyhisar lgevsgsegd yterqiglwg nlkvgyknfl flemtgrndw
      601 rsvlptnnws ffypsinasf iateaidalk dnkflnmlki rggwsqigqa sidpyalast
      661 yspsrgfpyp sgpgyttdnr ivdrnlkpem tygwevgfda smwdnridls atyystrtkd
      721 qtvptgvsta tgfssflrnt gevsnagvev alsvtairtk dvtltiggny thnenevisi
      781 ssdvprlqmt tggtaqvyai pgmyfpvimg tdyvrddqgr iivdrntgyp sradgvvllg
      841 ntnpknragv nlefryknwr lwtlfehrgg yviynngast ydfsgssirt tqydrerfvi
      901 pnssywdeds ktyventdvm vrdggtgfwa dgdgpynmai asnyvysgdf wkmreltity
      961 nlpakflgkt rviknasisa qgrnlflwvp dsniytdpey sftdgnavgi ttlgqtppsr
     1021 yfganititf
//
LOCUS       WP_098192231            1153 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098192231
VERSION     WP_098192231.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1153)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1153)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1153)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1153
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1153
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128800
     Region          119..1152
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpnclvisri gliyiltfli gfpitvssqt kpgllldisf ngesldmair kieklypvvl
       61 vydaqqlsay haptgswhqk spqfiikqll kntpfklmds ggriiifkkk lsgltvfngw
      121 vsgkdgmplp gitvqilgtn lgtvtdkngr fslhvkngvy nvtftsiayd pltipgipln
      181 ndtvvdhhfv mqereeslqq fvvtalgisr prstlgyalt eikspglnnv eapnilqals
      241 gkipglqvrg lspdpgasvy vvlrgessfn gnsqplfvvd gipitanssv agkvdygnrl
      301 sdlsiedias isvlrgagaa alygsragng vvvittktgn pggsswkvta ssslmidkaw
      361 qfphfqnlyg agtdvlaedt wgeaswgpgl ndgsykvqwn spkddegnfi plpwtaypgr
      421 vrdyfqlgqt fqqhiavnks fekgaarfsv ldtrnrgiip ntgynkdvlm fslqykfdpk
      481 iqfntnlsyt ysssdnrfsg drgsvinqly tmpanvntne lrnywkpgke gveqqsylhd
      541 mysgqaqvdn pfliayeqtn ayfrhrlngl vqikwtindy lnlalrsgid qfyeyrerkk
      601 pfssvnfing fyeeaklfsr einsdlllqf hkqfytvwni sadfgmnrmd qknydytiaa
      661 qqlkvpsiys lsngvdgsft yqsdfarkrv nstyatmqas ykdilfvnas grmdwsstlp
      721 ryhnayfypa iassllltrl lnlgennwvn rakfranwak vgkdtdpynl yntfqyianw
      781 dgisradiat mlknkllkpe ittatevgle lgmfkerlgl ditvyqstnk nqiiavplai
      841 ssgyserlmn agnirnrgie lqlswhgnkk plhvqyegyi nfsknwdkiv aldpgipnge
      901 iylsggegas vlakvggrmg dmyggtykkv pggpykgapw ltasgqyqle ggayekfgny
      961 npdfmlswnh gvkyknwfag alldwrqggt fysytaknlq sdgrvdvtlp grdasqgglp
     1021 wvdgngkerh dgmilygynl qddgtfapnd vilspeayyg nyywdfparn aynatyiklr
     1081 elslgynflh pakwiqnvrl vfmarnlfaw naagtgfdpe tsnkiensry qlgintwtlp
     1141 giktfgfkid csf
//
LOCUS       WP_098192278            1163 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098192278
VERSION     WP_098192278.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1163
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131366
     Region          155..1160
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvvknarras gclavamlfh fgsiaapara qveaiysstk arpewqeqsl ktilnrieqk
       61 yqvqinyvgs tikgilatmp aeknesitfv dylnrflepl glqaeelntk afviyrsaak
      121 papakkdsat ntqpvatava aeyptttipq qvqtktiegq videtglali gvtvvekgtr
      181 ngtqtdangr ykllnvhsna tlifsyigyk tqevhsgkrt tidvklltnv qsmkdvvitg
      241 yqkidknnft gqsitisgde lkkinpqnil asiqaydpsf rivenniags npnklpninv
      301 rgttalptst gdvsdlrmtr semnnitnlp liildgyqvn lqtiydldpn rietvtllkd
      361 aaatavygsr aangvlvfvt kapkegklel yynfelnvts pdltaysvld akdkleyerl
      421 aglysqsdae nidaleqkyy akldnvlrgy ntywlsqpvg tefgqrhsls lqggsqtvky
      481 gidaryqnnn gvmlgsgrer yslatnlayn lknnkllfrn qftisqvngk dspygsfdty
      541 vkmnpyypir dengrllrei dgwkyrdysn sggaittdyv lnplydaqtg sfsksqylef
      601 idafsmeyvi ssafrargei sltkrqnnnd rfisplsnqy ydwsgddlkd rgeyyytaek
      661 etqvdgnatl synkmlaggh finatyginf qsrdydrkdl aaqgftndrf tdinfariyk
      721 kdaspggeqr qerlfgtfvt vnysyqnrfl mdatfrldgs skfgvdarma pfwsyglgwn
      781 lhnekflqgt avsnlkirat tgltgdvsfp aylsnttyqy ytgdwystgv gavfkaygnp
      841 elrwqrtqny digadiglfk driyftpryy ykhtrdllad vnvppsngfs syktnlgemv
      901 nkgyevmlra npirsrnwsl tlsanmvrnt niitkisdal knyndavdke qqdnpdlrsv
      961 pllrfqegqs lrtiyavrsl gidpengkei fltkegkrty eydvrdivpv gdetpdiygy
     1021 lgaslvyknf midvrmftsl ggdlynqtlv drvenadpry nvdsrvlaer wkkpgdkaiy
     1081 kdisdlgttr vtsrfvqeen klelssvfls ydapakfykr lkmqnlrfsl nmndigywss
     1141 ikaergieyp farsftfsls trf
//
LOCUS       WP_098192313            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098192313
VERSION     WP_098192313.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118001
     Region          69..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myqqyilsrk akglwallva mmimghvaaq qkmvtmkgia yekstntpip glgiytgkpl
       61 kpiaataadg sfsitvpega evvfrsisya aysikakega kykimmaeqq sklketviig
      121 yqkksrevvs gattlisgke lqdvpvanvm elmqgkvagl niqnntgapg yagtiqmrgl
      181 nsiaisgsgs eaflrptspl fiidgvpvdp nsnyqygfdq agpglsplsl ippediesiq
      241 vlkdaqatal ygsrgaygvi lvttkrgksk vpivqytgnf fvsipptlrp viggqeerrr
      301 rinqymeytd slykaaeivn etpflsdsln pfynnstnwq glfydyaynq thnlivsggd
      361 drfnykanvg yynekgimkn tgferyalst nmtyrptqrl rvfstistsl glnkkgsgng
      421 llqtdvakag aqsslmpaps fysssasaia alrtdnnnkt anvrtsldvd yelfpglhva
      481 nnvsfenqsa teenfvpaai nsnfssmysf ydkktifnnr aslsyfktvn nvhnftiavf
      541 nelnrntyqa ntvklertps ddfkgpygnd gyysrggvmp gsyderivgn aatfsynydq
      601 myvldlsyrl dasstsgkkt pysnnpsigl rwnfnrlral ststwldyga iratwgknvt
      661 pqgdifdayg iytdrngary ndqpvsgiey enlpnndlkp vtnttlnfgf dmglwrsrit
      721 gtfdfyvkdv dnslyeidlp dvngfnkvks ndlawrnigf eyqitarllp stsewnmtfs
      781 lngsyvkdri trlpngkrem yyydksagqd ilyrvgknal tnvlynttgv yatdadvpvn
      841 pvtgkpvvvk svvndnvyyt plrggdpiwt dmngdyiide hdrvyagnsq plvnggaslf
      901 vqyknyslni ygayiayrki lnnaiaerfa sfskpsgnla mvpideynyw ekagdkatyp
      961 npydyarspy vrpyridqtl feedgsyfki nqitfsynfd raktrrygvt sarvyatvyn
     1021 mfmfsnysgp npenvtalgr dqsggyparr svtvglsvqf
//
LOCUS       WP_098192891             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098192891
VERSION     WP_098192891.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105843
     Region          28..978
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miktrllqtf lfcslwllla sianaqsrtl sgkvldengg gipgatvqik gtssgtstdd
       61 kgafkltlpa nantlivsfi gykklevdvk gksevtvnme lenttlsdvv vvgygtarkk
      121 dltgsvasvk akdfnkgvla apdqliqgkv aglmvinnsg apggattvri rgnsslrsgn
      181 qplyvvdgvp ldgrtakpaf tgavgttpds nplnfinsfd vasmevlkda sataiygsrg
      241 sngvvmittk qgvpgpaavd vnysvgfsnl lkkldvlsas eyrkalsdys ltngdygadv
      301 daldaitrtg itqninvavs ggnetsryra sfgyldqegi vkksgfkkyt anmngrfnfi
      361 dnragldysl lashstenla pisndagfrg slitqalqwn ptralynpdg sfnilddgsa
      421 vnpaamsaan ddvvningil gsispyfkfn dnleyrfiys inhqvgerea qlasfinipg
      481 ilgkgqafya tntltaqlft htlnfnkqln pnwhlgavvg yeyqkydykg rgltantftt
      541 daiayidalq dapqvntsin sfrnptseiq svfgrvnlnw mdkylltatl radgsskfge
      601 nnrygyfpsf aakwvtsnee flkgnqffny lalragwgit gnqefpagas qeqygttnsg
      661 saglnnvanp dlkwestkql nvgldfnlwd yrisgsvdyf hrnttnllfn lptilpapas
      721 tywinvpani inkgvefvvr aevvksndfn wavgvnatfl kneltnydga plltgaingq
      781 gvtgasvqri andyplntfy vrnfegfdkd glsmytddga lfmksnpnpk tllginteln
      841 ykkwtllasa hgafgyeiyn ntantvlpin glgntnvakk ligngenlsn aiatssryle
      901 ngnflkmdni tlsynlgdvs kfknasifvt gqnlfiitky sgfdpevntd kslngvtslg
      961 ieygpyptar tvqvgvnfrl
//
LOCUS       WP_098193248            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098193248
VERSION     WP_098193248.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118113
     Region          23..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrvllallm aiffvgqvfa qtrtikgkvt saedgtpiig atiivkgtnl gtvtsvdgty
       61 sinvpegrnv livkfigmke keitisgntm dvsleqdirt lnetvitaqa irrdksslgy
      121 sapvikseei mkgqnqsaln slsgkvagvn itgtanapgs ssrivlrggs sitgsnqali
      181 vidgipidns sviggsssls sidfgnrgnd inpddiesmt vlkgpaaaal ygsrasngal
      241 iittksgkgg rknmditfst tgtlsrvlsl pdlqnkygqg gtqinpdgtf fnyddpkenf
      301 swgfpfdgqp kewgqeingv rqmknysalp dnvkdffvtg kaltnnlslt ggsdktayyl
      361 slnslnsdgv mptsadlynr ysvrfngsae laknfktsvs lnyikinsdm iqggqgvasv
      421 fdnvlqtprd iplngknlkn pyntmegtlf dgdgnslygf ygaytvnpyy llakyknqnn
      481 vdritgnfti swapaewidi tnragvdyys drrkfkypkf ssmpadsttg nysaednvqg
      541 yvgkygesei nvsevlndlm itfkkrfstd fsasllvgnn irqsqfnqln setnsgglvi
      601 pgwynlnnsd gpvqstnfys ikrliglyge lnlnykdmly lgatarndws stlpkknnsf
      661 fypsvnlswi ftelmkdski snilnygklr asyaevgndp dpyllktyyd kttvsggfas
      721 iifpfqgtsg ltlgdrigne nlkpektsaf evgtelgffe nrlyidfsyy qnrskdliip
      781 ipispstgft srvsntgevk nsgvelmvrg tpvktqsgft weiygtytrn rnkvvslleg
      841 vdqiviggfs gmaivaavgk pygtfyaqdl lrddqgrvvv dgttglprft ptavylgsyn
      901 pdyqaslgsn fsyknfsfsf lfdtkqgaef ysrtksiiaf ngtsletveg greariwpns
      961 viedpntpgk ydlnttakfy nydyyanqkn rpngqdvida sfiklrevnl tyslpktlls
     1021 kanigaasvs lfgnnlwihr agnnkyadpe insggsgneq gfdftaqpsl anfgmnlkit
     1081 f
//
LOCUS       WP_098193620             939 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098193620
VERSION     WP_098193620.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 939)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 939)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 939)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..939
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..939
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103987
     Region          33..938
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkriyiplva vaflvnmqak aqtakdstkn tavidygfrs ekswrttgat ftitgddlar
       61 ttsgnllntl qarmpgltvv tgsgepgydn ptfyvrgqss wniagnrllv lldgypveln
      121 aigalspyei etvtlmkdaa atsiyglesg agvlsistkk gtlnskiqia angrygiltp
      181 melpkvmnay dytrlynqal qndnlpikyl apelyqsgnd pvhpnvdwyd ellkktstiq
      241 dynitfrggt dkaryfvlms ytnfeglykn avaidkdfgt nakytklnlr anadiqlsks
      301 lsigvnlsgi tedkntpngf tastvfnnlq ripaaafpvk npngtwgnss vynfnpvqll
      361 qqngiynsht rnlqtainat ekldaivkgl alvggvsfnn qyvgvyqkgf tvpsfeilkd
      421 aqdqaildgn gdityrtigs ssqsindggn qhwnrtsvqv gltydkaygk ntlngilqar
      481 rqsfnhdgqv yqvrsqglla avtydyakty ivdisasyng sadfaegqry glfpaiglgw
      541 ilsneaflqn nkiinflkvr gsygitgnmn edarflfeqw gvnsgsyilg tnntsrggrt
      601 egalpnnsft weekksfnlg fdvtawnkln ftadvfqekr nnildgtsgi paytgftfqr
      661 lntgsvtnrg felsatfhdk vrafeyylga taafarnkid qrtdipqphe ylyqkgyrig
      721 qmrglindgf yqetdfdang nllpgivkss fgvvkpgdlk fkdqdgngiv nmydiipvny
      781 aklpemtmsf nlgfkfkgfd fdafiqsvtn rtvsllnday dythpfvnnn nitifssnsw
      841 tpatantatt prlstlsndn nnvqsdfwmr ngnflklrsv elgytfpqkg flrkidavrv
      901 fvignnlltr dkldnleaer lsmgyplmks vsfglnvkl
//
LOCUS       WP_098193993            1164 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098193993
VERSION     WP_098193993.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1164
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128037
     Region          45..110
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          134..1161
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkylrfmya cctvglvlal qlavlgpasa aaksqedisv siqvknknie dvfatlsakt
       61 glsfhydkse cnvkqkitln cvnepleevl yqlstqtglk ftrknnkiiv rlpgiagnna
      121 lesvtldgkg slvinvkgtv kdakgspipg vtvmvkgtnn gtqtgpggty slqanvgeil
      181 vfrsmgynik eaiiptsglv dvvlednvka lsefvvtalg iqkkskelty atqqlngdel
      241 skvkdanvin slagkaagvt itrsasgigg sarvvlrgnk strenqplyi idgvpmanfs
      301 paqptdvwgq angiavtggr dggdgisnin pddietinil kgasaaalyg sqaangviii
      361 ttkkgksgrv ridvssdftv esvmklpelq ykygqtekpg atpgtpeswg evvnapnhvv
      421 dffnkgntwn nsislsggse kaqtyfsysn tnnkgilpss efkrhtlnfr eslrllndkl
      481 tvdanitfvn qkshnrlspg iyynplpgly lfprgqdfdd yathfegfvp srnfdlqrww
      541 nidysnpdad nwrgrddqqn pywvlyrtas ddnrdramts itakyqltdw lnvqargsfd
      601 ksydqyelka nagtqiviap angryineke rntqlyadli fnlnkklsen wrigatvgts
      661 itdtkmhdrn mvgvnqnasp gleyankfsi aniqanalda qhsiqrrqlq alfgsvqvgl
      721 kdylfldltg rndwsstfaf tptmssgffy ysagitnvis dmlslpsfin fakirasyaq
      781 vgndiapyss rpgqfsqqil sgvgrvtfnt rtplpgiymk peknesfeig fetrmfddkv
      841 nldftyyvnn nfnqymevpa pvgsgytiyy lnlgnirnhg veamltltpl rtnnfrwnss
      901 fnfaanrnki vklsdpdvpg aspsnmftlt qfgvnmygsf ireggswgdi yanrelaynd
      961 egqllvklns qtnryepvin tlsqepkkvg npnpdfmlgw nnsfdykdls vsflidgrfg
     1021 gkvmsvtqsv ldaygvskvt anardnggvp vnafdvendk avssldprdy yfnvggragi
     1081 gelymydats irlrelaisy klplkakwlr dvrlgiigrn lfffkcdapf dpelsmgtgn
     1141 glqgidvfgl patrslgvnl kvgf
//
LOCUS       WP_098194071             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga caeni].
ACCESSION   WP_098194071
VERSION     WP_098194071.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39898
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgvlkeas tenrvslvpa ivqqlvqskv tvwvekgags nawlpdeaye qagaviqnre
       61 tilqqatvll ciqplseqes gnlnpstvll gvyqplfqta kmkqwaqrql tvfsldnipr
      121 ttraqsmdvl ssqaniagyk aillaansys ryfpmfmtaa gsiapakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgak fvdvegaada ssaggyaveq tadyqakqaa
      241 aigeaakkad iiittaqipg kkapilitre mmdmmkpgsl ivdiaaatgg ntdiskdqqt
      301 vtykgvtvig dsnlpskmpa dasklyaknv lnflqliidk egqlslnfed divqgaciak
      361 ggqivnerll qaitaav
//
LOCUS       WP_098194403            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098194403
VERSION     WP_098194403.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113030
     Region          29..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtflrllti fslvmlvlpg tmwaqqkait gtviaegegp ipgatvrvkg tqritqsdvk
       61 gqfkieaatg eileisyvgy etkevvigts ttlsitlqts qeslgevvvt amgikkekka
      121 lgysvqevra delmrnknan lvnslngkva glnitnsgga pgasasiiir ggtslernnq
      181 plfvidgmpm dnstgqgdns afdgsvnlst tnsnramdin pediesisvl kgpaasalyg
      241 lraaagaiii ttkrgstgst nininsrytn nwanrlpdqq kiykqgsyyg gaftdqtmts
      301 wgdpfasgek qydnmedffq hanafdnnis isggnangnf ylsasdlyqs givpttdfkr
      361 stvrlnaeqk kgiftfgvna tysksktqkt ltgsglwgag gngymetvvt wprnldmkhy
      421 lnddggkyrl fpdqdtsadv dnpywiinkn pqsdrnsriv gsayvnakit dwfdasyrlg
      481 idnytstfrn lispgsgvke awyhgmlset nknysylysn llltfhkkfk dwdlsliagt
      541 saentyikst svraedfvip gfislenatt dnqyfndnis rnrivgafgd lkigyknmiy
      601 lgftgrndwt stfarwnrsf fypsanasfi ftelmqpnkv lsfgkirasi agvgkdanpy
      661 qtntylfgpe etigggfrny wsrgneglkp eytysyefgt elrflnnrlg fdatyyinrs
      721 vdqiltprvs natgyilssv ntgeiqnkgi efiinatpik nknltwdval nfshnngrvk
      781 slpgdisily vtdvqigyak aasfndgyfm glsgskwqtd stgallldwn tgypltstst
      841 tdlvgnrepk figginnsft fknfnlnfli dfrkggdvyn gtdylltayg msketekrge
      901 emtftgksln pgtgkyedvt rtveateqfy rdiyvknspf fiqevnwvrl rainlsyslp
      961 tkvlnrtnfl kgatltlsgt nlllltnydg mdpetsaaga gvvgsgssgi dyagvpntag
     1021 fsvglnlkf
//
LOCUS       WP_098194413            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098194413
VERSION     WP_098194413.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113657
     Region          29..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrwlsllll tcfaalcshd vsaqekkwvt gtvkdttgtp vifarvhekg tanqvptdek
       61 gafriqvadg atleissmgy esaqvivgqg slnitlqyas kglnevvvta lgisrekkai
      121 gysmqevkgg dlvnarevnv tnalsgkvag lqvmrssngp agsskillrg nnsltgdnqp
      181 livvdgvpin nasgglrtsa ngtanvdmwe pgmdagngls dinpndienv svlkgpaaaa
      241 lygsragngv ilittktgrk tpglgitvtq tngfeslflk peiqstfgqg esgafnaisn
      301 qswgekisgq tvtnwageqv alkaydnfkn fynsgnstnt gvvfqqqink sslytsmnyl
      361 kdnsmipgse lgrlnlttra vsrfgkgdrw ttdmkvqyin skahnrpvag lndrnparil
      421 ygfpstldig yfkknkvdef gnmiwynqsn qlnpywnsvy nlnddnrnrf imsgsikyqf
      481 tdwldaevrg ggdlyntqfe nkryggapga tngsysigke nfsevnystl itakkdnlfg
      541 kfggsfslgg nlmhnkysyf snsaanlqvp nlfkidnvdg nigltdvyse ykinsaygml
      601 smnydgvvfl ditgrndwss tlskanrsff ypsvslsyli tesikslpsw wsygkvrasy
      661 aavgnslqpy qlfntydigk spsgpvtagr ktvlydpnvr selikswefg gefrfvnnri
      721 gldvtyyksn atrqlidlpm dpgsgyesrk inagdiqneg velmldakil dnptglswnl
      781 manfsrnrnt vkdilsnedv ksyrlggyen vsiiaeagql ygqiygtkyq rvtdekseyy
      841 gqlllnnglp qatnetyllg nqmpkallgi tnsfaykgft fsflvdarfg geifsgsqsv
      901 lqynglaaet vkggardnfv vggvvsdgsg gyttnteevt pqqyyqaing gnigiieani
      961 ydatnvrlrn iqlnyqlpks maqkiamqga rigvsctnvw misshmkgid pesifatgtn
     1021 atgfensspp ttrafyvnlg lsf
//
LOCUS       WP_098194496            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098194496
VERSION     WP_098194496.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114365
     Region          22..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllllflc fafinqisaq nrsvkgtvtd engqpianas igvkgttlga fssekgefsl
       61 eipttakviv vsflgyttre iqltgessyq vqlqpssqnl egvvvtaygt tnrkaftgta
      121 ttitnekfkd lqistitgal qgnasgvlsv tstgqpgenp tirirgigsf nasneplilv
      181 dgapysgsin ninpadvesi tvlkdasata iygsraangi lqivtkkgkg ktrfsfsgis
      241 gyskravkey ekispaqmye ltwetlknda iadpslltqn svaspeeyat kvvaprlryn
      301 pfdvaqpvgm dgklvdnakl lyhddwidel trtgvrndyn fnisgsdpan tisyflsggy
      361 lhdqgiiies dfkrytgrar vdikpttwlk sgvninlays nqnypyqgsg ggsdvlsfar
      421 rigpiypvyl rdrttgdyll dgngnkifdf gnnsaelgil rpaaetrlyv pgqnpaattt
      481 lnpitnerlt angilygevq llkelsflsq yainynqida nlfwnpfygd gttsggysyr
      541 gitnlyaqnf tntftfkksf gnihylniva gmeavknrse ittasttgft stystqpsyg
      601 tvqsssgtld qsrmlgffgr lnydvaekyh lslslrrdgt trfadssrwg tfyavggawn
      661 ldkeafmksa eflsdlklka sygtqgnqfl pgsfpylgvy qsgwnigsas gvivnsvnng
      721 yltwekqqql dlgvefgfwe drltgsvvyf rrtsdallfd rplapssgin dvsdnvggve
      781 nngievelns lnikkknfew rtsfnitklk nkitqpapgt tqekggswyy wylpeyagvd
      841 asdglptwym ddpdnegkki ttkdynlatr yhvgsrlpdy tggitntfry kdfdltilas
      901 falggkmydg dyaglmgafn sgtalgsnas idilnrwqsv dnpgdgqtpk lttaainata
      961 sstrflynld ymrirnitlg yrlpqhllrq fhlenarffv dlqnpftffg gpkgtdpeag
     1021 glnaqsgsnn tttnktlaig inigl
//
LOCUS       WP_098194706            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098194706
VERSION     WP_098194706.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111569
     Region          21..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllllmll csgsllataq qvlkgtvkds vsqqpvpgat vkvvgtnkgv vtnengefel
       61 tvpanaqiqi ssigfenvil kasfirknvi fmkmrslela stvvvgygsq rrgtltnsis
      121 tvnssalspe knivsdvgka lqgrvagvfv anssgtpgst pniqirgtqs vnataggpll
      181 vidglvvegn tislnsinpq dienievlkd aasaaiygar gsngviiitt kkgrmnsaps
      241 fnvnaytgyn nvptnrrmls teeyrsafnd arnnrisdid nllnnpgnlt pgqisqlnne
      301 knrlngqlda lqladrstdw inavknknap vnniqasmsg ggsknnyyms igrysedapi
      361 gtgtferytg kiditqivnd wlklngnini tqgatknmsn nlvsafnarp dtpkdpvykp
      421 dgslgyyvgy qqhpfgvlmd nknknknimy lgnlsadikl fdglqfrsaf nttkyntvsr
      481 nfyspfsylg yysggeqetn gydnlsytfd nyftynkris klginatlgy tyysnefssf
      541 gyeingfpki dgisgpaags sygssgmips lntynkeisd ayflrtgfdw egkymlnasi
      601 rrdgssklle dkryswfpsi sggwdiaken flynnglfnq lklrasygis gnirpvgywd
      661 aqnllivgsy mgtsalklng iignpeirwe rtkqvdvgld aallnnrlsf tvdfynkltd
      721 glvsrnevsw iygasaipdn ignirnrgld levafsskag aaftwkvssn mninrniiis
      781 mkdsltnygt ytfggpmsks kvgqsvgsvl vyeslgvdpq tgdmiyndrn kdglwntndm
      841 itvpiampkf iggttislgy kgfglealfs yvsgnkvydy yeqtlrnydl dyfgvmpnkf
      901 divnkrwrqp gdktdvprai tgahgagnst dwnyrpstqf vydasyvrlr nlsvsytvpk
      961 klvaklkmns arfyvaaqnl ftisdyigfd peaasnsgii tsnlpnprst vlgldlsf
//
LOCUS       WP_098195079             933 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098195079
VERSION     WP_098195079.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 933)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..933
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103680
     Region          58..932
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklfpinkpg arymkqwgwa laaaislkas aqsdttvllk ndsswlsqkv qlwnkqsska
       61 dyvgaagsiy nkdvnstpva dvtnlmagri aglytlqlsg mngadaaafy lrgrtpiivi
      121 dgvvrsftnf npdeiesitv lkdalatamy gqraangaiv ittrnagkhn feinasaqag
      181 vmdflykpkl anafqyatly neaqenmtpg stprytqdel aawsnhtndp yaqpdvnwyd
      241 eiikqnplqq rynislagks snyhyftsle hfaqggnfit spsnsystnn dykrynirtn
      301 aavafnkdie ltlnvfgsla tgyqpgvgtv slannitstp qtaypvynad gsyggnsqwt
      361 nnlhagavss gylvnterti aadmalkykl ddfvkglwvk gqlsmnnyyl emidrsksfa
      421 vyqpddanpg eyirygengl vdagtaevns qirqsyynam igydrswksh qlnllatynv
      481 dnninnftel dlqyknlgln asynwnktyf aelglnygam nryepgkrga vfpslglgwv
      541 lsnmpffhpk nisylkiras vgqsawgdpn syfaylqnft igttgynvge tnsnisgvee
      601 arlvnkgitw ekalklnigv dasfydgqls ltadyyrnky sdelmvrgqn sgimgipfpe
      661 enigesrysg feasvnfspk tsgafkyfvn anfsaakntl lyngnpqypy swlnrtghpv
      721 gqsfglvadg fyqestditk tanwqgytpq pgdimykdln gdgvinaldq qaigtekpll
      781 yyglsagfsf kgldfsflvq gvnnrnfylg pnessafyng ygnvlemhmd rwtpannvna
      841 afprlslgtn innnqtstfw mrsgdyirlk nveigynfks llfphgkirt lrlfmngynl
      901 ltwkkdegdf dpesrmsifs nqriinggit lgl
//
LOCUS       WP_098195140            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098195140
VERSION     WP_098195140.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113670
     Region          23..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkflllis lllqmtafaq dvtvtgtvrs asdnvaligv siavsgthhg tttnqdgkfs
       61 lqvardavlv fsylgfetqq vavngrtnid vqlkpggsel sevvvttalg ikkqqkalgy
      121 avqevsgetm aktktatals altgkvagln vnnttdlfrn pgislrgrnp lividgipdp
      181 dadpyklnpd diesisvlkg taagalygam gvngailytt kkgrkgklnv efnsstmfqp
      241 gytvipevqt vygggdqgky ayvngsgggt egggwiwgpk ldqrdpstps gffettqyds
      301 pidpttnqri ktpwvsrgrn nirnffrtgl lstnsvsasi gsekgsfrva anhiyqkgvv
      361 pntdlnnssf siggnyqlss kltmdaklty nkeysdnypt vgygppnyly nlilwigpdi
      421 dirdlknywi pgkeglqqrn ynlswynnpf fvanellngy krnnsfgqvt fdykitdnfs
      481 vklrngfnqy ssnsdlrepy syvaysyisr gnystdvsny fdinsdliln ynhefskkfk
      541 invtaggann yrryessytt tdgltipgfy slsnsinplk asntlrerrt maaygmldve
      601 algflylslt grydktstlp vsnngyfyps agvsavlsdi irlprvisfl kvrgswakvn
      661 tgfinannpy ahittyglgp kwnnvpsltw pttfispglv petvqsgeyg ialglfgnrl
      721 nidatyfrnk dynnfanval sqgsgytsil knanvylrkg wefmlsgipi rngdftwdaa
      781 inlssvhrwl kdatdnpdgy lglvkegqrt driyitesra pdgqaiynsn gmqaytpvgq
      841 yfglgdadwi ygiqntfkyk nlslsfsfdg rlggliystt nqkmwwggta kgtvnsyrdd
      901 anegkstyvg pgvvvtegsv sydaygniis ddrkfapntt avnyisfmqt tsggmlnnyh
      961 yyngtylkmr elvltydfps kwikgafnsa tvslignnlf ilskipnvdp daesdnlqtp
     1021 smrsigfnvn lkf
//
LOCUS       WP_098195535            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098195535
VERSION     WP_098195535.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111298
     Region          46..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkialqnpkl ligfllnrfi asmalkcgvl llaalmtvsa vlaqsksvsg svtdettgek
       61 mfnvsirikg tttgtltkqd gtfkltvpgd dailvfssig yesqeisvag kttldiamkt
      121 nvnslndvvv vgygtvqkrn ltsavatiss kdflqggyns pmqmiegkva gltvsnpaag
      181 dpnrgtdiqi rgasslnagn gpliiidgmp ggdlrnialq diesitvlkd aaaaaiygsr
      241 gangvvlvtt kqakagnvsv tydsyfehdv vankpdilsa eefldkgrdt drgartnwyd
      301 elirtdnfgq nqllavgggn ensmfrisgn frtktaidia terkeygyra nfrqkalkgk
      361 lifsgnlsqr takeeytnyd afkqavklnp tlpvmdpddp tmfntfqgyd tynpvqdlla
      421 rengadqnys iidlnarlni lsnlsteikl akqsremlrr eyytsksaes ilnnrtgrar
      481 lqnerwndyt lewinnyntr idkheidvma gysyqefvtq gfwaenmdfl sdafsynnle
      541 agqwnreegr lgmdswkske kliaflgrln ynfdgkyfls asfryegntk fgvdnkwglf
      601 pavsaawrvs slpflegskt vndlklrasy getgrsgfar ytslaryggy grylndegew
      661 iqvygpanny npnlrwerav synigvdfsl fdnklsgnld ffdrrsngil dnydvpvgpy
      721 lheqmfvnvg ttsakgvell lnwnvynsrn fsysttiaas yaksklvsws nnefqgnyry
      781 lqdlpspgnp gpayrldpgt elgsfygyky agvdedgkil vwkdgvvgke kiiasseang
      841 drdrtyighg apryelgwgn tlryksldln lffrgrfdyq vlnlyqmyyg lqaepginll
      901 kdaytrnghi tsgkvitdyf lengdyfrld nltlgwnpkf ktdfiknari ygsirnvftv
      961 tkftgldpta igvvgltpgy galdvypvtr tytiglqvtl
//
LOCUS       WP_098195580             959 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098195580
VERSION     WP_098195580.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..959
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105744
     Region          136..>946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyistkiqf srelfskara gkpallklgt talllfisfq alvaqtvkln anktpfekvc
       61 kqiekqtgyy fvyakdlkdk alpvtavvkd episkaleiv fkdlpysykv vdkvvsvnta
      121 epkpipgsts aisdtftlyg qvfdqgipng glpnasvmtl ttkrmtltda tgnfvlhgvk
      181 weeklvvryi gyedytttts snlkrriiim klannqldkv vvtaygktsn rfntgniiti
      241 sgkeiedlpf qnplmalegr vpglvisqvn sdpsspfkie irgrnslnpt iptdpliivd
      301 gvpigpldli kstqtsgnld ispgldqsgi sagytggqsp lfginmhdie sisvlkdada
      361 taiygsrgan gviiiktkkg efgenrvnvn vskgfthpsr fynfldtdqy ramrkeafan
      421 dgieissdpt apgyapdlli wdstkytdwg kyfydalgqs tnasasvsgg nklstyrisg
      481 ayfdrqnigq rggtknmsls tnygirskne kfmlnmslnv gknkvdaint sdkstlppna
      541 pdplksngel nfdeyrgiyq fplafkslkq aynsntdris gsvnlsynii kgldftatlg
      601 ydnsnmeaks mipvaasdpv sntpptgsvn ngttkntsln fdptlvynks igqgiftamv
      661 gftynskets skfiratgft sddlinsmsn apnisvndrs aeykyaglys qigyrfkery
      721 linfsgrrdg ssrfgadnrf gnfgsigagw iiteepwmkt fipniltymk frgsygstgs
      781 dqvgeyqylt qwgnniaang dftvypyngv vpiisllhan nefhwernnk legaiefqlf
      841 rkinvnaswy knlcdnqlvs yptgiftgyt sftanlpakv enkgfelnit aqimrsanfy
      901 wnvgfntsrn sntilafpnl elspyanryk iggstndrfl leyngvdpet geftytdan
//
LOCUS       WP_098195633            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098195633
VERSION     WP_098195633.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118008
     Region          33..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmnvivklqr lcccigiisl chldtmaqsp giikgtitde dgtaipsasi lnknnkkvvi
       61 sdpkgnfsiv aqkgdsiiiq mmgyqrygfl tnttqknydv ilhsavrnlk dvvvtalgir
      121 reerelgyaf sevdgdaink aketnvinsl agkvpgliin staggpsgss rviirgntsi
      181 tgnnqplyvi dgvpmdnsny gqvgdtkyae gvdmgdaisa lnpddiekis vlkgpsasal
      241 ygssaangvi littkkgsrs kelgvelsst atfenqltkr dgvqylygqg rsgqlpldqq
      301 qaqgtmfinf gprldpninv igfdgvsrpy alaednfdsf frtgsslnnt lsltnatdks
      361 nfrfsagdlr yedivpnsni rrntfsfsgr skfgerldvs vratymkekv knraglgdsp
      421 tnigqnfngl annidqaifs dtykspggdy vewgggqyrl npywvlyems nltnkdrltg
      481 sinanykvnn wlnlmarast ditfldyqky spvttplals glmntmnqky ttnqadfiat
      541 ftkklnknik ltarlgasln qryrkgttga ysnmtvkdvv sinsyqdksi vennirreir
      601 sayglltfay kdylyvdatl rrdgsstlpg gnnvysypsv sssfiftdaf kihsnvlsfg
      661 kfraswaevg sdtdpymldv yynlypfsfn gvqpaklats iipntnlkpt rtrsfetgln
      721 mkffngrlnf dgtyytahsr dqinivpapv ssgyskqiin agmitnkgve lmvsgtpisk
      781 kdfswdlsvn farnineves lapdvpfial searwlgllv aakpgekyga imgydyqrdp
      841 ggniilnpnt ltpvptadrr vlgkgvfdwt gglttkfnyk nfslnavfdv kygadifsmt
      901 dlflvvrgss vktlpgreew iaseearmaa kmslgewraa gnvkgyvpeg vvqtgtdseg
      961 kpvyekntqa vdpstywsqf ysdgngiavp fiykatyvka reitlnyslp rsfnrkigfk
     1021 sasvglvarn pfilykdvpn vdpdsnynns ngqgleygsl psrrgwginl nvkf
//
LOCUS       WP_098196118            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            caeni].
ACCESSION   WP_098196118
VERSION     WP_098196118.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga caeni
  ORGANISM  Chitinophaga caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Chitinophaga caeni"
                     /db_xref="taxon:2029983"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115493
     Region          24..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkrlvvlfl llvtlagqgm aqsrtitgtv tsvedgspii gatviikgtn lgtvtnvdgt
       61 yslnvpdgkd ilifkfigms dkevkisgst vnvtlqadvk tltetvitan aikrekrslg
      121 ysaptvksde ltrgqapsal nglsgkvagv nitgtanapg sssrivlrgg ssiagnnqal
      181 ivvdgvpidn ssqiggssla stdfgnrand inpddiesmt ilkgpaaaal ygsrasngav
      241 iittksgkkg agnkkneitf nsavtfsnvl klpelqneyg qggggqldlr enwswgakfn
      301 gemqgwgqei ngvrqekpyv aqpdniknff elgrsannnl sisgagekst yylslnalns
      361 dgvmpgdydk ynkysvrfng ttelsnkfts sinvsytkin snmvaggqga ssvynnvlqt
      421 prdipldkmg nlnnpyygyd ldkgtygyyg aytvspyfil knyqnnnyvd rvagnfalhy
      481 kanswlevtn rlgadvysdr rnyiapkfsv kpvdqsgvdy nqnnirsnvg syseveynls
      541 eitndlmitg kkqltqdlsl svmlgnnirq rayhslsaat nssglvipgy ynlansngnq
      601 ttsnydekrr lvgvygainl gykdmlyldm tarndwsstl pkknnsffyp svsgswvfte
      661 llkdkgisni lnygklranf aqvgndadpy sltnyyskas inggfgstif pfngvpgftv
      721 ydevgnpnle peittayeig telnffnnnl tvdfsyyhni sknqiipvpl ayssgyvqat
      781 lnagkienkg velslrgtpi rtsyglnvef ygtftknvsn visvktgqlv vggfngmsiv
      841 aaegqpygsf yavdiarddk grvivdedgy pewtdspryl gsynpdyqas lgtnihykgw
      901 nfnmlfetkq ggvffsrtkd imafvgtsae tvrggrdphi wpnsvyldgd gkyventdrk
      961 fnpevyypsn mppgtsivda syvrlreasl syrlpknlln rtpfgditlg lfgnnlflwt
     1021 aksnefadpe instgagnaq gfdftaqpsl rnfgfnvkvs f
//
LOCUS       WP_098280029             308 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Bacillus cereus].
ACCESSION   WP_098280029
VERSION     WP_098280029.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..308
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35373
     Region          5..173
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
     Region          <252..301
                     /region_name="Abi_C"
                     /note="Abortive infection C-terminus; pfam14355"
                     /db_xref="CDD:433897"
ORIGIN      
        1 mgildifskr nkdnqksifk ydeipeplrv qiihiwrdai gqyvtggsyy thnssnetwd
       61 fihkslckey glvnliskgh nvfekciyfl heeksvervl diielsfrvi dteirtdryn
      121 wadkgitqpp ddaiqelnkr fqehgigyqy lngkivrvds dfiyreavep avnlmfgegf
      181 egaseefmka hehfknrndk eavtealkaf estmktifik kswklpqkqt ashliaglfa
      241 kelipsnlqt qlnslkttle glatirnqtt ahgqgeksvk iprhlvayal hlcatntvfl
      301 ieayktkk
//
LOCUS       WP_098401550             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia albertii].
ACCESSION   WP_098401550
VERSION     WP_098401550.1
KEYWORDS    RefSeq.
SOURCE      Escherichia albertii
  ORGANISM  Escherichia albertii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia albertii"
                     /db_xref="taxon:208962"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53660
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtriktnarr ffsllipfff ftsvhaeqtv spakpvtvea knetfapqhp dqylswkats
       61 elservdala edprlvilwa gypfsrdynk prghayaitd vretlrtgap knaedgtmpm
      121 acwsckspdv arliqkeged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaeramn aigkpfekgg rfdqqsmvcg qchveyyfdg kdkavkfpwd ngmkvenmeq
      241 yydkiafsdw tnalsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkatlqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gataaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_098410484             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Thioclava
            sp. ES.031].
ACCESSION   WP_098410484
VERSION     WP_098410484.1
KEYWORDS    RefSeq.
SOURCE      Thioclava sp. ES.031
  ORGANISM  Thioclava sp. ES.031
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Thioclava.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Thioclava sp. ES.031"
                     /db_xref="taxon:1798203"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55892
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egearvamtp dsalqlqklg hecfietgag vragftdeay eaanvtvikt
       61 aaalfkevdf vikvrppsdt evkrlkpgqt lisffypaqn eellkaaekt ganviamdmv
      121 prisraqkmd alssmaniag yravleagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigastslg aityafdvrp evaeqiesmg aefvyldfee aakdgaetgg yaapsspefr
      241 eaqlakfrel apdidivitt alipgrdapv lwtkdmveam kpgsvivdla aerggncelt
      301 vpdekivsdn gvtivgytdf psrmatqssa lystnirhmm tdltpekdgv vvhdmeddvi
      361 rgatvayqge itfpppkpkv aaiaaqkpke kakeltpeek raaevaefkk qtrnqvtlla
      421 vgaivllgvg lvapasfmqh fivfvlscfv gfqviwnvsh slhtplmavt naissiiilg
      481 allqigsgsw lvivlaalsv fmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_098413977             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio sp.
            ES.051].
ACCESSION   WP_098413977
VERSION     WP_098413977.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. ES.051
  ORGANISM  Vibrio sp. ES.051
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio sp. ES.051"
                     /db_xref="taxon:1761909"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54778
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agesrvaasp ksveqliklg fdvaiesqag klasfddaay eaagakivss
       61 eevwtsglil kvnapivdke knideiallk dgatlisfiw paqqtelmaq lsskninvla
      121 mdcvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaefltv efqeeagsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgkpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqvittd ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 irgvtvvkeg eitwpappik vsaqpqakqe qpvkkepkie qptsptkkiv glvaavgvfa
      421 wiasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gdgvvsflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_098421292             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter sp. LV10MA510-1].
ACCESSION   WP_098421292
VERSION     WP_098421292.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. LV10MA510-1
  ORGANISM  Marinobacter sp. LV10MA510-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter sp. LV10MA510-1"
                     /db_xref="taxon:1415567"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56023
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeiy aderrvaatp psvhkliglg yqvtvetsag eaahyhdsay eavgatiatd
       61 vgalwsdsdf ilkvrapmen palgkheadl mkeggflvsy iwpgqnpell eklaarkvtt
      121 faidslpris raqkmdalsa maniagyrav veaashfgrf ftgqmtaagk vppakvmvig
      181 agvaglaavg aanslgaivr afdtrlevke qiesmgaefl qldfgeeegs gtggyakqms
      241 defikaemal faeqakevdi iittalipgr papklitadm vksmkpgsvi vdlaserggn
      301 celtepgkiv ekhdvtligy tdlpsrmakv asdlyatnlf hllseltpek ngqpqvnmed
      361 dvirgltvvl dqevtwpppk phtpvspkaa pgteepsaeq kaaarkeser rslvgkgvvl
      421 iitiaalygi gayapdsflr hftvfvlacf igwqvvwnvt pslhtplmsv tnaisgiivi
      481 gailhlaqae slavgimafv avliasinvg ggfrvthrml kmfrr
//
LOCUS       WP_098423206             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter sp. LV10R520-4].
ACCESSION   WP_098423206
VERSION     WP_098423206.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. LV10R520-4
  ORGANISM  Marinobacter sp. LV10R520-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter sp. LV10R520-4"
                     /db_xref="taxon:1761796"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55989
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeiy aderrvaatp psvhkliglg yqvtvetsag eaahyhdsay eavgatiatd
       61 vgalwsdsdf ilkvrapmen palgkheadl ikeggflvsy iwpgqnpell eklaarkvtt
      121 faidslpris raqkmdalsa maniagyrav veaashfgrf ftgqmtaagk vppakvmvig
      181 agvaglaavg aanslgaivr afdtrlevke qiesmgaefl qldfgeeegs gtggyakqms
      241 defikaemal faeqakevdi iittalipgr papklitadm vksmkpgsvi vdlaserggn
      301 celtepgkiv ekhdvtligy tdlpsrmakv asdlyatnlf hlvteltpek ngqpkvnmed
      361 dvirgltvvl dqevtwpppq pqtpvspkaa pgteepsaeq kaaarkksdr rsliskgvll
      421 ivtvaalygi gahapdsflr hftvfvlacf igyqvvwnvt pslhtplmsv tnaisgiivi
      481 gailhlaqae nlavgimafv avliasinvg ggfrvthrml kmfrr
//
LOCUS       WP_098428290             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Bacillus sp. AFS088145].
ACCESSION   WP_098428290
VERSION     WP_098428290.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. AFS088145
  ORGANISM  Bacillus sp. AFS088145
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Bacillus sp. AFS088145"
                     /db_xref="taxon:2033514"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34633
     Region          5..164
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifetyskr mkkvegkiqd vyiyteipek lrvqaahils dtiginnnsa wnyihstmak
       61 elglfsltdn myhkdvdhcl dflmicsdee aidfielaff vidsealrtd yftsraifii
      121 kqspdeaiee lnyrfkdnnv gyefikgelv ridrqfihke avkpaiklly eedfqgaade
      181 flkahehyrk gnhkealvea lkafestmkt icdkkgyayq kdkdtsskli sillennlip
      241 eylrnhftgl rttlesglpt vrnkkaghgq gsalvtiepy fveyainlaa tnivllvnaf
      301 kss
//
LOCUS       WP_098453808             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sanguibacter antarcticus].
ACCESSION   WP_098453808
VERSION     WP_098453808.1
KEYWORDS    RefSeq.
SOURCE      Sanguibacter antarcticus
  ORGANISM  Sanguibacter antarcticus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Sanguibacteraceae; Sanguibacter.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Sanguibacter antarcticus"
                     /db_xref="taxon:372484"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53278
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipretr pgerlvaatp ttvaqlvklg ydvvveagag aeasfsdtay resgaaigda
       61 atawssdvvt cvnapddasv aqlrpgativ ammapaahpe rvaafaergv salaldavpr
      121 israqaldvl stmsnvagyr avieaaevyg gmftgqvtaa gktapakvfv igggvaglaa
      181 igaagslgaq vrafdvrpea geqiesmgaq fvqaqaaqqa vssdgyaqem tseqerltav
      241 myaeesahad ivittalvrg aaprtltaam vaamrpgsvi vdlaasgggn celtvpgsti
      301 vtdngvtivg ytdltsrlpk htsqlfgtni vnlmklltpd adgqvvldme dvvqrgmtvt
      361 lagevlwppp pvqvsavpag apvevaptvd pavraleeke aarragqrkl vgyglgavll
      421 glsvafspaa fagyftvfvl avfvgyyvis qvshslhtpl maqtnaisgi ilvgallqlg
      481 ndswwvtsla fvaasvasin ifggflvayr mismfrkda
//
LOCUS       WP_098464006             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Isoptericola jiangsuensis].
ACCESSION   WP_098464006
VERSION     WP_098464006.1
KEYWORDS    RefSeq.
SOURCE      Isoptericola jiangsuensis
  ORGANISM  Isoptericola jiangsuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Isoptericola.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Isoptericola jiangsuensis"
                     /db_xref="taxon:548579"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53150
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpresr agerlvaatp atvrkltalg hdvvvqagag sgaalpdday aeagarvvpp
       61 gevwtadvvt cvnaptpdei allrpgatlv aqlapgshpe lvevlaagqv talaldavpr
      121 israqsldvl saqsnvagyr avveaaeefg gmftgqvtaa gttppatvfv igagvaglaa
      181 igtasslgae vrafdvrpev geqiesmgat fvqadgasqe vssdgyaral tsdqeaatra
      241 tyaaesarad vvittalvrg tapttitatm vaamrpgsvi vdlaaagggn celtvpgqrv
      301 vsdngvvilg ytdlpgrlpr htsqllgtnv vnlltlmtpg kdgevvldld dvvvrgmtva
      361 hagevlwppp pvqvsaapaa ppppeppagp speevaeqqr lrgrrrtvla algavvagla
      421 iaasppdavg hftvfalavv vgfyvisavt halhtplmaq tnaisgiilv gallqigvdd
      481 wlvttlavva asvacinvfg gflvanrmir mfrrdtpvtq eatr
//
LOCUS       WP_098459959             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Propionicimonas paludicola].
ACCESSION   WP_098459959
VERSION     WP_098459959.1
KEYWORDS    RefSeq.
SOURCE      Propionicimonas paludicola
  ORGANISM  Propionicimonas paludicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Propionicimonas.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Propionicimonas paludicola"
                     /db_xref="taxon:185243"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53298
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipletq vgetrvaatp ktvaqliqlg hsvlvekgag tkasypdady aaagatvads
       61 paiwaaemva kinppseaei aklregavlv sllaparspe lvaalnerki talamdavpr
      121 israqaldvl ssmaniagyr avveaanefg sfftgqvtaa gkvppakvfv sgagvaglaa
      181 igtakslgai vratdlraev aeqvqsmgge fvavkaeqqk ssdgyakeas eaynqaaaqm
      241 yaeqckdvdi iittalipgr paprlitaem vatmkpgsvi vdmaasnggn vegsvadklv
      301 vtengvkiig ytdlagrlpt qasqlfgtnv vnlmklltpa kdgevvfdfe dvvvrgmtvs
      361 kdgevlwppp pvqvsaapta aveakpvedp avkaareaaq akakttrqli wsalaaalvv
      421 lavtfspasf vgaftvfala vvvgfyvvsg vahslhtplm aqtnaisgii lvgallqlgs
      481 tniavlvmsf iaatiasini fggflvsyrm lgmfkkea
//
LOCUS       WP_098457282             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Flavimobilis soli].
ACCESSION   WP_098457282
VERSION     WP_098457282.1
KEYWORDS    RefSeq.
SOURCE      Flavimobilis soli
  ORGANISM  Flavimobilis soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Jonesiaceae; Flavimobilis.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Flavimobilis soli"
                     /db_xref="taxon:442709"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51977
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mhigvpresd pgqrlvaatp qtveklvalg ydvvvetgag adasipddgy vaagatigdt
       61 davwgcdvvv kvdaptvsev armhadativ armspdddpa lveamraagv ialnlnsvpr
      121 israqaldvl stmsnvsgyr giieaaeaya gmfggqvtaa gstpparvfv igagvaglaa
      181 lgaagslgat vraydvrsdv aeqiesmgat yvrvdaaaqe sadgyasels deqeaatqrv
      241 yaaesaaadv vvttalirgk apititaemv aamrpgsviv dlaasgggnc eltvpgekiv
      301 tengvtiigy tdlpgrmpkh tsqlygtniv nlmklltpgk dgqvvldldd vvqrgitvtr
      361 agellwpppp vqvsvappap asapapaepa paveqkarkg tgvlvagalt allvvaavaf
      421 stasfashlt vfalavvvgf yvvtgvthsl htplmaqtna isgiilvgsl lqigstdtvv
      481 tvlavvaatf asinifggfs vasrmlamfr kea
//
LOCUS       WP_098465489             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas lurida].
ACCESSION   WP_098465489
VERSION     WP_098465489.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas lurida
  ORGANISM  Pseudomonas lurida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas lurida"
                     /db_xref="taxon:244566"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38749
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay eaagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlas avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_098470368             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Serinibacter salmoneus].
ACCESSION   WP_098470368
VERSION     WP_098470368.1
KEYWORDS    RefSeq.
SOURCE      Serinibacter salmoneus
  ORGANISM  Serinibacter salmoneus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Beutenbergiaceae; Serinibacter.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Serinibacter salmoneus"
                     /db_xref="taxon:556530"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52496
     Region          1..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mnigvprqpd gagptvsatp ttvialiklg yevlvesgag qratfpdaay eaagatigta
       61 eqawgadiva lvhtpgveei arlspgatli aplapaqrgd llealaqrri talaldavpr
      121 israqaldil stqsniagyr avieaaeayg gmfagqvtaa gktapatvfv igagvaglaa
      181 igaaaslgat vrafdvrpea aeqiasmgge pviapqaqqe iaadgyakpl taqqqaaamd
      241 vyavetaaad vvittalvrg tapttiteam vqamrpgsvv vdlaasgggn ceatvpgeri
      301 ttpggvvvig erdltaampr htsqllgtni vnllklatpg kdgalvldme dvvlrgmsvt
      361 gpdgvmwppp pvqvsaapaa paappppsea elaaqraaae qaasakakrr tityallavl
      421 lglgltfapa sflphitvfv lavvvgyyvi sqvshslhtp lmaqtnaisg iilvgallql
      481 gnadtwvtvl afiaaavasi nifggflvty rmlgmfqkga
//
LOCUS       WP_098482030             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Georgenia
            soli].
ACCESSION   WP_098482030
VERSION     WP_098482030.1
KEYWORDS    RefSeq.
SOURCE      Georgenia soli
  ORGANISM  Georgenia soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Allobogoriellales; Allobogoriellaceae; Georgenia.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Georgenia soli"
                     /db_xref="taxon:638953"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53789
     Region          4..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 makrigvpre grdgerlvaa tpatvqkilk lgydvvvehg agtaatfadd dyveagarvv
       61 pldevwgsdv vvavhapddr rlgllregav lvaqlwpgah pdlvttlaer gvtalaldav
      121 prisraqald tlstmsnvag yravieaaae ypgmftgqvt aagkippanv fvigggvagl
      181 aaigtasslg asvrafdvrp eageqiesmg atfahfaagq qevsgdgyar elgagqeaat
      241 lrlyaeetar adivittalv rgkaprtits emiaqmkpgs vivdlaasgg gnaegtvpgq
      301 rivtdndvvi lgytdlpsrm paqtsqlygt nivhlmgllt pgkdgqvmld ledpvqrgmt
      361 iahdgavlwp pppvqvsaap aadvaptksg eelaaeaaaa tvakartrgi rntvlaglgf
      421 llatlamtig aeeflvpftv falavvigfy visnvshslh tplmaqtnav sgiilvgall
      481 qlgnsnpvvt vlafvaaava sinifggflv srrminmfrk da
//
LOCUS       WP_098493954             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Collimonas
            sp. PA-H2].
ACCESSION   WP_098493954
VERSION     WP_098493954.1
KEYWORDS    RefSeq.
SOURCE      Collimonas sp. PA-H2
  ORGANISM  Collimonas sp. PA-H2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Collimonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Collimonas sp. PA-H2"
                     /db_xref="taxon:1881062"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38543
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaetr pgetrvaatp etvkklvaak hqvlvqsgag isssitdeay aaagaevvga
       61 aaafgmetvl kvrapsadel pllksgtvvv gmlnpfdadn iavmashglt afsleaaprt
      121 sraqsmdvls sqaniagyka vlmaantyqr fmpmlmtaag tvkaarmlim gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfitdee keiaqgvggy arpmpadwmr
      241 rqaelvhera kqadiiitta lipgrkapvl iseetvkamk pgsvildmav dqggncplse
      301 sgktvikhgv hiigegnlaa lvaadasaly arnlldflkl iinaegglvi nreddivaat
      361 llcsagevlr k
//
LOCUS       WP_098553909             531 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_098553909
VERSION     WP_098553909.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..531
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54860
     Region          3..531
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple iatgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagasva
       61 ataaelwags divlkvrqps adevalmreg gtligfvwpa qhpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmas isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvve elckgkdgti nvdfdddair
      361 gltvikegnv twppppikqa vvapkpaaap aaapakskgh ghagepmsak alaivfavga
      421 vafllvgqfa pasflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvappldela nagdrpsgli lglavgaltl tavnmfggfa vtrrmlamfr k
//
LOCUS       WP_098553444             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. JKS000303].
ACCESSION   WP_098553444
VERSION     WP_098553444.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. JKS000303
  ORGANISM  Burkholderia sp. JKS000303
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia sp. JKS000303"
                     /db_xref="taxon:1938747"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39213
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvpvetr stecrvaatp etvkkyvsqg hqvvvqagag daagvpddvy raagatigta
       61 adalsaalvl kvrapnadel almspgavlv gmldpfdaag harmaahgit afaleaaprt
      121 sraqsmdvls sqaniagyka iveaarhypr flpmlmtaag tikaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpletdee rdaaqgvggy arpmppswlq
      241 rqaalvhera kqadivvtta lipgrpapvl ltedtvramk pgsvvvdlaa grgadgggnc
      301 pltrpdeivv rhgvtfvght nlasmmaada salyarnvqe flklivpaar dggdaiainp
      361 dddivaacli ctdrkvvklh
//
LOCUS       WP_098510659             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis sulphurea].
ACCESSION   WP_098510659
VERSION     WP_098510659.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis sulphurea
  ORGANISM  Amycolatopsis sulphurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Amycolatopsis sulphurea"
                     /db_xref="taxon:76022"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38118
     Region          8..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maedgsrltv gvvtesrpge rrvalvpklv prlaqrdltt ivergagaga qltddaytea
       61 gaelgdpwqs dvvvkvaapa aeeiaklkrg alligfldpr gdpdgiaale kagirafame
      121 avprisraqa mdalssqssv agyravllaa ekltrffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgaqttgydv rpevgeqvrs lgarfldlgi eavgeggyar elteeeraeq
      241 qrrlteaitk fdvvvttalv pgrkaptlvt eeavqgmpag gvvldlages ggncalsrpg
      301 edvvaygvtv saplnlpagm pahaselyar nvtellellv tkegelrldf sdevvagacv
      361 agregses
//
LOCUS       WP_098693167             364 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            terpenica].
ACCESSION   WP_098693167
VERSION     WP_098693167.1
KEYWORDS    RefSeq.
SOURCE      Nocardia terpenica
  ORGANISM  Nocardia terpenica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Nocardia terpenica"
                     /db_xref="taxon:455432"
     Protein         1..364
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37607
     Region          8..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(21,76,95,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(50,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 metthgtrig vvrettpeer rvalvpkivp slskqgvqvv veagagagal ipddayvdag
       61 atigdpwsad vvvkvappnd aeiaklsagq tligflaprn adnkigalka agvqafavea
      121 iprisraqvm dalssqanva gykavllaaq estrffpmlt taagtvkpat vlvlgvgvag
      181 lqalatakrl ggrttgydvr pevadqvrsv gaqwldlgid aageggyare ltddekarqq
      241 qaledaikgf dvvittalvp grpaprlvta aavegmrpgs vivdlagetg gnceltepgk
      301 vvvrhdvtia splnlpatmp ehaselyskn iaalldlmlv dgklepdfgd qvladscvtr
      361 eeqs
//
LOCUS       WP_098660498             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Priestia megaterium].
ACCESSION   WP_098660498
VERSION     WP_098660498.1
KEYWORDS    RefSeq.
SOURCE      Priestia megaterium (Bacillus megaterium)
  ORGANISM  Priestia megaterium
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Priestia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Priestia megaterium"
                     /db_xref="taxon:1404"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35548
     Region          6..171
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 merfklfser nlldksndvy dyelvpqrlr iqlthilney indlgfstqf wrlvvlsikk
       61 efgilnlpgq gdrdavmnfl lgeddpetid tidlifhlin ksiidlnkti snrsgmrqls
      121 mdkdreivyq lkeciqeany rfkqnsfgye iidgqlikie nqmvhkevik paiqllfdeg
      181 fetasneffq ahehyrkgey tdaiidagra festmkiicd kkqysysqkd tasvlinklv
      241 tnnllpsnlq nhfnhlwntl scglptirna ngghgqgvqe nqvpeslvnf sinlaasniv
      301 flvklykes
//
LOCUS       WP_098716913             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_098716913
VERSION     WP_098716913.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53632
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfeksg rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tvgihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvilqweeqa rkngllsq
//
LOCUS       WP_098791258             297 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Priestia megaterium].
ACCESSION   WP_098791258
VERSION     WP_098791258.1
KEYWORDS    RefSeq.
SOURCE      Priestia megaterium (Bacillus megaterium)
  ORGANISM  Priestia megaterium
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Priestia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Priestia megaterium"
                     /db_xref="taxon:1404"
     Protein         1..297
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34406
     Region          5..159
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mgffqlfskr nnpakehdvy rydqipkklr iqivhilset fntsplrdkl wmmleqnikk
       61 efgilslegf daeesvkkfl lssnhrqain aidlifhris eliknssepv tkhlledrit
      121 nsidelnfrf kqcgigyefi dgqlikinnh lihqnivkpa iqllfeeefs tassefsqay
      181 khyrkreyee aitdaerafe stmkiichkk gytydekapa krlinvlltn nfipsylqne
      241 fnhlcntlec glptirnrng shgqgvtene ipsylvnfal nlaasnivfl vniyksn
//
LOCUS       WP_098840763             339 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Bacillus sp. AFS033286].
ACCESSION   WP_098840763
VERSION     WP_098840763.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. AFS033286
  ORGANISM  Bacillus sp. AFS033286
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Bacillus sp. AFS033286"
                     /db_xref="taxon:2033498"
     Protein         1..339
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=38943
     Region          36..204
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
     Region          <283..332
                     /region_name="Abi_C"
                     /note="Abortive infection C-terminus; pfam14355"
                     /db_xref="CDD:433897"
ORIGIN      
        1 melllsfnyc himeniafkw yngskkvrrl tlgildifsk rnkdnqksif kydeipqplr
       61 vqivhiwrda igqyvtggsf ytnsssnetw nfihkalcke yglvnlsskg ynvlekcicf
      121 lqeeksverv ldiielsfrv idteiredry nwtnkgitqp pddaiqelnk rfqehgigyq
      181 ylngkivrvd sdfiyreave pavnlmfgeg fegaseefmk ahehfkkgnd keavtealka
      241 festmktifi kkgwklpqkq tvspliaglf ekelipsnlq tqlnslkttl eglatirnqt
      301 tahgqgeksv kiprhlvaya lhlcatnivf lieayktkk
//
LOCUS       WP_098956264             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudonocardia sp. N23].
ACCESSION   WP_098956264
VERSION     WP_098956264.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia sp. N23
  ORGANISM  Pseudonocardia sp. N23
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Pseudonocardia sp. N23"
                     /db_xref="taxon:1987376"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52257
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mriavvaest ksetrvaltp etvrkvadlg yhvtvqsgag elagfadsay aeagadvaeg
       61 pvwdadvvvm inapqaeeia nlregsalva mlaprfeaer vtalagqgvt alsmdavpri
      121 sraqsmdvls smaniagyra vieaahafgr fftgqvtaag kvppakvlva gagvaglaai
      181 aaanslgavv ratdpraeva dqvrslggey laveveqeas tdgyakatse dydrraaeiy
      241 seqaadvdii ittalipgrp apklitaadv asmrpgsvlv dmaaaqggnv egsvagevvt
      301 tdhgvtiigy tdlparlpaq asqlygtnvl nllklmtpgk dgrltldled tvvrgltvah
      361 ggevlwpppa vsvsaapaaa qaaaapvekk pekvrsplak alppiigala lflvtafapa
      421 elaghltvfv laivigfyvi gnvhhalhtp lmsvtnaisg iivvgailqi gtgggglvlg
      481 laaaatllaa inivggfavt rrmlsmfsrs pgrs
//
LOCUS       WP_098966517             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_098966517
VERSION     WP_098966517.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38789
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael alikrgtvlv gmlnpfnndt iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera rqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_098970230             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098970230
VERSION     WP_098970230.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110784
     Region          9..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrketqkllv lsllgiisvn ltaqqkakkd tikgldevvv talgikrhdk slgystqtin
       61 sdeilqtqnn nwaqslegkv aglkiqtaga gplgtsritl rgdismnmgn ngalivvdgv
      121 plsdkrtgtg tgaygagsgg dlpidygdsf nsinpddies vsvlkgpsas alygsrgsrg
      181 aimittksgk trkgkiqvtl nsyssfdtvl kwpdyqyeyg qgtqqkdkng nyyysygasp
      241 dgvntgstss afgpkfdgqy yfqydpaieg qskerklwkp yknnikdfwq tgatysnsis
      301 iaqsnestaf rtsisylkne wmmpntgfnr fngaisldhk lsskvkigtk vnfsqttsdn
      361 lpatgynnqs isyfmifqnp nvdldwykpi wrkgqeqvdq vhpfssyidn pyliayenln
      421 ttnkkiltgn invsyqfakn ldvafksgle wsnemrtqrr pwssanylkg yyreqyirym
      481 dlnndvlfty knkfgdfgit asaggsiryy estmsdyrai glnkaglyql snatsldnrl
      541 pkpndnqvns vyalanfsyk dmifldvtsr ndwsstlprh nrsyfypsvs ssfvlsdifk
      601 lksdqfnfwk lrlswskvgn dtynymldky yenstfsgsv espllypnpn lkpemitnie
      661 ggldftllkn rltfnftayq insknqsivi pvlyetgynk riinsgelrn rgielvlnay
      721 pvknkdfswn inanwsmnrn kilslpdefq gqpytmasvg gvvyynavvg gslgdmygyg
      781 lmyspdgqvi ygadgltakp temkkignay pkwraglqne fkyknftvsf sfdgqykgma
      841 ysqshhkmse qgklthtlag rdnpgglivg qgvvqnadgt fsqntkgipv atyygdyyrr
      901 anvetnsfdt sfiklrdari sysfpksvte slkmtditla vfgrnlwmwt kfplfdpeaa
      961 tlddstitpg vemgqlptar tvgiqlnvkf
//
LOCUS       WP_098970374             919 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098970374
VERSION     WP_098970374.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..919
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103288
     Region          35..918
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqtyffrk vgpffiavpg llysqntkek dslkskqied ivvigyktqk rssltaavsv
       61 isdkklkdsn tpdvagllqg kaagaqilpg ggspgstasv kirgtsting psqalwvvdg
      121 vmmngvpnld pnqiesinil kdatstalyg srgangivqv ftkagisgks sltislnnsf
      181 ntfsngrfkl mdgtqlydyf tslknsptip gelrnpgynw lkdgtqtgav qnytidfrgg
      241 sensktyisg nyydesgtvk nydynrlsfr inheqtvkpw lilkpklsls ytakkdrqgs
      301 leqmylnmpw dnprdqngdl irlddaytgk wygrdysnyl ydlqwnygks nqldlignfd
      361 aeikltdylk fvttnnityk nyddmyytdp rsisgnsnkg glaesyvkdv skffnhmlrf
      421 dkdfgvhnvn alaayeytdr mykiskagvy aivpgaeifd ngaitgqkps gkkydrafna
      481 flfnaeyvyd kkyfvqgslr sesssafgts kknglfysys lgwnihkenf fqvkqinewk
      541 lrasrglvgn tpspnygwqd lyaltqiyng qigatwnqlg nkdltwesiy qnnigtdira
      601 fnnrlsinvd yfnnktrnll vlvtlpsltg vdrqylnvgd vknegwefnf nyaliksqsv
      661 nwdvgfnvst yknrvlstrn nstqllsnnq vaiagndvts fymrkwmgvn pdngaaqwev
      721 vnadgsksit snynqatlqi vgaatpdyyg sfttnlsinn fylnanvyfs qggqiynsyr
      781 elfdsdgayp yynqmvlknd wnrwekpgdv athplpifnn ntltnkpssr yledasyvkl
      841 rslrlgynfp qslteklhvr slsiyvmgen lftitkfsgv dpevgpsdad krdgnpysgn
      901 agaiypiprr fslglnfsf
//
LOCUS       WP_098970566             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098970566
VERSION     WP_098970566.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110647
     Region          2..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkvligls lvvsweayaq kvpqkgsadt lkinekkide vvitalgikk ekkaigyavq
       61 evkgdvleka kepnfinsls grvaglnikn stdlfqdpgi slrgakpliv ingvpdrtad
      121 lwrvnaddid nisvlkgpta salygsvgkd gaimittkkg kkgkisvsfn nstmfqtsfi
      181 ripkvqtvyg ggnngkyayv ngegsgsegg gwiwgpkldq kdptttsgyf etpqynspvd
      241 lvtgnlvplp wisrgkdnik nffetgliqs nnvsvdwgse katfrlsfsn iyqkgivpnt
      301 nlkttsisla gsvnpikdlm instltynke ytsnfpevgy gptnylynlv lwtgadvdvr
      361 dlrsywvagk egyqqrhynv syynnpyfqa yeylrpyykd nvlgnfnvey qivpnlsaka
      421 rfganiysln refrepksyi gygnkslgny tqvtgnyfdi tselglkyqn hysenftlrg
      481 eayisnfyre lknseirtdg litpgwynlf nsigplfvpa dgkrnrkefe qinsvygyvd
      541 lefyktfffn mtarydkvst lqkgnneyfy psisgsllln qllnlptwin faklrgsfaq
      601 vssgkiadnt ygyisafeks nvnwngkpsf sfgdilidgn ikpetvdswe vgtnigllkn
      661 rinfdvayfq trdynnlani piseamgyks yltngnvfqr kgieitlnad vikksdfkws
      721 allnlshyrr ylkeayggad httvyneang rfnfvkvger adkltampye tspdgqlvlq
      781 ngypvnstap feskmgysdp dwtygfshnf syknfslsll fdgriggtmy sttnqkmwwg
      841 giapgtvtpy rddanaghnt yiaqgvkivs gsitydqngn vksdtrvfap ndmsvnynay
      901 mqstsnafes nyhyykqtfi klrevtvtyn feksfinkln vsaasislig rnlwlasdik
      961 nvdpdsgmdq lqtpatrsfg inlnvkf
//
LOCUS       WP_098970720            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098970720
VERSION     WP_098970720.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119808
     Region          22..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknyilfpvi cfssliaaqq htvtgkites atgkplsgva viiqninavt ntdkngifsl
       61 ttaesrlsll iskagyesqs ldiqlplqke ltislsakvt eieevslstg yqkipkerst
      121 gsfssvdnkl lqqqvttnim drlpsiangl tvskgltedg qlmirglstm qgpknplivv
      181 dnfpyegsis ninpniiesv tilkdaaass iwgaraangv ivittksakt sqttsvefta
      241 nttlsakpdl dysrqisssd fidvemklfn qgyydtdlns anhpaltpvv tivnkekqgl
      301 lshndamnei nrlrnidvre qyskymyqpv enrqyalnif gstpklswts figydnntgn
      361 lsekyerlna rfqniwkpte kltvttgmyy tntitksgrs aynsitmrnn wkvpyiefad
      421 dagnplvmnh mldqdyknsl qgtglldwny ypltdwmhni vqnktnefil naglnyriik
      481 gldidikyqy qhnngesrtl ydeqsyyarn yvnnfakknm dgsisfvvpk ggifdkglse
      541 tavnnlrgql nynrnfgkhs isaiaggeir etitrydnnr yygyntntls tagidytkqy
      601 pnfvtgsmdf iergtslret nirfvslyan aaytynkryt lsgsvrqdas nlfglktnqq
      661 wnpfwsagls wnvsnetfyn sgflpylklr vsygfngnid psmvavttil fdtdlsvytg
      721 gntaridkfy npnlrwetik mmnigldfgl knniitgsve yftkegsnlf gtapldyttg
      781 vksmlwnvag mqghgldvel ktrnidkaik wnsiinfsiy ndkvtnyylp ttfannfvvn
      841 sgtiapisgi vglpvygvfa ykwagldpkt gdpqgylnge vskdytkiln sakgiedley
      901 fgsaipskyg sfintvayrq fsldvgityk fgywfrrssi nytdlissrd ghsdyakrwq
      961 npgdelwtnv psnpyttnsa rdafyngssi lvergdhirl qyltlnynfr keslrslpiq
     1021 nlqlfasann lgilwkanka gidpdynwgt yslkpvttys iglrtqf
//
LOCUS       WP_098971363             946 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098971363
VERSION     WP_098971363.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 946)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 946)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 946)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..946
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104200
     Region          32..945
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqsnlkysc liavlyfgmn vdaqvtsdsa kvqkidevvm igygsrkkvd nttsissisa
       61 eevtktkvln asqaiqgkaa gvqviasdap gstptvmirg lgtvlggrtp lyvvdgmftd
      121 ninninsndi ltydvlkdaa alaiygnraa ngviiittks grgklsvsyd glvgirnplk
      181 tikmasgsef anynnagaks dylnpdqpyn tdwfkeitrt giynqhnlsi sgssesakyf
      241 lslgnydeqs ilkgtnynrt tirtnnefri tkgirlaqtl satftnetpk sfgaftsayk
      301 qsslvpvyyp ngkygqpifd kstgnigyvg grfndvgnpv mklahdnqra knfllqgglk
      361 ldidifkdlk ftsqfsgeyg nyksynfvds rrfwldsdpm rtesqysats pltrltnksq
      421 nysnwllnny ltytkkvgeh dielvagtea svksgletli inrknvpvse dywnlsgvdy
      481 ygnlfsegdt kalesikgnr nttisyfgrl qykfmnryll satirrdgss qfaagqrwgt
      541 fpsfgagwii sqesfmqdgf fdmlklrggw gkignqtvpl nylplslgss ynygfgsspv
      601 sngvtvnkgy dpdlgwevte esslgldfgv lnnrltgtfd iynrktknli lgvvpymatg
      661 iselnyshmg svvnkgfevg lnwadkvged fsysvganys ynknklasmd tskpvsqivg
      721 gnlgngidtk lfnpsavgya lgsfylyead gyndkgelkf kdlngdgtid akdkrffdsy
      781 ipkstlgvnv smsyknwdfa lngygafgfk vyngkkaqrn ggenveasva nnfwtpnnrn
      841 aanpvnpssi pvastfyled gdffrinnis vgytfknvtd ymksiklyvs ainpfvfqky
      901 sgytselsgy nptdttaegd pykragield ayptlrsfvf gvnlnf
//
LOCUS       WP_098971463             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098971463
VERSION     WP_098971463.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109152
     Region          32..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrkqckigv lallllaeyg faqtkdslsk enaikevvvv afgkqkkeei tgsvqslkak
       61 dlsnlqngni lqgiggkvag vqvissgqpg sqptirmrgi gsinassdpl ivldgipysg
      121 nlnsiaasdi esisfledas snalygsrga ngviivntkr gknkglgiea dvrtgvnfrs
      181 iqdypvytsp qdyytafynr arigevarlk qpgavpsgpt phdvgltaln rlgynvynvp
      241 faqlirqdgs fnpdarllyq ddwkkllfkp alrreatvgi nangdqvksy tslhylddkg
      301 ylissgferf girsnidysi tsklkltsal sytyskqdfg etggfsnpfq farnispfyp
      361 vflrddnyqr lydsygnply dygdgsgpng atrsyavfen pvgnlqkdks qttsnitnin
      421 lglnyeiikg ldftynfgay lenvrnlqfg nteggtsssv ggtltkgsqf rytlnhqqll
      481 syqkkvdkhn fniligheln kiknegmsgn kqqlllpnsl sfdnavkitd lsgngyeyav
      541 egyfsrllyn ydgkyffnan vrrdgssvfa pesrwgtfyg lgaawnvake dflkdnsvvn
      601 alklkvsygq qgndnillda strdyyayqd iyginnfgdd kavvspkkig nrdlkwetsk
      661 nlnagfeasf fqnrltlnad yferkvsdmi yalplapsnv gsyvkygnig dminrgvqin
      721 anvdilkked iqwsiyangt hykntitklp aeqrgtglvs glfilteggd rytyylkefa
      781 gvnpengdal wyrtsinptt qkeektitnn ykeatdyntg ksaipkvygg fgtditykrl
      841 nlsvnfayqf ggygyddiyr slfhsdtygs nystdldktw tpenpnaslp rvdltstnqn
      901 gnstlyliks dyislqdvtl syqlpegfaq qaglsglkvy ltgnnlylws krkgydpras
      961 ltgvsdsyry sllssvslgf kltf
//
LOCUS       WP_098971747             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aeromonas
            sp. CU5].
ACCESSION   WP_098971747
VERSION     WP_098971747.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas sp. CU5
  ORGANISM  Aeromonas sp. CU5
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Aeromonas sp. CU5"
                     /db_xref="taxon:2033033"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53102
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevaiesgag qlasfddaaf eaagasvvps
       61 vwqadlifkv naptdaeiaq ikdgatlvsf iwpaqnpelv kklserninv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggefl kldfggedga ssdgyakvms defiaaemal
      241 faqqakevdi iittalipgr papklitkem vdsmkpgsvi vdlaaatggn ceytkptelf
      301 vtpngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgnvainse dvvqrnmtvi
      361 qagevtfppp aiavsaapqk pvaapikkae akqpsnkkfv fgalgiaafg wiasvapaaf
      421 lshftvfila cvvgyyvvwn vshslhtplm svtnaisgii vvgallqigq gstlvtalsf
      481 vavliasini fggftvtqrm lkmfrkd
//
LOCUS       WP_098972022             974 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098972022
VERSION     WP_098972022.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 974)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 974)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 974)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..974
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..974
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107941
     Region          14..973
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklntsllv lvltssiavt naqqkkdtmk tkeiegvvvt algikrekra lgyasqeikg
       61 dvisdagqtn avsalsgnva glqvtapssm ggstritmrg issvtgenrp liivdgipld
      121 nsnvngydte rgaggrdygd atfdinpddi esvtvlkggp aaalygyrag ngaiiyttks
      181 akrgktevql ntgvsfesiy irpklqnlyg ggselalrtq eidgviynip efgtdeswgp
      241 rydpnlyylg wdsfdpelpd qymklkqwva srkdvddffr vgttytnnvs vaksfentnv
      301 rfsytntkin givpnseikk dnfslnvssk ltdnlkadal fnyvrtagfn rpeqgygdns
      361 vaqkfyqwgq rqldfselqn yklpsngmqr swnrtswddg tpnfadnpyw tiyentsadt
      421 rnrffgnagl tynfskkvyv sgkvygdtys qtitsrvaig saaqslynvr ksnnsefnye
      481 grvhyndnfg dfslntfagf nimdrkwdim egrsvgglii pnlynlsnsr evprasnlsf
      541 hlgvrslfas vslgykdflf leatgrndwf smlnedqfyp sltgsfvfsk vlkadwvsfg
      601 kvragwsria ggsdpfirgt fatignsfwg sptysmpvik geknltpdlk ttkeiglemn
      661 ffknrvgfdv tyydvkttnl ilplpidpat gygskrinag emtnkgieam vnitpirstd
      721 fswdftwnft rnrnklvelq snlenliltd apfrvqlaaq vgysygtilg tdfvydsngn
      781 kvvdatgryk asaikplgsv lpdynmgfrn sfkyksfgls flidvqqggk yfstthmwgm
      841 nngmleetal ggnreagvil pgvkengapn dirldaptwg ksyyntvdaq nvfdasyikl
      901 rditlsydlp ksfignsiqg irvsafarnl fawnldykgv dpentsygsg niqgleggsl
      961 pstrmygvnv nfkf
//
LOCUS       WP_098972026             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098972026
VERSION     WP_098972026.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109031
     Region          31..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttgllv lvlsssiava haqekkdtik tkeiegvvvt algikrekks lgyasqeika
       61 galsdgttnt gniaaqlsgk vaglnvttnn nfggssnlli rgvktlgggn plividgspv
      121 nntytqekni dygnalsdin qediesinvl kgaaasalyg erglngvivi ttkngkgkdd
      181 gswgvtfssa iqvgfidkst fpeyqtkyga gyaqafgska gdglnyanfg adaswgpkfd
      241 pnlmvyqwds fnplspnagk atpwvaakng pikffnnpas yinsvtlekg qkgknisfty
      301 enmmsdglmp nshlnknnfs lkvnydltpk lhstfystlt lqdtkgrsit gysnntvtgf
      361 rqwwqtnvdl ndlesiylan vdpkvasaan nygnvtwsrk saangapayw nnpyfqayqn
      421 ytsdkryrsf tyaqvtydll dnitvtgkvs ydrsnltaen rlafgslpqa fgqsnnsigs
      481 gyarrdvlrn etnydlmvny kfditdninv sgvvggnirr nyvnsvyast egglvvpgiy
      541 alsnskkapl asdeiesitq tnsgyvtasf dffkkfyldg twrvdqsstl pagnnvynyp
      601 svtgslimse ildtknwmnf wklranyaev ggtadpyqlv nnyrsagils ntgiynpils
      661 qpnpdlrpqr skefeigtea hflrdritld vayyktktvd qiinlpvssg tgftgkvina
      721 gridntgvev qlglvpiksk dftwnidvnw sknknevidl ypgitnllln sfqggvslna
      781 rvgeawgtli gadytylngq kvidpktgky lqnpnqiign ttpdwiggir nsfnykgfsl
      841 sflidmrkgg difstdmyyg lssglyketa vgdyrdkpiv lpgvlpdgsq ntiglspfad
      901 nnaamgyktq psrefvydgs fiklreasig ytlpksllag tkiydakisi vgrnlwiihk
      961 nlpyadpeam vggginsygw sigsmpttrd lginvtfkf
//
LOCUS       WP_098972030            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098972030
VERSION     WP_098972030.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110687
     Region          12..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttsllv lmltssvaia naqekkndtv ktkeiegvvv talgikrekr slgyatqevk
       61 gdavnknptt nflnnlsgkv agleikqstn fggsinvvtr gyksildsnq alfvvdgvpv
      121 mnkninssgq tngaggydyg ssvsdinpnd ietinvlkga aatalygsra qngaiiittk
      181 rgkknkegig mefsssitvs sidkstfpky qtqygqgygg nsfpgtyqgs pivgfnndas
      241 ygsayddsmv wqygafipgs ptegkltpwr makngpitff ekatnyvnsi sfsggndvat
      301 yrfgytntna tdimpnseli knnftgnasy kladnltanf yasyitqktt grnttgyndn
      361 imtnfrqwwp tnvdikdlqy lykmsrknyt wnmrsrtdlr pafwdnpyfq ryenyqndsk
      421 drfagnfsls ydvskdinll fragrdsytm sveerkavgs ytgnsfglnv vnqpsgyals
      481 eykfsetnyd ligtykknit ddfnvnvlvg gninvqkdys nqqstsggls vpglytians
      541 assparpvis dlskyiygvf gqvslgyknt yylegtyrrd qttalgvghn vytypsisgs
      601 ivfsnliqqs wlnfgkvraa yakvgsdtga drlrnrylpq asygdvlvna ynailrnpel
      661 taqslnnfef giearmfnnr fgfdvawfqn kgfqqilplp isfgtgaasq yknagelrtr
      721 gfevsvngtp iktnnfswdl slnwsnpwsv vtalnpgien itigalqggv sinaplngdy
      781 gsiwtsdyvy dsngqkivgp ngaylvtdka iynqgsfqar wtaglsntln yknlslsfli
      841 dwrqggkvys ldqsygygtg lypdsvglnd lgnpvrntla ngggvimpgv madpnnpghy
      901 ipntirldks vssqnlqtdl pgaayvydas fvklrevait yrfdkkifns kfiqgmsmsl
      961 ignnlwiihk nlpyadpeag lssgniqgyq sgvmpttrni sfnvkinf
//
LOCUS       WP_098972256             955 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium].
ACCESSION   WP_098972256
VERSION     WP_098972256.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..955
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106591
     Region          49..954
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksytsigh vscvvmltva gvsfhaqiqs nsdtisrknt peasvlrekt dtlsplnkpl
       61 sekvssieev vlnagyykvk dkertgsiak vsakdienqp vtnvlsaaqg rmsgvsitqn
      121 tgtpgggfdi qirgknsirr egneplyiid gvpqasetps lystkilpws sinplnainp
      181 ndiesfeilk dadataiygs rgangviivt tkrgkkgrse lklntsysls ritrpmemmn
      241 teqyismrrq afqndnvayp atmydingtw dqsrhtdwqk eligsmaday svqlsmsggs
      301 enfsyqisyg hneqttvlpa dfkyktnnin anfsyltpdr klefnlvntf sfqqnnvqnd
      361 dltlksimls pnapalytsd gsinwengtf nnpvasllse ysnktaffnn glnvsyklfp
      421 flslkmnagi syqnfeersi kphtinnpsf gqtsmnstss rnnqvnfsyi lepqlvgayk
      481 tgnhqfefll gatlqktqse qgaiqgkgfe snalidniga asvktisdqv rsqynytavf
      541 arfnyqlkkr yivnltgrrd gssrfgannr fgnfgavgaa wlfseepflk dvkwlslgkl
      601 rgsigttgnd kigdyqylnt yiissgiyng qtglnparly npdfswektl kkelalelgl
      661 wngrfnfsga yyentssnql vgiplpattg fpsvqsnlpa kirntgweld tsvqvlrkgk
      721 frydtsfnls ipnntlvefp nlegstysnq yvigypttia rvyqyegidp atglykfkdf
      781 ngdgkitspd dnkaveklgv rffggwsnnf rwgnwsasfl wqfvkqrnwn ynrqmllpga
      841 lsnqpvevld awspsnpggs ymeysagynp qklslhgffq nstaaisdas yirlknvqln
      901 yripmqkmgi keamiyvqgq nlmtitnyfg mdpefylvgy lpplktyslg fqvtf
//
LOCUS       WP_098972368             962 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098972368
VERSION     WP_098972368.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 962)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..962
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106707
     Region          40..961
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvfkipvsv syltgrvlli gaisaspmfl sqkndsikek sidevvvvgy gtqkkskvsg
       61 avaeasldkl ssrslsgvge vlqgkapgvt vvneggdpng vpkvnirglg gvngetplyv
      121 vdgvvfngtp ninpndiqdi silkdasaai ygarssggvi littkrgkkg altvdfdvky
      181 ginqawrlke slnaaefqnv mrqayenagk lsslpmafna dkytdggitr tnwmneifrt
      241 gtiqeynvnl sggseksrff vgmnhrnleg illntqakry nfrvnsehkv kdwltigenm
      301 yysysdgnta ntkngytgal vaamyyppnv svytptgafs glpidvaggy gdminpvayl
      361 krisiqnpth eilinpyiev slakdlkfrs nfsqtfklgn ikeftsrvle vgkifdtnsl
      421 eyqsnnists laeqlltykf slgkhnfdal agftfqktte dgfrakafdf rseaevfryl
      481 qnaadtnkev ysykyrqalt sylarvnydy agkyiisllg rrdgtslvak qnhfanyysv
      541 sggwvasken fmneiswlsn lklrgsygil gnlggvsfqa vnplmirdnn iifgqdptqn
      601 iayyattkpn rdlkwgkseq tnfgvdasff hnslslqfdy fvkksthqif nvnlsstely
      661 idrylnaglf qdkgyelgin yngkskgdft ysigatisql kntvkqlagv deifvssnnv
      721 rgvlkptrik vgeslysyyg yrtggifqtq aeidnykdan gnliqpnakp gdikflkkdg
      781 ntgtlnnndf vnlgnpypkf syglsynmtw knfdlnlffq gvygnkifng lkfislnpgg
      841 tgqnynmdrd ilnawtpqnt ntniprlmqg dpggnyskvs dfyvedgsyl rlknltvgys
      901 lpgelykkld vnkirvyvts nnlftitkyt gfdpevgmet ygvdtgrypq arsfifglev
      961 gf
//
LOCUS       WP_098972376            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098972376
VERSION     WP_098972376.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119304
     Region          22..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtlatfav fllplyftaq einisgnvks engssvsgvn itdkntgkta ttdengnfti
       61 sahpndilef mspefsvytv evsskrqysv vlkktnekqi egvvitalgi akkkekigys
      121 tqevgtkqfe tittpsignl fsgqvaglnv snptgmqqap qftlrgnsnl vfvidgvive
      181 kevfqnldpn nieninvlkg atasalygsr grygailitt ksakkkgfsi efsqntmitg
      241 gftnlpktqt eygngshgky efwdgadggv ndgdmiwgpk fvpglqiaqw nspirdkvtg
      301 qtipwygavs gtqyndksry ervpidwryh dnlktfmkpa vinnnnfavs yrnnkdvyrl
      361 sgnfmnyddr vpnsylqkyg vnfssenhfg ekfifdtkfn fnqtftpnip nydynpsghm
      421 ytiliwmggd vngkdlknhm wvpgqegrqq anwnyawynn pwfgaeyykn qnrtniinaq
      481 tgleykatqd lsvkgkisiv enhskteils pysyfnydap rsggyilkdn ktwnlnydvl
      541 atykkkisen fdftinaggs afyyknnkne rstdglkvpe lysfdnsiga lknytylkek
      601 liysaystid iglynaffin fsgrndwsst lpmanrsyfy psasisavis nlvkmpeavn
      661 llkvsaswak vaydfqpysi rnyylnnkgi tfngnptfyy ptilnvensl kpeqtksyel
      721 glsagflnnr itldatyfrt ldynnilqfp saessgfisq yvngneyttk gfeislglvp
      781 vkttdftwkt linwstfeqk ltsiynnmpn ynniklgerm dsyydyewqk spdgkvilda
      841 ntgmptrant qtnlghfnpd wtfginnsfk yrklnlnigi dgsiggimrs qvvekmwwgg
      901 khpnsvayrd leyanpgtyy fvpdgvnyna atgqytqhtk aisfqdwaqn ypyqarvtqn
      961 eseefanvfd rtfiklrsvv leydfsylln pkgmvksfta nisaynlamw kksknlysdp
     1021 dfqirsgrtg dttndiqdps srwfgigfnl kf
//
LOCUS       WP_098972525             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas sp. CU5].
ACCESSION   WP_098972525
VERSION     WP_098972525.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas sp. CU5
  ORGANISM  Aeromonas sp. CU5
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas sp. CU5"
                     /db_xref="taxon:2033033"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53195
     Region          7..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mhvgsqhrht klglaalllt swlgasgwaq adeattqgki earselfake hadqftswqa
       61 tsesrertda laedpnmvvl wggypfakdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpevvnti gcadchdtas kefkggkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eayydeigfa dwthalsrtp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqskemlqgi vkqrkeavie tklkvekqlv hahfeakaaw
      361 dagatdaemk dilqdirhaq wrwdyaiash gvqmhapeva lkvlgsaldk aadartklar
      421 llaakgishe iaipdistke kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_098972385             966 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098972385
VERSION     WP_098972385.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 966)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 966)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 966)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..966
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..966
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106402
     Region          31..965
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnklivkigl lpslflging lygqntdstk aakieevvvt aygvkkekks lgysfqdvkg
       61 qtlvdaketn vtnalagkva glqvikggfg pgssskinlr gfnsfkgdnq plivvdgvpl
      121 snslgakpkn nneaanndfw npdldmgngl sdlnsedies msvlkggaas alygsrggng
      181 vilittksgk kkgglgisys tslgfeslfm kpdmqnnfsq gsngvvnpen sdnttswgpa
      241 ftesmkrydn lknffktgvn sqhnlsfqsn lgegsslyts agylhdnsqi pnstyerfnf
      301 makmnstfga nkrwtsevka qyistkgnnr psggqgdgnf ypaillmpqn iniidyregq
      361 mqnnvtsrwi tpnginpyws aynslnadkk drillngylk yqfndwlssd irlgtdfyal
      421 ntdarvwtgs srrnsystgn ekfyennyia sitakkdnlf gkwggslsvy gqmmetrtka
      481 lyfttqnlii pnafnvknts dnaavanfei dlwkkinsvf aaaeinydgy wflnattrtd
      541 wsstlnienr syiynsists lvltdmlnkm ngfhskfltf aklraayavt gnglepyely
      601 nnyvlstdpt ghitlsrqki lynanlkaek lktfevgadl kffnrvsldv syfnnnatgq
      661 lidlpmnpls gyekmkissg glhnrgfefv lntdilkken ftwnvnanls llrsnvdein
      721 gdvskypigg fdnitfytev gkpygaiygt kilrvedpns pyfgklivga nglpqatpdm
      781 qylgdqtprs lfgftssfay kniglsflvd griggkffsa tqlalqkagl asdtapggrr
      841 dnfvldavvq qnggyssntk eitqqdywaa vttgnlgite qnvydatnir lrniqlsytf
      901 pksifqkmal qsakvsftan nvwmiyskak gvdpesvfai ssnavgfenm afpttrsylf
      961 titlgf
//
LOCUS       WP_098972702            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium].
ACCESSION   WP_098972702
VERSION     WP_098972702.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110980
     Region          30..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknfcrlgh lqwmafssll fsgmaigqmr tisgtvtqng qplssvsvfq egadavtmtn
       61 asgkyqiqvs gqnlilifkh pdypeqkini gnltsisvsm drrerqieev vlnagyykvr
      121 ekestgsiak vsakdianqp vtnvlsaaqg rlsgvnitqn sgvagggyqi eirgrnslrt
      181 iatsgvdgnq plyvvdgvpi ggevasqysg saiaggsmnp lnsiapndie sleilkdada
      241 taiygsrgan gvvlittkkg rsgklglsfn ssysmsriis nlemmnteqy lnmrrqayak
      301 sgvttypsta ydvngtwdpq rytnwnktli gnmatasntq lslsggnedt tflisyghne
      361 qttvyskdfk ystdnissnl ahhskdrrfs lnvsnlftiq knnvinedvs rqsyllapna
      421 palynedgsl nwannsftnp vaaynatysn eniqylnnls aeyevvknlk vklnaginyq
      481 tfeewslrpn tiynpafvtg qssaysqayk ynqqrfsfil epqanwflek grnridilag
      541 ityqddvtkq gsmrgtgfes nifiqniaaa qtkvindqvt teyryaavfg rinyqwdkky
      601 ilnvtgrrdg ssrfgpnnkf anfgavgtaw ifsnekflke sewlsfgklr gslgtsgsdn
      661 igdyqyldtf avsstsiyng vtgiipsrlf npdfswektt kleaalelgf fknrinltaa
      721 wyrnrstnql vgyqlpaltg ftsvsanlna tvqntgvele lnarpftkgs fkwetgfnis
      781 fpknklidfp glsgstyanm yvigepisiv klyhleginp qtgqyrftdf ngdgkitspd
      841 drqvienigv ryfggwtnql qyknlslsfl fqfvkqkarn ynsvmtspgl mnnlpveald
      901 vwspdnpngf ympyqstana shtllqssda svsdasfirl kniqlsyrvp lgssnvfrev
      961 rlyiqgqnll tftnyfgvdp etgsssflpp lktyafgvqf nl
//
LOCUS       WP_098972891             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098972891
VERSION     WP_098972891.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109710
     Region          15..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlsa gvlffiggqt llaqkkandt ipqktkeide vvvvaygtqk kqsitgsitt
       61 inakqlqdaq asnamqsltg kvggvqisan sgqpgdppqv rfrgigslss snnplyvvdg
      121 vpfngninai snqdiesisf lkdasanaly gsrgangvvi ittkkakkgk fsvnfdtkfg
      181 vnsravkeyd iitdpgayye mfynrlvtdg vykgmtlgna ginaantmis dwlvynnynv
      241 adnqvidptt grlnpnakll yhddwsknlf kdrtrqeyni nisnsseknd iylslgylnd
      301 egyvinsgfk rytarlnnel rltsdikvgv nlnyaraekn apiqgagssq ysnlfswarn
      361 iapiypiwsr dtngnflldn kgqlqydfgt lsgpmglgrp yggtlnpygt tlldikrnte
      421 dnlsgrayas inflkdfnft ynlgydlvsg hyidysnnig gdaagyggsi tnattndyti
      481 tnqqllnwnk sfnkhalsvm vghetsdfks kmlagtknni aipdlpilsn atkfaglnsy
      541 ndnykvegfl srlnysydnk yffnasfrrd gssvfapenr wgnffglgaa wavtneafls
      601 gnkaitnlkl kasygeqgnd nilyagsvnl snrsyfgygr nyyayasqwe vvpdsdgnmt
      661 ivqvyegnrn ikwevsknln agfelslfnr vnidaqyfer gvqdmiynkp laastgtrfi
      721 aenigdmknr gvevsvdani fntpdfswnl fanvthykne itnlpssfis gvfkfekgvs
      781 aytyylrqfa gvdssngdal wymddangnk vttndytkak lylsdknlnp kayggfgtsv
      841 tykginvsvn fayqfggymy dnvyqgllps ggdnigqnyh kdvyntwtpt ntnaalpald
      901 lsrtnqmaas dlfliksdyi slqdasisyd lsknllpegl tgvkfgiygt nlamwskrrg
      961 mdprlariga sgnngvslnn ygvvrsisfg ltvkf
//
LOCUS       WP_098972893             981 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098972893
VERSION     WP_098972893.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..981
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107793
     Region          31..980
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msvklrvlsa galffigqas faqkakkdta ttkidevvvv aygkqkkeai vgsvsvvdek
       61 iiqtqqapsv lstlqgsvag lnlissggqp gtnptiyirg vgslngstep livvdgvpyn
      121 gninnisqdq vesitvlkda sstvlygsra sngvilintk kgklnsapkv tltsisgvss
      181 pavrlhktlg aadfmqyswq airnneqytn gltaaaaglk asnnlvstlg ynpynvatpi
      241 dasgnvapga sllwdtdwek eilnkaafkh ehrftlqggs dkttyflaad yldlagsvrs
      301 sdferiglrl nvdsnvkdwl kvgmngafts stssnpnqag ngytssiqwi ynianiyply
      361 mrdatgglll dglgnlqydy gdngtsgqlv naqrplfnne navgalynnk nivkrsnfti
      421 nayaqvnftk dlnlksqigy eqylldqnay thykfgaags vrgrvaqdrd lgktinftng
      481 lnyskklgdh gidaqalfev yqftydalaa qgtgflpnvy vlngstvpes vsgyvnrerm
      541 vsylgrlayn yknkyfvegs frsdgstrfs edtrwgnfys vggswvvske dffkndifny
      601 lklrgsygel gnnkilypng tqnyfpylsl yevgwnqlgq tgvilgnvvd rrltwektas
      661 tnvgldfgff nnritgtvey fnkksidliy aqplpestgs gsiitnvgsl knygweflin
      721 stnfknekfv wttslnfsli knkitemtqa sfingtkrwa vgrsafdfyl pvwagvdsad
      781 gmgmwylyek dsngniintk ttkdytlana vdnrqyvgss lpditggltn yfkvgnfdln
      841 ilanfsfggh vydssyaslm sgfsnagrqq svdvmnawqk pgdvtdtpin imkqnnnsgq
      901 strflykndy irlksltlgy nidpelltnf ginqfriflq gdnlwtwqsh kgidpeqnis
      961 gttdsrsyil ktmslgvtvg f
//
LOCUS       WP_098983923             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas sp. CA23].
ACCESSION   WP_098983923
VERSION     WP_098983923.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas sp. CA23
  ORGANISM  Aeromonas sp. CA23
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas sp. CA23"
                     /db_xref="taxon:2033032"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53423
     Region          25..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tclgasgwaq aadeaqpkgk iearselfak dhadqfrswk
       61 gtseskertd aladdpqmvv lwagypfskd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvinek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meeyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqndqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg ivqqrkdavt eiklkvekql vhahfeakaa
      361 wdagateaem kdiqqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakgish eiaipdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_098973018             919 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium indologenes].
ACCESSION   WP_098973018
VERSION     WP_098973018.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indologenes
  ORGANISM  Chryseobacterium indologenes
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Chryseobacterium indologenes"
                     /db_xref="taxon:253"
     Protein         1..919
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101035
     Region          33..917
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfttvlkv apafllasti mhaqttdsit kekkieevvl igygkqkksd ltgsitsvta
       61 kdfnggatsa gqliqgktpg vqitnnsgap gsgtkirirg tsslggensp lividgvpqd
      121 fvgvngvsdp lslinpndie tfdilkdasa taiygnrasn gvilittkkg sagrfkvnfs
      181 tvtslstkmg nvdvlnadef rqfvntyapa nyktklgnan tnwqdviyqt awgtdnnvsf
      241 sggikalpyr lsigyneqng ivrsnsfkrt svglnlnpkf fdnhlsvnvn akgtftdnrf
      301 vdggvikaat yfdptqpvys gnskyggyye wldnnspngy nvnassnplg midglrdvss
      361 vtrglgniql dykfhflpdl hfnvnagydy tkseghkvkd aryrigyedk gsenfysmek
      421 knklletyfn ytknisains gvdltagysy qdfniiipga mtyrgignnt kdvdfesrnt
      481 lisfygraif tiankyvisg sirrdgssrf ynltrdnvwg vfpgvslawk lneenfikni
      541 saistlklra gwgktgqqel palgvngnkp nnypalgayn psnpgayyqf gneyyymfrp
      601 anfnpnltwe ttvtknigld fgfaknrvtg sidlfrkdtk dllvfadepa gglsnaswqn
      661 igdmknegie gsvtiipvkn enttwelsfn athykpiitk lkdrggesfn mevggieggs
      721 gnriqahavg yapnsfwvyq qaydasgnpi sggyvdrngd gvintkdmyy yksttpdail
      781 gfstklshkk wdfalsarav lgnyvynnaa snsslksast neylqnifss aadykfsdfq
      841 yrsdiyvena sffrldnini gynfgeifsk gsnlkvygma qnvfviskys gldpevyggi
      901 dngyyqmpki ysigfnfqf
//
LOCUS       WP_099001317             309 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Enterobacteriaceae].
ACCESSION   WP_099001317
VERSION     WP_099001317.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35421
     Region          5..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifdlfskr qkrlrgevpd vyqytnlpnn frvqvihivk etigedygrg sdpggiykai
       61 ndtlcreygv fklrdypksn feavydffln ekdiekcldv ielsfkaidg yvrenhwrfh
      121 gheqksdsai eelnirfkes gigfqfesge lvrvdsqfih sdavkptlqi lgrskafega
      181 ndeflsaheh yrhqrfkecl ndclksfesl mkaihkkrsw eygstdtakk lissclsngl
      241 vpdymqnqfs slrillesgv ptirnkeggh gqgdevtnvp ehlasytlhl tasnllflak
      301 cdenftkkk
//
LOCUS       WP_099017991             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinicella litoralis].
ACCESSION   WP_099017991
VERSION     WP_099017991.1
KEYWORDS    RefSeq.
SOURCE      Marinicella litoralis
  ORGANISM  Marinicella litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Marinicellaceae; Marinicella.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Marinicella litoralis"
                     /db_xref="taxon:644220"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40139
     Region          3..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,76,95,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtitvgfvke rnegesrvam vpetaekilk lgwqvlfepd agvsagfpne aypemcqmak
       61 krndvlnaad vlvgvdalsd edlkeiknds vvvgmvspyq nqqrfdqava knitvfsmel
      121 iprtsraqam dvlssqasva gykavllaas eaprffpmlt taagtirpas vlvigagvag
      181 lqamatarrl ganvtgydvr petveqiksl gakfldlgve avgeggyara ltdeekltqq
      241 qnlakhltsv dvlittaavp grpapriita emvdamkags vivdlgaegg gnceptelgv
      301 tklvnnvkvi gpknlpatvp lhasemysrn vwnllnlmnh egefvinwed dilagcavtr
      361 egavvhpavt gikeggdks
//
LOCUS       WP_099025322             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium palauense].
ACCESSION   WP_099025322
VERSION     WP_099025322.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium palauense (Mycobacterium palauense)
  ORGANISM  Mycolicibacterium palauense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Mycolicibacterium palauense"
                     /db_xref="taxon:2034511"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38262
     Region          18..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(32,87,106,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(61,139..140,149..150,153..154,157..158,160..161,
                     163..168,170,172..174,177,200..201,289..290,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(134..135,139,142,145,186..189,209..211,239,250,
                     267..269,276,278)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(136..137,139,149,192..193,200,216..217,219..222)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(169..173,176,179,202,204)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtevdsgaar retktgsvsv gvvaesgade rrvalvpkav aalvksgvsv vveagagera
       61 llpdelytea gatvgdawaa dvvvkvapps aeevarlhsg qtligflapr nadtqipalk
      121 aagvqafave aiprisraqv mdalssqanv agykavllaa seatrffpml ttaagtvkpa
      181 tvlvlgvgva glqalatakr lggrttgydv rpevadqvrs vgaqwldlgi daageggyar
      241 eltdderaaq qkelekaitg fdvvittalv pgrpaprlvt aaavegmkpg svvvdlaget
      301 ggnceltepg qtvvrhgvti asplnlpgtm pehaselyak nltsllelmi kegalvpdfd
      361 devlaascvt reae
//
LOCUS       WP_099037763             506 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium neglectum].
ACCESSION   WP_099037763
VERSION     WP_099037763.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium neglectum
  ORGANISM  Mycobacterium neglectum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Mycobacterium neglectum"
                     /db_xref="taxon:242737"
     Protein         1..506
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51822
     Region          1..505
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresh vgetrvaatp qtvgqllklg ysvvvesgag aassfadaay veagasvgdp
       61 waadvvlkvn atsddeiakl rdgatlvsli spalnpelvq klsarpitvl amdavprisr
      121 aqsldvlssm aniagyravv eaahsfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivka tdprpevadq vkslggeyvs vdpaaaevsa tgyakemgdd ykaretalya
      241 elasdvdiii ttalipgkpa priitaemva smkpgsvlvd maasnggnve gtvkdqaivt
      301 dngvtiigyt dlagrlpata sqlygtnlvn llklltpekd gqltldfddv vqrsvtvvrd
      361 gettwppppv qvsaapapaa apvehkppkt pmttrrrlgi afsaaavlfa lialspaalq
      421 vhltvfalai vigyyvignv hhalhtplms vtnaisgiiv vgallqighg dvvitalata
      481 aillasinvf ggfavtrrml smfsrs
//
LOCUS       WP_099042102             364 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium neglectum].
ACCESSION   WP_099042102
VERSION     WP_099042102.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium neglectum
  ORGANISM  Mycobacterium neglectum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Mycobacterium neglectum"
                     /db_xref="taxon:242737"
     Protein         1..364
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38130
     Region          4..354
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,71,90,283,309,311)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,273..274,316..317,321,
                     324..325)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,223,234,
                     251..253,260,262)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrligvpret apgerrvalv pkvverlcgf glsvvvedga gggalipdeh yedagatign
       61 pwtadvvvkv npptddeitl lkpgsiltgf laprtrpela drlrearvtg fameavpris
      121 raqtmdalss qanvagykav lraaecstrf fpmlttaagt vkpstalvlg vgvaglqala
      181 takrlgartt gfdvrpevae qvrslgaqwl elgihaagdg gyaraltaee qaeqqlrlae
      241 aipgfdvvit talvpgrpap rlvtaeavrr mrpgsvvvdl ageaggncel tvpgetvvrh
      301 gitiasplnl patmpehase lyarniasll ehmltdgeiv pdlsdeilaa ccvtttsdql
      361 tetr
//
LOCUS       WP_099066438             391 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nostoc
            linckia].
ACCESSION   WP_099066438
VERSION     WP_099066438.1
KEYWORDS    RefSeq.
SOURCE      Nostoc linckia
  ORGANISM  Nostoc linckia
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Nostoc linckia"
                     /db_xref="taxon:92942"
     Protein         1..391
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41541
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dvvarlvkqg levwvesgag ersffsdpay eaagatiisd
       61 svklwseadi llkvsppqer edgrseidll kegavlisfl nplgnpvvaq qlanrkvtsl
      121 smeliprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkleeettaa ggyakeisea
      241 skqrtqevvt ehvknadvvi ttaqvpgkka prlvteemva qmkpgsvivd laaeqggnca
      301 ctepgkdivw ngvtiigpin lpssmpvhas qlysknltsl iqllinkeka lqvdfgddiv
      361 daacvthage irnqrvreal qalntqepav s
//
LOCUS       WP_099077764             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio sp.
            PID17_43].
ACCESSION   WP_099077764
VERSION     WP_099077764.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. PID17_43
  ORGANISM  Vibrio sp. PID17_43
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio sp. PID17_43"
                     /db_xref="taxon:1583451"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54621
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvviesrag vlasfddaay eaagakvvss
       61 eevwksglil kvnapivdee kgideiallp dsatlvsfiw paqnselmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgrpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqvitte ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvvkeg eitwpappiq vsaqpqakpq dpvkpqpkve eptspvkklg alavgvgafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsv iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_099085880             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agrobacterium tumefaciens].
ACCESSION   WP_099085880
VERSION     WP_099085880.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium tumefaciens (Rhizobium radiobacter)
  ORGANISM  Agrobacterium tumefaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Agrobacterium tumefaciens"
                     /db_xref="taxon:358"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55672
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely egearvgmtp dsaqalqklg ydcilqtgag kaagfsdday raagvtivds
       61 adalyagsdi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfae qqdgaatggy aapsspefre
      241 kqlekfrela pqidivitta lipgrdapkl wladmvammk pgsviidlaa erggncdltv
      301 pdqrvvsdng vivigytdfp srmatqastl ystnirhmmt dltpakdgkp vhnmeddvir
      361 gatvtyqgdi tfpppppkiq aiaaqkpker akeltpeekh akeraefkaq tksqvgllvi
      421 gtaalllvgl yapasfmshf ivfvlacfig fsviwnvshs lhtplmavtn aisgiviiga
      481 llqigsgnwl vvilaslsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_099096815             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Teichococcus rhizosphaerae].
ACCESSION   WP_099096815
VERSION     WP_099096815.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus rhizosphaerae
  ORGANISM  Teichococcus rhizosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Teichococcus rhizosphaerae"
                     /db_xref="taxon:1335062"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39558
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavlkerr agetrvaatp etarklmdlg lgvvvetgag agsgltdaay reagaeivpd
       61 aaaalagakv vlkvraplgt gegevdelal iprgalligt leavanprra qayaelgiea
      121 csmellprit raqsmdvlss qanlagyrav iegaaafdkg fpmlmtaagt ipaanvfimg
      181 agvaglqaia tarrlggrvs atdvrpaake eikslgaafv gyedeesraa qtaggyakql
      241 spefyarqae viaaavakad vvvctalvqg rraptlltaa mvesmrpgsv vvdiaadagg
      301 ncaltkpgea ivteggvkil ghtnwpgrip aaasalyarn lltflstfwd reakapklpq
      361 edeivrgvtl trggavvhpq lataaaa
//
LOCUS       WP_099104501            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            marina].
ACCESSION   WP_099104501
VERSION     WP_099104501.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella marina
  ORGANISM  Neolewinella marina
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Neolewinella marina"
                     /db_xref="taxon:438751"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109845
     Region          30..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklninhvhr gflfllfvlf assaalaqtt vtgtitdaen gdpligasil vtgtstgtvt
       61 dfdgnftlnv pagaesltvs ytgyatqtip ltgqteldit mtsgelldev vvvgygtvtq
      121 kqvtsavtsi dsedfnagni ndptqliqgk vagltiskvg gnanggsvir lrglssfggn
      181 qspliiidgv vganlntvdp adiesinvlk dgsaaaiygi qasagvilit tkrgaagdaq
      241 fsyrgyvtae eiakrpevad rnlylelvee tgrligaddp iafrnnvdyg gntdwidrvt
      301 rtgishvhnl sysggaggmt yrasvnyrdi qgigvdndgf rqingrlnin qsafndklnl
      361 svdvtatdrd adifnnnvfk yaitynptap arvdeagytv pdavaansld tyggyfeidn
      421 fdyfnpvaia qttaserqqt nilynlrasy diledvslsa sysrnredgi ngsfgsrfsr
      481 fgggaagspa rrgfasrsvn dnrndlfevt atyntdlgnn glellagysw qeyqfqgfna
      541 ggaglpsdaf gfnnlnvlnd iaagqiavgs yqasyrvigf fgrarlslgs aynitasvrr
      601 dgtsrngpen kwdffpavsa sadlvdalsl egpdqlkfrv gygitgslpn gnyaylqtfg
      661 tgpqfpqngg yiptispssn anpnlrfekk qefnagldfa fddyrltgsl dfyvrntgdl
      721 itsvivpspp flfssveanl nnvdlintgl elalgysfgd lggdgfsyep rltfstfstt
      781 ledngenpdf nfgaggvqef essspgspgq nldpvsrvii gedfggiytr rldvdatlas
      841 gqyvflgdge adkvlvgngl pdfsaslsnt frygpldlni flrgdfghdl vnmprnfygq
      901 qgnlatraie nvivndlflr gvtsapkvsd yfvedasfla ldnaqlgytf dlgpgtgfnd
      961 lrvyvagqnl fyitdysgvd pnvrffddqn sngiidggen altpgidrrs tffrtrsftf
     1021 gvnvgf
//
LOCUS       WP_099104485            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            marina].
ACCESSION   WP_099104485
VERSION     WP_099104485.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella marina
  ORGANISM  Neolewinella marina
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Neolewinella marina"
                     /db_xref="taxon:438751"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113981
     Region          23..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrlllvfgl tlfaigitma qntvsgtvtd eegegligvs ilaagtstgt vtdldgnynl
       61 tvpeggdali fsytgfttqr veinnrstid vtlepaseil eevivtaygi tkkeafsgsa
      121 dvvgseelet rnvtspiaai egnatgvqft sasgqpgssp givirgvgtl ngdtdplfiv
      181 dgiqfegdlt sinqediesi tvlkdassts lygsraangv vlittkrgne ggtqvsasvq
      241 hgfvsraipl ydevtpgqyy eamwealkns gaangdpafa sanifnslgy npfdvandei
      301 vgtdgklnpn antiyqsldw ydvmeqsstr tnynvnlatg gddhrvyfss syleeggyvv
      361 tteydrltsr lnadfdatnw ltmggsanvt vsnsrgpssa gsgsivnpfg fakgigsiyp
      421 vyvndrngnl vldeagnpif dsgegyseyg igsrpinqgr halqelllnd ertrnnlygf
      481 rffadfevve glnfrlnygr diqegiskey enniigdaqp tgrygevryr rqvenfnqll
      541 tynksfndih nldltlghes fdrnysqnsa saidqtaegi fefanfatpv slggytsvkr
      601 iegyfarany nfdtkyylsl sarrdgssvf adasrwgtfy sagvswrldq epfiqnisfi
      661 drlklrasyg evgnddlqdf flsqpryslt snagnpaiww sdignnnlqw etiesfdval
      721 eftlfnnfld gsleyykrns sdllydlpia lsnghnsfps nvgdmfnegv elgltgnlis
      781 krdlrwsvra tastfnneit slpdpfings krwdvgrsrf dfyllhtanv dpatgdqlfy
      841 myefdedgns vpviengvhq ttndwqeter aytgassipd flgsvsnnlf ykgfslnilv
      901 tygiggqild ngysammhsg sygrslhpdi lnawrqpgdi tdvprlengn idlvrtqstr
      961 fltdasflsl rnvnlsyvfn ssfvksigmn nlklsltgen lylmterdgl dpqynlagts
     1021 pgndfnparl itfglntnf
//
LOCUS       WP_099102487             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nostoc sp.
            'Peltigera malacea cyanobiont' DB3992].
ACCESSION   WP_099102487
VERSION     WP_099102487.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. 'Peltigera malacea cyanobiont' DB3992
  ORGANISM  Nostoc sp. 'Peltigera malacea cyanobiont' DB3992
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc; Nostoc cyanobionts.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Nostoc sp. 'Peltigera malacea cyanobiont'
                     DB3992"
                     /db_xref="taxon:1206980"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41000
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dtvarlvkqg levwveagag ersffsdpdy eaagaiiisd
       61 taklwgetdi llkvsppqer edgrsevdll kegavlvsfl nplgnpvvaq qlanrkvtal
      121 smemiprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkldeetvaa ggyakeisea
      241 skqrtqevva ehvknsdvvi ttaqvpgrqa prlvteemva qmkpgsvivd laadqggnca
      301 ctepgkdivw ngvtiigpin lpssmpihas qlyaknvtsl iqllikdkal qvdfsddivd
      361 aacvthagei rnqrvrdalq alsgvgag
//
LOCUS       WP_099105871             969 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            marina].
ACCESSION   WP_099105871
VERSION     WP_099105871.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella marina
  ORGANISM  Neolewinella marina
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 969)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 969)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 969)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..969
                     /organism="Neolewinella marina"
                     /db_xref="taxon:438751"
     Protein         1..969
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105933
     Region          28..967
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrnqlplag slllalflpc llfaqypvng tvtdrdgepl igvsilvvgt ttgtitdfdg
       61 qfqldiptdp aelrltytgf apqvievsrg igpievvmqe dianleqvvv tglastikrs
      121 nlanavatvs gdelsgvtsq qtvdgalygk ltgvnitqts gapgggyavr lrgvsslsgn
      181 nqplfivdgv yisnveipng srnasgansa seesasnria dinpddiesi evlkgasaaa
      241 iygtranagv iiittkkgvs getrvsfnqd lgfntiirkv grrsynadqi eeaygasara
      301 efeaaqsrge ifdyediiyg eqgfitdsrl rvsggddktn ffvssswrde agiikntgye
      361 rftarlnlsh kindrlriqs ntnyirssas rsfsgneneg glsygytlaf trdyvnlfpd
      421 engnypdnpn fsgnplqtrd qtrneeyvdr vlegininln llqtnqhsln vvlnggldfi
      481 lnktfvyvpe nfqsqrgrqn gfiaegkndl fnynysaiav hdyytdggin fttqagityi
      541 nqsadqllsq ttqliplqtn lsrgaaqetd qtllnveefg yvvqeevnln driiatagir
      601 fdksslngdp nklyafpras vamnlhefdf wtmgggfvnq lklraayget gnsasfgrlf
      661 tsltntsigg ragftvngqq gnsalepets seiefgtdig ladnkvnita tyyvrdvtnl
      721 lydrslptss gfsneirndl dlrnrgfefq lglnplrtpa vdyrttfnfw lnrseitrlg
      781 vvdgsegkdi psfvptgvaf glglgtfyin egspitglwe nvngvptqtg ntepdfqfgw
      841 nnnftffenl dvnflfhwre gsellnltrl ltdlgkttpr efddlggfie dgsyfrlrea
      901 gvayrfpldn kfikglkvgl sgrniftitd yssydpetsv kgggglstni evapfpsskq
      961 fylqigldf
//
LOCUS       WP_099105424            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            marina].
ACCESSION   WP_099105424
VERSION     WP_099105424.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella marina
  ORGANISM  Neolewinella marina
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Neolewinella marina"
                     /db_xref="taxon:438751"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111124
     Region          35..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlnthqgaan srlfppplwl llvaflcsts gllaqtisgq vldnedglpl igatvaeqgt
       61 tngtvsdidg nftlnltklp aviqvsyigy ssrevrleea qsdlvfrlse ganldevvvt
      121 algierstkn ityavqeldg dqlrttrdpn fantlngkva glvvttgagg pggaarivlr
      181 gnrsisgsnn alvvvdgvpi dnstrgqvgn dfggynnidg vsninpydie svsflkggaa
      241 aalygsrgan gvmlittksg segrvqvnvn sgvsfetpsl lpefqntygq gnggtsneta
      301 agswggettt ypdnvenffr tgvsldnsis lsggtattqa yfsytnnrnq giipnnelnr
      361 ntfnlrlqqs lgsklhgdfk ativdqsidn kvkvgeesgi vqnlykiprs vdladyenfe
      421 dedgnprywt tssiytnpyw tlnrtpnddn rdrrmflgsl tydltekikv tgrasldrsn
      481 dlltfriydr tllfagpggt yqegsgffqe nnfdlflngy qdvnedfrvd flvgtalnqr
      541 eskytfinan gllvpnkfst dfginvstns svsqreyqsv fgtasvtfrn flvldasarn
      601 dwsstlpaph sffypsagls livsdmvrlp dffsfaklrg tlsevgndad pyrllntysv
      661 qqggtngfia qdatrnipdl kpeitrslef gadvrmlrgr lgvdltwykt nsfnqlflvp
      721 lpaptgfsnq yinagnvqnk gveltiqarv vekenfgyis tvnfarnvnd iielsdktkr
      781 vflgggfgrt agplveeggr ygdlygegwa rdeqgrflvd dmglpigsgg getllgnfnp
      841 dftlgwnnkf dflgfnvsll idgrfggvmv sgtdanlafd gtadyttafr dgglvlpgvt
      901 edgtpnntav saeqfwtrvs ggrysfgeff tydatnvrir efsigygipv pqslgirtar
      961 lsltarnllf lyrgkaildi pgipertmnf dpdiqlgagn yqgveygnlp strtigfnlq
     1021 lgf
//
LOCUS       WP_099106268            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            marina].
ACCESSION   WP_099106268
VERSION     WP_099106268.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella marina
  ORGANISM  Neolewinella marina
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Neolewinella marina"
                     /db_xref="taxon:438751"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117196
     Region          24..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mshlrgwatl ggsllsills aqvtltgtvt dgtqplvgas vfmqaqpaqg tftdeggafs
       61 lpveslpdtl vvsyigyrdh hvpvavntpm plrirmvagv dvsevvvtal gvrrqnstlg
      121 ysvqqignee ltdvqavnfl dnlsgqvagl rvtagatgvg sssqvvirge tsftnnsplf
      181 vvdgvpisnn tvlnasdeaa agfqgvdfgn gameinpadv ssvsvlkgas aaalygtraa
      241 ngvivittkr ggkqpglgvs fnssltldqp frlpryqnly gqgqggqfaf vdglgggisd
      301 nitysygprl daglslpqfd spvtlpdgrv vrggdvavhg glpiaatpwv srpdnvrdfy
      361 etghtainhl aisgggesge frlsaadlrs esfipgvnlk rktlagrfef rpsdrfsvda
      421 slnylnsgsd nrpaggygse ninydltawl grqtdveslk eywqpglegi qqfsynytff
      481 dnpyftlren rnsftrdrlf gfvsvryell dnlsislrsg mdyssesrqf rrhyssnrfp
      541 rggyaehdvs yrevntdfll dyrtsfgavd mnllaggnrl tqraadaqys aftlaqpgif
      601 rlsnaaspvv aldrsaakqi nslyglarfg lreylfldlt grsdwssala sptdasstrf
      661 fypsaslsfv vsqawelpea isylqlrans aqvgndtdpf rttstfvaqt pfggqptfse
      721 qstlpqpdlq perttareag adlrlldyrl gldltyfsqr tdnqilslpi pqssgyrqqi
      781 vnggavrsrg weailslvpi tgrefnwttr lnfstttakv eslpagadrf tlsysriyns
      841 vnqtvyfive pggemgdiwg tghrktadgq filndrgelv adntlrklgn anpyfllgas
      901 ntfrwrnfgl dvlldwrqgg qlvsrtlsla gvagqleeta hrpengivip gvvntgteee
      961 pvyvantmai saesyyrsyy drnheennly dasylklrel rityqldreq lmgsflsglg
     1021 elslsligrn lyawsaiphf dpeqfaiqgq rivfgvedmt ypsarsfgls lglqf
//
LOCUS       WP_099106621            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            marina].
ACCESSION   WP_099106621
VERSION     WP_099106621.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella marina
  ORGANISM  Neolewinella marina
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Neolewinella marina"
                     /db_xref="taxon:438751"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115711
     Region          25..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklplhhlcg lllllsgslg aqraltgtvt daadpligat vmadgttvgt vtdyngyfel
       61 tvpdgverll itytgyqaqy lpitaqseyd vvlqesaldl sevvvtalgv krekkslgya
      121 vqdlgadaie qtrstnvvng lsgkvaglqv saanvpgggs qvtirgnssv lgnnqplyvi
      181 dgvpmegdfa apidgasdnn vygggiseis pdniasitvl kganaaalyg sraangvilv
      241 ttkngsqaeg ltisyagsys venpfvvpef qniygggtgg vtwyadgrng gitdplaveq
      301 frnvypdapl vgtagvdesw gapmdgrlvr hwwtgtelap lvpvpdswsn fwdtgttann
      361 tlsisnnygs gnfrfsfgrv dtkgllynnd yernnfrlni dqelapklrv qvsseyiksg
      421 sdnrqqpalw elgtwhhrhd dwgllrdyad ymdvhivreg daypyanwqh sfagnrfyeq
      481 eyltnanekd rllgniafty eflpslsllv rggtdlwtdt rravtrgeri ksgtertqsf
      541 sedvlrrqet nldfiltyng yfgedfslna qfggnhrtny fkrnyigvnd atinglynva
      601 nnasqntnvs rieekevnsf fgaasfgyks flyldvtarn dwsstlpven nsyfypsvsl
      661 sgvltdalpi sgrvlsyakv ragwaqvgsd tdpyrlrqvf apstpwnstt plfaeqatia
      721 ssdlrpertt gkeagldlrf lggrigldvt ayeqttedqi iniavsratg yesklinagk
      781 vrnrgvevvl sgavidlpkf gwdvalnyak nnntvlelyt desgneleti vlqsrrglsl
      841 earvgepfgt lfgsgfarve egplagevif engvpvkdpn lkvlgnvtpd wiggvrnmfr
      901 lgafsanfli dakiggdiae esssigmqtg vypltaigre egvigvgarn vgdaenpvyv
      961 vndvvaptrd vvgalsvrya negaifdasf vklreagity alpaalvdrv sflraasvsl
     1021 igrnlamlys nhsqvdpefn syggnlqgal nyttvpstrs fgvnlnltf
//
LOCUS       WP_099107323            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            marina].
ACCESSION   WP_099107323
VERSION     WP_099107323.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella marina
  ORGANISM  Neolewinella marina
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Neolewinella marina"
                     /db_xref="taxon:438751"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114476
     Region          22..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrlslviaf vcfafgiama qrtisgtvtd ksgqpligas ilvkgttsgt vtdidgkfal
       61 evptpaefli vsytgfstle ypvdgissev tielsesasq lnevvvtalg irkekkalgy
      121 svatigsgqv enrvesdvgr ilrgkaagvd itqtsgiags gtniiirgys singtnqplf
      181 vvdgvpfnsn tnsdlgsrqg gatassrfld ldpnniaein vlkglsatvl ygeqgangvi
      241 lvttkngqgg aeaqkgfevs vtqgiartev anlpdyqnty gngfsgnfgw ffsnwgpafd
      301 vrgqngiaed gtvehpldqd ryneafpeyd garyeykpyd nvteffntgt vyntsvsvdr
      361 nfgngisfna nysnlddtgf tpnnfykkhn agvggkvtld nglriqtsln ivssdrqapp
      421 asfnygsnps ggdasvfanv lytprsidlm glpyqnpidg tqvyyrrgsa iqnplwgvnn
      481 mfdkevvnry fgnvglqydl tdwltaqyri gvdaytqenr reinrggsqi pdgqllttsr
      541 rntiidhvfn vsfdtdlsda fnlsgvvgyn ervdkfdltg vnstnqfifd lftsdnfieh
      601 ngfqtvqdea yrgvyaslta gfnrylylta qarndwsstl eadqrsilyp svsvsfvptd
      661 afeslqgsrv lnylklragy gssarfpdpy ttrailgsat nvsqtpggrp lnintvsnrl
      721 gnrllepeli gelefgvegr ffnnrvgidv slydkqssdl lvdlpldpas gytttqinaa
      781 evsnkgieaq lnlvpfkgdf twdatlnftr nknivesltd gveeiafagf snlgnfaipg
      841 qpfgviqgip yqrgpnggll vnnsgsyepg nsidvigdpn pnytmnwlnt isykglsfff
      901 qwsytdggdi ysvttatmla rglttdtdfd rflplilege dsegnpnniq gyagdyffda
      961 yfnadegsif dgtvvrlrev alsyalpasl ldrtpfgsis lrisgenlfy napnfpegvn
     1021 fdpevlslgv gngrgfdflt gptakkygan ltltf
//
LOCUS       WP_099139263             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_099139263
VERSION     WP_099139263.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53569
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff fpsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheie ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_099143744             299 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Acinetobacter
            nosocomialis].
ACCESSION   WP_099143744
VERSION     WP_099143744.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter nosocomialis
  ORGANISM  Acinetobacter nosocomialis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Acinetobacter nosocomialis"
                     /db_xref="taxon:106654"
     Protein         <1..299
                     /product="STM4504/CBY_0614 family protein"
     Region          1..163
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 dlfskrqkkl rgeipdvyqy ddipktlkiq iihiirdvlg nesspsahqv yefihktlck
       61 eygrfslgeh yesdhkvifd fllnekkhey cldvieiffk vinkyvrena hkffsskqtp
      121 dkaieelnir fkeagvgyqf eqdelirvds qflhsevvkp vlqllgkdrd yqgafaefls
      181 ahehyrhqry keclneclka feslmksihk khswpfnpnd takklinscl nnglvpiylq
      241 nqfsslnill esgvptirnk egghgqghei kevpeyltsy alhltatnll flikceesi
//
LOCUS       WP_099145265             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_099145265
VERSION     WP_099145265.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53582
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkatp
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_099145971             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099145971
VERSION     WP_099145971.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108796
     Region          9..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvaqqkais vsgtvkdkqg epligvsiie kgtsngtvtd idgnykfttq tthpvlvfsy
       61 vgyqkkeqpv fgsvlnvtle ddsqvlnevv vtalgikkes kalsynvqev ssseivgvkd
      121 anfvnslsgk iagvvinsss sgigggakvv mrgaksisgn nnalyvidgi pmpslettqp
      181 tnfysgqgqs gdgasminpe diesmsvlsg aaasalygse aqngvimirt kkgkegrtsl
      241 tyanntsfms plvtpefqnt ygattgdfss wggklttpss ydpldfyqtg ynvghsisls
      301 tgtdknqtfv sasatnaegi vknnmldryn fsirntstfl ndkmhldlsa mymnvrennm
      361 vsegqymnpi vpvyllspsy nletyqifem ynesrnfktq ywpwgnqgig mqnpywitqr
      421 dnltnhksrf lisaglsydi akgftlsarg kmdetsalye kkysastdai faekygyyak
      481 ndestrqfyg dvmlnvdkyf gdwsltgavg tsiqdidyky yaiganlnav ankfslanmn
      541 issiepsqen yhdqtqsifa taqigwkskl yldltgrvdw asalawtdsk svaypsvgvt
      601 ailtdlipgl ksntvsflkl rgsysevgna prrytayqty sfksqfpvts ttypnndikp
      661 ertkawelgl eshffgdkln lnvslyktst ynqlfnptls stsgyrsiyi nggqidnkgl
      721 evsltlkqpi gpvdwsstft yslnrnkvvk llkpttlsnd ltisqdhldl inlgnvksmi
      781 kedgsmgdly vtslltdnqg yiyvdyqtnd vmvdknagpy ndgfiyagns aakyhmgwrn
      841 nfswkglslg flinarvggv gvsmtqalmd ingvskatad ardaggvsln gglvpavqky
      901 yqtigsgags myvysatnvr lgelslgydv pvnkwvswik slnvsfvgrn llmfyckapy
      961 dpeltastgt gfegmdyfml pslrnlgfsv rvnf
//
LOCUS       WP_099146355            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099146355
VERSION     WP_099146355.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117038
     Region          43..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmekckyll fcgtlalwma ggfqqvyaat epssqaiqqq snkvtgkvsd atgpiigasv
       61 vekgtangti tdldgnfsln vkagatlvvs yvgykseevk agrgplsitl kedakaldev
      121 vvtalgikre rkalgygide vkgealtkak etnlinsmag rvpglvvsqt aggpsgstrv
      181 ilrgstemtg nnqplyvvdg vpldntnfgs agtnggfdlg dgissinadd venmsvlkgp
      241 aasalygsra shgvilittk rankdkisve yngtltfdtq lakwdevqqi ygmgsngtys
      301 ydaisntnks wgpkadgsnm lkyfdgverp flivpdntsn ffrtgitatn saiigvnsgk
      361 tgirftytdm rnkdivpqth msrdifnlra ntstgkvdld fsvnytredv knrpalgdsk
      421 snigknlmtl attydqewlq tyqtadgeys nwngmdpynv npywdiyknf nkskkdlfrm
      481 ngkavwnidp hlklqatlga elnwftfddy kapttpgfea grlqnsafrn rmynfevlal
      541 ynnhwgdfdf natlggnvyk vnnqttvtta qdmkirdvps ltsfneisvv pgsyrkqins
      601 vygavnvgwk hmlyldatlr gdqsstlptg nnmymypsfs gsfvfseltk lgdllpygkl
      661 rmswaqvgsd tdpyqlglvy tkskyaypgy tvgyidngti pnkdlkptkt nsvemglelk
      721 flknrigldf tyysqisknq imgmasswtt gynyrlinag kienkgieia lstrpiqtrd
      781 fswdinlnfs knsnkvkeld gesdmfelek aswldvqvaa kvgenfgsiv gpdfqrnekg
      841 dilidpqtgl pqydksnhvl gnaswdwtgg lltnftyknl slvavfdvkv gadlysmsar
      901 aayesgkspe tlagrdawyr seeerlaagi akgadnwkpt ggfvapgvid ngdgtyrpnd
      961 iyinpedywm svcrnapsmf iydnsyvkcr eltlsynvpk swlknvvsgl tvsfvarnpf
     1021 ivwknipnid pdsnynnttg mgleygslps rrsygfnvnv kf
//
LOCUS       WP_099146350            1196 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099146350
VERSION     WP_099146350.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1196
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134108
     Region          35..102
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          114..1192
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknwklliv cflcvlcflp yqvnaqaqpq kkitiefsnk rlpsvlkrle kisgykilft
       61 yddvkkytvs gsakdksieq vldiiltskp leyhiedqfv tislkgpskq akvfnvkgvv
      121 isgddnqpli gatvlikgsk sgvltdidgk fsienvsnks vlqfsyigmk aqdltpsptm
      181 svtlmpdvqt lsevvvtgmq kmdkrlftga tnqltadnvk ldglpdisrg legraagvsv
      241 qnvsgtfgta pkirvrgats iygsskplwv vdgvimedai dvgpddlssg daetlissai
      301 aglnsddies fqilkdgsat siygaramag vivvttkkgk agvskisytg efttrmipsy
      361 nefnimnsqe qmgiykemeq kgwlnsgdlf raknsgvygr myklidefne ssgqfglsnt
      421 ltsrnsylre aemrntnwfd elfsnnisqn hsvsitsgse kssfyaslsa mldpgwykqs
      481 eikrytanin tsyniyknls inlisnasyr kqqapgtmns sldvasgevt rdfdinpysy
      541 alntsrtldp aadyvanyap fnilrelnnn yielnvvdvk fqgelkwkvl pelevsalga
      601 vryqtssqeh nilddsnqai ayrsglddat irkendwlyi npdnpyalpi svlpeggiyq
      661 rqdrkmlgld frstlswnhl fadkhitnff agmeindlqr tyssfqgwgm qysmgeipsy
      721 vyqffkqgve tgnkyyslsh sqtrsvagfa natysydgry tingtfryeg tnrmgrsrss
      781 rwlptwnvsg awnvheekff ksleptmsnl tlkasyslta drgpadvtns qaiirsyspy
      841 rpftdiqetg lyiedaense ltyekkheln lgidigfinn rinfsadwyt rnnydligli
      901 ptqgvggniy kfanvatmks ygteftlstk niktkdfsws sdfifahakn evtdlkgrtr
      961 mmelvsgsgf aregypvral fsipfaglde ngipqfning tvtstdinfq erekldylky
     1021 egptdptvtg sfgniftykg fklnifmtys fgnvvrlnpy fnykysdlsa mprefknrwt
     1081 lsgdevktnv pailsspqye anrtlyrayn aynysteria kgdfirmkei svaydfpqkw
     1141 iapakisnls lklqatnlfl iyadkklngq dpeffntggv aspvprqftl tlrlgl
//
LOCUS       WP_099146376            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099146376
VERSION     WP_099146376.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119175
     Region          25..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnkwllsl sigllccgsa yaqttvkgki tseggeplig atvavknstd gtvtdidgny
       61 slktkktltq kdllvfsyvg yktlqknyag ntmnvklaee sqqlndvvvt algikreekg
      121 lgyatetvkg dmitsalptn wstalngkva glsvissggp lnssrislrg dvslnqngnd
      181 alvvvdgvpm sspmtnpgva ygagsnsels vdygngfsdi npddiesiqv lkgasataly
      241 gtraangvim vttksgagap kgigvsysgn fsiddvmrwp dyqyefgqgl psnigpagsi
      301 yegqpyysyg kaedgsyast sgtssaygar fdanrlfyqy dpvtqgrasv atpwvayknn
      361 rkdlfqtgyt ltnsvaltgk sdrgsvrasi thtknewilp ntgfqritam vsaqqqisra
      421 lrinfkssyt yrklnntpal gynsnsisyf lifqnpnvnl dwlrpmwrtg qenvkqlqpy
      481 ssfignpyvi lyesenpsek hsnvssvsan lrinskfdfm irsgiqlsad qreqhrpisd
      541 vvfgngffkk qnvfdyelns dalftyhdsf anglrvnasa ggnmmqqsyd mlaasvvgli
      601 tpgvyklang vsnpnvqtvi kkkalnslyf tanfsykdkl fldvtgrndw sstlpksnrs
      661 ffypsvsvsa vmnewftlpe qisllkvrgs laqvgndtdp yktspyygts dfpgsaivss
      721 tlynqdfkpe istnyetgfd frmfhnrigl dftfyynrtk nqildapmdp ttgyrkatin
      781 sgcvrnrgye iqldvtpvvs rdfrwnatft wsknenrils laegadenql issigsvsii
      841 grvggttgdl wgyklvrdpe gnvvindngl persgeieyv gtaypkwkag lynefsyknf
      901 tlsvlldgqv ggkmyshshh kmteqgklqh tlngrlpgte fymskddpri aaaglspqdg
      961 mymiapgtvk nddgtyspnt kvvtvesyyk eyyrmanvet ntfdtsflkl remrleyklp
     1021 nstlkktpfs kasvalyarn lfcitdyplf dpesaalngs smvtgvetgs lptartfgln
     1081 invsf
//
LOCUS       WP_099146458            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099146458
VERSION     WP_099146458.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126715
     Region          36..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          114..1115
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknqaqkfi vlflfflfay swrveaqtgk ekqltmefkn eglpsifkrf ekvsgykvlf
       61 iydeissyts tgkvekatvd ealkviigkn plkyhidgqf initkkdskk ffsqvkgkvf
      121 seedgfpvig atiivegssn irtitdnngn fqlsdvpkds rvrisyvgle tqflnpssym
      181 svvmksdtka ldevvvtgmf nrkkegftgs avtikgedlk kystnnvaka iaavapglri
      241 mdninmgsnp nnlpdmrmrg ganmdmatqs avdfnstsnd vlavqgeyet yanqpllimd
      301 gfeisiqtla dmdpdrvasi vvlkdaaata iygsraangv iviesktpkp griwvtygge
      361 lrieapdmtg ynlmnareki daelqsglyt yggetvekwq lyqsklrevl agvntywldk
      421 plqtafqqrh tvtleggdea lryrmyvgyn sspgvmkdsk rdvltgsldf qyrlkkvllk
      481 nsitldnsva nespwgsfse ytrlnpylrp ygengeiqkr ldnfegvgge ssylnpmynt
      541 tfnskdqskn ftvrelfkve ynptnelrfe gafnlsksvg hrdifrpaqh tlfdnvtdpt
      601 lrgdyrrsqs eavnwgidlt gswnkqledh yltanarmsv lennsetygn yvtgfpndnm
      661 dnllfgkkyn ekvtgdertt rsigwvvagg ysykykysfd fnirldgssq fgknnrwapf
      721 wstglrwdlk kenflkdvsf isdfilrgty gttgsqgfdp yqahgyytys nlllpyyssd
      781 atgseilamh neslkwqttk stnlalelgf fdqrftarve yyrkitdnmv anislapslg
      841 fssypenlgk ienkgweisl saipykntak qaywtitvng shntdkllki seamkyrndk
      901 sasdlkdtpl pryeegesls riwvvrslgi dpasgdeill krngemtsav nwsandvvpi
      961 gntepkwqgy inssftyrgw gadvsfryqf ggqvynqtll dkvenanlky nvdrrvtqlr
     1021 wakpgdkaqf rilnpnglet katsrfimde nifqgsslsv yyrmdrtntk fishwglssa
     1081 kvtfnmedff ywstvkrerg lyypysrqft falnvaf
//
LOCUS       WP_099146467            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_099146467
VERSION     WP_099146467.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122037
     Region          26..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkitifslt llfalilplf anaqvtvkgi vtdesgvplv gvsvrykelp qvgvttdidg
       61 kfsikemkeg ktlvfsyigm knvehllkga tpfikikmes atseldqvvv tgytqttfkk
      121 mtgsvgiisa dqlkdqaqpt vdalmqgkia gvavsaisgq pgstqkirir gtntitgdge
      181 plwvidgvpm qsgstdmpts aeiksgqfdd lfmngvagin psdiesitil kdasaaaiyg
      241 sraaggvivv ttkkgksgka qinysgnvsv tlppqrnysl mnsqeklaye qglwdefsap
      301 gfeagtndyp vvgvvgiira grgkfagwsk eqqdtyieel gktntdwyde lfrnsvstth
      361 nlsingggdk ytyytslayt rnagllknnd ydrynltanl smhpsqkvki dfgasmsyqy
      421 skspalnsld pfqyayfanp yespynedgs yradetyyal geynnkktss kiipdcgfnv
      481 lremdetssr tkniktmvra gidysiinhl rfvglasyty stnrlkeiyg kntkaaldnr
      541 lsidnntnke yasilqrnvd nesymvrghf ayddsfgdhs vsliagaefr gsksdglysk
      601 rygydeitgn aitplpddpt gvgyeklkay laaidgsnge twseqrfvsf yasadyyykn
      661 kyvlnasfrt dgssnfgsdk qfnpnwaaga awnvseedfm aplkpvlnrl tlriatgftg
      721 ninrsvspqm iisyyddyrn isnniyhigk vvsppnpnlr wektqdvkva ldfgmlndrl
      781 tgivegyyrk skdivtgvqv lsstgftqqk yntanidnkg ieatlngtpv ktkdfnlsls
      841 aniaynknkv tkykasyssm gynnlwegyp vdaiysgryt gidpetglyt yqlrpdaeih
      901 tatdlnkpdn yryylgtsea pvtggfnvta eykgirlsvn gtfatgaknf efiksptsas
      961 tvsgngvfyy tereqvfqnd lfahhlnvpk vaadrwtpnn tngtyprvwn pfgevygfgy
     1021 ynpmhkeith gafltnlsya riksiilgyt lpkklisnsa lsnvdfslsl nnfftftsys
     1081 gmdpetpgat ypisrsvmfs vnvgf
//
LOCUS       WP_099146501            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099146501
VERSION     WP_099146501.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113089
     Region          29..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrafiisffv vifisaisfq atyaqqkdiv ltgmvtdhqg eplpgatvri gntqfgtvtd
       61 angryqlrgr wkkgdmiifs figmkdvrek ytgqnvqdaa mqqdtkslde vvvvarqnin
      121 eldiraksgv vqnvdmgrln skpmidmsla lqgsvpgliv tntgdlgskp eirirgnssf
      181 regdaanepl yvmdgqviss dafmtlnpad ikeikvlkda vacalygika angvieitsl
      241 rgnpdgrttt sysfnmgitt rgrrgvemmd tdeklelerr lqnrstpgyr ysedyyrkyf
      301 andpnlnqmi aegqeildsl rtihtdwfde lihlntyqrh nlsvrggsek tsyyvsanya
      361 qqggrvpgnd thrftatmsl dqqlgrvgyl slsanagyse tdtpngssys ptdliyqlnp
      421 yetktgklvs fsnetsdyty ndllsqynsk stdkrggvsg slnleplkgl sidavtgidm
      481 llnegmtlvp stsisernsg vdeaergkls keknvttnvs snvritynki faekhdftig
      541 gnmdyymtda dnvsitgygv gmqmspsain qsisgnrkpv vgsykektaq lglglvmgys
      601 fdntydlfat ykadassilp eskrwnaawa iglgwtisqy pflkdndvis rlnlkasygr
      661 manlagvsas stigtfsyst dyygnarllq llalyntdlk aeqtastdis lsvelfkrlt
      721 ldaniyrret sdalldvpvp lsngfstmkr nigvlrnegy elsaslkvld tsdwrlslrg
      781 slaynrnkvv dlyyadrlya seeaiipdye vgksydmiyg lkslginpit glpvfqgadg
      841 reipatenps kenivalgha tppysgifnl sfsyrdfdld mdfyyvfggv ksysysyvrs
      901 sddanknaik gqlqnmwfek gdegktyhsp fysssaiasl dypntetvgk sdylklsmvs
      961 lryrvphtfl ekncnfikya nvafqasnlf mitpykesdp etgslagtmq pvltinlslt
     1021 f
//
LOCUS       WP_099146775            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099146775
VERSION     WP_099146775.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115101
     Region          45..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnnnryirl iglifvlivg snltfaqnks krksakkplv eivsivtdek gsplknvsii
       61 cgegavvlyt dakgrfqtkv endatvmvea lgyedkvykl sgsnivpeki vlkkeplflt
      121 eeslvnradg gktykgnevg atsvlengqf gtfpdltltn mlqgkmlglq vrstvsglgn
      181 ntpdlfirgq hgmsentaiv iidgverpaa dlipeeieri ellkdataki lygaraangv
      241 lwvttrrgka nrriynatae vgvvqmtrtp dflnsyqyan lynearandg mtpyynqkql
      301 egyknskgan dllypnvdla dqllnqnany rkvsfdmtgg tdrvryalia gyvggsgfed
      361 vgytpqlnrl tlrgnldfnv tdfltisadv agrmemrkwg qldcgqvfta lsthrpneyp
      421 ltmspeetgl aggsdgiplf gaslrqpmna yaetmyggyt derytrsqtn iglkfdldml
      481 tkglkagafl sfdnydylql slskvyptya iktyrdfage eqimytqmkk tdvatsqsrk
      541 sttlqqtlgw nafagyentf nqkhdvsarl tymyskttnq gvtqdiinan yalrlnymyd
      601 rryaveadma lmgsnrfkpg nkyffsaagg lawilsnedf lkdneyvnfl klktsagilg
      661 ydrstehlly erawsqdgsf rfgttnngat ayystfvrag npnlkwekaa ewnigveglf
      721 lnnrlytein yfrekhtdii asvdasygdy tgnftyqdnm gsvlnhgieg mftwsdrind
      781 wsysvganfv wsknkvlkwn qvkhgeeyry tvgrstdamm glvaeglfgk dvainghvpq
      841 tfadyqegdi aykdlngdki idgrdvkelg nsfprttlgi dfsvsykgwg lylqgyselg
      901 vhtwatnayy wnngegkysk laldryhpan nptgsyprlt ttagennfrn ssfwlkntsf
      961 frmknvelsy tfnqfspssv vkkmkvfarg anlfvlssvk dldpellnag vtnypvtrtf
     1021 tggvsfvf
//
LOCUS       WP_099146782            1148 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099146782
VERSION     WP_099146782.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1148)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1148)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1148)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1148
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1148
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126382
     Region          40..1144
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvlrkism vllaassigt iyantgyema gvdivqqsgt vkgvvkdatg epvigasvlv
       61 kgtpngtitd vdgnfslsnv kkgdvlqisf vgyktlevky dgqplsvalq ddsqaldevv
      121 vtalgikkda kklgyavssi ssgdltktgg gnlasglygk atgvriqaap gggtsavsis
      181 vrglssitgn tqplvvmdgv pihngntnnd gywenqrins ngivdinped idnisilkga
      241 aasalygsea angvvmittk kgkkgggthi dfsanvsfdk vaympeiqke ygpgydnwal
      301 gsnadetalt gfrhtrldrn gnsittpnre tyyswgakfd psktvtyfdg teraytpidh
      361 nqwadifrtg vnqtynislt nsternnmrf sytyndalam qynsdnhkhn fnlsgtfdvt
      421 ktiklnytat ytdqyiknrp yrisrltnny ggmfggftdv ayirdhtits lgyknsiaai
      481 nggtadtltp deqflytpmg stalineyfw nilgkvqeen hnrfigsvnp tweiipgltl
      541 ggrlatdltt dkienknnte nahifstdgh ysdsyglins ryqivygdim lmwdktfaek
      601 hnitanlgwn arqetfyqsn vstsngltqe nwfhlnasvg tknadmeksd llrtgmflta
      661 sygydgwgfl egsvrqekts tlkhgnnsfv ypsvsasily tellkdkrps wwdygklras
      721 ygvvgnapei yranraydqk sltrsttyty nyvdvkvgnd gikpetkyef eigienkffn
      781 nrlgmefsyy yndikdqilt ttsaasmggq smlmnvgelt nkgfefsvng tpymnkdwrw
      841 dvraniawnk nvvkkladgl dvlshltvdn gaasleshvg damgdwyayt wktddkgnyi
      901 vgndglyvad kterhkvgna mpkftggfgt slswknltld vtfdfrvggs vlnlpwqymm
      961 dagnitdavg ardhstgglf yysdvedvtn kssihvltps evasikgsyk rgdkfnghyl
     1021 wdngviqkgv kedgtpndiv vtqfeindsq ygwgtgaaqs yanaiqknty vkcreislay
     1081 tlpmkltkkf acnnltvsaf arnpfyvyrs lklfdsettd gtnwiyqaqv ggstasartf
     1141 gvslrasf
//
LOCUS       WP_099146848            1121 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099146848
VERSION     WP_099146848.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1121)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1121)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1121)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1121
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1121
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124234
     Region          110..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnyrkkailm vvalfclnia ilaqavslkm nnvsvkeamt qlknksgysf vykvgdldtr
       61 kivsvkakql neaidqilyg qevvyevkgk niivqkgqar qntskdtkkr kvtgtvsdan
      121 gepiigatik ekgttngtas dldakfslev spgavlevsy igyqtqevkv gdrvslsvtl
      181 aenqqildev vvvgygttsr knlttsiatv ktekiskaat snisgmllgr aaglqatvas
      241 pqpggginis irgggtpiyv vdgvvmpsgs fevgtgstsl pssvnragla glnpndiesi
      301 eilkdasaai ygigaadgvi lvttkkgkeg kptivyegsy svqkhypyld vlsgpelmnm
      361 vnvfskenyl ydkgqypygn aayddkwtpi ftptqianap ttdwldkvlk tgavtnhnlt
      421 isggsekfky ylgvnyyked atvynsdmer yslrtnitsq ltnflkltti vnlnqnnytn
      481 stvggdvgnl rdqgagalfg aiyypsylpv ydaegqynvf srtpnpvsmq dindkseqng
      541 yymnfsldvd iiknmlsakv lyglnkents rdsyipsdiy yalqrksrgn lgygkrqqst
      601 legtltfqhk fgelldmnlm agmgryldsg dgsdisyena ndhiqgssvg madgpfypts
      661 ykyknekrsq fvrgsfdlfg ryvvsaslrr dgtdkffpsk kyalfpsvsl awkmneesfi
      721 kniswinmlk lrasygetgs dnlgttlygi vtttredvqf nnnsvtyipy ilsganyedv
      781 twqktvmkni gldfsvlrdr iwgsvdifrn dvthllgtap tellgmhgtr pingghykrt
      841 gvdvslnsln lqthnfkwts qitmshynav wiermpnydy qkyqkrknep mnafyyyktt
      901 diidvdksnm pesqrslgpa acmpgypive dkngdgiidv ndsymdnmlp klyfgfgntf
      961 twknfdldif mygqlgvkkw ndaysysada gnlsrgvdah nvgiysyniw ntqtntnghf
     1021 pgiaisksva lpenlgfdyt renasyvrvr nitlgynlgp kelsvfkgyi rgirvfvdfq
     1081 npltftkykg ydpeintsss nltggqypqm rvysigaklt f
//
LOCUS       WP_099147370            1173 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099147370
VERSION     WP_099147370.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1173
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131835
     Region          32..98
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          117..1172
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mndrrnsffr lfllillclg vqslraqtvt kvfkneplka vlkeverqtk ysiiyktdev
       61 nenkkitasf qqatvnnvla tvldkdveyk lqnrmiiitk kternttavp sqplhrvtgk
      121 vvdvngdpvi gasvqvigqs mgtitnldge ftlssvpana lvvvsyigfe kkeikvsdlq
      181 kssrvilred tatleevvvv gygtqkkinl tgavavvdsk amedrpvpra sqmlqgtvpn
      241 mnvtfgsgyp gasatinirg vnsisgnasp lvlidgiegd idrlnpndia sisvlkdass
      301 aaiygarasy gvilvttkeg sarkttvsyd gryswsnqtt stdfetrgyy sagindlfyt
      361 nyngkpytny teedyrqlwl rrndktenpe rpwvvtdqrd grdtyvyygn fdwynylyrk
      421 nrpmwehnis vsggneklny ylsgntvdqt gifrqnpdky kvynfrskis akitprltis
      481 nntkyhynsy sypglsginn nfntavnhal asfvpinpdg savyltslsn saildgmgai
      541 laygkhkned qryefsttfe asfnvmknln vranysylhy nyqtmnrtvn vpyskypgei
      601 sylttgsgvn qlketqtnhw yqafnvygdy mldiadhqik imagynyetk rlkdikvsrq
      661 gllsddlndl nlavgdamtm sggqneyall gafyrlnysy kggrylfets grydgssrfr
      721 srhrfgffps asvgwrisee pffgnlkkni dnvklrlsyg slgnqqvgyy dyiqtintng
      781 tmnyifgdqk kgsyasvsdp nsadltwetv stwnigldlg flnnrlnlta dayvrdtkgm
      841 qtsgkklpga yganepkqna anlrtkgwel mltwndafkl ankpfrynls vgladntski
      901 tkfdnpskil sdyyvgqklg diwgyvvdgl frtdeeaany nvdqtavnfv intaqvnpgl
      961 hagdmkfvdl dgdhtissgs ntaddpgdrk iignslpryt ysiqggfdwy gfdfsiylqg
     1021 vghqdwypgt nsvffwgpya rpyssfiprd flsqvwspen pdayfprpig ylalgnnrsl
     1081 gvvndrylqn laycrvknit vgytipavwt kkvkierlhi yfsgenlftf splksdyidp
     1141 eqasaensiq sangnaklyp wsktysfgvn vtf
//
LOCUS       WP_099147107             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099147107
VERSION     WP_099147107.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108306
     Region          3..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvsyvgmis qdvsikpgvi kvvlksdaka ldevvvtamg isrekkalgy avqdvksdql
       61 tqaansnlag alqgkvsgld vkpssgmpga ssqitirgar sfsgdntply vidgmpvtst
      121 pdvstdiqnn gsvsgadfan ravdidpndi esinilkgqa asalygiras ngviiittks
      181 gkglekgkpq vsfssnvsfd vvgrlpefqk tyaqgsggkf sptsgtswgp kiselpndat
      241 yggntdnkyt qqygkqqgky yvpqrasagl dpwatpqayd nakdffdtgi twsnslnvaq
      301 mlekssysis lgnthqdgii sstgmdrynv kvsadtklts nwssgftany ittsidkavt
      361 sgngllrtvy aappsydlag ipshvdgnly aqnsfrgsfd naywamennk ftedtnrffg
      421 nvytsyqtdf gttnhklnak ymvgvdaytt hyvdsygygs ntgggrgqie nygwtnatyn
      481 slltinydwh inedwglnav vgneiiqsnr kkyyeygtny nfpgwnhinn attqqteeet
      541 wknrtvgffg nisasyrnml yltltgrqdy vsnmprnnrs ffypsisagf ilteldalkn
      601 nvvnhaklrv syaevgqagd flenyystpt ygggfymltp imypmkgtta ytpyytifdp
      661 klkpqntrsy evgadvnfld nlitfsytys rqnvkdqife vplasstgas klltnggkih
      721 tntheftlgf npirtkninw dfafnwtkid nyvdelapgv enislggyvt pqvrasagek
      781 fpviygvgfk rdengnrlvd englpiagea qvigkvspdf lmgfnttlrl wkctisavld
      841 wkqggqmysr ttgladyygv skrtenregt iifdgyktdg tkndiaitga naqqvyysrl
      901 ndinessvyd nsfiklreva vnykilqkrs ielsvnafar niliwaqlpd ldpeasqgnn
      961 nmagafedys mpqtasfglg fnikf
//
LOCUS       WP_099147230             914 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_099147230
VERSION     WP_099147230.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..914
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101312
     Region          38..913
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvqharlify tllllvipce stlaqkipvt pidslitvgy atgslktlsg svekitetqm
       61 nkdqitnple airgrvpglt iqrgsngpaa ldavrlrgtt sltsgndpli ivdgvfgdls
      121 mltsiyptdi esftilkdas etaqygsrga sgvievttkk gmsgrtqvay ngsfgistvy
      181 knlkmlsgde yrrvasergi sildkgnntd fqkeieqtgl qqnhhiafyg gssessyrvs
      241 lgfmdrqgvi lnedmknfts nmnmnqkmfd gflncelgmf gsiqknhnlv dyqktfysaa
      301 tfnptypnhk dpvtnswdgi ttasqitnpl awmevqddda tshistharl tfnlleglkl
      361 nlfgaytyni vensqylpts vwangqaykg tkkresllgn mmltykknwk khffdvlala
      421 elqketytgy yttvsnfstd kfgynnlqag alrlwegtns yydqprlasf mgrfnytyad
      481 ryvltlnart dasskfganh kwgffpsasa awviseeefm kqlpmvdnlk frigyglagn
      541 qsgidsyttl nlvkpngvvp vgnsavvslg dlrntnpdlk wevkhtfntg idvalfgnrl
      601 llsanyynsr ttdmlylynv svppftyntl lanigsmrnw gteiaigitp lktkdmelni
      661 nanitfqrnk llslsgmyng emlsapeyks lasldgagfh ggynhivyqm vgqplgvfyl
      721 phstglesdg nggytygiad lngggvsled gedryvagqa vpktilgsni sfrykrfdls
      781 lqvngafghk iyngtsltym nmnifpdynv mkkapkqnik dqtatdywle kgdyvnfdyv
      841 tlgwnvpiek vqklkkyvrs lrlaftvnnl atisgysgls pminsstvns tlgvddkrgy
      901 plartytlgl sinf
//
LOCUS       WP_099147406             942 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099147406
VERSION     WP_099147406.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105090
     Region          39..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtiinsiykg kryailltti ltfyapvlfa qhiadsalve vaygqqpewr rtsaissirg
       61 edllkttsas lgnslqgqlp gltllqqsge pgydfsianl ylrgrtsyas gqkmlvyvdg
      121 feapieslst aeiesvtllk dasalalygm rgangvllvt tkkgcvsapq vsirlqtgiq
      181 qplgvpdpin aydyatlynq arvndglprl ytpeelnayq nntdpyfypn vnwkkailnn
      241 taplsmadls fkgggdvvqy yvmmnllqni gfykdtdkkr rensnayyas fnfrsnlniq
      301 iskhlstgln fsgsvgnrsi pggsssangl lgaiwrtapn afpvynpdgs yggnaaftnp
      361 vgnivsrgly kensrtfqli fmpkydlekl tkglsvsagi aynnymadss iknqnyarys
      421 lskgaggevl ytpygadspl esdegfrtdw srlnfkaqld ydrvfkqhql tasifflsdl
      481 yqkygsrddi kylnyagrvt ysynqkyige faasytgcdd yapgkrygff pafsagwils
      541 kenfmkninc veylklrasi glvgnnqnen grylfdqtys sngsyflgtg ssstggfrad
      601 mianpdiswe kervfnigld avllkglsve fdyfhkeryd ilsqpystip gfvgasygdi
      661 lpymnvgkvk nqgfegtiry esslknnfny yvetsawyak neivdmaeev klydyqyrkg
      721 rsvntpfvlv adglyqesdf dsngslkshl pvpqfgevnp gdikyidkng dgvvdsndsy
      781 pvgysnipew nyalkigfew kgidvealfh gvanrdiyls gplaysftdn gsasklalds
      841 wtpenpnasy prlstrtfen nyristywkr ngnyfrmkni rigytfpqsi araiklsrly
      901 vyanasnlft vshldgladp essslitypl trsynlgiki df
//
LOCUS       WP_099147483             923 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099147483
VERSION     WP_099147483.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 923)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..923
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104273
     Region          31..922
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mimnkslyiv afslafattg iaqnnegqdk vidlgtqttt elrktqavst iysdeldkna
       61 ttspynaiyg llpglsvmqn tswgtdksrl nvrgrgslng dtplfvvdgf arpleyinls
      121 eiesisvlkd gaatalwggr gangvvlitt krgiynqkdi kvdykfglgl pvnqpefada
      181 ytyakarnea lrydglqpdm deasflsggn sdlypnvdwq kealrnhtts hqlditfrgg
      241 gkrlryfsvl nykndmglln skytdytdry nsqmkkyfln lrmnldvdit datklklsml
      301 gmlretkrpt tseatlfeqi fntpsaafpv qtqngfwgsn nvlktnpian ladvgyykln
      361 qrmlqadlrl vqdlsvltrg lsaelaiayd nnatyqetak ksfmyqtiek gidgepiytn
      421 ygnpndelei snkglanqyi hanfeakvny hrtwdkhdft asamfrqesm tltgannsry
      481 rqyiigtagy nfdnrymvdi vancfgssvl gkndkyrayp aisaawilsn enfmkeisaf
      541 dylklrasyg rsgydiydyd mdkqywvgsg ayyfqagnts agsslkegvl ameqldleva
      601 dkynigldms lfkgltfsid gfydkhtnil idgsglissa igvtipqmna gkvetkgtel
      661 samwkkeykd fnyyiganfs yakskvvena egyqpygyls kkgypvgqcf gweaigyfrd
      721 eadiksspvq kfsevrpgdv kyrdlngdnv idnndqkaig ystaipeiyy ginlgfeykg
      781 fgvdalfqgv ahysvmlnta svywplrnnt nisnwylndr irwteetkdi anvprlttld
      841 nannfrnstq wlengsyfkl rnlnvyynlp sswvkkmkme kiqvyarann lfsldhvkym
      901 nsedlkinyp dmtsvyfgln inf
//
LOCUS       WP_099147537            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099147537
VERSION     WP_099147537.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118946
     Region          40..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklrflmac allaflwseg syanttlent gssqqqqywk ikgkvsdekg ealigatvki
       61 knathgtvtd vngnfeivlp pgsvliisyi gyreqelkin sqrtydivlk eetagldevv
      121 vtalgikrdr kalgyavsdv kgkelekake tnvinalagk ipglvisqta ggpagstrvi
      181 irgntsltgs nqplyvvdgv pldnsnfgsa gayggydlgd gissinpddi esmsvlkgpa
      241 asalygsraa hgvilittkk aqknqnrrai gvevnstvtf ekqlteyddv qtefgqgwdg
      301 rinlndddak sacaswgpry degiafkyfd gvtrpfiyrk dnikgffntg vtatnslils
      361 sakennsirl sytnltnkdi mpnakisrnt idlrtffkla eklevdfkvn yvneyvknrp
      421 aladsrtnva nnlmnlagnf dqvwlkdnym hsdgtyydwn rgdvwninpy wvqyamkntt
      481 qkdqyfavas fkysvnknly fkltgggenv nfsfmdyipy stpstllgql qkstfenksy
      541 nvefianyqn sfkrfnygit lggnvyhvdn kshtitaknm smhetvalqs flqkeitegs
      601 wrkeinslfg mvnlswkdll yadvtlrrdq sstlpvnnnv yfypsvggsf lfselikpnp
      661 ilsfgklras waqvgsdadp fmldlnyimt dktfgnystg yistgtipnk dlkpsktnsf
      721 eigvdlkfln nrigldftyy kqnsnnqimn vatsvtsgys tklinageie nsgveialnt
      781 tpvqtkdfsw dfnfnfskns nkvkslstgi eslelaaarw lgvkvlavpg eeygvimgqd
      841 flrneqgdvi inadsglpei tsdmkklgka twdwtggltt tfrykqftls aifdikvgad
      901 iysmtargla ksgkaaytvr grdewhksee qrleagvaeg nwqstggyva egvvkqvdaa
      961 gnvswvkntk aiapydywgy icdktaspfi ydnsyvkmre ltfgytfpkk mieryvesls
     1021 vsfvarnpfi iyknvpnidp dsnyntsaig leygslpsrr sfglnvnikf
//
LOCUS       WP_099147620            1174 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            celer].
ACCESSION   WP_099147620
VERSION     WP_099147620.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides celer
  ORGANISM  Bacteroides celer
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1174)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1174)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1174)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1174
                     /organism="Bacteroides celer"
                     /db_xref="taxon:2025659"
     Protein         1..1174
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131730
     Region          115..1173
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrynhciqfw gvlvlllvln vqfavaqtys vkyndqsvel virdlrkrtg yefvyqkqvi
       61 eeaphitgyf kdmtlqqlln riflneasid yeivkqtivl kkmnpdddfy fksnvtgmvt
      121 dendeplvgv svmqrstkng vatdvdgafs llvegknpsv evsyvgykkk nvtinrkmpf
      181 fvvklqpdet ildevlvtgf qnikresavg ayqtihskdl ddyftndvas rlegkvpglv
      241 synngngkng edalvirgag sfnartsplv vvdglpiegs letvnsydie tinvlkdasa
      301 asiygarasn gvivittkra hkdrisvdfn adltisenqs ysnrrwanas qyldveeanf
      361 nyvsndanly ngllgqynar psalspaarl mlrhklgevs dahyaatmnq wrqndyrrew
      421 qdamerqqiq hqynlafrtq gkrinsnivl nytgdnlgrv nesknsfras yngemdvtkw
      481 ldlsfgvnli serskthasg anlyndinsf apymsmrnad gsvaameaat ylgeeslgns
      541 slglkdesyn llnetnlnfs rerrnnirsy vhasfhilpe lvlstkfqye diiykdetyl
      601 egqsyymrhl ynlatsdgvh hlpeggmlst nnqngdyytf rvqgnyartf aekhaveaiv
      661 gfeyrqthnr yaknvllgyd dqtqtnmnhl infydlnqlq ssdlgtsysp agalpseedf
      721 ktqdvlhrfy slyananyty dsryaaqfsy rvdktdlfga dpkyrgrplw sagaswnlqn
      781 edfmkglkwi dvlklrasyg ltgnidqsvs syltaaiavn dinsskgatl ntppndqlrw
      841 ektaswnvgv dfsfignrls ggidwyykks tdllsltdid pttgwtslti nngkarntgv
      901 elqlngvild arttndvgln vslgiahnsn kilkvdhaas sgyealntmh qgdpinalys
      961 yrfagmqtde sgvqaygwyd akgnvhatdv qngefttadv vysgsldpki nitfspeitw
     1021 kgfslsamfa yygghvmraa medwtyggsq ygygnleepm psafanywta tdkntgiang
     1081 ctslstignp yyidqtvvka dfmklryivl gynfpkkmck klgigsmrlr aqmnnvakwv
     1141 rndlgidpea vdpysgyaia kprksyvmsl svnf
//
LOCUS       WP_099149132            1126 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099149132
VERSION     WP_099149132.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1126)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1126)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1126)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1126
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1126
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125879
     Region          31..96
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          155..1125
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 melkagfkqi lviillcigl splpgnnylp qnqplnevld qisekyqvii tynakllsni
       61 kvkfefkade slevavnral nstglrykql tekyyvvfke trsnkknikk lqrkfkqiqk
      121 leqeenlqvq qnidnhrgrr lgailnaaee alkerditgt vldeeglpli gasvkvkgaa
      181 tgtvtdldgk fsltiaddvk ylevsyigyt tqeiaignas iveivllsnv teldeivvvg
      241 ygtqqksdlt gsvaranies frespnvsvv qslqgtvpgl nigqvdatge npsisvrgst
      301 tingnqnvli vvdgiiftgs lnelnptdie sidvlkdpss maiygaqaan gviliktkgg
      361 kkaskpafty tasyttqnps neltvfdreg finksfdidw etsfeapdyt rlrsdwtydd
      421 ivtdpplrag fengtnydww dnatnsgyin ahnlsvrgse gkvsyflsgg ytdqkgyiln
      481 defqrvttri nieneildwf tigaqtfgsf sdysgtspsl gllsrmtplv tpwddngefi
      541 pnpnganldn pflfsladdf dkrnsifgnf fadidvpfie glnfrlnfgn nyrwnrqyns
      601 ntyansaags adkinnswyd wtldnilsyk rtfneihnld vtlvygrrer ffeqtaalgs
      661 nynnlrlsyn dlglggiqli nssawnesyi yqmgrinykf nykylvtati rrdgfsgfar
      721 nektalfpsl glgwviseep fmdaswinnl klrfsygtng nlvgryssla rlasfpayvf
      781 gdggttlfgq eiqnlanpnl swetttgsnf gldfilfdnk lsgsidyyat ttsdlifdvs
      841 ipqitgfnri ttnvgeidnr gleltlnttv mnrsdwnwnv tfnlasnqnk ivslidldad
      901 ddgqeddlva sglflgesin svftyesdgi iqlgeetptg ffvgthrivd qngdgaitpn
      961 drviigrqep ayrfgilnei kfrnftfrff insiqggkdg ylgrnmldgf gsgdnirrnn
     1021 fwtqfdywtp anpnaryrrl dqepavdyiy ygdrsfirlq ditlaydfdg dflqgigfdr
     1081 lklfvsgknl ktwtqwegwd petglgfgas grpvlkgisv gldatf
//
LOCUS       WP_099149141            1133 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099149141
VERSION     WP_099149141.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1133)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1133)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1133)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1133
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124035
     Region          55..104
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          161..1132
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkmkhllla milllagvgs palsahtadh svtmeqsill tevldqlsee ykvffsydad
       61 llrgievevd lsryrtleqa iaglleqsgl kydmigpkyc viykdnrqgn rnkrklerki
      121 rqiealenrg nlslqrttgs ddgkmpirsi srglsqlavv ftvtgtvand agepltgvni
      181 lvkgsgkgti tdidgkftle ldngdetlvl syighetlev pvrnrseiti tmrediaald
      241 evvvigygta kksdvtgavs sikseeitkv ssvrvddalr gkvaglqiip tssapgaast
      301 irirgsnsis anneplyvid gfigggnlnd inlndiesve vlkdasatal ygsrgangvi
      361 littkrgkag qsrmsydvyt gyqapirlfe mlnaseyasw tnevkgsniy pnpdalgegt
      421 dwqeevyrnd apitshtlsv sggsaktryf lsgnyfdqdg ifiesnlkry qfrvnadhdv
      481 ndrlrlgnsv tisrtidnpr stniintagw dptlpvrded gnftfqtvss efsadnpvan
      541 avlnvnqrtr nrllgnifge fepidgltyr lslganlnnf rnesyapstl ysqrgnqgta
      601 tisngenldl ltehtlsyak dfgdhslntl igytrqrifn tnsnvqtrgy vtdaftfnnl
      661 gagversaag sgsseigfes flfranyswk skilltlsar sdassvfaan nkralfpsga
      721 iawrlieedf iqgmgifddl klrvsygrlg npglgfgasl trlsnsgnny ilgtnqdvvs
      781 giaanslgnd nlkwettdqf digidagffd nrlqvtldyy skltndllin vqvpwltsfs
      841 tslsnfgqvs nkglelaist ininrndfrw ettfniatnk nevvdifnee gfiytnsigg
      901 veavasgilq egepigtfyg mvrdgiwnse qeiedsgltg fsvfaggkrf vdlngdgvis
      961 asedrqiigd anpdffggmg ntlsfkgfdl sfflsftvgn dvfnetdsrv gvaldnntfk
     1021 ryadrwtptn mdsdvpsaeg aartlitsdt gviedgsfvr lrnislgynf pvqslnwirs
     1081 arlyanavnl vtfdsysgyd peinrgfdnl rrgydqaqyp ttkiftlglq vgf
//
LOCUS       WP_099149150            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099149150
VERSION     WP_099149150.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112389
     Region          33..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mitysqpyfi rygrslllmi mvlmsyqfsf aqqevsgtva dengdpligv nvlaqgttig
       61 tvtdlegnyt lafpdevtal qfsytgyatq svdiggrtqi dvtlqfgaal devvvtaigi
      121 srekkalsys itevgadeis tvrdhnplns lvgkvagvni tqgtggpgag srivirgnns
      181 itsnnqpliv vdgmpidasg snsggsvyns nvtgggitdi npddiesisv lkgpnaaaly
      241 gsrasngvll ittkkgtarq gigvsinsni tfdnpmflpd yqneygqgta qnvpgnvtdl
      301 ksassswgpr ldgssqlyyt genrpytaqp tnvedffrta pkvintlale ggskdfnarf
      361 sytnnqtqsi lpnsdleshn ftlrtqmnls srlsldakat yfsqelnnkv sqgsegvlsy
      421 lyymprnvai qdletyqypd esldavsysa lganpywlln hdrnfnrrer llsfakltyq
      481 ftdwlsafar vgtdvtnvqg egitqpghhf vkqgalsasn arntetnadf lfminkdvgs
      541 slninvnlgg nasyrtgegv rftssnfkip trpilantve ndpfytplre kkvnslyasa
      601 sisydnfiyl ditgrndwss tlpednrsyf ypsfglsfll drfldpngat fdlikvrgny
      661 aevgndtdpy qlntlyfvaq dgylgrttls rdavrksesl lpesinslef gvelrmlrnr
      721 lyldmswyni estdliydvp vpaatgfsaf renigkvtnt gvefliggsp irtgsfnwdl
      781 sfnftanene lveliedles htlnttnsgn iaiqatvggg ygdiygttwr tndagqvivn
      841 sngiplastd rtllgnaqpd wigglsntlt yknlmlrfli dariggqvys atnasldgsg
      901 asveslqyrd ggitvdgvve qedgtfvpnt tqitaqqywg aysgiganyv fnqdnirlre
      961 fvlgynipas afgnsflqga nisligrnlf flskdiphvd peaslgtsnn gmgilsnnlp
     1021 tlrsigfnis lkf
//
LOCUS       WP_099149208            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099149208
VERSION     WP_099149208.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117087
     Region          23..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmtrlhllli lcmsgaisly adrplegiit dgnepligat vlvkgtakgt itdfegkfel
       61 mvaedaemli vsytgyetme vaigsqsyle iilketeitl gevvvtalgv erekkalgya
      121 vqdvdasela karstnvvng lsgrvagiqi taanapgggs qvtirgnasi lgnnqplyvi
      181 dgvpmegdfa apisnaddnn vygggvseis pdniesitvl kganaaalyg sraangvvli
      241 ttktgagteg isvdytggyt vedplvvptf qdtygggngy vtwyadgrng gitdplaveq
      301 fqaaygtdyp lngtagvdes wgapmdgrlv rtwwsgteva plvpvpdsws nlwetgstin
      361 nsvgisstys kgnfrfafgn lrqkgilynn dyrrdnyrfn ithnltdkls vkvsseyiks
      421 gsdnrqqpaf wepqtwhhrh ddwgklkdwk qfmgvhitre gdeypyanwq hsfamnrfye
      481 qeflthsndk drflgnialt yeftpalslm vrtgtdlwtd trvnvtrhaq iksgtlrtea
      541 fnedvlrrqe snsdfiftfn kyigqdlsvn aqfgganrtn yykrnytavn dvtinglynv
      601 annattntnr srieekevns lfgalsfgyr sflylditgr ndwsstlpva nnsyfypsfs
      661 lstvltemlq iqspvlsyak vraswaqvgn dtdpyrlsqi fnprdpwnas tpvfsestai
      721 anndlkpert tgiefgadlr ffgarlgldv tyynqtttdq iiniavskat gydskvinag
      781 eitnkgieav lygtlfkqkd ftwdvainfa knnnqivdly tdangnelet ivltsrrgls
      841 learvgqpyg tlfgsaylrv pdgpnagqii fkdgipqvdp nlqiignvtp dflggiqnsi
      901 swknfsisal idakiggdia dessstgmqt giypitalgr eegvigigvk nigseenpey
      961 vpndvvaptk svtrmlsvrs vnegaiydat yvklrevsis yalpntlmnk igfvksarls
     1021 lvgrnlamiy nghhqidpel nifggnlqga lyyatlpstr svgvnlnvvf
//
LOCUS       WP_099149339            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099149339
VERSION     WP_099149339.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116116
     Region          23..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikqlllvll vafitplsaq qiiqgrvtda atgeplvgvn iqikdtnyga vtdldgnyel
       61 ripgsggqff srkasppvlv ftytgfetqe idskdrdrvn veltttasel qevvitgtat
      121 grspklmsys vgriagpaig rvpadnlgss lqaripglrv srpggqpgqe vyyqirsans
      181 iangqqplvi ldgiflsegs ladipvqdid rievlkgsag aslygsqaan gviqiftkrg
      241 kdlevgktkv tyrnetgfse vvdqypvntl tqreiidsge pqpilgnpne gqlfsqelpn
      301 lqnyqedflf qrgvrqshal ivegktnatn flasyqrlqd kgvlqgldgy trnalrlnld
      361 hqvsnkfsvy lssaytqseq dliepvangp nnflsstllm tpmftldapn eedgtafdwd
      421 idntganitn plytrenisn rlgrnrllgq agvsyypkew lnisyaaald rsvrnfeqyl
      481 ekgylsttlp dgfgtlatan vqgsngggil qrdqvdqtfi srlnvsaqrg wggfnlatrl
      541 gflyeditqe iregkgedla vrnlnsldna rsnitissaa qeivaysgfl vadvdykeky
      601 lfsgllrreg sslfgpenrw anyyrvsgay ritqdlkikp fqelklrasm gtagirptye
      661 qrfeafslvn geltkntlgn ellkpaqste qeigldatig rslrlefnfs rintddqill
      721 vpltaaagfr gqwrnagsle akvyegglni dfarlfrfkg tamrwelftt fsrvqqtvts
      781 ldvpayytgp gaqqaslfvi eegrtlglme geifatsleq lqgqeginpa dfmindlgyv
      841 vrtdqlgtaq eapyklrdag gnpivdvigd inpdfrmgfa htlafrslel ytlfdwkkgg
      901 diynatkqwl ykdlrhaevg dnpnisanfy gsnglynalv annhfvedgs ffmlreaalt
      961 lmirqqslgg lfkkfdhirl sligrniftk tdysgfhpdv ssvprsesll stsapdargs
     1021 dlttpngdps lflvdsfnyp lprsftfsvq fgf
//
LOCUS       WP_099149560            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099149560
VERSION     WP_099149560.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114964
     Region          22..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklslvlml vvfacgfaia qrtisgtisd tsgepligas ilvkgttsgt vtdidgkytl
       61 svpdgsntlv vsytgfstke vevgtstvvd iamsesaevl sevvvtglgi kkekkalgyg
      121 vstldqtdia nrvesdvari lrgkatgvdi tqtsglagsg tnviirgyss itgtnqplfv
      181 idgipfntet nsiggftngg aaassrfldl dpnniaevsi lkglsatvly geagrngvil
      241 ittknraasd ntadkkfevs vtqqisssqv anlpdyqnty gngfsgdfgw ffsnwgpefs
      301 argrngiaed gtidhpydqs qynddfpeyi gvrypyqpye svenffqpgl tsntsiaisn
      361 nlgngssisa tysylsdegf lpdldeqrgg gpsnylnkhn fglggstela nglkinstfn
      421 yvdsesrllp tapafggdgn gfyaalvftp rsidlmnlpy qspldgsnvy yrrgsaiqnp
      481 rwtlnnssfn drvrrffstv elsyelapwl nalyrlgldq ytqnseeavn rggprningq
      541 lqsynrynni tdqvlnllyn frlgdnfdld giiganlrre vgrfngtnst nqfvygllnh
      601 nnfidhnsfs srveettigl yatttlgfks faylnlqarn dwtstleqan rsllypsasf
      661 sfipteaipg lqsrnflnyl klrvgygtsa gypnpyqtrs vlgtatntfv tgggsvlnin
      721 tvsnrlgnaa lkpelhkele fglegrfldn rigvelsvyd knssdiiidl dldpatgftn
      781 ttvnaaeltn kgielgldit pirgaftwdf kinytrnrse vvkiadgvdq vgiagytnlg
      841 niarvgepyg vffgspfvrt esgallvnnv gsyvvgsndd vigdpnpnyt anwinnfswk
      901 gfsfgfqwdy tdggdiysst vqallargnt vdtdvdrflp iilpgeladg tpnniqtyig
      961 daffdayfga neggvfdgtv irlrevslsy vlpesllens pfgrigitfs gqnlwynapn
     1021 fpvginfdpe vlslgvgngr gfdfrtgpta kkigftlnat f
//
LOCUS       WP_099149773            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099149773
VERSION     WP_099149773.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117163
     Region          24..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkytllifl icllsrlagw gqvtfsglvt dklsgealpf vnvssqgssf gtttdsegry
       61 eltlqavpea lifsyvgyat rtepvdgrtq inisldgstt dlsevvvtal glkrdkrdlg
      121 yavqkldnee lttvrqtnta dalagrvagv qvthggsgig sstrvvirge tslsgsnqpl
      181 fvidgipvsn ellanpvegs eagfqevdyg ngfaeisadd iesitvlkgp gaaalygnra
      241 aggvvvietk dgsqgqgigv sinsqvtvdq istypqyqnv ygqgsggvfa yedgfgggig
      301 dgglvsfgpe lngqlipqyd spstdingqp vraadilard gnpitatpfv ahpdnvknff
      361 etgltsiqni alsganpygs frvsysrldn egiipntdlk rnglslsgsy qlserlsvra
      421 fgnfinssst hrpalgygse nlfylfswmg rqvnlentpn ywqagqqgfr qfgynyqwld
      481 npyfsvyent ngfskdrilg nislqyalsd klnlrfrsgi dsyddlrqar rafstqrfpn
      541 gaykeeevry qesnhdllls yrdqigsdwn fslgiggyqf rqttgfksti anqlsvpniy
      601 nfgnskvplv vfqenaqkri nsvygmgtln yrnrffldlt lrndwsstlp adnnsfayys
      661 astslvlsef lalpnwltya karlslasvg ndtdplqlnn tlvfnqnyga fplltnsatl
      721 lnarlrperi nalegglelw ffndrvgvdl swyrnvasdq iialpasaas gytdrivngg
      781 kirsqglevv lnlvpvrtps fswetfvnfs rgnsyvdalp egidryvtgy trlyastens
      841 vfyiadpdgg rigdmygtgf rktedgqiiy ganglpirdt elrylgnynp dfivgmgnrf
      901 syknfslnvl ldwrqggviv srmlaigsts gvlehtlagr etgivgegvv nqgteesqey
      961 vpntttvsaa eyynqfynra neesalydas ylklrqvgiq ytlpksltrs wgveeirvgl
     1021 vgnnllifte nphfdpelsa mqgrnfaygv edmaypgtrs fgfnlglkf
//
LOCUS       WP_099150235             983 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099150235
VERSION     WP_099150235.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..983
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107931
     Region          41..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkakqskpl sgratatafr hllltpllll llssallsqt rvitgtvqsd eeniplvgvs
       61 iqvkgtstgt itdidgkyql eaanddvlvf syigyqnlee tvgersqvdv sllsaselld
      121 evvvigygta erkeitnsva svdakdfnkg nvndpaqllq gkvaglsiak pggdpnagfn
      181 irlrglstfg ansqplivid gvlggslqti dpndiesiev lkdgsaaaiy gtrgasgvii
      241 vttkrakvgd garidfnsyv atenvakfvq nstpqqylea ggvdngsetn wldmltrngl
      301 tqvynlsayn sigsgnyrvs vnyrdvngva lnsgfdqing rlsltqramn dklrlsfdlg
      361 vtkrnsqftp yetlrfaiia dptapiynnn npddgywepn tpeyhnpyai sqevtdqgif
      421 ktllgnirvd yelfnglslg afyshqyand lrsqyfsskt rftsasgqrg rankftedrk
      481 nelfeftgtf krnfgklsln avagyswqef lfenfnafnt nfitddllfn alelglgtav
      541 gsdatagmns qkeesrlisf fgrtifnfdn kyflslalrr egsskfgpnn rwgnfysisg
      601 gvdlvqaanv pmdvlklrvg ygvtgnlpnq nyeyrtrlsr gsrtffnsqr ylqgvnfasn
      661 pnpnlkweqk aetnigldfg fmdnringai dyyvrnttdv lqsisvpvpp nffpstllni
      721 gelksnglev tlnyaaiqgp sfsyntglvf stfntelvtl dgereqifig nlgppglngi
      781 nvirvaegqp igdimaplye glnddgqrii tdqngdgtis qeddavvvgn glpdfelswn
      841 nsvqfgnfdl savirgafgh slvninrayy espaaannyn pvrtkyylpe ltesenwnsy
      901 yveeadfvkl dnitlgynln fsnasvrslr fyasaqnlfv itgytgvdpe vhysygsvla
      961 pgvddrnsyf rtrtftfgin lgl
//
LOCUS       WP_099150250            1136 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099150250
VERSION     WP_099150250.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1136
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124345
     Region          43..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkyihftiv pgpllssval villlavclp fptsartsfa paftvsgqvt desgtglmgv
       61 tilvkgsgvg tttdvdgayq ievatredvl ifsyigyesq eivvgnqtri dvnlsenaet
      121 ldevvvtalg lsrqerslgy svgrvdgeel trvtqenvln glagkvsgvt instggtgss
      181 vsmvirgats lssdnqplfv vdgvplvntl nnitqfgnrn nvdygnaisd lnpddiadis
      241 ilkgpsaaal ygsragngvv littksgkkg qgvrvsvssn tvfdqpyqff grqtrfapgy
      301 fsftpddlpp gtvfsvnpae aagagieldq gyfavqwnsp rdangfqvpt elvsypdnvk
      361 nfvqtgittt ntvslsnntd imnyriaytn msnrgiipns nlsrnnlsig gsvkatdklt
      421 vssnvninss gsdnrpssnr gtnplqwaya vpantnildl kdywepgqeg vqqrtpangv
      481 ynnpyflane vnnsfnrdri fgnlkahlql tptfslqgry sldrysekre tkiapsytre
      541 tnngaygvvd lanseqnidv laaydqrfes fslnisaggn ilhatssfis nsskpsvgli
      601 vpnvytvgni kagaldyssa rtekviysay gmasfgfkdm iyldltarnd wsstlpkenq
      661 syfypsasls liasemmdlg rnisllkfrg gwarvgndan pyqlyptynd igqwgestrl
      721 sksgtiltpn lkpeeatswe lgmdlalfqn rlrfegtyyh vdnrnqiirn ipiagssgyd
      781 rininaglis segwefglgi tpvrtaavnw dlnanftrnr ttlealsdgi efirfwsdak
      841 ggawtyvgdq igdiydaail rvedpnspyy gypivggadf ewqevnaent rnkvgnynpd
      901 filglqnsls fknftlsftl dwrkggqfis qtyrymaeda ssqhwmdnli npggrtgrel
      961 rdwlvanqee fiingfnvvg gpsvnfggfp edfsgtvvyd gtfvpgvvql pdgsyaenlg
     1021 ennlipylpy vvsypwefas psmfdadfik lreaslsyql pagalkalgn iremslslyt
     1081 rniilwtkak igidperafq aeasrgnrgt qfmqgieryn vepwvlpigf klnftf
//
LOCUS       WP_099150516            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099150516
VERSION     WP_099150516.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121314
     Region          33..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrssncnkf kqiflvvlls fgfagfgwsq aatvsgqvts gegepligat vlelgtgngt
       61 vtdfdgnysl qltgnnaslq isytgyepqt vavnnrtrid lslaasseml devvvigygt
      121 qskatvtsai stvntaemen ttainpvqal qgkvagvdir insgmpgaga dfiirggtsl
      181 npssdgplvi vdgvirsmsd lnpndiesiq ilkdaastai ygargangiv littksggag
      241 ngngritfsy nnqydkqirf fpyttaeeyi svsrraaaln ldhpnsasrl tggsypystg
      301 ninnldhggg ygnsrhtlef lddlvnamgq dyvnnklnne gyqimtdpit gremifldnn
      361 yedvmrqtgv snnydlgfsg ggenlnvyss fgyadqqgaf ngtfyrrasf llnanykase
      421 rimvsagvny qladykgvls eqgtlrrsrg lphstrlyyd dgtpaigega gsprnllhel
      481 yyedynnerh rttvrlgldw eildglhfqp aasltnneff snyferyhdf drtrsmssdh
      541 lldrdfmfdg ifnyyksfgn hnlnvmagmn ltdnfdydlr gdgrnaptdy istlnaslte
      601 deratsfigt drflsyfgri nydlsqkylf svsarydgss rftdenqfaf fpavsagwnv
      661 hyedfwnvpw msrlklrssw gkagnnvlni ldtqgqygsg ynytwnagil ntrlansslv
      721 wettqsfdig aemgflenrf svnlgyynkl ttdkltsipl ayqtgftsil anygkirnrg
      781 levelrstpi nsngfrwnld fnfsfnrltv velpdngefg nriyggeiyd qatgqyikvg
      841 gyaegerigg iwafnmlgvy gsdaeaagap wdtkvsgywl svdpenqkva gdanwedvdg
      901 ngiiddrdqi figyaapdkv ggivntftwk gftmrfvmdy alghvisngw rarangnarn
      961 rvmtvedavn gnvwwqegdd akyprysaas dfdngkrnhv rntsyplvgp qhtysyghsa
     1021 yfskgdflaf rqlslayrlp asvasklrle nidftvtgnn lgyltaydgi spehyngges
     1081 geyyrptqli fgvkaty
//
LOCUS       WP_099151027            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099151027
VERSION     WP_099151027.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122777
     Region          24..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkivtsvll ifsvlfsfga faqktvsglv tdengealig vfilvegsqt gttteldgty
       61 ripglqassv lvfsyagket qsrtvgdane invvltslvl devvvtalgi prekqslgyg
      121 vsevegeelq kvpqenvlna lagkvpgvti nqtsgpgssv yvlirgmtsl ttdnqplfvv
      181 dgvpmsngvn nivqngdrnq vdygnaisdi npddiqnisv lkgpsaaaly gsraangvil
      241 ittksgawtk gfrasfstnn vfetagtlld yhylyanger navldegsay wggpqmdvgn
      301 taiqwnspvd angspiptel ksypnnmkef lqtgitsnnn iaisggneng nfrlsysnms
      361 hrglipnsdl yrnslstgid yklnskltvs sninivrses ndrpntgnrg anplqavyvw
      421 phvdirdlrd ywvpgkenie qfrpstegnn pyfiayaltn sflrdrlygn vkvnydltpe
      481 islfvrhsld ksnenretki pysysrhsng gyylsdlayq esntdflasy yktlskfdfn
      541 vsvggnymrr kntsnwigst nrrigltvpg lytveninrd nlgvnnslae kaiysvygma
      601 sfgydhklyv ditgrndwss tlpasnrsyf ypsvslswil setidlpsav slfklragwa
      661 qvgndtdpyr leptlgtgny nditttsvpa tllnpnlkpe iatstefgld fslwnnrlrl
      721 datyyimene nqifstalpq ssgysgklin agliessgwe islgltpvrr tnfswdvnfn
      781 ftknktvlke ltegrdfidl wqdnnggaft fvgdeigdiy sagyarvtdp nsqyygwpil
      841 dnnggwqelp sdrenrikvg nfnpdfllga qtslnfkrft lsasfdwrng gqfqsytyry
      901 gesdwkssrq lenlipggnm tqqelidllr snpdqyiipq ngnfprvggh tqatggfyyd
      961 dggnavagyd gafipgvfqv agadtpddfs ddvyeehlyp tegtlhpitd typwdfnqai
     1021 tfdasfvklr elslayqipk faglrnatva vftrnlilwt kakvgidper afeansgsqg
     1081 dtrmqfrqgl erqnimpftn pigfklsfdf
//
LOCUS       WP_099151876            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099151876
VERSION     WP_099151876.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117578
     Region          23..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrvsllaml mlsllswsfa qersitgtvt dagngeplig asvlvkgtls gtvtdfdgty
       61 qlslpagnsv lvftytgysa revtvgasnv vdvtlqqgla ldevivtaqg iqkekralgy
      121 avstvdggel eqkpesdvtr llkgkvagvn itstsgvsgs gtnvvirgys sltgsnqplf
      181 vvdgvpfntn tnkdngtndf leggqatssr fldldpnnia sisvlkglsa tvtygeqgrn
      241 gvilittkng saskasqkts vtlsqsyfst eiaslpnyqt nygggfhqnf gfffsnwgpn
      301 fntrggrgid asgqvrhpld altdpslkaq fpeyagaryd yrnynsteef fekgyvtnts
      361 lniqggsdka tfsgtfgytd dkgflpgnsv rklnlgiggr velannlmln stfnyvktdy
      421 atppisygdg sgifagggls vfsdvfyvpr gvdlsglpfe apadnrpvyy rsgndilnpr
      481 wttkyarnts vvdrfygqss lsykpttwls lnyrlgidty terqeyivnr iglasndyaa
      541 inngmyrttd ivntifdqna fatasfanil peldmdvtag lnyrqdefgr ngiestnqlv
      601 fgfiehsnft nqssvnslsg ldiqfsqler lvagyasitf dyknylyvnl agrndwsstv
      661 ekenntlfyp saslsfipte lmpqssvlny lklrlgygts agfpdpystr stlssnarqf
      721 vdrtgavitt nsnatyfedn gasailgnpn lkpelhkele fgvdaqlfnn rlgldltlyr
      781 ritndlitda pldpstgfsq ttinigeien rgievgldlt pvqvgdfrwn iytnfyayks
      841 vvnelgqgld evqiagftnq gnfavegevy gimkgtvidr deqgraiidg dgyynqaani
      901 qiignphpdf tmgitntitw kglslsaqld yrhggdmfsg taealfargl tkdtdfdrtq
      961 afvldgvtad gtpnttmita tnlyfdnigf gpdelsvfda ttirlrdvtl syslprsfla
     1021 nspfggisls lsgqnlwfna inmppnsnvd tdalgfgadg nglgfeflng psvrrygasl
     1081 rvqf
//
LOCUS       WP_099152089            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099152089
VERSION     WP_099152089.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121268
     Region          20..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkralffilv slfvtamqgq tvqgvvsssd geilvgatil vkgtttgsvt dldgkyqidl
       61 gdnadavlvf sytgytpqev evngrtqidv elasglilqe avvtglgisr drktlgyats
      121 tissqdlttt qvtnfasaly gkapgvsirs vpggatsgvn inirgfasit gntqplivmd
      181 gvpirngefn ntnywgdqyi rgngltdinp ediesisvlk gasaaalygs eavngvvlit
      241 tkkgrkkqgl gvdfnasysn dqvaylpryq nvrgpgyftn ladagqdeng fifydtdgdg
      301 npdtrglint svnfgpefdg qpvmawdgvv rpyeasnnsy adlfqnaqss svnlaiskgf
      361 enasvrfsft rqdnqmisfg sknernianl nasfdigdnl rttlsvkyin qftknrphkv
      421 drminnfggm mdrfesadwy fdryktslgy mfrtgtqatl tpdeniiyng fkssiadyvw
      481 rinehqiren snrviatvaq nwtivkgldl qgrfstdytt enieswnstr fpsalynnpa
      541 ggfslrnnin sllygdvllt yqaqltptfs ieamggytak riqtnfvsrg tagglspenf
      601 fdisasinvp nsgsdrsdfv sdgflgklel gykdylfveg tirrdrtstm apennsfvyp
      661 svnaslvlde afnlpnyfsf aklrasygvv gnypliyqan iaynqntlgv qamggrpily
      721 tnisgafgnd virpeqkhef efgldlaffn riqadityyn gkivdqilpv diprssgart
      781 vltnigtlrn kgielslsad ifknktgfsw nsrinyakns nvveklanda tellhadfdg
      841 naaqirsvvg qpmgdiyahp vatnesgeri vapnglyqld sekwekygna mpdfeggfln
      901 tisyknvfln vvadfsfggy imptgiywmt srglteesln ymnaerggls yyvdengkgv
      961 qttsgagpng etvfndgill egvlqsgeen tnvvsqalyy ngtynwggpq ygnsryelyv
     1021 dkndwvkvre islgfnmpqs lttklgmsra slsvfgrnlf fiyrtikdld peqtvagsrw
     1081 yqninnagnn psfrtfgvql sasf
//
LOCUS       WP_099152253             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099152253
VERSION     WP_099152253.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108955
     Region          21..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrllftilsi lcfsvgimaq rtvsgtvtst egepligvnv lvkgtttgtv tdfdgkysvs
       61 vpnqatlefs ytgytpqevn vtdqsvidit leegialgev vvtalgiere kssltfaqqt
      121 vegtellear dinflnslsg kaagveikks ssgpggstrv vlrgdkslng nsdplfvidg
      181 ipmannrsgq pgmwggfdgg dgmsqinpdd iesitvlrgs naaalygsqg angvvlittk
      241 egkegpakvs vssgitveni mlkpdlqfry gseggtkesw sttrgnydgs yvddffqtgt
      301 nqinsisisg gtartkayfs fgnvnargit pqntynrynv tfkqstkmln dkltvgsnii
      361 ltnevsrnrp aagyylnplt glyffprdrd fasfrdnysv idpdrnvigq nwfvidhhqs
      421 npywllneqp rtdqtnrmig svtldyqite klsvsargny dfasklqeqq ftsggnttni
      481 hpngswdywk ftdellytda llkfndnfgd fslgliggas yqktvfglgt rvdgdanngl
      541 lyanefffqn lppnvqvqst lnsrlvkqal fanatigfke mlfldlsgrn dwastlagtg
      601 nesyfypsfg atavlskmfe lpeavsfaki rysnskvgne vpynvvnpqn tiaasggvnr
      661 ntqqpfenlk peiitssefg tnwrffddrf gfdltyyntv stdqfinlpa psgsgytryy
      721 vnagkiinkg ielvvdvtpi ytpkltwtts fnfwtndnev vemhpdlasi ttgqsegygs
      781 rfeaggsigd iyvykfqrda qnriildend grplktamqe lagnlnpdws lgwnnnfkfg
      841 kfglnfivng kfggvafsqt esmldgagvs ertaadrdag gttidavqgd qpvstidpel
      901 yyraigdrng igepyvydrt nvrltqfsls yrtslfnntt pvtlslvgqn lfflyleapf
      961 dpelamstnr naasldnfnt patrtigfni nvnf
//
LOCUS       WP_099153223             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099153223
VERSION     WP_099153223.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110136
     Region          22..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlllvfll vgtamgtala qrnisgtiyd qetgealiga tvlvqgttvg tvsdlngqyn
       61 iivpagreil efsytgyapq eveigassvv dinlsadiaq lsevlvvgyn svkrsdltss
      121 vsvvegdqlt aqpiggidnl lqgtstglqv vgqngrpgga afirirgvgs vnasneplfi
      181 idgvqvtqad ynalnpndvs kvtvlkdaas taiygsrasn gvilistkkg rrdrkpqity
      241 nfqygekqqt ddgmtlmngn qkldyelalg irteeeaqai rddlgfletd wedvltrkgl
      301 vrthdlsisg gsdranyhfs lgtysergit vgssferltg rfnmdfdvtd wlkvgntfsl
      361 srtddnelrd vynvqnpfva iytynpyepe fvldengntv ldengnpvyn rtqqgfsite
      421 allnnpenkk qanaigsvyv qasilpkltf ksqvggnyqi yrreayikpg sildgyigdp
      481 napgiktdng sdrflynwfn tlsydftlgg qhqfnaligt eyyerdlqsy qingkgfpsa
      541 nfstqdnaae itggntarnq walwsqfgev rynfasryla sfslrrdgss rfgsqnkfgv
      601 fyagsvawnv asedffadag fdqlklrlsa gtsgnepgin nlywqgnydf isyndltasr
      661 pnqlsnqtlk weenfnysvg idfgvfnnrl sgsidyynrr tsdllfpepl srttgwtsrl
      721 anigemlnsg levevvgevi rsqdfnvalf anfttnknei inlknggedi idvnsgitll
      781 reglpvnnfy lnryagvdpi ngdalyldae gnvtnvysad davaldgkap qpkyfgsfgt
      841 ninvkgfdlt vnfyyaaghy tynfnenavl sdgargrsqh dvraldywka pgdvnvlprp
      901 sinnnvdvsd rflqkadyir lrnvnlgysl parlvenlhf qqirlfvqgt nlltfaphyt
      961 gdpevgvgsv entyvipgei sffnypqtmg wtlganvvf
//
LOCUS       WP_099152876             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099152876
VERSION     WP_099152876.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107083
     Region          28..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkvdyfsk wlllvlaitf cnfaiaqrti tgtvtdaetg epliganilv agtssgtitd
       61 fdgtynlsvp dgattldvsy tgyssqtiei gsqstidial sagelldevv vtgygtsksr
      121 evtgsivsvk eedfnkgnvn dptqllqgkv aglaiarpga npnggfnirl rglstvgasq
      181 qplvvidgvl ggdlnsvdpn diasidvlkd gsaaaiygtr gasgvilitt krgeagsskv
      241 nysgqlsles adrlpdvyqg qeyidaggtd lggnvnwfde llqtgttqth nlslsggtpt
      301 tsyrvsanyr dvegvavntg fnrinvrgnl tqkalnnrlt ismnlastss dqnlgfdeaf
      361 ryatiftpta pvirdvnnss ydqwggyfqv dafdyfnpva iieqntreqk vknissnirg
      421 dynitndlvv gmfysyqrsn rdfgqyisky sfwggglgsn gnairennen qdqlfrlear
      481 ynksfannld fkmqlgyefq dfafqgfraq ggdfltdaft ynnlgasldf dnglgnvssy
      541 kntnrlisyf grinlnfddr ffataslrrd gssrfgadek wglfpavslg adlarignms
      601 sfdqlklrag ygvtgqnvde sllslqrfgp gskfyfngsy vpsygpvsna npnlkwetkt
      661 dvnvgldfaf gdykwtgsle yyrtntsdgi flfpvpvppn lfpetklnvg eiensglelt
      721 layngslgag ksynitltgs rwftptlvtl sdpetgvgig gfrtganlgs pgqnntplvr
      781 leeggplgqf wglvvdpnnp vkengewnfv dvdgdgtqdd iadravigng fpkyqlglnt
      841 sfnlnnwdfn iffrgvfghd llntfrafye apgaisgynv lrssadiptl tdqpqfssrh
      901 vekadflrld nmtigytlga lpdgfsqiri yanaqnlftl tgyqgvnpep rfvddsafgp
      961 lapgidrrnt yfssrtfsfg vnlnf
//
LOCUS       WP_099153226             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099153226
VERSION     WP_099153226.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110211
     Region          22..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklalvlll vssavsltla qrtisgkvid esgesligat vlvkgtttgt vtdidgnysi
       61 rvpdgsntle fsytgyatqd vaigssnvvd vtmstdiaql sevivvgyns vkksdltssv
      121 ttvsgdklqa qpigsidnll qgqspglqvv aengrpggsa yirirgqgsv nasnaplfiv
      181 dgiqitqddy nainpndike vsvlkdaaat aiygsrasng vvlittkkgr rdrkptinyt
      241 fqygqkertd dgftmmdydq kldyevalga rtaeaadalr qqrsfketnw edvllrtgev
      301 rshnlsisgg genanyhfsl gsydeqgisi gsdfsrlngr fnmdfdvtdw lkvgntisls
      361 rteedelrdr ynvqnpfvav yaynayepef vyeddgtlrl dengepvynt thegfsisea
      421 qrnnpeeatr tnaignlyae asitdklrfk tqaggnyrif rrqyyiqpgs ildgyvgdpn
      481 apgiktdngs drfifnwfnt lsydfnlggv hqfntmigte yykqnfdsyr vdgkgfpsaq
      541 fftqdnaaei tggnttrtqw slwsqfgevr ynydsrylat fslrrdgssr fgsenqfgff
      601 yagsiawnig senfmsnssl fdqlklrlsa gtsgneptgl ywqgtygfgs ytdrttsipn
      661 qlsnatikwe enfnysagid fgilnnrisg svdyynrkty dllfpeplsr ttgwasrlan
      721 igemlnsgie velvadvvrs nnfsvslfgn lttnkneits lnnggediin gnsgltllre
      781 gltantfylv ryagvdpang delyfdkdgn vtnvysadda valegkspqp klfgtvgtnl
      841 nvygidvsas fyysygaysl nymlrdnisd ganfndnqdv aalnywkqpg dtgvlpkpsr
      901 nnntntttry lqktdyirlr nvsvgytlps tltqkfyvqn lrvflqatnl wtynpyfrgd
      961 pevgrgsees nltllgeatl ysypqtmgwt fgvnvvf
//
LOCUS       WP_099153272            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099153272
VERSION     WP_099153272.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118301
     Region          46..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqnftpele qarlnkqktl qrfakellll salilcswaa gaqssrtvtg qvmdengepl
       61 igvtilvegt stgtitdvdg gfsidvpdga qslsvsyigy ltqdveignq trievtmepd
      121 aigldevvvi gygttkkkdl tgavtsidae klettatsnm tdmlranapg lnvnfnasak
      181 gissadalev rgqtnvrdaa anaplivldg mlysgdladi npndiasfdi lkdassaaiy
      241 gsrasngvii ittkkgktgk ptinvsssig vatlsharld pmtgpqfidw riagfesner
      301 rqvdfpnyyd npnnlpsgvs vdewksydgs sassdlvgiw lnrigfspie ianykagnti
      361 dwtqyefqng lrndhnisis grtdnisyyw slgyvenegy vvnekfsavr srlnleasit
      421 nwlkvgtntq lavrdespip sstnltnvta yssfyeddgt tisyaptgni sasrhpwlel
      481 vyrdrstain tlssliygtv elplgitfth qfipqfsfen qfnhwssehp ewgnqggiae
      541 rlhrskyewq innilkwdkt fdkhhfsvtl lqnaekyqsw ydrvrrsqfq psdvlgfnni
      601 ggatndvaie sddqyetada lmarlnytfn drymftasyr rdgysafgqk hphanfasaa
      661 lgwiiseepf fningldllk lrlsygtngn rsigrysals dlatgryvqv idgqpqyvsq
      721 lyanrlansd lkwertgayn igidfatarg risgnfelyy mktedllvqr tlpnvtgyfn
      781 vftnlgqvdn rgfeislntv nvdnpgltwr snfilthntn kivhlygdmv dvedengnvi
      841 gqreaddvtn gwfighgidq iwdyevlgiw qsdeedeaar ysrepgdfkl ndvngdgvyt
      901 nddkvfqgyt kpryrvtlgn dvqvknwnls vklysylghf atnnhkrnnd vfydrgasfd
      961 vpywtpdnpn newarvesye sgfnvyenss firldnvals ydvpasflek frlsrmrmsv
     1021 iaqnpyvwsp vwtwmdpenr gytptyytfk lnltl
//
LOCUS       WP_099153777             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Flavilitoribacter nigricans].
ACCESSION   WP_099153777
VERSION     WP_099153777.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39284
     Region          1..357
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(13,72,91,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(42,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtigvlkeaa dkrvavvpdt vkklkelnld ilietqagvd ayfpdseyee agaaiashqd
       61 ilqkadvlis inpleepelk sldkgkmlis qfqpffdhdv adrlnglglr afsldmiprt
      121 tlaqsmdvls smasiagyka vleasrylpr yfpmmitaag sirpakilvl gagvaglqai
      181 atakrlgaqv eafdtrsaar eevkslgakf ieiegakedt gaggyaveqs eeflkrqree
      241 vqnrasksdi iittaqvrgr kapilvpkst vdnmrpgsvi vdlaastggn celtednqvv
      301 nhngvtiigd snlaalmpqd asvlysnnlf nffkilvkdg elsldmnnei vsgalittap
      361 ettise
//
LOCUS       WP_099153620            1157 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099153620
VERSION     WP_099153620.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1157)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1157)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1157)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1157
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1157
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129363
     Region          38..99
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          159..1156
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfkqpflgv clllclfggr lpaatgdhpp tnagdrllle vldelsetye vffsyenrll
       61 revrvdfkfr sgesldsamn rllksvgley raistkyyvi yqdskkgkkr anqlerkirq
      121 lkkleekgki nlkiqssnrl dkvrsitesa lllqqeqlvs gtvidndgip ligativekg
      181 tangtttdve gkfqinvgdd avltisyvgy ypldipvdgr teiaitmemd venlsevvvv
      241 gygtakksdi tgsvasfdsk aldrqpanni telmrsalpg lnvglstnae gssglqvrgp
      301 tslgannspl lvvddvifqg dlssinpadi esvnvlkdas aaavygsraa agviiittkk
      361 gstgkptinv rsatgwtqag viqdvygpge yldykaavfd qidagnqpgy yadpnklptg
      421 vslndwldyd glvgtatdpq diwlgrlqls dieianykag naldwrdiif qtglrmnntv
      481 svsgrtenls yytslgyvkn egilryqeya alrgrlnlem avtdflsmgi nlqassqeep
      541 tglpnhldiy ekqspfgdly yddgsyrhqp yddalavnpl lweykdnyyq qrelfsnlfa
      601 kvslpfglsy rvnwsnrayf iqdyrfnpvi asigaggdag srreqfdqrw mvdnilnwnr
      661 tlgshsfdlt flynvekaet fsssqsnsqf spndnlsyhd lstgfnpsig sndtratada
      721 mmgrlnygll dryyltltlr rdgysafgsk npratfpavs fawrlsdeaf lrdsklidnl
      781 klrlswgkng nrdigvysal srlngtsyiy gqstvigina tdlanadlkw etttsynagl
      841 dfgiggsgri sgsvdvyhsv tndlllqrtl piitgytdvf anlgevqnkg leislnsvnl
      901 nrdgftwgsn lsfwynrnki thlygdmvdi ldangnvigq reeddiengw yighaideif
      961 dyrvlgiwqv geedeaalyg rvpgdlkied vnrdslinfd dqvfqgyatp ryrlsfrndi
     1021 tfrqfdlsil mnafldyrgv nnehfnsrvq qqrvnkyitp ywtpdnpsne warldsknss
     1081 pvtrwydnks flrvqnitlg ytmprsllek wniqslrlya nvqnlpaftf ggwnyrwdve
     1141 tsaptplitt lgldlsf
//
LOCUS       WP_099154063            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099154063
VERSION     WP_099154063.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116000
     Region          21..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllglfil lgmaaglsaq itvtgkvtda dgipvigani ietgsaergt lngtisdidg
       61 mytisvptda slefsftgma nyttavdgrt vinvtmteqt alidevvvta lgfkarkdrs
      121 gstsssvgad airssgeagi lnslagkasg vkivrangdp gagtniqirg antiggstqp
      181 lvivdgvpis ndnlygsgss rsggvsqqsr lndlnpedve svqvlkgasa aalwgsraan
      241 gvlvittkqg klnqgmrvsf sstysvdein rrhplqtafg qgtggsyspt sanswgdkia
      301 nrtggadavr ntgeyfladn gdviypittk nsqdifvddn fdavfqtghy idnnltitgg
      361 ggkttnyfsl gyltqdgivr nsdyqratvr fnnqtfftdk vvlttkanyi ysdgnriqqn
      421 sntaglylgl lrtppdfdns syrgtyfnas gvafpdrqrs yrrylgnnin ptynnplwtt
      481 neqeatttvn rfnvssnlni tpvewlqfdl rggvdsyldk rvyfapigsa sfnngrldte
      541 dlsntelnfd aiarvefpdl vadkigfngt lgfnindrqr kvlyaatqtf lvnsdlqnfn
      601 ngvapfevsn sknhirsnrl ygilsfdlyd qlflnlsgtq eaastiqgty fypsadlawq
      661 flpsgnglls fgklraswgq vgvqptayrf gttyetftys tyddaldine fgggfrlndd
      721 qgnpdlkpei kteweigtdl rlfknrfslg ltyyqneikd illavslsps sgylskyans
      781 grmqnkglel dfgfkilenk sygldlygnf nnnrnevldl agvdrvpltd qsitsnaivg
      841 qplgilfgsr aarnddgsla ldvngfpild peqgiigdpn pdwrgglglr ayfknlsfni
      901 lfetyqggdf aertrfvlts fgtyatvgne vtldrdlvns qgvtfpagtt vrgnihnyga
      961 gdvlldeswy tslggglggs ainefsindg swtrlrevsl aylfrgdklk sftgmqslel
     1021 sitgrnlavw tdilgidpev nqsgvdngfg ieyftnpssr swvasvklnf
//
LOCUS       WP_099154468            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099154468
VERSION     WP_099154468.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112911
     Region          29..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmqtikkwaf llgaflllpa wlsaqnnlke isgkvldqmg qpiegaeisg kegaismrtn
       61 aeglfvirvd padalliead gyasrrvavs svvageqial ealdfhltek devqlpfgtm
      121 kkrritggvt aidpkeilty dneqlfggvl nsrvpglfgg snirglgdal vvvdgiprsa
      181 gslnlqeidq isvlrgisar mlygaqadkg vimvttkrgk afkrtmnitg etgtldpisf
      241 pdylgaadym glynealvnd gqdplynqqq iqatrngtdr vlypdedfyn stylkdraaf
      301 qklimessgg nqaaqyyvnl gwnrigtlln lgegaeentd rinlrgnvdy qlndwlkmsl
      361 dgialiditr gprysnfdgq nntaddfwsi stgiwpnayp tlipagrled sgllpsavlv
      421 ggdrvlggts naqfsevnly geltrngfqv ntnrvvqint gldfdlggia rgltakayls
      481 fdfinsfirq qenayaiyqp vlgmdttgnq vvaynkigvd ekrddqtipn gnigfnrrlg
      541 lygvldydrt ydndnslkit gvayrdqfee lgvlqtaknl hfglrgnymi qnkyiveatg
      601 vyagsprftg dqqfafspsl glgwvlteep flassslfqy lklnaswgil ntdqgvnnyy
      661 lyrtsyveps anfdriydyn nevssnnaln ivtgnpnigw vkrreinfgl eallgkslwl
      721 eanyfntesy dqitkltsty psvlggedft pfenfeaysd qgvelglqln qgrgdfrysi
      781 ganfvyaept aaevnepdal layrkregqp tdgmfayvae glfrdqadid nhalqtfgav
      841 qpgdikyqdl ngdgiinqnd qqlignsrsr fqyglnirlg fknldlfvqg igqtgaeryf
      901 ndpyywvfgn rkystevlgr wtpetagtat yprlsstsnp nnfrnstfwl yednwfnlrr
      961 vqltyalple vngikkvsiy lrganlltvs kirekrelni gstpqtrsfa vglnasf
//
LOCUS       WP_099155003             988 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099155003
VERSION     WP_099155003.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111479
     Region          38..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqvatpfll allllstlta saqilrgkil rygeaqsgls iqkngrgfks ltdingnfli
       61 kakegnklfv rqgdttwilp arqnmeiels elarepedta rpavekpamt sswgdtlgav
      121 ttiqrkdfnd gnifdpygli qglvpgltva kpggdplgny qvqlrglhtf deftsdprer
      181 vidrrqpllv idglpgadll tldpadiati rilrdvasta ayglrgangv ieietrlpgd
      241 dplsvtyhsy lahetptgmt dvlsatefar rtgtpntayy rpgfnlgddt dwqreisrkv
      301 wnhthqlaag gtfgntryql alnyrdqqgv akrsgfhqwn srlhlqqalw kdrlkigiqa
      361 ahtgrnfqdv epniflqaaq ynptspiysd tstryggyqq mpfylyfnpv aaqeqttreg
      421 hqkvntlggy vqleplagle lagrytrqhs drlygqhypr naffggydvg gsalrdaqll
      481 dnqhgqlsaa yglnwskhrl kvraaytyqr wdldyeqiia rqftnddfsy ertdgaanle
      541 rlqhrtldeq ialtstleyh wnktvfvkgl lrregasrlg pknkwawfpg lqtavslhri
      601 fnwsnrfhlr msygeagqlp pknfashwkv gpqdymyyag qyirsydftn tpnpgigaeh
      661 rsewnigldf gllanrirln ldwyrstsrd iiartelptp pypqisyfdn fgalqnqgle
      721 vglatqlidn tqlqwhtglq fstnttrmld mnhpqarnvi eyrgvgrlgs pglccttaqr
      781 leegekignf ygpvyqgidq egrwqladln nngipdfgde qqignaqpdl qfgwtndlqw
      841 gafelswmlr gilghdlina hrirlenpes lgpynvfssl fegeklrlrd ypvlssyyve
      901 dasfvrldyl tlayrfklpe sarlsglqly lnarnvftls aysgpdpdlw lnnagnllap
      961 gvaspssfge rglyfparsf tlgvrlem
//
LOCUS       WP_099155351            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavilitoribacter nigricans].
ACCESSION   WP_099155351
VERSION     WP_099155351.1
KEYWORDS    RefSeq.
SOURCE      Flavilitoribacter nigricans
  ORGANISM  Flavilitoribacter nigricans
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Flavilitoribacter.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Flavilitoribacter nigricans"
                     /db_xref="taxon:70997"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121758
     Region          32..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdftrrvasv lrlvslciaf csltaiqsfa qrtvngtvts aadnqpligv nvyekgtssg
       61 titdldgnft iqvadenasl vfsyvgfteq evalngrtqi aialaegvtl deavvtalni
      121 trdekslgya lqqvsgddvs avngsnfvst lagraagvnv vsngqasgsa svvirgmssl
      181 ssnnqplfiv dgipinnetd trtstngiad nmhldygnga aeinpddias vsvlkganat
      241 alygsraang aiiittksgk nrkgigvevs skttfesmla gpeyqreygq gknfdfafvd
      301 gygngtfdgv deswgprldg tlraqhdspt anglrggdvh gldfilgssg vdlnrrgaiq
      361 ptpfddpgdp vknfmengrt linnisffgs ndngnfrvsy tnfdntgilp ntdlrrntvt
      421 fsgdydlsdr lrvsakanyi rsesdnrpvn gygtesvmyl fiwwgqnvst eslrdywqrg
      481 legfqqfnyn ynyhdnpyft myentnalsk driignlsat yditddlslm lrggtdmfse
      541 yrfikrayst qrfpngqyre dkvnfretni dfllsykkqv nddwfvsanf ggnqmqrknh
      601 fqgisankll ipgvysftna dgplvqsisr peqqinslya faqvgyksml yldltarndw
      661 sstlpeanns yfypsaslsa vltemfdvps ssalsfaklr lgwaqvgsdt dpyrlsdpff
      721 fgstpwgnna taspsntlpn fdlkpeiqts vevgadlrff ngrigldaty yntvsknqil
      781 aidlphssgk tsrvinagki enqgveills lnpirtssgf nwntmfnfgl nrnkvlelpd
      841 gvdqyvyggn gitlvakegg slgdmwgtgl krvedpnspy ygeiifndgl vqqdntlrkl
      901 gnynpdftlg wmnelsyknf slsflfdgrq ggellsrtrl iaatsgnvve tlwgrapefg
      961 gahpgitdsg isyidestge tktdgvigdg vmevtddngn vigytentvd kpanayhnnr
     1021 yrrnnesegi ydatfiklre arlsytlpks vlgntfvnsl rislignnll lwakefnhgd
     1081 pellsfgggr yipgvenatv pstrsigfsv nvgf
//
LOCUS       WP_099171315             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Flavobacterium psychrophilum].
ACCESSION   WP_099171315
VERSION     WP_099171315.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         1..>980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          25..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklklnrflv llfalisqla laqeknatgv vtdasglplp gvnvvvkgtt rgastsfdgt
       61 fkiqaqqgei lvfsfmgmnt verpatkgma vklndestql advvvtalgi krekkslgya
      121 tqeikgnlvr eggntgnvls slsgksaglq ivnsgnfgga ssvvvrgmks iqgnnqaliv
      181 idgvavnnsn nssaysnyds gntasdvnpn diesinvlkg aaasalyger asagviiitt
      241 kkgksekgdn kwgvtfnsea qignidkstf atyqkkygag ygtnnygalg lddndvngdg
      301 iidhvaptyd daslgaqfdp nlsvyqwnaf dptspnfgka tpwvagandp stffetaitt
      361 snsltiekgn enssivinyn nynttgvlpn ssqkkntlss rfsykvnekl tsnvytsltf
      421 qntigrntvg yndniisgfr qwwqtnvdis eqkdayfrsg gqniswnikg ynkptefnka
      481 nfwnnpyfdr yqnyqsddrt rffgyasliy klnkvinvtg rvstdfwnqk denrladgsv
      541 aqlfgisqls vssgyflans srsetnvdlf adynkkfenk fsvggllgtn yrrnnynias
      601 tstengliip glyairnsag ktlptqetqq tsslgsayaq ltlgyndtyf legtsrfdks
      661 stlpkgsnvy fypsvsgsii lsnllkkdwl sfaklrgnwa qvgktalsyg iddtnnivgv
      721 tnlqvpvvsp rtfknnanlk peisteieag leakflnkrv gfdvsiyktn svnqiirtdi
      781 ssasgyaqkw inagelenkg ielqlnlvpv ktnnfswdis mnwgknenkv ikltdgvtnl
      841 llgtavgsvt fnategeayg tikgtdyvys pngdrvinps tgryvitask nnvlgnimpd
      901 wtgsirnnlt yknvnlsfli dgqkggsiys gdmfygtdsg lyestldire qgyvlpgvna
      961 tanpnvfntn ttaitaanrp
//
LOCUS       WP_099171761             737 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Flavobacterium psychrophilum].
ACCESSION   WP_099171761
VERSION     WP_099171761.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium psychrophilum
  ORGANISM  Flavobacterium psychrophilum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Flavobacterium psychrophilum"
                     /db_xref="taxon:96345"
     Protein         <1..737
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <1..736
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 tatdvmsmmt adqyrafvik tnpasnftne dvglgsfnwi davsrkgist gvdvsvsggs
       61 dkttyslsgn isdqqgfiig nglkkngfrl nlatdvkdwl rvgttigvse skmdrvgsen
      121 svaapftaay lqapnispyg edgkfqrtgf vsnvvaieal nindansfrv ngnvfadlrl
      181 hknlnfktef gidrssldef erqfeintag gfarsyqavq qkivntntln ykktfalkhn
      241 fnilgglsve ntgirdvtte gtgfasddli nvtsalnktt tdntttgsrl vglfsrlsyd
      301 fsgkylvels arrdgssrfg sdfrygnfga vgvawvvsee dflkesklvs nfklkanygi
      361 agndrigdyl arerteggvf pnyneatgiy tlrfanpnmk wersksydlg lelgmfnnkf
      421 rvnvdyynkt tnqlilrsnf svadnngivg ltgnagsmen kgfdldvald vfrdskfkwt
      481 ssfnfnnnkn tilelndaaa tdldgnkfis ggssqraivg hsvntfflir ysgvnpqtgn
      541 aewldrngna tttpkaddrv ivgdanpdft ggfnnnfkyg nwdlnalinf sygneimvdg
      601 lrftedarys ngfnkssdll niwekpgdna stpnitsptf rtfqqrstkq lrdasfarlk
      661 gvtlgynlvf dksssfaklv ksvrlyataq nlytlkndnl rgidpevtst tanlgqgetf
      721 ftppqtktfv fgarltf
//
LOCUS       WP_099189548            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            6B07].
ACCESSION   WP_099189548
VERSION     WP_099189548.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 6B07
  ORGANISM  Maribacter sp. 6B07
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Maribacter sp. 6B07"
                     /db_xref="taxon:2045442"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117003
     Region          25..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktllitml vflasfvaha qtvftgkvld enqvplpgat vvvkgttngv atdfdgnfsi
       61 elngsndilv vsyigyiaqe yntankitgt inlqpdsqql devvvtalgi erekkslgya
      121 sqeldndevv qarepnllns msgkvaglqi tnsptglggs arvsirgdas lningnsplf
      181 ivdgtpisne ivgssgsgtq svdygngaae inpqdiesin vlkgpaaaal ygsraangai
      241 iittkkgksq ssklgvsfnt gitvenvlml pdwqneygqg nnqqfsfvdg sgsgiadgvd
      301 eswgprldtg lmiaqfdspr tdgtrggdts vsnadiiptp wvsqpdntkd ffetgitktn
      361 siaisksgem gnmrlsfqnl dqegtlpntd lnrntlsfsg tmnvsdkvkv nanlnyvktd
      421 sdnrpavgyg tesimylfiw ygrqlntnnl rdywqpgleg iqqfnynyny hdnpyftmye
      481 ntnaqdkdrm fgnvsltydi senwklllrs grdfyrdfrv rkrafstqrf pfgtyqedni
      541 ffeesnsdfl lsydktfgek fnlniyaggn qlrqkqdftk svapqlinpg vysfnnsrqa
      601 vqvssnnsek rinslygyar fgydnvlfmd itgrndwsst lpegnnsyfy psvtlsaias
      661 dmfnmpdwvt fakvraayae vgndtdayrl rsfyqnetqf dsstpiltes slipnanlkp
      721 eitgsyefgl dlrflqsrin ldmtyydsat knqiinistd iasgyssqli nagevrnygf
      781 eaianfvpvl tdnfkwsstf nfatnksevk dlgddiqftl teangayiqa reggsisaiy
      841 grgfqrvede tseyfgqmii nnqgipertd dlvyqgdyap dftlgiqntf kyknvdlgfl
      901 idtrqggivv srtktigsts gqlqetlegr etgivaegvi ntgtaenpvy tpntinvdar
      961 tfnnryyerd nveaakydas ytklrevslg ysfpqkmidq lpitnarisv tgrnlilwtd
     1021 nphfdpetvg vsggtlqpgi enmsypssrs ftfnlqvnf
//
LOCUS       WP_099189980            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            6B07].
ACCESSION   WP_099189980
VERSION     WP_099189980.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 6B07
  ORGANISM  Maribacter sp. 6B07
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Maribacter sp. 6B07"
                     /db_xref="taxon:2045442"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110573
     Region          25..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkissflt vavllffqav igqdktvsgv vtddtgsplp gvnvvekgtt ngtstdfdgn
       61 ysinvdanat lvfsslgykt kevgvngrst vntsiaedas eldevvvtal girketkalg
      121 ysltevdaee iatiktpnai nslqgkiagv nisqnatgaa gssrvvirga sslsgnnqpl
      181 yvvdgipign gnngsaslwg gsdggdgiss lnpddiesis vlkggaasal ygsraaggvi
      241 ivttksgkgq egfgieigss vtfdkvdtsl qdfqteygqg vrgvrpssqs aaleagsssw
      301 geaydgvnsp qfdgvsrpys ylgnnvdkfy rtgstfintv aitsakenlt yrlsasnldn
      361 advlpnagln rksfsfnssa ilgdkitssv nakyiiekvq nrprlsdspg nanfsvallp
      421 gnidvttlqp stnpdgserq fsnntfstnp yfaaynfnne dvrnriiast slrydilnwl
      481 sltgrigidn diirrtsvep fgtaykplgg ineeerrynq vdadlilaae kditdkfais
      541 alvgannnhv ksenlflggn dfivpgledi gntvsqsrsr eyserkigsv ygslelsydr
      601 wayvtftgrn dwfstlsfpg kttpnddfyp svngslilsd afnmpsfvsf lklrggysev
      661 aggaqdpytl alnyeifgip isgqplgrvs gsivpnanlv afskseteig ldmrffnnrl
      721 sfdvayysne ttndivdvst siysgytgas anlgkvtneg ieflisgtpi rtndfswnmt
      781 vngayneglv vatddvnsdv nldeprtqnv rithivgety gsivgvsyer ddngtivyev
      841 gddgvprave gerkilgegv ppltlgfsns ftyknfnlnf lidgkfggqi fsgtntilys
      901 nglhkntleg rengltvsgv dqtgaafttt vapenladyy geiadiaeef vedsdyikfr
      961 qlslgyslpk kaldnvfltn vnvsliasnl fyikrsvdni dpesaytvgn sqgleyfgvp
     1021 ssrsygltin vkf
//
LOCUS       WP_099190481            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            6B07].
ACCESSION   WP_099190481
VERSION     WP_099190481.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 6B07
  ORGANISM  Maribacter sp. 6B07
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Maribacter sp. 6B07"
                     /db_xref="taxon:2045442"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117328
     Region          21..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhlllvltl fictmvnaqe titgtvkdtd gntipyvniv lsgtlngttt nengiytidv
       61 pelsgalefs vlgyetkiit innrrtidiv lgdssevlde vvltalglkr etkelgyvvq
      121 sldakgvtev ksvnfldnls gklagvtinq gatgvgsssk itirgeasfs nnnplfivdg
      181 vpinnnsvfn ftneaaagfq eidfgngame vnpddiaevs vlkgpsaaal ygtrasngvi
      241 iietksgkns kglgisynts ifvdsafqlp dfqneygqgn sgefafvdgl gggtndlity
      301 swgprldvgn lipqydspvt lpdgtvvrgg dtalysgipi tltefrsqpd nlknfyetgt
      361 tlinniaisn gfdtgnyrls ftdlrsesii pgvdldrqtv sarlnfepid qlrinssisy
      421 insnsdnrps ngygsenany slvawgprsl nienlknywq pglegiqqys ynytffdnpy
      481 filnenrnsf nrdrvfgnis asyditnhlt atvrtgmdys selrqlrray ssnrfanggy
      541 aehdvfyrev ntdflinytn qfndfnidvs lggnrldqka ftsqsqttsl aqpgifrlsn
      601 aaspievfef esnkrinsfy glakigykdf lfldvtgrnd wssalatpfs vdntsffyps
      661 vsssfivskv vslpevisfa klraswaqvg ndtdpyqttg afvaqtpfng qptfsnsnti
      721 anadlvpelt ssfevgadlr ffndqlrfdv syynaltkdq iislpigiss gytqqvvngg
      781 evrskglevi vgvspiisqn fkwnstlnfs tnrstveslp qdegrltlay sriydsqnqt
      841 vflqaeeggr vgdlygtgyl knengdfilt degryipdne lqklgnynpd fmlgfnnqfn
      901 yknwnmgfll dwrqggiivs rtralgnvgg qlaetafrpe tgivpegvvn tgtddnpvye
      961 antvavsaes yyrqfydrnh eenntydasf lklrqlsigy tfnnlslfnq datlslslig
     1021 knlfaitenp hfdpeqlavq gqgfisgved msyattrsig fkagfnf
//
LOCUS       WP_099191690            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            6B07].
ACCESSION   WP_099191690
VERSION     WP_099191690.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 6B07
  ORGANISM  Maribacter sp. 6B07
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Maribacter sp. 6B07"
                     /db_xref="taxon:2045442"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112869
     Region          26..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktyhvlsv lllmlfslst yaqtstvsgt viaedglplp gatillkgtt tgastdfdgn
       61 fsiqlsnsns ktlvisyigy kteeialtgm nqtinvtlme dsnaldevvl vgssvtqsrk
      121 klgnaittvk svelvkaspa nittslqgkv pgaqitqnsg dpaggfsirl rgpstikgss
      181 eplyvvdgvi tsnlttnvtn lnvdagdaap gqnrmvdinp ndienvniln gaaaaaiygs
      241 rasngvvvit tkkggnyedg pefyfkstfs vntirkkldl nligeefetv pnsalsgrlw
      301 pifgfdpndg nalttyrnls tdkfettryd yqdeifqtgf gsdnyfsakg gndkmgymas
      361 igylsnegii kntkfdrfsa rvnfnhkvtd wmsydlglyy ansksdekpd gnvfwspins
      421 initnntfdi tqrdangnlm aventrvnpl tiietfditq dvnhfipnlh lkikptekls
      481 idqiigvdty nqkgniyipv ypyenvnpay yddgyigsae akvfnwnydi nmayntnitd
      541 klnsvttagy sfqsselsfe gtqgrgldsn neptiplqtq pidtnldiyg fflqetlswd
      601 nklfltlagr idgatnfdvd ersnfypkvs gsyvlsnepf wntesflnsa rlrasygeag
      661 nltaispyer ygsytsndyl gsstlqqntr lgneglkper tkefeigtdl sffnnrasll
      721 ftyyrqnied livsrvlaps lggstrtenv gtmrnngiel yakitpiktd dltwdlnfny
      781 ssnrnkvlst vggditiesv tgappivreg ealgvfygty yatddngeli ltgestdgsp
      841 vgvpqqergd lttntpqrda dgqptgdvlr kvigdpnpdy ilgigtdlty knfnfsmlwe
      901 avqgfdvfda dkrtrqgvgv gqlaaqeltg elprgyiagi ypieefried gsfvklrevs
      961 lgyefpslfn sslenvrlsl igrnlvsfdk ffsydpetna ggqsnllrsv nfgnvpipmt
     1021 islslsanf
//
LOCUS       WP_099215296            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            discolor].
ACCESSION   WP_099215296
VERSION     WP_099215296.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum discolor
  ORGANISM  Tenacibaculum discolor
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Tenacibaculum discolor"
                     /db_xref="taxon:361581"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117689
     Region          25..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfngilt lflalivqis faqektisgt vsdqtgplpg vtilkkgttq gtetdfdgny
       61 sikvktgdvl ifsfvgmkta ertvgasnti slimetdnll eevvvtgygt stkqaytgta
      121 tviksenlea ksvsnvsqal agevagvtvv ngsgqpgsta tirirgfgti ngnsdplyvv
      181 dgvpytnsis ninpadiest tilkdatats iygsrgangv ivittkkgrn gvsnisvdvk
      241 tgvnmrllpa yevvksqdey ielsweslkn tgeflgnadp vayananlfs gagispdynm
      301 wdianvseli dpttgkvrpg vtrkytpedw sdygfqssir teanlsmsgg ndkttyfssf
      361 gylndkgylv nsdfkrystr lnlthnptdw leananidys ygiqtangqs edsgsifwft
      421 dnipsiyplf lrdsngnive dpvfggnqyd ygtnrgfggl tnaiadanld lnqnkrhsin
      481 gnfsfkvnft dylsftakyg anyyslvdns innpfygsaa gqagslfkeq rqalsqnflk
      541 mfnfnksfgr hnitallahe snewerdrty iskntvvnlf ngldnptnyv nvgsnpegyk
      601 eetglesyfa qanysyddky flsgtirrdg ssrfaknkwa tfwsaggswi mskenfmsna
      661 sfinylklka sygimgdqag agfysgqngy didnldgdis lilraiense ltwessemfq
      721 agtefrlfnn vidgsfdyyi kntddllfdv ripissgdai lttndgsivn rgfefdltgh
      781 iinkenfkld lsvngemlqn eitempydep egrnkiidid gafgraegrs rfdyympvwa
      841 gvdpangnpl wetnyvdtnn nglfdsgeei lelyeykvrn peadikqavt sdyteasnkf
      901 igksaiptvr gafrlsakih dfdissqfay slggygydgn yasvmgndqa ggnnyhidvr
      961 nrwqkpgdit nvprlysnqn irvisrstrf ltksdylaln nvrigynlpt tylentglsa
     1021 vniwfagdnl fllsarkgfn psasligssa ryrytplstf tlgirvki
//
LOCUS       WP_099215299            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            discolor].
ACCESSION   WP_099215299
VERSION     WP_099215299.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum discolor
  ORGANISM  Tenacibaculum discolor
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Tenacibaculum discolor"
                     /db_xref="taxon:361581"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118199
     Region          25..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lflalivqis faqektisgt vsdgtgplpg vnvlikgttt gvetdfdgkf
       61 sikaktgdil vfsfvgmkti ekkvspsstf nismssdnvl devvvtslgi krakkslgya
      121 sqeikgdkvs tvklnnvvns lsgkisgvqi kannnfggss nflirgvssl tgnnqplfiv
      181 dgipisnqie nsanqkngrr gfdygnaasd inpddvesin ilkgaaasai ygsrgangvv
      241 iittkkgkeg nmkvnvssgi tlgkidrstf lkyqdkygag ygpyygstgy fedidvngdg
      301 tsdlavptyd dgsfgapldg slvyqwdafv pehpnfqtat pyvagkntpa dffetshqin
      361 nsvsisgseg kvsyrlgytn fqnkgilpns kldkntfnfn gtlkvsdrls tgananfinq
      421 dvtgrnstgy gdnlmaqfrq wwqvnvdikd qkyiydltgk nyswnhvgsv ggsplkpqyw
      481 dnpywtryqn yqsdnrnrff gnafatykin dwldltakaa vdtysevred rravgsvpte
      541 fgltvgdqgs gyqrtqinft efnydlmlnf nkdisdklsl ngvlgmnirk eknqywrast
      601 ngglanpgvy slrnsvlpvn lpverlaekq vngyyaqatl gydnklfiel tdrydvsssl
      661 psdnnsynyy avsgsfifse linadwlnyg kfragyaevg ndlpannvyd tysvidhfgs
      721 valssfdgtk knenlvpert keielgietr flsnrlglnl swykkdtenq lmpvtttaat
      781 gftsrwvnag tiqnkgfevs ldgkiiktnd fkwnttinws kndnlvkely adveniqlas
      841 fqggvtinat kgqpygtirg tgfvyddngn kvvdsngyyk aqanqiigda npdwnagitn
      901 tlsyknlsls flidiqeggd vysldlhygq gtglptytaa lndlgnpvrd pvtsgpdsgg
      961 ilnpgvtedg qpnttrapad tyagafywgn ssrnpaaltv ydasyiklre lslkynfpkt
     1021 wlqnsavsdv tislvgrnlw iidknvpfad pesglgagna qgylsgsypt vrtvglnvnl
     1081 ef
//
LOCUS       WP_099216013            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            discolor].
ACCESSION   WP_099216013
VERSION     WP_099216013.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum discolor
  ORGANISM  Tenacibaculum discolor
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Tenacibaculum discolor"
                     /db_xref="taxon:361581"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118374
     Region          26..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlhwknvic vffffgflln msaqekkitg vvsdsagplp gvnvilkgtt igtetdfdgk
       61 yslkaktgdv lvfsfvgmqv tertvgaase lnvlmkedtn ildeivvvgy gtttkqsftg
      121 takvvktedl eaksvsnvsq alagevagvn vintsgqpgt vatirirgfg svngnrdply
      181 vvdgvpfsgs insinpsdia sttvlkdasa taiygsrgan gvimittkag rsgdtsveid
      241 lktgvnfqfl prydvikspd eylelswham anrgldidpt tdavafanan lfsdgigvlp
      301 tfnyfnttdv sqiidpvtgk vrpgltrkyt pedwndyafq psirteanik msggddktky
      361 fssfgylddk gysvnsgykr yaarlnlthk paewltakan vgytlsksiq ngqsedsgsi
      421 fwyadnipsi yplfkrdang nfiedskygg nqydyrdrgf gggtnaigda mynyvgverh
      481 slngnfsfkv dlaeglefet qygaqhysri ynnvqnpfyg favkqngtly qtkssaltqn
      541 flnifrynks fgdhnisala ahetnqreye istlskntiv nlqngitdan nyinvssppt
      601 gyktktales yfgqvsynyl rkyylsgair rdgssrffqk kwgtfgsvga swvvseenfm
      661 nnvefvnflk lkasygilgd qagvdiysgq dtytignlgg eislrpnaiq npsltwetsk
      721 mfqtgleftl fndiidgsvd yyikntedli fetrlapstg naildvndgk lrnsglefdi
      781 tarlvekenf klnfgvngem ydneltqmpi dpannerkll disgaygrak grgiydfymr
      841 ewagvdsqtg nplwtqyyhd annngtvddg egigslyeyk alnpdksisk tttskysdat
      901 qkyldksiip tirgafrfna kyhnftlstl fgyslggysy dnvyaglmdn dqigannwht
      961 dirnswknpg dvtdvprlis drnvqvnsrs srfitstdyl slsnvrlgyt ipsnlieksg
     1021 vkslnfwvsg dnlfllserd gfnpttsetg ssdvyryqpl ttitfgvrak f
//
LOCUS       WP_099216015            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            discolor].
ACCESSION   WP_099216015
VERSION     WP_099216015.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum discolor
  ORGANISM  Tenacibaculum discolor
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Tenacibaculum discolor"
                     /db_xref="taxon:361581"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114373
     Region          23..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklknylllm fifmsmsila qektvtgtvt dqtgalpgvs ivikgtdrgv etdfdgkyti
       61 kvnqgdilvf sfvglktver ivrtisvlni kmeedanlld evvvvaygtt tkeaftgsas
      121 vlgvkdlatr nvtspiaaie gratgvqfts aagpgaspdi virgvgtlng dtdplfivdg
      181 iqyegelnti nqediesftv lkdasstsly gsraangvvi ittkkgkkge vkvnltaqsg
      241 vvangvrtyd qvspgqyyev mwealknssa gggdpafasa niynqlgynp fnvpndeivg
      301 vdgklnpnar viyksldwfd elqqtgfrnn ynigisagge dhtvffsasy ldeesyvvts
      361 gferitarln adfdvsesik iggsanialt eargpssagt gsivnpfsfa lgmgsvypvy
      421 vndlqgnivr defgnpvfds gegfpeynig srptnqgrha lqelllnnes dkdntygfrf
      481 ygdikllkgl nlkvtygrdi nelfereyen aiigdaqpdg rlsedrgrre venfnqvlty
      541 vksfgshnld llaghesfer sisnieglat iqaangifef anfsnivdld gatfdkaieg
      601 yffranynyd nkyylsgsvr rdgssvfdmd krwgtfysvg aswridqenf mkdvsfinrl
      661 klrasygevg nddlldsyls qarfsitsna anpaiiftdi gnanlqweti enfdvalefa
      721 lfdnfldgsi eyykknstdl lyllpiapsn glnevpvnag dmfnsgwelg ltthlfnken
      781 fkwdftlqas tfkneitklp dpfingskrw aegrsrfdyf llrtagvdpd ngdqlfymye
      841 qdengesvpv ldangnhett ndwqeteray tgdssvpdll gsilnkityk dftfdflvty
      901 gvggkvldna yssmmhsgsy grslhpdiln awkqagditn vprlengnpd lvrtqsdrfl
      961 tdasfwalkn vnigytldkk vveslkmdni rfnlsgenlf lkskrkgldp qynlagtpsg
     1021 ddfsppriis fginvsf
//
LOCUS       WP_099231263             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_099231263
VERSION     WP_099231263.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39080
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihaslpdsay eaagatirgv
       61 ddtfasdlil kvmapnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyqtdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_099236510             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. ICMP 460].
ACCESSION   WP_099236510
VERSION     WP_099236510.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. ICMP 460
  ORGANISM  Pseudomonas sp. ICMP 460
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. ICMP 460"
                     /db_xref="taxon:1718917"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38547
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqngag lnasivdsay atagatlgsa
       61 gdafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera rqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vfnqegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_099241119             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Synechococcus sp. BDU 130192].
ACCESSION   WP_099241119
VERSION     WP_099241119.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. BDU 130192
  ORGANISM  Synechococcus sp. BDU 130192
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Synechococcus sp. BDU 130192"
                     /db_xref="taxon:2042059"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40015
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavaretv agerrvaltp dqvsrlvkkg weihveagag easllpdaay eeagakvvgd
       61 rqslwkeadl lvkvavptee evallpegsm vasllnplgq peiiqkladk kitalgmeli
      121 prtsraqsmd vlssqagvag ykavllaaaa lpkffpmltt aagtirpakv fvigagvagl
      181 qaiatarrlg avveafdirp avkeevqslg akfvevqlee etataggyak evsedskkks
      241 qalisdhvat advvittaqv pgrrapllvt ddmiarmqtg svlidlageq ggncegceag
      301 revqvhgati iapinlpstv pvhasqmfak nmatllqlli pegainldfa ddildsvcvt
      361 hqgeirnqrv kdalqqmavt a
//
LOCUS       WP_099246228             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pelagimonas phthalicica].
ACCESSION   WP_099246228
VERSION     WP_099246228.1
KEYWORDS    RefSeq.
SOURCE      Pelagimonas phthalicica
  ORGANISM  Pelagimonas phthalicica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Pelagimonas.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pelagimonas phthalicica"
                     /db_xref="taxon:1037362"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55301
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpleve agenrvamtp dsarqlqklg ydcviqsgag akagfsdady aaadvevveg
       61 aealwstadi iakvripqee eldrltsdkt litffnpggn eaglekakas ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvqseefr
      241 naqlakfrel apevdivitt alipnrpapk lwtedmiaam kpgsvivdla aerggnaegt
      301 vadekvvten gvtiigytdf psrmatqsst lyatnirhmm adltpekdgq inhnmeddvi
      361 rgatvthqge itfpppppkv aaiaakpkvv epeltpeekr aaevaafkaq tkqqvtllvv
      421 gaalilgvgl vapasfmqhf ivfvlsvfvg fqviwnvshs lhtplmavtn aissiiilga
      481 llqigsgggf lvvllaaisv ffaginifgg flvtrrmlam fqks
//
LOCUS       WP_099251877             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium sp. shizuoka-1].
ACCESSION   WP_099251877
VERSION     WP_099251877.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium sp. shizuoka-1
  ORGANISM  Mycobacterium sp. shizuoka-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Mycobacterium sp. shizuoka-1"
                     /db_xref="taxon:2039281"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52358
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipresl pgetrvaatp qtvgqliklg ydvlvesgag vaasfsdeaf veagagigta
       61 aealatdivl kvnaptsaei aalrdgatli slispalkpe lveelstrpi tvlamdavpr
      121 israqsldvl ssmaniagyr avveaahafg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaagslgai vratdprpev adqvkslgge ylsiespete vsatgyakem gddykareaq
      241 lyadqsqdvd iiittalipg rpapriitad mvasmksgsv ivdmaaangg nvegtvkdqa
      301 vvtdngvtii gytdlagrlp aqasqlygtn lvnllklltp ekdgtlvldf ddvvqrsvtv
      361 vrdgettwpp ppvqvsaapa paatttpavq qtkqpmtmgr rlgitfgaaa llfllialsp
      421 aalqvhltvf alaivigyyv ighvhhalht plmsvtnais giivvgallq ighgdaivtt
      481 laavaillas inifggfavt rrmlamfsrs
//
LOCUS       WP_099262875             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodopirellula bahusiensis].
ACCESSION   WP_099262875
VERSION     WP_099262875.1
KEYWORDS    RefSeq.
SOURCE      Rhodopirellula bahusiensis
  ORGANISM  Rhodopirellula bahusiensis
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Pirellulales; Pirellulaceae; Rhodopirellula.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Rhodopirellula bahusiensis"
                     /db_xref="taxon:2014065"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40574
     Region          2..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,95,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mmqigvprer wpgearvalv pasvkkliqs gfsveietga giqsgftdda yteagavlqt
       61 drtsvlsssd ivlrvrrpei eevsslrreg ihisfldpfn ekeligemak cgvtsvsmem
      121 iprstraqkm dalssqanla gyvtviqaay hskkifpmmm tpsgtirpar vfvigagvag
      181 lqaiatakrl garvdafdtr pvvaeqvrsl gakfveidlg evgqteqgya kaltpeqiel
      241 qkegqkkvia asdvvittaq lfgrpapriv trdmllamqp gsvvvdmave tggnvegsvl
      301 neivdvegvk iigqgnlpse vsrnasemys nnltalidef wdaetkqfaf apedeivqaa
      361 vitrggeivn etiaklhs
//
LOCUS       WP_099270077             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. ICMP 561].
ACCESSION   WP_099270077
VERSION     WP_099270077.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. ICMP 561
  ORGANISM  Pseudomonas sp. ICMP 561
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. ICMP 561"
                     /db_xref="taxon:1718918"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39022
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq lgekrvaatp etikkliaqg hrvtvqsgag itasvtdnay eaagatmgaa
       61 aetlsaelll kvcapndsel aqikrgtivi gmlnpfnset iakmaeqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllgahhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recavgvggy arpmpaswmq
      241 rqaiavhera rqsdivitta lipgrkapvl lsaetvaemk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tlvgytnlpa lvaadasaly arnlldfmkl lfdkdgqlhi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_099266966             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_099266966
VERSION     WP_099266966.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39002
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lhasfpdsay eaagaviddt
       61 hqtyaaelil kvvapdeeal sliksgsvvi gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllashhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_099273888             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limimaricola cinnabarinus].
ACCESSION   WP_099273888
VERSION     WP_099273888.1
KEYWORDS    RefSeq.
SOURCE      Limimaricola cinnabarinus
  ORGANISM  Limimaricola cinnabarinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Limimaricola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Limimaricola cinnabarinus"
                     /db_xref="taxon:1125964"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55152
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigapkeih dgearvamtp asardlqklg hdclietgag vaagftdaay eaagvtivpd
       61 aetlwaeaei vtkvrpplde elgrlregqt lisffypgqn aeslgrakda gatviamdmv
      121 prisraqkmd alssmaniag yravieaggs fgrfftgqvt aagkvpparv lvigagvagl
      181 aaigtatslg avtlafdvrp evaeqiesmg aefvyldfed sqdssatggy aapsspefre
      241 kqlakfrela pdidivista lipgrdapvl wtadmveamk pgsvivdlaa erggnceltv
      301 adekvvsdng vtiigytdfp srmatqsstl yatnirhmlt dltpakdgvv vhdmeddvir
      361 gatathegei typppkpkta aiaavpkkdk preltaeekr gqevaafrkq trdqvgllaa
      421 galvmlliga vapesfmshf ivfalacfvg fqviwgvshs lhtplmavtn aisgivilga
      481 llqigsgnwl vvilsfvsvl iasinivggf lvtrrmlamf rks
//
LOCUS       WP_099289892            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099289892
VERSION     WP_099289892.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124102
     Region          63..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkterkmy srksrakvkt rsprevtaai ylkmlllpll cclsllanav pardstvvke
       61 niikgrvmde kgqpmpgvtv lldstrlgvt tdtggnftlk lprekgvlvf sfigfktvka
      121 kfeagkllti rmkeetssld evtviaygtq rrrevvgams tvsgedikdi pspsianllq
      181 grvsgmnvtn mtgapggggt sinvrgynsf diageqrfsn plwvidgvpm qsftspvtgt
      241 ntlaeidpnd iesiqvlkda asaaiygsra angvmlvttk sgrlnqraki svnfshtwsf
      301 dpslpeltgg naerklrlea lrdfqqayfd vstntykyvn syresynenm hynyfwnkgd
      361 gagiaayqds lnpfynnstn ffkyyfrtak vlnanlqlsg gtsnvaynvg lgyydesgvl
      421 rntgfdrvnl lanffikplp kvesnvrfyl artgrkrasr ltaytgftsg eeleqipeel
      481 lttstilpge gtpafdemik rfntikedne syrvrtsldl sleivkglkl kssvaldftq
      541 qnqnlflpsg ldeygesyss gqvernltll nedlltyrht fvekhtvdvl lglsvqkder
      601 nsigtwgkds psdlihyisw fgnvynvnen ralkdgttgr evstsvgvfg rlnynylery
      661 flavtlrrda sskfgenvrw gtfpsyavaw tfseepfmdw skgildhgkl rvsygksgkq
      721 fdqpyiaqgs fspgdpylgn ptihpdlsrg lsnkyltwee tgqydfgldl dffdhrfgvv
      781 vdyyyrytdk llypvmlpgn ysafnrqwrn ayaisnegie levkwnairs eklnwnisfn
      841 iarnwnrlek senkrdflte dnttnlniig kalnglhvlk tggiynddkd vprmfingkd
      901 tplasngntq hyragdrvvy dvngdgvvns ddrvyagapa piaqggiits lewkgfdlnv
      961 lfnfvisrhi lnaargasvg tiigltpdds vtpvyvdlnn vsfwqkpgdk tdfpmnrleg
     1021 glgsfnsytt anvedvsyik lktfsigytl perwkkkvgf glrvfvsgen lftvtnysga
     1081 dpesvnimtg vdnlgnypln rkltlgitai f
//
LOCUS       WP_099290389            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099290389
VERSION     WP_099290389.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115667
     Region          44..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maytrlciiv icvlacgkvt fsaekyrvhl fhvtdtiiag derivvhgkv ldtthlpmvg
       61 vhvlekgttn gvvtdwegnf smkvrrtgtl ivsfvgyhtq fvavegkkdi ritleqesvl
      121 lddvivtalg irkkenslsy aasrvnrnel irvkdpnmiv tlmgkiagmq vnrsssgmgg
      181 svkvvmrgnr svagnnqply vidgipmlne sseqpstsig gtadagnrda gdgisnlnpe
      241 diesisilkg apaaalygtq aangvilitt khgeagkqev sfsssvlidk ammlpklqnh
      301 ygvsdevesw gerkdintgn pissffktgv taihsltfst gnehtqtyfs yantegkgim
      361 ethrlskhni nlrecatfyd gllkidgsvn llkqtvknrp vpggfymnpl vglyrfprgm
      421 diteyknhfe vwneerrlnv qnwhaptedf eqnpywvler ikgqdqrtrv iasiamrlil
      481 sahfslqarg svdylndkfr qkyyastapa lagsngryid asheqtltyg dvlgtykrkf
      541 enfsldislg vsinnnktne lrydsktasl kyanvfnian inmttsayia eqidatrqmq
      601 slfataqlgf rdylfldisa rndwsstlay tsresigffy psvgfswlid rtfslpewit
      661 ggkirgawsm vgndiplyit hpvshvlagg giqasdaapf eemkpeknva feagtewrlf
      721 ndrlrvdltc yntvtknqff klaakdgdty ayryvnagei rntgveielk gtpfedtkvk
      781 wetginyasn knkvlrlhee lpvfqygpyg fsssyamklk eggsfgdiyg kafkrddngk
      841 ilyetegdlk glprvegdgn tvrvgnanpn ftlgwtntfs wrnfmmtfli dgrvggkvls
      901 qtradmdlyg vtratgdard rgyvmleger itnvkgfyks ivggragvte yymydatnfr
      961 lrefslgysf pkqwlesvrv lrdihlafta rnlffiyrka pfdpdlilst gndnqaievy
     1021 gmpttrgmgf slrvtf
//
LOCUS       WP_099290450            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099290450
VERSION     WP_099290450.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115128
     Region          52..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktydrkvf krkllprkma viviirlfmv lllgfpllan aggrdstgve skevkgkvtd
       61 dkgvplpgvs vrlagtlvgt atdvdgkfkl llpadtatlv vsfigmktvs vklprlksge
      121 vrkelsivmq adeveladvv vtgiftrkke sftgsastys aaelktmgtq nvlqslktld
      181 pafaiiednq fgsdpnrlpn meirgkssml glrdeldadp nqplfildgf estlaaindl
      241 dinrvasiti lkdaastaiy gskaangviv vetvkpeagk lqvsyngnmn lsmpdlssyn
      301 lmnareklef erlagryepa swsavsevem nelyneklra iesgvdtywl aeplrvgvnq
      361 khslyvqgge gnflfglgag yngisgvmek sdrsvisgni dliyrvskfq fsnkfsltst
      421 dyknpivafs eyaaanpyyk kyndsgtvdk wlekndffka snplwnasqn srdegknlsl
      481 snyfmaeyfp taewrvrarl gitygnddte kfysrndtry edveaikkge yrsantrtnq
      541 vegelsvtya kllgkhrvnl vaggnvfsnk sltqgysaqg fpegdfsyps fsngypengt
      601 ptyyesvsrs vngyfntgys fddrylmdfs lrasgssvfg tsrkynttws vglgwnlhke
      661 kfimnhvgwi dllklrasig npgnqsfdsa qslltysfqy gamnyfglga vlsqvgnpdl
      721 ewqitvdkni gldvtlfnkr fsltadyyyk vtdpllikvs tplssgtpty mtnageqvsq
      781 gltasvsyyi fqnfaerfsw miranvrtqk skidkignkl stlnasgkga ntvryydgad
      841 pddiwavksa gidpsngkel fyakdgsyty dfsyddevic gntrpdvegv lgtslnwkgl
      901 svslnfryqm gadvfnealy skvenisrsa lnrnqdkral yerwqevgdm vrfkdiasae
      961 stpmssrfvq kenvltlesv yvgyefydgw ikklglsslk iqasardvfr astirsergi
     1021 aypfarsmea glsfnf
//
LOCUS       WP_099290602            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099290602
VERSION     WP_099290602.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121813
     Region          64..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          134..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mghqsifctr gqirlfgvsr ivlfacflll tsfvqaqerk nitvdfkeea lgevlkklek
       61 lspykilfty dhvqgykvta slknvtilda lkkvlegkpf tyseitdgky itvkyqsdkk
      121 nldgkvvtvk gvvldknkep lpgvtviikg tstgvatnad gmyeivvpts setvlqfsci
      181 gmkseevkvg kektinvtms eevnevdevv vngiytaskn sytgavstvr sedilavsqt
      241 nlfkaltvlv pgmrivdnne qgsnpnyipe iiirgttsik tsddqyglns pliivdgvet
      301 tleglydmdv fdiervdvlk dasataiygd kaangvivvt rkrvadsklr mrynfvpdiq
      361 fpdvssyslc nprqkleler rwgiyegmng ekemeynrkl klvnsgvytd waaipvriaw
      421 shshslsvtg rgggldysvt arygdahgvm kgdfrrnygi gfyfsyifrn kltvtfrsdi
      481 rktdsknspy gsysqwvvln pydcpydeyg elipklsfga vnpmynastg sfskskskni
      541 snnltfrwdv mkgmivnlsa nlslsdnrsd dyisslhtss mvgnesantk gryvlsgaeg
      601 tswsmtgsvs yslpfddkgs ilttnvgsti tqsnsssfgm egrgflkpvm ndinfartyp
      661 sggkprgsnd ysasvgvfan lnfifrnryf ldgsyrssgs svlggnnqwa pywsfgigwn
      721 ahnesfikal swistfrfrg sigfvgsgnf ggnmaqtiyt ygdayllglg aipsqlgnpd
      781 lkaqrtlnmn ggvvldileg wfqvnldfyr qrtkdallpi glplstgaat vqanlgesln
      841 wgmeisvssl lvrttdwllr ltvnthhten klmkisnala rqneanmrdk gvapklqlre
      901 gesmdaiyav dswginpang levflkkdtk eptytynved mvalgdtkpw fegssslsaa
      961 wrdisvgmaf sytfggyiyn straakveni ditknvdvra ytdrwvkpgd vvaypkgeye
     1021 qqrfvksarf vekknevyls svsisynlpq twvrgiglkr ltvgvtfsdv lrlstvkyer
     1081 gtsypfmrgf nfmisptf
//
LOCUS       WP_099290791            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099290791
VERSION     WP_099290791.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125413
     Region          25..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilllmal fcplwllaqn egdyrtikgv vmdsvtnetl igatvvidpd apesknlgpk
       61 gtitdidgnf elkvpkavny vvisfigykp lkldiskkte fkvllqpdqe qleevvvtgy
      121 qqiekrkats aiqtvkmddi krigvasidq llegqvagmt siptngapga pnkmrirstv
      181 sltgstdplw vldgmilegn dipanfsdkd nidnlyntsi agvnpadied itilkdaaat
      241 aiygaraang vivvttksgk kgkmrinasg svfytlrpdl gklnlmnase kvdfelglaa
      301 qknltyrsey ggvarilnky gqlevlqngg fnaistdaqn einklrssgv dwedevyrna
      361 lnqqynlsis gggelanyyf sggyyneegt trgtgferyn mtmktnfsll enlnvgvslf
      421 ltdskrksyv tdteaftnps nytrmvnpyl dvkdengdyi ydpdildndg rnmqfnfiee
      481 mdntsyslkn rsikpmitvd ykvtswlklf tqfsmqlens ktekiankns yfvrkykeks
      541 kytyrpsdgs psetryflpd ggviqywdnd lsqyqwklqg dfakyfgelh svnvmtglem
      601 rgskvtnvht kgfgydpnsl ttetlvipdg tdyqndanfk qysksfnedr flsyymtasy
      661 tydnrytmfg slrydgsnmf gverkykylp iwsisaawna dresflqnad wltnlklrvs
      721 ygiqgnvdkn tsplvvgswg ntsvlpegse psigvttppn pylrwektkn wnvgvdmgvl
      781 nnritfsvda yhrvssdlig tralpgengf dyasmnwakv tnkgiefsls tvnvktkdfr
      841 wtldfniahn kskinrieip dnsylpsreg ysigalfalk tagldengip mfwkngqkvs
      901 fndfygleln ydlfgdatlt snlsnqeyrd lftyigtsep kftgglinrf yyknfdltis
      961 gsfildqtvq espfydpsqt spgqnyskri fdvwsssnpn gkypallsst ledgslnmah
     1021 qwisvkdpgn sfrnydiwfk qmsyfrvnsi rlgytlpndi akklrlasmr vsletrnpfv
     1081 igtsykgyfd petygsiyaq plaktfscgl dltf
//
LOCUS       WP_099291292            1127 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Butyricimonas].
ACCESSION   WP_099291292
VERSION     WP_099291292.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas
  ORGANISM  Butyricimonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae.
REFERENCE   1  (residues 1 to 1127)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1127)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1127)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1127
                     /organism="Butyricimonas"
                     /db_xref="taxon:574697"
     Protein         1..1127
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126085
     Region          130..1119
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknrfdrqg ipvnlrkmfs gmklrvvfil lltftvssai laqsktvtln vkseplsdvl
       61 iyikdatgvq iifnenqlek vmcgpvslkd vsvkeaidav lkgkgffcev ldgvyvikre
      121 tkkeevkklt itgkvvdvqn nplpgvtvri kgttlgvatd vdgnysitlt agqekpvlvf
      181 sfvgmtskev vyadkdvinv tledetseid evvvtgifkk akesytgavs sitseqlkmy
      241 kgqnvlqtlk nidaslnfmv nnavgsnpna ipqinirgns slpmsvqeyn esasnavntp
      301 liimdgfeit leklmdyndd eiesinilkd aaataiygsr gsngvivvit kqpeagklri
      361 naeigmdiea pdlssydlln aaeklqlekm sglyesslpg ndvryteryn krlkavlagv
      421 dtdwlskplh tgvgshynlr meggseqfrw sgslayknvv gamkgssrrn fngsitlmyt
      481 idnlifknyt sygmnrgces rygsfstyae qqpydapyde ngnlvryfdg frysdldrqn
      541 plydaslnsf dktgyqsltn nfsiewnime glmlrgqlgi sstdnssdyf lpaehsyftt
      601 gdkkaeyatd egffrrglyr ygtgkeysys gnvtmtynrt faekhllsvg idwslaetqs
      661 rsysfelegf ssedmsflgn arqymkdgip nglktstrrf gltgnvnyiy dgryyvdlay
      721 rvdgsstfgs dkkyapfwss gigwnlhnes flqghpvitm lrlkgsyget gsqqgsstga
      781 sttykystdn kymnwngail qgwgnprltw qktnelnvgm evglwagrlk gelnvytkkt
      841 anllssmdlp lsmgyssyia nvgevknngw elalsgyair dyerevtlmf sgqlvynknr
      901 itklseaika qnelylqedv dvsnlfyegr pqnaiyavrs lgidpstgne ifldkdgnit
      961 dtwkpsdkvy lgakeqkyrg ngsilfmwkg ltvnvacsyy wggkaynetl lnkvevtknt
     1021 ltsqnvdarv lkarwfqagd vtffkqlsnt qtratsrfvm ndnvfeissv giqyrwdspw
     1081 vqkytragsi tfgvnmsdil hlssikmerg tsypyarniq gyikflf
//
LOCUS       WP_099291736            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099291736
VERSION     WP_099291736.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123622
     Region          53..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msknydsfsr grgcvmfllf flilpgwgvl nattipkiih tesqqvkdsl ihgvvvdekn
       61 vpmpgvtvrv egtkvgtatd nkgefklrlp gkggvliftf igfkekkvay kagaprmvvv
      121 leedveside vvvvgygttt rrkatgavsv ikaeelegip tsnianllqg rvagmdvtnm
      181 sgapgsggta itirgynsld veqgrrfsnp lwvvdgvpln sftspvtgtn llsdlnpdmi
      241 esiqilkdas saaiygsraa ngviivttkk gsknqkatfs vnasqtwsil pqlptvtigs
      301 aerrfrleqq rrsmvayrdp etgrykypts wkevyevggd akldgfweph rnliakkgni
      361 yqdslnafya hstnffpmyy rtgrvtnani qayggqermt ygiglgyyde egivkgtgyn
      421 ridlnsqmnv tpverfnvdl rfnaslagrm rgvrsgqlts vqnvetvpgd pyqlntflpg
      481 egtvvwdeii nqyqgihern rsvrlrsnfk lgldliegln isaslaadys ierrnyfapa
      541 sldvngwsns lgetginlmv lnenlisynk iigeshsisa iggfsyqydq ieynggyarn
      601 spsdkieyap gglpgltilg sgdfqqtval knyisdmeek tllswfarle ynylqkyfls
      661 asirrdgsst fgknnkwgtf paiaagwtft eenfmesfkn wfnfgklrvs wgmsgmhfyq
      721 nylalgimav dnssylgnpv itpvwndgly nqdlswekts qydfgldlnf lnyrlgvtld
      781 yyyrytedll mpvplpgnyn gfqnqwrnta aisnegielm veykffdrpd flwrmsvnga
      841 rnwnrfeksy dghdldnkii gkplnqmrvl rtegfindqa evpvswktdg sngpmnvgsg
      901 ymqpgdykiv dasgdghidg ndlvyigsal psisggivne lkwkgfdvnm llsyqlgrhi
      961 lypyavqsim mnndyyalvf dlekttfwek ngdradyarl qpgildnhvy dylldrnvsk
     1021 vnwlklktlt vgytlpsrwt rcwfidqlrf fvsgenlltw tnyigmdpet vdittgidgv
     1081 ltgngiqgsy plarkftigv tfkf
//
LOCUS       WP_099291797            1199 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Butyricimonas].
ACCESSION   WP_099291797
VERSION     WP_099291797.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas
  ORGANISM  Butyricimonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae.
REFERENCE   1  (residues 1 to 1199)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1199)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1199)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1199
                     /organism="Butyricimonas"
                     /db_xref="taxon:574697"
     Protein         1..1199
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134648
     Region          128..1198
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkpihcsl kerifrndrf lrqflallsl lvignvgitv aqavpkftvn fkdasltevl
       61 dylgknsdyt ftynsenvkn etvkitesfk datleqvltk clektrfdfn vvenhviikn
      121 rtvsmnefrv kgkvvdmkgq plpgvtimld gtkvgfvsdn qgafnavipv ekgvlslsfi
      181 gfktkkvnfe sgkelvvkme edvagldevt vvaygerkkr emigsvssvk gdeikeipss
      241 slesllqgrm agveitnmsg apggggaiva irgynslidq nslslgdyge plyvvdgipm
      301 qgftspvtgt ntlsaidpat iesievlkda asaaiygsra grgvilittk kgregeakfs
      361 anvsyswsql pstpeqtagr avrdyaltal rnqtrpyqdp vtgiykfphn lqeayglysy
      421 gavydgfwhk slvgiqegqn pvfsviqdsl npfynnatnw fkyafrtgkv lnaniqasgg
      481 sartqyliga gvydekgigy gsdftrvnll tnlnvqpvrn flvdsrislt ymsrqrgdat
      541 ggmksaqkie kmpvdptkts sflpgggwie eklletineq seknesfdlk aslvlnydil
      601 pglrlslngs asfslatlnl flprkldkyg lntskseier rlsvlnenll sykrsfnesh
      661 nidllaglsf qkntgnfnfg qgrggasdki hyiyegfpel paanmtvgdg dkilqharsd
      721 feetsmvswf arvaynykqr ylteftfrqd gssvfgdknk yanfpavalg wafseekfld
      781 wawwlsygkf rvsygksgei fpdayrahgl mipggeflgr plmniddnal knggminrel
      841 kwvkhdqydf gldmdffdyr lkfkidyyyr wstgviansk ipktiylyen rwvnandisn
      901 egleievvgd iirgenwswr trfnasrnwn rlkktfdgkd vgltngiphh mlgkplynlw
      961 afvhgkvyeh eseiptyytp ngekytmyla dnkypfgvgm kevvdmngdg iadyrdkrnm
     1021 gqtlpkiygg wahevrwknw dlnvllnysf grkiacmyrs dsmdpkevig gsnlyvdldd
     1081 vrfwekpgda aikgiypqls yfdatmlqfs liggvlssqv etvnyvklkq ltigynvpre
     1141 wcrkikldnv rvfftgenlf titgysgedp evvsiftgid nyrayplark ltlgltvnf
//
LOCUS       WP_099291838            1096 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099291838
VERSION     WP_099291838.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1096
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123345
     Region          99..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqnvfgqeqe ykntkitmnv kdmklnqvld tlasaakvrf fynhsqidvd krvsfdvkdr
       61 tldyvlllvl gdqsveveyq mnrvvvlkyk ksaqgvvvfk irgtvidaat ketlpgasii
      121 lkenkamgvv tdidgkffie vpegtsallv sfvgyeeeiv pvtgnmenvv ikltekqtel
      181 edvvvtgmap rkvesfsggy vtvkgselkk lspnnllkal qvfdpsfril ennragsnpn
      241 ampefrlrgd vqlgnggvda nsmemmmgdy sqrpnmplfv ldgfettlqr ivdldperve
      301 sitilkdaaa taiygskasn gvvvvetkkp lpgalnisys mnmgisvpdl sdynlmnake
      361 kleyerqagv ftttsqlnyy nyykaeiqrg vdtywlsepl rtavthrhtl smeggdealr
      421 ynlslnysre pgvmkesgrn tmglglslqy rrkkwniqnq ltlsnvrgdn spygsfslyt
      481 rlnpyyrktd engrytsfld qkilpgeggg tvtvvnplyn tlfkykdfte nfnvvdnfti
      541 ecaiqenfrv smgasitkgi srmekfksmn htdfipqedl tkkgsyeknt gdnvawsvna
      601 svnynytkdk hllslfarwn vdesknnsvn lqafgfpndn mtdflfayem ddrvrgsest
      661 srtvgligqv symydmrfav dfsvrgdlss qfgantgmap fwaagarwni hrekwfqntl
      721 isnlvvrgsy gvtgsqsysp yqaketytyd dllfpypssd ilgaqlkgig npdlgwsttk
      781 nrslaleigl wnsrvnasfs yynnytdell ldyniapstg fasktmnvga venegydiqf
      841 svmpiqdyer qiqwsvsang shnrnvikki snemkamnqk nlekkdgspe aiyeegkstt
      901 qlfvvpslgi dpatgqevfl trngektyiw dpldkiavgd qepklrgais saftyknwsv
      961 alactyelga wwynqtlvdk ienssaaynv drralssrws penrnaryks msivsqqtgm
     1021 ssrfvqkrne lsftslsvgy rfdpknfkfl qacriasvsl natmedlgri ssiktergld
     1081 ypfarmfnvs lsvlfn
//
LOCUS       WP_099291846            1161 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099291846
VERSION     WP_099291846.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1161
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130568
     Region          106..1160
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mritlllvll fgfyaeassq kvtlkvknmd lytvllqlkn qsgvrmlyda dytkqikcnd
       61 atfqeediav vlkkllkdtp ltfnvvngvf vinkaqekee kkksvtlkgr vqdekrepmp
      121 gvtiqlvgts igtvtdtkgr faitlplekg iiefsfigyv kqkvvfskdm andslqitlq
      181 eelvtlnevv vtgyqtlkkq smagstshvk agdltmlpgh tleqmlqgai pgmmvmnqsg
      241 ltgsrqkirv rgtstllgda eplwvvdgii qedplpfkas eltnigntdm indfvggais
      301 wlnpndiqdv tvlkdasata iygvkaangv ivittkkgek grmsitysgs fststkfsyd
      361 kmnlmnsker vdfsreiyet gglfeeqalg ylhyamkykl reisleefsk evrkmetant
      421 nwfdllfrnp fshshsisis ggnnqasfra sfgysdannt aigngrtsyt gnlstsatfw
      481 erlvtsftls gsmnkttafg itdpysyask tsraifcyde ngdyvfypik gykynylfeq
      541 rnsgnantvy sinsslnirf siwkdfvfqt lfgfnlssth geiyftehtn risqirgyey
      601 haidaatnal rqdgvlphgg eltqkenrnq nytwrnmlew nkninkhnfs lmvgqevrgt
      661 reegsswthy gylpdhgksf aivpptsyvg gstpnsyavv yptisdkkvn ylsffasgsy
      721 mfderyalna sirmdassrf gndrdaryqp vwsvglrwni trehwlenqd ilndvslrfs
      781 ygfqgnvaen vgpdlimtip ssgsidnkig kyvynikslp apgltweknk tinlgidfsi
      841 lhnkvnctfd yyrkrtedmi vnrivpyeng vtnmiinggn mvnsgwdmav slvpirtqdf
      901 vwslsttfss nnnkidtkle nkpdwktaas gklnkkgyav ssfwafkyag lnpgngapqf
      961 dfltekdnal vendatqymv yagkldpdfs tginmnfryk klslstafyl sfgnkrflnp
     1021 lyenttkapn endnltkemv krwkkqgdev ftdvpaipnn srnasispfg rltgqmypye
     1081 lynystarvv nasflrcsni tlaytmpekl iskfaqsmnf sftvtnpfri vskdfkgidp
     1141 evatgnqplt sdftlnlnis f
//
LOCUS       WP_099292118             929 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099292118
VERSION     WP_099292118.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 929)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 929)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 929)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..929
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..929
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104956
     Region          65..928
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikllrvker kypgifrsna svrglllgmi llgstavtma qvdsgekvqn srekgktwsa
       61 gdyfsgeqlr rfhptdllka lqvmepslrv agdaelygsd pnyvpktidi rgkksilgsd
      121 meenvlplim vdgyeisidr ladfdihrvk svsvikdaaa mavygirggn gvivittnet
      181 rpgtlrvryh fdggvdmadl ssydlmnakq klalekemgl ydgneelyrt rlkngntnwl
      241 kvplqkpfrh khrleveggd nsmlyqvyll atpgnkgimk gskrdmyavg trlnyshrgi
      301 svsdelrvdv iyskdspygi fmnymainpy yrkysedgva eaelgsgtfn pqpspfyett
      361 lsgfsknrtt rvinnlqaaw qiteeltlsg hfafskdfnk qdqfvspksy rfmglpieds
      421 efageyavrr nnttvyeekl mlnyrnefgh hrlntllgih syaskvysdn ytgvglasdh
      481 mnyisfaqky afdrkpggre frdrlfggya visydyadry madavlrvek ssrlapkkqv
      541 atswgingrw nihreemfag cellnrltlq agvgvvpgyq fdynqvnpvy aydidnpyln
      601 giknslglvt lsqinnynpr lkwrsdrnfy vgvqlsmwer idiqaryynt lskdlvvlkk
      661 sdvvtgfdek wvndgeirns glefslnagi wkdeeglsln llvngimnkn elvtvpdyyr
      721 ekynqayaet grqltegkav naiyavksdg vdpatgkeiy vgtngktgvw nvdditcqgd
      781 ptpklagsfg lsgnygnwdf ncmfryslgg kvynqeaaef vdmadlyang pvqmrnkwqk
      841 agqntkwqgf entltlptsr fvetrnvlsl sslhvgyrfd talaekmymk slrlgvscnd
      901 lfysssakme rgliypfarg ftfslqatf
//
LOCUS       WP_099292592            1130 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099292592
VERSION     WP_099292592.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1130
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128653
     Region          125..1128
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkksnllm mkrktgivlm lvlflqsfnt gicraqsade prltvefket pftgvldyik
       61 rhtkyeplyn neemkripav thsfksvpls dvlraclegt eytfsfyqnm iviqkrqrtl
      121 epvsvrgkvl dergdilpga tvlvkgttig gstsnqgifa fnlpkmdtiy lvvsfvgyes
      181 qevavadfsk etvvrmkpdt reveevvvtg ygnvrktsft gnfvtvkree llnvsktnvi
      241 kalevfdpsf riktnnrwgs dpnalpemqi rgqssigvkd ldrnslsksa lennpnlpif
      301 ildnfettiq kvydmdpnri esvtilkdaa atalygsras ngvvvittva prsgevrvty
      361 nmvgtvtmpn lydynlmnak eklaaevatg mydisdkelw vglftieeyq aklknviegv
      421 dtywlskplr sefnhkhsly veggneefry gidlsynnen gvmkgsyrdr idvgfsmlyt
      481 tpkvqvtnqi tygvtkekes pygdfstytk llpyekykde ngkmlrrlnw srvldfepin
      541 plyeaelgsy dkgktntitd nlsvnwyikp tlwvraeasv tqsvnkrekf idplsvhnnl
      601 qygddrsyvg sltksdrest swegkftisy nesilnhnin lsggaevrts knnsssgtyk
      661 gfqsaefssp efardmpnkp gfsetqtrlf gvyfrlnysy rdiyladatv rfdgssefgs
      721 dkryapflsa gvglnvhkyp fmerfgfinh lkvrgsfgqt gnvnfapyaa vpthvidtde
      781 wyvsgpatsl mstrgnrdlk wektnkldmg felgvlndlf yleftwynev tnglindasl
      841 psstgfttyl tnvgkvdnkg felhlraqll rtsdwyvavy anmahnknvi kkisdsqkay
      901 ndavneyynq tiesiwnddn pnlnrvmtky eegeslsaky glkslgidpa ngqelyvyrd
      961 gtvgyewrat emrnigdelp wgtgafgvnl rwknftfgts ftykfggdfy netliekven
     1021 aqiqtfnvdr ramaqrwqkf gdvvmykdik derqttqpts rfmqrenile wnsmnigyei
     1081 gseklkrfgi enirvevgtn dlwrlstvka erglsypyan svnfsvnvrf
//
LOCUS       WP_099292908            1161 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099292908
VERSION     WP_099292908.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1161
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130092
     Region          61..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          122..1160
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkrrsvyl rreqgwrkmt lwmffmlwgf lgfsqenkvs fkfvdqelss vlkelekadv
       61 ykfmfnyddv kgkkvtlevk dkkvleildl vlkdlpftyr tdgvmviirp kvadvsakkh
      121 ilkgkvvdtk gepmvgvtvr ldsttvgtas aadgtftlai dkpvgnlifs figfsakkva
      181 vtsgkevvvk meeevsdldq vtviaygsrk krelitsvas ikaddikeip aasletllqg
      241 rmagvgvniq sgspggggtn vavrgynslw ldeagggdgs plyvidgvpv hsftspvtgt
      301 ntiaeidpst iesvevlkda asaaiygsra angvilittk kgragegkfs vnlsysasvl
      361 pkaptqlggr eerlyhmavm raqrnayevk gkgyykypts yeeaanneai ydafwnsglg
      421 vgtksirmvq dslnpffnns tnwykyifrt gkilnaniqt sggtekmtym vgagyyketg
      481 impgsdfsrv nlltnlsfnp vkkltvdsrf ylaytdrsrg atsgdafkye sftvdpnyts
      541 slllkggave ekmlqmlngq venntsyrlr anlqlryeil kglsvstsla ldytqanqnq
      601 ftpsyldpnn nneskssgei ardmllsnen llsyvftlde vhnfdllfgl aydgskkwsn
      661 sghglrgpsd rieyvgsgfq dliydprvdd yralkdygsd fsetamvsyf grlaynydkk
      721 ylleatvrrd gssvfgadvr watfpslavg gafsterfmk wawwlnygki raswgrsgsq
      781 faipylaqgl mspgtifdgv qgmqpegvin rklkweesdq ydfgldmdff nyrlnltidy
      841 yykytralin keslpgdmyg fngvqwrntm aisnegleld akidilrdte vkwrtrfnis
      901 rnwnrfrksy sgrdfydkvi gkplsgiylf kdlgmiesda dvpyifdqsg kkqmlspegd
      961 eeyfftkgmr riadidgdgq iteddlvysg ttlpqayggl vneikwknfd vnilltytlg
     1021 rkmvnqfkys tlqgrlgvyp vfadvslsdf wqyagdgsky qtlglygnst linitgqtta
     1081 slenvhycrl kqltigynlp krimkklwld girifvtged lfllsnysgl dpevanigtg
     1141 fddgrtypla rkwtfgltvn f
//
LOCUS       WP_099294252            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099294252
VERSION     WP_099294252.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120294
     Region          48..98
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          110..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklclvlsll avlsvsargv aqnvklsmek ksvsllnvln elgeksgyef fynddevtgv
       61 kvsvsakdat vqeildqvlk gtsltyhivd dvfiitpkka tdekknvwri sgvvkdnkge
      121 llpgvtvvik gtqtgtatda ngkfkiefld aekksvtlvf sfigmvtqer eikeyvkegl
      181 eivmqpdeee leeviitgmg nkakssftgs atvvsrkqlm svgtksllqs laafvpglqi
      241 vknndmgsdp ntrpeilirg rssfegssnv ptfivdgaev dldyvfdmdm ndvetvtvlk
      301 dasasalygs kaakgvvvit trplragklr vsysgtlrts ipdvrdydll naaekleyer
      361 lakvyddsgk sqyekdavyn ekfkrvregv ntdwlskplr nsvsqnhnln iaggdeyiry
      421 tlgarygseq gvmkeskrdr yslnfrlsyn kqdkvyvsnt ttitsvnsee spygtfnkyv
      481 elnpydrayn ldgtlnkvls fgvsnplfea tlgsydrseq fylnnvldlr vevlpgfrve
      541 gffslnkskd dtekftspes yefrnkdase sgrievsnnk amtyegrvtl synkmfgtgt
      601 llnamgggnv qsserngngy agvglysdkl ghpafatryp egatpsgsqd lersmglfln
      661 anviyddryf adasiryegs skfgedqrft pfwslglgwn ihkekflnms stdriklrgs
      721 lgytgnasfs pyqamttyky dagldydkgi gaipmaignp dlkweralty nvgldvvlfk
      781 nrldftleyy skttdnllld vakapsvgtt takenmgkll ntgiefqtrv vavsnkswnw
      841 slslnmqhne nkikkisnal ekmneelnta egtllpppvy vegeslsavk avksggidpa
      901 tgqevfidrf gvptfiynyw dkrtygdsdp tvsgtlgtyl tfkgfalnml fnyelgatvy
      961 nqtlvtrveg anprrnadkr vfqsrwkevg drvkykniad qttpditsrf vrdeyminmq
     1021 slslsydftp eicqklylsr lrveflmndv frastikqer gfsypfarsf efslsaaf
//
LOCUS       WP_099294304            1192 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp. Marseille-P3923].
ACCESSION   WP_099294304
VERSION     WP_099294304.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp. Marseille-P3923
  ORGANISM  Butyricimonas sp. Marseille-P3923
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1192)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1192)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1192)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1192
                     /organism="Butyricimonas sp. Marseille-P3923"
                     /db_xref="taxon:1987504"
     Protein         1..1192
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134444
     Region          121..1191
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknrefrsl rdrillkkra clslflgvif ffpvyaqdkq plvsvsverq tvieifklle
       61 rqvvykfmyh dadilklgrk slnlkkvplr valdscvrgs qiayefvgdq ivfkreaekt
      121 rlvkgtiksv qgdllpgvtv llkgtstgvt tdskgqfils vppsnsivlq fsfvgmkgke
      181 vkvtnnqpls vvleednekl devvvtgyqn vrsrdmvgsy skvnaadimm paytsidqml
      241 qgkiaglmvm ntssrmgtsp eirirgtsti lgnkaplwvv dgviqpdpip fdrndamted
      301 lknivgsqis wlnpadieti tvlkdasata iygskasngv ivittkrgfn esrsikysmn
      361 lsfrrrptyg lfnlmdsker iqftrevfda ggsydasypp ikqldtyegl yrmymdqdis
      421 kddfvtelak lettntdwld lltrnavshn hnlsisggse kitysasvsy annkgvelkn
      481 sqeqmsgrln lgvklhpklr vdltligsld kvngygpgvn pmsyatstsr airayddegd
      541 rlfyqlpasy qyrtgitplk ynilneidnt ysrskttrvn atidlnwdil swlkyqlvag
      601 vskdeknges yagersyyva gkyrgydyga aikgdpdyaa avlpfggeff tsnasthnyn
      661 vqnkllvdkt fkeehrlnvm lgfevrstan kslqnkvwgy vpdrgkkvis ptlpsefvsq
      721 spsrleefsv ykdlysgawr httgtdnfls yfatlvysyr dryvlnasir ndesnrfgqd
      781 vnkrfdpsys vglswdvsee elvrrclpwl dqlrfrvsyg iqgnvvetis pdiivaqqgv
      841 vepfatygvs iaslpnpdls westktwnvg mdlqflkwvt mcleyyrras daiiyqpipk
      901 eygvpdmaln ggrvynhgve ftmnitpvrt kdfgwtigln tsknwnkakr idsgmtsvda
      961 flngvsdrvl kkgyplsafw sfsfkgldpe ngmpqfnlmd veagndidpt sflvysgese
     1021 pyftgglntr lrfkdftigg dfslllgakr rlpnlypnqe rlpspyanmd kdllkrwkqp
     1081 gdeertdipa yysggvsswm nlpngrqfsl yemwrqsdir vvnasflrcn qlsltwnmne
     1141 dwckklgiln lsvnlvmnna fviaskrlng fdpeldnsim pktyslgfsv gf
//
LOCUS       WP_099307016             397 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Zhengella
            mangrovi].
ACCESSION   WP_099307016
VERSION     WP_099307016.1
KEYWORDS    RefSeq.
SOURCE      Zhengella mangrovi
  ORGANISM  Zhengella mangrovi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Notoacmeibacteraceae; Zhengella.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Zhengella mangrovi"
                     /db_xref="taxon:1982044"
     Protein         1..397
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41215
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mahtvfipve adgaetrvaa spdtvkrlkg lglevvvekg aglksritdg eyekagatig
       61 saddagkadv vlkvrrpqaa eqkayksgal viatmdpfgh eddvksmaea glsafamefm
      121 pritraqvmd vlssqanlag yqavidaaae fdrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatakrlg aavtatdvrp aakeqvaslg gkfiavedde fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl isadmvksmk pgsvivdlav erggnvegak
      301 agevvdvdgv rivghlnmpg risasaslly aknlyaflet mvnketgevs vnpedelvka
      361 tllthggsvv hpafapkeep keiliaekgs ddtkgda
//
LOCUS       WP_099297191             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Corynebacterium dentalis].
ACCESSION   WP_099297191
VERSION     WP_099297191.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium dentalis
  ORGANISM  Corynebacterium dentalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Corynebacterium dentalis"
                     /db_xref="taxon:2014528"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53560
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipkepl alvsatpdtv skliklgydv svesgagdna nfpdsqyeea gakivgddvw
       61 tadiittldp ptaaqrtamq pgatiisrla pgrneeliee lasrnitsva mdtvprisra
      121 qsmdvlssqa niagyravve aantfgrlft gqvtaagkvp pavvyvigag vaglaaigta
      181 nsmgaivkat dlrpetaeqv esmgaefvei pvateksedg yakemtqdqa eaaaklyaae
      241 sakadivitt anipgrkspv lltaadvaam kpgsiivdma aanggncelt vpgeitttdn
      301 gvsiigytdl agrlpaqasq lygqnivnll klmtpekdgq iafdledviv rgitvtksqn
      361 dtagaaqadi lwppppvkvs aapasnqnnn adaataqpat eeevkkpsga wkwiagalgl
      421 alilaspmqv ateymllmla ivvgfyvits vthklhtplm aetnaisgii lvgailqvgs
      481 sniavaalaf laivvasini fggffvtrrm ltmfdggn
//
LOCUS       WP_099315318             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_099315318
VERSION     WP_099315318.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38883
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag ihasvpdsay eaagavigdt
       61 netyaaelil kvvapddeal nliksgsvvv gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaayhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_099337394             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter sp. LoGeW2-3].
ACCESSION   WP_099337394
VERSION     WP_099337394.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. LoGeW2-3
  ORGANISM  Acinetobacter sp. LoGeW2-3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter sp. LoGeW2-3"
                     /db_xref="taxon:1808001"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39810
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaetv vgenrvaatp etvkklisag hnvviergag vkaayidsvy eqvgaqitdd
       61 aytgsqlilk vrapkgeeiq klpanatvva mfdpyrntel dhfaaqnvsa falellprtl
      121 sraqnmdvls sqanlsgyka vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmseeeq qkaadaakng ygwmpgeqyi
      241 kdqaiivdka vsnadivitt allpgrdapr liraetvakm kpgsvildma vetggnvegs
      301 qcgetvvten gvkilgipni pstlsteasa lyarnvlnfv etlfdseknf ainpeeeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_099332928             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces minihominis].
ACCESSION   WP_099332928
VERSION     WP_099332928.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces minihominis
  ORGANISM  Actinomyces minihominis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Actinomyces minihominis"
                     /db_xref="taxon:2002838"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53807
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpaekp dqplvaatpd tvskliklgy tvavqsgaga lasypdyqye eagaelvdrd
       61 gafkadivlt ldapelydle kmhresvlis rlaptrnedl mrvlaemdit alamdvvpri
      121 sraqamdvls sqanvagyra iieaanefgr lftgqvtaag kmppahvyvi gagvaglaai
      181 gtansmgaev fasdvrpeva eqvnsmgarf ialpqaqeks tdgyakamte dqarlanavy
      241 akqsavsdiv ittanipgrt spillddeai aamkpgsviv dmaaanggnt tqtvagqkiv
      301 tdngvtiigw tdlagrlpaq ssqlyaqnvv nllklmtpgk dgqmvidlnd eiirgitltd
      361 dgqilwpppk iqvsaaptak aedavdhaka aaeaareaaa akqkrfawmg iaallavalv
      421 mvtpslaigh ymvfvlaiiv gfyvitgvah slhtplmsvt naisgiilvg aitqigssnl
      481 avtilsfiai vvasinifgg frvtarmltm fqkg
//
LOCUS       WP_099340117             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Fonsibacter ubiquis].
ACCESSION   WP_099340117
VERSION     WP_099340117.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Fonsibacter ubiquis
  ORGANISM  Candidatus Fonsibacter ubiquis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Candidatus Pelagibacterales; Candidatus Pelagibacterales incertae
            sedis; Candidatus Fonsibacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Candidatus Fonsibacter ubiquis"
                     /db_xref="taxon:1925548"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39811
     Region          1..358
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgsvidsd inekriaisl dtikkyisng fsvqlekdfg knsnindsel qklgakiltk
       61 eevyktsdii ikincpnete islikegail igsffphlnk dkinkllkkn ikifslellp
      121 ritraqsmdi lssqanlagy kavidsvyef nkavpmmmta agtitpakff vigagvaglq
      181 aiatakrlgg vvsatdvraa skeqveslgg kfvfvestkn letsggyake ldeddkkkqe
      241 ellkttiknq divictalip gkkaprivte emvksmksgs vicdlaveqg gnsafsepgk
      301 isivngvkii gyknfpsris esasilfakn ilnfleiiyd kvgkkikide ndeiikavyi
      361 nkeih
//
LOCUS       WP_099358301             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas dhakensis].
ACCESSION   WP_099358301
VERSION     WP_099358301.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53380
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tslgtsgwaq aadeaqikgk vearselfak dhadqfsswk
       61 atgesrertd alaedpnmvv lwagyafakd ynkprghfya ltdvretlrt gapksaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy ftgptkavkf pwdkgttveq
      241 meqyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg vvkqrkdaih dlklrvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakglsq eiaipdissk ekaqaalgmd mqqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_099365351            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099365351
VERSION     WP_099365351.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119218
     Region          27..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkdiivfl fliflgmsqn ansqqllrgv vldasshvpi plavvlhngk ktmtdsvgaf
       61 hlrvrtgdri rvtdiarhpk ehvfsdgdgt dltillepli eqleevvvss gyqelskkdv
      121 tgsvavvsra eleknpdpni lsrlrdavpg lifnkldvlq rqsisiggks tlfanseplv
      181 ildnfpyegd isdinpqdvq sitvlkdaaa aaiwgaragn gvivikskig imgqsnkfna
      241 smnlgisdpv dlfynarmts pefiemekrl fengyyrsqe ssqsntplsp avelmiahre
      301 glisadqldl slmelgahdv rkdlmkevyr pemrqqyavs hsfsgrgnag mvslgydrnr
      361 enlqgncndr ltltfnqqik vwkdrmtitp gigftqragd rpnripvdlr fgstsiypya
      421 vlrspqgdpl avtrsyrrkf lesalqqgll dweyvplsdv ehlqfrtndr mlraslnadl
      481 ellsglklsa dyrwlgswss gkslygpqsy yardmvnnyt flnggqlqyg ipqggildgr
      541 ygngsshnlr tqlqfdkdwe dhrfnilvgg evsdansrtd syrlygydpe hhvsgpvnyl
      601 vnykqysspf srripyqdsg sdltdrflsy ystlgyylkd rylfnasarl drsnifgvrs
      661 nqkgiplfsl saawsldred ffrplshlfs gmklrlsygh tgnvdnslss lmvaqrspvt
      721 adhtglpyst imnpanpelr wervaisnig vdmvllggkf dvtldsyrki grdllgsidf
      781 ptssgifsfy gntagtktwg tdislkgrfp iiakasstts fmfsynrdev thytlehpvt
      841 svlsaghigs fpvvgrpihs ifayhwsgld sengrplgli ngevsgdhrk iiqsskledl
      901 lfvgtsrprm fgslrqefiy snislaigls yrlgywyrre svnynhlfta trahgdfser
      961 wkvpgdelyt qvpsmptvrd nnevlfytns ailvepgdhi riqdiraqyr fqtreipgtv
     1021 alfghienvg mlwkssgkkl dpdhpnqkal rywtfgmrid f
//
LOCUS       WP_099365283            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099365283
VERSION     WP_099365283.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118209
     Region          43..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrsilrisq gslilllgls cisqasghvk yvplksyaaq elinvritvl dqssgnpleg
       61 vsisannrai gltgkdgvfs gsvvkgttls lrmigynstt vkvdqetysi klsavdesie
      121 evvvtalgik rdeqalgysa tsvkgeqlte alsnnwmdal sgkvagvnlm rsnagpvgtt
      181 kiilrgennl tgengalivv dgvimnggsg rssalgsdga ygtgsdnmpv dygngmddin
      241 pediesitvl kgpgaaalyg srgangavii ttksgsakgk gigitvnsna afesmnrspd
      301 lqyeygqgld gaahysfgss vdgsstsgts saygpkfdgq effqydpilq kvgptrtpwr
      361 aydgkngvng ffdvgrtftn tvsidgstdk ttarfsatnt hnkwivpntg ykknslalsv
      421 sskitdklti nskvnytnrw sdnlpgtgyg nqslmywyif wqpsadlnwl rnywvngeed
      481 rkiaypfsty penpyaisye finsnnrhti tgnaqavyqf skdlkahvra amdmgiedrn
      541 qnrpydagsk lregsyrsqs ifsketnidf lvtynkklnd dfdfsvnlgg asaridydrd
      601 emtsdglfyp gvynhnnsky gvktrqiier sqtnslyalv ttgykdflfl datfrrdwas
      661 tlatrlytdk elgfnypsin gsfvfskiwd lpefisfgkf rasyagtgsg vqkpfqtefn
      721 yenpnsllgg slanpstlan plikplstss lefgtdirmf nnkvkldiaw ykanssnqhl
      781 yrfvdpasgv srflvnfgev enkgleialn tdqikakdng fgwssyityt gnknlikqlt
      841 dstivlqqrs vgsgqivgmv ggslgdlygi gyerapdgqv iydestgyak ltseilylgn
      901 tipkgkmsfg nnfsykglrm nllfdtqwga vghslthykl aeqgktkntl pgryssiign
      961 gviqnadgty rqndviaknv deyyrshfgq dnaegstfpt dfikfrearl dyslnknlvs
     1021 rlginratig vygrdlfiwt kwpafdpefg tldggdivkg feiaqfpstr tfgfnlivgf
//
LOCUS       WP_099365734             919 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099365734
VERSION     WP_099365734.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..919
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102800
     Region          58..916
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mftkkyiisi cfailmanss iyaqniaakp atvdslhrld iapstisivg klyekpnisv
       61 sesgnlgasp vlmirglnsi nlssspliyi dgipmrysga nptflstfep drlgflnpnd
      121 inniqvlssg fempkiggrg sngileihte rgefggtkvd fianygliss nlnvprldaq
      181 smksylwsrf qeegmspaql dqhpifsesn pkynfqndwl nmikrdgvfq dyhlklkggd
      241 gdanylfavg ytnkeglike tnferiglrf nldyqlapni siynnlsytn tsghykefgs
      301 dynthpiyia sakapflgtn fvnadgsqsr ilasvdtlgl snplalvnnl snknqfnrid
      361 gvmgvnwkir gawdlksdls isyfnlsekq frpalgivpd lyrirqnsqr sssefylnwn
      421 gilsnsgkfs enlkyntsiq aaietyeeks vfgrkinagt ddfetlqqgv vdsasntryr
      481 snlmsyiaeg ilhwnerisl naslnvqgss nfgsnsrwni ypgakvyfyi leekplnkws
      541 inlgynrtgn hevrgfyhfn qyypenyfgy ggvyfgnian pslrpeitdn ydiqsiitpf
      601 gnrlqlnlgy yfkhttnlit hktilnelgl qdrfenagsi tnqglelglt sqiiakenia
      661 wnlstsvstl knkvtslpng aieqsignit giakegeqlg syygyrvlgv fqnesevnlk
      721 ksdgtvyhpg dyviedinnd giinsldkqi igtglpkffg yfsttfqykn fglnllfnfs
      781 qgadiynsfk qqmhlmkdfa nqdpsvlnrw rsddetgngl sravlddpsn ngassslwve
      841 dgsylklkqs slhynikgkp sqffknimiy lsadnlitwt kysgfdpevn glnisllrni
      901 dfgapplgkt fklglktsf
//
LOCUS       WP_099366010            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_099366010
VERSION     WP_099366010.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116160
     Region          25..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyikyiivl llftmqdvaw aqqritvtgt vydassgkrd plssvtilsn glsigstdnn
       61 gkfsinvpnn atlvfrtigy dsksvkvdnk tsltvgltss sekiaevtvt sgyqtksrtl
      121 ntgsavtisg kdiqgqpagd vmsllqgkva glniqnntga pgfrgsvtir gisninvtgn
      181 gnnafltpts plyvidgvpv ddnadysygf qqagpgvspa sqippedied itvlkdaaat
      241 slygsrgayg vilittkrgn skvpvvryng safmsavpql rsviggkeer lmrirqilmn
      301 dtsaihaldl vnntpflsds lnayynnstd wqsyfykpty nhnhnlnvsg gdvqfnykvv
      361 lgaydekgiq entgysrynl nmnmiynpvq kfkieallnn siqkqrmgsg ngllnngvat
      421 ggasssllpa pslyssvnsv lgalttdddn kvlntnatvn ifydlfrnfk agvynsyttv
      481 sstkdnfspa alnsnqakyy tyndrattly nraqlsyvfg frekpgdeel ahnfnlfafs
      541 elrasffksd amlndkvvnd qlrgpltlmt sylsskggti gytdlrtvaf agnfsynyks
      601 kyvldfnyrv dglstngpna gykknpsisl kwnfdresfl dawtwldygd frvsygsnis
      661 pngniyqayg klyaggrynn qntvisdlgt lpnlsleptk attynfgmdf sifqnrlsvm
      721 fdsyykqndh ifkekqlsss nsfnvigste isnvnygwef qatarplsps spfkwnlsgn
      781 fainreilak lpdglrefiq idnslgqsly yrlgtnslsn ylfntkgvyt sldqipvdpv
      841 tglpvrvggn gllnyfkpgd piytdldgny iidnydqvia gnsqpqitgg lmsllqykqw
      901 slevntsftl krdilnnsla aqfglfgkpt emgglvpisq ynfwqnvgdd avypnpfdfv
      961 rsailnpfrt nqtlfqedgs yfklnsvkvy ynvpqtlsqr ygmnrlsinf taanlgyitr
     1021 ysgpnpesvs algrdmsggy plpkqftlgl nvef
//
LOCUS       WP_099366014             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099366014
VERSION     WP_099366014.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111695
     Region          74..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvktsislsi alclsfgglq lnsahaktfg esslkgyrip fvksqvdtse ynaktdtigq
       61 mvkalqkfkn akdtinirea savpnlslqq iakghlagly vqepngepgt eqsmivqgps
      121 gilfskkdvy alqpavylng vplvadnpfa fdvqkydynr vgpannllaq inisniesvv
      181 lvkdpfelak lgpnaangal yittknakag irdislntyf gyatapkvnt vngvyennfr
      241 rpfyekygnq qryddyalyl rdstntayfg psnwndlyyk ntptysadlg itggneranf
      301 rffgsgtkna gnadetninr ynvffginma pfkwltvssn vnavrldrnr nkslrdrfae
      361 tryipdlstp lspnkdnfgl yldenkknvd nnrttsingn ltlssklnrf slqsslffdy
      421 negirdyftp stlmdgvsyi styfgynqrm iwnntigydf dlgddhsldl evghvyqgdt
      481 ykynyarayn gpndyvklvf vdpgaqgdsy lnalnagnfy vfryidkeln nllsfygsak
      541 ysykdifkln amvrrdgssn gqpdsrwmts pavsmtynlk dqlfagssff nqlelsagwg
      601 rnvriflddr yaagpqyrse sgwyeeptip gyggvlginr pyesgfigyg iklpyadrtn
      661 isldgtflnn rmnaaisvyn rndknqlvgv pvplesgysv nyksglevnn kgiefllngq
      721 iiqnpesfnw rssinlnynk nevtalpdgy keiingdnrl evgkpvtsyw iyknqgiynt
      781 dadvpaghtf ngiplfagdp qwadlnndnr idtrdkvmeg nrlpsliggw sntfayknfd
      841 lnfhfffatg hkilnqyqat kydfikreas nditsvkevs swqsfekekt ypiynpwsdv
      901 nayrvdqdlf ledasylklr svtlgydfkn asflnsssgk frrvylyata lnvltftkft
      961 gvdpelsnyn glydganlti prtfvlglkl dl
//
LOCUS       WP_099366388            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099366388
VERSION     WP_099366388.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116321
     Region          24..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkllslif vltcliglaf aqnrqvsgkv tseadgtplg gvsvnlvgts tatqtdasgn
       61 ysifvgenat lnfsyvgyts krvavgtqtt invsltgsdq eldeilvvay gtakkssftg
      121 sastvksdvi enrsissitk aldgaapgvv stlgtgqpgs natvrvrgfg sinassnply
      181 vvdgipfdgd lnsinpndve sltilkdaaa stlygsraan gvvmittksg kntngkinin
      241 fkanvgvnsr avgrydvmns qeyletvfqs yknreifllg vpeseagqna vnkmkgtvdp
      301 ifglneqynp ynvpvdqlfd latgkinpna slkwednwld evmannpvrq eyqfdasggs
      361 dkfkamasmn ylkdqgllkt tafdrysgrl nneftpvdwf kaslsgnfsk tssnmlnatg
      421 sstsnvwysa eqmapiypiw erdadggyvl dadgerlfdy gpnrasgaqq kfnsiavlyd
      481 dryfdfrdna gvrstiefnt rdekygafqg falafnlgtd yvsnaytyyy npyfgnaags
      541 grlnkewtkt fsytfnqllt ynrsfglhnv dalighesya fkfnllsgqk tgfpfggife
      601 lapgssitgs dsyennetle syfsrvqydy nnkyflsgsf rtdgssrfhe dirwgnfwsl
      661 ggawkiseee flqgndwins ltlkssygeq gnnglltasg sqayyawqaf ydltynngns
      721 ngagvvsven kktsweknrn fnvgfdgrfl ndrltvtfdw fsrktsdmll nrplalslgf
      781 dgyfdnigdm enkgfdlsig ydilkdngvl wnvtamgski nnkvikltde nkeiiggssi
      841 iregeainsf ymarsagvdp atgsqlywvy dnkadetdls khyissdksk aaasriiqgn
      901 ripkisgsls tnvayknfdf smmttysigg kiydvigyny ynplyignnf sreilrawkq
      961 pgditdvprv qkedthtltd ralvdasyfa iknisigytf gferfglksl rvfaqgdnla
     1021 ifsarkglnp qynftgttdy syspnktiaa gvnvkf
//
LOCUS       WP_099366390            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099366390
VERSION     WP_099366390.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112711
     Region          24..1019
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrllslif vmtclvgvaf aqnrqvsgkv tsasdgapls gvsvtvagst tgiqtdadgn
       61 ytisaanest lifsyigyet qrarvgektt vnvamvasdn aieevlvtta ygikrsaast
      121 gysnqtldsk altegkvvnl vtglqskvag lqvnllnngv npstrvvlrg nrsllgnnqa
      181 lividgtpvp nsmlaalnpn diesttvlkg anaanlygse gvngvliitt kkgakgsavi
      241 nfsnttsles vsflpkmqdk fgngydlety vpyentswgp kydgsevvvg ptlvngnewk
      301 lpysyvkdek mnfwdlgtti qndvsvsggd dngtyyasfq dvvlkgivpk dknrrtggrf
      361 nasrkfgnlt ssfnlnyayq npdmtvsgvy dnllnvpqni pitqlkdwqn nefatpdgyf
      421 sgyfinpyfg idnnrrntrq etfngnlelk ydfadwlsat yrlgnyafnt nykeynakvs
      481 ytkaydrptd npgsvtdrsd nvnrlnsdif vqaqkkvsdf dlgfilgntv rtdytkfnsi
      541 tanalvvpgl ynvsnrlgea tvgsdyskrt tvglfgqidv nykdmlylsv sgrndwtsvl
      601 detkrsyfyp gvslsfiase afpsikettp inflklyasg nrtanvnlga ynlqtafdia
      661 pgfpygnrpg ftvgntfanp dlkpefvnsy eggiqlgmfn drlnfegtya ysisdgqiip
      721 istswatgyd rayvnagtvt nntielslrg tpvltndwkw digmnfthyd nkvtdlyqgl
      781 deiplggyan sayvyavkge aypvikttay erdpqgrivv dketgypvra aamkimgqtn
      841 apknfglnts vrykeltlaa qldyrtgnvf ynrvgntnnf tglswesaqy drqpfvipns
      901 vylengnyie ntsiktqdgg feywynqhnt iqenyvkdas flklrevslt yslpyrwlen
      961 qkvvkrasig lvgrnlfmwl pkeniytdpe fsftdgnsqg isdminpptr iygfnlnitf
//
LOCUS       WP_099366393            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099366393
VERSION     WP_099366393.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118902
     Region          24..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkllrvfl lctmligvvy aqnrqvsgkv tsaedgspis gvtvsvqgan iatqtdgsgn
       61 ysinapangr lsfryvgyts qiitigtqst invqltadqg nleeivvtga ygirentkaa
      121 pfssqtlkad avnvtrqpnl nnalagqvtg lqvrsqsaaa lgrnteirlr gasgfgagdg
      181 aiyvvdgtil pnsddinidd iesvtvlqgp aasaqfgsqg angavvitlk kgyrgdylgi
      241 dlnlgatfdn vyilpnyqns yaggssaamk kytwtpgqpe ewkaldgkyy hdysddaswg
      301 prmvgqeyip wyawygghsr sfqttslvpq ennarefyet gvvlnnsiai skggenymtk
      361 isytnqding liptsglkrn ilnvtgeldl stkfkagvni nyvtqrlkge iddaysnqtt
      421 gsfnqwfhrd ldmdilkelr glrtedgifa swnkanpgay dpenprgfya anywynpyty
      481 ydnidranqr drlygniyfk yqvykdlsft atyrkqqntt fweymyrsdl dqsglqtsgn
      541 nplvkgyygt gntysnrtnf eimasynkri sdfsidanvv tdffrarsne nsgntvdglt
      601 vdnlftlsns ksqanqynyr sregynailg rgvfgykdml fanitlrndw fstlpadrns
      661 vlsksfgasf ifsdlikest pwlsygklrf awgeipmafg tgtsfgayay pgmaygvnqy
      721 kwngmaltst pdglvdpdlr gsvvsqkdmg ielrflndri gleftyfdgs qidfprsitl
      781 ngasgyssil tnvgriekkg feyilsgtpv kndnvlwnik atlsdlkdnd vteisekygv
      841 drivvagvwg stmptlihev gkrwgqiygn gikrnadgvq ivgddgmpln dkvffgsalp
      901 rftggvqnsv syknfslsan idwqfggkfv slsnmfgsfs gltartatln dkgnpirdav
      961 adgggvrvdg vtedgeavtt yvgaqeyfqg lynnstfddy iydltfvklr avslgynvpv
     1021 rnltwskfir sanisvvann plliyaktkd fdpsevsave gergqlpgtr gigfnlrigf
//
LOCUS       WP_099366435            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099366435
VERSION     WP_099366435.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117946
     Region          26..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiffmisv lftiaavahs qqrvfkvvda dskkgitavv svgnnnfptd nngyfklsiv
       61 nrpvklriqa lnyipldtll sdyngslifh lrpvvkeiee vvistgyqki kqeqltgsvq
      121 higshmlenq vstdvlsrle aissglsvdr staqgritir glssingpkd vlivvdnfpy
      181 dgnleninpn dvesitllkd aaassiwgsk agngvivitt kkgefnqdlq iqgsinnnvi
      241 skpnlyrlqq msssdyidve sylfsqgyyq sayddpsmpg ltpvietlyn adlspsekee
      301 rldrwrhldv rdefkskvyg vglnqqynlq anggnrrynw latagydrnr dnldalyarl
      361 tlryaleinl aknlsvdmni thanaqsksg kqgyteital ngtlypyaql tdedgnampl
      421 vqnyrlsyls tldgrladwk yypltdclfn kdeinlnntg invgmnyrya gfdvqalyrm
      481 erqqttneni ydaqsyfard ivnsfaqpad dgsisylvpq ggimdlqngy llannlrlql
      541 nydkrfgshh fnalagaerr slrnesnsfr yfgletntln tglvdltkry phyitgsnsf
      601 ipgrqslglt rnnfvsfygn asysyrdtyf iyasarrdas nlfgvstnnk wkplwsvgla
      661 wnvdndlpwl ksgaslklra sygfsgnadp srtglttity ntvspftqsn fasitrfynp
      721 dlrwetvgtl nigadfglfd rrisgsfdyy rkrakdlfgf ypidytsgvg ptmvrniasm
      781 eghgidlrle srnlvgnglq wgtiinfstn rdkvtdyydv stkggdyigt gtitglvgkp
      841 vysvfsyryg gldqqgnplg ylnndfstdy veltgngssl tdlryhgsal ptvfgnftnr
      901 lsynrlslev alaykfgyyf rrssiqytnl vgsgrghsdy slrwqntgde mhtnvpsfqy
      961 pvndsrslfy qlsevlvepa dhlrlqyvsl syqlenkfkn lgirdmriml nasnlgllwt
     1021 snkkdldpdy dnvlqpskay alalqfkf
//
LOCUS       WP_099366558            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099366558
VERSION     WP_099366558.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109910
     Region          26..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrflltff gvalyasclm aqqkavtgkv vssngevlsn vtvlvkgtdr mvqtnadgtf
       61 siqaapgetl vfrmigsder nqvvgagnvy nitlqssdea idevvvtamg ikqqarslgy
      121 saqnvsskel tesnqpnlvn tlqgkvagvq vtnsggspgt sasiyirggs slsgnnqplf
      181 vvdgipidns tpisqgglta glapasnrai dinpediasi svlkgpaasa lyglraasga
      241 viittkrgns gkgsisygnt fswdkanklp elqgvfkqgr ngifenesyl swgpefasne
      301 viydnlggff ktgfaqnhdl sasggserst fyvsgnlmeq ggiaknndfs rrsfrlnadh
      361 kifdnlkiga nmtymntgrt yfpqgsengv mgaiywprnv qmtdflnedg tqktlsenge
      421 naidnpywti nkkpitnrvn rviamgdvny npyewltlty rlgtdyygen fqsitaptsq
      481 tgltgymtes kannqlttst flanakqsvs dfnfdftvgh nietifretn tatarnfidp
      541 dfasinnala edrtvstsis rrrivgvfgd ftadwkniiy lnlkgrndwt stlragqnsf
      601 fypavstsii ltdlmkelsg nsstgflsya klraawaqvg kdapahklat tlgtyindft
      661 inprgfisnm ndtygnpnlv peftnslefg adlkmfnnri gldvtwyktn sdnqilstrt
      721 ppssgsflav lnggeienvg wegilnvqav kkhdfswsfd vnfsknkatv lnlpgfldrv
      781 elsdawvkgd aaqgaaflns tlfgingktw ktndagqyll dnngmpqvvs tlsnigdrnp
      841 dwiggitnnf qyknlglsfm wdvrqggdvf nataytlvls glspltldrg tavipgiies
      901 tgatnttaip lnqdyytsrf anngynfved gswirlryvs lsykapasft erlklsnlqf
      961 tltgrnlllf tdysgvdpev sgsgagvaga gsfgfdnlgv patrgfdlgl kfsf
//
LOCUS       WP_099366739            1152 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Sphingobacterium].
ACCESSION   WP_099366739
VERSION     WP_099366739.1
KEYWORDS    RefSeq.
SOURCE      unclassified Sphingobacterium
  ORGANISM  unclassified Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1152)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1152)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1152)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1152
                     /organism="unclassified Sphingobacterium"
                     /db_xref="taxon:2609468"
     Protein         1..1152
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126895
     Region          46..1132
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrlllfsla lgltmptyas faeakgkesl gknagwtkat svlqntvsgt vsgpdgviag
       61 atvtvvgsta ttvtdangkf tinaavgatl rvsfvgletk tvtvtgstin itltessdal
      121 eevvvvayga qkkehltgav ssvnvektlg srpisdagrg lqgavpglsv qipsgevgsd
      181 pimkirgqva sisgssnpli lvdnveipsi nminpndiae isvlkdaasa siygskaafg
      241 vvlittkkga ktetnnitys nnfslqtpfk pidiasidgl qytldahknm qsagsaggfw
      301 riseesirra kewqekyggv ignsdpvvyg rdwyvennek fgvrmydpva vmikdnaltn
      361 lhnlglngka gnttynisag ylnqngmmka akhddfkryn atlnvstkvt dylslrggam
      421 ysdgtkryan satgftadpw lylyrwsraf pigvqehgvd irdpyfdtak shtaykidry
      481 tnlnlgttvd lmtgwdvkad ytfssenngn rssmptfsgk stwygvepwn dengnriyvd
      541 englptdngg tmafkfpfen yitkaqsniy qrsfnsqrht fnafstygkk fgedhdfkam
      601 lgtnivafkw rnhfsrrtnl ineenpqfdf atgvqesggd tnwdsqvgvf grlnytfkek
      661 ylfetslryd gtskfpshlr wryypsvsag wiisnenfmq gisnvlsfak lrgswgmigd
      721 qsvsnslyvp tmdigpnnwl dgsgnyyysm ttpgavrndi rwqdiehlnv gadlkffnkl
      781 gvvfewyerk tnhmiipges lpgtfgttpa rgnfgnlstk gwelaidynh sfdnglrltv
      841 naniadaitt tykglqwnre wenrsvgtef vtgsrygdvw gyvtdrlyqk ddfvydadgn
      901 feqtaiifqg vskttnmlag nnpvyqtffe dgnnvmkmmp gdvkfvdvng dgyitsgsst
      961 fgdpgdrmvi gnstprydyg frlgadfkgf dlsvflqgvg kreiwgagql aipgfhvkdg
     1021 ampqaiaedy wredrtdafy prawhlggan egyvmrpqtr ylldmsyfki kninfgyslp
     1081 gallsranfk tariyvslen fftfdnlrgl pidpeaisgn smlltngnyn lgrtgtgnps
     1141 fksasvgiqi gl
//
LOCUS       WP_099366743            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099366743
VERSION     WP_099366743.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114914
     Region          23..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgrlllfvi glvfissnly aqrsisgkvt dskgdplggv tvqekgkgnq tltnssgnys
       61 isisedatlv frfigyttae rkpsgniqnv sltedqsnid evvvtafgie rdrktlgyst
      121 pkvsgdevae tqreaffngl qgrvpgltvn sssglpgasa qivlrgfisi sgdnnaliiv
      181 dgvpidnsvv neadmvhvgt nrendysnrg idinpedies yvimkgaeat amygsmgagg
      241 ailittkkgk agrasvnysy sgrfekpyry perqyiyaqg tngvytatsa yalgpkynen
      301 evlhtdntkn ffrtgfnhkh nltieggsda ityrwsneyf dnkgvvpnts lrrftsrltg
      361 tskinskmdm nttfsymnsh ndkankgdvg ylmallrfnp rwdvrdwide ggnrvlhasd
      421 iyneidnpfw daykntaydd vnrmiansqf nykpnswism qatlgmeysv tngfkiyhgq
      481 syngsgnssd pdlgemyiyt rgariftggy rvttrnsffd kkftmqnnla aniydyhynt
      541 dsqygrkmyd pnfyninnsd pderraknyi dryrimgasl qsvlsyksll sltltgrvda
      601 ssrlmpnnpv faypsaslaf nfsefdavke nynwldegkl rfsisrtgkg pfrsfatrsn
      661 letqmtsggg faygvnggnp nlfvettedm eggldlsffk rrftmdftyy rrrsidqifn
      721 prlsyatgfi lklinggtie angieiqsnv apirkpnfnw ditfnytkqr sivkslakdi
      781 pesydsdtwl tggvrsavfi gesigslsat kfkrndrgdi linpqnglpl lpsestfgyv
      841 gdriprftlg ivnkfrykdf tlnflwdsrv ggdvynlldy rlytlglssq tlnreeprvv
      901 hgvledglen tdnptpnnia vtpyytsgyy yssvtgekfv ekniwtvrlr ditlsylmpk
      961 nlvrrigpks dlslfctltd vvlltnysgl dpesnsntpg iggiggygid ygnmtrpigf
     1021 nfgfrlkl
//
LOCUS       WP_099366844             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099366844
VERSION     WP_099366844.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108657
     Region          29..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msklftrail sigllmlmsm svfaqtaslt gritdsegqa vlgatvqvqg tqaatasgpe
       61 gaysfqniav gnqtitvtam gyktaskaia ikagenvldi vientasdld eivvigygva
      121 rkkqisgsva svgpkdfnkg vvsspdqlla gkvagltvnr sggdptagat vqlrgpsslt
      181 asssplyvid gvvganielv apddivsmdv mkdasstaiy gsraangvif vttkrgkagt
      241 pvlsysgyaa terianqvnv lsaaehaafv eehglavsps eaghttdwqe aitrtgfshn
      301 hnlsmtggse gtrynasiny fsnqgivkrn dlerivarvg ldqnafddrl klalnlansl
      361 nrsnhvdygi fngaarfvpt spimsddpty apyggyfqvp grtgymnpva mlnqrdenrn
      421 nntllaslka dltlykgltw tnvlsyqqnq ydrkyymhrt dfdsnalgqg faqrtnlkni
      481 dqilesylny nltkdqhafd amvgysyqkt knndgviars tgflsddlga nnlnlgtlpn
      541 gynpfqdypy ilesllisyy grvgytfadk yilsaavrrd gsskfgannr watfgsvsga
      601 wriseeafmk dqtifsdlkl kagygvsgnq nidpyrqiii fgprdgqfyy ngewvnaygv
      661 nqnenpdlkw esasmfnagi dfellkgrfs gsveyynket kdllyeydvp sppyqynrll
      721 angasmtnkg vevvlnavvy rnenfsynts vnfarninkv gslasnieni gvsqrfeggi
      781 glegwtgqta sivlpghalg tfyvanyigy deatqktiyq kpngelvtqd qisapddymv
      841 mgqalpkfty gwnnnfqfkn wdfnfflrgm ygnqifnatr adlsrlqqan vtniskdave
      901 egifetplia ssrfledgsf lrldnatlgy tfktgnlrhl knarvyltaq nlftitnysg
      961 vdpevglggl apgidnrnyy pktrsfsmgv nftf
//
LOCUS       WP_099367243            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099367243
VERSION     WP_099367243.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116776
     Region          27..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklpsiisla vasvcsmqml aaqqqsiagk itntkgepiv gasvfikgtq qgtasnesgl
       61 fsinapnsav lritavgyap kevavngrts iqvqldqeeg aidevvvtal giqrsekslg
      121 ystqkidgdd ltftketnvl gslagkvaga qvtgssgasl ggtqkikirg insvtgggqp
      181 lmvidgtpis nanfssstgn gvdlgnvgqd inpediesin vlkgptasal yglrgqygvi
      241 mittkkgkkg pksisvdvns atsfeqvgnf mplqniygvg nnqtflklas gelyvngnde
      301 swgpkmdgtp vrmyysfykq dedygkatpf spqpnnikdf fqtgmntnng itiaggaens
      361 avrfsynnty ikgtypntwl krnnfalngs ldltdnltas aninyannng qrpvmgyqgs
      421 ftgatqwfqr nidinrlrny ryadgtimnw nvnpnttqel minntpsdwn npffdayenl
      481 nndnrdrvfg dagltykvlp elklsafvrk dlftqntsrk lsiggrsesg agsflsntgy
      541 svgkfqndet nyeflatydk vwddfslnan mggniyqrny dyltqktqgg lsspaffnie
      601 gsidrplnes yklkkqirsf ytmasigykd tyfldasirr disstlpkdn nsywypsvsg
      661 afvfsnligp salsfgklra syavagadvd pfdiltnyni gsvyatsnst intlsipdil
      721 nnpnlkpsfa hsyeigadlk ffqnrlgldv tyyqqrnkdq vislstssgt gfsratvnag
      781 dienngievs inatpvqten ftwtttlnga knnskiheli pgidsyelgs ntyssqtvyl
      841 yankgmafgs lvgpgyktde atgkilldns nmpiqqmnkd fgsvlpdftg gfinsfrykn
      901 vdlnamidfq aggqffswsk mlavksgqae etaamnsngk nvrdpladgg gyeingisea
      961 tgqevnafvd artyfrnnig triyeewlyd asyiklrevs lgytfnqnql gsspfksirv
     1021 aviarnpwmi wqkapkgldp selsagsasi swiekgelqt vrsygfnlsv kf
//
LOCUS       WP_099367738            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099367738
VERSION     WP_099367738.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113385
     Region          26..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msnlyakscs imlvmllsit tlfaqqtvtg rvtdangpla gvsvtvvgtn raaqsdqngn
       61 ysiqadngqk irfssmgyaf qeitvsgath nitlsadnsn idevvvtamg vkrerralgy
      121 sfqevkgesl tdarennvan alagkvsnlq vvkgsggpas sskiilrgfn sltgdnqpli
      181 vvdgvpmdnf vgasnndfwn ptadmgsglg dlnpediesm svlkggaasa lygsrasngv
      241 ilittksgka kdgvgisyst itgienmfmt pelqstfsqg aggiygrlas tswgakiagq
      301 evdmwdgska nlsaydnmsn ffktgfsttq ninfqqaisd kvnlytsaty lhddsktpgm
      361 klnrlnlinr vnakfgernq wstdvkvqym knmaynravg ghndgnfysq vllfphsldi
      421 tqfktgmdel gvnqiwytdp adapvnpywa ahnklstdtr drylmnatvk ydfndwlsad
      481 arvgtdtyst kyesktytga nlnnsystgv dkfyennyia siharkdnlf gnwggalsly
      541 gqimernrng inssagnlrv pnlftlgnni gnpsisesis rkqinsvyss ldinysnfwf
      601 itltarndwt stlhpdnnsy fypsastsli isdlvrvnge mpswfsfaki rasyaetgrd
      661 mdpyqlynty nvgndpnnvt taskgnilfn pgvvnelqks feagfetrfl ndrigidfay
      721 yktnstnqli nipmnnlsgy qgfkanagni qnqgfevvfn anilrdtplk wdlranvshn
      781 qnkiiklhdd vkrtelggyd dvkifaeegk yygaiygtrf lrvedveseh ygklilasqt
      841 glpqkasgpt tmlgdqtara lvgitnsfsy knfglsfqvd grfggkffag thraiqlsgs
      901 saetvvngdr anfvvdgvil dkdtyvqnnk evspenywaa vagngnlgit ehnllnatni
      961 rirnlmlnys ipsqvlkssa vksakfgisv nnlamlksyg kgvdpestfa lstnavgfey
     1021 lsfptsrsff lnisvgf
//
LOCUS       WP_099367785            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099367785
VERSION     WP_099367785.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117826
     Region          24..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqnllsfil lcalfigvah aqnrqvtgrv ssqttgenlp gatvkvvgts istqtdgagn
       61 ysisapangs ltitnvgfis qtvqinnrsv vnvvlaedet sldevivvay gtvkksdftg
      121 satqigekel dkrplsnplv alqgagpgiq tsapggapgs sptirirgig sysagsgali
      181 vvdgvpydgg msninpsdve sitvlkdaat iamygsrgan gvimvttrkg kagsptlqas
      241 aqfgynqngv pnyntvsage yyelmwqayt nnmiygeakl pvdiarqigs gllprnaagn
      301 qvyngktyqd ivqflgnyna fdipnnelvs vdgilnpnak fkysdyktwe destrngkrt
      361 eynvnysgss nntdffasan ylkdngwsyr sskerflgrl nlnsqikswl ktgmnlsags
      421 htdnnassgd ginnpfyfsr giapiypvyl rdpqtgnlil dangekrydy gnfvadygln
      481 rifnsgrhal aetmmnndfg nrefinaray ldinflpwlt lsttfspdft ntrgesyent
      541 evgdgapagr ysqgwtrsys ytfnqilran ntfglhnlet llghevysyk yesidgmrtg
      601 qgfdgmhvfs nfvdiaslts gktestmesy faranynyns ryylsamirr dgnskfhsdl
      661 rwnnfwsigg awrldqeaff qneninllkl rasygvlgna dvgyypyqat yglynnases
      721 gsamtslgss altwetqkpf digvdfafld nringtleyy hrnsdgllfs vpqpyhnggt
      781 tggsfainqn vgaatnkgie lsvngqlirk enfnwtlgin lttiknemtk mpletpeivd
      841 gaykrsvghs mydfwlrtyy gvdpdngnal ylglaenatf dpkyhkvidr gngvmdtvts
      901 ehgtarlsyv gksaiapvyg sivntfnykd fefgfvltyg lggyaydgqy aglmsagptn
      961 ganlhedllg awknpgdvsl ipamntsrtg qtsalsdrwl rkrsylniss inlaytipsq
     1021 yvsrigvkna rlyasaenly fwsakkgfnp vgaftgntgn stythartin fgvnfgf
//
LOCUS       WP_099368168            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.4].
ACCESSION   WP_099368168
VERSION     WP_099368168.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.4
  ORGANISM  Sphingobacterium sp. 1.A.4
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Sphingobacterium sp. 1.A.4"
                     /db_xref="taxon:2044603"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111931
     Region          50..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpnyyskqnh rtgfvrgsil cfallacsyg yanampkaat vevnsviaqq tvtgtvknga
       61 ngsplsgvti kvkgkdastq tdasgkfsia aengdvlqvs yigfanqevt vsgtmanvnl
      121 iseeesleev vvvgygtqrr keitsavasv kekdfnkggm rspmdlvqgk vaglnitrtq
      181 gsnpnsstsi qlrgmaslkg tnsplivvdg ipggnldlik qgdiesidvl kdgsaaaiyg
      241 trgnggvilv ttkkgkagaa qfeymtygqt ervnrkpsml sadqfrqliv qgenkpdldl
      301 gastdlydel inkdnfshfh nfiasgggen styrasfnye nakgiakqng reqfggrinf
      361 nqtgldnrlt ltanlaanfn kanllggktg dfeqtiqrnp tapimnpdgt yyqtqeynny
      421 npmsrlahri eernqqtfsg darlkfqild elsvsafgsy vrdnwndrqy rsildwdqrp
      481 ddteydgtgy aykrndlnwt ktfestidyn ktfndvhtft gllgysyqym taeyfnmsns
      541 gfstdgfldw dfnsgtaiin tkyprpalgs fkdentliaf fgrvnynyad kyfvtailrr
      601 egsskfgann kwgnfpaisa gwnisnedff gnkdvvnelk lragygvtgn qgipnylsfi
      661 rlgtggyypq dgvyyqtygv ennanpdlkw eqkaetnigl dfallnskit galdvyhrkt
      721 tdllyeynaq lpayvqpsiw ynvgevvnkg velqltafpi srenftwqvd ftgnyqknkl
      781 aklssdifks nwlefgglps pgnlgnamrl eeggeignfy gkrfagfdde gkwlfykadg
      841 stahagdmnn ddrayigngi pkfqaslgnr ftykgfdltv flrgkfkydi lntadmffgn
      901 kkwipnnvfe safgkhdqln ddpqysdyyl engsfvkidn itlgynirtk tplirnmyvy
      961 ltarniatit sysgidpelq dtgfdggids rgfyprtqsw tmglnigf
//
LOCUS       WP_099369409            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099369409
VERSION     WP_099369409.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119951
     Region          27..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksfrqilti licmiltkpc lgqqqytgqi fdgrgrpipf vtvhlipldr dvmtdslgkf
       61 lldlenlthv sfskqgyvkv rlsiqellat psltleesti sieevsintg yykikpeqat
      121 gsvvqidnql lnrnpssnil erlegvssgl qfdrrqsygd tklsptlrir glgsinsdse
      181 pliildnfpy qgdlqainpn diesvtilkd asaaaiwgak agngvivlts ksgkrertsi
      241 dfssnmtiak spnlfyspnf ipakdmmele eelyqkgnyy ffdffpipdy vsllnkrdkg
      301 eisqsdfere kqrmqqadir rdaakslyqg evqmrhhlai aakhekhsyr ssigwestke
      361 simgnssgra tlnfldqfqv nprlqvttdl qlgflkssan gysldllnag mlnlspyati
      421 fnadgsyasm nfehshayrd aaesnglldw tfnpvkdrsh rqftnlkntl qiqtgleysp
      481 letlsftlky rygnqlgknr ndydresyfi rnmvnaytqp dgtriipfgn imegnnstfn
      541 shnlrfqlnf nksfandhki nilagseish qnleynggfr yygyspenqt ymasidyatd
      601 yllrpagaar vpgsnfrnes ltdrfisyya nsiyefkdqh vlsasvrwda snifgvstnq
      661 kgvplwsigf senlkvlfkd avpqldlfki rgsygvsgnv nnsvsslatm rfeqldfvsg
      721 rpyakltsag npslrweklk tlnlgldvgm fsgrfnatfd yyqkkgldli gpnyldpttg
      781 iisiegtypv snlinyanlr tkgidlslav kpvqtnhfdw nvnllwswtg nkvtnylane
      841 nggassyvsn lqprqgysrd alfaweyggl gtngqlltpd gdqqygdyyn aavfedlkyi
      901 gvafppyqgs lrntlrfksl eistvvewkn gfyykrnsid ysrlfstgam hsdylkrwkt
      961 lgdelktnvp alpeqantiq dalyngssim fekgdfvrlt dltvhyavpl nstwirnfrl
     1021 ffqarnvgil wrssqenidp esvsarypqp rnytlglqle l
//
LOCUS       WP_099370026            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099370026
VERSION     WP_099370026.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116704
     Region          33..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfrtyfkl sllvflcnil qlqvlaqest vmlsgkvlde qqnpikdvii ssqnnkigts
       61 tnwegtfdle iplsieelkf erigystqiv niqggdstli vvlktdnhql dkiidlgysn
      121 ttfgdltgav sivqgdvler hpvanlsqtf agrlaglttq etfselsran tdlfvrgisa
      181 arsgdplvmi dgiptsynsn qsleyispne iesitilkda stqaiygiqg angvivvktk
      241 rgkkgpveik arldqsfqqv ttkplmynal qyaefsnqag vndglgpfsq fsedivshyr
      301 tgdspelyps nnwydkyfkd fasmqrlgvn itggndkvty fsnlnfmhqg gyfnteskdy
      361 danpkniwvn yrsnvdiqfn nylsgflrls gnvkrehvpg gasndatyas mflmppttyg
      421 pltpvikden gvelpgsgqv ivtdrvdqst ygilnrtgyy nhtvtnissq fglnldmsfl
      481 tqglnlsgvf ayqtnsvgsl attqnyeryi rsdnwdelef skkgeqnntp laygkshsyy
      541 yhltykgqld ysrvfgdhsi namayglfqd ltkantnape llpykrlstg aqlvynyddr
      601 yvlkgvfgys gseqyarshr ylftpavaas wiasnesfme stsewlsllk frgswgktan
      661 dqsdlqryay ldqitqqsgg pigylqylit erqtgnpniq aevstkanfg ldlglfnsit
      721 fsadifkekm enmvvgavst ipsyqgipls nyprlnqgif enkgyeltlr ydkrlndkls
      781 fyvegmfskn hntiiswnea qrtedfqyrl reegysygqq fgylvdysqg ngffnsqaei
      841 daagldygfg avrvgdlryq dlnadgiide rdqgpvgdgm vprityafsg glkysafdmn
      901 fifqgigdys rimmgpgiwe ttnggmytal hqnawtaery angetitwpa lsteksvnhe
      961 asdfvnfnks ylrlrnlelg ytlqrestkk igfdqirivl sgqnlftwdk mktkdfgpeg
     1021 sgyitfpvyr vysfgvnlml
//
LOCUS       WP_099370455            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099370455
VERSION     WP_099370455.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117221
     Region          27..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrtiyfylv glffalsign vhaqnilrgk vldelnqavs gatilekstq kqtltnqdge
       61 fsldspnpta qitvrflgyq dqtvsvnste sktiilvpsn dvleevvvta lgisrekkal
      121 gyavqevkst elqtrptnal aalsgkvagl qvissggnmg gstrtllrgi nsiagsnqpl
      181 yvvdgtpidn sdlnsagtin gsagkdvgnm iqdlnpddie nisvlkgpsa aalygsraan
      241 gvilittkra gkgenvsidv ntglefeniv rlpkrqhlyg qgysqtfqtv nidgkdykiv
      301 dyasdeswgp kldgtpvlqw ynlnpedaad ylnpspwlyp ehdvtyffnt glantnnvai
      361 sgnsgqtnyr fsytnknvkg tvpnaslgrn tlnfsggtkl gklsvntnin yihnnsigkp
      421 wtgasnrnii leayqwgavq vdykrlenyk radgtplawn rtgwqntpaa eatrfidnpf
      481 wsayesylee krdrfygnvg vqyevadwln vgakvhgdiy qfstedriav ysrsasqyee
      541 tsnrlneyny eflatakknw dkvslvanvg anlrnqsrkv dygitqggli ipnyynlkna
      601 snvkienfky nrriasvyas aslgyhdylf ldatvrndws stlptnansf iypsftgsfv
      661 fsqvpgfqad wlsfgkvrlg waqvgndtdp yqlykaydve qsfnglssnk lpstlnnsel
      721 kpeitsswet ginlqffrnr lgldvtyynn vsrnqilpip vssafgyeak vlnagrvenk
      781 gleiilngtp iqndnfewna slnysrnknk vlkldelvnt ltlssslinl varegqpygq
      841 llgydfvyad gqrvvkedgt ylrtsqlvpl gsvlpdylfg fqnnfryknf nfgflidgrv
      901 ggsfysqtyn vgmysgildr taennvredg lildgvkadv vfnpdgtytt snvrendtri
      961 taqqwgrnes tgpttfsifd gtfvklrevt lgyniplndp kvvkgvrvsa yarnvwniyt
     1021 kskyidpefa nssgnvqgie agniptplty gfnvnlkf
//
LOCUS       WP_099370606            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_099370606
VERSION     WP_099370606.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117432
     Region          24..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkllslif vltcfigaaf aqdrqvsgkv tsatdgapls gvsvalvgtg vaaqsdangd
       61 ytitvegsna vlnfsfvgft strvqvgtqt sinvqlvede msldevvvvg ygsttkeaft
      121 gsakkvdgak lqqknvsnis qaiagevagl qvvntsgqpg ssstirirgf gsvngnrdpl
      181 yvvdgvpfsg sissinnadi envtvlkdaa ataiygsrga ngvivvttkt grgatsyvea
      241 danfgtnmsl iprydviksp eeyiglswqa mynegvangv dgvkyandnl fsdrgidpln
      301 niwnvnsiad lidpetrkvk snvtrkfnpe nwedyafqna artdinvrfg gssdktnyft
      361 sfgylgdkgy sinsdferlt grvsvdhkvn kiinvgmnmn yakterntgg qsedsgsifw
      421 fvdnipsiyp lferdadgnt lpdpifggsi ydyginsark fgsltnaiad atydikrhnr
      481 nelngrayvn fniiegltfe nslgiqlynn lyndrgnkfy gssagqngsl yqrredlnyy
      541 nllnllryrk dfgdhsfeal aaheavkwks nildnsgynl isndvlefnn vvvsnpvssf
      601 tneyalesyf gqinydyqnk yylsgsirrd gssrfktdkw gtfgsigagw ivsnesfmqd
      661 qdifdflkyk isygligdqa gvgyypgytl vtpenvntel glkigddmgn tdltwetskm
      721 fqtgvefeig kylsgtveyy ikntdnlifq fglgpslgyp tilvndgqlr nqgiefdlvg
      781 hifknenfyl dlgingesfk nkitkmpiea stnlpktidi qgiygwaegh siydfymrdf
      841 vgvdaedgks mwkvyytdnd nngeftageq issmalftnp dnkeikestt ktysqatqyy
      901 vgksaipair gafnlrtgyk gfdlsaqvly slggyaydga yatlmsndpi ggnnwhkdih
      961 nswqkpgdvt dvprinndld anvvststrf ltkanylmln nvrlgynfks dwikafgaqa
     1021 lsvwvsadnl aiasarrgfn psthqagass myrysplsti sgglrvrf
//
LOCUS       WP_099370609            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099370609
VERSION     WP_099370609.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119675
     Region          24..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrllsmfl lctmligvvh aqnrqvsgkv tsasdgspia gatvnvvnnn tatqtdesgn
       61 ysisvptngq lqfryigfes qtitvgsqtt invqlvggdn sleevvvtga ygirentras
      121 stssqtltse kvnvtrqpnl nnslagqvsg lqvrsqsaaa lgrqtevrlr gasgfstgqg
      181 aiyvvngtiv pnsddlnmdd iasvtvlqgp aasaqfgsqg angavvitlk naykgdylgv
      241 dvnvganfdk ayimpnyqns yaggssqams qyvwqpnhpe ewkaldgkyy hdysddaswg
      301 prmvgqeyip wyawygghdr syktasltpq pdnardyfet gvvlnngiai skggdnystr
      361 fsynnqnvng liptsgldrh llnftgeldl ndkfsvgani nyvyqnlkge iddaysnqst
      421 gsfsqwfhrd ldinileelr glttpdgiya swnkanptay npanergfya anywynpyty
      481 ydlinrynqr drlfghvfar yqiysdlsiq atyrkqqntt fwetkyssdl nksglqttgn
      541 nalakgyygt gntysnrrni efllnykkei edfsidaniv adfyrsknne nsgntvdglt
      601 vdnlytlans vsqanqynwr eqeaynalmf rstfgyknfl fanvtlrndw fstlpkddns
      661 vlsksfgasf vfsdlikest pwlsygklra awgeipmalg ltsttfgayr ypgaeygvgq
      721 fkwngnslts tpdvivdpsi rgsvvtqkdl glelrflkdr igtevtywdg ssigfpqsit
      781 ingatgystl ltnvgeiekk gvefrvfgvp lrtqdldwsi satyanlakn dikeisekyd
      841 iqrlnvagvw gstmpylvhq egmrwgqiyg ngikrnaegv pilnedglye ndpavffgsv
      901 vpkhtggvqn tfrykdftla anidwsiggk fvslsnmfgs ysgltartat tndkgnpird
      961 dvndgggvrv dgvdkdnnpv thyvgaqdyy hwlndnktyd dfvydltfvk lraisigyni
     1021 pvkklgwskv lrtasvsvva nnplllyakt kdfdpsevsa lqgetgqlpg trgfgfnlrf
     1081 gf
//
LOCUS       WP_099370671            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099370671
VERSION     WP_099370671.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117342
     Region          24..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkvlsilv lcvllvgvty aqnreitgkv tsssdgspia gvsvsavgtt vgtqtdeggn
       61 ytltltepat elsfsyigys sqrvsisnqt vinvqlvrnd ealdevvvta lgisrdkksl
      121 gyasqevkgd vlnaarggnp lqslsgnvag avinapsssl ggstrivlrg igsltgenkp
      181 livvdgipmd nsnynnpntd rgaggrdygd tgfdinpdei esvnvlkggp asalygaraa
      241 ngvvliktkn akngrdeiif ntgvgfeslg itpklqklyg ggfetdfatq midgkeyklv
      301 dytadeswgp kldgqevlhw dafdpedtqn ylktrpwvyp skdyrsffnt gvsytnsial
      361 akayentsar lsasnvtqsg ivpnsdlkrt tvalsvnnkf gekltatgti nyirtngynr
      421 peqgygsnsi gqkmfqwgqv qldydrlkny ktslgeqktw nrtawnnatp kysdnyywiv
      481 neniatdqrd rfygnvelky diapglyatg niygdnytlk itertavgsq pvseylenir
      541 eftemnyear vhydkkwedf slnafigtnr rnttralnnt stngglivkd lysisnssqa
      601 psalvenfkk rvnsvfgnfs fgykdflfad fgwrndwsst lpkenssyfy psvtgslvfs
      661 qlvkadwlnf gklragwsqv gndtdpyrlr diylnttyan ttyignpyfl kslskmneel
      721 rpeskksyef gvemqmfqnr vgidvtyyne tttdlimnvq tgpetgynak fmnagkmnnq
      781 gieamltlvp vrhedyewts ninfsrnrnk lielyddiqt ltigtapfna sliamvdqpy
      841 gqiyttdiir dsngtpvvga nglylgtdvr nlgtilpdfn agwrnsfryk afnlsalidi
      901 qkggkfysis nmfgsytgvl eetaangire egiivdgvtg dvtrnpdgty tvtntaknet
      961 rvdaetyfnh fyggptsqnv fdadyvklre itfgydlpts ftsklrikna tisafarnla
     1021 awglanknfd pemattgsgn iqgfeggnlp asktfglnlk lqf
//
LOCUS       WP_099370679             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099370679
VERSION     WP_099370679.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108275
     Region          30..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mirdfyswhf rliiififsf qfvsaqqnlq lsgkvvddsg nvlagatvsi kgqnkqvssd
       61 psgnyvlqgl sagtiiveas yvghstseqt vnlsssqtld ftlssnaaei gevvvigygs
      121 vekkqvtgav snvqskdfqk gaitspdqli qgkvsgvsit snggspgags tirvrggasl
      181 sasnnplivv dgnplsgdnv pgsasplsli npndiesmti lkdanataiy gsrasngvil
      241 ittksgkigr pkftlssvns lstiasqvnv ltaeqirsfv nekgtdaqkg llgsantdwq
      301 dliyqnaltt dnnvtmsggl knmpyrvsig yleqagilkt dlmrrgtmgv nlsprfldnh
      361 lkldinfkgt mtnqefansg aigsaivfdp tqevydptsp yggffewqeg avpnslsprn
      421 pvsllenyrn rgaakrsign aqldysfhfl pelhanvnvg ydiaagngat tipfyaasnf
      481 ankgffqryk gksnntfieg ylsyvkdies insnvnvtag ygyydnketk ynfqsfnsfd
      541 evittptfpd dvqqnrllsy ygrliysfad ryilsgtira dgsskfnpdg rwgifpsaaf
      601 twrikgenfl kdnnsisdlk lrlsygetgn kdgianygfi psyyyssnea qyqvgnqfyh
      661 vyspiaydat lrwestattn igldygfwgg risgsidayh kktkdllati eipvgtnysn
      721 qlltnvgnme nrgvegsini qaiksdnfnw digfnmtvne skvtnltlne npdyqlaagw
      781 itggtgnviq yhtvglapyq yfvykqvydq qgqsmegvye dlngdgavtp adryyykkpa
      841 pdyfmgltts inykrltlnt vlranfgnyv ydnissnfgv arnilnpsrf vnnattdiyn
      901 tnfnnnqyys dyyinnasfl rmdnlgliyn vgnldkagtv tmtvnanvqn vftiskykgi
      961 dpelfngidy tmyprprvys lglnfgf
//
LOCUS       WP_099370765            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099370765
VERSION     WP_099370765.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122666
     Region          31..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlyyyslr riiaiiflsc itfaaysqsl lrgavtdqdg kplegitvsn qtqsqttqtd
       61 lrgnfsitak isdvllftsi gyesqtitle nlgslrifmv ptgenldevv vlgygsikks
      121 nltgsvsrld krvletgvrs npasalagti pglrvqqtsg rpgavpnivl rggtsytggg
      181 splvivdgli rsgfqdinqd diesidvlkd asataiygar asngvvlitt krgkegvsni
      241 takakigmns lnipfdflna edyiywsrks iqtsgiynpt qlnqltsavp fgtgnkykda
      301 ngnildgnvt nqavwstmfl ddtnrellnk gwrtmidpvt gkeiiftefn ygdqalnqna
      361 liqdynvamq ggndkgkyya slgkyyeegv pvktfydrlt filngdykik pwleslsgln
      421 fantkwrdan naeanymtra lgapptmrgy nengdlligr dnwdgnvmvn idkfirnnen
      481 qkltlsqgfn ikfseklnwk stgswylnqs mneafnkdyl nspgnwvrsr nssagydktl
      541 nqtynsvlny rdsflgkhnv damlgweffd synkglsasg sgaptddfmd laltsvdnlr
      601 sidsyhnryr insffgriny dydqkylltl tarrdgystl lnnrwgtfpg isigwnlhne
      661 emfsnfigqd qvvntlklra sygangdigp vtannrgyyy lqgrygtsny ngavgytmnn
      721 psnfglkwes litkevglet rlvnrldlsl ayyhrttfdk iaelvlpvta ggfpiltnng
      781 dmqnqgveid lnynilrnsd wmlnfnlnta ynankvlklp nngvennrqg gfqvydsvtk
      841 dliwvggiqe gqdpniayay qaegiirtqs dldnyalklq dligaktlvh pdvfegmsas
      901 ekalhypial gdvmwkdvng dgiinsydqv yqgrtvprwt ggfgiysswk nfslstrfdy
      961 algfvqydgp rawfmgmmqg tfnttqdvfd tytpentgak yptyyfadql fknntsrmss
     1021 mffnrgdyla wrevslsyrl prsiaekakl edlslsvtgq nlhywskstl fspesgsigq
     1081 ggggyplprt vifglqltf
//
LOCUS       WP_099371124             988 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_099371124
VERSION     WP_099371124.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112650
     Region          68..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msvlwkfksl lifmsmsvgh ahshnanfsn lslqdttetd svpppidtla elkpiyeldl
       61 pkfnnlrnmk gaslitansl qqyikgelpg vyvsesngep gtniqmfvrg iskpilsnrd
      121 iyasqplvvm dgvpligehp fafdiqnydi erigtennll snidfdnies ikvlkdlsav
      181 atygplaang vieitsrktp sdgqkrisin syigmsqrpn vttingayen afrkqfydly
      241 ttngrfnddd vypiylsdsl nndyygpsnw sdsyyqngln hgvnaniagg qpratfqfsl
      301 gnvktsgvad dtkfdkynar fylnlrpfkw lnfetlfnaa risrdrnrnl rnrfammgyf
      361 pdlgaplapn kevydtylqe fdksfdknfn nilegffrfq vnvgpfklks kfgvdynegy
      421 rdlfypstil ensnfasnyy gynqrlmvdn qisydkengs nyfyaevgnn lvwdtykyny
      481 ayaykgvndf iklnlletdp yddeylnpta fprqlvykfl drtkhnminf ygkasytyng
      541 sytaalilry dgssnaqpts rwffspilal gwnakndlmk eneavslfni rasvgrighy
      601 nlfdnysqgp sytaqfgytg nsivpgyngi avlvrpydvg wvgydlpwsy sdninigfdl
      661 gfknrniqvs ldayirdtkd qlimlpgkkd fgyqyqyesg mdvrnmgidl sasgnviqnd
      721 kvtwntgvvl gvntnkllal pfgydqievn drllkigeri dafwlyenng myqtdkevpe
      781 ssgqkmtyng ivlkagdpiw ndsngdnqit kedkviqgni ipklsgswnn mvayrnfdln
      841 lnfyfnlgrk ivnqemanrf nfienenass insikeityw ekrgdydqyp lynpwssvsp
      901 fqtnqtlfle dgsflklrta sigynfkdii gnrlgklgdl yvyisannll tlskysgrdp
      961 elvnymgydq gyslpiprty algfklkl
//
LOCUS       WP_099371127            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099371127
VERSION     WP_099371127.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116708
     Region          24..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkkliili lsifslqias aqnqevrgrv vdesnngigg vtilnaannr aitatsdngn
       61 faisvapntt llfkavgfaq rritvrpnqt slnvqmsstq dqveevvvrg yvarkketst
      121 gssyslgekd lrdvpvanle qlmqgkvpgl nvqvntgapg frgstqirgl stltttgsgs
      181 esilmptspl yvidgvpmda draaefglqq qgpgisplsl ippedvqsie ilkdaqatsl
      241 ygsqgaygvi iittkrgnsp vprinythst fmktppklre tlggnlerqi klaqilnnsr
      301 yeieidkime tpwladslna yynnstnwqd lyyqntfnqn hnlsldggne ilsyksnigy
      361 fnetgviknt gfnrysanlr mdyrparrfe ftgqvfaqlg kqnkgdgtgi lqtgvssggm
      421 nstllpppgf ysasadyisa irtkndnssk lirpyvegkf eimpglriqs alsyefasnn
      481 edkftpaaaa gqfsevysfa gresnlynrn ilnytkdfne thnifinlfn evrhaqrqnt
      541 itkqartpnd qfegplgfdg yfsrgggvls nfrnekalsf alsasygyks rylldlsyrl
      601 dgssangfen qytknpaigv rwnahheewi ksipwinlas irltwgvnvm ptstleriyg
      661 kynisglynq ipgigidyef ipnpnlkptt smqynagldl nlfnnkveii ydtyykkvdn
      721 llfesflsne vgfdklysnd agvanyghef ainlrplssa sdfswtfsin gaynrdvllq
      781 lpssfrgqfi kwgdsweqlh mvnrvgtpal snylmqnlgv yatdadvpvd pltglryrta
      841 dgtffkagdp iyldrngdyi ldqrdyirsg stqplwtggv qntlnyknfq fsiyasytas
      901 rtilnyalaq rlglytspfg lqtvvpidgl nywkqegdna qypnpfdfsr slsvqpfryd
      961 qtlweesgsy fkinniiiay vfdreflrrf kldrfriyas mdnvytfsky sgpnpenvss
     1021 lgrdlssgyp vpraytlgfn isf
//
LOCUS       WP_099371171            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099371171
VERSION     WP_099371171.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118309
     Region          30..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkakdklfrw allailvyfv qpaiaqrpki diagtvretg sssplslvsi rwqgseaatd
       61 gdgryaisas vgdtvtfsrm gyssemlvvp isisgprdif lrphvnried vvvhsgyqal
      121 nqkdlagsvs fisqgelern pgmnlldrmr dmvpglvfnk nttlkqqgrs isirgqstmf
      181 anaeplivld nfpyegdiqq ispedvesit vlkdaaaaai wgaragngvi vittkkgsre
      241 grpvvdfgin ygwsgrpdln yipkmssrdy igvermlfek gfyrsaessi nhapispave
      301 lliahrdgkv sshelqegia nlekgdiyad lsrlvyrpsw sqryhgslrt gtavsstmvs
      361 lgydrqagel venglqrltl slnqsfslwk grlqlepfls ysstatsspn rvttdlkfgn
      421 apiypyasll dpdgspsvig rdyrreftdr aegdgmldwg yrpllepgni eslqkdrqlr
      481 lgfqanfkid rhlsmglnyr yvgrsmggst hygpqsymar nlvnnyssia ggkveraipl
      541 ggimdrtged gnghngrlql qydrqwdsgs lkaiagaeis nshslwtqyr lygydaqhes
      601 slpvdymsay rlysnpnssq ripyqnssrd ltdrflsyys slnylysgry ilggslrldr
      661 snifgvesnq kgvplfsvsa gwnlhkerfm lplaesfqil kirasygltg nldnslsayt
      721 tsrlnpsiss ssglryayiv npanpelrwe rvhvanvgld lgllenrvvv nldlyrkvgt
      781 dlignapfpa ssgiirfygn tgstqtsgid llldgsyeig pvglrsvlll shirdrvtsy
      841 kveptvlnll sggyagnypv vgrpltamya lpwagldpqd grplgllege ktrdyaaivq
      901 ttsmedliyl gssrpslsgs lrqefgygnl slsigiayrl gywfrrssvn yntvlsgmgg
      961 hgdfaarwqr pgdesttqvp smpqainfne vtfyqyarvl mepgdhvrlq dirlqyalaa
     1021 qslfrraaff lyvdnvgmvw kktgsdldpd yplsrplrsf siglkldl
//
LOCUS       WP_099371173            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099371173
VERSION     WP_099371173.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123188
     Region          68..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqnktfknai pkffirsssa vkpfinenhc lkenflfpil ltigffllgh qlvaqenlsm
       61 gtkgklatgt vldavtgkpv qgvsirglev eaktdsmgrf qlpsdsserk islshvgnrd
      121 tavlldpstl pmeimlvpva nmieqvevvs tgyqqiprer atgsfalvds rtlqrspsmn
      181 ilsrlngvtn gllldrntgn adgmsirgrs tlfsstrplv vvdnfpyegd inslnpsdie
      241 svtvlkdata asiwgvrsan gvivittkka ketfsaefss nltvsdrpdl fyqkrmgsae
      301 lielesflfs kgeytralns syedvspvvd vldrlgkgei ssgraegllq qyagvdnrkd
      361 lseifyrpkf eqqyylglss ssrsvrstms vgydrslket vsvdqqrlnl rassqwkdas
      421 drfgaemnlw ysgnsnsngn algfsprfpy erllgddrap levsaagtlr ksytdtvgng
      481 mlldwkyrpv eelrgewnsy srsdrslryd fgargaiyrs lalkvnflss tgwqdwstly
      541 dpssffvrnm vnqfssidps tgtvtrpvpl gaimdrgtvr sdsrygraql dwnetlwedh
      601 rlsgllgaew rqdrvrsesp gyiygydrdl enfaevdifs ffpiyhngdy rrierygslr
      661 rqvdnnrswf glmsytfkdn ltvtasarkd asnifgvsan qkgvplwslg tsysfqdllg
      721 wppldrlklr vtygyngnvd ksttafltsv lyqnrnlwgs padritnppn salrwervsn
      781 lnigldfqal gnrfggsley yikrgkdlmg nspiapqtgv tefygnvart ktrgidaqvw
      841 vdwvrsgaar frtdliynht rdrvvdyyaa tstnsdvvta sgifpiagnp inslvlyrsa
      901 gldhkgdpmg ylggkesdey sgilngferd alivmgsmsp thygslrntl sfngfeisfq
      961 llyklgnylr rtnsmnssel iagrytfsdy hrrwqrpgde attqvprfvy prdlnreefy
     1021 qhssvlaysg savrlqdlrv syavlpfash rkaelqlflh annlgiiwra ngegldpdig
     1081 dgipspfemt lgiklnywk
//
LOCUS       WP_099371705            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099371705
VERSION     WP_099371705.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118616
     Region          42..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msktsmkfcv pllalllnan geslasshlp ylqvvqkdqq lidirltvvd kssgepiegv
       61 nimvgnrqig stnasgvfqk evikgteisf krigyaqssi kanknnirve lspldeside
      121 vvvtalgikr dekalgystt tvkgeqltea lssnwmdals gkvaglnlmr snagpvgttk
      181 iilrgennit genealiivd gvmvnggsgr rsaldsdnay gvssenmpvd ygsgmddinp
      241 edietitvlk gpgaaalygq raangaivit tksgskkdkg igvtvnsnvs fesmnrspal
      301 qyeygqglgg sahysygpse dghstagtss aygpkfdgqk ffqydpktqt vglertpwra
      361 ysgkngvnaf fdvgrtytns vsidgstdkt tarfsatnvq nkwivpntgy krntfaisvn
      421 srvsdklqin tkvnynnrws dnlpgsgygn qslmywyifw qpssdinglk dywvkgkene
      481 rikypfssyp enpyaivnef insnnrhvit gnaqttyqfs kelslllras mdlstenrfq
      541 nrpydagsrl pegshrtqai fgketnadfl lryqkeinkd fdfsitagga tlaneyrrde
      601 lasdgltfpg efnhsnskyg vrskqriekf etnsfyglmt aayreflfld atarmdwtst
      661 lhssafpdkk vnffypslng sfviseianl peiisfakir asiagtgsga qtpyltnfty
      721 qvgnpliggs ltnphllvnp llkplktnsl efgadirlfk nkvnldvsvy kansfnqhlr
      781 rivdassgvn rfimnvgevq ntgleialnt nqiknanfsw sslvtytanr nkilelsdss
      841 iviqarsigl gqiighvggs mgdmfglgyl rapdgqiiyd ertgyakltn yliplgnnyp
      901 kgklsfgntf nyrglklnll fdtqwggvah slthyklaeq gktrntlpgr ysgiigngvl
      961 qnpdgtfrkn dviatnidqy yrshfgpdna egnvfptdfl kfrearldyt lskkltqkin
     1021 vnratvgiyg rdlfiwtkwp afdpefgtld gpdvvkgfei aqfpstrtfg fnlivgf
//
LOCUS       WP_099371946            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099371946
VERSION     WP_099371946.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124100
     Region          42..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meiltktiis lknsslgiwi fillivflqp shvigqgnsn rikveglvid kntkkpiiga
       61 gvsllgsnsa ttvtdqqgrf tiespgngil kisflgygsq nipvnnrsel eilleestte
      121 mdevvvtalg itrqskslsy aqqsvdvesm teargsnlme mlsgkaagmq vvsgggplas
      181 trvvirgnns ltgnnqplyv idgvpvmngs gengdldfgn pvnsinpdei enieilkgan
      241 asalygsdaa ngvvlittrk arqkqglgit ygfnnmighl ynyptyqniy gagqsnrfkr
      301 egmnyfgnsg nglsfdpelp ygiwnpnmgn qdqrswglpm lgfdvvgrng qiksyvpqpg
      361 tieemyqtsn amtnslsvdk ltdqlalrfs ytftdsddil ekfniykrhn fnlnnntklt
      421 nwlnidanlr ytledvtnrg frsasnrnpi yvitnlprda sqselvpwkq edgkpfnfrg
      481 fsnpywllne tsnadsknlf agnltmnlrl skkfnmrirg atdvqqsdgw dftnlyspfq
      541 idgsyfkwkr mavnnnfegl lsysskiqnd isvnanlgas lqhidgdrmt skvnmlmykd
      601 qktltnsrip vsslefperk ekqaiygmts wgykdyafle ltarnewsst lpvnnnsyfy
      661 ysigsslvis dmfeslkgrt lgfwklrgsf aqvgndtgfd rlrtgyyrpe ngsflglpyf
      721 vgedvlkngg lkpektqswe lgtefrlwdn riiadftyyn krttdqivea dallasgyrr
      781 eilnageikn wgtevslsit pvksnlvtwt stfnwsknns rvvslldgvn ryemgsgdni
      841 klyaevgkpy gvfygndyrr gpegeiyvat dgkpsmdpdk ylgtvlpdwf ggwinnlkig
      901 kfelgtmidf qkggrvwsht afrggidgnt iqslegrweh iladlilgen geerkgflqp
      961 ghtvmpgany nensvlypdw erpkgvhlgn svydpslvge ywagkesiaw vspmdhwthn
     1021 nqssaaryiy dasyikirev slgfnlpndw ltktpfrnak isavgrniai lfqntpkgld
     1081 pqatstsgna qgfergfslp matygvdfkf sf
//
LOCUS       WP_099372389            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099372389
VERSION     WP_099372389.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111399
     Region          23..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktltflml wltaiqliya qerilkgtvv deqskapiag atvklipnnk atatddsgnf
       61 tievpagtig vnvsimgynq vnqsitpadt sitislaaaq ankiddvvvt amgvqrkaks
      121 lsystqtvkg eeltkvkdan pmnnltgkvs gmqinrsssg iggsvniilr gfksnrnnqp
      181 lyvidglpit ntggsgsega fggapdrgdi lstlnaddil sinvlkgasa salygsqgan
      241 gaimittkkg aegnlkidvs ssitadqafy lpklqyryaq ttegseeswg ekgsfndpvk
      301 dfyntgttli ntvslsggte kmqnyfsygn tsnkgilptn sfnqhsatfr nstnffdnkl
      361 sfdgsmmysr qdihnrptsg lyfspiagly lfprgldfdk yknfeylsts rnlylqdwwn
      421 inadagltgt hhsqnpfwvl nrnptfqlrd niiaqgqlky tindwlsvsa rgtlnkrwdk
      481 ferhvyagtq gvlsgevieg vlqdngrfir detestalyg dlllignktf aedwdlnfta
      541 gtsindtksn gwnldqlkla vankflmsni yreapinvln esisrrqlqs lfasanlgfk
      601 dkifldltar ndwsstlant pemkkgyfyw saglsavlsd mvkmpafity sklrltmaev
      661 gndvgiysti ptntlatgil nanvsgpyqg lplrpeisrs fevgyegrfw ndrinfdlal
      721 yktntkdqyf syqapvgqvf ttvflnagnv enkgieaalg idaikkenfs wntsvnftan
      781 rnkilelapk lgerysiggn fnvlrlngsf gdfwartflr dengvmvvdd tgrpqigpeg
      841 yvgnnnpksi igwnntfnyg kfglsftida rfggqvisvt dgylnsfgvs eesaaardag
      901 gldipavkmd gtpwegkipa qayysavgnr dgiiegqvyd atnirmreis ltyglpiqwk
      961 gvksasislt grnlfffrnd apydpelntt tgvgaqgyds falpatrsyg lnlkvsf
//
LOCUS       WP_099372402            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099372402
VERSION     WP_099372402.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115934
     Region          27..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklptclsia vaslcsiqml saqqlsiagk vtnangepia gasifvkgtq tgtasnengl
       61 fnlnapsdgt lqiravgyap levpiagktn fnvqlqqvdd aidevvvtal giernpkslg
      121 ygaqgvnsat lnankqsnlv nalqgkiaga nisstggapg qganiqirgi nsidptrpsq
      181 plfvidgilm dnststqggt aevrgmsnra vdinpddiet inilkggaat alyglrgang
      241 vvvittksgk agtikidyqg tvgfenvnkf pkmqdtysqg wqgvynkddf wpafgptvee
      301 aikldpthpa qlykpfeeaf dtgnqfrnsl sfsggsekft fltsisqlkh ngvlpatdfk
      361 nlqarlntnf tineklkgts sisvnnsggy rgnanryaeq liywsprhni rdyvlengtm
      421 nsygetdnpi yiahtnrfkd dvlrviggfd ltyspakwvd lmyrigvdty rddreataig
      481 yqgltderiv ydngvegadg rgfynvynnn yralnstfia tfkhqfnedf ggkvrvgqdi
      541 ydqvtkrnat eggdltvydw fdlgnanilk sssynekyrl mgffgelemt ykdylfltlt
      601 srtditstln pknraftyns aslsyvfsdh iklpevinfs klrlsyagig kdaapystsk
      661 gfgpytslpt gyigftrpal lgdenlkpef tntieaglem kfynsrlgfd lnfynsvskd
      721 qiikvpvtst tgyvtaaina gsirnrglei tlntvpvkke nftwnsdinf sfnrnkvlei
      781 redlddeivv ssefgylsst vsmrikpges ygtlygrtyk ryytpeeieq gldktreydd
      841 srplligang fpvlestsvp kklgnvqpsw iggwnntfny kslslnvlfd arvgqyrynq
      901 lgnfmaafge adytenrndy tvfdgvtadg nkntkevwlg qgkdpkngvn ygngyyrdyy
      961 rgnsqffved aswlrlrsvs igyglpqqwl enkfiknari svtgnnlllw tkysgydpen
     1021 sttasgsnie gfagmtypav rsflfslnvg f
//
LOCUS       WP_099372556            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099372556
VERSION     WP_099372556.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118927
     Region          43..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknhftkisk lglllmlgls yttharanls hfpmsefsaq evidvkitvv daktgnplng
       61 vnimnnnkai gftnsngvfq gsvlkgstis ikmigynats fkaekdnyti qltevdesie
      121 evvvtalgik reeqalgyaa stvkgeqlte alsnnwmdal sgkvagvnlm rsnsgpvgst
      181 kiilrgennl tgenealivv dgviinggsg rrsalgsdsp ygtgsdnmpv dygsgmddin
      241 pediesitvl kgpgaaalyg qrgangavii ttksgtqksk gigitvnsnt sfesmnrspe
      301 lqyvygqgld gaahysfgst vdggstsgts saygpkfdgq effqwdpltq kvgesrtpwr
      361 aydgkngvng ffdvgrtftn svsidgstdk ttarfsatnv qnkwivpntg ykrntlalsv
      421 nskvtdklti nskinynnrw sdnlpgsgyg nqslmywyif wqpsadinwl rnywvngeed
      481 rkisypfsty penpyaisye finannrhti tgnaqasyqf spnlmaqvra amdmstedrn
      541 qnrpydagsr lregsyrsqs vfsretnldf lvrynkeine dfdfsvtagg stlrneyrrd
      601 eltsdglfyp gvynhgnary gvktkqiiek fetnsiygli ttgykeflyl datarmdwts
      661 tlatiyypdk klnffypsin gsfvfsklwe lpefinfgki rasfagtgsg vqrpyqtsfv
      721 yenpnsligg alsnptslvn plirplrtts lefgtdirml knrikldvaw ykansmdqhl
      781 yrfvdpasgv srflvnfgev enkgleisln tdqvkkddft wssmltfttn kneikqltds
      841 sivlqqrsvg sgqivgmvgg slgdlygigy lrapdgqviy destgyaklt nqvvylgnti
      901 pkgkasfgns fsykglrlnv lfdtqwggvg hslthyklae qgktvntlpg rysgmigngv
      961 iqnadgtfrp ndvvaknide yyrshfgqdn aegstfptdf ikfrearldy slsknlvsrl
     1021 ginratigvy grdlfiwtkw pafdpefgtl dggdivkgfe iaqfpstrtf gfnlivgf
//
LOCUS       WP_099372676            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099372676
VERSION     WP_099372676.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118836
     Region          24..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhnllsfvl lfmlsiglvn aqnrqlsgrv tdsgdgspla nvsvrvvgas tatqtnaqgn
       61 ytltvsensk vefsfigyqs qtqsvtgrst invslvsssd eldevvvvay gtvkksdftg
      121 satqigskei dkrpisnvlt alqgagpgiq tstpsgapgs sptirirglg sysagqgalv
      181 vvdgvpfdgg maninpadve svtvlkdaat iamygsrgan gvimvttkkg nagkselnvs
      241 aqygfnengv payntvdagq yyelmwqayt nnlaygstai pidiarqlgs gvlprndkgl
      301 qlyngktyqd ivqylgnyna fdvsnetlvg vdgklnpaak fryegftswe deasrkgnrn
      361 eynvnysggf nstdiyssln ylkdngwglr ssnerfqgrl nvntkvtdwl ktgininaat
      421 inynfaadga ssinnpfyfs raiapiypvy vhdpatgklv ydefgakryd ygnlvsefgl
      481 srpfnsgrha iaetmfnssa anrdffgara yidinilpwl tfsttfspdi qnyksegyen
      541 tivgdgapag rynqswnrql sytfnqllra nntfgnhnle tvlghefysy kyesiygmrt
      601 gqgfqgvnif enftdisslt sginenties yfgrvnynyn skyylsamir adgnskfpsn
      661 lrweefwslg aawrldqedf fkndyvnllk lrasygklgn sdvgyypyqn gyeigynnas
      721 tpgsifaslg sdnltwetqk pldfgvdfsl fdnrlsgsfe yyyrnsdgll fsvnqpyhng
      781 gtwagsfavq qnvgamtnkg ieatvtgnli rkpefnwnlt fnvttvknei tkmpvetpei
      841 vsspykravg rslydfytrt yygvdpetge glylgledgv efdpdnathr lidngngrvd
      901 tvttnqnaar qswlnksalp pvygsiindf tyknfdfrfv ltyslgghfy dgyygglvss
      961 gpanganlhq dllnawkepg ditdvprmdv grtaqhgats sryltkasyl nisainvgyr
     1021 ipevysnrig ikrarvyasa enlfywsakk gfnplggitg ptgnssytha rtinfginfg
     1081 l
//
LOCUS       WP_099372774            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. 1.A.5].
ACCESSION   WP_099372774
VERSION     WP_099372774.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. 1.A.5
  ORGANISM  Sphingobacterium sp. 1.A.5
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Sphingobacterium sp. 1.A.5"
                     /db_xref="taxon:2044604"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111846
     Region          52..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikrfsspff ilkkrhflag slvislclns gftvasdfas etigvtaqqe evkgkvssgg
       61 aalagatvtv kedpsratst nesgdfaina kvgetlvfta ighdpkeiev agptmnvelf
      121 snlenidevv vtgystqkkg eisasivsld qkqlkdvksp nvsnllqgkv sgvdvvgtgr
      181 pgqqanvrir grsslssgtn plwvvdgvim hgvpninpnd ienisvlkda aattqygsrg
      241 tngvivvttk ralregegvf svnlssgvsk fnqgnfklmd sqqlwdfyqt fpnqkdidpn
      301 vtdevlgtny dwmengikag avndfaasym gktektsvya sanyygekgs ikgydyerlt
      361 grfnvdhklt dritfkpkln asyttylnke hslydmmlnl pwdnpfnadg svknpqdesa
      421 dfvwfgrdhr nylydrqyny gkgqtfdmqg nfdfsyrisd rftfesmnnl tyynqttmny
      481 adpksnagrn ekgtinqfsd kritrffnqm lkydetfgnh kvsgfaayey sdytysslna
      541 tgkgiapgse ilgnaasvln fggtkndysf qsgilqgtya ydnrynlmas frvdgssrfg
      601 knnqygafys vsgawnihne effnvpainl frlkasyggv gnvptyyyas ygtyglnaqy
      661 ngdpaaiqqn fqnanvswek sydanvglel gflnrinlsv dlyhkntsgl lyyvefpsta
      721 gwdgywlnig glrnkgveva lngsvfgpes pfqwdlgfnv ahnnnritsl nedqdipkgn
      781 qrfsvghdve swymrkwagv npengdpqwe aidpetgevt ltsnyndaal qfvgaatpkf
      841 qggfnsamsy kgfnlnasfa yqnggmtynt arewfdsdga yasynqlifm dgwsrwspen
      901 pnathpraey nntslsnkvs srylestnfl rlrnvtlgyt fsenlvnrlk lkglnvyvsg
      961 dnlwtstkfs gldpeaailg ndnsadkagg gdatsqypap krlifglnlt f
//
LOCUS       WP_099376259             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Janthinobacterium].
ACCESSION   WP_099376259
VERSION     WP_099376259.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38669
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qivvqsgagl qasipddaya aagaqigtaq
       61 eaygcaivlk vrapdagera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeek eiakgaggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvlkhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_099389220             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Janthinobacterium].
ACCESSION   WP_099389220
VERSION     WP_099389220.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium
  ORGANISM  Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium"
                     /db_xref="taxon:29580"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38730
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qivvqsgagl qasipddaya aagaqigtaq
       61 eaygcaivlk vrapdadera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvlkhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagseilrk
//
LOCUS       WP_099399194             394 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Iodobacter].
ACCESSION   WP_099399194
VERSION     WP_099399194.1
KEYWORDS    RefSeq.
SOURCE      unclassified Iodobacter
  ORGANISM  unclassified Iodobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chitinibacteraceae; Iodobacter.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="unclassified Iodobacter"
                     /db_xref="taxon:235634"
     Protein         1..394
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41414
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mliaipaevl pgefrvaatp etikklikag htvrveskag qhaaitdtay teagaeiapn
       61 paalyqgaql ilkvraplah elpllperaa lvalfdihry dhldalnakq isayalelip
      121 ritraqsmdv lssqaniagy ravllatqyy prfmpmlmta agtvkparvl ilgagvaglq
      181 aiatakrlga ivevfdvrpa treqveslgg kfievalnnd ekaaaetsgg yaremsddyk
      241 lrqsllidsq arladiiist aqipgkaapi lipaetvagm kagsviidla vdsggncpls
      301 ksdevvhsen gviivghsnl asllaadasa lyarnmltfl sllqdaegay aphsddeiik
      361 atllshhgeq lfgrapahaq gaiashtsqp tana
//
LOCUS       WP_099403966             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium rivuli].
ACCESSION   WP_099403966
VERSION     WP_099403966.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium rivuli
  ORGANISM  Janthinobacterium rivuli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium rivuli"
                     /db_xref="taxon:2751478"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38757
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qivvqsgagl qasipdeaya aagaqigtaq
       61 eaygcaivlk vrapdaeera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvvkhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_099405871             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinimonas sp. BJB300].
ACCESSION   WP_099405871
VERSION     WP_099405871.1
KEYWORDS    RefSeq.
SOURCE      Chitinimonas sp. BJB300
  ORGANISM  Chitinimonas sp. BJB300
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chitinibacteraceae; Chitinimonas.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Chitinimonas sp. BJB300"
                     /db_xref="taxon:1559339"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39172
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipkesa tretrvaatp etvkkyialg hvvtvqsgag vasaipdtaf feagaaiaad
       61 yaatvqdadi vfkvrspaae eigalksgaa vialtdphrn alladyaakq ldiyamelvp
      121 rttraqamdv lssqaniagy kavllatefy prffpmmmta agtvkparvl ilgagvaglq
      181 aiatakrlga vveafdvrpa akeqveslgg kfvevplnea ekkqaetagg yaremsddyk
      241 arqaalvdkh arnadivitt alipgrpapv likpetvagm kpgavlidla venggncpls
      301 qlnevvttdn gvklvgyanl pglvaadasa lyarnlfnfa glildmekgy vvnreddiva
      361 aslvthggqv lfgksa
//
LOCUS       WP_099411321             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium sp. BJB304].
ACCESSION   WP_099411321
VERSION     WP_099411321.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. BJB304
  ORGANISM  Janthinobacterium sp. BJB304
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium sp. BJB304"
                     /db_xref="taxon:1572871"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38657
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qvvvqsgagl qasipddaya aagaqigtaq
       61 eaygcaivlk vrapdagera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvvkhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_099426224             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chromobacterium violaceum].
ACCESSION   WP_099426224
VERSION     WP_099426224.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium violaceum
  ORGANISM  Chromobacterium violaceum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Chromobacterium violaceum"
                     /db_xref="taxon:536"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39607
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnivipaerl agehrvaatp dtvkklvaag havtveqgag laaalpdaaf laagagiaeq
       61 rqamlaaadi vlavrmpeaa daaalkpgav ligmlapyqn pllpqlaaqr vsafalellp
      121 rttraqsmdv lssqnniagy kavllagqfy prfmpmlmta agtvkaakal vlgvgvaglq
      181 aiatakrlga vveaydvrpa treqveslga kfvevpmsde ekaasggvya remsadfqar
      241 qnaliaqraa aadivittal ipgkpapqll saeavagmkp gsvivdlaae aggnceltra
      301 geaclspngv hlvgltnlpa mlaadassly arnlhtflgl lltpeglkid leddlvaatl
      361 iahqgeqrfg aaarpaaanh dkepqhg
//
LOCUS       WP_099433569             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Citrobacter].
ACCESSION   WP_099433569
VERSION     WP_099433569.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53469
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 maritlrarr ffslivplff isavyaeqtp epaksvtvea knevfapqhp dqylswkats
       61 eqskredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc gdchntaspd fakgkpeltl
      181 srpyaerame tigkpfdkag rfdqqsmvcg qchveyyfdg kdkavkfpwd dgmkvedmek
      241 yydaitfsdw tnslskapml kaqhpeyetw svgihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf pqtcanchtq dkaslqnvva erkkainglk ikvedqlvra hfeakaawda
      361 gateaemkpi lsdirhaqwr wdlaiashgi hmhapeeglr mlgiamdkaa dartklarll
      421 aakgitheia ipdistkeka qaaiglnmqq inadkqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_099437034            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099437034
VERSION     WP_099437034.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116621
     Region          25..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrklllfsv iclffaqaai aqnlikgvvk dtrgvgipgv svsvvnakka tvtdfegkys
       61 ipaaadatls ftylgyisqn apvagkaqld iilqedsktl gevvvtaigi kqqkkkigya
      121 tqevkldvls esktmnigna lsgqvagltv nnptgmfqap sfslrgknpl ivingipvet
      181 dffdvsgdni aninvlkgtt asalygsrgk ngailittkn aendgleini ntnnmvtagf
      241 tvfpktqtey gngsngkyef wdgedggisd gdmiwgpkfq pgvkiaqwns pirnkqtget
      301 iqwygnvkgt iyddkskyer vptdwvrhdn lndflrpgiv tnndfsvayk gakaqfyasg
      361 kysfqrgqvp ntslttggmn fnssfnltsn lqldatlsyn kvsspnypry gygpknhmyt
      421 iliwmgddvn gkdlrdhmyv pgmegyrqan ynyawynnpy faseeltqst drnvlnaqak
      481 lrwqvtpdls lqarasgren ksfdnmkspk symnygdsrn gdykmwnnsq mnvdldflas
      541 ynkeiskdlt ftlnagastf nrdiqqeyas sdglivpfvy slnntqgpvq atnyleqksi
      601 rsvygsanfd lfnavylnvt grndwsstla kenrsyfyps aslstmvsdy ikmpkaldyl
      661 klytswakvs ndlapysifs tytkdvtygs ipsvsypngi inpninpeks tsyevglsts
      721 lvkkvgleft yynvidenqi idlstseasg fktrkvngnk yktqgleima nynavktqnf
      781 rwdiaanwst svkklteiyn nqakfgdlkl neradsfygt vwqksatgev ildpntglpt
      841 rdnfnvnlgh sdpswrlglq nkfmikgfdv nididgawgg vmrsvtiekm wwggkhpssv
      901 efrdaeyaag kaiyipegvv itggelkrdv ngnvlsdtrt ykknttavnw qtwsqiypyq
      961 arvtedenkk fanvfdrsff klrrisvgyd lakvikmgsl ksvhvsaysy nplmwkkmpl
     1021 ldpdygddnn lqdpsarfig fslsvkl
//
LOCUS       WP_099437090            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099437090
VERSION     WP_099437090.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112655
     Region          27..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkiykifag ilisffflqt vqaqsvkitg tvtgnpdget ipgasiiikg kksgtttdgn
       61 gkfslaadvn dvlsisylgy atkeititaa tatlnitldv asnalsevvv talgiskekk
      121 slgyavqelk skdiataket nlinslagki agvqttnsqg dmgssriiir getsisgnnq
      181 plfvvdgvpv dnsqnlgiag srdfantisd insediesis vlkgpnaaal ygsraaagvi
      241 liktktgrgq kglgisvnsn ttfsnlltlp dyqnsfgqgt sgkfsfvdgk gggvndgvde
      301 swgpaldgrl ipqfnskgva vpfiahpdnv knffetgyal nngiaiagsg ekqdvrfsyn
      361 nltqggilpn ssqdknslll ntsyritpkl tlnasanyik snadnlpasg gkratgpmlq
      421 ftwfgrqvdv sqlknykden gndfnwnnsy ysnpyfiaye ntvgqkrdri ignaelnyki
      481 tsalsanfrt gndyytdrrk ikiaygtngt pfgsyeeday tvnenntegr lefnkklnsd
      541 fsidilgggn irtstfeqnd qkatklavng lytlsnsrdp lvssnfyskl rtyslfgsaq
      601 lgfrdyayln ltarndwdss lpepnlsyfy psvngslilt eafdiksdvl sfakirggws
      661 kvgkatdpyq lintysftap fdgnpqqsan tidlnpnllp eitksaeaga eiglfdnrik
      721 ldlsvyntns inqilkvdvs satgytqkli nggsinnkgi eiqlgltpik qkdfswdinl
      781 nysrnrskvt eldkegriss ytigtsgtld vlaavgqpyg tffgtayqrd aagqvivgan
      841 gtplidpakq ilgkftpnwi ggitnsftyr nfnlnflvda riggkvfsgt nstgtytgvl
      901 astmrgrnae nggltyttgg vtyndgmifd gvladgtknt kvisaeeyyk attksneefv
      961 ysasyiklre vrlsynipsq wvkkiglqea nfslvgrnlw iihkdipnid petafntgna
     1021 qglesltlpt trsfgfnlnf kf
//
LOCUS       WP_099437208             976 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099437208
VERSION     WP_099437208.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..976
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107018
     Region          124..946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkitkafaw lymqptfkii llmkgalllv mftclqvsan vysqekfsls lkqtevsnil
       61 tkiqkqsnyr ffynyaslkk lgkvdlqvkd agihaimeal mgsklpykia ddhvviigap
      121 eaqiaikgkv vdskgetlig vsvklqgtni gattnlngef vinapengil eftyvgyekq
      181 vvnidgrtnl titmvetnsn ldeivvvgyg tskkidvtgs iasvkgsdiq nlpvstvasa
      241 legratgvni vrndgtpgaa psirirgtgt indanplvvi dgvpsgnpda lsdvnpndia
      301 sieilkdass saiygtraan gvvlvttkrg nysqklatsi naytgvskst kyidlltapd
      361 lytlkrerft ndgaaieapw ndayystqrt dwqkailgsg kvnnidlnlq ggnevstyyf
      421 stsfydekgi idksyfkrfs trinsehkik pwlklgqnlq vtygetngfn nndsqtgllf
      481 salrfnpaip tmnedgtygt skafanqlgd innpystiqq adaynrkyra ianvfaevpi
      541 fadlkfrany gfdgtigrgy sfniedriqt rettsstltq teaenyshll dlvltydkvi
      601 skshitftgg yssqsfrgsy fsagrvgfdd tskdqrtlrk gnafltadgs yddpsglesv
      661 fargfydydg rflatltfra dgsskfaagn rwgyfpafsl gwrvsnekfm kdiswinnlk
      721 itggwgelgn qnirgfqyas sivvgntygt ngytfggfgv ngsavtitan pditweraam
      781 tnvsleagfl dnklnttity fdkntnkmlv palligtagr vtapdinign mnnrgveaev
      841 nyqsgdsfky sfgvngsfik nevtklygvn afipstvygr ssqeisrtye gqsiasfygw
      901 ktaglyqtqa evdndpylkn dtrkgsikpg dvrfvdingd gmidggielt lvilirkqhw
      961 afrpacrtrd liylqt
//
LOCUS       WP_099437224             733 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099437224
VERSION     WP_099437224.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 733)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 733)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..733
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=82591
     Region          <8..732
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrteafknen ntpssnpvdp nyapdlkiwd tksftdwqne ligrtanydh idlsasggts
       61 niqylistty hkqtsvfpsd fddsrvslhf ninsistnkk lkiqlsgnyl idnnllpqtd
      121 itvtalllap napslynddr slnwmpnsig nstwtnplsv feltysnktr nlignsvvsy
      181 kilkniefkt nlgytdlqtn eyfgtplttf kperrsistr tasytnsift swivepqlnf
      241 eqfiaqgkln iligatfqen tsdgqrlqgr gyssdqtled iksasdisig stlstkyryn
      301 ayfsrfsynw qdkylinlva rrdgssrfgk enlfhnfgsi glgwvlsnee slkkgsaiis
      361 flklrtsygi tgndqigeyq tlslfkpnnl pnpyqqttgl tidnlpnpyl qwevtrkmnf
      421 gldlglikdr ilvnanyfin rssnqllpft lpvmtgfgsi tsnfpakvqn sgweislnti
      481 nfnrkkfnws snlnftavrn kllsfpnien tsygflyqvg qplsitklyk yagvnqqtgt
      541 yqiydregnv tsepdnlkdk vvvlntapkf dggflnsfky kdfeldiflq fvkqigpnll
      601 fgnttflspg ylatgagagn qpttvldrwq kpgdiasvqr fssnfsvase fdnakssdaf
      661 ytdasfirlk nvslswhlph siinkihlrt arvyiqgqnl vtitkykgld permnlsslp
      721 slrvittgiq fgl
//
LOCUS       WP_099438143            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099438143
VERSION     WP_099438143.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120118
     Region          25..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiylrclt vllfslitia ayaqkkvtgt vtedsgspip gvsvfekgtn ngittdgsgk
       61 fslnvsnnav lviryigflt kevevgtstn mtiklqaddk aleevvitgl getrdkrnlg
      121 yamnqiggeq iraaktinpi salqglvpgl vvmpgqggpq stpkfqirga sslysgentp
      181 lividgimls ddvvlpsrgg eqdfgnvlkn inpddiesms vlkggsvtal ygsrasngvi
      241 littkkgysq kglgfsfshd etfdkayalp dmqkeygsgf tptdfvktsn gmnqinpasy
      301 gfsfgpkldg stvldvdger qiknsvlnnp lslyqtgryi nnniamqggn ekttfrfsya
      361 nnfskgispn nkldrhtfnl rgtqrladai fvdgtvsysn trgfnpqrls gdnsliyglt
      421 wgyptnfdld ywskqyldpi nggrstndpf gtnnlffmln efsqlqsenn frgalnakvn
      481 ftkwlqletn aalnwyntnr evrelgtgvg faggyygsem rnffdsryra nlnlnhtvnd
      541 fdlflqggae ltrsqvksas fnsrgglrip rqfrlsnsiq dpqvyegapn iaqifatygq
      601 gtvtykqwlt lnlyarnewn stlvysngtg nysyfypgad aafvftdafk lpeffnfgkl
      661 rasysitggg tdvyranagy yvrsgnyapi tggdgieqyg fenstlgeln lkplrtfske
      721 igfelkmlqk rlgidftvyk kntknqiigl gtsiesgvss qlinsgntqd wgielslsgt
      781 piktktgfsw dtyfnytlnr tkiislapgv ttvqlsggdg irtiaqvgge ystmvaaygy
      841 akyqardasg kpiddpnngk kvlttagsgg avyvrasnya nglknesqig stlpkfygsv
      901 rnifnykdfs lstlidakfg gyvfsdtyyy gsqtgnlknt llgrtpqtgg teytdadgvk
      961 qvgvvldgvf aqgtkingvd vggmthqeti dkgmriptit wryynnsngw sagirergaf
     1021 ksswvavrdi tlgydlpksf aakikmngir vnvsarnvgf lynnapdnin indftgtgag
     1081 daflgggtpy vrtfgfging sf
//
LOCUS       WP_099437686            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099437686
VERSION     WP_099437686.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116194
     Region          29..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqvlkmhfr vlgiiwlllq shsafaqgki sgtvidakdk tplpgatiil qdgsgksktd
       61 engkfeinve agsklkismt gydaqevias rgmvvelvfs avnlddvviv gygtqkkdlv
      121 tgsivtmtme dtrrnsptts lgnllagqma gvkvgvpagr pgtapgisir tktsfndqnv
      181 lyvidglvtd nsadfnnlsp ndidkvtvlk daattaayga rasggvivvt trrgskneka
      241 kinysfnsgf dkrgrnadlt saietgqiyn rmnptnnpwt qsdfdyfkni nngwgydqla
      301 qvwqdpyttt hnlsatgggd kityfiggsy tkqgafqkns syknynfran itadiaknft
      361 vfagvsannn vsdrlpstgv gdengiyrkq llwqpeqpvw tdggkpidyg wignvgaevn
      421 geggynkenn fkpvinlkgt ykipfvegls vssqyirtia nnrkknyftk ydmwvmkllg
      481 ssrqistrde dllslkkssq ignnyleesy rwndneqlnf qlnydhtfgn vhhvqgwlty
      541 eraetkgggf kagrekfpvy qtdqwwaasg drldswaqgd sdfnrgaeqt vgrksyvgqf
      601 fydydskyla sftyrydgsy kfsgdkrwgf fpsgslgwvi srenffsnvn giellkirat
      661 agttsadnin awqyqqsydp gtsayfgstp vtnvgisygs lvnpditwek srnynigidi
      721 nflkhfsgsv eyfnaktydi lvdrvaqvpp tfsrklptsn ygeyksegve mtfgyrnktn
      781 qlnyyanina syaaatplvr dkvvtypwev dvnrsaskiv afvqtgmirt qadldafvaa
      841 npnykfkgia palgqltyad lsgkdgkpdg ivddwdktii kknnnpvllg lnfgaewkgf
      901 sidasfdgsf rnykyinnlv dgnvewnrmw kpwandawtp enpnatlprr ysandnvrtv
      961 tntestfwlk nasflrmrll nvgysiptsi tnkigingvk lyfsgsnlfv iskfnkkyyd
     1021 pqlgdgfsyp vmknfnfgin vsl
//
LOCUS       WP_099439042            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099439042
VERSION     WP_099439042.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116082
     Region          30..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkicyslkkt slftvvmwll tfgiayaqst itgsvvdetn qplagasiki kgnksgtttn
       61 tegkfsisap anailiisfi gytpkelnig sqtvlnikld pdqsaldevv vtalgvkker
      121 kalgysvqev kgadlvkare pnaissltgk vagltispsp nlfgdpgiql rgrsgvlivv
      181 dnvivksdsw nlspddiesy tvlkgpnaaa lygalgisga ivittkkgsk nsrgfavdfn
      241 sstqlqtgyn aipkfqteyg agdgfkyafk dgmgsgindn dyfiwgprfe gqpitqynsp
      301 kdpvtgelqp lpwlargknn ledflnngll stnnlaisan ndkgdirlsm sqtyqkgtvp
      361 nsqiastnfn vngglnvgtk lrfetninyn kqytknyptl gygpqsliyl itvwggtdyd
      421 ikdlrnywkp gkegievynr eytlynnpwl vayenlrgyy kndvygyfkm dysiskklkf
      481 sartnvstyd lnrdtrypfg gtfyspyskv ggyeqsysql wennteasln ysdtfkdfnf
      541 kgalfgnlrt isakeitgat kgglvvpgvy tltnskepns ptnrlaskqv asaysfvdld
      601 yksyvflnlt grfdrsstlp kshntyfyps aslstvfsem ftlpkaisfl kargsyanva
      661 gdlgdstnpy dvynllsvys vygtrwnnnp gvgysgtlyn pnirpsrvkt ietglearfl
      721 nsrvgfdvay frniegpgiv nvtvsnssgv ssiqknayty lrkgweitln gspikgqdfs
      781 wdvlanwsts hrwlrdidgv ltrdgnihlg dradgyyitd fqrdaqgnmi vgtnglpayn
      841 pyssrigyad nnfiaginnt fryktlslsf qvdgrfggli nnyldgyqws agthpesase
      901 yryldwtnrn dpnwkgsvmt ngqkivsgql stdqdgnvis dtrvfapndk pvlwqtwarn
      961 yyqsgyqlar nrtyvklrev vltynlpakl tertkflqsa sislvgrnll yftgkgtqsm
     1021 dldqytgnns dfqtpsvksf glnlnltf
//
LOCUS       WP_099439103            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099439103
VERSION     WP_099439103.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115603
     Region          28..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikiilgvl vciglispnl kaqtknvklk gividegtkq pvpsvslvtg npsktvgfsd
       61 gkghfsvdlp vgitvefryi gyrpqklkvs veqlnlsikl keltqnmdev vvrgfvarsk
      121 elttgssftv kaeelqdvpv anieqllqgk vpglniqnnt gapgfrgttq lrglstlqvs
      181 nsnnetflqp tsplyvidgi pidadkasem gfdlqgpgis plslipqedv esieilrdaq
      241 atalygsraa ygviiintkr ghskiprvry tnnffvstpp alrktlggnd eravklqqiy
      301 gnalsfddii risktpllsd slnnyynnst nwqsifyrtt ynqthnlaid ggdekfnyka
      361 nmgyfankgi lkntgfsryt lnmnaelrpn drfrfttfls ggigkqqkgd glgflqrgva
      421 dnaqassllp gpsfyqssgg vvsaletlnd natrnirtsi daeysilpgl klvstvnysf
      481 ssdiedtftp aaannqfsqv ygfngrstsl ynrnmlnynv tfkekhslyv svandineqr
      541 gqtsairqar tpndqfqgpl gfdayssrgg gvlsynrakl asfwasasyd fmrkyildla
      601 yridgtsssg ldnpysknps iglrwnfgke nwmsnldwln sgsirlswgk nitptgslqs
      661 iygkynigsn ynnqqsigvd fgsipnpdlk pksremynlg ldfslfkgka dlnfdayfse
      721 iknelysrsm sntigfgnlp snetgmvnyg yemyfairpl sdkspfklnl sfngawnnni
      781 ltrlpegyng qnivfadgdg qhtilrvgrn tlsnyllinq gvfsqdsdvp vdpvsglryq
      841 tgqrfytagd pnirdvngdy imdrndyqit gnsqplltgg msanlsykgl giniyasyta
      901 krtilnnala srlsimnnpf gtnavvslpd vdmwrkpgdi akypyafdyn rygtirpfry
      961 dqnlweedgt ylkinnvtlf ysfpkefakr lgisnlrvqm sasniitfsg ysgpnpenvt
     1021 algrdlsagy pnsrdyifgi nldf
//
LOCUS       WP_099439107             859 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099439107
VERSION     WP_099439107.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..859
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=96295
     Region          4..858
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqqplvvld gipligehpf aydiqlnnyn rigtatnlls nidmnniaei kvlrdlsava
       61 iygpnaanga ivltskkagp vrqvsfnsyl gfapspkvtt lnsgyenafr kqfydrftsn
      121 grysdediyp qylsdsssnl yngpsnwvdd yyrnalvhni tadlsggnew anfrfsggnm
      181 rnqgvadsts lnrynvmfnv nmkpmkwlnv slmvnanrlq rdrnrslrdr faqtnylpsl
      241 amplspnkev yqqylaqfgk gyddnintll dgygkisvnf knvkissgis vdynegtrdi
      301 fyarplmegn syasnyfgyn qrlifenvis ynkhfgsdhl qivggqaiqw dlskynyaya
      361 yrgvndfikl nlidnnlnpt sfpanllfkf ldktrhnlfs vygktsydfs dkysvslllr
      421 gdassnaqpt srwffspvls agwnikndll sasenvssls lrlsagrlgk lntydnfgqg
      481 pqytadigyt gnvtipgfng fatlarpynf gwvgygipwa ytdqlnfgid fginnnrlqg
      541 sldlytktdk kqllgipaha eygyktsiep gmsvnnkgae lllsyaafqs gsggfswtps
      601 lnisynankl lalpgglnei iignsllrvg esvdrywllt negvynsvte ipsvngvpmq
      661 ytgttmqagd pkwkdqngdn kinntdktly ghnqpvvvgg lnndfkygkw slnmnlyfnl
      721 grslmnqqma ntldfinrdg eqtlesvkei tfwekkgdrn dyplynpwss vipyridqnl
      781 flenasfvkm rtlslgydlt salgkgkiks lyvyamatnl ftitgykgrd pelvpytgyd
      841 tgyglpiprt ytlglkmnl
//
LOCUS       WP_099439278            1123 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099439278
VERSION     WP_099439278.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1123)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1123)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1123)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1123
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1123
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123122
     Region          30..1122
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrififls vlccffattn lfgqtgglli sgqvisgsgg etlpgvsvkl kgtstgistd
       61 vngkyslrip anqgtlvfsy lgfktkevqv ngqskldvvl esdvtsmeev livgytqqsr
      121 tkttaaiskl apdelknias pnpvqalqgk iagvsvpvtt gqpgvgatni iirggtkpna
      181 ygsglgnnng sstgssdnns plvivdgvfr smndvnpdni eslqvmkdaa staiygarga
      241 ngviviktkg gkanakmtia lnhrttwetp ardydylnae eylrlarttv kntadaldkn
      301 nllnnggfsa gtrvytqkgq ygkninltal ydnivsvegq syvdnllsrg wkvmddpinp
      361 gtkllyadnn yqdmlwntdl stnenlslsg ggeksdfnls mgytnqagtf agtkykrydg
      421 lgnfgfkaad nfridvmlny qnvmpnyvdg fqnelvrgtr itplirtfkd dgnpmpgely
      481 tvrnrfhtlm yddtrtsser lvsrvagdlt itkglhfkps fsyliddyke lfmrkgtpad
      541 evqpatqrqk ndytknarql midqvlqydf sikdahnfta lggvnfirnt dhvaslgsqr
      601 gsndyiytin eppttvingv vmsnvtnfat tigesrsasa ftqinydyka kylfsgslry
      661 dgfsnfavqn kyaffpsasv gwnvnkedfw nvkainalkl raswgaagls dlsitdtygg
      721 yasildgrta nyaqssgilr snlanynlrw estettdfai dasflnsrin ltvdyynkrt
      781 kdrlaskplp sespfssiaf nngelrnrgv evelgatiik gndfkwdanf sfaynqalit
      841 klpdngrakn rqggdmifdp vsnslveagg faegerpypi yayrvtgvfa tdeeakawna
      901 kvkdnlaspq giavgkrggd yifddvngdg vidskdqvfm gyrnpnkmgg mqntfsykni
      961 slrftmdyam ghlisngala rslgqgrafn egapstaigp diwqkqgdvg kkyarfsfad
     1021 ydfgqrnylr naplgnnnsy nsdvsamysk gdflafreis isydvpkkvl ekikasglni
     1081 fatvynvgyl tkyeglnpev ytgfdpggyp rprqfllgvt lkf
//
LOCUS       WP_099439455            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099439455
VERSION     WP_099439455.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114399
     Region          19..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mglkikqgtt nklesivdkt itgrvmdekn lplagvsvlv kgskngtltn aegryilkgv
       61 pdnailvfss lgyntkevpa tnnsinvvli esandlselv vvgygtrskk dltgaisqvk
      121 atqlenqhpn svqdllrgnv pglnvafsas pkggsnsdlq vrgrssltag ttpllvldgv
      181 iypgqlsdin pndietidvl kdassaavyg akaasgvviv ttkkgrsdkp vitvnttigk
      241 asrevsehvy dangfvnwrt dvlksinaat igsqpyrfnd pralpsdvsl aqwfaydntp
      301 atsdpvdtwl trlkmfpvei anykagkstn wedliyrngf rqdhtigisg kkeevnyyls
      361 lgytnnnglt vgdqyknara rlnlegkaas fatvgvnfqy asrdesavpi dfgqvrnasp
      421 lgemyaadgv tlrpspnddl gnnrnpfmdn vyrerllkyn tifstiylkg dlpfgfsysv
      481 nvtpsydqtr efnhysalhv dyvarkgfan riettrfnwq idnvlkwnkt fdkihqfdvt
      541 fllnaeklkq tsgkvenegf dpndilgyhn igsgvkpivs stdmvttgda lmgrlnytlk
      601 skymltatir rdgysafgqr npratfpsva lgwvfsdegf mksvswlnya klrlsygsvg
      661 nrdidgylal snlntgkyly vnsagilvpv sqlyvdrmtn kdlrwestas fnggldfsif
      721 nnridgsvdv ykknttdlll lralpnvtgf fnvasnlgnv tntgfevsln snniknenfr
      781 wrtsvnfaln rnkiehlfge vnqlddkgnv igkierddpg ngwflgkdin aiwdlkvlgv
      841 wqqnevaeaa kygvkpgdfk vqdvngdykf tdadkqflgs rspkftasmr neftflknfd
      901 fsfsmysywg amtdyneakn nsgfqdrqns yklpywtpen pindyarlys sngsanysvy
      961 rktsfirldn vslaytlpkt lvqkgklnnv rifttvqnaa iyapdweywd pqnknptpry
     1021 vtlglnvtl
//
LOCUS       WP_099439543            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099439543
VERSION     WP_099439543.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110478
     Region          37..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msfrsysate gyletinlsr vslsqpdrqa iarkviitgv vldeksqpip gvgiktasnk
       61 stvtdangkf sieaeseael itfsylgyat qskaagngst pltikmalde gvnlddvvvv
      121 gvgygtlkqk evtssvahvg reefrqsgsr npldliqgkv aglqlsrpgg snpnsgvavq
      181 lrgavttqgn asplyvidgi pganpdllqq ddiasvdvlk dgsgaaiygt sanagviiit
      241 tkkgksgapt fdyssyfrke ylqnkpdflt aeefrqkias geikqkdfgn ntdffdglin
      301 hnnfsqnhnl altggtdkts yrasvnyrnl egisrengre eyglrlninq kglndrlsaq
      361 inlatnfnka nllggggwes estknptlsn fnadgsyrfd ltstneyarl aqetsyrkqq
      421 tssadgkvdl eiinglkasi fgsvqrnsyt dgqyrlkase dsmentnfpg ggyaakgnvl
      481 eqkfaveptl qyentfaekh kvtaiagysy rydifegssa snrgfindlf rednlsegsa
      541 lgvgkasmds ykndntliaf fgrvnyvfnn kymaqfilrh egsskfgknn rwanfpavsl
      601 gwnmsqenfm kdvkfinylk lragfgvtgn aplsnnisrv tlggggkylf pdgnyyetyg
      661 pnsnanpdlk wetkreynig vdftmfdnkl sgsidafkrd tkdlldsyts pqppyvrdni
      721 wtnvgtissk gielaltyka itnedfswst svtasttrni lesysntiyk reffttgpin
      781 gagalgdaft imagkqigif ygkrfagftp egkwlfynrn gekvlndqin nsrddlnatd
      841 laplgnavpk yyaswtnnfk yknfdltvfl rgkfdfdiln ttalsyankt wsgnllketf
      901 tkynqindty mysdyylesg sfvkideitl gynfklnvkg lrnlrvyatg qnlatftkys
      961 gndpdfvldn gigrefdgka lgidtrgpyp strsflfgin vgf
//
LOCUS       WP_099439804             463 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099439804
VERSION     WP_099439804.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..463
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49456
     Region          37..>434
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkldsnfrg fdlkcpvlll gifiifflpl vtkgqsrtvt givtdaqqip mpgitvvikn
       61 sknvtqtdae gryqiaatta delefsyigf dtqtikvgdk ttinitllss ttgldevvvv
      121 gygmqkkvnl tgsvatiesk slenrpitnv ssalaglapg vfvrqssgrp gsdgatirir
      181 gtgtlnsnna lviidgiqgv mdavnpedie sisvlkdaas asiygslaan gvilittkkg
      241 skkktvvtys gilsqtqpsn lptfvsdyvt hmnlvnegyr nlgqnniytq atidtwtdan
      301 qnptgvnslg vpnniaypnt nwgdvifqnk vlqnhnvsln ggaenisfll sagylgnpgt
      361 mkntelnryq franveakvt kfltvgtqtf asmqtagman tanafnflrq ttpgvypvld
      421 gkygfpqape esatannilt ylnstggvtg nqeliqlcmq twt
//
LOCUS       WP_099440298            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099440298
VERSION     WP_099440298.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116079
     Region          23..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfi flfiagsamg qdrtitgtvt gkddgqplpg vtvvikgtrv gtqtgsngky
       61 slsvpsgpat lefsylgyas qsitvtttnv invslasdlr dlaevvvtan sikrdrrslg
      121 yaaptissdv lvqggspspl talvgrvagm nissssntpg sstrivfrgg ssiagnnqal
      181 ividgvpvdn ssvtggadsr ssvdfgnran didpddiesi tpllgpaaaa lygsrasnga
      241 vqittksgkk gktqvtfnts nifssvlklp dfqneygqgy ytelddngnp teyfndtqen
      301 wswgapftge mqewgqsidg vrqskpysaa tnnvknffkt gfatdnnlnf sggtdkstfy
      361 lalntlnsng ifpgkqdvyn kygvrfngkt dfsdkfsagv sfnynkidar qiaggqndns
      421 vfdnvlqtpr dihvdqlgdl tnkyngfgyt dangvvhndk ygyygsytln pyyiienfvn
      481 ddvinrvtgn vnleykpvsw lniqerigtd tyaerrrqlt pkfsfspidk ntnqgnhisn
      541 ggyqidqfnv telvhdlmvt athsfnedfk gslmvgnnir qrntstnrta tnasaglvvp
      601 dwynlqnsng plnvitdnis krrlvglyad lnlsyknmlf legtarndws stlpvknnsf
      661 fypsvsgsfv fseliapnki lsygklrasv akvgndtdpy qllntfargt ingnfgstif
      721 pfgnvaalqa gttlgnanlk peittayevg telsfldnrl gvdftyyqnk sknqilaipi
      781 pnssgygfsv inagevqnkg ielslkgtpi rtqdvnvelf gtfykntnkv vdlapgvdqi
      841 vlggvggmsi vaakgrpyge fyavtnqtda qgrtivdaes glplattsaq ylgsynpkyq
      901 asfgtsitik qhlnvnvlfd vkhgnklysr tkdilafvgv saetggqrsg lpfpnsvyld
      961 dngnsvvntn vfynkqdyyp dlnpgmnvid gsfvkmrsag isysfnkaql ktlpfstlsv
     1021 glfgnnlfvw takenkyvdp evnsggatne qgfdftaqps vrnygfnvkv tf
//
LOCUS       WP_099441071            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            ginsengisoli].
ACCESSION   WP_099441071
VERSION     WP_099441071.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter ginsengisoli
  ORGANISM  Pedobacter ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Pedobacter ginsengisoli"
                     /db_xref="taxon:363852"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117094
     Region          29..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkqvillsi ffsciflckd lvaqtkkvtv sgtvvdggsk etmvgvsvat gkplkvltqt
       61 dgkghysvsv degatlvfty vsygtrtitl kagqttlnvt lkednktmee vvirgyqkrt
      121 revttgssfi vsgkevqdvp vsnveqllqg kvaglniqln tgapglrgti nirglstist
      181 tgsgnetflq ptsplyvidg vpmdadkase ygfqqqgpgv spislipqed iasievlkda
      241 tatalygsrg aygviliqtv rgnseiprir ytgnfymnai pklrnilggn nerelklyqi
      301 ntygrfrdqf misntpflad slnpyynnst dwqgvfyqnt ynqthniqld ggdskfsykt
      361 nlsyfsdkgi ikntgfdrys lnmnmdykpt srisffgsir gnvgkikkan gvgllqtgva
      421 sdgqkssllp gpsffqatss vlsalqtntd agpknlntyi egryelipgl nltsaasydy
      481 nvdtedtftp aaannqfaki yslygytsql ynrnnasytr sfndkhnffl nlfsemyvkk
      541 gqssitrler spndqfqgpl gydgyysrgg gilttfydqn qisfaaafty dfekkyifdl
      601 tyridgtsns gnkdpysknp svglkwnfnk enwlkdikwl nygdiritgg knifpvgslv
      661 diygkytprg fynnnprvgi eygsvpnpll kpknvtqfni gmdlglfngk ldvifdtyyk
      721 kvdnelftsm lsntlafnnf tsndaalsny gyelsftsrp lskeskfnwt vsvngawnnd
      781 vltklpaeyn gqfiqfdggk yaqhlakrvg rnslanflfv nqgvydntsd vpidpvtgfr
      841 lrnngsgdfl nsfqggdtrf fdangdyvid trdlqvvgnt qpvltggmsn tlsytmpsgs
      901 tlslniyaty takrsilnna ladrlrllsn pfgldavvpv ndlnmwtglg stnarfanay
      961 dyahnafvnn yryeqtlwme tgsyfkinqi tlsyafakkm arriglnnir tflsasniit
     1021 fspysgpnpe gvtaigrdgs ngypvprvyn lgfnvef
//
LOCUS       WP_099462998            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides provencensis].
ACCESSION   WP_099462998
VERSION     WP_099462998.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides provencensis
  ORGANISM  Parabacteroides provencensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Parabacteroides provencensis"
                     /db_xref="taxon:1944636"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122032
     Region          46..109
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          132..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkmnylkkts rlvvtacmla gmplvsgtvs aselqtqtms vqaetttlre lfdlieakfn
       61 ysflirnndi nmneritmdm snrsveeilk salknqhadf yvndnriivy ktsskqgsnp
      121 vvsekqaaqq tqkiagtvvd ahtgepiiga nilvkgttng tstdfdgnfv ledvpanatl
      181 visyigylpl emkstagkmt irlkedtqnl devvvvgygv qkkesltgam qvvssdklld
      241 attpsvenll sgkapgvyvt sgggqpgaag tvvirgkstv ngstdplwii dgvivgnsag
      301 slnpsdiesm silkdaasta iygsqgangv ivvttkkgkt gkatinvsak mgvnqlnrgn
      361 femmsrdell gyyksfanqq aipqetwdki gqgydydwwk ngsqlgfaqd ynlsvsggse
      421 kiktyisagi ydengavkgy dytrynfrfn vdyqatdwlt ikpkvwgtrs dimdqqhslg
      481 amyenmpwds pydkdgnliq ayrpsswvss dhvnyqydlq wnykkttkye fmgnfdfdik
      541 ftdwltfssv nnykygstly kkyddprssg gqaengqlqd kttsyyrvys nqllrfnkvf
      601 dkhsinaila yewntytaqv tdqiatgfap gfsvgdativ pkkakgsqne wavqsylfna
      661 nyaydsryll sfsfrrdgas nfgenakygn ffsisggwni hqenffkadw vqqlklrasy
      721 gsvgnrptel ypqyalysmg tgynglpgai isqvenkdlt wektytagvg idailfdrlt
      781 vnldyynkkt tdllynvplp gvtgvtgmfr nvgavknngf eatvavdilk ggdwnwnvsa
      841 nigvnrnkvt elygdkseiv ianansgilg pidkilkpge dvdtwyatew agvdpetgsp
      901 lwyttneage rvttsnysda skhqvivgkq tpdfyggfst dlswknidls avfgysvggq
      961 ifnydrtvyd sdggytsynq qkllsgwsrw ekpgdiathp kaeygnlsqs nkpssryled
     1021 adylrlrnlt igytlpckip yisnfrlffs genlfvisgf sgidpelpsn tdiatgkkva
     1081 gasgvasspy pmarkfmfgl nvsf
//
LOCUS       WP_099465480            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides provencensis].
ACCESSION   WP_099465480
VERSION     WP_099465480.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides provencensis
  ORGANISM  Parabacteroides provencensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Parabacteroides provencensis"
                     /db_xref="taxon:1944636"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115716
     Region          42..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkkfrpvsl illlgalsft gslyaipgte npaasvpqqt skvsgtveda lgpvtgasvi
       61 ikgttngtit dldgnftldg vkkgdiiqis figyvpqdip ytgqstltvh lsedtqklde
      121 vvvtalgmkr dkkalgyamq elkgddllss repnlansls gkvsglqivr ssngvggssk
      181 ivlrgnnslt gsnqplvvvd gtpmdnftgg vddvwgnsga dmgnglsdin pediesmtvl
      241 kgasaaalyg sragngvili ttksgrkteg lgltvnagit aetiflkphm qddfgqgsvg
      301 iydnqsrlsw gpkaegqtvk dwlgrdvplh tydnidaffg tgtsfnegvs fqqdikgtsv
      361 fasvnrsdda sitpesklnk tnitvrattf ldeakkwkvd akvnyinmna hnrpiqgvnp
      421 snafntiynl prslnikefe nsvdengkmi wydasnnpqe npywvtkyrq nedtrnrllg
      481 nlslkyaptd wfdielrggt dyytttknek vyaggnttpr glysegsetf yennfsflat
      541 arkdnlidrl ggfitfggnl mqqqrskmna sagellvpdl fslnngvdkp tvtselirrr
      601 mnslygslql nwdgylfldi tarndwsstm skvnrsyfyp svslsgvisd mvpklggamp
      661 dwfsfakvra syaevgndld pyqlynyfsv dkdqngntia kpgkvlfdss vrselikswe
      721 agfdfrffnn rlgidfawyk snatrqlldl pmdpfsgyas rkvnagniqn egvelslnge
      781 ifnspqgfnw nataqfslnr nkiidlypgv tlyniktfda vqivavqgsl ygdiygqtfq
      841 rvtdensphy gkivvgedgl plistdkskv gnqnpdwmlg ltnnfsykgf nlsflidfri
      901 ggdiysatas glytrgnaag tvvngdrqsf vvpnsvvqkg ndyvmnevkv tpqnywerig
      961 stgnyglpem ytynatnvrl rnitlgydfn rqmlkktpfq rvrlsatcnn vwmihynlpg
     1021 idpesvaatn tnatgfenga aptsrsytfn vtigf
//
LOCUS       WP_099465481            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides provencensis].
ACCESSION   WP_099465481
VERSION     WP_099465481.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides provencensis
  ORGANISM  Parabacteroides provencensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Parabacteroides provencensis"
                     /db_xref="taxon:1944636"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115036
     Region          42..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlknfkpvsl ilfagalcfs gnayadlapv kqstnisqqs gkvtgtveda lgpvtgasvv
       61 vkgttngtit dfdgnftleg vkkgdviqis figytsqeit yngqplgiin laedtqklde
      121 vvvtalgikr ekkalgyatq elkgdailds resnvtnals gkvsglqvvr ssggpgassk
      181 ivlrgnnsit gtnqplivid gipmdnfqgg vadawgnkgp dmgnglsdin pediesmnvl
      241 kgasaaalyg sragngvili ttksgkkqsg lgitvnagvt aetmfmqpdi qnsygqgstg
      301 iydvksrfsw gpiadgsvni dswngknvpm ytydnvgnyf dtgvsfnegi sfqqanegts
      361 vfasinrsdd kgivpgakls ktsinlrgtm efgpdkrwkl dgkvnylnni ghnrplqgin
      421 qsnafstiyn lprsinildl kncldedgnm iwwdtestpq enpywtkqyr tnedtrnrfl
      481 gtmslsykif dwwnvelkgg tdyyttttts klyaggnvtp kgnysegset fyennfsflt
      541 taqkdnllgk fggfvtfggn lmiqkrsvek istgdllipn lfsinnavdk nkmgleytlt
      601 qrkmnslygs fqinydgwmf lditarndws stmskvnrsy fypsvslsav isdmvqkngg
      661 slpewmtfak vrasfaevgn dldpyqlytv ysmskdpygn pvaspgsvlf npdvrselik
      721 sweagvdlkf lnnrlgidfa wyksnatrql ldlpldpfsg ysskkinagn iqnsgvelma
      781 yadifqnpkg fswnitanls fnrnkvidly egikemglsd gsfndevkvv ahtggmygdi
      841 ygkkfqrves gadagkiivd aqglplltsd lqylgnqqpk cmlgitntfn yknislsfli
      901 dariggkiys attakmyyng saagtvinga reefvvpnsv tasgdgytan ntsvtpqlyw
      961 qrvgtgnlgv geaflydatn vrlrnltlgy tfdkkllakt plerlrlsft annlwmiash
     1021 legidpesvs ttntnatgie lgaaptsrsy tfnvtvgf
//
LOCUS       WP_099465815             927 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides provencensis].
ACCESSION   WP_099465815
VERSION     WP_099465815.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides provencensis
  ORGANISM  Parabacteroides provencensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 927)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Parabacteroides provencensis"
                     /db_xref="taxon:1944636"
     Protein         1..927
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102528
     Region          44..926
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhvslkffq rivflfggii itisfsvaqd vpfrqdtikp fladtnhmde lvtigyatgn
       61 hrtisgsvdh vnkknmnegl lstpldalrg rvsgvsipmg gnspaalaav rvrgttsltg
      121 gndplviidg vfadlnllss iypadiedft ilkdasetaq ygargasgvi evttkkgkqg
      181 afsvsydgsf gvevayktld mlsadgfrqy akehqinmvd lgyntdfqee itrlgsiqnh
      241 hiafgggtes sqyraslgfv erekvirdin thnftakvni tqqafknrlt fdlgifgsll
      301 knhylndvqk mfysaatfnp typnhknent gkwdgvtnas qitnplawme vkdheanahi
      361 nthlklafnl snefvftafg sytynvidns qylptsvwah gqayrgerkt esllgslmls
      421 ykkdigehhl nllglaeaqk dimtgfyttv tnfstdrfgy dnlqagatrl wegtgsyyee
      481 phlvsflvra nyayanryia tvnaradass kvgennkwgf fpsasvawvv seegflknms
      541 finnlkvrag yglsgnqgai dsynslqlmk pngvvsvdgt ptvtmgtirn anpdlkwevk
      601 rtfnagldag lfenrfivsv dyynsktddm lylydvsvpp faynkmlanl gsmrnsgtel
      661 gigvtplrtk dmelninvnv tfqrnkllsl sgvykgeyms askytsisdl ngagfhggyn
      721 hivyqivgqp lgvfylpkct glvrnenggy nyevadldgn gvsledggdr yvagqampkt
      781 llgsnisfry kqfdlslqin gafghkiyng tyltymnvdi fpdynilkna psrnirdqta
      841 tdywlekgdy infdyinvgw nvplgslkky irnlrvsvsv nnlatitgys gltpminssi
      901 vsntlglddk rtypvsrsyt mglsfnf
//
LOCUS       WP_099471763             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paremcibacter congregatus].
ACCESSION   WP_099471763
VERSION     WP_099471763.1
KEYWORDS    RefSeq.
SOURCE      Paremcibacter congregatus
  ORGANISM  Paremcibacter congregatus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Emcibacterales; Emcibacteraceae; Paremcibacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Paremcibacter congregatus"
                     /db_xref="taxon:2043170"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40352
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,285..286,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpkerr pherrvaasp dtvkkliqlg fdvvvekdag lnssipdsaf saagatiaad
       61 aattyqdadv ifkvqrplhg negdidevsl ikpgaivaai lspandpasv eaytngnita
      121 famefmprit raqsmdvlss qsnlagyrav idaaaaysra fpmmmtaagt iapakvmvmg
      181 agvaglqaia takrlgavvs atdvravake qveslggkfv mveseetget eggyakemsd
      241 dykakqaeli attlakqdia ittalipgrt apvlitremv qsmkpgsiiv dlaaeaggnc
      301 eltkagevve engvkiighh nvpslvstda salfaknlln fitplvdagn kslnidwqde
      361 iivgtlltkd gaivherlkp qnqggn
//
LOCUS       WP_099493329             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_099493329
VERSION     WP_099493329.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38618
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasivdsay vtagatigsa
       61 gdafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_099506824             519 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Streptomyces].
ACCESSION   WP_099506824
VERSION     WP_099506824.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53305
     Region          1..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligivsear rgetrvaatp atvvqlvklg ydvvvepgag alssfpdeay veagarvgdp
       61 laadvvlgvn alsslqldgl kpgttvmgim spalnpalme dlakrpital amdavprisr
      121 aqsldvlssm aniagyravv eaahvfgrff tgqvtaagkv ppakvlvcga gvaglaaiga
      181 agslgaivya tdprpevadq vrslggeyls vdtgdageve vsatgyakem stdynsraae
      241 lyrdritemd ivittaqipg rqaptlitae mvalmrsgsv ivdmaaasgg nvegmvkdea
      301 vvtangvtii gytdlpgrlp aqasqlygtn lvnliklmtp dkdgrlvldf ddvvqrsmtv
      361 vrdgeltwpp ppvqvsaapa aapasapaev kpagpqtkpp vstqrrftvv gvgatvlfll
      421 aalspsallg hltvfalaiv igyyvigqvh halhtplmsv tnaisgiivv gallqighgd
      481 tpngavvtvl stiaillasv nifggfavtr rmlsmfsrs
//
LOCUS       WP_099509336             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            ossetica].
ACCESSION   WP_099509336
VERSION     WP_099509336.1
KEYWORDS    RefSeq.
SOURCE      Microvirga ossetica
  ORGANISM  Microvirga ossetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Microvirga ossetica"
                     /db_xref="taxon:1882682"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39083
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd gaetrvsatp etvkkykslg advvvqagag akagvpdaef eaagasiasg
       61 aaealkdadv vlkvrrpaeg eltgakpgal viaimdpygq daalkslada qvaafamelm
      121 pritraqvmd vlssqanlag yravidasae ygrafpmmmt aagtvpaari fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedee fkqaetaggy akemsaeyra
      241 kqadlvashi akqdivitta lipgrpapkl vtramvesmk pgsvivdlav erggnvelaq
      301 aggvvehngv kivghlnvpg rlaatassly aknlyafvet lvnketkela vkwddelvka
      361 tcltrdgaiv htafqpta
//
LOCUS       WP_099512882            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia miricola].
ACCESSION   WP_099512882
VERSION     WP_099512882.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia miricola
  ORGANISM  Elizabethkingia miricola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Elizabethkingia miricola"
                     /db_xref="taxon:172045"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113449
     Region          43..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfgnrkmila avfflgitat lkaqesvhdi ivrdkttqqp lsnvsikdta tgkeivtdgd
       61 gkvaievktd lqtyvisldg yitqdialst gklsdsvyll petkqlegvv ltgytrqska
      121 kttgsvssik aeviaktpva sldqalqgqv pglyvaspsg qpgamgrvti rgigsvqddk
      181 tnplyildgm pispevfavl npldyedivv lkdasataqy gsrgangviq itskkgknnd
      241 kghsqffyqn qfgissvnnq kwdmmnssqr lefeeilqdp nfpgwaysrk npykivngqk
      301 iaktesdyte gdqkladlra tntnwrklll rngvtnshyl smgggdqktn hysslsyfkq
      361 egvlpnsgve rfninsgvnh ksgrftssfn lnltggqtql sesdfdvset npvaslyfam
      421 pyekpydkdg nltpgvnrfg analtmyqdi srkekqlqgv lssnlsfeit knlkltstlg
      481 vnhqqtrftr iikqdtyfgs mvdpgeqgly erintqktsy manfgfnykk rwgsneveai
      541 alaefnkyst nydgfigygl ipglentpgg itpgtpdnnf ipkisggase nilvsqlgml
      601 rysyanrftl saslrrdgss rvpsenryky fyafgatwnm kneeflknwd alstlrlrls
      661 hgltgnaggf asdfgyrqly kpqhyngyta fvpispgnpn ynwemnkisd vglefglfkn
      721 riigevdlyn ritsdlfinr slsmtsgfes iadnmgkirn rgvefrlsgd ifrndnfswn
      781 lglnlaynqn rilslgsede ivtenysihk vgsalghfym vrwagvdpat gaplyydkng
      841 vvtkeynpen avmvkgsydp pikggittsf tyknfqvnal ftfvkgmyrl ntaelyrtsa
      901 dpnyriynqs admlnmwqkp gdvsqnpgaq yarymtdrel qsadyiklrn vsinyklkdl
      961 gslnkvfkev nifaqgqnll twtkwkgqdp eddnnwyqye yplprtitlg fnvlf
//
LOCUS       WP_099513938             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            ossetica].
ACCESSION   WP_099513938
VERSION     WP_099513938.1
KEYWORDS    RefSeq.
SOURCE      Microvirga ossetica
  ORGANISM  Microvirga ossetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Microvirga ossetica"
                     /db_xref="taxon:1882682"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54574
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkeaf pgearvamtp dsavalqklg htcfieagag taagisdaay aaagvsvvpd
       61 aaalyaatdv vtkvrppied evqrlrqgqt lisffwpaqn ssllelartr gatvvamdmv
      121 prisraqkmd alssmaniag yravieagna fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aqfvflafee aqdgaatggy aapsspafre
      241 rqlekfrela peidivitta lipgrpapkl wtadmvqamk pgsvivdlaa erggncdltv
      301 pdqtivteng vtvvgitdfp srmaaqastl ysnnirhmlt dltpnkdgvi hhnmdddvir
      361 gatvthqgav typppplkvp aiaaakpkdk skeltaeerr ageaaafkaq trsqvgllva
      421 ggllialvga yapasfmahf ivfalacfvg fqviwsvshs lhtplmaitn aisgivvlga
      481 llqvgsghwl vaalaslsfl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_099514796             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            ossetica].
ACCESSION   WP_099514796
VERSION     WP_099514796.1
KEYWORDS    RefSeq.
SOURCE      Microvirga ossetica
  ORGANISM  Microvirga ossetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Microvirga ossetica"
                     /db_xref="taxon:1882682"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54640
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkeif agearvaltp dsalalhklg hacvieagag kkagfpdaay aaagvavvps
       61 gqalfeaadv vvkvrppmee eighlrqgqt lisfvwpaqn edlleqakar gatliamdmv
      121 prisraqkmd alssmaniag yravieagna fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatalg aityafdvrp evaeqiasmg aqfvflefee aqdgaatggy aapsspefre
      241 kqlakfrela peidivitta lipgrpapkl wtadmvavmk pgsvivdlaa erggncdltv
      301 pdetivteng vtvvgttdfp srmaaqastl ysnnirhmla dltpnkdgvi hhnmdddvir
      361 gstvthqgai typppppkvp aiaarpkekv keltpeekra qeadafraqt rtqvgllvag
      421 gllialvgay apasfmahfi vfalacfvgf qviwsvshsl htplmavtna isgivvlgal
      481 lqvgsghwlv valaalsfli gtinivggfl vtrrmlamfq ks
//
LOCUS       WP_099515526             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            ossetica].
ACCESSION   WP_099515526
VERSION     WP_099515526.1
KEYWORDS    RefSeq.
SOURCE      Microvirga ossetica
  ORGANISM  Microvirga ossetica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Microvirga ossetica"
                     /db_xref="taxon:1882682"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55049
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalreif agenrvaltp dsalqlrklg hacmmesgag akagfsdaay aaagvevlps
       61 avavfraadv vvkvrgpers eaemlrsgqt lisffwpaqn vdlleqtraq gatviamdmv
      121 prisraqkmd alssmaniag yravieagnh fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aqfvflefee aqdgaatggy aapsspefre
      241 kqlakfrela peidivitta lipgrpapkl wtadmvdamk pgsvivdlaa erggncdltv
      301 pdekvmtang vtligytdfp srmaaqastl ysnnirhmlt dltpnkdgvi hhnmdddvir
      361 gatvthqgav typppppkvp aiaaakpkdk preltpeerr agevaafkaq trsqvgllva
      421 ggllialvga yapasfmahf ivfalacfvg fqviwgvshs lhtplmavtn aisgivvlga
      481 llqvgsshwl vvslaslsfl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_099526751             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sediminis].
ACCESSION   WP_099526751
VERSION     WP_099526751.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sediminis
  ORGANISM  Pseudomonas sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sediminis"
                     /db_xref="taxon:1691904"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38859
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikklvgqg hqvtvqagag isasipdsay eaagatignd
       61 saafgadlvl kvvaptdael ahmrvgavlv gmlnpfcnet iarmnargvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarilil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpqswme
      241 rqakavhera kqadivitta lipgrkaptl lhestvaemk pgsvvidlaa aqggncplte
      301 adkvvvkhgv tfvghtnlaa lvpadasaly arnlldflkl vidkegqfql nleddivaac
      361 lmcnagevvr kng
//
LOCUS       WP_099535094             390 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Limnothrix].
ACCESSION   WP_099535094
VERSION     WP_099535094.1
KEYWORDS    RefSeq.
SOURCE      unclassified Limnothrix
  ORGANISM  unclassified Limnothrix
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Pseudanabaenales; Pseudanabaenaceae; Limnothrix.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="unclassified Limnothrix"
                     /db_xref="taxon:2632864"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41109
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvavvkeva lderrvalvp dvvarwvkkg laiavetgag eragftdsay eaagatvtsd
       61 raqlwqtsdl vtkvlpptde elgwlksgsm lmgflepldr pqsiktlaer gitaislefv
      121 prstraqvad alssqanaag ykavllaaaa lpkyfpmltt aagtippakv lvlgvgvagl
      181 qaiatarrlg avveafdirp etrdevqslg arfvemmiee etsgqngyak avsdnlqari
      241 qatvaeraig advvittaki pgrrapimvt adtvaqmkpg svivdlaaeq ggncecsqpg
      301 hdhvvngvqi lapmhlastv tthtsmqyak ncsalldwli kdgqpvfnfa ddildavcit
      361 hggeirndrv rnlvatlset psaesmvlas
//
LOCUS       WP_099544540            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            4G9].
ACCESSION   WP_099544540
VERSION     WP_099544540.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 4G9
  ORGANISM  Maribacter sp. 4G9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Maribacter sp. 4G9"
                     /db_xref="taxon:1889777"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108628
     Region          24..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllksla vlgvflsfgl aqaqevsgtv sdasgplpga svvekgttng tqtdfdgnfs
       61 lsvgddavli fsyigyknqe ipvggqttid vtlvedtqal devivvgygn qakkeitssv
      121 vsvstedfnq gvvqeptqll qgkvaglsvv nrggnpnaep virlrgistv ggnqqplvvi
      181 dgilggslas vdpadienit vlkdgsaaai ygsrgsagvi vvttkrgkgn qplqlsyngq
      241 vgvstianqi dimnreefla tggndlgsdt dwrdqvtqtg faqvhniaas gggdgfnfri
      301 agnlrdtdni lintgfqqfn lrtnftgflf ddklkidvna aftqrdsqig fneamryats
      361 ynptapvfgd dapfafnssq fggyfetlgl fdsfnpvsia elnrndaaat tlnygvnlny
      421 kvtdnltfnl nyaaqnikrd nnqyypttnl wrgnalsptr rgradfrsee rrfrllegya
      481 aykgaaekln ytvtagysfq endynfnyfq vgdfppgvdf dwsnnisvaq dlleagrvva
      541 dsgredgdri irffgranvt fddaiffdas iaregssrfg senqwgifps vglgadlnky
      601 lelpninllk vragwgltga ippsvglyqq ifnvqngsdg qsgaattqag graanpdlkw
      661 eeksefnfgv efamdrfgat vdyfvrdind fitlanidaa enngfsqrwq nsgrlgvtgi
      721 elsanydvvr ndklkyntgl ifthnknile enpqgdqvlg nlgapgqnnt nvvrvkegee
      781 igqiwgpvfs gdvdangtpi lvdingdgnl vtgqgsaldd dadfrvlgsg ipdfelgwtn
      841 qitygnwdan vffravvghs lvnsfrafye piigsqasyn fvntslarsd irtaqfsdyy
      901 vekadflrld nmsvgytfnm kedsyikglr lslagqnlft itgytgvdpe pslqdgglgl
      961 snlegstpnq niqqvqanpl iagierreay ftsttitlgv nvnf
//
LOCUS       WP_099546275            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            4G9].
ACCESSION   WP_099546275
VERSION     WP_099546275.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 4G9
  ORGANISM  Maribacter sp. 4G9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Maribacter sp. 4G9"
                     /db_xref="taxon:1889777"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114857
     Region          25..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngllt lllalivhit yaqektvsgt vtdqdglplp gvnivvqgtt tgtqtdfdgn
       61 ysilasqgqt lvftyigqkt vrnvvgasst vnvtmeddaq aleevvvsal gvkkearalg
      121 yavqtvgtet itksnatdal saltgqaagv qitntsgnag agsrivirgq tslsgnnqal
      181 livdgvrinn dqfasearta gvagsnrgmd inpadiesin vlkgagaaal ygveggngvi
      241 vittkkgkag kfvvnvrsnv tlteankfpd lqnewvqgfn gewlgpetgt fgswgpssen
      301 lywdgsdyay dkngrivvgd tgglkkyqpy dpfevfttgv ttentfsisg ggekttfrms
      361 ygklsekgii pkndfdrntl nfsgsaqise rfnvnmsgty tnsqayriqq gsnisgfmlg
      421 llrtppsfdn sngngnqavn dpstyefadg sqrnyrgggg ydnpywiinn tprtdevnrf
      481 vgsvgftyki adwlnlagni gidtyaddrv qffdigsrtn pagtviydny nyrhtdnyfn
      541 vngniditdd fsfgyllgtn iyserytnty tqgdqlgikg fnnitnasiv qgdyditrek
      601 nigfygqldf eykrmlyltl tgrqdylstl edpvnyqlsd lalfypsanl gfvfseltgt
      661 gdflsfgklr aswaqvgaga pdayatstty evadigdgwt tgvtfpfqgn agfqinddlg
      721 nntlvpstit sqeigldlrl fknrlsfdla wyhrlaedqi lavpiarssg snssflnsge
      781 letngyeatv nakiidgenf kynlginfdk setivnalap gvntqslggf visnipgerf
      841 gqiyggaflr ddagniiidd npdsanfgyq iqdpqqrvig dptpdftigf nntftykdlt
      901 lnflfewkeg gdmwngtdwa ltwagtssvt edrgttrvit gvkqsdgsvn dipaeineyf
      961 yrssglngfg nvdehfvqda swlrlrtlnl tydltntiks dffsnisvsf tgnnlwldtp
     1021 ytgvdpetsl tgagsnaqgv dyfnnpgtks ygfgvnltf
//
LOCUS       WP_099547178            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            4G9].
ACCESSION   WP_099547178
VERSION     WP_099547178.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 4G9
  ORGANISM  Maribacter sp. 4G9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Maribacter sp. 4G9"
                     /db_xref="taxon:1889777"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117691
     Region          21..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyfmlvmtl fmtatvfcqn tvsgivtdat gnpipyvnvl lsgtnkgtit neegkfsint
       61 tdtkgvlefs vlgyqtqkvp indlsyievt llesseqlde vvltalglkr etkelgyvvq
      121 sldaqgvtev ksvnfldnla gklagvtinq gptgvgstsk itirgeasfs nnnplfivdg
      181 vpinnnsvfn ftneaaagfq eidfgngame vnpddiaevs vlkgpsaaal ygtrasngvi
      241 vietkngrns tglginynts ffvdtafqlp dfqneygqgq sgvfefvdgl gggisdnity
      301 swgprlnvgn lipqfdspvt ltdgtvvrgg dtalysglpi tptpfvshpd nlkdfyrtgt
      361 tlinniavas nfekgnyrls ftdlrsesii pgvnldrqti strlgfrpte klsinsaisy
      421 issksdnrps ngygsenvny slvgwgprsl nidslrdywq pglegvqqys fnytffdnpf
      481 fimyenrnsf nrdrifgnis asyditehlt asirsgmdys selrqlrraf ssnrfqnggy
      541 aehdvffrei ntdfllnytn rfnvlkldvs lggnrldqka ftsqsqttsl aqpgifrlsn
      601 aaspvevfqf esnkrinsfy glvklgyedf lflditgrnd wssalatpfs vdntsffyps
      661 vsssfilsqv vdlpqvisfa klraswaqvg ndtnpyqtts afvaqtpfig qptfsnqnti
      721 anpnlqpeqt ssfeigadir ffgdqlsfdv syynaltkdq iislpigiss gytqqvvnag
      781 svrskgleii tgispvvsdn fswnstlnfs tnraivedlp qedgrltlay sriydsqnqt
      841 vylqveeggr vgdlygtgyl knengdfilt degryipnnd lqklgnynpd fmlginnqfk
      901 yknwnlgfll dwrqggiivs rtralgnvgg qlaetlfrpe agivpvgvvn tgtnddpvyt
      961 pntvavsaes yyrqfydrnh eenntydasf lklrqfsigy tfkdlsvfnq eaqlnlslig
     1021 rnlfaftenp hfdpeqlavq gqgfisgved msyattrsig ikagfnf
//
LOCUS       WP_099550154             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_099550154
VERSION     WP_099550154.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38683
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag itasivdsay etagatigsa
       61 sdafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_099557503             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hartmannibacter diazotrophicus].
ACCESSION   WP_099557503
VERSION     WP_099557503.1
KEYWORDS    RefSeq.
SOURCE      Hartmannibacter diazotrophicus
  ORGANISM  Hartmannibacter diazotrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Hartmannibacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Hartmannibacter diazotrophicus"
                     /db_xref="taxon:1482074"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39392
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpkeva sgegrvavvp dvvkryvglg aevvvetgag alsripdgey eaagakiags
       61 aadtyagadv vlkvrrpeae elglipkgal viatmdpygh edavkamaea glvavamefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrafpmmmt aagtvpaarv fvmgagvagl
      181 qaiatakrlg avvsatdvrp askeqveslg gkfiavedee fkqaetaagy akpmsaeyqa
      241 kqaalvaehi kkqdvvitta lipgrqaprl vtaemlasmr pgsvlvdlav erggnvegav
      301 ageiveigav kivghrnvag riaatasqly aknlyafvet lvdkeakalk vdyedelvka
      361 tvltrdgavv hpafapkeaa
//
LOCUS       WP_099557915             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hartmannibacter diazotrophicus].
ACCESSION   WP_099557915
VERSION     WP_099557915.1
KEYWORDS    RefSeq.
SOURCE      Hartmannibacter diazotrophicus
  ORGANISM  Hartmannibacter diazotrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Hartmannibacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Hartmannibacter diazotrophicus"
                     /db_xref="taxon:1482074"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39392
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklvvpkeva sgegrvavvp dvvkryvglg aevvvetgag alsripdgey eaagakiags
       61 aadtyagadv vlkvrrpeae elglipkgal viatmdpygh edavkamaea glvavamefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrafpmmmt aagtvpaarv fvmgagvagl
      181 qaiatakrlg avvsatdvrp askeqveslg gkfiavedee fkqaetaagy akpmsaeyqa
      241 kqaalvaehi kkqdvvitta lipgrqaprl vtaemlasmr pgsvlvdlav erggnvegav
      301 ageiveigav kivghrnvag riaatasqly aknlyafvet lvdkeakalk vdyedelvka
      361 tvltrdgavv hpafapkeaa
//
LOCUS       WP_099572312            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            4U21].
ACCESSION   WP_099572312
VERSION     WP_099572312.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 4U21
  ORGANISM  Maribacter sp. 4U21
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Maribacter sp. 4U21"
                     /db_xref="taxon:1889779"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109141
     Region          24..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllkslf aigaflsfsi aqaqevtgtv sdasgplpga sviekgttng tqtdfdgnys
       61 ievgsdavlv vsyigyktte vavngqssin ftleedaqal eevviigygt ttvkdatgsv
      121 vsvtaedfng gviaspeqli qgktagvqit qssgapgagi nfnirgtssv rsnnnplfvv
      181 dgvplsggdt sansqdlgag tsgstnplsf lnpsdiesis vlkdasatai ygsrgangvv
      241 iittksgktg kgvfefnssl siaspansyd llgrddylna idsfggdraa adrgantnwq
      301 dvvtrtvasq nqnlawskny gkgnirttfg ygkqfgvven sslerttlrv nwnhrflndk
      361 lniqvsatgs sigdeqplis gsagfqgdll gaayaanptw pnsasfdpgn llnpanllae
      421 yqsfsvtdra llnasaaydi tpeltakvnv gydysestrr salsrdivgl tngtagngrg
      481 avndlnlesk llevtlnykk efensnldvl lgysfqdfgt sgrnvtgwgy stgdlnamgr
      541 dleasadaie asisgdyqqy gigtgqsqvf vnrlapaaat envalpfggi kvrslftdtf
      601 dntdelqsff trvqysladk ylftatvrad gssrfgsdnq ygifpsgaia wkiheedfig
      661 daistlklra gggitgnqdg lgfgnfvrre rfggapiqnd giinipgtna vafanpglkw
      721 eetlnygvgl dfgfnndrfs gsidvyrnet tdlllnvqaa qpspqpfffq nldatvlnqg
      781 ielavaydiv rsedfnfdas fnvaynenei qdfdgliqag tirgqgltga faqilagnqp
      841 lfsyflrdfq gfdangqpig dtqsfvgeda lpdvtggfsm nvsyknwdfs tylagqfgfs
      901 vynntenaff tagsiqngrn vtqnvignge sgtaaasvst rflekgdfvr lqnaslgyni
      961 pmsgeglfks lrlnltgqnl flitdysgld pevssapann dllngiptag idltaypnpr
     1021 tftlginatf
//
LOCUS       WP_099572880            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            4U21].
ACCESSION   WP_099572880
VERSION     WP_099572880.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 4U21
  ORGANISM  Maribacter sp. 4U21
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Maribacter sp. 4U21"
                     /db_xref="taxon:1889779"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116612
     Region          24..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkciwlfm lfltgmtway aqqktvtgnv tdeggvplpg vnilikgttt giqtdfdgny
       61 aiqvsvgevl vysyigqate ertvgqenii nvtmaedaqa lqevvvtaqg ivrekrslgy
      121 avttveaeav earpeadigr vlsgkvagvn itannglsgs gtniiirgfs satqsnqplf
      181 ivdgipfdsg tntqsnfldg ntessrfldi dpnaiesvsv lkglsatvly gnrgrngvil
      241 ittkgsvtgd apsktevslt qsvflsnavl pdyqdnyggg fhqgfgfffs nwgprfdrtd
      301 ddgianaaqy vgdspngtai lrhpfnfiad ptliagfedl lddpypykpy ngveeffrtg
      361 yvystsvnir ggsekvsfna nygrtedigf tpgnnlirnn fsiggnarls nkltasgvfn
      421 fvrtgfkspp navstgsgaa fnggaifgdi lytprsvdlt nlpfqaadgr svyyrsgndi
      481 qnpywtvans ktsqnterfi gnmslsyefn dwmnltyrlg ldsytelnsy sqnkggvdgp
      541 vlgilrtsva rnsifnhdli lssdkdlsen lnlkatlgln srrdtfsrdg lestgqlvfg
      601 vlehfnftvp sainsfsgip inrdfeenlv gvyldatlsy kdyiylnava rndwsstlet
      661 ennsilypga svsfiptaaf dgmqgnvlny lklrfgygss agfptpfntr dvltlgarnf
      721 idsngnvisg ntvsntlgnr dlkaerigel elgmdfrlfn rlnlnlsiye kttkdlitqq
      781 tldsstgftn tfvnigeirs qgveidydld iiknqgnglk fnlagnfttn etivtdlaeg
      841 tnnilltfav ageaanyave grpfgvflgs tflrddngnr ivggngrylv dntiseigdp
      901 npdwttalip sisykgltfs anlsyrhggd iysltaasli grgtvdadnp idreanyilp
      961 gvfadgtpnn vaisstevgf nsffggdine lsvfdgttir lqeaslgyai pkkllektpf
     1021 galsftlsgq nlwfkavnfp dninydtnas sagvgngqgi dyitgpsarr ygftvrasf
//
LOCUS       WP_099573191            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            4U21].
ACCESSION   WP_099573191
VERSION     WP_099573191.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 4U21
  ORGANISM  Maribacter sp. 4U21
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Maribacter sp. 4U21"
                     /db_xref="taxon:1889779"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117211
     Region          25..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkrngllt lllalivhls faqektvtgt vtdqdglplp gvnivvegtt ngtqtdfdgn
       61 ysisasqgqt llftyigqka mrqavgsgnt vnvqmtedaq aleevvvtaq gikkskqalg
      121 yavaevdkea leqrpegdvg riltgkasgv nitaqsglsg sgtsivirgl ssfsgsnqpl
      181 fivdgvpfds gtntvdsatn rdeangsaft ngnngssrfl dldpnniesv nvlkglaaat
      241 lygtagrngv ilittkngaa gtsggvkkne itvtsslfyn eiaslpdyqd qygngfdqaf
      301 gwffsnwgps fdrdgvagwg nqaaiddagt lahpyststs aiqaafpefq garydwrpyd
      361 svekffrtgv vksnsvnfng ssedgkvsyn anfghlddeg ftpgnnlqry tlglggrail
      421 snkftvsgtm nfsntdfksp piaastgnsv fgtgsslfan lfytprsvdi qglpfenpit
      481 rgsvyyrqnn siqhplwtvn naqnrqvtnr vfgnaalmyd indnlnltyr fgldvysenn
      541 tnsqnkggig gsvatqsgil qtwnntntil dhnfiltgqy elsekigfsf nagattrrev
      601 fdqngvassg qqafgvlrhf nfqlqdeiqf fqerniagly gqldfdydrk vyltlsgrnd
      661 yvsnlskenr sifypsasls iiptkliegl qsqnginymk lragygtsan fptgypvaat
      721 ldldtqdfqd gagrdvttnt sadqlgnpnl kpelleelef gletrlfnsr vsldasyytr
      781 ttkdliverp ldpstgfiqt qtnvgeissy gveldatvdl frseeeggfn wsinsnftan
      841 etevvdlgld tdivvyagfs nlgnaarvge plgvivgsri qrdendnfiv ngagsyaeen
      901 gtftigdpnp dwllnvgnsi nyknfsfnfl mnythggdiy srttsvllgr glttdtldrl
      961 nsfilpgvka dgtpndvavn nstfyfsnvl fgpdelgiyd asvirlqevs lgysmpskwl
     1021 dktpfgslsf tlsgqnlwye ainipkgtnf dpnvagvgvg ngrgfdylng pssrryglsv
     1081 katf
//
LOCUS       WP_099573391            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter sp.
            4U21].
ACCESSION   WP_099573391
VERSION     WP_099573391.1
KEYWORDS    RefSeq.
SOURCE      Maribacter sp. 4U21
  ORGANISM  Maribacter sp. 4U21
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Maribacter sp. 4U21"
                     /db_xref="taxon:1889779"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117166
     Region          20..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkylllamtm vmatittaqq disgtvtdvn giaipyvnvq lsgtnkgtit neegkyslev
       61 pnllgalqfs ilgfetqtvp innvailnvt leesseqlne vvltalglkr etkelgyvvq
      121 sldakgvtev kavnfldnla gklagvtinq gatgvgsssk itirgeasfs nnnplfivdg
      181 vpinnnsvfn ftneaaagfq evdfgngame vnpddiaevs vlkgpsaaal ygtraangvi
      241 vietkdgsks kglgisynts ffvdsafqlp dfqnefgqgq agvfefvdgl gggtsdnity
      301 swgprldvgn lipqfdspvt lpdgtvvrgg dtsvynglpi tptefrsnps nlrdfyetgt
      361 tainnlaiss gfdkgnfrls ftdlrsesii pgvnldrqti ssrlnfrptd klqirsslsy
      421 vnsqsdnrps ngygsenvny slvawgprsl nidslrdywq pgleglqqys fnytffdnpf
      481 filqenrnsf nrdrvfgnis asyditdkls atvrtgmdys seqrqfrraf ssnrfsnggy
      541 aehdvfyrei ntdfllnynn afgdfkvdvs lggnrldqka ftgqsqttsl aqpgifrlsn
      601 aaspievfef esnkrinsfy glakfgykdy lflditgrnd wssalatpfs vdnvsffyps
      661 vstsfilsnv telpqaisfa klrasyaqvg ndtnpyqttg afiaqtpfng qptfsdqnli
      721 anpnlrpeqt aaievgadir ffgdrlnldi syynavtkdq iislpigiss gftqqvvngg
      781 kvrskgveli lgatpvvtqn fkwnstvnfs tnrstvedlp qddgrltlaf sriydsqnqa
      841 vfvqveeggr igdlygtgyl knengdfilt degryipdnt lqnlgnsnpd fmvgfnnqfn
      901 ykkwdlgfll dwrqggiivs rtralgnvgg qlaetafrpe egivpqgvvn tgteenpvft
      961 pnttavtaes fyrqfydrnh eenntydasf lklrqfsvgy tfdnlrflqq daslrlslig
     1021 rnlfaitenp hfdpeqlavq gqgfvsgied msyattrsig fkagfnf
//
LOCUS       WP_099586231             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. 2822-17].
ACCESSION   WP_099586231
VERSION     WP_099586231.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. 2822-17
  ORGANISM  Pseudomonas sp. 2822-17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. 2822-17"
                     /db_xref="taxon:1712678"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38706
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag lkasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvlv gmlnpfnnet iaklagqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adetvvengv iicgptnlag avaadasaly arnlldflkl vfnkegqfel nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_099592802             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paramylibacter kogurei].
ACCESSION   WP_099592802
VERSION     WP_099592802.1
KEYWORDS    RefSeq.
SOURCE      Paramylibacter kogurei
  ORGANISM  Paramylibacter kogurei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paramylibacter.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Paramylibacter kogurei"
                     /db_xref="taxon:1889778"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55384
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtpkeif egetrvamtp asalelqklg yecliekgag taarfsdqdy kdagvtvvps
       61 aaalfkqadi vakvrppeda eikrlrkgqt lisffypaqn eelmnaankk gahviamdmv
      121 prisraqkmd alssmaniag yravmeagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaatslg amvyafdvrp evaeqiesmg aefvfldfde eqtdgaetgg yaapsspefr
      241 ekqlekfrel apemdivitt alipgrdapk lwledmvalq kpgsvvvdla aerggncdlt
      301 vadekivskn gvtiigytdl psrmaaqsst lystnirhmm tdltpekdgq inhdmeddvi
      361 rgatatfegd itfpppppkv aaiaakkpta peptaeeiaa eqaaamkkag tqqtallaig
      421 gvlmlliggf apasfmqhfi vfalscfvgf qviwnvshsl htplmaitna isgiiilgal
      481 lqiggngfiv gllaavsvli atinivggfm vtrrmlnmfq ks
//
LOCUS       WP_099597947            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. 5M10].
ACCESSION   WP_099597947
VERSION     WP_099597947.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. 5M10
  ORGANISM  Reichenbachiella sp. 5M10
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Reichenbachiella sp. 5M10"
                     /db_xref="taxon:1889772"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110988
     Region          23..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkrllilsl alcttlfvqa qtrtvsgsvt dsangdalpg vnvlvkgtsn gtvtdiggay
       61 tlevsdadvl vfsfigymss eqlvgtksvl dvamaadveq ldevvvtalg isrdkkslty
      121 asqevegdel trvkdanfmn sltgkaagvf vnrsgsgvgg strvvlrgns strnnsvlyv
      181 idgvpmnnys psqpsdvwgq nfgvagsagt ggagrdggdg ianinpedie sinvlkgasa
      241 aalygsqaan gvilittkkg ksgkvtvaas snftsesvlm mpemqysygq tspgaldswg
      301 gavdakdhvt dffdngktwi ntvsisggne maqtyfsyan tdskgiipsn elkkhnvtfk
      361 enlsvwkdrl kldgsvslit qttknransg myfnpltgly ffprgldfde ykehyevfna
      421 drnfntqnwv nnidvqqnpy wiinrnkned srnrvignvg atvkitedlk frvrgnidks
      481 idrydqrvha stqatlsdin gryvqqnaea tqmygdallm ynktfekfsv satvgasitd
      541 sevksqffds kggddirneg veglfyantf niqniavggt alfneggyhs qlqsvfgsln
      601 lgyngmlfld vtgrndwsst lpdtdffyps vgltavisem vdipsvdllk vrasfaqvgn
      661 avnaydlgsg sfnsiipygt vttptsrvep gqtldpemqn sfevgaevsv lnqrvsldla
      721 yyntvtenqr ipivapasqg ggffyingge iinkgieaal tvvpvstekf nwtstlnftk
      781 nnnevkelpd eledgklqlt apgvnnyamm ltegsqfgdi ygqkfarnad gaiivdadgr
      841 pqiqeggldy vgnpnpdymw gwnnnfnyrg islgflidar iggqvmsmte amndlygvsk
      901 etadardagg vdmdavyadg tpyvgllpaq efyttvggra giteqyvysa tnirlremsi
      961 gyslpssvme klgpiktakv sligrnlfff kndapfdpdv smstgtglqg vhvfglpstr
     1021 sigfnlsltl
//
LOCUS       WP_099598098            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. 5M10].
ACCESSION   WP_099598098
VERSION     WP_099598098.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. 5M10
  ORGANISM  Reichenbachiella sp. 5M10
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Reichenbachiella sp. 5M10"
                     /db_xref="taxon:1889772"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109852
     Region          32..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknyylfnfr ilfaiaamiv lsigeiyaqs svvtgvieda elgdpipgvn imiqgtqtgt
       61 vsdfegrysi tipssdavli ysfvgyqaqe vtvggrssin vsmeydvasl neivvigyge
      121 iekddatgsv ivldskgfna gaittpqeli mgkipgvvvt tgggaagtgs tirirggssl
      181 rasndplivv dgmplesagi sgmanplsti npndiesftv lkdasataiy gsrasngvii
      241 ittkqggsdk lkfsyngnvs vgvpvktldv ysgdeyralm qdrvdnhglt avaldrlgte
      301 ntdwqeeiyr naistdhnls isggasvlpy rvsvgytnqn gilkennmer tslnvmltps
      361 llndnlklsl takgslvend fsnpdaigsa vqfdptqpik ngnsryggyt awttdandin
      421 slpitiatsn pvaqleyrdn tstgqrlilg gkaeyrlpfv sglkatvnvg ydyfgsvgyd
      481 amdtlaswsy repsnqvkky eqtkenslld fylnynkgle gidskidlta gysyqhfyne
      541 gfssnrpaam tngsyegask neykneyyli sffgrlnytf kerylltatv rqdgssrfge
      601 dsrwglfpsl afawqinees flrdvdvlet lklrvgwgqt gqqdigdnyy pyiptytgsq
      661 tgayyqfgns fyptqrpnay daniqwettt tqnigldfaf lsgriggsvd vyhretadll
      721 nevpiaagtn fnnflttnvg tlvnkgveva ltggiistpd ltwelsanlt ynvneitklt
      781 lvedpsypgf qtggisggen nqiqinsvgh avntfymfeq iydqngmpie glyvdktgng
      841 gtvsgdnlnk yymenpapty ligissrmny kafdfsfsgr inldnyvynn nasnlgiyqn
      901 lynqagysan iltdvektqf mtaqywssiy lenasffrmd nitlgytfdr lmtdkvsgrv
      961 sftvqnafvi tdytgldpev ssgidnniyp rprtymvgln lnf
//
LOCUS       WP_099598751            1093 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. 5M10].
ACCESSION   WP_099598751
VERSION     WP_099598751.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. 5M10
  ORGANISM  Reichenbachiella sp. 5M10
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Reichenbachiella sp. 5M10"
                     /db_xref="taxon:1889772"
     Protein         1..1093
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121372
     Region          17..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlfllssmfs faqtpvtvqg qvldekgqpl lgvsvqvqns sigaisdleg nfrfraeegd
       61 vivvrmlgmq tqqfvasnat lvikmledse vldevvvngf qvvdrklftg aaarvemsdi
      121 kmtgvsdasr mlegrvagvt vdnvsgtfgt spkirirgns singnnqply vvdgviledl
      181 sevstddfis gnantlisss ianinpndiq syqilkdasa taiygaraan gvvvittkkg
      241 qegalkvnys gnfsvkirpt ysqfnllnsa eemsvyremq nkgliditta akaqsygamg
      301 kmyvlinqkk ipwgdgggln esflnqyena ntdwfdelfn dfglqqqhsl sfttgtdkst
      361 syyslsylnd qgqtiadnvn rltatarnny yvtpklnigf kftgsyrdqh apgtrnrefd
      421 pitgtysrdf dinplsfaln tsrsmrphde ngdleyfrrn yapfnileel kynymdinvi
      481 dvstqanfdy kpldnlsvng vvqlryantt rdhtvhersn qaeayradgt qffqdannll
      541 yrdpdnpgln pvvvlpqggf nyldqsdlls ffgrfsanws kkigldhnin vltgaevrys
      601 drversstam giiyesggvv vtdpniveff nlqnidmntl deshdrfvga flnggysykg
      661 kyvanftvry dgsnqlgksq ssrylptwnv sgawnvdqeg fmqgmdflse lkfratygls
      721 gnlppdasai lnlqsdvtir ptdvepylyi adltnedltw eklhefnigm dmglwnhrvs
      781 msadyfhres fdligqvlts giggeslkfg nfadmesngi eftlntvnvd ynnfiwstnf
      841 nigytrdrit nmdygprlad aldqngaavl ggprrglfsa rfaglsssgv ptfygendei
      901 vteidlqerd nltnilqyeg pseprggggf sntftykgls lgilvtykfd ykirlndgfr
      961 asyndfvalp gelkdrwvtp gdenvtnvpt iltyaqvqvg sdvqayslyn qsdvrvvngd
     1021 yvrlksvrls yripqpwiek vklrnasvsi egqnlallys dsklngqdpe ffssggvalp
     1081 qpkmvtfsln vgl
//
LOCUS       WP_099598955            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. 5M10].
ACCESSION   WP_099598955
VERSION     WP_099598955.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. 5M10
  ORGANISM  Reichenbachiella sp. 5M10
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Reichenbachiella sp. 5M10"
                     /db_xref="taxon:1889772"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114827
     Region          29..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlftlmkc clflvmcmgm snlvqaqski vgkvtddgdg seipgvnvmv kgttvgtvtd
       61 ldgnyslevp adaealvfsy igymkqevli sgrssidvsl vtdveqleev vvvgygvqkk
      121 kevtgavasl ksdellknat pdigdamqgq iagvnvqaas grpgeksnvq irgigsvnsg
      181 algplyvvdg vayqndpnia peqiesievl kdgaaaaiyg vrasngvili ttkrgkpgrm
      241 qvdfsayagv qnitsgtplm nteemlyvee vklaadgkep lvfvfnpdal dydtdfvgdv
      301 qndnalmqsy nlnvaggqen ltlslnanyf kqdgvlinsg ydrlttrlsg eyklgkfraf
      361 atvalteent qqepwalyey aviqkpwqkg indletfgqn qvivpddnpi qygflsrqln
      421 nednrvvnss nvainleyei idglsyqvnl grndwnyqrk ffqpqylayn sdgnlqpggs
      481 niqallneef tftskntlen ilkfqrqfgk hnvgatlvls yegytsknvg vgviglqsnd
      541 tdvlsqgieg taptgtestq nligkmarvq ygfnekylls asirydgssn fgkenrynpf
      601 ygisagwnvs eegffknass lsfinnlklr gsyaelgnqs iapyqyasvi eggvnypfgq
      661 egseflgvgn vqrryanpfi qwettisrni gldlsmldgr fnfsadvyln dkqdmllser
      721 ltpssgtwqt ravstynvrt inagnmqnkg ielalgyrde tnfgltwsvn gtftknvnev
      781 tdlngvegia yaggrpvvsr gestdyttyl skgyeggaff llehegvikt deqlndylll
      841 dpnarkgdmm yrdqltvdtd gdgkadagdg vindndrvya gsgqpefeag lmlnaafkgf
      901 dfyvqayysy gaeiyngskl yaygsgrhkd lyygwspqns dsdimaarts qehnntrars
      961 dyfledgtyl rirnitlgyt ipnsvlkdkv nklrfyvtaq npftftkyeg ydpevggdgl
     1021 ftrgvdmgny pvtrkflagl qlqf
//
LOCUS       WP_099599270            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. 5M10].
ACCESSION   WP_099599270
VERSION     WP_099599270.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. 5M10
  ORGANISM  Reichenbachiella sp. 5M10
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Reichenbachiella sp. 5M10"
                     /db_xref="taxon:1889772"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117991
     Region          37..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnptllnpkk irralqclvf vfvlmggtaa waqdqriqgq vldatgssvi gatvlvkgea
       61 sigsitdisg kytlnvpaga etlvvtsigy atqevtiggr svidvtlved vqelnevvvt
      121 algveretka lgysvqevqg ddmtearetn mvsglsgkva gvqvtnsgsg vggsarvtir
      181 gesslninan qplfvvdgvp isnqvqgasg sgnlevdygn aageinpddi atvsvlkgpa
      241 aaalygsraa ngailittks gkstkgigit insnttfenp lrlpewqnqy gqgnngqfaf
      301 vdgsgsgtad gvdeswgpsm dgqlipqfds prdvdgyrgg dlnapdgssi iptawdkspd
      361 nindffqtgv tltnsisiss ssdkgnvrls ytnldqkgmi pntdlkrntl alntgvnltd
      421 klkvnasiny intesgnrpa isygteslmy lwiwygrqvn tknlsnywmp glegtrqfny
      481 nynyhdnpyf ttyentngqs kdrvlgnvsa tykftdelsl mvrtgldvyn elrdrkrafs
      541 tqrfplgmyr edrlyfnern sdflltynkq fgqnfgltvs aggnqmsqty nynetvapql
      601 lipniynfsn savnlqvsqt dtekkinsly gyaqfslknm ifldvtgrnd wsstlpvqnn
      661 syfypsatls avisdmvnlp spvsfvklra ayaqvgndtr pysltnvyis etawgstqak
      721 tesstlanad lkpertssfe lgadvrffkg rlgfdftyyd nrtrdqiipi aldistgyns
      781 riinageiqn ngielmvnat piqlsngltw dmgvnftrnr skvielaegl daytmterng
      841 ayvqareger mgeiygvgfa rvedesspyy gqiihssegt plrgsdlenq gnynpdwmmg
      901 lqntlsfkgl slgflfdirq ggivvsrtkt igstsgqlke tlygradgyd lsvegngivs
      961 egvvenadgs yspntvkvas rnwhnryyer nnveaakyda syvklrevkl sysmpnkwfv
     1021 ntpvrtvkvs ivgrnlalwt enphfdpdvm amsggtlqpg ienmsypsar sygfniniql
//
LOCUS       WP_099599321            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. 5M10].
ACCESSION   WP_099599321
VERSION     WP_099599321.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. 5M10
  ORGANISM  Reichenbachiella sp. 5M10
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Reichenbachiella sp. 5M10"
                     /db_xref="taxon:1889772"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121664
     Region          21..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrviyllam lpsmlwaqdv krisgqvtdi esgepligas vyisleaiet ersvvgtitd
       61 iegmfsfqap adaknvtvty tgyesktyti egqytegiri elkqssdmln evvltgyqet
      121 tmrkttsais kvevkdikqa gvasvdqmlq gqlpgvfvqq tsgapgapvk inirgtasln
      181 gssdplwvld gmplegddvp tdfrdkdnid llksypiagi npddiesitv lkdasatsiy
      241 garaangviv ittkngqigk arinvsagtf vtqapdyskl klmnsdqkvd felylaerdd
      301 lnylsdkgev arildsygqy dqmssggfss lspeaqaain qlrttntnwg delyqmalnq
      361 qyglnisggn knndyyfsag yfeekgstig sgqqrfnlsl kdnfkiserl klgvaifgsq
      421 nrtysylsgi daytnpayya rtanpylalk dsngeyiydp dlveredlnl qynvleertn
      481 tsnelvvnsi ksifnikyaf dwglvvnsql glqldndsqe qvsdeesyyt rkyelksryt
      541 dgdgqyqyym pqggiiqntn sndfqynwks tlnygqvfyn rhevdvllga efrettnnsv
      601 ftrgfgfnpn tlttipityd kasdnsnfdt ytktalhnay ssffgtfsyt ydntyslfss
      661 lrydgsnlfg vnpkyrylpi wsvagswnia nedflyeagl dilklrasyg iqgnidksts
      721 pyvigtygst silpglqees isslgapnpd lrwekttstn vgldfgmgsg rlflsadlyy
      781 rkgtdlvglr svplesgynf ittnwatlvn kgfefslrtv nietdrfrws tnfnisankn
      841 vvekiqahdd sfkpslegys vnaifalkta gldgnglpif ekdgqqmsav dffqlrdgtt
      901 geqltreehr elytymgdgt pklnggfnns fryrqfdlqi aanfvikqlv qrtpsyhlts
      961 vnpsrnyste ilsastnglp aligfnspgi etslvytwfn sgddgltynd ldiwvseisy
     1021 lrinsirlgy nlskntldkl rlnsariyle grnllvlstd ydyyfdpety gspyaqpipr
     1081 miaagvnlsf
//
LOCUS       WP_099599763            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. 5M10].
ACCESSION   WP_099599763
VERSION     WP_099599763.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. 5M10
  ORGANISM  Reichenbachiella sp. 5M10
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Reichenbachiella sp. 5M10"
                     /db_xref="taxon:1889772"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118279
     Region          122..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mysniifyks kttaclvill mamaaawptw akgdfpqinl eiknaslvqi faqlseqtey
       61 kfsygehiis dqsaytvayk nkqlrealdl lseeagfsyt vldqmvlvrk nqapefgpve
      121 evkgrvvden nmplpganvi evgttngvvt nvngeftiel seagarvtvs figydseeta
      181 ssanmvvqlf pslqslqevv vigygttska dvtgsltkvd sdhfrqgint spelllqgka
      241 agvrvisssg epgagvdvmi rgagsirsgn splfvvdgvp lsnadvspgg pdsgiggsra
      301 knplnflnps diasisvlkd asaaaiygar gsngviiitt kkgrkdegtl tldsyvgvsq
      361 vakkldllda ktyaannpdq vydpnvstdw qdevfrnalt tsnslsfskg tdsgnyyasi
      421 sqmdqegvit gsdferlsgr invmesffdq qrlkvklnlt asqttdhsvp tsenagatge
      481 lithmlkanp trpvydadge lfdfdtegsy nplymldfyd detrtlrvlg nlevnfrivd
      541 gleyqfnygi drsfserntt fypntteiet tgayyqqnye nynhllehyl tfskvmgdsk
      601 ldllggfsyq kfersgtmfg lrelddnsvd pannpsvagn qeaiettgfa einelqsyfg
      661 rfnytykgky lvtasmradg strfgennky gyfpsfaagw nisdegflaq ssvistlklr
      721 sswgqtgnqe vpnkvtqety sttssngyyl ngedgelvng vtytrtanpd lkwevvtqfd
      781 vgfdfdlfqg glygsidyyn kettdailll paiqpnfssv wtnmegkivn qgvefslgsr
      841 iinsdnitwt ldvngatlkn evknlpvtei lsgnvsgsgv sgetvniykn gyaagsynly
      901 ehlgfdengi sqysdekkit esalptftyg intmfryrni dlsmsiigqt gaylfnntkl
      961 atdhmsnfls sknvtedela sgqsvndalr vsdyylensd fvrlnnvrla yhfntanikw
     1021 lknltlyatg qnlvtitdys gydptvntsk nvggnsslgi dyasypssrs ymigatikf
//
LOCUS       WP_099612406             514 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Vibrio].
ACCESSION   WP_099612406
VERSION     WP_099612406.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54130
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp ssveqliklg fdvviesqag ilasfedsaf qtagativdk
       61 eqvwnselil kvnapvshde ideiallkdg atlisfiwpa qqaelmekls skninvlamd
      121 cvprisraqa ldalssmani agyravveaa hefgrfftgq itaagkvppa kvfiagagva
      181 glaaigaags lgaivrafdv rpevkeqvqs mgadflevns qeaagsgdgy akemsdefnr
      241 kaaelyaeqa kdvdiiitta lipgkpapkl itkemvdsmk agsvivdlaa anggnceytv
      301 kdqvvvteng vkvigytdmv grlptqssql yatnlvnllk llckekdgti nidfddvvlr
      361 gvtvvkqgev twpappiqvs aqpqptpakp vvekvqaept spikkllgla vgvsafawva
      421 svapaaflgh ftvfvlacvv gyyvvwnvth alhtplmsvt naisgiivvg allqigqgng
      481 vvtalafiav liasinifgg ftvtkrmlem frkd
//
LOCUS       WP_099614225             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter profundi].
ACCESSION   WP_099614225
VERSION     WP_099614225.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter profundi
  ORGANISM  Marinobacter profundi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter profundi"
                     /db_xref="taxon:2666256"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55803
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mklgipkeif pderrvaatp psvhklialg ydvvveagag eaahyrdeay eavgaavavd
       61 tralwseadf ilkvrapmdn palgkheadl mkpgaflvsy iwpaqnpell qklaarnits
      121 faidslpris raqkmdalsa maniagyrav ieaanrfgrf ftgqvtaagk vppakvmvig
      181 agvaglaavg aansmgavvr afdtrlevke qiesmgaefl qldfgdedgs gsggyakqms
      241 defikaemal faeqarevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgkvv eqhgvtligy tdlpsrmakv asdlyatnlf hllteltpdk ngqpavnmdd
      361 dvirgltvvl ghdvtwpppq pqapvspkpa pgteepsaeq qaaarrqser rsligkgall
      421 vatvaalyav gahapesflr hftvfvlacf igwqviwnvt aslhtplmsv tnaisgiivi
      481 gamlhlarae siavgimafv avliasinvg ggfrvthrml rmfrk
//
LOCUS       WP_099618382             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter guineae].
ACCESSION   WP_099618382
VERSION     WP_099618382.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter guineae
  ORGANISM  Marinobacter guineae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter guineae"
                     /db_xref="taxon:432303"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55998
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipreif kderrvaatp psvhkliglg yevvvesgag eaanysdqay ekvgaaiavd
       61 ttslwqeadf ilkvrapmkn pslnkhevdl mkdgaflvsy iwpaqnpell eklaakkits
      121 faidslpris raqkmdalsa maniagyrav ieaannfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig aansmgaivr afdtrlevke qvesmgaefl vldfddedgs ggggyakqms
      241 defikaemal faeqaeevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgkva hhhgvtligy tdlpsrmakv asdlyatnlv hllteltpek dgqpqvnmed
      361 evirgltvvr enditwpppq pespvspkpa pgteepsaad kaaakkdadr rsligkgvll
      421 vvtalalygv gahapesflr hftvfvlacf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gamlhlaqae nlavgtmafv avliasinvg ggfrvthrml kmfrr
//
LOCUS       WP_099620622             457 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Caulobacter mirabilis].
ACCESSION   WP_099620622
VERSION     WP_099620622.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter mirabilis
  ORGANISM  Caulobacter mirabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Caulobacter mirabilis"
                     /db_xref="taxon:69666"
     Protein         1..457
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46208
     Region          3..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,95,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavvavtrer ragetrvaat petvkkligq gfavtvesga gvtaaipdae yaaagatvak
       61 tlkdalakad vlfkvrgpea eelaalkpga yvlatlnpyn eratleglak akagafamef
      121 vpritraqvm dvlssqanla gyraviease aygkalpmmm taagtvaaak vfimgvgvag
      181 lqaiatarrl gavvtatdvr patkeqvesl gakflavede efknaqtagg yakemsaeyq
      241 akqaellssh iakqdivitt alipgrpapk lvsaeqvasm kpgsvivdla veqggnvvga
      301 klgevaetan gvkilgrpnl pgriaadasa lyarnllafa gllldkdgkl apdfedeilk
      361 aalvtkdgai vheqlktapa atpkaapaak aapaakpaaa kkpaapkapa aktapakaaa
      421 pkaaaqksaa pkpaakapak pkaaaakpaa kpapkkk
//
LOCUS       WP_099644737            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Leeuwenhoekiella nanhaiensis].
ACCESSION   WP_099644737
VERSION     WP_099644737.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella nanhaiensis
  ORGANISM  Leeuwenhoekiella nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Leeuwenhoekiella nanhaiensis"
                     /db_xref="taxon:1655491"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117505
     Region          22..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhlyfglml llcafangqt lisgtvttss dgstvpfvnv vavdadanti tdengyysls
       61 lsakatqlrf saigfitqta aingqqtini vlqesttdld evvitalgle retkelgyvv
      121 qtieaeevsa vkapnfldnl agklagvtvs qgatgvgsss kitirgeasf snnnplfivd
      181 gtpinnntvf nntneaaagf qevdfgngam evnpddiasv svlkgpsaaa lygtrasngv
      241 iiietkngsq skglgisvnt svfldtpfkl pefqnqygqg nsgqfefvdg lgggvndlit
      301 yswgprldqg tliaqfdspv tlpdgsvvrg gdtalydglp itptpfnshp dnlkdfyqtg
      361 vttinnvaig sgfekgnyrl sftdlrseai ipgvnldrqt vaaklnfkpt dktrfnatin
      421 yvnsgsdnrp sngygsenvn yslvawgprs ldmnslrryw qpglegvqqf sfnytyfdnp
      481 ffimyenrns fnrdrvfgnl slkhqftenl slavrsgmdy ssetrqlrra fssnrfkngg
      541 yaehdvlyre vntdfllnyn kifgdlsvdi slggnrldqk astkqsqtvn laqpgifnln
      601 naaspidvfq fesrkrinsf ygiaklgyrd flflditgrn dwssalatpf svdetsffyp
      661 sasasfilse vaklpetfsy vqlrasvaqv gndtqpyqts gafisqtpyn gqptfsnqnf
      721 ipnanlkpeq ttsyevgadi rflkdrirld atyynnltqd qiislpiais sgynqqvvng
      781 gevrtrgvel ilnatpvlns nfkwnttfnf stsrsevesl pqadgrltla ysriydsanq
      841 tvwfqveegg rigdiygtgy rktengqfil tpsgsyiadn tlkklgnynp dfmlgwnsdf
      901 tyknwnlsfl fdwrqggelv srtralgtvg gqlaetanrp eegivpqgvv ntgtaenpqy
      961 vpnttavsae tyyrqfydrn heenniynas flklrqfsvg ytfdlkdgfl glangmninl
     1021 alvgrnlfai seiphfdpeq lavqgntfvs gvedmsyats rsiglkagfn f
//
LOCUS       WP_099645964            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Leeuwenhoekiella nanhaiensis].
ACCESSION   WP_099645964
VERSION     WP_099645964.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella nanhaiensis
  ORGANISM  Leeuwenhoekiella nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Leeuwenhoekiella nanhaiensis"
                     /db_xref="taxon:1655491"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116342
     Region          25..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgllt lllalvvqis faqtktvtgt vtdgsgvplp gvnilvqnst tgtqtdfdgn
       61 ysievatget lvfsyvgfqe eqrvvgasst invslqagea leevvvtalg isrekkslgy
      121 atqevsseel tetrntnaln alsgkvagvq isnatgnlgg ssrivirgig sitqenrpli
      181 vvdgipldns nynssttqag gggrdfgdtg fdinpddias mnvlkggaaa alygsrasng
      241 viqittksgk kgkgevvvns gitfeevnil pkvqklyggg ggnftigdqg gfnqatingt
      301 tfdvvdfatd eswgpryegq qvlhwdafdp efeddylqtr pwlypendgs tlfqtgysyn
      361 ngvafsqgge dsnmrmsinn tqtegilpnt klnktsvnfn gstkigdklk vdasvnftvt
      421 dgfnrpavgy tgesvilqly qfgqtsldyn rlqafqtpdg rqrtwnrisa tnplprytdn
      481 pywvlnknta edkrtrwygt vgatynftde lyavakvygd tydfrvnqrt avgsqalpgy
      541 sesdrdfqei nyetrvhfdk nvfdnklsin afvggnrrvn efhalasstn gglvvpnfyn
      601 lsnsaenpsv setdtqrqin slfgsvslgy dnfayltvtg rndwsstlpa dnnsyfypsf
      661 sgsfiasqfi nadwlsflkl ragyaevgsd tdpyqlrnvf igddpflgsv pfslnnsnkn
      721 selrpedkrt yefgveasff nrrlgfdity yneltkdlit pvqvdpstgf tstvlnagel
      781 enkgiellvn atplmtddfs wdvtfnfakn entllslaag letlqiarfp fngvslnavv
      841 gerygqirgt nfvyddqgnk vvndngsyae tqdvqnlgsi lpdynlgirn sftykgislg
      901 flidhqkggk frsltniwgn ysgileqtaa nnireeglil pgvtgdvtyn ddgsytvtnt
      961 aentqvisaq qfgtdyffgn dnqnvfdaty wklrevtlgy slpkkwlgna lsdvrvtafg
     1021 rnllvwgldn anfdpevats gsgniqgseg gslpstrsyg lnvqlkf
//
LOCUS       WP_099645969            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Leeuwenhoekiella nanhaiensis].
ACCESSION   WP_099645969
VERSION     WP_099645969.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella nanhaiensis
  ORGANISM  Leeuwenhoekiella nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Leeuwenhoekiella nanhaiensis"
                     /db_xref="taxon:1655491"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115672
     Region          25..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrlqgllv lfavlvvqis faqtktitgt vvdndgvplp gvnivvqgts tgtqtdfdgk
       61 ytiqadpgai lsftyvgfap qsvkvgaeet initmlqges leevvvtaqg irrekkalgy
      121 svssvgsdql eqrsegdvar vlsgkasgvt itaaggmsgs gtnvvirgls sfsgsnqalf
      181 vvdgipfasd tnasgdfisg ntgssrfldl dpnnianvev lkglaaatly gtqgkngvil
      241 ittkagaaka gkkkteitvs qtyntlelas lpdyqneygn gfdqsfgwff snwgpsfreg
      301 gvsgwgnqpa idenatlehp ysttavaatr aafpelqgar ydwkpynsve effspgyssn
      361 tsvningasa dgkssfnanl gyldeesfvp gnsltrtnfs vggrsqlsnk ftvsgtmnys
      421 rtdystppva asrgngtlgl slfanvfftp rsvdlmglpf qnpidgssvy yrngndiinp
      481 rwiganiknt qltnrvfwna svsyeindnl dltyrggadf ynernvqysn kggveftgai
      541 fgylntydnn niiwdhyaal ngaydlsdkl gmtfnvgatt rsttfdqqgv astgqivfnv
      601 qrhfnyanqt piqftekrni vgvlgqatfd ydnflfltas trtdwvsnlt tennsqsyps
      661 vsasflptsa fpslksdaln ylklrvglgq satfptgypt vgiveqntqv ygdgggittn
      721 qiagfranpd lkpellseye vgfesrlldn rvsfdftyfd rvtknlivre plspstgftf
      781 tqsnvgeiqg dgieidasid wirsadptgf nwktqvnfst ynpvvteqeq daiiyagstq
      841 lfiggnaaik gqplgaivgt aidrdengnf linsagnyvi seqdndgnip vigdpnpdyt
      901 mnlintlsyk nfnlgfqfsh ikggdimsst igvllgrgli tetlnrenty ilpgvsqstg
      961 epnnvqinns tyyfnnllfg paelkvydas vlrlqelsfg ytfpskfldk tpfgalsita
     1021 qgfnlwyday ntpkganfdp nvqgagigns qgfdfingps arryglsika sf
//
LOCUS       WP_099646061            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Leeuwenhoekiella nanhaiensis].
ACCESSION   WP_099646061
VERSION     WP_099646061.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella nanhaiensis
  ORGANISM  Leeuwenhoekiella nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Leeuwenhoekiella nanhaiensis"
                     /db_xref="taxon:1655491"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123290
     Region          120..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfqslyllkl rpvflallfl glvltpkktf aqqgeiqlnl nkptlanfik aiesqttyrf
       61 vynagkidsn rvidqsvnat nlrdalaivs aklpysftvk adqiiilapg dqtgsqqktr
      121 riqgkvldps glglpgatlt ikntkqgvmt dadgnfsyil stadipntql evkflgmetq
      181 titvgnqsvf niqmqeaqne ldqviitssy gtkklkeevv gsivtitdke iptqqasesv
      241 dkmlegqlag vlventtgig gpvsinirgq gslsplnnal lgtstqplii idgvimneqt
      301 aidnnffdgg nfsetlnnpl gqispddies invlkdaaav gvygadgang vilittkkgr
      361 kgamqysfss qlgiseainq ikylsgsqyt qlrneflrnt tgatvpqngi ntnwfellnq
      421 tgvynkynfs asgatqklny rasvtyldid epqvgngakq vnsninlgyr geklnlslsl
      481 spsyiqnkqp niyynyafap nlnpynedgs faflglngtp nplaaasqnr nvsdtygvlg
      541 sfnveyqllp elklsslfgv dykdkkqdry fsaanesgqt ngtfeldgmq yprwgrrlin
      601 krnstrwnwq tqgffekrlg lhsvdllagv elaeertdln yasgigfvnp eilnpvnaal
      661 qdddpetqen drfdnqtyvf dinnnsrvsv ysqfnynyag kyfllvnfrr dessvfgsds
      721 nvaynggagv swilskenfl sdadwldllk lkasygttgn srigsysalg lysreinggy
      781 ngqneafpsd apnpnlswek nnkfnfgidl nvfrklqlsv eyyyddlkdl itsrdipten
      841 gfgslqlnaa emynkgfevs atmnwvdtda fkwrtsfnla tlqnkvtslv glgsdystaa
      901 nalaqkvgys tsaiwginwv gidpatgrdl vskdgqiydv ftyrqlfned awevignnqp
      961 dvyggfsntf dfgfglslsv rgsyqaggee lvdyqlisqy nfintrnlsa nafdywrgpg
     1021 dtnaltpvvs nsnpiaanms rflydatfik inninlsysv pvsglnvpld elslfvdasn
     1081 vaywyrdnpp agrngirefk fvypqartls lglrtrf
//
LOCUS       WP_099646091            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Leeuwenhoekiella nanhaiensis].
ACCESSION   WP_099646091
VERSION     WP_099646091.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella nanhaiensis
  ORGANISM  Leeuwenhoekiella nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Leeuwenhoekiella nanhaiensis"
                     /db_xref="taxon:1655491"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116722
     Region          40..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkklqltcf lsllfcvalh ggfyaqetvd stavqnkegi evkgyikdat tgkgisginl
       61 tienfsaais nedgsfnikv pnsntllsis gqdyqskvvp vtaensqlei llfeahysqf
      121 yelarlpsge klqysntkaa svvdfedtqw snpinesvgd flqgkvsgln svrksgvpgs
      181 gaylnlrgfn slyatnkpll vvdgmiydde dygsgilqyn sssplamlev kdiedvtvlk
      241 dgsslygtkg angviiittt rpdelttkid ftmyggmnqq peqlpllrag qyrtyltqlv
      301 asrgdsqaqi aaqpwvsdnr asgeyftynn ntnwqdqvfr ttsnqnyylr ikggddiaky
      361 glsvgylnne gvtsyssler ystrlnaslr lteklfvdan lsfihntenq rdqglaykts
      421 pfylaltksp flavnavdav gdvspnladv difgvsnpva liengigvnk nyrffgnlhf
      481 kyvfnpnfsl nsilgltlnk eretffvpdf gvadivlpta ignnrsgsev qrlysiytdt
      541 wlsyskqlsn knffdfrlgf rsqsndsesd lglgynsatd dftsvgsgsn llrfvggslg
      601 ewkwinayln adynylnkyf ltlnaavdgs srfgdsiqqg gfglgdsyya algsvsgawl
      661 vssedflkns etinllklra sygvsgnddv gnytaqqlyv sqnllgvqgl vrdnignpel
      721 kwetvsklnl gvdlslfrdr lnasfdvyqn ktedmityes ittttgfdyi vtnsgsmktq
      781 gydlslngrl lktsdfgldv glnlsryvne vtslpgepii tefggatyit hegqdanlfy
      841 gyktngvyat taeanaegls rplgngnllp faggdirfed lngdkiiddq drtvignpnp
      901 dltgsfnakl nykrlslsal fyfsvgndly ngvrynlekm sgyenqsvav lnrwvaegqk
      961 tsipratwgd plgnasfsdr wiedgsylrl ktlmlsydip tqlqyikavq vyatannllt
     1021 ftnylgydpe fsatssifgq gadlglmpqf ttmqlglrlg l
//
LOCUS       WP_099646094            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Leeuwenhoekiella nanhaiensis].
ACCESSION   WP_099646094
VERSION     WP_099646094.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella nanhaiensis
  ORGANISM  Leeuwenhoekiella nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Leeuwenhoekiella nanhaiensis"
                     /db_xref="taxon:1655491"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121670
     Region          31..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqktthily cflltvllag nfglwaqgsd qvvrgtitds sngqpipgat iaeqdaenrt
       61 vngviadfdg nfairirnsn nklvistlgy tsqtipltgk stynvsltps vdeldavmis
      121 vekqvesgll niaernqtts nvtvkaseve ntqaasidea iqgrvpgvdi vansgdpgag
      181 mqirirgtss isgssdpliv vdgmpyetsi pqdfnfgtad qqgyaallni apsdiesiti
      241 lkdaaatamw gsrasggvlv intkrgavgk pkigynftgt ymelpntipm lsgdqysqli
      301 peafmnrngv plntltvkef qydpqevywf knygnntdwv eaisqtgltg ehvlslqggg
      361 ekaryytsvg yydskgvtkg tgfqringrl nldyivsdri rfrtdiayth tsternyvnt
      421 fgtsdrdrlr siaytkmpnm siyeyddvgd ltpnyfspai niqgaypnty npvalaeyts
      481 ntqvgdrivp hfnlqvdlvp krlvstfdiq fdfnntkana flpqnatgrp ftetvvnqas
      541 dadvdiasit sktnliytpd lgdnqslqal mslqtndfry eshqaltant asslltdpsv
      601 psrtqnsdlr lytnnsqars vaglisaqys lldryivnvg lrgdgnskfs adnryslfps
      661 vstrwrvsge sfmndfdfid dlslrasygq sggtprydyr ffniygnfda eylglngvyp
      721 qniqldnlrs etltgknvgl nlqlfnkklq ldvdvyqnrt tnllfenlai ssvsgygsls
      781 dqnvgtidnq gweiglyttp iktdkwkvdf nfnisrnqni ireiseffps eqgnidrnge
      841 ykrflqidnp fgsfygyrfk gvyadldatr ardaegnviv gpngqevfmr fnypaidytf
      901 qpgdaiyedi nkdgnidsrd ivylgnsnpk figgfgptvt lnnqfkfllf ftyrlnydii
      961 ngtdmvttnl ygydnqstav lsrwrnpgdq tnipravfqg gynwlgsdry vedasflrlr
     1021 satfsysfgk nflkkmkmdd lrifvtgdnl ltftnyrgqd pevsmrggdp fgiaidysrt
     1081 pptrrftlgi qtrf
//
LOCUS       WP_099646811            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Leeuwenhoekiella nanhaiensis].
ACCESSION   WP_099646811
VERSION     WP_099646811.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella nanhaiensis
  ORGANISM  Leeuwenhoekiella nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Leeuwenhoekiella nanhaiensis"
                     /db_xref="taxon:1655491"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110912
     Region          22..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklktiyllv fgllsfsgil aqtvtgtvtd ssgnpvpgvn viekgtsngt stdfdgnysi
       61 dvsgsnaile ysalgfvtve rsassgsvin vsmeesteel navvvtalgi kkeqkalgys
      121 ltevsgeava evpqvnaina lqgkiagvni tgaatgpagt skvvirgvss lsgtsqplyi
      181 vdgipinnqn lgsasrwggs dygdgisgin pddiesisvl kggaaaalyg srasagvivi
      241 ttksgkgqkg lgvdisssyq letvmtdlye fqteygqgln gvapttqqea ldagmqswga
      301 rlgsvasavq fdgvsrpysy tgdnidkyye tgttaintva isqagenynl rfsatdlsnd
      361 ditpnaglnr ksfslnagav ladkltlnvs gkyiieevnn rprtsdspgn gnftvalspp
      421 nidvnnykpg fnedgtefri ssnvyqqnpy wtafrfknes dknrfigstt lkyqftegly
      481 llgragidqf taritsvepf gtaykprggm qeqtfnvktv dadvilgydk qitedistst
      541 ligansnyvk neqinlignd fviptlvnie nvanrnysyn lgrvkrngly fssefsfrdy
      601 lyltvtgrnd wfstlskagk tapnnyfyps vntsfvfsda fempewltfg klragysdvg
      661 ggandpyqla ltyaitdtyt atgptvslgg innsalpnen lkpfskkeye igvdlrflrs
      721 rlnldltyya nktendivni ntstasgyss asinigelqn kgvemllsgs pvknpnfewn
      781 vsynltynen evtktdndgn pifpgdaayg vnsqsgylvg ypaatlygtt fvrdadgniq
      841 ydsngapsig pnavigqgva pwtmgitntf nyknfefsfl idgkfgadif sgtsafanfy
      901 gasnntlvgr engltvsgvn aagadfstti apenlslyyq rlydiaeanv qdadfikfrq
      961 vslgyslpss llestfirsa rvsfigrnlf flmrntenid pesaynntfa ngierfglps
     1021 trsyglsldv kf
//
LOCUS       WP_099647062            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Leeuwenhoekiella nanhaiensis].
ACCESSION   WP_099647062
VERSION     WP_099647062.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella nanhaiensis
  ORGANISM  Leeuwenhoekiella nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Leeuwenhoekiella nanhaiensis"
                     /db_xref="taxon:1655491"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112392
     Region          20..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqlmlgivf lfsiamvqaq titgtvtdsy gnpfpgvsvv iantnkgttt dfdgkysina
       61 tegavlrfsy lgmqtqnitv gsdtvidvql qedteqlnev ivnalgikke kraigyavqe
      121 inseeltrns nnevlgglqg kvagvnitnt sgaagggsni iirgitslnp sannqplfvv
      181 dgipisndap tgsilpstgs napssseqfs ftnrvsdinp qnvesvsilk gpaatalygl
      241 rgangvvvit tkrgsqnglr fdvkstvgfn evgktpesqd kyregyfqev vstenlnapt
      301 gytyadgytf gfwsfgpeyg pgdrnydnfr nmfrkgfvsq ntiginagge naslygsvgy
      361 skeegivpnt dyerknikln gninitdkfn iqpsityina ggnlanggdk svmsalsywt
      421 ptidvndyll pngeeknytn gitdnpryfa eksylnseln rilanaklay efsdwfnvsy
      481 qlgvdnyydk ryryvpgdvd vgsatngfiv reginyneit snlyanftkk lgedfnasll
      541 lgnqissidi arntkrgegl aeggrlnnyf aatnffqdqt gserkivglf gdlrldykns
      601 iflnitgrnd wsstlpkanr sffypsvsls yilsqtlkda gslpdfisya kfrasyaevg
      661 kdaqpytgvy ydqptnfpfg tvdgvsrest gasnnlvpes tvgkeigael rffdnrlgfd
      721 lafykqtsdn qilpvpvaqs sgfngfvlna geietngfea lvtitpvktk nfnwditvnf
      781 stvdtevlsl pdgideiifa dsgfagvisk lekggsigdl ygydwnrnen gerligsngl
      841 pslntgervi lgnampdwlg siqhtfrykg lslslllerk qggdlydssq rnsirngila
      901 vtetryqdii idgvladgtp nnipvladqn yyrnssafnr apelmvqdas wwrlrnitls
      961 yelgskitdk lpfdrvsfsa tgtnlilttd yrgydpegsq fsagtnaygf aglnipntrs
     1021 ylfsvnlnf
//
LOCUS       WP_099647164            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Leeuwenhoekiella nanhaiensis].
ACCESSION   WP_099647164
VERSION     WP_099647164.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella nanhaiensis
  ORGANISM  Leeuwenhoekiella nanhaiensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Leeuwenhoekiella nanhaiensis"
                     /db_xref="taxon:1655491"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117781
     Region          25..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskitwcfa svflllmqfa faqqktitgt vvdseglalp gvnvlvegtn tgtqtdfdgn
       61 ysisanqgdk iifsyvgfer qsitvgaadt ysitmqages leevvvvgyg tstkqaftgs
      121 astieakdie lknfanvsqs lageaagvqv intsgqpgtv stirirgfgs ingnrdplyv
      181 vdgvpftggl nsinpsdias ttilkdatat aiygsrgang vvlittksgt stetyievdv
      241 ktgvnasiip rysvitspee siglmweakv nrqvlngstr adaidfvntn lfgggtvgnr
      301 ilapgynmwn vadgaelidp atgqvrpgvt rrytperfed aafdsairte anlrmgggtd
      361 ksryyfsvgy ldddgyaint gykryttrln vssqikpwan iganigyays etiangqtdg
      421 aenlfefadk ippiypvflr ddnyqlvpdp ifggfqydyg sesgfrprpn adnlnpiasa
      481 kydfngairn einanvnati difegmtfet rfglqyfnni ddelgnqfyg vasgsggtld
      541 qdvtertvtn flqllrykrq fglhsfeafa ahesneyrqn ftstfktkai ipggrelsny
      601 ivfptaptgt eagntlesyf gqinydfdnk yfitgslrrd gssrfyrdkw dtfgsvgaaw
      661 vvsnenflns ndlirflklk asygltgdqg gvgffsginl fgvtnvnggf avapdtfana
      721 dltwetakqy qagveldlgs wldlsvdyfv kdtenlifer riapstgiai idvndgvlrn
      781 sglefdltgh lvktanysld lsingslpnn eittmpldnq tqepavfqnv gaygyangrs
      841 iydfymrdya gvdpadgypm wyqyfndans ngvldsgees ipsltpflde npdatvarqt
      901 tkayadatql fiekkgipvv ygafrlsaqa ynfslstqft yslggyayds qyaelmhdnn
      961 ggiigtnrht dvrnrwrqpg ditsvpliad nvipnvnsqs srfitstdfi alnnvllnyt
     1021 fdsrtlsnmg lsglslfasg dnlmyktarq gflpttsqsg nsgralyapl ttftvgvrak
     1081 f
//
LOCUS       WP_099649884             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            yeei].
ACCESSION   WP_099649884
VERSION     WP_099649884.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus yeei
  ORGANISM  Paracoccus yeei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus yeei"
                     /db_xref="taxon:147645"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55426
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkesy egearvavtp ssaahlkklg hevfvesgag vragfsdaay qaagvtvept
       61 aaalindvdv vvkvrppema eiaqmrrgqt lishfwpaqn aelleaareq gitaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv livgagvagl
      181 aaigaatslg aqvyafdvrp evaeqiesmg aefvyldfkd qvqdgaatgg yaapsspefr
      241 eaqlakfrel apemdivitt alipgrpapk lwtedmvaam kpgsvivdla aerggncdlt
      301 vpdqrivten gvvvigytdf psrmgaqase lygnnirhml adltpgkdgv ivqnmeddvi
      361 rgatvthdgd vtwpppppkv aaiaaqkpke kpkeltpeek raaevaafra qtksqvtllv
      421 vgailmllvg mfapasflsh fivfvlsvfi gfqviwnvsh slhtplmait naissiiivg
      481 allqigsgsw lvvllaalsv lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_099657004             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. 56].
ACCESSION   WP_099657004
VERSION     WP_099657004.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. 56
  ORGANISM  Acidovorax sp. 56
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Acidovorax sp. 56"
                     /db_xref="taxon:2035205"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38269
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mfigvpaetv agetrvaatp etvkkltalg hglrvqsgag laasvtdaay eaagaeitda
       61 agawgaplvl kvrcpseaea pwlrsgttlv gmlnpfdaag lqrlaaagvt ayaleaaprt
      121 traqsmdvls sqaniagyka vmiaadryqr ffpmlmtaag tvkaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvggy arpmppswle
      241 rqkmevakrv aqadvvitta lipgrpapvl vtpemvqamk agsvivdlaa pqggncplte
      301 pgstvvkhgv tlvgetnlpa lvaadassly arnvldflkl iinkegalhv dmqddivaac
      361 lmahegtlkr a
//
LOCUS       WP_099666244             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Janthinobacterium].
ACCESSION   WP_099666244
VERSION     WP_099666244.1
KEYWORDS    RefSeq.
SOURCE      unclassified Janthinobacterium
  ORGANISM  unclassified Janthinobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="unclassified Janthinobacterium"
                     /db_xref="taxon:2610881"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38758
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qivvqsgagl qasipddaya aagaqigtaq
       61 eaygcaivlk vrapdadera lmasgtvlig mlnpfdadni vamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvlkhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagseilrk
//
LOCUS       WP_099693964             307 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Sporosarcina sp. P26b].
ACCESSION   WP_099693964
VERSION     WP_099693964.1
KEYWORDS    RefSeq.
SOURCE      Sporosarcina sp. P26b
  ORGANISM  Sporosarcina sp. P26b
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Sporosarcina.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Sporosarcina sp. P26b"
                     /db_xref="taxon:2048253"
     Protein         1..307
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35258
     Region          4..165
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mvfelfsrrn stelkidvye ydeillsfrt qfamlisevv nefkrgyisd ssrfwdyvvs
       61 evqielglln lrgtisynhs pdskvnylms fllstddksa ldvmdllvfl hhayssstss
      121 vkekwemavk rinrklkens lgyeivgnql irvdnqyihn evvktaiqll qehqfhavsd
      181 eflkahehyk qgdykdavvn agkafestmk tictkngydy naqrdtantl ikhlidneli
      241 psymqnhiqg lkqalensan vlrnkngghg qgevvldvdd sivrytlnlc asnivflver
      301 ykemahh
//
LOCUS       WP_099702415             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Gloeocapsopsis sp. IPPAS B-1203].
ACCESSION   WP_099702415
VERSION     WP_099702415.1
KEYWORDS    RefSeq.
SOURCE      Gloeocapsopsis sp. IPPAS B-1203
  ORGANISM  Gloeocapsopsis sp. IPPAS B-1203
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Chroococcaceae;
            Gloeocapsopsis.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Gloeocapsopsis sp. IPPAS B-1203"
                     /db_xref="taxon:2049454"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41228
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavakeie vgerrvalip dtvarlvkkg ieiwveagag essfftdtdy etagakiitd
       61 tdalwreadi llkvgiprer edgrlevdll regavlisfl nplgepeiaq rlaqrqital
      121 smemiprttr aqsmdalssq asiagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vqlnedtvad ggyakevsea
      241 akqrtqevva ehikqsdvvi ttaqvpgkka pllvteemva rmkpgsvivd iaaeqggnca
      301 ctepgkdvqr ngvtiigpin lpssmpvhas qlyaknlfsl vqllikdgnl dvnfdddivs
      361 aacithagei rnqrvkeala tfssatag
//
LOCUS       WP_099708182            1096 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099708182
VERSION     WP_099708182.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1096
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119805
     Region          126..1095
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myfklsylnl krifflvlal laiqngyskt nflenskvkn ktekatlvsi fsklskqtdy
       61 kfsygqaiia dntvytvdfs ddsvtlilsd lskkanfnyn ingklvliqk teapktisrk
      121 aidrvkvkgk vveenkvpip gafiketsss nsttsnfdge feitvgegkt ievtymgykt
      181 ktvvaqtgfm tiqlepntae lsevlvvgyg kqakkdvtga vtqleaasfr qgvnisadnl
      241 lqgkvagvrv vstsgepgag vnvtirgvgs irsgstplfv vdgmplsndd ispsgtnvgf
      301 gsstaknpln flntsdiesi tvlkdasaaa iygargsngv vlvttkkgsk gegtltydsy
      361 mgvsnvahkl dvlnaseyrn aikdksfdhg gntdwqdvif rsaittnnal sfakqtesgn
      421 yyasvaqmdq qgiirnsnfk rlsgrinaae sfldnkrlkl kvnltasqtv ddgvptsddg
      481 gsngqlviht lmanptrsvf dangnytnfn mnahynpayl lsiyedqtnt lrvlgnlets
      541 frivngleyk lnigidrsts ernttiypni tdiskigkyv qnnldsknsl iehyltyngt
      601 fgkhkvealg gfsyqkfers gtsfsiegit dkgvgvkpei npgfkgilpv lsgyaqenel
      661 qsyfgrlnyt fnerylltas mradgstrfg dsnkygyfps falgwniske sflenieain
      721 nlklraswgq tgnqevenki tkasyslsga dgyylyddln lvngvsvvrt anpelkwevv
      781 tqsnlgldfn lwrdklygtl dyfnktttda ilnvtsplls ptptvwtnls nqgkivnkgf
      841 efmlgsklvd tkdftwnvdv ngatlnnkie dlpiseiltg tisgpgqsgv naniyksgya
      901 agsfyllqhi gfdskggnif kdqngdgkid nsdrviiega lptfyyglns dmryknftfs
      961 fsiigqtggy llnntglnal ninnlasdrn vstnyyesga nptnspilst lfleksdfir
     1021 lntarigynf dlkglnwlng ltlyvtgnnl vtithysgfd plinspkpsq gnqsigidya
     1081 ayptsrtfsf gatlkl
//
LOCUS       WP_099708501            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099708501
VERSION     WP_099708501.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123613
     Region          77..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknqfnpvna elltkqkkif lwtkknsiff fvtlcsissf ghtvkfslhl ekgeimehte
       61 ktkaernlnl vvddnpitgk vtgelgeslf gasvkvkgtn kvestdvdgs fsiaakegdv
      121 livsyvgfit kevtvgsqkq lnirlksaqn dlsdvviigy qkvhkknvna avstisskdl
      181 qdipvisvss iigslatgiq tptqtgapgg rgslvirgnt smsgsgyssp lyvidgvqts
      241 ledlagynts ntdflaslnp ndiekidflk dasaaaiygs rgangviiit tkkggaldkp
      301 eftfslntgi spipnlvtmn igsaernakm gmlykwwksd dvqtshvpmv lsdslnpafn
      361 nkvdyqglfy rtgisnkynl smrggsettn yrlslgyddv qgviknsgfk rytfsgnins
      421 kvgqnfenqf rvnllqtdnq tgqgnpdggr fqfnntlptd psnlnsslfy vsddkikalq
      481 gelsdklntd etvqvtlsdf lkydftpafs vnaqfnyvys sekknyyeps svreegdgfa
      541 syalynrknl ssdlyinyyk kfgnntvtav lgqktdynky edmfmyakgf gvdaikvind
      601 rytqgqingy tsiesnalls yfgrlgyrfk drymvdvafs rdgssrfged vryanfssia
      661 lgwiisdepf ikkitgnvls yaklrasygv ngneidenfl rygsyrlgyg gnplwsnlmn
      721 vstyggttgv vtdyntignp nlswvnskqw digfdmdlfn nrinitfday nkktenllfe
      781 tlfpaysgfn qaksnvagvm nygweamvkw qifsvgnpwk leistgmsqn knfvtklpng
      841 nkdyygydag rdrsygyvvg mplilpvqfk yeyivdnlnq lpinpytgei lhgksawgti
      901 apgtpiwkdy ngdylldeag dykldtsfkp tpdftgllni nlkykgwylq aysqfsfgsd
      961 iidsstqryl dnydrgddwa vkglqdlsgl yfwenpgdga agahypalyp arpnttpyyr
     1021 frsgqslwke sgdywkisna sigytieksr vleqihisrv riygsvinpy qwqrskvvad
     1081 asqvdemgyt lgngypqskt fslgldvkf
//
LOCUS       WP_099708517            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099708517
VERSION     WP_099708517.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121207
     Region          26..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllyesll vflmvlcsqg vsaqnktisg vitdsanmpi pfvtvkekgt kveasadeng
       61 aftisvkega tiivsligfk ttelkavdgm kiklatatne ldgvtvtalg qtkknksigy
      121 atsvikadal vktasptian glygkapgvr isstpggaga iniqirgins itgrnqplii
      181 ldgvpirdge vnnndywnqq rvknngladi npedienisi lkgasaaaly gseavngvvl
      241 itsksgkgkk glgidfstsy sgneiaylpr fqyergpgwt nanystgyla pdgfahydvd
      301 gngtfetrgv snsgnnfgpw fdgkpvmtwd gvirpysaqr dgyknmfqns wdsttnfals
      361 nntenssirf sytrieseal smgnnnkknn fnlnasfktg klktdvivsy mnqnlqnrtf
      421 amdrlvnnft gmlspfdngd wykakyktsl gykyvigkdt qsltpieniy rngfrgdiad
      481 yfwntgakqq deitnrlias vtetlsvtkd lalrgrvstd ltainienkn pvevplvyef
      541 gnegdrsgsf mmegqdynil ygdllatynk kinedfgina vvgysatret yrtlsrstkg
      601 glsvegwydl kssigiatsd skreetlkda vfgtlsgsfr nylfvegtir rdrtstmnpn
      661 nnaftypsvn ssfvlsdavk lpdfisyakm rgswgivgsy pgryganvaf iqntlgtqgt
      721 pnpvlttnsq dkygnegikp emkneyelgf etkffdrrlg ldfsyynaki kdqildltla
      781 pttgassila nvgelsnkgf evaltgspfr tanfswdvtl nwakninkvv klangatell
      841 hadydgsaaq lksvvgdpmg giyahpvktd asgkdmvdsd gflmidgdkw vkygsampkg
      901 vggllnsfty ksftldvnid ysyggslmpt ginwmtargl teeslkystn erggltyyme
      961 ngkgvqvpns atagpggqvl yrdgmlmngv tadgspntnv isqagyynmt ynwggpqyss
     1021 sryelyiqkn dyvklrevsl afnvpaayas kfgatklsls ffgrnlfyiy rtikdmdaea
     1081 ttagtkwtqn vnnagltpst rsygvmlras f
//
LOCUS       WP_099708633            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099708633
VERSION     WP_099708633.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109056
     Region          22..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiflifmi vftaqvslaq vksvkgvitd aegmplpgas vavqggqkgs stdfdglyti
       61 evqkgqtlvf syvgletqsi vvgdvstinv kmkqassnal nevvvtslgi krskktltya
      121 aqevkgeevt rvkdanlmns lsgkvagliv gkssagagga vkvtirgnss atnnqplyvv
      181 dgipllnsts amsnqvfgdt aggnrdggda ismmnpddie smtvlkgasa aalygsqgan
      241 gvilittkkg kegkvtatyn asvfvdnvvs lpdfqtnyga dpssdktwga akkspdhvkd
      301 fyntgvtmin sisvnsgtdk sttsltyant kvdgviptne fkknnialrq svklfddqit
      361 vdaalsyaeq tidnkptngl yfnpltgvyl fprgndfady yknyevfnpa rnlmtqrwps
      421 qtsdiiqnpg wilnrnasid knqslissaa itykannwls ikarggynrl yntfdkrmya
      481 gtnetlapst gryiysdses yqlygdliat intkfnddfs fsanlgtslt kstindayvs
      541 dsgqknglvn anwfntgnfv saernahtig gkkevqsvfa satfgykdml yldvtgrndw
      601 sstlvntdnl sffypsvgls ailsqmvtlp eaisyakvra syaevgndvs afltspvntl
      661 vggvvtppiv gpkpgsslkp emqnsyefgt ewrflnnrig fdftyyrnet knqlitspap
      721 ipnttgytny afnagsienk gfeitvtgka iqtdnfswdl glnyasnknt vldlgkgang
      781 evntviltng dpnsyryvmk egqpfgtiqg knilrnaqgq mllagvgada laqktdwvdm
      841 gssnpdfmlg fsnsfkykkl tlnvlidgrf ggnvmsltea mldsygvska tgdardaggv
      901 kvnaidgngn pvtvmsakny yssvgdraga tgeymykatn vklgelslgy tfdfsketvf
      961 ktvnlalvgk nlfffykdap fdpnvtlssg eglqgvdifg apstrsigvn lnltf
//
LOCUS       WP_099708636            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099708636
VERSION     WP_099708636.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115416
     Region          22..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqimlifmi vftaqvslaq vktikglvsd qnglplpgvt vviqgtktat qsdydgkyti
       61 qastgdvlvf syigiktkav tvagsatinv vltedaqnln evvvtalgik rqkkelgyav
      121 qdvkgdqlsk vittnvasgl sgriagvdvs lpatgiggss rviirgissi gesnqplyiv
      181 dgvpidnsgl nndsaaaskw fdgrdngdgi sslnpnnies ltvlkgaaas alygsralng
      241 vilittkkgs kgklqvelts gvsfdrvnak ykdfqgdygs gshgvlpdpt kapeelygyt
      301 tsawgpkfsn sigqqvkifd gsmkpyakvd nniqdffrtg ftttngials ggsetayvrf
      361 gynnlknddv ipnsglernd aslnatlksd kftldanvny miettanrpg lgdspnnvgy
      421 slsslapnid qawlqhykne dtgeiykwnn niyqlnpyft vdanhnsskk nrfmgnvagt
      481 yqfakwvglt frsgldtylf tskdfmspgg twparetgyl glnditvsem ntdvianfse
      541 iklatdltfs gilganrrdf rrqenssfgt niiepgteyi snfanqtina psvtktrtns
      601 vygsakldyk gylyaeftgr ndwfsvinkd afypgaslgf ifsdafniks dtfsygkfra
      661 swakvsnapg ayknslnytt yssydgqsvv nvkntsapna nltyqtkkgi efgletaffk
      721 nrlraditvy redtsdqtld lassatsgye flsvnagelr negieiflsg tpiktkdfew
      781 gidlnfsknk nsilslhpdi ntytisearw anaaivaqvg gqygsiigrd fqrtpqgemi
      841 vganglptyt enkvvlgkgv pdwaagltnr fsykgitlqf lldmkfgmdv ysmtnslaaa
      901 kglldvtteg rdefiaartq aaandpnfvf kdwvptagyv angvvntgta dnpvyvkntk
      961 pvdpqeywrs vtdatpapfi ydasyvklre vslgytipks vfegakinsi yvslfarnll
     1021 tfnkdlpnid pesmytsgng qgfeygslps rqsygfnikv tf
//
LOCUS       WP_099708699             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099708699
VERSION     WP_099708699.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108071
     Region          24..979
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkriktkfll lllllpfcvf aqntisgivl ekstkqpipg anikvlgtni stttdfdgkf
       61 qlsgvkadsk itfsytgytn qtiavagqkn itvnleednn qlkevvvqvg ygsvkkkdat
      121 gsvtalttkd fnkgnnitte nllsgrvagl tvnstgapgs ssqirirggs slfasndpli
      181 vidglpldna tntgsssfla slnpatvesi tvlkdasasa iygsrasngv iiittkkgsk
      241 tlsvdynvqy aagtltktvd vfsadefrsv iadrrsddls klgtantdwq raiyrntgtv
      301 dqslavrgsl fniiptsltl gntdqqglrl tnefkrntvg lvmnpvffdn hlklrlsany
      361 tnernrftda vegaaigfdp tqpikvdgap yggyfeyttg vdangnyplv staarnpvsq
      421 llntndrgin drffgnfeid ykfhflpalr avvnvgfdes ngerrrlvga dagsapsnnn
      481 ipygtneyte atrrnklldt ylvynktfks lnfeatagys yqkfqsskfe tgnilnpdlp
      541 stfpettldt dvvllgffar tnlnfrdkyl ltlsyrrdgs srfeeanrwg nfpsvafawk
      601 ikedffkest visdlklrls ygitgqqdip epngylqkyq vgggnseyyf gtspvpvalp
      661 skrtnnlkwe etssynagld fgfldnrlsa gldvyykesk dllvnaaisd gsnfsnrvyq
      721 nvgsfttkgv eftinanaik tldfnwnmnf niskferrik nlvngtdifl gdniagtgtp
      781 gqifregytp ysfyvykqly nnegkpidga fadlngnnik ndsdkyiynn pdpdftlgfa
      841 snmnykkfdf sfnlrasign rifnavdasr aqydamengg vlsnipkqvl dtnfqttsnv
      901 vlsdlyiena sflkmdnitl gytlnnwlns kaslrfstgv qnvfvltkys gldpeitnng
      961 vdktiyprqr svlfglnlkf
//
LOCUS       WP_099708980            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099708980
VERSION     WP_099708980.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123512
     Region          21..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlfymlsf llalsgyaqe rtikgtvvda kdglpipgvt vfvensavsn ntqqkgviqs
       61 sslgtvtdfd gtfefkinsn mkslrvtymg ylpytidiss qnnytislks dvaelkeivv
      121 tgyqkiekrk ltsavaqvem adikqagvas ldqmligqva gvavtqqtga pgtiskirir
      181 gtaslngaqd plwvldglpl egndvpqnyd kdnidvlsnf siaglnpddi kditilkdaa
      241 ataiygaraa ngvivvttkk grkgnmkvdf nvntfvtqkp dfsklnllns sqkvdfelsl
      301 asredltyrd tageisriln qanelgayrs ggfsslsptt qnsinalrsn ntnwgdllyr
      361 aafntqygls lsgggersdy yfslgaynee gatvgtgfdr ynltlknnfd vtdklhvgvg
      421 ifgtqskkts ylsdtdgftn psnysrnvnp ylipfnadgs ykydkdikgy gngtvavpfn
      481 fleerentny elitrsvkal ldvdynitkg lkastqiglq fdnnssekya gketyytrke
      541 rektsvfsng aysyflpvgg iiqnsntdff qynwktmvny nttlggkhel efmvgnelrk
      601 nkstsintka fgydpktlts tqiifptany aadtnyrtyl knenenafas ffatasytyn
      661 rkytffgsvr ydgsdlfgad pkykylplwa asgswavsee nflkdndvis nlrlrasygl
      721 qgnidkntsp yvvgtnqttv ilpgqtepvi svssppndkl rwekttntnv gmdlglfknr
      781 inivtdvygr kstdliglqs lavengfeyt nanwaqvtnk gyeislstrn idhpnfkwnt
      841 tinfahnksn vdriqtrsns ylpsreglpv navfalktag idengyplfv nkkgetvnsq
      901 tffalfdpya dffpgvlsqs kltdaetrdl ftyagdldpk ftggfmntfk ihnfdltiat
      961 tfnikqtvve kptfngtsld rgqnyttdal nawsptntgs hipgitspts gtgdswmayq
     1021 wyspgaaple mynyldtwvh emsfmrvssi rfgyslpkka inslfmenvr fsiegrnlfv
     1081 issdykgyfd petfgniyaq piprsislgc nltf
//
LOCUS       WP_099709394            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099709394
VERSION     WP_099709394.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116514
     Region          27..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfkffqrkt vvlffvllaq falaqervvs givsdnagmp lpgasvlikg tktgtqtdfd
       61 gkysikassn svlifnyigm ktqeitavnt tvnvvmaggs eqlqeivvta lgvkrekksl
      121 gyatqeikge dltkvntgnv ansisgkiag vqirrnnnig gstnviirgt tsltgnnqal
      181 wivdgiplnn dntnsadqks ggnvggydyg naaadinpdd ietmnvlkgs aasalygsra
      241 sngvilvtlk kgskskgglg vtfssgitvg vvdkktlpey qnqygggygd fygtvnlgsg
      301 vhpyaatdda swgpkfdpnl lvynwksfyp qlpgygkatp wtavqenpns fyqksvtyin
      361 nvavagsnen gdfrfgytny nmdqgilpns dnrkdnfnfs asynlkpktk isasanylka
      421 nakgmnetgy gdggnnflss irqwystsvd fkdlrdaynl tgenttwsva gptdlaiqfh
      481 dnpyfqrynn yntlardrff gnvnlttqvn dwfditgkga vdyyhqlqee riavgskrtp
      541 nalgqytryd ktfrevnfdl ilsfktgitd gikfngmvga nsrrsisnsi yaatngglvv
      601 pgiyalnnsi dkinspgesq ttlgtnsiya nasfnfldty flegsyrvdq sstlpkdnnt
      661 ysypsitgty ifsnhiktnw lsfgklrlny aetgndapfa vtsatypkgd nfgpdgirfs
      721 tensksnsnl kseltkgfea giefklfknr lgfdfsyyks nttnqilsie tpsqtgytra
      781 winagdvqnk gfevtmnvip vktenfswev kvnwstnkne vislggadri slgsfqgvgy
      841 vaevgkpvgq ligsgftyln gqkvirsngr ylqtagatig dvnpdwiggv nnaltyknft
      901 fnflidvkkg gdvysldqrf ghttgiyest vsnnhlghpq rdpiangggi llpgvkedgt
      961 pndkivsveg sngysfynsm peqqyvydas yvklrevgls yrlpskflak tfisnmifai
     1021 ngsnlwiisk nlpyadpeag lssgnlqgfq tgvlptskey nfnmkvqf
//
LOCUS       WP_099709537            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099709537
VERSION     WP_099709537.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115799
     Region          25..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv lllvlmaqls faqertvsgt vsdnagmplp gvsvlvkgtk sgtqtdfdgk
       61 fsikastsqv lvfsyigmkt qeiaassslv nvklgdaaqe legvvvttal gvkrekkslg
      121 yssqlvtaeq vnssptnnfl nnlsgkvagl eikansnfgg stnivlrgvk sitgnnqali
      181 vvdgvavsna nlndtdsqng rqgfdfgnsa sdidpnnies invlkgaaat alygsqasng
      241 aimittkkgk knsalgvsvs stvsvgaidk stmpryqtqy gegyggedss ytadvfgnpn
      301 glvastgdda sygnkfdpni mvyqwdafvl gnpnygkatp wvaakndpks ffqksttytn
      361 nvnlsggdek gaynlgftni nntgvlpnsl lnknslngnf srdlsdklts tafftftdqn
      421 ttgrnntgyg dnfiggfrqw wavnndikel ereynrtgqn ttwnqtdpts gnlapafwnn
      481 pyfdryqnye qdsrtrflag tslsykitpd fvllgratid ysndqqelrk avgshaetfg
      541 isgandgsgy slykrdfmqq tydfiatynf qlgenigaka lggytylrsd aysiqssttg
      601 glaspglysl ensnvflpar esqiayeksg lyaqlsldyk kflflegsfr ndkstalpte
      661 nsnynyysig sslifselvq adwlslgkvr inyaqvgndp aagrlgakvn nygidgnplf
      721 gnsptyldfa nlkpetqkaw eaglemsmfk nrlnfdlsly ktntedqifn vpqststgvn
      781 fatvnageie nkgielalsg kviktqdftw dlgvnwstnk ntvvslnqgr dnlllatfqg
      841 gaslnatvgq pygtlrgkdy tydangnkvi dadgfyvlas nkvigntqak wlggisnkfs
      901 yknlslnfli dvkkggdifs ldqaygqetg iydlgindlg nsvrnpltng adsggvilag
      961 vhadgtpntt ridastsggt afssdvnptk ayvydgsfvk lrevgftytv psqildklkl
     1021 kglsfsvign nvwiiqknlp ysdpeagssa gniqgfqsgv mpatkvysfn vklnf
//
LOCUS       WP_099709539            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099709539
VERSION     WP_099709539.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113736
     Region          27..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv lllvlvaqlt faqeravsgv vsdnsgmplp gvsvlvkgtr tgtqtdfdgk
       61 ysikastsqv lvfsyigmks qevsaattsv nvklkddsve legvvvttai gikrekkslg
      121 yasttlnsee lnkssqgnia dalkgkvagv tvssastdpg assgviirgf sslygnnqpl
      181 yvidgipinn gstysdslsg gydfgrgsgd inpedietms ilkggaatal ygsrgasgvi
      241 iittkkgkag kmsvsfanat sfteilrtpk yqdqfgqgwn gqhvliengs wgpkfdgvvr
      301 pwgsvvdnsq kikpysfqpd qlehffdtgt nalntlsisg gtgdtsvrls ysnsqqdgim
      361 psdadkfern tlgisgtskv nkmtitgsln yvntggsava tgqgltvmnn lmqiptdlpi
      421 tefknykdkf nnvsnyytpy gvtnpyftln engskyakdr vygsielkyd lnkwsnlvyr
      481 fgvdqssesi alweervdaa pgspndgsst espgsysesk titkqinhev lynldftlns
      541 dfqlqstfgf nmnqrtgsti sgavgsqdil gfhsldnsse tavatssrse rklyglynst
      601 slsfknqlfl ttnlrndwys tlpqgsrsvl yggvnlswaf tdtfpeiksv vnfgklrany
      661 getgvdtnpy qvqsvytkgn vglgfgnlty pfsgvngyev dnraanpdlk perrkeyefg
      721 ieasffknfi nidlsyydsk vvdqiiplal asttgyttqi anvgtisnkg feglvtfnwi
      781 kakstgfgws ttvnyaknns nlveldprlk qlnlggttsi gliaqkgqpl sliqgsvper
      841 dpqgnivvdi ngipvastqk qvygdtqydy tmgigntlsy knftldfsfd irqgglmfsr
      901 taditrftgn sitttynnrq pfivpgsvvk ttaadgsvty apntvavdsa hqddyyssda
      961 laretvidks fiklrevvlg yefpkkllgn apiqslslsv igrnlflwtp ksnqyidpet
     1021 stfgtdlsgq fgefsanpst rslgfsvkan f
//
LOCUS       WP_099711136             907 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099711136
VERSION     WP_099711136.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..907
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=99435
     Region          25..907
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlkftcllt flalimmqfs faqermisgi vsdnsgpipg anvtvkgtks saqtdldgky
       61 avkaktgdil vfsymgmqda vvtigasstv ntklkedgke ldevvvvayg kakkssytgs
      121 atqikseqle nrpltnalsv legstsgvqv qssagqpgsa pevrirgfss vngsntplyv
      181 vdgvpfagdi sninsndies ltvlkdasst slygskaang viiittktgk snkdkfslnv
      241 stgmtsrsik dykrvdayqy ypleweairn srpmatqaqi daaniyasgr vgtvlvtnpf
      301 nvpigsvvgt dgklnpnaql lypqdldwek qleragvrqn vdfsyqgkse ksnyfaslgh
      361 lneegyirnt gferttgrln lntslnnwfk tgvnisgtlt nsklgtdgva ntnsfnnpfr
      421 tirymgpiyp vfdhtengdy vlddngervy stlrgsgasn grnivyetln ntdvkkglal
      481 sgrtffeisf lkdfkfttna sidktysnrt ysyntligdg sptglmsked riftgvtynq
      541 llnyskkign hsvtallghe sfdyernwta gvktgqvapd niefinyatv ttlesitrny
      601 stesyfsrvg ydymdkyifs aslrrdsssk fakdnqwgnf wsfsgawivs kenflsdvsw
      661 vndlklrasm gqvgndshia sdrdedgtit nglnyyigqs tyklgndngg eggviiygsa
      721 atdlkwevnt qkdvavefgl fknrlkgsie yynrntdgli fdvpnalssg ldyrvenigs
      781 mvnkgfeitl dgvilktndf swslnvnast isnkitklpq keiidgtkkl tvgssiydyw
      841 lrdwygvdpa dgyalyvadp nlivagdstq rvvngvnvtt dqnkalyhya gsaipdlfgs
      901 fgntfky
//
LOCUS       WP_099711206            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099711206
VERSION     WP_099711206.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111577
     Region          23..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllfilfg iilfaqpvla qtktvtgtit sstdglslpg vsvliegtsk stvtdldgkf
       61 siavnegetl vftfvgfask kvkitagtns vnlkmteeln tlsevvvlgs tvratrkelg
      121 navtsikged lvkaqpggls talqgkiaga qvsqnsgdpa ggfsiklrgt ssilgssdpl
      181 yvidgvvlnn attnvtnlnv ttgnsnmqig qnrsadinpn diqsvevlng gaaaaiygsr
      241 aangvvlitt kkgvagetry tfstsvtsnq irkkldmnms dkqfvstspa lfpiqgnpas
      301 pttvtvlgrn letrttdvkr ydyqddifgt gvgtdtyfsl qggdektkyf aslgylvneg
      361 ivkntdfkra gakvrlkhdf nsklsatvgl nyvnsssnek pdgnvfwspi nainitnnty
      421 dihrrdingn lmavdpnrvn plsiiedfki tqntdriisd lqlnytpfkn fnadlifgid
      481 nynqrgnvfi prypyvvnpa yyndgyvsea snrvvqfnnd lnlrylwnin dkwkattygg
      541 ynvqtyrddf aaiegrnlkp fietinafnt lipgspsssq skynlwgyyl qetvgykdkl
      601 yltiagrqda stifssdnrs qfypkasasy vlsdekfmeg ihdavssvrf raswgksgsl
      661 taikpyarft nystgtllgn stftiegfkq gnldlkpeqs vtyevggdfg flkdrlnlsf
      721 syynadiddl llpvqlaase gatntiknig qmnnkgyein lkydlikken lhvdvfvnys
      781 snrnkvtglp qqrfkldsnl agapvfvemn kpigifygty farnsdgsll ltpdgypqte
      841 kgdvatgapq rdangqptgt ilnkqignpn pdyviafgan vnykkwglsv lfdgvqgvdv
      901 fdadyrtrqg vgsgtivtke lngelprgyi wsiynieefr vvdgsylklr evslnysfgk
      961 lnnffddlti tasgrnlisw dnftsfdpet nsggqssvak ynfgtvpips syslavkvqf
//
LOCUS       WP_099711773            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099711773
VERSION     WP_099711773.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109266
     Region          23..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfifsfla llllpaymsg qaikgkvvds sgmgipgavi sapqsrtsvd adfdgnftin
       61 akegeslkvs mlgfdavtvt atsgamvitl keagdtalke vvvigygtrk kidntsavss
      121 ikseeitkmk vinasqaiqg kaagvqvsts dapgstpsvv irgagtalgg rnplyvvdgm
      181 ptdninnint nditsyevlk dasslaiygt rgangvimit tkagkgkltv dvesfagfrt
      241 plksvkmana deyvrytnaa fskdypsgrf sanqpyntnw fdeitrtgsy tqnnisisgs
      301 senvkyffsv gnyeekgiln gsdygrttfr nnnefklsdk vkltqnfsvs sikntpmpls
      361 aftnayrqsp lvpvryadgk ygvpfvkdgi vgetgdsfnn vgnpvaqldy tneqqqtvtl
      421 qgglkldydi ikslkftsqf ngefytykqy nyvdnialws aadptrivad ypkdlnintl
      481 trsrdqyfnw nlsnyltfnk vfadihdiev tagieanvqg trekltidrk nvnansnyws
      541 lkdvnvagnv tglkdealnq rrlasyfarf qyklmdryll tgtvrrdgss qfaddkrwgt
      601 fpsvglgwiv skesflsnve pinllkirgs wgrlgnqnvp lntqlltsgl dysnlgsgtt
      661 insqvdpnls weiveelsgg fdfevlnsrl kgsfdvydkn ttntilnvkp ystsgitvat
      721 pshigevsnk gyeislrwdd kindnlsywv ggnfshnkne ltslknvqln piiggslgng
      781 qntkildnts vgqplgsffm yeyagvdptn gqmlyykadg skvaqsglde lkdkkyvgsl
      841 lptsnygvtl glnyknidfs vdgygtggak vyngkkaqrf ggenieasva rdfwtptntt
      901 ssnpapsnat pvastyyles adffrinnit lgyklplrdd qfisfcriyv nainpfisqk
      961 fsgfspdvts dgklvegtqg veldaypslr sfviganlkf
//
LOCUS       WP_099712054            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099712054
VERSION     WP_099712054.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115609
     Region          32..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklnryay lcillisigi kaqetkpliq sklegivida atkepvigas inikgtthgv
       61 qtdfdgkfyf qtgqkfpytl ivsflgykrl etvvnqnsvv ieitqeqnal sevvvtalgi
      121 skekkslgyt tqavkgkdlg etketnflns lsgrlagvri tnsqgdmgss rivirgetsi
      181 agnnqplfvv dgvpvdnsql gsvggatrdf knaiadinpq dietltvlkg pnaaalygsr
      241 aahgvvlitt ksgknqkglg itvntgitvs qvttlprfqn sfgqgsngkf sfvdgkgggv
      301 ndgvdeswgp kldgrlipqf nsngvavpfv ahpdnvkdff ntgltydnsi siaksddksd
      361 frlgvnnqkq lgtvpnsevn ktnftvntny qiskgvrvgv nanyivtdap alpggpsgnr
      421 aagvmlqflw fgrqvdteel qrnrnvnwnn syysnpywna yynttsqqrn rligdihlda
      481 klaegfnfkf rtgidyyndr rkyeikygtn gtpfgsyaed aytvseqnte giftytkkln
      541 ddfsldalag fnvrthsdan nyqkaprlav pdlytltnsr dpltssniys rlkvysayas
      601 aqfgfrnyaf fnvtarndws stlpsnnrsy fypsingsvi ltdalnlksn tldflklrgg
      661 wsevgndadp yqlstvynfq tafdgnpiqt ssqkklndnl kpettrstev gleasfwknr
      721 lhfdfayynt nsldqileik ttaasgynsq linagkinnh gveiqldgnp vqtenfkwnv
      781 avnyaknisk veildydkqi qnytigtsgg vdvlasvgqa ygalygtayl rdangnivvg
      841 anglpkadpq krvlghytpd ytggvtntlt yknlelsflv dasvggqifs gtnrtgnytg
      901 vldqtmpgrd aangglsyyv tgttktllpa gatapggaqv yddgmifkgv yadgtpnntl
      961 lsaqeyykas yniseaylys styvklrevk ltynvdkklv kklglagasf taagrnlffi
     1021 ykdapnidpe safntgnaqg leslslpttr svslnvnlkf
//
LOCUS       WP_099712302            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099712302
VERSION     WP_099712302.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111666
     Region          45..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiisfymgg rafcylffmg fllasapvqa nhsvrprsek lqqsqvqgti tdgssplpgv
       61 tvslrgksss gvisdfngqy sisaspsdtl visfigckta iipirgrkki diqlvydttv
      121 lqevrvnagy ysvkesertg niaritskdi esqpvsnvla tmqgrmagvn iiqstgvpgg
      181 gfdikirgqn sirtdanapl ylidgvpyas dpigynqtst vyptttspln sinpdniesi
      241 evlkdadata iygsrgangv vlittkkgka gktaftvnas tgvgnvtkfm klmnteqyla
      301 mrkqafindg vaynpwdydv ngtwdqnryt dwqkeliggt sritdlqagl sggsettqfl
      361 lsgnyhtqss vfpgdflykk ggsqinlnhr sqdsrfrltf sagytsqnnd qpafdltyda
      421 rslapnapal ydeqgnlnwe ngtwdnplrn lnakfesktn dliansvlsy elspglviks
      481 sfgytdlstv etrtspstiy npaynissas silyvnntdr sswsiepqis wekqlgrgkl
      541 dllagttfqn qnttrlyqsg tgfssnsliy nlasanyikv llndetlyky qaffgrinyn
      601 fdkryiinla grrdgssrfg pgnqfatfga vgaawlfsne nflknsswls fvklrssygt
      661 tgsdqigdyq ffntysttgv nydgiiglep trlynpdfgw etnkkleaal elgffkdrif
      721 ttaswyqnrs snqlvgvplp gttgftvlqs nlnavvqnrg leltlrtsnf sreqfswtts
      781 fnltfaknkl lsfpglessp ysqkyrigap lnmqlvyeyk ginpetgvye fedlnkdgki
      841 tfpedrqkvv dlnpeyyggl qnqfrfknwn ldflfqfvkq knrinsmgya gqmsnqstll
      901 tdswqttgdn atyqlyttgn nseavtadyl yersdaaitd asfirlknis ltyqlplqln
      961 avqcklmlqg qniltftryk ygdpeftssg ylpplkvvta giqltf
//
LOCUS       WP_099712722            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 9].
ACCESSION   WP_099712722
VERSION     WP_099712722.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 9
  ORGANISM  Flavobacterium sp. 9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Flavobacterium sp. 9"
                     /db_xref="taxon:2035198"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113794
     Region          37..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklislvf iggvifsana kevaitkhlf eqkssqievt gqiigqddgm piagatiyae
       61 snskiatisd engrfklnvp eneshvvisy mgyqttnfpl iqttnltirl kpaenvldqv
      121 lvtalgvkkt skaisyavte lkgteftkak etnianalvg kiagvnvsst atgpngstrv
      181 virgngslng nnqpmyvvnd lpidntqlnl pgigngpgst rinvdrgdgt svinpddikt
      241 itvlkggtaa alyganaang viliqtkrga aqkgigveyn tsftfeapsi ipdwqyeygs
      301 gangkkpttq aeavaagrws wgakmdgtnv iqfdgvarpy vaqknniknf yetgttfins
      361 ialsggteka tgrlsfsntd nqgvvpnsdf nrkslniasn vnmtdwlkfd vvaqynveks
      421 nnrvtvsdae anpnwgtymi antvdirnla pgydangvee awnpvavatn pyfvvnkikn
      481 sdtknrflgm invklnftpd lflqgrigqd ftnydffgyi pkttlnnpig yaqgsrvkls
      541 nlnseailny tkkniykdfs lnallgvntr ttlrdetrve gsgfvlddfy altnlstlty
      601 sypygktktn svygavdldy knvvflnftg rqdwfstlsk dnntvfypsv gtsiivsdil
      661 kmpefvsfak lrtswaqvgg atpdpyalnq sysmvqgghn gqqlqtptgs rvpnatlspl
      721 tsttfeigtd lgffnnrlnl dfayynratt ndivettisn asgastalln lgkmrnkgve
      781 fllsgkiins enfswdasfn gsynkntvea ltdqlnsitm atsvngyvti tsdvgrpysi
      841 ikgykplkda sgntvynvsg gsatiargpl eelgqgvhpw aagisndfky knisfsflid
      901 gkfggslysg tdlygtrmgl tkltldgres glpikgvdtn gnpvdmviap enlrtyydgl
      961 rnisstfvyd asfiklrqvi igyqlplekl kglsklqgas isfvarnlfi lykktpnvdp
     1021 esvfsagnaq gveqfgvpkt rsfglslnvk f
//
LOCUS       WP_099713447            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_099713447
VERSION     WP_099713447.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117247
     Region          25..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngilv llvvlmaqlt faqersvsgv vsdnaglpip gvsvlvkgtn sgtqtdfdgk
       61 ysikaspsqv lvfsyigmkt qevtassstv nvklassale lesvvvtalg ikrekkslgy
      121 stqevkgdav snvkssnfvn slsgkvagme iktsgnlggs tqvvirgnns iagnnqalfv
      181 vdgvpidnsn sntssqktgg ggfdygnaas dinpddieti nvlkgaaata lygsrasngv
      241 vmittkkgks qkgigvtins svtlgtadke tlpkyqnkyg agygpyydsa dgyfgladin
      301 gdgiddlttp ftedasygaa fdpsllvyqw nsiypqlpgy gkatpwvagk snpnsvwgta
      361 sttvnsvsld ggtdtsafrl gftnlmqegn lpngslkrnt isfsgsqnlt dklkastsfn
      421 fvktdgkgrn gtgyssnnvm qqfrqwnqmn vdfneqkeay fltrenitwn pnsstnlkpi
      481 ysdnpywtfy enyetdtrsr yfgnvaledk ltdwlsimgr fsfdsyselq eerinvgssd
      541 vskysrynnt vaeynydlml nfnknltekl nlegnigwsl rnniqnsifa atngglnkar
      601 lyslsnsvsp ilapveydan smvdgeyira slgydgyayl egtfrtdrss nlpkadnryn
      661 yfsvsgslvf skfieakwlt fgklranyae vgsdtspyrv fntfdigtpf dgtgvasnpg
      721 aqnnlnllpe rqesyefgle msflnrrlgf dvsyyndqni nqitsiplst atgynsavln
      781 agtienkgle vqfnatpfkt nsfkwdlnln wsqnkslvvs llngienlql aalqggvsin
      841 atpgqpygti rgsdfiyaan gqpivnqtgs rigtyqrtaa snvvigdinp dwkaglnnsf
      901 tyknlnlsfl idmqkggdvf sldtwygyat gmydfsaann dlgnprrdpi vgtlgnygan
      961 sggvimpgva pdgtpnqara nasvyttaeg yarapnklhv ydagyvklre asltynfdsk
     1021 mlkqlpftna sfsligrnlw iidkntpytd peaglssgnv qgyqsgayps ireigaslkl
     1081 qf
//
LOCUS       WP_099714530            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 11].
ACCESSION   WP_099714530
VERSION     WP_099714530.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 11
  ORGANISM  Flavobacterium sp. 11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Flavobacterium sp. 11"
                     /db_xref="taxon:357523"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110831
     Region          25..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskftwilt lclaffiqfs faqektvsgt vtsksdqmtm pgvnvvvqgt srgvqtdfng
       61 efsikasvge rlvisivgsk pvtvvvgaqn rinvqleddt tvlenviveg ynvtktkaks
      121 nvasvtvssk tiegrpnasf iqtlqaqvsg lnitsgtgqp ggnsqiiirg tgsingkvep
      181 lfvidgipln sdnfrsinpd diesvsvlkd agatsiygnr gangviivkt kkgsfdsalg
      241 vkyssttgfs tlqktkynlm nsqelltter aygrgrgftt gpnggpmtda qiaaapntdw
      301 ndyffrtgvt qnqvlslsag gknmtsftsl gyfdqqgilk gsdlkrfsfr snisgksnne
      361 kltystttsi nfsrrneana igtggvnqny vlgannsapy itpseystsa qlfadygtqg
      421 gtllltplfl idklktfenr idelkglini eggykitkdl sigtsialdy tqqnlytwqs
      481 psafnsllfa gaatapefed qlferdaait sntrlnynrt fnekhtvnag ayveyikahr
      541 ngfnfrqrgl npkttspgag tgyildgpan drfvptvgaf kqetglfsyf gtadydydsk
      601 ygfgatirrd assrfagdnr wgtfyslsgr wnidkeafmq gsvinalklr gsygtsgnqd
      661 vlngtylaln ntrelyttgv gyngtqsfil sqlavpdlrw ettaqanigl dfevfkgrls
      721 gsfdvyrkkt tdlfipvpls avnatptina nfgalenkgv eatlnydlik sangfnltln
      781 fngaynknti ldiagttgli dngttviqeg vtideffltr yqgvnpangn llflnaagei
      841 tenpnptvdr vltgksripl yqggfgfdss ykgfflttnf syaaevyrid fdlqglqnpt
      901 nnvgvfnisa dllnawtadn rvtdipalra anyaaqnnsd rylvdasyvr lrfasfgydv
      961 pkklldktpf ktvkafvqge nlvtfskwrg wdaesprtad qyqyptpkiv svglqlef
//
LOCUS       WP_099715050            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 11].
ACCESSION   WP_099715050
VERSION     WP_099715050.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 11
  ORGANISM  Flavobacterium sp. 11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Flavobacterium sp. 11"
                     /db_xref="taxon:357523"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109709
     Region          21..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrniifsfla lillpaymsg qvikgkvldk dgigipgami vaadsktstd tdfdgnfnin
       61 akvgevlkis mvgfdalsvp ataapmsiql qeskdtelke vviigygtrk kidnttaits
      121 lkaeeisktk vlnasqaiqg kaagvqviss dlpgstpsvi irglgtalgg rtplyivdgm
      181 pteninnvnt nditsyeilk dasalaiygt raangviiit tkkgkgdkvs vefesfagfr
      241 aplkkvkmag snkyshysns alqtttfsqd qpvntdwfda itrtgsytqn nvsvsgasen
      301 ikyffslgny qekailngld ysrttfrsnn efkiskkltl nqnfsfgsan stpkplsaft
      361 naykqspivp vrfsngqygv syvgadgfag tsgssfnnvg npvaqldyfd eeqrsitlqg
      421 glkldydilk slkftsqfng eyyswknynf edtktiwqsn nnpgqlssii ypadkninll
      481 tkgrnqyfnw nlsnyltynk vfadihdiel tagietsvrg areqltvark nvnadsnyws
      541 lagvdyvgtv vnyrdevfne nkiasyfgrf qyklmdrylf tgtirrdgss nfgkdyrwgt
      601 fpafglgwvi tkeefmanak gidllklrgg wgklgnqnvp lnnqayssgl tyylggsiln
      661 egttinsqvd pslsweitee tsagldfell nnrlkgsfdv ydktttnvil ntrpyitsgi
      721 snsspahvge vsnkgyeial rwddkltdnl sywvggnfsn nkneltglkd atlapitggd
      781 lgngqwtkll dntsvgkplg sfymyeyagf datngkmlyy tatgakvtqd aldanadkky
      841 vgsilpnsty gvtlginykn fdfsvdgygt sgakvyngkk aqrftgenie dslatdfwtv
      901 nnttaskpgp fnqvpvasty ylesgdffri nnitlgykip lkgeflnscr iyvnainpfi
      961 tqkfsgfspe lngngdpygt qgieldaypt lrsvviganl kf
//
LOCUS       WP_099715587             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 11].
ACCESSION   WP_099715587
VERSION     WP_099715587.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 11
  ORGANISM  Flavobacterium sp. 11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Flavobacterium sp. 11"
                     /db_xref="taxon:357523"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110130
     Region          35..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkksflkfw tttqlsklsc ilflcfitgl naqtrsikgi itddtstvpg vtikvknkpp
       61 tafsdengny tilaaendvl vfsylgykti qivvadqvti nvkltedatt lkeivinagy
      121 ysikekeqtg sivrmiakdi dkqpvtnvla amqgrlagvn iiqdggtpgg gfqikirgrn
      181 sirldgnepl yiidgvpysn esigstntst alpsqaspln sinpndiesi evlkdadata
      241 iygsrgangv vlitrkkgks gktnisvtas tavgtatkfv elmntqqyls mrkqafindg
      301 ipisdtdydi ngtwdqtryt nwqkellggs atindfrtsi sggsettqfl isgnyrtegt
      361 vlpgdfryik ggilssinht sldkkfkisf sgnytaqdnl qaatdltlta rylapnapal
      421 ydsngnlnwe ndtfenplap lkstyrantn dlvansvlsy elipgleiks nfgftdlkte
      481 evrtipstiy npvyevgsdn slmylnltsr qswiiepqlr gfknfrnhkf dvlvgmtsqq
      541 qrterlfqsg igfannnlin nlasaitknt tnsdtflyry qaffgrinys ydekyflnft
      601 grrdgssrfg pgkqyanfga igaawifske kfnpenskms fgklrfsygt tgndqigdyq
      661 fydtygttga nyqgiiglqp trlynadfgw etnrklelal etgffkdrif stlalyrnrs
      721 sdqlvgipmp attgflslna nldatvensg fefsvrtlni dsnsfkwstn fnvavaknkl
      781 lsfpnlsgst fanryvigqs idivklyqsk gvnpqtglyd fedlngdgsi tagdkqiskd
      841 lspkyfggiq nqldyknwql dfllqfvkrd nydyisnvpg ggqvnqsnts gdawqqigdq
      901 sssqlhttgl ngaavstyyr yiesdavitd gsfirlknis lsydiplqat tnvkcklfiq
      961 gqnlltftsy kagdpefkfs gflpplkvis ggmtlnf
//
LOCUS       WP_099716150            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 11].
ACCESSION   WP_099716150
VERSION     WP_099716150.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 11
  ORGANISM  Flavobacterium sp. 11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Flavobacterium sp. 11"
                     /db_xref="taxon:357523"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112420
     Region          25..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkilgqkllf flfvfsvhli ngqtktitgk vtdqsglplp gasimvketk lssisdldgn
       61 ysiktenrkt lvfsfmgfkt keiltsegsk idvtlddnsl algevvvtal gikrdkralg
      121 yasqelksdd inkvnstnfv snlsgkvtgv qitgsgngit sssrvvirgd kslninnnsp
      181 lfvvdgipin nntygvggns tnqrdlptdy gngaseinqe dvesvnvlkg aaasalygsr
      241 aangvivitt ksgkknkglg vsisssymts ealrlpeiqg vygagsklty dpgadtnlgp
      301 rldaglsilq ngspgysvgq gvalpfqfry dlndffrkgs sisnsvsitg sdektnfrls
      361 ygkttsediv pnsnlkrdni slnlnykisd kwkvitiaty tksgsdntpv tgygsqglmy
      421 nllwnhtnvd ldwlkdywit kdvqqnsmfs wgdnpfkiay eninafkkgr lygniastyd
      481 fnenlslmvr mgmdnsndfr wsrrpigssr ypqgmyreqs iafteynada lltydrtfgd
      541 fstklslgan rmnqytsegk iegqgisipg iynlqninvm piqsrniykk rinstygman
      601 igyknylyld ltarndwsst lpadnnsyfy psaslsfipt slfemnknid flkfranaas
      661 vgndtdpyrl vktyengala gtltnpstil nsnlkpeiat syevgveaqf fnkrvtldas
      721 yyitnsknqi vgldvsqatg stsnvinagk iqnkgieigl gitpvksenl ewsinanfsq
      781 nrgvvkelte gissyiiaqg pnggtvearv germgdmygr gylrspdgqi vfdntgspil
      841 dtqikkigny npdwmlglst nlrfknvtln alfdvrhggk iysmtnaigm esgilavslp
      901 gretgivgdg vvqnsdgsys pnttvisaen wyysnafrrd nieansfdas yvklrevsln
      961 yrfpqklika anvqnisigl vgnnlalwtk vpnidpetqs lsggtllpgf evlqlpssrs
     1021 ygvklnvsf
//
LOCUS       WP_099718026            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099718026
VERSION     WP_099718026.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114159
     Region          39..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklislvf iggvifsana ketaikkhlf eqkssqveis gqvigqddgm piagatiyak
       61 snkknasitd etgkfklnvp enethiivsy mgyatleyel savkdlvirl kpaenvldqv
      121 lvtalgvkks skavayavte lkgteftkak etnisnalvg kiagvnvsst atgpngstrv
      181 virgngslng nnqpmyvvnd lpidntqlnl pgigngagqt rinvdrgdgt avinpddikt
      241 itvlkggtaa alyganaang viliqtkrgs iqkgigveyn tsftfetpsi ipdwqyeygs
      301 gdankkpttk aeainygrws wgakmdgtdv iqfdgvkrpy spqknniknf yetgttfins
      361 ialsggteka tgrlsfsnmd nqsvvpnsgf nrksiniasn vnltdwlkfd vvaqynlekn
      421 nnrvtvsdae anpnwgtymi antvdirnla pgydengvee awnpvaiatn pyfvvnkikn
      481 sdtknrfigm lnvklnftpe lflqgrigqd ftnydffgyi pkttlnnpig yaqgskmkls
      541 nlnseailny tkkniygnfs lnalagvnsr ttlrdetrie gsgfvlddfy alsnlgtity
      601 syphgktktn svygavdldy knvvflnftg rqdwfstlsq dnnsvfypsv gtsiivsdiv
      661 kmpefisfak lrsswaqvgg atpdpyalnq sysmvqgghn geqlqtptsn rvpnstlspl
      721 tsttievgtd lgffnnrlnl dfawynrstt ndivettist asgansalln lgkmrnkgie
      781 flvsgkiins rnfswdasfn gsynenkvea ltdglnsitm atsvngyati tsdvghpyst
      841 ikgyrplkda kgntvytlsg gsaaiargpl eilgegvhpw tagitnefky knvsfsflid
      901 gkfggslysg tdlygtrmgl tkltlegren glpikgvdtn gnpvdmviap enlryyydgl
      961 ksisstfiyd asfiklrqii lgytlpvdki rglsklqgas isfiarnlfi lykktpnvdp
     1021 esvfsagnaq gveqfgvpkt rsfglslnik f
//
LOCUS       WP_099718134            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099718134
VERSION     WP_099718134.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124241
     Region          120..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtftiqpvlr kilfflaili sgfkgfsqnk litlhvknkp isliiksiee qtdfriiyna
       61 rkidadqlad ldvnnaslet tlklllkdkn isfyiqkkqv lltnavpdvt antqeterfi
      121 sgtvynakdk lplpgatirn kgtgmgaitd fngkfvyllk gnnindlvle vgflgmetqs
      181 qkadnkkqfv fhlqettdel npviitssyg ttklkeeivg sistlnakdi aveqasesvd
      241 kmitgqiagv lventtgvgg pvkinirgqg tlpsftnart gtstqplfiv dgvvmseefg
      301 ldstffsgng datetfsnpl mkiapenies isvlkdaaav giygadgang vilittkkgk
      361 kgktqfgfsn qlgissainq ikylngeqyt elrnefiknt spgsaltpyn gvntdwfsll
      421 nrtgvynkyn fnvsgstskf syrtnvsytk idepqlgndt kqlnaginlg fhhknlnvsl
      481 mlnpsfvqqh apnifysfay lptlspynad gsysflgssg itrgnplaai eqnknetnty
      541 gllsslnvsy qlnkaikfst lfgidytdke qdryysaene sgqflntfkl ngidyprwgr
      601 rlinqrnstk wnwqgqllfe kqlteshgid gvlgfelaed ktnfnyksav gfvnpnqvna
      661 isdavmddnp ntpedesknn qtfgndisnn srvsafaqvn ynykkryyfl anfrrdessv
      721 fgvdsnvayn ggagaswiis nenflnsnsw idflklktsy gstgnsrigs yrskglytih
      781 qngyngldga vpntapngdl sweknikfng gidfnifkrl efsveyyynn lsdliatrdi
      841 ptetgynslq lnaatmynkg fefstrikwi ksdafkwtta fnistienkv telkglgsdy
      901 sqaemalaqk igystttiwg lnwvgvdpat grdlvqkngk iydimtyrsl ytiadwepig
      961 drqpdafggf ynsfsfysnl vlsfrgdfqi ggeflakdvl idkysntfnr nlsvnandhw
     1021 rnpgdivsqp avtstpivan lskyvydaty irlsninlsy niplkntfln slavfadatn
     1081 vaywykeksp kgmngirefn ytypqartis lgvnakf
//
LOCUS       WP_099718175            1238 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099718175
VERSION     WP_099718175.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1238)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1238)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1238)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1238
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1238
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=137821
     Region          145..1237
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkpvvkqrl lyrimkitlf qfvlalvfss famannvngq kkldtkvtit venltldsal
       61 skieksahvk fsynsrlpql srkvsieanq etlssilsri lvpfniafse vsnqiilqkt
      121 tsedpfasad nhdslfevlt agpiikgkvt dasgsplpga tvlvkgtkta vltdfdgnfs
      181 iempsnsdkl visyvgmetr eigisnttpt ivlselgqnl kevvvttgye ktskrtftga
      241 iskisgaelk vdgvvdvsrm iegkaagvtv qnvtgsfgtt pkitvrgsss ifgdtkplwv
      301 idgvvqedii nvsfadlasg nsstllsssv aglnandiqs ieilkdasat siygsrslng
      361 vvvvttkqgr rdsplkvsys ventvrtvps ytqydilnsq esmsvfqemk qkgyldlsss
      421 ytgrfggayn ilakeinryd esngqfgvkn dqpninqflk kyelantdwf gvlfrpsitq
      481 nhslsfsggg knntfyaslg yytdpgwtia dnvkqltsni kgtffvndrl nitlstmgsv
      541 rdqqapgsye sqkdvvfgkv nrdfdinpfn yvlstsrtlr pyddngnyey yqnnwapmni
      601 vnelanntld ikvndirfqa dldykinkhl tynltgsary attsrehkiy edsnvvaayn
      661 agvgdnvntq iqkenvflyq npndltapki svlpsggflr kftndmtsyn irnsvtyrnt
      721 fnekhevegf fgtelrsvdr nndnftavgi qfdkgltsfi dpkiiekivn ggdsyydfga
      781 erertvgffg kvgytydrry tasltgrydg snrqgdtgss rwlptytvsg kwnvaeekfm
      841 knvesintla lrasygltat agpatnslai yksfitdrfn lsdrenairi edlqnkdltw
      901 ekqyetnigv dlgmfnnriq lttdiyrrka fdlidyvits gvggqsvkqg nnadmetkgi
      961 elgfttqnii tdsfkwsttl nfsvydqnit klankpsvfd lvdsnggntv ghprnsiysy
     1021 qftglnnqgl ptfilqdgae nnitkanfqd tndvmkylky egsiepnksi gfantftykn
     1081 wslyvfivgs ggnkvrlnpv ysneyndltv ftkeftnrwi npgdenvtnv pviadkilnr
     1141 nygendlqia yntynfsdvr vadgdfvrlk nislswefpk dfkrklglst ftlkgsavnp
     1201 wliysdkrlh gqdpefrntg gvafpitsqy tftlnvsl
//
LOCUS       WP_099718500            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099718500
VERSION     WP_099718500.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121215
     Region          26..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllyksll vflmvlcyeg vsaqnktisg vitdnanlpi psvivkekgt kqetltdeng
       61 afkisvkega tiivssigfk ttelkavdgm qvklasatne legvtvtalg qtkknkaigy
      121 atsiikadai tktasptian slygkapgvr itstpggaga iniqirgins itgrnqplii
      181 ldgvpirdge vnnsdywneq rvknngladi npedienisi lkgasaaaly gseavngvvl
      241 itsksgkgkk glgvdfstsy sgneiaylpr fqyargpgws nanfstgfla pngftqydtn
      301 gdgtldtrgv snssynygpw fdgqpvmtwd gvvrpyspqk dgyknmfqna wdattnialt
      361 nntensstrf sythiesegl smgnnnkknn fnlnasfktg klktdvivsy lnqnitnray
      421 gmdrlvnnft gmispfsngd wykaryktsl gykyvtgkdt qsltpseniy rngfradiad
      481 yfwntnakrq teitnrlias vtetlsitne ltlrgristd ltsvntenkn pveiplvykf
      541 gsegdasgsf lmdaqdynil ygdvlltynk kinedfgvna vlgysgtqet grtvsrytng
      601 glsvegwydm nssigtplsk stryetvkda ifgtlsgsfr nylfiegtir rdrtstmnpn
      661 nnaftypsvn ssfvlsdavt lpefisyakm rgswgivgny pdryranvaf vqntlgtqgt
      721 anpvlitnsq dvygnegikp emkneyelgf etkffdrrlg ldfsyynaki kdqildmtla
      781 pttgaskila nvgelnnkgf eialtgspfr tqdfswdvtl nwakninkiv klangasell
      841 hadydgsaaq lksvvgdpmg giyahpvktd angnkmvgsd gfymldgdkw ekygsamakg
      901 vggllntfty knftldvnid ysyggslmpt giswmtalgl teeslnastn erggltyyrd
      961 ngkgvqvpns atagpagqpv frdgmlmdgv nvdgtpntnv vsqagyyvtt ynwggpqyss
     1021 sryelyvkkn dyvklrelsl gfnvpasyas kigatkmsls lfgrnlfyiy rtikdmdaea
     1081 ttsgsrwdkn vnnagvspst rsygvmlras f
//
LOCUS       WP_099718624            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099718624
VERSION     WP_099718624.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118267
     Region          40..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqalikrcs fllftlmsvl syaqttnsqg tvtvtgtvtd nsggvmpgvn vtekstkntv
       61 ttdfngqyqi kvkaggtlvf sfigmkkkel plsgrtvvda kleedsnqle nivvvgyasq
      121 kkshltgsvv takmseisdl pvgdlgtalq grvlgvgvsg gstrpgaksn ltirqpysla
      181 kdggnlnply vidgvlqida qglndstlfd nldasevesi sflkdaaaai ygarsaqgvv
      241 lvttkrgtkg dpkftysgsy gindktyqtk tlnafefgky vnimngpngy nqpitdpqyf
      301 fsddeleyfk tlkntyldde wkpsfnlrqn lnvsggtdka tyfagvsyyk qngnlstldy
      361 ekwnfragtd iklssnwkag iqlsgfysdq tktfnkigge veendynkll mhvpyipnyv
      421 nglpmelpnn ndgnqryhyn eikrlnnlae ttattmtinm yteykfpfvk glmargayar
      481 tmgsgrgtqv gtgytlyqft glgtnghiyn ddittpplrs kfydngnrly fsnttnlsqq
      541 ynlnfsydrt fgkhsvsglf aierseatsn nevvfksnvl egtngqfnta tgpidgsttk
      601 sesgslsyvg rvnyayddky laeflfrsda stkfapenyw gnfysasvgw vmskedffks
      661 svidflkvry svgllgkddt kawlwrqryt fqgykggvfg gnsdltngwk measpnpdat
      721 wsdelkmnfg vdarflnnrl svtaesyynv gtnlllnktg nlpftiggtv aaqnygsvdt
      781 ygyelsvgws dkigkdtsyg idlrfgwsgd kvikgdfnde dilkpwnpkp gyssdngvwg
      841 ydyigmfktq edinayvsky nitsvfgtav anlkpgmlyy sdvrgaylgn gkfaapdgii
      901 dvndqvqlas kantqysigt tlrfayksfs lntvvnasfg ngwsdigsqa rkslktkipq
      961 ivdntvsiwn diydptvnpn gsmpnpafes insvaskfwe vdsfriacrn itlsyalpeg
     1021 alkalkmnsc kfnlvalnpf nlynpysfqe angsyldypt lrtislglnl gf
//
LOCUS       WP_099718902            1128 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099718902
VERSION     WP_099718902.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1128)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1128)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1128)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1128
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123457
     Region          52..117
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          131..1127
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnekrmrcvv kfqsikktaw lkaillialf fagftanadn nntnkrvtlk venesiknvf
       61 qkienqvdvh fmyesnqina nqkislklsn vileqaldki csnfllryei vnnnivikkt
      121 qktaavdqnk iivsgtvfsg ddnmplpgvg ikdknsnata ttdfdgtfkm einaaeallv
      181 fsyvgyinke vkvsksetit vklaadvkql qevvvmgygs vkkkevlgav gsvsmketss
      241 rtynnaaell qgtvagvtvi ndggdptasp tinirgigsl naetplivld giiysgslnt
      301 lnpndiasis vlkdaasaai ygarasggvi litskkgisd rinvnvnyqg gfqnvakkld
      361 vlnaaeyada mntardnagl pripafdpaf eptarttktn wmdeifrtge iqdlslsing
      421 kteksnffls gsyrknegvl lntygerytv rantsfklad nftigenlsy sltdgqtant
      481 anaytgaila avfyppnati yredgsgqfg gvpekyigsy gdvinpvayl krldnrnpvs
      541 tilinpyaew eivpglkvks nwgytriqdn atdfstkite pgkifdfnrl tkkaatttdl
      601 lseqtvsyek sfgkhnlkal agytyqetkr dfytvegtgf dsedpsqryl lnakliqqtg
      661 aglsdeiiss yvgrinydfn qkylisgivr rdgtskllse nrwkvypsvs agwliseegf
      721 mkgisstvsn lklraswgqi gnlgnlgpyq fsvpltqtqa ligatptiny gyaeselsnp
      781 nlrwesseqt nlgldftmfn ntllgsvday vktnkdmlvr dqlpgvsgtp lgrivnsgdv
      841 enkgieaslt yqktrgefkf ditanaafls nkivsikddl tsleplnlsr vrslplaniy
      901 qvgspvgafy gyatdglfqs naeakayvns nnvayqpnav agdmkfkdvn gdgvinnsdr
      961 vvlgspfpkt tfslntnfry kgfdmnifls gaagnsvfna vkhtglngsf pgynllaesk
     1021 nawsptntnt nipvlsstdn nnnfgrisdf yvedasflrl rnlsigytik enwlngkakl
     1081 rffvsgqnlf titnysgmdp evglrnfgmd lgkyplsriy mtglnatf
//
LOCUS       WP_099718931            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099718931
VERSION     WP_099718931.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115797
     Region          32..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilnrytw lcillisigi naqetkpliq sklegtvida itkepvigas inikgtthgv
       61 vtdldgkfff qtgqkfpytl vvsylgykkk evvvnqnsvi idlteeqnvl sevvvtalgi
      121 tkekkslgyt tqslknkdia dtketnflns lagklagvri tnsqgdmgss riiirgetsi
      181 agnnqplfvv dgvpvdnsql nsggatrdfk naisdlnpqd ietltvlkgp naaalygsra
      241 ahgvvlittk sgksqkglgi svssgitisq vatlpsfqns fgqgsngkfs yvdgkgggin
      301 dgvdeswgpk ldgrlipqfy sngqavpfva npdnvrdffn tgltfdnsis varsddksdf
      361 rlginnqkqn gtvpnsevnk tnftintnyq isknvkvgvt gnyivtdapa lpggpmgara
      421 agvmlqflwf grqvdinqlr nnrdvnwnns yysnpywnay ynttsqqrnr ligdihldak
      481 ladglnfkfr tgvdyyndrr kyqikygtng tpfgsyaeda ytvsesnteg iftytkklsd
      541 dfsldalagf nirnhsdann yqkaprlavp dlytlnnsrd pltsyntlsk lrvysayasa
      601 qfgyknyafv nvtarndwss tlpssnrsyf ypsingslvl sealnlksnt ldflklrggw
      661 sevgndadpy qlstvynfqt afdgnpiqts sqkklnenlk pettrstevg veasfwknrl
      721 hfdaayyntn sfdqileikt tassgynsql inagkinnrg ieiqldgtpi qtqdfkwnvg
      781 vnyskniskv eildydkqiq nytigssggv dvlasvgqay galygtayqr dasgnivvga
      841 nglpkadpqk kvlghytpdy lagvtntlty knielsflvd asvggelfsg tnrtgnytgv
      901 laqtlpgrda angglsyyyp gnntanpktl vaggtapsgv tvyddgmifk gvyadgtann
      961 qvisaqeyyk asyniseayv ysstfvklre vklaynlnks fvkklgleaa sitavgrnlf
     1021 fiykdapnid petafntgna qgleslalpt trsyslnvnl kf
//
LOCUS       WP_099719103            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099719103
VERSION     WP_099719103.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110761
     Region          44..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnyfsfykgg ralycliflg filafsssla gtkrhfrfmp qqsqvqgtit dgsgplpgvt
       61 iaiknkvnst aisdyngqys itaspsdtli vsfigfktsy ipingrkivd vkllydtttl
      121 qevrvnagyy svkesertgs iaritskdie tqpvtnvlat mqgrmagvsi tqttgvpggg
      181 fdikirgqns lradanaply vidgvpyssd pvghgqtttl fpaltsping inpdqiesie
      241 vlkdadatsi ygsrgangvv littkkgksg kttfivnast gagsvtkfvk lmdtaqylsm
      301 rrqayandgi tsypasaydi ngkwdqnryt dwqkellggt svftdiqgtv sggsqntnfl
      361 lsgnyhtett vfpgeflykk ggsqfslnhq senqkfkiqf stgytiqdnd qpssdlstva
      421 qtlapnapal yngdgslnwe gstwqnplrn lpskfesksy dllantvlsy eilpkfliks
      481 sfgysdlrhs etrispstiy dpklnynssy stlflnntsr nswivepqls wgtglsagel
      541 eiligatfqr qstdqlvqsg agfpsnnliy nlssattvra vtdtetlyky qaffgrinyn
      601 ykeryivnft arrdgssrfg tgnqfaffga ggaawlfske sflkdvhwls fgklrtsygt
      661 tgsdqigdyk fldtysvsgv lyngqtglqp tglynenfaw etnrkfeaal etgflqdrif
      721 ftaawyrnrs snqlvgipma sttgfqslls nldaevensg leftlrtvnl sqgplqwisn
      781 lnisfsrnkl lsfpglagst ysqryrinep lnivllydyk gidpntglyq fsdlnndgki
      841 taagdkqiiy nlnpeyfggf qnqliykglk ldflfqfvkq knynypigaa gqmynqpekl
      901 qaswqapgdt spyqiftagn naaavtagsr fsestaaisd asyirlknis lsydlplngl
      961 ktkcrlftqg qnlltftkyk dgdpefisag flpplkviti giqltf
//
LOCUS       WP_099719295            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099719295
VERSION     WP_099719295.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115137
     Region          32..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkstklilw isilfisvgi kaqnteptiq sklngtivdq itnqpvigas vnikgtthsv
       61 etdldgkfyf qtgqkfpytl qisyigylsk evvvdgspiv iklteqvekl deivvvgygt
      121 sakktftgst akidakqian rpaqsfdqll ggqasglniv qpsgslnntp virirginsi
      181 tsslypliiv dgvtvftgta ggaignnpls dinpndiesi dvlkdasaaa vygsraangv
      241 ivittkkgkk gkvninydvw vswnkannlp kllnaqdyvt ikneartnag ltpgfalgqn
      301 adgstqetnw ydvayhtgvs qnhnlsfsga tnstnyfvsa nysdqngilk tnefkrqgir
      361 lnfeqkvtns fivgtnfsyn ntlnsgpnsg sstpnsvass sgnsvntqyi glqplgrlty
      421 ilpsnvsvyn adgsyninpa ngnigygpns pslgvfnayn lqtildldkn tsenntfigs
      481 vyaeleilkn lkfktvygin nfvvenkefr npysgdgfst kggatnsntk yqrsnwtntl
      541 tysivfnekh nlkallgqek nvrtidgwga iktgltdpff tsfqggftti tpgvsvqten
      601 vllsyfssia ydydkkylln lnfrrdglsa lasgnkwgnf ggasvgwnis eedfyknssi
      661 kevlnafkvr asygivgnse lndyaslsqy tagtyagvpt lnfsqsgnsn lkwetskkfd
      721 fgvnlalfnn ritieadyyk nnindlilna pqalsqgipn nsiaanvgsl ynkgfeltvn
      781 aniiddndfq wnaslnlsti knkvtslggy gdiyptalst fgiqnitreg ysvgsifavp
      841 ttgvnpengn rvyvnannee vqynaltkaf tylngtaapa idnyrdgriq gpslptyygg
      901 lnnnlsyrnf dltigltfsg gnklyngtrs tlsdqrffnn gtfikdrwtt pgqvtdvpkl
      961 vygdsfsggf sssnsayved gsylklknii lsyripvkne linkyissak vyaqgsnllt
     1021 wtkyrgsdpe isingnsins gkdqnvpans svftlglnvg f
//
LOCUS       WP_099719309            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099719309
VERSION     WP_099719309.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124011
     Region          22..1111
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkflnvlll llaiagysqe nrtitgiild eadqspipga svfvennsis nktslagiih
       61 seaigttsdf dgkfqlkigk dvtslrvtfm gykpytleit sqkeytirlk sdvaqlqevv
      121 ltgyqkiekr kltsaitkvd masiqqsgvs gvdqllmgqv agvavttpsg apgapakiri
      181 rgtaslngtq dplwvldglp lenndvpkny dkenidqlan ysiaglnpdd ikditilkda
      241 aataiygara angvivvttk kgrrgkmvvn fntntfitqr pdfdklnlln ssqkvdleln
      301 masradltyr dtggevaril nganeldafr tggfsslsag tqqsinnlrk qntnwgnlly
      361 qdavntqhgl slsgggeksd yyfslgyyde ngatvgtgfk rynltlknny eitdkfkvgi
      421 gifgaenktt syltdldgft npanysrnvn pyltpynadg sykydpdias ysdiklpfnf
      481 leernntsyd lktraikalf daeykitkdl rvtsqlglqf dnsssekyag qetfytrrqr
      541 erssyfadnt qkyflpdggi iqntntdffq ynlktmvnys ktlgenheie vmagnelrrn
      601 kttsiatkgf gfdektlttq qiifpnstfa kesfyktyvk neyenafvsf fatasytykr
      661 kysfygsvry dgsdlfgvdp kykylplwsa sgswlvsqes flkdskvisn lrlrasyglq
      721 gnidkntspy vvgsnqttti lpgqsestiv vlsppnsklr wektqntnfg fdlgvlnnri
      781 tlvtdiygrk stdliglkal plengfeftn mnwaqvsnkg feialstkni drpnfkwntn
      841 fnfahnkskv drleirdnsy lpnqeghavn avfgfktngi dengyplfvn kkgetvnaqt
      901 ffglydplag vfpgmfsqsd lsaaefrdlf tylgdkdpkf tgglintfkv snfdltiaas
      961 fnikqtvtrt ppyngtlvdr gqnyttdiln awspnntssn lpgitskdsg tgdswmaynw
     1021 fsggnpinty nyldtwvsem symrlssvrf gytfpktfle kidiqsirvn iearnlfvis
     1081 sdykgyfdpe tfgniyaqpv prsltlgfnv tf
//
LOCUS       WP_099719689            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099719689
VERSION     WP_099719689.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109401
     Region          25..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfifsfla llllpsymmg qaqaikgkvv dssgmgipga iiassdarat adadfdgnft
       61 inakpgdilk vsmlgfnsvs vpataapmti tlkeaedtal kevvvigygt rkkidntsav
      121 ssikseeitk mkvinasqai qgkaagvqvs tsdapgstps vvirgagtal ggrnplyvvd
      181 gmpteninni ntnditsyei lkdasslaiy gtrgangvim ittkagkgkl vvdvesftgf
      241 rtplktvkma nadeyvrysn aayindypqg rfsanqpynt dwldaitrtg sytqnniais
      301 gssenvkyff svgnyeekgi lngsdygrtt irnnnefkls dkvkitqnfs vstikntpmp
      361 lsaftnayrq splvpvryan gkygvpfvsn gvvaetgasf nnvgnpvaql dytneqqqtv
      421 mlqgglkldy diikslkfts qfngefytyk qynyvdnqal wlsadptrvv skypgdlnvn
      481 tltrnrdqyf nwnlsnylty nkvfaeihdv evtagieanv qgtrekltid rknvnansny
      541 wslkdvnvag tvtglkdeal nqrrlasyfa rfqyklmdry lltgtvrrdg ssqfaedkrw
      601 gtfpsvglgw vvskesflsn veqinllkir gswgrlgnqn vplntqllts gldysglggt
      661 tinsqvdpnl sweiveelsg gfdfevlnsr lkgsfdvydk nttntilnvk pystsgitva
      721 tpahvgevsn kgyeislrwd dkindnlsyw vggnfshnkn eltslknvql npiiggslgn
      781 gqntkildnt svgqplgsfy myeyagvdqt ngqmlyykad gskvaqsgld elkdkkyvgs
      841 llptsnygvt lglnyknidf svdgygtgga kvyngkkaqr fggenveasm angfwtptnt
      901 tssipapsnl tpyastyyle sadffrinni tlgyklplre dsfisfcriy vnainpfitq
      961 kfsgfspdvv sdgklvegtq gveldaypsl rsfviganlk f
//
LOCUS       WP_099720006            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099720006
VERSION     WP_099720006.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111842
     Region          23..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllfilfg tilfaqpifa qtktvsgtik sesdglslpg vsvliegtsk stvtdldgkf
       61 sisvnenetl vfsfvgfgak kvkisnstnv inlrmaeetn tlsevvvlgs tvratrkelg
      121 navtslkged likaqpggls talqgkiaga qvsqnsgdpa ggfsiklrgt ssilgssdpl
      181 yvidgvvlnn attnvtnlnv ttgnsnmqig qnrssdinpn diqsievlng gaaaaiygsr
      241 aangvvlitt kkgvagetry tfstsvtsnq irkkldlnts nkqfvnaspa lfpiqgnpks
      301 pttvnvlgrd letrtidvqr ydyqddiftt gvgtdtyfsl qggdektkyf aslgylvneg
      361 ivkntdfkrt gakvrlkhdf nsklsatvgl nyinsasnek pdgnvfwspi nsinitnnty
      421 dinkrdangn llavdpnrvn plsiietfki kqntdriisd lqlnyvpfkn fnadmifgvd
      481 nynqrgnvfi prypyvvnpa yyndgyvsea tnrvvqfnnd lnlrylwnin dkwkattygg
      541 ynvqtyrdnf aavegrnlkp fietinafnt lipgspsssq skynlwgfyl qetigykdkl
      601 yitlagrqda stifskdnrs qfypkaslsy vlsdekfmeg ihdvvssarl rgswgksgsl
      661 taikpyarft nystgtllgn stftiegfkq gnldlkpeqs vtyeiggdfg fikdrlnlsf
      721 syynadiddl llpvqlaase gatntiknig qmnnkgfevn lkydlikken lhldlfvnys
      781 snrnkvtglp qqrfkldsnl agapvfvemd kpigifygty farnadgsll ltptgypqte
      841 kgdvntgvpq rdasgqptgt ilnkqignpn pdyiisfgtn lnykkfglsv lfdgvqgvnv
      901 fdadyrtrqg vgsgtlvake lsgelprgyi wsvynieefr vvdgsylklr evslnysfgk
      961 lnnffddlvi tasgrnlisw dnftsfdpet nsggqssvak ynfgtvpips syslavkvqf
//
LOCUS       WP_099720026            1009 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099720026
VERSION     WP_099720026.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1009
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112073
     Region          44..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktyslkkgl aalwypfifg fylfctpala rntlysplsq qqtqisgivt daalplsgvs
       61 isvknqknit vtdfdgkfvi tvsandilif tyigyktiei pvakrlminv qmqedtttlq
      121 evkinagyys vkesertgsi akitakdidk qpvtnilsam qgrmagvtit qttgtpgggf
      181 dvqirgtnsl radgnqplyi ingvpyasns isnnnissii ipssnvspls tinpsdiesi
      241 evlkdadata iygsrgangv ilintkkgke gktrftintn tavgnvtrym dlmhtdqyle
      301 mrkeafandg ivkypvaayd ingtwdqsry tdwqkeligg taqindgqis insgsaqtqf
      361 llsgnyhnet tvfpgdykyk rgganfnlnh qsadnkfkin lsasyssqnn nlpatdftre
      421 arslspnaps lydafgnlnw engtfnnplr nleavykant anliantils yqiipeleik
      481 tnigfsnlhy detrtspsti ynpslglgse ssslfvnnsk reswiiepql nwnkkighgk
      541 ieflagatfq qqktaqlvqe adgfasnsli ydlasatyly vftnqqtqyk yqaffgrvnf
      601 nwkdryilnf tgrrdgssrf gpgnqfanfg aigaawlfsk epslenkils fgklrasygt
      661 tgndqigdyn fldtyssagn nyqgtvglqp nrlynanfgw etnkkmeial elgfiqdrif
      721 lttayyrnrs snqlvgvplp gttgfnsila nlnatventg leltirtvni ekqnfkwttn
      781 lnltvpknnl iafpqlenst yvnqyvigks iniqkvynyi glntqtgiyq fedvnkdgki
      841 sspddrqtvk dfspkyyggl qnqfnikrwq ldflfqyvkq enwnsismlg mpggmsnktt
      901 ealnrwqnpg dtgpyqmyss gtnslvtaan nlytnsnaai sdasylrlkn isisynlpen
      961 slknlkcris lqgqniltft sykgadpefi vsgflpplki yalglqlif
//
LOCUS       WP_099720387            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099720387
VERSION     WP_099720387.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115114
     Region          27..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv lllvlvaqls faqeravsgt vsdnagmplp gvsvlvkgtk tgtqtdfdgk
       61 fsikasssqv lvfsyigmkt qevaatsanv nvkladagaq elegvvvtaf gikrekkslg
      121 yatttlkseq ltavvntnpf etlsgkiagv disapsqpga stkviirgln titgntgply
      181 vvdgspinnt asgtgndgig tstrsydsgn gisdldpnni esmtvlkgaa asalygsrag
      241 ggviiittkk gkantgikvd alastefsqv arvphlqeqf gqgwnglgys gsnsysneng
      301 swgpafngev rpwgtiynns qqvkpytalk nnvrdfyktg tlatqsvtls gggdtsdfsl
      361 vfsnvnsdgv vptdadlykk qslgfngglk snkftlrtsl nyiykdqnvv ntgqgddagq
      421 gstlqqellq iptdisivdl adyknnpfnt nsyyftpyag npyfavnens tkiygnnlfg
      481 nvnlsykitd kitaswqvgg nvrserfksy gaivdyepgs pqdgkknkvv ggvtegrsey
      541 sefdtffnln yntnlsedwt lnllggfnyn kretdelfnt vtglgiknyy elsnsasrpv
      601 itqnnlmrkt gavyasaefa fknryfatlt grqdvtstlp ignnsyfypa lslgaividn
      661 gstflklrga askiandtep yatenayipg saaanfgvit spiggvsyye asgrlgnsql
      721 kpettieyev gaegsffknr isydialyhk ttsdlivnlp ldpstgfisk yinaaeivnk
      781 gielsltgsp iknkdfswni tytftknlne vtktadgfen idlttgysvt yratkgqpig
      841 tyfayvpktn aagqivvnpt sgmyelsdei qrvgdsqrdf vmglqntfky knfnlgfsld
      901 wkeggemysy tkrlshfvgn gietafndrn tfivpnsvne vvtngvvsyv enktpvsyen
      961 vssfyntqdn payennhvid ktfvrlrevn fnydfpsals knmglnkitl gvyarnlfmw
     1021 tpganpyvdp evstygasrs isdfgefgsn psqrsiggvl klsf
//
LOCUS       WP_099720474            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 2].
ACCESSION   WP_099720474
VERSION     WP_099720474.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 2
  ORGANISM  Flavobacterium sp. 2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Flavobacterium sp. 2"
                     /db_xref="taxon:308053"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116166
     Region          25..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqklkglmv fifvlsmqli faqekkitgt vsdnagvplp gvsvlvkgtk sgtqtdfdgk
       61 yaikantnqv lifsyvgmkt qevvvnssli niklvdnate legvvvttam gvkrekkslg
      121 yatqqisgkd ldggagnanv anllagkaag vevsrntnfg gstnvvirgn ksltgnnqal
      181 wvidgvpvdn snsnsttqtt grggydygns vsdinqedie sinilkgaaa talygsraan
      241 gvvmvttkkg kiadqkvgft fsssftvgtv dkstfpkyqt kygagygigs sfldpessip
      301 tvdtsndasy gdaftgqpvy qwdaftpysk nygqatpwsa akngpitffk taqtnvnsls
      361 lekaterssl slsyvntlqs gilpnselkk nqlsarfsqk itdkltanay aavtlqstvg
      421 rnstgyndni lgnfrqwwqt ntdlkelenv ykasggqnvt wnwsdptsae glvpaywdnp
      481 yftryqnyss dnrtrlfsya sldykitdwl salgrvsldt ykelqeerra vgsiasgfgl
      541 spvnetsgyk rydnnfqein ydfmlnfnkk faenfsltgi lganvrrddk esvlsstigg
      601 lvtpgiyals nsryalpfpt eakytkqvng iyaqaslgfk dtyfidasvr rdesstlpkg
      661 nnsyiypavs gsllfsnlmk aewmnlgkfr mnyaevgnda dalqltntyt rssnfnnepm
      721 ytlpnlnrnp nlkpertksf evgletsmfn rrlgldvtyy ktnsvdqivs aavssgsgft
      781 nawvnggnie nkgleiqiig tpiktkdfsw dvivnwsnnr skvvslpggi enlqlaafqg
      841 gvttnatlye aygsikgtdy vytngqptid qktgkymvtn tsdntignit pdwiggirnk
      901 ftyknvslgf lidtqkggdi fsldmyygla tglyketavg tiretgilna gvapdgtpnt
      961 vmsqnpgvys nnygylaepa kafvydasyv klrevsisyn fpksmfqgtf vnsatfsllg
     1021 snlwiisknl pyadpesgls sgnnsrgysv gslpttrdig fnltfkf
//
LOCUS       WP_099731869             532 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Acidovorax].
ACCESSION   WP_099731869
VERSION     WP_099731869.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55475
     Region          11..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtspvpqpq rigvpretfp gekrvatvpd vvekliklgf tvavesgagd aanfsddayr
       61 aagaeivgda aslwaasdiv fkvrppssde valmregttl vdfiwpaqnp elmqqlaark
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rkmyaeqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg qavvrhgvti vgytdlasrl akqsstlyat nllrlteelc kakdgvavvn
      361 meddairglt vvkegsitwp applkqapap apkaaapvae kksshgtgap msaktltivf
      421 avlavlfwai gayapvaflg hftvfvlacf igymvvwnvt palhtplmsv tnaissiiai
      481 galvqiappd agvngrpdgl ilwlafaalv ltainmfggf avtrrmlamf rk
//
LOCUS       WP_099739843             537 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Comamonas
            sp. 26].
ACCESSION   WP_099739843
VERSION     WP_099739843.1
KEYWORDS    RefSeq.
SOURCE      Comamonas sp. 26
  ORGANISM  Comamonas sp. 26
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Comamonas sp. 26"
                     /db_xref="taxon:2035201"
     Protein         1..537
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56111
     Region          13..537
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mstpanqsts aqrigipret fplekrvatv pevveklikl gfsvsvesga gdaanfsdda
       61 yraagaevlp taaavwaaad iifkvrpptt eevalmregq illdfiwpaq npdlmqqlaa
      121 kkvtvlaids lprtlsraqk mdaltsmagv sgyravieaa nafgryfngq itaagkvppa
      181 kvfiagagva glsaigtaan lgaivrandt raevadqvis lggefvkvdy eedgaggggy
      241 akvmsegfqa aqramyaqqa kdvdiiitta lipgkpapkl itaemvqsmk pgsvivdmaa
      301 eqggnceltv pdhavvrhgv tiigytdlas rlakqsstly annllrltee lckakngvav
      361 vnmeddairg ltvvkngeit wpapplaqap kpaakpaeap vvqkkgghgh gssgplpakt
      421 lviifavaaa vfwligayap aaflghftvf vlacfigymv vwnvtpalht plmsvtnais
      481 siiaigalvq iappdtagtg rpdelirwla faavvltavn mfggfavtrr mlamfqk
//
LOCUS       WP_099742315             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. 62].
ACCESSION   WP_099742315
VERSION     WP_099742315.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. 62
  ORGANISM  Acidovorax sp. 62
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Acidovorax sp. 62"
                     /db_xref="taxon:2035203"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38295
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mfigvpaetv agetrvaatp etvkkltalg hglrvqsgag laasvtdaay eaagaeitda
       61 agawgaplvl kvrcpseaea pwlrsgttlv gmlnpfdaag lqrlaaagvt ayaleaaprt
      121 traqsmdvls sqaniagyka vmiaadryqr ffpmlmtaag tvkaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvggy arpmppswle
      241 rqkmevakrv aqadvvitta lipgrpapvl vtpemvqamk agsvivdlaa pqggncplte
      301 pgstvvkhgv tlvgetnlpa lvaadassly arnvldflkl iinkegalyv dmqddivaac
      361 lmahegtlkr a
//
LOCUS       WP_099761897             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium sp. 35].
ACCESSION   WP_099761897
VERSION     WP_099761897.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. 35
  ORGANISM  Janthinobacterium sp. 35
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium sp. 35"
                     /db_xref="taxon:2035210"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38683
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qvivqagagl qasipdaaya aagaqigtaq
       61 eayacaivlk vrapdasera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpflteeeq eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvikhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_099764975            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099764975
VERSION     WP_099764975.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110769
     Region          35..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlsa galfflgqia yaqqkpgdta taetaieevv vigysqvpke tyvgtaskvd
       61 aksidsknvs svsqalages agvrvintsg qpgtdatiri rgfgsvsgnr splyvldgmp
      121 ytgnvsainp edienmiilk datatsiyga rgangvvvmn tkkgranksv iqleskvgfn
      181 mallprysti kspeeyvgls wqavrnrgkl lgnadptaya ntnlfgtggi sadyniwgtp
      241 asqlidpttg kvrpgagrly dpenwedyaf qtsartennl sisggsgktt yytnigylsd
      301 kgysinsdye rytgrlnlsh qarpwlrgdf nlgyayskan rngqtsdsgs ifwfvdnips
      361 iyplfrrdaa gnkiadphfg gyefdygdgp ngrgfggltn sigdatnnln kfykheinan
      421 mflkaditkf lsfetriggq yynnsndqvt npfygsaasq ngyiqktkte lmsynwlqll
      481 rfnkrfgdhn vmafvahenn sweqkflsag rpniidmipe lnvgigesls esytnnytle
      541 syfgqltydy kgkyffngsi rrdgssrflq dkwdtfasag lgwlvskesf lsdnkiitnl
      601 klkgsygtvg dqagvgnypg ynvynpgnfm glpgatynrs gypeltwekf kvfqagvelg
      661 lfknraield vdyynrktdn lifdtrlaps tgnailkvnd gnmvnqgvef tlkahiinkk
      721 difldfgvng eflrnkltkm pfdvstgqrk ildlseagfg raegkslydy ymreyagvns
      781 atgaaqwtvn ytdnngngtf dageqitsly eyqsqnpnad irtgvtevya qatqkfldks
      841 aipdirgafn ldfgyksftl gvqflysmgg yaydsayagl mangqigtnn whtdilnrwq
      901 npgditdvpr mssnyaadvn fasrssrflv ksdyialnni rlgynlpqdf vksigmtgfs
      961 lfvsgdnlwi askrkgfnps vsetggsnty nyaplstitf gakinf
//
LOCUS       WP_099764777             982 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099764777
VERSION     WP_099764777.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 982)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 982)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 982)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..982
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108391
     Region          36..981
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfqlsllta vlffaggqav eaqkakrdti keehiidevv vvaygsqkke tmvgsntevk
       61 akqfadrpis sigqaldgas agvkvstgtg qpgsspsiqi rgigsygitt aplyivdgtv
      121 ytgslaainp ndiasfnilk daastslygs aaangvilit tksgrkgkds fnfgmstgyv
      181 qrsipeydrv nvhqyypliw eairngrlts vptstlaqan tyattqlisg vlktnvfnva
      241 dnqlvidgil npnaelkysd fdwqkplmnt gfrqnyelny sggsntttyf ssvgytnetg
      301 yliksdferf tarlkvdsqv kswlklgtsi sgvssngnns vegvdsnssy inpyrwsrtm
      361 gpiyspyahd pntnallydn agnvmydags argadaaagr nviqetllnk dlsknyyiis
      421 rayaevkvdp yltlstnvgy dirnnrrsty gnriigdaap ggsaekitvt eqtltwnqll
      481 nykrkfgkhn feyllgheny kftyeylygy kkgqivddnd elinfvtptt ltsrtdnyrk
      541 egvfsrlnyd fnskyllsgs irwdgssrfs kdvrwdsfws fgagwrvkge eflkdsnlis
      601 dlkirgsyge vgndrtdsyy mykstytlgy nnaqepgilf gfladptitw etnkqsdigi
      661 dfgffnnris gsveyykrvt edlifpvpip vssgvpdnni srnvgtmynr gfefsinadv
      721 iknenftwni nanastlknq vtelsngite iingtkkvsv ghsiydywlr qwygvdpadg
      781 splflvadty agttaadirt vngtsvttnf nkakydysgt aipdlfgsfg taitykqwsf
      841 samftyqlgg ktydsnyaal mssysqggal stdilnrwtt pgqitdvpal nsstytssni
      901 gssrwlissd fitfrqatls ynfssenlsq lglsglkilv sgenlwskta rkglepaqaf
      961 ngtttnrytp ariitigfnv sf
//
LOCUS       WP_099766808            1209 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099766808
VERSION     WP_099766808.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1209)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1209)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1209)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1209
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..1209
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134444
     Region          146..1206
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mifllnrryp ewygvptyri llghfgngrl farrlhlilf illtsamlav apavkaqnit
       61 lnvqsaplke vfrqiekqsg ylfwysddfi krsipvtvsv nkmplravld kifadqpfty
      121 evvgetialk eklltkdipg sqsnkktvtg tvtdgkgepl tgvsinlkgs vltvvtdfkg
      181 vfsievphkd avlrfsyigy qtyeqrvgdh dlqfnvvlke spemlkgvei vstgyqtlpk
      241 eratgsfvqi nnellnrris tnvldrlegi asgvvfnrnn lpsnermgis irgrstidpl
      301 vnanplvvld nfpyegdlan inpndiesit llkdaaaasi wgaragngvi vitskkgafn
      361 kplkvelntn vtigakpdlf yspnfiksad yidaetylfn qgfydsdltt nisrpmvspv
      421 vellakkran paltnqvdae iagfrgldvr ndyekyvyrk svnqqyalnl nggsdhaayh
      481 vsigydhnns nlvqntfsrl tlhsqttfql lkkleltagi nyfqtkaenn tdgsaygsfv
      541 agapkygaiy pyarladdsg nplavskdfq qgyiqtmasl gfldykyqpl eeislsentk
      601 rinnlivrgt lkykfsdals iqgqyqyekq ntldrnlqsq emystrvlin rfaqrnattg
      661 iftypvplgs ilaldntdlv snnfrtqvny drnfgakhsv aaiagaeire vetliygrts
      721 ygyndelgta vgninygtsy pinpsgnvai tapsgavtgr lnrlisyfan asytydgkyt
      781 atlsarkdga nifgvktndr itplwsaglg welsregfyg ldflpyaklr atygfngnvy
      841 nasayltfnt tltntltglr yatvgrapns elswekvrni nlgldfatkn nmisgtlefy
      901 ikdgldliqs tplapstgft syfgnaasnr tqgmdlslnt knltgklrwn tmfllsylkd
      961 kithydtqyt tanlisaasq ftsgtgplly ptvgrslfgv ysyrwagldp ntgdpqgylh
     1021 gqvskdylgi mtnvgpdnmi yhgssrpsvf gsvmntfsyg nftvsvnviy klgyyfrrtt
     1081 tstnlqnifq rltmhsdysr rwqksgdelt tdvpsvvyps ntnrdafyqg asvlvergdh
     1141 irlqdiglgy tfnksqfkel pfrslqisly annlgilwae nkknldpdsi yiytspnpkt
     1201 isfgvkgtf
//
LOCUS       WP_099766832            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099766832
VERSION     WP_099766832.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124237
     Region          22..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlillpl laaqiafaqe kktitgkied gntsamisga svkietqsvs tktdlvgiie
       61 svsvgtvtds ngkfilelpa dtksvlvsyp gyesrviqis egqtnytvrl ipevsdknki
      121 qeviitgyqk iekrkqtsav atvkmdninq agvasvdqml sgqvagvvvt pqtgspggpa
      181 kirirgtasl sgpqdplwvv dglplegndv pnfsdkdnid qlqnfsiagl npndiediti
      241 lkdaaataiy garaangvis ittkkgkkgt mrinfsadtf vtsrpdfnkl nllnasekvd
      301 lelmlasrad ltyradkgev mrilmkngql ddyrngglga lnsitrqqld glrsnntdwg
      361 kllyrnaink qygvsisggs drsdyyfslg aydeegttig tgfkrynltl knnyklsdkl
      421 sagisvfgtq seresfvtda dasinpinys rnanpylspy npdgsyrydq didgfsdryi
      481 pfnfveeren tsytlknrsl kaifdleyki tkdlkitsql gmqydsnkte kfaaqntyft
      541 rkmregtryy kdgafryflp dggikqnwdn effqynwklq aaystkinsr heidlmagte
      601 irktednttl trafgyddtt rkataivfpn sndasdrrye tyremppven ayasmfatas
      661 ytfdqkytff gsvrydgtnl fgvnkkykyl piwavsgswl vtkenfmknl taisnlrlra
      721 syglqgnidr ntspffigey ydttilpgsk eniinvispp ndklrwektt nvnfgldlgm
      781 lknrisftad iysrkgtdmi smketpletg feytmmnwgs ltnkgfelal strnidkenf
      841 kwsttinfah nksnvlseqp rnnallpsre glpvnavfal ktagmdengn pmfwkgnekv
      901 savdffklyd vyadflpgql vdtklsneel rnlftyvgdr dpkftggiin tfkvhnfdmt
      961 isaafsfkqt vmsspsyrgm dldrgrnytk diyeagtrlp gitspdmesn pgwmankwfa
     1021 dnrsnaynll dvwakeisyv rissirlgyt lpkeftnpmg isslrlsieg rnlfvfsngy
     1081 kgyfdpetyg niyaqpiaks vtvgfnisf
//
LOCUS       WP_099767035             943 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099767035
VERSION     WP_099767035.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 943)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 943)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 943)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..943
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..943
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104554
     Region          35..942
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlrisrslg vvavlyftan fsaqtkvkds vpkenkidei vmigyggvkk qnltsavssv
       61 ksdafddrpl ynvgqalqgq aagvnviqss gkpgagldvk irgnnsisss vsplyvvdgi
      121 qtnditgint ddildmtilk dasstaiygv ngssgvviit tkrgklgkpq lnfnaywgvs
      181 kavknidvln ldqyksllsd iqanggsdyl stvnnaryag intdwgkevf qtgfdqnynv
      241 nyafgnekvk aytalgyqdi agiinpskfq rtsvkinlda viapwlklns svnyfftslt
      301 ntndnlstar ggvvlsafnt prflpvygtd vnldpsdpiv ynqttgqind gykpgqfapn
      361 pyqsswenpv ayqsrkdktq tqrflsnlgl dvkllknlvw kpiisfdmtd srnvkftdgy
      421 qtsygrskmg igseeyylyq eynfentlty tlkksahdls llggvqinqk smenryfage
      481 kfeegttlfn ydlagtkgyd nhkeilrnas ffgralytyd gkytlmgvfr yngfsglape
      541 rkwgffpgvs aswlvskedf ladsktisel klrggwgqtg nvsgvpaysh fnifdpyftn
      601 geavysvkqy dssdltwett tdanigvdfg ffnnriklav daykrttkdl vfpfilgssv
      661 apiyrnfgsl enkglefsln tinikkenft wnssfnisfa enkitdlssq ylksisaani
      721 dgygqiirlq pgqsistfyg ykvdkvdpnt gdliykdlng ngyldvddrt tignpnpkyt
      781 fgfsnnftlk nwyldmlitg svgndvfnat rfdlemmndy knqstavlnr wttvgqitdv
      841 pransnsaqa isdrfvedgs yiklkavtlg ynfnkpfkgl nklnvyvtgq niftitdysg
      901 mdpevnafsp nrnttgaeks vfgidygtyp qvrtfiiglk anf
//
LOCUS       WP_099767790             940 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099767790
VERSION     WP_099767790.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..940
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104594
     Region          21..939
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrdlkysc liaviyfgmn vnaqttpkdt lakeqkidev vligygsqkk enitgsigiv
       61 sakdlankpn anpissiqgr lagvqvlnsg tpggsprvdi rgissltgkt vfivdgmitd
      121 disflgsqdi esmsvlkdps slaiygaraa ngaviiktkt gkskkpvfnf nsylgiktvt
      181 ntpkmvnsdq yiqlyneklv ndkvnnptfl nrsaypldtd wykeilrtsi insndfsaag
      241 svgklnyygs lgylqdegnl aagqginsgs gfnrfnskln lsykvndhit ignnftfskm
      301 rtdqalnpll dayssppvyg pidpttggyq yftlakipns rakldlyrsq ireerllnnv
      361 wgeykflsdf tfrisytsdn instkyeftp tfgyvpvsdq kpsklitrds rtrnyiwdnt
      421 lswkrnfgkh niellagfsr trnsysqaya ealrvnydgt nsslaisngt dvfltsfddg
      481 ernvipyqdr iesffgrlny dyggkylvna slrrdgtsky sandrhkvfp aisagwvvsk
      541 enfmseqnvf sllklraswg klgnpdvqra ytlnttkiqe gayygnngap aqtidkiidp
      601 nigwetttgr dlglemglfn nklkidatyf dkdtkdvvyg ivqgtvsgag nwnnyitnay
      661 sfnnrgfevs vnydtkindn ikigvygnlt tlknkitsvf ngsylqtgas lygnsiirlq
      721 egqavgsyyg yqvqgvfqnq aevdaaaiqn gatpggfkfs didgngvida rdktflgspi
      781 pkgtygfgvn lnvydfdfai dfqgvfgnki ynfnreqryg neswdldfyn nrwhgegtsn
      841 sypmatnnqa iilpnsfyve dgsyirirni qvgynlpqaf nkamsitklr lyvsaqnpwt
      901 sfkyngfspe ilntdrvqmg idnniypisa iytigmnltf
//
LOCUS       WP_099768699             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099768699
VERSION     WP_099768699.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107431
     Region          22..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltasllv lvlsssivva haqqkndtik tkeiegvvvt algikrekks lgyaseevka
       61 aeltggttnt gnvasllsgk vaglqvntnn nfggsanlli rgykslsggs plividgspv
      121 nnntvagsif dygnflsdin qediesinvl kgaaasalyg ergsdgvili vtksgrgtnd
      181 gswgvtltsg itagfidkst fpeyqtkyga gytskfnggt apdgnnyanf lddasygpaf
      241 nsnllvhqwd sfdpsspnyg katpwvaakn gpieffdtpi tyvntitiek gtkssnlsls
      301 ysnmlsnglm pnselrknti sakfshdftd klhasvfttl tlqgtkgrne tgysdnivsg
      361 frqwwqtnvd vlalrdaynn ngnsnfswnr tsatdatpqf wnnpyfqryq nyqsddrtrl
      421 fsyaqlkydv sknfgitgkl syddlqmvie erlmngslpq vfgasglnvs sgysrtnvkn
      481 tetnfdlfan ykfditsdln vsgiaggnvr rnlvdnifas tegglskpgl faisnsvrsi
      541 lppdetyaks vtsslyatas fgyknmlyvd gtyrvdrssn lpkanntydy ysvagslils
      601 elwkqdwlsf wkiranyaev gssttnyrlq ntfkargegl fdqpfflanp dlkpqrsket
      661 efgmeaqffk nrlgfdiaiy ktrtfdqiin lpvssatgyr tflvnagqin nkgievqlng
      721 tpfktdkfsw dvnvnwskne nevislngns qnyllasyqn nvslnarvge afgaivgsdy
      781 vydangqkvi nattgrylkn nnqvignitp dwiggirnsf rykdfslsfl idmkkggdvf
      841 spdmgygist glyaetadyr esgvvypgvn pngnvnttat tqpgisgrvd gynampnirf
      901 vydasyvklr easigyslpk svlantsird akisivgrnl wiihknlpya dpetgtgngl
      961 aakgqsigsl pttrdigidi tlkf
//
LOCUS       WP_099768701            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099768701
VERSION     WP_099768701.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110542
     Region          33..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttsvlf vvlsssflva naqerknrdt iktqnigeiv vtgalgikkk adaltgstai
       61 vkteeltkag npnavqaltg kvsglqinvp nssvnaqati nlrgqrsltg dngalividg
      121 apstaaifqq lppeviesvn vfkgqqgsal ygergsngvi ivttrkgsks ekiqftlsag
      181 idasfvyklp iiqqkygagy pdstfepglg eiggttwvpy entswgplys dpaiggqnvi
      241 igtpdangqf vmgkysprkd nikdffktgf lyqnglsmnv ggsdsyaffs inrtqndfvv
      301 drdrltrnnl lfkagkklgn frvdgtfnmv dqqtsetdsn lyddllqtps hinvkdfsap
      361 nlehyfstfa dnpywtvqna rynnksttfs gilnaeytin dhinisylgn vlsvsglges
      421 ynngwkfgke fansgtsydg msfldfghtn iesnyfksvs rrfnyygdlm lnfnyqltdd
      481 lgmklnignn irddsftvst vgginlqipg fyhinnvgna spasdlqntq trirsmagfa
      541 nldlsfkdyl flnstfriek ssvgatrpty tddlkiksyp yysvgvsfvp tkafeslkgg
      601 fmnyakvtas ytkvgstnai aayatdevtg lipsgfpmtn asflinrnpt npnikpefts
      661 tkeasvqlgf lndritfega vfrsdvsdli tnistsnasg tstlrdnigd aynkgyeldl
      721 gltpiktqdf ewnlrasyst ytsevtelkg gvddiallay atpgvgiyvk kgeqyplikg
      781 tkyqrddqgr iivgadgmpl atsgfevlgk vnpdyilgfs tsirfkgfrl sgtadyrtgn
      841 sfvamtknql aftgglekta dfdrsqgyiv pnsvknvgta snpvyvvndi pvggdgtyaa
      901 aanyfstngl fnavgeefvi dgsafkirei alsytlpkav lsstfinslt fgvyarnpfa
      961 wyaksnrnfa dpetssnsgg vnqrpgqalg vggvnangia ftgqyptfrt fgfnmsatf
//
LOCUS       WP_099768995            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099768995
VERSION     WP_099768995.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119132
     Region          22..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlatftv fllplyltaq einisgnvks engssvsgvn itdkstgkta vtdesgnfti
       61 sanpkdilef yapdfsiytv evsskrqysv vlkkanekqi egvvitalgi akkkekigya
      121 tqevgtkqfe tittpsignl fsgqvaglni snptgmqqap eftlrgnsnl vfvidgvive
      181 revfqnldpn nieninvlkg atasalygsr grygavlitt ksakkngfsv efsqntmvtt
      241 gftnlpktqt eygngshgky efwdgadggv ndgdmiwgpk fvpglkvaqw nspirdkltg
      301 qvvpwygavt gtqyndksry ervpidwtyh dnlntflkpa vinnnsfavs yknnkdiyrl
      361 sgnfmnyddr vpdsylqryg vnfssenhlg eklifdtkfn fnqtftpnip nydynpsghm
      421 ytiliwmgad vdgrdlkshm wipgregvaq anwnyawynn pwfgaekykn knrtniinaq
      481 tgleykated fsvkgkvsvv enhnkqeils pysyfnysap rsggyllnds ktwnlnsdil
      541 atykkkisdn fdftinaggs tfyykndidn astdglkipe lyalenstga vkyydylkek
      601 liysaystid iglynaffin vsgrndwsst lpkanrsyfy psasvsavis nlvkmpeavn
      661 mlklsaswak vaydfqpyat rnyyfnnkga tyngnpmfny ptilniensl kpeqtksyel
      721 gvsaglfknr ltldvtyfrt ldynnilefp tapssgftsq yvngneyttk gleisvglvp
      781 vktanftwrs linwstyeqk ltsiydnmsn ynnikpgerm dtyydytwkk spdgkvilda
      841 ktgmptrada psnlghfnpd wtfgfnntfk ykkftlnigi dgsiggvmrs qvvekmwwgg
      901 khpnstayrd leyanpgtyy fvpdgvnyna asgtysphtk pisfqdwaqn ypyqarvted
      961 eselfanvfd rtfiklrsvv leydfsylln pkgmiknftv nlsgynlamw kksknlysdp
     1021 dfkigigndn kdrtkigsgn diqdpssrwi gvgfnlkf
//
LOCUS       WP_099769016             952 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099769016
VERSION     WP_099769016.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 952)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 952)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 952)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..952
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104314
     Region          31..950
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnsklrvlsv gvlffingmy daqkkkpdta dtkkieevvi lgynrtstkp kdvsanttvs
       61 aevmenrpnv sflnslqgsa pgvtiasnsg spgsakidlv irgisslsad teplviidgv
      121 ptganqfrnl nsediesisi lrdaaatsiy gnrgangvll vrtkggkfns klklsysalt
      181 gvsvmpknky niadshqllk iqknggvlkg atmtdqqiad fdintnwekt ffkadvtqqh
      241 nisatfggen tsvysslgyl eqgglvpntk fqrftfrnni tgrsedkrfn ytaiiglgys
      301 krsqlnqenn sgingnvvqn pllgsfialp ylksgqygng rdlfnaigna ssangnfayv
      361 ledvlkgdqs vfgkfnetsi fastttsyki tdditlnnrt gadvkygnsf agrhpngyls
      421 ivvasnagie yggsetisns relnfttvts vnynkvfgeh tiglgaymey nkvhfyssgq
      481 vqngldpktf aigtgvgyia fdpdkdiylp avgatkvtag alsyfatady dfadkygfsg
      541 tlrrdgsyrf apgskwgtfw svggrwnidk egfmsgsffd mlklrasygt qgnaniiaag
      601 ddtnplllat gisreinvva ngygntpgyf lnnfanatvq weeikqgnig ldfrilknkl
      661 egnvdvyrkn temlyynips sailgqynyr gnygslkneg velvlrynvl snqnykltlf
      721 anasynenki tkllipvttg sllleeggti newnlvpylg vnpnngnely ldsngnvseq
      781 aldkdrrktg knyfpkytgg fglnsefkgf fldvlfsfqa kfwrsdnqls walnpaymrs
      841 gnnvsadlln awtpdnrdtd ipslnapvss itdrllfdas ylrlknislg ysvpkkffne
      901 nsviksakif vqgenimtws kwrgydpegl gtfplsvypn prtfslgvnl df
//
LOCUS       WP_099769022             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 52].
ACCESSION   WP_099769022
VERSION     WP_099769022.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 52
  ORGANISM  Chryseobacterium sp. 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Chryseobacterium sp. 52"
                     /db_xref="taxon:2035213"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106647
     Region          28..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktvipvll vfslsayaqe tkkadtantt kieevvvtsl gikrqarslt yssqqiggde
       61 ltevktpnfl nsisgkvsnv qinrtngvgs svrvlmrgnk sanssqplyv idgipiingv
      121 gkapeasqys tmpdagdvls sinpddiesm nflkgasasa lygsmggngv ilittkkgkl
      181 grssisynts ltvdqayslp klqhsylsyd pavsgqapgi sneswgakga skdhlkdflq
      241 ngttwvnsls fesgtekstn yfsignttnk givpssyfdq ynisfrnssk ylndkltlda
      301 nfigslqnsv nrqtpgvsfs plvslywlpr gvdfdqynds nysfidktrl lpaqnwwaig
      361 pdgkfngnpa tqnpywilnr nkvtvnnknt ysalslayqi npwlsarvrg nyswnvtdsq
      421 rgvsaysdpn litssgingr llqnkyenss tygdvllvgs pklsedisld ftvggsints
      481 rntvteidna ylsapnlftv snlqwnvdrs vgdgfhnlyy stkkqiqsvf asaslgyknm
      541 fyvdmtfrnd wdsslaltgt ngydyesvga navlssifkl petisfwkir gsyatvglgl
      601 panlttatsp yntaygyivd agqilypkys lvtdpafsel fvkpelnktf eagtelrlfk
      661 nrlsfdityy nskatnqllp vtissnlggl psgsyyvnag kiqntgfess lsykilnsek
      721 lgwtaslngs tnknkivelf pdrlkvpenq llaltgggay tklklggsfg diygikflrd
      781 dqgrilvdad gkpladknlg ylgnpnpkfm lgfnnsfnig klgisflidg kfggkvlslt
      841 ekandmlgvs qtsasardag gvsipnavya pgtpnagaay tgltdakvyy kavganqega
      901 gideayiysa ttvrlrqasi aytfdvnssy lrsatvsivg tnlfffykka pfdpeqvsgn
      961 tpggvgvdsf gipitrsigl slkanf
//
LOCUS       WP_099787343             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Massilia
            eurypsychrophila].
ACCESSION   WP_099787343
VERSION     WP_099787343.1
KEYWORDS    RefSeq.
SOURCE      Massilia eurypsychrophila (Mokoshia eurypsychrophila)
  ORGANISM  Massilia eurypsychrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Massilia eurypsychrophila"
                     /db_xref="taxon:1485217"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38767
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qvivqsgagl haavlddaya aagatigsaa
       61 dafgadmvlk vrapdaters mmkqgavlig mlnpfdadni aamagaglta faleavprit
      121 raqsmdvlss qaniagykav mvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpyltdeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgrpapvli seetvkamkp gsvivdlavs qggncplsem
      301 nktvlkhgvw ivgepdlatl vaadasalya rnvldflklm idkddalaid redeilkasl
      361 vcmsgevlrk
//
LOCUS       WP_099794705             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. 54].
ACCESSION   WP_099794705
VERSION     WP_099794705.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. 54
  ORGANISM  Variovorax sp. 54
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Variovorax sp. 54"
                     /db_xref="taxon:2035212"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38784
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeta agetrvavtp etvkklvasg hivrvqsgag vaasvtdaay qtagaeitda
       61 agafsadmvl kvrtpsdaea aqlkagavvi gmlnpfdaag lqrlaaagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarlvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmppswla
      241 rqqievakrv aladvvista lipgraaptl itedmvksmk pgsvivdiaa gkgpvnpdgg
      301 vggncplsea dktvvkhgvt ivgetnlaal vaadasalya rnvldflklv vtkegalkid
      361 leddivaacr vtqdgqvtrk
//
LOCUS       WP_099797999             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Parathermosynechococcus lividus].
ACCESSION   WP_099797999
VERSION     WP_099797999.1
KEYWORDS    RefSeq.
SOURCE      Parathermosynechococcus lividus
  ORGANISM  Parathermosynechococcus lividus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Acaryochloridales; Thermosynechococcaceae; Parathermosynechococcus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Parathermosynechococcus lividus"
                     /db_xref="taxon:33070"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40703
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvgvvkere vgeqrvalip dvvaklvqqg yhicveagag dmahfsdddy raagadiyps
       61 iedvwggvdv llkvsplrdr evewirpgtt lisflnplgn pwqmqhlaer hitafaleci
      121 prssraqsmd alssqaavag yaavllaasn lprffpmltt aagtiapakv fvigagvagl
      181 qaiatarrlg avveafdirp avkeevqslg akfvevnlde dtvaaggyak dvsesakhkt
      241 qeaiaahvhs advvittaqv pgkpapllvt ermvasmkpg svivdlaaeq ggncactepg
      301 rsichqrvti igainlpssm aihasqmyak nistllkyls pnqelqlnfg ddiidaacit
      361 hegqvrnprv lqllhpadtl avsv
//
LOCUS       WP_099800555             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_099800555
VERSION     WP_099800555.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35925
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlmk
      181 aynrlilndf acvvrechaa frsvllrihe rkgivyheqd slntlmanlm argvisaeyv
      241 hkfhflsdvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vap
//
LOCUS       WP_099815286             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_099815286
VERSION     WP_099815286.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38734
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etlkkligqg hqvtvqrgag lnasipdsay eaagaslgsa
       61 adaygaqlil kvvapndqel alinsgsllv gmlnpfnsel igkmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvqangv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_099827428             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oceaniglobus indicus].
ACCESSION   WP_099827428
VERSION     WP_099827428.1
KEYWORDS    RefSeq.
SOURCE      Oceaniglobus indicus
  ORGANISM  Oceaniglobus indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Oceaniglobus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Oceaniglobus indicus"
                     /db_xref="taxon:2047749"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55108
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtpaevm pgenrvamtp esvvmlkklg ydcviqagag gaagftdaay ekagaevaad
       61 adalwsgvdv iakvrepssd evsrlkpgqt lisffwpgan ealleqakdt gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aitlafdvrp evseqiesmg aefvfldfee ssqdssatgg yaapsspefr
      241 ekqlekfrel apdidivict alipnreape lwtedmvqam kpgsvivdla aerggncklt
      301 vkdekivtdn gvtiigytdf psrmaaqsst lyannirhmm tdltpekdgq vvhnmdddvi
      361 rgatvthgge itfpppkpkv aaiaaakpkp kakeltpeek rdaeiaafrs atksqagmlv
      421 igalvllvig ayapasfmsh livfalacfi gfqviwgvah slhtplmavt naisgivivg
      481 allqvgsgnw lvvllaaisv liasinivgg flvtrrmlam fqks
//
LOCUS       WP_099859954             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Roseateles
            chitinivorans].
ACCESSION   WP_099859954
VERSION     WP_099859954.1
KEYWORDS    RefSeq.
SOURCE      Roseateles chitinivorans
  ORGANISM  Roseateles chitinivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Roseateles chitinivorans"
                     /db_xref="taxon:2917965"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38772
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpqeta agearvaatp etvkkliaqg htlrvqqgag ldasvtdeay aaagadivdr
       61 asafgcelvl kvrspdagel alfkpgavla gmlnpfdrdg lqrladarlt afaleaaprt
      121 traqsmdvls sqanlagyka vmlgafhyqr lfpmlmtaag tikaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf ievpyetdee rqaaegvggy arpmppswlq
      241 rqqievakrv aqadvvitta lipgrpapvl vtedmvramk pgsvivdiaa paggncplte
      301 pgqtvrkhgv tlvgetnlps lvaadassly arnvldflkl vltkeggfal padddivtac
      361 lvahegqvlr qa
//
LOCUS       WP_099865468             406 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neopararhizobium haloflavum].
ACCESSION   WP_099865468
VERSION     WP_099865468.1
KEYWORDS    RefSeq.
SOURCE      Neopararhizobium haloflavum
  ORGANISM  Neopararhizobium haloflavum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Neopararhizobium.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Neopararhizobium haloflavum"
                     /db_xref="taxon:2037914"
     Protein         1..406
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42052
     Region          3..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maktifiake taegesrvag spdsikklag lgfdvvveag agagsripde afeqagarig
       61 qagdaaaadv vlkvrrpasg elsgykkgal vvaimdpygn etaikemadk gvtafamelm
      121 pritraqsmd vlssqanlag yqavidaaht fdrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatakrlg aavsatdvrp aakeqvaslg gkfvavende fkeaeaaggy akemskeyqa
      241 eqaelvaehi akqdivitta lipgrpaprl vtremlksmk pgsivvdlav erggnvegae
      301 agkiaevegv rvigynnvpg riaasaslly aknlltflqt makdgevtid fddeivkqta
      361 lthdgrvvhp kfggaepetp kdepstpanv gqetapstad eqkgea
//
LOCUS       WP_099867851             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neopararhizobium haloflavum].
ACCESSION   WP_099867851
VERSION     WP_099867851.1
KEYWORDS    RefSeq.
SOURCE      Neopararhizobium haloflavum
  ORGANISM  Neopararhizobium haloflavum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Neopararhizobium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Neopararhizobium haloflavum"
                     /db_xref="taxon:2037914"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53653
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpketl dgerrvamtp esamrlaklg yeclieegag iaadfkdday reagvtvvad
       61 atrlwreadi ilkvrppaed einrltadkt lisfigaahd aalldrlaat natviamdav
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkmppakv lvigagvagl
      181 saigtaqalg amvrafdvrp evaeqiesmg atflmldfee dgsgeggyak paspefiake
      241 melfaaqape vdivittali pgrpapklwp aemvramkpg svvvdlaaeq ggnceltqpg
      301 tivetdngvk vvgftdypsr maaqasalya tnlrhmmddl tpskdgtpvv nmdddvirga
      361 tvvkdgavtw pppppkvrai aqpkkkpaaa atspasekka gslpfflaga allaliglfa
      421 paefvarftv fvlacfvgyq vvwnvtpalh tplmsvtnai sgiivlgall qmsapsglvv
      481 alavlaalia siniaggfyv trrmlnmfrk d
//
LOCUS       WP_099870244              97 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_099870244
VERSION     WP_099870244.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..97
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=10379
ORIGIN      
        1 malavlmtta ggavvnaeqr lhspvgfeqr devllelkes tqpfgqgvqh lepinppvtq
       61 mapsvqkssw fgsflggvqk lwnalccsvg ltwckvk
//
LOCUS       WP_099904212             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. TLI_171].
ACCESSION   WP_099904212
VERSION     WP_099904212.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TLI_171
  ORGANISM  Streptomyces sp. TLI_171
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces sp. TLI_171"
                     /db_xref="taxon:1938859"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52760
     Region          13..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msehdssprp pqrvgvvaes apgetrvaat pstvrgllal gyevvvesga gsasgfddra
       61 yaeagagvgd awaadvvlkv napsdaevar lrdgatlvgl ltpaqrpell aalsarpvta
      121 lsldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvrslggeyl pvevaqeast dgyakatsad
      241 ydraaaelyh aqaadvdivv ttalipgrpa pklltaedva amkpgsvivd maaaqggnva
      301 gtvagrtvvt dngvtiigyt dlasrlpaqa sqlfgtnlvn llklltpgkd grlvldfedv
      361 vqravtvvrd gettwppppv avsaapaaap aaapavaepr psrvtpavrf gliglgmlal
      421 flvvgfaptq laenftvftl avvigyyvig kvhhalhtpl msvtnaisgi vvigallqig
      481 hesvlvtvls fvailltsvn ifggfavtrr mlsmfskg
//
LOCUS       WP_099913830             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Puniceibacterium antarcticum].
ACCESSION   WP_099913830
VERSION     WP_099913830.1
KEYWORDS    RefSeq.
SOURCE      Puniceibacterium antarcticum
  ORGANISM  Puniceibacterium antarcticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Puniceibacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Puniceibacterium antarcticum"
                     /db_xref="taxon:1206336"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55455
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egearvamtp dsarmlqklg ydcaietgag vaagftdeay anagveifnt
       61 aaglwkeadv vakvrpptdt eikrlsdgkl lisffwpaqn gelmeaaakk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvfldfee aakdgaesgg yasvsspeft
      241 aaqlkkfrei apdidivitt alipnreape lwtkdmvesm kpgsviidla aekggncklt
      301 vmdqkivtdn gvtiigytdf psrmatqast lyatnirhmm tdltpgkdgv vnhnmeddvi
      361 rgatithake vtfpppppkv kaiaaqkpke kvkektpaek raeevaafka qtksqvtlla
      421 vggalvlfag lfapasfmqh livfvlsvfi gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgsg lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_099914029             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Massilia
            psychrophila].
ACCESSION   WP_099914029
VERSION     WP_099914029.1
KEYWORDS    RefSeq.
SOURCE      Massilia psychrophila (Mokoshia psychrophila)
  ORGANISM  Massilia psychrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Massilia psychrophila"
                     /db_xref="taxon:1603353"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38777
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qvivqsgagl qasiideayv aagatigsaa
       61 dafgcdvvlk vrapvdaera lmksaavlig mlnpfdaant aamaasnlqa faleavprit
      121 raqsmdvlss qaniagykav mvaantyqrf mpmlmtaagt vkaarvlvmg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpfitdeer eiakgaggya rampadwmrr
      241 qaelvherak ladiiittal ipgrpapvli seetvkamkp gsvivdlavs qggncplsem
      301 nktvlkhgvy ivgepdlatl vaadasalya rnvldflkli idkddqlvid reddilkasl
      361 icsggevlrk
//
LOCUS       WP_099953896             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium currus].
ACCESSION   WP_099953896
VERSION     WP_099953896.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium currus
  ORGANISM  Methylobacterium currus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Methylobacterium currus"
                     /db_xref="taxon:2051553"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39371
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd paeprvaavp etvkkykalg aevtvqsgag lkagvpdady eaagasiapd
       61 akaaadgadi vlkvrrpaae elpalkrgai viaimdpygh edevkamada gvsaiamelm
      121 pritraqvmd vlssqanlag yravvdgaav ygralpmmmt aagtvpaari fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedee fkqaetaggy akemsaeykk
      241 kqaelvashi akqdivvtta lipgrpaprl vtadmvaamr pgsvlvdlav erggnvegvk
      301 adeivetqng vkivgyanvp grlaatsssl yarnlyafve tlvdkaskal avkwddelvk
      361 atcltrdgav vhpnfqpkaa
//
LOCUS       WP_099978726             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_099978726
VERSION     WP_099978726.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38884
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvplemq agetrvaatp etikklisqg hritvqrgag iqasvpdsaf eaagavigea
       61 seafagelil kvvapndnel alinsgsvvi gmlnpfnnel igkmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv egsdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera rvadiiitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adevvvahgv tlvghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_099980521             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Trueperella pyogenes].
ACCESSION   WP_099980521
VERSION     WP_099980521.1
KEYWORDS    RefSeq.
SOURCE      Trueperella pyogenes
  ORGANISM  Trueperella pyogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Trueperella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Trueperella pyogenes"
                     /db_xref="taxon:1661"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52890
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresg gqtlvaatpd tvgklsklgy evvvehdags aasfpdslye sagarivske
       61 eawaadivta ldapaladld lmrsgatlis rmapgrnpdi lqalssrsit glamdmvpri
      121 sraqsmdvls sqanvagyra vieaahhfgr lfsgqvtaag kvapanvyvi gagvaglaai
      181 gtansmgaiv katdvrpeta eqvesmgagf vaipvatees adgyakemgq eqaaaaekly
      241 teqaawadiv ittaaipgrr spvlltaeav agmkpgsviv dmgaanggnv vgsrpdevvv
      301 tdngvviigy selaarlpgq asqlygqnvf nffklatpdk dgvlhldldd eivrsmlvtl
      361 dervmypppp vkvsaapapv passeevtsa eakekswiak hwwkiaagav ftwliltapa
      421 gstthflvfa lavvigfyvi tsvthalhtp lmsvtnaisg iivvgalmqv sassvvvqil
      481 sfiaiavasi nifggflvte rmlkmfhrs
//
LOCUS       WP_099989823             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_099989823
VERSION     WP_099989823.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53571
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifillipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_099993494             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas salmonicida].
ACCESSION   WP_099993494
VERSION     WP_099993494.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53293
     Region          22..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrlt rlglaalllt tcfgasglaq adeatpkgki earselfakd hvdqfsswke
       61 tsesatrtda laedpqmvvl wggypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggseivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eqyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqskemlqgi vqqrkdavte iklkvekqlv hahfeakaaw
      361 dagatetqmk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llatkgishe ialpdistke kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_100000995             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium zundukense].
ACCESSION   WP_100000995
VERSION     WP_100000995.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium zundukense
  ORGANISM  Phyllobacterium zundukense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Phyllobacterium zundukense"
                     /db_xref="taxon:1867719"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44308
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke idtneprvgg saetvkklig lgftvivetg agtasripdr efeaagatig
       61 kaadvkgadv vlkvrrpata elksykqgav iiamldpygn daavkelada gvtaftmefm
      121 pritraqvmd vlssqanlag yqavvdaaee ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaalvndhi akqdivitta lipgrpaprl vtremysrmr pgsviidlav erggnvegav
      301 agkivevdgi kivghlnvag riaatasqly aknlvaffet lvdkdsksvk infddelvka
      361 tvlthggkvv hpnfanaava apaakpaakk vapaakdapv kaeakkaapk kattpkaapk
      421 ktegea
//
LOCUS       WP_100003333             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium zundukense].
ACCESSION   WP_100003333
VERSION     WP_100003333.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium zundukense
  ORGANISM  Phyllobacterium zundukense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Phyllobacterium zundukense"
                     /db_xref="taxon:1867719"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55157
     Region          4..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mgqkvgslke lasgesrvam tpesaqqlqk lghaclveag agkgagisde ayraagvtvv
       61 edaaalfaaa dvivkvrppt veeverlsag qtllsffypg qnavllerak erganiiamd
      121 mvprisraqk mdalssmani agyramieag nnfgrfftgq vtaagkvppa kvlvigagva
      181 glaaigvats lggqtyafdv rpevaeqies mgaefvyldf ddgqedgaas ggyaapsspa
      241 frekqlakfr qlapemdivi ttalipgrda pklwladmva amrpgsvivd laaerggncn
      301 ltvaderivs dngvivigyt dfpsrmaaqs salyatnirh mladltpgkd gvivhnmedd
      361 virgatvvfe gaityppppp kiaaiaarkp kgkvkeptpe ekrateataf rtqtrsqlal
      421 lavgtalllf vgayapsafm shfvvfvlac fvgfqviwnv shslhtplma vtnavsgivi
      481 lgallqigsg nwlvtvlaal avliatiniv ggflvtrrml amfqks
//
LOCUS       WP_100030566             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_100030566
VERSION     WP_100030566.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53557
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmel
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_100036841             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_100036841
VERSION     WP_100036841.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53598
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mirikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkl qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_100074099             964 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium camelliae].
ACCESSION   WP_100074099
VERSION     WP_100074099.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium camelliae
  ORGANISM  Chryseobacterium camelliae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 964)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 964)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 964)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..964
                     /organism="Chryseobacterium camelliae"
                     /db_xref="taxon:1265445"
     Protein         1..964
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105825
     Region          39..963
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgfkpikin katvffamal lpsslaysqa krdtlpkekk ieevvvigyg tqrkeavtgs
       61 vatvkgdalr evpsanitqa lqgraagvdi sqsstkpgas mqirirgtrs ltgsndpliv
      121 ldgipfvgsl sdisssdiks idilkdasat aiygsrgang vilvttnrgs kgqkprftyn
      181 nftgvqtlfs kypmmdgpkf aklrayatpf nsanplyatt gdesvnnntd wqdlyykpam
      241 itshdigvsg gteggnynvg lsyfkqdali plqnyerfal rmavdqqvgk nfkfgfttnt
      301 nysqsegngl npgavlgysp lvnpynadgs lkrtmitagg idqtwiytrq sieslgdkyv
      361 detksfasyn nmygeltlpl nglkyrlnvg ldyrtsnsgn yagvgvfntn plgpssagrg
      421 nnqtyhwvle nlltydrnfg khkinavaly saednkytss ymsaknvpad ffqyynlgqs
      481 pqaditvrpe dqvytkngll samgrvmytf dnkymitatl radgssrlap gnkwhtypal
      541 slgwnvtnes fmqnikainl lklragwgqt snqavapyst lgqmavapyn fgsgsstgvy
      601 vtqapnpglg weysktqnyg vdfglfnnrl sgsveyykth tfdlltsknl pmssglvnvi
      661 snvaetenkg fevalngvif dnpegftwea gvnfytnrnk ilalasgidk desnlwfvgh
      721 ninalydyqy iglwqagdqh mgilepgdpr dvvgsikvly tggynadgtp vraigpadrq
      781 ifdtapkfqg gfnmrfaykn fdlstvgafq hggilistly gsasylnrmt grgnnvdvdy
      841 wtedntdayf prpgrhlsgd npkysstlam fdasyvklrt itlgyninkd flkdlkinsf
      901 rvyftvtnpv vlfspyhkfs gmdpepnsfg nqnqavngyq srqlvigtnn pstrnylmgi
      961 nltf
//
LOCUS       WP_100073893             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_100073893
VERSION     WP_100073893.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38862
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lrasvpdsay eaagavigdt
       61 neiyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adevvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_100074616             939 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium camelliae].
ACCESSION   WP_100074616
VERSION     WP_100074616.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium camelliae
  ORGANISM  Chryseobacterium camelliae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 939)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 939)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 939)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..939
                     /organism="Chryseobacterium camelliae"
                     /db_xref="taxon:1265445"
     Protein         1..939
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104465
     Region          35..938
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrdlkysc liavlyfgmn vnaqttprdt takeqkieev vlvgygtqkk envtgsigvv
       61 sakdladkpn anpmssvqgk lagvnivnsg spgssprvdi rgvgslsgyt vfivdgtitn
      121 disflnpqdi esmsvlkdps slaifgaqaa ngaviiktkt gkgkpvynfn sylgfkkitn
      181 ipkmansdqy ielyneklin dtgssngsls ranfpadtnw fneifrktsi inandfsasg
      241 slgklnyyas lgllqdegnf nagnninsgn gfnrfsskln lsykitdnlt igdnftfskt
      301 rtdainnpll naynappifs pmnaatgdyq ffngysianp iavldlfrgq treerllnnv
      361 waeykflkdf tlrvsyttdn yntnqyeytp vltylpkdqq kptklltrds rtrnyvwdnt
      421 lgwkkqlgdh nlevlagfsr vrnsyqqsyl ealnvnyngt neslnifngt givgttydvg
      481 rdvvpyqdri eslfarvnyd ykgkyllngs vrrdgtskys sgdrfrtfpa vsagwviske
      541 nfmsgqnvfn llklraswgk lgnpnvpray tqlvtfinsg ayygntgypa atidqfidpn
      601 igwetttgrd vgvemalfnn klkiegtyyd kdskdvvygv vqgtvsgagn wnnyitnays
      661 fnnrgfevnv nydtkitdkv rlgvygnltt lknkitsvfg gsyletgasl fgnpiirlqe
      721 gqavgsyygy qvsgvfqnqa dvnawaqqtn atvggfkfad idgngvidsr dktflgspip
      781 kgtygfginl nvydfdiavd fqgvygnkiy nynreqrygn enwdldfynn rwrgqgtsnt
      841 ypmttnnqdi ikpnsffved gsyirlrnvt igynlpkdfa rsmaltrlrl yvsaqnpwts
      901 fkyngfspei lntdrvqmgi dqniapisai ytfgmnltf
//
LOCUS       WP_100075554            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium camelliae].
ACCESSION   WP_100075554
VERSION     WP_100075554.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium camelliae
  ORGANISM  Chryseobacterium camelliae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Chryseobacterium camelliae"
                     /db_xref="taxon:1265445"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110644
     Region          32..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkitvgilt lvlssslavs naqekrsdtv rtqeiegvvv talgikrekk slgyatqevk
       61 gedvnknptp nflnnlsgqv agldvkqstn fggsinvvlr gfksfsgsnq plfvvdgvpi
      121 innnintssq atgrygidyg naasdinpnd ietinvlkga aaaalygsra angaiiittk
      181 kgkknqkgig veysssvtis sidrttfpky qteygqgyvg edewgsyngd laagfgsdas
      241 ygpkydpnll vyqydafipg spnfgkatpw tmakngpisf fkngsnftns vslsggdnta
      301 tyrinytnqd atdimpnssl vknnfggnas ykitekltas lyanyitqkt kgrndtgyng
      361 niltgfrqww ptnvdvkqqe efynishqny twnitsptdl apqywdniyf qryqnyqnds
      421 rdrfsgnvsl sydvskelnf llrlsndsys mtteerkang svpnifglnp ntpqpsgyqi
      481 gnyrlserny dfigtykkdl tedlnlngvl gtniryntay sdihstvggl svpnyfdisn
      541 skerplnqtt dvskqiiglf aqaslgyknt yylegtirrd qstalskgnn vywypsvsgs
      601 vvfsnlikap wlsfakaran yavvgndtda nqlidtylag spfgsqpvyq fngvlknpdl
      661 vaeklksmef gietsflknr igfdatwykn dsenlisnvl vsyasgttlq kqnignlrte
      721 afelslrltp iksqsfswnl vanwsnpktt italkngvdn lalqtntsqg gvtlnaplgg
      781 lygtiygsdf iyapdgqkvi dpntgaymkt tttnnnlgsy qaqwfgglrn tvtyknlsls
      841 flidmkkggk vfsldqsygy gtgiyadsvg lndlgnpirn tlangggiiq qgvipdpnnp
      901 gqyitnnvrl dkswssqvln tdppaaafvy dasyiklrea sitynlskea lgskfiqgms
      961 fsligsnlwi ihknlpyadp eaglssgnlq gyqsgvmptt rnfsfnvkvn f
//
LOCUS       WP_100075259             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium camelliae].
ACCESSION   WP_100075259
VERSION     WP_100075259.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium camelliae
  ORGANISM  Chryseobacterium camelliae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Chryseobacterium camelliae"
                     /db_xref="taxon:1265445"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110558
     Region          21..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkethkllv lsllglvsvn lsaqqkikkd tiknidevvv talgikrndk slgyvaekin
       61 seeilrtqnn nwaqslegkv aglkiqtaga gplgsalikl rgdismnmdq nnalivvdgv
      121 plngtttgtg fsaygagska dlpidygngl ntinpddies itvlkgstaa alygsrgagg
      181 aimittksgk tkkgkiqitl nsyssydtvl kwpdyqyeyg qgtmqkdasg nyyysygasa
      241 dgvntgstss afgpkfagqs yfqydptveg qslqrqlwrp ykdnikgfwq tgttfsnnva
      301 lessnentsf rtsltylkne wmmpntgfdr lnaalsfdhk lneklkvgvk fnysktssdn
      361 lpatgysnqs isyfmifqnp nvdlawyspi wkkgqyqidq ihpfssyidn pyliayemln
      421 gvdkhfitgn vnlnykftkn fevmlrsgle ltneertqkr pwssanylqg myreqhikqm
      481 dmnndilfty knkfkdfdfs asaggniryl eytmgdyiad gllrpgvytl pngianinki
      541 aapgdrqvns tyglvnisyk nkvfldltar ndwsstlpke nrsyfypsaa tsvilsdifn
      601 lssnnfnywk lraswsrvgn dtnpymllky ynnsnfngsv espslypnpn lkpemltnme
      661 agmdfsiikn risysitayq nnnknqiiri palwetgyss rvinageirn rglemtlnty
      721 pvknknfsws vnanwsmnrn timslpeefq gepyimgsvg gvvyynavvg gslgdmygyg
      781 lmyspdgqvv fgsdgltakp tktkkignay pkwragiqnd fryrnftisf sfdgqykgig
      841 ysqshhkmte qgklthtlig rdnpgglivg egvvqnadgs yspntkgipv styyadyyrr
      901 anvetnsfdt sfvklrdari sysfpksvtd elkitdltla lfgrnlwmwt kfplfdpeva
      961 tlndsqitsg veigqlptar tvgiqlnvkf
//
LOCUS       WP_100075847             962 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium camelliae].
ACCESSION   WP_100075847
VERSION     WP_100075847.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium camelliae
  ORGANISM  Chryseobacterium camelliae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 962)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Chryseobacterium camelliae"
                     /db_xref="taxon:1265445"
     Protein         1..962
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106699
     Region          37..961
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvfkipvsv gyltgrvlli galsasplfl aqkkdslkek sldevvvvgy gtqkktkvsg
       61 avteasldki tsrslsgvge alqgkaagvt vvneggdpng tpkvnirglg gingetplyv
      121 vdgvvfngtp sinpndiqdi svlkdasaai ygarssggvi littkkgrkg nltvdfdvky
      181 glnqawkike tlnaaefqdv mykayenagk lnnlpiafnp nlypdgritr tdwmkeifrt
      241 gaiqeynmnv sggneksryf vgmnhrnleg illntqskry nfrvnsehkv kdwltigenm
      301 yynysdgnta dtrngytgai vaamyyppnv pvytssgafs glpvdvaggy gdvinpvayl
      361 krisirnpth eilinpyaei tlakdlkyrs nfsqtfkigd mktftarvpe vgkifdmnsl
      421 eyqsnnssts laeqlltykf spgrhnfdfl agftfqktvd dgfiaksydf rseaetfqyl
      481 qnaadtnrev ssyrfrqalv sylarvnydy agkyivsvlg rrdgsslvap qnrfanyyav
      541 sgawvpsken fmkdiawlsn lkfrgsygil gnlggissqa vnplmtrynn vifgqdpsqn
      601 iayyattrpn pdlkwgkseq tdfgmdasff hnslslqfdy fiknskdqif nvslpstaty
      661 snqyinaglf qdkgyelgin ynskktgdft ysigvvfsql kntvkqlagv deifindngv
      721 rgvlkptrvk vgdplysfyg yrtggifqsq eeinnykdan gnliqpnakp gdikflkkeg
      781 ntgtlnnsdf vnlgspypkf syglsynmtw knfdlnlfvq gvygnkifng lkfislnpgg
      841 tgqnynmdrd ilnawtpqnt dtniprlvqg dpsgnyskvs dfyvedgsyl rlknltigys
      901 lpielyrkld vsklriyvtt nnlltitkyt gfdpevgmns ygvdtgrypq arafifglev
      961 gl
//
LOCUS       WP_100076439             951 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium camelliae].
ACCESSION   WP_100076439
VERSION     WP_100076439.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium camelliae
  ORGANISM  Chryseobacterium camelliae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 951)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Chryseobacterium camelliae"
                     /db_xref="taxon:1265445"
     Protein         1..951
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103628
     Region          36..949
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklsvlsa gvlffvgqaa faqttkrnrd tattekqiee vvvlgyskks tkakstaasv
       61 tvdskalenr pnisfinslq gnapgisins tsgspgsgki nvmvrgmssi nastdplyvi
      121 dglitsatqf rnlntedies isvlkdaqat siygnrgang vvvintknar fnsglkvtyd
      181 vltsfsvlpk tkynvlgstd llnlqneygv gegagltpeq iaaypntdwn kqffrtgmlq
      241 qhtlgitsgg kninnytsig yldsegtfrs tdfkrftlrn nlsgksddgk ltfgmqlavg
      301 yskrnqldqe tnsniqnntv qnplfgsllt psylepypfv ngqdmfnqlg gsgvnypgwi
      361 ladiirggvr nqftetsila nanvnykitd wlsvgnrtgm dyresdrdia rdptgylalv
      421 arasgaqygg feqmtntkdl tvnsvtnitl dkkfgdhslt vagyldyvka hylfksntqn
      481 gldpfnwafg agtgyipfnp stpslylpsv sagkinagtl ayvgtvdydy agkygisgtv
      541 rrdgsyrfpk enrwetfwsv ggrwnidked flagssvkll klrgsygttg nqnliqpann
      601 gnplftgtnv ytdlissgtg ymntvgyaav ignpnvkwek vtqanigldf glfnnfvegt
      661 fdvykkttdr lfnsitlsaa tgqysingnn gelenkgveg slrfnilknk dynvsifang
      721 aynknkilsf egadlsgdnv eapggpigqw nlyhyvgvna qtgeqqflda ngniteapta
      781 ndkvltgksy vpkftggfgv nadykgwfad vlfsyqaggy qydniysylm dpsalgqgmn
      841 fagdilnswt pnntntnips iqannigleg ssdrflfktd yirlknvtfg ynfnkdllrg
      901 lpitslkvfv qgenlatwte wkgydpepii pysqgvypnp rvvsvglnvq f
//
LOCUS       WP_100076603             983 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium camelliae].
ACCESSION   WP_100076603
VERSION     WP_100076603.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium camelliae
  ORGANISM  Chryseobacterium camelliae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Chryseobacterium camelliae"
                     /db_xref="taxon:1265445"
     Protein         1..983
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108188
     Region          27..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiklslvtt avlffsgmhf adaqrtksdt aakekqidev vivaygsqrk etlvgsntev
       61 kakqfadrpi snigqaldga sagvkiaast gqpgsapniq irgigsygis tsplyvvdgv
      121 iytgslsaln pndiasfnil kdaastslyg saaangvvli ttksgrkgtd alnfsmstgy
      181 vgrsipeydr vdvyqyyplv weamrngrfa tnptlglaaa ntfatnnlis gvlktnvfnv
      241 adnalvidgi lnpnaqlkyt dldwqkplik tgfrqnyeln ysggsnktty fssvsytnet
      301 gylvksdfer ftarlkvdsq lkswlklgts isgvssngnn sldgadnnss yinpyswtrt
      361 mgpiyspyah dpntfatlyd aagnimydag sargadaaag rnviqetlln rdisknyyii
      421 srayaevkvd pyltlstnvg ydirnnrrgr yinkiigdaa pagaaeksty teqtltfnql
      481 lnykrkfgsh nfeyllghen ykymyeymyg ykqgqtvdnn ddlinfvtpt sltsqtdnyr
      541 kesvfsrlny dydskyllsg sirwdassrf kedvrwhsfw svgagwrikg edflsdsrfv
      601 selklrgsyg evgndgtnsy ymykstyslg ynnasepgil fgfladptit wetnkqtdlg
      661 vdfglfggri tgtaeyynri tddlifpvpl pvsggvpgns isknvgtmyn rgfeftinad
      721 iiktesftwn vnanastlkn qitelssgit eiingskkis vghsiydywl rqwygvdpad
      781 gsplflvadt yagttasdir tvngtlvttn fnkakydysg taipdlfgsf gtaftfkqws
      841 lsamftyqlg gmtydtnyqs lmssypqgsa lstdilnrwt tpgqitdvpa lnsstyvssn
      901 aassrwlvks dfislrqagl sysfnptdis qygltafril vsgenlwskt arkgleptqs
      961 fngtttnryt pariitigfn lsf
//
LOCUS       WP_100076786            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium camelliae].
ACCESSION   WP_100076786
VERSION     WP_100076786.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium camelliae
  ORGANISM  Chryseobacterium camelliae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Chryseobacterium camelliae"
                     /db_xref="taxon:1265445"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118314
     Region          119..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktaisiav lgvlclsemt hayvpatcqq svnsaripvk qvfeklgkkt rtqffysasd
       61 mqgilvddtk inysslkeal sylkksysid fiiqnntvtv rriakssdnr plsihmdamk
      121 rdtisprekn idevvmvgyg kqnrkdisgs issidekqmk gvasgnfgdi iagkatgiqv
      181 sqanaspgss ptirvrgigt ltagsnpliv vdgfpltegt nlnsidpnsi akidilkdaa
      241 ssaiygsrga ngvilietkq gkkgkmevtl dsyygiqtrs dkaklvdayd mavfmkesrd
      301 nnylskganr sisddtatrk nkgaslreli pdylkpyler qpglintdwy ntvlrpapis
      361 qttftvtggg dkskyaftgs ylnqkgivig sdyekystnv nlstdlsdql kigvsitpsf
      421 sqgsildmvs ggrsynpiam attmypffap ydangnlnis eqikantptd aalvenpvam
      481 vdmtsrkytl fktfgnvftq ltflkdfnyr fsvggdysny eynffdpstv gsyrsaapdv
      541 tmasrteyir knylvenllt fdkkigshtf naiagqsyqe ennnqllvea tgfpdnsitn
      601 iaggssfknt lsqykwtlis yfsrlsysfd nkynfmasyr rdgssrfgvn skwgdfyals
      661 lgwtlsnenf fpkndfidpv klryskgsng nnqipnfgal slmaeenylf sgalasgyra
      721 stapnpnisw eksksdnfgi dfslfrnfln vsadyyilmr dgllldvpvp qqsgystslq
      781 nigkvrnrgl eiqlstrplh igqhleysnn lsfsvntnkv lalangqnqi iagannfavt
      841 kvggsiaemy gynitgvyts qqqidssphi tgtlvgdyim edlngdgkid nndkksfgsg
      901 ipkyilgfsn tlkyknleln fmlyselgkk vyngdlvsst esgegfgvas qyyfdhryna
      961 etnpggsfam pnmnfsnnrk eartsniffm ngdyvrlrsl klaynlpksi tenlkiksaq
     1021 iyfmgnnllt itsyrgqnid attdnvltqg ydsayypvtr vysfgmnfkf
//
LOCUS       WP_100082266             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pleomorphomonas carboxyditropha].
ACCESSION   WP_100082266
VERSION     WP_100082266.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas carboxyditropha
  ORGANISM  Pleomorphomonas carboxyditropha
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pleomorphomonas carboxyditropha"
                     /db_xref="taxon:2023338"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39486
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkepd peegrvaitp etakrfiglg atvlveagag vrslildfdy smvgavvaet
       61 aadavgdadv vltvrrpsqd ilshlkkgal aiammdpygd daaikamadt gvtafamefm
      121 pritraqvmd vlssqanlag yqavidasye ygraipmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedee fkqaetaagy akpmsaeyqa
      241 kqaalvaehi kkqdivitta lipgrpaprl vsadmvksmk pgsvivdlav erggnvagak
      301 lgevvttpeg irivghknvp griaatasql yaknlftfve tlvdkkekvl avnwddelvk
      361 ataltrdgav ihpafln
//
LOCUS       WP_100077306             888 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium camelliae].
ACCESSION   WP_100077306
VERSION     WP_100077306.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium camelliae
  ORGANISM  Chryseobacterium camelliae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Chryseobacterium camelliae"
                     /db_xref="taxon:1265445"
     Protein         1..888
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=99307
     Region          14..886
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvhaqtkdsa tkekkieevv ligygrqkkt dltgsvtais akdfnegsin speqliqgkt
       61 sgiqittngg apgsgstiri rggaslnasn dplividgvp vdnngisgaa nplalinpnd
      121 iesfsilkda saaaiygsra sngviiittk rgssgklran ystitsvytk mgnidmlsad
      181 afrqvvrdka taqyqgllgs sntnwqdqiy qtalgvdntv slsggikalp yrlslgyfnq
      241 egiirtntie rstaslnlnp kffdkhlein fnvkgtyven rfkddgaigs avvfdptqsv
      301 ydpsfsnygg ywewldpstg kpntnatknp lsmlnqrwdl syvkrvlgni qfdykfhflp
      361 elranlnvgy dysdangntt vlptaaiayy nqgsyrrysq ekknklldfy fnylktfesi
      421 rstvdltvgy syqdwqrsep faptvygtgv snpasgndff tqntiisyfg rlnytfnnky
      481 lltaslrrdg ssrfseenri gyfpsvalaw ridqenflkd sktistlklr agwgetgqqe
      541 lnlgdypyla ryilsdsgaq yqlgnqfynt yraqgydknl kwettvtknl gldfgflndr
      601 ingtidvyek eskdlisfip vpalsnltny lltnvgdmrn rgieaninvk avdtenfkwe
      661 fnvnathfrs eitnlnssqt lvntiggatg ttiqvntegy qpnsfyvyqq vydnngkpie
      721 gvyvdrngdg iintddlyry kspapdvllg fsskfnfknw dlgftmrasi gnyvynnvas
      781 qygteqaitl nnylqnihss yletgfkrtq llsdyyvena sfvrmdninl gynfprfikd
      841 sklrifgsvq nafiitkysg ldpevfngid nnlyqrprvy slgfnfqf
//
LOCUS       WP_100089378             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella alvi].
ACCESSION   WP_100089378
VERSION     WP_100089378.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella alvi
  ORGANISM  Snodgrassella alvi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Snodgrassella alvi"
                     /db_xref="taxon:1196083"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54096
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg heviiehdag kaaslsdgly heagatvada
       61 atvwqcplif kvnapntdei aamnegtilv sfimpaqqpe lleqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flhldyqeee sssgdgyakt msaayieaem
      241 klfaeqarqv diiittaaip gkpapklitr dmvdsmregs vivdlaaatg gnceytepgk
      301 iittangvki igytdmanrl agqssqlygt nlvnlakllt pnkdgelaln fedviirnmt
      361 vthegnsmyp pppiqvsaap kaapkavapt taapavqpdt akkkmiwaai avmlvlwvga
      421 vapvafldhf mvfvlscvvg yfvvwnvnhs lhtplmsvtn aisgiivlga llqigqghgf
      481 vsllafiava ivsvnifggf avtrrmlnmf rk
//
LOCUS       WP_100088963             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            parahaemolyticus].
ACCESSION   WP_100088963
VERSION     WP_100088963.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54674
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvviesqag vlasfddaay eaagakvvss
       61 devwasglil kvnapivdee kgideiallq dgatlvsfiw paqnaelmkq lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaefltv dfqedsgsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgrpap klitkemvds mkagsvivdl aaanggncey
      301 tvkdqvimtd ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvikeg eitwpappiq vsaqpqakqa qpvkkepkve eptsptkkli glvaavgafa
      421 wiasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvsflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_100093656             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingorhabdus sp. YGSMI21].
ACCESSION   WP_100093656
VERSION     WP_100093656.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. YGSMI21
  ORGANISM  Sphingorhabdus sp. YGSMI21
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Sphingorhabdus sp. YGSMI21"
                     /db_xref="taxon:2077182"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39221
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkela dgearvsasp etvkkfialg atmavekgag etaavadtdy tdmgatvgtr
       61 aavlkdadiv lavqgpdpqs lkgmkkgawl vaslnpfger ervdayaklg idalamefmp
      121 ritraqsmdi lssqsnlsgy kavilaaney grafpmmmta agtvsaarcf vmgvgvaglq
      181 aiatarrlga qvsatdvrsa tkeqiqslga kpifvesveg iegegsggya temseeyqka
      241 qaelvsshia kqdivittal ipgraaprli sdaqiatmrn gsvivdlaae qggnvegava
      301 gkvvvkhgvk ivgaqnipam maadssalfs rnlynflsay wdeeakrpvl pdddevtigi
      361 rltrdgkvvn erllg
//
LOCUS       WP_100099645             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella alvi].
ACCESSION   WP_100099645
VERSION     WP_100099645.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella alvi
  ORGANISM  Snodgrassella alvi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Snodgrassella alvi"
                     /db_xref="taxon:1196083"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54255
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg heviiehdag kaaslsdgly qeagatvada
       61 stvwqcplif kvnapnadei tamnegtilv sfimpaqqpk lleqlqekki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgai vnafdtrpev adqiesmggn flhldyqeee sssgdgyakt msaayieaem
      241 klfaeqakqv diiittaaip gkpapklitr emvdsmregs vivdlaaatg gnceytepgk
      301 iittangvki igytdmanrl agqssqlygt nlvnlarllt pnkdgelaln fedviirnmt
      361 vthegnsmyp pppiqvsaap kvapkavasa attptiqpdt tkkkiiwaai avilllwvga
      421 vapvaflnhf mvfvlscvvg yfvvwnvnha lhtplmsvtn aisgiivlga llqigqghgf
      481 vsllafiava ivsinifggf avtrrmlnmf rk
//
LOCUS       WP_100102619             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella communis].
ACCESSION   WP_100102619
VERSION     WP_100102619.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella communis
  ORGANISM  Snodgrassella communis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Snodgrassella communis"
                     /db_xref="taxon:2946699"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53979
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg heviiehdag kaaslsdgly heagatvaea
       61 atiwqcplif kvnapntdei aamnegtilv sfimpaqqpe lleqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flhldyqeee sssgdgyakt msaayieaem
      241 klfaeqarqv diiittaaip gkpapklitr dmvdsmregs vivdlaaatg gnceytepgk
      301 iittangvki igytdmanrl agqssqlyga nlvnlakllt pnhdgelaln fedviirtmt
      361 vthegnslyp pppiqvsatp kaapkaaast taapavppnt akkkliwaai avilvlwvga
      421 vapvaflnhf mvfvlscvvg yfvvwnvnha lhtplmsvtn aisgiivlga llqigqghgf
      481 vsllafiava ivsvnifggf avtrrmlnmf rk
//
LOCUS       WP_100114086             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella alvi].
ACCESSION   WP_100114086
VERSION     WP_100114086.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella alvi
  ORGANISM  Snodgrassella alvi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Snodgrassella alvi"
                     /db_xref="taxon:1196083"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54098
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg heviiehdag kaaslsdgly heagatvada
       61 atvwqcplif kvnapntdei aamnegtilv sfimpaqqpe lleqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flhldyqeee sssgdgyakt msaayieaem
      241 klfaeqarqv diiittaaip gkpapklitr dmvdsmregs vivdlaaatg gnceytepgk
      301 iittangvki igytdmanrl agqssqlygt nlvnlakllt pnkdgelaln fedviirnmt
      361 vthegnsmyp pppiqvsaap kaapkavapt taapavqtnt akkkmiwaai avmlvlwvga
      421 vapvaflnhf mvfvlscvvg yfvvwnvnhs lhtplmsvtn aisgiivlga llqigqghgf
      481 vsllafiava ivsvnifggf avtrrmlnmf rk
//
LOCUS       WP_100118006             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. G3-2].
ACCESSION   WP_100118006
VERSION     WP_100118006.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. G3-2
  ORGANISM  Limnohabitans sp. G3-2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Limnohabitans sp. G3-2"
                     /db_xref="taxon:1100711"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55266
     Region          12..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtgdhaatp qrigvpkeif pgekrvatvp davtklvklg favvveqgag dladlsdaaf
       61 veagatiapn aaalwrdsdm vfkvraptpd evalmhegqt ligflwpaqn pdlmqqlaak
      121 kvtalsidal prtlsraqkm daltsmagvs gyravvesan afgrffngqi taagkvppak
      181 vfiagagvag laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya
      241 kvmsegfqaa qremyakqar evdiiittal ipgkpapkli taemvqsmkp gsvivdmaae
      301 qggnceltep gkavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv
      361 nmeddairgl tvikngeitw papplavapk papkpaaapa akkghghgep sgpmpvgqll
      421 ivsavaavll vlvgayapaa flshftvfvl acfvgymvvw nvkpalhtpl msvtnaissi
      481 iaigalvqis pmaaagrpnt ligilaalal vltainmfgg favtqrmlam frk
//
LOCUS       WP_100115489             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella alvi].
ACCESSION   WP_100115489
VERSION     WP_100115489.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella alvi
  ORGANISM  Snodgrassella alvi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Snodgrassella alvi"
                     /db_xref="taxon:1196083"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54016
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg hevviehdag kaaslsdgly qeagatvada
       61 divwqcplif kvnapnkeei asmqsgtilv sfimpaqqse lvqqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flqldyqeee sssgdgyakt msaayieaem
      241 klfaeqakqv diiittaaip gkpapklitr emvdsmregs vivdlaaatg gnceytepgk
      301 iittangvki igytdmanrl agqssqlygt nlvnlarllt pnkdgelaln fedviirnmt
      361 vthegnsmyp pppiqvsaap kaepkvaapa pvataqptsa nkkiiwaaia vilmlwigav
      421 apvaflnhfm vfvlacvvgy fvvwnvnhal htplmsvtna isgiivvgal lqigqghgfv
      481 sllafiavai vsvnifggfa vtrrmlnmfr k
//
LOCUS       WP_100120591             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella communis].
ACCESSION   WP_100120591
VERSION     WP_100120591.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella communis
  ORGANISM  Snodgrassella communis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Snodgrassella communis"
                     /db_xref="taxon:2946699"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54186
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg heviiehdag kaaslsdgly heagatvada
       61 ttvwqcplif kvnapntdei eamnegtili sfimpaqqpe lleqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rffigqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flrldyqeee sssgdgyakt msaayieaem
      241 klfaeqarqv diiittaaip gkpapklitr emvdsmhegs vivdlaaatg gnceytepgk
      301 imttangvki igytdmanrl agqssqlygt nlvnlakllt pnhdgelaln fedviirnmt
      361 vthegnsmyp pppiqvsatp kaapkvaast taapavppnt akkkliwaai avilvlwvga
      421 vapvaflnhf mvfvlscvvg yfvvwnvnha lhtplmsvtn aisgiivlga llqigqghgf
      481 vsllafiava ivsvnifggf avtrrmlnmf rk
//
LOCUS       WP_100123614             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella alvi].
ACCESSION   WP_100123614
VERSION     WP_100123614.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella alvi
  ORGANISM  Snodgrassella alvi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Snodgrassella alvi"
                     /db_xref="taxon:1196083"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54267
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg heviiehdag kaaslsdgly qeagatvada
       61 atvwqcplif kvnapnadei temnegtilv sfimpaqqpk lleqlqekki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgai vnafdtrpev adqiesmggn flhldyqeee sssgdgyakt msaayieaem
      241 klfaeqakqv diiittaaip gkpapklitr emvdsmregs vivdlaaatg gnceytepgk
      301 iittangvki igytdmanrl agqssqlygt nlvnlarllt pnkdgelaln fedviirnmt
      361 vthegnsmyp pppiqvsaap kvapkavasa aatptiqpdt tkkkiiwaai avilllwvga
      421 vapvaflnhf mvfvlscvvg yfvvwnvnha lhtplmsvtn aisgiivlga llqigqghgf
      481 vsllafiava ivsinifggf avtrrmlnmf rk
//
LOCUS       WP_100134134             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. B9-3].
ACCESSION   WP_100134134
VERSION     WP_100134134.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. B9-3
  ORGANISM  Limnohabitans sp. B9-3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Limnohabitans sp. B9-3"
                     /db_xref="taxon:1100707"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38505
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpaeis agetrvaitp etakkliaqg havrvqsgag vaasitdday aavgvaivda
       61 aqawasdlvl kvrvpeaaea asirsgsavv gmlepfnteg lqrlatagav gfaleaaprt
      121 traqsmdvls sqaniagyka vmlgadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi eatdvrpsvk eqveslggkf idvpfetaee keaaegvggy arpmpqswld
      241 rqkievakrv aqadvvitta lipgraapvl vtadmvqamk pgsviidiaa gkgadgvggn
      301 cplteagktv ikhgvtlvge tnlpalvaad asalyarnvl dflklvinke galhidledd
      361 ivaaclvtrd gavvkk
//
LOCUS       WP_100138478             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella alvi].
ACCESSION   WP_100138478
VERSION     WP_100138478.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella alvi
  ORGANISM  Snodgrassella alvi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Snodgrassella alvi"
                     /db_xref="taxon:1196083"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54131
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvsqliklg heviiehdag kaaslsdgly heagatvada
       61 ttvwqcplif kvnapninei aamnegtilv sfimpaqqpe lleqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaeilv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flhldyqeee ssngdgyakt msaayieaem
      241 klfaeqarqv diiittaaip gkpapklitr dmvdsmregs vivdlaaatg gnceytepgk
      301 iittangvki igytdmanrl agqssqlygt nlvnlakllt pnkdgelaln fedviirnmt
      361 vthegnsmyp pppiqvsaap kaapkaaapt taapavqpdt akkkiiwaai avmlvlwvga
      421 vapvaflnhf mvfvlscvvg yfvvwnvnhs lhtplmsvtn aisgiivlga llqigqghgf
      481 vsllafiava ivsinifggf avtrrmlnmf rk
//
LOCUS       WP_100139418             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella alvi].
ACCESSION   WP_100139418
VERSION     WP_100139418.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella alvi
  ORGANISM  Snodgrassella alvi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Snodgrassella alvi"
                     /db_xref="taxon:1196083"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54072
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg heviiehdag kaaslsdgly heagatvada
       61 ttvwqcplif kvnapnkdei aamnegtilv sfimpaqqpe lleqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flrldyqeee sssgdgyakt msaayieaem
      241 klfaeqarqv diiittaaip gkpapklitr emvdsmregs vivdlaaatg gnceytepgk
      301 imttangvki igytdmanrl agqssqlyga nlvnlakllt pnhdgelaln fedviirnmt
      361 vthegnslyp pppiqvsatp kaapkaaast taapavppnt akkkliwaai avilvlwvga
      421 vapvaflnhf mvfvlscvvg yfvvwnvnha lhtplmsvtn aisgiivlga llqigqghgf
      481 vsllafiava ivsvnifggf avtrrmlnmf rk
//
LOCUS       WP_100140335             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella alvi].
ACCESSION   WP_100140335
VERSION     WP_100140335.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella alvi
  ORGANISM  Snodgrassella alvi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Snodgrassella alvi"
                     /db_xref="taxon:1196083"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53975
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg hevvvehdag kaaslsdgly seagaiitdt
       61 atvwqcplif kvnapnadei tamnegtilv sfimpaqqpe lleklqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flrldyqeee sssgdgyakt msaayiaaem
      241 elfaaqakqv diiittaaip gkpapklitr emvdsmregs vivdlaaatg gnceytepgk
      301 ivttangvki igytdmanrl agqssqlygt nlvnlarllt pnkdgelaln fedviirnmt
      361 vthagnsmyp pppiqvsaap kaaaknaapv saaapsvapd kskkkiiwaa iavilmlwig
      421 avapvaflnh fmvfvlscvv gyfvvwnvnh alhtplmsvt naisgiivvg allqigqghg
      481 fvsllafiav aivsvnifgg favtrrmlnm frk
//
LOCUS       WP_100142138             467 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella carassii].
ACCESSION   WP_100142138
VERSION     WP_100142138.1
KEYWORDS    RefSeq.
SOURCE      Shewanella carassii
  ORGANISM  Shewanella carassii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Shewanella carassii"
                     /db_xref="taxon:1987584"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51856
     Region          1..467
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvkkinqksf alsalvaasl maagafasdk teprnevykd kfknqyatwh dtaesseivd
       61 vlaedpnlvv lwagygfakd ynaprghiya vtdlrntlrt gapktaedgp mpmacwscks
      121 pdvprlieeq gedgyfsgkw akggpevvna igcgdchekg spklrlgrpf aerametlgm
      181 pfdkasrkdk qsmvcaqchv eyyfekvegr kgfvkfpwdq gttvesmeay ydaiefadwt
      241 halsktpmlk aqhpgyetwq lgvhgknnvt cvdchmpkvt sdkgrkftdh kvgnpfdrye
      301 etcaqchtqs kefmenltae rkakvkelkl kaedqivkah feaaaawkag ateaemkpil
      361 tdirhaqwrw dyaiashgva ahapdealrv lgtavdkaan arvklaqlla kkgivepval
      421 pdistkakaq aalgmdmkkm vsdkedfkkn vlpkwdaeak kreatyk
//
LOCUS       WP_100147337             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. JirII-31].
ACCESSION   WP_100147337
VERSION     WP_100147337.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. JirII-31
  ORGANISM  Limnohabitans sp. JirII-31
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Limnohabitans sp. JirII-31"
                     /db_xref="taxon:1977908"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38769
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpvett agetrvaitp etakklmaqg htvriqsgag vaasvtdaay aavgaelvda
       61 stawgcdlvl kvrgpseaet slikagstvv gmlepfnaqg lqrlasagat gfaleaaprt
      121 traqsmdvls sqaniagyka vmlaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi eatdvrpsvk eqveslgakf idvpfetqee kdaaegvggy arpmpaswle
      241 rqkvevakrv aqadvvitta lipgraapvl vtedmvkamk pgsviidiaa gkgaqgtdgn
      301 cplteagktv ikhgvtlvge tnlpalvaad ssalyarnvl dflkliinke gvlhidledd
      361 ivaaclmtrd gavvkk
//
LOCUS       WP_100150201             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella communis].
ACCESSION   WP_100150201
VERSION     WP_100150201.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella communis
  ORGANISM  Snodgrassella communis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Snodgrassella communis"
                     /db_xref="taxon:2946699"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54232
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg heviiehdag kaaslsdgly heagatvada
       61 ttvwqcplif kvnapnkdei aamnedtilv sfimpaqqpe lleqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flrldyqeee sssgdgyakt msaayieaem
      241 klfaeqarqv diiittaaip gkpapklitr emvdsmhegs vivdlaaatg gnceytkpgk
      301 iittangvki igytdmanrl agqssqlygt nlvnlakllt pnqdgelaln fedviirnmt
      361 vthegnsmyp pppiqvsatp kaapkaaast ttaapavppn takkkliwaa iavilvlwvg
      421 avapvaflnh fmvfvlscvv gyfvvwnvnh alhtplmsvt naisgiivlg allqigqghg
      481 fvsllafiav aivsvnifgg favtrrmlnm frk
//
LOCUS       WP_100162275             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudooceanicola lipolyticus].
ACCESSION   WP_100162275
VERSION     WP_100162275.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola lipolyticus
  ORGANISM  Pseudooceanicola lipolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudooceanicola lipolyticus"
                     /db_xref="taxon:2029104"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55631
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif dgenrvamtp dsalalqklg hdcviesgag ekagfmdaay eqagvkvvkt
       61 aaelwkeaev vakvrppsee elgqlhagqt lisffypgsn eelmkkaadt gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqiesmg aefvyldfee aqqdgaatgg yaapsspefr
      241 eaqlkkfrel apevdivitt alipnrpapv lwtkdmvelm kpgsvivdla aerggncelt
      301 qpdekivtdn gvtivgytdf psrmatqsst lyatnirhmm tdltpekdgv vnhnmeddvi
      361 rgatithake vtfpppppkv qaiaaqkpkd kpkeltpeek kaqeaaafka qtksqvtlla
      421 vgtvlmlllg avapasfmah fivfalacfv gfqviwnvsh alhtplmavt naisgiiilg
      481 allqigsgnw lvvvlsliav liasinivgg flvtrrmlam fqks
//
LOCUS       WP_100172394             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. 15K].
ACCESSION   WP_100172394
VERSION     WP_100172394.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. 15K
  ORGANISM  Limnohabitans sp. 15K
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Limnohabitans sp. 15K"
                     /db_xref="taxon:1100706"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55037
     Region          12..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqsgdtvvtp qrigvpkeif pgekrvatvp davtklvklg favvveqgag dladlsdaaf
       61 veagatiapn aaalwsgsdi vfkvraptsd evalmhegqt ligflwpaqn pdlmqqlaak
      121 kvtalsidal prtlsraqkm daltsmagvs gyravvesan afgrffngqi taagkvppak
      181 vfiagagvag laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya
      241 kvmsegfqaa qremyakqak ecdiiittal ipgkpapkli taamvqsmkp gsvivdmaae
      301 qggnceltep gkavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv
      361 nmeddairgl tvikdgeitw papplvvaak papkpaaapa akkghghgep sgpmpvgqll
      421 ivsavaavll vlvgayapaa flshftvfvl acfvgymvvw nvkpalhtpl msvtnaissi
      481 iaigalvqis pmaaagrpnt ligilaalal vltainmfgg favtqrmlam frk
//
LOCUS       WP_100179436             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Bradyrhizobium].
ACCESSION   WP_100179436
VERSION     WP_100179436.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39253
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfralg aeiavepgag lksglpdsef iaagatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneaa lktiadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegakpge
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 trdgavihpn fqpka
//
LOCUS       WP_100198075             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudorhodobacter sp. MZDSW-24AT].
ACCESSION   WP_100198075
VERSION     WP_100198075.1
KEYWORDS    RefSeq.
SOURCE      Pseudorhodobacter sp. MZDSW-24AT
  ORGANISM  Pseudorhodobacter sp. MZDSW-24AT
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudorhodobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Pseudorhodobacter sp. MZDSW-24AT"
                     /db_xref="taxon:2052957"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54691
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egenrvamtp esavqliklg hacvietgag akagftdaay eaagvavvpt
       61 aaalyeaadi vvkvrgpeae eakllragqt lisffwpaqn adllaqvaaq gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aivnafdvrp evaeqiesmg anfvflefda selpdgaatg gyaapsspaf
      241 aakqlakfre lapemdivit talipgrpap klwttdmvam mkpgsvivdl aaerggncdl
      301 tvpdqkivte ngvtivgytd fpsrmaaqas tlysnnirhm ladltpkkdg vvahnmeddv
      361 irgatvahag avtypppppk vaaiaaakpk ekvkeltpee rraqetaafk aqtkqqvtll
      421 avggalilaa glvappsfmq hfivfvlsvf igfqviwnvs hslhtplmav tnaissivil
      481 galiqigsss flitllaalg vlmcavnifg gflvtrrmla mfqks
//
LOCUS       WP_100200359             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces carminius].
ACCESSION   WP_100200359
VERSION     WP_100200359.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces carminius
  ORGANISM  Streptomyces carminius
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Streptomyces carminius"
                     /db_xref="taxon:2665496"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52984
     Region          13..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msvhqlahhp pqrigvvaes aseetrvaat patvrlllgl gyevvvasga geasgfadqa
       61 yldagaeigt awdadvvlkv napsdaeitr lregatvval lspaqrpgll raladagvta
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvkslggeyl pvrvaqeagt dgyaratsad
      241 ydraaaelyr eqagdvdvvi ttalipgrpa prlltagdva vmkpgsvivd maaaqggnve
      301 gtvpgrvvvt gngvtiight dlasrlpaqa sqlfgtnlan lvklltpggd grlaidfdda
      361 vqravtvvrd gevtwppppv avsavpaeqp aaapaapepe rperpgpapa grfglitlgm
      421 aavfglvafa paqlaenftv ftlavvigyy vigkvhhalh tplmsvtnai sgivvigall
      481 qighgsrivt alsfaaillt svnifggfav trrmlsmfsk g
//
LOCUS       WP_100208535            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            frigoris].
ACCESSION   WP_100208535
VERSION     WP_100208535.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium frigoris
  ORGANISM  Flavobacterium frigoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Flavobacterium frigoris"
                     /db_xref="taxon:229204"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107900
     Region          24..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknslikglm vfltilctsl tysqdvsgtv sdasgplpga silvkgttig aqtdldgkft
       61 irnvganavl vfsyiglkaq evsvagktsv kvilkedsae lqevivvgyg tvkkkdatga
      121 vdqigakdfd nvsspspaql lrgkvagvqv tqssgepggg vsvrvrgnss irsgngplyv
      181 idgvpmdggn vsagggltsn tgaqdlgtss arnplnfinq ndiesisvlk dasstaiygs
      241 rgangvivit tkkgkskepq lsysssvtfs kmsgnfgvms peqfvaaggd dkgsrsydwk
      301 dailrngfsm nhdlsfskst ensntrvslg asntdgivkn tgldkysati ynsndffgga
      361 lkveervmya slkdqttlls nsagfigsai gtalywnptl piykadgtyn vvsntylnpv
      421 qllnsyndyt ntnkflgsin ttwkinsklk ytflfgvess tsarkvellp tieilntaqa
      481 vvpgtgtdpn tnpaitkfgq avinsqnkfn ktfehtlnyn ndfsdnfnld alvgysyydy
      541 tadgfqssai gfdknqsnli dniegglqne yrvssfrnrt elqsyfarin atlydkliit
      601 atlrsdgstk lgvnnkydyf psagvaykiv enkdgivndf kirgnlgktg nqefapnsai
      661 srgayglngs lnldsnanad lkwettksyg vgadfeffnn rltgsvdyfq rdtkdlifpv
      721 paaatqpgpa sprfknlpgn linkgveval sykviekedf swdvsgnasf lknemtnfag
      781 fistgglngq glsgayaqvi tndkpiysyy myewrgydst gnsvyadaag ndtglgtaak
      841 klldkqplpk invgfntnfs yknfdlgasf ygayghyiyn nttnayffkg aflggrnvtq
      901 eaatseqaqg dpnspstkyl ekgdflrlgn ltfgytvkga ildrfkmsta rlyvnasnlf
      961 vitsysgsdp evdtdktlng vpsagmeyls yprdksvsvg lnvtf
//
LOCUS       WP_100211555            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            maritimum].
ACCESSION   WP_100211555
VERSION     WP_100211555.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum maritimum
  ORGANISM  Tenacibaculum maritimum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Tenacibaculum maritimum"
                     /db_xref="taxon:107401"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113421
     Region          25..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lflalvvqis faqektisgt vsdnsgplpg vnvlikgtsk gtetdfdgky
       61 sikttsgdvl ifrfigmktv nktvgnsnti nvtleedanv leevvvkgal gverveksig
      121 yaqqnlagde lstavesnla nslggkvsgi qitnssgsvg astrvvlrgp tsitgnnqpl
      181 yvidgipvnn qnfgnaggng gvdlpsgisd inpddiesis vlkgpnaaal ygiragngai
      241 vittkkgkkg hglginytss vmfqnplvlp nyqnsygqgs nptyfqfvdg qngvgdgvde
      301 swgapldvgl efvqftsfid grngepmpwv srpdnvkdff ntgsvithnv sfagsqedvt
      361 yrfsagtfdq egivpntdff krnlggnvnw tannkltigf nanytnsysn nvssggysan
      421 nqvqqlvwsg rnvdinalrn yqnlplagan tgaagtplnw ntqyqnnpfw aldnntntyn
      481 rdrligaanl aykisddfsi stkvsmdqfs qreerrrakg tnespngsyt eilrnyreln
      541 teilasynkd lsddfkisln aggnrmyrks nlfkgvapal qvdklwsldn laggstletd
      601 ddinaqkins iygfanfnyk dylflevtgr ndwssvlpta nnsffypsfn lsgvisdmad
      661 lgqtinylkv rggwakvgst galtpynlrp vyeittlgsi tvadintqlw nsnlnpestt
      721 slelgfetrl fnnrvsldvt yyatksedll lpgsisrgsg fnsawnnlat mtnkgielql
      781 gttaiktedf klgvdinfak nenlvtdikg dleahqlnry wgsylrareg qpygtiegrk
      841 fkrnakgqie inpatglpli skkneilgdv qpdwtggvrl sadykgikls alfdakigge
      901 vytmthawgr ysgileetin gretglvvpg vlegtntpnn lvvtakafnh gafgnnvees
      961 svfdasyvkl revvlsysip kdwientgin dlkfslvgrn lailhknaph idpetgfsan
     1021 nrdqglefgq ipsvssygfn mslkf
//
LOCUS       WP_100211549            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            maritimum].
ACCESSION   WP_100211549
VERSION     WP_100211549.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum maritimum
  ORGANISM  Tenacibaculum maritimum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Tenacibaculum maritimum"
                     /db_xref="taxon:107401"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113841
     Region          23..1019
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyivlyifl lianilfgqe tflkgmvida knkkglanvt vynistnqgt vtglggkfni
       61 svkpkeklvf nylgykehvy kithknnitv ylqqeeefld evvivakkni ndialrkatg
      121 vtanievakl ekratsnime slqgqvaglt iksdgelgkp lkirirgtst lpiktngvke
      181 edrilfdnka neplfvldgq visanafetl nvndvkeiki lkdamanaly gvkaangvie
      241 itskrgvngk ttysfslqqg itfrgnpsql mmeteeklnf erlsknpktp gyrnseeyir
      301 iknpnainin eliaqgkrrl dsikrintnw fhelsrmsmy ksynlssrgg skntrfyisg
      361 nftkqggkfd gnqierftgr snyeynvskn iyvmlnsgfg fsesttphss nysptsliyq
      421 lnpyeekekg tlisypnrtf knlinqyrks evdsrfnfsa nitatlakdl yvssiigmdy
      481 lateslaitp ptayseissg fpvkergkvs krklittnft antrvnytke fgehhislsg
      541 ntdyyknsnd figiagyglp skllsgagin nditgtrksv tssskttdav lgygvsalyv
      601 wndkvdvygs ykrdgasllp nhkrwntfwa vgagyqfskn ekgtisnlkl rgsygitasl
      661 sgitpslivp tftygangyq girelylksl fnkevvpekn tsinlgmdig lfsnintsve
      721 vyhrrtdnml ltvpiapsng fteqlknigv mdnqgvefti natpinttcf twmttaniay
      781 nknivvdlye gktlnlsgnp ypdyeegkpa dliyglvslg inaadgtpif qrkdgsilng
      841 isgkpekddf vilgyatppy tggwyhnfiy egwqvsfdly ysfggkavyt nqtkvydaad
      901 syrnlpkghl dktwftpgdd hktykslfln gnnfyetaqy antntigstn firlnnimlr
      961 yrfsdsylrk igssfiknwt myaqlkniat wssfkggdpe sanlqgssqp iftvgtnltf
//
LOCUS       WP_100211559            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            maritimum].
ACCESSION   WP_100211559
VERSION     WP_100211559.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum maritimum
  ORGANISM  Tenacibaculum maritimum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Tenacibaculum maritimum"
                     /db_xref="taxon:107401"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111587
     Region          25..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lflalivqis faqdkiisgv vsdesgplpg vtiikkgtti gvetdfdgny
       61 tinaksgdvl vfnfvgmktt qrtvkssnqi nvvmendnvl eevvilgyns kskdiltsgv
      121 stvtaqeisa vssttnitna lqgkaagvvv taangkpgeg afvrirgigs anagqeplyi
      181 vdgipvsesd lnlinssdve sisvlkdass taaygargsn gvvvmttkqg kqgakakikf
      241 ssqigfsekv kdnftmmnae qklqyereig kgtgsnlsen ewnrlvsynh dwqndllktg
      301 fiksngisis ggsekssyfv sfksesdtgi idglngfert tgrinlssel ndwldfrits
      361 gvshtfstep rdtnnvqnpf aamytynsye plynldsngn iildsngqpt ynlthsgfsi
      421 seairnnpss eeylrfigsa aldfkflenk liytpqislt yntlrsesyi qpgsvldgyi
      481 gdkkapgikt drgnssftyn flnkisynds fdevhnygit lftefynnnf rryrlsskgf
      541 pspdlntqdn saeptnassf rseetlfsta alldynynek yvlsaslrrd gssrfgdnkk
      601 ygvfwsasaa wnihkevflk anfindlklr vsygtsgndr vpgryssldt ysltsynges
      661 aaypnnvpnk dlqweskasf dlgldftlfn rrvngvinyf ntktkdlifq enlaqstgaa
      721 gnpsrfvnlg kisstgleae lngdliknen ftwnlgania fvrtivdelp ggldkhpssy
      781 pniilreger mnthflvrya gvnpkngral yydkngvite kynpndavvl kdktpspdfd
      841 gslntklsyk gislsanmyf kygnyiynnq esqhltdgns ivdnqrldaf nfwrkpgdvn
      901 vlpnpkdpln tsersdrflq dgsylrlrsi klgydlpkkw lgknsffsgv nmylqgqniw
      961 tyaphfkgdp evgfaseesv grnsvgfipg aanlnsyptv ksfllgidvt f
//
LOCUS       WP_100211815            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            maritimum].
ACCESSION   WP_100211815
VERSION     WP_100211815.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum maritimum
  ORGANISM  Tenacibaculum maritimum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Tenacibaculum maritimum"
                     /db_xref="taxon:107401"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117633
     Region          21..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkplhafill llanniysqt titgkitsnt dgaplpfvti tssktngtvs dengtyritv
       61 ppktkelifs figyatqkia lnnstvmnvt liedtenlee vvitalgvqr aakklgyaiq
      121 slksedvnsv ksvnfldnls gkiagvsitq gatgvgsssk itirgessfs nnnplfvvdg
      181 tpinnetvfn ftneaaagfq eidfgngame vnpddiasvs ilkgpsaaal ygtrasngvi
      241 viktkggkts kepqvsinss lfidtafklp kfqneygqgn sgqftytdgl gggindnity
      301 swgpkldagi lipqfdspvl lpdgtivrgg dtslysgani tptefksnpn nlkdfyktgi
      361 tsinniaian gfetgnyrls ftdlrsesii pgvnlnrqtv atklnfnlhn kttvssfisy
      421 ansnsdnrpa ngygsenvny slvawgprsl ninnlknywq pgleniqqys fnytffdnpy
      481 filhenrnsf erdrifgniq vkhqlsdqls isfrsgmdys seirqlrrsf ssnrfknggy
      541 aehtvsyrev ntdflinyqn tfanfsldis fggnrlnqta stkqsqtvnl aqpgifnlnn
      601 aaspidifqf sskkrinsly giaklgykdv lflditgrnd wssalatpfs vdgtsffyps
      661 isssfilsnt lqlpkaisfa kirasiaqvg ndtspyqtsg afisqtpvng qptfsnqnfi
      721 pnpnlkpest tsyefgadir ffndrlgvdf tyynsnttdq iislpiavss gynhqvvngg
      781 eintsgleii instpiknkn fkwntsfnfa tnraiiqnlp qangritlay sriydsanqt
      841 vwfqveeggr igdfygtgyl knengdfiid sngryiadnt lkklgnynpd ftlgwntdlt
      901 yknwnlnflf dwkqggklvs rtsalgnvgg qlaetsyrpd agiiaqgvvn tgtannpiyk
      961 pntkaisaes yyrqfydrnh eenntydasf lklrqfalsh sfnlkndrfg lknggdltls
     1021 ligrnlfsia eiphldpeql avqgnsfing vedmsyattr sigfkiglnf
//
LOCUS       WP_100221965            1093 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Anaerophaga
            thermohalophila].
ACCESSION   WP_100221965
VERSION     WP_100221965.1
KEYWORDS    RefSeq.
SOURCE      Anaerophaga thermohalophila
  ORGANISM  Anaerophaga thermohalophila
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinilabiliaceae; Anaerophaga.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Anaerophaga thermohalophila"
                     /db_xref="taxon:177400"
     Protein         1..1093
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121297
     Region          32..97
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          113..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitmvllvf cgltlsakta daqknevtvk menatildif rqieetsdyg fffkndeldl
       61 ekrysldved atleevlqkl leeggynyqi vgenvvvtrr septvmvqqq ettvsgtvtd
      121 eygnpvpgvt vtikgsttgt itdmdgnfei sdvpddatlv fsfvgmqtve kivdadvinv
      181 smqqavigld evvaigygsv kkadvtssvs sikaddfvkg svkdpgqliq gkvagltivn
      241 psgdptsnse illrgnttlv gssisplvli dgvpgdmntv apediesidv lkdgsaaaiy
      301 gtrgtngvil ittrrasghf essvevssyv nvqtisrepn lstaadfrkq ieagfrdant
      361 dlghstdwld eitrtpvshv hnvtfrggde ktnyllnvny dsaegiflks ynkdfkgrad
      421 inhnmfdnkl klnlsilgsd rklngfngyn yrqaliqnpt apvkdengew fqqltkfeye
      481 npvsnlmesn gmtrehltrf nsnivfnpvd eltlssvlsy skwnqnggys etkqhistlr
      541 dnrnayasig asesidklae ltaeysdvig nhrftalagy syqeniyttm smenwdfptd
      601 qfgyydiglg eatkngdvpn pqssyhsetn ligffgrvsy syadrylfmg slrregasql
      661 wgtdnawgtf pavsfgwrlt eepfmagqdi fddikfrvgy gvtgtqpsdl fmgvalmgyd
      721 qyiysngqwi ktlipsqnan pdlqweekhe mnygvdftll dgrmsgsidh yirkidgllf
      781 dyavpsppnl ypttranvge menkgleill tgvpiqnedf ewttsvtfst nsnklislsn
      841 diyqtssdyf ttgytgppvq tfthivkige signfygfkv igigndpdda snygqwiyeg
      901 qdgepvnysd fghsfddkkv ignglpnyya gwtnnfrykn wdlsitqrga fdfqvanmqr
      961 mmyenptytq ynllrdafnp vfgktqlksp hefnshyied gdywkidnit lgyninntgv
     1021 dflksarvyv sssntltitg ydgidpevsl vteggtsqgg ininsgagls pgidnrdkyp
     1081 tvrtftfgvn lkf
//
LOCUS       WP_100234432             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium forestalis].
ACCESSION   WP_100234432
VERSION     WP_100234432.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium forestalis
  ORGANISM  Bradyrhizobium forestalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium forestalis"
                     /db_xref="taxon:1419263"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39163
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pleprvaasp dtvkkfkalg aeiavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygneaa lkaiadagva afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpaprlvsa dmvksmkpgs vlvdlaverg gnvegakpge
      301 vvdadgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpka
//
LOCUS       WP_100242058             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter tandoii].
ACCESSION   WP_100242058
VERSION     WP_100242058.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter tandoii
  ORGANISM  Acinetobacter tandoii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter tandoii"
                     /db_xref="taxon:202954"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39903
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgehrvaatp etvkklinag htvviqrgag vnaayidsay eqvgakited
       61 aytgsqlilk vrapkgeeiq klasnttvva mfdpyrntel dqfasqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmseeeq qraadaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 qcgttittsn gvkilgipni pstvsteasa lyarnvfnfv etlfdkdknf vlnqedeiqk
      361 almvthggqv llkrg
//
LOCUS       WP_100251222             410 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium sp. UNC300MFChir4.1].
ACCESSION   WP_100251222
VERSION     WP_100251222.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. UNC300MFChir4.1
  ORGANISM  Methylobacterium sp. UNC300MFChir4.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Methylobacterium sp. UNC300MFChir4.1"
                     /db_xref="taxon:1502747"
     Protein         1..410
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42149
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd saeprvaavp etvkkfktlg advvvqsgag qkagildsey eaagasiags
       61 aadasgdadl vlkvrrpsae elpqlkrgat viaimdpygn edalkamaea gidgfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrampmmmt aagtvpaarv fvmgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsaeyqk
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 agevvtndrg vkivghvnvp grlaatsssl yarnlyafve tlidkeskal ainwddelvk
      361 atnltrdgsv vhasfqpktd gaaseaasvg lakseaskas gaatppagaq
//
LOCUS       WP_100262751            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_100262751
VERSION     WP_100262751.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115060
     Region          41..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkrlksvsm llflmgastg aayavanpgv tgvkitqqsg tctgvvkdat getvigasvv
       61 vkgttngtit gidgdfslsg vkkgdiiqis fvgyqtvevp wngqplnvtl qddtqtlqev
      121 vvtalgikre kkalgyamqe vkgdalvaar etnlanalsg kvsgvqiirs sngpagsski
      181 qlrgsnsvtg lnqplivvdg vpldnftgad nndmwnpstd mgnglsdins ediesmsvlk
      241 gasaaalygs ragngvilit tkkgtksegl gvtfsgsvsv envfmkperq tifgqgsngi
      301 fnatsssnwg paitgqsytd wngrtqnmqy fdnvanffkt gvnlteniaf sqqfdrtsvy
      361 lsatrmddfs kipgaeysrt nlmsritssf gkdnrwsvda kvqyilsdat nrpisgarsd
      421 nyfysmymmp isldirefkq aknpedgkmy wwekgsgqnp ywakdyntnq dkrnrfllng
      481 slkyqitdwl naeikagsdm yftetetkly agspssengr ysfgeqkfye nnfsflvtaq
      541 kdrvlgdfgg vftfggnlme rkstgvsnsv saltvpdlfw ltnstdsnrs isqtythrkt
      601 nslygtlgvn ydgwafldlt grndwsstls ksnrsffyps isaswvisdm innrgkgmpe
      661 wftyakarvs faqvgndldp yqlynvygig siyetggtsa svsgstlfne dvrselissw
      721 eagaevrffn nrlgldvawy ksnakrqlln lpmnslsgfs smkinagniq nsgveimlna
      781 tpvqtkeftw dtqvnfstnk nkiieladgi neytlgtydn lkilavaggn ygeiwgttyl
      841 rvtdenspyy gkmllndagl pqgdskiqki gdqqatclvg wtntfsyknf tlsflvdari
      901 ggeifsgsnr mlqangvaac tvvngkrdkf vvdgviadgn ggyspstiev epqsywtavt
      961 gstgnmgige anlydatnvr lrnvslnytf prkmlakgpf qqvklgmscn nvwmihsnlh
     1021 gidpesvfat stnatgfena ssptsrtflf nvtlgf
//
LOCUS       WP_100262965             908 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_100262965
VERSION     WP_100262965.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 908)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 908)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 908)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..908
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..907
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 yigyqtqeip vgnggkkdit lqddselmde vvvigygtqr kgdvtsavas vkaedftagk
       61 igdaaelikg kvagltiakg sgdpnaesti rlrgvislqg gstplvlvdg iegglgtvsp
      121 eniasidvlk dasaaaiygt rgangvilit tkngqresrt aanysgymsl skfgktldfy
      181 gaeeirqglt nyadkgydtd wldavsrtaf thnhnfnisg gsknttysad ftyrkeegvl
      241 letyneemrm rfdvshwmln dmlkvnfnmv ktfhkngpid aaglgiyrqa imrnptepiw
      301 nedgtfyenf avnyyynpvg iireqdgkyn sentrmtgni tfepiknwqt nlmlsrrvts
      361 dhnrgyytse yfsqksenht gyayhsqney ttdnlevtsk ynhtwnkhrf dalvgynyqy
      421 nvnegfgann ydyptdfylw nnlglgtalk dgkagmssyk ndntligffg rvsygydnky
      481 nvllsvrreg sskfgennkw atfpsvslgw tisnekfmeg ltwlnnlklr agygvtgviv
      541 gdsynsltry eygspyfydn gvwhqglsvk snpnpdlkwe tskefnigld wavlderlsg
      601 sidvyqkkts dmlydftvpt ppnlynktla nagkmrnqgi eiavnaipvr tkdfewkttv
      661 tashnankll slsndlyets nqidhaylge pinlstqrme vgrsmgqfyg mksvgvseng
      721 lwlienaktg eieeftdnml snddyrqylg nalpklylgw nnsfryknfd lsfqmtgqfg
      781 fkilnepray yennsiaynr lksvqkapyg gqytlstaqk qtfvsyyled gdflkitnit
      841 lgyniplkss kfvknirayv sadnlfcitg ydgldpemsn gdiwslgidw rdkypstrsf
      901 tfglnvsf
//
LOCUS       WP_100262968             912 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_100262968
VERSION     WP_100262968.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 912)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 912)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 912)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..912
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..911
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 yigyqtqeip vgnggkkdit mqddselmde vvvigygtqr kgdvtsaiss vksesfvkga
       61 vtdagqliqg kvaglnislp sgdptgntqi mlrgisslkg gtsplvlvdg vpgslntvap
      121 edvesidvlk dgsataiygt rgtngviiit tkqsrkemap tidyngyvsv snilnrpdfm
      181 daddlrqkwn egytfnganl kdfgantdwl geltrtavsh shnlslrggs kntnytasin
      241 ytnrqgtfik tdfeaingrm dithsmydnk ltanvstfvs qhtmprswnt yayrqalihn
      301 ptepvkdeng dwferdlyfy dnpvsyiret igemkrknir fngsltfrpi esltlkamya
      361 rrsttstdgy yqtkkhvstt ksgrngyayr ydsdfdnnli eltanfqkaf gkhnvsvlig
      421 ynyedntnsn lsmsnydfpt daysynkmea gmalkrgeas mtsyknsdkl iglftrvsyn
      481 fndryllmas lrhegsskfg kdhkwgnfpg islgwrinre nfmknvnwmd nlklrvgygv
      541 tginvadpyt slsslnynga flyngtwvka letirnnnad lrwekkhefn vgldwdvlgg
      601 rlggtvdyyi rrtkdalwdy evpvppymyp tmlanaseme nkgleilira tpiqtekftw
      661 ntnvsystns nkvvalssek fsmdqdyfyt gytgepiqtt thivqvgkpi gtfyglksvd
      721 itddglwlve nkkgehvlae etdatdwqvl gngipkhyln wnntfnffnf dlsinmrgaf
      781 gfqilnyqrm yyenakpeiq ynrlnsafdk vygktqlkdd qryvsyyved gdywkidnvt
      841 lgytfklskq hiiknlriya svlnlatitg ykgmdpevpl ssntygllda gtdnrdkypt
      901 nrtytfgvnl tf
//
LOCUS       WP_100263003            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_100263003
VERSION     WP_100263003.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115827
     Region          25..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkqclviv mtllclcvka qnlrvtgvvr dksdviigas vmvknstvgt vtdmdgrysv
       61 evpangvlif syigytpvek qvdgqtvinv tmnddvqaid evvvtaigik qqkkklgytt
      121 qqvntealdq pgtvnvgnal sgqvagltvn nptgifqaps fslrgktplm vidgvpvesd
      181 lfdvspenie sinvlkgtaa aalygsrgkd gailittkla kedgltvtag lssmvsagft
      241 vfpetqtefg sgsngqyafw dgadggisdg dmtwgprfag qkiaqwnspi rnketgetip
      301 wwgdvsgtiy ddqskyervp iawephdnlr dflrtgiitk atfsvasksk kanynfngdf
      361 snqrgqvpnt svytgglnfn smynlsnsvt lsanlsynkv yspnyprygy gpknhmytil
      421 lwmgndvngk elaehyyrpd fegtrqanyn yawynnpyfa aneltqkhdr ntmngqlkln
      481 wdvipglslq graagrlest fedmsvpksy mnygdsrngd yktwntdqld inadflatyt
      541 rafsrnftlt vnagtslyyr qirkqsqstd glivakvynl gnslnpvsat nsmnekaies
      601 vygsvnvdlf eslfltftgr ndwsstlakg nnsyfypsvs lstlvneyvk lpswmdylkv
      661 ngawaqvssd ldpyslyaty sngtlygsip svtypgtlln anilpqktts yevgvstsfl
      721 hnrigidlty yhmldensii elpissasaf tkryvngney ttngfelivs atpvknknft
      781 wnvatnwssn irkltgiygd qekfgdlkkg dradamyate wektpdgrli ldantglptq
      841 safktkvgnq spdvrfglqn tfkikdftvn idmdgaiggt listttqkmw wggkhpkstm
      901 yrqeeydngg kpvyvpegvn ivsgevtydv ngnivsdtrv ykknetavni qtwaqnypyr
      961 avvrteesel fantfsrsfl klrrvavtyd ltkfiqsqfi kgldvtvfgn nlavlkktpy
     1021 ldpdfgasdg dlqdpsaryv gvsanikf
//
LOCUS       WP_100263181            1176 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_100263181
VERSION     WP_100263181.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1176)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1176)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1176)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1176
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131960
     Region          128..1175
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msaklssknf yggnlmvkcf valviffcsv gnlfaqtetk vtinvdkvli rtalerlqke
       61 tkvhfvydee nidqdkrvsl sytqaplkiv ledfckqtsl ryevkrnlil ilpgkadrnv
      121 nrqsflmkgv vtdedgesii gatvmiggts kgtvtdingq ytlevqsgdl vsftfvgmtd
      181 kvikaqvnkk mvnvqlesna taladvvitg yqtlskerat gsfdkvdssv lssrptadls
      241 talqglvagm qatekedgsi dflirgsssl yadkkpllvv dgfpiqgdfs sinpndvesv
      301 tvlkdaaaas iwgarsangv ivvttkkgkk dkvqvdvqaf vrigtnpdle yimnqadsrt
      361 mvdyemrafe nnwkmaawey aptfskiqns ltlaqelyya nkyqglskee meqglerlrn
      421 tsnrqqlkdy lmqtqllqqy nvsisggter msnymslmye kndestikrg yekfminynn
      481 sykvtkwlta nlittlqrkd qetsgvtige fsnlspyeml lnedgsyatn lnvynraele
      541 klpleklpys dwsynmlrev rgreykttnt myrvqlglna qiikglnydm rvqyestsse
      601 yknydsedtf yarnlvnsyt eynnetqevg vsripkggvl rsgkteysny vfrnqlnynn
      661 sfaekheisa lagieisqyd tegtvnpyvy gynkekntss vppygygsnv dsfknffgns
      721 atieggntsy slrcdryvsy ytnigyvydg kygasfsarg dgsnfvsddp slrwspmwsv
      781 gakwnigkee fikdidwiny lnlratygin gnaekstspl tlvsvgssvn sttgtitgni
      841 ssfgnpslrw ektyttnigv dfdlfrskls gkldfynrks kdvigqvtip svygtstqkf
      901 nnaeilnrgv eleltgnfhi psvdlgirst vtyaynynki lklyypalyc yelveadthv
      961 egrpvgslys ydfwgtengi pyvigangdk ismndvsvhn rslgldilhy sgttipphtf
     1021 gwsnqftwnn fslyvyltgn fggifrapta gsipsvgsgk tfvsssikdf adsdgtlypt
     1081 wplkdesnfy lwdrytpnle yfvqdasfir lkeinleynl skklagklhl rgaklfvqar
     1141 nlgliycand ygydpewlpg snkpsatiaf ganinf
//
LOCUS       WP_100266094             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mariprofundus ferrinatatus].
ACCESSION   WP_100266094
VERSION     WP_100266094.1
KEYWORDS    RefSeq.
SOURCE      Mariprofundus ferrinatatus
  ORGANISM  Mariprofundus ferrinatatus
            Bacteria; Pseudomonadati; Pseudomonadota; Candidatius
            Mariprofundia; Mariprofundales; Mariprofundaceae; Mariprofundus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Mariprofundus ferrinatatus"
                     /db_xref="taxon:1921087"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39948
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mliavpaetq thekrvaatp etvgklvaag ctvvvereag haarfpdaay ekagarlvdg
       61 fraccadadl vlkvrapstv elkdiksgta vaallspftn pllkdyadag lacfcmemip
      121 risraqsmdv lssqaniagy kavllamehy grfmpmlmta agtvqpakvl ilgagvaglq
      181 aiatarrmga tvevfdvraa akeqvqslga rfvevasdqd aedsggyake mdddykrrqs
      241 elvaehvaks diiittalip gkpapvlise emvksmkpgs vivdlavemg gncplsemdq
      301 vvekygvmlv gvgnipslma tdasqlyarn mlnfiqpmld aesgrlnidm edevvaaali
      361 crdgeflkpq llgaevk
//
LOCUS       WP_100267804             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            fluvialis].
ACCESSION   WP_100267804
VERSION     WP_100267804.1
KEYWORDS    RefSeq.
SOURCE      Vibrio fluvialis
  ORGANISM  Vibrio fluvialis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Vibrio fluvialis"
                     /db_xref="taxon:676"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54481
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp tsveqliklg fevaiesqag slasfedtay eaagakvvsk
       61 ddvwqsdivl kvnapvsnee vdeisllkeg atlisfiwpa qnpelmeklt vksinvmamd
      121 cvprisraqa ldalssmani agyravveaa hefgrfftgq itaagkvppa kvfvagagva
      181 glaaigaags lgaivrafdv rpevkeqvqs mgaeflevdy kensgsgdgy akemsddfnk
      241 kaaelyaaqa kdvdiiitta lipgkpapkl vtkemvdsmk pgsvivdlaa anggnceytv
      301 kdqvfitpng vkiigytdmv grlptqssql yatnlvnllk llckekdgni dinfedvvlr
      361 gvtvvkggei twpappiqvs aqpqqqakvq pikekkveep vspikklagl vigvgafawi
      421 asvapaaflg hftvfvlacv vgyyvvwnvt hslhtplmsv tnaisgiivv gallqigqgn
      481 gavtflafia vliasinifg gftvtkrmle mfrkn
//
LOCUS       WP_100276744             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mariprofundus aestuarium].
ACCESSION   WP_100276744
VERSION     WP_100276744.1
KEYWORDS    RefSeq.
SOURCE      Mariprofundus aestuarium
  ORGANISM  Mariprofundus aestuarium
            Bacteria; Pseudomonadati; Pseudomonadota; Candidatius
            Mariprofundia; Mariprofundales; Mariprofundaceae; Mariprofundus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Mariprofundus aestuarium"
                     /db_xref="taxon:1921086"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39880
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mliavpaetq ahekrvaatp etvgkfiaag ckvvvergag hearftdaay ekagarlaes
       61 frdtcgdadl ilkvralsgv elndvssgta vaslvspftn pllqdyakag lacfamemvp
      121 risraqsmdv lssqaniagy kavllamehy grfmpmlmta agtvqpakvl ilgagvaglq
      181 aiatarrmga tvevfdvraa akeqveslga kfveveseqd aedaggyake mdddykrrqs
      241 elvakhvaks diiittalip grpapvlite emvksmkpgs vivdlavemg gncplsemdq
      301 vvekygvmlv gvgnipalma tdasqlyarn lynfiapmle aetgklqinl ddevieasli
      361 cqggellksq llgaevk
//
LOCUS       WP_100283187             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingomonas psychrotolerans].
ACCESSION   WP_100283187
VERSION     WP_100283187.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas psychrotolerans
  ORGANISM  Sphingomonas psychrotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Sphingomonas psychrotolerans"
                     /db_xref="taxon:1327635"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38325
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkeat agerrvsatp etvkkfiglg atvavetgag etasiadqgf adagatiggr
       61 sevladadiv lgvqgpdpda lpglkqgawi vaglnpfger arvdryaalg aealamelmp
      121 ritraqsmdi lssqsnlagy kavldaasey grafpmmmta agtvsaakvf vmgvgvaglq
      181 aiatarrlga qvsatdvraa treqiqslga kpifvenvkg iegegsggya temsdeykaa
      241 qaelvsshia kqdivittal ipgrpaprli sdaqiasmkp gsvivdlave aggnvegava
      301 gevaivhgvk ivghrnvpsr laadtsalfa rnlfnflsaf wdkeagkpvl ddeignairl
      361 tqggkvvher llg
//
LOCUS       WP_100286792             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_100286792
VERSION     WP_100286792.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53590
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarml
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_100289003             497 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Conservatibacter flavescens].
ACCESSION   WP_100289003
VERSION     WP_100289003.1
KEYWORDS    RefSeq.
SOURCE      Conservatibacter flavescens
  ORGANISM  Conservatibacter flavescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Conservatibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Conservatibacter flavescens"
                     /db_xref="taxon:28161"
     gene            1..497
                     /gene="nrfA"
     Protein         1..497
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=54989
     Region          8..495
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msivsgviiv nivrkslvaa savlslalis qnalaefkyt pieqevkapn pelkiesanh
       61 kfadkypkqf ktwadtskst aldsvneedp rtvvlwagya fakdykkprg hfyavtdvrn
      121 ilrtgapgvt gdaqpmacwt ckgpdvarli aewgeegyfs gkwskggaev vnsigcadch
      181 dttsqdfaeg kpalrvarph vlrafnkldk efdtmdrtdq ragvcanchv eyyfagdlkq
      241 vtfpwekgvt adaieahyde igftdwthkl skaqmlkaqh pdyetwslgi hgkngvtcid
      301 chmpkvkgad gkvftdhkig npfdafestc anchdqskek lqdivktrkk eikdvmlrle
      361 dqlvhahfea kaawdagatk eemepalvdi rhaqwrwdys aaghgghmha pdvvlhvlgt
      421 gldkaadart klarilakhg vteavkipdi staeaawkav gidieaerka kdeflrtvvp
      481 qwdkeakekg llpkdek
//
LOCUS       WP_100296834             479 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Caviibacterium pharyngocola].
ACCESSION   WP_100296834
VERSION     WP_100296834.1
KEYWORDS    RefSeq.
SOURCE      Caviibacterium pharyngocola
  ORGANISM  Caviibacterium pharyngocola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Caviibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Caviibacterium pharyngocola"
                     /db_xref="taxon:28159"
     gene            1..479
                     /gene="nrfA"
     Protein         1..479
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52990
     Region          30..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mhsaaaetka vttesgkmap tlqelakpsd vkiesnndkf aeryarqyns wketskstei
       61 vpaievdprm ivlwggyafs keynkprghf yavtdvrnil rtgapmdang gpqpmacwtc
      121 kgpdvarlia ewgeegyfng kwakggaevv nsigcadchd ttsqdfaegk palriarphv
      181 lraldaiskd fpqldktdkr aavcanchve yyfdknvtnn vvfpwfngvd vdgiekyydd
      241 iefkdwvhsv skapmlkaqh pdyetwslgi hgkngvtcid chmpkvqgad gkvytdhkig
      301 npfdafestc anchdqskek lqsivasrkh dikdvmikle dqlvrahfea kaawdagate
      361 aemkdalqai rhaqwrwdys aaghgghiha pdvllkvias gldraadara klaailvkhg
      421 vqtpvqvpdi staelawkai gidiekerad kekflkevvp qwnkealdkg lileappak
//
LOCUS       WP_100313866             796 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum aggregans].
ACCESSION   WP_100313866
VERSION     WP_100313866.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum aggregans
  ORGANISM  Thermoflavifilum aggregans
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Thermoflavifilum aggregans"
                     /db_xref="taxon:454188"
     Protein         1..796
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=87708
     Region          37..>786
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnsthcls rrvfsvalfa tllffskavf aqqshlirgq vfesngrtpl pgvtvvvkgt
       61 qsgtvtdndg ryqievspgd slefryvgyq erhirvdgqs qinvslipva sslnelvvig
      121 ygtvkkkdlt gsvsvvnmkd aeknptydva rmlqgqvagi svhgsgepgg yvqiklrgit
      181 tfgnnsplfv vdgvpvdapf dfstddiesi qvlkdasaaa iygaraatgv iiittkkgkp
      241 gplkvsydgy ygwqripkyi pvtdrvgyqk ittaaelnag ltiapandps npkyisnint
      301 dwqkaalktg iiqdhhinls ggseninydl glsyfdqtgi qvgpqkydry tlnanfgghk
      361 grfnygakla ytqshkgnya atqghavfgg tvtamltaip tvpvydstrl ggyggsdaal
      421 qraisanvvg innlvhdysd rnrafgniwg eleiipnlky klnlsydrtd yknyhfepkf
      481 dmgyyyinnt fylseqlgna ntglventlt yhlqtgkhqf dflagmtyqe dhnqwmlgta
      541 qdttnlqfqt fsavsnpaak glssyleast llsylgriny nfadrylftv nfrrdgssrf
      601 spahrygdfa gfaaawnisn ekfiqlpkli sslklrgsyg elgnqnfgny lyqsyidnsv
      661 nydfndqlai gattvsvadp slkwestivs dvgidaglfn ealtftieyf nreskdiitn
      721 ipipysvgsf pqtvttnaas lrntgleltf tyhkttgqlh yditfngstl snkvlkleeq
      781 tipfmvmqvk pklvil
//
LOCUS       WP_100314282             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thermoflavifilum aggregans].
ACCESSION   WP_100314282
VERSION     WP_100314282.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum aggregans
  ORGANISM  Thermoflavifilum aggregans
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Thermoflavifilum aggregans"
                     /db_xref="taxon:454188"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40479
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvigickepe genrvsclpd vvrqlvqlgq evwivsgage rayasdadyk avgahladek
       61 evcqradmlc rmhfpeddal iaearektiw vgmyqplyha aemqkmanrg mtvcsldaip
      121 rttraqsmdv lssqaniagy kavilaaahy phyfpmlmta agsiqpakvl vlgagvaglq
      181 aiatarrlga vveafdtrpa vkeevmslga kfievegaad psaaggyave qsadyqrrqk
      241 ekiaatiaka divittaqip gkrapllvtr emvesmrags vivdlaastg gnteltrnge
      301 tivhhgvtii gnsnlpstvp adasklygrn llhflqllis kdgrlqfnfe ddivsaacvv
      361 yegkirdtri lqtvqqa
//
LOCUS       WP_100314510            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum aggregans].
ACCESSION   WP_100314510
VERSION     WP_100314510.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum aggregans
  ORGANISM  Thermoflavifilum aggregans
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Thermoflavifilum aggregans"
                     /db_xref="taxon:454188"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114320
     Region          29..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskalpirvl wlsflcvims ftsslaqekm vsgqvlapdg splvgvtvkv kgtnrgtttd
       61 vngrfqlsta pgetlqfsfi gytpqevkvd dqsafrvtlq ptrsqlnevv vtalgqqqqe
      121 rtlgyavqki sgadienthr tdfvealqgr vagltvstts gmpgasdaiq lrginsigls
      181 nsplfivdgv pvdnstfsta sltsinqsav dyanrrfdft nriadlnpnd iesitvlkgp
      241 eatalygida tsgaivittk sgkagkptvd yngtltttkl yrfpevqrvy drgfngvfdp
      301 ssvsyfgpri pagtqfydni hhffrtgirq thdlsfsggn nqityrlsss ylddqgvvpn
      361 tdykrinval rvnarisnkl stdasisyiq adntkaekgp tsfllglylw ppymdvrdyl
      421 npdgskklvy pnhtpdqeyd npffsvnknh fydktrrvig nfgitydplr wlsisgrlgn
      481 dayttngmiy ynanstfayq fkgridqyts ivqnlytqll vkasydfgqw htslllgnav
      541 ynnsnhteaq sgqnflvndf vslnianplt isnltslvrk rligvfgefn lgykeifhlq
      601 ltgrndwtst lpigrnhffy psanlsfaft eipalaglkq visfgklras vaqvgkdapp
      661 yqiypgllpq tttgggfafn fngpnpylrp eqttsysyga hlefynsrli ldgeyyktks
      721 ihqivplvrk syapgfvlyt inggsltnhg leltltatpv qtsalrwdit vnyafnrskl
      781 lslpsgvtef ynsdtwlygn lrngmkvggp lttftgatwm rnnngdilin plngyplkdn
      841 sfqvvgdrnp kytggvnnsf ewkgftlsfl fdfrrggdvf natalqlyrl glstatlnre
      901 tpvvvkgvlk dgmensskpt pntiqitpmy nsnyfsnvsv esdfveknin wirlrdvylm
      961 ydipkkwlgr qhtiqalsvs isssnlfmit nysgqdpdvn gttpatlgsg gagidynvvg
     1021 kprvfnftln arf
//
LOCUS       WP_100314870            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum aggregans].
ACCESSION   WP_100314870
VERSION     WP_100314870.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum aggregans
  ORGANISM  Thermoflavifilum aggregans
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Thermoflavifilum aggregans"
                     /db_xref="taxon:454188"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118701
     Region          23..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvllflta llfstvwafg qqrtitgkvi sqdgnpipfa tvqikgttsg tttnqngsft
       61 ievpadavlh issigyeaqd vqvgaqnqlv irllptaqnl keivvtalgi ernknelpya
      121 aqqvsgdqvt ntrsdnflsa lsgkvaglqi ksnnnlggst divlrgyksi tgnnqalivi
      181 dgvpvdnsnf nsssqrngfa gydygntgtd inpddiasin vlkgaaatal ygsraangvv
      241 littkkgkkg lgitfnigga tasmdkstwp kyqheygagy fdpdyytysd appspdphfl
      301 yemvngqyal vvpttedasf gakfdpsllv yqwdafdpss pnygkptpwv aakndpttff
      361 etpysyntsv fvqggddrqt fklgytrtgd kgilpnshlt kdmvdfssty nitpklkata
      421 sinytkenai grygsgyday npatnfreww emnvdikeqk aayfrtlkni twnmtdpvgg
      481 nigpiywdnq yfvryqnyet dsrnryfgyl mlnydptswl slmgrvsldq yaglqeergn
      541 vgsvnvpyys rynnnfkefn ydflanfnkd itsslnfkal lganlrrtyf nsiyastngg
      601 lvipglyals nslnpinaps etaeqievgg vfggitltyk nflildatar qdqsstlpan
      661 knkyfypsis ggfifsqllk nvtwlsfgkl rlnyaevgnd apwafisdvy dkptpygsva
      721 lfsvpnrknn aelkpertks yegginlgfi nnrigvdvty fktntinqii nisipaetgy
      781 tskvinagnv enkgwevtln lvpvktndfs wnldlnwary rnkvislysg vkniqlgafq
      841 ggvtlnateg qpfgvlkgkd fvylngrpvv ksngyyqits stdnvignin pdwtggvsnt
      901 ftyknfrlnf lidikqggdl fsidqwygqg tglyiesval nangksirdp vdqgggyifp
      961 gvtadgkent tyaaitglrg fgylnmpnka yiydasyikl revnltyslp esvvshmhpf
     1021 ktidisvygh nlwiihknlp yadpeegpss gniqgfqvgs yptyrmygcn lkftf
//
LOCUS       WP_100314875            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum aggregans].
ACCESSION   WP_100314875
VERSION     WP_100314875.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum aggregans
  ORGANISM  Thermoflavifilum aggregans
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Thermoflavifilum aggregans"
                     /db_xref="taxon:454188"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119355
     Region          23..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvllflta llfstvwafg qqrtitgkvv dqngnpipya tvqiqgtnqg tttdqqgnft
       61 ieapanavlh isyigyqakd vpvnnqshlq vtlqstaqal nevvvtalgv qrearslgys
      121 vgevnnqdln vskpinvaqg lvgrlagvqv stlnngvnpt vrvqlrgerh iysdnqalvv
      181 idgvevnpnq latlnpediq svsvlkgasa aalygaeatn gvlivttkrg aeggkpiinf
      241 sstvtlekis yfpklqdqfs gyggetgtfn lgpgkenwpa inpytgfany ipfenqqygp
      301 pfdgnpqngf iggansqgqy flvpfrpikp dqriaffntg vttqnnisys ggdqknsyli
      361 slqdvnikgv vpkdqarrtt arfngvktyg kftaqynlsy srqtsdvagn dftqsnghyn
      421 apgsvdplgr fgsggwpvyw nilntpanip itslknwqdt ssfasinnyy nayytnpywq
      481 idqsrlqnka dnfqadlsas lqatswlnil yrvglvtnns yqhdfrypvq fsaysstdpw
      541 gagnyqsggp vagsvwdgnd ytrrlqqdvl ltftkkigdy sgtlivgnti wdhyrhyqge
      601 gsanlylpgm fnidyrqgea dveefiseer rigtfgdltl gyknglflhg nfrrdyssll
      661 vkghnaynvw dvdaswvftd fipsikgnil sygkiraays ntgqitvppy siqpafnvtg
      721 gypygsvasl slsstynnpn ivpentieke vglelgfwnd rinveadyyr dnnrnqtlpv
      781 nlssstgyts afinagevlt wgwefdvkvn piirtpsgfr wdaganlsin dskvlsligs
      841 vqdfnmglnn havvgqplpv meltdlqrdp eghvvidpst gypildntpk ivgrttpkyi
      901 lglntdlkyk nftltiigdy rggygfysna gqnldftgas ahtaqngrqs fifpnsvyqd
      961 pttgkyvpnt niyvydgsig fwvysdyrra gttywlnaaa wkvrtislsy dfsqfiqrtk
     1021 fihgasfsll andvlmfrpk qnvwtdpefn ytnsnsfgyt tfyelpptrk fsavlnltf
//
LOCUS       WP_100314877            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum aggregans].
ACCESSION   WP_100314877
VERSION     WP_100314877.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum aggregans
  ORGANISM  Thermoflavifilum aggregans
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Thermoflavifilum aggregans"
                     /db_xref="taxon:454188"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118606
     Region          23..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvllflta llfstvwafg qqrtitgkvv dqngnpipya tvqiqgtnqg tttdqqgnft
       61 ieapanavlr isslgytprn vqvgnqsslt iqlsgsaaql selvvtalgi qrekralgys
      121 vqdvnseqlt vnhptnplne lsgkvsglqi isasgapgsa vrvqlrgats ilgdnqplfv
      181 idgipvdnse nltandgggt agvgeanrll dlnpddiesi svlkgpaaaa lygsqasnga
      241 iiittkkggp lgrktfhvty slaftddqvn klperqnkfa qgifgmylgp dassglrays
      301 fgplmdtmvy dgdhtylwds hgrlvgksqn pngqkaivyd pykffqhglg lvhnlafsgs
      361 dkdisyrvsl shsdqggvip lsrfkktgis lntdyrftpq fsissavtyv ydfanrpqqg
      421 snlngvmlgl lrtppsfdns agvtdptdpr aymlqdgsgr qrsyrgtggy dnpywtvnmn
      481 pftdktnrvf gnitanynpf qwltiterfg gdyyvenqhq iyskgssgan aagmvfedqv
      541 tnqiinndlf atahkkfgsd fdasfmignn ifdtrykrlh lqgnglnfne fqginntqsq
      601 tlslgqsevr ryafysrlsg gykdylfldl tgrletsstl ptnhntyfyp sanlsfiftq
      661 algihsnvls fgklrasfaq vgkdldpysl qtywvrasag dgwtngitfp fngltgfqks
      721 tvlgnnnlka ektsqyevgt elhfwgdrvn idytyyhyks snllnqvsia nssgygaiyl
      781 naadmenngh evtvdlipvk vkdftwdlvv nwatnqnkvl klgpgidrld fngfagifvs
      841 alvgkpygii ygtgyvhqvp gdvkspliid dqgspgdgqy glpiiandle ylgnpnpkwt
      901 gsigntftwk gfslyvlfea rqkyqmwngt wgamtnfgvs kntenrytqy vfpgiqghld
      961 nngnvittgk pndisvtlde nyytgvgsgf avnepyvqda swvrlreasl gytfdghklf
     1021 kqahppfesi tvsvvgrnlw lhtkytgvdp etslfgsqva qgfdyfnnpg vktwgvnlnv
     1081 rf
//
LOCUS       WP_100314879             696 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Thermoflavifilum aggregans].
ACCESSION   WP_100314879
VERSION     WP_100314879.1
KEYWORDS    RefSeq.
SOURCE      Thermoflavifilum aggregans
  ORGANISM  Thermoflavifilum aggregans
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Thermoflavifilum.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Thermoflavifilum aggregans"
                     /db_xref="taxon:454188"
     Protein         1..696
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=79154
     Region          <2..695
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdvvtrtghq qqynisasgg terttfylsg glfkqqaati gsdltrystd fslnnrvsek
       61 isfginanis dvdqhtpyag gafrnpllaa yfllpnakat dsngipdtsa snlitglfnp
      121 lainefdrnn fnalrilsnf sgdynilknl rysmrfgiey dniremrywn pfygdgknyq
      181 glgsqnitni fnwvwtntln yryyfqpnty fnilvgyesq lnqfkvtdle nrifpynlnl
      241 yvlavgakpt tasnnaadfa iasafsraef nyqnryvvsg sfrrdgssrf gankrfgdfy
      301 svgfswnadq ekffqqgsls slistlkfri sygengnadf gnyvwrelya fnsnfsynqv
      361 gggapntpgn pnltweknkp fdvglnlgiw snrlnidfdw ynrkttgllf nvpvsytsgf
      421 gsypdnigsl qnrgielsvd aqpvrsaftw digfnlslnk nkiltlpnhq gfvngsfyek
      481 egydiqtwyv rkyagvdpqt gnarwyydpn qykdslttsy skaqrilfgs aspkgfgsvf
      541 ttlsykgikl yaqfyyqwgn yvrdvwaryt qgdgfgafyn ktkkelqrwq kpgditdvpk
      601 yvynnptssy efstrflykg dyvrlreiql sydfspnllq klyvhaltiy lrgenlltwv
      661 kdknlvydpd aagitgqlnl tvptiktvsa ginlgf
//
LOCUS       WP_100336214            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            chitinivorans].
ACCESSION   WP_100336214
VERSION     WP_100336214.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter chitinivorans
  ORGANISM  Hymenobacter chitinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Hymenobacter chitinivorans"
                     /db_xref="taxon:89969"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109372
     Region          26..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkftwltfl lllslpglgl aqtqpvtgkv tdakggslpg vtvivrgtqq gtstdasgvy
       61 siaaadtatl vfssigftpq tiavrsrrvi dvtlsenaqq lgevvvtaln varerktlgy
      121 svtevkgetl tqarennvan slvgkvagln vnstsggags ssnviirgvs slnqtnqply
      181 vingvpvesq psiantggqy dnspdlgdai sninpddies isvlkgaaas alygyrakag
      241 vilittksak nnegiefnsn yvaeriynlt dwqyeygqga nnikpttaag aaqvgnsswg
      301 grldgsnvvq fdgtlrpyva qrdnlqnfyr tgsswtntla fskaftggsv rlsasnltnk
      361 avvpnsglgr qtfnfvgtfd pfkhltidar anyileqadn rpiladgagn anfnvtflpt
      421 sldvrslepa vnadrtelqy ntgnpyntnp yfaaykfvnn trrerllssv saryafengl
      481 flqgrvgrdg ytdrftsvtp sgtaylptgk itelttqftd lnvdgllgkt fevggdfaft
      541 pnlgasyrrt kseafqnigs dlavfgvntl gnaknksaqs ffsdqevhsa ygslemayre
      601 llfvtatvrr dwfstlatpg kdnklynttp gvsasfvfse lvkpeflsfg kiragysevs
      661 qatlpfqtql syaflptsln glplgtispd nvnipntglr psrateievg telafvqnrv
      721 rldltfykkn skdeivfapa sissgyqgav lnsgemenkg vemlltvqpi rttdfswtss
      781 fnaaynkntv lslaagqqqs vyatsrsgvg fvgqivgqpy gqvlaydyky npdgsiattp
      841 ngvpargelk sfgtafhpwt egwsndfvyk rlslgvlidg kfggkifsat dyygtlfglh
      901 krtlenregt fgsdkidaat yystlannvs kdfvqnadfi klrqvtlgys fpsalfgnhi
      961 qrltlslvar nlaflkrktd nidpegnyna faqglelggv ppvrtfglnl sarf
//
LOCUS       WP_100338848            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            chitinivorans].
ACCESSION   WP_100338848
VERSION     WP_100338848.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter chitinivorans
  ORGANISM  Hymenobacter chitinivorans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Hymenobacter chitinivorans"
                     /db_xref="taxon:89969"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116159
     Region          24..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllllslf lsltligsaw aqnrvisgrv ldvttneglp gvsvlvkgts vgtatnaegt
       61 ytlsvpadat tlifkqlgyg sqeraitnsn tidvtlsvnt eelsevvvta lgvsrekral
      121 gyaiaeikpd qlvqksepda lralagkvtg vsvtsasstp ggstriiirg ntsltrtngp
      181 lfiidgvpfd nrqfdsddvl vegtvnsnra ididpnnies qtilkggaaa alygsraagg
      241 viiittktgs sargakgiql gytssfslek vaglpdyqns ygtganfvgp fttngswgpr
      301 fgspeapvsi phpqagnanf pnipagttip yqaapnnvkd ffdtgrqfdn sitltgnsdn
      361 akfaavlsrs dntgiipnss fvrnnvsagg sgfynkftig gnvtytnsdq rgpliggssa
      421 qggssalsrl mfmprnldlq nlpntdpitn gsvfgwlstq adnpiwsttn nsytsrvdri
      481 assitgsyai kewltlayrg glntytdsrr stirpgntgk ygtgrivedh lqnteleqtv
      541 sltfdknlte dislralign qinqrqfeaa sflgtgiiif gidnlgntta vqpygpqfqk
      601 krlmgllsea tlgykdwafl tgklrrdqss tlnkngeign tgrgyfyyav egswvfseal
      661 kldlpwfssg kvranysrvg ndadpysagl tryinnpryg nnvgttdfpf ggvpalalss
      721 qignpaltpe ftnewefgad lnflknrlii ntsvydrrtt nqigevtlps atgygvlltn
      781 fgeisnkgie laatvipvdl rgfrwtstfn fthnknmves ltdgldllvi epgfgsgliq
      841 pilqpgqpyg alygsnadrd dqgnllidps tgrlipalnp kilgnpnpqf qmgfinqfty
      901 kgltlntlid yrkggsiyst tlqqelgrgv trdtedrerl vvikgvkgdp nthqplrdad
      961 gntipnntai sindyyfgvg saalsgtaeq slydattvrl reitlgydlp ksllqktpfg
     1021 sinvslsgrn lwwyspnipk ytnfdpetst ynsgsnvqgi eytnspsvrr yginlrvnf
//
LOCUS       WP_100339586             949 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter auburnensis].
ACCESSION   WP_100339586
VERSION     WP_100339586.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter auburnensis
  ORGANISM  Mucilaginibacter auburnensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Mucilaginibacter auburnensis"
                     /db_xref="taxon:1457233"
     Protein         1..949
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104216
     Region          25..945
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknirncca llivllsgfa tayaqektds lvnvafrtva kkdlivpaas vditeilkks
       61 ystnsldnlg sfiagytgnv wgqaplvlvd giprrasdir mtevqsisvl kgasavvlyg
      121 ssaakgvvmi ttkrgsikpl qidvrantgi yvpksypnyl naadyktlyn ealandgiap
      181 aytadeinat ragtnpyrya didffgsdyl kkfynksdvt mevsggneaa ryytnfglsy
      241 nndllkygeq knnnslqfni rgnvdvklsk rlsatidaaa vsansyvgkg nfwgatstia
      301 pnfnkfspli pismldpnnp alqtivknsn hvidgkyllg gqstnqtnvl sdmlaagydr
      361 tksntfmynl gfnadlgavl qglsfkttts ldytslytes yslpyatyrp twstvngqdi
      421 itdlqkfgvd rnstnesvgt ssytqtvslk aqfgydrtfn ndhnvnaall gwgyttqfss
      481 dggsgyqpvk ntnlgfqagy nykrryyldf sgavlhsakl ppgkrngfsp tvsagwrise
      541 enfikdnlpf isdlklrssy ssvkqdldvt gtrpgttgav dqflyqgyys nnatlggfyt
      601 wrdglaggrt tlvgqadnpn ltfvqrnefs vgldaalfnn kitldlnyfs qitdgllarg
      661 tsiypsyfag sgdfrpwiny nkekrtgfdf avnlnekvge vqfslgvtgm vfnskvlrrd
      721 elpaepylar tglpidanfg yiaegffqsq adiansarqt fggtsvmpgd ikyrdvnkdg
      781 vidakdqvnl ghsgsgvspf sygvnltvkw krltmfvlgs gvsgavgyks npyywvagng
      841 kysdivlgrw tdatkataty prltttsgsn nlqnstfwmy ninrfnlsrv qftydfndkl
      901 fnksfvhnls vyvqgdnllv iskerkfmet nvgsapqtrf fnigvrgsf
//
LOCUS       WP_100339763            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter auburnensis].
ACCESSION   WP_100339763
VERSION     WP_100339763.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter auburnensis
  ORGANISM  Mucilaginibacter auburnensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Mucilaginibacter auburnensis"
                     /db_xref="taxon:1457233"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114999
     Region          24..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllvslc flmlfltqaf aqnrtitgtv takddglpip gvtvkikgtt ngvptdasgk
       61 ysisaptgav lqfsfvafqt kevtvggqsv lnvilesdnk llsevvvtal gierqkrelg
      121 yasavvknea inagsavnla nglqgkvsgl nitttnsgvf envkinlrgi rsltgnnnpl
      181 llvdgvqtdi nylssinpnd iedvniikgs sgagiygsda rngviivttk kgsktgapvv
      241 tvsnstqfqs vsffpsfqnq fglggggnaa glggydpien wswgprydga mtqigpdldg
      301 ivdpvfgalt tqkikyspnn srkeffktgt ivqndvsyse knfflslqda ltngivpndk
      361 nrrsgfrlnv akeygrlkvg vntnyvqnny nlfdqegmsd ynvtqnvgln qglmnllfnt
      421 ngfvnlqdyk dyknnpyasy nyyftnygln pyfaidnwrk egkkqdlkad lnldfkvadw
      481 lnltyrgslt sttlverrks rgenanafgh dergfglipg aveeraytqq rmsselfasf
      541 nkqinedfkv taiagtyvrq ddgrdtrvga tvlnvkdlyn igqrageltg sspmrrsrlf
      601 avygsagvgy kgwanievta rnektsvlae glnsyfypgv tgsvilsdai dglknnnvls
      661 ylklrggwnk tgnsdiapyq laatfdqggg fpygstagys agnttynpal kpefiqatev
      721 gleagflnsr inveltafnq kmtdqiipia vssgtgytqa yvnaasfrnr glemdlkltp
      781 lvnlgqvhvn faanatynes vvtsvypgld qvfiggytaa gnyaikdypa fmiratdynr
      841 dpatgkvivs altgaptaat ntviygqtlp kwvvglnpsv rwkslnlsal feykgghqay
      901 adigdamswt gvsdlsatns rerfifpnsv yqavaggpyi pntsvtlnsp egfwtgvgrs
      961 vksnylisaa swrfrelsis ydlpvaavfg stktvkalsv altarnlvlw lpknnkyqdp
     1021 dftfsgastg fgtggttgvt tgnqagisns tinppvrtig gnitvtf
//
LOCUS       WP_100340502            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter auburnensis].
ACCESSION   WP_100340502
VERSION     WP_100340502.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter auburnensis
  ORGANISM  Mucilaginibacter auburnensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Mucilaginibacter auburnensis"
                     /db_xref="taxon:1457233"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119912
     Region          59..1110
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrrgtpsy nsivtgvfav llcassaqae nntnsnaaal gplaklaaan vlvkpvpakt
       61 vtgkvvdskg ealigvsiae qgttkgvvtd adgnysisve gnnsilvfty igyetqsqtv
      121 gartvinvtl qnkssnleev vvtalgikre skklgyaatt anveeiqqnr ttnvmssleg
      181 kvaglnispp aagpgsstri rlrgqaafng atnsplivvn glpmdqgeqs vgpnnttdrg
      241 dalqqinqdd iesftvlkgs taaalygsra angaiiittk sgakntkfgv eftsnfaadq
      301 vldynryqmi ygngvwdatk lsgrkpasqg esvtygaqtw gakydgspvt yfdgstgtys
      361 pnpnriteyy rtgtsfnnal alsggnasts frlsysnqda kgispvndyh kkianlglns
      421 kitekltltf nlnytnevnn nppqvgfqga gapnflyrms paiplrlfrd savnpatlse
      481 aqtsgfqttl lnpyysnprq flvrkadrfl stttarydff kflylqgrva fdynsalneg
      541 ntphgvgasn llqngtgpay sgsynvntnw qrnmnydfll gtnnqrfgdf saeltlggni
      601 rddrgsgvra stanglivkd lysiengvqk nvnydfnrqq vnslygvadf gyksflylti
      661 tdrvdwfsvl tppsfiisnp knsvnypsvs gsfvfsellp nvkwlnygkl rasyartgsa
      721 gginnfssql gyslnanpft angysytlgn fnanypnpfv tpfdviekei glevktlnsr
      781 lnfdvavyhk ssqnqilntp lsaasgfttr pvnignlrnk gievlidgtp iktanftwnt
      841 smnaaynesl vlkladgqtt qvvnafnang neflgklsyv vgmamnqlqs ptylrnaagq
      901 ilvtkdgall atkydvnfgq adpkwtggwn ntfrykrlsl lvhidykfgg kmfsstalng
      961 lrqgltqasl vgreggvkfp giiydptggp ggtpgptngt nnadravgvv pstfyadyrt
     1021 lqiadpfvfk sdfvklrnit vsydfsdmlk nvkyikgisv safvrnvail hkdvpdidpe
     1081 amastgdsrl gyeqstiptt rtfglnlnvk f
//
LOCUS       WP_100341228            1214 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter auburnensis].
ACCESSION   WP_100341228
VERSION     WP_100341228.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter auburnensis
  ORGANISM  Mucilaginibacter auburnensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1214)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1214)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1214)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1214
                     /organism="Mucilaginibacter auburnensis"
                     /db_xref="taxon:1457233"
     Protein         1..1214
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134011
     Region          126..1213
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrntftkltr clllflclgc cynayaqngn srisltdaik svqtrfktql ayehglldnk
       61 fttandlkgs qaeealknil ypnnliflyv sennytivar nasffnsgtp avsvtvnktg
      121 gvathtvrgn itgdngeplp fvnvwvkgtn qatrsdddgg fllpavnstd visfsmmgye
      181 trelvagndi klnvslranq tmlnevsivs ngyqtisker atgaafslsa keieehpqnn
      241 iiqrlegltp gmqinlssgd rgffyqsggs iatvqganst trtvgtndyg vtirgkntlq
      301 geqsplvvld gaiteldmst lnpsdienit vlkdaaaasi wgvragngvi vittkkgkrn
      361 skptvnfntl ltfgekpdlg yfrtmtsaqq layekeladr sllpapnpsn yfnalsyysp
      421 gtnlafalka gtitqaqyaa qasalsaidn rdqiskyllq gaksqqynls inggsennty
      481 fyslsyskes pyevrnygsr ltatmnnswk lfnwatlsts fkgsffnlvn ngislntlyn
      541 ptqstlmpyq qladangngi yfdrlnpaft stlssvykdw rynyldelal gdntqktsny
      601 afnvnlkvpl feglsasaly ttersfnfnr qfydpatfym rdalnyytyp tatgnslnit
      661 nggalqqsnt nqnnyslrgq ldfdrtfnkr hqltaiagte iretnigqnt stlwgynmat
      721 gitntninfn tssptyayia glsptayttf nkggyptqvd kqrrflsyys naaytldnky
      781 ilsasvrydd ynnfgldrky ratplwsaga kwhisrenfl kdvkwidqla iratygvngn
      841 lslntypfty islgsndgvt gqssaniial anpqlrwekt ivknlgidfs lfksrlngsf
      901 evfdkngkdl vysfpissvy qgnispqltr naatltgwgv easlngvivr ktdfswsagl
      961 sfayntnkit dgrfneaaya snlgtspssi syisgypsdk lfvyrnagld asgmtqiydr
     1021 ngdivksstv tltslsdlky agrttapyfg gfntnvrykq fslfaqfsyq fgnvflkpsi
     1081 qnyisssttl rydlsadiak rwmqpgdean tvvpglaggs atqisliryq nsdinvlkgd
     1141 yirmrqltfa yqipnavlnr fkirgaqvgi tannlgliwr ankegydpdf anyvgslrgl
     1201 paarsytlnl nlnf
//
LOCUS       WP_100341599            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter auburnensis].
ACCESSION   WP_100341599
VERSION     WP_100341599.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter auburnensis
  ORGANISM  Mucilaginibacter auburnensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Mucilaginibacter auburnensis"
                     /db_xref="taxon:1457233"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112414
     Region          34..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkifkvnill hlvlalfclk lkaqqtkqge lnarvqnskg epvqgasvis lgneitntdk
       61 egafsiittp gkrlvitalg yqsltidadt tlklitlkse adqvqvafqk qdrseilggv
      121 snfnvaemle knyymstsdy lssflpgyng tngnvwgsgt ltmvdgvprd ignvlpteid
      181 qitllkgaqa valygsqasr gvlivttkrg tsgqdafkvr fnagvftprg ypdyvgaaey
      241 mtlynearrn dgagtlyddv tinntasgkn lfrypdvnyy sseflkksvn radvtaefrg
      301 gnekarfyan mgfyqqgsll nvgtgkdegv srfnvrgnld ikfnkaitgk inaslayydt
      361 ktakgnywgn aatlrpnwya pliplsaven pndpkwqtfk dspflvdgqy lvggrqdmtt
      421 tpfgalytqg lekyssrqfq fdaglnfdlg salkgltfnt vfgldyynrf ylsenindys
      481 vqvatwnand kitniqrygl vdkasrgrsl tdayqrlvtf ysgqfnyknt fnkvhnvsgl
      541 llvnaflrqi sevyhgdgna nlgfqagyny dqkyyvdfts nyvhsakles qnsnafspvv
      601 tvgwrmskek flakssvvnd lrltatagil htdmdfteyf lfrsaygngd afrfnegrqs
      661 ngtnvlrgan anlvfvqrke lnfgvdatlf nrllqvnasy yriemnglpl knanaypnyf
      721 vfgstnfipa ienynnnlyt gfdfgasink rvgqvglnvg ltgtyinnka lkrrevyeak
      781 wsylsrvgqp vdgiwglqsd gffmnqaqin aspsqtgiag sslragdlky vdqngdgkid
      841 nndivylars tpsfilglni takwknftlf mllngatggk gnktndyfrv rqerkyseyv
      901 rdrtiinkdv sgnwevtqlg ayprltttag dnnfrdsdfw lydnsyinls kvqlsydfpt
      961 gvikskivkn lgvyvsgfdl ltisknrkil qtnigaapql tffnlgvkat l
//
LOCUS       WP_100341700            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter auburnensis].
ACCESSION   WP_100341700
VERSION     WP_100341700.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter auburnensis
  ORGANISM  Mucilaginibacter auburnensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Mucilaginibacter auburnensis"
                     /db_xref="taxon:1457233"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115825
     Region          30..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnftflrqf mllpvlllcc lsafsqatri tgrvtdtkgq alpgvtvtlk gttaatstnv
       61 sgnytfnapr qltkndvllf nsigfqtrei afngqkeidl qltednqsls evvvtalgik
      121 reekslgyaa qtiksnaved aktnnwvnsl sgkvaglniq gtgsgpmgss ritlrgensl
      181 nldnnqaliv idgvpvsski tgtgykahla tdspvdfgsd vsdinpddia sitvlkgpga
      241 talygsraag galiittksg arkdggigit ynlnmsidqv nrwpdyqyey gegrtqayys
      301 ygdsadgint stgaaagraw gpkfngqqyf qydpntpnni aatrtpwkay pdyikgffqt
      361 gstitnnlsi eggddkssar lsvshldnkw ivpntgyqrs svalsvnqrv stklkvngka
      421 tytnkqsdnl paagynnqtl myflaigtap nidhnwfkpy wqpglegvqq knpfnpgpdn
      481 pyidlyedln kmnkngfigt asatyefndk lnvmfrtsld msnefrsqqr pysitkypkg
      541 myreqnvfnf esntdvllty kdkvtekidf sfnaganamk qtynfagiya dqlaqpgvyq
      601 lsnsldpava dpqrsekain siyaatqwsy nnaiflditg rndwsstlpy grnsffypsv
      661 stsfslgdmf tlpkqisfak lrlsyaqvgn dtrpyqttky ydkiysntft nsptlfnpnl
      721 kpeitssyea gldmrffgnr lstdiavyrn nsrnqilaip ldptsgyasa lvnagliesn
      781 gvevvlrgtp vstpnfswnt tlnfsrnrsy vreladglts qviyshdgnv tiearvggrm
      841 gdmygrgfqr spdgkivygs tglpaqldpv akvwgnafpd wkagllneft irkvrisfll
      901 dyqrggsmfs qsnhkyntlg ktkvtlpgrd ggivgdgvvl gsdgvyrpnt vnvsaasyyd
      961 nyyqisnaet nifdatylkl rearvefnlp arwlgksgfk sismavygrd lfnitkfpgf
     1021 dpeggnlnsg tltpgvelmq fpsartmgln ltlkl
//
LOCUS       WP_100342323             959 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter auburnensis].
ACCESSION   WP_100342323
VERSION     WP_100342323.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter auburnensis
  ORGANISM  Mucilaginibacter auburnensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Mucilaginibacter auburnensis"
                     /db_xref="taxon:1457233"
     Protein         1..959
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106049
     Region          42..958
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrniyiktcc vflgtyfsil raeaqqards vqtvttdsli nvafrkvpnr dvlgavssvn
       61 vaelinksyg anglnnlqsf vggyagggad galniwgqap lvlidgiprr aadvrmteve
      121 svtvlkdass valygsraak gvvlittkrg aekpltvdlr vnggflvpks ypnylnaady
      181 mtfynealrn dgltnkftda eisntragin pwrypdlnly ssdflrkmty rtdltgeisg
      241 gnkdakyysn iglgynnnll klgqskkana ldvnvranvd mrinswlkas vdavvimnne
      301 ytargdfyga aatlrpnddy fsylvpidrl dpanaqlqai aknsnfvidg kyllgglstr
      361 qtsdlsqila sgyiktkrnt lmfnagaead lgnltpgltf gmrfsmdyts ryseaftvay
      421 atyqptwatv ngtdvitnlt qfgndgiata envgsslynq tisfnprlmy qrtfgqkhnv
      481 tgaligwgym tqvssdpnnd ggsdyqnirn tnlgiqagyn fnhkyyvdft gavihsgklp
      541 nsnrnslspt atlgwrisee dffknhvsfv ddlkltatys slkqdldits ngadyylyqg
      601 nittpgtygw rdgtssgsyv lygrganpnf tfverkefra gldaflfkha lnlnanyfhq
      661 etkgllangl atvypsyyng ngsfqpwlnf nndmrkgvdf sanytskigk lkfslgfvgm
      721 iykseatkrd evyensyqnr vgkpldasfg yiaeglfqsq aeidaharqt fggtlkpgdi
      781 kykdingdnv idtrdqvylg rngggaspft ygvnltlkwk nltmlvlgsg qsgaigykns
      841 syywvtglgk ysdvvlnrwt petastatyp rlstnsttnn fqnstywmyd nnrfdlrrvq
      901 ftydfnktaf gktsfihgms vyvngdnllv iskerklmet nigsapqtrf ynigikatf
//
LOCUS       WP_100374863            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium geocarposphaerae].
ACCESSION   WP_100374863
VERSION     WP_100374863.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium geocarposphaerae
  ORGANISM  Chryseobacterium geocarposphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Chryseobacterium geocarposphaerae"
                     /db_xref="taxon:1416776"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117728
     Region          22..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlatfai fllplyltaq eitisgnvks engsgvsgas itdkntgkta itdangnfti
       61 sanpkdilef yapdfstyti evsnrknysv vlkkvsekqi egvvitalgi akkkekigys
      121 tqevgtkqfe tittpsignl fsgqvaglnv snptgmqqap eftlrgnsnl vfvidgvive
      181 kevfqnldpn nidninvlkg atasalygsr grygallitt ksakkkgftv efsqntmita
      241 gftnlpktqt eygngshgky efwdgadggv ndgdmiwgpk fvpgtkiaqw nspirdkqtg
      301 eiipwygtva gsqyndksry ervpidwkyh dnlktfmkpa vinnnnfsis yknnkdiyrl
      361 sgnfmnyddr ipgaylqryg vnfssenhis dklifdtkfn fnqtftpnip nydynpsghm
      421 ytiliwmggd vdgrdlknhl wvpgqegktq anwnyawynn pwfgaeyykn knrtdiinaq
      481 agleykatpd fsvkgkismv enhnkqeiqs pysyfnysap rsggyilndt ktwnlnsdvl
      541 atykkkisdn fdftinaggs tfyykndidn astdglkvpe vysldnsigs vkyydylkek
      601 liysvystid vglynaffin vsgrndwsst lpkanrsyfy psaslsavis nlvnmpkavs
      661 llklsaswak vaydfqpysi rnyylnnsgi tfngnptyyy ptvlnyensl kpeqtksyel
      721 glsagflnnr itldatyfrt ldynnilqfp sspssgftsq yvngneyttk gveislgivp
      781 vktnnftwks linwstyeqk ltsiygdmpn ynnitlgerm dsfydytwqk spdgkvilnp
      841 ntgmptratt ptnlghfnpd wtfgfnntfk ykkltlsigi dgsiggvmrs qvvekmwwgg
      901 khpnstmfrd leyanpgtyy fvpdgvnynp atgtytphtk aisfqdwaqn ypyqarvted
      961 esglfanvfd rtfvklrsvi leydfsslln pkgmvkgfta nisgynlamw kksknlysdp
     1021 dykiksgndi qdpssrwfgi gfnlkf
//
LOCUS       WP_100375351            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium geocarposphaerae].
ACCESSION   WP_100375351
VERSION     WP_100375351.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium geocarposphaerae
  ORGANISM  Chryseobacterium geocarposphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Chryseobacterium geocarposphaerae"
                     /db_xref="taxon:1416776"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111163
     Region          45..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myhkinffkf kklipialif lvanqahaeg fskhspisfq vkepitgsvk dqegsaiega
       61 kitvvetget attdasgnft isanigqals isyegyttqi lkisgssvsv slkskkgats
      121 ieevtlvgyg sqkksdvtga isqlkaanfk egmnisvdnl mqgkvagvri vqtsgepgag
      181 vnvsirgigs irsgstplfv vdgvplnndp vsasspdfgl gntaaknpln flntsdiesi
      241 tvlkdasaaa iygargsngv vlvttkrgkk geplftydty lgfssvikkl dlltadeyra
      301 agidksydhg gntdwqdeiy rnavssnhsv sfskatdtgs yfaslshmdq dgivlnssfk
      361 rttarinaee sflddkrlkv kvnltasdir etgipnggta gsdgqliiha lmanptrsvy
      421 dengnytnfn mnahynplyl lsvyqdktnt frvlgnteat lriipglnyk fnlgidrsls
      481 ernttmfpni tdrspkgiys qanldaynil lehyltydfs lgrhnfnwla gfsyqkfkat
      541 atywgvrnfl aqgagippei npgysgdvfi pqpgtdqene lqsyfgrvny nfdkkyflta
      601 slradgstrf gdnnkygyfp svavgwtisn enflkgnpvi nelklraswg qtgnqevqnk
      661 itkpsyslaa sagyylydnl nlingvlinr taypdlkwet veqsnigldf sllknklygs
      721 leyynkstkd ailripspvl sptpmiwrns dgtiknkgie fslgyeiikn enftwnldvn
      781 gatvnnkitg lpvseiysgs vsgpglsgvt anvykngyqa gsfymyhylg idangkyiye
      841 dvdgdgtigq kdkkifegpi pkftfginsy mkykkfdfsf sfigqtggyl vnntaldlni
      901 nnlasdrnvl knfydsgasf tnqpqlssly leksdfirln nvrlgytfdi nqlkflksin
      961 lyvsaqnllt itsytgydpl vdtskqvegn qslgidytty psaktfilga tvkf
//
LOCUS       WP_100375290             959 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium geocarposphaerae].
ACCESSION   WP_100375290
VERSION     WP_100375290.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium geocarposphaerae
  ORGANISM  Chryseobacterium geocarposphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Chryseobacterium geocarposphaerae"
                     /db_xref="taxon:1416776"
     Protein         1..959
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105235
     Region          39..958
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrfylaktn kaalffamal lpsglaysqt kkdtvakekk ieevvvigyg tqrkeavtgs
       61 vatvkgealr evptanitqa lqsrsagvei nqtsskpgat mkirirgtrs lsdsandpli
      121 vldgipfvgs lgdisssdik svdilkdasa taiygsrgan gvilvttnrg skgqkprfty
      181 nsftgsqtlf srypmmngaq ltklrhdand likngdsekd gvdtdwqkly ykpamitnhd
      241 vgvsggtdgg nynvglsylk qdaivplqsy erfgfrlgld qqvgkifkfg fttnsnyvks
      301 egngvasapt lgysplaspy defgnprrtl tmssnmdqaw vytrksldal gdkyvdetka
      361 fssynniyge vklpidglky rinvgldfrt snsgnytgvg vfninpasis sagkgnnqty
      421 hwtienllty dktfgkhkin avalysseqn tytssymsak nvpadffqyy nlgqspqadi
      481 tvrpedqsya rtglvsymgr amytydnkym itatlrrdga svlaeghkwn typaisvgwn
      541 itnenfmkaf qfvnllklry gwgetsnqai apyttlgslt vnpynfggay stgvsintap
      601 npylgweysk thnagldfgf lnnringtve yyrthtsgil qnkslpstsg ipggvlqnvg
      661 dienkgweas lnaiiidkpd gfswdagvnw yanknkilsl asgaqrdenn lwfvghnvns
      721 lydyqyvglw qqgdpylsil epqvgaapgm ikvlytggyn adgtpvraig pedrqiidtn
      781 pdwqggfnmr faykgfelst vgafqkggvl issiygsagy lnrltgrgnn vdvdyytddn
      841 tdarfpkpgg llsgdnpkyl stlglfdasy vklrtitlgy nlnkdflkdl ninslriyft
      901 vtnpliiysp yhkmsgmdpe pnstgdqnqa vsgyknrqli igtnnpatrn filginlsf
//
LOCUS       WP_100367146             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Yoonia
            maricola].
ACCESSION   WP_100367146
VERSION     WP_100367146.1
KEYWORDS    RefSeq.
SOURCE      Yoonia maricola
  ORGANISM  Yoonia maricola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Yoonia maricola"
                     /db_xref="taxon:420999"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55485
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif egedrvamtp asakdlqklg yecmietgag agagfsdqay kdagvevakt
       61 atalykaadi vakvrppsda etkklregqt lisffypaqn eklmeaankk gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqvesmg aefvfldfee eqqdgsatgg yaavsspefa
      241 aaqlakfrei apdidivitt alipgrdape lwtkdmvdsm kpgsvivdla aerggncklt
      301 vmdekivtdn gvtiigytdf psrmaaqsst lyatnirhmm tdltpekdgm pnhnmeddvi
      361 rgatathkge itfpppppkv aaiaaapkke apkeltaeek raaevaafqk etktqvglla
      421 agaalilgig lipgmpasfm qhfivfvlsv figfqviwnv ahslhtplma vtnaissiii
      481 lgaliqigss salitllaal gifmaainif ggflvtrrml amfqks
//
LOCUS       WP_100375997             941 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium geocarposphaerae].
ACCESSION   WP_100375997
VERSION     WP_100375997.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium geocarposphaerae
  ORGANISM  Chryseobacterium geocarposphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 941)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Chryseobacterium geocarposphaerae"
                     /db_xref="taxon:1416776"
     Protein         1..941
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104393
     Region          36..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrdlkysc liavlyfgmn vnaqvtpkkd svtkeqkiee vvligygsqk kenvtgsigv
       61 vsakdladkp nsnpmssvqg kvagvnivna gspgtsprvd irgvgsltgn tvfivdgtit
      121 ndisflnpqd iesmsilkdp sslaifgaqa angaviiktk tgrgkpvynf nsylgfkklt
      181 nvprmantkq yielyneklm ndngnsngsl spnqfsadtn wfdevfrkss iinandfsas
      241 gslgklnyyg sigylqdegi fdaghninsg ngfnrlntkl nlsykitdnl tigdnftfsk
      301 mrtdavnspl lnaynsppif dpmnsatgny qffngysian pravldlfrs qtrqerllnn
      361 vwaeykflkd ftfkvsyttd nyntskyeyt pvltyvpvgd qkptklitrd srdrnyiwdn
      421 tltwkksfgn hnleilggfs rvrnsyqpty sealnvfyng tneslsisng tdilvidnrv
      481 vdkynnvpnq drteslfari nydykgkyli ngsvrrdgts kyskddrfrt fpavsagwvi
      541 skedfmssqn vfnllklras ygklgnpnvn rsydalvnvi tsgayygstg ypastitefi
      601 dpsigwettt grdvglemgl lnnklkieat yfdkdtkdvv ygvvqgtvsg asnwnnyvtn
      661 aysfknkgfe vmanydakls envrlgvygn lttldnkits vyggsyletg aslfgnsivr
      721 lqegqsvgay ygyqvagvfq tdaeaaasgq sgakagwfkf adqdgngvid srdktflgsp
      781 ipkgtygfgv nmnvysfdis vdfqgvfgnk iynynreqrf gnenwdldfy nnrwtgpgss
      841 nsysmttnnq siilpssfyv engsyirlrn vtigytlpkd laksmlltkl rlyvsaqnpw
      901 tsfkyngfsp eilntdrvqm gidnniapis aiytfgmnlt f
//
LOCUS       WP_100376049            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium geocarposphaerae].
ACCESSION   WP_100376049
VERSION     WP_100376049.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium geocarposphaerae
  ORGANISM  Chryseobacterium geocarposphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Chryseobacterium geocarposphaerae"
                     /db_xref="taxon:1416776"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119428
     Region          21..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklyiplll cctlsltaqh tlsgyvitee nslplsgati nilnsktvii tdkngffklp
       61 asgekitlni shsgyrsvsl dvtlpldtpl rivlshkvnd iqevnistgy qkipkeratg
      121 sftftdnkll nqqvstnild rlanvaggvf lergrsgspq lmvrglstin gpksplivvd
      181 nfpyegdisn inpnmvesit vlkdasaasi wgaraangvi vittktgkfn qpvkvefnfn
      241 tsyspkpdfg ylktmsssdf ievekglfqk gfynsdinss shpvlspvvd llnkakngli
      301 ssdeadrqir qlssidakeq frrymytpse krqyyvgvtg gapaflwsta lgyddntgnl
      361 gedynrmnlr fqnvwkpvnk lsltsslyyt etttksgrta yggiimgrns fvpymklade
      421 ngrplvvnkd ynqnykdsfe kgklndwnyy pltdwqndqv ktkasevmvn aginykiwkg
      481 leadvkyqhq rlndnsdnlh narsyyarny vnsfaqinng nvtfivpkgg ildqsssltt
      541 innirgqlsy ngqwnrhnis titggesrda vrtyhynryy gfdeermtsg avdyahqypl
      601 lptgstdfiq rnqslgkrtt rfvslyanaa ytydnrytis asfrrdasnl fglktndqwn
      661 pfwsvgtlwd iskenfyriv wlpslklrgs fgyngnidpa mvavstiayd ldnsvytgtp
      721 maridnyynp nlrwetsrmv nigldfssrn nrisgsveyf tkkgtnlfgp aqmdyttgid
      781 ymrsnvaeik gkgmdivlkt fnidkviqwn tilnfsiyhd kiskyyllnp manqfigngs
      841 svpisgiegk pvysifayqw agldpktgdp rgylngavsn dysaltgagt svndlvffgs
      901 alptaygsfi nsvgyqnfsl digivfklgy yfrrssinyt nlyrswtghs dfenrwqkeg
      961 deaftdvpsn tlqsnanrda fysgssvlve kadhirlqyi nlnyrfsenf lrstmfkdls
     1021 lfinlsdlgl lwkanksgid pdfnlggngl kppsvytigl ranf
//
LOCUS       WP_100376710            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium geocarposphaerae].
ACCESSION   WP_100376710
VERSION     WP_100376710.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium geocarposphaerae
  ORGANISM  Chryseobacterium geocarposphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Chryseobacterium geocarposphaerae"
                     /db_xref="taxon:1416776"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110274
     Region          32..1008
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltagvlv lvlssslava naqqtkkdsi ktqeiegvvv talgikrekk slgyssqtld
       61 aekvnsvptt nfinnlsgkv agmeiknngn fggssnivlr gaksitgdnq alivldgvpi
      121 isgnlnsgda srgrdgfdfg natadidpnn iesinvlkga aatalygsma angaviittk
      181 kgkrskslgl sinstvsvgs mdkstfpeyq klygagynga dsfisadvng dgipdtvapt
      241 gddasygpay npnllvyqwn afvpgnpnfg katpwvaakn dpskffqksl sfvnsfnlng
      301 gdelntynlt ftnnnetgil pnsklnknml sgnfsrkfad nftvrtfltf ndqttvgrns
      361 vgyndniltg frqwwplnvd ilelrdeyfr tnknytwnmn apldgdlsaa fwnnpywdry
      421 qnyssddktr litgaelsyd vtkkfnilgr atvdytsskq elrkavgsha eefglaqade
      481 tsgywvyddm iirqtydlig rytwnvsdkf nalfvaggqf mdqhqrsten sttggliipg
      541 lytvgnsray ypsiennirg qksgvyaqas fdydkylfle gtirndtsta lpksnrnyty
      601 fslgssfvfs elfksswlnf gkvrlsyaev gndmafgrpg ffssrgtvsg lpmadisnty
      661 vdfdalkper qkswevglet smfkrrvtld vslyktntkd llfsvpqsps tsysfslina
      721 getqnkgvev algivpikss dfqwdinvnw sknkntvval nqgrnnlqla sfqettlnat
      781 vgeaygtfrg tgfvydangn kvvdddghyl vatdrvlgni qadwiggvyn tfryknfslg
      841 flidvkkggs vysldqsygg ltgiyaysag lndlgnpvrn pltngpnsgg iilpgvkqdg
      901 rpndvridas yaggaygtda gipqeafiyd asyvklreak isytlpsdll kntfikgmtl
      961 sllgqnlwii hknlpdadpe agtssgniqg fqsgvmpstr iysfnvkldf
//
LOCUS       WP_100376944             911 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium geocarposphaerae].
ACCESSION   WP_100376944
VERSION     WP_100376944.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium geocarposphaerae
  ORGANISM  Chryseobacterium geocarposphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Chryseobacterium geocarposphaerae"
                     /db_xref="taxon:1416776"
     Protein         1..911
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=99433
     Region          33..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfttvlki apafllassm ihaqtkdsit kekkieevvl igygkqkktd itgsissisa
       61 kdfnggatsp gqliqgktpg vsivgnsgap gagtairirg igslsgsqsp lividgvpqd
      121 fsgisgasdp lslinpndiq tfdilkdasa taiygnrasn gvilittkqg tagklkinfs
      181 tlasvstkmg nvdvldadaf rsfvnqnasp syvarlgsan tnwqdqiyqk awgtdnnvsf
      241 sggvkglpyr vslgyneqng ivktnsfrrt saafnlnpkf fdnhlsvnvn akgtftdnrf
      301 patgvianat yfdptqpvys gnsnyggyye wldpasntgl nvnatanpva qlnavrdvss
      361 vwralgniql dyklhflpdl hfnvnagydy skgegaitid payksgigvl gsyrpysmek
      421 knklletyfn ytknitslkt nvdltagyay qdfhttaplv vtnqgngqta gqvnpvdrkl
      481 vllsfygrai ftiankyiis gsirrdgssr fyngtrdnlw gnfpgvsvaw kineeeflkn
      541 sglntlklra gwgktgnnel gdnyypafas yspsvpgaqy qfgsqyyyml rpdiynpnlt
      601 wettttqnlg vdygfaknri ygaidvfkkk aekllvdspi aagdlsnhni lnvgsmdtkg
      661 iegsitfvpi knerttwevs fnathynskv tnlvsaands ffipigditg gvgnkiqaha
      721 vgyqpysflv yqqvydnngk pldgvfvdrn gdgvtnasdm yyykstqpda ilgfntkvny
      781 knwdfglsar avlgnyvynn aasnsslqsa stnsylqnvy ssspqyqfsl pryfsdlfie
      841 nasffrldnv nlgynfkdvf skgsslkvyg mlqnvfvitk ysgvdpeifg nidngyyqmp
      901 kvyslglnfq f
//
LOCUS       WP_100377251             943 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium geocarposphaerae].
ACCESSION   WP_100377251
VERSION     WP_100377251.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium geocarposphaerae
  ORGANISM  Chryseobacterium geocarposphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 943)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 943)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 943)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..943
                     /organism="Chryseobacterium geocarposphaerae"
                     /db_xref="taxon:1416776"
     Protein         1..943
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104447
     Region          35..942
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklkllst gvlfflgsas llaqengrrk kdtadvkdie evvvvglkst tkkqavista
       61 kiesekinnr pnsnlmniaq gqlagvnist gsgqpgakpt vvirgfstin gntdplyvid
      121 gfptnadsfr slnpndvesm evlkdasata mygnrgangv ivirtkgggf asktvfnyrs
      181 qigvstlqnn rynmadakql ltlekmasag kgvgmtydei anfnvntnwl dyffnpsllq
      241 shdfgittgg qnlssytnvg yleqqgvlst tglkrfslrt nvngktnnnk ftyrvgvyag
      301 lsrntqassl gtggvnqnlv igglrgapyi spndyvsggg isanlvntpl flmdkertyk
      361 satddlrldl tseanykitd eltatmrana qllsldgnsy qtpdawnsvy fkasnqtwig
      421 wetmstsrqf nfnnlyqlsy skrigdhkid vlggyeynny mikttsftqn glnpkvwvpg
      481 tgtgypafva gdnynvpnvs agqsrlnmys yfanldydyk skygvvanvr rdatsrfskd
      541 nrwgtfwsvg arwnineenf mkniewvnil kirgsygtag nqrivdgtif aglnpkayln
      601 syvtgsnsyn gtqalgislg ypdlhwettk qwnagvdfel fkrrlrgtfd vyekkgveif
      661 ypwpqsylig tgavnmnspi dlknngiein faydviknsn ltltlrgnga mnkervynlp
      721 seplidgtip mqysvngqly qapyvyhylg vnqsngnllf edangnptet pttadlkplk
      781 ygfnpkfqgg fgfdldykgw fvnttftyva kvyrydydwa svmdpsnlgs fnvsadllna
      841 wtptntntni pslkaqniny dglsdrflvd gsylrlrnvq vgynvpksli kntfvnslsi
      901 tlqaenlvtw skwkgfdaes nigsdqgryp spriytlgfd ikf
//
LOCUS       WP_100377850             983 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium geocarposphaerae].
ACCESSION   WP_100377850
VERSION     WP_100377850.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium geocarposphaerae
  ORGANISM  Chryseobacterium geocarposphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Chryseobacterium geocarposphaerae"
                     /db_xref="taxon:1416776"
     Protein         1..983
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108262
     Region          36..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklrlslitt avlffaggqi veaqrtkkdt tttekqidev vivaygsqkk etlvgsntei
       61 kakqfadrpi snigqaidga spgvkvstgt gqpgsapsiq vrgigsygis tsplyvvdgv
      121 iytgslsain pndiasfnil kdaastslyg saaangvvli ttksgrkgtd vlnfnmstgy
      181 vgrsipeydr vdvyqyypli weairngrft tnpgaglaaa ntyattnlis gvlktnvfnv
      241 adnllvvdgv lnpnaqlkyt dldwqgplmk tgfrqnyeln ysggtnktty fssvsytnet
      301 gyliksdfer ftarlkvdsq ikswlklgts isgvssngnn sidgadnnta yinpynwtrt
      361 mgpiyspyah dpntfatlyd aagnivydag gargadaaag rniiqetlln kdisknyyii
      421 srsyaefkvd pyltlstnvg ydirnnrrsr yvnkligdaa pagaaekttf teqtltwnql
      481 lnykrkfdvh nfefllghen ykyiyeyfna ykqgqtvddn delinfvtpt tvtsqtdnyk
      541 kesvfsrlny dykskyllsg sirwdassrf akdvrwnsfw svgagwrikg edflkdsrli
      601 sdlklrgsyg evgndgtnsy ymykstyslg ynnaqepgil fgfladpsit wesnkqtdvg
      661 ldfgflnnri tgsvdyynri tddlifpvpv pvssgvpgnn isknvgtmyn rgfefalsad
      721 viknenftws inanastlkn qvtelsqgit eiingtkkvs vghsvydywl rqwygvdpad
      781 gsplflvada yagttasdir tvngtqvttn fnkakydysg saipdlfgsf gtsisykqws
      841 lstmftyqlg gmtydsnyqs lmssysqgga lstdilnrwt tpgqitdvpa lnsstytssn
      901 aassrwlvks dfitfrqatl aysfspesis qygltsfrll lsgeniwskt arkglepaqt
      961 fngttsnryt parivtigfs lsf
//
LOCUS       WP_100378062             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium geocarposphaerae].
ACCESSION   WP_100378062
VERSION     WP_100378062.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium geocarposphaerae
  ORGANISM  Chryseobacterium geocarposphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Chryseobacterium geocarposphaerae"
                     /db_xref="taxon:1416776"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110441
     Region          29..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrketqkllv lsllglvsvn laaqqkakkd tiksidevvv talgikrhdk slgyvaekvn
       61 seeilktqnn nwaqalegkv aglkiqtaga gplgsslikl rgdismnpan ngalivvdgv
      121 plnssttgtg fsaygagska dlpidygnnl ntinlddies mtilkgstas alygsrgagg
      181 aimittksgk nkkgkiqvsf nsyssfdtvl kwpdyqyeyg qgtmtkdkng nyyysygasa
      241 dgvstggtss afgpkfdgqy yfqydptieg qskerqlwrp ykdnikgfwk tgstysnnva
      301 lessnentsf rssltylkne wmmpntgfdr lnaalsfdhk lnerlrvafk fnysktksdn
      361 lpatgysnqs isyfmifqnp nvdlawyapi wkkdkyqteq vhpfssfidn pyliayemln
      421 svdknfitgs anlnykvskn feislrsgle vnnearaqkr pwntanylqg myreqfikqm
      481 dlnndllfty kksfnnidlt asaggniryt evkmfdytge gllkpgfyam pnaisvisky
      541 aapndkqins tyglvnlsyk nlvfldltar ndwsstlpsa frsyfypsaa tsvilsdifk
      601 lssnnlnlwk lraswskvgn dtdpymliky fknsdftgsv espsmypnpd lkpemltnie
      661 ggmdfsilkn rlnysvtayq nnnknqivri palletgyst riinagevrn rgiemtlntf
      721 piknknfsws vnanwsmnrn kilslpeefh gepytmgsvg gvvyynavvg gslgdmygyg
      781 lmyspdgqvi ygsdgltakp temkkignay pkwraglqne frykgftisf sfdgqykgma
      841 ysqshhkmte qgklkhtlvg rdnpgglivg qgvvqnpdgs fspntkgvlv styyadywrr
      901 anvetnsfdt sfvklrdari sytfpksite qlklseltfa lfgrnlwmwt kfplfdpeaa
      961 tldnnqitpg vemgqlptar tvgvqlnakf
//
LOCUS       WP_100379689             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter brandtiae].
ACCESSION   WP_100379689
VERSION     WP_100379689.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter brandtiae
  ORGANISM  Polynucleobacter brandtiae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Polynucleobacter brandtiae"
                     /db_xref="taxon:1938816"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39415
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpleir pgetrvaatp etikkliaqg htvvvqkdag vrasqpdsay eavgatigsa
       61 sdalgaeivf kvrapeaael qqihsgsvli gmldpfdndn iaamaaqgit afsleaaprt
      121 traqsmdvls sqaniagyka vmvatneyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpyetdee reiakgvggy arpmpeawmk
      241 rqaalvaeka qqadivitta lipgrkppvl lhsdtvakmk pgsividlaa grgdngsgnc
      301 plteadkivq kngvkiigyt nlasmvaada salysrnlld fmklivdaqa klviptdddi
      361 vtaclmcrdg qairkn
//
LOCUS       WP_100408815             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. 69].
ACCESSION   WP_100408815
VERSION     WP_100408815.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. 69
  ORGANISM  Acidovorax sp. 69
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Acidovorax sp. 69"
                     /db_xref="taxon:2035202"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55452
     Region          11..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtspvpqpq rigvpreifp gekrvatvpd vvekliklgf svavesgagd aanfsddayr
       61 sagaevigda aalwaasdiv lkvrppsgde valmregstl idfiwpaqnp dlmqqlasrk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rkmyaeqakd vdiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg qavvrhgvti vgytdlasrl arqsstlyat nllrlteelc kakdgvavvn
      361 meddairglt vvkdgaitwp applkqaaap apkaaaapva vkksshgpga pmsaktltiv
      421 favlavlfwa igsyapvafl ghftvfvlac figymvvwnv tpalhtplms vtnaissiia
      481 igalvqiapp daslngrpag lilwlafaat vltainmfgg favtrrmlam frk
//
LOCUS       WP_100423564             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sediminihabitans luteus].
ACCESSION   WP_100423564
VERSION     WP_100423564.1
KEYWORDS    RefSeq.
SOURCE      Sediminihabitans luteus
  ORGANISM  Sediminihabitans luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Sediminihabitans.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Sediminihabitans luteus"
                     /db_xref="taxon:1138585"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52814
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpretr pgerlvaatp rtvgqlvdlg yevvvesgag erahlgdeaf taagarvvga
       61 deawaadvvt avnppaasdv arltpgatlv smlgpaahpd lveslrargv talaldavpr
      121 israqaldvl stlsnvagyr avveaatelg amfsgqvtaa gktppatvfv igagvaglaa
      181 igtaaslgaq vrafdvrpev geqiesmgat fvqaaqaqqe vsadgyasal taeqealtra
      241 myaeesarad vvittalvrg tapttitadm vaamkpgsvi vdlaasgggn celtvpgerv
      301 vtandvvivg atdltsrmpq htaqlfgtnv vhlmalltpg kdgvlvldld dvvqrgmtva
      361 hagetlwppp pvqvsaapaa aapapepaqd paeveraaae qrrlrsrrrt vgatlaavlv
      421 vlalsfspps vvghatvlil avfvgyyvis hvshslhtpl maqtnaisgi ilvgallqig
      481 sddllvtvla cvaatvasin ifggfavayr mlamfrkga
//
LOCUS       WP_100430224            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100430224
VERSION     WP_100430224.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110830
     Region          21..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnfifsfla lillpaymsg qvikgkvldl ngmgvpgafi vagdsnvsay sdfdgtfnin
       61 akvgqilkis lvgfdavsia ataepmtitm keskdtelke vvvigygtrk kvdnttaiss
      121 ikteeitrtk vlnasqaiqg kaagvqviss dlpgstpsvi irglgtalgg rtplyivdgm
      181 qseninnina nditsyeilk dasalaiygt raangviiit tkkgkgdkvs veiesyagir
      241 eplkkvkmag snkyayysna alqstvfsqd qpvntdwfde itrtgiyyqn nlsvsgaten
      301 ikyffslgny eekavlngld ygrttfrnnn eykiskkltl nqnfsftsak stpkplsaft
      361 naykqspivp vyfpdgkygv srvgddgfas etgssfnnvg npaaqlnffd eqqrsitlqg
      421 glkldyeiik slkftsqfng eyytwkqyny ddtkniwlaa npnkvstdye kefpnaninl
      481 ltkgreeyfn wnlsnyltyn kifneihdve ltagietsvr gprekltiar knvnansnyw
      541 slkgdndyet nitsyqdevf netklasyfg rfqyklmdry lftgtlrrdg ssnfgkdyrw
      601 gnfpafglgw vitkesfmqd vkainmlklr ggwgrlgnqn vplnnqsyts gpnaylggsi
      661 lnqgttissq idpslsweit eessigldfe lldsrlkgtf dvydkntsnv ilntkpyfts
      721 gitaaspahv gevsnkgyei slrwddkind disywvggnf snnkneltgl kdviltqlvg
      781 gglgngqdtk lldnttvgqp lgsfyiyeya gfdstngkml yynaagekvt qdalnantdk
      841 kyvgssltks nygvtlglty knfdfsvdgy gtsgakvyng kkaqrfsgen iengvatdfw
      901 tpnnltasnp apfnqvpvas tyylesgdff rinnitlgyk lpiqsnnfis scrfyvnain
      961 pfitqkfsgf spelngdgnp ygtqgvelda yptlrsfvig anlkf
//
LOCUS       WP_100430371            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100430371
VERSION     WP_100430371.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111520
     Region          44..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktfsfsrdv kafcflflmg tvlslspiqa knklrkslsi nqqqqiqgtv tdginplagv
       61 sisikgksna tvtdyngqyt lsaapedili fsyigyktqi vsvqgrtavn islqenetkl
      121 qevkinagyy svknsertgs iaritaksie kqpvtnvlav mqgrmagvni tqttgvpggg
      181 fniqirgrns lrtegndply iidglpfase nvgntnlsag ilpnaginpl nginpsdien
      241 ievlkdadat aiygsrgang vvlittkkgr snktevtina ytgagkvtrt ldlmhtdqyl
      301 emrreafand gvavypsyay dlngtwnqnr ytdwqkelig gtaltqniea gvsggnsktq
      361 flirathfre ttvfpgdfsy gktalhfsin hvsennkfsi nfsgnyvadk ndllgtdltr
      421 qaiilspnap elytpdgtln wengtwsnpl rfleqkylak tntlvansvl sykilpnlel
      481 kttlgfsdtr ldeskeapst mynpslglds sastymsnya kqqswniepq lswqkgiggg
      541 tiniligttf qqrtkdqqal yatgfasnsl idniaaassl silnnnstty rynaifgrin
      601 ynwrqkyiln atgrrdgssr fgpdkrfanf galgaawlfs kenfianavp flsfgklras
      661 ygitgsdqig dyqylntynt sggnyqgiat lqpirlynpd fswetnkkke iaiemgfind
      721 rifttvarys nrssnqlvgt plpgttgfts vqsnlnavve nsgwefelrt vnfqnmpfkw
      781 sttanltipk nkllefpnle gstyasqyvi gesldirkvy hytginpttg iyqfedynkn
      841 gtisgaadrq kivsinpeff ggiensltyk nwqfdflfqf vkqigvnyns aaplpgtlsn
      901 qdteilnrwq eqgdtegvqk ytagsngaas aafnnyrssd aaytdasfir lknlslayti
      961 peswsksarc riylqgqnll tfthfkgldp enqslgilpp lqvlaigvql tf
//
LOCUS       WP_100430492            1007 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100430492
VERSION     WP_100430492.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1007
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112232
     Region          34..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mryiqlkivl cfvlfaflpa kifaqidqkl nlagivigag gkplenvtvv skkdnittat
       61 dnkgsysisv tantdiefsv agyttlvvka taavsdvnln kensnlvqva fkkeesrdlm
      121 ggisfvnlpe ileknyttys ldgvqaligg lngniwgmng ilvlvdgvpr dinsvlstev
      181 eqitflkgvs avalygsraa kgvvyittkk gkvqkqqitt rfdngvfvpk slpkylgsae
      241 ymhyynqarv ndgldptysd etiynyaagk npyryadvny yapkyvkefy fnydanveit
      301 ggnksakyyt vvnfssqqdp lqsfgeaann nsnrfnvrgn vdlqindrfs atiganaiys
      361 tsrgvntdyw gsaatlrpyl fsplvpismi essddasmal vnnsnyivdg qyllggtqln
      421 ptnpfaaiya gghntyssrq fqfntginve lgdvidgltf rtdfavdysn aysqsynnsy
      481 atyeaswnny agidqitslt kygkdsktgi enlsgsslfq tvafsgqfny vkkikeqhnl
      541 samligsgyq qsqsavyhkt snanlglnls ynfdqkyyae fngayvhsak faegnregfs
      601 ptmsigwkls eedfmkdvta vnnlklsisg gilntdldvs nyylyesiyt qtdgqwfswr
      661 dgalnrstdv rrgenldlsf akrnelnvgl egaffknlit lntnffvnei tgnviqassl
      721 ypnyfvtgfp ntsflpyiny nndkrigfdy dvrfnkkign vdlalgltgt yvdseatkra
      781 elfddsyqnr qgrpldalwg lrsngffmda lditnspsqt fgqvkpgdik yidqngdgii
      841 dnkdevylgk agwygapftf ginftskwnn ftfftiftgq tganamknnt yfqmdgedky
      901 sinvrdswte etketaiypr vsslssdnnf rssdfwmyst nrvnlskvql tydfpkkmlq
      961 ktfftelsvy algsnlltis enrdvmelni ggepltryyn lgvkalf
//
LOCUS       WP_100430552            1136 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100430552
VERSION     WP_100430552.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1136
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125613
     Region          130..1134
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mylvtkknss kkkvlffllv alltqltfaa tiksqstest pvlvsknvye lktlfkaien
       61 qtdysllytd evaklktltp vssgthtlav llkeaaikfk vvyqindgli tfktntstrd
      121 kiisvlakqi kisgkvtdns gkpipgatil iegtssgvqt dfdgsytiea eegqilvfsc
      181 igfktikqti gqenkinvvl teeaemlkel vitalgikre ekalgyamqk vqgssvqtvk
      241 gidvatsltg rvagllvkns tefaeaptve lrgenallvi dgvpygnmtl rdipaddies
      301 lnvlkgatas alygyrgasg aivvttkkgr dkkglavsvn sstmftagyl aipktqtvfg
      361 rqidavtniy kgtgswgvpm egqnviqwdp iskanklmpy latgkdnfkn fleqgyilnn
      421 nfsitqqgeh gsirssatwv ankgqypnsq ydkytytlgg didldkfkls ssvsinkqts
      481 pnigfngykg ydpmysiliw sspdydlrdy kdywlvknet qnnsytgtnn npyfdryerl
      541 hsidrqvfng fvsgtyelap glnavlrtgf dtynnkqvir iskgslqgag nstvilngte
      601 iwgeslkgsy negmgsgyss ntdfiltgnk kikdfdiesl fggtiyyted qgieartqgg
      661 ltipgfyslk ssvtsavvns tiykrqvnsl ygrlagswks mlflegtlrn dwsstlpkst
      721 rsylypsiss sflvseilpk ydwlslwkfr gswtssktpa gvydsnsvyn ittsawgssn
      781 sasypdtvrg nevapessst wevgtvanlf kkrasldftf yskrmfdflk atsvssasgf
      841 ssnytninee itrrgleltl svtpvkttdw qwdltanwsk yaryytklds qfsadkpwvk
      901 vgeradafvl neflkdgngn miyenglpvy sayesvhgya dpdwiwglts slrykdftln
      961 ismdgrvggl aqtttemymw qsgnhpdsvn dirykdattg tsnylgdgvk vvsgnviyns
     1021 ygeitsdtrq yaandvyvty enyvkrvhkg nawggtpspy dtysttflkl relsltyvvp
     1081 qrachfirak sasisaigqn lflwakdfky sdpdggsdnf sdpsqrfvgc nvklef
//
LOCUS       WP_100430555            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100430555
VERSION     WP_100430555.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115545
     Region          25..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfknlmil lmmlvssliv aqtstfrgkv ldelneplpg asvlikgttt vvitdlngvf
       61 eielpngneq livsflgyia vnffpenkkt atislkpdsh nldevvvtal gikkekkkls
      121 ysvqevqgdl tkgrdanimn slsgkvsglv vtaspeffts pnlylrgkkp livvdgvplg
      181 tnswnispdd iqsinvlkga naaalygsvg gngaiqittk rgtqnkkdyv vefnnntifq
      241 ggynalpktq naygpgsygn ysfvdgkgag indadydqwg prfdgqlitq ydspigadgk
      301 liatpwlarg kdnfenfmen gllttnnlal asnfdkgnir fslsntsqkg inpntklniy
      361 nfnlsgryni sdktwvdass nfnfqtspnn pnvqygpnsy iynmliwgga dydirdlrdy
      421 wqegkeglqq knfeytrynn pyfmayewlr gyykndysgq islnhkfnsn fdmlirtnma
      481 vtnlfenekf pysmttydre kaqgdykeky nygfknysdf mlnynktiks feikatlgan
      541 inidktrksf astnyliipg lynlsnsqtp vqptnynshf etqswygsmd lsyksflflg
      601 atgrfdtdsr lpeqnntffy psvglsavls evvkiplvdf lkvrtsyakv ggsldiysnl
      661 dtyrlrdpft idgktynaay vsevlsninl epafnssvel gmetrmlknr fgfdvtyyen
      721 tngpqifdlk ysetsgysgs kqngittktk gievslfvkp iksnsfnwdf ninwstykey
      781 lkevydgien ngrikigerv dafyindfmr spegklivgn dgkplinpyq tkvgykapdw
      841 smgitnnvsy knlalnftfd gryggkieny vnqkmwqsgr hedsntpera ndvigvksyv
      901 tdavvvtgge lisdgqgnti tdtrtfaqnt tkmyyqdyak ayhgnyaani idktffklre
      961 isltyafpas flkqsfiena sislvgrdli yfsknknidl dqflnesssp lqtptvksyg
     1021 inlnfkf
//
LOCUS       WP_100430913            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100430913
VERSION     WP_100430913.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109882
     Region          22..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkiflivmv iftthvtlaq skkisgfvsd aagapipgan vnvkgetnga stdfdgkfti
       61 evktgatlvv sylgyetrnv evgesstidv klisasstal tevvvtslgi kkskksltys
      121 aqelkgedlv rakdpnlmnt iagkiagvav tksaggtggs tkvtirgnss ttnnnplyvv
      181 dgvpmlniss yqpndsfgnt qggnrdggdv igllnpddfe gmtvlkgasa talygsqgar
      241 gvvlltskka kegvatfrvs snttvetaay lpkfqtsyia kpgadeswga aqstpdhtrd
      301 ffetgltqis sfgfstgsqn satnisyant sangiiptns lsknnfsirq mgkffgdrlt
      361 vnananytsq yvtnrptsgl yfnpltglyl mprgydfney knnfekfdpa rnmmvqnwmt
      421 nrdieqnpyw glnrnkskdg nqymngsvgv nykvnnwlsv gsrynydrvt sqfdkeiyas
      481 tqgtlshang ryisiddvss qnygdliati ntkitedltf fanvggsftk tslndetvld
      541 sdpsglgitn wftlhnfnsn tgnyqnygfr reqqsvfaaa tfgyknmlyl ditgrndwss
      601 tlantddmsf fypsigatwl isetftmpea isfgkvrasy aqvgndvpaf ytsptsrfva
      661 gtmnsnptvg prpgtslkpe sqdsyelgte wrfvnnrfgi eltyynnktk nqlltipapa
      721 tnpegfqnya fnggviknng ievlvnarii dndkfkwdat vnysknnnev sglpdelggs
      781 iiltvpgvns yryslingrp fgvieginle kdaqgrvlln edgsiqktgf eevgnanpdy
      841 mlglsnsfky gklflnftid grfggdvmsl teavndkfgv skttgdarda ggvdinavya
      901 pgttkagqaf agkynaesyy sqvggregat geyvysatnv slrelalgyt fdlknskifk
      961 tanlslvgrn lfffykdapf dpnislstgn glqgidvyaa pstrsiglnl nvtf
//
LOCUS       WP_100431108            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100431108
VERSION     WP_100431108.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119240
     Region          57..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrpkiiqhk lkflskptll vlllgssvvg evyatnsdss vnlslnaakl esvqqnitit
       61 gkvvsaddnm gipgvnvsik gvkggtvstd fdggyvinvt spdailvfse igfraqevkv
      121 esqrvinvkl vpdvsklnev vvvgygtqkk atltgaveii sskvfedrav tnvglalqgq
      181 tpglvvtrss srpgneglaf airgassvng sepliivdgv pvlnaqsfqn mnpddiesis
      241 vlkdgsaaiy gsrasngvvl vttkrgkgki kvnfntnlrf vtnglvgysp tmqeyatmwl
      301 eankeettpn wwiwgnkdnl lnmqkgvegk ydlfgtdffi fnanrieemf strysyqhnl
      361 svsggddkst yrlslafadn qgnlataydg ekqlnarfny dfnlserlkl essisiintn
      421 agqpskglga ilystdmpfy paknpygqwf apfngidgga iknsaattsd ggrydkkrlt
      481 grvdlkgtyk iwngisiegl asiqnerfnd eryvipvrly dwygnpkgna yqtdgvnnvy
      541 qasaeskfyh yyqallrydk tfnekhnvsv mggvnaekwt aqgisasrvg fedlgiydis
      601 vaatttqtng gykdingrys ylarlnynyn ekyiaevtgr rdgnsrfakg ykfqnfgsaq
      661 lgwvftkeef lspidnilnf gklrgsisst gneakglgaf dylslmgigs avlgqpasqq
      721 tasynnglis ytrtwervtq knvgidlgff tnrlttnfdl yekenigmli gvtypsvlgg
      781 appktnsgnf ntkgwefvig wkdnikdfsy nvsfnmgdak tmvsgvenad sygagqngiv
      841 nglpwkpifl yktdgyfkdq advdayyqay gtsdalaglp knnqavalrp gdtrrvdvag
      901 tgnitangnk nsslvymgdg tphytyginm gatwkgfdfn tffqghleqn imrsgymayp
      961 fralftnqnp tflgktwtee npdamyprlt vnptragwny gnndfmlqns ryirlktliv
     1021 gyslpaglts rlkltkvrvy fsgndlweas sikdgfdpes genatdgdna gypfgrtwsf
     1081 glnigf
//
LOCUS       WP_100431120            1108 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100431120
VERSION     WP_100431120.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1108
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120725
     Region          25..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miqkvlklll vfclfsfqha ksqnitvtgk itdgagmplp gativvkgsp tgassdfdgv
       61 yslevpslsa vlvvsyvgyv tkeitlkgsa tlnvtlisss qnlnevvvta lgqakvkksl
      121 gyatsvikae aivktgspti ansmygkapg vritstpgga gniniqirgi nsitgknqpl
      181 ivldgvpird gaatnndywn dqrirsngla dinpedieni silkgasaaa lygseavngv
      241 vlitsksgkg kkgfgidfnt sysnnqiayl prfqyergpg wtnanyssgf lapdgfahyd
      301 tngdgvadtr gvsnssnnfg pwfdgqpvms wdgvirpysp qkdgyknmfq dawdevtnva
      361 lsnntdnsni rfsythnesq glsmgnmnkk ntlnlntsfk tgenlktdvi vsymnqnvhn
      421 raigmdrlin nftgmispfd ngdwykakyq tslgykyvtg snqsltpsen iirngfkadv
      481 adyfwntnai qqdeitnrli asvtetysiy kdlklrgrvs tdltsvntet knpnerplvy
      541 aasgayqmda ndynilygdv mltynkkine afevgatagy tatketgfsl srftdgglsv
      601 rnwydmnasv niakssdkky evvkdavfgt isgnyknylf legtirkdrt stmnpnnnaf
      661 typsvnssfi vsdafelpev isyaklrasw givgnyaeiy kgnvafnqtt lgdqgtktpv
      721 litnsvsnyg neslkpemkn eyeigfetkf fknrlgldls yynakiydqi ldltlapttg
      781 aksiianvge lnnqgveial tatpiktasf swdltlnwak nvnkvvklan ganellhadf
      841 dgsaaqlksv vgdpmggiya hpvktdangn qmvdsdgfym idgdkwekyg saipqgvggl
      901 lntftyknlt ldvnidysyg gylmptgvnw mtsrgltees lnystnergg ltyymdangk
      961 gvqvansata gpggqtlyrd gmlmngvttd gatntnvisq agyynmtynw ggpqysssry
     1021 elyiqennyi kmreisltyn lptawaskig askftfsayg rnlffiyrsi kdmdpeatta
     1081 gskwsqnisn agtnpatrsi gcmlrasf
//
LOCUS       WP_100431210            1127 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100431210
VERSION     WP_100431210.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1127)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1127)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1127)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1127
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1127
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123591
     Region          31..1126
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqtlvvrrc svilfvlmsm ityaqtavsq ikvtgtvtdn agmplsgvnv teksskntvt
       61 tdfigkyqin vksdatlvfs figmrkmeip lsgrtvlntk lqddtnqles vvvvgygsqk
      121 kkdltgaiat ikaadlenlp vtnlsdalrg qvaglsvtsg sgrpgdagti sirqsfgfgk
      181 dansgvpliv iddmvqvdaa tglatmetfn rldpseiesm tilkdasaai ygsrasqgav
      241 virtkkgksg kakfsyssqf avndaishtk tmsayefgvf nnrfltgalv pgnvidpkvl
      301 fsakeleemk gldydwleka wkpaiqqkht lnisggtdni tyfagatrft qdanlgyqky
      361 ekwnyrtgit akiannldfs asmsgnsgfv dkaftkasgs vggydtgage qadydflvhm
      421 pkfvpwqttv dgkeyymspf pntnknfgsa nannniagwn yfanmnngsh qttddasynf
      481 ttslnykvag ikglsfkgtf artqnssnae qiqlpydlar itnyqlqdnh lasaaypsat
      541 iknpevggii dyvietnirn srvyyntsfs kstqmdffan ydrtfgrhqv samfgaerse
      601 snyattrlay fntpkdyqgd wrtagtvdtg nstafkgnna tmsyfgtlny syqskylaqf
      661 lirsdastkf apehywgtfp slqlgwvvsk edwfannvsa vnffklrysi gktgkdnlpp
      721 wkwiqfydlt pnkgytfgsg ggqlgssvtp kivpnretaw dstlknnfgi dmaflenrlq
      781 fnadfyydis kdmitdlssa igvpvsvggg faeenyatvn awgselsisw sdkvkgnlsy
      841 dvgvnfgygd nkivkypnqg nllpsnnasr egyssgfnpv wgfktwkgts tgdgilrtda
      901 dianywkylt dnatavggvp sylgngdptk iqkgsmafqd vagtlqndgt ltgpdgqiid
      961 kndytklaks srtytintnl gikysgfslk tqiatswgga tfvdlvsqst ssasnmware
     1021 pfwndmygtd npngkypnla aagatstsdf wqldtfrcvv rnltltydip kqvfvntkiq
     1081 nislgvtgnn lwdlynpypg hyrnmyddsg vgyptlrtws infnisf
//
LOCUS       WP_100432957            1096 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100432957
VERSION     WP_100432957.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1096
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121943
     Region          35..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqqitnify sfafacvila vlpvlaqqgn ktflvrgqvi dssdklsvpg atiaeqdaen
       61 rtisgavsdi dgnfairvkd pnnklfisti gyksqrieik gresikvllv stvesltevv
      121 visakkadng lmkiddrnrt tssisinaad laytqaasid ealqgrmagv ditadsgdpg
      181 agmqirirgt ssisgssdpl ivvdgmpyet tipadfnfgt adeqsysall niaqtdieti
      241 tvlkdaaata mwgsraasgv llittkrggv sapkitytfk qtfsktpstv pmlngdqysq
      301 lipeeymnrn gvplntltvk efqydpqdvy yfknygqntd widaitqtgk tgehnlsllg
      361 ggekaryfss igyynskgvt kgtgleklna rlnldyvvsd rirfrtdiay shndtqrnyv
      421 nnfssnddkd llrgvayikm pnmsifeyde mgnltpnyft pasnvqgtys gtynpvamae
      481 fatnnqvvdr itphfnvnvd iipkvlfstf dlqfdysstk iktflpqnat grpftetvvn
      541 rasdadidqs giitktnfvy qpdlgekqnl qvllslqtnd skstsyeamt sntasslltd
      601 psipsrtqns eltlksgygq yrsvgavtsv qyglldryii nlglradgns rfgpenrygy
      661 fpsistrwrv sgepfmknit aindlsikas ygesgrapns dyrfynvytn ystqyldlng
      721 vipsnielsn lrweklkgtn lgftlqmfkn rvmidldlyk nlttdliskd lqltsvsgyn
      781 kvdqnvgtle nkgfelnlnt tpyrskhwkv dfnfnissne ntikeiseyy psesgntdkn
      841 geykrflqvd npfgsfygyr fkgvykdlea tkatdangnk ivgpngeqvl mrfnypitdy
      901 tfqpgdakye dinhdgnids rdvvylgnsn pkfiggfgpn itlnnqfklm lffsyrlgyd
      961 vvngadmkat nmysysnqst avlsrwrnpg dvtdmpraly gsgynwlgsd ryvenasfmr
     1021 lrsvtfsyil gknlvkklrl qdvncyitad niitftnykg qdpevnmksg dpfaiaidns
     1081 stpptkrvtl gvtlrf
//
LOCUS       WP_100433004            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100433004
VERSION     WP_100433004.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111522
     Region          24..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykkllf lllllpfcai aqnkiegtvl dnvsgqpipg vnvkvkgstt gtstdfdgkf
       61 qlanvkptdv ltitymgyqs ktvtvgsqns ltvkleedsn qlkevvvqvg ygsikkkdat
      121 gavavltskd fnkgavvsad qliagkvsgv vvttaggspd stsnirirgg sslsasnnpl
      181 iiidgvaldn itpagsanpm slvnpndiet fsilkdasat aiygsrasng vilittkkgt
      241 sgtpqfsytn itsigyinkn idmmdgaafs kfiqtnfpaq tnllgiddpt ttavdnlatp
      301 qiegrilsnt dwqkviyrna vssdhnfsak anlfkkipfr asigyldyeg lvktndykry
      361 sgalklspsl ledhlkidln akvlrsekna vdeasaigsa lnmdptkpvy dtrasnifgg
      421 yyqnlnpttq niagqinpln ileqrkrpee inkflgnaqf dyklhflpsv ravvnlglea
      481 snshieevyg dyaiqtygln qttknnilnp gvnykedqti tnktlnsyfv ytlpstsgfv
      541 skfdvqagyd yqnfvvdgnk sifrynptth irepftenln ntnnryynsy niqsffgrsn
      601 vdllnkylft ftvradgssl fksdnrwgif pavgfawrmk desflknvet lgdlklrlgy
      661 gitgqqdiis vagyypttpl fspgtvtsqy lpgintysak pfddsltwek tttinagidf
      721 elfkngllsg tvdfyakktn dllakvpgkp gqsltnefva nvgsltnkgv evslnlkpia
      781 tdditwiing naayneskit dlkgvtsnpv adsklptgtg iafaynavgq apfsawvleq
      841 vydasgkpiq gayvdrnkdg iitnddkyyv alrpkftfgf gtsltyknad fsanfrgqsg
      901 gktynsrnlv agnvarafdt qantlnnild mdipfqntln gvessdyfle nasfvrceni
      961 tlgykfkelv kgldlrvyta annlfiitky sgqdpenfng idnnfyprpt iyslgvnldf
//
LOCUS       WP_100432961            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100432961
VERSION     WP_100432961.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116210
     Region          43..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkiikltcl vsiffaggle aqlyaqtakd staivpqkkv qgilvqgvvk saktntalsg
       61 iniavegfsa aisnndgsfe iqvpnlqall tisgqdfqtk vypvknrksg lnillsevyy
      121 spayqkatlp sgdimqynnt natsvidfkk eqwstpvtes aagflqsrtt gltsiknsga
      181 pnagsylalr gfnslygsnr plivvdgmiy ddedygsgii snndsspltn idvkdiedit
      241 imkdgtslyg tkgangvini tttratelst kidftmyggv nqtpdempll dadgyrthls
      301 qleatrglsq qqiaslpymn dnvgsagyyk yhnqtnwqnq vfkssinqny flkvrggddi
      361 akfglsvgyl dskgivvgtd skrysvrlna alrlteklsv danlsfinnq qnqwnqgfay
      421 ttspqylslt kapfltnriv ndagevspnw edvdyfnvsn pnaildngma tnnnyrffgn
      481 lkfnyaiska wnvssiagls fnkeretffi pdkgvtdfml ptaigknrsg sevqsyngly
      541 tdtfasymkt fyndhnldvr fgfraqsnkt etdlglgyns stddftsvta gssllrqvgg
      601 algewhwlnm yasgnynfrn kyfltanyav dgssrfgdda stgaskyalm tsisgawlis
      661 sedfmkgind vdylklrvgf gtsgnddign ysaqtyyvsq nllgmqglvr gnigntnlqw
      721 etvtktnlgv dfglfkerin gtfdvfsnkt snmivyekta aengfdsves nsgamrtyga
      781 elgmnariin tpdftfdfgy kvshynnrvq nlpsgdilte fggatyltsv gkdanlfygl
      841 nsngvystta eaiadglskr ltngnlvpfs ggdmrftdvn gdkviddkdr mvignpnatv
      901 tgsfstdfty krfslkalfn fsagndlyng mrynlekmgg yenqsaavan rwraegqqtd
      961 ipkavwgdpm gnaafsdrwi edgsylrlkn lvigydvpvn dskhikyiql yatannlltf
     1021 tkylgfdpef satssifgqg adiglapqft syqlglrlgl
//
LOCUS       WP_100433131            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100433131
VERSION     WP_100433131.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115334
     Region          32..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 melkfncqks askivllffm ffsfgyigaq skikgtvkdv aglgipgvsv tqkgtknmvg
       61 tdmdgnysid lkdngqhvlv ftsigfkrve esvqgrttin valaednqvl eevtvigygt
      121 qkkklttgam sslktesfte rpisrvdqgl igqvagvrvk ttsglpgqpf sveirgggsi
      181 tagneplyvl dgfpiyteps nanggfsngs pldninpndi asvevlkdaa aasiygsraa
      241 ngvvlittkk gklgktkfsf ntygginkea nrvdmlssqq widrskvmld aqwaasgisg
      301 asasqtmper iatynltnpt tplnptntky ysyiydarwd ipghpgldyi dwqdkvfqtg
      361 eftncqftas gatdavnyyv sanyqkntgy ivgtdytvfs aranvdikls dnfkmginla
      421 psysikndpg vegkdntlfk altatpvfes tsnaagekyt tryawgsstt nmlnalnrtg
      481 knsmyrnlis tyatyqfvkg ltwkstinfd nsdntfegyt pndvissirg tyntyrrqni
      541 vnentlnydk slgnhnfnvl lgqsfnsyei mkstltsgal ynsssietlp agsigstsge
      601 kntllsyfar lqynykekyl lsssirsdgs skfgserrwg tfyslalgwr ikkeafldnv
      661 dwlsdlklrt slgtngsnni gsyawrstla tynysiggaa aigqgvsgia npelhweesk
      721 sidfgldfsf lknrisgtfe vyrkdnsdll lrvpvptasg fpsyltnige vqnqgwefei
      781 ntvnitakdf qwktsanish nenkvlalgp dqtkieisng fdggvpfikl evgkpmytif
      841 glqqngvvtq adidkggtti ggkslvlgdp ryidqnadgk insvdrvdlg nptpkftwgi
      901 tndfkykdld lsilvqgqng gtvygltgra idrtgmgqve nsldvdpavr gnwrttfgyq
      961 ansdwlyksd yisvrsisvg ynlkeavkni kridnirlyv tgenifyrnk ykvgfnpeai
     1021 ntsgssnndf avpvdyggtp laksvvlgvn infn
//
LOCUS       WP_100433315            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100433315
VERSION     WP_100433315.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113554
     Region          25..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngllv llvvlvaqlt faqersvsgi vsdnagmplp gvsvlvkgtk ngtqsdfdgk
       61 yainakptdv lvfsyigmkp seksastttl nvklasgatq lesvvvtafg ikrkpkdlgy
      121 svssikaeei tndaepdlvr slngkvagvn vgvstgvaga anritirgvt sfsgnnqpli
      181 ivdgiaysdp qvttssqvtg gggyesalss ldpndiasvd vlkstsaaal ygsravngvi
      241 vittksgsps skktnklsvn vgsaaylenv nnlpdfqnty gagsnfnysn sngswgprfd
      301 slatiptwpt llaafpsqfg ptvpyvakpn nvkdlfrtgt vtdntvgfny sgeegsfnat
      361 isnmaqdgyi pyntydrtgf svggnfklan kltvganmsy sgtkqvgaff genqfdgaas
      421 sfartmflar nwdmnlpyed angasvtpng tqfdhplwsw khdqiithtn rtvggvnlny
      481 efnenisaty ragmnrytld rnqirdlhsr adggvgsltn dkftnedies tllvnfdykl
      541 sddfgmksil ganflqnnns rlafygkgfs vpnvftfgnt lnvsnladyr fekrniglfa
      601 dvtfsfkdyl flnatarndw ssslpksnns yfypgvnasf iltdalhmdn diltfakirg
      661 gwakvgkdav seftsatyal gnsyngnpti anptdlgdqn vkpefteeie fgtdleffkk
      721 rialglsvyk ktstnlitpi tvptstgylt yntnlgamvn kgleieltlv pvqtndfkwt
      781 lfstftkndn evtklkdgld rfnlqantva yvqkgeaygv fygskfardd egnflinqsg
      841 ggiiadptpg iigdpnpdfk msfintfkyk nftltaqfdy rkggdissst iesllgrgvt
      901 kdtedrekty iipgyygdsn gvaivdasgn kipntvqlsm nelyfspagg ntfainsvde
      961 adiydgtvfr lrdvnltysl pqemlkkspf gqvsisllgs nlwyfapnvp khtnfdpdtt
     1021 sygstniqgi evsaaptarr fgvklnltf
//
LOCUS       WP_100433317            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100433317
VERSION     WP_100433317.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115984
     Region          27..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfnglla lfvvlvaqit faqerfvsgv vsdnagvplp gvsvlikgtq ngtqsdfdgk
       61 ysikaqpsdv lvfsyvgmkt tersassttl nvklasdatq lesvvvtamg ikrekkslgy
      121 ssqqvegkdl nggtaspnva nllsgkvagl evsrntnfgg stnvvirgnk sltgnnqalw
      181 vidgvpvdns nsnalaqltg gggydygnti sdinqedies invlkgaaat alygsrasng
      241 vvmvttkkgk atkdnkvgft fssnasigtv dkstfpeyqn kygsgygfgs sflgtgtpdt
      301 vdtsndasyg dafdgtpvyq wdaftpyspn fgkatpwtaa kngpitffnd aktytnslsl
      361 ekstdrssls msyvntnqtg ilpnselkkn qlsarfsqki tdkltanvya avtlqntigr
      421 nstgyndnim gnfrqwwqtn tdiksleqvy kasggqnvtw nwsdptspeg ltpaywdnpy
      481 ftryqnyssd ertrlfsyas ldykitdwms algrvsldty nqlqeerrav gsipsafgls
      541 padeasgyqr ntinfqevny dlmlnfnkki genislngvl ggsirrtdkd nvlastiggl
      601 vtpgiyalsn sryelpfpke qiinagvngi yaqgsvgyld tyfidasirr dasstlpkgn
      661 nsyvypavsg sfvfsnvlks dwlnlgkvrv nyaevgndap alslvntynr npnfqdqpvy
      721 tnaltnpfrs innnpnlkpe rtksfeigle ssffdrrlsf datyyktnsv dqivaaavss
      781 asavtnayvn ggnienkgle lqitgtpirt kdfswditvn wsnneskvvs lpdgvdnlql
      841 gsfqggvtvn atpgeaygtl kgtdyvytng ektidqatgk ylittsatnn ignvtpdwmg
      901 girnkftykn islgflidtq qggdifsldm yyglatglyk etavdniren gilnagvapn
      961 gtpntvvvkn pgtfsnnygy lvepnkafvy dasyvklrev sitynfpktm fegtfvnsas
     1021 lsllgsnlwi isknlpyadp esglssgnss rgysvgslpt trdigfnltl kf
//
LOCUS       WP_100433319            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 1].
ACCESSION   WP_100433319
VERSION     WP_100433319.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 1
  ORGANISM  Flavobacterium sp. 1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Flavobacterium sp. 1"
                     /db_xref="taxon:2035200"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113897
     Region          25..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv llvvlvaqlt faqersvsgi vsdnagmplp gvsilvkgtk ngtqsdfdgr
       61 ytikaqpsdv lqfsylgmks seksasstsl nvkltsnate lesvvvtamg ikrerkalgy
      121 atqeiksgel tkgsnnslag alqgklagvt itpssgapga ssqivirgar sftgnntply
      181 vvdgmpiast adystgnsvt gsdsanravd idpndiesin vlkgqaasai yglrasngvi
      241 vittksgkgt skngkptinf sssitadnvs rkidyqneya qgsgnlfnpt ssltwgpkis
      301 elpnstgygg nvsnalnggd itthagkyyv pqratagldp wvtpqvydnf geffktgitv
      361 nntfsltqst eksnyaftfg ssnqngfipa tgfdrynakg afstklgndw ktgfvgnyvq
      421 tkiekatgan dssvagafas prsydlkgng yenptdpykq iyyrpngfnn pywaaahnkf
      481 deqtdrfygn syvefapkis tddihkisfr yqlgadaytt dyrdikefgn aqttaghlei
      541 ygitsrtvns lftvnyeyki sddlnltala gneindryek sysmtgndln fggwpnlknt
      601 kqtiasdnia knrtfglfgn lnlsyknfif lgttirkdiv ssmprdnrsf vypsvslglv
      661 ltelealkgn silsfaklrg swaevgqagt yyanfysvps ysggfwqnsp vsyplggvns
      721 ytpnnvmydp nlkpqntksy evggelrlfk dlisidytfs rqdvvdqifq vplagstgaa
      781 tlvmnggkih tnshelivgi tpvkttnfew nvsanytqid nyvdelkegv pniflggftt
      841 pqvrasiger fpviygtafk rddkgniivd anglalsget kslgevapkf nlggttsfry
      901 kkltlaatfd wknggkmysg tnslldtygl stktgnrdel miqegvtesg avntkgatkq
      961 dtytrysnia etaiydasfv klrelslgyt mpqfskgfdv rlsafarnil lsskipnldp
     1021 essqgnnnia ggferlsipq ttsfglgmnl tin
//
LOCUS       WP_100475565             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacteroides abscessus].
ACCESSION   WP_100475565
VERSION     WP_100475565.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37286
     Region          6..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdqpvtigv vresgederr valvpkaiag ligkgvnivi esgagerall pdelyteaga
       61 tvgdawsadv vvkvappaaa evarlrqgqt ligflaprna ensigalrsa gvqafaveai
      121 prisraqvmd alssqanvag yksvlvaase strffpmltt aagtvkpalv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwldlgida ageggyarel tdeerqkqqq
      241 aledaikgfd vvittalvpg rpaprlvtaa avqgmkpgsv vvdlagetgg nceltepgqt
      301 vvkhgvtias plnlpatmpe haselyakni tsvlellikd galapdfdde ivagscvtre
      361 vs
//
LOCUS       WP_100485112             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacteroides abscessus].
ACCESSION   WP_100485112
VERSION     WP_100485112.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37286
     Region          6..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdqpvtigv vresgederr valvpkaiag ligkgvnivi esgagerall pdelyteaga
       61 tvgdawsadv vvkvapptaa evarlrqgqa ligflaprna ensigalrsa gvqafaveai
      121 prisraqvmd alssqanvag yksvlvaase strffpmltt aagtvkpalv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwldlgida ageggyarel tdeerqkqqq
      241 aledaikgfd vvittalvpg rpaprlvtaa avqgmkpgsv vvdlagetgg nceltepgqt
      301 vvkhgvtias plnlpatmpe haselyakni tsvlellikd galapdfdde ivagscvtre
      361 vs
//
LOCUS       WP_100499881             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus chilensis].
ACCESSION   WP_100499881
VERSION     WP_100499881.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus chilensis
  ORGANISM  Geodermatophilus chilensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Geodermatophilus chilensis"
                     /db_xref="taxon:2035835"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52909
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpretr pgetrvaatp ttvrqlialg hdvlvetgag aaasfpdday reagarvgta
       61 edawgadvvl hvakptpeev grlhggavlv stlapaldpd llatlaarpi talamdavpr
      121 israqsldvl ssmaniagyr avieaahafg rsftgqvtaa gkvppatvlv vgagvaglaa
      181 igaasslgav vratdvrpev aeqiasmgge yvgvpadeap sgggtgyasv tsedydrraa
      241 amyaeqarev divittalip grpaprlite emvasmkpgs vivdmaagqg gnvagsvpde
      301 vvvtpngvti igytdlpgrl pgqasqlfgt nlvnlvkllt pgkdgrlvld lddvvqrsmt
      361 vvrdgellwp pppvqvsaap aaapaarppa pvarpkaprs partaavvgv aalllflaaa
      421 fspnqlignl tvfalavvvg fyvignvhha lhtplmsvtn aisgiivvga llqmghtsal
      481 vtvlatvavl vasinvfggf avtrrmlgmf trgparatte r
//
LOCUS       WP_100504288             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter ruhlandii].
ACCESSION   WP_100504288
VERSION     WP_100504288.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter ruhlandii
  ORGANISM  Achromobacter ruhlandii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter ruhlandii"
                     /db_xref="taxon:72557"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38311
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkyvggk htvvvergag taaryldeay eaagatlgsa
       61 healgaelvm kvrapsaael pqmkagavvi gmldpfdaeg laqmaaaglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgvggy arpmppawma
      241 rqaalvserc kqadivitta lipgrpaptl vsaetvaamk pgsvlvdlav erggncplse
      301 kgkvvekhgv tlvgltnlpg lvatdasaly arnildflkl iinadgalai qrddeivaac
      361 lvceggnvtr gs
//
LOCUS       WP_100515741             360 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium goodii].
ACCESSION   WP_100515741
VERSION     WP_100515741.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium goodii (Mycobacterium goodii)
  ORGANISM  Mycolicibacterium goodii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Mycolicibacterium goodii"
                     /db_xref="taxon:134601"
     Protein         1..360
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37150
     Region          4..355
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,71,90,283,309,311)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,273..274,316..317,321,
                     324..325)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,223,234,
                     251..253,260,262)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtligvpret aegerrvalv pkvverlsak glevvvessa gagalfsded yeragatigd
       61 pwpadvvvkv npptsdeisq lkpgsvligf laprtqpela srlrladvta famesipris
      121 raqtmdalss qanvagykav llaaslstrf vpmlttaagt vkpasalvlg vgvaglqala
      181 takrlgaktt gydvrpevae qvrsvgaqwl dlgidaageg gyarelsdae raqqqqaled
      241 aitkfdivit talvpgrpap rlvtaaaasg mqpgsvvvdl agetggncel tepgqtivhh
      301 gvtiasplnl patmpehase lyaknvtall dllvtdgava pdftdeivsa scitrtegdi
//
LOCUS       WP_100516344             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium goodii].
ACCESSION   WP_100516344
VERSION     WP_100516344.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium goodii (Mycobacterium goodii)
  ORGANISM  Mycolicibacterium goodii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Mycolicibacterium goodii"
                     /db_xref="taxon:134601"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52190
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl saetrvaatp qtvgqiiklg yavvvesgag aassfsdaay vqagaeigda
       61 wdadvvlkvn apddaeigkl rdgatlvsli spalrpdlve klsarpitvl amdavprisr
      121 aqsldvlssm aniagyravv eaahtfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivra tdprpevadq vaslggeyla vdpeaaevsa tgyakemgdd ykareaalya
      241 eqckdvdiii ttalipgkpa priitaemva smkpgsvivd maaanggnve gtvkdqaivt
      301 dngvtiigyt dlagrlpaqs sqlygtnlvn llklltpekd gkvvldfddv vqrsitvvrd
      361 geitwppppv qvsaapaaaq paaapvvked kqpmstgrrl glafsaaavl fvliaaspaa
      421 lqvhlvvfal aivigyyvig nvhhalhtpl msvtnaisgi ivvgallqig hhhtaitala
      481 fvaillasin vfggfavtrr mlamfsrs
//
LOCUS       WP_100558650             441 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Brucella
            pituitosa].
ACCESSION   WP_100558650
VERSION     WP_100558650.1
KEYWORDS    RefSeq.
SOURCE      Brucella pituitosa (Ochrobactrum pituitosum)
  ORGANISM  Brucella pituitosa
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Brucella pituitosa"
                     /db_xref="taxon:571256"
     Protein         1..441
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45711
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifipke sdpnetrvaa saetvkkfia lgfdvvvekg ageksriidt efsgagarig
       61 taadakaadv ilkvrrpnda elkgyksgta lfamldpygh eeavaalgka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaset ydrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedee fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vtkemvaamr pgsvlidlav erggnvegai
      301 agqvadvngv kivghlnvpg riaatasqly arnlyaflet lvdkeakllk ldpeeelvka
      361 tllthegkiv hpafakaeae aapavvtekv akpkaapkak apavkaeaak eaasatakpv
      421 akttrkapak aaktsadgge a
//
LOCUS       WP_100602072             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. CB02959].
ACCESSION   WP_100602072
VERSION     WP_100602072.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. CB02959
  ORGANISM  Streptomyces sp. CB02959
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Streptomyces sp. CB02959"
                     /db_xref="taxon:2020330"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52223
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtvgvlkear agenrvsatp atiesirklg ydvivdsgag vaagftdsay qaagarigda
       61 taadvvlgvn apspqqldrv rpeatvialf apafdpamve dlgrrpftvl smdavprisr
      121 aqsmdvlssm aniagyravv eaahefgrff tgqvtaagkv ppakvlvaga gvaglaaiga
      181 sgalgaivra tdprpevadq vrslggeyls iespeaevsk tgyakemgdd ykareaelys
      241 aqcgeadivi ttalipgrpa ptlitaetva gmkpgsvivd maaanggnvv gtvagekvvt
      301 engvtiigyt dlagrlpaqa sqlygtnlvn llklmtpgkd aslvldwddp vqrsitvvre
      361 gelawppppv qvsavpspaa aaaaaatesa kpkkapmtaa rrfgavalsa lalfliagfa
      421 paallphvtv fvlaivigyy vighvhhalh tplmsvtnai sgivvvgall qignsstavt
      481 alsfvailla sinvfggfav trrmlamfnr s
//
LOCUS       WP_100610642            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Confluentibacter lentus].
ACCESSION   WP_100610642
VERSION     WP_100610642.1
KEYWORDS    RefSeq.
SOURCE      Confluentibacter lentus
  ORGANISM  Confluentibacter lentus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Confluentibacter.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Confluentibacter lentus"
                     /db_xref="taxon:1699412"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119704
     Region          25..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lllafvvqlt faqektvsgt vidgsglpip gatvlvkgts tgtssdfdgn
       61 ysiranqgat lvfsfvgyvt kevavgtsnt invslnedvq aleevlivgy gtstkksyag
      121 taatisaenl eaksfsnvtq alagevagvt vintsgqpgt vatvrvrgyg splgnrsply
      181 vvdgiplagn felnsinpad iksttvlkda tataiygsrg angvvllttk sgssaeagyi
      241 evdvktgvnt qiipryqvvs speeyigyvw egiynrgvvt gqanpidyan nrllgdngig
      301 agynmwnaat gaalidpvtr tvrtgvsrlf tpekyadlaf gtgfrtetnl rmgggseksk
      361 yfvslgyldd kgysinsdyk rytarlnlns dvkdwlelsa nfayaysest nngqidgaen
      421 lfefadkmap iypvyarypn sgeliadpiy ggfqydygsp tggttpdpsr aftrnrpnan
      481 llnpigsall dfdgrqtnai ngnlsanikl tdfltlentf ggqysflrrn nasnhvygtg
      541 antngnitvt dqvrwtqtfl qllrfnksfg lhtiealaah etfeqsfiqs rafkqnvilp
      601 gvyrlnnyle sssppdgyed gsglesyfgq vnysyadkyy ltgsirtdgs srfvddqwgv
      661 fgsvgaawvv seedfmadsf isylkakasy gitgdqqgvs tvlgfdtfna nfvggalaid
      721 lrntgaaglt wetskmfqag lemslgnyld vnidyyrknt dnlffqqrrg psagiatitv
      781 ndgvvlnsgl efdltghiin kedfkldism ngeilsnkml empldpsngl pkiidsgsst
      841 daafyayaeg ksifdiwmre wagvdpadgr pmwyqyyddv nnnntldsge gtffidngnn
      901 gnanlsgslf eyqqrasntn ikktvtktya natqtyinks fipdlrgafr isgqiknfdf
      961 stqftysigg yaydaqyael msdrfgaagn nyhkdianrw qqpgdvtnvp llsdnavins
     1021 tststrfits tdfialnnar igytlpskfa sraglnsvnl wvsgdnlfin svrkgfnptv
     1081 tevgnsarqi yapattitlg arvkf
//
LOCUS       WP_100627440            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            formosus].
ACCESSION   WP_100627440
VERSION     WP_100627440.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus formosus
  ORGANISM  Algoriphagus formosus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Algoriphagus formosus"
                     /db_xref="taxon:2007308"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112776
     Region          26..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilsisyg lafmllfsiq aysqtriltg tvvgeadglp ipgvtvldkt nqtgtttdvd
       61 gkysisvsdn svlvfsfigy asqeftvgnq siinvtlaed iselgefvvt sfgmernqka
      121 lgysvtqlgg dkftesrtvn vgnaltgkva gvnvtppatg aagstrvvir ggssltgndq
      181 plyvvngvpi esgnlgsagi wggndggdgl aainpddies ltvlkgntaa alygaraang
      241 vilittksgs arkgigisfn snftmesvvd etnfqriygp gengrkpltq deainnaing
      301 wgapydgsqt vqfdgvqrpy sylgedfndf yrngmtwnns ialsggnent tyrfafsnlt
      361 nndvvpnagf drnvaninvn skqgkftlav tgqyskqtat nrprlsdspg nanfsmvvkp
      421 gniplsvikg dpnkpgalpd gnelryqsnv fqtnpywavy qwgredvtdr imgnmslryd
      481 ftdwlyaqgr fgtdfqirde yafeaygtaf kprgsynttm rtiqetnadf ligfdktfgd
      541 fsvdgflgsn imrrtiesqr gggndlvvpf fhsvtnvaap tfgygfselg insyfaaanv
      601 gyknviflnl tgrqdqfstl spansklfyp svglsavisd mivlpefvtf akirgnwgqv
      661 gggapnpyal nlqyglvgag hlganlgqin ngsipnsgls pytsteyeig adlrffenrl
      721 gidvayyrrr ttddilnqgi satsgfgstt vnigelenrg iellinatpv iagdfqwnis
      781 fnfannvsev lslgtnaagd pvefinldea rtrrerirhi vgqplgmitg fkhleidgqk
      841 vyddngfpvt tpgfetiaeg rhpisggitn tftwkgfrlm tlidfrsggs vmsgtnyfay
      901 qfglhqntlq grdgnltvsg vtpegtpgtw tipadpsdpn nylidqywqr yaqvtenvvy
      961 dasfgklrel sfgytfprtf vektpfqsls lsfvgrnlai lwskvpnidp eaaytvsgns
     1021 qgleyfavpa nrsfgfnlsa nf
//
LOCUS       WP_100616307            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Confluentibacter citreus].
ACCESSION   WP_100616307
VERSION     WP_100616307.1
KEYWORDS    RefSeq.
SOURCE      Confluentibacter citreus
  ORGANISM  Confluentibacter citreus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Confluentibacter.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Confluentibacter citreus"
                     /db_xref="taxon:2007307"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117023
     Region          25..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lllafvvqlt faqektvsgt iidgsglpip gatvlvkgts tgtasdfdgn
       61 ysiratqgat lvfsfvgyvt qevtvgasns invtlsedvq sleevlivgy gtstkqsftg
      121 tattidaeni elknysnisq slageaagvt vintsgqpgn tstirirgfg svngnrdply
      181 vidgvpysgs lnainpsdik sttilkdata taiygsrgan gvilittksg tssesyvevd
      241 vktgtnvqll pryqvitspe esialvwdak vnrqrltgdp npintvnntl ftsilapgyn
      301 mwnvangael idpvtgqvrp gvtrrytpes yedlsfntay rteanvrmgg gddkskyfis
      361 ggylnddgya intgykrytt rlninsnvke wlnvganlsy tysesinngq tdgaenlfef
      421 adkmnpfypv flrdnngqlv pdpifggnqy dygsnsgfrd rpnsnnlnpi asalydfngn
      481 drnevvtsfn lgiditeglt fesiygaqys nnifksvgnq fygvataneg dlfqstteri
      541 ttnflqllry kkefgkhsve ilaahesnky dqsfatafks kaiipggkel dnyivnlqqp
      601 tgrteartle syfsqlnydf ddkyyltasv rrdgssrfan nkwdtfysig gawilsnesf
      661 lndnnlltfl klkgsygrtg ddagvdiysg intfgvtnvg grfavapelf anpdltweta
      721 nqyqvgvefs lgtfldatvd yyikdtenli fnrrispssg vatltvndgv lrnsglevdl
      781 vahlvktadf kldltvngam ynneiktmpi dpqtgapaah nivglygysq grsiydfyir
      841 eyagvdpadg ypmwfryfdd vnsngifdag dttitsltpy latnpdanva kattktyans
      901 tqvfvnksgi pdvagafrln atfhnfslst qfaysiggwa ydsqyaelmh dnnggitatn
      961 shidirkrwq qpgditsvpl sadrvipnvn ssstrfitkt dflalnnvvl gynfpeetld
     1021 rigmsglnly vsgdnlyftg arkgfnptts edggsdrgvy aplttftlgv rakf
//
LOCUS       WP_100627662             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus formosus].
ACCESSION   WP_100627662
VERSION     WP_100627662.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus formosus
  ORGANISM  Algoriphagus formosus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Algoriphagus formosus"
                     /db_xref="taxon:2007308"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40705
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,72,91,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtigllkepe genrvallpe sakaliqlqv qiivesrage kafasdkdye aigasihsra
       61 evlqadlilg iqppseeeql slkdrqvlvc lfqplsnkel verfldkkit sfsmdnvprt
      121 traqamdvls smatvagyka vlmaashspr ffpmfmtaag siipskvlil gagvaglqai
      181 asarrlgavv eafdvraaae eevkslgakf vkvegakdea saggyaveqs eeykakqqal
      241 iqehakksni iictaqipgr kapvlitket vaemapgsvi vdlaastggn celtennqii
      301 ekhgvtiigd snlpgtmpmd askmygknmv nflkliigke gelmlnwedd ivqntcvthq
      361 geirservkk ilypsein
//
LOCUS       WP_100628262             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            formosus].
ACCESSION   WP_100628262
VERSION     WP_100628262.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus formosus
  ORGANISM  Algoriphagus formosus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Algoriphagus formosus"
                     /db_xref="taxon:2007308"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109228
     Region          30..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnylqqfkt lafaltllfg vsflanaqnr titgtvldas lgdpvpgatv lvkgttrgva
       61 tdldgkftld iqsgdqilvv sfvgyltqev eignqssfti nleediqsle eavvigygsq
      121 dkkeitsavv gvkpedfnrg nvanpaqllq gkvaglsitr pggnpnagfn irlrglstfg
      181 anssplivld gvigaslenv dpndiqsidv lkdgsaaaiy gargssgvil itttkkgske
      241 graevsinsf gtldqatnli pvlspeefva rggtdfgset dwrqelirda ysyttnasis
      301 ggfnntnyla svnyrsnngv akgisnerln trinlsqaal dnrlrfnvnl sfttvesnsv
      361 pesafryati ynptapifed tedanqrfgg yfqrdlfdff npvalinqqr gineiktalt
      421 syrveydflp nltlsaqyse drrnelignf wsiqdfqvgf gargsaerit ndrvqrifes
      481 tlryevdlfd glnlallggv gtqttknqgf garsrqflfd tgwdnlgaga lrignftnmy
      541 syanqdqlns vfgranfnyn nflffsasvr aetysgfgpe nqtgvfpafs lgsdftqifd
      601 mgvfsqfkpr vsygvtgnlp psptlalgvf gngnridldg dplstddiyv giiqnsnpnr
      661 flkwetkref nvgvdfgiwd nkvtgsmdyy trnisdllfn vpvgggpnif dpgrfntvgs
      721 twvnladlsn agfefavavn glnlgevlwt psgnftiyqk tqieslsasg lgfdelrfat
      781 pgspgqnnnp iiynrvgqtl gdiygprllg lsesgeyils ttnpdeferl gnglpkgefg
      841 fannfawrnw tlnfflrgvw ghdlynsyrg fyenadgasv twnsvitekt ptnpvvtstp
      901 tfnssyveda sfirldnmel gynfrtnspn igsfrvyfaa qnlftitnyt gidpearvtd
      961 senddnftta lspgierrdq yfqtrsftlg lslnfk
//
LOCUS       WP_100629981             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            formosus].
ACCESSION   WP_100629981
VERSION     WP_100629981.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus formosus
  ORGANISM  Algoriphagus formosus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Algoriphagus formosus"
                     /db_xref="taxon:2007308"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107528
     Region          25..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkfyklslp llflwlstgm awaqisvsgt vtdertsepl igasilikgt ttgtitdidg
       61 nfslsiqnad gatlvvssig yltkeinvss smsnlniqln qdatnleevv vtglassvkr
      121 snlanavstv sakdltgttt iqttdgalyg kvagatirsn ggapgggmsi qlrgisslsg
      181 asqpliivdg vyisnatqrt grasvtgagg snqddganrl adlnpadiet ievlkgpsaa
      241 aiygtranag viiittkrga egrttvslsq digfaeplrl lgvddwsedk infffpearr
      301 plelerfraa qssgnfidye dffynnqatl lntrvnvsgg nektkffvsg nisdeegtvr
      361 ntgfqrysvr anidhkisna irlgvssnyi qsntdrgftg nqnntgasig ysiayvpnyf
      421 dlrrnadgty pvnpyfsdnp vavtdnavnn sevnrfiqaf tldidllkte nsfltaniag
      481 gldflqnrtl iylpeflqfq raqanpgdvl kgkqesfntn fqaalvynwf lgkvnmnsqa
      541 glvrldfnns alfnrgrglv pgqtnlgqaa iqeinqefns evqeagiflq qeanfedkii
      601 gtvgirwdks tlngdpnqyy afpraslavn lanfdfwsss vfnqvkpria ygetagpvgf
      661 gatftplggt niggllgsvv stqigntqir petatelefg vdvgmfnnrl sleatyyikn
      721 tqnniqslrl spatgvnttp sneaelqnkg ieialsgniv enpnfkwfsr ilfwrnqiem
      781 trlgiptyta gafgaglgtf lyaegysptt ivgtpadpnv pggftiwgns qpdfnlsffn
      841 nfsiykglel siltdwrqgg dninltsflt dsggttngwf dddngdgvpn grqrepepyn
      901 nagrwvqdat fvkireigly ytipratiqe wfgsavqnir vggsvnnafl ftnyegydpe
      961 tstfgaqava nnvdiapypt prrvffhlti df
//
LOCUS       WP_100628425            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            formosus].
ACCESSION   WP_100628425
VERSION     WP_100628425.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus formosus
  ORGANISM  Algoriphagus formosus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Algoriphagus formosus"
                     /db_xref="taxon:2007308"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115964
     Region          25..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkallfvva lftmtlsyev saqqrvitgq visdedglgl pgatvlvkgt tvgtttdldg
       61 nysisvpdgg tvlifsfvgl etkeevignr svinvtlttd aeqlsevvvt aigierekka
      121 lgyavtsvgn eqlenrpeqd varvlqgkvp gvnitstngm sgsgtnmvir gyssatgsnq
      181 plfvvdgvpf ntstnaqngf ttggattssr fldidpnnie nisvlkglsa tvlygdqgrn
      241 gvilittksg askrraaevt inqsvftnea aslptygtiy gngfqqapgf ffsnfgprmd
      301 egrtvnhpya tssvqavrea fpefweggiv ggtpvqyeyk ayadpsevff rtglisntsv
      361 qvaggsdrts fnasfgytde egftpgnnlk kynfglgins avndkltvks sftfaitdle
      421 sppvnaafgs gpsggipsaf ahvlytprsv dlgglpfenp idrssvyyrg gndivnplwl
      481 vryyqntsdv nrffnstsvi ydinddfsit yrigldtyte lqelkynrgg psaslattsg
      541 yyrssniqnt iwnqdliinw kkqfsdkfgm saliggnsry dsysqngvas qgqlafglfr
      601 hsnftqsssn daysganlnf teeerrmgvy anvtldydsy lfvnlsarnd wtstvepenr
      661 rilypgasvs flpgtafnwn sstvndlklr lgygtsagfp rpyrtrnvlv qsarafdrdg
      721 svtqthsvan tlgnpnlkpe lheevefgve gvmfnnkltf dlslyqkntr dlitqspidp
      781 atgftstain igkirtrgie fqatvnpvst asgfnwnsti nwglyrsvtv elgggleevl
      841 vagfttlgnf aipgepfnii kglgfdrdeq tgepiilsng lhkpaadlqv lgdpnpawtg
      901 swinsfsfkg ftlsammeyr hkgavfsntv tatlargvtk dpvadreltf impgvkedgt
      961 pndiqitasd yffagyqgat depnvfdgsm irlrevslgy eipmnlmakt pfkrasials
     1021 gtnlwflaln fppnmnydvd vlgtgvgngl gfdfvtgpss rrfggtvtlt f
//
LOCUS       WP_100630028            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            formosus].
ACCESSION   WP_100630028
VERSION     WP_100630028.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus formosus
  ORGANISM  Algoriphagus formosus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Algoriphagus formosus"
                     /db_xref="taxon:2007308"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112852
     Region          25..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknyykfmll fllscstvgm smaqqtvtgk vttqedglpl pgvsvvvdgt tngtvsdidg
       61 nysisvpnsd avlvfsfigf etqrvsvgnt svinvimkke esqldevivt afgisqekka
      121 lgyaaqsids eaitktrqqn vvnalqgqva gvqvtnsgga pgqsariiir ginsldpsad
      181 nqplfvvdgv pvdnstvesg gtprgmsnri adinpndies msvlkgaaat alygvraang
      241 aviittkkgk agqirvdfns slgfdrlvkk prlqdeygqg fsgerndssf wpswganiae
      301 endpdyvyqn nwerafdtgi qfdnsisvsg gneqatfygs fgrldqngii pfsnwdrtsa
      361 klsgtikvse kfnfsgsmny insggnrvph drflermmyw settdvrdyi nedgtmrtyg
      421 ntnpiydarf atyednvnrv igninlnysp tewmtlsyrl gvdnysdsrt eitpgpkgid
      481 gevalsstgf ieetrinsrd itsnfyitlq kqwnsdwntt lrlgndifer kfdrvtatgs
      541 nfvipdffnl nnttqifasq gksirrlvgf ysdlmvdykn flflnvtgrn disstlpknn
      601 nsffypsvnl gyvfsenfdl pswvtfgklr aswaqvgkdt nphilgsffv spsvfplngq
      661 vgfsrnsvfg dpnlrpeltt slefgaqfaf fnnkanldvt yyktnskdqi ipvpisdatg
      721 fssyitnage ienrgwefvi ggtpiergdf rwdvsanltt naneivaire gieqivvgsq
      781 fgyagstvtm ileegeaygn ifgssyvrpg apegateldr glpqligang fpvrngnqlv
      841 lgnavpkffg glrndfsykg fefsflidfr sglqqydqfg nflsafgkqe dserrndfvv
      901 fpgvladgsq ntqevwlgqg vgpdgvnyga gywrnhyrgv senfvkdadf iklrnitlay
      961 nlqpnvlert pfrtarisla anniilstpw dgfdpesfsa gaggnavgft glgfpgvqsy
     1021 fvtlnlgl
//
LOCUS       WP_100630303            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            formosus].
ACCESSION   WP_100630303
VERSION     WP_100630303.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus formosus
  ORGANISM  Algoriphagus formosus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Algoriphagus formosus"
                     /db_xref="taxon:2007308"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119032
     Region          29..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnpkytktwk vligllllfg qsfaqeakre isgvvrdvmd rsplpgvnli vkgstygtvs
       61 ddegkftlsi pegeavllvs yigyesqeis lvanqaflei glspldlnlq evtvvssgfq
      121 elplsrstgs yvginqelvd rrvstnlidr ledvtpglif nrdisgiesg esisirgtst
      181 lissaepliv vdnlaydgpl ssinpndves itvlkdaaaa siwgaragng vivittkqgk
      241 ygkplqvnlt snftafervn pfydpkmsin slidkqldly engafnslir nrrnpvippl
      301 aetlyafdqg liseqerdla iqqfrnsdir rdidrylrrp asqqqyalnl sggsrnhhyq
      361 vsmgydknls seidadfsrl tlsaqqswkl akerltvstg aywvqsessn gmpqvsglfp
      421 yerladeagn pvevyrdysv rfknsvsdil plswayvple eigrsntrir sndlrlftal
      481 nyrildgldw svnyqywtnq gqnnihnnpd syearnlins faqplgngev dlpvplggfl
      541 dqrisnsysh nlrtqvnyqk kwddhrlnvf aggeikdfqs efygnrsygy laenaaslpv
      601 dyltrfvnqg snrsrnipfv eefggrvdrf vsafgnlgys fqdrflvnas lrrdasnlfg
      661 vntnqksvpl wsaglgwvis eegfldedwi dflklrlsyg fngntnpnat avstarrfva
      721 gqnlitrlps laiqtppnpe lrwerikiin agldfeflns rvsgsaeyfq ksgldllgni
      781 pifissgftn atlnyastrt kgwdfvmnti ntkglvrwet nffhsvlndq vlevenlpta
      841 nqlinytpal ptpqigrplf siysfpfagl dasdgaplgi vegepsrdys tifaeatpen
      901 iqfhgsgrpt nfgafrntvr ykgfslsani tyrlgyfvkr sgvdyidinr ggfghadyes
      961 rwqqpgdeli tsipadpgti dplmngfyls saalvergdh irfqdlrigy dwqptnkgag
     1021 ifrqlesyiy innlgilwka skalpdpdfq vsqnlrsvai gfrasf
//
LOCUS       WP_100637827             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter salexigens].
ACCESSION   WP_100637827
VERSION     WP_100637827.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter salexigens
  ORGANISM  Marinobacter salexigens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter salexigens"
                     /db_xref="taxon:1925763"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56073
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkeif tderrvaatp psvhkliglg yevvvesgag esahyrdeay eavgatiaed
       61 ttslwgeadf ilkvrapmln palgkheadl mkegaflvsy iwpaqnsdll nqlagrkitt
      121 faidslpris raqkmdalsa maniagyrav veaanhfgrf ftgqitaagk vppakvmvig
      181 agvaglaavg aanslgaivr afdtrlevke qiesmgaefl qldfgeeegs gtggyakqms
      241 defikaemal faeqakevdi iittalipgk papklitedm vksmkpgsvi vdlaserggn
      301 celtepgkiv eqhdvtligy tdlpsrmakv asdlyatnlf hlmteltpek dgqpkvnmdd
      361 dvirgltvvl dqdvtwpppq pqtptspkpa pgteepsaeq kaaahkesqr rsligkgavl
      421 ivtlaalygv gayapesflr hftvfvlacf igwqvvwnvt aslhtplmsv tnaisgiivi
      481 gailhlaqan nvavgimafv avliasinvg ggfrvthrml nmfrk
//
LOCUS       WP_100672895             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium meliloti].
ACCESSION   WP_100672895
VERSION     WP_100672895.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39574
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfiake sdpnegrvag svesvkklka lgfdvvveag aglisripdq eyekagarig
       61 taadaktadv vlkvrrptvq eisgyrsgav viaimdpygn deaisamaga glttfamelm
      121 pritraqsmd vlssqanlag yqavidaaye ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsgeyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vsremldsmk pgsvvvdlav erggnvegae
      301 agkvtevggi rivghlnvag riaasaslly aknlvtflet mvsketkala lnmedelvka
      361 talthggavv hpafggamrg ek
//
LOCUS       WP_100676956            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Avrilella
            dinanensis].
ACCESSION   WP_100676956
VERSION     WP_100676956.1
KEYWORDS    RefSeq.
SOURCE      Avrilella dinanensis
  ORGANISM  Avrilella dinanensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Avrilella.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Avrilella dinanensis"
                     /db_xref="taxon:2008672"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111626
     Region          25..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskftwift lfmvlavqlv saqektvtgt vtdadfgdpi pgvsvllegt qygtetdmdg
       61 kysinarpgq rlvfkftgfa dmymtvgqsd mlnvvmvesv dealeelvie gyrnvakeks
      121 stasttvsak tiegrpnasi lqrlqgqipg lsistgsgqp gsndtsvilr glgsingave
      181 plyvidgipv ssdrfrslnp ndfesvtvlk dagataiygn rgangvivin tkkgsfdsal
      241 qikyvgttgv sslqkndynm mnaeealayt gytrqmlglg gtnydtnwqd vffrdaisqd
      301 htlsftagak nlstytsvgy adyegalknt glkrfsfvnn lngkndngrl tfgttvsany
      361 sksdiqpvsg satfadnfff gsfiafpffs peqwdgenwe dirdnvspng rmnvlmspfm
      421 lmdrmknygr iqdefklvtg aninydlgsg fnvgsrigvd yqtisqfsfn dpssyisnsg
      481 tpaeqiyrgs tagveerrll insttnltwq kdlsdkssls iagyveylkg hfknsyyske
      541 gydpyffdrr dgdsgsipdn edndfyvpva gmsvanaglf syfgiasydy dsrygleatv
      601 rrdasfrfvd dykwgtfwsv sgrwnisned fmsgsvfndl klrasygtag nqditgggif
      661 ggaylyetvy gsasgynnht slvlaqlpnr alqwesittt nigldfgvfe nrlrgsvdvy
      721 rkqtddlyqn vplsaingtt glmsnygair negievivag dvirnentrl tlnfngaynk
      781 nsildipheg gffwdgsglt amqegdmlgq fymheftrvd pstgealfld kdgnetaapr
      841 dedlrltgks ympkyvgsfg fdfehkgwfl qanftyaqdv yrydndyffl tfpgfngsin
      901 qsndakdiwt qpgdvasips asasnldyfs gssfylrdas yvrlryltlg hsfapkslef
      961 igltglrvya qaenlmtwsk wkgwdaesnr gvdmaqyptp ktvsfgvevq f
//
LOCUS       WP_100678931             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_100678931
VERSION     WP_100678931.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53584
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrigap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_100689190             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter aromaticivorans].
ACCESSION   WP_100689190
VERSION     WP_100689190.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter aromaticivorans
  ORGANISM  Marinobacter aromaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter aromaticivorans"
                     /db_xref="taxon:1494078"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56160
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeif tderrvaatp psvhklinlg yevtvetgag eaahyrdeay eavgatiavd
       61 trslwsdadf ilkvrapmln palgkheadl mkegaflvsy iwpaqnpell eklaarkitt
      121 faidslpris raqkmdalsa maniagyrav veaanhfgrf ftgqvtaagk vppakvmvig
      181 agvaglaavg aanslgaivr afdtrlevke qiesmgaefl qldfgdeegs gtggyakqms
      241 defikaemal faeqakevdi iittalipgk papklitaem vksmkpgsvi vdlaserggn
      301 celtepgkiv ehhevtligy tdlpsrmakv asdlyatnlf hlvteltpek dgqpqvnmed
      361 dvirgltvvl gqdvtwpppq pqtptspkpa pgteepsaeq kaaahkesrr rsligkgavl
      421 ivtlaalygv gayapesflr hftvfvlacf igwqvvwnvt aslhtplmsv tnaisgiivi
      481 gamlhlaqae naivgimafv avliasinvg ggfrvthrml kmfrk
//
LOCUS       WP_100694590             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Advenella
            sp. S44].
ACCESSION   WP_100694590
VERSION     WP_100694590.1
KEYWORDS    RefSeq.
SOURCE      Advenella sp. S44
  ORGANISM  Advenella sp. S44
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Advenella sp. S44"
                     /db_xref="taxon:1982755"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54018
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigivkeql agetrvaatp ssveqllklg ftvviesgag aaasfddaay ekagasiapa
       61 dqvwqsdlvy kvnapedtei trmktgatlv sfiwpaqnpe lvqklsehgi tvlamdmvpr
      121 israqsldal ssmaniggyr avieaahhfg rfftgqitaa gkvppakvlv igagvaglaa
      181 igtagslgai vrafdtrlev aeqiesmggq flkldfgden gsssdgyakt mseefikaem
      241 alfaeqakev diiittalip gkpapklitr emvdsmrpgs vivdmaaaag gnceytepgq
      301 vittasgvkv igytdlpgrl paqssqlyat nlvnlsklms kekdgqiqld qedtvfrnmt
      361 vvhngsvtyp pppiqvsaas skpaaqkpep kpvkppksaa fkfgilalvc vtfawvgana
      421 paeflshftv fvlacvvgyy vvwnvthalh tplmsvtnai sgiivigavv qighgsglvn
      481 ilafiavlia siniaggflv trrmlkmfmk gkge
//
LOCUS       WP_100704861             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            hartskeerlii].
ACCESSION   WP_100704861
VERSION     WP_100704861.1
KEYWORDS    RefSeq.
SOURCE      Leptospira hartskeerlii
  ORGANISM  Leptospira hartskeerlii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira hartskeerlii"
                     /db_xref="taxon:2023177"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41127
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvlkeak eetrvavtpd vvdalkkiga sviiekgage gsyfsdedyk kagatiqsra
       61 dilkksdlvv sihladgasl skikkgafyl gmfqpavnpq vikklaaqkv tvlsldaiar
      121 itraqsmdvl ssqatvagyk avliasnhlt rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvqslgak fvevegaths aaaggyaveq tedykkrqqe
      241 aiekfaakad viittalipg rkapiiitkk ivdrmkagsv vvdlaspngg nceytqhgkv
      301 vltkngvsiv ghqnlagslp sdasrmfakn vlnylkllvk ekkinfdlnd eviasttith
      361 egeirhkltl dalggskqeg kkpaakkka
//
LOCUS       WP_100708626             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            saintgironsiae].
ACCESSION   WP_100708626
VERSION     WP_100708626.1
KEYWORDS    RefSeq.
SOURCE      Leptospira saintgironsiae
  ORGANISM  Leptospira saintgironsiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira saintgironsiae"
                     /db_xref="taxon:2023183"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41035
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvlkeak eetrvavtpd vvdafkkiga sviiekgage gsffsdedyk kagatiqsra
       61 dvlkksdivv sihladgasl skikkgafyl gmfqpavnpq vikklaagkv tvlsldaiar
      121 itraqsmdvl ssqatvagyk avliasthlt rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvqslgak fvevegaths aaaggyaveq teeykkrqqe
      241 aiekfaakad viittalipg rkapiiitkk ivdkmkagsv vvdlaspngg nceytqhgkv
      301 vltkngvsvv ghqnlagslp sdasrmfakn vlnylkllvk ekkvnfdlnd eviasttith
      361 egeirhkltl dalggskqeg kkptakkka
//
LOCUS       WP_100711985             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            perolatii].
ACCESSION   WP_100711985
VERSION     WP_100711985.1
KEYWORDS    RefSeq.
SOURCE      Leptospira perolatii
  ORGANISM  Leptospira perolatii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Leptospira perolatii"
                     /db_xref="taxon:2023191"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40964
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvlkeak eetrvsitpd vvdalkklga tvvvekgage nsyfsdeqyk kagatissrp
       61 dvlkkadilv sihladagtl skikkggiyl gmfqpamnaq tikklasqqv tvqsldaiar
      121 itraqsmdvl ssqatvagyk avllaathlt rffpmlttaa gtitpasmlv igagvaglqa
      181 iatarrlgav vdvfdtrpev keqvqslgak fvevegakhs aaaggyaieq teeykkrqqe
      241 aidkfagkad viittalipg rkapliinkk ivdgmkpgsv vvdlassmgg nceytqhgkt
      301 iitkngvsvi ghtnlagslp gdasrmfakn vlnflkqlvk ekkvnmdfnd eviasttith
      361 egqirhkltl dalnvkvgkk paakkea
//
LOCUS       WP_100718696             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            meyeri].
ACCESSION   WP_100718696
VERSION     WP_100718696.1
KEYWORDS    RefSeq.
SOURCE      Leptospira meyeri
  ORGANISM  Leptospira meyeri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Leptospira meyeri"
                     /db_xref="taxon:29508"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40339
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikeps yenrvaitpd vvdplkklgf tvsvettagd naffsdqdyk dvgatvesrd
       61 ailsgsdivv sihsldeasa kkigkdkiyi atlsplafpk kvkeianasf kifsmdtipr
      121 itraqsmdvl ssqatvsgyk avllaasnys rffpmlttaa gtitparvli lgagvaglqa
      181 iatsrrlgav vdvfdtrpev keqcmslgak fvevegaada sntggyaveq sedyqrrqke
      241 aiakyaekad iiittalipg rkapllitke mvdkmrqgsv ivdlaaingg ncevtendkt
      301 ivykgitvig nsnlqstqpm daskmyakni vnflklfvnk ekqfsinled eiinacmiae
      361 ngvirhkptl allge
//
LOCUS       WP_100719704             308 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Leptospira meyeri].
ACCESSION   WP_100719704
VERSION     WP_100719704.1
KEYWORDS    RefSeq.
SOURCE      Leptospira meyeri
  ORGANISM  Leptospira meyeri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Leptospira meyeri"
                     /db_xref="taxon:29508"
     Protein         1..308
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35889
     Region          4..174
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mifdlfskkq krirgevpdv ytyndipdkl rvqivhiiqd tigihknhyg dddkvrkayq
       61 ffqntlcrey gkfflvdkyn spdidvlnff lqtedfeqai dvidlifkyi ekiiggenyq
      121 kylyctqvkm rpeqaieeln hrfkehgigy qfeeeiirvd styahseivk ptltllrgik
      181 fkgandeylk ahehyrhgrn kecltdclka fesvlkiick ekawaynqtd tskkliqicl
      241 qnnlipnftq nqftslqsll esgiptirnk lgghgqgqip qkvddemtry alnltgsnii
      301 flieqsgl
//
LOCUS       WP_100721300            1125 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_100721300
VERSION     WP_100721300.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1125
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126740
     Region          31..1123
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntssmiriv issllmaifs qtclaqvave ikgtvrsvtg eslpgatviv egtargvitd
       61 vegrftlkar kgqmlkvsfv gmkprlikas sgimniilqd nvqeiegvvv tgyqqiknrv
      121 ftgaaasvkl deiklngvsd vsrmlegria glsiqnvtgs fgaaprinir ggasimgnvq
      181 plwvidgavy edlvsltldq lasgdavtli ssavaglnas diediqvlkd asatsiygar
      241 alngvivitt rsgkrnapnr fsysyelsmr sipsytnfdl lnsqesmsvy qemgrkgyfs
      301 lqntlygrrs gvyyqmykal ntidpatgqy ylentddvkr afmrereyan tnwfkelfth
      361 rpihthtvtf sgggensamy asigfyddrg wtladhvkri taniknsfyw nedkikatis
      421 aqgnlrnqns pgtipqrrnt vigtferdfd inpfsyalst srtlrphnad gerefyrnnw
      481 apfnilneye nnylktevld lklqgelsyr lndhievkgl amvrhavtks shfiaeasnv
      541 vqafranetp yvareniyll knkddpmqlp gvalthggif nktetslrsy lgrlaldynr
      601 qlsehniraf gfteiryadr smnpfqgygi qydrgnqvfs nplvfeklan egdtyfslte
      661 ryergvtlsg satygyagky ifngvfnyeg antagkysrs rwlptwniga kwnldqekfm
      721 rkhttisrla lrtsygltak mneqavnstt vfkhvmvnrt llkdrenalr ilhlenrdlt
      781 wekmyelnfg lelglfgnri satfdvyqrn sfdlidlirt sgvggqyyky anfgdmrtrg
      841 velaiqtqni ltdkfswstt vtisgmkqki trllntpntf dmvagtgrgn ivgfprgslf
      901 sfnfqglnsn glptfdfgly psnkgansei sgadfldaqy sksyliyhgp iepqyiggis
      961 ntfkyknwef scfvtmqagn kirmnpsfdp afadlnvfsk eyynrwlnpg derktnipvi
     1021 psqdlirnig keniekaynt ynysqnrvad gsfvrmknis lgyrlpqrfl shlkikqmnv
     1081 kvnvtnpfli ysdrklngqd pefyrsggvs lptpkqytmt lnvef
//
LOCUS       WP_100722385             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            haakeii].
ACCESSION   WP_100722385
VERSION     WP_100722385.1
KEYWORDS    RefSeq.
SOURCE      Leptospira haakeii
  ORGANISM  Leptospira haakeii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira haakeii"
                     /db_xref="taxon:2023198"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41077
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvlkeak eetrvavtpd vvdafkkiga sviiekgage gsyfsdedyk kagatiqsra
       61 dvlkksdlvv sihladgasl skikkgafyl gmfqpavnpq vikklaagkv tvlsldaiar
      121 itraqsmdvl ssqatvagyk avliasthlt rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvqslgak fvevegaths aaaggyaveq teeykkrqqe
      241 aiekfaakad viittalipg rkapiiitkk ivdrmkagsv vvdlaspngg nceytqhgkv
      301 vitkngvsvv ghqnlagslp sdasrmfakn vlnylkllik ekkinfdlnd eviasttith
      361 egeirhkltl dalggskkeg kkpaakkka
//
LOCUS       WP_100725790             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            levettii].
ACCESSION   WP_100725790
VERSION     WP_100725790.1
KEYWORDS    RefSeq.
SOURCE      Leptospira levettii
  ORGANISM  Leptospira levettii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Leptospira levettii"
                     /db_xref="taxon:2023178"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40330
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikeps yenrvaitpd vidplkklgf svaiettagd saffsdqdyk dvgatvesrd
       61 silsgsdivv sihaldeasa kkigkdkmyi atlsplafpk kvkeiasasf kifsmdtipr
      121 itraqsmdvl ssqatvsgyk avllaasnys rffpmlttaa gtitparvli lgagvaglqa
      181 iatsrrlgav vdvfdtrpev keqcmslgak fvevegaada sntggyaveq sddyqrrqke
      241 aiakfaekad iiittalipg krapllitke mvdkmrqgsv ivdlaavngg nceltendkt
      301 ivykgitiig nsnlqstqpm daskmyakni vnflklfvnk ekqfninled eiinacmiae
      361 ngsirhkptl tllge
//
LOCUS       WP_100738603            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_100738603
VERSION     WP_100738603.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115526
     Region          24..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrklmlllt clfmgiglvt aqtqkvtgvv iseedgqpvv gasvlakgtt vgvitdvdgk
       61 ftlsgipssa ktlqisyigm qtaevaiapv ikvilktdak aldevvvtam giskekkalg
      121 yavqdvkgdk ltqasssnls salqgkvsgv eispssgmpg asskmtirgs rsftgdntpl
      181 yvvdgmpiss stdldtfnsv tgsdyanrav didpndiesi nilkgqaasa lygmrasngv
      241 vvittksgkg arkgkpevti ntglsfdkvs tmpdfqkefa qgfngafsps dsrswgplis
      301 elandpkygg ntdnsytqkf gkhqgqyyvd qrakagldpw atpraydnak dffntgvtwn
      361 ssanvaqsld kgsyslslgs ttangivpst gmdrynaklt aqaqlsknws tgfngnfvys
      421 kikkqtgann gimatvygap ssydlggips haegdpytqn tyrsttgfdg aywavennsf
      481 kertqrffgn afakystdfg tedhkldvky qlgtdayttn ytdtwgyghs ngtgsieeqs
      541 vtnneinsll tvtydwkitp eldlnvlygn elvdnsskyk ynlgsnfnfp gwnhianasi
      601 ysstgtyhre rtvgnfgnis layrnmlyln atvrndivss mprnnrsfty psvslgfift
      661 elealkndvl tygkirasya evgqagtyyp syyrtpvygg gfssgtpiqy pigsissyip
      721 yykiydpnlk pqntksyeig adfsfwngli slnytysrqn vkdqifevpl atstgyseli
      781 tnggsvhtns heitlsvnpi qtknfnwdfa fnfskidnyv dklapgvssi mlggfvdpqv
      841 rlsagdkfpv iygtsyqrne egqivvdeng mptlgenrvl gnvspdfrmg fnttfefykf
      901 rlsavldwkq ggcmyagsvs tldyygvtqk sadyrkadhf yfekpavkql adgsyapndi
      961 kisgenayny fdrlstisea gvygssflkl reialsypvl nksylgvtvn vfarnlllws
     1021 emdngidpes sqgnnnmaga ferfslpgts sygfgitvkf
//
LOCUS       WP_100737764             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            kmetyi].
ACCESSION   WP_100737764
VERSION     WP_100737764.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kmetyi
  ORGANISM  Leptospira kmetyi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira kmetyi"
                     /db_xref="taxon:408139"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41254
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigilkeak eetrvsvtpd ivdalkkiga tvlvekgage qsfyhdedyk kagaslvsrq
       61 dvlsksniiv sihladpptl akiksgtiyl gmfqpamnaq tiqklaakkv evlsldaiar
      121 itraqsmdvl ssqatvagyk avllaashla rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvqslgak fvevegashs aaaggyaveq teeykkrqqe
      241 aidkyaqrad viittalipg rkapllitkk ivdnmksgsv vvdlassmgg nceytkhgqn
      301 vitpkgvtvi ghknlagsip adaskmfskn vlnflkllik dkkinldlnd eilsstsith
      361 egevrhkltl dalgnksgta kpkksaskk
//
LOCUS       WP_100743884             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            harrisiae].
ACCESSION   WP_100743884
VERSION     WP_100743884.1
KEYWORDS    RefSeq.
SOURCE      Leptospira harrisiae
  ORGANISM  Leptospira harrisiae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Leptospira harrisiae"
                     /db_xref="taxon:2023189"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40350
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikeps yenrvaitpd vvdplkklgf tvsvettagd naffsdqdfk dvgatvesrd
       61 silsgsdivv sihaldeasa kkigkdkiyi atlsplafpk kvkeianasf kifsmdtipr
      121 itraqsmdvl ssqatvsgyk avllaasnys rffpmlttaa gtitparvli lgagvaglqa
      181 iatsrrlgav vdvfdtrpev keqcmslgak fvevegaada sntggyaveq sedyqrrqke
      241 aiakyaekad iiittalipg rkapllitke mvdkmrqgsv ivdlaavngg ncevtendkt
      301 ivykgitvig nsnlqstqpm daskmyakni vnflklfvnk ekqfninled eiinacmiae
      361 nglirhkptl allge
//
LOCUS       WP_100745424             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            ellisii].
ACCESSION   WP_100745424
VERSION     WP_100745424.1
KEYWORDS    RefSeq.
SOURCE      Leptospira ellisii
  ORGANISM  Leptospira ellisii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira ellisii"
                     /db_xref="taxon:2023197"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41086
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigilkeak eetrvsvtpd iidalkkiga svvvekgage qsfyhdenyk kagatlvsrq
       61 dvisksniiv sihladpatl akiksgtiyl gmfqpamnap tiqklaakkv evlsldaiar
      121 itraqsmdvl ssqatvagyk avllaaahla rffpmlttaa gtitpasvli igagvaglqa
      181 iasarrlgav vdvfdtrpev keqvqslgak fvevegashs aaaggyaveq tdeykkrqqe
      241 aidkfaqkad viittalipg rkapvlitkk ivdnmksgsv vvdlaspmgg nceytkhgqn
      301 vitakgitvi ghknlagsip ndsskmfgkn vlnflkllik dkkinldlnd eilssttity
      361 ggeirhkltq dalgsksgaa kpkksvskk
//
LOCUS       WP_100757508             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            wolffii].
ACCESSION   WP_100757508
VERSION     WP_100757508.1
KEYWORDS    RefSeq.
SOURCE      Leptospira wolffii
  ORGANISM  Leptospira wolffii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Leptospira wolffii"
                     /db_xref="taxon:409998"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40668
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvlkeak eetrvavtpd vvdalkkiga svtvekgage gsyfsdedyk kagasiaara
       61 dvlkksdilv sihladgasl skikkgaiyl gmfqpasnas vvkkfagqks tlvsldaiar
      121 itraqsmdvl ssqatvsgyk avllaathlt rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvqslgak fvevegaths aaaggyaveq teeykkrqqe
      241 aiekfaakad aiittalipg rkapiiitkk ivdkmksgsv vvdlassngg nceytqhgkt
      301 vltkngvsvi ghlnlpgslp sdasrmfakn vlnflkllik dkkvnldlnd eiissttiah
      361 egeirhkltl dalgskdggk kpaskkka
//
LOCUS       WP_100763530             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            barantonii].
ACCESSION   WP_100763530
VERSION     WP_100763530.1
KEYWORDS    RefSeq.
SOURCE      Leptospira barantonii
  ORGANISM  Leptospira barantonii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira barantonii"
                     /db_xref="taxon:2023184"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41205
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigilkeak eetrvsvtpd iidalkkiga tvlvekgage qayyhdedyk kagaslvsrq
       61 dvlsksniiv sihladpatl akiksgtiyl gmfqpamnap tiqklaakkv evlsldaiar
      121 itraqsmdvl ssqatvagyk avllaashla rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvqslgak fvevegashs aaaggyaveq teeykkrqqe
      241 aidkyaqrad viittalipg rkapllitkk ivdnmksgsv vvdlassmgg nceytkhgqn
      301 vvtpkgitvi ghknlagsip adaskmfskn vfnflkllik dkkinldlnd evlsstsith
      361 egevrhkltl dalgnksgta kakksaskk
//
LOCUS       WP_100767747             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            neocaledonica].
ACCESSION   WP_100767747
VERSION     WP_100767747.1
KEYWORDS    RefSeq.
SOURCE      Leptospira neocaledonica
  ORGANISM  Leptospira neocaledonica
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira neocaledonica"
                     /db_xref="taxon:2023192"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41071
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvlkeak eetrvavtpd vvdalkkiga sviiekgage gsyfsdedyk kagasiqsra
       61 dilkksdlvv sihladgasl skikkgafyl gmfqpavnpq vikklasgkv tvlsldaiar
      121 itraqsmdvl ssqatvagyk avliastylt rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvqslgak fvevegashs aaaggyaveq teeykkrqqe
      241 aiekfaakad viittalipg rkapiiitkk ivdrmkagsv vidlaspngg nceytqhgkv
      301 vltkngvsvv ghqnlagslp sdasrmfakn ilnylkllvk ekkinfdlnd eviasttith
      361 egeirhkltl dalggskqdg kkpaakkka
//
LOCUS       WP_100774911             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sp. S27].
ACCESSION   WP_100774911
VERSION     WP_100774911.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sp. S27
  ORGANISM  Psychroflexus sp. S27
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Psychroflexus sp. S27"
                     /db_xref="taxon:1982757"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111485
     Region          32..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkffythqcg fglillfiff statakaqnt yklsgqvtdt tgqaipgvhi qrinttngat
       61 tdfdghyniq vtgtdrlsft ylgyqaqtia vnnrklinvq lspstealde vvinagyyrv
      121 kdrertgsie kvtsedielq pvtnpiealq grmagvevvq stgvpgaapt irirgqsslr
      181 tnfddngnlp lyiidgmpin sspidsqiql fegagvdpln tldlsniesi evlkdadata
      241 iygsrgangv vlittksgqk nqgikvstkl ytgmsrvdnf lnllntqqyl kirkqafend
      301 gvepneynaf dlvlwdenry tdwqkelfgk taelrsasfn isnanettsy iigasyqkqg
      361 mvfpgdfsye kktfnlnlnh qskdkkfkln lsanyglddn dlfnsstfvs taltlapnap
      421 rlynddgsln wedstwsnpl atlenegklk tnnlisnlgl tyrlspslsf kssfgythlt
      481 seeniqtpie sydpamwdrv tnrsqysdir rnswivepqi hyrktwgqhh fntivgatfq
      541 enkntsltis grgyidrnli gnleaadqvs iikdrdftyk ysaifarlay dwkekyylnl
      601 tgrrdgssrf gpdkrfanfg aigaawifte enffdkylnw lsfgkirgsy gttgndqigd
      661 yryldayeat pgpeglyptq ltnndfswet nkkleaalel sflnnrihte iawyrnrssn
      721 qlvgyplpai tgfskveanl patvenkgwe lglsakvfqk qsfqwntsln mtipssklva
      781 fpdieetaya ntyrvgqals ldilyqfegv dpdtgyytvk dvnedgsydy ddrlitkdlg
      841 rkffggvynk lnyknfslsf lfefvkqngr ktsslppgrl gnnlksvtey gssspedlqa
      901 psqsinafla fnryaynsef sitdasfirl ktlslgyeis ndftknigls qfklfvhaqn
      961 lltitdyegl dpqspgskal pslqsltggl qltf
//
LOCUS       WP_100776421            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sp. S27].
ACCESSION   WP_100776421
VERSION     WP_100776421.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sp. S27
  ORGANISM  Psychroflexus sp. S27
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Psychroflexus sp. S27"
                     /db_xref="taxon:1982757"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116590
     Region          25..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfsgflt lllvlavqis faqtktvtgn vtgedglpip gvnviekets ngtqtdfdgn
       61 ytidvetgkv lvfsylgmkt qeievgsqst ievslqedaa eldevvvtgy stsskksftg
      121 satrvsadel nkksvsnvsq alageaagvr vintsgqpgs saqirirgig svngntaply
      181 vvdgvpyngn insinpqdie sttilkdaaa taiygsrgan gvivietktg sgktgsievs
      241 tktgfnynli prhdviespe ryielgwegl knygmykegf dqagsidyan delfgdgqgi
      301 gshynmwnva dggelinpst gqvrdgvtrr ynpedwedyg fqtsnrtean ikisggdekt
      361 syftsfgylk digyivdsdy erysgrlnlq hkakewltgn mnvgytiset ndngqssdsg
      421 sifwftdnip aiyplflrdg agdmvpdpyy ggnqydyged grrfgaqans iadakystsk
      481 derheintns ylkaditdyl saevrfgsqy ynnsansrns pfygpsrgen gsifkqktel
      541 fsanfqqiir fsesygnhni dalaahesns werqtlyagk sdvidpegte fnnavvvstp
      601 pgsyvdnytl esyfananyn yddtyflsgt vrrdgssrfl ddnkwgtfgs vsaawvmsne
      661 dfltdvdaid flklkasygl igeqggvgly pgydrfdign vnddpsfsfg trgnkdltwe
      721 tskmfqvgve snigdflevn idyyrknted llfdrrqaps tgiailtvnd gellnsglef
      781 dvkaniiktp dfylnaging evlnnelkam pidpstgtnk vldvaglygr seghslydfy
      841 treyvgvdpa nglpiwntyf dvdtgqdirs lheyttanpn anidvretnd panatkrytg
      901 qsaipdvrga fnlsagykgf sisaqflyqi gghaydgaya dlmhngvvgg nnwhtdinnr
      961 wqqpgditdv pridnnatkn vnasstrfit kadflslnnv rlgydlpsaf lqdsgiadas
     1021 iyvtgdnlfl fskrdgfnps tsisgastyr ysplstftvg vtlkf
//
LOCUS       WP_100776774            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sp. S27].
ACCESSION   WP_100776774
VERSION     WP_100776774.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sp. S27
  ORGANISM  Psychroflexus sp. S27
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Psychroflexus sp. S27"
                     /db_xref="taxon:1982757"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117005
     Region          25..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkvkntvll lftllsagmf aqqvtvtgav kdadgiplpg vnilvkgtsn gtqtdfdgqf
       61 tiqaetgkml vfsylgmktq evevsgdaei evvlesdank ldevvvtalg ikrekkslgy
      121 atqevggesv sdvatqnftn alsgkvaglk vkssgtmggs tnvvirgnas ltgsnqalfv
      181 vdgtpiinqn sntgdqksgr ggydygnaas dinpdniesi nilrgaaata lygeraanga
      241 ivietkkgar nkgmgvsirs svtfadvnke tlpkyqkkyg agysagydtg dgflltding
      301 dgideettpf tadasygakf dpnrmiyqwn siypeldtyl qatpwtaakh tpndiwetgh
      361 ttinsvaldg gnedgnfris ytnlnqkgtl pnsrikrdni kfsgshdltd rltaaanvtf
      421 iktdgkgrfg tgydgqnlmq tfrqwhqtnv diydqrdayf strknitwnp nsafdrtpiy
      481 tdnpywvrye nyqtdtrnry ygnvnlsyei sdvfsvlgrf tfdtyselqe erinvgsaav
      541 ssysrfdnrv aeynydliln fnkdltsdln ldgnvgfnlr rneqtfiraa tngglnapgf
      601 yalsnskdpl nppseyeadq mvdgifaras lgymntyyle gtirrdrsst lpssdntyyy
      661 psvstsills niieeewldf aklranyaqv gsatdpynvy ntyvvsapfn gqgsaslsst
      721 lnnldlkset stsyeigles sfindrvnfd isyyrtrted qitpvdisna tgygrkllna
      781 geienkglev lvglvpirte dfswnmnvnw sknenevisl agdlenlqla sfqggvsina
      841 apgepygair gtdyvydnqg nkvvdangyy eisssnnevl gniqpdwnag itntfnyknl
      901 sfsflidiqe ggdifsldtw ygmgtglydv tagindlgne mrapiadggg vilpgvdasg
      961 nqntvripvg tasdspygys ndankghvyd asfiklrems ltyrlddklv eklpftgasl
     1021 sligrnlwii dknmpysdpe aglssgniqg yqsgaypsar eyginvklkf
//
LOCUS       WP_100788378            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_100788378
VERSION     WP_100788378.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123435
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrhvfilll sfagvltsaf aasrqvqgvv issednmpli gasvyikaed lskdgnspti
       61 tgvitdidgk fnisvpegvt rlfcsyvghe vqelrlvpgk dqyeitlfps aqmldavvvt
      121 gyqtverrkl taavgklnis detigavksi dqalagqiag lsvtstsgap gapakirirg
      181 tsslngtqdp lwvldgiple gtdvpqsnvl ndvsniqqss iaglnpadie nitvlkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs skftymptls tnrlnmlnsq ekvdlelell
      301 rsnfaygdnk ggvskiisgy gltdaykkgg wsaltpeaqt disrlrntet dwgdilfrda
      361 fnqeyslsls ggnervtyyt sigyyqengn vkgvgldrln ivaktsykvn rilkfgvslf
      421 vnrrnnktyl tdtyglvnpv yysrkanpyy qpfdangnyv ydfdvqnnsd tdlgfnifee
      481 rkntsneeti nalssifdae lrfndklkft tqlglqldka skeqiadkes fsmriirkns
      541 kywdsasqsn kyfipdggvh kayentnsqi twkamgeyrd sfndihelev mvgtelrktw
      601 yetlfsagyg fdrqtlttkp vvfpdedrar qfplhqktyk enayvsffst asyslmnryt
      661 fggsirfdgs dlfgvdkkyr ylplysvsgl wrlsnepfmq gtrkwmdnla frvsygiqgn
      721 idkntspfll gkyivdnilp ggsehmidin sapnkklrwe ktqsvnvgld fsvlnqainl
      781 svdyyyrkgt dligkqmlpl etgfvstnin wasmvnkgve vslstrnvat knfswytnln
      841 faynnnkvlr eaipeaqtip gregypvdai faiktaglde egyplfydke gkkvtlkely
      901 rlqdpfglgf tvnsdvtpae ersfysyigs qdtpytggli ntfsyknwel tanlsfnlgg
      961 yvrttpsynf infdrgqnvn sdildrwtpe ntdgrlpali tsekradeyy wydqkseiyk
     1021 nldiwvkkln yfrlqnlrlg yrlpekmiks lgmgsasvai egrnllvfgs syknfldpes
     1081 mynpyappip ksitfslnln f
//
LOCUS       WP_100788497            1132 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_100788497
VERSION     WP_100788497.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1132
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126109
     Region          52..117
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          131..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkaipchk agritsffll isifllipsi ttpvyavety tqqtvftlha tnktvkevfe
       61 yieknsefvv lyskdllpvl qkkvsvsidk qnvesilnil skeaglkyni ndrqititkv
      121 taeapqqekk ikitgqvlde ngegipgani vikgnstlgt vtnvegnftl mapenstlva
      181 sfigytpvei plkgkkivvf klvpdaqsle evvvvgfgtq kkasvvgavq sikpaelrvp
      241 ssnlstsfag riagvismqr tgepgadgan fwirgaatfs gttdplifid gvevsagdmn
      301 aipseaienf silkdasata lygargangv ilittrtgkd lekarinvri dntftaptrt
      361 lkladavtam klrneailtr npdgtpafsd dkiqgtlegr nqyvypnvdw fdymfkdysm
      421 nqsanlnvmg gtkkvdyfis asinndngml kkdpnntfdn niqnlrysfq snvgawltss
      481 tkvnvrinsq ivnyngpsts mddlykyvme apsmyfapvy pninredhti fgnksggpig
      541 sggfsiyrnp yasmvqgssk qsaytintaf eleqkldflt kglnfkalvs fknwskttvn
      601 rsfspyfyel qnpqeqedgs ylydynsisk grtaletsts ttgdrlmnlq atlnyqrmfg
      661 dkhdvgamlv ylqreynlnn pdnnyyntlp ernqglagrv tyaydgryla efnfgyngse
      721 nfekgsrygf fpslavgyli snekffeplt kvisnlkira syglvgnadi gsnrfpyltk
      781 vdlggagfvf gdqwqtssng atittygaek vtweigkkyn vgfdlglfnk lslnvdffre
      841 drkdiflrrn tipaesgitg dlrpygnlgk vrnqgvdmsl dynhavskdf misakgtfty
      901 aknqymeide pdyeyaymsq vgrplnqykg yialglfkdq eeidnspkqi ltrvvqpgdi
      961 kyadlnndgk idgndqtyig npelpqisyg lgvsiqykkw dasiffqgvg krsimlsdih
     1021 pfggesygvm qfvadnhwte anpnpeamyp rltngknnnn npnstywlrd gsyirlknve
     1081 lgysykflra yisgqnlltf skfklwdpel ytsnglkypt qimgsiglqf tf
//
LOCUS       WP_100788498             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            adleri].
ACCESSION   WP_100788498
VERSION     WP_100788498.1
KEYWORDS    RefSeq.
SOURCE      Leptospira adleri
  ORGANISM  Leptospira adleri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira adleri"
                     /db_xref="taxon:2023186"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41265
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigilkeak eetrvsvtpd iidalkkiga tvlvekgage qsyyhdedyk kagaslvsrq
       61 diisksniiv slhladpatl akikpgtiyl gmfqpamnaq tiqklaskkv dvlsldaiar
      121 itraqsmdvl ssqatvagyk avllaashla rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvqslgak fvevegaqhs aaaggyaveq teeykkrqqe
      241 aidkfaqrad viittalipg rkapllitkk ivdnmksgsv vvdlassmgg nceytkhgqn
      301 vitpkgvtvi ghknlagsip ndaskmfskn vlnflkllik ekkinldlnd eilssttith
      361 ggeirhkltl dalgsksgaa kpkksaskk
//
LOCUS       WP_100789114             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            brenneri].
ACCESSION   WP_100789114
VERSION     WP_100789114.1
KEYWORDS    RefSeq.
SOURCE      Leptospira brenneri
  ORGANISM  Leptospira brenneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Leptospira brenneri"
                     /db_xref="taxon:2023182"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40169
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikeps yenrvaitpd vvdplkklgf tvsvettagd naffsdqdyk dvgatveskd
       61 ailsgsdivv sihtldeasa kkigkdkiyi atlsplafpk kvkevasasf kifsmdtipr
      121 itraqsmdvl ssqatvsgyk avllaasnys rffpmlttaa gtitparvli lgagvaglqa
      181 iatsrrlgav vdvfdtrpev keqcmslgak fvevegaada sntggyaveq tedyqrrqke
      241 aiakyaekad iiittalipg kkapvlitka mvdtmrqgsv ivdlaavngg ncevtendkt
      301 ivykgitvig nsnlqstqpm daskmyakni vnflklfvnk ekqfninled eiinacmiae
      361 ngvvrhkptl allge
//
LOCUS       WP_100792477             308 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Leptospira brenneri].
ACCESSION   WP_100792477
VERSION     WP_100792477.1
KEYWORDS    RefSeq.
SOURCE      Leptospira brenneri
  ORGANISM  Leptospira brenneri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Leptospira brenneri"
                     /db_xref="taxon:2023182"
     Protein         1..308
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35854
     Region          4..174
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mifdlfskkq krlrgeipdv ysyedipnrl rvqivhiiqd aigidknyyg yenkvnksyq
       61 fiqrtlcrey gkfylldrdn lpqidvlnff lqtkdyeeai dvidlafkyi ervingdnyq
      121 eylyntevki ksdqaieeln drfkehaigy qfngeiirvd styshseiak ptltllrgkk
      181 figaneeylk ahehyrhgrn kecltdclka fesvlkiick ekgwtfsptd tskkliqicf
      241 qnnlipsftq nqftslqnll esgiptirnk lgghgqgqvp qkvddemtry alnltgtnii
      301 flieqsgl
//
LOCUS       WP_100802927             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacter sp.
            MAR_2010_11].
ACCESSION   WP_100802927
VERSION     WP_100802927.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacter sp. MAR_2010_11
  ORGANISM  Ulvibacter sp. MAR_2010_11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacter.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Ulvibacter sp. MAR_2010_11"
                     /db_xref="taxon:1250229"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106957
     Region          27..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqknsnsrr lllllflfpc fvfaqttltg kisdpngttv pfanviekgt tngtttdidg
       61 nfsisvaslp atlvfsslgy etieqtanna spmnitlaes aealsevvvt glatsikrsn
      121 sanavasisa eelvgttppp tldgalygkf agavvnansg apggglsikl rgatslqgnt
      181 splyiidgvy vdnssiqpgl nlvsaaaagg sasnqdnptn riadinpedi anieilkgas
      241 aaaiygsraa agvviittkr gkagetlfkf nqstgwteai nllglrdyne qrvrdtfgea
      301 avaqfvaarn egrlidyeke iygekgflsn tnfsmsggdv kskfyagvsh nneqgivnrt
      361 gyektslrln ldhkatdylk lslstnyiys rsdrgffnnd nsgttigvtl tgttpwlqlf
      421 pdangvypdn psgasnplqt rdlvtnretv nriimggsan ldiykadnss lelilrggvd
      481 fygqqsraif pkalqfqkls ngglngvsvq getqnknynl saflvhnfnt asdisfrtqa
      541 gltneffdqn tqlisatglv asetnvdqaa ntgvnqtrlr qedsgffvqe einfqdkfia
      601 tfgvrgdkss nngdanklny ypkgslavnl nefgfwsdgs kwnqfklraa ygeagnfppf
      661 galftsynaf ttdgllgisl igirgdktlk serqkelefg tdiaffnnrl slsgtyyikt
      721 iddlilrasl epstgfttef vnagelqnkg ieislnttpv mtddfqwdlg vnffqnrsei
      781 trldvepfnv gafgatlgty rieegssatq ivgigpnpgd ngfqkfgdse adfqmsfnns
      841 lnykslqltf lwhwkkggdn vnlttllsdl ngtthdyddv aldpdgvlgn gdyrlsqlgs
      901 saevfvedas ylrlrelgly yslpdrllsg iiggnidaik lgvsgtnlin ifdynsydpe
      961 vsnfgggtif tgvevtpfps skrilfhlgi nf
//
LOCUS       WP_100803204            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacter sp.
            MAR_2010_11].
ACCESSION   WP_100803204
VERSION     WP_100803204.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacter sp. MAR_2010_11
  ORGANISM  Ulvibacter sp. MAR_2010_11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacter.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Ulvibacter sp. MAR_2010_11"
                     /db_xref="taxon:1250229"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117710
     Region          25..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfsgilt lllafvvqlt faqektisgs vtdntglplp gvnivvkgts ngtqtdfdgn
       61 ysiqtaigqt lvysyvgftt ierpvtaatn sisvqlqeda avleevvvta sgikkekkal
      121 gyavssvkee aikdnpetdl trilsgksag idittqngls gsankviirg mnsfsgdnna
      181 lyvidgvpys ndtnaagsfv dgnmgtsrsf didpsnieni dilkglaatt lygtegrngv
      241 ilittktgss knlaskqeve lsssyffnev aslpdyqnky gggfdqaygl fysnwgpgfy
      301 kdgvggwgaf vddtntdvnk pynsdgtlph pystsaylas nfpdfqaqfe glrykwepqn
      361 sverffktgt vasfaanirg rsednkynyg msfahvsdeg ftpgnevdrs nltvsggaql
      421 snkinvrgsl nytltnlktp pvsasfgssi fgsgssvfgd llytprsidf fslpfeapdg
      481 ssiyyrddna iqhplwtvkn srfaqkvnrv ngfgaidfni tdnlnlsyqa svdtysedni
      541 nrqnkggvtg valtdsgfys tynnantifd hkvvlsgsny smlndnltid flagatsrst
      601 dynrigvtsy gqqvfdffdh ggfsssnpie fhqkrnilgl ygqvgfdikr ffyvnfagrn
      661 dwvsnavnns lfypsasvsf iptsafpglk sdgginylkl ragygtsanf stgyptvtnv
      721 vlnaqswlds nnnfitsntt nstigntnik pelfselefg veanlfqrvr ldfsyytrtt
      781 ndliiqdqki alstgasttd tnigeiksdg ievdlgidii ksdgfnwnfn vnftksesev
      841 tdlgqdteli iyegftnlgn garvgyplgs mfgariarde ngnllvdgag nylsedided
      901 gllpfigdpn pdfimnysnt fsykglslnv avghtsggdm ysvtiaslmg rglttdtedr
      961 lstyilpgvn sttglpntvq innsnfyfdn gfaspadels iydasvvrlr evslgyslps
     1021 kllektpfgk ivikasgynl wydayntpeg infdpnvsgl gagngqgfef ltgpsskryg
     1081 fsvnatf
//
LOCUS       WP_100803207            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacter sp.
            MAR_2010_11].
ACCESSION   WP_100803207
VERSION     WP_100803207.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacter sp. MAR_2010_11
  ORGANISM  Ulvibacter sp. MAR_2010_11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacter.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Ulvibacter sp. MAR_2010_11"
                     /db_xref="taxon:1250229"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112372
     Region          25..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkirgilt illalvvqvt faqektvsgt vsddtglplp ganiiiketn tgtqsdfdgn
       61 ytitasigqt lvfsyvgfdt qefkvgaans invnmvagnm lsevvvtgys trnqtvqtsa
      121 vvsisaseis elspttsvdn llqgkaagvq vtaangkpgq gafvrirgvg sltagasspl
      181 yvvdgavire edlgnipndd ienitilkda attarygsrg asgvvvittk ngnrnkdaiv
      241 kyssrygfts rikpnfnimn aeqklqyeae lyalgvttag slpgvttlpg sperqflldn
      301 qtdwqdlmlk egivqnnnvs fsggsekmdy yfsvghdrnt giidqldgfe rfnsrlnlnf
      361 dakdwlslgv nvgysrstsd eprdrnnvqn pframydynp yetefvlded gnvvldengn
      421 pvysathttf nvrgallsep aiqiennlla svdaevrftk dfsyginvaa nsvnqrnesy
      481 skpggildai igdpnnpgnk ldtgiyrydf tisnrlnynl sannhhlnal glfeynknqn
      541 sgyrlrsigf psallttqsn aneptlastt rdvitlvsyg vfadydykek ylasasvryd
      601 gssnfgsdnr fgvfysgslg wniakedffq vdaindlklr aaygtvgnrn giaryasqsl
      661 vtfgsypggs gtqvgnfgnp gikwettttt nvglefnlfn rrvrgvtdyf irrtedllfl
      721 iptadeagvi dtagqlgvvg nlgiienrgl evslqgdifk senfkwtlgg nivfldteiv
      781 elpdndgdge gddvfpntaf niayregqmi nehyliryag vdpatgaply ygadgntyra
      841 gdlpdgenrv fqgkstiadk eggffsnity kgfglrtdfv fkagnwvnnf vksnlisdga
      901 niddnqalda fnywqqpgdt nvypsplisq eelqavnsdr flekgdyvrm rnitlsynfs
      961 rsmlanspln afrvyvqgqn lltftkffgd pevglssget isfansvapg eatlysypnt
     1021 ksiqvgidvs f
//
LOCUS       WP_100812257             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium sp. BR1].
ACCESSION   WP_100812257
VERSION     WP_100812257.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. BR1
  ORGANISM  Microbacterium sp. BR1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Microbacterium sp. BR1"
                     /db_xref="taxon:1070896"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52992
     Region          3..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msqigivaeg prekrvaatp atitklialg ydvvveagag aassfpdaay aasgatvvsa
       61 seawasmivl kvdaptpeev arladgatli allspalrsd lveslatrei taialdavpr
      121 israqsmdvl ssmanisgyr avieaanefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvasigge ylevvvpdea kevstdgyak attaaydrra
      241 aeiyseqaad vdiiittali pgraaprlit aadvarmkpg svivdmaaaq ggnvegsveg
      301 ervvtdngvv ilgftdlpgr lpqqasqlfa tnlvnlikll tpgkdgqlhl dfddvvqrtv
      361 tvvrrgevtw ppppvqvsaa pqktvaapsv aaelkkpmss rargwlvaag iavlfavcaf
      421 appplpqhfl vltlsvvvgf yvighvahal htplmsvtna isgiiivgam vqimapdltv
      481 qilaavgvll asinifggfa vtrrmlamfq kgqnr
//
LOCUS       WP_100841612            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 5].
ACCESSION   WP_100841612
VERSION     WP_100841612.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 5
  ORGANISM  Flavobacterium sp. 5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Flavobacterium sp. 5"
                     /db_xref="taxon:2035199"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113282
     Region          36..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikqhfkkg ltsfyaltil lgllmtnema aqknttisgv ikddtgltmp gvniiekgtn
       61 nstttdfdgk falklttdna alvisfisfq tqtitvagrs sldiklksee qtlkevvvvg
      121 ygtvkksdvt gaistikpet iternvinpl eaiqgstpgv qitsssgrsg dgynvvirgn
      181 nsllsnstpl yvvdgvptdn idflnpqdia rmdvlkdass aaiygsrgas gviiiatksg
      241 ttakagisvs letsygtkna vrlpemmtga ewwqyhqtay lsatpltqtp aqlataagtn
      301 spllvsrans gysfdwydai lqpgmtanny invsgradng lsynmafgiq ndkglidkds
      361 ndkysfklgv nhrinnkfst ganltiarle telgsdfamq egtrfsplms pyavdadgne
      421 ipgqlffqpg kltypdgtwa inktstvnpl meianssqte kswqtignvy fqyqalewls
      481 fkttfaagif ngvnssayga kttagvklsp aginsasikn iqnfnytwdn qidlkhtfnq
      541 dhtvsalllq smysnvdens fmysnnqpfe vgsnnmgsgv qtsyqitsgy akntlnsyav
      601 rvnygykdky litasnrwdg ssvlsegnkw asfpsvavgw ninkesflen nntisnlklr
      661 vsfgytgndn vapytsqall nqqtfyangg ntvagwqskn lantdltwek trelnlgldf
      721 gflgnkitgs vdvydrlsdk liyeqklpye tgwdktfsnv gsvsnkgiev glttkniksn
      781 lvdwetsftf tknvnklesi ynqdqvsdig ntlilgselk pnynyvydgv wqeseatqaa
      841 tygmypgqak ikdvngdgkf naadrtvign anpewqgsiy sklkvgqfdl nfsiltsqgq
      901 tvlstfhqnf advsgrsfqk ipmdyfvptn gaglqanasn anprpgpast tagagpfwss
      961 gmayyrevdy vkiknislgy sfgpdllkkl kmsnlriyvn vldpfvftdf dgydpewaga
     1021 afginrpasv ttqlglsvkf
//
LOCUS       WP_100842529             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 5].
ACCESSION   WP_100842529
VERSION     WP_100842529.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 5
  ORGANISM  Flavobacterium sp. 5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Flavobacterium sp. 5"
                     /db_xref="taxon:2035199"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107996
     Region          24..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiykkllf lflllpfcaf sqnvvkgtvl dsgsgqpipg vnvkvqgtpn gvstdfdgkf
       61 qipnakqgdk ivftfmgykn eiitftnqkt ltvslesean qlvevkiqvg ygsvkkkdat
      121 gavvalgakd fnkganvtte dlfkgkvagl tvnstgapga ksemrirggs slfasndpli
      181 vidglpldnn tnigsssfla slnpstvesi avlkdasata iygsrasngv iiittkkgsk
      241 tlavdynvmy gfgklvktvd vfsaddyral iaesdknrgt nyssklgtan tdwqkeiyrs
      301 tgyldqnlsv rgnllnvipt sltlgntnqq glrltnefer ntvglvmnpa ffdnhlklkl
      361 aanyaneknr ftdgvegaai gfdptqpvrv dgapyggffe yttginsdgk ytldpnsarn
      421 pvsqllmvnd rgtsnrvfgn fevdyklhff pdlravvnvg fdqsngerkr lvgddagsaa
      481 annnvpygtn eyteatkrnk lldtyfaynk kvnefnidat agysyqrfes tkfetgniln
      541 pdlastfpet tidtdvvlig lfgraninfq dkylltlsyr rdgssrfeee nrwgnfpaaa
      601 fawkmkedff kdsktisdfk frvsygitgq qdipepngyl qkynlgggns qyyfgdvsmp
      661 valpskrtkd lkweetsvfn igvdfglfnn rlttavdvfa keskdllvna aisdgsnfsn
      721 rvyqnvgsft tkgvelsina ivlqsdsfnw nvnltatkfe rrikdlvnnt dillgdniag
      781 tgtpgqvfse gyapysyyvf kqlydtagkp idgafading dgvkndadky iyhnpdpdav
      841 fgfsssmnyk hidfsfnlra signrifnai dasraqfdnl enggvlsnvp ssilqtgfqt
      901 tsnvvlsdiy iedasflkmd nislgytftn wlndkatlrv stgvqnafvi tkysgldpei
      961 tnngvdktiy prqrsilfgl nikf
//
LOCUS       WP_100843376            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 5].
ACCESSION   WP_100843376
VERSION     WP_100843376.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 5
  ORGANISM  Flavobacterium sp. 5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Flavobacterium sp. 5"
                     /db_xref="taxon:2035199"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112693
     Region          25..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv llvvlvaqlt faqersvsgv vsdnagmplp gvsvlikgtk ngtqsdfdgk
       61 fsikaqpsdv lifsyigmkt seksanstti nvklasdatq lesvvvtgna kgrsikemty
      121 svgqvnasal ekvpaldait alqgkvsglk insasgepgs eiavqlrsan slstgqkpmv
      181 ildgvilegg ladintqdie rievvkgaag aslygsraas gviqifskrg kglngksrit
      241 yrtesgfsni tnkldlatqh kyeltpdgtd faydatgnri vetdnlgnnp ypskykmydl
      301 qdrvyrsgsf tshhlavegg ndptnfllsy drqdsksvid ltntysrnnf rlnldhkisd
      361 kfkigasmvy snskkdpfim gnngvlfdai ilepisnlda pnangtpfly qpseftttee
      421 nplyiiannd rteernrfig synaaydvtk wfkataeysi dfeqsnfvdf fnkgylgskp
      481 rtnlnngyla katfsgkaen lraeglfsks fgdfngnlkv gflderyknd fsrtegsgla
      541 vsdiktldnl lgptkqttsr seeiitdsyy gvldadylkr alfsvayrie gsslfgentr
      601 wnnyyrasga yriitsdsni ngieefklra sigtagirpl ygmrdetftl qngtaskstl
      661 gneelrpava keielgfnis flkrfnaefn yvktntddqi llvplngltg ysgqwrnage
      721 meassyeasl gvniinnkdw nwdlnvlwdk ssqkvkrldv psyytgpgtq essfflvaqg
      781 enfgamygdk fittlndlps glnqsdynin skgyvvsntt glpvkykddk gntnvkigdi
      841 tpdfnmsftt nlrykdftly gliywkkggd iynkvkqwly rdsrsadiqn egltddfyas
      901 aaglyntnqa ssafvedgsf vrlkecslyy tltkekigkn vgfidevkfg ivgrnlltft
      961 dytgqdpeis spsentrtel tsrstdgtgs nsnnpggdpn vfkvdnfsyp tlksfslsvq
     1021 fkf
//
LOCUS       WP_100843378            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 5].
ACCESSION   WP_100843378
VERSION     WP_100843378.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 5
  ORGANISM  Flavobacterium sp. 5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Flavobacterium sp. 5"
                     /db_xref="taxon:2035199"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114012
     Region          25..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv llvvlvaqlt faqersvsgi vsdnagmplp gvsvlikgtk ngtqsdfdgk
       61 ytikaapsdi lvftyvgmkp seksassttv ntkltsdatq leivvvtamg ikrekkalgy
      121 atqevkaeel tkgnnnslag alqgklagvq itpssgapga ssqivirgar sftgnntply
      181 vidgmpvasq adystgdsvt gsdssnraid idpndiesin vlkgqaasai yglrasngvi
      241 vittksgkga skngkptisf stsitadnvs rkpdyqteya qgstntydpt sslswgpkis
      301 slpndpkygg nisnvlnggd ittnagkyyv pqratagldp wvspkvydnf gdffktgitv
      361 nnsfsitqat eksnyafslg ssnqdgfipa tgfdrynaka afstklsdew ktgfvgnyvq
      421 tkiekatgan dssvagafas pisydlkgng yenpldpykq iyyrptgfnn pywaaahnif
      481 deqtdrfygn syvefapkis tndqhkisfr yqlgadsytt nyrdiqeygn kqttqghldl
      541 ygitsrtins lftvnyeyki sddlnltala gneindryek sydmigndln fggwanlgna
      601 kqtvatdnit knrtfglfgn lnlsyknfif lgttvrkdiv ssmprdnrsf vypsvslglv
      661 ltelealkgn stisfaklrg swaevgqagt yfdnyytvps ygggfwansp vnyplggins
      721 yipnnlvyds nlkpqntksy elggelrlfe nrisidytya rqnvidqifd vplagstgaa
      781 syrtnggkih tnshellvtv ipvkttnfdw tlsanftktd nyvdelkpgv dniflggfst
      841 pqirasvger fpviygtsfa rddkgniivd skglalaget kalgqvapkf nlggstsfry
      901 kqitlaatfe wknggkmysg tnslldtygl saktgnrdel lvqegvtktg evntkgatkq
      961 dtytrysnia esaiydasfv klreisigyt mpqfskgfdi rfsafarnil lssklpnldp
     1021 essqgnnnma ggferlsipq ttsvgvgmnl tin
//
LOCUS       WP_100843742            1241 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 5].
ACCESSION   WP_100843742
VERSION     WP_100843742.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 5
  ORGANISM  Flavobacterium sp. 5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1241)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1241)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1241)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1241
                     /organism="Flavobacterium sp. 5"
                     /db_xref="taxon:2035199"
     Protein         1..1241
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=137901
     Region          144..1240
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkpvvkqrl lyrimkitlf qmvlafvfst vmmansakgq kkldtkvtis itnlslsnal
       61 skleksanvk fsynsritql nqkvnitand ellstilnei llplsinyse vsnqivleni
      121 takestnlgl lgtlnsnlia ativkgkvid sngnplpgas vlvkgskvat ltdfdggfsl
      181 evptgstklv isyigmqtke itvsgdyvtv vlselgqnln eviittgyek tskrtftgaa
      241 skitdkelkv dgvvdvsrmi egkaagvtvq nvtgtfgtap kitvrgsssi fgdtkplwvi
      301 dgvvqediin lsfadlasgn setllsssia glnandiqsi eilkdasats iygsrslngv
      361 vvvttkqgrr dsplkitysl eqslrtvpny nqydilnsqe smsifkemea kgyldlpttv
      421 ngryggayni lgraintyvp etnsylvnnd pvsrnnflkk yelantdwfn vlfrpsitqn
      481 hslsfsgggk nntfyaslgy ysdpgwtiad qvkqlssnik gtffvndkln itlstlasvr
      541 nqdapgsyes ekdevfgkvt rdfdinpfny vlntsrtlrp ydengnleyy rnnwasmnii
      601 nelknnymei evkdirfqld ldykinshlt ydltgsarya ntsrehkile nsnvvgayka
      661 gtpegedgvn tlvrdqnvfl yqdpndltap kvsvlpnggf lrkftndmts ynlrnsityr
      721 ntfkekhele gffgtelrsv drnsdnftaa glqydrglta ftdpriiekv inggdsyygf
      781 nvekertvgf fgklgytydr rytasvtgry dgsnrqgdsg ssrwlptytf sgkwnlseen
      841 fmknatavnn lslrgsyglt atagpatnsl aiyksyvtdr fnlddresgi qidqlqngsl
      901 twekqfetnl gvdlamfnnr iqfttdvysr kafdlvdyvi tsgiggqrik qgnnanmetk
      961 glevgfttkn insanfkwst tlnfsvynqe itklenkpta fdlidgnggn tvghprnsiy
     1021 syqftglnnq glptfimadg ekdnitgadf qdnknvtdyl kyegsiepnk siglantfty
     1081 knwslyvffv gsggnkvrln pvydstyddl tvftkeftnr winpgdenyt nvpviadkrl
     1141 nsnyggsrtl arayntynys dvrvadgdfv rlknislswe fpkdfkkklg vtaftlrgss
     1201 vnpwliysdk klngqdpefr ntggvampvt tqytfainls f
//
LOCUS       WP_100843997            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 5].
ACCESSION   WP_100843997
VERSION     WP_100843997.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 5
  ORGANISM  Flavobacterium sp. 5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Flavobacterium sp. 5"
                     /db_xref="taxon:2035199"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111234
     Region          44..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknisfykgg rafyyliimg silsfsplqa npflrqnklq sqqfqiqgtv tdgsnplpgv
       61 siaiknktkt atvtdyngey nlfaspkdtl vfsyvgfktv fvavhdqpvi nvvlqadatt
      121 lkevkinagy ysvkesertg siaritakdi esqpvsnvla tmqgrmagvd iiqdggtagg
      181 gftikirgln slrangnepl yiidgvpyss etigysdttp gmatptspln sinpsdvesi
      241 evlkdadata iygsrgangv vlvttkkgra gktkvsvtas tgigkvtkmv dmmhtqdyln
      301 mrrqgfvndk itayprtayd vngswdqnry tdwqeellgg tatifsmqgv vsggsdltqy
      361 llsgtyrset tvipgdfgyd rtavhfnmnh asedkkfklv fsagysfqqn vqptedltrk
      421 arnlapnapa lydengelny enntfqnpla plksfstakt ndlvtnavls yevvpslelk
      481 anlgftdlnn geqqiipsti ynpayeigsd nsilytnata rqswivepql hwshnfensk
      541 idilvgataq qqrssrlyqy gvgfssnsli tdlasatdky viasdetiyk yqaffgriny
      601 nyqekyivnl tgrrdgssrf gpgkqfaafg aigaawlfsn enflknnsvv sfgklrasyg
      661 tggndqigdy qfldtyassg lnyqnavgld ptrlfnpdfg wessqkfeva letgffqdrl
      721 fltlahyrnq ssnqlvgipl pgttgftsin anldatvqns gleltlrtvn ysgthfkwts
      781 nfnisaaknk llsfpglegs tysnryivge stsivkvyny kgvnpqtglf evedvngdgk
      841 italddkkrv edltpeyygg lqnvlqyknw qldflfqfvk qknydwspsv qggsffnqqe
      901 dlvnawqkpg diapyqmyts grnrpavtay nnylnsnami vdgsylrlkn ielsymlplq
      961 tkkascrlsl qgqnvltctp ykggdpefky tgylpplqvy sagvqltf
//
LOCUS       WP_100844381            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 5].
ACCESSION   WP_100844381
VERSION     WP_100844381.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 5
  ORGANISM  Flavobacterium sp. 5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Flavobacterium sp. 5"
                     /db_xref="taxon:2035199"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111333
     Region          44..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnfsffrgg kafcflflmg vilsfsplqa nnslrhslvt iqqfkiqgtv tdggnplagv
       61 sisikgkpna tvtdynghyt lsaspedilv fsyigyrtqq vsvqgrttin islqenttkl
      121 qevkinagyy svknsertgs iskittkdie kqpvtnvlat mqgrmagvdi tqdtgtpggg
      181 fqikirglns lreegneply iidgvpysse vigysnttsg iptptsplns inpndiesie
      241 vlkdadatai ygsrgangvv littkkgkag ktnvtvsass gigkvtkmid lmntqqylem
      301 rrqgfandgv ttypdwaydi ngtwdqnrnt dwqkellggt avitnmqasv sggsdltqyl
      361 lsgtyhtett vlpgdfeydk aavhfsmnhr sedkkfkltf stgytaqdnl qpetdisrta
      421 rnlapnapal ydadgnlnfe nstfrnplaa lraittaktn dliantvlsy qispswelka
      481 nlgltdlkna eqrllpstmy dpayglgsnr ssmfsnntqr kswivepqlr wnhdfgiski
      541 dilvggtaqq qtssrlylfg ygfasnsqit diasatqksi yvsdetlyky qaffgrlnyn
      601 wdqkyivnit grrdgssrfg pgkqfatfga vgaawlfske nflkentvls fgklrasygs
      661 sgsdqigdyq yldtytssgl nyngaigldp trlynpdfsw einkkleaal emgllsdrif
      721 ftlawyrnrs snqlvgiplp gttgfssina nlnatvqnmg leftlrtlnf esrnfkwttn
      781 fnisashnkl lsfpglegst ysnryviges tsivktyqln gvnpqtglye vedinkdgmi
      841 tsledkknie dltpkyfggl enqfqygnwq ldflfqfvkq knydyspsvp ggsffnqnsd
      901 mtnawqhagd qvpfqmntsg engdavnayy nyldsnasiv nasfirlknv alsydlpqqa
      961 ikgvhckisl lgqnvltftp ykggdpefky taylpplrii tagvqltf
//
LOCUS       WP_100844823            1013 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 5].
ACCESSION   WP_100844823
VERSION     WP_100844823.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 5
  ORGANISM  Flavobacterium sp. 5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Flavobacterium sp. 5"
                     /db_xref="taxon:2035199"
     Protein         1..1013
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108876
     Region          22..1012
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkiflivmv ifttqvtlaq vktikglvsd akgiplpsan isvkgesnst stdfdgsfti
       61 eaktgatlei sylgyetksv tvgesntinv klneagstal tevvvtslgi kkskksltys
      121 aqelkgeevt rvkdanmmns lsgkvagliv gkssagaggs vkvtirgnss atsnqplyvi
      181 dgipmlnsss tqsnqvfgdt aggnrdggda ismmnpddie smtvlkgasa salygsqgan
      241 gvilvttkkg kegkvtanfn ssvfadnvvs lpefqtsyga eagatttwga kknspdhvkd
      301 fyntgmtyin svginggtdk mstsltfant kvdgiiptne fkknnialrq sikmfddrvt
      361 vdaslsyaeq kivnkpvnal yfnpltgvyl fprgndfdyy knnfevfdpa rnlmtqnwpt
      421 gtsdiiqnpy wilnrnqsid knqslissaa isykannwls vkarggynkl sntfdkrmya
      481 gtnltlsgan gryiysdses sqlygdliat intkfndafs fnavvgtslt kstvndaiin
      541 dsgttkgglv yanwfnignf dsvgknnqlv gankevqsvf asatfgyqem lfldvtgrnd
      601 wsstlvntdn lgffypsvgl taiisemvkl peaitfgkvr asyaqvgndv gaflttplnt
      661 ivggqfsvpq vgqsptsslk pekqnsfelg tewrfaqnri gfdftyyqne tknqliqapa
      721 pvpntigyan yafnagsiqn kgfeitlsak pviagdfswd lnlnyasnkn tvldlgpgvn
      781 ggvntvvltn gdpnsyryvl evgkpfgqiq gknivrndqg qilldadgri qktafqdlgs
      841 snpdfmlgfs ntfkykkafl nvlvdgrfgg hvmsmtqaml dfygvsqvta dardaggvai
      901 navdtngnav ttmsakdyyn qvgdrsgatg eymykatnvk lgelslgysf dfskttifkt
      961 vnvslvgknl fffykdapfd pnvtlssgeg lqgvdifgmp strsigvnln ltf
//
LOCUS       WP_100844862            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 5].
ACCESSION   WP_100844862
VERSION     WP_100844862.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 5
  ORGANISM  Flavobacterium sp. 5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Flavobacterium sp. 5"
                     /db_xref="taxon:2035199"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117211
     Region          45..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrvksknv klskiilllc lvslfkvsii raetfdmtfe qsqdrilkgk vvneigspln
       61 gvnvvvkgts rgtvtdkngd ftidvpekkn vlifsyismk dqevtingqn ditvvmtdqa
      121 eslkevvlig yqsvqkktvt gamttvkakd ienvpyasid qilagkvagl tslstsgepg
      181 artvtnirgs nsvglggisy plyvvdgiiy dindmpssyg nnplaslnpn eiesvdvlkd
      241 asasaiygsr gangvilikt kagsknqrpt frvnaytgig lkpslrtvtv grlerqlkld
      301 aisknykdld hnfhmgltds lnvafnnhtd wqdlfiqnak isnvdasvsg afgknqykvs
      361 lgyydetgvi igyrlkrfsp tmflslyltd kinftvnvmp sfmdtkhgfg ngetfpfstw
      421 afpssfwnis dkqkkaykge agnldddkrv gllanarlni nftkdllfts sfsynffenr
      481 rdqfqsafiy qvdkdaavse hfvtnineie nyltytksln dqhhfsailg lqassqdnks
      541 sylrgqgslg stvsgispgv dlsgnsyiee kkrmgvfgrf sydykekylf sssyrrdgss
      601 rynsgerwtd fysvatgwlv seesffepvk evvnflkfrg sygvtgndpa syyaqyniyt
      661 gnasydgssf gvnnpaqaat yngvptvsqn ysdfagskdv twekypqvnv gidlnmfnnr
      721 vqinadwyar dsqdvfystl vapatsgynf ysgnavnirn tgyeftlstv nlgntsnfkw
      781 stsfniafnd nyvtklpdgg kdltvgppwl qytltegmpl fnyrvwdiqg vyatdaevpt
      841 dpltgqkmkf ygetikagdp kyvdqngdhi idnldkkyag spnpkasggi sndfryknws
      901 msifcnfvyg rkiwnayisd rlngsrtaap wadwgsratl giiqdlnyyq gpgdttaeyg
      961 svisnnsnvd rfnvansqyi edgsffrikn irlgysvper fgkkiglsal qfygmadnva
     1021 lftkstlpdp eavgsdgyss gnnyplaikf tlglsatf
//
LOCUS       WP_100845053            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 5].
ACCESSION   WP_100845053
VERSION     WP_100845053.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 5
  ORGANISM  Flavobacterium sp. 5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Flavobacterium sp. 5"
                     /db_xref="taxon:2035199"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114024
     Region          39..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklitllf iggiifsgna teaaikkqrf dqksaqveis gqvigqddgm piagatiyak
       61 snnkiatitd esgrfklnvp enethiiisy igyarlefnl qqttdliiki kpaenvleqv
      121 vvtalgvkks nkavsyavte lkgneftkak esnianalvg kiagvnvsst atgpngstrv
      181 virgngslng nnqpmyvvnd lpidntqlnl pgigngagst rinvdrgdgt svinpddiks
      241 itvlkggtaa alyganaang viliqtkrgs aqkgigveyn tsftfetpsi ipdwqyeygs
      301 gaggkkpttk eeaiadgrws wgakmdgsnv iqfdgverpy vaqknniknf yktgttfins
      361 ialsggneka tgrlsflnmd nqgvvpnsdf nrksvniasn vnltnwlkfd avvqynleks
      421 nnrptvsdae anpnwgtymi antvdirnls pgydengiee awnpvavatn pyfavnkiqn
      481 sdtknrfigm lnvkvnftpe lflqgrigqd ytdyeffgyi pkttlnnpvg yaqgsrmkls
      541 nlnseailny tkkniydnfs lnalvgvnsr tnlrdetkve gsnfvlddfy alsnlstlty
      601 typygktktn svygavdldy knlvflnftg rqdwfstlsa enntvfypsv gtsvilseiv
      661 kmpewvsftk lrtswaqvgg atpdpyalnq sysmvqgghn gqqlqtptst rvpnstlspl
      721 tsttfeigad lgflnnrlni dfawynratt ddivettisn asgantalln lgkmrnkgve
      781 llvsgkiias gnfswdasfn gaynkntvea ltdqlssitm atsvngyvti tsdvgrpyst
      841 ikgykpltda ngntvynvsg gsatiargpl eelgqgvhpw sagisnefky ksfsfsflvd
      901 gkfggslysg tdlygtrmgl tkltlegren glpikgvdtk gnpvdmviap enlrtyydgl
      961 ksisstfvyd asfvklrqvv fgyqlpiekl kglsklqgas isfiarnlfi lykktpnvdp
     1021 esvfsagnaq gveqfgvpkt rsfglslnvk f
//
LOCUS       WP_100850563             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. SGAir0191].
ACCESSION   WP_100850563
VERSION     WP_100850563.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. SGAir0191
  ORGANISM  Pseudomonas sp. SGAir0191
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. SGAir0191"
                     /db_xref="taxon:2217867"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38756
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikkligqg hqvtvqqgag vnasipdsay eavgarlgsa
       61 aeaygaqlvl kvvaptddel almssgsllv gmlnpfnndi iakmaarglt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee rdcaqgvggy arpmpaswmq
      241 rqaqsvhera rqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adevvhahgv tivgptnlpa lvaadastly arnlldftkl lfdkdgalti nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_100846657             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas baetica].
ACCESSION   WP_100846657
VERSION     WP_100846657.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas baetica
  ORGANISM  Pseudomonas baetica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas baetica"
                     /db_xref="taxon:674054"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38839
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_100857072             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter spanius].
ACCESSION   WP_100857072
VERSION     WP_100857072.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter spanius
  ORGANISM  Achromobacter spanius
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter spanius"
                     /db_xref="taxon:217203"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38560
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkylggk htvvvergag aaarypdday eaagatlgsa
       61 qdalgaelvl kvrapsptel phmkpgavvi gmldpfdaeg iehmaatglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaegkggy aramppgwma
      241 rqaalvserc kqadivitta lipgrpaptl vsadtvaamr pgsvlvdlav erggncplse
      301 kgqivekhgv tiigltnlpg lvatdasaly arnvmdflkl iinadgalai qrddeivvac
      361 lvceggnvar rt
//
LOCUS       WP_100859116             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas lusitana].
ACCESSION   WP_100859116
VERSION     WP_100859116.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas lusitana
  ORGANISM  Aeromonas lusitana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas lusitana"
                     /db_xref="taxon:931529"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53420
     Region          25..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsqntlw rpglaalllt almgtsslvq adetapkgki earnelfakd hidqfdswts
       61 tsesaertda laedpqmvvl wagypfskdy nkprghfyal tdvreslrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf ngptkavkfp wdkgtrveqm
      241 eeyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqskemlqdi vhqrkeaite iklkvekqlv hahfeakaaw
      361 dagateaemk diqqdirhaq wrwdfsiash gvqahapeva lrmlgsaldk aadartklar
      421 llatkgishe iaipdisske kaqaalgmdm kqmnadkaqf lkttvpawea eakaagrlaq
//
LOCUS       WP_100860004             508 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Aeromonas].
ACCESSION   WP_100860004
VERSION     WP_100860004.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53411
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevaieagag llasfddaaf eaagasvvps
       61 vwqadlifkv naptdaeiaq ikdgatlvsf iwpaqnpelv kklserninv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggefl kldfgsedga ssdgyakvms defikaemel
      241 faqqakevdi iittalipgr papklitkem vdsmkpgsvi vdlaaatggn ceytvptelf
      301 vtpngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgnvaidfe dvvqrnmtvi
      361 qagdvtfppp piavsaapqk paakaapkka eekkpsnkkf vwgalgiaaf gwvaavapaa
      421 flshftvfil acvvgyyvvw nvshslhtpl msvtnaisgi ivvgallqig qgstlvtvla
      481 fiavliasin ifggftvtqr mlkmfrkd
//
LOCUS       WP_100874736             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium sp. 64].
ACCESSION   WP_100874736
VERSION     WP_100874736.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. 64
  ORGANISM  Janthinobacterium sp. 64
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium sp. 64"
                     /db_xref="taxon:2035208"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38667
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qiivqagagl qasipdeaya aagaqigtaq
       61 eaygcaivlk vrapdagera lmasgtvlvg mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpflteeek eiakgaggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvvkhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_100883871             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Prochlorococcus marinus].
ACCESSION   WP_100883871
VERSION     WP_100883871.1
KEYWORDS    RefSeq.
SOURCE      Prochlorococcus marinus
  ORGANISM  Prochlorococcus marinus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Prochlorococcus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Prochlorococcus marinus"
                     /db_xref="taxon:1219"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39726
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtkilipset ssgerrvsat peavkklksl gcdvfiessa gklsgfsdls yeesgatiin
       61 nldqkiwgea dlifcvqtps ednltklkkg avllgllnpy gnkellriin snkisalsle
      121 llprisraqs sdvlssqani agykavllaa seldryfpml mtaagtvqpa kvvvlgggva
      181 glqavatakr lgaivfvsdi rpavkeqves lgarfielpe veekpgeagg yakavtpefl
      241 skqkatltky lseadvaict aqvlgkkapv lidspmiekm rpgavvidla vsqggncegt
      301 ksnetiikng vkligagelp ssvpydassl yaknltslit pfikdgvikl dkedelisgc
      361 llsdegvvlq nkvfen
//
LOCUS       WP_100894105            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100894105
VERSION     WP_100894105.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114145
     Region          21..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnfritfivm lfvccfsygq qtitgsvvde gntplmgvsi vvanttngtt tdfdgnytin
       61 aakgdvltfs smgfktkqit vlnaavinvt lledaaalee vvvtalgikr ekkalgyavq
      121 evkgasleka kepnlvnslt gkvaglnikn stdlfqnpei slrgatplvv idgipdrsad
      181 iwkinsddve sisvlkgata salygsagrn gaimitskkg ekgrltvtvn ssvlfqpsfi
      241 kvpdvqrvyg ngnqgqyayi nglgsgsegg gwiwgpkvnq ldpstvsgff ettqynsptd
      301 aagnlipipf tsrgkdnikd ffqtgsiqtn nvsvnwgndk asyrmsvsnv yqkgivpntd
      361 lgntsfaigg tlnpsdnfkv ssnltynkqy tdnfpevgyg ptnylynlvl wtgvdvdvkd
      421 lrnywregqe gyqqrhfnvs yynnpyfqay eyergydkdn iygnvafeyn itpelsvkst
      481 sginvyslnr tykepksyvg ygnkslgnft nadsryfdii tdfglkfekn fsdnftlkse
      541 vaysnyyrks taastqtdgl nipgfynlan nagvsyiasn leqeeaiksv ygfvdmsfyn
      601 afylsitgrn dkvstlpken nsffypsvsg slvlsslfdm pqaisfaklr gswsrvsegk
      661 igddpysyiq aydkgttwng ntsasfgssl lspglepets dtwevganvr lfnnrlgldv
      721 ayfeakdynn liyspisegs gfesillngd eykrkglefv fdakpiqtan fswdmlvnfs
      781 rfrrfqeeiy gdreqtegfv kvgertdqiy anvyqtnssg eviyengfpv ndpyqryigd
      841 ddpdwtygit ntfkyknlnl sflfdgrigg liysttnqkm wwggkhkgtv kqfrddanng
      901 issyiapgvk vvsgtatydv ngnitsdtrt yapndvavny infmqttsng qnknyhyyke
      961 sfvklrevtl tynfpkkalt ntpihefsls ligrnlwlns dvpnvdpdsg vdalqapstr
     1021 niglnlnvkf
//
LOCUS       WP_100894341            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100894341
VERSION     WP_100894341.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116303
     Region          22..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiaiiavvq lfaltvfaqs ntytskildt dnqpipfatv keigkenytt ttidgdftlq
       61 tsstsfviqv ssigftskki titngnfpas itlmpsdeql keivvtalgi erekqslvsa
      121 vtrvssdklt evtltnvvns lagqvagvqi tngssgvgss srivirgens lsgsnqplfv
      181 vdgvpisneq itsdlvnnga lqevdfgngg seispddias isilkgagsa alygaraang
      241 vvvittkrgk nkkgfgvtts nsltvetllt lpdyqnvygg gsngqysfqn gkgagvndgg
      301 lssygprldq gllvnqfnsp svdingnpvr agdviartna dgsftpitat pwvsnpnnvr
      361 nffetgitkq nniainssge ngssrlsysn lrnegivpnt dldrdgisls lhqklteqln
      421 vnafvnyint rsgnrpnlgy gyenplygfn wtgrqadvsa lknywqagqe gvqhydinyl
      481 wltnpyltvn entnsfnknr vlgnvsavyd itnklnvavr agldtyadkr efrravstna
      541 npqgsfredd isfrelntdi lvsykdaind dlkytvslga nrfdqeikys yaeasqlalp
      601 giytlansrt plkgdsrlfe krinsvygtg nlsykdalyl dltyrndwss tlpsnnnsfg
      661 yysaglsfva ssllklpepi sylnfrfsaa svgndtnpyq ntqnflfnqn ygsnfrvtne
      721 tvlknanlkp erlnayeagl etwffngrlq ldaaayqnts vdqiisrpis essgfgsfnv
      781 nggkvqttgl elllsgtvik nadfqwqssv nfstfkskvk elpsgvdqfv tgtanifsgg
      841 ggsnsvfyia kkdgrvgdmy gtgfvevdgq ivhdsngfpv qdpnlrllgn ynpdftmgfn
      901 nkfsyrgldf tflfdwrkgg tivsrtkalg stsgvlketl egresgiiga gvvntgtadn
      961 pqyspnttvv aaqaynnaff drgneasaly sasyvklrqv svyynfpaki vdaigfnkik
     1021 iglvgsnlll ftenphfdpe lnalqeqsit ygvedfsyps trsfgvslkt ef
//
LOCUS       WP_100894279            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100894279
VERSION     WP_100894279.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123586
     Region          22..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkflftlff vavtaawaqd trtitgevig aedgmplpga svyvsknmia netgvagvie
       61 ntsigvvvdf ngkfslklpi gvtqitvsyl gyqtktinlt asssytislk envdsldevi
      121 ltgyqkvekr kltssvakvk mddieqigvs svdqllqgqv agvvattqtg apgapakiri
      181 rgtaslsgpq dplwvvdglp ldgndvpdfs dkdnidqlrn yaiaglnpsd ieditilkda
      241 aataiygara angvivvttr rgksgkmrvn fsantffsak pnfdelnlmn sqqkvdfelg
      301 laartdldfr tnkgevtril snsgelgtyq tngfsslsta tqsqinalkn nnanwgdlly
      361 qtsvntqysl gisggtdtsd yyfslgyyde egttigtgle rynitlknnf disdrlsaga
      421 svflsqskke syltgtdaft npanysrnvn pyftpyaadg synydqdieg tdgryvpfnf
      481 leerentayn lknqavkaif dgaykitndl tfstqlglqf dktstekyaa eetyfsrker
      541 eksrrydssi sdyyyyflpe ggiiqnwned ffqynwksll tydtsfgkhe iegllgsefr
      601 rskftnimsr gfgynkntlt ttpiifpned tanessyqty dkttaenaya sfyatgsyty
      661 drkytffgsv rydgsnlfgv dpkykylplw svsgswlase edflktsdvi snlrfrgsyg
      721 lqgnidrnts pfvigeynkt silpgtseet ivvtsppnak lrwekttntn vgmdlglfng
      781 risiaadvyk rnstdliglr svplengfef tnlnwaevtn kgyeislstr nivtkdfswt
      841 tninishnks nvdkiqvrdn sflpsreglp vnavfalkta gidesgyplf krgdevvsav
      901 elfkltdpwa dffpgfites gltneefrdl fsyvgdqdpk ysggiintfk yknldftvaa
      961 nfnlkqtvve rqpyngtqid rgqnysarvl nawsptntts nlpgivgets gadgswmayk
     1021 wfsginpiet mplldtwvke msyirinsmr vgysfpkslt tklnissfrl nlegknllvf
     1081 gsnydgyfdp etygniyaqp isktialgln vtf
//
LOCUS       WP_100894455            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100894455
VERSION     WP_100894455.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116838
     Region          24..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknqltlii allaifvgys qgslkgkvld esnvplggas viikgtktgv atdfdgrfei
       61 nslqentvil vsyigyvtke vtitneafvt iqlfpdsekl neivvtalgi tksekkigya
      121 tqkieteiid einapnvgnl ftgqvaglsv snptgllqsp sfslrgktpl ividgiavet
      181 dffdvsanni adinvlkgtt asalygsrgr ngailittkn akveglevsv shntmvsagf
      241 tvfpetqtey gngsngkyef wdgkdggisd gdmiwgpkfe pgvlvsqwns piydnvtget
      301 tpwwgdvagt qyddksrysr vptpweyhnn lkdfmetgvi sstdfsiask sdkgsfrlsg
      361 nyssqkdrvp nselktggls fksrtkltns ltldsklsyn kvyspnyprh gygpknhmyt
      421 iliwmgddvd gqdlknhlyv pgqegyrqan wnyawynnvy faanelnqky danlinaqlk
      481 lnykitedfk lqargsavlk dvfedrespk tylnygdare gdyktwnner ltvdydilas
      541 ynkaindnis fdinagastf yrkyqqeyns tdglvvpfvy slnntkgnln astyleekai
      601 nsvygtlgld lynavfltva arndwsstlp kenrsyfyps aslstivsny itmpkaidyv
      661 kffgswakvs ndlspyntea yysnngvfgg nvklqypngl vnadikpess tsfelgmsta
      721 flknklsldv tyynvvdtnq iidlpisnts gfenrkvngn eyttnglevv lnatpirtdn
      781 frwdigtnws kkvkkiteiy gnndrynnlk lneradsyya tvwqksadgd lilgsnglpi
      841 kdnfqrnlgh sdpswtlglq nsfkfknlsv nvgidgvwgg lmrsltvekm wwggkhpnst
      901 efrdaeyaag qpvyvpkgvn vtsgelvtdt dgtvisdtre yqknttavsw qtwsqnypyr
      961 aavsykenkk fanifdrsff klrtlsfkyn ftelvniesi knlditlsgy nlfvwkkadi
     1021 idpdfgndnn lqdpstrylg lgvnvkf
//
LOCUS       WP_100895005            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100895005
VERSION     WP_100895005.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111686
     Region          25..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkvawilt pllvllmsfs ygqektitgn vtdqdglplp gvsvlvvgtt tgtqtdfdgn
       61 ytikasvgqv lrysyvgqkt adrkvgssst vnvqlaedae aleevivlgy stksvdevtg
      121 ssvqvssedi kdvpvlsvdq alqgkvaglq isttsgtpga qqdirirgvg sinasnsply
      181 vidgvpvvse nfsgsanrts lsslvslnsk diesmtvlkd asataaygar gsngvivitt
      241 krgksgkavf nfssvlgfqn naynkrsplt asqratlide atfnaygegf dferdeardf
      301 avannlgnia nwdgseydwp glmenkdali qdynfsasgg tektnyyasl gfneteptvi
      361 gdsfrrisgk lsfqtwlrdn vkldnsinvs nsrqnpvlen gaffnnphlt ryymtpfanp
      421 ynadgtynin nlgtsvfntl ytnendevyn kytrattntk ldwelienlt fssrigldfs
      481 lseykaynnr yhgdsdgdvn gsstasdekn ynwvsqnsln yqfklgskhn fdvtalfeyq
      541 knnytylyay genfstdglt niasagsnfd asssftdwtn isylgmlnyn fdgryildat
      601 frregssrfa nghrygnfgs vglgwnvhre dflegsvfne lrlrgswgit gnsgiatnty
      661 qaflaydady agngavypsq lgneflswen getvdagfdf gvfdnrlsgs fayfnkrtyd
      721 llqdvplspt tgfasqntni gevvnkgiea qlnydifrse dfnwsisgnf atvdnevtkl
      781 aldstgeein psatstyktt evglpigawf mrtwagvdte tgeptwyvng vdgevtsnya
      841 saarvnqdea salptfsggf sthieykgif mdaslyyagg hkvyeqyaqh yfrtnsftlg
      901 syngveelle rwqqpgdvtd vpklvyngad nfhatssrhl ydgdyirlkd ltfgynlpak
      961 ftedigldai sftvkgtnly twvkddglkl dpevgaagyt glvtppvksv vfgvnvkf
//
LOCUS       WP_100895003            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100895003
VERSION     WP_100895003.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118259
     Region          25..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrakvtwilt pllvllmsfs ygqektitgn vtdqdglplp gvsvlvvgtt tgtqsdfdgn
       61 ytikakvgqt lrytyigqka tdrkvgssst iniqmeqdae aldevivtgf gnvsktsfag
      121 sakvvageni sqksftnvsq alageaagvs vfntsgqpgs tstvrirgfg svngsqaply
      181 ivddapfrgs lndinpndik svtvlkdasa tslygargan gvivittkrg sdtgneisvs
      241 iktganfqgi gryetidspe eyigiawegt yqrgllenng dqvaavdyan anlfeganad
      301 vsdispvynm wntsdsgaig vselidpatg mvrpgvtrry spedwedfaf qsanriegnv
      361 slantgenss vytsvgfidd qgyasntdyq rlnarisatn kykdfikmnt slnyaqsetn
      421 nngtgsssss qfwwidnips iyplftrdan gnkiddpiyg gslydygled grgfgfatng
      481 vadsqinisr skdnsvnftn dlkitlvegl tldnnfsyqy fmsddidlne pfyspakgqg
      541 gvinrsrsev knyslrtglr ynksfgatnl safvshvats ykfnyleaer sklvtpfgtd
      601 isngvvnaps dgftrdette syianatldf sskyflnatf nrdassrfln ekwgnfysvg
      661 aawvlsqedf msgsnfvdfl kvkgsygvlg nsgvltgtan nyypgynlys vnnlndnisl
      721 afatkgnpdl twessnqfnv gvefelggfv dgsveaysks ttdmffdrrv gpsvgyalis
      781 vndgemvnsg vefdldfklv qndkfslslg ingstfknel kampidpstg eqqkldisgn
      841 ygrtvgrsly dyympvyagv nvdtgaaqwe rsfndldgdg vfgtgdeiit nltsytndnp
      901 danvvqdite vyseaadkfi nktaipdvtg sfrlnarygn ftlstlfnys lggyaydtay
      961 anlmdndyag tnnfhvdird rwmqpgdvtd iprqdarfqi qqsatstrfl vksdylalnn
     1021 vrlgytlpsd iskqiglknl dfyitgdnla ffskrqgfnp stsitggssi yrynplstvv
     1081 lgvnlkl
//
LOCUS       WP_100895357            1169 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100895357
VERSION     WP_100895357.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1169)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1169)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1169)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1169
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1169
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131219
     Region          129..1168
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikiinpiy frkragvlkf imriflflfc ttvfsftsne vfsqnakvfi ekdkvisvde
       61 aftiirnqtd ytflyhedlf kdfpsivvkk gsirtnells nffelkgyhf sltknntiii
      121 sskpalsqqk itgkitdvng vpllgvtvll rgtrdgvvtd fdgnysinvs kgntlvysyi
      181 gfdtvekivg aettlnivmk rnatqldevv lstgyqkisk eratgsfdkv dskvldtkvs
      241 qsilnkiege lsgllfddvd gpvirgigsl evaptplivv dgfpisqgie sinpndvkdi
      301 tvlkdaaaas iwgiraangv ivittkkgnr srkpviefst nysitpknnl edlkyastns
      361 flefekhrad newsllpegn nqpalgagie tylklnegli sqaeadaiin slrgldsrke
      421 fqnlfmndsy wsqynfaisg ggknsvyrss isynknennn ffknndsdql ianlrgifnv
      481 tpkltisndf nftsskresn gmssgdysnl fqyqnildan gnqvaqpygl gqdfkdekva
      541 sgypynwdhn lmqefnnkdn siegtsiriq tavdykildn lsvrgsyqye wnnsegnslf
      601 nentyyvrdl vntytrveng efinhvnkgs iyrfnnatnk trqgriqlny nesfndnkhr
      661 vtalagyelr qvkntfnnnt lygfdpqalt sasiafgerv pvtssgvnpt rallnpssva
      721 yeenryvsyy angaytylnk ytltgsirld dtnlfgaskd yrniplysig gkwdinnegf
      781 fkgkvfntls lrgtygvngn vdrntgpyli agnsrnyvtd vefayirnvk npelrlekvy
      841 vtnlgidfgl fnntisgnvd yyhkkstdll spvsfpsvyg fnnatinvge menegvdvnl
      901 ninvaqktdl kynttlrfsh nkntvtkvdv peetvttylr gqplvgnplr yiysyksagl
      961 dangdpltln engelvnvdg kvnvagtlee aaientdalv ysgtttpkyy gswvnnisyk
     1021 nfyvrtlvty klghvfrntn ildytnassy itanihsdfe nrwqnpgden ttsiprlpll
     1081 rsdayklgys yyasgdqfvd sashirfkei ilgynfdkkv lkntgidafk vslqatnigl
     1141 infnkwnedp esfvlpttpt ftlnfsfnf
//
LOCUS       WP_100896364            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100896364
VERSION     WP_100896364.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114663
     Region          20..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkntlvllfs vlfttiaysq qisgtvtdse gipllgvtiv vkgtqngttt dfdgkyiina
       61 kqadvlkfsy igmlpkevtv gtttvvnvtl eedasqldev vvtafgvekk ekslgysvtq
      121 vksedlnltg qanalealqg rvagvqinrt sgssgggvdi lirgvtsvnp drsnqpliiv
      181 dgialnndtf sgnvspsags nspssseqfs fsnragdinp ediesynvlk gaaatalygv
      241 raangaivit tkkgkkgkak vnftasttfr nlektpnlqe tyregfsgap rtlydpdsdt
      301 gfnrvqngts fyswgpkytd dsytlesgdv vdltndqfys pydlfktgvn tqvnlnisga
      361 tekmdyffsv gnnneegilp gtyydktnfr lksgyqvtdn fsintsisys ksggnrgnsg
      421 dksvmsslsy ysgtfpindy qnpdgtqrny tfgvidnpry fieksslfdd vnrwvgnail
      481 kyspkdwlni tysaqvdnys dqrnrfvpad ldvgtqvggf ivnqninfta lesnflvams
      541 kdwsddfrtd ltlghqvsdt krnyadvrge tlnvpginel gntintfane svtqlrnvgv
      601 fgelklsyld klfltvtgrn dwvstlpkdn rsffypsvsl aydvsgvfgd ndvftfgklr
      661 aswaevgkgp lfgqvghyfv vdgdfpfgga ggyrsstalg dldivpernq steigadlrf
      721 fknrirldya yyktrvkdqi fgvgtayssg isrivrnagd fevfghefll sadiiksqdf
      781 kwevvlnwst segkvldipd diesiifads gfagvtseir egdkmgslyg wkwryenger
      841 yidangkpei dfterqkvgn afpdyitsla nnfkwknlgf nflleykkgg diydagrrns
      901 irngilevte frdettilsg vmddgnggyi pnttevlidq nyyrsstdyn raseilvqda
      961 swvklrnigv tydlpskfve kinldrfsis asaqnilvwt pydgydpegn qysagsnvyg
     1021 ftglniplsq synfginigf
//
LOCUS       WP_100896429             981 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100896429
VERSION     WP_100896429.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..981
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107031
     Region          23..980
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnklkniflg vfllfpllff aqqtvsgkit dnvtkspllg vnvvvkgttn gsisdfdgly
       61 eiknvnmgdv llftsigynp kevkvtsstl nvemtestea ldevvvigyg tttvkdatgs
      121 iekvstdefn sgaitspeql itgktagvsv vapggqpgqg atitirgnss lsannsplvv
      181 idgvpvdqgt tggssvsaln sinpndiesf vvlkdassta iygsrasagv ilittksgkl
      241 naplkvevnt ngsvgtvqkk ldvlnasqyr nvligsqnea lavpllgnad tdwqdqifqe
      301 aygtdanlti skgfessair gsigyttqeg lvktskfert sgslnfrqnl fdndlkinvn
      361 lngsitnddf vnggvigaal qfdptqpiys gnnnyggyye wlnndgsinn laprnplgli
      421 nqssneaetk raignikldy yapfldglnf nvtlgfdyne rygktstdpn sasaqnaqsi
      481 tgsygslrrs tladffvnyk kevesikstf eltvghtfqk fyrenyannp lisgtenstf
      541 fathnaiesy vsrlrysyds kylltlsyrt dgssrfsgdn rwgnfsaaaf awniseenfl
      601 kdsetvsnlk lrigygetgq qeinqdfgyl pvyqvstdnq qyqlgdtfyn tirpagydan
      661 ikweesktyn igldygffnn ringsieyyt resndilnqi pipsgsnltn qlitnigdle
      721 nsgfefsins difhredfnw nlgfnlsylt nkitklntvd dpsfigvatg gisggvgntv
      781 qihqvgsaqs sflvyqqvyd adgkplegvy vdrdgdgvsg gssdtgdlyv kenpsadyll
      841 gfssytnykn wdlnftmras ignyaynnva sstgnefgln slssnrnvst sildtgfknn
      901 qllsdyyiqd asflkmdnvt lgynfknafk ddkvslrlqt tvqnvftitn ydgidpeisg
      961 gidnnfyprp rtfllglnlk f
//
LOCUS       WP_100896549            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100896549
VERSION     WP_100896549.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111791
     Region          25..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkqthylll fvlflltsgm vaqnktvtgt vtdeagvpll gvnvlekgts ngtstdfdgk
       61 ytitvagdss ileftsigyt aksatvagqt tlnvsmveda eqlgevvvta lgikkeakal
      121 gysltevggd elsnvkqvsa inslqgkvag vnitqnstga agssrviirg nstltgnnqp
      181 lyvvdgipig nensgsagty ggsdggdgis sinpddiasv svlkggaaaa lygsragngv
      241 iiittkngsq kkglgveiss svtfdevdts ltdfqtsygq gtrgrvpanq seafdlglss
      301 wgpkldgssv vqwdgeerpy syvgdnrdhf yrtgttfint iaitsgsekm syrlsvsdld
      361 nqdivpnsgi nrksfslnts avladkltsq vnvkyivenv nnrprlsdap gnanytvall
      421 spnvdvrdmn pganpdgser gysaniysqn pyysaynfsn qdlknriias tslrydildw
      481 lyastrvgvd hytrkstsie pwgtaykllg gmnetegryt qidadvmlgi dknitekfai
      541 dglvgantnh vktetlilgg dnfvvpgfed isnlrdqsrs refqerkisg iygslgfsyd
      601 kwayltftgr ndwfstlsyp gkttpnnefy fsvntsvils dvlelpsfid flkirggysg
      661 vagggdlayq laptyqifgq ghqgqtlgri ngssvpnpnl vpwekdetei gldlrlfgnr
      721 lsfdvayyqn ettkdivnis tsvfsgydsa tanigklenk gieflisgtp iqtenfrwnt
      781 sfngsynkse vtatndegtp isldeprtqn arithvvgep ygsivgvsyn rddagniiyd
      841 insegvpiaq egerkilgeg vppltlgwsn tfrykdfslg flidgkfggq llsgtnalgy
      901 stglhketlk grenglvvsg idgdtgqpft ttvapedlqt yygrvsriae efvedsdyik
      961 frefslgysl pekmlektfi ssvnvsliar nlfyisrsid nvdpestyns gnsqgleyfg
     1021 vpstrnygfs lnvkf
//
LOCUS       WP_100896731            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100896731
VERSION     WP_100896731.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117445
     Region          25..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkqkgilt lllafivhlt faqqktvsgt vtdqdgiplp gvnilvqgtt tgtqtdfdgk
       61 ysisassgqv lvftylgqtp tsktvsnqnv invqmkedae alqevivtgl giskkekaig
      121 yavqkvtges idnakevnlv nslqgkvagv qiqgssstlg gssritirgs nsflgnnqpl
      181 fvidgvpvsn qsysnsgqer gfgggnydyg nsasdidpss iktmsvlkga aataiygsrg
      241 angvilittk ngsekkglgv tfdssitide vrnliphqrm ygggssypta sgfneftqdg
      301 vaylapnygk dgswgpkfds nvnvrhwdsw dpgasnyket rpwvapdnty esffnsgitl
      361 mnsvslsgan dkgsfrlgys nvdqtgttpn galqrntvni nttynltdkl kagltmsyik
      421 tdaqnrnitg ysngnplqgf tqwwqtqldv krlqnqqntt egnqytwnpk givtdasgnl
      481 tsfdptpnyf dnpswvrdnf mqedtrnrvf gnanfsyain enlslssqfg tdisqfslie
      541 giplrsvdps kyleterkfq etnfevrlny qkdfsedftf sgilganrmr qftkritaat
      601 sgglvvdrff nvsnsiaavn tdtfeankgi nsifgstsfg fkdmlfldls arndwsstlp
      661 kknnsyfypa asisfalsel dfikgsnvvn fvklrasiaq agndaaayrl sdvyspltpn
      721 fgsfpmytvp nsqqnpdlvn elttetefgi lvklfnsrls idasyydrlt edqifnvpts
      781 sstgytskll nagsmknsgf efqisgtpiq tenfrwdigl nltqqknevv ellkdenget
      841 lvesinmggt waadlriqeg kpymalygqd yiyddngskv vgddgaylft ddrvylgsai
      901 adwvggists ftyknftlsg lidfqeggii hssslqwaky sgmspetvaf ngesdtrang
      961 milpgvtstg aenttridpq tyyqtywnra apnvydasfv kfrdlrlsys lpakilkdlp
     1021 ftsvnlsvfg rnlaiisadv pyidpqvitg sgnvqglena qvpptrsfgv nlsakf
//
LOCUS       WP_100896733            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cellulophaga
            sp. RHA19].
ACCESSION   WP_100896733
VERSION     WP_100896733.1
KEYWORDS    RefSeq.
SOURCE      Cellulophaga sp. RHA19
  ORGANISM  Cellulophaga sp. RHA19
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Cellulophaga.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Cellulophaga sp. RHA19"
                     /db_xref="taxon:1798237"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116535
     Region          25..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkqrgilt lllafivhlt faqqktisgt vtdqdgiplp gvnilvkgtt tgtqtdfdgk
       61 ytisasngqv llftylgqtp tsrtvdnqnm invkmtedae alqevvvtal gisrekkslg
      121 ystqtvsgdd iaetrssnal namsgkvagv qvsnnsgslg gstrivlrgp ssitqenrpl
      181 mvvdgipldn snynsnatqs ggggrdfgda gfdinpddie tmnilkggaa aalygsrasn
      241 gvilittksg kkgkaqitin sgvtfdkvni lpkvqnlygg gagdastigq vgfgttting
      301 teysvvdygt deswgpryeg qqvlhwdafd pefsndylqt rpwvapkndk dsfwntgity
      361 nngvsfsqgt ekstvrlsan ktsthgivpn selnkssvnf natsqltekl kvdalvnlti
      421 tdgfnrpasg ytgsgvvqqm yqfgqtsldf erlknykred gtqrswnrvs aedgsprysd
      481 npywtlyent sedkrtrwyg nigatynftd elyvvakiya dtydfrindr ravgsqspaf
      541 yseadrdfqe vnyearlhfd kkfmddkisv nsfigtnrrd nefhrlsaat sgglvvpgly
      601 nisnssdpaq atefdsykrv nsvygsvslg ydnfayltvv grsdwsstlp endnsffypg
      661 vngsivfsnl ikadwlsfgk irggyaevgs dtdpyqlatt fvadipflgd vpfstngvsq
      721 npnlrpelkq tyevglemaf lknrisfdlt yyneetsdli tpvtvdpstg ynstftnagv
      781 lrnrgiealv nitpiqtedf swdftwnfsk nnnelleiid gveslqiasf pfnsvsinav
      841 vgesygvirg tnfvfddqgn kvvnangsya etqnvenlgs ilpdynmgfk ntlryknlsl
      901 gflvdvqkgg kyrsltniwg nysgileqta tnnkrevgtv legvtgtity dangdyvvtn
      961 tspntqvisa qqegtdyffg adaanvfnad yiklrevsls yklpssllkn tgitavnisa
     1021 fgrnlgvwgl dnenfdpeva tsgsgniqgs eggslpstks yglnlqlkf
//
LOCUS       WP_100900812             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nostoc
            flagelliforme].
ACCESSION   WP_100900812
VERSION     WP_100900812.1
KEYWORDS    RefSeq.
SOURCE      Nostoc flagelliforme
  ORGANISM  Nostoc flagelliforme
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Nostoc flagelliforme"
                     /db_xref="taxon:1306274"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41553
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dtvtrlvkqg levwveagag ersffcdsdy eaagatiisd
       61 taklwgetdi llkvsppqer edgrseidll kegavllsfl nplgnpvvaq qlanrkvtal
      121 smemiprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkldeetvaa ggyakeisea
      241 skqrtqevvt ehiknsdvvi ttaqvpgrqa prlvteemva qmkpgsvivd laaeqggnca
      301 ctepgkdivw ngvtiigpin lpssmpihas qlyaknvtsl mqllikdkal qvdfsddivd
      361 aacvthagei rnqrvrdalq alntqqpavn
//
LOCUS       WP_100922083             361 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Thiodictyon syntrophicum].
ACCESSION   WP_100922083
VERSION     WP_100922083.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Thiodictyon syntrophicum
  ORGANISM  Candidatus Thiodictyon syntrophicum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiodictyon.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Candidatus Thiodictyon syntrophicum"
                     /db_xref="taxon:1166950"
     Protein         1..361
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37809
     Region          1..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvsletr pgearvastp evvkkfaakg fevlvergag vragypdtey eaagarvtdr
       61 agaydtdlll kvrrpdaadv admraggiyi glmegcgede mvaamrakgi rvlamermpr
      121 tsraqsmdvl ssqaniagyr avieaaaryg rffpmmmtsa gsakparlvv lgagvaglqa
      181 iatarrlgae vfgydvrpet reqilslgak pidldlgetg sgeggyakel saeakarqqa
      241 aladqlarah viittaqipc rpapvlvtea vvqrlrpgsv ivdlaagsgg ncpltvpdqv
      301 verhgvvivg htnypsmvaa dasafyaknl anlieimvdk gdagpvlkdl mqdditaaml
      361 g
//
LOCUS       WP_100923607            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. SZ-18].
ACCESSION   WP_100923607
VERSION     WP_100923607.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. SZ-18
  ORGANISM  Tenacibaculum sp. SZ-18
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Tenacibaculum sp. SZ-18"
                     /db_xref="taxon:754423"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111571
     Region          23..1023
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkillllcf slmsfwgina qtkisgkvts kmdgeplpgv nvvikgtnkg vetdfdgqys
       61 ieaksgdtle fsfigmetfr vkvgnnniin velqegnvld evvvtalgik kekkaltysa
      121 qevsgdeltk vkqtnplnsl sgksagitin rsssglggta kvvlrgnast snndplyvid
      181 gipmlnqgng sngsepgtdi fgsqtgnrdg gdamslinpd diqsitvlkg ssasalygsq
      241 gangvilitt kkgkegklsv nvnssitmde vmslpklqse yqsasvnnpi aengrvsdpk
      301 swgsrasgls ndaegffktg ytsinalslt agnakaqtyf sfantlgsgv ipqnrlvrns
      361 ltlretakfl ndkidvsasv nlsdqsiwnr ptnglysnpl tgvylhpvgi drniykdkye
      421 yfdtsrniyd qfassfdeni qqnpywlinr npsydkvqrv lanlslkyqi tenfslqtrg
      481 sydktfftfd krqyagtdpv nsgdngryil ektentqqyi dlianysrdf gedisftgll
      541 gtsltkfkig dklfldsgrd gnglnfpnvf tlanfqntnn iaqsvanrev qsifgsanig
      601 ykkmlyldvt grtdwsstlv ntnstsffyp svgltgifse mfelpevinf aklrvsyaev
      661 gkdipvyati plnsinstnn gisnapfapi pgetleperq ksfeigaefr lfdnrlgvef
      721 tyydtktlnq iffiqaapnp qgytqnivna geitnkgiel vingkpivtd nftwnstlnf
      781 aqnenkvvsv hpslqngeai itgrgvngye fsliegedfg sikarslvrd engvpvvnss
      841 gtlqstdftt vahaqpdftl gwnnsftfkd fsfsflidgk fggnvvsvte avndkygvsq
      901 atadarntng gqinvvdeng vasqitaqey ynaiggrdgm lgeyvydatn vslrelsigy
      961 klpiksdffe sirlsliann lfflykeapf dpnitastgl glqgvdifnq pstrslglnv
     1021 ninf
//
LOCUS       WP_100924607             973 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. SZ-18].
ACCESSION   WP_100924607
VERSION     WP_100924607.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. SZ-18
  ORGANISM  Tenacibaculum sp. SZ-18
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 973)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 973)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Tenacibaculum sp. SZ-18"
                     /db_xref="taxon:754423"
     Protein         1..973
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106739
     Region          23..972
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnktkqllsl tlflfclfah aqqtitgtvt ekstgeplpg vsiiikgqvk gtesnfdgny
       61 vikdvkstdi lvfsfvglkt kevsvgnltt inveledsaq vleevvvvgy gtttvkdatg
      121 sveaitekef tkgnivtpen llsgrvsgvd irtsgapgsg sqitirggss isasnspliv
      181 idglpieens vagsrgvlan inpndiesfs vlkdasatai ygsrasngvi iittkkgksa
      241 ytldvdyqyt fgevldrvnv fsgdafrsiv qqqrpgdvgl lgnantnwqd eifrttgssl
      301 inatvkggil gfiptrlsvg fttqegsllt sqfdrknvsl smnpsffndh lninlnynrn
      361 fedsrfadsg qigaalrfdp tqpvydsssp fggfyehrng nnllnttknp vaalllansr
      421 gkvfrhfgnl nfdykfhflp elravlnlgf dkaegetsfl snfnygraad inllfagvns
      481 tgfsersnrl ldgylnykka fdkvtldata gysyqkfeef ggtsgnildp asfadtftat
      541 dvvnigffgr lnvdflnkyl ltlnyrrdgt srfsadnrwg nfggaafawk vsnedflads
      601 nvisdlklra sygltgqqnl pnvndvylsr yrfgnqnsqf qfannpirai ipsvinpdlk
      661 weetttlefg ldyglfdnkf sgslnwfnkv sddllfnaal pdgvnfansv iqnigklein
      721 giefslngdi lntedinwnf nfnatyldre itelangqdv rtggtaggtg ntiqilregf
      781 apnsfhvfkq lydsagnpie gayadlnddg vindddrylk edpsadltfg fqsnfnyknf
      841 dlsfnlrasv gnyvynnvns araqlallqd nevlgnipts vldtnfints dvinsdiyle
      901 nasflrmdni tlgytfdrpi kkftknsvri wagvqnvfii tnysgldpev fggidntiyp
      961 rsrnfmlgan vkf
//
LOCUS       WP_100925429            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. SZ-18].
ACCESSION   WP_100925429
VERSION     WP_100925429.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. SZ-18
  ORGANISM  Tenacibaculum sp. SZ-18
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Tenacibaculum sp. SZ-18"
                     /db_xref="taxon:754423"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115661
     Region          25..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mitkfngila lffafivqis faqektisgi vsdqsgplpg vsvqkkgsat gtetdfdgky
       61 tikaksgdvl ifrfvgmktv ektvgisnti dvvmgedsnv leevvvtgva tgtsrkklgv
      121 svnsislkkl espgtqsidq alqgkiagti iqsttgqpgq qqniilrain slnssqpmil
      181 idgvqildss tsiggasnqs srladidftt vervetisga aagtiygaqg angviniitk
      241 rgkagkmkvt vrtdvgvvda iagdklrrsq fhryqtdaqg flvdlngirv tdlndeaqyg
      301 avaindvavg ssqlgaagin ntpfaeqtfd atdvlfntav nqtlgvnlvg gsektsylla
      361 anrtqqesvl vpgeyvkyda rfnlgvdlad nlkvsgrfdv inssndtgtn tdnanannli
      421 nnvfqnlphv dllnvrnrdn dlviqpdltd pnssnpfffr ryqtrldeit ryisnfnlny
      481 sptdyltfdv kygydtytqn ftffqenksd hqqervltnn ktgrinfitn qeyfqnflas
      541 atlsldfkeq fgwdtnivst ttinfdwrdr nlvsnsvsgt dnpfgafgty nisqsstkvf
      601 ngysespfrt ygylvnqkfd fgslfgfsag frqdfsnrfg sgldftfpra dayfniadtf
      661 endsvnllkl raaygeagiq ppfssnlitl pgttlggdvg lsfpanlsne alevertsel
      721 evgldygftp segawfsnvs gfinyftret tgaifrgela pttgasgiqs nnydlssngl
      781 elsadtqvyt sedfgwnfgv rftkskatld riasgqplvv sdnfvleegq evgtfslfev
      841 vtdinqtdle gnpiiaaadq dnftkassgy ivnkntgnvv itpdkrtlgs sqpdfvmtfi
      901 ndfqisdfvn vsmqldwfqg leaynnakqw lynnglhedt svpvtiedps gtaqtgafvq
      961 yytslyntnv plshfledas flrlrsvavn fklkkfiktd fidaldvria grnlftitdy
     1021 tgldpeasrt fgntfqrgfd eftmpntksi nlgvtvsf
//
LOCUS       WP_100925433            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. SZ-18].
ACCESSION   WP_100925433
VERSION     WP_100925433.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. SZ-18
  ORGANISM  Tenacibaculum sp. SZ-18
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Tenacibaculum sp. SZ-18"
                     /db_xref="taxon:754423"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120385
     Region          25..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lllalvvqis faqertisgt vsdesgplpg vsvlkkgtts gtetdfdgny
       61 sikaktgdvl vfsfvgmkta ervvgssnni svtletdnll eevivvgygt atkqsyagta
      121 atvatenlea ksfsnvsqal tgevagvtvi ntsgqpgtig tvrvrgygsp ngnraplyvi
      181 dgipfagtfd lnsvnpadik sttvlkdata taiygsrgan gvilittktg tssersyiea
      241 dvksgvnvqi iprydvmrsp eqyiglvweg lynrgvvtgn adpvafanst flgdngigag
      301 ynmwnatggd lidpvtrtvr sgvqrlftpe ryadyafgeg irteanlrmg ggsakskyfv
      361 smgylddsgy svnsdfkryt trlnltsdvk dwlklqsnig yalaqstnng qtngsenvfe
      421 fadkmapiyp vfarfpntgd lipdpiygga qydygsptgs tngftrnrpn anllnpigsa
      481 ildfvggeth singnfsadf klsdeltlet kfggqysyqe finagnhvyg taatnngtln
      541 ltnttrwsqt flqllrykts fgdhslevla ahetferrfe rdfdnkqfvv vpglynldny
      601 levqspstgy adgsgiesyf gqanynfknk yyltaslrtd gssrfvndkw gtfgsvgaaw
      661 vvseedfmqd nlisylkaka swgvtgdqdg vstasgfdiy nanlvgsdla idlarpgnpe
      721 ltwetsrqwq agiemslgny idanfdyyrk ntdnlffnqr tgpssgissi lvndgevlna
      781 gfefdvtahl inkenfkldl alngevlnne milmpidpst glpkvidsns sgdgayafak
      841 grsifdfwmp ewagvdpsdg spmwyqyydd lngnnqldad epssydtgtq wfvqdstddt
      901 ntesvnttgs lfeyrqlvpn anikkvvtkn yatatnkfid kefipdvrga frlsgkigaf
      961 dfatqftysl ggyaydgqya elmsdrfgaa gnnyhtdiln rwqqpgditd vpllsdnavv
     1021 natrlstrfv tstdfialnn arigytvpsn fmensgidgi nlwvsgdnlf intaragfnp
     1081 sireagnsgr riyapattit mgvrvkf
//
LOCUS       WP_100925185            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. SZ-18].
ACCESSION   WP_100925185
VERSION     WP_100925185.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. SZ-18
  ORGANISM  Tenacibaculum sp. SZ-18
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Tenacibaculum sp. SZ-18"
                     /db_xref="taxon:754423"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110487
     Region          24..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknifkyfl laltfvssia ataqdvkgvv sdasgdlpgv nvlvkgtnrg vetgldgsyv
       61 iknvksndvl ifsfigyktv evpingesvv nvtleedsdt leevvvvgyg tkkkslvtga
      121 issidskeik sisnqrvdqv lqgrvsgvtv ssssgspgsg tkirirgtgs sgsadplfiv
      181 dgmkvstidn iapsdianie vlkdaasaai ygtegangvi ivttkkgtrg glqvnfntqi
      241 gfqfvntdme lmnasqfvty lneagnasiv nngvdtnwid etfdtafmqr ydvslsgsmk
      301 ntsyyfsgsh tnqegvvvgd nssfkrntfr lniqsqvtdw leigvnsnts fidrkgiven
      361 sdtrgviqnm liidpltpvi ytdgvpadvf drseangvpv lrdkdgnvyg yptystgevi
      421 npvayanaiq eninendqfl ttiygkfsim egltftsryg yeqnqflsqr ntnayyvase
      481 aantqyninr skqnfrrwlw enfatynksf dnhnfkllag ysaeqsrrpa ftneaysiav
      541 tdfngfnins pttifdqnsp iqlayrdnlv siygrlsyny mgkylfeasv rrdksdkfpa
      601 gnraavfpsf sagwlmsken fwsdesainy mklraswgqn gnknnlrgna diiaitnqvg
      661 glglnylgnv gaqitgfane nlvwetseql gfgvdlrafn sklnftadyy kkttndlafv
      721 agelitpgsa gfvsndfngg tvvnqgfefe vgysdttesg fsyqinanls tldnevteiq
      781 fvpegtsivg agapqnadgv trfteglpaw yfygyktdgi dpatgeinrv dtngdgsitn
      841 ddktmigsph pdvlfggnir lgykgfdfnv qwqgtignei iatyhqpsrp itnkplhffe
      901 grwtgagdsn atfpspgnit saydtdlvve dgsfmrikqi qfgytlpqsi tdklhvsslr
      961 myvsfddvft ftnykgldpe ignfgfndig vdrgfyptaa ralfgfslnf
//
LOCUS       WP_100930102             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Sagittula].
ACCESSION   WP_100930102
VERSION     WP_100930102.1
KEYWORDS    RefSeq.
SOURCE      unclassified Sagittula
  ORGANISM  unclassified Sagittula
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sagittula.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="unclassified Sagittula"
                     /db_xref="taxon:2624628"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55689
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpteve vgenrvamtp dsarqlqklg ydcliesgag qkagfadaly eeagvtvvet
       61 adalwsqsdi iakvriptad eldrltpekt litffnpggn aeglekakek ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqadgsasgg yasvsspefr
      241 eaqlakfrel apemdivitt alipnreapk lwladmvaam kpgsviidla aekggnvegt
      301 vkdekvvten gvtivgytdf psrmatqsst lyatnirhmm tdltpekdgk vnhnmdddvi
      361 rgatvayqge itfpppppkv qaiaaqkkek pkeltpeekr akevaafkaq tksqvtllai
      421 ggalmllvgl vapasflqhf ivfvlsvfig fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigagnwl vvilaaisvf faginifggf lvtrrmlamf qks
//
LOCUS       WP_100944807            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100944807
VERSION     WP_100944807.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113226
     Region          25..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkniqltll vffttsfsvl fsqnitvsgn vtdelnnglp gvavqvkgtk kgtftdfkgn
       61 ynltvekgek lifsfmgyks reiiadkiki nitlteseta ldeivitaef glkrvqrsig
      121 ssvqkidgkt iedsgrenfi salagrvagl nigstsgspg asntvilrni tsisgnnqpl
      181 yvvdgipmnn stfdpsgmag ggfsvrdmdf ssrgndfnpe diesitvlkg agaaalygsd
      241 asngaiiitt kkgtagkgkv kfsnyikfsk aygypemqdk yangaygttn yyftskfggq
      301 ypegtktydn idavlqtgfq erynvsiegg seeatirasf sqlnetgvlk ttdysrtnls
      361 lsgranvtdw ltfegalqyt sttntkvrkg tagplysaml wpmvddmsny laedgshmrn
      421 peyyldedll nplfgmnknk yydesdrfis nialnitpsk ntfiraqvgw dvgmqtfvts
      481 nhpyyanrna gegqynlvqs nfsdptinil tgytnnffde kfsfsgqlgy hqlengvtra
      541 asyggkfiep nfqsinntdp ltqtarqrnt krrvqgvsgs fefgydniaf itlrarndws
      601 stlpvnnnsy fypalegali vsdfdfmkni kpinylklrg swaqvgkdar plqidpelqn
      661 tnltgggfky gftgpnpnlk peittaheag idlrlfnnrv kasftyfete nsdqivqgfr
      721 lsyatgfvln tmnvgtfktk gweanidvdv iktddftwnv gvngskgtse vvflpenvte
      781 yynpntwnsg nirngimrge pittltgray drndngdili spttglplta sqwsiigdre
      841 pklrfgvmts lkyknfrvss lfagrlgatv vngtkrymmq rgtswesval rerqpqifng
      901 vikdgnensa nptqntisvd yrtygstifs ggdedwlekd vnylrmqefr fsyrlpeeal
      961 rktkilskmd lffvandlft wtnysgidav gntvsaaagg tggegidvfs mpnprsfsig
     1021 lsltln
//
LOCUS       WP_100944856            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100944856
VERSION     WP_100944856.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119019
     Region          28..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkdsniiy mifillftlp tlsygqekti tgtvvslrdn ipfpsatvfi katkkgtatd
       61 fdgkytikvk vgdvlvfsyv gykttevtvt nkvvinvale essamldeiv itgygkqsrs
      121 klttsvskld tkilenstrs naatalqgti aglrvtnttg qpgatpqivl rggtnfngtg
      181 splilidgip gsfyalnsdd iesievlkda aataiygars adgvilvttk tgkvgkssin
      241 ykykysmnse rddqkyigaa dhinynrqsi awyreiagns gafgaflngs nsaglgnntt
      301 tdpfttqllt psnqyllkqp gwasipdvld ptqqilfydn qevgdriyqt seskdhylsf
      361 dggnekgtyy lglgvldndg lvlgsgfkry sgkfsgsyev annvkvnsni lyahsslnrs
      421 plggddtvfr rfqgqastsr tfnsnadgtl tddyapgqnq sfgnplyyqd kfvrknleqr
      481 lsasvgvnwe iidnldvsvt gshftvnnhn esfnrayrvg ttdgplrtgr easvslqrtl
      541 rnqltgtlny tksvgkhsfn aligaeyykd nyfstsagtr nsptdlietl nagaeadgip
      601 tsfeseyvii snfgrllydy dnrylfgfty rndgssrlgn nkfgffpgvs fgwnahketf
      661 fedssisnvv tklkprlsyg vngnlevlsn ygvygsygsq gvyngqtgya nsslptldlf
      721 weksttlnag ldvsflndri siitdiysrd ikdklanltl pyytgfsgil tnngtirnrg
      781 felqingdii rndnltwnvg atfttnknyv vklpendndl nrqggtliwn adtqseewvg
      841 gyqegqrsgg dlvvafeqag iyatqaeada dnaitdeymp gasrnkrwag dvkwvdqnkd
      901 giingldrkv igrttpdfvg gittnlnykn fslfvktdfa tghlvwnhvk nkgygqtqgn
      961 laqpievlds wsptntdtdl prfvfvngak niwrgsegsg slqnyannkf wekgnylalr
     1021 eitvsynvpt ayfkdaikrl svyatgtnlh yfksmsgdtp evggvqygqf pvpktitigl
     1081 nltf
//
LOCUS       WP_100944969            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100944969
VERSION     WP_100944969.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114115
     Region          25..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkypflfyl fflitiiply aqssikgivk daagellpgv sviiksttkg tstnfngefe
       61 lkvaidetle fsfmgyktkk vhlknysdli illeedafqm deivvtalgi ekekkalgya
      121 vqdvkgdnin kakesnfvns ltgkvaglti qnstdlfqna vvklrgstpl ividgipdrs
      181 adiwkvnsdn iesisvlkgt tasalygsig rngalmivtk kgkegkvsvt vnsskifqts
      241 firvpdvqtt ygtgnqgnya yingsgggte gggwiwgpkl dqkdastssg fvettqfnsp
      301 tdtngnlvpl pflsrgknni knffetgsil snsigidwgs ekakvrfsaa nisqegivpn
      361 tslenasfsi ntsvdlsekl kvsggltynn qysdnfpevg ygptnylynl ilwtgadvdv
      421 rdlknywkkg eegyqqrhfn ssyynnpyfq ayeylrgydk ntvfgnfnas yeitsgltlk
      481 grvgvnnysl yrtykepksy igygnksrgn fsistanyfd mtsgvaleyk keitedfgir
      541 gqvgtesfys kyitgsqstd glnipefynl snnagasiva enkiqkqgvn siygfvdfdf
      601 kntyylsltg rndvvstlrs gnnsffypsv sgslivsklv elpnwvsfak irgswamvsd
      661 gkisndpygy isgydkgrgw ngtssvnssn tyissdikpe ststweigan vkllgnrlgl
      721 dvayyksrdy nniinssvsk psaysyvlln gdeyqrqgle fvlsgkpvkt enfkwdisan
      781 lsknertqte iyggkdktan nikvgertda iytevyqtnp ngdiiykngl pvadpynrfi
      841 gnsnsdwvfg itnnlsyknf dfsfsfdgrn ggviysttnq kmwwggthsg tvnqfrddan
      901 ngnstyvgqg vvvtggdvty nvdggilsdt rtykendvai nyinfmqkts nranynhhyy
      961 sqsfiklrev tlsyrfdeqv lsntffnaas lslvgrnlll fsdapnidpd sgsdnlqtps
     1021 trniginlkl kf
//
LOCUS       WP_100945446            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100945446
VERSION     WP_100945446.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117236
     Region          21..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhnflilms fflstiafsq qvlsgkilde tggplpgatv niingdkwts sdfdgnftie
       61 ykneksiiki aylgyvsqei tigkrksisi tlqpednmln eiivtalgik rtqkkvgyat
      121 qkvdaaavke itapnvagli tgkvsgltvs nptglfqaps ftlrgktpli vvdgipvstd
      181 fydispddil eitvlkgtsa salygyrggn gaiqittskg kksdgleitv ahnimvsagf
      241 tvfpetqtay gngsngkyef wdgqdggisd gdmiwgpkfe pgvkisqwns pildntngev
      301 tpwwgdvsgt kyddksrysr vptpwkyhnn lkdflktgvm nttsfsvans tekgsyrvsg
      361 nykshtgrvp ntsiksgglt fnsstklsdk ltldsklayn kvfspnyprh gygpknhmyt
      421 iliwmgddvn gkelnehryi pgqegyrqan ynyawynnvy faahelnqry dsnvlngqlk
      481 lnyqisddfs mqamgssvmk drfenrespk sylnygdprd gdyktwntns ldvdynllmt
      541 ynkdisdrfs lsanagasse yhkyqqeyna tdgiivpely slnntkgnik gnthfsersv
      601 nsvygmleld fdnklfltft grtdkhsvlp knnnslfyps vslstmvsew fdlpesinyl
      661 kvfgswaqvk rsldayqins yynnagmfng spvlsypggl vnpdiegslt tnvelglsag
      721 flnnrisldf ayynaideds iinlpislgs gfssrkenah qfttngyevs vratpikndn
      781 frwdvltnws kkvqrvtrld egaekyndlk lnertdafya tvweksadgq lildsktsmp
      841 tknaykqnig nknpdwrlgl entfkykdfs lkvgvdgvwg gllrsrtvek mwwggkhpns
      901 tihrdaeykn gigtvytptg vnvtggsvqk dlngnitsdt rtysahttpv swqswsqnyp
      961 yraqvtskes kifanvfdrt yfklrtvals ydlnkvikae gfkqinasln gynlfiwkka
     1021 diidpdfgdd dnlqdpstry lglgltfkf
//
LOCUS       WP_100945660             972 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100945660
VERSION     WP_100945660.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 972)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 972)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..972
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107226
     Region          23..971
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkfklflig illtssftmf aqqtvkgvvk ekttgqplpg vsvvvkgtkr gvqtdfngnf
       61 sinkvktadv lvfrylgyad keviiksnyn ltvqldesae qlneivivgy gtttvkdatg
      121 svesitakdf tkgnivtpen llsgrvsgvn vttsgapgsg sqitirggss igasnsplii
      181 idglpiqeeg vtgsrgvlas inpgdiesfs vlkdasatai ygsrasngvi iittkkgrke
      241 ytldldmqyt fgevldrvnv fsadeyrnlv tqkrpgdagl lgntntnwqd qilrstvssl
      301 ynltakgqif gaiptrlslg fanqegavlt sqfdrktisl smnpsllqdh lkinlnynra
      361 fedsrfgdsg qigaalrydp tqsiydassp fagyfqhrng nvvsngtqnp vaslllannt
      421 gfnfrqygnl nfdykfhflp elrgvvnvgf dktkgstnnl nrfqignadl ikqfagsksn
      481 gtqersnelf dsyfnyvkvl edlkldltag ysyqrfenfg sdtgntrdsd sfattfadpd
      541 vvnigffgra kfsylkkyll tlnfrrdgts rfsennrwgn fggaaiawni sdedflkdsk
      601 vvsnlklras ygltgqqnlp gvndlyldry rfgnensryl fgnnvvqsti psvvnpdlkw
      661 eqtttiefgv dyglfdnrfs gsvsafrkis ddllfnaala dgtnfgnsai qnigqlqing
      721 leftlngdil ksedynwnft fnatyldrei telannqdvr tggiaggtgn tiqllregfa
      781 pnsfhvykql ynlagepieg ayadlngdni indddrylke npnadvtlgf qssfnykdfd
      841 lafnlrasig nfnynnvnsa raqydllkdn avlgniptsv lntgfqrtsd vinsdiyien
      901 asylrmdnvt lgytfnnpik kfsysniriw agvqnvftwt nysgldpevf ngidnliypr
      961 srnflvgani kf
//
LOCUS       WP_100945954            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100945954
VERSION     WP_100945954.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121987
     Region          21..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkliyllif ipslliaqqe kviegivida elqmpivgas vyvssaiign etntegilqg
       61 amlgtttnfd gnfslkigad ikfilvsymg yetekidvsk vtgtisvalr esseslgeii
      121 itgyqkiekr kmtsayakie medinqagva svdqmlvgql sgvviqptsg apgapskisi
      181 rgaatlngss dplwvldgip ldgndipqdf rdkdnidnlq sypiaglnpd diesitvlkd
      241 asatsiygar aangvivits kngkkgamri nvnanvfvtq kpdfsklnlm nssqkvdfel
      301 llasrsdlky qqdrggvari lnnygeynnf rdngfaslss aaqneinnlk ntntnwgdel
      361 yqmavnqqyg vsisggsenn dyyfstgifd etgatkgtgq krfnitlkdn fnvndklklg
      421 valfgsqtit ssyitgaday tnpsnysrna npylkvkdan gnyvydpdlv eredlnlnyn
      481 vleerentny elvssslkai fdagyklngd ihfntqlglq ldfdktekys geesyytrky
      541 eqrsqyasst gtsyympkgg iiqnwnsdvf qynwkttany ntsfndvhel dvmlgtefrr
      601 nkrtqihakg fgynsntlts iaitderslt nslfdpyqkt ysenayasff gtasytydkk
      661 ytaftslryd gsnlfgvnpk yrylpiwsfa gswnvykedf mynldfvsdl klrasygvqg
      721 nidkttspfv vgeyytssil pgvseetira lnapnadlrw ektvssnigl digllnnkiy
      781 isgdyyarks tdliglrsvp lesgynfint nwatvsnkgf elsinttnid tpnfkwtsgf
      841 nishnksivd nieireedfk pslkgysvna ifaiktagld snglplfwke gkkvsavdfy
      901 nleegtngnq ltreehrnly syvgdgtpkf sggfrnsfky kqfdlrvltn fnikqtvkga
      961 psynlalaqp gnnyntdilk agtgsypali gltspgfdtd lvytwfnssd dgktyndldi
     1021 wvkdisyirv ssvklsyaip kskleklnis slnfniegrn lfvfgtdydg ffdpetygsl
     1081 yaqpipkiis vgfnlsf
//
LOCUS       WP_100947012            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100947012
VERSION     WP_100947012.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109268
     Region          24..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklvilti lcltltlnfy sqeitvkgkv sdssgellgv svlikgttkg tstdfngays
       61 iksskgdili fsslgyktke viisrsllnv vleedssald evvvtsfgik rqkkslgyaa
      121 qalkseelle gnqnnmvntl qgkvsgvtvt ssggapgass vimirggtsi tgnnqplmiv
      181 dglpidnstd sslevastnr asdlnpedie sitvlkgpaa aalygiqaae gavvittkrg
      241 regvskvfls sslsvdniig tpsiqrnygk geqipqvggg viynddspls wgeqipsgtk
      301 tynhikdfyt tgvtqnhfls ysggsaksnt yfsignlane gvipttsydk ttfritqnsk
      361 lsdkltlgvs gnyirtnins trqgnatggs itsllnypst vnvkdyedad gaqkgfytgq
      421 efdnvywsle nspntnelnr figslgldya inknlnlsyk fgadiydqhs rritangsln
      481 dtrsdgyisq yerlykkyts nfiatydtql ssnfelnlla gntiedsnvk tdyltgkdfl
      541 apgiynisni akenqsiter isrkrnvgvf geiklgykka lflnvtgrnd wsstlpsksr
      601 sffypsvggs avltdlfnik segnglsylk lrgtwaqvgk dapigqlesy lvtqinglgs
      661 tgyayngvdv gnaalepeft nsweigfdsn flnnrvsfna tyyksisdnq ilsdirvppt
      721 agtfyatlng geienkgiea llsvklmpst sdfqwtmnfn fgsnkttvvd lpgelkevyl
      781 sdswtflnsa agagvlnasl fslrgkralk nddgevligv ngyptladet yaevdrqpdf
      841 tlgisssmry knfglsflld ivegntvyna tasalafygv gantsdrget tiipgvkadg
      901 sindisvtkd qvyyqdyysr lsdnfvedgs ytrlryvsln yqlgknaidr lpisklefsl
      961 tgrnlvtftn ysgvdpeina fgggvpgags vgvdnlgtpn tkgfdvgikl tf
//
LOCUS       WP_100946485            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100946485
VERSION     WP_100946485.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123070
     Region          31..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkinkltkll pifglliili gtigraygqe rtlkgrivdn eknklpgvav fikgttygsa
       61 sdfdgnysin indnntilvf kslgfvtqei ivgnrtilni slvpdenqle eiiitalgvk
      121 ketrkigyst qqvkgseltk areanpinsl agkvagltvg vstellgapq vvlrgnpgvl
      181 yvvdgvpins nswnisaddi etytvlkgan aaalygfrgq ngailvttkk gtkddrkfsi
      241 eynssimfee gylakpakqs eygagnnyqy afgndtydad gsfrrtnvwg prfegqnipq
      301 wdspvdpitg vrqgtpwlak gvnnlenfme tgiiatnsls iaasgekhdl rmsisnnyqk
      361 gmvpntklni tnfnisagyn ftdrlkiegn lnlniqnspn vpetssgpqg ymysfevygs
      421 shwdvrdmrd yyggiagveg vqqqfaeygr tnnpyfisne wlkehqktdv ygyaklsyki
      481 ndffdisart qvttwnqlrt ekvpfsiisy kpyaagagpd lragdyredk rtlfennsdl
      541 llnfnkdfgd nfnvsaiaga slrtfrynss fvttdylivp giysfsntrf pvkaysfrse
      601 mevasayyta dfsyknyltl gvtgrvdwls tlpkdnraif ypsislstvv sdyidlpeai
      661 sfmklrgsya nvkggltsst igsaykgvtg lgisnligqv nevttsydgp synnqnnyni
      721 fngyandpaa sfsntlanrs lesysvtsye vgldmkflrn rlgldvtyft singpqifpl
      781 eiasstgfke qtingvttqk nglevslfgs vikntdgfnw dvsanwstyk eklkdvyngi
      841 ssiylpgpdh vfnvgdrldg yygyeflrss drqiihssag vplkaprgtn nkrllghtnp
      901 dfvfginnkf syknlslsfq fdgrvggviy neayayalna gnqldlttga ygearrkewd
      961 stlngtvaat pafvgegvvi tngtpsydaa gnisnmkelt fapnekvtll kgyvqsvygg
     1021 garvdeayln sktflklref tigytfpkel lkntfienas vslvgrnlly faetkdfdld
     1081 qfpsgynsts rssskktilq spstrrfgln inltf
//
LOCUS       WP_100947166             973 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100947166
VERSION     WP_100947166.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 973)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 973)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..973
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107073
     Region          28..972
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksisifit mlffsailfa qeksivvtvv dgagapipga svivkettkg wstdfdgvvt
       61 iksnsgsivv isslgympke vtisnekkik vslqesssql eeivvvaygt qkketitssv
      121 vsidsdklad vttpevatml qgkvtgvqvl psggspgssp nilirgrssi nstnsplwvi
      181 dgvivgnsdp klnpndvasi svlkdasats lygnrgangv iivttkrgki gakpqikvsi
      241 ktavnqfnpg gfelmnsrel ydyhtelgnt sswfnedlls rdydwvdgat kdafvkdasl
      301 tftaatethn lfistgyyee dgtvkgnkln rytfrtnldy nindkltikp kinfvfdnrd
      361 ntreaplyea ytnmpwdlpf nkdgsvvnan taqgddwlgr dkrnyffdqq wnysnsesfd
      421 lfasfdfdyk itsnltyist nnfrygtyes fsysdprsng grtsngalsd ytyrglsrft
      481 nqmlkfsnsy gekhtvnall ayeyndsssk nisarsenil vngqvqdvgi kpaavvgnen
      541 esaqqsflfs adydydglyf vkgslrvdga safakdyryg efysiaagwn vhkedffnid
      601 qinklklras ygavgnqpgg fgfldlydvr fqyagiiaak pfqlatenlt weksietnig
      661 idtrlfnvld vtvdyynken sgllyfrkls dqtgfggryq nigsitnkgv efslaadivn
      721 kkdfgisagl nmsfndntvd klsegtdiig gstiiregee lgtfymrkwl gvdpatgeps
      781 yevvdattge rtttnvynda tnqisgtsna dftggfntaf ryknftlssn wsysygsely
      841 nssrnlfdsd gfylqfnqmk lpegssrwqq pgdiathpka vvggypggnq tstryledgs
      901 ylrlnnvrfs ydvsesvlgs lglsgmnfyi tgdnlvtftn ftgvdptigg angsvslgyp
      961 iprryalgln itf
//
LOCUS       WP_100947185            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100947185
VERSION     WP_100947185.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115865
     Region          25..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktynliiv lfmllvvqss faqlktisgt vtekgskipl pevsvfinqv nkgditdfdg
       61 rysikaedlk gktltfsylg yktvtinltg edqvinatle pdstnlneiv vtalgikres
      121 kalgysltkv dgedlstvks lsavnslqgr vagvnissgs ggaagssrvi irgassltgn
      181 nqplyvidgi pvinntngsv vgatnnatgd ggddisslnp ddiesvsvlk gssaaalygs
      241 lasngvimit tksgknkkkm gieysssftf dkvntglqdf qttygqgnnr lrpgyeydlt
      301 gnpveiglka saiddsyvss lqswgapldg slvynwdgvk rpysyagnnl dkfyktgvts
      361 intlalakgg edynyrlsfs nldnkdifpn ttlkrrsisl nasakisskl tstintkyiv
      421 edvhnrisig dtpgnantva fvlpsslniy dlkpgsneeg telrfqpsqf isnpywatnd
      481 fnnddtknrl tasttlkydv ndwlsvtgrt gidtydlsrk rvtpfgtayr pagelyqvks
      541 tyklvnsdvm lgidkditdk isinsilgan srtssfesls algrgfivvg ledlnnttlp
      601 eptygffetk tnsiygsfea synrylyvtf tgrndwfstl sfpgkttpnd gfywsvsqsl
      661 llsqafdlpe ainyakvrts yaqvaggarn ayslnldyai tgsfqgqsfg qlngnsipnp
      721 nlipfqknef evgfegrffn srlhldmayy anktqndivr aaasqssgft ssilnigelq
      781 nkgfefligg spiktedfsw ntsfnfgynn seiihtdded tainvdgslt rsrtaiishi
      841 vgenygvifg ssykrdengt imynnsgtip kpvqgenkil gqgvapytmg fsnrfsykdf
      901 slsflidakf ggsvhsgtnr elmmrglhkk tlkgredgle vsgidnatgq aftkvvapen
      961 lrtyygfige ensgiseefv ystdfikfre vslsyslpqt alknvfidnv rlsvigrnlf
     1021 fisrkidnvd peaslnnlns qgierfgtps trsygfsvnv kf
//
LOCUS       WP_100947352            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100947352
VERSION     WP_100947352.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118176
     Region          21..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhismwill lftsiifsqt tvtgtitdkn tgekipdvsi sssikngtts nlngtyaivi
       61 sdteqsltft ylgyktqkin vgnrnviniq lteqetslne vvvtalgvnr ktkelgyvvq
      121 elkakeltev ktanfldnls gklagvtisq gatgvgsssk itirgeasfs nnnplfivdg
      181 tpinnntvfn ftdesatgfq eidfgngame vnaddiesvt vlkgpsaaal ygtrasngvi
      241 viktkdgskk kglgisinss itldnafrlp dfqneygqgn ggnfeysngl gagindvisy
      301 swgprldagn lisqfdspvt lpngatvrgg dtslysgnli tptlfksnpd nlkdfyqtgv
      361 ttinnisind rfergsyrls ftdldsqsii pgvnlerktv alkvifnpte ktrvtssiny
      421 vnsssnnrps ngygsenany slvawgprsl ninslreywq pgleglqqyn fnyryfdnpf
      481 filnentnsf nrdrvfgnia vnhkftdkls vsfrsgmdys sekrkfnrnf ssnrfangay
      541 aehdvfyrev ntdflvnytd kfedfsfdas fggnrldqta stkqaqttnl aqpgifslnn
      601 aaspveffqf eskkrinsly givkfgykdy lyaditgrnd wssalatsfs vdgvsffyps
      661 vstsfivsna telpenisfa klrasvaqvg ndtnpyqtss afvsqtsfng qptfsnqdfi
      721 pnanlkpeit tsyevgadlr flkdrlnidf tyynsttkdq iislpiaiss gynqqvingg
      781 kvnttgveii lggrpiknek ftwnttfnfa tnrsviknlp qeegrltlay sriydsanqt
      841 vyfqveeggr igdfygtgyl knangdfiiv ddaakpedng kfiadnnlqk lgnynpdftl
      901 gwnnnfsyqn wtasflfdwr qggeivsrts algnvggqla etvfrpdagi iaqgvgrssg
      961 lpntiavspe syyrqfydrn heennvydas ylklrqfsig yklnlkegfl glkdtstldl
     1021 sfignnlfvi tenphfdpeq lavqgngfvs gvedmsyats rslgfkvgfn f
//
LOCUS       WP_100947273            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100947273
VERSION     WP_100947273.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115685
     Region          25..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkftfflt flflvsvqft vaqekrikgi vkegsdplpg vsilikgtlk gtqtdfngny
       61 aikantgdvl vfsyvgmeak evtvnnsnii dvflegsnll deivitalgk vrkkksvgfa
      121 qqsvegqdlv ktnevdinns iagkvsgvqa lgnsgatfdg alirlrgnsn vlyvvdgvrv
      181 qsagdintad iesisvlkgg aatalygtda sggviivtss kakqgqsikl qlstemanat
      241 nileyqneyg ggytqdfitl pngelrpdyg adqswgpkld gtlvrhwdsw ivgdpeygkl
      301 rpwsanpnnv kdfyetatvn kailtfqsgg enhhlsttir nvsqegilpn terkttqisv
      361 nadynvtkkl tldaninyqi rntlnnpqlg ytgsgsffrp nlwwqrqldi hrlkdykrng
      421 qfvswnlqsp tnptpaywds pyfefyenrn eqdknaifgk lalnykvnek lsanlqyrrt
      481 fshfnsykig afggrggatd pqfeettssr aenevygtmn fndkygdegk iefastagfq
      541 iknetynsty assvggltvp gfysvetsvd rptynattyk eesravfgnv nigyndiiyl
      601 daslradwss tanpdnnrli tygvsssfif sellqdagfl sfgklragis sapsfpnayl
      661 inatyqssgn yngsplfsip staanpliag astkesefgl emkffdnkia ldltyyntki
      721 edfprldllp sstgsstiyr ntgketrsgf egslnfkpis tenfkwdvgi nfatidwkvn
      781 eidanddpnt pstrrldrtw tfnnsyvvlr dvegeskgni ygvkakrdsq griiidqsag
      841 dwsenaivre ddqlignflp dltggltnti hykdfelsas idfqvggdyy sqskrwatgs
      901 ghsietvgvn dkgnsirddv sngggirldg vdsvtgepvt ryfdatayfd rqlpafaenl
      961 vydasyvklr qlslsynlpk evseklgvdn iqtsifgnnl wliyaadeid pseienvsgs
     1021 slgrsgagfr waegaqfpst rtfglnlsvt f
//
LOCUS       WP_100947378            1194 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100947378
VERSION     WP_100947378.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1194)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1194)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1194)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1194
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1194
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132717
     Region          106..1193
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtfiylfct isfafvsseg vsqnakikid sditisveev felikkqtdy tfvyenslfn
       61 klpkvvlnkg iivvkellnk sleksnvvyi fnkdgsillk kkivqqkitg tlidknsmpi
      121 igasvsvkgt gkgtatdfdg kysiaaskgd vlvfqslgfq tkevavgssl vlnvsleest
      181 enlaeivitt gydkinkksf tgaattinav dlkidgindv srmlegkvag vnvqnitgtf
      241 gaapqitirg sssvfgnnnp lyvidgvvqe diveqdldal tsgdastlis ssiaginatd
      301 ikkidilkda satsiygara rngvivittk sgkkssplkv tytleqtvrd ipsysqydil
      361 dsketvgalq glreqgflkl pavgnarfsg iygilekqin sfqnggfgvv ntqegrnkfl
      421 qqyelantnw fktlfrqslm qnhsinfsgg gennsfyasi gfvsdpgwsi adkvtrltsn
      481 ikntyyfsdk fkitlatvas irdqkapgtf rrvadvvdgq fsrdfdinpf syalntsral
      541 rprdnngdle yytnnwapfn ileelqnnti dldvkdirfq fdasykitda ltydlnmssr
      601 yvnstrehqv reksnvvray nsdgtpvian aniflytdpn npdaipvtvf pegglyiknd
      661 ntltsyyvrn sfkydktfnn khninallgq elryvdrlrn eftgyglqfe ngftpftdpr
      721 llekiitdgd nyfdlardre rtvaffgrat ysyddkyifs atgrydgsnr qgestssrwl
      781 ptatvsgkwn asdenfikds nvinnlqfrs syglsaspgp atnalaifrs eitdrltvke
      841 retflniddl enseltwekq yelnlgfdlg lfnnriqvta dvwkrdvfdn idlvrtngig
      901 gqlfkfgnna didtkgvefa ittknikttd fswstslnfs yfdqkitklq neprvidlvd
      961 lqggnvvgfp lnslfsfkfn glnnqgvptf elpegddsvt dvnfqdseni ldylvsngsv
     1021 qanmnggfsn tfkyknwdlr vlitgaggnv vrlnpaldnf ytgtnvftks tvnrwmfdgd
     1081 etrtnipkiv dvrnnnsfgs salsraynay nfstdrvasg dflrmknvsl gynfdgnvld
     1141 kiglsslrvq fqgtnlfliy sdaklngqdp efygtggval pitrqftmsl nigi
//
LOCUS       WP_100947732            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            sp. ALD11].
ACCESSION   WP_100947732
VERSION     WP_100947732.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter sp. ALD11
  ORGANISM  Polaribacter sp. ALD11
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Polaribacter sp. ALD11"
                     /db_xref="taxon:2058137"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111795
     Region          25..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngflt lllalvvqit faqektvsgt vseelgplpg asiliqgtst gtqtdfngky
       61 sirakegdvi ifsylgyspv kktvgssstv nvtlkqgenv lneivvtalg ikrkpkelsy
      121 svqtvqsddl tktkavnvat amvgkvsglq intinngvnp strvvlrgnr sllgnnqali
      181 vidgypssrn aidrispddi qnitvlkgan asalygsdag ngvlvittkk gkgklsvtyt
      241 stlqmesvay lpefqqefga ggfpdgtlyp lenvnwgprf dgrlvdaset yddgrvwqvp
      301 fspikdrnkn ffdtgvttrh gvslsagdet gdflmsldqt nvsgivpkdk fnrtnfrlks
      361 skqmgnlkvg gnfsfyrshs ntvgsggrqg rpvywnvlnt plhiplsemk nwrdgeftrn
      421 evsyfrfyen pyfiidtqrn yadyteftli adaeykftdn lkatlragyt sgtnettref
      481 ggfnyafklg dayanmdpyg psnadglsts trintdfivn yqkdvstdfn inatvghnmr
      541 mtsgkeinvs gtnlfipdfy nvstrsgelv gdesysqlrk mavyadvtlg fkdflflnlt
      601 grndftstlp tdnnsyfypg agvsfvasea fpaitsdngl sflkasfnit ktgndpaaya
      661 anniffvpdn ypygntvgls qsstvadpel npefttslea gldfrlfknr vnanitgykt
      721 nstdqlapvn istasgatrl ytnigeiqnl gievdlsgtl irsedftwdl glnysgykse
      781 vislkdgvdk vdlggfadaq iiarvgspyp misttdyerd sqgrvvvgan gdpiqaagnv
      841 dqgqtsptat mgfnttlkyk nftfyavmdy rtgavffngi vdaleftglt qhsatsgrqp
      901 fvfpnsvysd ggtgfventn rltsnggnaf wsaynnvksn yvtdasiiki revllsysfn
      961 kdvidaigvs dlsigaygrn lftfrpdsnv ytdpefnfte gnaigigtqa qtpptrqfgl
     1021 tlnvkf
//
LOCUS       WP_100952009             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. SK17].
ACCESSION   WP_100952009
VERSION     WP_100952009.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. SK17
  ORGANISM  Bradyrhizobium sp. SK17
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bradyrhizobium sp. SK17"
                     /db_xref="taxon:2057741"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38949
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aevavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeatels qykrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegakage
      301 vvetdgikiv gytnvagrva asasslyarn lfsfietmvd kaskalavnw ddelvkatal
      361 tkdgavihpn fqpk
//
LOCUS       WP_100953376             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. SK17].
ACCESSION   WP_100953376
VERSION     WP_100953376.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. SK17
  ORGANISM  Bradyrhizobium sp. SK17
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Bradyrhizobium sp. SK17"
                     /db_xref="taxon:2057741"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38975
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aevavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeatels qykrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegakpge
      301 vvetdgikiv gytnvagrva asasslyarn lfsfietmvd kaskalavnw ddelvkatal
      361 tkdgavihpn fqpk
//
LOCUS       WP_100963519             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Allobosea
            sp. FBZP-16].
ACCESSION   WP_100963519
VERSION     WP_100963519.1
KEYWORDS    RefSeq.
SOURCE      Allobosea sp. FBZP-16
  ORGANISM  Allobosea sp. FBZP-16
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Allobosea sp. FBZP-16"
                     /db_xref="taxon:2065382"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55612
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspkelf agearvamtp dsaqqlqklg ydclietgag laagftdday raagvtvves
       61 aaalwdeadi iakvrppeta eaerlkagkt lisffypaqn kellefckgk danviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfkg qqqdgaatgg yaapsspefr
      241 eaqlkkfrel apqidivitt alipgrdapv lwtadmveam kpgsvivdla aerggncelt
      301 kpdekivtpn gvtivgytdf psrmaaqsst lyatnirhmm tdltpakdgk pvhnmeddvi
      361 rgatvtfegt itfpppppkv aaiaaqkpke kakeltpeek rakeaaafka qtqsqlmllg
      421 vgtvlmlivg ayapvsfmsh fivfalacfv gfqviwnvsh slhtplmavt naisgiivlg
      481 allqigsssw lvtflamisv liasinivgg flvtrrmlam fqks
//
LOCUS       WP_100988126            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100988126
VERSION     WP_100988126.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110224
     Region          54..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmeksykksr fggnvgqvgi tqlpvfnwkg lqrfvmalal lgllgnqaaw aqertvtgkv
       61 tdptgsvlpg vsiqvkgtqr gtntngdgvy tltnvpdnat lvlsfigytt qevavgnrtt
      121 vdvkladdtk alqevvvvgy gtqkakdvtg svatlgpkdf nkgvisspeq llqgrvagvq
      181 itpasgepga anniqirgav slrggntply vidgvpldgg dfsngtpdfg tgtttarnpl
      241 sflnpsdien isvlkdasaa aiygargang vvlittrkgr agapqfnfsa saavssslkk
      301 ydllsptdfl agvkaaggdp tlstvnagan tnwqneilrt svsqiynasf gggtndtryl
      361 fslgyqdqqg lvkgtgqqri tgrinasqdl fnkkvtlavn attssvtday altgnqagal
      421 gnlfgamiga nptypvfrnt sdtsayyqla ggsyrnpram ldyyhdkgvt nrtlanvsat
      481 wnvlpglslk anfgvdnsas trttsidsrl ngqftvplgs vtnqvfadat tglggaayin
      541 slnrlsklve ytanynrdlg pgkleavagf ayqtfgtrts yvaasrfpfd esvisytdni
      601 gaantltgta igggssrsqn dlqsyfaran ynfkekyllt atvrvdgssr fgvnnkygtf
      661 psvagawris qesfipksif ddlkiranyg ivgnqdftgg askiiytyns sgsqiqqnnp
      721 npdlkweqnt ttglgidfsv lkgqlsgsid yyhragsntl lqvfyaqpap vnykwinlpg
      781 qivsqgieln liyqvvqkaq fgweavfnlt tlnikaqdig tdqavgavsg qglsgayaer
      841 itngyapfsf fipqftgfds ngystyadng rstyqgspfa klrlgltnnf tfglwtaslf
      901 vngqfggkiy nntanalfak galknarnvt ydvansteng lnpasvstrf leksdyvrit
      961 nltisrrfdl pqggfaksls lsltgqnlfi ftgytglnpd vntvtyngng ngipslgidy
     1021 tpyptprtvt lglnvgf
//
LOCUS       WP_100989244            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100989244
VERSION     WP_100989244.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120593
     Region          22..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 makdllrlii mmlivstpal aqtisgrvta stdgqslpgv silvkgtssg titdtegkyt
       61 iaaaknrvlv fsfigyktke vavenrasld vvldedasmi nevvvtafgm tqekralgya
      121 taivnnesli ktaspnfata lygkapgvti natpggatsg vsisirglas itgntqpliv
      181 mdgipirnge arntdywgdq rirgnglldl npadienisi lkgasaaaly gseavngvvl
      241 vttktgkgkk glgvdfsasy svdkiaylpr yqnvrgpgyf knyadggqda ngfisydtng
      301 dgvgdtrgll natvnfgpkf dgqpvmafdg vvrpyvasgn syanlfqnah tsninlaisk
      361 vtdnstmrfs ytrqdngmis ygakneknim nlnasfsvnk klrtdlmvny vnqythnrpf
      421 kvdrminnft gmmnrfesad wyfnkyqtsq gykfvtgtnq sltpneniir ngfkpdigdy
      481 vwstrantyd eysnrviasv tqhydildnl klrgriatdl taeriedkqr ssiplafgys
      541 gsfamnnnly snvygdlflt ytkkinedit vlasggytan kmlntyvsrs tngglstenf
      601 fdvsasvnta ggsntrdrsl rdafvgtlnf dyknfffieg tirrdrtsll apgnnaftyp
      661 svnsslvfsd lfrlpavinf aklraswgiv gnyppiysan naynqgslsv qqsggssvly
      721 tnissdygnd kirpeqkhef efgleaklfk grvgvdlsyy naqivdqilp ltiaatsgak
      781 tilanigtlr nqglelalnv spirntelng lnwdltlnla knsnkveklt nnstellhad
      841 ydgnaaqlrs vvgqpmgdiy vhgilknadg rnvvgpngiy qldannwika gnampkltgg
      901 llnslsykgf tldvvvdfry ggsimptgin wltsrgltee sltamdaehg glsyyndang
      961 kgipttasag pggevvyhdg mlmdgvlptg eantniisqa vyynntynwg gpqysssrye
     1021 lyvkentyik mreislgyri panisrkigs qnltlsvfgr nlffiyrtlk dldaeqtnss
     1081 trwaeninna gnnpsfrtmg vmlrasf
//
LOCUS       WP_100989622            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100989622
VERSION     WP_100989622.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111948
     Region          32..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meqklrraip glllflgiwv igaalpafaa dkevtgnvtd ekgndlagat vtikgtnrgt
       61 ntdgrghyri tvpdanavlv fsyigyakqe vavgarsvid mkllpgdaal devvvtalgi
      121 kkdtralgys vttiessaln varetnvins lqgrvaglni apssggpgts srinlrgvsn
      181 fsggsplfvi ngipmdntqr gnsgewggst ngdgisninp ddvetmtvlk gasaaalygt
      241 raangvilit tksgsknsgl sveynvnlqa dkiidfsdyq yeygqgtqgk rptdvasakn
      301 sgiyswgekm dgalytqfdg kqypyspvkd nlqnfyrtat tltntvalsg gndqtsfrls
      361 lssldaqsvl rnsglkrktf nlninqkvts kfdvsvmgny vdqqdenraq lmdgpmnany
      421 gikvlatsfn qaalqpgynt itgdestfsd dtyktnpwfv vnqyknnfdr krlisaitgk
      481 yqfadwiylq grigydaind gafnitpfgt aysrlggigq aksqttelni dgllginrni
      541 tqainlnval ganlrknkie sigisgnqln ipylytisnt lsknqsygyn erqvqsayyt
      601 adfnyknylt lsttgrydvy stlpsanrgi fapsvsasfv fselwkstll nfgklrasya
      661 qtsgeayday ltsqyyslgn tynglpqggf sstlpnvnlk pfrlkefeig fetkflnnrv
      721 gidlayfnre tngeivngpl siasgytsrv lnlgstknsg vellitgtpl vskgfkwdvs
      781 fnitsvknti vdidgtanps plilgtyrpl ngniahvkgm aaaqvlaydy kydangkmii
      841 gdngvpvrgd fkpmgsalpn lygglnnsfn fgdfsfsflf dykfgakvls atnhysivdg
      901 lnkitlvgre ggvvadgvla tgevnaknvp aytyypalvt nisklnvfsa dfiklrqvvl
      961 gyhlparwfs ntkfpfeais fslvgrnlat llkhtdnfdp eagissdvry agieglqmps
     1021 trtfgftlna rfkk
//
LOCUS       WP_100989885            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100989885
VERSION     WP_100989885.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116288
     Region          24..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknlllsil lvcstwaatw aqdrkitgkv ssaedgdglp gvsvvvkgtt igsvtdangt
       61 yaisapaaks tlifsfigmk tkevelgans vvdvkmasdt kqlaeivvtg vgvatdkrki
      121 aisvesvssk dlpqapsasi dqaligkipg aqitsrsgtp gadvnillrg intinrgtqp
      181 milidgiqmg atslqtidln aiervevvqg aaaatiygaq gangviqlfs kkgkngqmni
      241 disssiaqnt ylnvgglska kyhafvtdas nniigssgkp ivfdaangiy senvqynstd
      301 ptatnskpyd anlqyhdhfd yffkpantfn nsvalsgggp kgdfsvsasn shqesnirdn
      361 gyfdrsnlma nigmnlakgl tlrsitqlay tkstlktsdr tilfsllnay pladfdlttt
      421 dgsipynmnq tiginasnps yrqaytrnnd nkvdiiqnln lnykfpkfve ldakyglnfq
      481 tqnrdlefqn qannanikyw ltqgtatyis nyntnntgdl tkyvntkmfq nflatatavf
      541 dlkedfglki piksvtqasf dwrnsklney tsaamglpaa yspynaants swrvyrdyke
      601 pfitygylvn qrfeygdflg isggfrsdfs safgqgskpf tfprgdaylr lsslkfwens
      661 pvngflpelk lraaygqagi qpqpfdryvt itpttlgtnt afyyangqsn palgvevsee
      721 lelgtdmvfs lmkgsswlna iavsatywnr ktkdaiyqvd vapsvglgkl tdnaftlgsn
      781 glqmslnstv ynggnfkwnt tvnfgkqssk iiavrgdapv vvtsnagstn yvlkagekig
      841 qlygykvihs vdevspltgt afipqadqes ytlasngivv nkltkqpyft adkfsfgdpn
      901 pkfnmsfind ftfknfltvg fqldwvngnh lynqtkewmy rdgihsdyan pitidgqtga
      961 wtafyrgvya qrtangtkdy fyedasflrl rnvsvgldfa klfkipgtrk vqlvlsgrnl
     1021 wtltkytgfd peissgtsns awdrgtdhst mpnyksyqas lnigf
//
LOCUS       WP_100989899            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100989899
VERSION     WP_100989899.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117850
     Region          24..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkficmsml licalsitaw aqdrriigkv tsaedgsslp gvsvvlkgts kgtttdaggi
       61 fdisvpsakg itlvfsfvgv atqevpvgnq sevnvslvsd srlltevvvt gsgvatskak
      121 lgiavesvsa kdlpqtptas idqaligkip gaqisstsgn pgdpvnillr ginsvqggtk
      181 plimvdgvqi astdinsldl snvdrvevvq gaasasiyga qgangviqvf tkkgkkgrta
      241 vnfsssysan eflntgnvhk adlhpyltda nnniidtqgn ildytqygai egisykygga
      301 tryaiqdirn dantpysgnl kyydhfkqvf ktgsttnnni nvsgaseksd fniaaannht
      361 sspiltkeng yidrsnlsan igtelfkgft irsttqlvyt kntlkpglga aygpfnggng
      421 nvgsvynfln tspffdltrk ladgtypvyp tadflsvnag npyyqasytd ainnkidvlq
      481 nfnanykink fleldakygi nyrnetarwt yfnqsqntss eyyqswtany apdnkgeidn
      541 fqynntfqnf lgtafirtdf qddfhiklpi qtstqisfdy rknrstqydt ygvglstapp
      601 fnvaatssqa vandivtpfi tygylvnqkv dfgdyggita gfrtdwssaf gagstpftfp
      661 hfdghiapls ffknsslsnt lpyfklraay geagiqpgaf drypvlsqrn lgsglvytvp
      721 tttqnpnlkv evskeleigt dftiggnsnr awlsslsgsf tywkrssanv iytvsvppsl
      781 gstgqltnai dmssngvqfs lslpiyrskd lkwdfttnfg hqvskidais ggadiiltsn
      841 agstalvltp gqpigqvygy ktltsldfkn qegvpyitda nrgnytmvgn yvvdkttyqp
      901 qftnetyplm npnpkfnasf ingvsfknfv tlnfqfdwvy gshlynqtke wmyrdgisgd
      961 fskpvtidgk tgaytaywsg ayyglwgstr gagnnatkdf fvedasfvrl rnislafdia
     1021 kvvklpylnk aqivftgrnl mtftkytgyd peissgtsns sfdrgvdhst lpniksyqvg
     1081 lnigf
//
LOCUS       WP_100990380            1147 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100990380
VERSION     WP_100990380.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1147)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1147)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1147)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1147
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1147
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125251
     Region          137..1143
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskrvlcqkt lqkimrigfy qaflsvafvt lvhahvvngq kvleqkvtfq mtnadvekvl
       61 dkietvthvk flynpqifgp erklnykfqn eslsdvlnrv lspyqvayev fqeriilkrq
      121 esqsngqsat kqeapkrkit gvvldekgat lpgvsvvlke tqkgtttvad gtfsldipdq
      181 grdgvpavlv fsfvgykrqe vtvgsqsnls vslvpeastl gevvvtafgi arekkalsya
      241 vtevkgnelt qarennvana ltgkiagvna tgmatgpggs sriiirgngs lngnnqplyv
      301 ingmpmdnst pggtaadgng mnvdrgdgig ginpddiesi svlkggpaaa lygarasngv
      361 ilittkkgrs qkgigvevns nttfediavi pnwqyeygqg vdgkkpttit eakstgrlsy
      421 garmdglpti qvdgqlhpys pqkdnlknfy rtgsnyinsi aftggsetmn frlglnntqs
      481 nsivpnssfa rrianlsmna flgkklsvet vfqynveegt nrpkvgyadf nphwatylia
      541 nvvdirslap gydpvtgkem ewnpvpaapn pyfvinkfkn ndvkhrfisq gsirydildn
      601 lflkgsvsqd yysfsseyvq ptnnayqplg tyearkttss etngmltlny ntnfnnisfs
      661 alaglnaqrs ifdqtviags eftvpyfysy tnlatstttp tylksainsv fasadfgykn
      721 vayltlsgrq dwfsvlnpks nsifypsvgg sliltdamrl pkaisfaklr aswaqvggat
      781 vnayqiyqyy smqqgghngr pvqvlsssqv pnpdlkplts ttyeggfeak flnnrlgidl
      841 tlynrkttdd ivtsnialss gytsallnvg vlsnkgvell ltgtpvskgp ftwdvsynma
      901 ynkskierla dgitgidvgt gvggglvrnv ldrpygtvwg yskktdasgn vvfntasgya
      961 vrgdlqeigq gtppltmgit nnfryknfsl nilvdgkfgs ivysnlyqya yrfglpqetl
     1021 pgretgitvt gvtpegnpys ktwakeevdt yydndknyts ifmfnndfvk lrqvilsynl
     1081 pvsklpflkl qsatisfvar nlailykdkk nqyfdpesgy tstnaqglea fgvprtrslg
     1141 vnlmvkf
//
LOCUS       WP_100990370            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100990370
VERSION     WP_100990370.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113302
     Region          24..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkhllccfl lvitaagplw aqnrqitgtl rdeqgqaisg anvvikgttr gtttdavgef
       61 klsvpneatt ltvssvgytg kdvavsssqs qlsvtlvsdd rvlgevvvta lgikreakal
      121 syatqtikpa qinevrdgnv lntlqgkiag ayitqgsggp gtgsrivlrg nrsiqgtnna
      181 lmvvdgvpin nstfgqatsd fgsvansdga sninpddien vtvlrgasaa alygsqaang
      241 vilittkrgk agrvsvdvns gvsidkpfal pmvqnqfgqg iggkldpavg aswgaamtgq
      301 sytnylgnad tytaqpnnir dffrtavsfn nsigitggse ksqtylsytn nalqgtvpgn
      361 dlmrhtinlr lsnqisskfs tdakityinq svvnkprtge enapvidlyq iprnvgiata
      421 qnyqapnafg lptptawpst lssiyqnpyw vtnqtainqy rdrvigfila kyqltdflsi
      481 qgranldkyf dkneesygqg tilwanqagg kfarnnivnt qswydllieg knklssdlti
      541 dyqagaiiqd trfqstnata dglnvpnryn lnfgtnqtlg ddysrvqtqs lfgqaslawr
      601 daifinaslr ndwsstlpkp ysfqypsvga svvlsdllkl sgplsflkin gsfaqvgnga
      661 spyllqtnys ysqgagsgfi srdgtqaign lkpeitksle fgvdarffsn rigatvtayk
      721 tnsinqllkl glapasgfsd qyinagdirn mglevvingt aiktdrltwd ltlnmglnrn
      781 kivslspdik taflsggygr saspivqegg aygdivsyrw akdangqymi gsqsnsttvs
      841 easvvstglp vatkeqefig nfnpkmllgf tntftfkgfs lrflvdarlg giavsgtemn
      901 lafsgipevt alnraggwvl pgvtagvaga dgvtmigagk tnsqaitaeq fwqtvsgkry
      961 gwgeffayda tnvrlreisi gygipvpsns fiksarlsfv arnlfwiyrg sslldipgig
     1021 krkmwfdpdv nisngnfqgv eygtlpsnrs lglnlklsf
//
LOCUS       WP_100990392            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100990392
VERSION     WP_100990392.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113873
     Region          24..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkalillfh llvcsslafa qtnkitgrvt gpdkeglpgv nvlvggtsvg tatdasgnys
       61 inapatasli fsyisyvsqt vpinnrsivn vqliedakai devivtalgi kkeaktlgya
      121 tatvnadqis vnrtpnfvsg lqgkmagvni ttmgtgpagt akirirgqss fsgqnnpliv
      181 vngvpidnsn yslggdfgsr aanssdggdg lssinpddie tmtvlkgata aalygsrakd
      241 gvvmittksr gagkgysvty ntnfttdtpl dftdfqyeyg qgeggkrptt pdptsgvwsf
      301 gekfqpgmtq vlfdnktypy epvynrvkqf yrvgtnftnt vtvanngqng gfslsfgntd
      361 nkgimenntf nrkvinlgft qnitskltas gninyskenn inppqlntqd fsvstvvftl
      421 ansmpfdalr dnqtkpngde yvfsrflvrn npyysmsrhf enirrdrlfg nvalkyqftd
      481 wlylqariaq dyyirnqdyn ipngyapiak apvgyvngsy tqdvrqnter nldfilgank
      541 tfgkigvdit lggnaryarn dynsvtvqdf vtpglytvan griknpiyal aekninslfg
      601 aatlsyrdym flnvtarndw fstlapanrs ilypsvtssf vfsqafenlp pwlsfgklra
      661 ayaqvgsdnv dpysnalyya vdnnsfpnps gqlvpvggin atvvpnknlr plriqeaevg
      721 lelklfnskl gldftyyhkt tddqilaaqi sdassytskl invgrsmnqg leilltgspv
      781 vsqnfrwdvs anvsyntskv lrlglspndt vitvnsgggr tlnqvvgkpi gqlytftylr
      841 daqgrqvfdq nsgmplrnnt lknvgnalpt yfggitntft yrgislsali dfklghkmia
      901 grninymrhg lskrtlpgrd vgyvigngvn pngeinqtka avqpfyesin plginedfvf
      961 nagfwklrqv slgydfskll pqglfikglk lnavannvli ikkwtenmdp eealvssdng
     1021 vgldfwpglp ptrsigfnln vrf
//
LOCUS       WP_100991019            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100991019
VERSION     WP_100991019.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119394
     Region          26..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkvligswl lsllfclpll aqdaavtgrv tssddgsglp gvsvvvkgtt rgtttdvngn
       61 yqintgsntt ltfsfvgfkp qdvvvgnrns vnvvlaadas tlnevvvtgf giqrtereig
      121 tsiarisnsq itqaapinva ngltgkvsgl qvsttnngvg agarltlrgn rsflgnnqal
      181 livdgvisdi sflssinpnd idqttvlkgp saaalygsda sngaliittl rgtknnkpqi
      241 tytnntqfes isympglqtq fganggegvp fydrnyarty vpyenqqfgt pfdgslqplg
      301 ygvqirdsng ntridtlkip ysapskdprk affntgvtqq hdisyrvgdn lnyfglslqr
      361 vdqkgvvpnd kyqrtnlsik ggrsidkftt nagmqfsyqn sntengdfnq nrpvywnvln
      421 qqpqaplnsy plnditspyg dvngyynayy pnpywqitgd nsrkvtniyt lqgsadvsyk
      481 ftnwlsvlyr vggqfynsql kahiadvtfs dyatgdpwea gniassaggh tnatvqdatq
      541 lrtrftgdll vtvnpkfgdf ttrlilgqqt rqeyarstyd yagalvvpgt ynvanrlgna
      601 tlaeynsqnr llgafgdftl gykeavfiha sgrndwtsll apsnrsffyp avdasvvlse
      661 iipglkgnsi lsyakirgsl skvgqvnvap yqlqnvfnpg tgfpfgsqag feqsnqqndp
      721 nlkpeftnsr evglevglfd rfnleavyyn tlttnqtvpi gisqatgyst alintgtmqn
      781 qgfeldlrsi rplvntggft wdinanftyl eskvtdlyqd lprinipygs dpyrptltgg
      841 asnvyaaksy aypalfvsdi qriqssdaka pnydptgqyt grpvvdatgy pildpnlkya
      901 gttqpkyrfg ftntfkfkgl tlaavveyrg gaviynalgn aleftgagvr svyagrqnfv
      961 fpnsvlvtnn pdgittatvt pntnvttkdg nlvfwtnsgy hnaassyvts adfwklrevv
     1021 lsyniptkii gytkfiksln valtgrnlim lrpktnvftd pefsggtnan dtsnavgttt
     1081 eyqtpptrly gfrlsfgf
//
LOCUS       WP_100991021            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100991021
VERSION     WP_100991021.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118040
     Region          25..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkfllaqfi lclfafplla qnraitgkit ssedgsvlpg vtvlikgtnq gtttnaegaf
       61 qinaakgatl qisfigfatq svtldnqttv nlalkpdasq lqeivvtaqg irknqreigy
      121 aiskvntedv tvgrspqlaq alagkvtgla vynvnnsvdp avkivlrgyr sltgnnealv
      181 vldgmqttst ilstinpndi esvsilkggq aatlygssgi ngaliittkk gakgklkvny
      241 snstnfeqis fmpqtqdkyg sgshyatafg tagyktdyla rmadnwrsye nqqygdafdg
      301 slriqgrtae dgsqllipys avpngrrkaf ntgvsvnnqv nfqggdetss fymsienqsv
      361 ngivpgdksn rtgtrlsatk eygkltasfn agyvqgvynr tssdfynnvl nqpanlplsd
      421 lrnwqtnpla npngfyndyy nnpyfeadnn rlnykdanin gnlnltlkat nwlsitnrvg
      481 imnnsrtgkn ttgkftytdw aksksfipap ffrdgdgtgi yraitdtpgs vldysgtenv
      541 innefqvqls kdlgplsnrl ilgnslyqrt tnnigvgsns ivvpdvynvs nrqgiltggq
      601 iltqerrlgy yadltmnykn ylivngsfrf dqtskfykpn raanfwsypy ygaavsfiat
      661 dafpsiksef lnyfklrany nknandnipl ygldltypng tsfpygstvg ltvgntlpdp
      721 nlkpetvyss eiggefqlln nrinvdvsay tqnskgqvit vrvpnstgfq nllinvgetk
      781 nwgyeaevky liarggkfsw dasvrysynd nkvvdlypgi nefqiggfsy antnvikdqr
      841 fpilktdgyq yapdnsgrvl vnattgyplr ntsllprggv lprhiaglgs kmeygnfgft
      901 fnfeyrggnv mfsdlgrqmt ftgtgkwted raphvfpnsa ilnadgsvsa natnvreaey
      961 slwvdnyrli senfvtpgwf iklrdinlsy rvpqslltkt klfsgasiav ygrnlftivd
     1021 klnyytdpef syqgnptpgs qststpttns svgiginttg qtppvrqygv ninltf
//
LOCUS       WP_100991358            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100991358
VERSION     WP_100991358.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124025
     Region          40..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpfstfqli lrqtlpiiml vgvcfthvla ngsaknkpar titgnvtigt nnqsiagani
       61 vikgtqigti tdqrgnysit vnadnavlvy sfigyktqev vvgnksiidv alvennevlg
      121 evvvtalgik rearslgysv gevqgkdlsr vaqenvlnsl agrvagvqis stgpsgssvs
      181 miirgaksln tdnqplfvvd gvpvanslnn vsqigndnrv dygnaisdin pddvenisil
      241 kgpsaaalyg sragngvvli ttksgsksqk mtvsvtsntv fdqpykylkm gskfatgilp
      301 ftpdnnpypg gilqidesss ggvgpeldkg ynaiqwnspv gsdgnqiptp lvshpnnvrd
      361 fvrtgitstn gvsisnnsek ityrlsysnm ssrgivpnsd lfkntlaist nvrvnskltl
      421 stnldfsrnn snnrpagerg tnplqwaygv gshidindlr nywvpgkegl qqqsqsigny
      481 nnpwflayev nngyvrdrvf gnlkaewqit peiklmgrya ldtyseqret kiaksytgep
      541 ngayglinlk ryernadfla tytkrfnals vvvsaggnnr ysqstdlsns sksgagliip
      601 glytiqniap nnlqysnyly kkaiysayat anlgykdmiy ldltarndws stlpvnnrsy
      661 fypsaslsll lneivhlsnn vdmfklragv aqvgndanpy slyptlgdag awngvtrlsk
      721 sgsillpnlk peiatsyevg idynmfrnrl rfsgtyymsd nrnqilpsqi spssgfttkn
      781 inagllesrg ielslggtlv dkgglrwdlt tnftknttri kelaegipyy tlwtdakgga
      841 wtyvgdkvgd iydaevitvt dqkssyygyp ildndgswqs ksatntknki gnfnpnfmlg
      901 aqsslsykgf tlnfsldwra ggdfvsqtyr ymesdlrsqr fldnlinpgd rtgdalrnwl
      961 venadkniki qgnyfpivgg ptaayggypf efggktyayg vfnpgviaqy dsqgnitgyt
     1021 enlggagtki ipygdnypws ftraatfdas fvklrevslg yelpaqfvks iglqsatfsv
     1081 ysrniilwta akinvdpema fqpqsspqag tqfkqgiery nvtpwtipvg fklgltf
//
LOCUS       WP_100991692            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100991692
VERSION     WP_100991692.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115000
     Region          33..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhtlrekak icflalwsil lishatqaqd hrltgrvtsg kdqqpipgvn ilvrntqlgt
       61 ttdgngnftl nvpanatlvf saigyagstv dvgnktqlnv tlqeaeqslg evvvtalgik
      121 keakrlgyat aivnpeqvtt nrsvnfinal qgkiagvnis slgtgaagts kirirgqssf
      181 sgqnsplivi ngvpvdntnf gqnngntgsd nsigsrdrny sdggdglssi npddiegmtv
      241 lkggtaaaly gsrakdgail ittktkgtgq gigvtynmny tsdhpldytd yqyeygqgey
      301 gvrptapnpt sgvwsfgekf agqtqvlfgg ltvpyapvrn rintfyrdgs tmtnsiavss
      361 gnekggfnls vsnldnkgit rnnsfnrkti nlgfsynlsp rlsvtgsmny sneynknppq
      421 iaqqdnstpt viytlansmp ldvleanqin patgnefiys rfmnrtnpyf vlnnkfenir
      481 rdrlfgnisa rynvtdwlyv qgrvgqdyws rdqdynfptg qaslaaapag fvngayvqea
      541 rrfrevntdf liganrkfgv igidltlggn qlyrrsdlns vlatdfvvrg lytpqngrvk
      601 dpqyslserk vnslygaaei sykdvlflng tvrndwfstl spanrsilyp svtgsfvfsq
      661 afnnlpswln fgklraayae vgsdgdvgpy snnlfygvna nlfpnpsgng qpvgfitsnt
      721 vpsatlkpsr vaetevglel klfnnrvgld vavynkitsd qivakqssda sgytsslins
      781 gqsrnqgiev llnmspvrtk nfswdvtlng synqtkllkl ltdtpgeqiv vgtgiyvgel
      841 rqvvgqqlgq lytygykrda qgqlingtdg lpvrtdapvs fgsalprfig gitngfnykg
      901 vslsflidfk lggkmisgtn lnafrhglqk etligrgead nkmvgpgvna ngevnavraf
      961 vqdyysvgrs kslgeqvvyd aglwklrqis lgydftkvlp knlfikgvrl savannvail
     1021 kkwvpnmdpe qfgfssdnli glestglptt rsigfnlnvk f
//
LOCUS       WP_100992801            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100992801
VERSION     WP_100992801.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111904
     Region          26..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkillgswl lsllfclpll aqdvavsgri tssddgstlp gvsvqvkgtt rgaitdadgn
       61 ykisvpadar lvfsfigytg qevavgnktt invslvagsq sldeivvtaq gierdkrslg
      121 yatqeiggni laqrsepnll nalqgklagv sitgssgapg astninirgi tsfngsnqpl
      181 ivvdgiifsn dvnttqntlf gsqpsnrlad inpesiesvn vlkgpaaavl ygsrasagai
      241 vittksgrnq nnktevtvns synvqnvygi pkfqndygqg annlltptsn nswgppfvgg
      301 ptsvtnaqgl vvpyqaypnn vrdfyrqgsi lqnsvniasg datrnyiiai gntlqngvvq
      361 nskfnrtnvq lggesrlqng lkisgtgtyv qtvsrgipgg ngastfgqit riprsydlan
      421 evyqdingks vyftpatnnp qwsvnnerld sqvdrffgnf qlsydvgkwl tiayrvtgdt
      481 ytdrrkltlp igsgraplge vqqdnffrne lngdllitak kdnifldgln anlllgnnin
      541 qrktqesaad aasltlpgfy ninsgtvftg tfenssvrrl vgyygqlsln ynnylflels
      601 gradqsstlp kanntyfypa asvsfvptda fkinsdvlsy akirasiakv grdadpylls
      661 tiytttaygn nvasitypla pnntpgfsig trigsntlkp efvtsyeagi nlgffknrls
      721 idatyfdsks tqqifnvavs nssgfdtrtt nvgelqnrgv elvlnatpir vggfkwdatl
      781 nytfirnkvv siapgvvssn iagnsfigia psiyegypyg vivstansrv qntnptglyy
      841 datgqyagqy vvngstgqfa pgvansvisn pqpnytaglt ntfsykglal svlvdtrqgg
      901 qlfsfnavda rsngslyatt idrdqprilp gviqnadgsf rpnniqlpaq tywgalggla
      961 segavydatv yrlrevalny tlpksllgkt pfgtisvgvs grnlffyapn fpadpetntq
     1021 gagniqgldl ngppntrnfg gnirltf
//
LOCUS       WP_100992057            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100992057
VERSION     WP_100992057.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117555
     Region          24..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msrilllsfl lvsslwstaw aqerrivgkv tsaedgsslp gvsvvvkgts kgtstdasgi
       61 fdmsvpakgt tlvfsfvgvt tqevvvgnqs evnvslvsds rlltevvvtg sgvatskakl
      121 giaiesvsak dlpqtptasi dqalvgkipg aqisstsgnp gdpvnillrg insvqggtkp
      181 limvdgvqva atdinsldls nierievaqg aasasiygaq gangviqvft kkgkkgrtsv
      241 nfsssfsane flntgnvrka dlhpyltdgn nnivdakgni ldytengait gisykyggat
      301 ryaiqdirnd antpysgnlk yydhfkqvfs tgitsnnnvn vsgaseksdf niaasnnhtt
      361 spiltkengy idrsnlsani gteifkgfti rsttqlvytk ntlkpglgam yspfnggsgn
      421 vgqvygflnt spffdltrkl sdgtypvypt adflsvnagn pyyqaaytda innkidvlqn
      481 fqaeykinkf ltldgkygin yrnetarwty lnqsqnitse yygsyasnya pdnkgeidnf
      541 qytntfqnfl gtafirtdfq ndfhinlpiq tstqvsfdyr knkstqydty gvglstappf
      601 nvaatasqav dkdivtpfit ygylvnqkvd fgdyggitag frtdwssafg agstpftfph
      661 fdghvsplsf fknssianal pyfklraayg eagiqpgafd rypvlsqrnl gsglvytipt
      721 ttqnpnlkve vskeleigtd ftiggnsnrt wfnsisgaft ywkrssanvi ytvsvppslg
      781 stgqltnaid mssngvqfsl slpiyrskdl kwdfttnfgh qiskidaisg gadiiltsla
      841 gstalvltpg qpigqvygyk altsldyvnq egvryisaan eggyqlvdgr vvskttyqpq
      901 ftnetyplmn pnpkfnmsfi ngvsfknfvt lnfqfdwvyg sklynqtkew myrdgisgdf
      961 tkqvtidgkt gafpaywsga yynlwgstrg agnnatkdff vedasfvrlr nislafdiak
     1021 ivklpylnka qivftgrnlm tftkytgydp evssgssnss fdrgvdhstl pntksyqvgl
     1081 nigf
//
LOCUS       WP_100992762            1152 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100992762
VERSION     WP_100992762.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1152)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1152)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1152)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1152
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1152
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125445
     Region          72..123
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          158..1149
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknqyillsm llggvytmpq psvaqvltra qpayestasr qqssanaldg qrnrrsrslk
       61 kalselerrf ninfaydeql vtgrqtdael dglsleqaln qliesqglry rkvndklfai
      121 qsapakkvgl afptegtapa latvsnalpd lteapqvkri tgqvtdetnq glpganiiek
      181 gtttgattda ngnfvlnvsd aattltvssv gyasqdvtig nnsvvnvklv pddrtlnevv
      241 vigyqtvrkr dvtgandvis stqankvtan slaesiqgls pgvtvrntgv pgqqasiqir
      301 gvasflntdp lyiidgmiad anptinnddi esiqvlkdas aaaiygsraa ngvviittkq
      361 gkegpirvsf sgkygiqqvy krwdvmdatn faatqrtqyq nagqtppssv atgtfnpnin
      421 tnwqdqvlqt gnlqdynltl sggtktgtyl isgsyfsnkg yvigsgfdra slrintksql
      481 grftfgenal ltnsniqnfp agnpiydmag mlpvipvqdp syidagnpgg ygigrnpdav
      541 tyafnpvavr nlasnksnfa klvgnayldv kltdwltyra naglevsfdy tqnlrrigty
      601 qysaspvass vgedrsryls mlfehtlnfn kafglhsing vvgisqqttr rditsgsrtn
      661 lgfaggqyfn tinaatgisn saggtpddyr ilgyigrvny tyndkylltl tgrvdqdsrf
      721 ganyrtgffp siagawrisq ekffhvdwis dlklnasygk lgivvptlgs fpytafinnn
      781 praifgidqt anvgayqaql anpdlrweer iqqnygvsas flrnrittei nvynslsnda
      841 ilnlavpgyl gnlrgnpyvn tasirnrgve fsatyrnneh avkwdvsgnf ttiknrvenv
      901 gnqgqninyi qsgntrsqvg qavgqwyvlk taglfqnqee innykgtngn liqpnakpgd
      961 ikyvdtngdg qitqnddrqf vgspwpklqa gaqanasygq fslnvqltgv fgytvyndvr
     1021 rgldsyqltn frndispwtt tntntsdprl gleagdqgii snnfaytdrw lenasyvrvr
     1081 nveigytlpk tllstlkirn arvyvsgqnl ftitqytgld pdvtganiqe rgvdnghwps
     1141 prvvsvgvnc df
//
LOCUS       WP_100994153            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Spirosoma
            pollinicola].
ACCESSION   WP_100994153
VERSION     WP_100994153.1
KEYWORDS    RefSeq.
SOURCE      Spirosoma pollinicola
  ORGANISM  Spirosoma pollinicola
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Spirosoma.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Spirosoma pollinicola"
                     /db_xref="taxon:2057025"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116143
     Region          16..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maflfcllts lsalaqtisg ritsgddnqp lpgvsivvkg tnagttsrad gtysinvqss
       61 stltfsfigy atqeiavanr tkldvtmvag drtltevvvt algikkdirq tgvsiqsvdg
      121 aqllkarepn ainslvgkvs gltigassel lrrpnivlrg ntdvlfvvdg vpinsdtwni
      181 saddietysv lkgasasaly gfrgkngail ittkrgtkdk rgfavdvnts qmvdngflai
      241 pkvqdeygpg dhgvyefvdg kgggkndgdy diwgprfegq lipqydspvd pvtgkrtgtp
      301 wvargkdnlk rflqpgllst nnisvsssge kydlrfsvsh nyqrglvpnt klnsttfkvs
      361 tgynfsnrlr fegdvqvnrq ytpnipdvdy gpnsmiyniv iwggadwdvd qlknywqpgk
      421 egtqqiyaey qrynnpwfva kewlrghykt divgqtslky niatgldlsl rtqvstwnll
      481 rtekfpysat sygreetkgd yredrrnlld nntdlllkyd krvspllnin aiaggnlrvy
      541 nynsnytstn ylnvpgvynf anslnpvias nfnsdmrvls ayysadftlk dfltvsttgr
      601 mdklstlpkg nntffypsva lstvlsdylr lpqaisflkf rasyanvkdg ltqstigvps
      661 fpvgygqqya ssydgptyqn aavyatpytv gntptayftn alnnpnikpn stsqtevgld
      721 vrflnnrlaf daayyisddg prifnlpise ttgyssalvn giktqkkgie lsltgkvlrs
      781 tnglnwdvla nwstykevyk dfypgvtaln tffkvgdrtd kyytstfvra pdgqiindag
      841 grpirttvaq yvgninpdwv fglnnrfsyk nltfsfqvdg rvggvisdyi qqksyaggri
      901 intvqgdmgv arindtkgik sylgegvqvs ngasinynsd gfvtnyaelq fqpnttkafl
      961 qdyiarrygf dggnmisrsf vklrevvlgy slpqtfisrl gvkqasvsfv arnllyfaek
     1021 kdididqfts ggrsdlqtpt trrygfnlnl tf
//
LOCUS       WP_100996949            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Lacinutrix sp.
            Bg11-31].
ACCESSION   WP_100996949
VERSION     WP_100996949.1
KEYWORDS    RefSeq.
SOURCE      Lacinutrix sp. Bg11-31
  ORGANISM  Lacinutrix sp. Bg11-31
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lacinutrix.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Lacinutrix sp. Bg11-31"
                     /db_xref="taxon:2057808"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111461
     Region          25..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lllafvvqls faqgktisgt isdgdnlplp gvnvvvkgts ngtttdfdgn
       61 ysisantgdv lvfsfvgnne ektvgannki sftmlenqle evvitalgik kaekaigysv
      121 qkvsgdglte aregnlvnal sgkaagiqvt nssgsvgass rivlrgnsti tgnnqplfvv
      181 dgvpldnssy ssagsgggrd lpngaadinp ddiesisvlk gpnaaalygv rgangvivit
      241 tksggnkdgs fsvninsnat fsnplklpsy qnsygqggdt nyfefvdgas ggigdgvdes
      301 wgpaldvgle fvqwnsqlng gqalpwvsnp dnvkdffdtg valsnsisvt kggqggsmrf
      361 slgkseqdgm vpftelnrln lgfngkmdlg kkfhggmsms yinsesdnlp tggynnenpm
      421 qqfiwsarqv nfsdlrdwrn fplapsntaa agtplnwnhn fqnnpywile nnrntfaknr
      481 yvgniyftyd fsdkfsatak ysrdqyaqae siikakgsne spdgaytevk rdyteaniel
      541 llsyntdlsd dftlslnagt ngmkrnyssl igsapglelp glynlsnilt gatptysnys
      601 serrinsvyg fgsigyndyl flefsgrndw asvlpvanns ffypsvslsa ivsdmveldg
      661 akidylklrg gwskvgstga lgpynlnqty glsnnafgnq astpntrfsn tltpetvtgy
      721 eagidvrmfn skikfsatyy nqlstdlllp iqlsastgvt sawknageme nkgielslga
      781 tviendnfkl gvdfnwaknk nevvslggld syilgsqwgv rlearpgqpy gvlvgrgfer
      841 ndsgqviyen glpkiddtyk vlgdiapdwt ggvslnmqyk gftlntlvda kiggdvhsms
      901 yawgryagtl eetlegretg vvgngvmsdg sggyvqnnvv ttaklfnqna fgngveesai
      961 fdasyvklrs vsigyslpqs llkgtfisna kfavvgrnla ilhsnvphid petgfssgng
     1021 eqgqefgqip sarsigfnvn lsf
//
LOCUS       WP_101013125            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Nonlabens sp.
            MB-3u-79].
ACCESSION   WP_101013125
VERSION     WP_101013125.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens sp. MB-3u-79
  ORGANISM  Nonlabens sp. MB-3u-79
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Nonlabens sp. MB-3u-79"
                     /db_xref="taxon:2058134"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116852
     Region          20..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgitlfmll lcgfigaaqi sitgiisdta gdpiafanvt ergtsngttt dvngfysltv
       61 andgilvcsy igyqtaiipv gdevimnltl eegdqletvv vtalgvkrne relgyavqtl
      121 dseqiqevks vnlvdnlqgk iagitvtpga tgvgasskit irgeasfsnn nplfivdgtp
      181 innntvfnfs neaaagfqev dfgngagevn qddiesvsvl kgpaaaalyg traangaiii
      241 etknggknkg lgisyntsff vdsafklpef qneygqgnsg qfeyvdglgg gvndnisysw
      301 gprldqglli pqfdspvtlp dgstvrggdt svysglpita tpftsnpdnl knfyntgyta
      361 inniaitdgf engnyrlsft dlrsesiipg vdldrqtvaa klnftpndkt kirasvnyvn
      421 sasgnrpsng ygsenvnysl vawgprslni dnlrnywqpg legvqqysfn ytffdnpyfi
      481 lqenrnsfgr drlfgnvsls rkltpeltat vrtgmdysne krrfirnfst nrfrsgayae
      541 hdvfyreint dfllnykkqm gvinfdasvg gnrlsqtast tqvqttslaq pgifslnnaa
      601 spiesfgfrs ekrinsfyaf akagyknfly leatarndws salatpfsaa ntsffypsvs
      661 tsfilsnvvd lpsaidfaki rasyaqvgnd tnpyqtqgtf isqtnvnsqp tfsnqdfipn
      721 qnlrpeltss velgfdirfl kqrlnldfty ynaltkdqil slpigiasgf sqqvvnagav
      781 rnkgfevvfn aipirttdfe wsatvnfasn raivedlpqe egrltlaysr vydsqnqtvw
      841 hqveeggrig dlygtgylrn engdfvltpe grfiadpelr klgnynadft mgfnnsftyk
      901 nwdasflldw rqggiivsrt lalgavggql aetanrpdgg ivangvintg sstnptyvqn
      961 ttavsaesyy rqfydrnhee nnvydasylk lrqfsvgysf dlnkgalglf ddgaqmrvsl
     1021 igrnlfafsk iphfdpeqla vqgqgfingv edmsyastrs igikagiqf
//
LOCUS       WP_101013113             960 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Nonlabens sp.
            MB-3u-79].
ACCESSION   WP_101013113
VERSION     WP_101013113.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens sp. MB-3u-79
  ORGANISM  Nonlabens sp. MB-3u-79
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 960)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 960)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 960)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..960
                     /organism="Nonlabens sp. MB-3u-79"
                     /db_xref="taxon:2058134"
     Protein         1..960
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104124
     Region          23..959
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqkskavll lfllpffafa qsvitgtvle snglpalgat vsvkgtsngt stdfdgkykl
       61 nnvpndaviv fsfigyttqe ipftgqtlin itleenpsel daivligygs ikkanvtsaq
      121 ttvdeeefnk gaivspgqll agkvagvqvt aasgrpgdgp virvrpgstl sgnadalyvv
      181 dgvpldqrna slnsinpadi esftilkdas ataiygnras ngvvlittkk aklnsdlkle
      241 ydvqfavnqv qnyadvlsad efrqlitdqg rdpsvlgtan tdwqneiyqn gtrvihnlta
      301 ekgyettsir aslgytnehg tllrsgyera tlglnvrqnf lkgdlrftft sqmaqeeirn
      361 adagaigaav vfdptqpifn nsgayggyfe ytnttgpepn aprnplglln sldsqldnsq
      421 arlnlnaayn irqvpglkft gnagidynef dsysirdfns gagargnnrs fsegfrrnql
      481 ldgrfdykrt lgaldtdmel tlggsyqdfm rqtggrssvn gglqdnplav destlitafa
      541 rasfdikdlv ilsasasrng ssrfseenrw anfygisgal kltntnfvqn sgflsqlkir
      601 ggfgqtgqqn iaasfpfirv ftpgqpqaav qfgnqfvtti rpegitdpkw ettdqwnagi
      661 dlgffddrit gsvdgfyret fdvlqyaplp agglenfgfi nagetksrgi essisikmiq
      721 seninwtlsa natvqeieit dlagadntpv piggisggvg ntiqewavgf dpttfsvfrq
      781 vydqdgnpld gvfvdtngdn iindadrvry kkanhdlyfg ftsnfnyknl dlsftfrgaa
      841 ggynynnvas naanygsifp tntqnpiyin apvdvldtnf sqqrlfsdyy iqkadfikld
      901 nislgynfpg ekvdirasvt gtnlititdy dgvdpevfgg vdnnlfprnr glifglgfkf
//
LOCUS       WP_101013336            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Nonlabens sp.
            MB-3u-79].
ACCESSION   WP_101013336
VERSION     WP_101013336.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens sp. MB-3u-79
  ORGANISM  Nonlabens sp. MB-3u-79
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Nonlabens sp. MB-3u-79"
                     /db_xref="taxon:2058134"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111034
     Region          24..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklngilt lllalvvqva faqqtvtgkv tdtegglfga vvsvkggtan tttdfdgnys
       61 iqansedtlv ftysgydqvm vlvgdqtvin tlmktsldav vvvgfrdavk erinvaasvv
      121 tsetienrpn asfvqtlsgq vaglniftns gqpganstvn lrgvgsingn teplflidgi
      181 pvdednfrsl npqdiasvvv lkdaagtsiy gnrgangviv ietrkgkyeq plkvnatsiq
      241 sftnlmgndy nymdsqqllt lerdrgvgfg angfdgsgtp ltdaqiagap ntdwkdvffr
      301 tgvstnntvt lssggknstq ftslgyfdqe gvlvqsklkr fnirtningr senkrftygl
      361 nlnanysvnn epnsigsgai nrnyvlgafi svpylqptdy tnatelvaat ptlesifrst
      421 plilldrlns yqrdeeevkv lgsanfgyki tddltlrnvs gfdyqnivlt rsqgsdswns
      481 lffqnsfnag qagfafqqts rqfsfnsvts laynktfnek htldvglyte yfkahfrgfg
      541 franglnptl fspgdgagfi gdnggsdvfv dninatvlns glfsyfgsld ydydskygfs
      601 atlrrdassr fsstnrwgtf ysiagrwnvs nedfwgdnnp fdtlkirasy gtvgnqnvng
      661 ggyftgltlt edlygsvggy ggvqglaptv fgisdlkwet trqtnlgidf eavdrrlrgn
      721 idlyykdted lfqarnisga vgtggyslfg nfgtmtnkgi didlrykifq pknqgdfgle
      781 lgvvgnfnen virdlptedg qsigvgregg rlgeyfsvpy agvnpangel lhydingnlt
      841 enpnddtdrr wlnknltpef qggitlnady knfflttqwn yatgidrfdf nladvvdits
      901 vrqfnvsadl ldawtptnrv taipsldatn vlalnnsnrw lreadylrlr fvsfgyafdk
      961 svvekfhltn lrlfvnaenl vtfskwrgfd aavlsngsrt yptpriisvg veigi
//
LOCUS       WP_101015290            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olleya sp.
            Bg11-27].
ACCESSION   WP_101015290
VERSION     WP_101015290.1
KEYWORDS    RefSeq.
SOURCE      Olleya sp. Bg11-27
  ORGANISM  Olleya sp. Bg11-27
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Olleya sp. Bg11-27"
                     /db_xref="taxon:2058135"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112107
     Region          26..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkaksalf amlfmciaaf aqdgvtingt vvdaeynmpl pnvnvvvvgt sngastdfdg
       61 qyqiqvksgd vlqfsyigyt aqtvvvgdqk iidvslsvda ntleevvvvg ygtrkkshlt
      121 gaiskvvned lediavarvd dalvgqvsgv niqstdgsag saptitirga gsitgsstpl
      181 ivvdglvvds dylgsldmnd vksfevlkda astsiygsrg angiimistk dgkegktkfs
      241 yntftgfkqa khsdaytfsv aetaaaelaa tgtnsdrtky kqllgdntnw qdiifdggni
      301 tshsfaargg skktkfstal sylhdegvll tddykkyslk lkvdtqlndk fsfgvnltps
      361 vtdrrrfdgs thdilrqpsw lpvyldehsi qfvnrlrdgg vyadaqigdy aqqrmfdnyd
      421 latgtplasg gtsisntsnt npaakilerd rtdnkfkifg svygkydisd alsfkltggg
      481 diqytkrrrw qgvqasrnga aaaqldlfne krvhgsldgy faydkslgnh eisfvggmat
      541 erwkysndai sgngftsdkl qtisaatsii dfsseeyedv lfsmfarany afnnkylasv
      601 sfrrdgssif gannkfgnfp afsagwivsn esfleesdfi stlklrasyg ftgsnaldtn
      661 nnqvdfypsy slldpstavv ngnitnaynp inianedlqw erlvefnpgi dfgfannvit
      721 gsldyynrts dqlllnnpvs attgftsalv nlgkvknsgi elelrsrnvs nenfswnttl
      781 iasknenelv dfadsngqiq nvdskraaew vnlegqpiss fygwvvdsei pleylsdpyh
      841 plggqaqdvy vkdlngdgii ddddktilgn pypdlvwsls ndfkiynfdf sfmfqgshga
      901 qvrnmadqyl fnhfnsaqdf isstpnqefi kekiftnsiv qdasyvalrt inigynlprd
      961 vveklqvnkl rlyisgqnlm yftadgytgw npesidetsg ttygyqrggs pinqtvsvgl
     1021 nvef
//
LOCUS       WP_101016689            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olleya sp.
            Bg11-27].
ACCESSION   WP_101016689
VERSION     WP_101016689.1
KEYWORDS    RefSeq.
SOURCE      Olleya sp. Bg11-27
  ORGANISM  Olleya sp. Bg11-27
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Olleya sp. Bg11-27"
                     /db_xref="taxon:2058135"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116230
     Region          21..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiylcall lvstfsiaqt titgtvtsae dgqtlpyvni vtsnnsgtit dndgqysiti
       61 ldntetlsfs figyktqqia itnqttinva liedasslde vvitalgler dtkelgyvvq
      121 slsskgltev kavnfldnla gklagvtisq gatgvgsssk itirgeasfs nnnplfvvdg
      181 vpinnntvfn ftneaaagfq eidfgngamd vnaddieevs vlkgpsaaal ygtrasngvi
      241 viktkggkks kglgisints vfvdsafrlp efqnsygqgn sgqfeyvdgl gggindnity
      301 swgpqldagv ftpqfdspvv lpngtivrgg dtalyngdai tptllksnpd nlkgfyqtgv
      361 ttinniaisn gfdtgdyrls ftdlrsesii pgvnldrqtv aaklnfeptd kttistsisy
      421 tnstsdnrps ngygsenvny slvawgprsl dinslknywq pglegvqqys fnytffdnpy
      481 filyentnsf nrdrvfgnva fkhqftdafs lqlrtgmdys sekrelkrsy ssnrfkngay
      541 aehdvffrei ntdfllnynk tfgdfkvdvs aggnrldqka stkqaqtvnl aqpgifslnn
      601 aaspievfqf dskkrinsfy giaklgykdf lylditgrnd wssalatpfs vdgtsffyps
      661 asasfilsnv ttlpkavsfa klrasvaqvg ndtnayqtsg afisqtpyng qptfsnqdfi
      721 pnanlkpest tnyefgadvr flndrirfdl tyynaitkdq iislpipiss gyeqqvvngg
      781 kvkstgieii agitpiktnn fkwnttfnfa knkatiealp qadgrltlay sriydsanqt
      841 vwfqveeggq igdfygtgyl knedgqfiid sdgryiadnt lkklgnynpd ftlgwnnafs
      901 yknwtasflf dwrqggeivs rtsalgnvgg qlaeteyrpe dgivaegvta sgqpntvavs
      961 aesyyrqfyd rnheennvyd asylklrqfs igynfklkeg flgleeggdi aisligrnlf
     1021 vitenphfdp eqlavqgdgf vsgvedmsya ssrsfglkas lnf
//
LOCUS       WP_101020263            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olleya sp.
            Bg11-27].
ACCESSION   WP_101020263
VERSION     WP_101020263.1
KEYWORDS    RefSeq.
SOURCE      Olleya sp. Bg11-27
  ORGANISM  Olleya sp. Bg11-27
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Olleya sp. Bg11-27"
                     /db_xref="taxon:2058135"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116719
     Region          25..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktnlnrilt lflvmvasls yaqertisgm isdenglplp sativikgts igstsdfdgk
       61 ysiqastgqv lnfsyvgyds veksvgtsss lnvilqpgns ldevvvtalg ikrekkslgy
      121 atqevdgeav skvkssnfvn slsgkvagld ikssgtlggs tnvvirgsns isgnnqalfv
      181 vdgvpisnsn tntaaqqsgg ggydygnass dvnpddieti nvlkgaaata lygsrgmhga
      241 viittkkgkt kkgigvtiss svmlgsadke tlpqyqdkyg agygayyddp tgnffyedld
      301 gdgnpdlitp ttedasygaa fdpnllvfqw dnlypqlegy gqaspwvage ndpnyvwgts
      361 gtfvnsvgld gssdtssfrl gytnmlqegn lpnseikrns itfsgsndfs dkltattnft
      421 ytktsgkgry gtgydsnnvm qqfrqwwqtn vdlraqknay fstgenitwn tssptdlspi
      481 ysdnpywtfy enyetdsrnr yfgnvalnye indwlsfmgr faydtytelq eertnvgsan
      541 vskysrfnnq vaeynydlfl nfnrdlnekl nldgnvgfnl rrqtwesira etngglgipg
      601 lysltnsvsp iiapieysak kmvdgmfara slgydgfafi egtyrrdrss alpvdnntyg
      661 yysvsgslvf skfiktdwls fgklranyae vgddtgpyrv yntygisapf dgsgiasnps
      721 alnnlelkpq rqnsyefgle mavlnrragl dlayynttte dqivnvpgsa stgyasrwen
      781 agtienkgie vqlygtpikt ddfnwnisvn wsknenevle lrdgienlqi aslqggvsin
      841 atpgepygti rgtnyiyqdg ekvigadgyy lisdtsneii gnvnpdwkag inntitykni
      901 slnflvdiqq ggdifsldtw ygyatglydf taglndlgnp vrnpvttgnd sggvilpgvq
      961 adgtpntvra sattyrnpwg yaknpnaahv ydasyvklre lsltyklgek tlqnlpftna
     1021 slsiigrnlw iihknlpysd peaglssgnv qgyqsgayps ireigaslkl qf
//
LOCUS       WP_101020268            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olleya sp.
            Bg11-27].
ACCESSION   WP_101020268
VERSION     WP_101020268.1
KEYWORDS    RefSeq.
SOURCE      Olleya sp. Bg11-27
  ORGANISM  Olleya sp. Bg11-27
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Olleya sp. Bg11-27"
                     /db_xref="taxon:2058135"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110007
     Region          25..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lflafvvqit faqdktvsgi isddnglplp satvvvdgts tgistdfdgk
       61 yaikakvgdk lkfsyvgysn kvivvgsest invslspdna ldevvitafg skkrdeltsa
      121 vttlssddia klspttsidn mlqgvapgvq vvagngkpgq tafvrirgvg svnassaply
      181 vidgiiapdl ssvnpseiet msilkdaata slygaraang vviiktksgn knrearvtin
      241 srvgfgqkie dnfemmdaaq kiqyerelna lgvsnaaata gagittaaey nslvsrntdw
      301 qeellknsyi qsnsisvdgg tekasyffsl ahdratgiia tidgferlsg rmnvnmqakd
      361 wlnistnlsv sttssdeprd rnnvqnpfra mydynpyetk yvldadnnvv ldsngnpeyn
      421 rtsagfsvae alvnntevey ntyiiggvsa vanltdhwtn tfkmgasnta frreswlkpg
      481 sildqivgdp dnpgsktdng sneldmtitn llsynttiae khnltvtglf eynkrtfrty
      541 sltsigfand fqgvqavatl ptatstnyfe ralvsyggfl dydyegkyla taslrrdgss
      601 tfgannrygt fwsgsaawnl skenflkdnn yiddlklrvs agtsgnsngl asyasiavid
      661 fgslngqsaa ipsdngnadl gfeknfiwgi gteftafnrr lrgvvdyyer ttsdlllnan
      721 lssfggepdg sifsnigemv nkgvevelsy dlikgedvgd fnltvggnia fidnevtklv
      781 ptaaapeged iivgnsiikv geeiytynmv gyagvnpang eplffdadgn vtnvynasnt
      841 qvlsgkspla dfdgginlfm tykgfdlgad fyyksgnyie nlmensmlsd gtgvdsnqrl
      901 dafnywrnpg dtnvlpsplf gvaaqqssdr flqkgdyirl rnlsigyklp sivtnkmnik
      961 slrlyvqgqn lwtyapyfng dpevgigsge tanavgfgnf nlysyptqqs iqlglelqf
//
LOCUS       WP_101032802             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            sp. Actino-trap-3].
ACCESSION   WP_101032802
VERSION     WP_101032802.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. Actino-trap-3
  ORGANISM  Shewanella sp. Actino-trap-3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Shewanella sp. Actino-trap-3"
                     /db_xref="taxon:2058331"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53568
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresi egetrvaatp atviqlkklg fsvaieaqag vkssfdnaaf eaagadivdn
       61 vyqadfifkv napsddeiaq mkpgttlvsf iwpaqnpelv eklstnnitv mamdmvpris
      121 raqsldalss maniggyrav ieaahefgrf ftgqitaagk vppakvliig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggsfl klefenkegg ssdgyaktms eefiaaemal
      241 faeqakevdi iittalipgr papklitkdm vdtmkpgsvi vdlaaatggn ceytvkgerf
      301 itdngvkvlg ytdlpgrlpa qssqlygtnl vnlmklmcke kdgnavldfd dvvmrnmtvt
      361 rggeitfppp aisvsaapqk paastepkaa kvekapsklk yilgaigiag faavasvapa
      421 eflshftvfi lacvvgyyvv wnvshslhtp lmsvtnaisg iivvgallqi gqgsalvtal
      481 affavliasi nifggftvtq rmlkmfrkd
//
LOCUS       WP_101034231             462 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Shewanella].
ACCESSION   WP_101034231
VERSION     WP_101034231.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     gene            1..462
                     /gene="nrfA"
     Protein         1..462
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51483
     Region          1..462
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnvksialga viaasfmaag amasdktepr nevykdkfsk qydswhatee skevvdmlek
       61 vpslvvlwag ygfakdynap rghmyavtdv tnslrtgapk naqdgpmpma cwsckspdvp
      121 rvieeqgedg yfsgkwakgg peivnvlgca dchekgsskl rmsrpfaara mdtlntpfdk
      181 asrkdkqsmv caqchveyyf ektaerpgfv kfpwdmgttv eqmevyydsm efsdwthavs
      241 ktpmlkaqhp gyetwkmgvh gqnnvscvdc hmpkvtndkg rkytdhkvgn pfdrfeetca
      301 tchsqskefm vkqveeskhk aqdlkarvet qlvkahfeak aawdagatev emkpilmdir
      361 hsqwrwdyat ashgasshap aevlrilgts ldkaadarvk laqllgakgv kqpiaypdts
      421 tkakaqaalg mnmktmnaek aefkktlvpq wkeeakkrea ty
//
LOCUS       WP_101039108             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychromonas sp. MB-3u-54].
ACCESSION   WP_101039108
VERSION     WP_101039108.1
KEYWORDS    RefSeq.
SOURCE      Psychromonas sp. MB-3u-54
  ORGANISM  Psychromonas sp. MB-3u-54
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Psychromonadaceae; Psychromonas.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Psychromonas sp. MB-3u-54"
                     /db_xref="taxon:2058319"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54304
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipreiq enenrvaatp ntvellikqg ftflvetnag iaasfsdqay qnsgaeigtd
       61 kdlvwqsdii fkvnaptdpe islmkegatl vsfiwpaqnp ellekltskk isviamdsvp
      121 rtsraqalda lssmaniagy ravieaanqf grfftgqita agkvppakil iigagvagls
      181 algtagslga ivrafdtrpe vkeqvesmga eflvveyeee tevstsgyak tmsagyqkaq
      241 aammaeqakd vdiiittali pgkpapllvt kemiasmkag svivdlaaqa ggnaaltvkd
      301 evfltdngvk ivgytdlpsr lptqssqlys tnlvnlmkll ckdkdgiini dfedevirga
      361 tvvkegeisw pppainvsaa papkaeaaks apvvekkaen kwvkpiaavv aavlfgwlas
      421 vapanflahf tvfilacivg ygvvwnvahs lhtplmsvtn aisgiiiiga llqvgqgngf
      481 vttlstiail iatinivggf tvtqrmlkmf qkdk
//
LOCUS       WP_101042425            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. Bg11-29].
ACCESSION   WP_101042425
VERSION     WP_101042425.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. Bg11-29
  ORGANISM  Tenacibaculum sp. Bg11-29
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Tenacibaculum sp. Bg11-29"
                     /db_xref="taxon:2058306"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115997
     Region          21..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvtllllsf lftqiifaqe ktisgivsde sgglpgvsii ikgttsgvet dfdgnfsing
       61 kqndvlvfsf vgkktvekti gssnkinvsm vddenllnei vvtalgikre kkslgyatqe
      121 vkgddltkvn sgniansisg kvsgiqirkn nniggstnvv irgttslsgn nqalwvvdgi
      181 pldnsntntl dqtrggntgg ydfgnaasdi npddiesini lkgaaasaly gerasngvii
      241 vttkkgenqq glgvsinssv tvgvvdfdtl pvyqtqyggg yantfpstqi dlgdglhyre
      301 rtgdaswgpa ydknllvyrw nsfhpelsty gkatpwiapk nngnsiyqns itynnsislt
      361 agneqgnfrf syskqkldqg ilpnsssgrd ifnlsssykl sdkttitaga tytktvskga
      421 netgygsggn nfssslrqwt stsvdykdle naykesgknl swsingpfdr rvafhdnpyf
      481 qrdqnfslln rgrffgnfnl theiadwvsv tgkasidsyn qgqqeriavg skrqsqsagq
      541 ysrydktyke snldlvfsfn tdvtdnikfs gllggnirrs tssdtfsitl ggliapnvfa
      601 isnsvntpdp atervltfgs nsayasgtfs indtyflegt vrtdrtstlp tsnniytyps
      661 atttyifskh lkadwlsfgk vrvnyaetgg gtnpfnlapg ffklvnyggg nvrftnentr
      721 knselkpert kgyetglelk lfknrigldi syyktnttnq imsvpstgat gytnawinag
      781 nienkgiels ltgtpiknen fswettinwt rnrnktisld gsprltlgsf qrilsvaevg
      841 kpvgllvasg ydyyngvksd anrivdangd ytrvnsqiig dinpdwtggi nnklkyknli
      901 lsflvdmkkg gdvwsldqky grstgiyatt agnnelgnpm rdpvtsgsds ggvllqgvfa
      961 dgtkntvrsp ieeqygfpee qfvydasyik lrevsisysl pskfleksmf knitfsangs
     1021 nlwiihknlp yadpeagtss gnlqgfqtgv lpttkeysfn vkvqf
//
LOCUS       WP_101042687            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. Bg11-29].
ACCESSION   WP_101042687
VERSION     WP_101042687.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. Bg11-29
  ORGANISM  Tenacibaculum sp. Bg11-29
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Tenacibaculum sp. Bg11-29"
                     /db_xref="taxon:2058306"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114585
     Region          22..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkvfsfill fitinitaqk litgkviday nkepligvti vngqkktgay tdlngnfkli
       61 atskltfsyi gyktkilnlp nsnktltvtl eplaellnev eiiakknind idlrkatgai
      121 ttiksqklin kptinalqpl qgqvagltir asgelgkplk irirgtstlp iktptnsklt
      181 deqrelldnk anqplfvldg qiisadafat lnvndideik vlkdasanal ygvkasngvi
      241 eitskrging etqyafsfqq gitfkgkpnr smmateekla ferlsknkat pgyylseefi
      301 rktfsgdpni eelvvngkqk ldsiknintn wfnelarist yqsynistrg gndnskfyvs
      361 gnfsnhggkf dgneinrftg rlnyeynvsk niysmfnagf gfsesktphg snhsptnliy
      421 elnpyeqkna gklisyngyt fkelinqynk tsndnrfnfs anitaklakn lniatvigid
      481 ylvneslsii pptayseiik gttinergqa sktkvvntnl ntntrlnynl nfgkhnlsfs
      541 tnmdyykstn dfigisghgl pskllsgagi nnsltgatra ktssskiqea tlgfgfstly
      601 dwndkidvyg sykrdassll psdkrwntfw atgigytlsn esflknnswl nrlkfrtsyg
      661 itaslagisp slaiptfsyt tssylgirdf sllnlfnkyl rpeentsinf gvdlqlfnaf
      721 nltaevyhrr tkdmlltvsi ppsngftqql knvgvmdnqg leislntsli knnafhwnts
      781 atfsynrnkv vdlydgptln vtnkedgysy pdyqegqptd iiyglvslgi npadghplfq
      841 rkngnsfdgn tekpnkedfi vlgratppft ggwfhnlsyk nwqlgldiyy sfggkavhtn
      901 rskvyseedv hknlnagqln qtwftigdvn ktyptlnlht nqfgglnnla ntqnisstdf
      961 irlnnimlry nfdnkmlqki skgfiknwgi ytqvsnvytw tnfgggdpes gnlqgssqpi
     1021 ltfgtnitf
//
LOCUS       WP_101042978            1116 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. Bg11-29].
ACCESSION   WP_101042978
VERSION     WP_101042978.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. Bg11-29
  ORGANISM  Tenacibaculum sp. Bg11-29
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Tenacibaculum sp. Bg11-29"
                     /db_xref="taxon:2058306"
     Protein         1..1116
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124317
     Region          26..1115
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhkitktlil ffilafqlty gqenltitgv vsdkagplpg vtvlikgstr gtetdfdgkf
       61 sikaklndvl sfsfvgmatt ekvitsntsi nitmiedmni lnevevvatg ydkinkkaft
      121 gsavsvgfad lkidgitdis rmlegkaagv niqnisgtfg aapkitirgs ssifgnnspl
      181 yvidgvvqed ivetnldqla sgnaetliss siaginandi kkidilkdas atslygarar
      241 ngvvvittks grkespmkis ysleqtvrdi psysqydild skenlsvlke leakgalelp
      301 siaqaryggi yyimadrint ydeatgkfll entpeaknrf lqqyesantn wfkqlfrqsl
      361 tqnhslslsg ggknnafyss lsffsdpgws iaekvsrltf nvkntfylsd klnvtlssna
      421 sirkqkapgt ferqtdnftg sssrnfdinp fsyalntsrt lrprdnngnl eyyrnnwadf
      481 nileetknns idlnlrdikf qidasykfsd kitydfnaaa ryvnstrehn vkersnvvka
      541 ynsnettivr daniflyqdp nnpdaipvpv lpeggiytkn dnylttfylr nsfsyndtfn
      601 dkhnlnvllg qemryvdrer nsftgyglqf dngyvpftds rildkliseg gnyfnisqer
      661 ertvaffgka sygydskyif sltgrydgsn rqgkssssrw lptgsvsakw nvseedflan
      721 sntisnlslr ssyglvatpg satnaaaifr sqitdrllpg dresylnite lqnseltwek
      781 qyelnlgldv gfmnnrvtls advysrdifd nidfvrtsgi ggefikqgnn advkvkglel
      841 slntknivtd nftwsssfnf syydqeitkl qnrpivfdli dgtggniegy pinamfsfdf
      901 ngldsqgypt fklptnnnts ggpdfqeten itdflvyegs vdpnisagis nnfsyknwnl
      961 nvlitgaggn kirlnplysn nysdtnvfsk diknrwvlpg denftnipvi tgfdsnegdp
     1021 frsslsrlyn aynystvrva dgdfvrmkni slgytfgkdv tdklglssfn vkfqgtnlfl
     1081 lysdsrlngq dpefyntggv alpirrqytf slnigi
//
LOCUS       WP_101043534            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. Bg11-29].
ACCESSION   WP_101043534
VERSION     WP_101043534.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. Bg11-29
  ORGANISM  Tenacibaculum sp. Bg11-29
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Tenacibaculum sp. Bg11-29"
                     /db_xref="taxon:2058306"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124626
     Region          26..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkiiiyllf ltsfsvfaqk tkketkiisg tiidgprnep lpgvtvfast riignktdid
       61 nviqgsmigs ttdfdghftf ngpkeikyii isylgfetqk invesksrnl iikleekeei
      121 lgeiivtgyq kiekrkvtss faklkaddvk rsgvanidqm lsgeisgvfi qptnggpgap
      181 akiqirgtst lngssdplwv ldgiplqgnd ipkdfndkdn idnlqsyaia ginpedikdi
      241 tilkdasats iygaraangv ivittkkgke gamrinfnsn tfltlkpnfs klnlmnssek
      301 vdfelklarr sdlnyqkerg gvarilqlhn eydnfqtngf ssiapqaqke innlrdlngn
      361 wgdklyqaal nqqyglnvsg gseksryyfs lgyydeegtt kgtglnryni tfkndydvnd
      421 klnvgvsvft srnksksyit gadantnpay ysrrvnpyft plnsdgsyny dldlverssl
      481 nfkynpleer intnqelttf svkpiidlty kynnrltlyt qlgmqfdfdk tekfagkety
      541 ytrkyrynsr yldkdgnsay flpeggiiqn wnsdsfqynw kttlnynkti nsiheidaii
      601 gtefredkrt eihtkgfgfn pntlntiqit ndrvlgsalf npykksinen ayasffgtms
      661 ytydrkytif gslrydgsnl fgvnpkfryl plwsvsaswd vtkesffdfd ainefkiras
      721 ygvqgnidks tspfvtgiyn dvnilpdnte esiavisapn kdlrwektvs snigfdlglf
      781 nnkinisady yyrkstdlig lqsvplesgf nfintnwatl snrgvelain tkniitddfs
      841 wtssfnisqn knkveeiqik dndfkpslkg ygvnaifaik tagldsnglp lfwkdgkkit
      901 avdfynlteg vdgsqltree hrnlysyvgn gdpeftggft nrfqykdfnl tiatnfnlnq
      961 tikrsptyhp tqisptynyn kevlnagtgn ypsfigattp gfetdlvynw ynqydtgnty
     1021 kdldiwveki syirinnikl gynvpakyle rinlsrlsfn lsgrnlfvfg tdydgyfdpe
     1081 tlgssyaqpi pkvisfgfnl sf
//
LOCUS       WP_101044967            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. Bg11-29].
ACCESSION   WP_101044967
VERSION     WP_101044967.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. Bg11-29
  ORGANISM  Tenacibaculum sp. Bg11-29
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Tenacibaculum sp. Bg11-29"
                     /db_xref="taxon:2058306"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111446
     Region          25..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknkillcf cffllmiqvs vaqektitgv isskadglpl pgvniivkgt vkgvetdfdg
       61 kykinasskd vlmfsfvgme nssvlvgnks iinvqlsegt llkevvvtal gikkerkslt
      121 ysaqevsgde ltkvkqtnpi nslsgksagi tisrsssglg gtakvvlrgn ssttnndply
      181 vidgipmlns gngsngsepg tdifgsqtgn rdggdamsli npddiasiti lkgasasaly
      241 gsqgangvil vttkkgkegr lsvnvsssft vdnvmslpkl qseyqsasvg gaiaengnvi
      301 dakswgakks glsndaksff ntgytsinsi altsgsakmq tyfsyantla egvvpqnkli
      361 knnvtlreta kflndkidis asinlsdqri nnrptnglys naltgvylhp vgidrdtykn
      421 kfeyfnqvtn mmdqyttsfd gniqqnpywl inrspskdvv qrvlanvsak yqitenfslq
      481 srvsydksff kfdkrqyagt dpvnsgdngr yilektentq qyidlianys kafsedltft
      541 gllgtsltky aigdqillds grdgmglnfp neftianftt tnnirqsvgn revqsvfgsv
      601 nlgykemiyl dvtgradwss tlvntnstsf fypsvgltgv fsemfnmpea infaklrvsy
      661 aevgkdipvy atiplnsinl tntsvssasf apiegetlkp erqksfeigt ewrflnnrlg
      721 feltyyntkt enqiffiqaa pnpngysqni vnageisnkg ielvlngkpv rnenftwnta
      781 infaqnknev vsvhpslqdg eaiitargvn gyefsliege dfgsikarsl ernengvpvi
      841 ndsgtlkdlg fktvahaqpd falgwnntfd yknfsfgfli dgkfggdvvs vteavndkyg
      901 vsqatadarn tnggminvvn eagvgsqita qeyynaiggr dgmlgeyvyn atnvslrels
      961 igyklpikdd ffksvrlsli gnnlfffyke apfdpniaas tgiglqgvdi ysqpstrsvg
     1021 vnvninf
//
LOCUS       WP_101045469            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. Bg11-29].
ACCESSION   WP_101045469
VERSION     WP_101045469.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. Bg11-29
  ORGANISM  Tenacibaculum sp. Bg11-29
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Tenacibaculum sp. Bg11-29"
                     /db_xref="taxon:2058306"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120582
     Region          27..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mndfrlfvsi lisvfiggti laqntsisgv itdgsfplpg asvildgttt gvntdfdgkf
       61 tlkkitsekv tlkisfigyv nklvplqlnk gentnvgtii lkesaqqlee vvitalgikk
      121 eekslgysvs nlkakelnea ketnlvnaln gkiagvqitn gstgvgstsr vvirgesslt
      181 lggngplfvv dgvpihnnti fgsgentggs emqevdygng aseidpdsve sisvlkgana
      241 aalygsrgsn gvilintkta rrnkglsisi ntgttleeal rlpkyqnkyg qgwsgefeya
      301 dglnnslgkn dqedvswgpe angqlitqfd spaegglrag difsrgwvrd angkvispts
      361 ipndvtatpf tarpnnvenf yrtghtttfs taigfgsdks dflfsfglld negiipntgl
      421 krrsyrvngs idvtdklkis lksnyinsns tnrpssgygs esamymftwy grtvntealk
      481 eywqrgyegl eqynynyawh dnpyfmlnen tnafnkhrvl gnikleyqfs enlkfqaksg
      541 mdyytdrres kraystqrfl kgaykderad fkevntdflf sydknlndvw glnanfggnq
      601 mkqeinflsn ianglvipel ynlqnsvsnl vteqykeeke inslygtlgi sydnkvfvdi
      661 tarndwsstl peknnsyfyp sasvsllmne ifempaafsf fkirgslakv gndtspynlk
      721 tpysyqtpya gnktlsrsti llnenlkpem stsfevgtdl kmfngavgvd ftyykstsen
      781 qimtvpitnt vgysaqvina gkienkgiea lltlkpirne nfawtssinf sknegkvlal
      841 aentdvltmg yasvygaets kvfvqarkge rlgnmygrkf eryngkivyk dgkplvndel
      901 qllgnynpdf slgfknsfky knfdfsflvd wkqggtiisr tkqiatyagn legsenrnny
      961 edivpdgvkq vgdeyvaltd adavgwwtyy kpmydrrnqq etgivdatyv klrevkfgyd
     1021 vptsfvqklg meslkisivg rnlglwtpss nphfdpetla mqgsnivpgi edvsypssrs
     1081 ygvnflfkf
//
LOCUS       WP_101046975            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. Bg11-29].
ACCESSION   WP_101046975
VERSION     WP_101046975.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. Bg11-29
  ORGANISM  Tenacibaculum sp. Bg11-29
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Tenacibaculum sp. Bg11-29"
                     /db_xref="taxon:2058306"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113761
     Region          25..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfngilt lflalivqis faqdrtisgt vtdesgplpg vtvlkkgtts gtetdfegky
       61 siksktgdvl vfsfvgmkti qktvsnsski nlvmendnll eevvvtalgi kkeartlgyg
      121 tdvvkgkdlv varesnilns iqgkatgvqi tnsggnvggs skiiirgvss lsgrnspiwv
      181 vdgilindsq taggsrisgn rdfgngasvv npddveslti lkgaaataly gsraaagaii
      241 vttkrgkasp dgnatvsiss slrvddlfrv pdyqqeyamg tqgkfnggsv gfdwgpkisg
      301 qivdnlpvtg ltgkltavkd ngirdffrsg ytninnfsis datermdyrl sitslnqtgi
      361 vpgsefnrln fnfnagvkhs dklesrfgiq ytnaetigta psgandpnii glssfsstld
      421 qklfspwvdt ngnqinhvkg ddrvlannpl flrnenqndr eddryigyfq laykpitdls
      481 lsarvgfdle ddrrllensk ttvgrllgtf dsdnirrnvl tgdfianytt nlsddlslnl
      541 ltgiqynsrl ferqrirgtd lavpelfspg naaqtiatrd faesrligay gsaelgyknw
      601 atltltarnd wsstlpkdnn sffypsasla fvftdafdis ndiltygkfr tswaqvgndt
      661 gayqldftyn pistangqyg lnnnfpynga laysksntip panlkpesqt syefgfdlrm
      721 fknklsidfs yfnsrnedqi lniaipestg faqktanvgr vdqkgfeigl dltaistenf
      781 swntginfsk ansevielve gleritlssa fgnvqviaep gkpfqlyand yirdeetgrp
      841 iidpttgrrq agdfksfgsv lpdwtagftn risykgftln atidakwggv mksstvenlq
      901 tgglvketlv gregtvidte gilvttdpit gvvtrkdndv plrnaqdfwt slddgsvsap
      961 fifdasfvkl revslnyafp srylnngngf fktlsigveg rnlallyskv phidpesnlf
     1021 gsggaggfgi erastpstrs vglsvkmtf
//
LOCUS       WP_101046971            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            sp. Bg11-29].
ACCESSION   WP_101046971
VERSION     WP_101046971.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum sp. Bg11-29
  ORGANISM  Tenacibaculum sp. Bg11-29
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Tenacibaculum sp. Bg11-29"
                     /db_xref="taxon:2058306"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119406
     Region          25..1095
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lflalivqis faqdrtisgt vtdetgplpg vsilkkgttl gvetdfngky
       61 sikaktgdvl vfnfvgmksv ektvdtsiai nitmvsdnvl deivvtalgi srdkkslgys
      121 tqevkgealt tnksgnfvna lsgkasgiqi rknnnmggst nvvirgnasl tgsnqalfvi
      181 dgvpisnans nstsqgnavg gyydygnaas dinpediesi nilkgaaasa lygsraangv
      241 imittkkgkd sqgigvtins gmtfgkidks tfanyqtkyg agygpyysgp gshwniedvt
      301 gdgnddqvav ytedgsygaa fdpsllvyqw dsfdpespny rtatpwvnak ngpitfyesp
      361 vtitnsisld qstekgnyri nytqfdqsgl mpnssqkkhn fsmsgslkmn dkftatayan
      421 yiktsakgrn stgygdnins mfrqwwqtnv dlkqqkdsyf atgrnvtwnp ktskagsvpi
      481 fwdnpywary enyqsdsrdr fvgnvslnye indwlnvtgr iatdtyneiq eerrangsva
      541 safgvsrgnv dsgygrrnis ntetnydlmf nldkdlteki nlkaivgtni rrntfksiys
      601 stagglsvpk lyslqnsggp lplaierder igvdgiygsa sfgyndtffi datvrrdhss
      661 tlpkdnssfi ypsfagsfvf skltnfdwls fgklranyae vgnsapfdfl ydtydvnipp
      721 gtsstsvdnt kknpnlkper tksfeigldm kllknrlgfd iayyktnsvd qivrvpvsta
      781 sgylnkvlna geienkgiel sltgtpiktd nftwntnvnw sknkskvlsl edgitnlqlg
      841 sfqggvtina tvgqpygviq gtdytyldge kvvdaatgqy vksttsdkvi gdtnpdwlmg
      901 isnnfkyknf slsflidiqk ggsifsldqy yglatglyae taytndlgnp vrnplvfnqy
      961 dtdgagipsa gyvatsggfi nsgvnadgsv nttriradrf gafgyrrglp nsafvydasy
     1021 vklrevaity nftkellnnt fltggsisft gsnlwiihkn lphadpesgl sagnlqgysv
     1081 gslpttrdfg fnvklqf
//
LOCUS       WP_101047550             527 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Macromonas
            nakdongensis].
ACCESSION   WP_101047550
VERSION     WP_101047550.1
KEYWORDS    RefSeq.
SOURCE      Macromonas nakdongensis
  ORGANISM  Macromonas nakdongensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Macromonas.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Macromonas nakdongensis"
                     /db_xref="taxon:1843082"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54772
     Region          1..527
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpketf agekrvatvp dvveklvklg fsvqvesgag daahfaddty raagatvvpd
       61 ahtiwgqsdi vfkvrppaae evaqlregaa lvgfvwpaqn pnlmaqlqak qatvlaidcl
      121 prqlsraqkm daltsqagvs gyravveaan afgrffngqi taagkvppak vfiagagvag
      181 laaigtaanl gaivrandtr aevadqvksl ggefvkvdye eegsggggya kvmsegfqaa
      241 qramyaqqak ecdiiittal ipgkpapkli taemvqsmrp gsvivdmaae qggnceltvp
      301 geavvrhgvt ivgytdlasr lakqsstlys tnllrlteel cktkdgvihv nfeddairgl
      361 tvvkegeltw papqpklppa paakpaaaaa pkapahghgp gepmsaksla tvfgvgavlf
      421 wlvgsfapas flshftvfvl acfvgymvvw nvtpslhtpl msvtnaissi iaigalvqva
      481 ppldavgaan rpnslilgla lvalvltain mfggfavtrr mlamfrk
//
LOCUS       WP_101048577             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Macromonas
            nakdongensis].
ACCESSION   WP_101048577
VERSION     WP_101048577.1
KEYWORDS    RefSeq.
SOURCE      Macromonas nakdongensis
  ORGANISM  Macromonas nakdongensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Macromonas.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Macromonas nakdongensis"
                     /db_xref="taxon:1843082"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39306
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpaevm agesrvavtp etarklvgqg hevrvqsgag lrasatdsay qaagaqivda
       61 agaygselvl kvraplpaer almqpgtalv gmlnpfdadg laalaaaglt cfaleaaprt
      121 traqgldvls sqaniagyka vmvaanqygr ifpmlmtaag tlkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvggy arpmppswle
      241 rqqvevaqrv aqadivista lipgraapvl iteemvksmk pgsvivdiaa gkgpkgvggn
      301 cplteadttv qkhgvfiige tnlpalvpad ssslyarnvl dflklivppa akgepaaslq
      361 vdleddivaa clmtqggevk rks
//
LOCUS       WP_101051943             518 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Methylomonas].
ACCESSION   WP_101051943
VERSION     WP_101051943.1
KEYWORDS    RefSeq.
SOURCE      unclassified Methylomonas
  ORGANISM  unclassified Methylomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylomonas.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="unclassified Methylomonas"
                     /db_xref="taxon:2608980"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54908
     Region          1..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkevh dgekrvattp eaaekiiklg fevlvesgag dnanisdday raagvqvvat
       61 aqelwqhsdi vmkvrapefh pqlaideadl lregqqlisf iwpaqnealm qklaakkvsv
      121 lamdsvprms raqkmdalss maniagyrai veaaqhfgrf ftgqitaagk ippakvlvig
      181 agvaglaaig aakgmgaivr afdtrpevke qiesmdaefl mldfqedgsg tggyaktmsk
      241 efieaemalf aqqakevdii vttalipgkp apelitaemv asmkpgsviv dlaaeqggnc
      301 alteknqvvv khdvtiigyt nlpsrlanqs sqlyatnlrh lltdltpgkd gntvinmede
      361 virgatvike gnitwppppp klsaapkqaa aaeaaaavet kslipepikq wlpialaalv
      421 ffavgatapt sflshftvfv lacfvgyqvi wnvspslhtp lmsvtnaisg iivigalvqv
      481 sspdsiigil savailiasi niaggflvtr rmlemfrk
//
LOCUS       WP_101052496             467 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella chilikensis].
ACCESSION   WP_101052496
VERSION     WP_101052496.1
KEYWORDS    RefSeq.
SOURCE      Shewanella chilikensis
  ORGANISM  Shewanella chilikensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Shewanella chilikensis"
                     /db_xref="taxon:558541"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51840
     Region          1..466
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvkklnqksf alsalvaasl maagafasdk teprnevykd kfknqyaswh dtaksseivd
       61 vlaedpnlvi mwagygfakd ynaprghiya vtdvrntlrt gapksaedgp mpmacwscks
      121 pdvprlieeq gedgyftgkw akggpevvna igcgdchekg spklrlgrpf aerametlgt
      181 pfdkasrkdk qsmvcgqchv eyyfekvegr kgfvkfpwdq gttvesmeay ydaiefadwt
      241 halsktpmlk aqhpgyetwq lgvhgknnvt cvdchmpkvt ndkgrkftdh kvgnpfdrfe
      301 etcaqchtqs kefmenltae rkvkvnelkl kaedqivkah feaaaawkag atevemkpil
      361 tdirhaqwrw dyaiashgva ahapdealrv lgtavdkaan arvklaqlla kkgitepval
      421 pdistkakaq aalgmdmkkm vadkedfkkn vlpkwdaeak kreatyn
//
LOCUS       WP_101063034             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Moritella
            sp. Urea-trap-13].
ACCESSION   WP_101063034
VERSION     WP_101063034.1
KEYWORDS    RefSeq.
SOURCE      Moritella sp. Urea-trap-13
  ORGANISM  Moritella sp. Urea-trap-13
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Moritella sp. Urea-trap-13"
                     /db_xref="taxon:2058327"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54114
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl kgetrvaatp atveqlqklg fsvlvesnag qlssfsdatf eaagatisad
       61 tkevwaadiv lkvnapandk eikllqkgts lisfiwpaqn eelleklakr einvlamdsv
      121 prisrsqsld alssmaniag yraviesane fgrfftgqit aagkvppakv lilgagvagl
      181 aavgaagslg aivraydtrp evkeqitslg aefltvdfee sagsgdgyak vmsddykvqe
      241 qkmlaeqvad adivittali pgrpaprlvs qemvdamkag svivdlaavn ggnvepsvvd
      301 qvittaggvk vigynemarr lpaqasqlyg tnlvnllkll tpekdgemsi nfddvvqrgv
      361 tvvkdgeitw pappiqvsaa pqaakkeevk aapakpekkk tgiykailag ggiwaysala
      421 syvpaeflnh lmvfalacvi gyyliwdvas slhtplmsvt naisgivilg affqmgaesg
      481 lvtflaflgt fiatiniagg favtermlkm frk
//
LOCUS       WP_101067910             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseovarius salinarum].
ACCESSION   WP_101067910
VERSION     WP_101067910.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius salinarum
  ORGANISM  Roseovarius salinarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseovarius salinarum"
                     /db_xref="taxon:1981892"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55823
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevr egearvamtp dsaralrklg ydcaietgag vaagfsdaay eeagvevikt
       61 aaqlwkaadi vakvrqptdt evkrlkkgqt lisffnpaen eaqmqmaadk gatviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfde eqqdgsgtgg yaapsspefq
      241 akqlekfrel apdvdivitt alipgrpape lwtedmvksm krgsvivdla aerggnctlt
      301 kpdekvvtdn dvtiigytdf psrmatqsst lyatnirhmm tdltpekdgk pvhdmeddvi
      361 rgstvahgge vtypppppkv qaiaaapkke pereltpeek raqelaafke qtkrqvtllg
      421 vgavlvlavg lvapasfmqh fivfvlsvfv gfqviwgvsh slhtplmavt naissiiilg
      481 almqigsssv litilaalav fmaainifgg flvtrrmlam fqks
//
LOCUS       WP_101062145             201 aa            linear   BCT 07-JUL-2024
DEFINITION  cytochrome c nitrite reductase pentaheme subunit [Moritella sp.
            Urea-trap-13].
ACCESSION   WP_101062145
VERSION     WP_101062145.1
KEYWORDS    RefSeq.
SOURCE      Moritella sp. Urea-trap-13
  ORGANISM  Moritella sp. Urea-trap-13
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03146.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Moritella sp. Urea-trap-13"
                     /db_xref="taxon:2058327"
     gene            1..201
                     /gene="nrfB"
     Protein         1..201
                     /product="cytochrome c nitrite reductase pentaheme
                     subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=22248
     Region          44..193
                     /region_name="cyt_nit_nrfB"
                     /note="cytochrome c nitrite reductase, pentaheme subunit;
                     TIGR03146"
                     /db_xref="CDD:132190"
ORIGIN      
        1 mgnvkltirt tisfllfici ygfnfsvtae ssdrqavnas tdsrhqvtfi rdsddactqc
       61 hkdsketrqg thgektalkl grdlkcvech ntvgpnhren asqvtkysaa qsqigthktl
      121 ldfdailkat dnctechtpe rlqektwvhd vhakkatcss chvihadgek egmqalerka
      181 qiaqcvdchk dfnlnqegkg d
//
LOCUS       WP_101062143             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Moritella sp. Urea-trap-13].
ACCESSION   WP_101062143
VERSION     WP_101062143.1
KEYWORDS    RefSeq.
SOURCE      Moritella sp. Urea-trap-13
  ORGANISM  Moritella sp. Urea-trap-13
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Moritella sp. Urea-trap-13"
                     /db_xref="taxon:2058327"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53570
     Region          34..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvsvyktlkp tsgvtallat lllsmstsvf aadqvtekle prnekfqqah pdqyktwkat
       61 seskeledal qgdpnmvimw agygfskdyn karghfyaid dirntlrtgg ptnakngpmv
      121 mscwsckspd varfieenge dayfsgkwak ggaevvnaig cadchdtrsd afkngepalk
      181 ltrphveram eaigkpfaeq grldqqaqvc aqchveyyft gptkavkfpw dkgttvdqme
      241 eyydeigfkd wthavsktpm lkaqhpgyet wregihgknn vtcvdchmpk vknadgtvft
      301 dhkvgnpfdr fqdtcancht qskemlqdvv ksrkqqvtem kllaekqiia ahfeakaawd
      361 agatqaemde iqlnirhaqw rwdyaiashg vhmhapeval rilgtaldra tdartqlirl
      421 lakkgitdpi eipdistkel aqqalgmdmd kmkkekaefl ktlvpkwkae aekreaty
//
LOCUS       WP_101071155             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Rhodohalobacter barkolensis].
ACCESSION   WP_101071155
VERSION     WP_101071155.1
KEYWORDS    RefSeq.
SOURCE      Rhodohalobacter barkolensis
  ORGANISM  Rhodohalobacter barkolensis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Rhodohalobacter.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Rhodohalobacter barkolensis"
                     /db_xref="taxon:2053187"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107213
     Region          26..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknqykstlf ivlflflysg sayaqftvng tivdaesnep lfgvtvvdaq tgdgaatnin
       61 gefslnvsge sttlrvtyig yitqnvdvtr ngnsvveiei elepdisrld eivvtglasn
      121 vkrsnlgnsv atvsrkelag ttigqsldns lsgkipgvni vanggspggg snvqlrgist
      181 lgsgssqply iidgvyvdnt vistgrssvs gaggsnqdds asrisdlnpe diesievlkg
      241 psaaaiyggr anagviiitt krgqagetrv gikqdigfts alnllgfddw sedkidlvys
      301 gqraeaekai frqngnlldy eeefygetgl lsntqisasg gnertqfyvs agvqseegii
      361 kntgfdrnni rlnldhsinn nisvtsnsny irtdsdrgft gnqngtggsi gyniayvpsy
      421 fdlrpdengl ypnnpyfaen pynlrdnaen nqlvnrflqs vrldanlyss dnsflrfntq
      481 vgldylnsns iiyfpesfqs qqasstpgdv ihgkqdnfnl nmqaflvynv dvsdfnfntq
      541 vgytrlyees nrllnrgrgl apgqtnlnqa qvqsvfsqvf qevseiglva qeeinwddki
      601 iaslgvrfdk stlnaqqntf ypfpkaslav nltsfdfwnv deielfklrt aygetggkaq
      661 fgntfealgg vniggglgsv istraidpdl kpetaseief gadisafqgr vgleatyyik
      721 nvrdlildlt passtgitai atnaaelenk gvelaltasp yrssnlswit rlmywsndse
      781 itrldipsyd tgafglslgq yliregespt sivgnpqdpd ltfygdaqpd yqmswynefs
      841 flgnfefsfl fqyqkggdni nltnflldgg gntpdwsndd dgdgtpngld rgpfnpsqfv
      901 edasyiklre vglyytlpge vvsnffnaqr mrfgvsgqnl llfsdyssyd pevsnfgaqp
      961 vsqsvevtpy psarrvffhi nldf
//
LOCUS       WP_101073038            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Rhodohalobacter barkolensis].
ACCESSION   WP_101073038
VERSION     WP_101073038.1
KEYWORDS    RefSeq.
SOURCE      Rhodohalobacter barkolensis
  ORGANISM  Rhodohalobacter barkolensis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Rhodohalobacter.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Rhodohalobacter barkolensis"
                     /db_xref="taxon:2053187"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114216
     Region          30..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkvlrfkll sllgifflls asqafaqgsv sgtvtdaetg eeligvnvvl pslnigdatg
       61 sdgtylltdv pegeyriear yvgfetvrrt itvedgqeti vnfemsaavd elgevivtaf
      121 gveresrsig ysiqdvsaed igragsdnll galqgqvsgv qinqggggag qgmqifirgf
      181 nsldptadnq plfvvdgvpi dnstteasig vrgmsnramd lspndiesis vlksapatal
      241 ygvraangav iittkkgeag diqvdfahsi sredvinqpd yqdvygpgfg fssapdgfwp
      301 awgapysetp eltyynnwen smrtgiginn svsvsggten vtfytsisns nnrgilpnnd
      361 wdrtsirvsg elfqgpltva asanyinsgg srvpfinfma rlaywntsad vtdwrhedgt
      421 mksdsrdgrg sgrnpiydae intyeddvnr lignlrtsye fadwlsleym lgidtysder
      481 tdiepgprgl enefvwsnvg gyrqegriss tdlssnlaan inldltqdig mslrvgndif
      541 drssntvrar gerfsasefn hfsnaanisi yqrlsqrrli glygdlnldw ndvlylnvtg
      601 rndwtstlpk dersffypsv nlgyvfsdmi elpnwmtygk frasyaevgk dappystqdv
      661 yvapsifpld sqigftkgat inssdlkper ttsselgfdl rflnnrlgfd ftwykanskd
      721 miipvpvsna tgssqfitna geienrgiel svratpvetr dfqwninsnf trnrnevvai
      781 rdgvdaiflg qisayinnpf mqlipgesyg aiwgthyary gadpesntid tslpiiigdd
      841 gfpvvesdpk ivgdatpdwt anlfnqfnyk swdfsfnidi vygvdkynkl dnwdaafght
      901 tktlnredyv vfdgvledgs pntqevwlgq gvdpetgrny gagyhrntyr vaveesteda
      961 syvklrsval gytlpqsvle nipftnirag vnannillwt pfsqydpeaf vssgsnlvgl
     1021 vdlaypgtrs ltfslnfsf
//
LOCUS       WP_101073571            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Rhodohalobacter barkolensis].
ACCESSION   WP_101073571
VERSION     WP_101073571.1
KEYWORDS    RefSeq.
SOURCE      Rhodohalobacter barkolensis
  ORGANISM  Rhodohalobacter barkolensis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Rhodohalobacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Rhodohalobacter barkolensis"
                     /db_xref="taxon:2053187"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115117
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkylllpil viqlsiqlgf aqsgtiqgnv tdisgeplpg vnviidledr tigastnldg
       61 yyeitnvpvg fvevrtryig yqpvtrevdv ndgeitvvnf elsqatvgld elvvtgtgge
      121 vskrslghtv ssvdfegeef aasssiqdal qgkiagvnvn lqsgmvdqep kirirgtssi
      181 smsnqpviyv dgvrvqglgg fapgvgaggl gapsalsnin fdaverveil kgpaaatlyg
      241 sqansgviqi ftkqgatesa prfnaeyttr fiqmpdrfkr ntgfaetade qqrvrdvlgl
      301 dvdfyepfes pfqlidlyst gigqefsagv qgggegmtyf anlsyshtdg pfnpqsstfn
      361 ggavggaddv ykklyfngnl nfiptdelrf rvqtsytnsn tsvygtgiti ytptstarys
      421 kpervglnsq fdtfgavfat vregtypeis dnanqgrlvl qtdyfitegl svdatfgvdy
      481 rdqrstdysp fgyavdgvap skdgtisign rqqliwsyeg kinwnfdfnq nlknsfvagf
      541 qgyseetnst sstgnnfsgp glsvlgatas qssnsafqev tnlgifaqdq ieykdwmywt
      601 vgvrldassa fgdefnyaty pklslsflpf eafntsvsni stfrlraaig qsgqqpgafd
      661 rfktftpvss pegsginpgn lgnddlkpet atewevgfdl glfderfsie atywdrvvkd
      721 alidrsysps ggfttpqltn vgelegrgve isadynviek snfslnifan taylyeqvts
      781 lggtpsikvd agyirdrmfi kegyspgsyf gtklpegidf pfdlsgngtp snqaeleaff
      841 snpvdpstln ayimvagpng ealpggssyl dhylgkptpd wegsfgfstr flngfslstr
      901 fqyatgnyyh hnltdafrrt nagigrnfme stelesilkn patttaerie agkrwvnemv
      961 alspfdglne veqadyirws nlsvsyslpv tfveefglts atitatgnnl alwtkyggvd
     1021 platgegstg ndgglyenfg ggmdtygtpl lrtfsmtlka sf
//
LOCUS       WP_101073894             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodohalobacter barkolensis].
ACCESSION   WP_101073894
VERSION     WP_101073894.1
KEYWORDS    RefSeq.
SOURCE      Rhodohalobacter barkolensis
  ORGANISM  Rhodohalobacter barkolensis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Rhodohalobacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rhodohalobacter barkolensis"
                     /db_xref="taxon:2053187"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40397
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mivgvckete alekrvaltp egteklskmg ltiyiesesg lassysdqqy idsgaeikkr
       61 nqilsetdll lavqaplaed lekmkknsal iaflwplqhk kyvdfllnad ltgmamdtip
      121 risraqsmda lssmsniagy kaallganhl drylpmmmta agtippakvl vlgagvaglq
      181 aiatakrlga vveafdirpa vkeqveslga kfvevpleee setkggyake lsdqnkekqr
      241 evihkhvaks divittalip gkpapqlitr qmvedmsags viidiaaeqg gncevtepgk
      301 tirhnevivd gplnlpssla hhasklyskn ilslldllik dgqpnfnfdd eiianatvth
      361 ngelispfvk enmk
//
LOCUS       WP_101074105            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Rhodohalobacter barkolensis].
ACCESSION   WP_101074105
VERSION     WP_101074105.1
KEYWORDS    RefSeq.
SOURCE      Rhodohalobacter barkolensis
  ORGANISM  Rhodohalobacter barkolensis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Rhodohalobacter.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Rhodohalobacter barkolensis"
                     /db_xref="taxon:2053187"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121422
     Region          25..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkklllssl mvlvsvsfaf aqsstvtgti tdantdepip qvnvfivelq tgdatdmdgq
       61 ysianvehgt ynvrissvgy ttlereitvd annttfdfqm npdvrllddv vvtafgvsre
      121 qrslgysvqd vnaeklarvq qdnivgalag kvagvqvvgs tsfggserir irganglsdg
      181 qplfvvdgtp ianqsfvtnq ggsttgrdlg nlasdlnlqn vesvsvlkga aaaalygnra
      241 adgvilittk nasmgenipl qvefnhnttf edvyilpeyq neyaggytqn fiqytdprdg
      301 qtynglnyaa deswgpkmdg tmyrpwwswf dhdftgdgqn dygtevplvp qennvrdffe
      361 tglrmsnsls itggssnasf ragltntsns givpnsqldr tslsfngals hsdkftsria
      421 fnyvntateg rpatgysavq gnsvqsfnqw fqrqldmdkl rqyrtddgtl mswnirsntd
      481 trplywdspf fsinenkqnd drdriygnyq lsynvnenie lqgklhldty sfnvedriat
      541 ggleqdwfyt aqrsrrevny eaglryqedf qdvsvsgyfg gniltqnyss lqqqtqggls
      601 vpnffnidas idrpgvsnyn eqkevrslfg tttigyqdlv yldltgrndw ssalpadnns
      661 ffyygvsgsl vftefdmfan qdilsfgklr asiaqvgndl dpfrvfqtfn sgtpfgslpt
      721 qsvpntlfnp dlepaissdy efgidlrfld grlrtdvnyy nsvreneile ldvsgasgye
      781 stlvnagkft ttgweialga tpvqtsdwsv evdvnwstsk svvdeltegi errllenasf
      841 giqlfavege ewgeaittga yggyllddeg rrivnsngty aleynkplgn ilpdwnggfn
      901 lgvnykdfsi gafidfqkgg kfysisrmfg tysgltantv gnnalgnpmr dplvdsngnt
      961 tyingdgdev aytslpldqt santggvlie gvdtdgneva ylrnaanwgi dqfynkeawl
     1021 edasyiklre lrftynlpvs lldrtpisra avsldlrnpl liysstsgvd ptaiqnnang
     1081 fgfweggglp gtrsigfnvn lnf
//
LOCUS       WP_101074112            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Rhodohalobacter barkolensis].
ACCESSION   WP_101074112
VERSION     WP_101074112.1
KEYWORDS    RefSeq.
SOURCE      Rhodohalobacter barkolensis
  ORGANISM  Rhodohalobacter barkolensis
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Rhodohalobacter.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Rhodohalobacter barkolensis"
                     /db_xref="taxon:2053187"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112236
     Region          31..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miqkilqslt sllllvaisg faglahaqtg tltgtvtdes tgetlvgatv mivdlergap
       61 tdiegmymid niptgtyevr fsyvgyttvt etieisegen vydlemsmds agldevvvtg
      121 ygnfsdrnft gsvsqvsses fenapvssin ealsgniagv nispstgtpg avqqarirgi
      181 ssinassapl yvidgvpvqs gsnaqstats sldvlssisa ndiesvtvlk dasstalyga
      241 rgsngvivie tksgssgdvq yslsmqrgvn nravdgpgtl nanewdqlfy dsagnylesl
      301 gapsdrasvd allfpsgwdg etstdwgdvv rndnaiqqey qlaaqggndr ttfytsasff
      361 eqegqaigsg lerlsgklnl thqfderltf snnfsgsfve qdgilegagy fgspvlaeyf
      421 mlptdnayne dgspnlglss nifnpvyvqd tdidrkrnir vinntnldfe itdnlafssn
      481 lsldylltee kyydnpfygd gedvrgavdd intrnfnyvw rnslnyiyqa neqnlfdfrf
      541 isesqknknn fleaygegia aanlynlntt aspqfvgsst tdwavqsfig lvnyryddkv
      601 ivdgsvrheg ntrfgednrw gtfwslgvgy ilteedffad iegldflrvr tsygqtgnas
      661 iglnnyqtlv gfggyndqpn iqptqfgnpn ltwekansfd vsvdfeafem leggvnffrk
      721 dsydllfnvp lsrvsghnsq vqnvgelynq gfefelsadi vrtqdfgwnl ggnltlvene
      781 itelprdqng dpieitsatr ytavegyevn awymrewagv dpdngdplwy mddgeggrtt
      841 tnsynqadty yqganaqptt yggintrvdv knfyvqanms falgykvfdn wanymrsdgn
      901 ggfnaafgqy gtaadyweep gdiadnprpv lfstnqanaa ssrflydgdh irlkslnigy
      961 niptqlieqv glssatlffn grnlwtyafd ddlkwdpeqk adgftdlnaq pmrsltfglk
     1021 anf
//
LOCUS       WP_101082419             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychromonas sp. Urea-02u-13].
ACCESSION   WP_101082419
VERSION     WP_101082419.1
KEYWORDS    RefSeq.
SOURCE      Psychromonas sp. Urea-02u-13
  ORGANISM  Psychromonas sp. Urea-02u-13
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Psychromonadaceae; Psychromonas.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Psychromonas sp. Urea-02u-13"
                     /db_xref="taxon:2058326"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53788
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipreiq dnenrvaatp ntvellikqg feflvennag aaasfsdqay tdagavigtd
       61 tvaiwqsdii fkvnaptdae ielikegatl vsfiwpaqnp ellkkleakn vsviamdsvp
      121 rtsraqalda lssmaniagy ravieaanqf grfftgqita agkvppakvl ivgagvagla
      181 algaagslga ivrafdtrpe vkeqiesmga eflevnyvee tevsttgyak tmsagyqqaq
      241 admmaeqakd vdiiittali pgkpapkiit eamiasmksg svivdlaaaa ggnaaltvkd
      301 evfttdngvk iigytdlpsr lptqssqlys tnlvnlmkll cknkdgqidi dfedevirga
      361 tvvkegeisw papainvsaa papkaeekva vveekapnkw ikpvsalvav glfgwlasva
      421 padflahftv fmlacvvgyg vvwnvahslh tplmsvtnai sgiiiigall qvgsdstvvt
      481 vlstiailia tinivggftv thrmlkmfqk d
//
LOCUS       WP_101086077             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            sp. ALD9].
ACCESSION   WP_101086077
VERSION     WP_101086077.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. ALD9
  ORGANISM  Shewanella sp. ALD9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Shewanella sp. ALD9"
                     /db_xref="taxon:2058330"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53456
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresi egetrvaatp atvvqliklg fsvaieaqag vkssfdnaaf eaagadvvdn
       61 vydadfifkv napsddeiak mkpgttlvsf iwpaqnpelv eklsshnitv mamdmvpris
      121 raqsldalss maniggyrav ieaahefgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggsfl klefenkegg ssdgyakvms eefiaaemal
      241 faeqakdvdi iittalipgr papklitkdm vdtmkpgsvi vdlaaatggn ceytvtgerf
      301 itengvkvlg ytdlpgrlpa qssqlygtnl vnlmklmcka kdgnavldfd dvvmrnmtvt
      361 rggeitfppp aisvsaapqk paasiepkaa kvdkvpsklk yilavlglag faavasvapa
      421 eflshftvfi lscvvgyyvv wnvshslhtp lmsvtnaisg iivvgallqi gqgsalvtal
      481 afvavliasi nifggftvtq rmlkmfrkd
//
LOCUS       WP_101091446             467 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [unclassified Shewanella].
ACCESSION   WP_101091446
VERSION     WP_101091446.1
KEYWORDS    RefSeq.
SOURCE      unclassified Shewanella
  ORGANISM  unclassified Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="unclassified Shewanella"
                     /db_xref="taxon:196818"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52193
     Region          1..467
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvrtltkkaf alsamvaasl iagsafasdk teprnevykd kfknqyetwh etseskevvd
       61 mleqvpslvv lwagygfakd ynaprghmyv itdlrntlrt gapksaedgp mpmacwscks
      121 pdvprmieeq gedgyfagkw skggpeivna lgcadchvkg ssklrmsrpf aerametlgt
      181 pfdkaskkdk qsmvcgqchv eyyfektkdk kgfvkfpwdn gttveqmevy ydniefsdwt
      241 havsktpmlk aqhpgyetwq lgvhgknnvs ctdchmpkvk sekgrkftdh kvgnpfdrfe
      301 etcgscheqs kefmvnlted rkhkvadlka raeaqlvkah feakaawdag atetemkpil
      361 mdirhsqwrw dyatashgva ahaadealrv lgtavdkaad ariklaqlla vkgvkqpiay
      421 pdtstkakaq aalgmdmkkm nadkaefkkt lvpqweaeae kreatyk
//
LOCUS       WP_101092421             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_101092421
VERSION     WP_101092421.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53762
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafs rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_101091760             395 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Shewanella].
ACCESSION   WP_101091760
VERSION     WP_101091760.1
KEYWORDS    RefSeq.
SOURCE      unclassified Shewanella
  ORGANISM  unclassified Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="unclassified Shewanella"
                     /db_xref="taxon:196818"
     Protein         1..395
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41636
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgipkesh agesrvalip anvarllkkn vqvlvesdag shagftdedy vaagatiapr
       61 eqvlsdsdvi tvvnakdeql aelkatikpn qivigmmdpl ahpenaqaia etgataiale
      121 lvpritraqs mdilssmati sgykavllaa hkaprifpmm mtaagtlkpa rafimgvgva
      181 glqacatakr lgavveaydi rpaareqiis vgakpveldl etentetkgg yaaeqtddfl
      241 krqqqamanv laqqdivitt aaipgrkapi litkemvdgm kngtiivdla aetggncelt
      301 evdkevvykg vtilgpsnvp gsaanhasqm ygtnienllk llvdkegvlt ldfedeivrd
      361 tvvahqgeva sarlrdilgl palepvitaa tpeek
//
LOCUS       WP_101093136             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_101093136
VERSION     WP_101093136.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53613
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_101097308             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_101097308
VERSION     WP_101097308.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53905
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsedel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_101109509             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychromonas sp. psych-6C06].
ACCESSION   WP_101109509
VERSION     WP_101109509.1
KEYWORDS    RefSeq.
SOURCE      Psychromonas sp. psych-6C06
  ORGANISM  Psychromonas sp. psych-6C06
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Psychromonadaceae; Psychromonas.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Psychromonas sp. psych-6C06"
                     /db_xref="taxon:2058089"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54361
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipreiq enenrvaatp ktvellrkqg ftflvetnag anasfsdqlf seagaeisae
       61 tnavlasdii fkvnaptese iaqfkegatl vsfiwpaqnp ellkkleakn isviamdsvp
      121 rtsraqalda lssmaniagy raviesanqf grfftgqita agkvppakvl iigagvagla
      181 algaagslga ivrafdtrpe vkeqvesmga eflvvdyqde eevssdgyak tmsegyqqaq
      241 aammaeqakd vdiiittali pgkpapklis eemiksmkag svivdlaaqa ggnaaltvkd
      301 eiftsengvk iigytdlpsr lptqssqlya tnlvnlmkll cknkdgqidi dfedevirga
      361 tvvkegeisw pppainvsaa paakaeeake avvveekapn kwikpvaaiv gaglfgwlat
      421 vaptdflahf tvfmlacivg ygvvwnvahs lhtplmsvtn aisgiiivga llqvgsdnvv
      481 vtvlstiail iatinivggf tvthrmlkmf qkdk
//
LOCUS       WP_101115060             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio sp.
            vnigr-6D03].
ACCESSION   WP_101115060
VERSION     WP_101115060.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. vnigr-6D03
  ORGANISM  Vibrio sp. vnigr-6D03
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Vibrio sp. vnigr-6D03"
                     /db_xref="taxon:2058088"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54468
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpketl agerrvaatp ktveqllklg fdvsvesqag vlasfddaaf esagatvvsr
       61 dnvwksdlil kvnapqvdpe sgvdefdlik egaslisfiw paqnealmdk lsskninvma
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv qsmgaeflev dfqensgsgd gyakemsdef
      241 nkkaeelyaa qakdvdiiit talipgrpap klitkamvds mkagsvivdl aaanggncey
      301 tvadevittp ngvkivgytd mvgrlptqss qlygtnlvnl lkllckekdg nidinfedvv
      361 lrgvtvvkeg eitwpappiq vsaqpevkpk aqpveatkee epasplkkva alaigvgafa
      421 wvasvapasf lahftvfvla cvvgyyvvwn vshslhtplm svtnaisgii vvgallqigq
      481 gsgvvtflsf iavliasini fggftvtkrm lemfrkd
//
LOCUS       WP_101116469             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_101116469
VERSION     WP_101116469.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53834
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_101127015             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_101127015
VERSION     WP_101127015.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53758
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_101131405             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_101131405
VERSION     WP_101131405.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53949
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwvcpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_101132477             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_101132477
VERSION     WP_101132477.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53892
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsddgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_101137070            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ALD4].
ACCESSION   WP_101137070
VERSION     WP_101137070.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ALD4
  ORGANISM  Flavobacterium sp. ALD4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Flavobacterium sp. ALD4"
                     /db_xref="taxon:2058314"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113318
     Region          27..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngilv llvvlmaqlt faqeravtgv vsdnagmpip gvsvlvkgtk fgtqtdfdgk
       61 faikaapsqi lifsyigmls qevkatstlv nvkmkssave legvvvtafg ikrkpkqlgy
      121 svssvktedi tessepdlvr slqgkvagvn vnvstgaaga anqitirgis tfsgdiqpli
      181 ivdgiaynnt qvttsnqvtg gggyesalss ldpndiasvn vlksaaaaal ygsravngvi
      241 vittksgsls tkqnkklsvn fgsgvfleqi anlpdyqnty gagvnfnyan angswgprfd
      301 sretiptwpt llaafptqfg ptvpyvakpn nvkdlfrtgs iaentiglsy anqdgsfnvt
      361 isdlgqngyi psntydrtsf saggtfklan kltaganmsy adtkqvgaff genqfggsss
      421 sfartlflar nwdlnlpyed ltdgrsvtpn gtqfdhplws wkhdqittnt trtvvglnls
      481 yafndninvf yragvnkysl eraeirdlys rasgglgslv tdnfsnqdie stllvnfkyk
      541 ltddiglaai vgnnilqnsn krtqnegtgf kvanifnlgn vltvvnnads gsekrsvgvf
      601 advtfdykef lyinatgrnd wssslpkesn syfypsvsas fiitealnmn snilsfakir
      661 ggygkvgrda ssefinqtfn lgvaynntat ignstsladp nikpefteev evgadleffk
      721 rrvivdvsly kktstdlitp itvpttsgfa qyntnlgsie nkgvelaltl vpfrtkdfkw
      781 slqtnytkne nkvtklidgl erfplranav gyvevgqayg ffygtkfard angnflidka
      841 ggviqdptpg yignpqadfr mafintftyk gfslkaqfdw keggdisstt intllgrgvt
      901 kdtenrentf iipgfygntt tgtalldasg aqipnttqls mnelyfspsn sntfginsvd
      961 easvydatvy rlsnvsltyd fpakfidktp fgsvslsaig nnlwyfapnv pkytnfdpdv
     1021 tslgsgtsqg ieiasaptsk rfgiklnltf
//
LOCUS       WP_101137067            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ALD4].
ACCESSION   WP_101137067
VERSION     WP_101137067.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ALD4
  ORGANISM  Flavobacterium sp. ALD4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Flavobacterium sp. ALD4"
                     /db_xref="taxon:2058314"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111580
     Region          27..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngilv llvvlmaqlt faqeravtgv vsdntgmpip gvsvlikgtn sgtqtdfdgk
       61 faikatpsqt liftyigmkt qslaatsavm nvkmmgsave legvivtalg ikksknsvts
      121 atqavnneel tqaanpnvvq slvgkvsglq inkssngvng tsrivlrgsr sitgnnealv
      181 vidnaisssa vlqqlppeli asvnvikgmq gaalygeqgv ngviivttvk gkekgkitvn
      241 vnsavdfesv sfmpktqqky gqgwdgvhyp eengswgipy dgvlratglp qadglelqqp
      301 ysfikdnvkd fyqtgityqn gfsvnagtsd syvllsankv ktefvvngdq lernsflfka
      361 gkkfgklsid gnvnynyqks sqtstdlldd liqtpgnvdl nlfknsgneg nyniyfknpf
      421 wtidndrtda rrtfintias lkyelndhin ftytgnlqft nrdqqshinq ysetpaltga
      481 ganrnqtsef fanqsslrty ygdflvnfdy dltddlnlka nvgsnmqdrr fnitsqggqn
      541 ldipgwyhin nvlspsnpsn ldnrlqksnr asvlanvdlg ykdylflnlt grndwtsvls
      601 kennnffyps agvsfiptla feglksntln ylklsanivk vgnsssiqpy atseigvfpt
      661 gfpygqlgsy iinqrptdkn irpefvttke gnisiglfnn ritidgsayi sntkdlitaa
      721 tassasglat sqsnigdmtt kgieidlglv pvktesfkwd lrtsyssnks vinslsagan
      781 einlfsdatt gtgifaqvgq efplikgtkf lrddngsiiv nqfglptras snsilgkatp
      841 dyilglsnsf eykglrltvv mdyrtghqii sgtkydltwp grleesaafd revgfilpns
      901 vvetapssgi ytpntsiysa agydpngiid yystlsrage hnvidatafk vrelalsysv
      961 pnstidkigl tslrfgvnar npftvlaksn kgytdpeass stanngngig ysgtgqypnt
     1021 rtfggsinlt f
//
LOCUS       WP_101137072            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. ALD4].
ACCESSION   WP_101137072
VERSION     WP_101137072.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. ALD4
  ORGANISM  Flavobacterium sp. ALD4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Flavobacterium sp. ALD4"
                     /db_xref="taxon:2058314"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117201
     Region          25..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngilv llvvlmaqlt faqervvtgv vsdnagmpip gvsvlvkgtk lgtntdfdgk
       61 yaikaspsqi ltfsyigmkt qsmaassstv nitmtgdafe legvvvtalg ikrekkslgy
      121 atqevsgdev snvkssnfvn slsgkvagld iktsgnlggs tqvvirgnns isgnnqalfv
      181 vdgipidngn snsqdqktgr ggfdygnaas dinpddiasi nvlkgaaata lygsrasngv
      241 vmivtkkggk qkgigvtins sitlgtadks tlpkyqnkyg agygpyydgp ggyfglydvn
      301 gdgvddlttv ftedasygaa fdpslmvyqw nsiypqlpdt yqkatpwiag kntpnsvwgt
      361 gstavnsvsl dggtdkssfr lgftnllqeg nlpnssikrn tisfsgshdl sdkltvstyf
      421 nfvkndgkgr ngtgyssgni mqqfrqwnqm nvdfneqkda yfltgdnitw npnspdnlsp
      481 iysdnpywtf yenyetdtrt rlfgnvaidn kindwlsasv rfsfdtysel qeerknvgsa
      541 dvseysrynn nvaeynydam lnfnkdltdk lnlegnigvn lrnnvrnsif avtngglnik
      601 slyslsnsvs pinapseyds ssmvdgeyir aslgydgfay legsyrtdrs stlpqennrf
      661 gyysvsgslv fsslidapwl sfgkvranya evgsatdpyr vfntlsfgtp fngtavasnp
      721 ttlanlnllp erqnsyeigl emsflkrrig fdlsyynnqn inqitnipls tstgygsavl
      781 nagtienkgv evqlnatpfk tadfqwdlnl nwsqnkslvv ellngidnlq laslqggisi
      841 natpgqpygt irgsdyiyad ngqpivnqtg sasrigtypr tsssnnvigd inadwkagln
      901 nsityknfnl sflldmqkgg dvfsldtwyg yatgmydfsa adnelgnpvr npitgtpgny
      961 gadsggvimp gvapdgtpnq vranadiyan awgyarapnk ahvydagyik lrqasltynf
     1021 ddkvlsrlpf nnvsvsligr nlwiidksvp yadpeaglss gnvqgyqsga qpsireigas
     1081 lklqf
//
LOCUS       WP_101146441             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            sp. MES3-P3E].
ACCESSION   WP_101146441
VERSION     WP_101146441.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. MES3-P3E
  ORGANISM  Halomonas sp. MES3-P3E
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas sp. MES3-P3E"
                     /db_xref="taxon:2058321"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55510
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkesa rgearvaltp esakqiqklg heclvetgag laagfnddty rdagvtvveg
       61 adalwrdaev vikvrepsde eaerlregqt liaffwpaqn eallekckaq gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfed sqdgsesggy aspsspefre
      241 kqlecfreqa advdivitta lipgkpapkl wledmvaamk pgsviidlaa ekggncdltk
      301 pdervvsdng vvvigytdfp srmatqssll yatnirhmlt dltpekegvi nhnmdddvir
      361 gatvthqgdi tfpppppkvk aigaskpkkk ekeptpeekk aaelatfkaq tkrqvgllav
      421 ggalmlllgq vapasfmqhf ivfvlacfig fqviwkvshs lhtplmavtn aisgiiilga
      481 ilqigsgsav vsvlaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_101149518             311 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Aeromonas hydrophila].
ACCESSION   WP_101149518
VERSION     WP_101149518.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas hydrophila
  ORGANISM  Aeromonas hydrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Aeromonas hydrophila"
                     /db_xref="taxon:644"
     Protein         1..311
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35938
     Region          5..173
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiheiyskr qmrlrgefnd vyqydfipdk lriqicklyn sffdcnhqem nqlynsvydi
       61 ltmeygvdsl nyfsddiefr spknsntqil fsfakrdant dcfldvlelv mqhirnaqnr
      121 ghriimsvsd atneingrfr enavgyqldp dsltiirvds qfvhsevvkp altllniepa
      181 yvgvldefms ahehyrhkny kdailhcgks fesmlkaihe krgwaydkhk dtanklilsc
      241 vdkglfpsfq qdqlmqvrki lecgvptirn ktaghgqghe vtevpehlvs ymihltasnl
      301 lflakadeyl a
//
LOCUS       WP_101159616             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Choline-02u-1].
ACCESSION   WP_101159616
VERSION     WP_101159616.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Choline-02u-1
  ORGANISM  Pseudomonas sp. Choline-02u-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. Choline-02u-1"
                     /db_xref="taxon:2058307"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38802
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq igetrvaatp etikklisqg hkvtvqsgag vkasvvdsay eaagasigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaqtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_101153793             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Colwellia
            sp. Bg11-28].
ACCESSION   WP_101153793
VERSION     WP_101153793.1
KEYWORDS    RefSeq.
SOURCE      Colwellia sp. Bg11-28
  ORGANISM  Colwellia sp. Bg11-28
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Colwellia sp. Bg11-28"
                     /db_xref="taxon:2058305"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54023
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesf lgerrvaaap ssvsaliklg ftvqvqkgag tkasftdqef sdanaaivsk
       61 kacwqseilf kvnaptleev elmndgstll sfiapaqsse llealrsksi ttlamemvpr
      121 mtrsqpmdal ssmaniagyr avieashhfg rfftgqitaa gkmppakvmi igagvaglaa
      181 lgtagslgai vrafdtrpev keqiesmgae fleldyeepe dtgsgdgyak emskafidae
      241 malfaeqakd vdiiittami pgrpapklit ekmvesmkag svivdlaaag ggncectvpg
      301 kvvdtygvkv igytdlvsrl pnqasqlyan nlmnltkllc knkdgtldid fddvvirnmt
      361 vvkedeitfp pppiqvsaap vkkatveaae pieevaspik kyafigagia lfgwvasiap
      421 adflthftvf vlacvigyyv vwnvshslht plmsvtnais giiivgallq igsdnivvqi
      481 latlatlvat inivggfkvt srmlkmfsk
//
LOCUS       WP_101163340             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudoalteromonas sp. 78C3].
ACCESSION   WP_101163340
VERSION     WP_101163340.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. 78C3
  ORGANISM  Pseudoalteromonas sp. 78C3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Pseudoalteromonas sp. 78C3"
                     /db_xref="taxon:2058300"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53725
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkeih tgerrvattp dvvskltklg fdvvietgag maanyadday geagckivns
       61 aqdvwaqsdi vlkvqapegd entllksgqt licflwpaqn pemlkdltqr gitaiaidsi
      121 prisraqkmd arssmanisg yraiveaaqh fgrfftgqit aagrvapakv lvigagvagl
      181 aaigaaksmg aivrsfdtra evkeqiesmd aeflmldfkd edgsgeggya kvmsdefiea
      241 emalfaaqak dvdiivttal ipgkpapkli tsemvasmks gsvivdlaae qggnceltvp
      301 gkvavchgvs iigytdlpsr laaqssqlys nnlhnllaem tpekdgklfv dmtndvvlga
      361 tictegkitw pppaptlsap pkkvaatpkp tivekkksvf gpiigaaiga lallglggva
      421 padfmshftv fvlacfvgym viwsvspalh tplmsvtnai ssiivigali qisspddtik
      481 wfavftvlia sinivggfav thrmlkmfrk
//
LOCUS       WP_101203391            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olleya sp.
            1-3].
ACCESSION   WP_101203391
VERSION     WP_101203391.1
KEYWORDS    RefSeq.
SOURCE      Olleya sp. 1-3
  ORGANISM  Olleya sp. 1-3
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Olleya sp. 1-3"
                     /db_xref="taxon:2058323"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116044
     Region          25..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktnlnrilt lflvmvasls yaqertisgt itdenglplp sativvkgts ngstsdfdgn
       61 ysiqasngqv lnfsyvgyds vektigasst isvslqpgnt ldevvvtalg ikrekkslgy
      121 atqevagdev skvkssnfvn slsgkvagld vkssgtlggs tnvvirgnas iagnnqalfv
      181 idgipvdngn snsadqvsgr ggydygnaas dinpddiati nvlkgaaata lygsrasngv
      241 vmittkkgkk rkgigvtlns sytvgsadte tlpvyqkkyg agygqfyddp sgffgytdid
      301 gdgnpdlttp ftedasygaa fdpnldvyqw nsiypqltdt yqqatpwvag andpnsvwks
      361 gatsvnsvsl dggndtssfr lgftnmlqeg nlpnseikrn tinfsashdl nekltasttf
      421 tytktngkgr ygtgydannv mqqfrqwfqt nvdvgaleda yfatgdnitw nptsatnlsp
      481 iysdnpywtf yenyetdqrn ryfgnfaldy eindwlsvlg rftfdtysef qeertnvgss
      541 nvssysrynn nvaeynydfi ltanknitek lniegnlgfn lrrndrssiy aqtngglnlp
      601 glyalsnsvn ainapaeyea vskvdglyar aslgydgfay legtyrrdrs stlpiennty
      661 gyfsvasslv fskfidadwl sfgklsanya evgsdtnnyn vfntygigtp fsgtgiasnp
      721 gsknnlelkp erqenyefgl dtqffnrrlg lnvsyyhttn rdqitsvpvs natgytsvll
      781 nagtmenkgl evqlsatpik tenfswdvnv nwaknkslvi sladgidnlq laspqggisi
      841 natpgqpygt irgtdlvynd agqpivqang yyersgsnei igdinpewta glnnsfnykn
      901 fnlsflidmq kggdvfsldt wygyatglyd itagtnelgn pvrnpvttga dsggvilpgv
      961 qadgsvntvr asasnyanpw gyaraansqh iydagfiklr easitykfdd kilsqvpfta
     1021 asisligrnl wiidkstpya dpeaglssgn iqgyqsgsyp sireigaslk lqf
//
LOCUS       WP_101203389            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Olleya].
ACCESSION   WP_101203389
VERSION     WP_101203389.1
KEYWORDS    RefSeq.
SOURCE      Olleya
  ORGANISM  Olleya
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Olleya"
                     /db_xref="taxon:336276"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110424
     Region          25..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lflafvvqit faqdktvsgv vsdengiplt satvlvigts ngtstdfdgn
       61 ysiktkvgdk lqfsyvgygn kevtvggant inmtlapdna ldevvitgfg skkrdqltsa
      121 vttlsaddit klspstsidn mlqgvapgvq vvagngkpgq tafvrirgvg sinassaply
      181 vidgviapdl nsvnpgdiet msilkdaats slygsraang vviiktktgn rnrdarvsis
      241 srvgygqria dnfemmnaaq kiqyerelsa lgignaaalp gaqvstqeey dfliardtdw
      301 edellrnsyi qnnsisidgg tekssyfvsf ahdrntgiiq sisgferlsg rlnlnvqakd
      361 wlqvstnvsv tgttsdeprd rnnvqnpfra mydynpyetk flldddnnqv ldgagnpifn
      421 ptragfpise alinnpeqdn tlfiiggita vanlsdkwtn tfkvgatnts yrresfikpg
      481 svldgfvgda dnpgiktdng sneldltvtn llnysttigd khnvsltglf efnkrtfrny
      541 slssagfsnd fqsvqavatl ptaastnlft rsllgyggfl dydydgkyla tasvrrdgss
      601 tfgidnrygv fwsgslawnl skenfladsd ivddlklras agtsgnsngl asyasvatld
      661 fgslngasta iptdngnsdl gfeknyiwgv gvefagfdrr irgvidyyer ttsdlllnap
      721 lsslggepdg sifsnigemt nkglelelsa diiraedfgd ftltvggnia fldnevtklv
      781 ssstdpngad illttngdnn iirvgeeiyt yylvryagvn pangeplfyd idgnitnqyn
      841 addavalegk spiakfdgga nlnmtykgfd ftadlyykvg nyvqnylegn mlsngtgvds
      901 nqrvdafnyw knpgdtnvlp splfgneagn tsdrllqkgd yvrlrnltig ytlpskftet
      961 lnisslrlfl qgqnlwtyap hfngdpevgi gsgetdtsvn fgnynlysyp qtqslqmgve
     1021 lkf
//
LOCUS       WP_101204098            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Olleya sp.
            1-3].
ACCESSION   WP_101204098
VERSION     WP_101204098.1
KEYWORDS    RefSeq.
SOURCE      Olleya sp. 1-3
  ORGANISM  Olleya sp. 1-3
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Olleya sp. 1-3"
                     /db_xref="taxon:2058323"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116495
     Region          21..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiylcall lvstfsiaqt titgtvtsae dgqtlpyvni vtsnnsgtit dnegqysitv
       61 ldhmetlsfs figyktqqia itnqttinva lmedasslde vvitalgler dtkelgyvvq
      121 slsskgltev kavnfldnla gklagvtisq gatgvgsssk itirgeasfs nnnplfvvdg
      181 vpinnntvfn ftneaaagfq eidfgngamd vnaddieevs vlkgpsaaal ygtrasngvi
      241 viktkggkks kglgisints ifvdsafrlp efqnsygqgn sgqfeyvdgl gggindnity
      301 swgpqldagv ftpqfdspvv lpngtivrgg dtalyngdai tptllksnpd nlkdfyqtgv
      361 ttinniaisn gfdtgdyrls ftdlrsesii pgvnldrqtv aaklnfeptd kttistsisy
      421 tnstsdnrps ngygsenvny slvawgprsl dinslknywq pglegvqqys fnytffdnpy
      481 filyentnsf nrdrvfgnva fkhqftdafs lqlrtgmdys sekrelkrsy ssnrfkngay
      541 aehdvffrei ntdfllnynk tfgdfkvdvs aggnrldqka stkqaqtvnl aqpgifslnn
      601 aaspievfqf dskkrinsfy giaklgykdf lylditgrnd wssalatpfs vdgtsffyps
      661 asasfilsnv ttlpkavsfa klrasvaqvg ndtnayqtsg afisqtpyng qptfsnqdfi
      721 pnanlkpest tnyefgadvr flndrirfdf tyynaitkdq iislpipiss gyeqqvvngg
      781 kvkstgveii agitpiktnn fkwnttfnfa knkatieelp qadgrltlay sriydsanqt
      841 vwfqveeggq igdfygtgyl knedgqfiid sdgryiadnt lkklgnynpd ftlgwnndfs
      901 yknwtasflf dwrqggeivs rtsalgnvgg qlaeteyrpe dgivaegvta sgqpntvavs
      961 aesyyrqfyd rnheennvyd asylklrqfs igynfklkeg flgleeggdi aisligrnlf
     1021 vitenphfdp eqlavqgdgf vsgvedmsya ssrsfglkas lnf
//
LOCUS       WP_101204837             383 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Psychrobacter].
ACCESSION   WP_101204837
VERSION     WP_101204837.1
KEYWORDS    RefSeq.
SOURCE      unclassified Psychrobacter
  ORGANISM  unclassified Psychrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="unclassified Psychrobacter"
                     /db_xref="taxon:196806"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39883
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvisadi tsesrvaitp davkklrklg fevviqsgag qaayyadely qaagadiass
       61 rtevitqski ittvndlpae ateslssgqi vigmldpyrn tqldtyaakg atvfamellp
      121 rtlsraqnmd vlssqanlag ykavllaane ysrpfpmfmt sagtvkpakv vilgvgvagl
      181 qaiatakrlg avveasdlrp tareqveslg gkwldvpmsa eeaetakstg gyawtpseqy
      241 vkdqaavvdk alsnadiiit taqipgrnap rlvhgatlak mkagsvlidm aagtggnveg
      301 svpnetittd ngvrivgaan ipsmlaaqss dlyannlvnf ittliaptgd dasaslalnl
      361 dmedeiqgal avthdsqvrl akr
//
LOCUS       WP_101208947             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. 43NM1].
ACCESSION   WP_101208947
VERSION     WP_101208947.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. 43NM1
  ORGANISM  Pseudomonas sp. 43NM1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. 43NM1"
                     /db_xref="taxon:1904755"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38637
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag vrasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vfnkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_101211782             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Psychrobacter sp.
            Sarcosine-3u-12].
ACCESSION   WP_101211782
VERSION     WP_101211782.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp. Sarcosine-3u-12
  ORGANISM  Psychrobacter sp. Sarcosine-3u-12
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Psychrobacter sp. Sarcosine-3u-12"
                     /db_xref="taxon:2058325"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36055
     Region          5..173
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mavhdlyfkr qkqlrgeyte vyqydqiprt lknqivfiwk evvgvdtwya rtqeegqksr
       61 fykqiysill kelglekfst ekhyqdpffr riegffkeve dveielsive lvfsnaiklr
      121 rlsatespsn lnfikelnqr frengvgyqy endqiirvds efihaeavkp alqllsnpmy
      181 kgaqeeflka hehyrhgryd saltdclkaf estmkiiihk rswvcdknaa skklidccla
      241 nelipkfwtd qfnslsnilt ssigtprnkl sghgkgnddi evpehliqyv lhmtasiivf
      301 likaeeslk
//
LOCUS       WP_101212979             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychrobium sp. 1_MG-2023].
ACCESSION   WP_101212979
VERSION     WP_101212979.1
KEYWORDS    RefSeq.
SOURCE      Psychrobium sp. 1_MG-2023
  ORGANISM  Psychrobium sp. 1_MG-2023
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Psychrobium.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Psychrobium sp. 1_MG-2023"
                     /db_xref="taxon:3062624"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54509
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mfigvpkenl lgetrvaatp qtvsqlkklg fdviiesgag kaasfndqaf idagatiged
       61 aaqvfasdvv lkvnapttge dnttdevall kdqatlisfi wpaqndtlme klssrninvm
      121 amdcvprmsr sqsldalssm aniggyravi eaanqfgrff tgqitaagkv ppakvlviga
      181 gvaglaaiga agslgaivra fdtrpevkeq insmgaefle ldfeeesgsg dgyaktmske
      241 fieaemalfa eqakdvdiii ttalipgkpa pklitkemvd smkpgsvivd laaanggnce
      301 ycqtgelfvt endvkvlgyt dlpgrlpvqa sqlygtnlvn llkllapekd gevtidfede
      361 vvrgvtvvks geitwpappi kvsvtpvkea andipaepek qempkevklg lfaaglagfg
      421 aiasyappef lahftvfvla cvigyyvvwn vshslhtplm svtnaisgii vvgallqvgt
      481 dsvlvtilal iatliatini vggfyvtqrm lkmfrk
//
LOCUS       WP_101217846             514 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudoalteromonas].
ACCESSION   WP_101217846
VERSION     WP_101217846.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54211
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkeih tgerrvattp dvvskltklg fdvvietgag maanyadday geagckivns
       61 aqdvwaqsdi vlkvqapegd entllksgqt licflwpaqn pemlkdltqr gitaiaidsi
      121 prisraqkmd arssmanisg yraiveaaqh fgrfftgqit aagrvapakv lvigagvagl
      181 aaigaaksmg aivrsfdtra evkeqiesmd aeflmldfkd edgsgeggya kvmsdefiea
      241 emalfaaqak dvdiivttal ipgkpapkli tsemvasmks gsvivdlaae qggnceltvp
      301 gkvavchgvs iigytdlpsr laaqssqlys nnlynllaem tpekdgklfv dmtndvvlga
      361 tictegkttw pppaptlsat akkvaatpkp kpkptivekk ksvfghiiga aigalallgl
      421 ggvapadfms hftvfvlacf vgymviwsvs palhtplmsv tnaissiivi galiqisstd
      481 dtikwfavft vliasinivg gfavthrmlk mfrk
//
LOCUS       WP_101220812             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas fluorescens].
ACCESSION   WP_101220812
VERSION     WP_101220812.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38704
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel allksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 anqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_101238511             974 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101238511
VERSION     WP_101238511.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 974)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 974)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 974)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..974
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..974
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106998
     Region          39..972
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlta gvlfftgqav faqkkpsdtl khkeaketki devvvlgysk vstkakdvta
       61 sttvtaekfe nrpttsflns lqgeapglti nstsgqpgsg kidviirgvg slsagseply
      121 vidgiisnat qyrnlndsdi esasilkdaa atsiygnraa ngvivintkr gkynspmrfs
      181 yngftgvsfl pktdynmsnt qqiltlekra gaglgatltd aqinnyavnt dwrkvffnag
      241 ftqkhdvamt vggqnvnlys slgyfdqtgi vsnvsdfkrf tfrnnlngks engkftygaq
      301 valsfskrhq ldeetnanis nnsiqnplhg anaglpylqs giyqngwqvy daigtnfdgg
      361 kniysledvl rkgsmpnert etgivaninl aykltnyltl nhksgvdyky qetnfarapw
      421 nylaiataag ganatvnpnp fggiedfskt refnynaits lnfnktfgdk htinggvyld
      481 ylkviyngts qrrtglnpin wvfgagtgyv dpvyyanpsg gspivyyvps asaskikaga
      541 layfatvdyd ydskygvsal irrdgsyrfv senkwatfws iagrwnidke sfmqgsifdm
      601 lklrasygeq gnqniiavta gnnpmlvgtn lvrdtyvagt gynniagalg vgvfanpdvr
      661 werlaqtnig ldfrllnrrl egnidvydkt tkdlyndinl saitgttsik gnngklqnrg
      721 vevllrynii qnqntklsiy gntaynknki lslvkddiag strnvvggpv dqwflapylg
      781 vnpangqaly edingnptet innttdarat gknmypvwsg gfglnfeykg vfvdahftyq
      841 akvwkydnam qwlydpssig twnqsadmln awsptnvtgd ipslkatnlq llgysdrflk
      901 dasfvrlknv sigyslpksv lqntfvkgmk vflqaenlit wtkwrgydpe pnftyslsvy
      961 pnmktvslga nief
//
LOCUS       WP_101239129             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101239129
VERSION     WP_101239129.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111125
     Region          35..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrketqkllv lsllglisvn ltaqqkakkd tikgldevvv talgikrhdk slgyatqtvk
       61 sdeilqtqnn nwaaalegkv aglkiqtaga gplgtsritl rgdismnmgn ndalivvdgv
      121 plsgkktgtg taaygagsgg dlpidygdsf nsinpddies vtilkgptas alygsrgsrg
      181 aimittksgk srkgkiqvtl nsytsydtvl kwpdyqyeyg qgtqqrdkng nyyysygasa
      241 dgvntgstss afgpkfdgqy yfqydptveg qslerklwqp yknnikdfwq vgsnysnsls
      301 ieqsnettaf rtslsylkne wmmpntgfnr lngalsfdhk lssklkigak vnfsqtksdn
      361 lpatgynnqs isyfmifqnp nvdlawyrpi wksgqdqvdq ihpfssyidn pyliayenln
      421 svnkklltgn inisyqlskh fdiayktgle wnnefrtqrr pwssanypkg yyreqyiryf
      481 dlnndillty knkfgnfgvt gsaggniryh eytmndyrai glnraglyql snatsldnrl
      541 pspndnqvns vyalanfsyk dmifldvtar ndwsstlpsr nrsyfypsla ssfvlsdifk
      601 lksdnfnfwk lrlswskvgn dtynymleky yensvftgsv espllypdpn lrpemitnie
      661 ggmdftflkn rltfnftayq nnskdqsiii pvlyetgynr riinagelrn rgieltlnay
      721 piknkdfsws vnanwsmnrn kilslpeefq gqpytmgsvg gvayynavvg gslgdmygyg
      781 lmyspdgqvi ygsdgltgkp ndmkkignvy pkwraglqne fryknitisf sfdgqykgma
      841 yshshhkmse qgklthtlvg rdnpgglivg egvvqnpdgs fstntkgipv styygdyyrr
      901 anietnsfdt sfiklrdari afsfpksvie plkvreltla lfgrnlwmwt kfpmfdpeva
      961 tldnstitpg vemgqlptsr tvgiqlnvkf
//
LOCUS       WP_101239373            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101239373
VERSION     WP_101239373.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110860
     Region          32..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltasvli valsssffvv naqnrggdti ktknieeivv tgalglkkka daitnaqqvv
       61 gtkelnqass pnavqaltgk vsglqitqtd ngvgatsriv irgnksisgd nqalividnv
      121 issasilsqi ppdmienvnv ikglqgaaly gqqgvngvii vttkrgtkse kiqftltnsv
      181 emtqafmfpk vqtqygkgvp geavdpngdp dfngtsyvpw entswgpayn dpriggmmmp
      241 sglpqdnnqf iyeryspikn hfakffkngl ilqngltvts ggsdsyatls vnrvennfvv
      301 dkdkltqnsf lfkagkkfdn lridgtvnyi skiidetssd lyndiiqmpt mndirkykns
      361 gidgflsaft knpyyqieht rrktindyls gilslqydfn khinltytgn vflnnvrqds
      421 hddgfkatrv yantgtvldg gtiqdysqna dftsyyinrt vstrsyygdi mlnfnydltd
      481 dinlklnign niqdsyitsr amggsgliap gwydirnvkn liqpgdrnga nvldnlgfen
      541 tttrrrivag fanldlsykd ylflnstlrv eqssvlstyf ngelhnkpyp yysvglsfip
      601 tkafeglkng ivnhikiaps ftkvgntsgi lpydtsnvgi apsgypfngl lgygintnpt
      661 nrtiqpefmy ttdlnvqlgf fndritlegs iyqsdtqnli tnaslsnttg maklkdnfgk
      721 trmrgfeidl gatpfksqnf twnlragfas srskvlelpe gldevaiavp yqsfgigvfa
      781 vrgedftvlk atsferddqg riivdkagvp lidskfknmg ritpdytltf ntniryknft
      841 lsgtmdfrkg gkfaamgknv lqfagltedt agfdrsqgyv vpnsvqlvng qyvanntpvn
      901 gtadyngvvn yftsqamqkl getmvldata fkvreiglsy dlpksvlast fvnsltvgif
      961 arnpffvyak enrnyadpet ayssgngagi aitgqypsqr sfgvnlkvsf
//
LOCUS       WP_101238583             965 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101238583
VERSION     WP_101238583.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 965)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 965)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 965)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         <1..965
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          12..964
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 aadttkttdi qevvvtslgi krqarsltys sqqiggdelt evktpnllns ingkvsnvqi
       61 nrtngvgssv rvimrgnksv snsqplyvid gipiinqtgk sanisqyanm pdpgdvlssi
      121 npddiesinf lkgasasaly gsaggngail ittrkgkigk ssisystslt vdrayslpkl
      181 qhsylsydps mpnqnpgdni eswgakgask dylkdflqtg ttwvnslsfq sgnekstnyf
      241 signttnkgi vpmsyfdqyn isfrnsskfl ddkltldanf igsiqdsknr qtpgasfspl
      301 tslywlprgv dfdqysgdqy sfinkkrllp aqnwweikpd gtfkgnpetq npywilnrna
      361 vtvknknays aitlsyeinp wltarvrgny swsnsdsqrd isafsapsll aggengrilk
      421 nvyensstyg dvlligspkl sesisldfti ggsvnsvnnk vteidnayla ypnlftlnnl
      481 qwnvdrspgd gyhniywnvk kqvrsvfasa svgyknmfyv dmtfrndwds tlsltgrsgf
      541 dyesvgvnai lssvfklpea infwkvrgsy asvglglsan tsnaiveyyk aysygvdagt
      601 iiypkssfvt dqnykdlfpk pelnktfeag telrmfknkl sfdityynsn atnqlletti
      661 ssnlggiptg syfinagkir ntgfesslsy kifdnekfgw tasinasank nkivelfpps
      721 lsipqdqlfs ltgggeftkm klggsfgdly gvkfqrddqg rilvdqngvp lgttgvpgyl
      781 gnpnpkfilg fgntfnigkl gvsflidgkf ggqvlsltek andlygvsqr tadardaggv
      841 tisnavyapg tplagqayng vtdakayykr tggaggigtg ideaymysat tvrlrqaais
      901 ytfdinakym rnatvslvgt nlfffykkap fdpeqvsgnt pggvgvdsfg lpitrsigls
      961 lkanf
//
LOCUS       WP_101239375            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101239375
VERSION     WP_101239375.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110427
     Region          32..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttsllv laltssvama naqekkndtv ktkeiegvvv talgikrekr slgyatqevk
       61 gdavnknptt nflnnlsgkv agleikqstn fggsinvvtr gyksllgdnq alfvvdgipi
      121 lnkninttsq ntggggydyg ssisdinpnd ietvnvlkga aatalygsra qngviiittk
      181 rgkknkegig mefstsltms fvdkstfpky qtqygqgyrg tsfagtlggs pvvdfgndas
      241 ygspydgspv wqygaftpgs ptegkrtpwq iakngpvkff dvgatnvnsl afsggddrat
      301 yrlsytntna sdimpnssli knnfsgnasy kltdkltanf yanyvtqktk grnttgyndn
      361 imtnfrqwwa tnvdikdldy lyrtykknyt wningsddls pafwdnpyfq ryenyqndsr
      421 drfagnfsln ydiskefnll frmgtdgytm iteerkavgs yvgnsfglni vpqpsgyals
      481 nykfnetnyd liatykkdit ddlnisalvg gninvqkafs nqqstsggly tpgiytians
      541 ksnparplis diskyvygaf aqlslgyknt yylegtfrrd qstalpsnha vywypslsas
      601 vvfsnlikas wlnfgkvraa yaevgsdtaa dqllnryfaq psygdipvya ynavlrnfdl
      661 ksqglknlev gieakmfnnr lgfdvswfqn kaydqilalp vsyatgssak tqnagelttk
      721 gfeiavnvtp iktsnfswdl nlnwsnpwtk vtalspgien isigrlqgga svnaplngdy
      781 gtlwtsdfvy dsngqkivgp ngaylvtdka iygqgsfqar wsaglsnmit yknlslsfli
      841 dwrqggkifs ldqaygygtg iypesvglnd lgnpirntla ngggiiqpgv madpnnpghy
      901 ipntirldrs qssqvlqtdl pqsayiydas fvklrevait ykfdknifns kfiqgmsvsl
      961 ignnlwiihk nlpysdpeag lsagniqgyq sgplpstrni slnvkinf
//
LOCUS       WP_101239377            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101239377
VERSION     WP_101239377.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109746
     Region          31..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttgllv lvlsssfaia naqvkkdtvk tkeiegvvvt algikrekks lgyasqeika
       61 galsdgttnt gniaaqlsgk vaglsvttnn nfggssnlli rgmktlgggn plividgspv
      121 nnantqekni dygnalsdin qediesinvl kgaaasalyg erglngvivi ttkngkgkdd
      181 gswgvtfssa iqvgfidkst fpeyqtryga gysqkfgtqa anglnnanfn adaswgpkfd
      241 pnllvyqwds ydpsspnygk atpwvaakng pikffnnpas yinsvtlekg qkgknisfty
      301 dnmmsdglip nshlnknnfs lkvnydltpk lhstfystmt lqdtkgrsit gysnnpmtgf
      361 rqwwqtnvdl kdleqaylan inpsvasaan nygnvtwnrk saangaaayw nnpyfqayqn
      421 ytsdkrfrnf tyaqvtydll dnisvtgkvs ydrsnlmaen rlavgslpqa fgqsnntigs
      481 gyarrdilrt etnydlmvny kfditdnini sgvvggnirr nyfnstyast egglivpgiy
      541 alsnsrkspl atdetewttq tnsgyvtasl dfykkfylda twrvdqsstl yignnvynyp
      601 svtgavimse ilntkswmnf wkiranyaev ggtadpyqlm nnyraagiln gvgiynsilt
      661 epflnlqpqr akefevgtev hflrdritld fayyktktin qifstasplp tsaaigytgk
      721 vfnagridns gvevqlglvp ikskdftwnv dvnwsknknq vvslypgitn llvnsfqggv
      781 slnaregeaw gtligsdyty vngqkvidpn tgkylqnpnq vignttpdwi ggirnsfsyk
      841 gfslsflidm rkggdvfstd myyglssgly ketaigdyrd kpivlagvlp dgtpnniqls
      901 pfdnngamgy ktqpsrefvy dgsfiklrea sigymlpksl lagtkiydak isivgrnlwi
      961 ihknlpyadp eamvggglns ygwsigampt trdlginvtf kf
//
LOCUS       WP_101239379            1013 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101239379
VERSION     WP_101239379.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..1013
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111507
     Region          14..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklktsllv lvltssiavt naqqkkdtmk tkeiegvvvt algikrekks lgyasqevks
       61 selfggttnt gniasqlsgk vaglnvtsts nfggssnlvi rgikslggsn plvvidgspv
      121 nnsttsfgne nggfdlgnal sdinqedies vnvlkgaaas alygerglng vivittkngk
      181 gkqddswgvt lsssvqagfi dkstfakyqd rygagydpsf yygtgpggkk nanfgedasw
      241 gpefnpnllv yqwdsfdpts pnykkatpwv aakngplkff etpmsfinsi slskgskgfn
      301 fnltydnnls ngllpnsdlr kntistkiny dlnsklhatv ystltiqgtt grtetgyndn
      361 ivtgfrqwwq tnvdlvalkn ayinnvgnpt vdnnygnvtw nrisasngrp afwnnpyfqr
      421 yqnystddrt rtfsyvqlty dvddhinitg klsydntnlv ferrlaegsy pqrfgvsgka
      481 igsgyhrydl krseinydlf anykydltsw lnisgivggn vrrnrqssie astegglikr
      541 gyysldnska pllnpvefea tvqtnslyat asfdfnkvfy ldgtirrdvt stlpngnnky
      601 tygsisgsvi lsellktqks vmnfwkvrgn yaevggtads yqlkysyyta gyfntgngni
      661 niyrpqtilk nenlkpqrsr efefgtevhf lrdriifdga yydtktfdql itpdisagsg
      721 klaaainagq innkgvelhl gvnpirttdf swdidvnwar nrnkvvslee glqvyqlvgl
      781 vggasivasv gnqwgdiygk dyvylngekv vdpttgyylt eknkvignvq akwtggirns
      841 fryknlslsf lidvrkggdv fssdmyyglg sglfpetavd gyrtnipile gvnpngqrnt
      901 tpvnaaainp leygnnpydg yaivpdkrfv ydgsfvklre asitysfpks vlantfmnea
      961 kvsiigrnlw iihknlpyad pessqmggly sygssvgalp ttrelgvnft fkf
//
LOCUS       WP_101239750             948 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101239750
VERSION     WP_101239750.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..948
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106211
     Region          15..946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklsvlsa galffigqta waqkvkkdtv lqenkidevv vtgyqkkakd eiaqaqstit
       61 adelktqtpt tsvgnmlqgr asgvfvqsrn gqpgstaein irgisgfsgn seplyvvdgi
      121 ymtarqfnav ngndvenmvv lkdaaataqy gsrgangvvv vttkkgrngr tqysfenrlg
      181 fsqkisdkel nfemmnsaqk lqyeremral glsglpnyta nqeqellkld hnwqkdilrt
      241 sflqsylfsa rggseknkfy yslgydkdng ivrdingldr ytgrfnfenn lsdklkvgld
      301 lgiayqytqn vrdrnnaqsp fgsmyrynpf esvynpdgsy nynlrqgfni iealrnnldy
      361 eqrlrltgnv fgeykinknl syrmyfntly dnlvntnnlk rgsqldvivn gaaglgtlrk
      421 ttfysfnyiy gnridfkkqf edhfisatgv vefnseften iaasgtnykn pnsdapsnti
      481 psdkntftgd kvkstlfsll glfeynykkk ylitgsirqd ksskfgannk sgifwsgsla
      541 wniakeefln ggffnelklr gsygtvgndr sipnfanvgy vsygdygtga tmtpttiagn
      601 pdikwetnkt tdlgidfafl nnrfrgaiev yradrndfiq llplpyesgn ysvyrnlgdm
      661 rnegleteft fdvirkknlk lslrgnstwq rskitsldgv stqrnlgets lkvgetpyfy
      721 rlveyagvnp adgkalyytd ratpdagenf ytingrtatd vynatadikd ltnkspipkf
      781 fggfgftlea ygfdlsadfs fktgaytyny qtkilqsass rtnnmstdaf nywknpgdtn
      841 vlpkptavgl rdsdqfleks dylrfrtlmv gytfskqtlg esipvnsirv yvqgqnlltw
      901 tsfkgdpeva vgsgenqlgv sqtyvsgsya lfsypavrqf mfgvqvef
//
LOCUS       WP_101239752             948 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101239752
VERSION     WP_101239752.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..948
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104424
     Region          34..946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlta gvlfftgqav faqekdskkd ketkieevvv lgysktatka ktttssvtvg
       61 aetlenrpni svlnsiqgta pgivvnsasg spgsgkfnil irgasslngs tdplyvvdgv
      121 itsgsqfrnl nsydietfsi lkdaqataiy gnraangvvv ittkggkfns glkvsydals
      181 sfsklpnady nmangqqlll lqknlqtglg atlsndqinn wgvntdwnkq ftrvgisqqh
      241 nlsitgggen innffslgyl dsegtvrstd fkrftmrnnl ngkskdgkls fgaivglgys
      301 krnqlddetn sgianntlqn plfggilsrp yigpspyang qelfnaiktd atnnrqwvlq
      361 dninggirnr ftelsisana nvnykitdyl svgnrtgiey kqyerifars plgylsisva
      421 nsdgsryggn edftttrdlt fnsitnitfn ksfgdhtita aaymdyikah vsstfqrqng
      481 lnplqwefga gtgyipfnpd tpniyrpsns askvtagtla yfatvdydyk dkygvsgvvr
      541 rdgsyrflpt nrwetfwsva grwnidkedf mansgfrllk lrasigttgn qnlgivtdna
      601 nplallpnnf ldlysgfsgy qnmlgynfvn lsnpyleweq vkqsnigldf nfkgliegsv
      661 dyyqkrtsrm fndlqrsavt gyysirgndg ildnkgiegl ikynvirnqn tklsifanaa
      721 ynsnkivsmn senlagdvvn aiggpagqyq lytyvgvnrd ngnlqfldkn gnvteaptsa
      781 drvltgksry akftggfgfn fqhkgwfldt lfsfqqggwi ydnlqswimd psaaanrnls
      841 adllnawtpd nrdtdvpalk annlslgssd rflhrsdfir lknitlgynf skdqlgklpv
      901 rgikvfvqae nlytwtdwkg fdpepitsys lnvypnpktv svglnvdf
//
LOCUS       WP_101239767            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101239767
VERSION     WP_101239767.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124371
     Region          22..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlillpl laaqvalaqe kktitgkied gntssviaga sikietqsvs tktdldgiie
       61 svsvgtvadk dgkfileipv gtksilvsyp gyesriilin edktnytvrl apevsdknki
      121 qeviitgyqk iekrkqtsav stvkmdninq agvasvdqml sgqiagvvvt petgspggpa
      181 kirirgtasl sgpqdplwvi dglplegndv pnfsdkdnid qlqnfsiagl npndiediti
      241 lkdaaataiy garaangvis ittkkgkkgn mrinfsadtf vtarpdfdkl nlmnasekvd
      301 lelmlakrsd ltyradrgev mriltqnnql ndfrsgglda ltpftrnqin alrnnstdwg
      361 kllyrnainr qygvsvsggg esadyyfslg yfdeqgttig tgfkrynltl knnyklsdkl
      421 tagisvfgta sekesfmtda daaaspvnys rnanpylspy nadgsyrydk didgfkdvyv
      481 pfnfleeren tdytlknhsl kaildleykv skslkftsql giqydtnkte kyaaentyft
      541 rkfregtryy kdgqyryylp vggikqnwdn dffqynwklq gtystkinsv heidlmagte
      601 irktddnttl trafgynast ktgtpivfps sndaaekkye tyremprven ayasmfatas
      661 ytydqkytff gsvrydgtnl fgvnkkyryl piwavsgswl vtkenfmqni tpvsnlrlra
      721 syglqgnidr ntspffigey nyanilpgmr edvinvispp ndklrwektt nvnfgldlgl
      781 fknrinltad vysrkgtdmi smretplesg feytmanwgs ltnkgfelai strninkenf
      841 kwsttinfah nksnvvseqp rdnarlptre glpvnavfal ktagidengn pmfwkgnekv
      901 kiedlfglyd pyadflpgyf aqsklsneem rnlftyvgdr dpkftggiin tfkihdfdlt
      961 vsatfnfkqt vmktpsykgm eldrgrnytr diyeagtslp gitspemdsn pgwmgnkwlt
     1021 dnnyniynll diwakeisyv rissirlgyt lpkqftspmg isslrlsveg rnlfvfsngy
     1081 kgyfdpetyg niyaqpitrs vtlgfnvsf
//
LOCUS       WP_101248522             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Telmatospirillum siberiense].
ACCESSION   WP_101248522
VERSION     WP_101248522.1
KEYWORDS    RefSeq.
SOURCE      Telmatospirillum siberiense
  ORGANISM  Telmatospirillum siberiense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Telmatospirillum.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Telmatospirillum siberiense"
                     /db_xref="taxon:382514"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39808
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipkerr anearvaasp dtikkfvgmg fdvvvetgag egasladdsf vaagasiaad
       61 eaaalkdadi vlkiqrplta eegldelalf kkgavlighl aalqnkpqae ayakagvtaf
      121 alellprisr aqnmdilssq snlagyksvl daaaeygraf pmmmtaagtv pparilvlga
      181 gvaglqaiat akrmgavvya fdvrpavkeq veslggkfve vdasaardae tkggyakemd
      241 edykrkqadk iaetlkktdi aistalipgk papiliteem vkgmrkgsvi vdlaveaggn
      301 cplseygkvv vkhgvilvgh anvparlaad tsllfaknll nflslsydke skgltinwdd
      361 eiikgtaltr dgqvvhpala g
//
LOCUS       WP_101239939             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101239939
VERSION     WP_101239939.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109363
     Region          32..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkqcklgv lalllfaeyg faqskdslsk enaikevvvv afgkqkkeei tgsvqslkak
       61 dlsnlqngnv lqgiggkvag vqvissgqpg sqptirmrgi gsinassdpl ivldgipysg
      121 nlnsiagsdi esisfledas snalygsrga ngviivntkr gknkklsvdv dvktgvnfrs
      181 iedysvytsp qdyytafynr arigevarlk qpgavpsgpt phdvgltaln rlgynvysvp
      241 fsqlirqdgs fnpeaqllyq dnwkkllfkp alrreanvgi nasgdqvksy tslnylddkg
      301 ylissgferf girsnldyti tpklklttal sytyskqdfg etggfsnpfq farnispfyp
      361 vflrddnyqr lydshgnaly dygdgqgpng atrsyavfen pvgnlqkdks qttsnianan
      421 lglnyeiikg ldftynfgay lenirtlqfg nteggtsssv ggtitrgsqf rytlnhqqll
      481 tyqkkfdqhn fniligheln tiknegisgt kqqlllpdsw sfdnavkitd lsgsgyeyav
      541 egyfsrllyn ydgkyffnan irrdgssvfs pesrwgnfyg lgaawniake dflkdntvin
      601 alklkasygq qgndnillnn strdyyayqd iyginnfgdg kpvlslkkqg nkdlkwetsn
      661 nlnagfelsl fnnrislnad yferkvsdmi yalplppsna gsyvkygnig dmtnrgvqan
      721 vnvdilrnen vqwsfyanat hyknkitrlp aeqrgtglvt glfilteggd rytyylkefa
      781 gvnpdngdal wyrtsinptt qkeertitnn ykeatdyntg ksaipkvygg fgtditykrl
      841 nlslnfayqf ggygyddiyr slfhsdtygs nystdlnktw tpenpnaalp rvdltstnqn
      901 gnstlyliks dyislqdvtl syqlsdefak qaglsdlkvy ltgnnlylws krkgydpras
      961 ltgvsdayky sllssvslgf kltf
//
LOCUS       WP_101240346             919 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. PMSZPI].
ACCESSION   WP_101240346
VERSION     WP_101240346.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. PMSZPI
  ORGANISM  Chryseobacterium sp. PMSZPI
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Chryseobacterium sp. PMSZPI"
                     /db_xref="taxon:1033900"
     Protein         1..919
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101056
     Region          33..917
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfttvlkv apafllasti mhaqtkdstt kekkidevvl igygkqkksd ltgsitsvta
       61 kdfnggatsa gqliqgktpg vqitnnsgap gsgtkirirg tsslggensp lividgvpqd
      121 fvgvngvsdp lslinpndie tfdilkdasa taiygnrasn gvilittkkg sagrfkvnfs
      181 tvtslstkmg nvdvlnadef rsfvnanase nyrkklgman tnwqdliyqt awgtdnnvaf
      241 sggikalpyr lsigyneqng ivrsnsfrrt svglnlnpkf fdnhlsvnvn akgtftdnrf
      301 vdggvikaat yfdptqpvys gnskyggyye wldanspngy nvnatsnplg midglrdvss
      361 vtrglgniql dykfhflpdl hfnvnagydy tksdghkvkd aryrigyedk gsenfysmek
      421 knklletyfn ytknisaint gvdltagysy qdfniiipga ityrgignnt kdvdfesrnt
      481 lisfygraif tiankyvisg sirrdgssrf ynltrdnvwg vfpgvslawk lneesfikni
      541 saistlklra gwgktgqqel palgingnkp nnypalgayn psnpgayyqf gneyyymfrp
      601 anfnpnltwe ttvtknigld fgfaknrvtg sidlfrkdtk dllvfadepa gglsnaswqn
      661 igdmknegie gsitvipvkn enttwelsfn athykpiitk lkdrggesfn mevggieggs
      721 gnriqahavg yapnsfwvyq qaydangnpi nggyvdrngd gvintkdmyy yksttpdail
      781 gfstklshkn wdfalsarav lgnyvynnaa snsslksast neylqnvfss aadykfsdfq
      841 yrsdiyvena sffrldnini gynfgeifsk gsnlkvygma qnvfviskys gldpevyggi
      901 dngyyqmpri ysigfnfqf
//
LOCUS       WP_101259568            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            filiforme].
ACCESSION   WP_101259568
VERSION     WP_101259568.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum filiforme
  ORGANISM  Labilibaculum filiforme
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Labilibaculum filiforme"
                     /db_xref="taxon:1940526"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114925
     Region          24..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslfsmli lfviglqsvl aqsrevsgvv tsaddglsip gvsvivkgtt igtttdfdgn
       61 yslsvpvdgk tlvfsfvgmt mqeraitttt invvmetesi gmdevvvtam gvtrekkalg
      121 yaatsiggde igksqavnpm salqgkvagv distapgpgs tqnvmirgas sfgnnqplyi
      181 vdgvpitneq nssgsalnsq vdfgsginai npddiedmtv lkgaaataly gsraangvim
      241 ittksgkdte gkvrvsysgs vtlsrvgrlp dvqsqfgqgw sgdraldeng nwgpaydgkd
      301 rvwgnvvdns qqikpyvfle drvrdfyetg knvknsvsls ggnastnyfm slsqnsvdgv
      361 iptdndsykr ytiatkgshk agnltisssv nfstektkav asgqgtsvfr slyesandis
      421 ivdlenyndk fnnldnyftp ygvnpyyvln ensavqnkkk ifgkfqldye ftkdlnlsyr
      481 fggdyetsrs ethtaiiaft pgapndgsss anpgsyseir rsrtqvnhdl masfkkslne
      541 dftmnaivgl nvnersynwl ngsinsidip gfynlsnsla psvstqydek rrliglyanv
      601 dfsyrnyayl tltarndwss tlptgqndyf ypgvtgsflv tdylkyndid tgilnfakvr
      661 aaygmtgnda dpysvydryv safsgnpgyp diddlsfpig gvnsymasnr lgnpdltnel
      721 tkefelgvea qffnsrlgid fsyynrlteg liselpkdps sgyttqmanl gdvrnqgief
      781 vlnftpvkta nftwdvsynv alnrnemenl dvdevylggf ggagiyaveg eamgqfkiaa
      841 vkkvevdgvm ktvvdgsgnp qpttetefig kdinekyrmg ltntfsykgf vlgatldfry
      901 ggymysytkd ylhwtgaste tvlndrktfl vpnsvvsdgr ggyventtpv dptalhkfyg
      961 dgggfdgdad niidrsylkl rnvslsysls dnfckrlhvs avnlslsasn illwtpaena
     1021 yidpetttfg ndvtakfgey gagpsnefyt fgltftl
//
LOCUS       WP_101259571            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            filiforme].
ACCESSION   WP_101259571
VERSION     WP_101259571.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum filiforme
  ORGANISM  Labilibaculum filiforme
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Labilibaculum filiforme"
                     /db_xref="taxon:1940526"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117684
     Region          24..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslfsmli lfviglqsvl aqsrevsgvv tsaddglsip gvsvivkgtt igtttdfdgk
       61 yslnvpadgk vlifsfvgmt mqeheitsst invvmqsesi gmdevvvvay gtttkksftg
      121 tatqvdadki esknasnitq alqgevagvq visnngqpgs taeirirgig singsrsply
      181 ivdgtplqgd insispsdia sttvlkdasa taiygsrgan gvviittkqg ksgkssieid
      241 lkkginirll peydvftrpe eyvetawsal ktrglllgna dpaayasagl ftgdtkasgf
      301 ndyynmwdva gdqlidpatg kfntgvnrky spkrwkdelf qgaqrteagi risggtdktt
      361 yftsfsyldd egyylnsdye rftgrvnikh evkswlkgtm nmsfmnsesn lsggqdedsn
      421 ngfwlvanmp plypvyarda nsnkiedtvl ggyvydygdg qygtrrfasl tnavasstyd
      481 varttnnqfs gnskleatyk dftfsstfgl eylnssydnl gnmfwggsan qggsiykrkr
      541 ewfaftttnm lryakqfgeh nisafiaqea skrefremsa fksgladpws lelnnaivss
      601 psgsytdelm ltsyfgqily dfdekyffqg vlrrdgsskf tndkwgtfgs vgggwmisre
      661 sfmeptsnfl nelklkasyg vageqggigs ydsrllyevs nqndklalte shvgnpdltw
      721 eetaqfsigt efelfnrisg sveyyikntd nllfnkrvgp sngyaiiqvn dgtmenrgle
      781 vildfevvks edlkvnfgin aafeknelta mplesgsgeq kvidvsglyg ravghslfdi
      841 ytaeyagvdp tngraqwnry ynevggvkdy iadmeiylaq nkgnigeigk ettteysdat
      901 qkfinktpip tvrgsfnlda sykgfslaal fnyslggygy dsnyaalmdd dllgsnnwhk
      961 diknawkqsg ditdvpaits glsgysdanr tsdrfvtktd ylslqsvvls ysfnkrmldk
     1021 lklkglklfv sgdnlwtttk rkgfypnase vgassryqyv slssitggin vkf
//
LOCUS       WP_101260345            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            filiforme].
ACCESSION   WP_101260345
VERSION     WP_101260345.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum filiforme
  ORGANISM  Labilibaculum filiforme
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Labilibaculum filiforme"
                     /db_xref="taxon:1940526"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114257
     Region          58..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkcylrnlh sslanplglg skigifalll gimvfpfsag anvnkltndn tavlaaqqvv
       61 tgvvtedsgm slpgvsvvik gttigtvtdi dgkyeisapd ansvlvfsfv gmetkeitig
      121 sqsvinvvml tnalqvdevv vtalgikrdk kalgyavqdv kadeitkags sdlvsslqgk
      181 vagvqinqsg ggvggtsrid irgssslign dqpiwivdgv pfdngnsseg gvwggtsrag
      241 gaydlnpedi esisilkgpn aaalygergg ngvvlvttkk gargkglgis ysggftmsea
      301 aymldlqdky gqgsngvydn sstsswgpem ngqmleswtg emmpyeaqkd rlkdftrtgt
      361 tqkhsvaftg gnddgtfras lgkdilngiy edhkvekitf dlradydine wlnidtkvsf
      421 fntkgearpe ignysyvsyf ntmpmnirnq dlapgydiig gehveklytt tnanyrnpyf
      481 lqaqtvnede kdrtfgyvaa nlkitsdlta kfkygmdfyq fsgvggyiyg dnvdanrpny
      541 nptqskfkeq nyefllsynk vinddftigl nfgannrnsi retlsassgk lasegnffla
      601 agsninases lseeevrsmy afgqvayknm lfldftarnd wsstltsadi dfdndyfyps
      661 vslsgvvsem iempdwisfa kvrgswaqvg kgtqpfftaq nyslgnwnyg ltvgnvpsis
      721 idpklksels tsiefgadir flqnrigldf tyyyeqtenq igylqnveet gyskeltnig
      781 eilnkgieft lstvpvktkd ltvgvnfnfa mnegtleelk deisrydfgs svvaykggkl
      841 gdilgnvynr nesgaiiide nglmtinqdd nivignlqad wtgainlsvd ykglflsalv
      901 svqqggdiis ssersatsag taaqttangr iaffadgvte agglndvmis aeeywrqvsk
      961 vdeeflydas hmklkelaig ynlpksllsk iphnpvksar vsfvgrnlfy fykntpgtap
     1021 dasaysteya aqaydfspvp sartygvsln vgf
//
LOCUS       WP_101260751            1108 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            filiforme].
ACCESSION   WP_101260751
VERSION     WP_101260751.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum filiforme
  ORGANISM  Labilibaculum filiforme
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Labilibaculum filiforme"
                     /db_xref="taxon:1940526"
     Protein         1..1108
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123948
     Region          22..1107
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrllsllli llpvfgwaqe mkqikgtvls agdgevliga svyidkstig tetnmkgiie
       61 nitlgtitdf dgnftlevpk elntiacsfl gfetqmvdit gkssvtikls dstselgevi
      121 vtgyqkiekr kltsavvkvn adnirqagvp nvdqmlsgqi agvtsvvqgg apgapakiri
      181 rgtaslngtq dplwvldgip legnevpdyn dkdnidqlyn ssvgglnpqd iaditilkda
      241 aataiygara angvivittk kgkvgkmivn ltsntsfisr pdfdklnlmn sdekvdlema
      301 laartdltyn sqyggvsqil nansdwdnyq sggvsaisse sldainalrs vdanledely
      361 qnavnqdhsl sisggsdlat yyfslgahte kgttigtsln rynvtlktdf nlrdnlrlgv
      421 slfanerksk syltgssklt npanyvrlan pylklrdedn nyvynvdedg lyniayipfn
      481 ileeragtqn klkgqsinai fdlewdlnah lkfrtqygiq idktntkkea eeetffarks
      541 rhlsryfegg epfyfipegg vlqnweadnt aynwknivey nqlfnekhev elmignelrq
      601 neytqvfsaa ygwnaermts kpvifrdead aasfplfnkt yrknryasff atgsytydrr
      661 ytffgsirfd gsdlfgvdpk yrylplyals gawnaseesf ltnvdwlssl kfrasyglqg
      721 nidkesspyi igtpttvsnl pgtnedgidi sglpneklrw ektstyniga dlslfrhair
      781 msfdyyerkg tdligtqslp yetgfssmsv nwaemtnkgw elsistrnik tdnfewntnf
      841 niahnenkvl kekipasqfl psregysans vwviktkgld engyplfdkn gtavtgkelf
      901 dlydqyadfw pgnyagsnln teqvrdlfty agdsdpeysg giintfkykn idlsisanfn
      961 lgmdilaqpt ysmteydrgr ntsrklldvi ngtnktlpnl lgstsadgay wmekqwydni
     1021 dnagtyrhld twlkevnymr issirlgytl pnemlkrvrl snvrfslear npfvisngyd
     1081 gyfdpesygn iyaqpqqksy tlgvnltf
//
LOCUS       WP_101261390            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            filiforme].
ACCESSION   WP_101261390
VERSION     WP_101261390.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum filiforme
  ORGANISM  Labilibaculum filiforme
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Labilibaculum filiforme"
                     /db_xref="taxon:1940526"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116101
     Region          24..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkmiglfvf lifmgmqvvn aqnkqisgtv tsaedglgmp gvsvvlkgtt igastnidgq
       61 fsleakptdv llisfvgmit qevrvgekts fnivmetesi gmdevvvtal gvtrekkslg
      121 yavtelgges iaegkesniv nslsgkvagv nirqantmgg sanilirgta slmgnnqalf
      181 vvdgvpmdns ntntadqssg rggydygnaa sdinpddvas vsilkgaaas alygsraang
      241 vvlittkkgt kkkngigvtv nsgitfntin ketmpeyqye ygagyapews fegsdglngk
      301 tvvntnddas wgpafdpnlq vvhwdaldpn adnygetrpw iapkstvydf fetgvkytns
      361 valnggndfg sfrlsytnsd esgilpnssi kknsmaikad yklteklkvs asanyvntkg
      421 kgrfgtgydd nnpmqnfaqw fqtnldfdrm kenyqtadgg qltwnasnpn elapayannp
      481 ywtryknyed dernrlfgya aldyelndmf sltyrtsidf yherqneria vgsntqskfs
      541 tydrtysewn tdlmlkfkkt vndfslngll gvnyldrniq sifgstsggl vvpglytvan
      601 sqvaksptet llekntksgy gsfsvgyknf aylegsfrvd rtstlptsen tyfypavsgs
      661 lilselgaik dlsflsfakl rlnyaevgnd tdpynitsay tqyvnwgsna sfsvngtlkn
      721 pelksertds yevgleanff nnrfgfdlal yksnsfdqim dvnvsrasgy srafvnsgei
      781 enkgielgin ltpvkmndft wdmnvnwakn knevislyng vnniqilsaw dvtmnatvge
      841 aygvlkgtdf vytngkktvd angyytktad ddkvigniqp dwtggitntf sykgitlral
      901 vdiqkggdiy svdrkyglat glyketagln skgnpkrdav sngggilhan avnidgtpnt
      961 tfaradswgg dqyygrtpta ryvydasyvk lrevslsyti pkrilnstfl tnavvsavgr
     1021 nlwiihkntp gfdpetgqss gneqgiangs ypttrtygfn vtlgf
//
LOCUS       WP_101268135             392 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassospira marina].
ACCESSION   WP_101268135
VERSION     WP_101268135.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira marina
  ORGANISM  Thalassospira marina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Thalassospira marina"
                     /db_xref="taxon:2048283"
     Protein         1..392
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40952
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,98,295,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,285..286,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpreiw pgekrvaitp dtvkkytglg fevvietgag enasiaddry tdagatiakt
       61 akaatadadv ilkvrppmve gktnelaayk kgatviglie pydraeligk maeaglasfa
      121 melvprisra qsmdvlssqs nlagyravid aahefgrifp mmmtaagtla ptrvvvvgag
      181 vaglqaiata krlgavvsaf dvrpavkeqv qslggtfiev edddaanaet aggyaremsd
      241 dykkkqaakl kevlaktdiv ittalipgrp apeivtadmv agmkngsiii dlaserggnv
      301 agvkpgestv tengvkiigp snivssvatd atamyaknll nfvtlmvdse kkalvfnred
      361 qiiaetmltq dgkvvhpkfg getapeteaa ng
//
LOCUS       WP_101265225             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. S09G 359].
ACCESSION   WP_101265225
VERSION     WP_101265225.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. S09G 359
  ORGANISM  Pseudomonas sp. S09G 359
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. S09G 359"
                     /db_xref="taxon:2054919"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38649
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag lkasvvdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaaqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adetvvengv iicgptnlag avaadasaly arnlldflkl vfnkegqfel nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_101276932             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Stutzerimonas stutzeri subgroup].
ACCESSION   WP_101276932
VERSION     WP_101276932.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri subgroup
  ORGANISM  Stutzerimonas stutzeri subgroup
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas stutzeri subgroup"
                     /db_xref="taxon:578833"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38779
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkligqg hrvtlqsgag llssvpdsay eavgatigda
       61 aaafaaelvl kvnapddael aqmqsgsvll gmlnpfdndc iarmaargvt afaleaaprt
      121 sraqsldvls sqaniagyka vlvgalhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhera lqsdivitta lipgrkaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvaadasaly arnlldflkl vidkdgqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_101289080             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pleomorphomonas diazotrophica].
ACCESSION   WP_101289080
VERSION     WP_101289080.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphomonas diazotrophica
  ORGANISM  Pleomorphomonas diazotrophica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pleomorphomonas diazotrophica"
                     /db_xref="taxon:1166257"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39442
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkepd peegrvaitp etakrfialg atvvveagag lrslildfdy tmvgavvaes
       61 iadavrdadv lltvrrpsqd vlsqlktgal avammdpygd daavkamagt gvtafamefm
      121 pritraqvmd vlssqanlag yqavidasse ygraipmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedee fkqaetaagy akpmsaeyqa
      241 kqaalvaehi kkqdivitta lipgrpaprl vsadmvksmk pgsvlvdlav erggnvegak
      301 lgeivttpeg irivghrnvp griaatasql yaknlfafve tlidktakvl avnwddelvk
      361 ataltrdgav ihpafln
//
LOCUS       WP_101293804             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_101293804
VERSION     WP_101293804.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38820
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqrgag inasvpdsay eaagatigsa
       61 adafgaqlvl kvvapddsel vqiksgtvlv gmlnpfnndi iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlpa qvgadasaly arnlldfmkl lfdkdsalvi nleddivaac
      361 lmcrdgqiir kng
//
LOCUS       WP_101299903             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassospira lohafexi].
ACCESSION   WP_101299903
VERSION     WP_101299903.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira lohafexi
  ORGANISM  Thalassospira lohafexi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Thalassospira lohafexi"
                     /db_xref="taxon:744227"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40478
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,98,295,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,285..286,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpkeiw pgekrvavtp etvkklkslg fdvaieagag idaaipddrf vdagatiakt
       61 mkttvkdadv ifkvrppvid gktneltayk kgaavvalle pfdrkellda makagvdgys
      121 melmprisra qsmdvlssqs nlagyravle aahefgriyp mmmtaagtla parvlvvgag
      181 vaglqaiata krlgavvsaf dvrpavkeqv qslggtfiev eddeadaaet sggyakemsd
      241 dykkkqadkl kevlaktdiv ittalipgrp apeivtadmv agmkpgsvii dlaaerggnv
      301 agvklgqtit tangvkligp enitsavatd atamyaknll nfitlsvdte kgalvfnged
      361 qiiaetrlth dgkivhpkfg geavang
//
LOCUS       WP_101305382             518 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Microbacterium].
ACCESSION   WP_101305382
VERSION     WP_101305382.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium
  ORGANISM  Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Microbacterium"
                     /db_xref="taxon:33882"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51724
     Region          3..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 marigivrer dgetrvaasp ttvgkiralg ydvsvetgag aassfpdaay taagatiatr
       61 deawgadvvl svaaptdaei allqpgatli gilspalnpd llaalaargv talamdavpr
      121 israqsmdvl ssmaniagyr avveaanefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvasiggt ylevvvpdeq kevsadgyak atsaaydaaa
      241 aklygdqaad vdivittali pgraaprlit aadvaamkpg svivdmaagq ggnvegsvag
      301 ervvtangvi vlgytdlagr lpqqasqlyg tnllnllall tpgkdgqlvi ddtdvvqrav
      361 tvtrggavtw ppppvqvsaa patpgadaaa stpapaakkg lsagaktgli vagiaalflv
      421 cavapaplpq hilvltlsvv igfyvigkva halhtplmsv tnaisgiivv gamtqivvpn
      481 pvvqvlaaia vllasinifg gfavtrrmla mfqkgdqk
//
LOCUS       WP_101307889            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            manganireducens].
ACCESSION   WP_101307889
VERSION     WP_101307889.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum manganireducens
  ORGANISM  Labilibaculum manganireducens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Labilibaculum manganireducens"
                     /db_xref="taxon:1940525"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114183
     Region          58..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkcylrnlh ssltnplglg skigifallc ammvlpfsan anvntltndn ssvsatqqvv
       61 tgavtedsgm slpgvsvvvk gtttgtvtdi dgkfeitvpe stsilvfsfv gmqtqeitvg
      121 sqsvinivma tdalqvdevi vtalgikrek kalgyavqdv kadeltqagn sdlvsslegk
      181 vagvqinqsg ggvggtsrie irgasslsgn neplwvvdgv pfdngnsrdg siwggtsrag
      241 gafdlnpedi esvsilkgpn aaalygergg ngvvlvttkk gtrgkglgis ysggftmsea
      301 aymldlqdky gqgsngvydk nnasswgpem ngqlleswtg emipyeaqkd rlkdftrtgt
      361 tqkhnvaltg gneegayrvs igkdimngly edhkvekltf dlradydinn wlnvdtkvsy
      421 fqtegnerpe ignysyvsyf ntmpmnirnq dlapgyniis gqhveklykn pnanlrnpyf
      481 lqaqttnyde knrtfgyvaa nikinsdlka kfkygmdfyd fssvegylfa dnvdasrpny
      541 nptqsnfkee nyefllsynk dinedftigv nvgandmrrv skglsansgr lssegdffla
      601 agsnikases asesevrsvy gfgqvayknm lfldltarnd wsstltasda qydnsyfyps
      661 vslsgivsem tdlpdwvsfa kvrgswakvg katepyntsq sytlesgnyn ltrgivsdqr
      721 vviglkpeis tsweigadlr llnnrlgidf tyyneetknq ilavpgvqss gyntilinag
      781 litnkgvelm lttvpvktkd ltvgldfnfa knesvmekla ngvpeynfgm nvmaipgekl
      841 gvirgtvydr dvngniiidn sglmviaqgd dhvlgnvqpd wtgsinlsvd ykglfltalv
      901 svqeggdils ssergavsag taarttennr msffvdgvta sggannvivs aeeywrqlak
      961 vdeefmydas hmklrevavg ynlpksllsk iphnpiknar vslvgrnlfy fykhtpgtap
     1021 dasaystdfa aqafdfspvp sartygfsln vgf
//
LOCUS       WP_101308989             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            manganireducens].
ACCESSION   WP_101308989
VERSION     WP_101308989.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum manganireducens
  ORGANISM  Labilibaculum manganireducens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Labilibaculum manganireducens"
                     /db_xref="taxon:1940525"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110422
     Region          28..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mriqyryiil tlfvfltmkg wsqtgdttgk iidrngnpvs gavvsiesnp enkvytnang
       61 efsifapdsa alvvqtsknd fkkvsakkge sitiqmdffs eavelgygih qtigestgav
      121 slttheqvnk rsafsvsnal ygnalgltam qnsgavwdtg atlsirglqt lsnngilvvv
      181 dgierdiqyv vpeevesvsv lrdaaavaly gykgingvls ittlrgkyqt seinvsydha
      241 fnwqsrlpkf adsytyasav nealsndgks arysenelga fksgeypnly pnidwmdevf
      301 rengcsnmyn vnfrgggkkv ryftmlnlqg nqgfidnsdv ndgystqmky skgnirtnld
      361 idvsstttvq vnlmgvlnef srpglgsdnl isklyttpsa afpiktsdgi wggsetwgen
      421 mnpvaltqar gyskghtrsl yadvkltqdl nsiteglsas lragydnvaa yweghtknya
      481 yasenvaswv dgkpsdisty sagadsgief gskldwqdrh snlfanvdyq kesgknkffs
      541 slmysyehhv knsqnhtyyr qnvagyihyv ynnryvadlt latsgsnkla pgekwgfspt
      601 vsaawiisne nfmknvkpvd flklraswgv intdyipted ywkqtfgsgg syplggsysd
      661 yggmwegrla stntsrekai kynlgldagi lngvvitada yfekrkdiwv saggansavl
      721 gisspytnag ivdswgletg lnynkqlgdf kislggkftl aknkvkemle epkayeylrq
      781 tgksvdqifg lqaigffvdq adianspaqq fnevkpgdik fkdqnndgvi ndydnvamgy
      841 ntsvpeiyys fdlgfewkgl glsatfqgve rytailntqs vyrplvdntt isehyynnrw
      901 tpenpsakyp rlttesndnn fqtnsvwlad asflklrnce iyyklaetyl sklrlksakf
      961 yvrgidllci dninlsdpes vgvaypmtrs invglaigf
//
LOCUS       WP_101308246            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            manganireducens].
ACCESSION   WP_101308246
VERSION     WP_101308246.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum manganireducens
  ORGANISM  Labilibaculum manganireducens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Labilibaculum manganireducens"
                     /db_xref="taxon:1940525"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114477
     Region          24..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslfsmli lcviglqsvl aqsrevsgvv tsaddglsip gvsvivkgtt igtttdfdgn
       61 yslnvpadgk vlvfsfvgmt mqeleitsst invvmetesi gvdevvvtal gikrskkalg
      121 yavqdvkaed lqktgtpdla kalqgkvagv dikmssgmpg assqivirgs rsfsgnntpl
      181 yvidgmpvas taaystgnst agadvsnral dinpndiesi nvlkgqaaaa lyglrasngv
      241 viittksgkg gaigkavvsi nqttsfdvvs rtpdyqkkws qgsagkyspr tsmswggkis
      301 elpndptygg ngnghegmyr vpqledagld pwvtpqvynn wddyfetgft sttginvsqa
      361 tekgnfsvgv gytdqegial ntgmqrwnak aaaesklnen ftvgfssnfa kttvdklsag
      421 ndasiagals apasynlkgi pnhaqgdpyk qiyyrsltfd npywvqnnnt fneetnrfyg
      481 ngfvqyaksl gdgmdltvky qlgmdtytth yqdifgfgsk gktgeisnyg vtdmtynsll
      541 tanfdwtind dfrlnvivgn elnhnrtkqy dqygqefnfg gwnhvqnant vtagekkykd
      601 rtvgvfssvs lswkdmmfln vtgrndvtss mprgnrsffy psvslgfvas eldvvknidw
      661 ltfakirgsy aevgqagtyk enfyekpgys ggfwsgepit ypmggvssyi asdvlydpkl
      721 kpqntksyel ginlkfaknr igidytysrq nvedqifsvp lagstgassv mmnggqvhtn
      781 ghevmlyltp istkdftwdi nvnyskitnv vdklapgves iqlggfvtpq vragiadtyp
      841 viygsqykrn engqilvden pssttygmpm agepgvigsv spdfivggst tftyknfslg
      901 atfewknggq mysgsnglld lygmskrted restfiyngy kadgsrndiv rggasdsgay
      961 qtlfsdvltn ideyyihgns fvklrelsfk yrlpkglipn idvavstfar nillwteldn
     1021 fdpessqgnn nmsggferfs lpqttsygfs idvkf
//
LOCUS       WP_101309261            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            manganireducens].
ACCESSION   WP_101309261
VERSION     WP_101309261.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum manganireducens
  ORGANISM  Labilibaculum manganireducens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Labilibaculum manganireducens"
                     /db_xref="taxon:1940525"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112271
     Region          39..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkleqksr snlkhyqlmf llflsvvfcs stiglaqekv egivldeigs plpgvtvlik
       61 sttigtitns egyfnldakv gdivsisfig yktydinvvk empkqevhle adfvgleevv
      121 aigygtqrkg dvtsaitsvk sedfivgkig daaelvkgki aglsitkssg dpnatssiml
      181 rgittikgsv qplvlvdgie gslttvapen iasidvlkda saaaiygtrg angviiistk
      241 sgkrdsqata tysayvslse wyktldfmdt ndiiygrtnf eyggydtdwl eavsrkagyt
      301 qnhslsltgg tksstyaasi tfsdeegimr ksdsndikaq mdfsqyamnd ilkfninvly
      361 tthkntnnnn nyvyrqalir npsspvyned gtyfeefsrf qyfnpvaiqn emigdtrtky
      421 arvtgnitfe pikgwktnlm lskkeiettg etyytsqyyt qatggikgsa skssgndvsd
      481 nlelttsydf sieksrisai vgysylynvh dgfsasnsnf psesylynnl gqgtylsded
      541 hvagmasdkr ddklvgffgr atygydnrfn amvsfrregs skfgennkwg nfpaaslgwt
      601 vsnenfmksi swltnlklrt gygvtgvipt dsylslttfd ydaygkhlnt dgkwtpslkv
      661 aqnpnpdlkw ektsewnigl dwavldsrls gaidvytkkt vdllydyavp vppnmydvtt
      721 anvgqmrnng ievmvnaipv ktsefewnst ltlshnenkl lslsndlyet dnfsevggvg
      781 dpisvatham eighrlgdfw glrsvgvskd gvvlvqvknd ddtwsvkefd tkyneeknrq
      841 rlgnglpqiy agwsntfryk gfdlnlqftg qfgyqilnsq rsfyennsia ynrlksaanl
      901 ygavdaagaa vinpetgsql qvgltnsmsq gvwsdhieng dfvklsnatl gytiplsaka
      961 ksyvnnlrvy vsgqnlfcit gysgldpevd nnflapgidg rdkyptvrsy tiglsvnf
//
LOCUS       WP_101310042             939 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            manganireducens].
ACCESSION   WP_101310042
VERSION     WP_101310042.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum manganireducens
  ORGANISM  Labilibaculum manganireducens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 939)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 939)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 939)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..939
                     /organism="Labilibaculum manganireducens"
                     /db_xref="taxon:1940525"
     Protein         1..939
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104674
     Region          65..937
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrykiials fisglclyty aqgqelrdsi sakpkkfige avhigyhktq sfeestssta
       61 avsskefdkr saknianslf ghglgltvlq nsgryagsep tmyvrglqts sdntplvlvd
      121 gierdisgis peevetvtil kdaaataiyg ykgingvini stkrgeyett kvnvsfdhal
      181 dmqvrrpefv nsftyakamn ealkndgysv rysqneldal esgeypylyp dvdwidetfr
      241 dlgytnnynv sfsggtkrfr yyalakltgn sgfienhdmn sgystqdkys kanlrtnmdv
      301 dltettkmkl dvlgilsesk tpgagnlwss iyalpaaafp vqledgtwgg ntiwagtmnp
      361 aavsqdaays kyhsrslfad mtlsqdlsai teglgasamf aydnsatyse dhtktfgygs
      421 qtvtewldnk pasisnysgg vessmgsaak itsftrvfnf aatayydkai sdnqklyaql
      481 kwdyeyrnik gvnqtwytqn aslyahyglk dkyfaaftlv asasnqlasd hkwalsptis
      541 aawllskedf mknlswidll kvrasfgiin sdeipgtnyw eqtyggggyy pfdtnysvgt
      601 sswslgqlas lnsthekafk ynfgidarmf dgldlnldty fehradiwid sdgkyssvlg
      661 ftapyenggi vnswgielgt kynktfgdvt vklganftla knkikeqyee lrlyenlvtt
      721 nkplkqtygl valgffkdqs didnspeqlf gdikpgdiky kdvngdgqid tndktaigys
      781 ttapeiyysf nlgaewkglg fdavfqgtgr ysallntssv ywplinntti sqeyydkrwt
      841 sesesakypr ltsqnnnnnf qtntiwledr sflklrsvev yynlpqsliq ktkfiknakf
      901 yvrgvdlvcf dkiktadper sgagypliks yiagvsidf
//
LOCUS       WP_101310405            1108 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            manganireducens].
ACCESSION   WP_101310405
VERSION     WP_101310405.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum manganireducens
  ORGANISM  Labilibaculum manganireducens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Labilibaculum manganireducens"
                     /db_xref="taxon:1940525"
     Protein         1..1108
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124057
     Region          22..1107
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrllsllli llpafgwaqe mkqikgtvls esdgdvliga svyidkstig aetnikgiie
       61 nitlgtitdf dgnftlevpk elntiacsfl gfetqmvdit gksfitikls nstselsevv
      121 vtgyqkiekr kltsavvkvn adnirqagvp nvdqmlsgqi agvtsivqgg apgapakiri
      181 rgtaslngtq dplwvldgip legnevpdyn dkdnidqlyn ssvgglnpqd iaditilkda
      241 aataiygara angvivittk kgkagqmkvn ltsntsfisr pdfdklnlmn snekvdlema
      301 lasradltyn sqygsisqil nanndwdnyq tggvsaiape slaainalrs vdanledely
      361 qnavnqdhsl sisggsdlat yyfslgahte kgttigtsln rynvtlktdf nlrdnlrlgv
      421 slfanernsk syltgssklt npanyvrlan pylklrdedn nyvynvdedg lyniayipfn
      481 ileeragtqn klkgqsvnai ldlewdlnsh lkfrtqygiq idktntkkea eeetffarke
      541 rhksryfsgg eplyfipegg vlqnweadns synwkniiey nqlfndqhev elmvgnelrq
      601 neftqvysaa ygwnaermts kpvifrdead aksfplfskv yrknryasff atasytydrr
      661 ytffgsirfd gsdlfgvdpk yrylplyals gawnaseesf lsdidwlsrl kfrasyglqg
      721 nidkesspyi igtpttvsnl pgtnedgidv sglpndklrw ektstynigt dlslfhhair
      781 msfdyyerkg tdligtqnlp hetgfsamsv nwaemtnkgw elsiatrnvk tetfewntsf
      841 niahnenkvl kekipanqfl psregysans vwviktkgld engyplfdkn gtavtgkeff
      901 dlydqyadfw pgnyagsnlt teqvrelfty agdsdpkysg giintfkykn idlavsanfn
      961 lgmnilaqpd ysmteydrgr ntsrklldvi ngtnknlpnl lgstsadgay wmekqwydni
     1021 dnagtyrhld twlkkvnymr issirlgytl pnimlkrirl snvrfslear npfvisngyd
     1081 gyfdpesygn iyaqpqqksy tlgvnltf
//
LOCUS       WP_101310583            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            manganireducens].
ACCESSION   WP_101310583
VERSION     WP_101310583.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum manganireducens
  ORGANISM  Labilibaculum manganireducens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Labilibaculum manganireducens"
                     /db_xref="taxon:1940525"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118878
     Region          24..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkmiglfvl lifmgiqvvn aqskqisgti tsaedglgmp gvsvvlkgtt igastdidgr
       61 fsleakstdi llisfvgmvt qeisvgdktv invvmetesi gvdevvvtal gvtrekkalg
      121 yavqevgadd lnkvkqtdal salsgkisgv qvssssnfsg skrilirgan sifgenqpli
      181 vvdgipmdns nfnstsaqsg gggvdygnml ndinpddien mtvlkgaaaa iygsraangv
      241 iiintkraka gkdeirvdfs ssiaidkvad lpalqrkygg gaivsdangg vngfeqvtid
      301 gtnylvpqya vdeswgpayd pnikvlgwda fdqasfpddy lkprswiapk ndvedffetg
      361 vsyvnsmavt rtgkdygvrf aytnthnegi vpeskhdrhn ftvsgntkll dklnvqgain
      421 yvrsetsgrp tfgytdnsfa qkffqwgqrq ldfgrlknyk nidgtqrtwn rqswdnstpk
      481 ysdnaywivn enftdderdr fygnisvdye iaeglvakas vygdtytfsi rertavgsqs
      541 tssyyeakri nseynyeftl nyskrfnedf nitamagans rrkkldllrg sttgglvvpn
      601 iyslgnsvgn vstndyyeek nvnsvfgsas igyknfwfvd ftarndwsst lpednnsyfy
      661 psvstsflfs ellpevswld fsklrlgwaq vgndtdpykv fgtfeantng pfqgaprfst
      721 detklnehlk peettsyeig melsflqnrf gvdvtyfnnv tkdqiipldv saatgydaky
      781 inagemenkg leltlkgspi rtkdlswdin inyakinnkl ielypgidal diqrapfggv
      841 ylrasvgdty gtlwgtdfif ddkgnkvvsa sgqylktadl vplgsvlpdy nvgirnnity
      901 knfdfsflfd vqkggkfysl shnwgmysgm leasaqtndk ginireavad gggikikgvt
      961 gtvtydadgn ysvtntapne iyvegqdwag rhyhgaggps aqnvfnadyv klrevtlgyn
     1021 fpktmigplr slklsvygkn lwtggldkkg fdpensvggs gniqgieggm ipntrsygfn
     1081 lqlgf
//
LOCUS       WP_101310799            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Labilibaculum
            manganireducens].
ACCESSION   WP_101310799
VERSION     WP_101310799.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum manganireducens
  ORGANISM  Labilibaculum manganireducens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Labilibaculum manganireducens"
                     /db_xref="taxon:1940525"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114835
     Region          21..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkitlllli ftnvlivnaq iklsgrvndq qgnslpgvnv vlkgtvkgtv tsldgnysie
       61 aksddvlvfs fmgfaskeep vkgrtlinvv lgedvqqlne vvataigikq qkkkigyate
      121 kivddvivqa kslnlggalt gqvagltvtn ptgifqspdf qlrgkkpliv ldgipvetdf
      181 fdiptenies invlkgtsas alygsrgkng ailltskkgt skelqttvst tlmvsagyaa
      241 fpdpqheygs gsngqyefwd gadggisdgd mtwgpkfepg kmiaqwnspi rdkvtgetie
      301 wyggvkntky ddrsryervp tpwiqhnnlk nflstgiisn tdmsismktd rgqfmmtgky
      361 ayqkgqvpss rvnsgglnfn gsykltedlt legglsyskv yspnyprygy gpknhmytvl
      421 vwmsddvdge alknhfwipg qegyqqanyn yawynnpyfa sselkqahdr nvisgqvklr
      481 wdvlpnlsiq grgavrmkdl fenmqspksy mnygdsregd yktwnseqtn fdtdvlltyt
      541 anisddlnlt vnggasyfyr kyqqeyaatd glivpgiynm gnsqgpvmat nyleekatss
      601 vyatatldvf kswfltltgr ndksstmptq nnsyfypsva lstmvsdyit mpkqvdylkv
      661 ygswaqvssd ldpyqiesty snngtfgmsp kisypagivn snikpeksts tefglstsff
      721 knrlglegty ykvidenqii qlplskasgf ssryvngney etkglelals aklinkafkw
      781 nvrtnwsfnk ktltkiygge ekyndlrvgd raddmwgtqw qktddgrlii dpntgltikd
      841 sekgylghsd pnarfgfqnt fnykkftlnv dfdgviggvm ssktiqklww ggrhpesttg
      901 rdaeyaagka vyvpkgvnvl angdiventt avswqtwsqn ypyranvted enkkfanvfd
      961 rsyvklrkva ltynfdnnnk vrllngaait lfannvavlk niplvdpdfk tgndddlqdp
     1021 saryigvttk ftf
//
LOCUS       WP_101322671             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_101322671
VERSION     WP_101322671.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38728
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp dtlkklvgqg hqvtvqrgag lnasipdsay eaagatlgsa
       61 adafgaqlvl kvvapsdqel alinrgsllv gmlnpfnsel igkmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee recaqgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvlehgv tivgptnlpa qvaadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgnvir nng
//
LOCUS       WP_101348288             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aeromonas
            sobria].
ACCESSION   WP_101348288
VERSION     WP_101348288.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas sobria
  ORGANISM  Aeromonas sobria
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Aeromonas sobria"
                     /db_xref="taxon:646"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53169
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevaiesgag qlasfddaaf eaagasvvps
       61 vwqadlifkv naptdaeiaq ikdgatlvsf iwpaqnselv kklserninv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggefl kldfggedga ssdgyakvms defiaaemal
      241 faqqakevdi iittalipgr papklitkem vdsmkpgsvi vdlaaatggn ceytkptelf
      301 vtpngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgnvaidfe dvvqrnmtvi
      361 qagevtfppp aisvsaapqk pvaapikkae akqpsnkkfv fgalgiaafg wiasvapaaf
      421 lshftvfila cvvgyyvvwn vshslhtplm svtnaisgii vvgallqigq gstlvtalsf
      481 vavliasini fggftvtqrm lkmfrkd
//
LOCUS       WP_101359990            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_101359990
VERSION     WP_101359990.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113373
     Region          43..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfgnrklila affflgmkat lkaqesvhdi ivrdkstqqp lsnvsikntt tgkeivtdgn
       61 gkvaievnev sqtyaisleg yiaqdialsv gklpdsvyll petkqlegvv ltgytrqska
      121 kttgavssik aeaiaktpva sldqalqgqi pglyvaspsg qpgamgrvti rgigsvqddk
      181 tnplyildgm pispeifavl npldyenivv lkdasataqy gsrgangviq itskkgkdnd
      241 kghsqffyqn qfgissvnnq kwdmmnssqr lefeeilqdp nfpgwvysrk npykivngqk
      301 iaktdadyte gdqkladlqa tntnwrklll rngvtnshyl smgggnqktn hysslsyfkq
      361 egvlpnsgve rfninsgvnh ksgrftssfn lnltggqtql sesdfdvset npvaslyfam
      421 pyekpydkdg nltpgvnrfg analtmyqdi srkekqlqgv lssnlsfeit knlkltstlg
      481 vnhqqtrftr iikpdtyfgs mvdpgeqgly erintqktsy manfgfnykk rwgsneveai
      541 vlaefnkyst nydgftgygl ipglentpgg itpgtpdnnf ipkisggase nilvsqlgml
      601 rysyanrftl sgsirrdgss rvptdnryky fyafgatwni kneeflknwg alstlrlrls
      661 hgltgnaggf asdfgyrqly kpqhyngyta fipispgnpn ynwemnkisd vglefglfkn
      721 riigevdlyn rvtsdlfinr slsmtsgfes iadnmgkirn rglefrlsgd lfrndnfswn
      781 lglnlaynqn rilslgsene ivtenysihk vgsalghfym vrwagvdpat gaplyydknd
      841 avtkeynpen avmvkgaydp pikggittsf tyknlqvnal ftfvkgmyrl ntaelyrtsa
      901 dpnyriynqs tdmlnmwqkp gdisqnpgaq yarymtdrel qsadyiklrn vsinyklkdl
      961 gslnkvfkei nifaqgqnll twtkwkgqdp eddnnwyqye yplprtitlg fnvlf
//
LOCUS       WP_101360024             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_101360024
VERSION     WP_101360024.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110253
     Region          30..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklqllialg lvsgleayaq nvpktngtdt lktgekkide vvitalgikk ekkalgyavq
       61 evkgdvfeka kepnfinsls grvaglnirn stdlfqdpgi nlrgakpliv idgvpdrtad
      121 lwrvnaddid nisvlkgpta salygsvgkd gaimittkkg kkgkltvsfn nstmfqtsfi
      181 ripevqtvyg ggnngkyayi ngqgsgsegg gwiwgpkldq rdpntpsgyf etpqynstvd
      241 pvtgkliplp wisrgknnik nffetgliqs nnvsvdwgse katfrlslsn iyqkgivpnt
      301 nlkttsisla gsvnpvknlt itsaltynkt ytsnfpevgy gptnylynlv lwtgadvdvr
      361 dlrnywvpgk egyqqrhynv syynnpyfqa yeyqrpyykd nvmgnvnldy qivpkltaka
      421 rvgvnvysln reyrepksyi gygnkslgny sqvnnnyfdi tselglkyqn nysdnftlsa
      481 egyvanyyre mknseirtdg lvtpgwynlf nsigplfipt dgnrnrkeye qinsvygyvd
      541 mefyktffln mtarydkvst lpkgnneyfy psvsgsllln qlfnlpswin lakvrgsyas
      601 vtsgkigndt ygyisafekr agwngqpafa fgnslidqni kpettdswei gtnlvflrnr
      661 inldvayfna rdynqleevp lsegsgyksf ltngnvykrk gieftlsadv ikktdfrwst
      721 qvnfsqyrky lteayggkpy ttiynqsngr nnivmvgera dkltavayet spdgqlvlkn
      781 gypvsslapm eanmgysnpd wtygfshnfs yknfslsllf dgriggmmys ttnqkmwwgg
      841 iapgtvnqfr ddanagknty iapgvkvteg sitydkngnv vsdtrkfapn dvavnynaym
      901 qstsnafesn yhyykqtfik lrevtltynf gksfveklnl saasisligr nlwlaskikn
      961 idpdsgldnl qtpatrsfgv ninvkf
//
LOCUS       WP_101360379             928 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_101360379
VERSION     WP_101360379.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 928)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..928
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103241
     Region          28..927
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvnykvfta slffmgvcvy sqkkdtllke nkidevivvg ygkstkskmt dnvakisaes
       61 ikeipnanfq nalvgkaagv qinqtngkle agfninirgs asisagtgpl yvidgiplin
      121 rdestnsapv nplvtlsase iesveilkda ssaaiygsrg sngvvlittk tgkkgkpkls
      181 fnisqgfsnp thkvrflnak eyvellleag rnvndedfvi rrfnrysnnt dwrngaidtd
      241 wqkyifrqga vrdadfsvsg gddnynymft asnndskgii rgndlgrnta rlnvsakvtd
      301 klklgmnlgf srtsidrvan dnafvtpmqa vaqapispaf idgepftgtt yanflledky
      361 anyntfikrl tgklsaeyki lknltfnsdl gydyynqkek nyrgrntpqm atdgyaynsr
      421 vdtenlvftn ylsynlrfgs nnisavagte ynknrrefgs vtgirfpsdd fqninsagei
      481 iegrgeasey tffsyfarvn ydykgkyllk gsirwdgssr fgqenrygvf pafsagwvis
      541 kesflsesnt ifllklrasw gktgnaeigd faardqwqat kykqlpgiep iqpanpdltw
      601 ekstqtdigl dfglfsnkis geidlynkkt ngllfqqnip ytsgyssiyr nigdmsnkgf
      661 evvlntqnfr rddftwntsf niarnnnkit alpdnnadqi igntilrvge rsasfyltey
      721 agvdsangda lyykntlksd gtldktttnq yseanrivtg tftplwtggl tntleyknfd
      781 lsftlygefg asiynsggkf mstagswfdn qtadqmnrwq kpgditnvpq arlgeengtq
      841 estrylekrd fvrlrnfslg ytlnkdlmks lgvnklriyi sainlltftk ysgydpeala
      901 dtgrggggat fysappartf tfglnvnf
//
LOCUS       WP_101360480             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_101360480
VERSION     WP_101360480.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109454
     Region          32..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqqckiga lalilfaeys faqtrdsltk ensikevvvv afgkqkkeei tgsvqslktk
       61 dlanlqngni lqgiggkvag vqvissgqpg sqptirmrgi gsinassdpl ivldgipyng
      121 nlnsipgtdi esisfledas snalygsrga ngviivntkr gktnglriea dvktginfrs
      181 iedypvytsp kdyytafynr arvgeiarlk qagavptgas phevgisaln klgynaynlp
      241 fnqlisqdgs fnpnaqllyq ddwkkllfkp alrreasvgi tanneqvksy tslnylddqg
      301 ylissgferf girsnldyai tsklkltsgl sythskqdfg etggfsnpfq farniapfyp
      361 vflrnnnyqi vydkngkaly dygdgqgpng aarsyavyen pvgnlqqdks qttsnitnin
      421 lglnyeiikg ldftynfgay lenikdlrfg ntiggtsasv ggnltmssif rntlnhqqll
      481 tyqkkigkhn fnilvgheln ktksdrfsgt kqqlvlpnsl sfdnavkitd lsgngyeyav
      541 egyfsrllyn ydnkyffnan irrdgssvfs pdsrwgnfyg lgaawniake dflkgnntin
      601 slklkvsygq qgndnillen sdrdyyayqd iyginnfgeg kpvlslrkqg nkdlkwetsk
      661 nlnagfeisl lknrislnad yferkvsdmi ytlplppsna gsyikygnig dminrgvqan
      721 lnidilrsde lqwsfyanat hyknkitklp aeqrstglvs glfilneggd rytyylkkfa
      781 gtdpnngdal wyrtninpnt kkeettitnn ykeatdyntg ksaipkiygg fgtdftykgf
      841 nlavnfayqf ggygyddiyr slfhsdtyas nystdldktw tpenpnaalp rvdlnstnqn
      901 gnstlyliks dyislqditl syqlpadftq higlsalkiy ltgnnlylws krkgydpras
      961 ltgvsnsyry sllssvslgf klnf
//
LOCUS       WP_101360643             991 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_101360643
VERSION     WP_101360643.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..991
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110504
     Region          32..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnknvkslla lvltgcisqa afsqktkdtv ktkvidevvv talgikrmnk slgyaaenkd
       61 skifedtqnn nwvnalegkv aglkiqtaga gplgsaritl rgeksfdmds nnalividgv
      121 pmsnnttgtg asaygagagg dlpidygngi nsinpddias vtilkgasaa alygsraang
      181 aimittksga gskklrvsfs sdtsfdtvlk wpdyqyeygq gtlnkdksgk fyysygased
      241 gvntgstssa fgpkfngqsy fqydpniigp slerqlwrpy knnikgfwqa getysnnlsl
      301 ensndktsfr tslgyvknnw mmpntgfnrf nfstslthql neklkittkv myskmmsdnl
      361 patgynnqsi syfmifqnpn vdlawyrpiw kpgkegidqv hpfssyidnp ymiayemlns
      421 annnqlnani tlnykinnnf dvmfrsglew qndirsqrrp fssanypqgy yreehitnqe
      481 ynndilftyk nsqkdskigi saslggsiry neyryemtra tglrkpniyt lsnglslfsa
      541 ipspkdrqen siyglvslny gkyvyldlta rndwtstlrk gnnsffypsv stsfilsdif
      601 gikntfdfwk lrlsvagvgn gtkpyrldry ysigeisgsv vapntlnnin llpekntnye
      661 ggmdfsmfkn rlginftfyk nitknqivei paltesgfrs rfinsgsven kgleitlnat
      721 pikkpnftwn inanwsanrn kvlslpaefe gnpytvasvg dvlfyqvrig gslgdmygyk
      781 lqrtpdgqvi ydpstglptr padieyvgna fpewraglqn efkiknfris fsfdgqykgm
      841 aysqshhkms eqgklghtlw grenpdgmvi gegviknadg sfspntkkvl ltnyygdyyr
      901 ranvetnsfd tsfiklrdar vsytfpdasi gklklkelti alygknlwmw tkfplfdpea
      961 atlnnstitp gaevgqlpsa rtigmqlnvk f
//
LOCUS       WP_101360796             928 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_101360796
VERSION     WP_101360796.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 928)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..928
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104164
     Region          35..927
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktqiknfgk vgvcfflmsg mihaqttkkd slnekkieev vvlgyktqrk gntsesysli
       61 kkedlkavtt pnvanmiqgr aagvqviqss gapgsgasii irgatsisga rnpiwvvdgv
      121 ifngspnldp nqiesisvlk daastalygs rgasgvvqvt tksgkkgtnq lsvtanttys
      181 vfntgkfklm ngqqmydfws demkysdvdf tsvlrnrnfd wlnagtqsgl iqnytvefsg
      241 gtdksktyis gnyykeegsv ignkmdriaf rlnheyevnn klilkpkvsm tyntnynqqh
      301 slyqmylnmp wdspyladgk igrprldypt sgsdkwwgrd msnyyydlqr dyskgsnfnv
      361 svngdfdyki lknlvfssvn nftlyyddsm sysdplsigg sanggaiyky ttkrlsryfn
      421 qmlkynktfg ehsidalaay efqdsknesv nasvshivgg kevldagast mqkptgggns
      481 ymfqgflfnt nysyagkyla qfsirrdgas iygadvrygt fwsasaawnm hkesflqrdw
      541 ltelklrasy glvgnqpgsv yygwqdlyyt tipgtslgyt ydgfpgavlt qvenkkyswe
      601 ivkttnvgfd frifnrlgit adfyikdnnd msyrytypvl agqvwqyqni gklrnkgfei
      661 avnydvvknq nfkwtldfni glnrnkiisl kdgkpipngn kryiegedin afymrkwsgv
      721 dskngdplwe vvasdgtist tnnynaatlq kvgtatpdyf gginsslqyk gifldinaff
      781 skggliyngp relfdsdgay ptynqmyiae qgwtrwqkqg deathpkavy nntslsnkts
      841 sryledasfi kirsirlgyn iprqwlegmk iknasiyvna enmftftkfs ftdpevgfgp
      901 ngtspynead aahypvprki tlgvnltf
//
LOCUS       WP_101360807             963 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_101360807
VERSION     WP_101360807.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..963
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105836
     Region          15..962
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklcmlsa gvlffighsi aaqkvkkdts svkdidevvv vgygvkaskk vttsvskvkg
       61 eelikvsaas adallqgatt glqvsptsga pgagfnvrlr gvssitssnd plyvvdgipi
      121 sssspsgnvg yggqtgslls qlnladvdsi evlkdaaaaa iygsraangv ilittkkgkk
      181 grvnfslnst vgfqnpikky ekmkageyyk mldlaefntt psrgetywst ingvwspasg
      241 qsiedfyksd fgddylnhvy renqpiyels asvsggndqt syymgfsnfd qagaivgqey
      301 srqtftlnld qklsdmfkvm gsvrlsneyn trvngdnsiy aplttailep pgqliwnndg
      361 gynittwsfs nplqsgtdik sltktfgvnt slgleskfss klsmitrfnl erinydesrl
      421 fpldtyqgrg asgeanyngi lyntftgfnt ltysekisen frfilmggle yfnrkiaets
      481 vqtknvplga tspdagsekt issyypslgn rtfsyfsrls leifknlfvd atfradsssk
      541 laydnrteyf psvsaayils dnkwfknnii nfmklkagwg elgnqsglgn fetaasarty
      601 vygllpavnv aplygsgipl ansaliwert aqtdtgveig lfnnrisity dfynkksrql
      661 llnataalen gaetyksnaa emynrghevg vsatilkqtn liwnsqfnit fnknevtkli
      721 gekpvpidfg fatrvdvgqp vgaffglral giyksdteip ramfdqgvra gdvkyeding
      781 dgnidsndrv fmgksqpdff gnfrntfrfk nfdlsaniif vfgqdmynss lrfagisgnp
      841 lfgkfanqtd ywtpeninss lprpvrgfsq swnnqvssrf ienasyirlr elqlgytlpt
      901 smlnigsmtl rlfiavdnlw twtdysgpep evnafgqanv atgtdfftqg mnktfkfgin
      961 lnf
//
LOCUS       WP_101395287             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phycicoccus duodecadis].
ACCESSION   WP_101395287
VERSION     WP_101395287.1
KEYWORDS    RefSeq.
SOURCE      Phycicoccus duodecadis
  ORGANISM  Phycicoccus duodecadis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Phycicoccus.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Phycicoccus duodecadis"
                     /db_xref="taxon:173053"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53434
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresr pgetrvaatp rtveqlvalg yvvfvehgag rlasfddgay rtagadvidd
       61 avwnadvilk inapsddele rlrpgqlvas lmspalepel vqqlaargvt amamdavpri
      121 sraqsldvls smaniggyra vieaahefgs fftgqvtaag kvppakvlvv gagvaglaai
      181 gtanslgavv rafdarpeva eqvesmgarf lridvddagp sadgyakets adfdakaaal
      241 yaeqaadvdi vittalipgr paprllteem vasmkpgsvv vdmaaanggn vagtvagqkv
      301 vtdhgvtilg ytdlpgrlpt qasqlfgtnl vnlmklltpg qdgevvldld dvvqrgmtvv
      361 regevlwppp pvqvsaaapa pgsavatldr vapepkapms gstklalaaa gaalfllvsa
      421 fapapflrhf mvfmlavvig fyvignvhha lhtplmsvtn aisgiivvga llqvgrgsaa
      481 vtvlafvgil vasinvfggf rvtarmlgmf rreeatr
//
LOCUS       WP_101360805            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_101360805
VERSION     WP_101360805.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110361
     Region          15..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklfmfsa galffighsa maqkvkkdta svqdidevvv vgyskvsrss fvgtaskvdm
       61 ssvdnksvst vsqalageva gvrvinpsgq pgreatirir gigsvngnrd plyvvdgapy
      121 sgnisainpd diesmvilkd atataiygar gangvivlnt kkgrgksyvq iesrvgvnts
      181 llprysviks pedyiglswe alynqgffng nadpvsyans rlfsgggina yynmwnataa
      241 qlidpvtkkv rpgierrytp enwereafsp gfrtennfsi gggdaktkyy tnigylkdeg
      301 ysinsqyery tgrlnvshqa kpwlkgdfni gyaysktkng gqssdsgsif wfvdnipsiy
      361 plylrdangn lvpdpyyggn vfdygangrg fgaltnsigd atiskmgnik heinanffle
      421 akftdflkfe trlsgqyynd srdvlnspfy gssasqggri skskqemlsy tflqllrfnk
      481 kwgdhsveaf aaheanfykw qflsaartgl itpdipefnn attqqrgesy tndyglesyf
      541 gqanydydnk ylvsftirrd gssrflknkw gtfasagigw visrenflnn kslpylklra
      601 sygtngdqag vgyypgynvy dpgnmmgsia avfnrngypd ltwesanqaq igldyslfki
      661 kliegtvdvy rkttknlifd srlapstgna vervndgqli nqgiefnlig hiikkkdfyl
      721 dlsingaler nkltkmpidr atglpkvidl avsgygrvag rsmydyymre wagvnpdtga
      781 akwfvnyvda nnngafdage qisslyeyvq snpnakiseg ttevysqatq rfvgksampd
      841 isgaanlsvg ykgfslnvqm lysfggyayd gayaglmang qvggnnwstd ifnrwqkpgd
      901 vtdvprltsn rtgdtnytsv strfltkkny fllnnvtlgy nvpkqmlegl glnalqltls
      961 gdnlwlaskr rgfnpstset ggssmytysp lstftfgvkv nf
//
LOCUS       WP_101443568            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            ramchanderi].
ACCESSION   WP_101443568
VERSION     WP_101443568.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter ramchanderi
  ORGANISM  Pontibacter ramchanderi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Pontibacter ramchanderi"
                     /db_xref="taxon:1179743"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116796
     Region          33..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqertftlfk rllpalllll lccqlavaqs lsvqgkvtde qgqglpgasv avkgttngti
       61 tdgngnyklt vrgqedvlvv sfigytlqel pignrdfini qlqpdqrqls evvvtalgie
      121 reqkalgyav stvsaeeitn arsnnfasal sgkvaglnmv spgsgpvnsv ritlrgdnsl
      181 dpnknnaliv ldgvpmnsgm tssgvgnayg agsgndvpid fgngiadinp ddiesitvlk
      241 gpgaaalygs raangamiit tksgargkkg lgvtvnsnls fndvlrwpdy qyeygqgtgr
      301 afnkegqlyy sygasadgah tggtssafgp rfdgqyyyqy dptlegqsae pqlwrpykdn
      361 ikgfwqtgst ltnsvslegg ndkgsarasi thsknewimp ntgferltaa vslnykiaer
      421 lrltskvnyt qkssdnlpat gynnqsiayf mifqnpnvdl awyapkwkqg keqidqvhpf
      481 ssfidnpyli ayemtnamss ygtvgniaat yelspkfefm lrsgvdmrse drqqrrpyst
      541 anfqrgyyke qnifsyemnt dglftfrdkl gdridfrasv ggnvmnrkyn hvngyvdaln
      601 ipgvykltng vnnpmletfn shkrvhsiya fssfsyddki fvdvtgrndw sstlpvqnns
      661 ffypsintsf ilsdllvlpr qvsfaklrls aaqvgndtdp yktskyygrs efpgsatvpt
      721 tlhndnfkpe ittsyeagte fmlfngrigm dvavyrnltr nqilevpmdp ttgysravln
      781 ggkvrnqgie lalnatpvdl gnliwkttvt wsrnrnkvle laegltdqqv igtggnasii
      841 akdggttgdi ygfgflrapd gqiiytkdgl parpseiqyi gnayadwkgg flnevtyknf
      901 rfnvlldgqy gglvysqthh kmseqgklkh tlrgredgyi igegvvangd gtfspntkqv
      961 slpdyyadyy rranvesnsf dasylklrev rleytlpkqf lsrtkvlqga svalygrdla
     1021 mitkfpifdp etaalngsti lpgvemgqlp tprtwgmnlt lkl
//
LOCUS       WP_101443207            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            ramchanderi].
ACCESSION   WP_101443207
VERSION     WP_101443207.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter ramchanderi
  ORGANISM  Pontibacter ramchanderi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Pontibacter ramchanderi"
                     /db_xref="taxon:1179743"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108027
     Region          38..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkvylfgra sgkaillcfl llaaacqlai aqgaryaitg tvtdartksp lpgvvvkfqn
       61 hniatatdan gqynlsaslp pgnyqltfsf igfkpqslpv tlgdqqsvqv naqiqedivg
      121 ldevivtgts vatskkqlgn aistvsaasl ensvatsvdq alagkvagaq isqnsgnpag
      181 gisvrlrgts tvvgsgdply ivdgviinng spelidlggy aqnrlvdinp ndierieiik
      241 gaaaaaiygs rasngvvqif tkrgvegapk vavstqfrvs evrktldynq ypfrfvnnia
      301 sdltqepvtr ydyqdkifrt aigtennvsv sggsantqyy msgnflsnqg iidnttfkrg
      361 garlridqtl knwisvslga nyvlstseei pngglseayg altgfifsnn finpepvngv
      421 ypstaptail rrtnpleain rfdfgqrtsr figdfqvnlt plnglnisyv lgfdnstqia
      481 tgfipvrntt psydagysrr adrtsyllnn dlnasyrtfl tdwlesttgi ggtiqtekyy
      541 stgitgtqlg piaqvsssga tvvssdgrad inimgffaqq tfgigdrffl tgagrydvss
      601 vfgednrwqf ypklsasyli snesfwqgfr dvipifklra sygqagnlta igaydrytny
      661 npvslpglpg vipstllgnp gikperqvet efgadmsfld grlglefsvy kkdvedlllf
      721 igltpssgfl nqyanigtmt nkgfelmltg apvqtekvsw tstliysrnk nevnnipggv
      781 lpfpggfgqv aavdgyplga fystyfarns dgsllltpag lpqperagrn pengqpsgat
      841 vpkvigdpnp dwtgswvndv svgnrlsfrt qfdavygfdv fnftrrvger dlygglagye
      901 pelrgevpkg tsaalfgife nyiedgsfik lrevsvaydf kpaflggnnv rlslagrnlf
      961 siddysgydp evnaagqtna vrgfdfvevp iprtyalgln ftf
//
LOCUS       WP_101443403            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            ramchanderi].
ACCESSION   WP_101443403
VERSION     WP_101443403.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter ramchanderi
  ORGANISM  Pontibacter ramchanderi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Pontibacter ramchanderi"
                     /db_xref="taxon:1179743"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117775
     Region          27..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgkkllsiil plmvlwsasa faqeravsgk vtdastgtgl pgvsvavkgt ttgiatdaeg
       61 nyqlrvpdan atlvfrflgy vtqemavgnl stinvslktd trqldevvvt algiersers
      121 lgyatqqvqg dnltftkeqn vlgslagkva gvqvtgssga smggtqkiki rgvnsinggd
      181 qplivvdgtp isnanfagad qadygnlaqd inpediesin vlkgpaasal ygirgqfgvi
      241 mittkkgqkg pkkvgvqins afsvekavnf mplqnmyggg ssqtwrtlpn gdkyvdmsvd
      301 eswgpkmdgt pvrqifsfyp qdpeygqltp fvphpdnikd yyetgynlnn gvtitggnen
      361 stfrlsvndt rvegvepntw lnrnnvglsg sldlskklmv stninyarnn aqrpaqgsey
      421 gsrymvqwfq rnvdmkrmkn yryadgtfln wnlrrpsttt geitnfnply wnnpyfeaye
      481 nisndnrerv fgdvgltyqi lpslkvsgfv rndsytqnie trqafggrrv pafttgkyqg
      541 retnyellaq ytkefgdfsl nvnaggnifd trytalymas egglanpgfy nikgsidrpt
      601 tnqtlrrkqi rslygmasvg ykdtyfvdas lrndisstlp pdnnsywyps vsgsmvfsel
      661 idwsplsfgk irasyaqags dlspyettpf ysvgtvyggp ptvntlfvpd nlnnpnvkps
      721 fahsyeagld mrflngrlgl dvtlyqqknk dqilrlpisg tsgyssttin aglirnkgie
      781 vvlsatpiqt slftwntvfn anrnrnmive lhpdidvltq ysttyssvts ylnhyvgqpy
      841 gslvgqayqr dpatgqklig angmplytda thnfgtvqpd atggwqnifk vwkfdlsami
      901 dyqfggqffs rskmlavrtg qdpitvatnd rganvrdale agggvkvegi yapgtkvngv
      961 dvsgqpasny vnaqsyyntv vgrrvyeewl ydasyiklre lrlgytldks mlgrlpfqsv
     1021 gvalisrnva qlwqkapegi dpseistgsq siswyesgmn nsvrsyginl nitl
//
LOCUS       WP_101443862            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            ramchanderi].
ACCESSION   WP_101443862
VERSION     WP_101443862.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter ramchanderi
  ORGANISM  Pontibacter ramchanderi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Pontibacter ramchanderi"
                     /db_xref="taxon:1179743"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114841
     Region          23..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlllsfil alvflqqgma qtrtvtgtvt dqetgqglpg vavlvqgttv gtatgasgey
       61 tinvpegsnt lvfrfigytt vtrnignett invtmsvdtr qlqevvvtav gierterslg
      121 yavqnvggeq laqrsepnvv nalqgkvagv eiisssglpg agtqvfirgi ssatgnnqpl
      181 fvvdgipidn stnftsaptv ggaaysnrgl dinpndiesm tvlkgpaaaa lygsraanga
      241 iiittkkgqa gdankkfevt vtssfnlqnv yglpeyqndy gagtnfrysp nvtdswgprf
      301 gtpgittvpn vpgnpqetle yraypdnvkd ffetgtifdn glqlagagan tryifsanst
      361 nqsgiipnsg ldrfslraag taelsygisv dasiiyante qegslqgnsg tspwftlpfi
      421 prsfdvnnvp ykigpgqqap tlftqlardn prwsvnenfy esevnrtits atlnwkpqff
      481 qdlsftyrvg ldqysdrrre aiafgsinsn gntalnrrgs qiyddifyrq fnqdvfgvyt
      541 kdlnedislr fllgnqinti ntdnrnirae dlitpefynl inhtntnifp tntetrrrlv
      601 glysqlglsy rnwlflelqg rndwsstlal dnnsyfypaa slgfvftdaf dianpilsyg
      661 klrgsyarvg ndagvyltnt vfvnqgfgnn vagisfpfng tvaavtrsnr rgnldlnpef
      721 ttsyeagvel glfdgrtsld vnyffnkttd qifnvdvpgs tgfttftqna geiqnkgwei
      781 satgspftse dgfrwdvnvn ftdikskvvs lapglnqftl ltgagtgaft glspvlipgq
      841 pfgviqssaf lrddqgrfii npntgvpvvd qnpqiiadpn adwwgslgnn fsykgfnlnv
      901 llqyvhggdf ysrqtqiarl rgvleeqtdr erpymfegvi lnadgtsrpn ttqisaqeyw
      961 valnaanefa vfdasvfrlr evtlgyelpa silertpfga asisitgrnl ffyapnlpha
     1021 dpesnqlggn trgfefnspp avrnygvnlr ftf
//
LOCUS       WP_101444402            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            ramchanderi].
ACCESSION   WP_101444402
VERSION     WP_101444402.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter ramchanderi
  ORGANISM  Pontibacter ramchanderi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Pontibacter ramchanderi"
                     /db_xref="taxon:1179743"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111364
     Region          25..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfrhllalaf fllmalgvfa qdlavsgqvt eqatgtalpg vtvrvketnn gtttnpdgef
       61 qirakegevl vfsyigyasq eipvngnags lqvqlqpgnt qlsevvvtga lgikrparel
      121 gtasaqlnta elnqgkvvnp ilglaskvsg lrinlfdskv dpdvqvnlrg irshtgnnap
      181 lyvvdgvpip dinrlnpndi esinvlkgan aaavygsdgv ngvlmittkk gragtqriny
      241 sntttfdnvs rlpeqqtefg qglngvydpl qyqswgprfd gelrpvgpvl pdgsqwqlpy
      301 sahpdgrkaf fntgfttqnd lnfsggdeks tyyfslqdvl tkgiiegdkn rragarfngs
      361 rsfgklstsy nlnyvfnksd vtqsepwstv yrlpvslpfa dlkdwenkph anpnywfstn
      421 qpnpyfnadn qrtvneqqtl tgnielnyei spwinaiyrl glysrntdtr ttvgkftytt
      481 pgrtnipgsv ndatnnfrri nsdfildmhk dfgkfstrll lgnnvrtdds kttnlsasal
      541 vvpglfnqdn rlgqlggqsa irqrrqvavf geltagynny lfltftgrqe avsvlspenr
      601 syfypgvsss fvfsdaidal knnstlsygk vyasynrtgn vvvepyqlqn vysqsngfpy
      661 gnlpgfslgt sdanpnlkpe fvtslevgtq lsffqnrlnl eaayvdaktt dgtiladisa
      721 gsgftsawvn afkasnkiie lningdviqr gdlvwnvgan lthikskvde iyggidqlfh
      781 frqnylivgk pynsylftdy krdpegrviv dpktgnpvsg selyyggtgt ppyqlglnts
      841 lqykgfqlga qfdwrmgavv yteaaarmis dgtsplttqy grepfvipns vietspgvft
      901 pntdvktkgd rnyfanhyat vqsnyavsad ffkmrelsls ytlpmhwldg qklvkeatig
      961 fvgrnlfsiw akdniyndpe fvyaggsseg ymswrhlppt rtfgfnvnva f
//
LOCUS       WP_101445184            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            ramchanderi].
ACCESSION   WP_101445184
VERSION     WP_101445184.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter ramchanderi
  ORGANISM  Pontibacter ramchanderi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Pontibacter ramchanderi"
                     /db_xref="taxon:1179743"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113024
     Region          28..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkvftkqfl lclvlclftg lafaqqkrti tgtvkdeqga pvpfasvqvk gttigattgd
       61 dgsfslsvde gavlvvksig ydtkevrvgt astvavtlgt sssqlsevvv talgierekk
      121 slgyavqevg gerlvesrea nlanaltgkv aglqitrssn gpagsskivl rgnnslvgdn
      181 qplivvdgip idnftgrnnn dywnpgldmg ngladinaed iesisvlkgp saaalygsra
      241 gngvilittk sgrpqeglgi tisstvgyde iftypqlqnv fgqgtegsyn eqsglswgpr
      301 aegqpeknwr gesaplriyd nidnffgkgl yssqnvsfqq qynktsvyts fnrfdnegis
      361 pgvelsrtnl maravshfgk tdrwttdtkv qytksdarnr piggnnpnns fgtlfglprs
      421 idvrdfeqav deegkmiwyg sssqmnpywn grynlnqdvr drfilngsvk ydftdwmsae
      481 ikgggdmhyt taenklyggs pqtpsgrysl nkqnfmetny stlltaqrdn vigrlggmvt
      541 lggnlmsqkf ssisgsagel evpnlfslnn grsnpsvgqd lrehkinsvy gsvqfnwdgy
      601 lfldatfrnd wsstlskenr syfypslsas yvftdmleti ggtapswlsf gklrasyaev
      661 gnslgpyely ntywvgkdpi gnptagrnpi lynpnlrsel vkayeaglea rffnnrigvd
      721 vawyksnatr qlinlpmdpl sgysfrkina gdiqnkgvev mvnaelirnp agfnwnitgn
      781 fsrnrntved lyedievypl ggfddvrvwa vvggeygeiy gstfkrvddp espyhgqlll
      841 tsaglpavge qgvrlgnqqa dalvgvinsl rykglgltfq vdariggeif sgthvsmqrn
      901 gtgaatlrng gresfvvegv iqdpntgayt vnttavtpqn ywnavagvgn lgiteaniyd
      961 atnvrlrnvq lsyalpsgll srlplqrasv gvtatnvwli sshmdgldpe svfatgtnat
     1021 gfengsmptt rsvlfnltlg f
//
LOCUS       WP_101446334            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            ramchanderi].
ACCESSION   WP_101446334
VERSION     WP_101446334.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter ramchanderi
  ORGANISM  Pontibacter ramchanderi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Pontibacter ramchanderi"
                     /db_xref="taxon:1179743"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113662
     Region          37..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkklqcylw gicfllfhft anaqsttvtg tvtaasdntp lpgvtvavkg qprgtntdtd
       61 gkfsisvapt dvlvfsfigm ksaerpvgtn tvinvalqan eqslnevvvt algikqekka
      121 lgyavtevkg atiaqtqren fvnglagrva gvevnassgl pgssssivir gisslsgsnq
      181 plfvvdglpi snnttstgvf assiggtars fenrgvdftn raadinpedi esitvlkgpe
      241 aaalygieaa sgaivittkr gqagkariny snsfridriv rypeiqqkyd rgingftvdg
      301 denigffgap ypsevqfydn vknffddaft qkhniaftgg neaaqyrisg sftdaqgfip
      361 ntgleritls saitaklskr lstdvtfdyt rsdndqafrg aggpllqllr wpstddasny
      421 ltpsgnrrdf apfatavenp ffnvnknifn sltdryrlna tltadvtdwm klvgqagvdy
      481 ytekntivrh pesnagrsfg gifdqavvtn rnltfqyyaq ftaptlfndk lrtdiklgst
      541 vydwntfsaa atgeqfmapn lysinntalt tqraynnltq rrlvgawgsf nasyndilfl
      601 tltgrndwss tlpvqnnsff ypsaglsfvf telepfqgfk nvlsygklra siaqvgkdar
      661 pysirpfyes aqttgggfry gftgpslnlr pemttsyefg telkffndrf gidatyfkkk
      721 svdqivqnlr lsyatgfvlm tfnagemens gielqlngtp iqksnfswdv lmnftknesk
      781 ltklpgdvqe fynsdtwlyg nvrvgsrlgg plttftgydy qrndngdvli npstglplln
      841 tsewvvvgdr npdfnigltn tftyknlsln flldirkggd vynatehylt vtglskrtld
      901 retprvvtgv lrdglentan ptqnnipidl yrnsdywssi yphqnfvekd vnwvrmrdvt
      961 lnyrmptsim qrikfvedln vfvtgtdlfl itnysgldpv angnsaavgg aggsgldygn
     1021 fplprginfg iragf
//
LOCUS       WP_101446837            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            ramchanderi].
ACCESSION   WP_101446837
VERSION     WP_101446837.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter ramchanderi
  ORGANISM  Pontibacter ramchanderi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Pontibacter ramchanderi"
                     /db_xref="taxon:1179743"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115158
     Region          25..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkntftlilf mlfvlgssga waqqrqvsgr vtasdtgegm pgvsvalkgt ttgvstdaeg
       61 nyqiqvpdnn avlvfrflgy qtrevtvgsq stinvnlatd aqelgevmvt algitrekka
      121 lgyaaqgvqa keltehrqpn vlnamqgkva gatisstgga pgqgtkiqir ginsidvnks
      181 neplfvidgv imdnststfg qsadlrgmsn rltdlnpddi esinvlkgga atalyglrga
      241 ngvvvittks gqqgslrvny tgtvgieevn kfpdmqdtyt qgysgvydrn sfwpswgptv
      301 eearrldpth peklynhfkd ayemghqyrn slsfsggtea itflsslshf rhegvlpftn
      361 yenfsarlnt dfkisdkvrs ganfnyinsg gfrynadrfn eslsywsprw dvkdfrkpdg
      421 tmqsygndnp lygaatnrme ddvnrfigsf hvgyspvswl dlsyrvgldn ytddrtrtap
      481 gprgiaderv yedneqgfvy eyttkfrtin ssflatantk fgenfnatfr lghelydrrv
      541 kgfgvegdnl tvydyfdlrn arllrstqtq sdyrlmgifg easvdygnfl fltltgrndi
      601 tstlrkpnns ffypsvslsy vfsdhlqlps vinqsklrls yagigkdase yatssgfapy
      661 nslptgytgf traallgnea lkpeftntfe aglemafldn rlgfdftyyh slskdliini
      721 dvasstgyvr aavnsgkmrn rgvelvlnat pvrtesftwd tklifsanrn kilsireglt
      781 eipyasqfgy vgstvtmkli pgqpfgniyg shwqryygpg eepdplfidt drpivigeng
      841 fpvrapltsq kilgnsqpdw iggltntfty knlsltslfd arvgherynq mgnffsafgi
      901 aeytenrnef kvfegvladg tpntkqvwlg qgigpdgvgy gdgfyrrfhr gvsenfveda
      961 swvrlrsltl sytlpnswfe ktfirnssvg ltgnnlilwt dfsgfdpens atpsgsnvdg
     1021 fagftypavr sylftlnvgf
//
LOCUS       WP_101447299            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            ramchanderi].
ACCESSION   WP_101447299
VERSION     WP_101447299.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter ramchanderi
  ORGANISM  Pontibacter ramchanderi
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Pontibacter ramchanderi"
                     /db_xref="taxon:1179743"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116912
     Region          26..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilmlcll lvsaliheam aqvraitgtv tdastnqplp gvtvlvkgts vgtatgadgt
       61 ytvnvpegsn tlvfrfigyq tverpigtnt tlnvsmgtdt rqlgevvvta lgiernrnel
      121 aysaqevsgd qitrarnenv vnslsgkvag ldirtnntmg gstnviirgy ssltgenqal
      181 fvidgvpvsn annngsnqat grggadfgna aadlnpdnie svnvlkgaaa talygsraan
      241 gvimittkkg aknslniavn sgvtwssidk styvkyqkey gggyfqgfra srdlgsgvap
      301 vvrfqddasy gprfdpnlqv yqwdaidplh pnfgktrpwv aaendptsfy rrglnsnqsv
      361 vvsgggdktt fnlgytrndi kgnlpnstid kdmfnfnasy easerltvsa sgnytrtvgv
      421 grygtgysgn npnqqfrqww qtnvdleeqk dayfrnrqni twnwnssntg piysdnpywt
      481 qyenysndsr dniygyatvn ykitdwmsal grasfnttsd mqeervavgs aglssysryn
      541 rdfnetnfdl mlnfnkdise efkfngllgt nlrrdraesi ftatngglvv prlysisnsa
      601 spvnpptety wrrgvdgifa nasfgfrdty fmelsarqdk sttlpvddnt yfypaagvnv
      661 lfsnlvetsw lshgkvriny aevgndappl siydvydkpt gfgstpifsm pstknnpnlk
      721 perkksmeag ieaeffnnlf gfdftvyken qidqimpvsq taasgftnry vnagevenkg
      781 fevaafvtpi qtgdftwtmn fnfarnrnkv islyedvqnl tlasfqggvs lnaaigqpyg
      841 virgndfvyt ngqrtvgang yyllsdrsdv iignpnpdwt ggfnntvtfk gvslgflidv
      901 rkggdvfsld qwygeatgly ahtaglnakg npsrlpvdeg ggvllpgvke dgtpndiyae
      961 nqdgdgmtpy gyaannyega prawyvydgs fvklrevals yalpqslvgn lgfvkgvdlq
     1021 ligrnlwiih knmeysdpee glssgnagrg yqsgaypavr tygfnvklnf
//
LOCUS       WP_101447958            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            MAR_2010_214].
ACCESSION   WP_101447958
VERSION     WP_101447958.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. MAR_2010_214
  ORGANISM  Aquimarina sp. MAR_2010_214
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Aquimarina sp. MAR_2010_214"
                     /db_xref="taxon:1250026"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112811
     Region          26..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvsklliflt fvlclfssvt laqnkktvsg ivtgedgmpl vgvnviekgt sngtstdfdg
       61 nytvevsdls gilifsslgf eekeisingq seikvslied teqlgevvvt algikrarks
      121 lgysvqevkg ttvlearenn lansisgkva glqivrgsng pagsskivlr gnnsltgdnq
      181 plividgipm nnftgatend ffnpsqdlgn glgdlnpedi esvsvlkgga aaalygsrag
      241 ngvilittkt gktreglgit fsattgfqsi flkpeiqnsy gqgtngvfed qsvsswgpki
      301 egqsvedweg kqvalqaydn ldhyynggfn qtysisfqqq vndatsvyss vnflnddsni
      361 pgatlerlnl ltravskfgk kdnwttdvkv qytnlkaenr plnganisnp yrtvallprs
      421 lniaefemht dpsnnmrwyl dtnavnpyws ieknlsedsr drfllngslk yemtdwlsae
      481 ikagadlytt ntesklysgs plsntgrysl gkntfiekny salltasknn iigefggvlt
      541 lggnlmsnra sglssnsgdl evpnlfslnn ginnatieqi fsekkinsly gslqlnyggy
      601 ffieatgrnd wsstlskanr sffypsists lvftemfnel pewlnfskir asyasvgndl
      661 dayklynfyt igsdpnnntt atsgdvlfns dvkneliksl evgfegrffn srlaidfawy
      721 ksnatnqlie lpldplsgfn seiinagdiq negyelgisg kildnlkefs wdvnlnystn
      781 kntileltde vtkyrlggfd nlsilafrgg nygeiwgtky rrvedpsdan fgkiivdgdg
      841 lplateesfn lgnqqpdami gfsntftykn islgflidar lggeifsgtn lalqeignas
      901 atvvnggred ilvdgvvddg sgnfttntva vspenywtai tgrsgnlgin eaniydatni
      961 rlrnvnlsys lpskwlekie iqkmtlgisa nnvwmikshl ngvdpesvya tstnatgfes
     1021 lsspttrsii lnvsvsf
//
LOCUS       WP_101449969            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            MAR_2010_214].
ACCESSION   WP_101449969
VERSION     WP_101449969.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. MAR_2010_214
  ORGANISM  Aquimarina sp. MAR_2010_214
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Aquimarina sp. MAR_2010_214"
                     /db_xref="taxon:1250026"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117835
     Region          24..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntkinlsvi lmlifctlgf aqektvsgki tedsgiplpg vniliketss gtqsdfdgny
       61 slqveagqtl ifsylgfkte eklvgnettv nmtmyqdats ldeivvtalg isrskkslgy
      121 atqkiesedi skakgvnfvn slsgklagva vsrnnnfggs tnviirgyss ltgnnqplfv
      181 idgtpvsnri nnsrnstagr ggydygnaas dinpddiesi nvlkgaaasa lygsragngv
      241 iiittkkgsk nkglgitins nttfskfdpk tfaryqkeyg ggygasfvqe dvngdgildn
      301 vvdtggdasw gprfdsnllv yqsgaffpen pnyrtptpwv aakndptsif qtgllqstnv
      361 svdgasdkgn frlgftnveq tgilpnslik rqtvdfggsy kltdkvtara kvtytknsgr
      421 grfatgyden svlpglrqwy qtnvdlreqr dayfrlgrna twnlrssart gddpyaprpq
      481 ywdnpywtly enyqtdgrdr vfgnvaltyk vndwfdvlar vtmdrfdeir eervnvssfn
      541 pseynrfngf fremnydmig nfnfditekl nfkgllgmnl trtnrssifa etngglntfg
      601 fyslsnsvnp iappierkss mgvngyyasa sfgydnilfl datyridrss tlpdgkrqfn
      661 ypsistsflf snlftsdwln fgklrlnyae vgnsagvllv ddvytfvngf agqslfslpn
      721 nknnptlkhe tvisyeagle iklfknrfgf ditayqtnsk dqilpldist stgfnskivn
      781 ageienkgye vslfgtpikt ekfewninvn wstyksevvs lldgidnlsl sgtlqedvsi
      841 natvgepygt irgssfkyln gqrvvdengy yvtneengvi gniipdwngg inntfrykna
      901 slsflidmqk ggdiysldht ygyatgifpe tagrndlgnp irdavadggg iiapgvredg
      961 tpntvrtpvn sfdspfiyyr stdeqdvyda sfvklrevif sytlptklld nlpindvvvs
     1021 vigrnlwiid knipysdpea glsagnlqgf qssayptske ygfnlkvkf
//
LOCUS       WP_101450523            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            MAR_2010_214].
ACCESSION   WP_101450523
VERSION     WP_101450523.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. MAR_2010_214
  ORGANISM  Aquimarina sp. MAR_2010_214
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Aquimarina sp. MAR_2010_214"
                     /db_xref="taxon:1250026"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118579
     Region          26..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkssltlfsv lfyffstvvs sqessitgii tdgqtplpga nvmlqetqkg vvtdfdgnfe
       61 iigiqegqys ivisylgfed kvisitihpg eikslgsiel iasaesldev vvtalgieke
      121 kkrlgyavqe vqgdqlttar etnvtnslag raagvqitgg gsgvgstsli tirgegslip
      181 gnnsplfvvd gipisnrtvs nrsegnletd ygngaqdinp ddvksisilk gpnatalygs
      241 rglngvvlit tksaertkgl gisftqnvtf enalripkyq nqygqgagge fafldgfggg
      301 vndnideswg prlngqliaq hdspttsgfr agdfavrprn sdgtfadeii ltpwksnpdn
      361 iedffrtgst ittnlaltgg nefgnlrlsl tnlesegilp ntdydrrtya lngsynlakw
      421 lkvsssvnyv nsksnnrpnn sygtenimyl wvwfgrqidm nslrnywqpg legrqqfnyn
      481 ynwhdnpfft lnentngfdk nrifgnarvd initpslslm lrtgvdyfse lrasrrayst
      541 qrfakgqyre ddiyfkeqnt dfllqynktl nedftmglsl ggntreeenr ykrisansls
      601 vpgiynfens aeplsktqfn dkrkinslya fanfsyknfl flditgrndw sstlpkddns
      661 yfypsvglsa vvsdmvelpe mfsfvklrgg wavvgndtdp yalrntfsfn epfgnfqrvn
      721 asdilrnenl kpeeasstev gadirffnnr lgfdvtyyks tvknqiltlp vsntsgfksr
      781 iinageienr gfevvlnakp iksksgftwe tnvnftsarg eikslveglg tytissnyvn
      841 vlaqvggrmg diygtglvtv ddpnsqffgq vvhnedgfsk rdpnlkklgn ynpdftvgwq
      901 ntftykgfnf gflfdwrqgg eimsrttlig gtsgmmdfta vgretgiise gviqnadgsy
      961 rpndivlsgr dyywwrynrg neeigifdas flklrevrlg ynfpqkilkk tiiksmslsl
     1021 vgrnlalwte nphfdpetis fnggnivlgv edmalpssrs yginlnvtf
//
LOCUS       WP_101461429             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            tegillarcae].
ACCESSION   WP_101461429
VERSION     WP_101461429.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus tegillarcae
  ORGANISM  Paracoccus tegillarcae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus tegillarcae"
                     /db_xref="taxon:1529068"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55796
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalketq dgearvavtp ssaahlqklg hevyvqagag egagfsdddy rnagvtvegs
       61 aadltkavdv vakvrppsda eldgmdegqt lisffypgqn ealmerardk gvtavamdmv
      121 prisraqkmd alssmaniag yrsvieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 asigtatslg aqvyafdvrp evaeqiesmg aefvyldfee qtkdgaetgg yaapsspefr
      241 eaqlkkfrel apqmdvvitt alipgrdapv lwtkdmveam kpgsvivdla aekggncelt
      301 qadkrivsdn gviiigytdf asrmsaqase lygnnirhfm tdltpkkdgv idhnmdddvi
      361 rgatvthdhe itypppkpki aaiaaqkpke kkkeltpeer kaadaatfka etkqqylllg
      421 iggvllllig lvapasfmsh fivfvlacfv gfkiiwnvah slhtplmait naissiiilg
      481 almqigsgsw lvvilsslai lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_101472852            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            lindanitolerans].
ACCESSION   WP_101472852
VERSION     WP_101472852.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium lindanitolerans
  ORGANISM  Flavobacterium lindanitolerans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Flavobacterium lindanitolerans"
                     /db_xref="taxon:428988"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111908
     Region          25..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklngllt lvlalimqis faqertisgt vsdqsglplp gvsvtikgtt mgtqtdfdgk
       61 fqikasppdi lvfsfigmtt kevmatandf nivmeddatq letvvvtalg ikrnpkelsy
      121 stqvvksdel nqakavnaat alvgkvsglq intinsgvnp qtrvvlrgar sisgnneali
      181 vidgvpsals tlselnpndi esttilkgan aaalygsags ngaimittkk grngkmtlqy
      241 nstitfeqvq fipdrqtrfg qgwageldpv entnwgapld gslvqvgpel pdgsirefsy
      301 varknnikdf fnvgttkqng fsisqgdeng nlffsaqdvk tegiipgdly hkntfrlnts
      361 knsgnwsvtg nvsyftdktd iagsltgsdd essfftdtes grslysqllq tpiniplevy
      421 sqgdlqdyft nyaynpywil knsrrisste rfqgsvdlgy kindwfnvly rggvsmlssd
      481 fkhtnnghvf tdgsgredln qgvsdgsnfe rrinsdlmln fdfnltkdit akiilgnnir
      541 dirtkeigir gdnlvvegly nvslrtgelr gvefnsrlrs iglygsaelg fkdflflnvt
      601 grndwssali kennsyfyps ygisfiptsa fpelkgkvln fakltasytk vgnstsayan
      661 qntyvrsvgf pygdltsfnl sstvalaglk pefttskefg lnleffnkri wldasyyisn
      721 stdqiinaaa ssssgatral lnagelqtkg leldlgfvpi qtedfswdfr vsysapktev
      781 ksllpgvnel slggfstagv yavvgqeypi ikgtayerdd qgrviidqat gnpiqssalk
      841 nlgkttpdyi vglstnfnyk gfrlsavfdy rtghvfynei gqmldftgss vqsaqtgrlp
      901 fvfpnssyqt apgvytants iptssggqpf wdsvysniae nyvidatafk creialsysf
      961 pkkvldnspf egitiganar nvfmilpkan rytdpefgft tgnavgvgtv nevpptrsyg
     1021 fnvtltf
//
LOCUS       WP_101493363             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. RO1].
ACCESSION   WP_101493363
VERSION     WP_101493363.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. RO1
  ORGANISM  Variovorax sp. RO1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Variovorax sp. RO1"
                     /db_xref="taxon:2066034"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38899
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeta agetrvavtp etvkklvasg hivrvqsgag vaasvtdaay qtagaeitdq
       61 agafsadmvl kvrtpsdaea aqlkagavvi gmlnpfdavg lqrlaaagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmppswla
      241 rqqievakrv aladvvista lipgraaptl iteemvksmk pgsvivdiaa gkgpvnpdgg
      301 vggncplsea dktvvkhgvt ivgetnlaal vaadasalya rnvldflklv vtkegalkid
      361 leddivtacr vtqdgqvtrk
//
LOCUS       WP_101500904             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            jeotgali].
ACCESSION   WP_101500904
VERSION     WP_101500904.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus jeotgali
  ORGANISM  Paracoccus jeotgali
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus jeotgali"
                     /db_xref="taxon:2065379"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55784
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalketh dgearvaitp astahlkklg hevhiesgag aragfsdaay eaagvtvhpd
       61 aasltaavdv vakvrppsda eiermrdgqt vishfypaqn pellekaraq gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvpparv lvvgagvagl
      181 aaigtavslg aqvlafdvrp evaeqiesmg aefvylefde ptqdgaatgg yaapsspefr
      241 ekqlakfrel apqvdivitt alipgrdapv lwtrdmveam kpgsvivdla aekggncelt
      301 ipdekfiten dvtivgytdf psrmaaqsse lygnnvrhfm tdltpgkdgv iqhnmdddvi
      361 rgatvthdgd itypppppki aaiaaqkpre kkreltpaer reqemqlfrd qtrrqvtllt
      421 vggalmllvg llapasfmqh fivfvlavfi gfqviwnvsh slhtplmait naissiiivg
      481 almqigsggg livvlaalsv lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_101519890             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Kineobactrum sediminis].
ACCESSION   WP_101519890
VERSION     WP_101519890.1
KEYWORDS    RefSeq.
SOURCE      Kineobactrum sediminis
  ORGANISM  Kineobactrum sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Kineobactrum.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Kineobactrum sediminis"
                     /db_xref="taxon:1905677"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40903
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaipreth pgenrvpvtp etakklcrlg aelviesdmg lgsgftddqy ieagatvstd
       61 realfreadm llrlrkpqrd evpmmksgci hisyldpfne hdlvralqeq gvtaismemi
      121 prttrsqkmd alssqanlag yvmvlqaath lprifpmmmt pagtlkparv fvigagvagl
      181 qaiatakrlg arvtafdtra vvaeqvqslg asfleidlge tgetsagyat eltpeqiqkq
      241 rdaqkatiae sdvvittaqv fgrkppvivt sdmvegmqpg svivdmaaet ggnvegsvan
      301 evvnvngvti igkgnlpnev crdashmyan nlfnlvedvw dkeknlfaid fehdilpgcv
      361 ithggevtne tiknilegan
//
LOCUS       WP_101517837             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudohalioglobus lutimaris].
ACCESSION   WP_101517837
VERSION     WP_101517837.1
KEYWORDS    RefSeq.
SOURCE      Pseudohalioglobus lutimaris
  ORGANISM  Pseudohalioglobus lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Pseudohalioglobus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Pseudohalioglobus lutimaris"
                     /db_xref="taxon:1737061"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40651
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaipretq pgenrvpitp dvakklvhmg adlvieaglg vgagftdeey vkagatvssd
       61 rkelfasadl llrlnkptve eigqmqrgci hisyldpfne relisafkea gvtaismemi
      121 prttrsqkmd alssqanlag yvmvmkaash lprifpmmmt pagtlkpasv fvigagvagl
      181 qaiatakrlg akvtafdtrp vvaeqvqslg gkfleidlge tgetaggyak eltpeqvelq
      241 rqaqkdviak sdvvittaqv fgrkppvlvt qdmiqgmqpg svivdmaaet ggnvegsrpg
      301 divewsgvti igtgnwagev ardasqmyss nlfnlvednw ckeqklfqvd fnddilpgci
      361 ithggevtne tiknimegea
//
LOCUS       WP_101525735             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides houyundeii].
ACCESSION   WP_101525735
VERSION     WP_101525735.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides houyundeii
  ORGANISM  Nocardioides houyundeii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nocardioides houyundeii"
                     /db_xref="taxon:2045452"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52635
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigiprear pgetlvaata ktaeqltklg ydvvvesgag qaadlrdesy aeagirvgda
       61 devwssdvvv kvnaptdaei arlrrgatvv slmaparspe lvdklaaagv talamdavpr
      121 israqsmdvl ssmanvagyr avieaahvfg rqftgqvtaa gkvpparvfv vgagvaglaa
      181 igaagsmgai vrafdvrpev aeqvesmggq fvtvdmesev ssdgyakemt aeqeaatalm
      241 ydeearnadi vittalipgr papklitaet vaamqpgsvi vdmaaanggn caltqtgdkv
      301 vtdnlvtilg ytdlagrlaa qtsqlfgtnv vnlfklltpe kdgqmvldmd dvvqrgitvv
      361 fdgetmwppp pvqvsaapaa paaaaaepve pkkpadprrk vfgaalaavl faalatvspp
      421 eflshftvfa lavvvgyyvi snvahalhtp lmsetnaisg iilvggilqv gstnalvsvl
      481 avlavlvasi nifggflvtl rmlemfrkd
//
LOCUS       WP_101532696             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cohaesibacter celericrescens].
ACCESSION   WP_101532696
VERSION     WP_101532696.1
KEYWORDS    RefSeq.
SOURCE      Cohaesibacter celericrescens
  ORGANISM  Cohaesibacter celericrescens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Cohaesibacteraceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cohaesibacter celericrescens"
                     /db_xref="taxon:2067669"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55544
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeqy igearvamtp ssakllqklg ydciletgag vlagfsdaay veagveivsg
       61 adilwetadi vakvrqpqet elkylakdkt lisffnpaan qegmdaakaa ganviamemv
      121 prisraqkmd alssmaniag yrsvieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aalgtsvalg avtyafdvrp evaeqvesmg aefvyldfee eqqdgastgg yasvsspefr
      241 eaqlakfrel apeidivitt alipnreape lwtedmvaam ktgsvivdla aekggncklt
      301 vkdkkivtdn gvtivgytdf psrmanqsse lyssnirhmm tdltpekdgq ikhdmeddvi
      361 rgstvtfege itfpppppki kaiaaqpkke vkqltpeekk aaeaaafkan tlsqikllag
      421 gglfmlliga yapasfmshf ivfalacfig fqviwsvsha lhtplmavtn aisgivilga
      481 llqvgsgswl vmvlsgisil iatinivggf lvtrrmlamf qks
//
LOCUS       WP_101541741             940 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cutis].
ACCESSION   WP_101541741
VERSION     WP_101541741.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cutis
  ORGANISM  Bacteroides cutis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Bacteroides cutis"
                     /db_xref="taxon:2024197"
     Protein         1..940
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104628
     Region          43..939
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiqkklll lalasmsvwt sasaqsakel mdslsisgeq tqvayrkvas kdmlggvstv
       61 nveelmkkny ytstlnnmqg yvggwngsll wgldeylalv dgtprsldtv kpdeiesitf
      121 lkgaqavvly gsraakgavl vttkrgkisp ltidvrantg wevakaypey lgsaeymtly
      181 nealkndgld pkygadeiyy sstgrnpyry pnvdfyssdf iqkaynrsdv taeisagsdr
      241 arfyanisyy nvgdqmnfgq gkynrndrfs vrgnvdvnls ktvsayvnsn vsfynskgtv
      301 ggnywslast frpnrvapli plsmidpnas avwellktsn niidgqyfla gtqndltnvf
      361 adyyaagkss stkrnlqfda gvnidlgkvl qglsfhaqys mdyatsyttk ydnkyatfip
      421 vwgnfngydm ivdltksdtn dektgkqnis gsnsdrtism nahldynrvf gnahqldaml
      481 lvsgfqqtfa geyhrtcnan iglqasynyk hkyyaefsgs lihsarlaeg hrnafspsft
      541 lgwnlaeedf lkgsafdelm vsasgsilnt dmgidyymyk ggydmegssw gwydggslkt
      601 srslrganed ltflkrkels aniraslwkk mitadasffv nsmegaiiss gnlfpsyfdy
      661 sdtqtflpyi nynndrrmgf dfslnyntrf gevdfsagin gtyyatkatk rddsnyenvy
      721 qyrqgkaiss iwgyeclgff nneaeiagap sqtalgggip kpgdlrykdq ngdniidskd
      781 qvalgqfnsp ftmginltak yrnftlfvlg tgniggqnlk kssyywvsge dkyskvvrgr
      841 wteetaatat yprlttgngn nnftnsdfwm yknnrfdlak vqltydfpts mlrgklvnsl
      901 svyvsganll tiskerehfe tnvgsapqtr fynlgvkatf
//
LOCUS       WP_101542039             918 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cutis].
ACCESSION   WP_101542039
VERSION     WP_101542039.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cutis
  ORGANISM  Bacteroides cutis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 918)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 918)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Bacteroides cutis"
                     /db_xref="taxon:2024197"
     Protein         1..918
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102858
     Region          38..916
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnksiklita vlllsssvat aqvadsiqqy rrgmvfdrke attaggtvts erlshktsin
       61 asnslyglip glytmqnant awgdaatmyi rglgttnsrt plimidgfer gieditvqei
      121 esvtvlkdaa alalygvrga ngvvyiktkr gvvgkpvinf nyefnfgtpn rlpkfvdgyt
      181 yaqalneglr ndglsprysq reldafrdqt ypdfypnvdw wdealrdhsy gdnvnfniqg
      241 gsekvryfaq lnwlddrgil kpvsdnegys gqlkyskvni rtnldiqatk ttqvqigmlg
      301 nfaehnrpga tvgnlfgaly qvpsgafpvk tanglwggnd iysnnpvayi sgmgyarsqs
      361 ralyadmnim qdlsaitpgl sasmqigfds ngsywdnntr tfayesavkg wdgeedkyek
      421 lreetalsfs ssvgsivrrf tfgaqanydk mwndhklnat lfysmdktss qrqnksraym
      481 dvaaqahyty knrylldftl sgsaasvldp ddrwgifpsi gagwilseed wlkdngidll
      541 klrasygitg radyemglwk lyfgggngyy fgqtpagasg yaenqiaveg ltyekshkln
      601 vgidlvvwkn lsltidgyyd hrtdilvdgs taissifgms vpkrndgivn sygvevaaaw
      661 ndriadfsyq iggqlsfnrn kiiemneeyr lydyqkrtgq slgqifgyev egiyqsqeei
      721 dqrevkqylg vvrpgdlkfk dqngdkkidk ydavpmgyne tcpelyfgfn lgaeykglgf
      781 maqfqgvshy skylntnsvy rpltgnstis qyywdnrwsq dtpngtlprl ttqgsdnnyn
      841 vnslwvtdas flklrtlely yqmperwmkk agfvkgvkly arghdlfsld gidiadpeal
      901 gtthptmrqy tfgfnlqf
//
LOCUS       WP_101542245             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cutis].
ACCESSION   WP_101542245
VERSION     WP_101542245.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cutis
  ORGANISM  Bacteroides cutis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Bacteroides cutis"
                     /db_xref="taxon:2024197"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108666
     Region          31..981
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvkrtkqcl frhflilagl lvtmaasaqq ftvkgtvrdm sgepiiganv mvkgtsngsi
       61 tdvdgnysvs dvssssvlvf sfigyknqei ackgqreinv vlaedlqtld evvvvgygsl
      121 skkelsssiv qvdkskfqqg amnnpmemlt gkvaglnvvn tasanpnsgs slqirgatsi
      181 tasndplivi dgvaggdirn lssqdiesmt vlkdagsaai ygtrgangvi littkkgage
      241 pgtakvtyds wfgvniaksg pdilspdefr rsrrgtdyga stdwydlllr dfsydnnqyv
      301 sidgstkngy ygasfnykka tgidlksdre eyggrfvieq rvidnrlqln gslnarrvne
      361 twgndgmfdt alsmnptmpl yddngnyyqp ssptgtrnpv aelkdidnng qrmyvlgtae
      421 aklnilrsek hmlntsisys lhyndlkqqy ftpstsgesy wngykgraev tyqkwytqrl
      481 ewlanyaltl ddhsikavag ytyensrwer lqasnsdfay dnikwhdigs gsylnagkag
      541 matgqsvakl igtfgrinyn wknllmasas iryegstkfg kdhkwgafps vslawemanm
      601 gfmkgasdvv kslkprisyg vtgrsdfdsy lslatystkg syfmdgewvk gyapsvnanp
      661 elgweksist nvgidfvfwn rlrgsidwfd rqskdllyny tapqppfvys nilvnvgttq
      721 nrgielsvdg difkgtkvew tsginysygt tklkvlsntm yqasyvelyq kpgvgtseyf
      781 friqeggkvg qfygyeyagv edgkmliytd egekvpvsea dakykryign gtptsylsws
      841 ntlryknfdl niffrgafgf eifnmrkygm glqgcgtdnv lrdaylkdkd ivtgggviss
      901 fflekgdyfk lenvtlgynf tpkpnkiles mrvfvsaknl ftltgysgnd psivsvnglt
      961 pgvdtnsayp tatqlslglt lrfk
//
LOCUS       WP_101542299             992 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_101542299
VERSION     WP_101542299.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111782
     Region          21..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkflytigl altcslgmma qtvngvvkdi hgkplpgvkv srvgemrnns vtdnngvfal
       61 dlekgdyiel nyadvvmkrv rvdgesltiv ldskkdavvd lgfvrrteet qtqsvstiya
      121 dqleksstsm ykvnnslfgl lsglhlsqnv gwhanadmrv rgqgglngaa plilvdgfrr
      181 aldhsileei esvqvlkdga atalygaraa ngvilvntkr gaynsfdidv nyrhgfnlpi
      241 nqpemadayt yamaqnealy ydglplqyts tqlemfkngs nplyypnvdw vkegmrdmse
      301 nnqfnlvvrg ggkrarylam ldyknefgll nenythyser ynsqireydl slrmnldvdi
      361 testkvkfdl fgvitedkrp ntgidaifqn lykvpatafp iktinnnwgs ntifkmnpia
      421 aiadvgyvqq nrrllygdmr ltqdfsmflk glsaelavgy dnsavfeeig sksymyevsy
      481 ladnglpvsq tygtnttmqi sssklssqil rhsveaklny drafgshqva aavvyrqdge
      541 dglernasyy rqnvmgvlgy nynnrymvdf vgnyygtsil lkgdkfrfyp avsagwnlan
      601 eaflqdvsyl dllklraswg ksaidnlsyg lgnhfwtgsg kypfgdgmtd vnglreqklp
      661 irqlnletat kynigvdvrl wnnltataey yydhrtdilc snnkvssilg itapqqnige
      721 vksqgielsl gwndqikdfk yyananwawn gseviengqa yqpydylytk ghkvgqlfgl
      781 eaigyfrdek ditdspeqtf stvrpgdiky kdqngdnrid sedrvaigks tavpemvygl
      841 nlgfeyrgig idmvfngisg ltkqlnvanv hrplrngntn iatwylkdkv rwteqtkdia
      901 nlprlstlsn ennyqastqw iadgsffklr tlnvhytlpq kwsqkmkmdk fqvyaraenv
      961 fsidkidyfn cedialgypd lftvyvglni nf
//
LOCUS       WP_101545020            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cutis].
ACCESSION   WP_101545020
VERSION     WP_101545020.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cutis
  ORGANISM  Bacteroides cutis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Bacteroides cutis"
                     /db_xref="taxon:2024197"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123508
     Region          24..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrllivll clvgvlssvf atdrqvqgvv issednlpli gasvyivaed lkktgsaqaa
       61 igvitdidgk fsisvpsgit rlfcsylgyd vqevklvpnk dryeitlhvs ahmldavvvt
      121 gyqtverrkl taavskldis detigavksi dqalagqvag lavtptsgap gapakirirg
      181 taslhgtqdp lwvldgiple gtdipqqeel sditnmrqss iaglnpadie nitilkdaaa
      241 taiygaraan gvivittkkg kvgkpvvnfs srftytptls ldrlnlmnas ekvgleldmi
      301 rnnyspenkk ggvynilsky nevsafqsgg wdalsvdaqa dinrlkgint nwsdilfrda
      361 fnqeynlsls ggtekvtyyt slgyykengn megvsmdrfn vvgktsykvn rmlklgvslf
      421 anrrkntdyp tdkfgmsnpv yysrkanpyf elydkdgnyn ydydiqnntd tdlkfnifee
      481 rrntslesvv nsfssifdae lrfndklkit sqfgyqldka skeeiadwds yamrslykks
      541 nydqngetky flpqggvqkk yensnsqitw ktmgeyrdsf ndihelevmv gtelrktwye
      601 tlfsagygfd rrtlttkpvv fpdesyassf plhettyken ayvsfystas ysllnrytvg
      661 gsirfdgsdl fgvdkkyryl plysvsalwr lsqepfmqea kwidnlvfra syglqgnidk
      721 ntspfllgky rvesilpgis edmidinsap nkklrwektq svnvgfdfsv lnqainlgvd
      781 yyyrrgtdli alrmlpletg ftsmnvnwas menkgvevsl strnittknf swytifnfay
      841 ngnrvlheni peqqttpgre gypvgaifal ktagvdketg nmmfynpkge kvtlkelyrl
      901 vdewgigias sdvtpaeert fysyigssda pytggfintf tyknwelsan fsltmggyvr
      961 tqptydiiqp dygknynrdv lsrwtpqnrd aafpafmtsa snpeeyywyd akpiwrdldi
     1021 wvkklnyvrl qnlrlgyrvp esltkrlgmn satvsvegrn lfvfgsgynn ymdpesmynp
     1081 fatpvpksvt fslnlnf
//
LOCUS       WP_101571910            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Alistipes sp.
            cv1].
ACCESSION   WP_101571910
VERSION     WP_101571910.1
KEYWORDS    RefSeq.
SOURCE      Alistipes sp. cv1
  ORGANISM  Alistipes sp. cv1
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae; Alistipes.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Alistipes sp. cv1"
                     /db_xref="taxon:1622071"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118763
     Region          38..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 minnmrhkvn ikiallltcm flsafgakis aqsstvytik gvvtdefgkp lsgvvvnset
       61 gkngtstdie gsyiltvddg skdivfsylg ykdkkvaiae ketidaklep dalksdeiid
      121 mgfvqqrrga isgavssvkg tpieaapvss fgaamngfvt nlmvrqnnyv lgnetvsmli
      181 rgasnpqngw qtplimidgv mssynsndvl ryltakeves itllkdastq alygvkgnag
      241 vlvittkrgk kgpvridvsy dqsvqqptis prfyhsweya tfkneatynd npslgktpvy
      301 spvdianyis genrelypdn nwrdmfykkl ttmsraninv tggsdkftyf tqvnfmhqgg
      361 qfkttneryk sgfntnwfny rtnvdikvnk ylssylrlsg nvrrdrapgs dafynaqqgl
      421 yedmywrgan iygpltpavy dqatgemldp ggklvveekn tysiygvlnr mgynkatsvn
      481 insqfgldld lsfvtkglkl ggyiayqtyg ynsltaiqsn elvkrkttdd psvlafetig
      541 ttkdselsyg kgyssyyhld yrayldyqrt fgkhnvqata fiyyqnlska dmgssnnvlp
      601 fntvlsgvea aygydnryfv kvdlgysate qfapdrrwia tpaisgawnl anehfmknvk
      661 wlnefkiras ygrtaeddlq ngrhgylden qfgtggsvpv laystwenkk gyallqaqtm
      721 lkqnygidvg lfngftfsfd yfkermdnml ihatstipsy qgipinnypa tqvgvyenkg
      781 ydlsanyykr inadwsfnvg gwvsyarnkv iykdetelge sysyrrkeeg fplgtsfglm
      841 vdysngngyf nsqeeidrye ctygwnmpsp rvgdlifkdi ngdyiidekd qvpfgyggip
      901 qvfyafnggf kyknlefsfl fqgvartggf esstwhlnye giytrlhega wtperyaagk
      961 eitapalsns qtssdmrnns ynwndraflr lknveiaytl plnvskkisa dkirfslsgq
     1021 nlvtwgrmkn kdiepeyggl ytipayrvyn vgvsvlf
//
LOCUS       WP_101594961             508 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Actinotignum].
ACCESSION   WP_101594961
VERSION     WP_101594961.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52115
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mlvgipkstr pgdplvagtp dtvaklialg yevavetgag eassypdsqy esagarlvsa
       61 qeawaadivl atdapdvsyl drmsrgatli armnpagspe lieelsrrel talaldaipr
      121 israqsmdvr ssmanisgyr avieaashfg rlftgqvtaa gkvppatvyv igagvaglaa
      181 vgtansmgai vkatdvradv aeqvqsmgae fveipvrqes adgyaremta dqanaagvvy
      241 areaaaadiv ittalipgkp apllldseav aamkpgsviv dlaaanggnv agtrpgeivh
      301 tvngvtiigy edlalrlpgq asqlfgqnlv nflklttpqk dgqlvldted divrgilvtl
      361 ggavawpppp ikvsaapaap pappappaap eparpsavry lwaglaaava lwilftapps
      421 mtshfivfml acvvgfyvit svthalhtpl msvtnaisgi ivvgailqlg sghiavtila
      481 aialtiasin ifggflvtar mlsmfkrs
//
LOCUS       WP_101603333            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_101603333
VERSION     WP_101603333.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117888
     Region          24..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnskfylflc cmflctslaf aqtikvtgtv tdkmgpviga timvknstng tvtdidghyr
       61 leasigdilt fsfvgyntve kevksnnpmi nveltddvqa idevvvtaig ikqqkkkigy
      121 ttqqinsdvl natpslnvgs alsgqvagll vanptgifqa psfklrgntp livldgvpve
      181 tdffdissen iesvnvlkgt aasalygsrg kngailitsk takkeglein fstnnmitag
      241 favlpetqhq ygsgsngkye fwdgadggis dgdmtwgpkl nvgtkvaqwn spirdkvtgk
      301 eipwwgdvkg tqyddksrye rvpidwvshd nlkdflqtgl vtnnnisiay kgekaryfvt
      361 gqyayqkgqv pstqmhsggv nfnstfdlaq nlqldanlay nkvvspsypr ygygpknhmy
      421 tivvwmgddv ngkelrkhky vpgqegyrqa synyawynnp yfaaeelqqs enrdvvngql
      481 rlnyqllpnl niqgraalrq ktilqemkvp ktymnygdsr egdykvwndh qtnvdadvla
      541 tytqdltpdi lftlnagssv fyrnyrqeyq stdglivpfv ysikntqgps itdanrneks
      601 irsiygsvnl dlykyayltl tgrndwsstl akgsnsyfyp svaistmvse yvklptfmdy
      661 lkmygswavv stdlspyqii stytkdtnyg snpsisypss lvnyyikpqk ttsweaglst
      721 sffrnrlsfd ltyyhtiden qiidlnisna sgftsrkvng nqyttngwei manvqaiqnr
      781 dfqwefalnw sksikkltei yggqkkfgdl kvgdradafy gsqwqksadg elildengmp
      841 tkdaykqylg hldpnfrmgm qntfrykdft lsvdldgayk gviysvlsek lwwggkhpes
      901 veyrdaqyaa ghpvyvpngv vvtggelkrd idgnvisdtr tyrrnttavd wqqwcqnypy
      961 qayvsskena kfanvfdrsy iklrrvalty nftkllskqs pvkgltatif gnnlavwkkv
     1021 pfvdpdytgd sndggandpt aryigmgini kf
//
LOCUS       WP_101603104            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_101603104
VERSION     WP_101603104.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123065
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrhvfilll sfvgaltsaf aadrqvqgvv issednmpli gasvyikaed lskdgnsptm
       61 tgvitdingk fnisvpegvt rlfcsyvgyd vqeiklvpgk nqyeitlsps aqmldavvvt
      121 gyqtverrkl taavgklnis detigavksi dqalagqiag lsvtstsgap gapakirirg
      181 tsslngtqdp lwvldgiple gtdvpqseil ndisniqqss iaglnpadie nitvlkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs skftymptls skrlnllnsq ekvdlelell
      301 rsnfaygdnk ggvskiisgy gltdaykngg wgaltseaqa dinrlrdtet dwndilfrda
      361 fnqeyslsls ggnervtyyt sigyykengn vkgvgldrln ivaktsykvn rmlkfgaslf
      421 anrrnnktyl tdtyglvnpv yysrkanpyy qpfdangnyv ydfdvqntsd tdlgfnifee
      481 rkntsneeti naissifdae lrfndklkft tqlglqleka skeqiadqes fsmrltrkns
      541 kywdsasqsn kyfipdggvh kayentnsqi twkamgeyrd sfndihelei mvgtelrktw
      601 yetlfsagyg fdrqtlttkp vifpdedrak qfplhkktyk enayvsffst asyslmnryt
      661 fggsirfdgs dlfgvdkkyr ylplysisgl wrlsnepfmq gagkwmdnla frasygiqgn
      721 idkntspfll gkyvvdnilp ggsehmidin sapnkklrwe ktqsvnvgfd fsvlnqainl
      781 svdyyyrkgt dligrqmlpl etgfvstsvn wasmtnkgve vslstrnvat qnfswytnfn
      841 faynnnkvlq eaipeaqttp gregypvsai faiktaglde dgyplfydke gkkvtlkely
      901 rlqdpyglgf tvssdvtpae ergfysymgs gdtpytggli ntfsyknwel tanlsfnlgg
      961 yvrttpsyns infdrgqnvn rdildrwtpe ntdghlpali tsekradeyy wydqksdiyr
     1021 nldiwvkkln yfrlqnlrlg yrlpekmtka lgmgsasvai egrnllvfgs syknfldpes
     1081 mynpyappip ksvtfslnln f
//
LOCUS       WP_101602994             914 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_101602994
VERSION     WP_101602994.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..914
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101627
     Region          41..913
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqhriihip tfvlalflmf ttsvlraqdk pvwladslit vgyatgnkkn isgsvekite
       61 lgmnkdqitn pleairgrvp gltiekgtng paaldavrlr gttsltsgnd pliivdgvfg
      121 dlsmltsiyp tdiesftilk dasetaqygs rgasgvieit tkkgirgktr vsyngsfgis
      181 svyknlemls gsefrnlaqq qgisildkgn etnflkeieq tglqqnhhva fyggtdassy
      241 rvslgfmdrq giilnedmkn ftsnmnmtqh vfddflvcel gmfgsiqknh nlfdlqktfy
      301 saatfnptyp dhrnpetssw dqitnasqit nplawmevkd hdatshisth arltfnllre
      361 lklilfgsyt ynivensqyl ptsvwahgqa ykgtrkmesl lgnlmltykk nrnkhyfdvl
      421 alaelqkety sgfyttvtnf nsdqfgynnl qagairlweg tnsyfeqprl asflgrfnyt
      481 fddryiltvn artdasskfg anhkwgffps vsaawvvsee kfmkrislvd nlkfrigygl
      541 agnqsgidsy ttlnlvkpng vvpvgssqvv tlgnmrntnp dlkwevkrtf nagadlgmfg
      601 nrllfslnyy nsktsdmlyl ynvsvppfty ntllanigsm rnsgteiavg itplktrdme
      661 lninvnvtfq qnkllslsgm yggenisape ykslasldga gfhggynhiv yqmigqplgv
      721 fylphckgli sdgnggytyd iadlngggvs ledgedryva gqavpktllg snisfrykrf
      781 dlsvqingaf ghkiyngtsl tymnmnifpd ynvmkkapgr nikdqtatdy wlekgdyvnf
      841 dyvtigwnvp vskwkkyvqs lrltltvnnl atitgysgls pminsstvns tlgvddkrgy
      901 plartytlgl sinf
//
LOCUS       WP_101603582            1016 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_101603582
VERSION     WP_101603582.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1016
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113140
     Region          24..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktviisifi ilstfttyaq qrdivltgtv tdhqngplpg atirikgtqf gtvtdtdghy
       61 llrgkwkend lilfsfigmk eirvkytgqk vqdaamqedp kaldevviva rqnineldir
      121 aksgvvqrvd verlnskpmi dmslalqgav pgliitntgd lgskpeirir gnssfrkgdm
      181 aneplyvmdg kvissdafmt lnpadiqeik vlkdavacal ygikaangvi eitsqrgnpd
      241 grlttsysfn igittrgrrg vkmmdseekl elerrlqnis tpgyrysedy yrkyyatapn
      301 ldeliaegrq vldslkniht dwfdelihrs iyqrhnlsik ggtdktsyyi stnyakqggr
      361 vpgndtqrft armsldqklg nwgyfslstd agysatdtpn gsthsptdlv yqlnpyetkt
      421 gklisyseks seytlndlms qyhskstdkr ggvsgsfnlr pfkgleidav tgidfllnea
      481 ltlvpstsia eremgiaiae rgkltkeknt ttnissniri tynktfagrh dltiggnmdy
      541 yltqtdnisa tgygvgtqms lnainhsitg arkptassll dktaqlgfgv vmgysfdsty
      601 dlfttykada ssvlppdkrw naawaiglgw tlsrypflkn nkvitllnlk gshgrmanls
      661 gvsasatigt fsystnyygn arllqllgfy ntdlkpeqts ttdfslsief fkrltlglnl
      721 yrretsdall dvpiplsngf ntmkrnigvl rnegyelnaa ikvldtpdwr vslrgslayn
      781 rnkvislyyt drlytsetal tpdyevgkay nmlyglkslg inpitglpvf qgadgseisp
      841 tqnparenfi vlghstppys gtfnlnfsyr nfdldmdfyy vfggikpyny syirsadsan
      901 knaiqkqlen mwfhrgdegk iyhspfyisp anaslqqpnt etvgksdylk lamlslryrv
      961 phtfleknch fikyaniafq asnlfmitpy kesdpetgsl agamqpvlti nlsltf
//
LOCUS       WP_101604138            1132 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            fragilis].
ACCESSION   WP_101604138
VERSION     WP_101604138.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides fragilis
  ORGANISM  Bacteroides fragilis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Bacteroides fragilis"
                     /db_xref="taxon:817"
     Protein         1..1132
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125920
     Region          52..117
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          132..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkaipchk agritsffll isifllipsi ttpvhaakty aqqtvftlha adktvkevle
       61 yveknsefvv lyskdllpil qkkvsvsidk qnvesilnil skevglkyti ndrqititka
      121 ptetpqqekk tkitgqvlde ngegvpganv tikgnnslga vtniegnftl mapenstlia
      181 sfigytpvei qlkgkkivvf kltpdaqale evvvvgfgtq kkasvvgavq sikpaelrvp
      241 ssnlstsfag riagvismqr tgepgsdgan fwirgaatfs gttdplifid gvevsagdmn
      301 aipseaienf silkdasata lygargangv ilittrsgkd lerarinvri dntftaptrt
      361 lkladavtam qlrneailtr npdgtpafsa dkiqgtlenr nqyvypnvdw fdymfkdysm
      421 nqsanlnvmg gtkkvdyfis asinndngml kkdpnntfdn niqnlrysfq snvgawltss
      481 tkvnvrinsq ivnyngpsts mddlykyvme apsmyfapvy pninnedhti fgnksggpig
      541 aggfsiyrnp yasmvqgssk qsaysintaf eleqkldfit kglnfkalvs fknwskttvn
      601 rsfspyfyel qnpqqqedgs yiydynsisk grtaletsts ttgdrlmnlq atlnyqhtfd
      661 dkhdvgamlv ylqreynlnn pdnnyyntlp krnqglagrl tyaydgryla efnfgyngse
      721 nfekgsrygf fpslavgyli sneqffeplt kvisnlkira syglvgnadi gsnrfpyltk
      781 vdlsgagfvf gdqwqtssng atittygaek vtweigkkyn vgfdlglfnk lslnvdffre
      841 drkdiflrrn tipaesgitg dlrpygnlgk vrnqgvdmsl dynhavnkdf misakgtfty
      901 aknqyveide pdyefsymsq vgrplnqykg yialglfkdq eeidnspkqi ltgvvqpgdi
      961 kyadlnndgk idgndqtyig npelpqisyg lgvsiqykkw dasiffqgvg krsimlsdih
     1021 pfggesygvm qfvadnrwte anpnseamyp rltngknnnn npnstywlrd gsyirlknve
     1081 lgysykflra yisgqnlltf skfklwdpel ytsnglkypt qimgsiglqf tf
//
LOCUS       WP_101609568             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis sp. BJA-103].
ACCESSION   WP_101609568
VERSION     WP_101609568.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis sp. BJA-103
  ORGANISM  Amycolatopsis sp. BJA-103
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Amycolatopsis sp. BJA-103"
                     /db_xref="taxon:1911175"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38370
     Region          8..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maaeneqltv gvvretgqge rrvalvpkli ervsgrglrv vvepgagaga lladevfeqa
       61 gavigdpwda divvkvapps aaevaklkqg tiligflnpr adpdgiaale sagvrafave
      121 aiprisraqa mdalssqssv agyravllaa ekltrffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgaqttgydv rpevgeqvks igakflalgi eaageggyar elteeekaeq
      241 qrrlteaitr fdvvittalv pgrkapilvt adavkgmpag gvvvdlages ggnceltkpg
      301 eeivehdvti csplnlaaem pahsselyar nvtellellv dkegklaldf sdeivagacv
      361 agaresekqg ge
//
LOCUS       WP_101631078             891 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides thetaiotaomicron].
ACCESSION   WP_101631078
VERSION     WP_101631078.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 891)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 891)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 891)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..891
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         <1..891
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..890
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 qqvkgdeltn ikdanfinal sgkvagvtin assagagaaa rvvmrgtksl ekndnalyvi
       61 dgipmfnvns gdnaggtmnk qpgsnsvadi npediesmti ltgpsaaaly gsdasngvil
      121 ittkkgtvgk vqisysnsts fsspmmmpkf qniygnrege lgswgslmdt psnfdpsdff
      181 ntgmtemngf tlttgteqnq tyasvsttns tgilpnnayn rynfsirnta kfcdnklsld
      241 lgaqyiiqnn knmvgsgqyf nplvslylfp rgenfqevqm yerysearnl mvqywpesif
      301 gtdldmqnpy wimnrmqnel skrrymfnas lkwditdwvn vtgrvrvdns dsdsyekyya
      361 strgtftess skgyyghtkq ndrsvyadvm asinknffdd klslnatvga sindiqedam
      421 ylkggleqip nffhygninv ntskrneskw hdqvqsvfas aelgwnhqly ltvtgrndwa
      481 sqlaftskgs yfypsvglsw lvsesvklpk aisylkvrgs waevasspnr yltqmqytyn
      541 eqtntyeypa shyntnlkpe ntkswelgvn akflgnrinl dmtfyrsntf nqtfyvdasa
      601 ssgyknnivq tgniqnqgie lalgysdtfd kvkvstnfty tlnqnkivsl angainpetg
      661 eaiemeyysk gtlgtsggpt lrlyengsmg diyinqrlrq spngyiwkdp sngslaient
      721 eyrkvgsilp kyylgwngsv awkgwnlgfa ftgrfgglvv sdtqamidky gvsessavar
      781 qaggvwvgds kvdaeeyysk vttavgtyyt ysatnirlse lslsyqlpkt wfknhvnmtl
      841 gltgknlwmi yckapydpes tssvtsnfyq gvdyfqqpsl rslgfnvklt f
//
LOCUS       WP_101654730             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neptunicoccus cionae].
ACCESSION   WP_101654730
VERSION     WP_101654730.1
KEYWORDS    RefSeq.
SOURCE      Neptunicoccus cionae
  ORGANISM  Neptunicoccus cionae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Neptunicoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Neptunicoccus cionae"
                     /db_xref="taxon:2035344"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55918
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtpkeif enearvamtp dsarqlqklg yecvietgag ekarfsdedy keagvevvkt
       61 aaalyksadi iakvrppeei eikrlrkgqt lisffypgqn aelmdaankk gahviamdmv
      121 prisraqkmd alssmaniag yravmeagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaatslg aqvyafdvrp evaeqiesmg aefvylefee dakdgaetgg yaapsspefr
      241 eaqlakfrel apemdivitt alipgrdapk lwtadmvamq kagsvvvdla aerggncdlt
      301 vpdekivsen gvtivgytdf psrmaaqsst lyatnirhmm tdltpekdgv vnhnmeddvi
      361 rgatatfege itfpppppkv kaiaaqkpka evkeltaeek kaaeaaafrt etrnqvtlla
      421 iggalilgvg lvapasfmqh fivfvlavfv gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgsf lvillaalsv fmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_101680708             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus pauculus].
ACCESSION   WP_101680708
VERSION     WP_101680708.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus pauculus
  ORGANISM  Cupriavidus pauculus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Cupriavidus pauculus"
                     /db_xref="taxon:82633"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39209
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipletr agetrvaatp etvkkyvaqg hqvtvqtgag vrasipdaaf eaagarvgsa
       61 adalgaelvl kvrapddaer gqmkpgsvlv gmlnpfdven narmasaavt afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfvtdee reiaqgvggy arpmpadwmr
      241 rqaelvhqra tqadiiitta lipgrrapvl laedtvkqmk pgsvvvdlaa aqggncpltv
      301 adevverhgv vlightnlas mvgadasaly arnvldflkl iidkdgrytl nleddivaac
      361 lmckdgqvvr qqaa
//
LOCUS       WP_101686684             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Dermabacter hominis].
ACCESSION   WP_101686684
VERSION     WP_101686684.1
KEYWORDS    RefSeq.
SOURCE      Dermabacter hominis
  ORGANISM  Dermabacter hominis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Dermabacter.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Dermabacter hominis"
                     /db_xref="taxon:36740"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53711
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipretl edqplvaatp dtvrklrklg ydvavergag erasyldaay aeagaeivge
       61 evwqsdiitt ldtppremre rmlagavlis rmapgrnpel idelkehrlt alamdavpri
      121 sraqsmdvls smaniagyra vieaasnfgr lftgqvtaag kvppanvyvi gagvaglaai
      181 gtansmgaiv katdlrpeaa eqvesmgaef vpieakteks edgyakemta dqakaaaely
      241 srqsaeadiv ittanipgrk apvlltaadv qnmkpgsviv dmaaanggnc eltrpgevyq
      301 tengvtivgh tdlagrlpgq asqlygqniv nlmklvtpqk ngvmmldfed tivrgitvtf
      361 ahdgqadvlw ppppvkvsaa papapeaapa paeapeakks hagtiaaiig gilgvalvla
      421 spfqvaeqym vlmlaivvgy yvitsvthsl htplmsetna isgiilvgai lqvgsaniav
      481 ailsfiaivi asinifggft vthrmlsmfs reg
//
LOCUS       WP_101687675             529 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Corynebacterium].
ACCESSION   WP_101687675
VERSION     WP_101687675.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..529
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54570
     Region          1..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigiplepd pqqtivaatp etvgklvklg yevavqadag laakftdady esagativde
       61 svwhsdivvt ldtppeqfra llndgamlis rlapgrneel veelaqrnit alamdavpri
      121 sraqsmdvls smaniggyra vveaasaygr lftgqvtaag kmppatvyvi gagvgglaai
      181 gtansmgavv katdlrpeag eqvesmgaef ipipaaaeks edgyakemtn dqaaaaakly
      241 seqsaqadiv ittanipgrr spllltaadv aamkpgsviv dmaaagggnc emtvpgktiv
      301 tdngvtiigy tdlagrlpaq asslygqnif nlfklitpek dgspvlnled eiirgitvtk
      361 arpqngagat gaeilwpppp ikvavtpaap lqeqqahqaa leenapekvs fmgsglgski
      421 alglmallai vvmlsaphsv sanfmvltla ivlgfyvisa vtprlhtplm setnaisgiv
      481 lvgailqvgs snllvsglaf aaivvssini fggfavtdrm lgmfvkeea
//
LOCUS       WP_101688468             920 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pseudodysgonomonas massiliensis].
ACCESSION   WP_101688468
VERSION     WP_101688468.1
KEYWORDS    RefSeq.
SOURCE      Pseudodysgonomonas massiliensis
  ORGANISM  Pseudodysgonomonas massiliensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Pseudodysgonomonas.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Pseudodysgonomonas massiliensis"
                     /db_xref="taxon:2040292"
     Protein         1..920
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101714
     Region          41..919
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikhtfirsc tillllpiii lgandaaaqv qtspkdsivd leevmvigya tgslskvsga
       61 idrisevdmn kgltvsplda irgriagvni spanngpavm ssvrvrgtts ltggndplii
      121 vdgifgnmnt lssiypadie sftvlkdase taqygsrgas gvieiitkkg sdkpfnisym
      181 gnisvddvak nlkmlsgney rqvaksnnfe iadlgantnf lkemtrlgii hnhhlalssg
      241 tptfnyrmsa gfinsegvvk nnnsknytak ldihqkafnn rltidagmfg svlkqnylfd
      301 fqktfysaaa fnptypnhrn kttgkwdqis yasqitnpla wlevdddeen slinahanvk
      361 ffitddlkvt afgsytynsi ensqylpttv wghgqaykgl kktehlmgni vlnykkyfgd
      421 hyidlvgmte yqrekltgfy ttatnfstde fgynnlqaga lrlwegtnsy fedprllsfm
      481 grvnyvydnr yiltlnargd gsskvgknnr wgffpsgsva waihkeefmk aypifnelkf
      541 rmgyglagnq naidsyvsqq lmkpngvtpv ggsptvtlst irnanpdlkw evkktfdvgi
      601 dlalldnrvf fkadyynskt tdmlytyavs vppfaynsll anlgsmrnsg lelslgiapi
      661 kqkdielnin anvtfqsnkl lsldgeynge qmntpkyinv aelngagmhg gynqivyhiv
      721 gqplgvfylp kstglvegtd gknrygiedl ngggvslddg edryiagqvt pkvlmgtnig
      781 frykdfditm qingafghki yngtsltymn mnalpdynvm kkapkanihd ltatdywlek
      841 gdyvnidylt lgwnvplknl ntdgkalrlt fsvqnlatit sysglspmin nqvldqtlgi
      901 ddkrtypvsr tfsfglsfkf
//
LOCUS       WP_101688949            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pseudodysgonomonas massiliensis].
ACCESSION   WP_101688949
VERSION     WP_101688949.1
KEYWORDS    RefSeq.
SOURCE      Pseudodysgonomonas massiliensis
  ORGANISM  Pseudodysgonomonas massiliensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Pseudodysgonomonas.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Pseudodysgonomonas massiliensis"
                     /db_xref="taxon:2040292"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117223
     Region          38..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkenlkerr nghliqsfil gilmfmaipg faqqkvaiqg vvfdsnnepv iaatvqekgi
       61 atsgvmtdid gnftlnvtnt natlvvtyvg mktteinldg ktsititmqe sdvvlddvvv
      121 talgiersrk slgyalqevk gadlletrda nvanslagki agldirqsps gaggssrivl
      181 rgnssltgnn qplivvdgvp idgstgsdnd dqwgeqlvdr gsgmadispd diesmsvlkg
      241 paaaalygsr agngvimikt ktgkgtkglg vsysmnltid dlmttpkfqn qygqgtqgei
      301 nttkdhgrfs wgapisgqty tdyvgreliy dkggadmkdf lqtghtwtns vditnatdks
      361 tvrlgvshlr nkgvvpnnef nrtsatlrat sqlskklsvd akgsfvhqnt enmlrlggnh
      421 dnifsqflvm prsvnlnnlr lgdngyhaty dhivdpyawp agtqmvesse nivgkpvsyv
      481 yplsgntanp yfsaynnttv nrrnrfmgfa sakyeftdwl nlqvrygidy istryeniqg
      541 tgtvfstyad vrgnimtdnn egyemntdfl ltfnkrfvnd rlgilasagg nmmysrfdgi
      601 yatanglhve yfysmmngmd vrssqshtrk klnslygtas lswddayyld vtarndwsst
      661 lpqknwsyfy psvgfswlfs etfasklgpi nygkirlswa qvgndtnpya tipyanmsgg
      721 nvlpslvkin pdlksetvts yevglelsaf nnrlgldfsf ynkdakdqif aipvspttgy
      781 fsrminagki rnrgielvln gkpvvskdfn wnvifnfskn tneivrldnr idefllshss
      841 yskvlrivak eggkfgdmyg tkylrndagq lilgsdglpq atqemhylgn aspkwmggli
      901 nqfsykgidl afqidirygg kvymgslrqg aeagtldfta anrekgsiel hgvnkdgeav
      961 tshtqaqeyw arvaggygpt eewvkdatnl rlrelsigyn lpksvlsktf irsakisfvg
     1021 rnlwmihskv kgfdpeagys tgnaqgfeyg smptlrsfgf nlnvtf
//
LOCUS       WP_101689485            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pseudodysgonomonas massiliensis].
ACCESSION   WP_101689485
VERSION     WP_101689485.1
KEYWORDS    RefSeq.
SOURCE      Pseudodysgonomonas massiliensis
  ORGANISM  Pseudodysgonomonas massiliensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Pseudodysgonomonas.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Pseudodysgonomonas massiliensis"
                     /db_xref="taxon:2040292"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112637
     Region          29..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyikigivl calltffvlr vdaqtvmkid ikasiidhng dpvigavvsa edgneqaltn
       61 idgvfvmqvd kgsklkieal gynttyanaa adltqiilsq vaekelvqva yrkmykedvl
      121 ggvssvsivn nldknyttsa ldgmqayigg fqgnlwgmdg slilvdgipr daefvkpsei
      181 eqisflkgas atvlygsraa kgviyittkr gkaeeqrinv rantgfdvvk rypkylgsge
      241 ymslynearq ndglealysd etiynyasgn npfrypdvny yssdylkkay ntsdvtaeit
      301 ggnerakfyt nisyaysggl ikfgeaekdn strlnirgni dlklneyiss rinaaaifyn
      361 grsahgdywa sastsrphrf aplipisyie qddenswlmi ensnhlidgk yllggsqldq
      421 tnvfadiyas gynkyvsrqf lfdagvdfkl dnilkglafh ttfaidytss ynqsydneya
      481 vyeaswnnys gkdligkltk ygedtksgvq nikdswsrqt iafsgyfdyk ttiednhnit
      541 amliangfqq sesavyhkvs nanlglqlgy nlkkkyyfdf sgavihsakl psgnrqafsp
      601 tfslgwkise edflsnssav dflkltasag ivntdldisd yylyesiysq tdgawygwld
      661 gasnqstdsk rgenpnltfa krkeitfgve gslfdrllsf dlsffanrmt gkviqastiy
      721 pnyfvtgwps ssflpyinfn ederigidfa mnfnkrigav dwtlgvagty nkskaitrde
      781 lyedkyqnra gkpldglwgl ksaglyqsde eianspshsf gevkpgdiky idqnndnvid
      841 skdevylgra gwngspftfg inltakwrdf tffalgvgef ganamknnsy fwvqgdgkys
      901 dvvrgrwtee tkdtatyprl tslnsdnnfr ssdfwlyktd rfnlakvqit ydlpkqifhk
      961 tfvrglsvyv sganlltiak erkiletnyg tapqtrfynf glkamf
//
LOCUS       WP_101689536            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pseudodysgonomonas massiliensis].
ACCESSION   WP_101689536
VERSION     WP_101689536.1
KEYWORDS    RefSeq.
SOURCE      Pseudodysgonomonas massiliensis
  ORGANISM  Pseudodysgonomonas massiliensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Pseudodysgonomonas.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Pseudodysgonomonas massiliensis"
                     /db_xref="taxon:2040292"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123780
     Region          26..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkvvftil cfllslgyaf aqtqnikglv ldennepiig atvsvkgstt gtltdadgef
       61 sinipsnvkt ltfsfigyet qdvavkqnmr itlkpssqql deivvtgitr tdkrlftgsa
      121 dklsadkiml dgitdvsrsl egrsagvsvq nvtgtfgtap kirvrgatsi fgnskplwvv
      181 dgviiedvmd vsaddlssgn aetlissaia glnaediesf dilkdgsats vygaramagv
      241 ivvttkkgra ghskinytge ftyrvkplyn efnitnsqeq mgiyqemyek gwlnhaeisn
      301 asssgvygkm felinrgell ntydakkeyl rqaeyrntnw fknlfndnvm hkhtvsltsg
      361 tdksnyyasi stlqdqgwtk qssvklytan lnatynifdn lsfnlitsgs yrkqrapgtl
      421 gseldpvsge irrdfdinpy syalntsral dlntfykrsy adfnilheld nnyldlnvtd
      481 irfqgqlnwr pitglnlsvl gsvrysante ehhilddsnq asayramptt iirdknplly
      541 tdpdnpyaip isilpeggiy krtdrrllay dfratanysk vfdethilnl dggmeyntsq
      601 rrqtwfrgwg mqyslgevpy yayqvfkkgr ednnqyyemk nilnnqvaff gvatysykgr
      661 ytlngtlrye gtnklgksss arwlptwnig avwniheesf fkaleptlsh lslkssyslt
      721 gdrgpdfvtn sravirsftp wrpfadvges gtyiqylens dltyekkhef niglnigfln
      781 nrintevswy krnnydligy mfsqgvgges lkygnvaeme sdglelsist knittkdfsw
      841 stdfiyshtk nkvtdlmsrk raidlvsgtg faregyshrs ifsyqfvgls eegfpivine
      901 egkeatsnin fqeidnldhl vysgtadptd fgslgntfry knfnfnfflt yswgnvvrld
      961 pvfkdsytdl tamprefknr wtvpgderyt nvpviasarq vkndreleta ynaynystar
     1021 iakgdfirlk evsltynfde kvlktlklsn mslklqatnl fllyadkkln gqdpeffntg
     1081 gvaspvprqf tltlrlgl
//
LOCUS       WP_101690874            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pseudodysgonomonas massiliensis].
ACCESSION   WP_101690874
VERSION     WP_101690874.1
KEYWORDS    RefSeq.
SOURCE      Pseudodysgonomonas massiliensis
  ORGANISM  Pseudodysgonomonas massiliensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Pseudodysgonomonas.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Pseudodysgonomonas massiliensis"
                     /db_xref="taxon:2040292"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123762
     Region          6..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqsngfvakg tivdetgepa igatisikgt tvgvisdvdg kfeikvpsnk ttlvfsyigf
       61 ntkevlasen mnivlesnsq vltevvvtgi tkmdkrmftg attkltnddv kidglsdisr
      121 slegraagvt vqnvsgtfga apkirvrgat sifgsskplw vvdgviledv eevnaddlss
      181 gdaltlissa iaglnaddiq dfqilkdgsa tsiygarama gvivvttkrg raghhsvnyt
      241 gefsyrmvpt ysnynimnsq eqmgfykelk dkgwlsfaet ytrknsgvyg hmyrlldqyd
      301 qtsgifglpn taeaqyaylq eaemrntnwf nelfnhnvsq nhsvsissgs ektqfygsls
      361 amldpgwtmk nkanrytanf natfnlaknl slsilsngsf rkqtapgams qendpvfgev
      421 trsfdinpyn yalnasrtld antfytrnyt gfnikhelnn nymdlsvsgf kfqgevkwsi
      481 ipglewsnig aikydaaste hhikdasnqa nayramgnsl tqtnnpylyd dpdypyqhpv
      541 silpeggffq ktdnkmfafd frssifftri fnedhylnin agaefnsydr eknwvmqwgr
      601 qyelgdiayy pyeyfkqgne egskyytiln sysrkvgmya nptysykqry tltttlrydg
      661 snklgkskat rwlptwnigl swnaheedfm ksiqktlsyl kfrgsysltg etgpdyinna
      721 tmmvmsntpw rptsslletg lqigygnsle akygiphlag fqnqdltyek klelnigvdf
      781 glfdnrvsvv tdwytrknyd ligpvftell gmkygniatm kshgvevsin trniqnkdfs
      841 wnttfnfsyn qtkitkllsq ssilklvrgs gyakqgyadr avfsipfagl nsegiptfyn
      901 engeitindv nlqevrpdhq tflkyegptn ppysgslgni lnyknfrlnv fltysfgnvl
      961 rldpffkysy sdldalpkef knrwtmpgde qfttipvvas khqyaensyl rtaynlynys
     1021 teriakgdfv rlkelsltyt fdkkilpksf nnlslklqat nlfllyadkk lngsdpeffa
     1081 sggvalpmar qftftlrlgl
//
LOCUS       WP_101690189            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pseudodysgonomonas massiliensis].
ACCESSION   WP_101690189
VERSION     WP_101690189.1
KEYWORDS    RefSeq.
SOURCE      Pseudodysgonomonas massiliensis
  ORGANISM  Pseudodysgonomonas massiliensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Pseudodysgonomonas.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Pseudodysgonomonas massiliensis"
                     /db_xref="taxon:2040292"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116151
     Region          29..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvnkksqk ipfllmlmlf tcisasaqfq vkgkivsand sepiigvaik engtnngtit
       61 dldgnysinl qsgnatltvs yvgynsqtik vdgrntidir meekteilde vvvvgygiqk
      121 ksdltgaias vngddiknlt tvdaaaalqg kaagiqilnt sgapgsgasi rvrgyssnse
      181 nlgpllivdg lkvdniqyld psmiesievl kdaasaaiyg aqagngvvli ttktgngang
      241 rpkiiysfka inqslgktpe lfgakdwiky kelsgydmkt ltqsygvdyd npqetdwvne
      301 vfgsswatqh sitfqdgndk ghfftsvnyi nndgivrgkk dtytrltgql nadyklydwi
      361 kvgtntsiek watrdithqs aygsmltpal lldpltpvyw dsvddfttsm qeqyavnpst
      421 ilvapngkyy atskfqmddn gnpllqrdrr hvknsgitvr gtafldltpi dgivmtsrls
      481 yrigqhnshd yaepyymngq akatdysisa aannsryyqw enfvnfnrtf fekhnigama
      541 gmsytdyasd nvsasatgtg gnkiltgdad nfkfldfvns aetttkninn lpsdvrslsy
      601 fgrflyaydn rynlqfnyra dafdtsklpa dkrwgkfpsv avgwnisnek fikdnistda
      661 lsflkfrasw grngnvnvlg nypyvspisy nsawyqygdn palhygsyps glanpnlkwe
      721 tseqldfgmd mrflnnrlgi sldyynkdtk dllisinpvp evytnstivn agkinnrgfe
      781 veaswkdnig dlkysihgnl stlknkvtyl ydditridsn qggvdgtnnm vrssfeeghs
      841 iwyfraydya gvdketgspl frnhegnivs sseltdqdmt digssiptlt ygltinleyk
      901 gidltifgtg vagnkifnvl yrpdspmrns lkyymdnaws etnknasmps vasvaqdrff
      961 wsssasmfng syfkikqiql gytlpktftk kmavkelrff vslddfftfs sypgmdpeta
     1021 ttsnnggggy digtyptmkk ctfgasiaf
//
LOCUS       WP_101690935            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pseudodysgonomonas massiliensis].
ACCESSION   WP_101690935
VERSION     WP_101690935.1
KEYWORDS    RefSeq.
SOURCE      Pseudodysgonomonas massiliensis
  ORGANISM  Pseudodysgonomonas massiliensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Dysgonomonadaceae; Pseudodysgonomonas.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Pseudodysgonomonas massiliensis"
                     /db_xref="taxon:2040292"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112826
     Region          38..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mwktiksvfs tfsvilylta vigaflmspt anaqeakftv qgtvqdanep iigasvlikn
       61 ttagtmtsid gtftlggvkm gdiivisyig yepqeisftg qndlnitlvp kstemnavvv
      121 tamgikrqek alaynvqqit nedlttvkda nfmnslvgkv agvtinssaa gagssarvvm
      181 rgvksltgsn salyvidgip mfepegdegg lfvdqagadp iadlnpedie sinmltgpsa
      241 aalygsaaaa gvvlintkkg qegktsftys nnttfstpyi kpkmqnryvn avgqleswga
      301 qktsnydpfd ffntaaniin sitfstgtsk nqtfasaaat nstgnlpntk ynrynfsirn
      361 tanflndklt ldlgasyiiq ndrnmtgqgq yqnpllplyl fprgdnfdei rnyerynetf
      421 gfydqywpyt nagislqnpy wianrnvrdn skrrymfnat lkyqivdwld vtgrvrvdnn
      481 tnrytykkya gtdrlfagla ggyddmqtts gdiygdiman vnkrvgdwti aanvglsind
      541 srsetighsg qlkdsnpnlf silnlnheik ykpkqwnari qekaifanve igwksmlymt
      601 vtgrndwpsq lagskessff ypsvglsgvv temvklptwv sflkvrgsfs evgtsfaqrl
      661 pnptyaysee srsyallsky plydlrpekt qsweigmnsk lfqkisldlt yyksntknqt
      721 feiplgsssg wksafvqsgd iqnqgiemri gysdqwgdfr ystnynftwn qnkikrlang
      781 vnnpvtgepi qmeywqqgnf gnldaqivlt eggtlgdvya qsilatdang diwvdpqsga
      841 ikteqleite kklgsilpkf nmgwshslgy kdielgvtfs grvggivlsg tealldqygv
      901 skrsadardn ggvpinygkl daktyyqtls gsgsyytysa tnfrlqelsl nytlpskwfn
      961 dkmrmtvgfv gknlwmiyck apfdpelsas ksnnyyqgyd yfmlpstrni gfnvklqf
//
LOCUS       WP_101710030             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chromobacterium sp. ATCC 53434].
ACCESSION   WP_101710030
VERSION     WP_101710030.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium sp. ATCC 53434
  ORGANISM  Chromobacterium sp. ATCC 53434
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Chromobacterium sp. ATCC 53434"
                     /db_xref="taxon:2059672"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39567
     Region          1..337
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqivipaerl agerrvaatp dtvgklvgag havgvergag laaaipdaay aaagaaives
       61 rqdllagadv vlcvrtpeaa dieamragaa ligmlsphhn pllpqlaaqg vsafalellp
      121 rttraqsmda lssqnniagy kavllacqfy prfmpmlmta agtvkaarvl vlgvgvaglq
      181 aiatakrlga vveaydvrpa treqveslga kfvevpmtde ekaanagvya remtaeflar
      241 qnellarraa aadiviatal ipgkpaprll daaavagmra gsvivdlaae aggnceltra
      301 geaclsdngv hlvgllnlpa mlaadassly arnlhtflgl llgpdgltld laddllaatl
      361 ithqgeqrfg aaaspaaadq dkephhg
//
LOCUS       WP_101724265            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            TH156].
ACCESSION   WP_101724265
VERSION     WP_101724265.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. TH156
  ORGANISM  Emticicia sp. TH156
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Emticicia sp. TH156"
                     /db_xref="taxon:2067454"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116839
     Region          22..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkyltffcl mvclelsaqt llsghisaed gsalpgatvr llasgastls daegrfeill
       61 rlekdtltvs higylstrvp vsalivrsld irlipaesll nevmvstgyq slpqervtgs
      121 fekinaslin rsvstdllsr legvtslyfd nragiggrkl slrgrstila gadpliivdg
      181 fpyessletl npndvesitl lkdaaaasiw gvraangviv vetkkgkaak pvfefrtnyt
      241 lgmqpdlyya psmaskdfie veqllfdkgy ynssltnnrf plispavevl aaqrsgkita
      301 qeastrlsgl vaqdvrrdma qyfyrkslnq qysasyrggt dlytyylsag wdqnlsnrvr
      361 dgnsrlslls snhirplknl qlqsvisytq srstannpvs nlaptskaly pyaalatadg
      421 kalpldkdyr qafidtlkds rlldwnyrpl delrladntn lqhtfrfntg vnyqllpgls
      481 advkyqyetq lsdmrnyyaq etytarnlin rftqingnlv nrpvplggil dlaetrlsah
      541 taraqvnyav nwgerhalnv lagseirqtt alsnnyrtyg yddqtlvfgs vnyvdllpty
      601 hnlngtqriv npagfnhtls rftsfygngs yvlddrysls fsvrkdasnl fgvranqkgv
      661 plwsaglswq lseeaffsna gidllklrlt ygfngnvdnt vsalttlayy snaalsgldy
      721 gmvanpgnpd lrwersgmln lgldfglknr mfsgsidyyv rrgtdllgea pidpttgvts
      781 ptgsfaykgn vaamrgtgld valhfsqtsg altwktdliy gyatnqvtky qalstvasay
      841 vgsgnlitpv kgqpvyalys yawagldpit gdpqgylegq vsknytsirn aspatlvyhg
      901 savpehfgsi rntlsyksis isanvvyklg yyfrrstihy anlfstwqhh adyaqrwkap
      961 gdeaftqvps lvypnvsnrd afynsaatlv ekgdhvrlqd inlsydfpaa gnrnswqcyl
     1021 yinqigmlwk anasgldpdy yasgfpvpts yalglklnl
//
LOCUS       WP_101724694            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            TH156].
ACCESSION   WP_101724694
VERSION     WP_101724694.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. TH156
  ORGANISM  Emticicia sp. TH156
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Emticicia sp. TH156"
                     /db_xref="taxon:2067454"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117207
     Region          24..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklllasim lvlgsyayaq nvnvtgkvta ddgsvlpgvs vvvkgtnvgv qtdangiyki
       61 sakkgasllf sfigfesqtv pvgnsstidi tlksdaaqln evvvtaqgir knlrevgyay
      121 skvstedvtv grspqlaqal sgkvtglavy nvnnsvdpqv kvvlrgfrsl tgnnealivl
      181 dgiqttstvl alinpndien isilkggqaa tlygsaging alvittkkgs kgklkvnysn
      241 stnveqisfl pefqdkygsg shyypsygsa gyssdplvrm kgnwrsyenq qfgdpfdgsl
      301 rqlgrsasdg ttnivpyaav knarykafdt gvsmnnqigf tggdengtyy mslenqkiqg
      361 ivpgdksert garvassrdy nklnvgfnas ytqakydrts sdfyndvinq panlplqdyr
      421 dwqnnkfanp naffndyynn pyfnadnnrr vykdanisgt lsltykvtpw atisnrlgam
      481 nnsrtqkstt gkflysdyak tkafiaepfy rdgdgtgvyr aitdilggvt dytktenvin
      541 nefqlllekd fgpfanklif gnsvyqryik evqvgsssiv vpdvynvsnr qgeltgyent
      601 ymnrrvgyya dltsnfknwl ilngtfrydq tslfykptra tnlwsypyyg valsfiptda
      661 fpsikssvln yaklrvnynk nandnidfyg ldltypngan fpygntvglt vgntlpdanl
      721 kpesvtsgei ggefqlfdnr vnidvsaytq ksvgqvitvk vpnstgfpnl linvgetknf
      781 gyegefkyli srgtkfswda svrysyndnk vlelypgine fvlpdgysya ntnvikgsrf
      841 pmlktdgyqy apdgsgyrlv sattgyplrq ttltprggtl prhivglgsr mnygnftftf
      901 nfeyrggnym ysdlgrqmtf tgsgkwtenr tdqifpnsay ldadgkvvpn ttvkvrepey
      961 alwvdqyrni senfvtkawf iklrdinlsy nvpqsvlskv kifsgasial ygrnlitivd
     1021 kmnyytdpey srttgnglgl nstgqtppvr qygvnlnltf
//
LOCUS       WP_101724696            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            TH156].
ACCESSION   WP_101724696
VERSION     WP_101724696.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. TH156
  ORGANISM  Emticicia sp. TH156
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Emticicia sp. TH156"
                     /db_xref="taxon:2067454"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114636
     Region          23..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllacfm lawasftfaq dvtvtgkvta ddgsalpgvs vilkgttkgt qtnadgnysi
       61 aatkgssllf sfigfesqtv avgnmsvinv tlksdaaqln evvvtalgis rekksltyta
      121 qsissdkltv srdanvgnal agkiagvqvl gqsgakfgsp nirirgvnsl tggdplyvvd
      181 gtpvgsiadv nmddvenltv lkgpsataly gnrasggviv ittkraksge ttftinhstt
      241 mdrvgllpky qneygggysq ewetfnynpa ihpaawasfn gqkildysad eswgprldgs
      301 phrsafswqp gpefgqltpf easpnnvrdf fekpfshntn lafakggdnf qsrvsythld
      361 nngiipnskq lrdyisaknt fnitkkfsat lditysatra knvpadnygs sggttgsmgl
      421 ptgvpvaavg ynqtvgsfnq wfqrqlkied lrnyknpdgt yrswniggpl dpkpkywdsp
      481 ytqmyestnl nnndriygsf glsykifdfl tasvttrrdw rnyygegria tgtlnagglg
      541 ayanytttgy ennheallal dktlgkislv gtaggnirys rttvlsqats ggltspgfyn
      601 iaaskdrpsv gnslierqvn slfgsasigy dntyflegtv rndwsstlpv ahnsyiypsv
      661 gasvvvseli pknsilsfak irgsyaqvgt dvdpyriyqt ysignafgsn ptlylptqlp
      721 nadlkpglss ayeggidlkf lnnrisveft ayknqnknqi lalsvppasg ysstlinagm
      781 ietkgfelhi gatpirttsg ftwdvdinld rntskvvelq egltnyqlgg ptwrtltvna
      841 rvgeqwgilq gkgyvtndkg ekvvgadghy lvqdnkllgs vlpkfkggll nvftyknfsl
      901 ranidfivgg kffsttrmfn ayaglaaeta glnelgkpkr dpvsagggil lpgvtadgkp
      961 ntvrvetqef yedkmfgfne awiydqtyvk lrevslgyni pkgflngkaf ksarvslivr
     1021 npvliysaag ggidiseaev ywteggqlpp vrsyginlnl gf
//
LOCUS       WP_101725617            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            TH156].
ACCESSION   WP_101725617
VERSION     WP_101725617.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. TH156
  ORGANISM  Emticicia sp. TH156
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Emticicia sp. TH156"
                     /db_xref="taxon:2067454"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119618
     Region          52..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkailltas mffwthsycq ktfhgrvase sddsavsgay lannegqvla qtdsmghfkl
       61 lwvkgviris hvgfvtvyfn pdtlksatft vllrpsinml eevqvitgyq klpgerstgs
      121 fvnvgnelln rvsgydvisr legvtnglaf drrglnrenl srspelrirg intlyaessp
      181 livldnfpye gsldninpnd vlsitvlkda aaasiwgara angvivittk rggggppkis
      241 wnintqisam pdlyynpqtl askdfiaier elfgkgfyva nnnraftpav eqwlkvkegl
      301 lsadeaerii sgyekhdirk eaqqwlyqkg vsrqynlsmq ggtekhtyys svgydqqssy
      361 vqentarrlt fttannysft sklhaglnln fitrnsknng ltlsdmettg iqtiypyasl
      421 adaagsplpi prdyrdlyke ttaaaglldw nyyplsevrk rnhtaqemes ristslsynw
      481 trtistelly qfqhftsqne qiyeeesyyv rnlinrftqk dgtriipngg iyhaangngk
      541 iqsgrlqlnf nenytnstmd giagvelren rqvsfpgall yaydaglgqg qnifnyaafy
      601 pvrpesqsrv pavgqqrrtv tdryvsyygn lgyhyrtkyt itasarwdas nlfgvktnqk
      661 gvplwhtglg walskedfyq lkflpylrvr ltygsagntv knitaypvys yvasdnvsgl
      721 pygqlqtagn pdlrwektst gnmaldfask nsrvsgsiey yikkttdlig esimdpttgi
      781 vsrsilptgv vnrinyasth tkgidveikt rntsgpvlwe svwmynyvnn rvikynasqr
      841 ilasafvagp vpkpgnsida iysypwfgls svngsplvpv engalgsspe sysrymgslt
      901 pddltyhgsa vpvhtgslrn tvkwknisfm ltllwkggyf frrtgmdyfg linnstvhkd
      961 yynrwqktgd elithvpsfp vslnnnrenl yryaevliek gdhlrlqdis lnytlpamka
     1021 fqrlniylnc rnvgilwkas kvgldpdypn srypnpsvfs iglsgtf
//
LOCUS       WP_101725790            1129 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            TH156].
ACCESSION   WP_101725790
VERSION     WP_101725790.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. TH156
  ORGANISM  Emticicia sp. TH156
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Emticicia sp. TH156"
                     /db_xref="taxon:2067454"
     Protein         1..1129
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122897
     Region          33..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklnftlrsm lrglvlygfl lgvcapavwa qtrvvtgkvt akedgtampg vnialkgtqr
       61 gtssnangty sievsgsnav lvfsfvgyqa idvpvgnrst vdvalelsse slkevvvtal
      121 gikreekslg ysigkvdgkd lgrisnenvl namagkvagv ainatggtgs svsmvirgak
      181 slsndnqplf vidgvpiint lnnvsqiggd nrvdygnais dlnpdnvesv silkgpsaaa
      241 lygsragngv vlittkngsk akkltvnltt ntvfdqpyrf ldfhhkfatg ilpftpdknp
      301 ypggilqide gsaggvgpel dkgykaiqwn spkdangksi ptelvshpnn vrdfvqtgit
      361 ttngisisns ndfinyrvay snmtnrgiip gsdlfknsla vatsmklsnk lrlstnidls
      421 rnnsnnrpag erganplqwa yalsphidin elkdywvpgq eglqqksqsa knfnnpwfla
      481 hevknafern rlfgnmkady qitpelslmg rysldsygen retkiassyt aeprgaygli
      541 nlrrfesnad flatynknvn dlsltfsagg nirntkysdv anqsrngtgl iipglftlqn
      601 iaptnlqyss yyskklvysl yatatvgfkd lvfvdltgrn dwsstlpsan rsyfypaasv
      661 sllanelfan sspnlnmlkl ragvaqvgnd tnpyallntl gsneawsgit rlsksgtill
      721 pdlkpeiats ydlgvdltmf knklrvsgty ymvenrnqii ptklppssgy tskninagll
      781 vsrgteitvg gtplerngwr ldltanfyrn rtiikelspg idfytlwtda kggawtyvge
      841 tvgdiydsel vtvtdksspy ygypildsdg swqaksasns rnkignfnpd filglqtsls
      901 yknfslnmtf dwrqggdfis qtyrygesdl ksqrfldnli npnglsgqal rdylvnndlv
      961 rvvgnkfniv ggptaeyggf pytyggntyp ygvfnpgvia qydesgkivg ytenlggpgt
     1021 kiipygdnyp wdftraamfd asfiklrevs lgyelpsgfv krlglqsanv svysrnimlw
     1081 taakigidpe mayqpqasaq agtqfkqgie rynvmpwvmp vgfklgltf
//
LOCUS       WP_101726749            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            TH156].
ACCESSION   WP_101726749
VERSION     WP_101726749.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. TH156
  ORGANISM  Emticicia sp. TH156
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Emticicia sp. TH156"
                     /db_xref="taxon:2067454"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114294
     Region          33..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhfypakns sfklkllvlw lylcplalla qtrqlsgrvi gsvnkdpmpg vgitvkgtqr
       61 gaitdaagnf kidaaagetl vfsfigyltq eikagnssti evalvedtqa leevvvtalg
      121 ikkeskrlgy aaetvkvsei qqnrtvnvma slegkiagld isppssgaga stkirlrgqs
      181 afagannspl ivinglpmdq gargangfat stasvdlgdn mqqfnpddve smtvlkgata
      241 aaiygsraan gaiiittksg nkntgigley ssnyaadevl dftdfqyeyg qgqggikptt
      301 qgqaittgqf gwgakydgkp tiqfdgverp ylpqknrikn fyrtgsaftn tialsggngm
      361 gsfrasysnq dalgispnnd yhkkifnagi nqkignkltt tlninytnei nnnppqvgvq
      421 gigspnflyr lsnsigldvl kekavadngt erqtsgfqtt llnpyyimdr qfirnkrdrf
      481 lgtatvkydi fkwlylqgrv nmdygvsfle qnlptgvgts tplnqagtgy ngsygvntsn
      541 grqmnmdfll agnkefgdfs advslggnif tnrsrtfdqs vtdftvrdly siengitksq
      601 sfgvyteqvn slygfaelgy kdmiylnltg rndwfsvlnp knnssfypsv sgsfifsell
      661 keipwlsygk lrasfadvgs anginafsgl ltygilqnaf ngyplgtinn tnspnpllrp
      721 fsvserevgl elrmfksrvn ldiayydkqt rdqiltvvvs nssgydgtpl nlgslqnrgm
      781 efmldvtpvq tgnftwkssf ntainttkvl alapntnrlv vtsfggnefi gslvyevgqp
      841 lnqlaaktyk rndkgeiivn ssgrlvpndg advllgsalp kftggwnntf syknlsllvh
      901 ldykaggkil sstalnglrq ghtkaslvgr nggvvfpavy angeknttav dpqsfytdyr
      961 naqiadpflf ksdfiklrni tlnydatrli gsrvkfikgl alsvscrnvl iikkyladld
     1021 peafassgdf rvgyeqttlp ttrtygvnln vkf
//
LOCUS       WP_101726631            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            TH156].
ACCESSION   WP_101726631
VERSION     WP_101726631.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. TH156
  ORGANISM  Emticicia sp. TH156
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Emticicia sp. TH156"
                     /db_xref="taxon:2067454"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117950
     Region          28..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkhlllcmv vllssllmsr aiyaqtivsg kvssaagegi pgvsvmlkgt kqgtnsdang
       61 nfrvsnvnan svlvfsaigy lteersvgnq ttinvtlned tkalnevvvt algikkdirr
      121 igvaiqsidg aatikarepn ainalagkva gltigtqpel lrkpnislrg nseilfvvdg
      181 vpinsdtwni spddietysv lkgasasaly gfrgkngail ittkrgskdk rgysvelnss
      241 tmidngfyai pkvqdlygpg dhgryafvdg kggglndgdy dggwgpkfeg qlipqydspv
      301 dpktgirqgt pwvargkdnl erflqagils tnniavsatg ekynlrfsas qisqrgivpn
      361 tklnisnfnv sadykfsnrl sftsnlqynk qytpnipdvn ygpnsiiynm tlwagadwnv
      421 ddmrnywqpg kegiqqiyae yqrynnpyfm syewlrghyk tdiigqaalt ykftdyleas
      481 frsqvttwnl frnekmpysa gaygrderrg dyredrrnlf enntdvlvkf dkdlfsglna
      541 kvwaggnirt feydsqygst dylnvpglyn fsnsanpvrt anfasamrvn sayysadfty
      601 knfltigttg rvdklstqpa gnntffypsv sastvlsdyl svpsaisflk lrasyanvkd
      661 gltrstigtt pslgdgnpig ygdqyyspyd gpaysnsavy stpfaynnqp aayftgtlnn
      721 pslkpsstsq telgldfrvl qnrigldvty fisdegprif slpistttgy saalvngikt
      781 qkrgweialt gsplksadgl nwdvlvnyst yqeklteiyp gvenlntffk vgdrldkfyg
      841 safvrtptgq iindasgrpi tapvaqflgy inpkfvfgin nkfsyknvnv sfqfdgrigg
      901 visnyiqrqt yrggrhigit qgamgiareq dylgvkayvg egvvlannpa vpikydadgk
      961 vtnyaelqyr andtkqfvqd yvsryyntde gnlmsrsfgm lrevvigynl pekwfgksir
     1021 nasvslvgrn llyfaekkdi dlnqyitngg sglqtpstrr yginlnftf
//
LOCUS       WP_101727028            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Emticicia sp.
            TH156].
ACCESSION   WP_101727028
VERSION     WP_101727028.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. TH156
  ORGANISM  Emticicia sp. TH156
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Emticicia sp. TH156"
                     /db_xref="taxon:2067454"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115531
     Region          23..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkhlyyliv mlllplcila qdkvlsgvvs saeegvlpgv sialkgtaig tltdasgkfs
       61 ikvpasggil visaigfatv eeridnrtiy nislaadsra lnevvvtalg isrekkslgf
      121 sqqevkgdnl vearstnvvn slsgriagvr issnggpgsg stiqirgsss vsgnnqpliv
      181 ldgvplqqqy dkqfgggise inpdnikeis vlkgpnaaal ygsraangvi litskdgags
      241 kglgieynan ftaerplvkp dfqntygggn gyvtwysdgw sgtiqpdayd qykaaygtvt
      301 pgrttgtdgt deswgapmdg rlvrqwftgk dvapltpqpn nwnefwetgt sftnhlaltg
      361 andkgnfrla fdrldqkgla ykndfertnv klnssynlnk flsaavsgey iksggnrtyq
      421 ngdtfiwshr hvswdqlany rdytgvhiqr avagklpdtd ppnwqhtyft npfytneflp
      481 nrndkdrllg nitinakllp flklmlrsgt dfwtdtrini anfervrngn rtpgtfseev
      541 lrrqetnhdf lftfdkgfgk nftlvaqagg avrrnyykrn ftnvgelvvd gvynlsnsnp
      601 sqnsvasrie ktnvqslygs aqfgylnalf ldvtarndws stlpanarsy fypslsasav
      661 itdlvsipkt ilsfgkvras waqvgndadp yqlaqtfras gswngsipey yenltisnst
      721 lkpeittgie lgldlrffkn kvgldltyyd qdtknqilgv eiskasgydk rilnagrinn
      781 kgieitlsgt pfetrngfkw dvavnfarnr nlvvelaegl ttytlqerrg lisiaqvgqp
      841 ygslygigfk hapdgqivyv dglpvvettp rvlgniqpdf tggitnnfsy krlslsflid
      901 vkkggdffde gtgtarwtgq yaetgigree giigkgvkni gsaespqyvp ndvivaanql
      961 ygynnprryh eaaifdgsyi klrevsigir lpesilkkar iqnaklslvg rnlailfkns
     1021 phidpevdrf ggnsqgfayg elpssrslgf nlslgf
//
LOCUS       WP_101728435             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Emticicia
            sp. TH156].
ACCESSION   WP_101728435
VERSION     WP_101728435.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. TH156
  ORGANISM  Emticicia sp. TH156
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Emticicia sp. TH156"
                     /db_xref="taxon:2067454"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39271
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiailketk pferrvalsp evckqliqag ftcaieknag issffedasy eavgaqvald
       61 ksvllsdadt vvkvnpltte evsfmkkgav slsfmyaaan peliaasvkq gisafsvdai
      121 prisraqkmd alssqanlag yksviigayh lgkifpllmt aagtikpakv vimgagvagl
      181 qaiatakrlg avvevsdirp etkeqveslg gkfievkgde sikieggyvk gvsedflkkq
      241 qeviarhise adlvittali pgkkapllvp eevvksmklg svivdmaveq ggncacseyg
      301 qtvvkhgvti vgepnipsll plnaselyak nmatfllhla tkdgfkwema eeitkgsliv
      361 hegkavhasv m
//
LOCUS       WP_101738966             529 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Corynebacterium].
ACCESSION   WP_101738966
VERSION     WP_101738966.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..529
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54536
     Region          1..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigiplepd pqqtivaatp etvgklvklg yevavqadag laakftdady esagativde
       61 svwhsdivvt ldtppeqfra llndgamlis rlapgrneel veelahrnit alamdavpri
      121 sraqsmdvls smaniggyra vveaaaaygr lftgqvtaag kmppatvyvi gagvgglaai
      181 gtansmgaiv katdlrpeag eqvesmgaef ipipaateks edgyakemtn dqaaaaakly
      241 seqsaqadiv ittanipgrr spllltaadv aamkpgsviv dmaaagggnc evtvpgktiv
      301 tdngvtiigy tdlagrlpaq asslygqnif nlfklitpek dgspvlnled eiirgitvtk
      361 arpqngagat gaeilwpppp ikvavtpaap lqeqqaqqaa leenapekvs fmgsglgski
      421 algltallai vvmlsaphsv sanfmvltla ivlgfyvisa vtprlhtplm setnaisgiv
      481 lvgailqvgs snllvsglaf aaivvssini fggfavtdrm lgmfvkeea
//
LOCUS       WP_101747550             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Endozoicomonas acroporae].
ACCESSION   WP_101747550
VERSION     WP_101747550.1
KEYWORDS    RefSeq.
SOURCE      Endozoicomonas acroporae
  ORGANISM  Endozoicomonas acroporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Endozoicomonadaceae; Endozoicomonas.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Endozoicomonas acroporae"
                     /db_xref="taxon:1701104"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54373
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipgeiq enenrvaatp dtvgklqklg fdvviergag vkanfgdeaf tqagarvvdr
       61 devwnsdiil kvnapidgei allkdgatla sfiwpaqnea lmnklsqrnv nilamdsvpr
      121 lsrsqsldal ssmaniggyr avveashefg rffngqitaa gkippakvlv igagvaglaa
      181 lgaagsmgai vrafdtrpev keqvesmgae flelvfspee eeqqdssdgy akemsqafid
      241 aemalfmeqa rdvdiiitta lipgkpapkl itedmvkamk pgsvivdlaa qtggncactv
      301 kdqitvahgv kvigytdlps rlptqssqly gtnlvnllkl lcpnkdgqid infddevirg
      361 ltvirdgsit wppppvkvsa apaagpepvv akepeqeaka rpwlkpvlma vgavlfgcva
      421 naapgsfleh ftvfvlasiv gyyviwnvts alhtplmsvt naisgivvvg glvqmgsdnn
      481 ivlalsgiai tvavinivgg favtqrmlkm frld
//
LOCUS       WP_101751582             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            zhejiangensis].
ACCESSION   WP_101751582
VERSION     WP_101751582.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus zhejiangensis
  ORGANISM  Paracoccus zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus zhejiangensis"
                     /db_xref="taxon:1077935"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55270
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalretq egearvavtp ssaahlqklg hevyveagag kaagfgdedy rragvtveas
       61 aadligavdv vakvrppseg eigqmregqt visffypaqs aalleqakdq gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 asigaavslg aqvyafdvrp evaeqiesmg aefvyldfse aqtdgaatgg yaapsspefr
      241 eaqlarfrel apqmdivitt alipgrdapk lwtadmvaam ktgsvivdla aerggncdlt
      301 vpderivten gvviigytdf psrmgaqsse lygnnirhfm adltpkkdgv iahnmeddvi
      361 rgatvthdha itypppppki aaiaaqkpke kkkeltpeer raaeaaafka etrsqlmllg
      421 ggglllllig lvapasfmsh fivfvlacfv gfrviwnvah slhtplmait naissiiilg
      481 almqigsgsw lvlilaalsv lmagvnifgg fmvtrrmlam fqks
//
LOCUS       WP_101751608             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            zhejiangensis].
ACCESSION   WP_101751608
VERSION     WP_101751608.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus zhejiangensis
  ORGANISM  Paracoccus zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus zhejiangensis"
                     /db_xref="taxon:1077935"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55300
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalretq egearvavtp ssaahlqklg hevyveagag kaagfsdedy rragvtveas
       61 aadligavdv vakvrppseg eigqmregqt visffypaqs aalleqakdq gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 asigaavslg aqvyafdvrp evaeqiesmg aefvyldfse aqtdgaatgg yaapsspefr
      241 eaqlarfrel apqmdivitt alipgrdapk lwtadmvaam ktgsvivdla aerggncdlt
      301 vpderivten gvviigytdf psrmgaqsse lygnnirhfm adltpkkdgv iahnmeddvi
      361 rgatvthdha itypppppki aaiaaqkpke kkkeltpeer raaeaaafka etrsqlmllg
      421 ggglllllig lvapasfmsh fivfvlacfv gfrviwnvah slhtplmait naissiiilg
      481 almqigsgsw lvlilaalsv lmagvnifgg fmvtrrmlam fqks
//
LOCUS       WP_101756563             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oceanicoccus sp. KOV_DT_Chl].
ACCESSION   WP_101756563
VERSION     WP_101756563.1
KEYWORDS    RefSeq.
SOURCE      Oceanicoccus sp. KOV_DT_Chl
  ORGANISM  Oceanicoccus sp. KOV_DT_Chl
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Oceanicoccus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Oceanicoccus sp. KOV_DT_Chl"
                     /db_xref="taxon:1904639"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39923
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigiprela agetrvpvip dsvkrftdqg aqvqieagmg kavriddsay ekagativsd
       61 raalladadi ilrlrkpela evsqlkkgsi hisfldpfne halvdafaaa evtsismemi
      121 prttraqkmd alssqaslag yamvvlaaer ldkilpmmmt pagtispsrv fiigagvagl
      181 qaiatakrlg arvdafdtrp vvkeqveslg gkfveidlgd tgqtaggyan altpeqvqlq
      241 legqkkicaq sdivittaql fgrpapivvt kdmlaamkpg svvvdlaves ggnvegsvag
      301 eeieingvkv iglanmpgrv asnasqmysa nlhnlvleyw nkdtqqfdln mddeiikgcv
      361 ithggelvnd mikksra
//
LOCUS       WP_101767793             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Photobacterium carnosum].
ACCESSION   WP_101767793
VERSION     WP_101767793.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium carnosum
  ORGANISM  Photobacterium carnosum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Photobacterium carnosum"
                     /db_xref="taxon:2023717"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54909
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkevf anetrvaatp ktveqllkmg fsvvvehgag tlasfddaaf eaagaelatt
       61 eavwqadlil kvnapqvnpa tgvdefelik dgaslvsfiw paqnsellek latkninvma
      121 mdsvprisra qaldalssma niagyravie aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaeflev dfkedtstgd gyakemsnef
      241 nqaaerlyae qakdvdiiit talipgrpap klitkemvds mksgsvivdl aaanggncay
      301 teankvitta ngvkiigytd mvgrlptqas qlygtnlvnl lkllckekdg tidinfddev
      361 lrgltvikag eitwpappik vsavkqqpkt vekvqlkkae pmsplkkygm maagialfaw
      421 vghysppefl ahftvfilsc vvgyyvvwnv shslhtplms vtnaisgiii vgallqigqg
      481 sgivsvlafv avliasinif ggftvtkrml emfrkdk
//
LOCUS       WP_101775351             486 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Pasteurella oralis].
ACCESSION   WP_101775351
VERSION     WP_101775351.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella oralis
  ORGANISM  Pasteurella oralis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Pasteurella oralis"
                     /db_xref="taxon:1071947"
     gene            1..486
                     /gene="nrfA"
     Protein         1..486
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53903
     Region          1..485
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnafkksllv aaslawgfsv vpsaiaeykp iaqpvepanp nlkiesrndl fkdkypkqyq
       61 swadtakstd ldsvnyedpr vvvlwagyaf akdynkprgh fyavtdvrni lrtgapmipd
      121 agpmpmacwa ckspdvprli aergeagyfg atwasggaev vnpigcadch dttskefaeg
      181 kpalriarpy vlralekidh kfetadktdq raalcanchv eyyfagdlkq vtfpwdngit
      241 vdamekyydd igfvdwthav skapmlkaqh pdyetwmlgv hgkngvtcid chmpkvqgad
      301 gkvytdhqig npfnafestc anchdqskek lkemvksrkt eikdvmlrle dqlvaahfea
      361 kaaweagatk eemkdalqsi rhaqwrwdya aaghgghiha pdvllkvlgt gldratdart
      421 elvrvlakhg itdpvklpdi staenawkat gvdiekdrka kaeflktvvp qwdkearekg
      481 llpaek
//
LOCUS       WP_101795613             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium medicae].
ACCESSION   WP_101795613
VERSION     WP_101795613.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39561
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfiake sdpnegrvag sidsvkklks lgfdvvvesg agqgsripdq dyekagarig
       61 katdaktadv ilkvrrpsaq evagyrsgai viaimdpygn eesisamaga gltsfamelm
      121 pritraqsmd vlssqanlag yqavidaane ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsgeyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vtremldsmk pgsvavdlav erggniegae
      301 adkvtevggv kivghlnvpg riaasaslly aknlvtflet mvsketkala lnmedelvka
      361 talthggsvv hpafggamkg ek
//
LOCUS       WP_101795983             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Novosphingobium sp. TH158].
ACCESSION   WP_101795983
VERSION     WP_101795983.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. TH158
  ORGANISM  Novosphingobium sp. TH158
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Novosphingobium sp. TH158"
                     /db_xref="taxon:2067455"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38864
     Region          5..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(19,76,95,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maealriavl kehangetrv aatpetvkkf ialgaavave agagagasip dadyaavgae
       61 vksgavtgad ivlgvqgpep kdlsgvraga wivatldpfr erarvdeyas lglealamef
      121 mpritraqsm dvlssqsnla gykavieaan lygrafpmmm taagtvsaak afvmgvgvag
      181 lqaiatarrl gaqvsatdvr satkeqiqsl gakpifvenv agiegegagg yatemseeyq
      241 kaqaelvssh iakqdivitt alipgrpapr lisdaqiasm kpgsvifdla vaqggnvegs
      301 aadqvvekhg vkilgysntp aklpadasal yarnlynfls afwdkeqgkp vldeeigdav
      361 rltrdgkvvn erllga
//
LOCUS       WP_101820016             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Gordonia
            terrae].
ACCESSION   WP_101820016
VERSION     WP_101820016.1
KEYWORDS    RefSeq.
SOURCE      Gordonia terrae
  ORGANISM  Gordonia terrae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Gordonia terrae"
                     /db_xref="taxon:2055"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38629
     Region          1..356
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,70,89,282,308,310)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,122..123,132..133,136..137,140..141,143..144,
                     146..151,153,155..157,160,183..184,272..273,315..316,320,
                     323..324)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(117..118,122,125,128,169..172,192..194,222,233,
                     250..252,259,261)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,122,132,175..176,183,199..200,202..205)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(152..156,159,162,185,187)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtvgvvreta egerrvalvp kvvaalvgkg vpvvveagag lgalipdeay teagatigdp
       61 ygsdvvlrvs ppsdseigkl rsgqkligfl aprnadnqig tlrdagveay aveaiprisr
      121 aqvmdalssq anvagyksvv vaadvstrff pmlttaagtv kpatvlvlgv gvaglqalat
      181 akrlgarttg ydvrpevaeq vrsvgaqwld lgidaagegg yarelteser aqqqhaleda
      241 ikgfdvvitt alvpgrpapr lvtaaavegm kpgsvvidla getggncelt epgqtvvkhd
      301 vtiaaplnlp atmpehasel ysknllalie lmlddngsit pdfddeviaa acvtrdepga
      361 gnevsgpkdg qqevka
//
LOCUS       WP_101810926             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            sicca].
ACCESSION   WP_101810926
VERSION     WP_101810926.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sicca
  ORGANISM  Neisseria sicca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria sicca"
                     /db_xref="taxon:490"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53943
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacplly kvnapsegel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkkltpavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_101895546             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ketobacter
            alkanivorans].
ACCESSION   WP_101895546
VERSION     WP_101895546.1
KEYWORDS    RefSeq.
SOURCE      Ketobacter alkanivorans
  ORGANISM  Ketobacter alkanivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Ketobacteraceae; Ketobacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Ketobacter alkanivorans"
                     /db_xref="taxon:1917421"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40785
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mlvgipkeiy pgenrvavip sgiqnltsag fdvvvqsgag eashydddef rnvgasiapd
       61 aqslyaqadl ilkvrhlvdd epnmikegst licmldgwfn lelvqqlaak nvrsfalefi
      121 pritraqsmd vlssmaaisg yravlagamv lpqyfpmlmt aagtihpakv fiigagvagl
      181 maistarrlg avveaydtrv evkeqveslg akfvefdlpq eegtsaggya kqqseefyra
      241 qreqmlakva qsdlvittaa ipgrpsprlv tadmlkcmkk gsvvvdlaae rggnvegtvk
      301 nqkvyvdgvt iigyidhpsr vpvhasqlft knistfllnm akegelnlnm edeivaatli
      361 tedgeikhag lkeaiekgas
//
LOCUS       WP_101901812            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            dicentrarchi].
ACCESSION   WP_101901812
VERSION     WP_101901812.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum dicentrarchi
  ORGANISM  Tenacibaculum dicentrarchi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Tenacibaculum dicentrarchi"
                     /db_xref="taxon:669041"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122845
     Region          24..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqitktliv ffiltfqlty gqkittsgvv sdksgplpgv tilikgtafg tetdfdgqyt
       61 ikttkkdvlv fsfvgmkpvs ktvnstaain vvmtedenll neivvtgitv tdkrlftgas
      121 tslkaadikl dgvpeisrgl egraagvtvq nvsgtfgaap rirvrgatsi ygnskplwvv
      181 dgiiledaid vsagdlssgd astlissaia glnsddiesf evlkdgsats iygaramagv
      241 ivittkkgka gvsnvnytns ttfrmrpsyn dfnimnsqeq msvyeemrag gwlnyskvan
      301 aresgvygem yqlydkldan gnfivrntaq sraaflrkae lrntdwfkel fninalqsha
      361 vnvssgtdra tyyaslsamv dpgwtkassv nrytanfksi fkisdkltls sisngsfrkq
      421 kapgtlsqdt dlvtgtvkrd fdinpfsyal ntsrvldptk nytrnytdfn iskeleenyi
      481 dinvvdlkfq selkykvnsk inlsalgalk yqtsslehnt tefsnqanaf radyneiirn
      541 anpflytdpd nqyatpisvl peggifrktt hsmlgydfrg tfsykdvind dhtvnfyaga
      601 eansadrkkt nftgwglqys lgevpfygye lfkksieent lyyglkntky rnlaffgntt
      661 yswkrrytln gtfryegsnk lgkskasrwl ptwnvsgawn vheedffhhl aplesltfra
      721 sysltadrgp envsnslvdi rsknpwrpsa gskesalyvk glenseltye kkhelnlgfd
      781 tslfdgrlav gadwyqrnnf dligptntqg iggeitkygn iaemkssgle lsisgtpikt
      841 edfswqtsfv ysktknevtk ldsqqrvidl vtgygfakqg ypvkaifsip faglneeglp
      901 tfqdqegnvs igevyfqerd kldflkysgs adptdvgsfg nifkyknlrl nifttysfgn
      961 virlnpvfss rysdlsalpk efenrwilpg dekftnvpvi astrqenrvg vsdlrtayna
     1021 ynysdariak gdfvrlkevs lafqfpkeyv tkinvkslsl klqatnlfll ysddklngqd
     1081 peffnsggva tplakqftft lklgl
//
LOCUS       WP_101902969            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            dicentrarchi].
ACCESSION   WP_101902969
VERSION     WP_101902969.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum dicentrarchi
  ORGANISM  Tenacibaculum dicentrarchi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Tenacibaculum dicentrarchi"
                     /db_xref="taxon:669041"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118454
     Region          26..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnpryknvlc ilfflgflvn vtaqqkmitg tvsdsagplp gvnvvikgtv sgvetdfdgt
       61 ytvkaeanqs lvfsfvgmqn vtklvgaktt invvmqedan vleevvvvgy gtstksaftg
      121 takvvkaevl aaksvsnisq alageaagvq vintsgqpgk satirirgfg svngnrdplf
      181 vvdgvpfdga lntinpsdia sttilkdata taiygsrgan gvvlittksg kngvssiefd
      241 vktgvnfsnl arystikspe eyiglsweam rnkgdfngea datayananl fsgkginsay
      301 nlwnvsdisk lidpatgkvr agvarkytpe nwadygfqts irteanlkms ggddktkyfs
      361 sfgyledkgy vlnsdykryt srlnlthnpt dwlkasvnlg ytfgkttsng qsedsgsvfw
      421 fvdnipsiyp lftrdtngkk iddpiygghi ydfgdagrgf galtnsiana kynlkqserh
      481 slnanfsfnf qlaenlsfes rygaqyysfi dndiqnpfyg saagsdtkgr lfkqnryavt
      541 qnflnmfkyn tsfgdhkvdf iaahesnqwk rqrgytdvkr vvnlnngldd ptnyvetagk
      601 stgyreeiai esffgqanyn ydgkyfftts vrrdgtsrfk nnkwgtfgsi ggswivtken
      661 fmndvefvnn lkvkvsygil gdqsigsels diyagqngyd ienlggqisl pvrarqnael
      721 twetskmfqt gveftlfdnl vdasfdyyvk ntedlifdrr lgpslgdale kvndgklkna
      781 gfefditthi inkknytfdv slngeflkne ltqmpidpst gkaklldqsg nygrskghsl
      841 fdyymrewag vdandgaamw nvnyvdankn dafdkgeeik nynkfltdnp dakisqgttk
      901 vysqatqkyv dksaiptvrg afrlsakihd fdissqfays lggyaydgay anlmsngqvg
      961 gnnwstdmrd rwqkkgditn vprlysnevt avtssstrfl tstdylalnn irvgytipvq
     1021 yikkaglgsv nlyasgdnlf llskrdgfnp atsetgssdq yrysplttfa lgvrikf
//
LOCUS       WP_101903157            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            dicentrarchi].
ACCESSION   WP_101903157
VERSION     WP_101903157.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum dicentrarchi
  ORGANISM  Tenacibaculum dicentrarchi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Tenacibaculum dicentrarchi"
                     /db_xref="taxon:669041"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115855
     Region          21..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvtllwllf lvsqftfaqe ktisgvvsde sgglpgvsii ikgtttgvet dfdgnysina
       61 kqndilvfsf vgkatvqktv gtsnkinvvl addanllnev vvtalgikrk pksigsaqqt
      121 vkgddltktr etdistalag kvsgiqftgq psssfkgadv rlrgaknvly vvdgirlnss
      181 tdvntedies mtvlkglaat alygpsgkng aiviiskkak sgnskivfns siglssvvgl
      241 peyqnqyggg yrndgkgsad entssigywn tlngqkivny aadeswgpel dgtlvrqwds
      301 wikgdpefgk lrawsanpdn ikdfyrtgqv tnnsltfskg gegysirttl gqvkqdlvle
      361 nsdrkttrvn tnlsfdlnkk ltfsttvnys nrvtkndpdg qynnlasnln qwwqrqidvs
      421 rlkdykrnge mvswninspt nprpkywnsp yftlyedgnl etkdaifgkv alaykitekl
      481 nasvaykrai nqyersdktg fgglapesfr erkttssede ifaitnysnt wndfelkasa
      541 gfqlidrkyn tldtwsvggl ttkdfysigt skdrpgintt kfrvqergmf lttdlgykel
      601 vyltgsyrid ygstanadnn rldtkglsas fifselipen nilsfgklra gtsqapyfpn
      661 pfqlnptyda gtsygsngts iapntavnpn legglrsene fgielrflhn risldatyfs
      721 redknlpsdv slptstgyys fvsnegeqss ngfelaisgd iiktddlkwn vainaatlkr
      781 kvdfiakgvk tniidswgpq llerrgeewg aiygnaykrd akgnkvlgad glyefennky
      841 lgsilpdvtg gftsnltykn fdlslgfdyq vggkfygvtr rytnysgngi etvgnnslgn
      901 pirnkiigag aheaysvnlt daapnsggql tsgvdadgna qsflvtpakl wkenlvsihe
      961 efvndatylk lrtirlgynv pksalensff tdinlsvfan nvwlihsevk gidpselqgr
     1021 srgsringyn nyewiengql paartigint kftf
//
LOCUS       WP_101903604            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            dicentrarchi].
ACCESSION   WP_101903604
VERSION     WP_101903604.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum dicentrarchi
  ORGANISM  Tenacibaculum dicentrarchi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Tenacibaculum dicentrarchi"
                     /db_xref="taxon:669041"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120295
     Region          26..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnfklfvsi llgvfissti laqsstisgv isdgsyplpg asvvlegttt gadtdfdgkf
       61 elnkvsfekv tlkisfigyq ekrvqvslsk gahkklgtiv lkqleqqlde vvitalgikk
      121 eekalgysvs nlkaaelnqa ketnlvnaln gkiagvqitn gstgvgstsr vvirgeaslt
      181 stangplfvv dgipihnnti fgtgqntggn emqevdygng aseidpdnva nisvlkgana
      241 aalygsrgsn gvilittkta rrnkgltvtv ntgttiekal rlpkyqnkyg qgwagkfkya
      301 dglandlgin dqedvswgpe angqlvtqfd spttsgvrag difvrgwvrd angkiisptt
      361 mpndiiatpf varpnnvenf yktgftttfs taigfgadks dflfsfgsld nqgiipntgl
      421 krksyrings vnltdklkis lksnyiksss dnrpssgygs esamymftwy grtvntsalk
      481 nywqkgyegl eqynynyawh dnpyfmlnen tnafnkhrll gniqleyqll knlkfqaktg
      541 mdyyadkras kraystqrfl kgaykdervd ftevntdflf sydkkindaw nvdvnfggnq
      601 mkqeinflss manglvipgl ynlqnsisdv vttqykeeke inslygtlgi gyknkvfvdv
      661 tarndwsstl paknnsyfyp sasvsllidk ifempeafsf fkirgsfaqv gndtsaynlk
      721 tpysyqtpya gnktlsrssv llnenlkpem stsyefgtdl rmfngavgvd ftyykstsed
      781 qimsvpitnt vgysaqiina gkienkgiea lltikpirne nfawttslnf sknqgtvvel
      841 tenmdvltma yasvygaets kvfiqarkge klgnmygrkf erhngkivyk dgkpvvndkl
      901 qllgnynpdf slgfknsfky knfdlsvlmd wkqggtiisr tkqiaayagn ldvsenrnny
      961 qdivpdgvkk vggeyvaltd adaigwwsyy kplynrknqq etgivdatyv klreikfgyn
     1021 vpaylikklg meslkvsivg rnlglwtpss nphfdpetla mqganvvpgi edvsypssks
     1081 yginflfkf
//
LOCUS       WP_101904683             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            harveyi].
ACCESSION   WP_101904683
VERSION     WP_101904683.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53077
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmsap iavatlfasq lflagaplaa eekglmdprn dafeqqhpdq yhswkatses
       61 ehiedalged pnmvilwagy gfakdynkar ghfyalddvr qtlrtgapsd eksgpvpmac
      121 wsckspdvar vieergedgy fegkwarlgs eivnpigcsd chdtrseefk kgepalaltr
      181 pyverafdti gknfdqqsrl dkqasvcaqc hveyyftgpt kavkfpwdmg ttvndmekyy
      241 dalnfkdwth avskapmlka qhpgyetwrd gihgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfed tcaqchtqtk eqlqgivstr kaqvlnmklt aekqivaahf eagaawkaga
      361 teeemqpilq dirhaqwrwd yaiashgvhm hapevalevl gtavdraada rtklvrllat
      421 kgitdpvqip distkakaqq algmdmekmn adkkhfletv vpdwdkaaae reaty
//
LOCUS       WP_101906684            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            dicentrarchi].
ACCESSION   WP_101906684
VERSION     WP_101906684.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum dicentrarchi
  ORGANISM  Tenacibaculum dicentrarchi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Tenacibaculum dicentrarchi"
                     /db_xref="taxon:669041"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122937
     Region          24..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqitktliv ffiltfqlty gqkittsgvv sdksgplpgv tilikgtafg tetdfdgqyt
       61 ikttkkdvlv fsfvgmkpvs ktvnstaain vvmtedenll neivvtgitv tdkrlftgas
      121 tslkaadikl dgvpeisrgl egraagvtvq nvsgtfgaap rirvrgatsi ygnskplwvv
      181 dgiiledaid vsagdlssgd astlissaia glnsddiesf evlkdgsats iygaramagv
      241 ivittkkgka gvsnvnytns ttfrmrpsyn dfnimnsqeq msvyeemrag gwlnyskvan
      301 aresgvygem yqlydkldan gnfivrntaq sraaflrkae lrntdwfkel fninalqsha
      361 vnvssgtdra tyyaslsamv dpgwtkassv nrytanfksi fkisdkltls sisngsfrkq
      421 kapgtlsqdt dlvtgtvkrd fdinpfsyal ntsrvldptk nytrnytdfn iskeleenyi
      481 dinvvdlkfq selkykvnsk inlsalgalk yqtsslehnt tefsnqanaf radyneiirn
      541 anpflytdpd nqyatpisvl peggifrktt hsmlgydfrg tfsykdvind dhtvnfyaga
      601 eansadrkkt nftgwglqys lgevpfygye lfkksieent lyyglkntky rnlaffgntt
      661 yswkrrytln gtfryegsnk lgkskasrwl ptwnvsgawn vheedffhhl aplesltfra
      721 sysltadrgp envsnslvdi rsknpwrpsa gskesalyvk glenseltye kkhelnlgfd
      781 tslfdgrlav gadwyqrnnf dligptntqg iggeitkygn iaemkssgle lsisgtpikt
      841 edfswqtsfv ysktknevtk ldsqqrvidl vtgygfakqg ypvkaifsip faglneeglp
      901 tfqdqegnvs igevyfqerd kldflkysgs adptdvgsfg nifkyknlrl nifttysfgn
      961 virlnpvfss rysdlsalpk efenrwilpg denftnvpvi astrqenrvg eydlrtayna
     1021 ynysdariak gdfvrlkevs lafqfpkeyv tkinvkslsl klqatnlfll ysddklngqd
     1081 peffnsggva tplakqftft lklgl
//
LOCUS       WP_101907312            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            dicentrarchi].
ACCESSION   WP_101907312
VERSION     WP_101907312.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum dicentrarchi
  ORGANISM  Tenacibaculum dicentrarchi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Tenacibaculum dicentrarchi"
                     /db_xref="taxon:669041"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120277
     Region          26..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnfklfvsi llgvfissti laqsstisgv isdgsyplpg asvvlegttt gadtdfdgkf
       61 elnkvtsekv tlkisfigyq ekrvqvslsk gahkklgtiv lkqleqqlde vvitalgikk
      121 eekalgysvs nlkaaelnqa ketnlvnaln gkiagvqitn gstgvgstsr vvirgeaslt
      181 stangplfvv dgipihnnti fgtgqntggn emqevdygng aseidpdnva nisvlkgana
      241 aalygsrgsn gvilittkta rrnkgltvtv ntgttiekal rlpkyqnkyg qgwagkfkya
      301 dglandlgin dqedvswgpe angqlvtqfd spttsgvrag difvrgwfrd angkiisptt
      361 mpndiiatpf varpnnvenf yktgftttfs taigfgadks dflfsfgsld nqgiipntgl
      421 krksyrings vdltdklkis lksnyiksss dnrpssgygs esamymftwy grtvntsalk
      481 nywqkgyegl eqynynyawh dnpyfmlnen tnafnkhrll gniqleyqvl knlkfqaksg
      541 ldyytdkras kraystqrfl kgaykdervd ftevntdflf sydkkindaw nvdvnfggnq
      601 mkqeinflss manglvipgl ynlqnsisdv vttqykeeke inslygtlgi gyknkvfvdv
      661 tarndwsstl paknnsyfyp sasvsllidk ifempeafsf fkirgsfaqv gndtsaynlk
      721 tpysyqtpya gnktlsrssv llnenlkpem stsyefgtdl rmfngavgid ftyykstsed
      781 qimsvpitnt vgysaqiina gkienkgiea lltikpirne nfawttslnf sknqgtvvel
      841 tenmdvltma yasvygaets kvfiqarkge klgnmygrkf erhngkivyk dgkpvvndkl
      901 qllgnynpdf slgfknsfky knfdlsvlmd wkqggtiisr tkqiaayagn ldisenrnny
      961 qdivpdgvkk vgaeyvaltd adaigwwsyy kplynrknqq etgivdatyv klreikfgyn
     1021 vpadlieklg meslkvsivg rnlglwtpss nphfdpetla mqganvvpgi edvsypssks
     1081 yginflfkf
//
LOCUS       WP_101907430            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            dicentrarchi].
ACCESSION   WP_101907430
VERSION     WP_101907430.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum dicentrarchi
  ORGANISM  Tenacibaculum dicentrarchi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Tenacibaculum dicentrarchi"
                     /db_xref="taxon:669041"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118594
     Region          26..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnpryknvlc ilfflgflvn vtaqqkmitg tvsdsagplp gvnvvikgtv sgvetdfdgt
       61 ytvkaeanqs lvfsfvgmqn vtklvgaktt invvmqedan vleevvvvgy gtstksaftg
      121 takvvkaevl aaksvsnisq alageaagvq vintsgqpgk satirirgfg svngnrdplf
      181 vvdgvpfdga lntinpsdia sttilkdata taiygsrgan gvvlittksg kngvssiefd
      241 vktgvnfsnl arystikspe eyiglsweam rnkgdfngea datayananl fskksinsay
      301 nlwnvsdisk lidpatgkvr agvarkytpe nwadygfqts irteanlkms ggddktkyfs
      361 sfgyledkgy vlnsdykryt srlnlthnpt dwlkasvnlg ytfgkttsng qsedsgsvfw
      421 fvdnipsiyp lftrdtngkk iddpiygghi ydfgdagrgf galtnsiana kynlkqserh
      481 slnanfsfnf qlaenlsfes rygaqyysfi dndiqnpfyg sasggdtkgr lfkqnryavt
      541 qnflnmfkyn tsfgdhkvdf iaahesnqwk rqrgytdvkr vvnlnngldd ptnyvetagk
      601 stgyreeiai esffgqanyn ydgkyfftts vrrdgtsrfk nnkwgtfgsi ggswivtken
      661 fmndvefvnn lkvkvsygil gdqsigsels dlyagqngyd ienlggqisl pvrarqnael
      721 twetskmfqt gveftlfdnl vdasfdyyvk ntedlifdrr lgpsigdale kvndgklkna
      781 gfefditthi inkknytfdv slngeflkne ltqmpidpst gkaklldqsg nygrskghsl
      841 fdyymrewag vdandgaamw nvnyvdankn dafdkgeeik nynkfltdnp dakisqgttk
      901 vysqatqkyv dksaiptvrg afrlsakiyd fdissqfays lggyaydgay anlmsngqig
      961 gnnwstdmrd rwqkkgditn vprlysnevt avissstrfl tstdylalnn irvgytipvq
     1021 yikkaglgsv nlyasgdnlf llskrdgfnp atsetgssdq yrysplttfa lgvrikf
//
LOCUS       WP_101907022            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            dicentrarchi].
ACCESSION   WP_101907022
VERSION     WP_101907022.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum dicentrarchi
  ORGANISM  Tenacibaculum dicentrarchi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Tenacibaculum dicentrarchi"
                     /db_xref="taxon:669041"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117167
     Region          25..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lllalivqfs faqdktisgi vsdesgplpg vtvlkkgttq gtetdfngky
       61 tikskngdil vfnfvgmkti qktvgtsnqi nivmendnvl devvvtalgi krekkslgya
      121 sqeiksdain ggttktgnia sqlsgkvagl nvtttnnfgg ssnmvirgvk slgggspliv
      181 idgspinnss tftggndygn alsdinqddi asmnilkgaa asalygergi ngvivittkn
      241 gksgddnswg ikfssgitvg tidkatfpey qntygggygq gfdhgndytn ydsdgsggpk
      301 ydgslkyhwd afdttspnfg kkrayvaakn gpsslfktsf tktnsisiqk gnqsknmtft
      361 yenfdsdwil pnseleknnf slkvnydltp klhtsfyssl tlqdtqgrnt tgysdnlmsm
      421 frqwwnvdvd ilqqkdsyfr nkaiassdnr ygniswnrks ptnskpaywn npyfqlyeny
      481 gsdsryrsfs ygrmtydind nlgvtgkiay dksmlniekr iatgsiamdf gasentvpsg
      541 ysrqdiarse tnldlmlnyn yklveeinvs gvlganlrkn dynsiyaste gglvvpgiys
      601 lantvkspla atenqyntet nsayltasfd fykkfyldat wrldksstlp avnntynyps
      661 vtgalivsef ykpewlsfwk vranyaevgs tadpyelqns yasagllngv glydtnytkk
      721 nsnlkpqrsk eyefgtemmf lnkritldfa yyntktfdqi islpvstatg yskkvvnagq
      781 innsgfeaql glvavkndnf twsidlnwsk nknkvislsg dsenyqlasy nggvslnafk
      841 gkpwgtligp gyvedkngnk vletyqnkek tktyarykrv gnknlgnvtp dwiggmrnsf
      901 tyknfgfsfl idvrkggkvf stdmyyglgt glyketvgnn vrqtgvvlpg vfedgtkntf
      961 iardpqayga vdgwkvnpse afvydggfvk lreaaisysl pksvlknsfi ndakislvgr
     1021 nlwiiskdlp yadpeamvgg gtrsyghsig stpttrdigl nitfkf
//
LOCUS       WP_101907563            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            dicentrarchi].
ACCESSION   WP_101907563
VERSION     WP_101907563.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum dicentrarchi
  ORGANISM  Tenacibaculum dicentrarchi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Tenacibaculum dicentrarchi"
                     /db_xref="taxon:669041"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112497
     Region          21..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvtllwllf lvsqftfaqe ktisgvvsde sgglpgvsii ikgtttgvet dfdgnysina
       61 kqndilifsf vgkatvqktv gtsnkinvvl addanllnev vvtalgikrk sdeittanqv
      121 vkadeitkae vptvtqglvg kvsglqintt sqgakptfdl rlrgnrsltg nnsalividg
      181 aisssvvlna ldpksiesvn vikgangaal ygsdgsngvl ivttkkgnnd gkfrvtigts
      241 vqvqelaylp erqttygqgw gtginlaeng gwgpafdgsi qpvgvaapgf eqmyapyvgd
      301 adniksffkk gfqkqhnigl stgsldkgyv nfsaglldvt siipnekykr ssfnfkagkk
      361 vgkltvdgai syivdsekva ssettrgdns vygallqtpt nvnldqfkdf tgnerntrhw
      421 nsyylspywv ldnvrsttks divnttinlg yeindninft vlgnaifrqt nteykrnaft
      481 epvvrvgdrt assryttrnr ttreiysnyk fnfdydlted itfkanvggd irefnrkyly
      541 sgvnnlaies lsniasgasa ptvtdakykr raiglfgnfd fgfrdylfln ltgrndwtsk
      601 lskdnnsffy psagvsfvpt kafpslktnv lnkmklsysf vkvgndaagi nainaiyekp
      661 aafpygdlts frpdrtitdp nltpefiash efglnvdlyr srvtldvsaf tskntdqvvk
      721 vassrasgve eaginigets sqgfevdlgf vpiqtddlrw dlrvsyatnk tvvdkisdsl
      781 devvisddtd vdivakkgee fplikgiayq rddkgriivd astgnplqtd akvvlgkvtp
      841 dyilgltsal nykgftlstt ldyrtghsiy ssvkkelvrn glavetvqsg rkgfilpnsv
      901 isdgkggyvp ntnvitggtt snsitnyytg nfgdsaenfv ldatalkvre isltydmpkd
      961 flkntgvnsl qiglsarnpf vllsnenrgf tdpeynsasg sdttnkagds fnnaggasry
     1021 dllpptryyg lsvnlsl
//
LOCUS       WP_101913968            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            finnmarkense].
ACCESSION   WP_101913968
VERSION     WP_101913968.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum finnmarkense
  ORGANISM  Tenacibaculum finnmarkense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Tenacibaculum finnmarkense"
                     /db_xref="taxon:2781243"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122849
     Region          25..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqitktliv ffiltfqlty gqkkitasgv vsdqsgplpg vtilikgtaf gtetnfdgey
       61 tikttqkdvl vfsfvgmktv kktvnstaai nvvmtedenl lneivvtgit vtdkrlftga
      121 stslkaadik ldgvpeisrg legraagvtv qnvsgtfgaa prirvrgats iygnskplwv
      181 vdgiiledai dvsagdlssg dastlisssi aglnaddies fevlkdgsat siygaramag
      241 vivittkkgk agvsninytn sttfrmrpsy tdfnimnsqe qmsvyeemra ggwlnyskva
      301 naresgvyge myqlydklda ngnfliknta qsraaflrka elrntdwfke lfninalqsh
      361 avnvssgtdr atyyaslsai vdpgwtkass vnrytanfks ifkvsdkltf ssistgsfrk
      421 qkapgtlsqd tdlvtgtvkr dfdinpfsya lntsrvldpa knytrnytdf niskeleeny
      481 idinvanlkf qselkykvns kinlsalgal kyqtsslehn ttefsnqana fradyneiir
      541 nanpflytdp dnqyatpisv lpeggifrkt thsmlgydfr gtfsykdvin ddhtvnfyag
      601 aeansadrkk tnftgwglqy slgevpfygy elfkksieen tlyyglkntk yrnlaffgnt
      661 tyswkrrytl ngtfryegsn klgkskasrw lptwnvsgaw nvheedffdh ldplesltfr
      721 asysltadrg pesvsnslvd irsknpwrps agskesalyv aglenselty ekkhelnvgf
      781 dtslfdgrla igadwyqrnn fdligptntq giggeiikyg nvaemkssgl elsisgtpik
      841 tedfswqtsf vysktknevt kldsqqrvid lvtgygfakq gypvkaifsi pfaglneegl
      901 ptfqdqegev sigelnfqer dkldflkysg sadptdvgsf gnifkyknlr lnifttysfg
      961 nvirlnpvfs srysdlsalp kefenrwilp gdenftnvpv iastrqenrv geydlrtayn
     1021 aynysdaria kgdfvrlkev slafqfpkey vtkinvksls lklqatnlfl lysddklngq
     1081 dpeffnaggv asplakqitf tlklgl
//
LOCUS       WP_101914374            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            finnmarkense].
ACCESSION   WP_101914374
VERSION     WP_101914374.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum finnmarkense
  ORGANISM  Tenacibaculum finnmarkense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Tenacibaculum finnmarkense"
                     /db_xref="taxon:2781243"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120158
     Region          26..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnfklfvsi llgvfissti laqsstisgv isdgsyplpg asvvlagtti gadtdfdgkf
       61 elnkvtsekv tlkisfigyq ekrvqvslsk gahkklgtiv lkqleqqlde vvitalgikk
      121 eekalgysvs nlkaaelnqa ketnlvnaln gkiagvqitn gstgvgstsr vvirgeaslt
      181 stangplfvv dgvpihnnti fgtgqntggn emqevdygng aseidpdnva nisvlkgana
      241 aalygsrgsn gvilittkta rrnkgltvtv ntgttiekal rlpkyqnkyg qgwagkfkya
      301 dglandlgin dqedvswgpe angqlvtqfd spttsgvrag difvrgwvrd angkiisptt
      361 mpndiiatpf varpnnvenf yktgftttfs taigfgadks dflfsfgsld nqgiipntgl
      421 krksyrings vdltdklkis lksnyiksss dnrpssgygs esamymftwy grtvntsalk
      481 nywqkgyegl eqynynyawh dnpyfmlnen tnafnkhrll gniqleyqvl knlkfqaksg
      541 ldyytdkras kraystqrfl kgaykdervd ftevntdflf sydkkindaw nvdmnfggnq
      601 mkqeinflss manglvipgl ynlqnsisnv vttqykeeke inslygtlgi gyknkvfvdv
      661 tarndwsstl paknnsyfyp sasvsllidk ifempeafsf fkirgsfaqv gndtsaynlk
      721 tpysyqtpya gnktlsrssv llnenlkpem stsyefgtdl rmfngavgid ftyykstsed
      781 qimsvpitnt vgysaqiina gkienkgiea lltikpirne nfawttslnf sknqgtvvel
      841 tenmdvltma yasvygaets kvfiqarkge klgnmygrkf erhngkivyk dgkpvvndkl
      901 qllgnynpdf slgfknsfky knfdlsvlmd wkqggtiisr tkqiaayagn ldisenrnny
      961 qdivpdgvkk vgseyvaltd adaigwwsyy kplynrknqq etgivdatyv klrevkfgyn
     1021 vpagliekla meslkvsivg rnlglwtpss nphfdpetla mqganvvpgi edvsypssks
     1081 yginflfkf
//
LOCUS       WP_101914879            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            finnmarkense].
ACCESSION   WP_101914879
VERSION     WP_101914879.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum finnmarkense
  ORGANISM  Tenacibaculum finnmarkense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Tenacibaculum finnmarkense"
                     /db_xref="taxon:2781243"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116602
     Region          25..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lllalivqfs faqdrtisgi vsddsgplpg vtvlkkgttq gtetdfdgky
       61 tiksktgeil vfnfvgmkti qktigtsnqi nivmendnvl deivvtalgi krekkslgya
      121 sqeiksdain ggttktgnia sqlsgkvagl nvtttnnfgg ssnmvirgvk slgggspliv
      181 idgspinnss tfaggndygn alsdinqddi asmnilkgaa asalygergi ngvivittkn
      241 gksgddnswg ikfssgitvg tidkatfpey qntygggygq gfdhgndytn ydsdgsggpk
      301 ydgslkyhwd afdttspnfg kkrayvaakn gpsslfktsf tktnsisiqk gdqsknmtft
      361 yenfdsdwil pnseleknnf slkvnydltp klhtsfyssl tlqdtqgrnt tgysdnlmsm
      421 frqwwnvdvd vleqkdsyfr nkaiasadnr ygniswnrks ptnskpaywn npyfqlyena
      481 gsdnryrsfs ygritydind nlgvtgkvay dksmlniekr iaagsiamdf gasentvpsg
      541 ysrqdiarse tnldlmlnyn yelvedikvs gvlganlrkn dynsiyaste gglvvpgiys
      601 lantvkspla atenqyntet nsayltasfd fykkfyldat wrldksstlp aanntynyps
      661 vtgalivsef ykpewlsfwk vranyaevgs tadpyelqns yasagllngv glydtnytkk
      721 nsnlkpqrsk eyefgtemmf lnkritfdfa yyntktfdqi islpvstatg yskkvvnagq
      781 innsgfeaql glvavkndnf twnidlnwsk nknkvvslsg dsenyqlasy pggvslnafk
      841 gkpwgtligp gykedkngnk lmetyqskgv tyaryikdgs knlgnvtpdw iggmrnsfty
      901 knfgfsflid vrkggkvfst dmyyglgtgl yketagnnvr qtgvvlpgvf edgtkntiia
      961 rnpqaygavd gwkvkpseaf vydggfvklr eaaisyslpk salknsfind akislvgrnl
     1021 wiiskdlpya dpeamvgggt rsyghsigst pttrdiglnl tfkf
//
LOCUS       WP_101914916            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            finnmarkense].
ACCESSION   WP_101914916
VERSION     WP_101914916.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum finnmarkense
  ORGANISM  Tenacibaculum finnmarkense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Tenacibaculum finnmarkense"
                     /db_xref="taxon:2781243"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111712
     Region          21..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvtllwllf lvsqftfaqe ktisgvvsde sgglpgvsii ikgtttgvet dfdgnysina
       61 kqndilifsf vgkattrktv gasnkinvvl addenllnei vvtalgikrk sdeittanqv
      121 vkadeitkae vptvtqglvg kvsglqintt sqgakptfdl rlrgnrsltg nnsalividg
      181 aisssvvlna ldpksiesvn vikgangaal ygsdgsngvl ivttkkgnnd gkfrvtigts
      241 vqvqelaylp erqttygqgw gtginlgeng gwgpafdgsi qpigvaapgs aqmyapyvgn
      301 adnindffnt gfqrqhnigl stgsladgyv nfsaglldvt siipnekykr ssfnfkagkk
      361 vgkltvdgav syivdsekva ssetdrgdns vygallqtpt nidvnrfkdl qgderntrhw
      421 nsyylspswv ldnvrsttks diintsinlg yeindninfs vlgnavfrqt nkeykrnaft
      481 epvvrvgdrt asstfytrnr ttreiysnyk fnfdynlted itfkaniggd irefnrkyly
      541 ssvdnlaies laniasgasa psvtdakylr rafgvfgnfd fgfrdylfln ltgrndwtsk
      601 lskdnnsffy psagvsfvpt kafpslkndv lnkmklsysf vkvgndaagt yainaiyekp
      661 aafpygtvts frpdrtitdp nltpeftash efglnvdlyr sritldasvf sskntdqvvq
      721 vaasrasglt taginigqts stgfeidlgf vpiktedfrw dlrasystnk tvvdkisdsl
      781 deivisndns vdivaqkgqe fplikgiayq rddkgrviid antgnplqtd akvvlgkvtp
      841 dyvlglsssf nyknfslstt ldyrtghsiy ssvkqelsrn glavetiqsg rkgfiypnsv
      901 isdgkdgyip ntnvitggtt snsitnyygg sfndvqenfv ldatalkvre islsydmpkd
      961 flkntgvstl qiglsarnpf vilskenrgf tdpeynstgg dnsanaggaa rydllpptry
     1021 yglsvnlsl
//
LOCUS       WP_101916662            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            piscium].
ACCESSION   WP_101916662
VERSION     WP_101916662.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum piscium
  ORGANISM  Tenacibaculum piscium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Tenacibaculum piscium"
                     /db_xref="taxon:1458515"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117331
     Region          25..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkttfngilt lllalivqis faqektvsgt vsdesgplpg vtvlkkgtnq gtetnfdgky
       61 tiktktgdvl vfsfigmksi qkiigssnti niimkndnil devvvtalgi srdkkslgya
      121 tqevkgdelt tnksgnfvna lsgkasgiqi rknnnmggst nvvirgnasl tgnnqalfvi
      181 dgvpignsss nassqaegvg gyydygnpas dinpediasi nilkgaaasa lygsraangv
      241 imittkkgkd skgigvtins gasfgkidks tftkfqtkyg agygpfydgp gsqwlledin
      301 gdgtkdlvap ymedasygaa fdpkllvyqw dsfdpaspny kkktpwvspk ngpieffetp
      361 ititnsisld qssekgnfri nytqfdqtgl mpnssqkkhn fsmsgnlkmt ekftatayan
      421 yikskakgrn stgyndnilt mfkqwgqtnv dlqqqkdsyf stkrnitwnp atsdagsapi
      481 fwdnpywkry enyqndsrdr fvgnislnye indwlnvtgr istdtyneiq eerrangsvp
      541 aafgvsrgnv dagygrknis ntetnydfmf nldrnltedl nlkaivgtni rrntfksiya
      601 stagglsvpk lyslqnsigp lplpierdek vgvdgvygsa slgfkntfff datirrdhss
      661 tlpndnstfy ypsfagsfvf skllnqdwls fgklranyae vgnsapfdyl ndtyrvniap
      721 gtpstsvgnt kknidlkper tesievglem kvlqnrlgfd layyknnsid qivgvpvsta
      781 tgysskilna geienkglev singtpiktd nfswnanvnw skneskvisl tkgisnlqlg
      841 dfqggvtina tvgqpygviq gtdftylngk kvvdaesgey vktsssdkii gdtspdwlmg
      901 isnsfkyknv slsflvdfqk ggsifsldqs yglatgvnae tafindlgnp vrnsiadggg
      961 minpgvnsdg atnttrirtd rygafgyrrg lpnaafvyda sfvklrevai tynftdkimn
     1021 ntfltggsis fsgsnlwiih knlphadpes glssgnlqgy stgslpttrn fgfnlklkf
//
LOCUS       WP_101917651            1038 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            piscium].
ACCESSION   WP_101917651
VERSION     WP_101917651.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum piscium
  ORGANISM  Tenacibaculum piscium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Tenacibaculum piscium"
                     /db_xref="taxon:1458515"
     Protein         1..1038
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112556
     Region          25..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lllalvvqis faqdrtisgt vsdesgplpg vtvlrkgiak gtetdfdgky
       61 tiatkqgevl ifsfvgmkta qktvgasnsi nlvmqndnvl deivvtalgi krksdeitta
      121 nqvvkaseit kaevptvtqg lvgkvsglqi nttsqgakpt fdlrlrgnrs ltgnnsaliv
      181 idgaisssvv lnaldpksie svnvikgang aalygsdgsn gvlivttkkg nndgkfrvti
      241 gtsvqvqela ylperqttyg qgwgtginla enggwgpafd gsiqpvgvaa pgfeqmyapy
      301 vgdadniksf fkkgfqkqhn iglstgsleq gyvnfsagll dvtsiipnek ykrssfnfka
      361 gkkvgkvtvd gaisyivdse kvassettrg dnsvygallq tptnvnldqf kdftgnernt
      421 rhwnsyylsp ywvldnvrst tksdivntti nlgyeindni nftvlgnaif rqtnteykrn
      481 aftepvvrvg drtassrytt rnrttreiys nykfnfdydl teditfkanv ggdirefnrk
      541 ylysgvnnla ieslsniasg asaptvtdak ykrraiglfg nfdfgfrdyl flnmtarndw
      601 tsklskdnns ffypsagvsf vptkafpslk tnvlnkmkls ysfvkvgnda aginainaiy
      661 ekpaafpygd ltsfrpdrti tdpnltpefi ashefglnvd lyrsrvtldf saftskntdq
      721 vvkvassras gveeaginig etssqgfevd lgfvpiktdd lrwdlrvsya tnktvvdkis
      781 dsldevvisn dtdvdivakk geefplikgi ayqrddkgrv ivdastgnpl qtdakvvlgk
      841 vipdyvlglt salnykgftl sttldyrtgh siyssvkkel vrnglavetv qsgrkgfilp
      901 nsvisdgkgg yvpntnvitg gttsnsitny ytgnfgdsae nfvldatalk vreisltydm
      961 pkdflkntgv nslqiglsar npfvllsndn rgftdpeyns aggdtskagd sfnnaggasr
     1021 ydllpptryy glsvnlsl
//
LOCUS       WP_101917663            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            piscium].
ACCESSION   WP_101917663
VERSION     WP_101917663.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum piscium
  ORGANISM  Tenacibaculum piscium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Tenacibaculum piscium"
                     /db_xref="taxon:1458515"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115855
     Region          21..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvtllwllf litqvtfaqe kmisgvvsde sgglpgvsii ikgtttgvet dfdgnyaika
       61 kqndilvfsf vgkatvqktv gassklnvtl addqnllnev vvtalgikre kkslgyatqe
      121 vkgdelskva tsnvanaisg kvsgvairks gniggstnvv irgntsitgn nqalwvidgv
      181 pmnndntnta dqkaggndgg fdygnaasdi npddiasmsv lkgaaasaly gsraangvii
      241 ittkkgreak gfgvtvnsgv tvgsvdketl peyqkeygag wggfganidl gsgshpflft
      301 addaawgpky dskllvygwe sfhpelatyg karayvapkn dpnsfyqkst tftnsvslqg
      361 stdkssfrlg ytkyeqnegi lpnskykkdn fsfsashnls eettvnasan yiktdalgln
      421 etgygtggng yassvrqwyt sdvdfatmkd ayfktrrnlt wnvwsptnre aafhdnpyfq
      481 ryenynnfnr drffgnfsin tkfnswmgat aragidtysq iqeertaigs krtgnlkgky
      541 srydktfref nmdlilnfnt ditenisftg liganarrsk drnvfsvtng gllvpkmysl
      601 ensietpnpa tenlvtigtn sayanasfgf ndtyylegtf rvdeastlps dsnvytypsi
      661 sgtyifskhl kadwfsfgkl rmnyaetgnd asfaviqsty tkqtnydgkp rfaiegtkkn
      721 pdlksestsa yeaglelkfl knrigldisa yrtvtsdqim dvaaapttgy yryyvnagev
      781 enkgieigls lvpvktndft wrtninwskn knkvrslfdd ldqfeigffq giksvakvgr
      841 plgtmiglgy krndkgqpiv gtdghyetve dviigdanpd wiagitnsfs yknfnfsflv
      901 dvkqggsvfs ldqkfgqstg iysntvgnnh lgnpvrnpvt tgadsggvin pgvladgtkn
      961 ekiiamdyya agkkpeeafv ydasyvklre vslsysvpsk fldksfiknv tlsasasnlw
     1021 iiskelpyad peatassgnl qgfqtgamps tkeynfnvkf nf
//
LOCUS       WP_101920899             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tabrizicola sp. TH137].
ACCESSION   WP_101920899
VERSION     WP_101920899.1
KEYWORDS    RefSeq.
SOURCE      Tabrizicola sp. TH137
  ORGANISM  Tabrizicola sp. TH137
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tabrizicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Tabrizicola sp. TH137"
                     /db_xref="taxon:2067452"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55195
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreif egenrvamtp dsvqalaklg htsvieagag akagfsdeay raagaevlpd
       61 akavfaaadv vvkvrgpeas eaallkkgqt lisffwpaqn eallkqvada gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtsvslg aivhafdvrp evaeqiesmg anfvflefeq tqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrpapkl wtedmvkmmk rgsvivdlaa erggncdltv
      301 pdqkivteng vtvvgytdfp srmaaqastl yatnirhmlt dltpkkdgvi hhnmeddvir
      361 gatvahegav typppppkia aiaaakpkek pkeltpeekr aqeaaafkkq trdqvamlvv
      421 ggglilaagl yapasfmshf ivfvlsvyvg vqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgnwl vvilaalsvf maginifggf mvtrrmlamf qks
//
LOCUS       WP_101942417             529 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Uliginosibacterium sp. TH139].
ACCESSION   WP_101942417
VERSION     WP_101942417.1
KEYWORDS    RefSeq.
SOURCE      Uliginosibacterium sp. TH139
  ORGANISM  Uliginosibacterium sp. TH139
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Uliginosibacterium.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Uliginosibacterium sp. TH139"
                     /db_xref="taxon:2067453"
     Protein         1..529
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55482
     Region          3..529
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mslligvpre vfagekrvat vpdvveklik lgfrvvvesg agelanfsdd ayrasgaeia
       61 gsaaelwsea divfkvrgpn daevelmrag stlisfiwpa qnpelmqkla akkvtvlaid
      121 alprqlsraq kmdaltsqag vagyraviea angfgrffng qitaagkvpp akvfiagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqremyakq arevdiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtiigytdlv srlsrqsstl yatnlfrlte elcktkdgli nvnfeddair
      361 gltvikdgei twpapapkip aaaakpaaaa apgakksshg hgepsepmsh qkmavtfgia
      421 aalfwiigan apaaflghft vfvlacfvgy mvvwnvkpal htplmsvtna vssiiaigal
      481 vqiappltad isrpdevirw lavgaivlat inmfggfavt qrmlamfrk
//
LOCUS       WP_101948778             359 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium sp. 3519A].
ACCESSION   WP_101948778
VERSION     WP_101948778.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium sp. 3519A
  ORGANISM  Mycobacterium sp. 3519A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Mycobacterium sp. 3519A"
                     /db_xref="taxon:2057184"
     Protein         1..359
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37250
     Region          4..356
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,71,90,283,309,311)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,273..274,316..317,321,
                     324..325)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,223,234,
                     251..253,260,262)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtligvpret aaderrvalv pkvveklraa gldvvvesga gtgalipdeq yeragatigd
       61 pwpadlvvkv npptkdeial lkpestivgf laprthpeva edlrlagvtg fameaipris
      121 raqamdalss qanvagykav lvaaseatrf fpmlttaagt vkpatvlvlg vgvaglqala
      181 takrlggktt gydvrpevad qvrsvgaqwl dlgidaageg gyarelteae raqqqdalek
      241 aitgfdvvit talvpgrpap rlvtaaavrg mkpgsvvvdl agetggncel tepgqtvvkh
      301 dvtiasplnl patmpehase lyakniasll ellikdgeva pdfedevvaa scvtreetn
//
LOCUS       WP_101950895             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium sp. 3519A].
ACCESSION   WP_101950895
VERSION     WP_101950895.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium sp. 3519A
  ORGANISM  Mycobacterium sp. 3519A
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Mycobacterium sp. 3519A"
                     /db_xref="taxon:2057184"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51909
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgetrvaatp qtvgqliklg yevvvesgag aassfsdaaf neagaeigda
       61 wtadvvlkvn apdkaeiaal regatlisli spalkpelve qlatrpitvl amdavprisr
      121 aqsmdvlssm aniagyravi eaagkfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivra tdprpevadq vaslggeyla vdpaaaevsa tgyakemgdd ykareaqlya
      241 eqskdvdiii ttalipgkpa priitadmva smkpgsvivd maaanggnve gtvkdqaivt
      301 dngvtiigyt dlagrlpaqa sqlygtnlvn llklltpekd gklildfedv vqrsvtvvrd
      361 geitwppppv qvsaapaaaa aapvetkpak qpmtiarrlg ltfaaaavlf alialspaal
      421 qvhltvfala ivigyyvign vhhalhtplm svtnaisgii vvgallqigh gaavvtvlat
      481 latllasinv fggfavtrrm lamfsrs
//
LOCUS       WP_101955151            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            finnmarkense].
ACCESSION   WP_101955151
VERSION     WP_101955151.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum finnmarkense
  ORGANISM  Tenacibaculum finnmarkense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Tenacibaculum finnmarkense"
                     /db_xref="taxon:2781243"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118346
     Region          26..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnpryknvlc ilfflgflvn vsaqqkmitg tvsdsagplp gvnvvikgtv tgaetdfdgt
       61 ytvkasagqr lvfsfvgmqn itklvgaktt invvmqedan vleevvvvgy gtstksaftg
      121 takvvkaevl aaksvsnisq alageaagvq vintsgqpga satirirgfg svngnrdplf
      181 vvdgvpfdga lntinpsdia sttilkdata taiygsrgan gvvlittksg kngvssield
      241 vktgvnfsnl arystikspe eyiglsweam rnkgdfngka datayananl fsgkgvnsay
      301 nlwnvsdvsk lidpatgkvr agvarkytpe nwadygfqts irteanlkms ggddktkyfs
      361 sfgyledkgy vlnsdykryt srlnlthnpt dwlkasvnlg ytfgkttsng qsedsgsvfw
      421 fvdnipsiyp lftrdtngkk iddpiygghi ydfgdagrgf galtnsiana kynlkrserh
      481 slnanfsfnf qlaenlsfes rygaqyysyi hnniqnpfyg saaggdtkgr lfkqnqyavt
      541 qnflnmfkyn tsfgdhkvdf iaahesnqwk rqrgytdvkr vvnlnngldd ptnyvetagk
      601 stgyreetai esffgqanyn ydgkyfftts vrrdgtsrfk nnkwgtfgsi ggswivtken
      661 fmndvefvnn lkvkvsygil gdqsigsrls diyagqngyd ienlggqisl pvrarqnael
      721 twetskmfqt gveftlfdnl vdasfdyyvk ntedlifdrr lgpsigdale kvndgklkna
      781 gfefditthi inkknytfdv slngeflkne ltqmpidpst gkaklldqsg nygrskghsl
      841 fdyymrewag vdandgaamw nvnyvdankn dafdkgeeik nynkfltdnp dakisqgttk
      901 vysqatqkyv dksaiptvrg afrlsakihd fdissqfays lggyaydgay anlmsngqvg
      961 gnnwstdmrd rwqkkgditn vprlysnevt avtssstrfl tstdylalnn irvgytipvq
     1021 yikkaglgsv nlyasgdnlf llskrdgfnp atsetgssdq yrysplttfa fgvrikf
//
LOCUS       WP_101955258            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            finnmarkense].
ACCESSION   WP_101955258
VERSION     WP_101955258.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum finnmarkense
  ORGANISM  Tenacibaculum finnmarkense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Tenacibaculum finnmarkense"
                     /db_xref="taxon:2781243"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122884
     Region          25..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqitktliv ffiltfqlty gqkkitasgv vsdqsgplpg vtilikgtaf gtetnfdgey
       61 tikttqkdvl vysfvgmktv kktvnstaai nvvmtedenl lneivvtgit vtdkrlftga
      121 stslkaadik ldgvpeisrg legraagvtv qnvsgtfgaa prirvrgats iygnskplwv
      181 vdgiiledai dvsagdlssg dastlisssi aglnaddies fevlkdgsat siygaramag
      241 vivittkkgk agvsninytn sttfrmrpsy tdfnimnsqe qmsvyeemra ggwlnyskva
      301 naresgvyge myqlydklda ngnfliknta qsraaflrka elrntdwfke lfninalqsh
      361 avnvssgtdr atyyaslsai vdpgwtkass vnrytanfks ifkvsdkltf ssistgsfrk
      421 qkapgtlsqd tdlvtgtvkr dfdinpfsya lntsrvldpa knytrnytdf niskeleeny
      481 idinvanlkf qselkykvns kinlsalgal kyqtsslehn ttefsnqana fradyneiir
      541 nanpflytdp dnqyatpisv lpeggifrkt thsmlgydfr gtfsykdvin ddhtvnfyag
      601 aeansadrkk tnftgwglqy slgevpfygy elfkksieen tlyyglkntk yrnlaffgnt
      661 tyswkrrytl ngtfryegsn klgkskasrw lptwnvsgaw nvheedffvh ldplesltfr
      721 asysltadrg pesvsnslvd irsynpwrps agskesalyv aglenselty ekkhelnvgf
      781 dtslfdgrla igadwyqrnn fdligptntq giggeiikyg nvaemkssgl elsisgtpik
      841 tedfswqtsf vysktknevt kldsqqrvid lvtgygfakq gypvkaifsi pfaglneegl
      901 ptfqdqegev sigelnfqer dkldflkysg sadptdvgsf gnifkyknlr lnifttysfg
      961 nvirlnpvfs srysdlsalp kefenrwilp gdenftnvpv iastrqenrv geydlrtayn
     1021 aynysdaria kgdfvrlkev slafqfpkey vtkinvksls lklqatnlfl lysddklngq
     1081 dpeffnaggv asplakqitf tlklgl
//
LOCUS       WP_101955572            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            finnmarkense].
ACCESSION   WP_101955572
VERSION     WP_101955572.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum finnmarkense
  ORGANISM  Tenacibaculum finnmarkense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Tenacibaculum finnmarkense"
                     /db_xref="taxon:2781243"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111693
     Region          21..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvtllwllf lvsqftfaqe ktisgvvsde sgglpgvsii ikgtttgvet dfdgnysina
       61 kqndilifsf vgkattrktv gasnkinvvl addenllnei vvtalgikrk sdeittanqv
      121 vkadeitkae vptvtqglvg kvsglqintt sqgakptfdl rlrgnrsltg nnsalividg
      181 aisssvvlna ldpksiesvn vikgangaal ygsdgsngvl ivttkkgnnd gkfrvtigts
      241 vqvqelaylp erqttygqgw gtginlaeng gwgpafdgsl qpigvaapgs aqmyapyvgn
      301 adnindffnt gfqrqhnigl stgsladgyv nfsaglldvt siipnekykr ssfnfkagkk
      361 vgkltvdgav syivdsekva ssetdrgdns vygallqtpt nidvnrfkdl qgderntrhw
      421 nsyylspswv ldnvrsttks diintsinlg yeindninfs vlgnavfrqt nkeykrnaft
      481 epvvrvgdrt asstfstrnr ttreiysnyk fnfdynlted itfkaniggd irefnrkyly
      541 ssvdnlaies laniasgasa psvtdakylr rafgvfgnfd fgfrdylfln ltgrndwtsk
      601 lskdnnsffy psagvsfvpt kafpslkndv lnkmklsysf vkvgndaagt yainaiyekp
      661 dafpygtvts frpdrtitdp nltpeftash efglnvdlyr sritldasvf sskntdqvvq
      721 vaasrasglt taginigqts stgfeidlgf vpiktedfrw dlrasystnk tvvdkisdsl
      781 deivisndns vdivaqkgqe fplikgiayq rddkgrviid antgnplqtd akvvlgkvtp
      841 dyvlglsssf nyknfslstt ldyrtghsiy ssvkqelsrn glavetiqsg rkgfiypnsv
      901 ikgadgkftp ntnvitggtt ansitnyytg sfndtqenfv ldatalkvre islsydmpkd
      961 flkntgvstl qiglsarnpf vilskenrgf tdpeynstgg dnsanaggaa rydllpptry
     1021 yglsvnlsl
//
LOCUS       WP_101955832            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            finnmarkense].
ACCESSION   WP_101955832
VERSION     WP_101955832.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum finnmarkense
  ORGANISM  Tenacibaculum finnmarkense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Tenacibaculum finnmarkense"
                     /db_xref="taxon:2781243"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116644
     Region          25..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lllalivqfs faqdrtisgi vsdesgplpg vtvlkkgttq gtetdfngky
       61 tikskngdil vfnfvgmkti qktvgtsnqi nivmendnvl devvvtalgi krekkslgya
      121 sqeiksdain ggttktgnia sqlsgkvagl nvtttnnfgg ssnmvirgvk slgggspliv
      181 idgspinnss tftggndygn alsdinqddi asmnilkgaa asalygergi ngvivittkn
      241 gksgddnswg ikfssgitvg tidkatfpey qntygggygq gfdhgndytn ydsdgsggpk
      301 ydgslkyhwd afdttspnfg kkrayvaakn gpsslfktsf tktnsisiqk gdqsknmtft
      361 yenfdsdwil pnseleknnf slkvnydltp klhtsfyssl tlqdtqgrnt tgysdnlmsm
      421 frqwwnvdvd vleqkdsyfr nkaiasvdnr ygniswnrks ptnskpaywn npyfqlyena
      481 gsdnryrsfs ygritydind nlgvtgkvay dksmlniekr iaagsiamdf gasentvpsg
      541 ysrqdiarse tnldlmlnyn yelvedikvs gvlganlrkn dynsiyaste gglvvpgiys
      601 lantvkspla atenqyntet nsayltasfd fykkfyldat wrldksstlp aanntynyps
      661 vtgalivsef ykpewlsfwk vranyaevgs tadpyelqns yasagllngv glydtnytkk
      721 nsnlkpqrsk eyefgtemmf lnkritfdfa yyntktfdqi islpvstatg yskkvvnagq
      781 innsgfeaql glvavkndnf twnidlnwsk nknkvvslsg dsenyqlasy pggvslnafk
      841 gkpwgtligp gykedkngnk lmetyqskgv tyaryikdgs knlgnvtpdw iggmrnsfty
      901 knfgfsflid vrkggkvfst dmyyglgtgl yketagnnvr qtgvvlpgvf edgtkntiia
      961 rnpqaygavd gwkvkpseaf vydggfvklr eaaisyslpk salknsfind akislvgrnl
     1021 wiiskdlpya dpeamvgggt rsyghsigst pttrdiglnl tfkf
//
LOCUS       WP_101956166            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            finnmarkense].
ACCESSION   WP_101956166
VERSION     WP_101956166.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum finnmarkense
  ORGANISM  Tenacibaculum finnmarkense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Tenacibaculum finnmarkense"
                     /db_xref="taxon:2781243"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120126
     Region          26..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnfklfvsi llgvfissti laqsstisgv isdgsyplpg asvvlagtti gadtdfdgkf
       61 elnkvtsekv tlkisfigyq ekrvqvslsk gahkklgtiv lkqleqqlde vvitalgikk
      121 eekalgysvs nlkaaelnqa ketnlvnaln gkiagvqitn gstgvgstsr vvirgeaslt
      181 stangplfvv dgvpihnnti fgtgqntggn emqevdygng aseidpdnva nisvlkgana
      241 aalygsrgsn gvilittkta rrnkgltvtv ntgttiekal rlpkyqnkyg qgwagkfkya
      301 dglandlgin dqedvswgpe angqlvtqfd spttsgvrag difvrgwvrd angkiisptt
      361 mpndiiatpf varpnnvenf yktgftttfs taigfgadks dflfsfgsld nqgiipntgl
      421 krksyrings vdltdklkis lksnyiksss dnrpssgygs esamymftwy grtvntsalk
      481 nywqkgyegl eqynynyawh dnpyfmlnen tnafnkhrll gniqleyqvl knlkfqaksg
      541 ldyytdkras kraystqrfl kgaykdervd ftevntdflf sydkkindaw nvdvnfggnq
      601 mkqeinflss manglvipgl ynlqnsisnv vttqykeeke inslygtlgi gyknkvfvdv
      661 tarndwsstl paknnsyfyp sasvsllidk ifempeafsf fkirgsfaqv gndtsaynlk
      721 tpysyqtpya gnktlsrssv llnenlkpem stsyefgtdl rmfngavgid ftyykstsed
      781 qimsvpitnt vgysaqiina gkienkgiea lltikpirne nfawttslnf sknqgtvvel
      841 tenmdvltma yasvygaets kvfiqarkge klgnmygrkf erhngkivyk dgkpvvndkl
      901 qllgnynpdf slgfknsfky knfdlsvlmd wkqggtiisr tkqiaayagn ldisenrnny
      961 qdivpdgvkk vgseyvaltd adaigwwsyy kplynrknqq etgivdatyv klrevkfgyn
     1021 vpagliekla meslkvsivg rnlglwtpss nphfdpetla mqganvvpgi edvsypssks
     1081 yginflfkf
//
LOCUS       WP_101960838             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            harveyi].
ACCESSION   WP_101960838
VERSION     WP_101960838.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54533
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvaiesqag vlasfddaay eaagakivss
       61 eevwtsglil kvnaplvdee kgideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgrpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqvitta ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvvkeg evtwpappiq vsaqpqakpq epvkpqpkve eptspvkkfg alavgagafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_101984954             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_101984954
VERSION     WP_101984954.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53575
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaesklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_102018532             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. TH135].
ACCESSION   WP_102018532
VERSION     WP_102018532.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. TH135
  ORGANISM  Rhizobium sp. TH135
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rhizobium sp. TH135"
                     /db_xref="taxon:2067451"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55054
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspreiy agearvamtp dsaaqlqklg yecviesgag kaaglsdday raagvtvvet
       61 aaalfetadi iakvrppets evdrlgpgkt lisffypaqn salleqakak gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aqfvylefea tqdgaatggy aapsspefre
      241 kqlakfrela peidivitta lipgrdapkl wladmvaamk pgsvvvdlaa erggncdltv
      301 adqkivseng vtivgytdfp srmaaqsstl ystnirhmmt dltpakdgvv vhnmeddvir
      361 gatvtkdgei typppppkiq aiaaakpkek vkeltpeekr aqeiaafktq trnqvgmlag
      421 ggalillagl yapasfmshf ivfvlacfvg fqviwnvshs lhtplmaitn aissiiilga
      481 lmqigsgnfl viilgalsvl maginifggf mvtrrmlamf qks
//
LOCUS       WP_102013064             227 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Klebsiella pneumoniae].
ACCESSION   WP_102013064
VERSION     WP_102013064.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         <1..227
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          <1..226
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 dlasqnggnc eytvpgevvt tangvkiigy tdlpgrlptq ssqlygtnlv nllkllckek
       61 dgnividfdd vvvrgvtvvr egeitwpapp iqvsaqpqaa akkveapkea vkpaspwrky
      121 almalaiilf gwlanvapke flghftvfal acvvgyyvvw nvshalhtpl msvtnaisgi
      181 ivvgallqig hggwvsflsf iavliasini fggftvtqrm lkmfrkg
//
LOCUS       WP_102035897             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            sp. 11B5].
ACCESSION   WP_102035897
VERSION     WP_102035897.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. 11B5
  ORGANISM  Shewanella sp. 11B5
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Shewanella sp. 11B5"
                     /db_xref="taxon:2058298"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53401
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresi kgetrvaatp atvvqliklg fsvaieaqag vkssfdnaaf eaagadvvdn
       61 vydadfifkv napsddeiak mkpgttlvsf iwpaqnpelv eklsshnitv mamdmvpris
      121 raqsldalss maniggyrav ieaahefgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggsfl klefenkegg ssdgyaktms eefiaaemal
      241 faeqakdvdi iittalipgr papklitkdm vdtmkpgsvi vdlaaatggn ceytvtgerf
      301 itdngvkvlg ytdlpgrlpa qssqlygtnl vnlmklmcka kdgnavldfd dvvmrnmtvt
      361 rggeitfppp aisvsaapqk paasiepkaa kvdkapsklk yilgvlglag faavasvapa
      421 eflshftvfi lscvvgyyvv wnvshslhtp lmsvtnaisg iivvgallqi gqgsalvtal
      481 afvavliasi nifggftvtq rmlkmfrkd
//
LOCUS       WP_102030811             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhodococcus].
ACCESSION   WP_102030811
VERSION     WP_102030811.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37995
     Region          12..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(25,80,99,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(54,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgtgravtar ptvgvvretn dgerrvalvp mivpslikkg ldvvvesgag lgalipdeay
       61 aeagarigda wsadvvlkva ppsdaevarm rsgqtligfl aprnaenqig altaagvqaf
      121 avesiprisr aqvmdalssq anvagykavl vaasestrff pmlttaagtv kpatvlvlgv
      181 gvaglqalat akrlggrttg ydvrpevadq vrsvgaqwld lgidaagegg yarelteder
      241 aqqqaaleea ikgfdvvitt alvpgrpapr lvtaaavegm kpgsvvvdla getggncelt
      301 epgqtvvkha vticsplnlp atmpehasql ysknvvalle lmldenggla pdfsdeilag
      361 acvtrskenv
//
LOCUS       WP_102038336             467 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella sp. GutCb].
ACCESSION   WP_102038336
VERSION     WP_102038336.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. GutCb
  ORGANISM  Shewanella sp. GutCb
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Shewanella sp. GutCb"
                     /db_xref="taxon:2058315"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52221
     Region          1..467
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvrtltkkaf alsamvaasl iagsafasdk teprnevykd kfknqyetwh etseskevvd
       61 mleqvpslvv lwagygfakd ynaprghmyv itdlrntlrt gapksaedgp mpmacwscks
      121 pdvprmieeq gedgyfagkw skggpeivna lgcadchvkg ssklrmsrpf aerametlgt
      181 pfdkaskkdk qsmvcgqchv eyyfektkdk kgfvkfpwdn gttveqmevy ydniefsdwt
      241 havsktpmlk aqhpgyetwq lgvhgknnvs ctdchmpkvk sekgrkftdh kvgnpfdrfe
      301 etcgscheqs kefmvnlted rkhkvadlka raeaqlvkah feakaawdag atetemkpil
      361 mdirhsqwrw dyatashgva ahaadealrv lgtavdkaad ariklaqlla vkgvkqpivy
      421 pdtstkakaq aalgmdmkkm nadkaefkkt lvpqweaeae kreatyk
//
LOCUS       WP_102052970             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_102052970
VERSION     WP_102052970.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38735
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqsgag vnasvpdsay eaagatigsa
       61 sdafgaqlil kvvapndsel gqiksgsvll gmlnpfnndv iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlpa mvgadasaly arnlldfmkl lfdkdgqfti nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_102061265             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. QC2].
ACCESSION   WP_102061265
VERSION     WP_102061265.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. QC2
  ORGANISM  Pseudomonas sp. QC2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. QC2"
                     /db_xref="taxon:2065822"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38686
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag lkasvvdnay eaagatigsa
       61 ndafgaelil kvvapsdgel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_102066801             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ralstonia
            pickettii].
ACCESSION   WP_102066801
VERSION     WP_102066801.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia pickettii
  ORGANISM  Ralstonia pickettii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Ralstonia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Ralstonia pickettii"
                     /db_xref="taxon:329"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39288
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipqetr adetrvaatp etvkkyvalg hqvtvqsgag vaaaqpdday vaagakigta
       61 aealgaqivl kvrspeaael aqmqpgavlv gmlnpfdden tarlaaanit afaleaaprt
      121 traqsmdvls sqaniagyka vmvaanhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfltdee reiaqgvggy arpmpadwmr
      241 rqaelvhtra tqadivitta lipgrraptl lseatvqamk pgsvvvdlaa aqggncplte
      301 adrvvvkhgv tlvgytnlas mvaadasaly arnvldflkl iidkdgglni nreddivaac
      361 llsqagqvvr apaatsaak
//
LOCUS       WP_102071555             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pollutimonas nitritireducens].
ACCESSION   WP_102071555
VERSION     WP_102071555.1
KEYWORDS    RefSeq.
SOURCE      Pollutimonas nitritireducens
  ORGANISM  Pollutimonas nitritireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pollutimonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pollutimonas nitritireducens"
                     /db_xref="taxon:2045209"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38740
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigiprerl sgearvaatp etvrkylank htvvveqgag iaahypdaay aeagaqlgda
       61 aqalgadivl kvrapdaqer qhikpgallv gmldpfdaag iaalaqtgvt afaleaapri
      121 traqsldvls sqanlagyka vllaanqygr lipmmmtaag tlkaarvvvl gagvaglqai
      181 atakrlgavv easdvrpaak eqieslgakf idvpfetdee rdiaqgiggy arpmpaswmt
      241 rqallvaerc rqadivista lipgrpapvl isaetvqamk pgsvivdlav erggncplse
      301 kdkvvekhgv tligysnlpa mvatdasaly arnvldfmkl ianadgqlai qqedeiitac
      361 lmcadgkvir sa
//
LOCUS       WP_102073456             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pollutimonas subterranea].
ACCESSION   WP_102073456
VERSION     WP_102073456.1
KEYWORDS    RefSeq.
SOURCE      Pollutimonas subterranea
  ORGANISM  Pollutimonas subterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pollutimonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pollutimonas subterranea"
                     /db_xref="taxon:2045210"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38867
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigiprecl sgearvaatp etvkkylank htvvveqgag iaahypdeay aeagaqlgds
       61 tqalaadivl kvrtpdaqer qhirrgavlv gmldpfdaag iaalaetgvt afaleaapri
      121 traqsldvls sqanlagyka vllaanqygr lipmmmtaag tlkaarvvvl gagvaglqai
      181 atakrlgavv easdvrpaak eqieslgakf idvpfetdee reiaqgiggy arpmpaswma
      241 rqallvaerc rqadivista lipgrpapvl isaetvkgmk pgsvivdlav erggncplse
      301 kdkvvekhgv tligysnlpa mvatdasaly arnvldfmkl itnadgqlai qqddeiitac
      361 lmcadgkvlr sa
//
LOCUS       WP_102087182            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sp. MES1-P1E].
ACCESSION   WP_102087182
VERSION     WP_102087182.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sp. MES1-P1E
  ORGANISM  Psychroflexus sp. MES1-P1E
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Psychroflexus sp. MES1-P1E"
                     /db_xref="taxon:2058320"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113009
     Region          26..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktyyllsl flmvffahss faqiatisgt vtsengiplp gvsilikgts kgvisdfdgn
       61 fsvnvadgag ktlaisyigf rtvevkltge nqivnvilee dfnaldevii vgssltqsrk
      121 klgnavttik skelvkgapv nittslqgkv pgaqitqnsg dpaggfsirl rgpstikgss
      181 eplyvvdgvi tsnlttnvtn lnvtagdaqp gqnrmvdinp ndiesiniln gaaaaaiygs
      241 rasngvvvit tkrglstkdg pelyfkstfn vstirkkldl nlrgeefeti adsplsgrlw
      301 pifgfnpdtg altpfnylds nkfdttrydy qdevfqtgfg tdnyfsardg nekmnymasi
      361 gylsnegiir ntsfnrfsar lnfnhnpvdw lsydvglyya nsqsdekpdg nvfwspinsi
      421 nitnnvfdit rrdasgnlla ventrinpls iietfditqq vnhyipnlhv kiipfenfii
      481 dqiigidtyn qkgnifipvy pyegvnpayf dqgfvgqaea kifnwnydin atfdtdinen
      541 lssqttagys fqasklefda vqgrdldsnn dptvslqtqp idtkldifgf flqetlsykd
      601 klfltlagri dgatnfdvdq rsnfypkisg syvlsnesfw addsfinsar lrasygeagn
      661 ltaispyerf ssytsndflg nttlqqnnrl gnenlapert kefeigtdls ffdnrasllf
      721 tyyrqniedl ivsrvlapsi ggssrtenvg tmrndgiely aritpikrdd fvwdvnfnfs
      781 snknevlkti ggdisivtvs gappvvqegq plgvfygtyf ardgngelil sgssttgapq
      841 gvpqpergdl atgspqrdan gqpigdllrk vigdpnpdyi lavgtdfayk kftfsmlwea
      901 vqgfdvfdad krtrqgvglg rlagqeltge lprgyiagiy pieefrmedg sfvklrevsi
      961 gyqfpslfid nlkdvkiali grnlisfdnf fsydpetnag gqsnllrsvn fgnvpipmtf
     1021 slslsanf
//
LOCUS       WP_102087209            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sp. MES1-P1E].
ACCESSION   WP_102087209
VERSION     WP_102087209.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sp. MES1-P1E
  ORGANISM  Psychroflexus sp. MES1-P1E
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Psychroflexus sp. MES1-P1E"
                     /db_xref="taxon:2058320"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116848
     Region          25..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqnvnwifl flfalishvg faqsqevtgt vvdnsglplp gvnviedgts ngtqtdfdgn
       61 fsieveqgav lvfsylgmke qkvtvgsqss fevtlkndtg qldevvital gitrekkslg
      121 ystqqvaged ltvtrssnai nslsgrvagv qisnssanlg gstrilirgi gsvtqenrpl
      181 yvidgvplan dnfnpggtst ggggrdfgdt gsdinpddie nmqvlkggpa aalygnrain
      241 gvilittksg kkgkgqvvvn sglsfesvnv tpnvqkkygg gagnpntlgp gsfnsqtigg
      301 tdyqlvdyat deswgpqydp ntsvlhwdaf dpefaddfln prpwvypend qedffrtgvt
      361 lnnsvsfsng ddnsqyrasi sniqaegvvp nsnldkttvn fngttkvgdk lkvgsnfnyt
      421 rtsgfnrpst gysgnsvilq fyqfgqtqld serlkkyvtp sgqqrtwnrv afdnptpryt
      481 dnpywiinnn taqdernrfy gkifanyqit ddlsaevnay gdtygaeinq rrvngsqaqs
      541 fysqfntnyk efnyegrlsy nkkfldnklt lnavgglnrr dvristlsge tqgglivngl
      601 fnlgnsanqs tvsdddsslr vnsvfatasv gydnflylna svrndwdssl padnnsylyp
      661 svssslvfse lvefdwlnfg klrggyaqvg ggtdpnnlrt vysnpnnlnf lgnptfsqpg
      721 nklnpnllpe qkktweigle mgflknrisf dftyynerte dlitpvsvdp gtgytgttvn
      781 agelenkgie llvnvrpiet edfswdvtvn farnrnklls lidgveslql arfpfngvsl
      841 navvgeaygq irgtnyvfdd lgnkvisagg syletqdven lgsilpdfnm girnsisykn
      901 frlsalidiq qggkfrsltn iwgnysgile qtargniree gvvlsgvtgd vtfnddgsyt
      961 vtntatnttv isaqqegqdh ffgndnqnvf dadyvklrel nltytfnkew fggfvqdvql
     1021 safgrnlavw gldnenfdpe iatggsgnvq gseggslpst lsyglnlqlk f
//
LOCUS       WP_102080106             379 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Ralstonia].
ACCESSION   WP_102080106
VERSION     WP_102080106.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia
  ORGANISM  Ralstonia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Ralstonia"
                     /db_xref="taxon:48736"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39384
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipqetr adetrvaatp etvkkyvaqg hqvtvqsgag vaaaqpdeay vaagarigta
       61 aealgaqivl kvrspepael aqmqpgavlv gmlnpfdddn tarlaaanvt afaleaaprt
      121 traqsmdvls sqaniagyka vmvaanhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfltdee reiaqgvggy arpmppdwmr
      241 rqaelvhera kqadivitta lipgrraptl lseatvqamk pgsvvvdlaa aqggncplte
      301 adrvvvkhgv tlvgytnlas mvaadasaly arnvldflkl iidkdgglvi nreddivaac
      361 llcqggqvvr apaatsaat
//
LOCUS       WP_102088318             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Psychroflexus sp. MES1-P1E].
ACCESSION   WP_102088318
VERSION     WP_102088318.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sp. MES1-P1E
  ORGANISM  Psychroflexus sp. MES1-P1E
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Psychroflexus sp. MES1-P1E"
                     /db_xref="taxon:2058320"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35821
     Region          5..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifelfskr qkrlrgefpk iytydsipeh lrvqivhiik daigvvihgr knepeevyef
       61 ihqtlcreyg ifslgdryrk ndednvlnfl lttknnekvi dvielsfkyi driikpsyde
      121 yelntrveik pdeaieelne rfkehgigys fdgseiirvd styahaeitk ptisllwntk
      181 fdganeeylk ahehyrhgrn keclteclka lestmkiics ekgwnykqtd taktliqicf
      241 enqlvptftq nqftslksll esgiptirnk lgghgqgqtq qivddemtry glnltgtnii
      301 flieqsgik
//
LOCUS       WP_102088600            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sp. MES1-P1E].
ACCESSION   WP_102088600
VERSION     WP_102088600.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sp. MES1-P1E
  ORGANISM  Psychroflexus sp. MES1-P1E
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Psychroflexus sp. MES1-P1E"
                     /db_xref="taxon:2058320"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111088
     Region          26..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqnlltkii cvmflflggl lhsqsvsgtv ndkvvslpgv nisvkgtnng vqtdmngtyt
       61 lkdvsiddii vfsylgyktq evvysgqlvl diilledask ldeivvigyg tttvkdatga
      121 vttvsakdfn ggviaspeql iqgkaagvqi sqasgepgsg iairirgtss vrsnnnplfv
      181 vdgiplsdgg tagaadiggg ggsarnplsf lnpndiesmt vlkdasatai ygsrgangvv
      241 iittksgirg sggvfefnsn tsfstvsktf dllngpqfls aisqyggnas eldfgantdw
      301 qdvvfrdvis kdnsfsysnn ygdgyvrasl glvdqqgvve nssqakftgr inashkfldd
      361 klkvdvnaty sriddeapfi tnsagsqgdl lgatyfanpt wpndlnftsg dgklnprqll
      421 dyyedlnetd rvlvnagaey silsnlkakv nlgydqskat rtqvlspdad gfnngvtgng
      481 raalqdlnve nkliditlny tkdfgnsnle vlagysfqsf rnygrtiqgf glntsnlaem
      541 annlenaadl iqgsigdtpy qqygfssngl finqilpiin snvsltsptg ipvnsvtgnf
      601 ydntdelqsf fgrvnykind kylftftlra dgstrfgtnn qygyfpsgaf awqlhqedfi
      661 peafstlkmr vgygitgnqd glgygnflpr qrfadpsign ggevnppgfs lvsfanpdlk
      721 weetaqfgig fdygffndrl ngsvdiyhks ttdlllqqes aqpavqpfvf snldasvinq
      781 giefmanydi iqqddmnwnf gfnvaynene vqdfdgliqt ggingngltg afaqllaegr
      841 plfsyylref agfdengisi ypngdqqqfv dksalpditl gintsfsyrn wdvnafltgq
      901 ygqyiynnta nafftagiin sgqnvnanvl tngesganap dvstrflekg dflrlqnlsv
      961 gysvnlkees flnglrfsli gqnlfvitpy sgldpevdtp sslnnipsag idytsfprat
     1021 tvtfglnasf
//
LOCUS       WP_102088892            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sp. MES1-P1E].
ACCESSION   WP_102088892
VERSION     WP_102088892.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sp. MES1-P1E
  ORGANISM  Psychroflexus sp. MES1-P1E
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Psychroflexus sp. MES1-P1E"
                     /db_xref="taxon:2058320"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111692
     Region          26..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngilt lilvlfvqit faqtntvtgt vtdpdglplp gvnilikgen tgtqtdfdgn
       61 ysiqaspdqt lifryvgftt knvkignklq idvnmsidsa tldevivtgy snrnqtvats
      121 atvtisaaei nelaptttid nllqgkaagv qvtaangkpg qgafvrirgt gsltagassp
      181 lylvdgapid edvlaaipns diaeikilkd asttarygsr gangvviitt ksgnrnkdak
      241 itlnsrfgqt eriepnfkmm naqqkfqyea emfalgisga sglpgvttep gsperqflld
      301 nqtdwedlil rkgilqsnnv sisggsekld yyfstghdrn tgiidqiggf erintrlnvn
      361 fdakewlkig vnvgysrsts deprdrnnvq naframldyn pyetefvldd vgnpvldasg
      421 npvysptsts fnlrgalise psknidnlls ssftadikls dnfsynfras inslnersdr
      481 askpggilqe ligsaefpgt ktdngsysfd ltvtnslnyn lkkgkntlnl lglyeynmne
      541 fnsynvssrg fsspllttqa saaevtfgss grsrlalvsy glfadydfdq kylftasgrf
      601 dgssnfgsge qygfffsvsg gydisrenff dvepidelif rgsygttgnr sglgrysqlg
      661 tvgfnsypgg sstipsnien salkwetsyn tnigvqlsmf ngrltavsdy firdtedllf
      721 eipkadesgi esvngnlgei qntgfeislr gdvirnedvs wtlggnvlfl dteivslpdg
      781 edvfpntfni lyregakine hnlvrwagvd patgrsqyld annnvvfada lteedaedar
      841 vlqgkstiad ieggfysnfr yknislrtdf vfksgnwinn vvrqqrnadg dqvdsnqats
      901 afnywkqpgd tnvqpsplyr qddinvnsdr flekgdyirl rnvtlaynfs kevlektpfs
      961 slrfyvqgqn lltftdfygd pevgissges isfgntvapg eitlysypnl ksfqigldvs
     1021 f
//
LOCUS       WP_102089255             970 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Psychroflexus
            sp. MES1-P1E].
ACCESSION   WP_102089255
VERSION     WP_102089255.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus sp. MES1-P1E
  ORGANISM  Psychroflexus sp. MES1-P1E
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 970)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Psychroflexus sp. MES1-P1E"
                     /db_xref="taxon:2058320"
     Protein         1..970
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106628
     Region          23..969
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtikllgll lmllpmsifa qstvsgtvvd nsgmpipgvn iavkntnkgt ttdfdgnyli
       61 vlengetlsf syvgfrtkdi vfngkntsie vsmvedaeal sevvvvgygn qtvksisgsv
      121 asvtekdfnk gnivtsesli qgrvpglsvt kgggpgsgse irirggssfn annsplivld
      181 glpldnsvad gtrsilstin pndiesfsvl kdasaaaiyg irasngviii ntkkgrgels
      241 vsldvqqnit tienivdvls agqfrnlvae nfpgrlgelg santnwqdei yrdakssdin
      301 lsvrgalfgk ipsrlslnrs dqqglrqtsk fdrttaslsl nprlfddhlk vglnanysne
      361 dnrfadgveg naisfdptqp vrspgspygg ffefldndgs aasnvprnpv sqllqtrnis
      421 nadrlfgnln ldykfhflpk lrlvtnlgyd rtdsggsltr pgtsalgvna eqgefignes
      481 ryeqtrtnas adsyfiyknn fndfglkltt gysyqkfese rfttneildp naqeprttva
      541 ddvvligyfg ranfsfqdky fvnasirrdg vskfspenrf eyfpsvsgaw ilteedfled
      601 snlinslkvr agwgqlgqqd vpstsdylrr yqtglsnqqy nfgnpiipfq plytnpdikw
      661 eilteinlgv dfelfnnrls gsvdvferta ddllsnvpvp dganfsnqgf qnigefvskg
      721 ievnldynvi rqddinwnvn ynftaidrei tklafgqdif vggiaggtgn tiqvqregaw
      781 pnsfftyaql ydqagqpieg ayadlngdgt vddrdryvsg ngqadvlmgf qsnftyknfd
      841 fnfnlrasfg ndiynnvnss raqlgnlnlv spnnlpvqvl etgfartpdv ilsdffveda
      901 sflrmdnitl gytlrgfnre stslrfwmgl qnafvitdys gvdpelnisg idntiyprgr
      961 tyllgvnynf
//
LOCUS       WP_102112048             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Niveispirillum cyanobacteriorum].
ACCESSION   WP_102112048
VERSION     WP_102112048.1
KEYWORDS    RefSeq.
SOURCE      Niveispirillum cyanobacteriorum
  ORGANISM  Niveispirillum cyanobacteriorum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Niveispirillum.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Niveispirillum cyanobacteriorum"
                     /db_xref="taxon:1612173"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40206
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,323,325)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,330..331,335,
                     338..339)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipkerr ahelrvaatp dtvrkyiglg fevvvetgag lgsaitdeaf taagatiaad
       61 vtstltgadi ilkvqrplae gegdvnelal ikpgailiag lspygapetv aayaagkida
      121 famefmprit raqsmdilss qsnlagyrav ieaanefgra fpmmmtaagt vpparalimg
      181 agvaglqaia takrlgavvs atdvrpatke qveslggtfv avmdeefqqa qtaggyakem
      241 skeyqakqaa liaetikkqd ivittalipg rkapvlvtdd mlktmkqgai lvdlaceqgg
      301 nvegavagev vekygvkivg rinmpgriav dasalyaknl lnfitpfvdk etktlkmnwe
      361 ddvvkgtglt rdgavvhpsf nkpaa
//
LOCUS       WP_102092430             383 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Psychrobacter].
ACCESSION   WP_102092430
VERSION     WP_102092430.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter
  ORGANISM  Psychrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Psychrobacter"
                     /db_xref="taxon:497"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39854
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvisadi tsesrvaitp davkklrklg fevviqsgag qaayyadely qaagadiass
       61 rtevitqski ittvndlpae ateslssgqi vigmldpyrn tqldtyaakg atvfamellp
      121 rtlsraqnmd vlssqanlag ykavllaane ysrpfpmfmt sagtvkpakv vilgvgvagl
      181 qaiatakrlg avveasdlrp tareqveslg gkwldvpmsa eeaetakstg gyawtpseqy
      241 vkdqaavvdk alsnadivit taqipgrnap rlvhgatlak mkagsvlidm aagtggnveg
      301 svpdqtittd ngvrivgaan ipsmlaaqss dlyannlvnf ittliapasd dasaslalnv
      361 dmedeiqgal avthdsqvrl akr
//
LOCUS       WP_102107007             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oceaniglobus roseus].
ACCESSION   WP_102107007
VERSION     WP_102107007.1
KEYWORDS    RefSeq.
SOURCE      Oceaniglobus roseus
  ORGANISM  Oceaniglobus roseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Oceaniglobus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Oceaniglobus roseus"
                     /db_xref="taxon:1737570"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55611
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspsevl pgerrvamtp dsarmlaklg hscvvqsgag leagftdday rdadvevvad
       61 avalwaaadv vakvrpptde evgrlregql lisffypgan kellekakdt gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg amtyafdvrp evseqiesmg aefvfldfee ssqdssatgg yaapsspefr
      241 ekqlekfrel apdmdivict alipnreape lwtpdmveam kpgsviidla aerggncklt
      301 kvderivtdn gvtiigytdf psrmaaqsst lyatnirhmm tdltpdkdgr irhnmeddvi
      361 rgatvthage itfpppppkv aaiaaakpkp kakeqtpeek raaevaafka qtknqvtlla
      421 vggvlllalg lvapasfmqh fivfvlsvfi gfqviwgvah slhtplmavt naissiivlg
      481 almqigsgsv pvvilsalav fmtginifgg flvtrrmlam fqks
//
LOCUS       WP_102123828             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium sp. ROICE36].
ACCESSION   WP_102123828
VERSION     WP_102123828.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. ROICE36
  ORGANISM  Janthinobacterium sp. ROICE36
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium sp. ROICE36"
                     /db_xref="taxon:2048670"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38721
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklavkh qivvqagagl qasipdeaya aagaqigtaq
       61 eaygcaivlk vrapdapera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpflteeek eiakgaggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvikhgvy ivgepnlatl vaadasalya rnvldflkli idkddlllid redeiikasl
      361 vcadsailrk
//
LOCUS       WP_102139979             477 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Providencia].
ACCESSION   WP_102139979
VERSION     WP_102139979.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Providencia"
                     /db_xref="taxon:586"
     gene            1..477
                     /gene="nrfA"
     Protein         1..477
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53351
     Region          11..477
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 manirnnalc llslvagifl ftsvhaqtpt kdststinar netfeaahpd qyhswratse
       61 qsnredalae dprlvvlwag ypfsrdynkp rghayaiidv retlrtgapk daqdgplpma
      121 cwsckspdva rliqehgedg yfegkwakgg pevvnvlgca dchktdsadf akgkpeltls
      181 rpyaeramet igkpfdkasr fdqqsmvcgq chveyyfsgd kkavkfpwdn gtkveemevy
      241 ydnvgfsdwt nslskapmlk aqhpeyetws agihgknnvt cidchmpklq nekgelytsh
      301 kignpfdnfe qtcstchtqs kqqlqdvvae rkvaiqemki kaedqlvrah feakaawdag
      361 atedemkpil tdirhaqwrw dlaiashgih mhapdeglrm lggsmdkaad artklarllg
      421 skgitheiai pdistkekaq qaigldmqki naekqeflkt vvpqwdeqar kndllak
//
LOCUS       WP_102144098             361 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium hubeiense].
ACCESSION   WP_102144098
VERSION     WP_102144098.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium hubeiense
  ORGANISM  Mycobacterium hubeiense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Mycobacterium hubeiense"
                     /db_xref="taxon:1867256"
     Protein         1..361
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37181
     Region          7..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdtqttvgv vresvaderr valvpkavas lvnrgvavvv eagagegall pddlytavga
       61 tigdawsadv vvkvapptpd evdrlksgqt ligflaprna dnqidalkak gvqafaleai
      121 prisraqvmd alssqanvag ykavllaase strffpmltt aagtvkpasv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg anwldlgiea ageggyarel tdeekaqqqk
      241 kleeaitgfd vvittalvpg rpaprlvtaa avegmkpgsv vvdlagetgg nceltepgkt
      301 vvkhgvtias plnlpatmpe haselyskni talldllikd gtlapdfdde viaascvtre
      361 a
//
LOCUS       WP_102147662             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Fischerella thermalis].
ACCESSION   WP_102147662
VERSION     WP_102147662.1
KEYWORDS    RefSeq.
SOURCE      Fischerella thermalis
  ORGANISM  Fischerella thermalis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae; Fischerella.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Fischerella thermalis"
                     /db_xref="taxon:372787"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41072
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalvp divarlvkqg leiwveagag eraffndaay eaagatiiad
       61 tnrlwseadi llkvspprer edgrseidll kegsvlisfl nplanpviaq klaarkvtal
      121 smemiprttr aqsmdalssq asiagykavl iaaaalpkyf pmlttaagti apakifimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve ikldeettaa ggyakeisea
      241 skkrtqevvt ehiknadvvi ttaqvpgkka pllvtedmvk qmkpgsvivd iaaeqggnca
      301 ctdpgrdiva hgvtiigpin lpsslpvhas qlyaknltsl mqllmkdknv einfaddiid
      361 aacithagei rstrikealq tvtsavs
//
LOCUS       WP_102152211             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Fischerella thermalis].
ACCESSION   WP_102152211
VERSION     WP_102152211.1
KEYWORDS    RefSeq.
SOURCE      Fischerella thermalis
  ORGANISM  Fischerella thermalis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae; Fischerella.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Fischerella thermalis"
                     /db_xref="taxon:372787"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41003
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalvp divarlvkqg leiwveagag eraffndaay eaagatiiad
       61 sdrlwseadi llkvsppqer edgrseidll kegsvlisfl nplgnpviaq klaarkvtal
      121 smemiprttr aqsmdalssq asiagykavl iaaaalpkyf pmlttaagti apakifimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve ikldeettaa ggyakeisea
      241 skkrtqevvt ehiknadvvi ttaqvpgkka pllvtedmvk qmkpgsvivd iaaeqggnca
      301 ctdpgkdivv hgvtiigpin lpsslpvhas qlyaknltsl mqllmkdknv evnfaddiid
      361 aacithagei rstrikealq tvtsavs
//
LOCUS       WP_102165824             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinotignum urinale].
ACCESSION   WP_102165824
VERSION     WP_102165824.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum urinale
  ORGANISM  Actinotignum urinale
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinotignum.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Actinotignum urinale"
                     /db_xref="taxon:190146"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52531
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqvgipknpr tgsplvagtp dtvtkliklg ytvavesgag sesaypdsqy eaagativga
       61 teawqadivl vpdapetqql dmmksgstli sriepgnnpd yvdalaarki talamdaipr
      121 israqsmdvr ssmanisgyr avieaashfg rlftgqvtaa gkvppatiyv igagvaglaa
      181 lgtansmgai vkatdvrsdv aeqvqsmgae fveipvtqes adgyaremta dqadaagvvy
      241 areaqaadiv ittalipnrp apilisketv akmkpgsviv dlaaanggnv egtvpgevvv
      301 tdnnvtiigy kdlalrlpgq asqlfgqnlv nflklitpek dgelvldled tivrgvtvtq
      361 estimwpppp vqvsaapatk paapaaaeav eekapspmrf vwfgiaalia laivftapah
      421 maghftvfml acvvgfyvit nvthalhtpl msvtnaisgi ivvgavlqla tgsiavlvma
      481 aiaiviasin ifggftvtar mlsmfkrs
//
LOCUS       WP_102171004             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Fischerella thermalis].
ACCESSION   WP_102171004
VERSION     WP_102171004.1
KEYWORDS    RefSeq.
SOURCE      Fischerella thermalis
  ORGANISM  Fischerella thermalis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae; Fischerella.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Fischerella thermalis"
                     /db_xref="taxon:372787"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41102
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalvp divarlvkqg leiwveagag eraffndaay eaagatiitd
       61 tnrlwseadi llkvspprer edgrseidll kegsvlisfl nplgnpviaq klaarkvtal
      121 smemiprttr aqsmdalssq asiagykavl iaaaalpkyf pmlttaagti apakifimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve ikldeettaa ggyakeisea
      241 skkrtqevvt ehiknadvvi ttaqvpgkka pllvteemvk qmkpgsvivd iaaeqggnca
      301 ctdpgrdiva hgvtiigpin lpsslpvhas qlyaknltsl mqllmkdknv einfaddiid
      361 aacithagei rstrikealq tvtsavs
//
LOCUS       WP_102187502            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_102187502
VERSION     WP_102187502.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113990
     Region          23..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvlfilfl iflscvsira qqkpitgnvv drngnpiewv svvvkhtnvh tttnqtgayn
       61 iiasvgdtls fsiigfdkeq rivgksnrmd imlheskdiv ladlvvtgys kqerrdltgs
      121 vasvklddnv sfrsvdqmlq gkapgvfmtt ssgalgsanv liirglssii gdnnplyvid
      181 gvpiygtdrs anstdvsgga ipaasmmgmq tgggslqynt dlkysfeknp latlnpddie
      241 sieilkdafa taiygsrgas gvvlittkkg skarprvtvn ytlgvdnplg klkllngkqy
      301 aqiysqyfng mnfpelydtd widavtrtav shnisasfsg gtqktvyfls laasdndsyv
      361 innnmkrysa rlnlttaiss kldlgvnvsi srldnnalqa peifasaikk apnlpiyded
      421 gsyyygyapn skgdpetynp vaqayindeg sedtrtigna ylewhpmswl ilrseigtdl
      481 ynsfssirkg alpdhvkgva gnqaqetttl ntkyvvtntl nvnkvfgdhf mqgivgqsye
      541 ytrerlnava gddffspdlv gvgaarskrv isaysqqsal fsafarlnyq yrmkymlglt
      601 yridgssrfn rshrylgtps vsagwrmsne rffrkalpfi nqaklrasfg vsskdgnnsy
      661 ygaqaiykln savnygdrny lqmsqpgndn lnwehtltwn ggldleafks rlkltldyyy
      721 kkttnmlfps nlplytgykk enqniadmmn sgldlqiise nivgknfgwq tvlnvstttn
      781 kilklnfegn qldqlnssfk yyqegkaaaq wylhrwagvd pntgdplwty adgtqstvpp
      841 aannetsqln kfvcgtalpt vygsisnslt yrnfeldiff nyalgshmin atratmltyt
      901 qnatnlskem mnlwqvpgqi tdipklnnas iigaydytta vtsdrflenn sylrlktltl
      961 syhvspallr ryklcrqlrv yatftnlftv tgysgldpev safgssvtas gydnctmpss
     1021 rsmqfgvsat f
//
LOCUS       WP_102187532            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_102187532
VERSION     WP_102187532.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121342
     Region          24..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkktiymli allacvlqvq aqervitgvv ldgdlkdepl igatvgkgag kvstgtvtdy
       61 egkfklsvgk dtkaisvsyv gyttqtislk pgvnhykivl mpdahsinev vvtgyqridr
      121 rkltasvttv disdkavgav knidqalagq iaglstvsss gapgapvkir irgtasingt
      181 qeplwvldgi plegtdipsm enlndiddmy qtsiaginps dienitvlkd aaataiygar
      241 aangvivitt kkgkegrpvi nfsakytysp klnidrlnll nadekvdlel gllasdytyr
      301 ehkgevanil ktlnetetyk regrnalsal aqtqinalrn ihtdwndilf rhamnqeyna
      361 siaggsnrsg yytsvgyyde qgnvkgvdnk rfnmtlkady rinkmlklga svyanqrkqn
      421 syltdtngft npvyysrlan pyflpfvegk yhydvnvqgk edssldfnif eerentshkr
      481 tdrslmaifn gelqftpdlk ltsqfglqyd nyslekyage nsfamrkehf natyaykdgk
      541 rsylpeggmh kttsynslqw twkalleyah rfnkvhdvel lagtevrhin sssvysaayg
      601 ydartltthp vifpnettae srplhrenqa enayvswfat gsytlfyryt lggsvrfdgs
      661 dvfgvakkyr ylplysvsgl wrvhqerfak kakwlsnlsl rasygiqgni dkntspylig
      721 fydktsilpg kgeqmikaet apnpdlrwek tknvnfgvdl glwnnaitls adyyyrrssd
      781 ligmrmlpqe tgfsattinw asmensgwei algsrniytk nfkwttnlnl gfntnkilne
      841 svaenstyps regypvgalf ayktagldkd gyplfvnkeg nkvtaaellk lnnagastls
      901 aseqralyty mgstdpkvsg gfinhfeykd wqlginfifn lgmkvrvqps ynpttydrgl
      961 nvnrdilqrw tpnnnqtafp klmtkdvrvp ehiqyseynt ysmldtwvkd rsymrlqslr
     1021 lgyklpskwl nkvgvtnasl slegrnlfvv atdytnyldp etmgnpfaqp maksvifgln
     1081 mnf
//
LOCUS       WP_102187648            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_102187648
VERSION     WP_102187648.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121290
     Region          25..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllflmvc fmsctaamaq taihgrvlne gtnepligat vveqntsngt vtdvdgafrl
       61 tvaklpvsik vsyigysekv vtvtsaqpli irmqdisnel setvvigysg siirskmtns
      121 iakvkneslt tgmfsnpsqa lsgavaglkv vqgsgnpnas ptivlrggtd ydgsgaplvv
      181 vdgmirssma dvnpndiqsm evmkdagata iygsranngv ilittkkgkd gegkvgfssk
      241 lswnyfnnpy kfldagdyly yqrrsylyae qkgtvtlssl sgnqpygtgn kyeadgnkss
      301 agiwgvyeyg alapdvqkel igkgwrtmtd pvtnktliyv nnhmedfnin tpsfsqdynv
      361 nfsggndrgh yytslgynns egnainnynr rlsfllntdy kikkwltsys sfnfstakyl
      421 gispfagegn yfsrnfsypp tfraynnkge lllgknsgdg nqkflenaid qdysrqkftf
      481 sqdfrfsivd gltldlkgdw yyqyytgqsf yhtylsspgr ystghksfae sekhltqtyn
      541 vllnynktlg khtvsgllgw eyfhqklfdl qasgsnpann yfrdleytvt degkrmvdtg
      601 hskfitqsyf arvnydydak ylvgitvrrd gisklskdnr wgtfpglslg wvfshekfme
      661 kttgwlsfgk vraswgkngn vnsswvgdyt vqgayamdty hgttsyylnn iptayltwet
      721 srtlelgldl gflnnkiqtn itwydrvtsd kyanivipas sgftsitsnn gklrnrgvel
      781 etnchilnta dwkvdwafni arntnkilql pdngrdknrq ggyevytgng dkkmwvggya
      841 enetpgdlwv fqaegiykty deipgnlidk stsnnggnnk flygpaayqs tgkaagglai
      901 mpgdikwkdv ngdgvidnyd lvkvgnmtpk wtggttltas wkglaltarl dfalgfktyd
      961 yrtpwimgnm qgtyntltnv kdtwsednpn akypiyiwad qlnarnydry nsmfvyngdy
     1021 lsfreltlsy slprqwlskv siesltvsvt gqnlgylcaa pyvfspevas nwggyplprm
     1081 lvlglnltf
//
LOCUS       WP_102187730            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_102187730
VERSION     WP_102187730.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122058
     Region          31..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkallffc fclislaiva qnpqksdamv qvvttitdtd gnplggatvk vkgkpvgvia
       61 dmdgkislwv drgntitvsy lgmksktikv tsaltknivl endaslleqv vvtgytrttk
      121 rrttgsvsti takdlnknpt anldmllqgk magvdvkals grpgesakvr irgtntitgn
      181 adplwvvdgv alqkdlptis kaqmlsgnfs difsngiagi npndiesvtv lkdasaaaiy
      241 gsraaggviv vttkrgvagk lrinysanat mvtrppravd lmdskeklaw eqelwdeysk
      301 pyfekneryp vvgivgmirs gygqykgmnk eqqdaeiarl gshttnwfde lfrnsvsqsh
      361 nlslsggsek stfyvslgys enaglvkktd ysryninskl dikpnkrvkl glsldlgwqt
      421 snspslavdl fkyayfanpy ervydeqgny aadqtyynim langskstlp lpdngvnimr
      481 einntssktk nfsttvigni tiniidnlnf eglgsysytt nngdnindkd tytawqdrpf
      541 dlktltskrt yssiaqsssy nssynlrgql hyfntfndkh yisgllgsei rgqyaksifa
      601 krygydpvsg nsampvypeg ktfeyndlkn yallmdnlsg qnivedrfas fyfsadyvyn
      661 nryvfsftgr tdgsnnfgsk eqfnptgslg lswnvdqesf meklkpiiss lslrtaygft
      721 gninksvhpq vimdyrqsfr ktdtdyyrmg wikkapnpnl rwektkdmkm sidagflndr
      781 irmtgeiykr itsdavsevf ipystgfrnq sfntsklsnt gaeftlsanv ikqddwnlli
      841 sgniaynrnr lleyksivsg lgegiyvgyp igsifsgkva gidsrlglit yeprpdavfe
      901 tsadrnnaen ylfylgtsna ptnggysmsl sykrltlsls gtyslggkil nqinspvgyg
      961 slsgttveki psqmndlyvn hlnvtrdvvn rwttknhrtd ahprildayg kyygldnyvv
     1021 sspkitkasl ledvsyfkig slnlaysfdt kliqriglss lsvsftadni ytftnysgid
     1081 pespgavypm arsfsmgvfv gf
//
LOCUS       WP_102189125            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_102189125
VERSION     WP_102189125.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122883
     Region          24..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrltmllv slflcvglan aqtqingtvt saddgqpvig asvmiagtkt gvvtnvdgkf
       61 sltsnkknpm itvsyigmks qtlhgtqnmr ivlhsdaqkv devvvtgmqk mdkrlftgaa
      121 tkvdaekakl dgvadisrsl egrvagvsvq nvsgtfgtap kirvrgatsi ygsskplwvv
      181 dgvimedvte vdadqlssgd aatlissaia glnsddiesf qilkdgsats iygaramagv
      241 ivvttkkgkv gttrinytge ftsrlkpsys qfnimnsqeq mgiyremean glisfartyr
      301 asssgvygkm yqlmntydst tgkfllphtq kgmndylmka emrntnwfne lfssaismnh
      361 svsvssgtek aqyyasfsim ddpgwteqsk vqrytastna lfnlskkvsl nlisnaayrk
      421 qkspgalnqh vdavtgevsr efdinpysya intsraldpn eyyttnyapf nihnelannf
      481 mdfdvidmki qgelkykpit kvelavlgay kfstttqanq irensnmama framddatmr
      541 dnnprlykdp dkpnslpfsv lpnggfyret kykmnswdfr atasyndvya ndhivnlfgg
      601 mevnntdrsr syfngvgmqy dmgylgaydy nyfkqaseen dvyyslgngy nrevaffatg
      661 tysykgryti ngttryegsn rlgkvrsarw lptwnvsgaw naheeawfgd afkntlthat
      721 lkasysltgd kpatinaqpi iesfnpwrpf atdkesglem ydfanpdlty ekkhelnlgi
      781 dlgffnnrln vtfdwytrnn ydligprttn gtkgtiteya nvasmksnge efaitskniv
      841 tkdfqwttdf ifshvktevt dldnrkrfid mvtgsgftmk gypyrslfsi dfqglnasgv
      901 ptflnqdgkl ttsdfnfqsr vldylkyegp tdptvtgslg nvfsykgfhl nvfatyafgn
      961 kvrldpafss yysdldampk efknrwtvag deaktnipai adlrtmqgdt rlgyaynayn
     1021 rstarvakgd firmkeisla ydfprhlltp lhlntlnlkl qatnlfllya dknlngqdpe
     1081 ffnvggvavp marqltltvr vgl
//
LOCUS       WP_102189172            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_102189172
VERSION     WP_102189172.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123488
     Region          28..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtgkkilifl lmtfyslcvt laqdkglfii kgkvvdside plpgvsvkak nmstktvttd
       61 dgsfiikvnk epielvfsyi gmrektvlck sqkaitvvle dnavnldnvv itgyqeidkr
      121 klsssittmk mselqtpstn sldqmlqgri aglavmnlss tvgvapkiri rgsssitgnr
      181 epiwvvdgii ldepvsvsve elnnidnvnf ignaisginp ddieridvlk dvsataiygv
      241 kaangvivvt tkrgkgerpt isykanwgvt mapnygildl mnskerievs eemlnrglef
      301 ktyrptdmgy egelqklwsk etdydtfrkr vkdlkelntd wmnllfrnal sqqhsvsvsg
      361 ggkrvdyyvs lgylhqegvs iveklkqltg kvkvnmqltn hleagvdlst nssdanyahh
      421 sialldyayr tsraipafhd dgtyfyynnd vtkyaslpfn ifnelnttgq dvakkstnik
      481 inltwrpwdw lklqsltgms tsasnqenwa deqsfyvskm rlvpyggkii tgneyyyeda
      541 ilplggelky enssskrytf rnvvdlnktw kkhhlfasvg telisiqlns hrgrylgymp
      601 frgktfadid vsiykgyara vqasplqiid ntlntmslfs tmtytfddry ianfnirtdg
      661 snrfgqdrsv rflpvwstsg rwnvhrekml qswswldela lrasygvqgn vhpsqtpyli
      721 vkqenynsil gefvatlkqf pnkhlrwekt vsynfgidfs ifhdrvsasl dvynkkgydq
      781 iiqrriapsn gadfvtineg dienkgwela fnvvplrtkd lvwsmsfntg qnfnkvtqeg
      841 dtkatwqdyv ngtlikngya vnslyayrfk glngqtglpm fygetekdeh gktiinsqqe
      901 afdaafvyvg krepdltggf sssfkykslt lnalfsfalg nkirlndlyt tsgqglpypq
      961 qnmshefvnr wrqpgdeykt nipalsdnqm ryvsydrvyp iadnrwdmyn ksdirvasgs
     1021 flrcrsvslr yeltkklldv lhlrggyvsf etsnlfvlkd pllrgrdpeq islssgavpp
     1081 rigfacqisl tf
//
LOCUS       WP_102191481             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium aurantiacum].
ACCESSION   WP_102191481
VERSION     WP_102191481.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium aurantiacum
  ORGANISM  Microbacterium aurantiacum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Microbacterium aurantiacum"
                     /db_xref="taxon:162393"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52458
     Region          4..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mavigivrep agesrvsatp atvgslrklg hevvvergag aaasypddgf vaagativdr
       61 aaawgseivl aitapdaeai gllsddatii allspalrpd lvealaqrgi talaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvssigge ylpvdvavaa stdgyakats edydrraaei
      241 yteqaadvdi iittalipgr paprlitasd varmkagsvi vdmaagqggn vegsvagqrt
      301 vtdngviilg ytdlasrlat qasqlygtnv anlvalltpa kdgrltldfe dvvqrsvtvv
      361 rdgevtwppp pvqvaaapap avrsaaaeia tpakmsagrk gllialgvaa lfavnafapa
      421 plpqhftvlm lsvvvgfyvi gkvhhalhtp lmsvtnaisg vivvgamlqv tsanpvvqal
      481 aaiavllasi nifggfsvtr rmlamftlgr saqggrk
//
LOCUS       WP_102199581            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102199581
VERSION     WP_102199581.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111175
     Region          27..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvqckktftf lfslfllgcg fvqaqqitvk gkvsdekeav vgvnvlvkgt trgtvtdvng
       61 dytlnadkgs vlvfqalgyv tqnvtvgdnp tinvtlvadn tqlnevvvta lgiardkksl
      121 gyavtevkgs dftqareinl gnalsgkvag vnatatatgp ggssrvlirg ngslsgnnqp
      181 lyvvngvpid ntnqnsagmw ggfdtgdgln sinpddiesi svlkggtaaa lygsrasngv
      241 ilittktgkg qkgigveyng tftmdrpfhf ndwqyeygqg rngakptsqd eaiqtgalsw
      301 garidgspsi qfdgvsrpyt aqrdnvknfy nngstfsntv avaggndvan frfsasslds
      361 ksiiensgyn rksfnlsana nlskkvifeg vaqynveegk nrtflsdtpk npnygaqlia
      421 ntvdirsldp gynaagdevr wnsnsystnp yfvtnkvrnn dlrnrflgnf slrynvtdhl
      481 yirgrigtdn nsirylngep sgiayetrgt msrresqine tngelivgft kdfsnfsvna
      541 lvggnqmrrk ieglnyngqy fivpytyfls ntitktpgye ysafginslf asadfgyknl
      601 lfltltgrqd wfstlakdkn slfypsagvs fvlsdalnsk pswlsygkvr asiaqvgggy
      661 pspyaltqry epqtnlyinn iplvnikggt ipnaalqpnt stttelgiea klfnnklgvd
      721 ltlydrvtkn dpvtastsaa sgydnvllnv gevrnkgiel lltgtpvrts ggfnwdvsfn
      781 vayndnrver iaqglsqyel dqsrtqsayi yhfegqpygm itgfkqktda ngnlvynsat
      841 glpiqsalma lgrgvppltt gitnsfsykn fsfsflvdgk fggkmysatn yyatangltk
      901 etlvgreggv tvrgvdenga eltktikaqd yysssdylri tdrfvyssdf iklrqftfgy
      961 slpksllgnv vqsaslslva rnllvlyskv pnvdpesnfs sgnaqglemf gvpparsygl
     1021 nlmlkf
//
LOCUS       WP_102200272            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102200272
VERSION     WP_102200272.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113141
     Region          22..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrlsilll llsslwataq drqltgvits sedgqplpgv sisikgtakg attnadgayq
       61 lavssgntlv fsyvgftske vvlgdestln iqlqmnassl sevvvtalgi trekkalgys
      121 vqeiggkqlt qaretnlvna lsgkiagvqv tnsngspgas srmlirgsss ignnnqplfv
      181 vdgvpidngn ynnnptavdy gngaaslnpd diesmsvlkg paaaalygsr gangvvlitl
      241 ksgkgsrgig vsvnsnttfd tpfrlpewqn eygqgakgqf rfvdgrgggv ndgvdeswgp
      301 rldgrlieqf dspvvngvrt ptpwvahpdn vnqffktgkt ytnnisltgg idkgdfrlsl
      361 tdlnqsgilp ftnykrqtvs lnagwnltpk lniratgnyv kdgsdnrtnw glyfiwfgrq
      421 vdmenlqnyt apgsiyqnnw nynywtnpyy qlanskrene kdrlfgnisa tykftdwlsl
      481 martgtdfyt drrktknaar tsnlfdgyne eqifvqesns dfllnathkf gefdvtanvg
      541 gnhrknfyqr dymsaaelai prvwnmgnsr lrpvtensys kkvvnslyas anlgfrnylf
      601 ldltarndws salpasnrsy fypsaavsav ltdmfsvqss flsfakirgg iarvgndtdp
      661 yrllqafdya nawgsqaslk esnellnael kpeitssyei gtelkfwqnr igldvtyydk
      721 qsynqilkvd vsnasgfssk wlnagllqnr gveiqltgta vktnsfkwdi tlnwarnqnk
      781 vkelvdnltt ytlgtmrgmg iearvgqpyg tffgqgflrn pegkivydqs gypvidpvrr
      841 vlgnftprwi gglqntfayk nlslttlidm kqggdifsqt inigrytgvl kettvgretg
      901 ivgdgvvnvg taanpeyvpn tknisseewh hkyylltnne etifdgsyvk lrevrltyvf
      961 pgkvfkrlpf rditisavgr nlallhsnip hidpetsyyg dtnvqgieng qipttrsvgf
     1021 nislnl
//
LOCUS       WP_102200120            1038 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102200120
VERSION     WP_102200120.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1038
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113340
     Region          31..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkisflcfqa rfgrlfallw lmslsamaqn itgkvtnaad gsplpgvtvv ekgstkgtvt
       61 daqgqytlna aseatlvfsy lgfvpqeipl ggrttvdvvl kedtkslnev vvtalgiqrd
      121 kkalgysvte vkgseftqar emnvanalsg kvagvnasgm stgpggssrv virgngslng
      181 nsqplyving mpidnstpgg spqtgaggln vdrgdgiggi npddiesisv lkggtaaaly
      241 gsraangvil ittkkgvaqk gigvdfnstf taetpsvfpk wqyeygqgdq grkpatqqea
      301 ldwgrrsfga kmdgqpytif ngtqqsyspq rnninnfyel gttfsntlal sggseninfr
      361 fslanmdsks iqpnskfnrk vgnlnvnakl tknlsleava qynieeatnr psagdatgnp
      421 nwavymlant vdirqlspgy datgreiqwn etpyasnsyf vvnryknndt knrfigqfnl
      481 qynfldnlyi rgsvsrdfyn ykytgiipsg tvytlnaage yhdinssvse tngmltahyn
      541 tklgndfhlt alaggnmrkf lssetyidgt qfivpnfysy tnlnnfttrp ynpkiatnsl
      601 fgsldldykg fafltltgrq dwfstlspsn nslfypsvgg sfvlsqavel pqwvsfakar
      661 aswaqvgags vdpfitnqsy glvqgghdgr plqqvtqyng vnlitnaslr pltsttyevg
      721 idakffnnrl gidltyydrk ttddivrttv srasgyneal lnvgalsnrg vealitynpi
      781 knknfswnvs ynmaynrsev mqlvpgvntl elassvggwa fvhhqvgrpf gvikgytmdr
      841 dangnvifnt atgyqqrsal kelgqgvppw tmglnntfty knfsldvlid gkfgnkifst
      901 mdvyatrfgl hqmtlpgren glpvsgvtsq gdsysrtvpv kdlrlyydnl knytdlflyd
      961 asfvklrqiv lnyaipvkns kifrgasvsl varnpfilyk ktdnfdpeas ytnsnaqgfe
     1021 afalprtrsm gvnlmlkf
//
LOCUS       WP_102200287            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102200287
VERSION     WP_102200287.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115921
     Region          23..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqlllkvllp vllwvqvqaa laqqvtgvvr stadqqplag vtvqikgttr gtvtnaegty
       61 tvtaqpgetl rfsfigykae elavpengvl nvnlnneesa lqevvvtalg iakekkslgy
      121 svqelkstei sqaretnlvn alsgkiagvn itnsqgnmgs srivirgets iagnnqplfv
      181 vdgipvdnsq fgstgtnrdy pnaiadinpd nietisvlkg pnaaalygsr aangvilikt
      241 kggkgnkglg vtlnaahtfe nllvlpdyqn vygqgtgglf sykdgkgggl ndgtdeswgp
      301 kmdgrllpqf fsrgeavpfv phpdnvknff ktghtnnigv siagsdakfd yrfsfnntrq
      361 tgvvpntdit knnfsvngty hlndrltint sanfirsesd nlsalggrgs svmlqflwfg
      421 rqvdtgllrd yrangendfn wnhsyysnpy lllyentnaq rrdrffgnvn lnykindwll
      481 amvrtgndfy tdrrkskisy gtngtpfgsy aedayvvnen ntdfalnfnr klsddfdleg
      541 lvggnirsnf yeqnyqqapr lavaglytln nsrdplvsnn vfrrrrvysa yasaqlgfrn
      601 yaflnltarn dwsstlppgs nsyfypsvna svvltdafni rtnwlsfaki rggwaevgnd
      661 tdpyqltnty pfnqpfgsnp lltvsdvlln rnlkpeitqs seiglelalf ksrvradfsy
      721 ynsdsynqil radvspttgy kqkllnaghi nnhgfeaqls gtpvqtsggf kwnvivnfsr
      781 niskvvsldd qgllnqyilg sngttqvlag vgqrygalyg safqrdasgn vvvgangfpl
      841 knanlqtlgy ytpkwiggit nafsykgwnl svlidtkqgg qiysatnatg rytgvlestl
      901 pgrdaehggl syyyagnnts stpvqvagpd akapngeriy sdgiifngvt adgqanktiv
      961 paeryykniy snsagvneas vfdasfiklr evrlsyalpq nlvkrlslqg vnisligrnl
     1021 aflqkkapni dpetafntgn gqgleslqlp ttrsygvnln isf
//
LOCUS       WP_102201438            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102201438
VERSION     WP_102201438.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111675
     Region          22..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllfftfl mlfgwiaqaq drivtgtvta sedgapipgv tvvvkgsntg tntdakgtyr
       61 ltlpangttl vfsavgfgrk eeeingrtti dvvlqssves lnevvvtaqg ierdtrslgy
      121 atqnvngsal aqrsepnvln tlqgkvagvn itsssgapga stninirgit sfngsnqplv
      181 vvdgiifnnd vdnsqntlfg sqpssrladi spesiesinv lkgpaasvly gsrasagviv
      241 ittksgkgln gktevtfnss vnwqnvaylp klqnqygqgt qnnyvnnstn swgpafgtpg
      301 fetvqnfrge tvpyraypnn irdfyktgtm fqnalniagg dqnnnfaati sstiqngvvr
      361 esdfdrhsvq vggnsklkng iklggtityv ksaqkntlmg nggsafgqit riprsydlvn
      421 tpyldpltge dfyfvngqnh plwsiqntff nsnvdrvfgn lsvgyditnw lnvsyrvtad
      481 tytdnrkqiq rvgaarapqg qidedlrfrs elngdllina kkndlfvqgl nanlllgqnl
      541 nqrsyresgv iseslaipgf dnvgvgsvft ksyastnrrr lvghygqlsl dyksylflel
      601 sgrvdqsstl pkeqnayfyp saalsfvple afnvkteavs ylkvrgniar vgrdadpyrl
      661 qsfftsatfg nnvaditfpl nvggtslpgf qpdgrigstn lkpefvnsfe vglnvgffnn
      721 rlgvdftyfn trstsqifnv aisnssgydt rttnigemqn kgielqlsat pirtssfkwd
      781 vllnftrirn kvvaisegvn nsnitgdsfs giapsiavgy pygviigtan artesgellv
      841 npntglfvpg iagqvisnpq kdwvagltnn fsykgftlsa lvdvnkggql ysfsqvdmrn
      901 agqteitgvd rnqprilpgv ilnadgttrp nniqisaqsy wqslgglasq gavfdatayr
      961 lrevalnyal pssllsrtpf gnisigvsgr nlwmyapgfp sdpeintqga gniqgldlng
     1021 ipttrnygvn lrvtf
//
LOCUS       WP_102201865            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102201865
VERSION     WP_102201865.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112795
     Region          24..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkillatvm llstlvmhay gqsrvvtgkv taledgsgli gvtvravgst avgtttnqdg
       61 syslnvpssv kslsfsfvgf ktsvldipan nvvnvslevn qsdlnevvvt aggltaqrre
      121 lgtqattikn teitqgkaan laaglsgkvp gllisavssg lnpnyrlvlr gnrsltgnnq
      181 alviidniis pnsilgnlnp ediediqvln gagaaalygs dasngalivt tkkgkagrte
      241 vkiahtttle kvsflpqlqk qfgsgttpdd vpsytpyenq qygpafdgsm vnigkplqdg
      301 siqsvpysyk gsredfwetg vqnqtdfsis sgdekstyyi sgqffdqkst vpydkyqrys
      361 vranstrkis dkltatfntn fianrydqss qaatvyqnll mspgqvdvtq ysdwrnnpfa
      421 npngyyneyy tnpyftlenn rvntrndyfq gnvelkwnpi kplsityrvg lstrnvsnks
      481 tvgkftftdy tksisgsskt dipgsvsdys gfntqlvndl iaqyntslgs nfslnvvagi
      541 ssrdnsskdv svgasglvis dlynvgnsln nptagesnfk arqlgvygdv rlgfkeylyl
      601 hvtgrndwrs vlakdnrsff ypaadlsfia sdaipalsqs nwlqslklrg gyskvgqvnl
      661 gnftnfgaya lattfsqayg ypyasgagft lgntlvasni kpemttgaev gfdfelkklg
      721 inggitlykt ntvdqtitvn vssasgfssl rtnvgevqnk glesylnitp irtasgfevs
      781 lganytynqn evisladqln elvlssvgta srvlakkgsp fpllqvttyn rdpqgriivd
      841 pttgypasng tfsdlgittp phvlglntgi kykglrlsal feyrnghyiy naistgydfs
      901 gagirtawyn rdrfvipnss yqtadgnyva nnniavrsgg adfwtdgtrn tsigenyans
      961 agfwklrelv vaynfpasil skanfikaat vsvqgrnlfi wvpktnlytd peysangtds
     1021 navgitnlgq tpparyfggt lsltf
//
LOCUS       WP_102202302            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102202302
VERSION     WP_102202302.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113811
     Region          23..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkrlllsif tlflfsgsla laqqirgkvt vegdntplpg vnvslkgtss gtvtnangey
       61 sinltsgrtv lvfsyigyvn qevdatgrst vdvtlkadnk qfnevvvtal gisrdkkalg
      121 yaaqgvgsee lvqnhqpnlv nalqgkvagv tisstggapg qgarilirgi nsidvsrdnq
      181 plfvidgvll dnststlgnd aagrgmsnra adinpediet inilkggaat alyglrgang
      241 vvvittksgk agalranysg tygfenvnky pdvqdkytig wqgqydpnsf wpswgptvee
      301 arkidpthpa klynhfkday rtgqqfqnnl sfsggtdkin flssishlnq qgvipftnye
      361 klslrlnsni kfsdkfttgv nlnfinsggd rynagrynet lsywsprydv rdyltpdgtm
      421 kaysgdnanp mynamtnkfr dnvnrliggv nftyaplswl tftyragldt ysedrlqtap
      481 gpkgiageyi sgdnglgfvy qyhtnfrait stfaasathk fgdlnttlrl ghdlydrrir
      541 sfgaegrelt vydyfdlrna ktivpvqsae dyrlmglfge ltfdykdylf ltltgrndmt
      601 sslqspnnsf fypsaslgyv fsqhfnlpev lsmgklrasy aqigkdaapy statgyssyq
      661 nlpsgltgft rgallgnpnl rpeftdtyea glelgflnnr lgldftyyns lskdqiiqvn
      721 vssgtgyvra ainsgemrnr gvelilratp iktskfnwdi nlnfsanrnk iesirqdlte
      781 isyasefgya nstvtmklvp glaygnlygr ayqryypntg eeqpavldrd rpivigangf
      841 pvigtaqkll gntqpkwlgg lnntlrygnf tftalfdarv gqdrynqmgn ffsafgiaky
      901 tenrndtkvf egvlangtpn tkavwlgqgv gpdgvnygng fyrnvhrgvs elfiedaswv
      961 rlrsaslsys ipsswikssi vknarlsvtg nnlwlwtkyt gfdpeasttn sgsnvdgfsg
     1021 fsypavrsfl fslnvgf
//
LOCUS       WP_102202425            1143 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102202425
VERSION     WP_102202425.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1143
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126525
     Region          62..111
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          146..1142
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfftslht wglvvclalp gqpaspllsp tewqsslqlk ntsqrklkdv lhelkerfgv
       61 dilfgdqlvq gltvpktald pkasleenld rvlknsglhy rkakdgayli vgqrldktte
      121 relpqtsars sspvasqqps levqdqvitg kvtdekgegl pgvnillkgt srgnttdaeg
      181 nfkltipena dntlvfslvg ymsqevavgt rttldvqlkq diksleevvv igygtvkksd
      241 vtgavasids kniekvnrvd aasaiqgqvp gvmvqrtdnk pgsggfniri rgastihtte
      301 taanagytpg qnplfivdgi fvndisflnp adidrmdvlk dasataiygs rgtngvviiq
      361 tkkgesgklt vrynnyvgvk evyhlppiyn ttgyvdylkd vvvgnqyasg nynftrndvn
      421 lpnylnaeel knindgvstn widlitrkgf qtnhtldlsg gnkstvyaig fgytqdkgtt
      481 rgedfnrytl rgnlssdlts wlnlsynnyv tvatqnagsf eafrsayrlk pigraynedg
      541 slkflptake tqvtnplldi eneiretkyl nylgdiavrl klvpgmtfts kfspnikytr
      601 ygeyrgkytk ssvgnqsstr aqvenyldfs ytwdnivnyd tkinddnkin atfvysqyna
      661 qnesyalqvr nfssddylfy nlgagstvnn yssrylkqtl esftgrinys lkdkyiftvt
      721 grydgssila egnkwaffps aafawrmide gflksqnlfs daklrlsygk tgnngagggl
      781 splgslslls psytnindqs mstlfitgla nknltwehta einvgldfgl fknrltgsld
      841 vydrttnnii ffrplplatg fpgtydnigk asnrgvelgl navvidankf rwsvnlnfaa
      901 nrnkvlklng ssdeiifgsq gatlihkvgq pmgsfyyfka ngiwgndqve earkygqkpg
      961 qvrvvdvdgd gqitesrdrm iignsapkwt ggmthsftyk nfdlsvfayt sqgamaasnf
     1021 hrsfafaydn eparlwngyr tdywtpdnqt snwfqpgngg tyssaykymd vsfvkvgymt
     1081 lgyrlpadll skarigslrv yatvqnpftf tkydgwdpen asrndwggaf msrtymagln
     1141 lsf
//
LOCUS       WP_102202591             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102202591
VERSION     WP_102202591.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108655
     Region          40..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlsylhvsgp rrrwsglwll lpallfsysl valprpaavt vtgkvisntg gplpgvsile
       61 kgtnngtltd adgnykinvq gansvltfty ighvkqeitv gnqpvinvtl eesssalqev
      121 vvvgygtldk kevtsaithv sgkdlltvgv tnpisalqgk vsgltitntg ggdpnsmpsi
      181 qlrgvssrda glgplvvvng vpggvlenin qndiesidvl kggaasaiyg trgsngviii
      241 ttkkgsqgsr vdyngygafd faamplktls aseflaqnrg tdfgaqtdwl ksitrpsafs
      301 hkhtlsfsgg darnnyrata dyrdaqgldl rsgreeygar lmlnhtsann lytltlnvap
      361 ryfksnnady dsfdqaltln ptlpifdpqn ptrynriqsg fsspfnpver lrteqsgteg
      421 kildynasll vnllptlttq ltfgqftrdy fdfffrpsts tyaaqyqgsm nsasraynky
      481 dqrslewvgn ysltkgahdv kvlggysyqy fqssglsgen rqmpsdalty nnigtglyqq
      541 vegrngmgty kndsrliaff grinyalqdk ylfsaslrre gsskfgynhk wgnfpaasvg
      601 wrlsqetfmk tlswiddlkl radygvtgnq dfgnylsldt ysgygyypln gsqyqvwgps
      661 qntnydlrwe taenlnfgid fsifkerfsg sinyytrknk dllgfysvpl ppniqgstya
      721 nvgtmqnsgi elqlnaqvvs tsaftytmaf agatnsnkfv sfsnaayqgq nyidvvglps
      781 pgspgtaqrl qegqrigtfy mlhaagvgdd gkllvynqkg diipadkann ddkrvvgngl
      841 pkatlslnnt ftykkwdasv ffravvgykl fntqafytgt pgtqsnanvl tsaygggkya
      901 kltnqattvi lsdyfledgs flkldnvtlg ytpkvnlkai rsirlyaaar nlltftsftg
      961 gdpdryping lypginssrs yyptttqila giqlgl
//
LOCUS       WP_102202699             523 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102202699
VERSION     WP_102202699.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..523
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=56568
     Region          23..>523
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msksllsflf lvltgsflya qttvkgvvts sqegvplpgv svavkgtttg tvtnaegryt
       61 livprgqtvl vfsnigftrs eiditnkttv dvilqeesqv lnevmvvgyg tvskethvgs
      121 saqvkaidia krpvsnalna lvgaapgvqt iqsggapgsa pairvrgfgs isasnsalyv
      181 vdgvpfnmnt sslnpddies invlkdastt aiygsrgang vilittkkgk nnrnnlnfna
      241 svgtisrglp eyetvsaqey yplmwevqrn tlqygslrip qevagsiaag qttqylgrny
      301 tgiydllkyn pfnvannqiv dangvlnpna qllypedlnw vkaiqrggqs rqnynisydg
      361 ganksdyfas vgytkeqgyl lksdferfta rvnmntqptq wfktglnlng sysrsntdag
      421 tggtsfinpf yitrfmgpiy pvykhdpatg ayvldkdgnk vydmgdsrpf ssgrhavwen
      481 elndrkeetg iiggrayati nilpslkats nisfdlqdrh rrt
//
LOCUS       WP_102202779            1179 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102202779
VERSION     WP_102202779.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1179)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1179)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1179)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1179
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1179
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130111
     Region          59..108
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          154..1178
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkritllyg lpafmylcgp pgvraqeivr agqeqvreas asgqslehrl qevekqykvs
       61 ilynpelvsk krvkdfrkyt sleqtleqll kpygltfkkv sdsfyivsee kksntsavnl
      121 lpnkfvplen ltnlsrseri satsltmplm aaltvqgkvs dattgeplpg vnvvikntsq
      181 gvttnrsgey slpnvpenav lvfssigyqg qeiavqnrsq inisltsssq eldqvvvvgy
      241 sqqrrstltg svaqigadql kqapplnvsn vlagrlpgvi vtqpygqpga dnatinvrgi
      301 sttgsnaplv ivdgierpft aldpneietv svlkdasaaa vygaraangv ilittkrgkt
      361 gkptityetn fsqntntrfp kflngpdymr wykraeeldn qylvsqgktp faltytdeei
      421 aslangtnqs eflgntdwvg mltnntsvsq yhnvsvnggt drvryfttlg ywnqngvikn
      481 tnykrynvrt nidadvndfi strldltvrm edrmnpalap tdqnyqnpfi laqrmqpnlp
      541 mfnpaglpvg gntdagvgnp ivavndignr naeattfngn lsmnvkipgv qglqarllvs
      601 ydktitevkt fvepamlavr nrnangwlwt parmsaynvn nliqdyshsy rttfqpsily
      661 drtfgknafn glllyeysgw gtngfgaqar nfpitdlldi nfgskaaedl raatgsstqy
      721 krggyvgrvn ytyddkylfe vaarydasvn fpestrwgff psaslgwvls kenfwqplnt
      781 pinffklrls agklgndvvg iyqylnsfql rttptvaign qvvstlynta panpritwee
      841 atmynggiel glwnsnlsle vdyfykvtsn iltgqsgvya psvggnfast vnagkvdnrg
      901 vdlqlayskk hnklsykiig nftyahnrvl rinesvnapa aqrrvghpvn tkfgflvdgl
      961 yqtqeevdrg psfpygpgap gyvkyvdlng dgkisfeqdv trigrsntpe imyglnlqag
     1021 ygpfdfsall qgaarsnvil agvynsgvqg ntvytqtfag ngnspyflve dswrpdnpda
     1081 kyprltanka gltnqngyqn sffvrdgsyl rlkslqigys lpkdflsrlk iqqwrfyaag
     1141 snlltfdkik yadpetpsvv qagfypqqrv fsigtnitf
//
LOCUS       WP_102202847            1176 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102202847
VERSION     WP_102202847.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1176)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1176)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1176)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1176
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127011
     Region          53..115
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          133..1172
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mglllrrkss glvgllitgi vcsaagqtpa yfaraeaere erprpatpat kgltevfqql
       61 ekkyrvqfay qkklvqdkri qatvgdskrs leenlqqvls plnltyekig etyiiserlr
      121 esvtpkkssk aeikvkgkvt akdgtelpgv nvrvkgtgig avtnaqgeyl itapsetsvl
      181 vfsfigyasq eldiagktti dvvlenetkq ltevvvtaag ierkanalgy svstlsttdl
      241 aqknepdpvr alagkvagvn vqggggvagg atnitirgns slgnnnqply vvdgvpfdns
      301 tfapvtgnnq tqsnqstasr afdidpnniq smtvlkgaaa aalygsraan gaiiittkas
      361 akksrkgtei tyntsysaet iaglpeyqql ygqgtngdyr savygssgsa ystratiphp
      421 laragfsaad fpqfyeadgv tpvqvpyrsy agknqrdffr tgsvyenalt vnsgsekgnf
      481 tvglsrttnq givpgneiar tsinvggnar ldnkfyvrgt inyvmtdqks ppiggsgsim
      541 stmyylptsy dltgypyenp ntganvydya gvdnpywsir hspatsnvdr yygnfvlgfd
      601 plswlniqnt agfnaytdrr vsvlgkgssv yangtintdh iyrqeldntl lvtitktikq
      661 dfslraifgn ninqrmtdrs afvgtniita ginninntst itlgslpnnr amirqrfyaf
      721 ftditldykg faslnivgrn dvsstlppen rsylygging sfifteafgl nspilnfgkv
      781 rvgytqvgne aqpyqtvnvf nanasagdld apfsnpvqsn vstmtlgdvl snarlkpefi
      841 tefeagtelq ffnnrlsidl tyyhkrstsq iftvksapst gftdriinlg qtsnkgielg
      901 isatpvslas gfrwninanf trnrnnvddl ggfaqlvygn nihiagqpyg qiygsryard
      961 negnilvnpq takpiaaats gpignpnpkf ivglnnsfsy kritfdvlfd wkqggaiyst
     1021 nignalsrgv trdtenretl wvgpgvlgnv ntlepildes gnkipnntal tvidyffsgg
     1081 ygpggigegy vfdatvfrlr elslgyqlps nilqktpfgs vsislsgrnl wykapntpky
     1141 mnydpevstg aannagfdsl gvpttrrfgv nlrasf
//
LOCUS       WP_102202902            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102202902
VERSION     WP_102202902.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119115
     Region          24..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqllllifl fttslsawaq tgslsgtvqd ekgaavpgas vvvkgtntgt tsdsegkfrl
       61 nvtqanptlv vsaigylrqe vavanqtvit itlqedakal tevivtgfgi kqearklsya
      121 aqeakgldlq ransanlvna lqgkiagvqi dqgsggpmss sririrgnas lnsntqplfv
      181 idgvlvrpgt tgadswgaaq dfgnimknfn adnvesmsvl kgaaasalyg sealngvvli
      241 ttkqgrqqkg lgvnfnhtts letayrfvdv qneygagisp nfakgadgvd qvvnntsswp
      301 ysfgpkldgr mvrdldgrmv pwvannpldf fqtgkfinnn lsvegandrg sfrvsysnly
      361 nttimpggae mkrnnfnvra tqklgkvfnl dvsadytind nlnpirqggt fnpvfrfvyg
      421 rprsfdidyw vnnyesptgg rkvntadpyn ispflwqtfh ynttrnervf rgnidvnmnf
      481 tpwltgllra nlqneqynte nkfegdmqgf ngeysefsls nnqsriqgvl tlnrdlsssv
      541 hlnlsagget nrvlggrdyr vttngglrlp gvfalsnsvs tligsgvlnp ssrkdamyay
      601 gdvsfkdqlf vnftarqefs stlkyangag ekayfypslg vawdftqtfk nlantlsfgk
      661 lrasygftgs didpwtlnrd gfysagsifn singqiqryg frdnilanpn irsrrarewe
      721 vgadvrffdn rltldvavyn klttnemfrl pvaqesgtts rtinggriln rgvefilsgt
      781 piknkdfqwt tsfnfsrnrn kileladgid tyelslafga dvrsvakagg dygtivstya
      841 yardpqgrkl igaasgtngg yltylrsgaa gqgskelgtm menfllsnvn tlryknfsat
      901 fqldskiggv massthaygs afgsfknsls grdaehggia ftdnqgvqrn dgiipdgvla
      961 agvkanvdgv qvdlggmtyq eavdkgylkp ipayayydnl snwgsgirey svfenswvav
     1021 reasigydvp sallnrikvq slrvsivgrn lgylyrtakd ginpqgllsn ragefaeygg
     1081 lpfsrnigvs vnvgl
//
LOCUS       WP_102202908            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102202908
VERSION     WP_102202908.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115631
     Region          27..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqtsilffl llvlsiaspg wsqtpllqgt vtdeqgqflp gvnvllkgtt tgvvttangt
       61 falrpprplt padqlvfsfv gyataevaig sstqlnvrlk asplalqevv vtalgikree
      121 kslgyaaqsl senvvkdart nnwvnslagk vaglniqgtg agpmgsarit lrgesslnld
      181 nnqalivvdg vpvssritgt gynshlsads pvdygsslsd lnpddienvt vlkgpgatal
      241 ygsraaggal iittksgark dqgigvtvns nvsiegvnrw pdyqfeygeg rtstyfsyld
      301 spdgpntatt vaagrawgpr fngqsyyqyn psapngkpte rtpwvpykdy isgffqtglt
      361 ysnslslegg tdkgsarfsl thlknkwiip ntgferinaa lsvnqkvsdr lkingrvnys
      421 nkksdnlpaa gynnqtlmyf lilgttpnir pewfkpywat gleqvqqrnp fnptpdnpyl
      481 imyemlnkmn khgvigtlsa tyqlsdhidl lvrsgldmsy efrsqqrpfs mtryprgmyr
      541 eqnvfsyesn tdfllsyknq lssrvhlnas aggnamrqly dfaglyadql aqpgiyqisn
      601 sldqavadpl ktrkainsly aaaqfsldek ifvdltgrnd wsstlpygnn sffypsvsss
      661 fllhellplp qsfsfaklra swaqvgndtr pyqtdryydk iygnsftnat tlfnanlkpe
      721 itssyefgld vrllnnrvgl dvayynnrsr nqilaipldp vsgytnalin aglinsrgle
      781 lkltgrplat sqwnwnstll wsrnrshvre laagitnqvi ynhntnvsie arvgglmgdm
      841 ygrgfqrspd gqiiyssvgl papldpenkk wgnafadwka swlnefsyrg vrlsvlldgq
      901 kggslfsqtn hknntlgktn vtlpgredgi igqgvvkqpd gsftpntvkv aassyydnyy
      961 aitnaetnif dasflkirev rlefnlpkrw lqrtglrqts lalygrdlfn ftkfpgfdpe
     1021 ggnlnggtlt pgvelaqfps trviganltl kl
//
LOCUS       WP_102203072            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102203072
VERSION     WP_102203072.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118740
     Region          29..96
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          102..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mitrvpgllv alwisfgiwn qagaqqltlr lqqaslttif seiekqagvq fhydaqdipl
       61 krrfdfnstg pfpvilrdls slsnlaflqk gnrilvrtqa qrrvsgrvmd rsekiplpgv
      121 svrsstgrvl avtnaegyyt gtisavdlnq arlefrmvgm kpilsqplgs sstldiemep
      181 esrqmnelvi tnaytngtpk eevigsisqi nakelqpyrp iesfdkmleg laagvyvept
      241 tqlgtpvkin irgqgtltpv ggtrttstqp lfvidgipim eqergdaaqi fsgetlinpi
      301 aginpqdias isilkdasat tiyganaang viiittkags agrtaahvsv srgvstfinr
      361 mkllsgpeyf tlkreallns gftesqaaaq agsstidtdw lglttrnasy tainadvsgg
      421 kegttyrfst gyryqqasal kndlqqinls lkvnsilnrk lklgvtlspt iikksgldnf
      481 knnaylppnl spydaegnft tllgvpnpla vlaqneavtd alafngnanl hyavapnfti
      541 sgtigtnfsq skdvsydsak natgstkggq lqifdrqtlg wlgylqgtyt qtfqqkhsvq
      601 viagleaqdq rtvllagsgt nftydrirei sqatrqsass srqenatvsy ytqatydfkk
      661 kylftssira dqssmfgsdf nlalnsavgl swiiskepfl qnhpaftflk lrtsygstgn
      721 srigsyaarg lynfsygnyn gyvaavpets sapnpnlswe knlklnlgld ltlfdrlsit
      781 aeyyqntihd lisnvevple tgygsisynt anmrnqgfdi tlqthfiqsk hfkwrstltt
      841 gfnrnrilqy nqgftsvysd pastaseana airegystta iwgirwagvn petgneqfya
      901 pdgsvvdrtt irtyprssyv vlgdrlpkaq ggwvnelsyk qfsltlnily nlgenrmept
      961 qfmgdgrniq hsnmsvnlld rwqkpgdvap vsklliekgl vtnssrylqd lthlklsnvt
     1021 lhysltsals rrlrmqgvsa flnvtnvayc ykdksptgrn gvretrfafp eartlsvgln
     1081 lsl
//
LOCUS       WP_102203442             357 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            sp. BAB-5405].
ACCESSION   WP_102203442
VERSION     WP_102203442.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter sp. BAB-5405
  ORGANISM  Siphonobacter sp. BAB-5405
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Siphonobacter sp. BAB-5405"
                     /db_xref="taxon:1864825"
     Protein         1..357
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=39116
     Region          23..>343
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiywlllp llllslpgfc qdriikgtvs dknealpgvs iyekgvptng tttdangnfr
       61 ltikgsasil virsigykla eeqvgsrtti nvtleseeqg lnevivvgfg eqkkitltga
      121 vsmvsgkeir enpsaslqnt lagrlpgffs qqpsgrpgad gadfyirgvs syngnnrpli
      181 ivddieysye qfarldpnei enlsilkdas ttaiygvrga ngvvvvstrr gkegpakisv
      241 riessltqpt kipqyldaye sarlynqaqi ndnnanpnpn frprfsqedl elfrngndpy
      301 ghpninwkdv lfkkfseqyr gnldlsggte rvqvfciagv slsewnakrf rsgpggq
//
LOCUS       WP_102213792             539 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Corynebacterium].
ACCESSION   WP_102213792
VERSION     WP_102213792.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..539
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55321
     Region          1..536
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipiepd arqplvaatp dtvakliklg ydvdvqagag dhaaypddly aaagarlvge
       61 dvwradiitt ldappaefrr qmkpgamlvs rlapgrnpel vddlasshft alamdavprl
      121 sraqsmdvls smaniagyra vveaansfgr lftgqvtaag kvppatvyvi gagvgglaai
      181 gtansmgaiv katdlrpeag eqvesmgaef ipipvaseks tdgyakemtd dqataaakly
      241 aeqsaaadiv ittanipgrq sprlltaddv ramrpgsviv dmaaanggnc eltvpgeviv
      301 tdngvtiigh tdlagrlpgq asqlygqniv nlfklitpdk dgtpildldd eivrgitvtl
      361 ngassskggd tgnveaettg aatdtrilwp pppvqvsatp aaaaqeklaa aataeapekv
      421 sfmggskaki glglaialga avilaspasv svnymvltla ivlgfyvisa vtprlhtplm
      481 setnaisgiv lvgailvvss tnvivsslaf laivlssini fggftitdrm lgmfrkeea
//
LOCUS       WP_102218232             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Gleimia
            europaea].
ACCESSION   WP_102218232
VERSION     WP_102218232.1
KEYWORDS    RefSeq.
SOURCE      Gleimia europaea
  ORGANISM  Gleimia europaea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Gleimia.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Gleimia europaea"
                     /db_xref="taxon:66228"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53912
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkegn gqplvaatpd tvkklialgy evaleerage lasyldaqyq eagariatse
       61 tvwdsdivla ldapttsqld mmhegatlia rlaparnpel iealssrgit alamdtvpri
      121 sraqsmdvls smanvagyra iieaaaeygr lftgqvtaag kmpparvyvi gagvaglaai
      181 gtansmgaqv yatdvrpevg eqvesmganf vaipaasevs sdgyakemtd aqrdaaltly
      241 teqaaasdiv ittanvpgrk spllltaqav agmkpgsviv dmaaanggnc eltvpgervv
      301 tengviilgi tdlagrlpaq ssqlygqniv nllklmtpek dgqivfdled eivrgitith
      361 lrdvmwpppp vkvsaapaaa tpkpdpalea aqateearke aakkrnrfiw tlvaavlgla
      421 lvwvspapvl ghymvlalai ilgfyvitsv thslhtplms vtnaisgiil vgailqvgsg
      481 nllvstlsfi aivvasinif ggftvthrml amfkkd
//
LOCUS       WP_102216912             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Gleimia
            hominis].
ACCESSION   WP_102216912
VERSION     WP_102216912.1
KEYWORDS    RefSeq.
SOURCE      Gleimia hominis
  ORGANISM  Gleimia hominis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Gleimia.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Gleimia hominis"
                     /db_xref="taxon:595468"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53717
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpnegt errlvastpk svgnliklgy evtvesgage cshypdyqfe dagahigdap
       61 sawgadivls vgtptteqld lmkegatlia qlaparnedl adslaerkit alamdtvpri
      121 sraqsmdvls sqanvagyra vieaasvfgh lftgqvtaag kmpparvyvi gagvaglaai
      181 gtansmgaqv yatdvrpeva eqvesmgatf vpipvaqqes tdgyakelsq ddldaaqkly
      241 tqqaaqadiv ittanvpgrk spvlltrsav eqmkpgsvvv dmaaanggnc elteagrvtt
      301 tdsgvlivgy tdlparlpaq ssqlygqnvv nllklltpnk dgqlnldldd evvraitvth
      361 rgdilwpppp ikvsaarptp aakpdpaaea kqkaeqsrka aakkrhrilg gglaalvlaa
      421 lvlasptavi ghymvlalav vvgfyvitnv thslhtplms vtnaisgiil vgailqvgsa
      481 nllvsalsvv aimvasinif ggftvthrml amfkkd
//
LOCUS       WP_102220954             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Fischerella thermalis].
ACCESSION   WP_102220954
VERSION     WP_102220954.1
KEYWORDS    RefSeq.
SOURCE      Fischerella thermalis
  ORGANISM  Fischerella thermalis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Hapalosiphonaceae; Fischerella.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Fischerella thermalis"
                     /db_xref="taxon:372787"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41094
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalvp divarlikqg leiwveagag eraffndaay eaagatiiad
       61 tnrlwseadi llkvspprer edgrseidll kegsvlisfl nplanpliaq klaarkvtal
      121 smemiprttr aqsmdalssq asiagykavl iaaaalpkyf pmlttaagti apakilimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve ikldeettaa ggyakeisea
      241 srkrtqevvt ehiknadvvi ttaqvpgkka pllvtedmvk qmkpgsvivd iaaeqggnca
      301 ctdpgrdiva hgvtiigpin lpsslpvhas qlyaknltsl mqllmkdknv einfaddiid
      361 aacithagei rstrikealq tvtsavs
//
LOCUS       WP_102227277             351 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Acidimangrovimonas sediminis].
ACCESSION   WP_102227277
VERSION     WP_102227277.1
KEYWORDS    RefSeq.
SOURCE      Acidimangrovimonas sediminis
  ORGANISM  Acidimangrovimonas sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Acidimangrovimonas.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Acidimangrovimonas sediminis"
                     /db_xref="taxon:2056283"
     Protein         <1..>351
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          <1..351
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 aqkmdalssm aniagyravv eaannfgrff tgqvtaagkv ppakvlvvga gvaglaaigt
       61 stslgaitya fdvrpevaeq iesmgaefvy ldfeeaqadg aatggyaaps spefrekqle
      121 kfralapemd vvittalipg rpapklwlkd mveamkpgsv vvdlaaergg ncdltvpdek
      181 vvsengvtiv gytdfpsrma tqsstlyann irhmiadltp gkdgvidhdm eddvirgatv
      241 ahagavtfpp pppkvqaiaa qkpkakekap tpeerratea aafraqtrrq vtligigavv
      301 lllvglvapa sfmqhfivfv lscfigfqvi wnvahslhtp lmavtnaiss i
//
LOCUS       WP_102236056             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brachybacterium sp. UMB0905].
ACCESSION   WP_102236056
VERSION     WP_102236056.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium sp. UMB0905
  ORGANISM  Brachybacterium sp. UMB0905
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Brachybacterium sp. UMB0905"
                     /db_xref="taxon:2069310"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53729
     Region          1..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipcead psqavvsatp dtvaklialg ydvaveagag eraafpdeqy aaagaqivge
       61 evwdadilta ldapppelra rirpgrhlia rlapgrspel ieefersait alamdavpri
      121 sraqsmdvls slaniagyra vveaashfgr lftgqvtaag kippatvyvi gagvaglaai
      181 gtansmgavv ratdlrpeva eqvesmgaef vpipaaaers adgyakemta eqaeaaarly
      241 taqlasadiv ittasipgra aprlltaqdv agmrpgsviv dmaaagggnc eltvpgevit
      301 tdngviivgh tdlagrlpaq asqlygqnlv nllalmtpak dgmlqidled eivrgitltr
      361 aridregptp qvvadvlwpp ppvqvsaapa paappppdpt pvepapqrsr awwmiplall
      421 gaalvlaspl avashyvvll lavivgfyvi tavthalhtp lmsetnaisg iilvgailqi
      481 gsanwlvtvl afiaivvasi nvfggftvth rmlgmfrkda
//
LOCUS       WP_102292096             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Vibrio cyclitrophicus].
ACCESSION   WP_102292096
VERSION     WP_102292096.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cyclitrophicus
  ORGANISM  Vibrio cyclitrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Vibrio cyclitrophicus"
                     /db_xref="taxon:47951"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35590
     Region          5..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiyelystr nkakypevyq ykvvsdklrt qvaqilvaai gnrrnyggyl tpsedvytsi
       61 ynilkreyge sslgrhpegs aawledylln yantehfidv leltcrfidk hvrknwanfh
      121 hndnpsqrpd daleelnerm kragfgyeft ngiivrideq yihaevvkpa lfilqgfega
      181 keeflsaheh yrhgnfeeci tdccksfesl mkaichekgw iddkehdklp aakliqkcie
      241 nelvpvymqn qftgfrqile sgvptirnkt aghgtgrevr eipqglvsyt lhltatnivf
      301 lgncyhemk
//
LOCUS       WP_102294094             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium sp. AD80].
ACCESSION   WP_102294094
VERSION     WP_102294094.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. AD80
  ORGANISM  Janthinobacterium sp. AD80
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium sp. AD80"
                     /db_xref="taxon:1528773"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38701
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qiivqagagl qasipddaya aagaqigtaq
       61 eaygcaivlk vrapdagera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lmaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvvkhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_102405368             477 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            sp. 10N.261.55.A7].
ACCESSION   WP_102405368
VERSION     WP_102405368.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. 10N.261.55.A7
  ORGANISM  Vibrio sp. 10N.261.55.A7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Vibrio sp. 10N.261.55.A7"
                     /db_xref="taxon:1880851"
     gene            1..477
                     /gene="nrfA"
     Protein         1..477
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53408
     Region          1..477
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkklhwipns aaamilvatv ifgatsvsas eekglaeadp rnhtyeqkhp dqyqswkats
       61 esehledala edpnmvimwa gygfakdynk arghffavdd vrqtlrtggp tdeasgpmpm
      121 acwsckspdv grvieerged gyfegkwarl gaeianpigc adchdtrsee fkngepalai
      181 tkpyverafe aidkpfehqs rldqqasvca qchveyyftg ptkavkfpwd rgtrvsemee
      241 yydalnfkdw thkvskapml kaqhpgyetw rdgihgknkv vcvdchmpkv tkedgtvytd
      301 hkvgnpfdrf edtcaqchtq tkdqlreivs srkaqvlnmk ltaekqivaa hfeagaawda
      361 gateeemapi lmdirhaqwr wdyaiashgi hmhapeiale vlgtavdsaa dartklirll
      421 atkgitepie ipdistkaka qqalgmdmea mnkekqeflk tivpnwekaa eereaty
//
LOCUS       WP_102406644            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides bouchesdurhonensis].
ACCESSION   WP_102406644
VERSION     WP_102406644.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides bouchesdurhonensis
  ORGANISM  Parabacteroides bouchesdurhonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Parabacteroides bouchesdurhonensis"
                     /db_xref="taxon:1936995"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114226
     Region          46..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msrnvrqrkk lvqtaiilgl lsgigtinad avvpsegiti sqqkeivvkg tvkdktgeti
       61 pganivvkgt nagtttdydg nfslqvpana ilevsfigyk tadvavnnqn ninvvlsstv
      121 eeldevvvta lgirrekkal gyamqeikte smaeirsesv anmlqgkvag vqisqsatgv
      181 ggstrvvlrg ttslsgnnqp lwvvdgmpis dnqtdkagqw ggidysgaaa einpediesi
      241 svlkganaaa mygsraqngv iivttkkgks gklqleyngn ihfskaydsy eyqniygqgs
      301 ggtftvgate swgpkmtgqm idnwrgangi ykdsrydtqy aflpqdnyve efyrtgvnyt
      361 ntltasggsd nltsrfsfsd srnqgitpnh slnkqyydls sefkskyldi nakinfmrqk
      421 gnnrpalgey gimkslitlp rgirlsdlrn pvgldgytvn wtgqsnefrn pftdtmteng
      481 nqdernrlig kvqltgkitd ylrvtgrvgi dwyhdqirny gsytqtytst syshtmatnq
      541 efnadlmlnf dkqfgdfsvi anlgtattsf kwnnvsgssg yfsiphlial gngnnqttse
      601 gyskkrvnsi lgnatigwks riyldvtarn dwsstlpsnn wsyfypsvsl sgilsemikl
      661 peqitywkir gsfakvgndt npyrllsvyt ldktngdiln atasttfplt nlkpedtrsy
      721 evgteyrmfn grlgldftyy nantinqilt vkvpissgys sklinagkmk syglevsltg
      781 tpiqtkdwtw dvtlnwglnr tecveldpnl krfvigetri gkvvvdeggr ygdivgigyk
      841 rdangrvlig dnglpitese kvlgnmtpdw tgsfstslrw knlslnalid vrcggdlist
      901 tdlyassaga skrtlagree gmvvngives tgqentktvs aqsywsaigg aygvaeefmy
      961 dasyvkfrel sigytlpkaw lkdlpiqsvk lsavgrdlfy ifknapvtpe asfsredyaq
     1021 afeyaalpst rsfgftlnvk f
//
LOCUS       WP_102407192            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides bouchesdurhonensis].
ACCESSION   WP_102407192
VERSION     WP_102407192.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides bouchesdurhonensis
  ORGANISM  Parabacteroides bouchesdurhonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Parabacteroides bouchesdurhonensis"
                     /db_xref="taxon:1936995"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111359
     Region          24..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrksfilfvl fcigtctsvl waqkkvsgvv mdkdasmpli gcnvvekgtt ngtvtdldgq
       61 yalevgdnav lqfsylgmet ieepvggrtv invdmfsdsq kieevvvtam giqrkakslt
      121 yatqqlagqe ltrakdanli nslqgkaagm vitpnatgag gsskivlrgn ksvygnnqpl
      181 ividgipmnn pettqlsgey egrdggdalg nlnpddiasm nvlkgasaaa lygsmaangv
      241 imittkkgrd gaarvdfssn itletplalp klqgrygavk tgdqlslmsw gekiadndkk
      301 amdnvndfyr tgstyinsvt inggtekmqs flsyanttal gimptndfqr hnmsmretfn
      361 lfnnrltvda slsyitqkat nrphggtyin pltglysfpq ngdfgyykkn fetfddsrnl
      421 maqnwytsld dftanpywvl nrvqskekrd rimasatakl kitdylniqg rlsvdntfdk
      481 ferkwhattn inwaahangr yrqerfdakq fygdfmanfn ktwnekweln aslgtsfmes
      541 kvqntfldsd klglieanff vpeningngn qrtsnphkrl nsvfgtvqfg ynsmiyldvt
      601 grndwasala ythnysyfyp svgltallne mipisekvnl lkirgsysvv gndvpayity
      661 pmdginlgql epntkepfse mkpekmhsme fgidlamfdn rfnfdityyk tnnknqyfti
      721 daplasgyeq yyinagdiqn qgfeasasyr wdfakdwswk pefnisyndn kikklddrla
      781 dgvqvgsgag yrfmlkeggs ygdiygkdlk rnddgslvls dkgeimltdn dvylgnvnpk
      841 wqlgwgntft ykdfslyfli dgkiggntis mtqsyldsfg vteetadard nggvdigngq
      901 kmdaqkyyss tsgkegakgn yvysatnfrl relslgytfr nllgasknln lsfvarnlff
      961 iykdspndpd lsvstnnawk gydsfglpat rsyginlkvt f
//
LOCUS       WP_102409018            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides bouchesdurhonensis].
ACCESSION   WP_102409018
VERSION     WP_102409018.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides bouchesdurhonensis
  ORGANISM  Parabacteroides bouchesdurhonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Parabacteroides bouchesdurhonensis"
                     /db_xref="taxon:1936995"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116207
     Region          43..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkkfrpvsl illmgialsf sgslyanpet enpvidisqq ngkvsgtved algpvtgasv
       61 iikgttngti tdldgnftle gvkkgdiiqi sfigyitqdi pytgqstikv dlvedtqkld
      121 evvvtalgmk rdkkalgyam qelkgddlia srepnlansl sgkvsglqiv rssngvggss
      181 kivlrgnnsl tgsnqplivv dgtpmdnftg gvddvwgnsg admgnglsdi npediesmtv
      241 lkgasaaaly gsragngvil ittksgrkte gvgitvnagi taetiflkph mqdnfgqgsv
      301 nvydnqsrls wgpkadgqmv tdwlgrevpl htydnidaff rtgtsfnegv sfqqdingts
      361 vftsinrsdd asitpeskln ktnitvratt fldkdkkwka dakvnyinmn ahnrpiqgvn
      421 psnafntiyn lprslnikef encvdengnm iwydasknpq enpywvtkyr qnedtrnrll
      481 gnvslkyapt dwfdielrgg tdyytttkne kvyaggntsp rglysegset fyennfsfla
      541 tarkdnlinr lggfitfggn lmqqqrnkmn asagellvpd lfslnngvnk ptvtselirr
      601 kmnslygslq lnwdgylfld vtarndwsst mskanrsyfy psvslsavis dmlpklgsqm
      661 pdwfsfakvr asyaevgndl dpyqlynyfs vskdpngnnm akpgkvlfds nvrseliksw
      721 eagfdirffn nrlgldaawy ksnatrqlld lpmdpfsgys srkvnagniq negvelslng
      781 aifdnprgfn wnataqfsln rnkiidlypg vtlydiktfd aiqivavqgs lygdiygqtf
      841 qrvtdknsph ygkivvgddg lplistdksk vgnqnpdwml gltnsfaykg fnlsflidfr
      901 iggdlysata sglytrgnae gtvvngdrqp fvvpnsvmqk gngyvennvq vtpqnyweri
      961 gstgnyglpe mytydatnvr lrnitfgyef drqmlkktpf qrvrlsatcn nvwmihynlp
     1021 gidpesvaat ntnatgfeng aaptsrsytf nvtigf
//
LOCUS       WP_102408484            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides bouchesdurhonensis].
ACCESSION   WP_102408484
VERSION     WP_102408484.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides bouchesdurhonensis
  ORGANISM  Parabacteroides bouchesdurhonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Parabacteroides bouchesdurhonensis"
                     /db_xref="taxon:1936995"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114945
     Region          42..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlknskpvsl illagalcfs gnvyadlapv kqgttisqqs gkvtgtvedd fgpvtgasvv
       61 vkgttngtit dfdgnftled vkkgdiiqis figyttleip yngqalgsik laedtqklde
      121 vvvtalgikr ekkalgyatq elkgdailda resnvtnals gkvsglqvvr ssggpgsssk
      181 ivlrgnssit gtnqplivvd gvpmdnfqgg vadawgnkgp dmgnglsdin pediesmnvl
      241 kgasaaalyg sragngvili ttksgkkqtg lgitvnagvt aetmfmepdi qssfgqgstg
      301 iynvksrssw gpiadgsvni dswngqnvpm ytydnvgnyf dtgvsfnegi sfqqanegts
      361 vfasinrsdd kgivpgakls ktsinlrgtm efgpdkrwkl dgkvnylnni ghnrplqgin
      421 qsnafstiyn lprsinildl kncvdsegqm iwwdtektpq enpywtkdyr tnedtrnrfl
      481 gtmslsykif dwwnvelkgg tdyytttttn klyaggnvtp kgnysegset fyennfsflt
      541 taqkdnllgk fggfvtfggn lmmqkrtkek istgdllipn lfsvnnaadk nnmgyeytlt
      601 qrkmnslygs lqinydgwmf ldltarndws stmssanrsy fypsvslsav vsdmiqkngg
      661 slpdwmtfak vrasfaevgn dldpyqlytv ysmdkdpfgn pvakpgdvly npdvrselik
      721 sweagvdlkf lnnrlgidfa wyksnatrql ldlpldpfsg ysskkinagn iqnagveima
      781 yadifqnpkg fswnitanls fnrnkvidly eginemglsd gsfndevkvv artgglygdi
      841 ygrkfqrves gpdagkiivd aqglplltse lqylgnqqpk cmlgitntfn yknislsfli
      901 dariggkiys attaklyyng aaagtvvnga reefvvpnsv tasgdsytan ttpvtpqlyw
      961 eragngnlgv geaflydatn vrlrnltlgy sfdkkllakt pierlrlsft annvwmiash
     1021 megidpesvs ttntnatgie lgaaptsrsy tfnvtvgf
//
LOCUS       WP_102419072             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium sp. 4858].
ACCESSION   WP_102419072
VERSION     WP_102419072.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium sp. 4858
  ORGANISM  Mycobacterium sp. 4858
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Mycobacterium sp. 4858"
                     /db_xref="taxon:2057185"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37312
     Region          7..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdaqttvgv vaesgaderr valvpkavas ligsgvavvv esgagegall pdqlyteaga
       61 sigdawsadv vvkvapptke evarlrrgqt ligflaprna dnsigaltea gvqafaleai
      121 prisraqvmd alssqanvag ykavllaase strffpmltt aagtvkpasv lvlgvgvagl
      181 qalatakrlg artsgydvrp evadqvrsvg aqwldigida ageggyarel teeeraqqqq
      241 slekaiagfd vvittalvpg rpaprlvtaa avesmkpgsv vvdlagetgg nceltepgrt
      301 vvkhdvtias plnlpatmpe haselyskni talldllikd gklapdfdde vvaaacvtra
      361 gkega
//
LOCUS       WP_102429832             434 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            breoganii].
ACCESSION   WP_102429832
VERSION     WP_102429832.1
KEYWORDS    RefSeq.
SOURCE      Vibrio breoganii
  ORGANISM  Vibrio breoganii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Vibrio breoganii"
                     /db_xref="taxon:553239"
     gene            1..434
                     /gene="nrfA"
     Protein         1..434
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=48339
     Region          2..434
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 meeahpdqyh swkatsesee iddalagdpn mvilwagygf akdynkargh fyavddvrqt
       61 lrtggptdae sgpmpmacws ckspdvarvi dergedgyfe gkwarlggei vnpigcsdch
      121 dtgsekfkng epelaitrpy vdramqaigk pfeeqsrldq qasvcaqchv eyyfvkdakn
      181 avkfpwdmgt svgemelyyd algfadwthg vskapmlkaq hpgyetwrdg ihgknnvvca
      241 dchmpkvere dgtvytdhki gnpfdrfedt canchtqskd qlqgivstrk aqvlnmklta
      301 ekqivaahfe akaawdagat eqemepilqd irhaqwrwdy aiashgvhmh apeialevlg
      361 tavdraadar tktirllakk gitdpvpipd istkekaqaa lgmdmdamna ekehflktvv
      421 pkweeeakar eaty
//
LOCUS       WP_102438441             397 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Shewanella].
ACCESSION   WP_102438441
VERSION     WP_102438441.1
KEYWORDS    RefSeq.
SOURCE      unclassified Shewanella
  ORGANISM  unclassified Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="unclassified Shewanella"
                     /db_xref="taxon:196818"
     Protein         1..397
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41948
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,97,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklglpkesh pgelrvalip anvtallkkq lqvivesgag qnagftdddy vkvgatiass
       61 raallneadi itvvnckgeq fdeikalikp qqlligmmdp linpqnaqai adtgasaial
      121 elipritraq smdvlssmat isgykavlla ahkaprlfpm mmtaagtlkp trafimgvgv
      181 aglqacatak rlgavveayd irpaareqii svgakpveld ieaentetkg gyateqsddf
      241 lkrqqqaman vlaqqdivit taaipgrkap vlitkemvdg mkngtiivdl aaesggncel
      301 trvdevimhn gvmilgpsnv pstaanhasq mygknvenll nlivskegel vldfedeivr
      361 dtvvahgkev tsarlrdllg laplatpead tsveeka
//
LOCUS       WP_102452103             308 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Vibrio breoganii].
ACCESSION   WP_102452103
VERSION     WP_102452103.1
KEYWORDS    RefSeq.
SOURCE      Vibrio breoganii
  ORGANISM  Vibrio breoganii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Vibrio breoganii"
                     /db_xref="taxon:553239"
     Protein         1..308
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35681
     Region          5..170
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maihelysmr nkakypdvyq yerasrklrt qvaqilvati gnkigydyqk tpsqevyeii
       61 fdilkrayge delaghysgs shwlhkyltg dyldieefld vveltcdvid khvrprwarf
      121 knndnvfqnp ddaleeiner mkrdgfgyef tdgiivride qyihaeavkp alcilqnyea
      181 prqefleahe hyrhrnfkec lmncgrafeg mmkiicdkeg weynpkkaga snlialckdk
      241 glfethtqeh lnglaktles gvppirneka ghakpepiev sehitkytlh ltavnlvfln
      301 dcyeamkk
//
LOCUS       WP_102467890             471 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [unclassified Vibrio].
ACCESSION   WP_102467890
VERSION     WP_102467890.1
KEYWORDS    RefSeq.
SOURCE      unclassified Vibrio
  ORGANISM  unclassified Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="unclassified Vibrio"
                     /db_xref="taxon:2614977"
     gene            1..471
                     /gene="nrfA"
     Protein         1..471
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52539
     Region          3..471
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnkhwiissv aslailgaas apafaatkdg ladprnqtye enhpdqyktw kqtsesdgie
       61 dalkqdpnmv ilwagygfak dynkarghff aiddvtqtlr tggptdpksg pmpmacwsck
      121 spdvarviee rgedgyfegk warlggeisn pigcadchdt rsekfkngep elaltrpyve
      181 rafeaigkkf edqsrldqqa svcaqchvey yftgpnksvk fpwdrgtrvg emeqyyddie
      241 fkdwqhavsk apmlkaqhpg fetwregihg kngvvcvdch mpkvtkedgt vytdhkvgnp
      301 fdrfedtcan chtqskdqlq givssrkaqv lnmkltaekq ivaahfeaga awdagateee
      361 mkpilmdirh aqwrwdyaia shgvhmhape valevlgtsv gkaadarakl irllakkgit
      421 dpveipdist kekaqaalgm dmdkmnaekq hfletvvpqw eaekearesk y
//
LOCUS       WP_102510546             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sanguibacter massiliensis].
ACCESSION   WP_102510546
VERSION     WP_102510546.1
KEYWORDS    RefSeq.
SOURCE      Sanguibacter massiliensis
  ORGANISM  Sanguibacter massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Sanguibacteraceae; Sanguibacter.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Sanguibacter massiliensis"
                     /db_xref="taxon:1973217"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51875
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkesa pdqrlvaatp qtvgklvdlg yevvveegag sgasipdaly taagatvvda
       61 agawsadvvi tvdgpgagdv erlaegatlv arlapddtpe lvealrergv talnlmsvpr
      121 israqaldvl stmsnvsgyr giieaaesya gmfggqvtaa gstpparvfv igagvaglaa
      181 lgaagslgae vraydvradv aeqiesmgat fvrveadaqe sadgyakelt adqeaataav
      241 yaaesaaadv vvttalirgk apititaemv aamkpgsvvv dlaasgggnc eltmpgekiv
      301 tdngvtiigy tdlpgrmpkh tsqlygtniv nlmklltpak dgelvldled vvqrgitvtr
      361 ageilwpppp vqvsaapapa paapaeaapi aqapakpakk katgtligga itaalvvaav
      421 afstatfash ltvfalavvv gfyvvtgvth slhtplmaqt naisgiilvg sllqigsdnl
      481 vvtilavvaa tfasinifgg fsvasrmlam fqkea
//
LOCUS       WP_102519162             397 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            sp. 10N.286.48.A6].
ACCESSION   WP_102519162
VERSION     WP_102519162.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. 10N.286.48.A6
  ORGANISM  Shewanella sp. 10N.286.48.A6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Shewanella sp. 10N.286.48.A6"
                     /db_xref="taxon:1880833"
     Protein         1..397
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41948
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,97,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklglpkesh pgelrvalip anvtallkkq lqvivesgag qnagftdddy vkvgatiass
       61 raallneadi itvvnckgeq fdeikalikp qqlligmmdp linpqnaqai adtgasaial
      121 elipritraq smdvlssmat isgykavlla ahkaprlfpm mmtaagtlkp trafimgvgv
      181 aglqacatak rlgavveayd irpaareqii svgakpveld ieaentetkg gyateqsddf
      241 lkrqqqaman vlaqqdivit taaipgrkap vlitkemvdg mkngtiivdl aaesggncel
      301 trvdevvmhn gvmilgpsnv pstaanhasq mygknvenll nlivskegel vldfedeivr
      361 dtvvahgkev tsarlrdllg laplatpead ttveeka
//
LOCUS       WP_102521211             476 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            tapetis].
ACCESSION   WP_102521211
VERSION     WP_102521211.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tapetis
  ORGANISM  Vibrio tapetis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Vibrio tapetis"
                     /db_xref="taxon:52443"
     gene            1..476
                     /gene="nrfA"
     Protein         1..476
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53236
     Region          1..476
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkkhwirnsa aallfgssyl fsmgclaape tneigdprnq tyeenhpdqy nswkatsesk
       61 alddalasdp nmvimwagyg fakdynkarg hfyavddvrq tlrtgaptda nsgpmpmacw
      121 sckspdvars ieergedgyf egkwarlgae iinpigcadc hdtksdefkn gepaltitrp
      181 yverafeaig kkfddqsrld qqasvcaqch veyyftgptk gvkfpwdngt kvgemetyyd
      241 alnfkdwthk vskapmlkaq hpgyetwreg ihgknnvvca dchmpkvtke dgtvytdhki
      301 gnpldrfedt canchtqske tmidivgtrk qqvtnmklta ekqivaahfe agaawdagat
      361 eeemqdilld irhaqwrwdy aiashgvhmh apevaleilg tavdraadar tklvrllakk
      421 gilepieipd istkaaaqka lgmpmdkmns dkdtflktvv pqwekeaaer eskyey
//
LOCUS       WP_102531995             397 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            sp. 10N.286.52.B9].
ACCESSION   WP_102531995
VERSION     WP_102531995.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. 10N.286.52.B9
  ORGANISM  Shewanella sp. 10N.286.52.B9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Shewanella sp. 10N.286.52.B9"
                     /db_xref="taxon:1880837"
     Protein         1..397
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41932
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,97,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklglpkesh pgelrvalip anvtallkkq lqvivesgag qnagftdddy vkvgatiass
       61 raallneadi itvvnckgeq fdeikalikp qqlligmmdp linpqnaqai avtgasaial
      121 elipritraq smdvlssmat isgykavlla ahkaprlfpm mmtaagtlkp trafimgvgv
      181 aglqacatak rlgavveayd irpaareqii svgakpveld ieaentetkg gyateqsddf
      241 lkrqqqaman vlaqqdivit taaipgrkap vlitkemvdg mkngtiivdl aaesggncel
      301 trvdevimhn gvmilgpsnv pstaanhasq mygknvenll nlivskegel vldfedeivr
      361 dtvvahgkev tsarlrdllg laplatpead tsveeka
//
LOCUS       WP_102578428             307 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Vibrio lentus].
ACCESSION   WP_102578428
VERSION     WP_102578428.1
KEYWORDS    RefSeq.
SOURCE      Vibrio lentus
  ORGANISM  Vibrio lentus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Vibrio lentus"
                     /db_xref="taxon:136468"
     Protein         1..307
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35393
     Region          5..173
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mgifdlyssr nkpkypelyq ytkasdklrk qlvhivadsi gmrvagrydn pkksqglyhd
       61 mflilakeyg vfelyghnqg sfkwleqhiq naktteqfld ilelickfid kvvrpdwdsf
      121 wysdgikqrp dealkeiner mkrdgfgfey tngqlirvds qyvhaevvkp alsildnhkg
      181 areeflsahe hyrhnkyeec lvdcnkafes lmksiygkrg weyqktatak klirvgldng
      241 liptylqeqf nnfssllesg iptirnkeag hgqgesvrdv pkplvkyalh ltatnivflg
      301 dcdialk
//
LOCUS       WP_102588302             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            urumqiensis].
ACCESSION   WP_102588302
VERSION     WP_102588302.1
KEYWORDS    RefSeq.
SOURCE      Halomonas urumqiensis
  ORGANISM  Halomonas urumqiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas urumqiensis"
                     /db_xref="taxon:1684789"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55520
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkera kgearvaltp esaghiqklg heclvqsgag eaagfsddky reagvsvvdd
       61 adtlwrdaev vvkvrepide evellregqt lisffwpaqn eellercrgk gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfde sqdgsetggy aapsspefre
      241 kqlecfraqa pdidivitta lipgrpapkl wladmveamk pgsviidlaa ekggncdltr
      301 adekvvsdng vtvvgytdfp srmatqssll ystnirhmlt dltpekdgai vhnmeddvir
      361 gstvthagei tfpppppkvk aiaaakpkpk ekaptpeekr aadlatfkaq tkrqatllgv
      421 ggammlllgq iapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgiiilga
      481 vlqigsgsav vvilaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_102600332             305 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Vibrio parahaemolyticus].
ACCESSION   WP_102600332
VERSION     WP_102600332.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..305
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34675
     Region          8..171
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mgifelhssr nkpkypelyq ydyasiklrr qlihifagai gsrkgargqt qsqrvyksmf
       61 siiareygvf elsghsqgsf swleqhiqst giieqfldvl elackhidvs vrgelirfqs
      121 tdrisqlpdd aineinermr rdgfgyeytn gqlirvdsqy vhaevvkpal sildnhigar
      181 eeflsahehy rhnkyeeclv dcnkafeslm ksiyskrgwd yqktatakkl irvgldngli
      241 psylqeqfnh fssllesgip tirnkeaghg qgesvrdvpe alvkyalhlt atnivflgdc
      301 ditlg
//
LOCUS       WP_102592492             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_102592492
VERSION     WP_102592492.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38745
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvlv gmlnpfsset iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_102596241             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_102596241
VERSION     WP_102596241.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36063
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmlktgipti rnknaghgqg adikevpeel vsymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_102603298             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Citrobacter freundii complex sp. CFNIH2].
ACCESSION   WP_102603298
VERSION     WP_102603298.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii complex sp. CFNIH2
  ORGANISM  Citrobacter freundii complex sp. CFNIH2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter freundii complex sp. CFNIH2"
                     /db_xref="taxon:2066049"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53497
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 maritlrarr ffslivplff isavyaeqtp epaktvtvea knevfapqhp dqylswkats
       61 eqskredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc gdchntaspd fakgkpeltl
      181 srpyaerame tigkpfdkag rfdqqsmvcg qchveyyfdg kdkavkfpwd dgmkvedmek
      241 yydaitfadw tnslskapml kaqhpeyetw svgihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf pqtcanchtq dkaslqnvva erkkainglk ikvedqlvra hfeakaawda
      361 gateaemkpi lsdirhaqwr wdlaiashgi hmhapeeglr mlgiamdkaa dartklarll
      421 atkgitheia ipdistkeka qaaiglnmqq inadkqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_102607047             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            symbiotica].
ACCESSION   WP_102607047
VERSION     WP_102607047.1
KEYWORDS    RefSeq.
SOURCE      Trinickia symbiotica
  ORGANISM  Trinickia symbiotica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Trinickia symbiotica"
                     /db_xref="taxon:863227"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38694
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpaetv agesrvavtp etakklvalg hsvlvqsgag laaaaddaay eaagaqitdv
       61 agvfgcglil kvrapsarel emmrpgsalv gmlnpfdsag vgklaaagit afaleavprt
      121 traqsmdvls sqaniagyka vmiaadryqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgasi easdvrpsvk eqaeslgakf idvpyetdee reiaegvggy arpmpqswld
      241 rqkaavakrv aqadivitta lipgraaptl iteemvrsmk pgsvivdlaa gkgpdgtggn
      301 cplteadrtv vkhgvtlvge tnlpalvaad asalyarnvl dfvklvlpkg adaisipddd
      361 eivaacviap ereteei
//
LOCUS       WP_102609472             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            soli].
ACCESSION   WP_102609472
VERSION     WP_102609472.1
KEYWORDS    RefSeq.
SOURCE      Trinickia soli
  ORGANISM  Trinickia soli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Trinickia soli"
                     /db_xref="taxon:380675"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39723
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahearvaatp etvkkyvqag hrvtiergag aaasftddaf aavgaelvea
       61 daafsadlvl kvqapsetel alfkrgavlv gmldpfnpsn aehvaqaglt afaleaaprt
      121 traqsldvls sqaniagyka vliaadlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf idvpyetqee reaaegvggy arpmppswla
      241 rqsaavhera kaadivitta lipgrdaptl lsaetvqamr pgsvvvdlaa grgaelagmp
      301 gvrggncplt epdkvvtkhg itivghtnlp amvaadassl yarnlfdflk livtkegaln
      361 idmnddivaa tllardgavt rkaa
//
LOCUS       WP_102621137             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_102621137
VERSION     WP_102621137.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38806
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvvdsay eaagatigsa
       61 sdafgaelil kvvapsdtel alikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyeteee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv tivgptnlag evaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_102630564             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia rhynchosiae].
ACCESSION   WP_102630564
VERSION     WP_102630564.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia rhynchosiae
  ORGANISM  Paraburkholderia rhynchosiae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia rhynchosiae"
                     /db_xref="taxon:487049"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39429
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvaqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgaelvl kvqsptdael pllrrgatlv gmldpfnten ssklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyeteee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvetvqamk pgsvlvdlaa grgaeyegqr
      301 ggncpltead kvvvkhgvti vgytnlasmv padasslyar nlldflkliv tkegtlnidl
      361 addivaatll ardgevarka
//
LOCUS       WP_102626777             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            heilongjiangensis].
ACCESSION   WP_102626777
VERSION     WP_102626777.1
KEYWORDS    RefSeq.
SOURCE      Halomonas heilongjiangensis
  ORGANISM  Halomonas heilongjiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas heilongjiangensis"
                     /db_xref="taxon:1387883"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54975
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapresa agearvaltp esaqqiqklg heclvesgag vaagfddday raagvtvvdg
       61 aealwseaev vikvrepsee evgrlrqgqt liaffwpaqn eallekcraq gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgsgtggy aapsspefre
      241 kqlalfreqa pdvdivitta lipgrpapkl wladmveamk pgsvivdlaa ekggncdltr
      301 adekvvsdng vtvvgytdfp srmatqasll yatnirhmlt dltpekdgai vhdmeddvir
      361 gatvthagev tfpppppkvk aiaaakpkek vkeptpeekk aaehaaflaq tkrqvtllgv
      421 ggalmlvlgq vapasflqhf ivfalacfvg fqviwgvshs lhtplmavtn aisgiiilga
      481 ilqigsgswi vgvlaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_102634963             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia rhynchosiae].
ACCESSION   WP_102634963
VERSION     WP_102634963.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia rhynchosiae
  ORGANISM  Paraburkholderia rhynchosiae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Paraburkholderia rhynchosiae"
                     /db_xref="taxon:487049"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39374
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaear aretrvaatp etvkkyvaqg hrvtiqsgag vgasfqdeaf aavgaeivda
       61 atafaadlvf kvqspsdael pqmkrgavli gmldpfnaen aqklaaaglt afaleaaprt
      121 traqsldvls sqaniagyqa vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmpqswls
      241 rqaalvhdra kqadivitta lipgrpaptl isvetvqsmk sgsvlvdlaa grgpefdghk
      301 ggncpltvad qvvvhngvmi aghtnlasmv asdasalyar nmldfmkliv tnegslnidl
      361 tddivaatll crdgelark
//
LOCUS       WP_102643858             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            dabaoshanensis].
ACCESSION   WP_102643858
VERSION     WP_102643858.1
KEYWORDS    RefSeq.
SOURCE      Trinickia dabaoshanensis
  ORGANISM  Trinickia dabaoshanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Trinickia dabaoshanensis"
                     /db_xref="taxon:564714"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39779
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahearvaatp etvkkyvqag hrvtiergag aaasftdday asvgaelvea
       61 daafsadlvl kvqsptetel almkrgavlv gmlepfnaen aarlatagit afaleaaprt
      121 traqsldvls sqaniagyka vllaadlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetqee rdaaegvggy arpmppswla
      241 rqaaqvhera kaadivitta lipgrdaptl lssetvqamr pgsvivdlaa grgpelagla
      301 gvrggncplt epdkvvtkyg vvivghtnlp amvaadassl yarnvfdflk livtkeglln
      361 idvsddivaa tllardgavt rkaa
//
LOCUS       WP_102654417             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Billgrantia endophytica].
ACCESSION   WP_102654417
VERSION     WP_102654417.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia endophytica
  ORGANISM  Billgrantia endophytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Billgrantia endophytica"
                     /db_xref="taxon:2033802"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55722
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspkery rgearvaltp esaqqiqklg heclvesgag eaagfsdety reagvtvvad
       61 aaslwretdv vikvrepsde eadllregqt liaffwpaqn eallerckar gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 saigtaaslg avvrafdvrp evaeqiesmg aeflfldfee aqdgsgsggy aapsspefre
      241 kqlalfreqa pdvdivvtta lipgrpapkl wledmvkamk pgsvivdlaa ekggncdlte
      301 pdkkvvsdng vtivgytdfp srmatqssll yatnirhmlt dltpakdgai vqnmeddvir
      361 gatvahrgei tfpppppkvk aiaaakpker vkeptleekk aaelatfkvq tkrqltllgv
      421 ggalmlvlgq vapvsfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn avsgiiilga
      481 ilqigsgnwi vvllaavsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_102664902             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas salmonicida].
ACCESSION   WP_102664902
VERSION     WP_102664902.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53130
     Region          22..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrlt rlglaalllt tcfgasglaq adeatpkgki earselfakd hvdqfsswkg
       61 tsesatrtda laedpqmvvl wggypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggseivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eqyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqgkemlqgi vqqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaqmk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llatkgishe ialpdistke kaqaalgmdm kqmnsdkaqf lkttvparda eakaagrlaq
//
LOCUS       WP_102665316             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aeromonas
            salmonicida].
ACCESSION   WP_102665316
VERSION     WP_102665316.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53223
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevaieagag qlasfddaaf eaagasvvps
       61 vwqadlifkv naptdaeiaq ikdgatlvsf iwpaqnpelv kklserninv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggefl kldfgsedga ssdgyakvms defiaaemal
      241 faqqakevdi iittalipgr papklitkem vdsmkpgsvi vdlaaatggn ceytkptelf
      301 vtlngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgqvaidfe dvvqrnmtvi
      361 qagevtfppp aisvsaapqk paaapikkae ekqpsnkkfv fgalgiaafg wvaavapaaf
      421 lshftvfila cvvgyyvvwn vshslhtplm svtnaisgii vvgallqigq gstlvtalsf
      481 vavliasini fggftvtqrm lkmfrkd
//
LOCUS       WP_102685615             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_102685615
VERSION     WP_102685615.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38561
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagasigsa
       61 ndafaaelil kvvapsdsel aliksgtvvv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaaavhera kqadivitta lipgrkaptl lsaqtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlas avaadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_102684787             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_102684787
VERSION     WP_102684787.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38877
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvgqg hqvtvqrgag lkasipdsay eavganlgea
       61 adafgaqlvv kvvapsdqel alinsgslla gmlnpfnnel iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvmengv tlvgptnlpa qvgadasaly arnlldfmkl lfdkdgnlvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_102689256             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_102689256
VERSION     WP_102689256.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38864
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvattp etikkligqg hqvtvqrgag lnasipdsay eaagaslgsa
       61 adaygaqlvl kvvapndqel alinsgslla gmlnpfnsel iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera rqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvrengv tivgptnlpa qlgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_102696498            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            buccalis].
ACCESSION   WP_102696498
VERSION     WP_102696498.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121020
     Region          22..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiytilll mlcalqgfaq eriingtvkd gdlkdeplig atiskgsgkv ssgtitdyeg
       61 kfklpvdkst keitvsyigy ttqtiklkag vnhyeivlmp dahsinevvv tgyqridrrk
      121 ltaavttvdi sdkavgavkn idqalagqia glstvsssga pgapvkirir gtasingtqe
      181 plwvldgipl egtdipsmen lndiddmyqt siaginpsdi enitvlkdaa ataiygaraa
      241 ngvivittkk gkegrpvvnf sakytyspkl nidrlnllna dekvnlelal lgsdytfran
      301 kgevanilkt lneteaykkg gwnalspsaq tqinalrsin tdwndillrs afnqeynasv
      361 aggsdrakyy tsvgyydeqg nvkgvdnkrf nmtlktdyri nkilklgasv yanqrkqssy
      421 ltdtngftnp vyysrlanpy fqpfidgkyn ydtnvqgket sslnfnifee renshnrrtd
      481 rsmmaifdae lqftkdlklt sqfglqydny slekyagens yamrkeklnt vydfkdgkrs
      541 ylpeggthkt tsynslqwtw kamleyarrf nkihdvella gsevrhidse siysaaygyd
      601 artltthpvi fpsevsaesl plhrenkaen ayvswfatgs ytllyrytlg gsvrfdgsdv
      661 fgvakkyryl plysvsalwr vhqekflkna kwlnnfalra sygiqgnidk ntspyligly
      721 dktsilpgkg eqmikaetap npdlrwektk nvnlgtdiav lnnaltlsvd yyyrrssdli
      781 gmrmlpletg faattinwas menkgweial gsrniytkdf hwttnlnlgf ntnkilnesv
      841 aenstypgre gypvgaifay ktagldaegy pvfvgaagek ltaeeffkln kagastlsae
      901 kqrnlytymg ttdpkvsggf inhfeykdwq lgvnfifnlg mkvrvqptys ptnydrglnt
      961 nrdilsrwta nhtnttfprl mvsgyrvpey vqyseyntys mldtwvrnns ymrlqsvrlg
     1021 yklpktwvnr vgianasvsv earnlfvmas nytnyldpet mgnpfaqpip ksvifglnln
     1081 f
//
LOCUS       WP_102696778            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            buccalis].
ACCESSION   WP_102696778
VERSION     WP_102696778.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116315
     Region          35..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktffsqsl vvgiialfsl sgpllaqqpa gsdrftiegt vvdntnnepi agatvrlksg
       61 lrgtatnaeg kfvvkecsaq dvfqvsfigy kpknftvgkh rrftiyleen stqieqvvvt
      121 gfqklkknsf tgsativtse dlkkvnskda vkalqvfdps frimdnlgfg adpnqmheis
      181 irgassisqn rgldvenqrl tqrtnlrdnp nmpifmldgf evdvqkiydm dinriesmti
      241 lkdaaataly gsraangvvi vttvppkage iridynttle lsfpdlsdyn ltnateklqv
      301 ekdaglyvgt fgvatidker eyndklnevr rgvntdwlar plrnaynwrn dvslsggvne
      361 vrymlnlnyd nnagvmkgsr rdrygagmmi dyrlrdwlhi qnkvtlnrts yedspygyfn
      421 dysqqlpyda iyddagellr elpmshranp lwrerylqsy sgrggitdvt dnlsvnihft
      481 pslylrgtfs vsqvktdskt fkdpkdsflf rtvannrkgs ldvsgdtrlk wnanamlhfn
      541 krlkrhflnl tagvdaqetn drrlsyrleg fnigslndpi yaatqtdkti dtksttrlfg
      601 vlgalnytfd eiylldasfr mdgssqfged krfapfasvg vglnvhnysf vkklpwintl
      661 rlrgtygstg kvnfsrfdvi ssykadtkaw yytgpavrlf tmgnsalswe itksldvgft
      721 aelfknrlyi eaayykkttd gmidrisirp ssgftsysgn vgsienkgfe lktnitlfrn
      781 rdwsvvanan lganknrisk lddaieeynk kirdnydaeh pqyqnlqnrp liqyyvgast
      841 taiyampslg idpasgkelf rkkdgtitke wnasdmvvcg dtnpdaqgsf ginvaykgiy
      901 mnasflyafg gqvynqtlle kvenaqikdq nvdrrvitdr wrkvgdiapf yglgeksstr
      961 ptsrfvqndn yvhfnslsig ydfsrklisk lklsalsvti nasdlarwnt vrverglsyp
     1021 yahtysislr asy
//
LOCUS       WP_102696420            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            buccalis].
ACCESSION   WP_102696420
VERSION     WP_102696420.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122101
     Region          31..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkktllffc fclislaiva qnpqksdamv kvvttitdtd gnplggatvk vkgkpvgvia
       61 dmdgkvslwv drgntitvsy lgmksktikv tsaltknivl endaslldqv vvtgytrttk
      121 rrttgsvsti taedlnknpt anldmllqgk magvdvkals grpgesakvr irgtntitgn
      181 adplwvvdgv alqkdlptis kaqmlsgnfs difsngiagi npndiesvtv lkdasaaaiy
      241 gsraaggviv vttkrgvagk lrinysanat mvtrppravd lmdskeklaw eqelwdeysk
      301 pyfekneryp vigivgmirs gygqykgmnk eqqdaeiarl gshttnwfde lfrnsvsqsh
      361 nlslsggsek stfyvslgys enaglvkktd ysryninskl dikpnkrvkl glsldlgwqt
      421 snspslavdl fkyayfanpy ervyddqgny apdqtyynim langskstlp lpdngvnimr
      481 einntssktk nfsstvigni siniidnlnf eglgsysytt nngdnindkd tytawqdrpf
      541 dlktltskrt yssiaqsssy nssynlrgql hyfntfndkh yisgllgsei rgqyaksifa
      601 krygydpvsg nsampvypeg ktfeyndlkn yallmdnlsg qnivedrfas fyfsadyvyn
      661 nryvfsftgr tdgsnnfgsk eqfnptgslg lswnvdqesf meklkpiiss lslrtaygft
      721 gninksvhpq vimdyrqsfr ktdtdyyrmg wikkapnpnl rwektkdmkv sidagflndr
      781 irmtgeiykr vtsdavsevf ipystgfrnq sfntsklsnt gaeftlsaqv ikqddwnlli
      841 sgniaynrnr lleyksivsg lgegfyvgyp igsifsgkva gidsrlglit yeprpdavfe
      901 tsadrnnaen ylfylgtsna ptnggysmsl sykrltlsls gtyslggkil nqinspvgyg
      961 slsgnkveki psqmndlyvn hlnvtrdvvn rwttknhrtd ahprildayg kyygldnyvv
     1021 sspkitkasl ledvsyfkig slnlaysfdt kliqriglss lsvsftadni ytftnysgid
     1081 pespgavypm arsfsmgvfv gf
//
LOCUS       WP_102696864            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            buccalis].
ACCESSION   WP_102696864
VERSION     WP_102696864.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123838
     Region          25..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkltillv dlflcigvan aqtlingtvt saddgqpvig asvmvvgtkt gvvtnvdgkf
       61 sltstksnpm itvtyigmkt qtlrgtqnmk ivlqsdaqkv devvvtgmqk mdkrlftgas
      121 tkvdaekskl dgvadisrsl egraagvsvq nvsgtfgtap kirvrgatsi ygsskplwvv
      181 dgvimedvte vnadqlssgd aatvissaia glnaddiesf qilkdgsats iygaramsgv
      241 ivvttkkgka gkthinytge ftmrlkpsys qfnimnsqeq mgiykelean gmlsfgrthr
      301 astsgvygkm yqlmntydpt tgnfllpnte dgkikylqaa emrntnwfde lfsnavsmnh
      361 sisissgtek aqyytsfsmm ndpgwteqsn vrrytfstna lynmskhlsl nlignaayrk
      421 qkspgamnqh vdnvtgavtr dfdinpysya intsrtldan efyvrnyapf nihhelannf
      481 ndydvidtkv qaelkykpit kvelamlgay kfstttqanq irdnsnvama framddatml
      541 ygnqrlytdp dvpnslpfsv lpnagfyret kykmnswdfr atasyndvya ndhivnlfgg
      601 mevnntdrnr syfngvgmqy emgllgsydy ryfkqsseen eiyydlsngh srevsffgtg
      661 tyswkgryti ngtvryegsn rlgkarsarw lptwnisgaw nmheepwfek afknslthat
      721 fkasysltgd kpavtnaavi iqsynpwrpf tvdkesglei wdfandelty ekkhelnlgm
      781 dlgflnnrin vtfdwyrrnn ydligpritn gtkgtiveya nvasmksnge elsisskniv
      841 skdftwntdf ifshvktevt slknrrnliq mitgsgftle gypyrslfsm dfqglnengi
      901 ptfinengek ttsgiyfqsr niehlkyegp vdptytgslg ntfsykgwhl ivfatyafgn
      961 kvrldpafys wysdldatpk efrnrwtkag demttnvpai pdlrqrqqdq rlsyaynayn
     1021 rstervakgd firmkeisls ydfpqrwany lhlnkvnlkl qgtnlfliya dkklngqdpe
     1081 ffnaggvavp marqltmtlr vgl
//
LOCUS       WP_102697325            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            buccalis].
ACCESSION   WP_102697325
VERSION     WP_102697325.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112513
     Region          20..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlagmlsala ptaasaqesk vfgyvtnaqn epligvtvrv dgtkhatvtd adgryrlsip
       61 kragisleft yvgyatqhvk ckqnarldvk mkenvnhige vviraksnin aidlraksgv
      121 vanvdmqqlk dkpmidmgla lqgmvpglmv antgelgkap eirirgnssf rkgntanepl
      181 yvldgqiisa etfynlppqd iagikvlkna aacalygvka angvleitsq rgysgkptis
      241 ystnigvtgr gkrgvalmrt deklrfehll enpaapgyry sedyfnkyes gnpdkarlia
      301 egkvlldkls kvdtdwfdel iktnvyqrht lslkggndit tyyisanyal qggrmegndk
      361 rryslhlsld qrigsigylm lgvnggyakt ntptgtsfdp tslvynlnpy etkkgklysy
      421 pnqtfkdllh qykqddtekd agatanftlt pldgltlayi tgidlsfstn hrfvpassys
      481 eqksgfpemr lgvysrskna tvnfssnfra tyskslaeth dltlsanmdy yfydydavgi
      541 tgygvgnida psainhslhg mrqpevrnpr drnaqlgigl vagysykdiy dlyatykada
      601 ssilpadkrw svawatgigw tpsryewlkd nkiltslnlk asygvtsnln gvsvsqttgt
      661 fmfdnsgyde vrmldlvmly nkelrpernt stdfgmsfel wrrftidvnw ynrrtdqall
      721 dvpiasssgy tmmkrnvgvl dntgcevsmn mrlldhfdyr lslsaslsyn rnkvidlydg
      781 drlymseddi lpayevgksy dmlyglhslg inpltgypvf ltpdgkekqa keklykrdfm
      841 alghltppyn galnisaqyk sldfdisfyy tiggvrqfdy qyvrnrdnsn knaiaglvkk
      901 mwfkkgdenm iyntpfysdv iaqdnialya nsrtigksdm lklsmislry hlpgnmlrry
      961 vpfihfasla vqgsnlytwt sysesdpesg klsgtlqpvf tfclnltf
//
LOCUS       WP_102697545             773 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            buccalis].
ACCESSION   WP_102697545
VERSION     WP_102697545.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..773
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=87510
     Region          <21..772
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkeisyaqf qqevekvrmn ntdwfkelfr hsvshnhsvs lsggtdrfky yasinssftn
       61 gisvgndakn ysasvsidtr lsdiinlgvr lnaasnktng ffrvdpyqya stinraipay
      121 nedgslfyya ksqdanrrmy nilhemdctg ntnttnsval sanlrwtilq glqfeglfgy
      181 nlsnvvgssf adeqsffisn lrgyefglye pgeleykksr lphggelntt enrntnytlr
      241 gtlsynkifg evhrmslmag seirsnkydg ynttlygyfp nrgksiifpp rqvidpldas
      301 rwiendlyhq fnnaiidrki ntvgmfatgm ysyderyifs asirsdasnr fgqdernrfl
      361 pvwsagarwn iinepwikdi rwisdfnfra sygwqgnvas nygpdliael grgrdfidlr
      421 tgryilkiks lpydnlrwek tksinlgvdf gvwknriafs aeyyskhttd livskavpye
      481 ygvmfmping gdmnnygfef tatftpvrtk dwvwnisvnt aknfneikst maenqnwraa
      541 sggsihkegy pvgafwawdf agldaqggyp lfriptieeg adkldatsfm kyagttepdi
      601 sgglstvlrw ksitlsssfs ialggkrflt dlfsedylnn stpsaysnls kemvnrwqkp
      661 gdeqhtqips ipnhnipmvy lpngsneyah rlynystarv vnasfmrcnn islsytvpak
      721 liqrmslnnl sisgsvsnpf ivvskdykgi dpevatgaqp imptysvtln igi
//
LOCUS       WP_102697561            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            buccalis].
ACCESSION   WP_102697561
VERSION     WP_102697561.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114795
     Region          33..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkeyafrl smraclavlf mlvslslhaq nstvkgtvvd nlgepvigat vkvkgsnvst
       61 itdidghyai vcpshstlef syvgtrtlsv stdgkstidv tlenesqaid evvvtalgik
      121 rqsrslgyst tkvggedfql ardpnignal sgkiagvnva gngtgstgts rviirgnasl
      181 tgnnmplyvv dgvpfdntnq gsagmwggmd tgdglnnina ddiesiqvlk gaaasalygy
      241 rggngailit tksgkknqpv tvelnenltv nsiydyrdwq dvyglglngi kptdvkaaqe
      301 gesnswgavm dgseatnflg ntykyspvdn wknfygtgvt sntsaavsgs aqnviyrfga
      361 sfnkeksilp nagnrqlgfn mnttydifkn lhltvtanyt fdksngrsnl sdgngntnaa
      421 llyrgnsfdi twmegtekgw gttlegkemi ggtnvyfnnp ywlqyrktnd lrrerlvgsv
      481 nlrwdvtdwl ylqgavqrdg ysiefkqvqp igaaadpkgw mteneknfye nnfnfllgln
      541 kafgdwslga tfggnkqfnn trqyivtdgg rpfivnglws mnnlddkrpa kahiryqvns
      601 lygtadlgwk nqlflnltar ndwfstladd snshfypsat lswvftdtfr eqlpeafdfg
      661 kfrvgmasas ngtsayqnll lyqlrnykvn gqstatqnng nklpnntlkp vhisefeagl
      721 nlsffqsrln fdmayyvkkt tddiatvsts sasgygskvi nagkmknngf efmvdaypvr
      781 nkdfqwnttl nfaynnsnve flgdgvdrls idgaqsrngn vyiynvvgsp ygeiignkyk
      841 rneqgqlllk kglpqageqt slgngvyswt ggwhntftyk dftlgfllda kfgakifsgt
      901 nymlyyygmh ketlngrtke npigkivaag ideetgkana tavssqdyyr aitraniaee
      961 fvydasyikl relslgytfp kamlsrvkfv kglsfsivar nlwtimkhtp nidpesalna
     1021 sngqglelng ypatrnvgfn lnvkf
//
LOCUS       WP_102698036            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            buccalis].
ACCESSION   WP_102698036
VERSION     WP_102698036.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115744
     Region          41..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkknmllgl lsaglmwmpa satlaaqmnn aamsvqqnqg ikgtvvdatg etligasvkv
       61 vgttngavtd ldgnftlnck pgvtlevsyi gyktmtvkaa ngmkiqmqed gkaldevvvt
      121 algikrdrka lgygleevkg eeltkaketn vinslsgkva glvvqntagg asgstrvllr
      181 gntemagnnq plyvvdgvpl dntnfgsage sggydlgdgi sainpddiet mtvlkgpaas
      241 alygsrashg vilittkkae kdrisveyng sytvdtqlak wddiqeiyga gyngelpass
      301 tsgtnaswgp kaddfmfkyf dgeerpflmh pnnasdffrt gfttqnsail svnsgktgmr
      361 fsvtdmrnkd ilpntnmsrd nfnlrvntsa gpvdfdftan ytrekvknrp algdsqsnvg
      421 knlmtlagty dqtwlkryed adgnysnwng ndqynknpyw dlyknsntsd kdvfrftgka
      481 iwnidkhlkl qgtigtdins mnfedfiakt tpgtpagklt dqifnnrtln aeilalynns
      541 wgdfdvnata ggnifkvnnk tttniglnqq mngiqsimny qeqntresmy kkqinslyas
      601 aslgykhtyy legtlrgdks stlptnnnty vypsvsgslv fsefiknkkf inygkirasw
      661 akvgsdtdpy llalnyttgk ysysgytigm ianstqpnkd lkptmtgsye vglemkflng
      721 rlgldatyyn qnsknqilsl astttsgyay rlinageiqn qgieialnar alqikdfawd
      781 lgvnfskntn kvksltdgmd yfelakaywc gvsvgakvge nygairghdf lyndkgqvvv
      841 daatglpkid qkiktignst wdwtggfyst fsyknfrlsa afdvkvgadi ysmsmrsayq
      901 tgkakgtlag reewytseea rkasgmdlaa wretgnckgf vvggvidngd gtyrkndiav
      961 npedywkhva ngvqsafvyd nsyvkcreit fgytfpesil gkyakgltvs fvarnpfivw
     1021 knipnidpds syntsglgle ygslpsrksy glnvnvkf
//
LOCUS       WP_102698142            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            buccalis].
ACCESSION   WP_102698142
VERSION     WP_102698142.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella buccalis (Prevotella buccalis)
  ORGANISM  Hoylesella buccalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Hoylesella buccalis"
                     /db_xref="taxon:28127"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115920
     Region          48..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 melskqltfl ekglfsivll sglsgmanva nasttqiskt dfvqqsqktv tgivlddrgd
       61 pvigasvsvk gektgavtdi dgkftirteg navlvvsyig feqqsisvtn kntirvvlvp
      121 ntselnevvv talgikrekk algyamqevn tssltenksa svanmlqgkv agvqisqsgt
      181 glggstrivm rglnsltgnn qplwvvdgmp indgtteqan qwggsdcaga aseinpedie
      241 sisilkgana aalygsraqn gaivittkkg rqgqplsley ngnlsvsday spysyqnqyg
      301 qgsngdynts sqmswgapld grmvdnwrst iykdarydky allpqkdyit dfyrtgvsfa
      361 ntltvsagge ylsgrlsytd srsndivpny sqnrqylnmn tefrnkqltv gakvsymrel
      421 ttnrpgqgey glmvqlvkmp rgirladlrd prgtgpyinn svnwsgpsdn yanpyalssg
      481 engnkaernr iigqvtasyk ftdylhltgr agidrysdhv rnfntmpdvt stasqylnsm
      541 lvnkefnadl ilyfdrsfnd fsvnanvgta vmntknesly gssgkfaipn vcnlgngltq
      601 ttgegyskke iqsaffattv gyknmayvdi tgrndwsstl pkenrsyfyp svsssvilsq
      661 mfklprwvty wkvrgswakv gndtdpykla tyyylwttgn kldangdkan pgilkqylsk
      721 skaldnlkpe sttsaelgte ahfldnrlsi dftyyttstk nqilgvdmpg ssgyssklin
      781 agkikshgye lmvnatplkt kdwnwdinln wglnrtecvm ldseisryel gstragkvvv
      841 etgkkygnii gkaykrneag qivvndkglp esvsdkvign iqpdwtgsig nmlrykdlvl
      901 sslvdirmgg dfisstdnya cqqgtaakti ygrqqgeqii vdgvtadgkk nnvglnaety
      961 wtniagpegi meafmhkgty vkmrelslgy ilpqawfahm pikyvkvslv grdlfyfyka
     1021 apinpegafs rndyaqafel asmpptrayg ltvnvkf
//
LOCUS       WP_102705601             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Oligella
            urethralis].
ACCESSION   WP_102705601
VERSION     WP_102705601.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54277
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkeqf agetrvaatp ttvtqliklg ydvavesgag qlakfddaay teagasvvsr
       61 ddvfksdiiy kinapsdaei damdegtilv sfvqpaqnpv lveklrakki tamavdmvpr
      121 israqsmdvl ssmanisgyr avieaahhfg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igaagslgai vkafdtrlev aeqiesmgge flkldfpqea ggsgdgyakv msdefikaem
      241 alfaeqakvv diiittaaip gkpspklitk emvdsmkpgs vivdlaalgg gnceytvpge
      301 vvvtdnnvtv igytdlpnrl agqssqlyst nlvnlsklit pakdgqavld fddviirnmt
      361 vthagelmfp pppiqvsaap qqaapaaapa tkpekapkpl wqklalpvig vliylwashy
      421 apqeflnhlt vfmlscvvgy yvvwnvthal htplmsvtna isgiiivgal iqmsningfa
      481 sflafisvfl vsinifggfy vtrrmlnmfr kg
//
LOCUS       WP_102754697            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102754697
VERSION     WP_102754697.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122513
     Region          113..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtfillfcv tffsftpkht nsqntkvvid stmevtvykv fdiitkadfs ffyeedwfkd
       61 ypkvvlkkgt irvkkllntc ipteafdlki vgksifikkk tnedknsqrr ffgvvknqag
      121 qaimdatvli kgsgkgtvtn sdgrfsitea hpktvlvfss lgykteeiti gnqnsinitl
      181 eedvykletv eivghyyers qrenpgsvyk ieaktierqp vsnplaamng yipgvnivqn
      241 tglpgsgyki eirgknfina dteplyivdg vpysskslsf plvnsilpke splslinpid
      301 iesvevlkda dataiygsrg angvvliktk rgkegktrir vnvstglasv prfinllnte
      361 qylnmrleal andgytpeta pdaiqeimpd lfdwdqnryt dwqeeliggt anrnmgqisf
      421 sggneqtqfl fsgsyqnett vfpgnskygk asvqsninhq spderfqvnv ltnyvvddnr
      481 lplgeltvea ynlapnapdl yndqgnlnwn gwtlslvdnp lrllegeyra knkslllstv
      541 isynpipdle fkanlgytdy rreeykasrh tmfnpdfgft sangssivtn nasrqswnve
      601 pqvkweknwg eanfnilvgt tfqqrlthqv sitgqgfqnn nqildvfaai eiedgidqes
      661 kynyhaifgr lnfkwagkyi mnltgrrdgs srfgpgrqfg nfgavgaawi fseetfledy
      721 eflsygklrt sygvtgsdni gdygfyntyd tftlndrsyi asillpnklf nptfgweett
      781 kfevglelgf lkdrvlftta wysnrssnql igiplprttg fnsvnanfda tventgfeid
      841 frstnveknd fkwtttfnis ipknklvrfd gleqstfadq fvvgqplsiq klyhatgvdp
      901 etgvyqfedy nkdgdidpsa lsedrqwied tspefhggln nsfsyknlnl diffqfkkqr
      961 gtnvfynssy pgdffnqpes vlnrwqkngd vapvqrysvv gseaisafsn yrnssamytd
     1021 tsfirlrnvs lsytipkafi pgldaniffq gqnlltitks lkadpehsgv mtlpvlrhft
     1081 vglelsf
//
LOCUS       WP_102754939            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102754939
VERSION     WP_102754939.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124868
     Region          128..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mttrfneikl khtkyvllii tvfafcnsvi glpskyhisq ndkivikkda svsldevfei
       61 vkkqtnymfv yhhslfkdfp dinlrkgvfs lkkllshvlt gknvsvvfst nntilikeki
      121 nnlkrqqfsv sgivtdesgv pisgvtvlik vankgtitdf dgqytisvtd sanvlvfsyl
      181 gykeqeivvg nqtiinvtlk eeidqlkait inagyyntne rertgsiski dakniekqpv
      241 nnplaamqgh lpgvnitqst glpgggfrvr irgqnfidin kggsngstnd plyvvdgipy
      301 dsstlestav gdqiinsrgv splnainptd iesievlkda dataiygsrg angvilistk
      361 kgkegktqik fnvsttlgqv anfiellnte qyleirnetf vndgytletl pdlyssqvrd
      421 lnfwdqsryt dwqkvllggt ayrqnaqlsf srgnkqtqfl lsggylvett vfpgdskysk
      481 asmrvninhq sedsrfklnf sgsynadinn lptidftgna rrlapiapvl yddqgnlnwe
      541 nltfqnplal letkyransr glianttssy qpipqklefk vnlgytnynl dsykaephta
      601 lnpgiafyds rhsnivinng vreswivepq inwqydgent vlkllvgatf qhtkeqqlvl
      661 ygkgfpsndv lldisqadvr stvqdivsey kyqsffsrin inyrdkyiln ltgrrdgssr
      721 fgpgkqfgyf gaigsawlfs eetflednni lifgklrasy gitgsdnign ynffdtyeyk
      781 lngiynglsl aptrlfnpdf aweetkklev alelgffkkr illstawyrn rssnqlinmp
      841 lpaitgfvgv nsnfdaiven tgieidlnti niqndhftws ttfnisanrn klvsfpglkg
      901 stfqsrlvig qplivsqlyh figvnqetgm aqfedynndg fldfndrrrf edltpkyfgg
      961 lgntfqyknl qlemffqftk qkafsylsrv typgrsvsnl pvsvlnrwqq vgdispiqry
     1021 sitdnnvfda wddykrsdaa ivdasfirlr nvslsyiipk tvtkevdlsi ylqgqnlftf
     1081 tsydgadpdv qvsnkfptlr qftlglslsf
//
LOCUS       WP_102755763            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102755763
VERSION     WP_102755763.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122996
     Region          127..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiklireqa fvrkhllfiv mrvfifllct tvfgfstent fsqeriiida dkevsvnevf
       61 riiknqtkyr flypeglfde tkrihlkkge illtkllkqs fsgsnvkfel sknhtivike
      121 krlqqlikgk vndddglpls gvsilikgtt tgaatdfdgn yqisadtgdv lefsflgytt
      181 qeiivteasq tidvtlkviv gkldeiivta qgirkekkal gyavttlegt evenkaesdv
      241 srslqgkvag vqifvesgst gdqanirvrg nlsitgnnep llvvdnvpfs gnlidinpnn
      301 iknisvlkgl nasilygseg rngvilittk sgsssigekk isinfsqtvy tnevaslpdy
      361 qntygqgrdn afsggdivsw gaafseldfi phpyannpsf pefagveipy eatpnnvkdf
      421 fdtgigkita lnfnssqekt afnlsagytd etgiigkndl krfnlaiggs aqitdklnis
      481 atfnyttrkr nsqsgltlfs tllylprnld lfnlpyqdpi tganvyfnse ehplwtinnt
      541 gsnddvtrlf ttintkydin nhwslnyrig idnngsdgfd frnkggdiar tgflslsynk
      601 seiidqslil ntnyklsdki gfdsqlglns kttnvksnss rsgdqvvfgf frpnnfdtqt
      661 anatrarenl lgvfaalefn ydrylflsls grndwsstle kenqsifypg asvsflptsa
      721 fnfdsktvny lkvraayats agfpsrfntr qtlesdsnrf vtedgsiras tvprdlanpn
      781 lkaelhkefe vgiesklfnn rvsldasvfk rvskdqivnr rldtstgfga tsinigrvdt
      841 dgvelnlgvd ifksenfnwn ltnvftayes tvvelssgpf algrsrfaie geafgviqtn
      901 yaakdsegnf lidpnngeil ssnqvglpdk ivgdptpdwr latinsfsyr nftlstqfey
      961 thggdnlsdt fselvengvl rgsenrdgsf iipgvygdrs tglpfldang qpipntiqqn
     1021 gnrtasgnyy dardnyvfda svfrireval syningrknn lpfdnlaitl sgrnlffiap
     1081 nypkyanldp evdkastvvp stkryaigin vsf
//
LOCUS       WP_102755771            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102755771
VERSION     WP_102755771.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122428
     Region          127..1111
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikltkars lvrkrllfii mrtlifllct tvfsfttkts fsqekvtidt dkevpvdevf
       61 niirdqtkyr flypqdlfan apkvqlkkgv iqmsklleqc fsgsnvkfel skdhtivike
      121 kppqqlikge vndggaglpl pgvsilikgt tvgtftdfdg kyqiranqgd vlvfsflgft
      181 tqeitvtdis qainvnlkat igvldevivt aqgikkdkka lgyavttlag rdvenkaesd
      241 vsrsligkva gvqinvgsga tgseaeirir dnlsinngns plivvdnvpf ngglidinpn
      301 niktvsvlkg lnasilygsd grngvilitt ksgsasigee kvsinfsqtm ytnqvanlpd
      361 yqnkfgqgnd nayddtslns wgpafseldl vphplsnnqs fpefadvqip yqavpnnvkd
      421 ffdtgigtvt alnisssqek tafnlslgyt detgiignnd lkrfnlglgg svqitdkwnv
      481 satfnytare rnfngglfdv llflprsldl rslpfedpgt genvyyrdea nplwtidnvn
      541 nndrvvrlfs tlntkyefnn nwsvnyrigi dadvsdsfdt tnrgafgnne sgrlslsydr
      601 deiidqslil ntkyqltnkl gldgklglns rtinvlsnss dfqdqdlldf frpdnfntqt
      661 gdasrarenl lgafaqldfn ydrflflsls grndwsstie kenqsifypg vsvsflptsa
      721 fnfdskvvny lklraayats sgfpgrfrtr atfrsepfef itangairsn sasstlpnsn
      781 lkpelhrefe igiesklfnn rvtlqasayk rsskdqivtk ridasvgfsq tvtnigrvdg
      841 egleielgvd iinndrfkwn manvftaytt evvelnapin lgnggraieg qpfgvfegty
      901 avrdnqgnfl inpnngeliv sstagldnev igdptpdwrl tninsfsykn ftltaqleyt
      961 qggdqfsgta idllsagvtk dtenrdgtft ipgvygdigt gqplldtngq tipnnvqlna
     1021 srlasgnyye addrkifdst lfrireials ynldgakynl pfdnlaitls grnvfykapn
     1081 ypkytnidpd vggrttstps tkryalgvsv sf
//
LOCUS       WP_102756613            1191 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102756613
VERSION     WP_102756613.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1191)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1191)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1191)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1191
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1191
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134175
     Region          128..1188
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meikltnllf yfrkkflihl mrafiffict tafslapnnv fsqrvkinid adktvtvdei
       61 fkiikaqtdy rfiyqedmfk gfpsvnlkrg tirankllqe ilpkgnfkfn isgkntivik
      121 rkpaivqqki qgkvtdenge pligvvvivk gtlrgattsf dgiykidaqe getlvlsylg
      181 yldseviigq gttynvqmap ssfeldtvei vstgyqtisk erstgsferv nektldlkin
      241 qnifskiege vagvttdtdg nfiirglsti sansdplivv dgfpieqnqn tinpndvesi
      301 tilkdaaaas iwgiraangv ivivtkkgnr ngkltinasv ntsitpepdl faapiadaat
      361 qvayqrevfe rggfhdqtnl fngnlnvasg qvlnpvvqtl llqdrgdiss eeaqsrleql
      421 entdirreys rliqrpeiwt qynfsinggs ekydfrssis yndnqkelin tkanqylinf
      481 ansfnisskl kvsgsinfsq skesfgstsv nddfgrfsgs dsfetprass aqnllstsin
      541 srilddngny lpmqnflaln qeasnlaler gfpydwtynl kqeldnadni lretalrlnt
      601 glnyniidgl dasvtyqyew qqqnirdfhn eqsfytrfrv nlftqldpst qlpvsnaipv
      661 gaildidtrn qrahtfrtql nfdklfnekh qvtaiagyev rktiaerats rqygydersl
      721 daklvdfttd fteslplrfa slipdfnenv fvenrfisyf anasytfdnk ytisgstrld
      781 dtnlfgasde yrniplysvg akwnianeff tgnqninrlq lratygingn vdrstspqll
      841 itpknisfpf vngtnaditg lpnpelrler tnalnlgldf glfgnlisgs veyykkdsed
      901 llaftsvnpi sgvngarinn gtlrnegfdi nltlrplrgd nfrytttgnf svntntlikv
      961 dvqsnaqifd yvngnlaipd lplrtiysyn yqgldrngap qflnennriv dfranifepd
     1021 alveegsllp kyygswvnnl eyknfylrtl ttfkaghvfr yrnasfipan rvsplenvpa
     1081 dyvnrwqnpg denntdipai pafqdrgilg yayyrdsnkf vddashirls qlsfgyvfpt
     1141 ktlerlgmns lqigfqadnm vvwnfnkwdv dpesafiprq atytlnisas f
//
LOCUS       WP_102756738            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102756738
VERSION     WP_102756738.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112118
     Region          25..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mckkllnfla fvfllsssvi qaqsirvsgt vtdgngiplp gvnvlekgtn ngtsadfdgg
       61 ysisvngsav lvfssigfvt qevtvgaqtv invslvesvq aldeivvtal gikrekkalg
      121 ysmqevsset vtaaangnin talqgkvagv nittsggigg narvdlrgts slngndeilw
      181 vidgvpfsad dtsdpddlfg gisnggglld inpddietvs vlkggqaaal ygsrgangvv
      241 littksgkkt eglgisytgs tvfseasyfl dlqneygqgl ngnydptsga awgprfdgvs
      301 rpswtgeqlp yeaasdqldd ftrtaismrh alslskasee gnfrvsiakd ktegvfennq
      361 idklnfdvka aydinswlnv dtkisyiknk gqqrpevgny syvsffnrmp anirtqdlsp
      421 gfvivngera eylygsstdl tanpnannrn pyfiqdqifn sdtrnrffgy fastfkftdd
      481 lklklkygld tyryealdgy rypdnasdqr pnfntsekfy seenmeflls ynkdlsekin
      541 fglsvggnkm hresqllrst sgklassndf flnagttlnt nesfsqreiq svygyldvsy
      601 ndylfltata rndwssalpi dnnsyfypsv glsalisema tmpdwisylk lrgswaqvgk
      661 dtqpylanpv fsfstwnfnl ltsgvpqglv dpnlkpeist tsevglelkl fksrfgidit
      721 yynertknqi vntangqssg ydlfltnlgl isnkgleiia nivpvktedf nmgltlnfak
      781 nkgvleefdk sldgedlpyf ffnsntipeq vraevgrkmg diygfaferd aegqfvigad
      841 glptrsadvv klgniqpdft gsigidlnyk nvslnallgm qqggdiyslt eagatgsgta
      901 arttslgrep ffvpgnlsdg spnltivspq qywsrvagvt essiydasfm kltelalgys
      961 iprkvldklg ngvinrakfs lvgrnlfyly rntpgtvpds gvyntsfgaq afdfspvpvt
     1021 rsvgfslnln f
//
LOCUS       WP_102756990            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102756990
VERSION     WP_102756990.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113258
     Region          25..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsvmlt lflalavqla faqektisgv isdesglplp gasvlvkgtk tgtssnfdgr
       61 ysirasqgqs lvfsfvgyst keiiigasnt iditliedae slqevivtgt akgrsikels
      121 falgqvnnel ldnvpatsag qalqgkisgl nispsggqpg sdvsiqlrta nsiatgqnpl
      181 iildgvileg gladintedi drievakgaa gaslygsraa ngviqifskr gkysdkvnvt
      241 yrselgwrnv nseydlatth kflmlpdgsn fdlstgsrql dpdgfadnpy pagstlydnq
      301 drvfqtghfn shfasinggg etarylfsys rlddegiike vdnyrrdnfr lnldsklsek
      361 lnvktslfyg nssrdagins gstlnalfat lmtepihdml apneedgspy nydfdtidgn
      421 nrnplyslan ndreerrnrv lgnvaldyev mpwltlngsy sydyenntfe nyipkgylsd
      481 spdgqaqnig fiqrsnfngr aqnirfnalf skafgeddaf nlnlrlsyln erynstfnns
      541 egynlavsdi rsldnikdrp alasesqtii sdsyfaiadi dykkkyifsg vvrregsslf
      601 gpdtrwanyf raslayrlte dfeipgvqel klrasygtag irptyemrfe tftlrngaat
      661 kstignnelk paktgemelg inidfldrfn fefnyvkait ddqilnvpls aatgfgsqwr
      721 nageiegttl easlnydiir nndfswnlgi vwdkskqeit rldvpsyltg pgtqnttffr
      781 veegqnfgim ygsdfirsls dlpagldpnd yqvnaegyvv daatgstpva rvddegnaff
      841 vigditpdfr mginttlkyk nlslytlfdw kqggdiynrt nqwlyrdtrh avsansqvpa
      901 afyaglyntg npssgfiedg sfvklrelsl yytldgekmg nignfiermr igfigrnlit
      961 wtdytgfdpe itnqaeagrs dltsrdtngl gndantpggd pnvfkvdnfp ypttrsysfs
     1021 iqlnf
//
LOCUS       WP_102756992            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102756992
VERSION     WP_102756992.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121294
     Region          25..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkfsvrlt lflvlavqlv faqkrtvsgk vsdesglplp gasilekgtt ngtstnfdgk
       61 ysinvdqgai lvfsfvgyts qeitvsssnt vnvvlqedss vldevvital gisrdkkslg
      121 yatqevkgeq lttikngnfa naisgkasgi kitrtnnlgg stnvlirgnt sltgnnqalf
      181 vidgipisnr ntntrsqeqa gggsydygna asdinpddie svnvlkgaaa salygsraan
      241 gvimittkkg rkskgygvsi ssgvafgsid kstfvkyqkd ygggygpyyg dceclywnnn
      301 ididgdglld isvpfsedas ygarfdpnll ifqwdaldpd npnyrkatpw inakngpitf
      361 fetpvtltns vsldgageeg sfrinytnfd qkglmpnssl krhnftmsgs hnfnkklhat
      421 gyasyiktng lgrnstgynd nilggfrqww qtnvdvqqqk diyfatkrnv twnpksasnl
      481 tpiywdnpyw tryenyqtde rnrfignasl tydlkdwlti tgriatdtyn elqeerrqig
      541 svptafgigi grdgsiqrnt vesgylrrdi tatetnydlm fnidkdlndn lnlkallgin
      601 inrrefsrlt satqgglgvp glytlknskg plalpvetvw kngtdgiyas aslgyqdtyy
      661 idatirrdhv stlpkdnssf yypgisgsfi fsklidvdwl tfgkfntnya evgngasgpn
      721 qlvdyydvni pigspstsin ntknnpnlkp ertksyefgf eldffqnrlg idatyyhsks
      781 idqiagvrvs eatgflykki nageienkgi emtlsgtpik ndnftwnvnv nwtrnrnkvl
      841 slaeglqtlq lgsfqggiti naevgkpygv iygsdytyln pdnpkaserl idpvsgqylk
      901 tstsdhvigd snpdwqmgis nnfiyknlsl sflidiqkgg siwsldqyyg latglpaets
      961 findlgnpvr npitgtpeny gadsggfinq gvnpdgsvnq trirtdrfga wgyrrglpdr
     1021 afsydagyvk lrevaltynv penlvkdwfi tgasfslvgs nlwiidkdlp hadpesglga
     1081 gnlqgyttgs lpttrdigin iklqf
//
LOCUS       WP_102757205            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102757205
VERSION     WP_102757205.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116734
     Region          26..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdkhkllliw amlvcitgyt qevflgkvmd ennvplpgat ivlkgssqga stdfdgnfki
       61 dvpslnetli isyvgyttle faingqsrad iilqpdseql nevvvtalgi krekkslgya
      121 sqelnsdevd agkennllnn lsgkvaglqi tsspsglggs arvsirgeas lningnsplf
      181 vvdgtpisne ivgstgtgtq dvdygngaae inpesiesin vlkgpaaaal ygaraangai
      241 iittkkgsgn grlsvsinss vgienilmlp dwqneygqgn nkqfefvdgs gsgiadgvde
      301 swgprldtgl lipqfdspra dgtrggdylv sdapitatpw vsnpnntkdf frtgtilrns
      361 ismsksgdfg nyrisyqnlq qegtvpntdl krnslnfnsa fnlndkitln tninyvktds
      421 dnrpslsygt esimylfiwy grqvnthnlr dywmpgrenl qqfnynynyh dnpyfnvyen
      481 tnsqdkdriy gnvslsykln dhwnvmvrtg rdfyrdlrak krafstqrfp lgfyrednvf
      541 feesnsdfli tynnkfndiw gvtvsaggnq frqkqdftqt vapqlinpgv ysfnntrrpl
      601 evttndkekr inslygfaqf syddklfldi tgrndwsstl ptdnnsyfyp satvsaiase
      661 vfempdfvtf aklrlayaev gndtdpyklt sffvnespfg dnpaltessl ipnanlkper
      721 tasyefgldl rlfksklnld vtyysgatkn qiipistdvs sgytsklina gevknygfea
      781 itnitpirtd dfswrtsfnf stnkskvtdl ggvnytltdr ngafiqareg gsisaiygrg
      841 fqrvddpgsa nhgkiiynaq gipqrtddlv yqgdyapdyt lgfqnmfkyk nfdlsflidt
      901 rqggivvsrt ktigstsgql ketligreng ivgdgvvevs pgvyqpnttn idartynnqy
      961 ykrdnveaak ydasytklre vtlgytfskn lveklkltna rfsltgrnll lwtdnphfdp
     1021 etvavsggtl qpgienmayp ssrsftfnlk ldf
//
LOCUS       WP_102757235            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102757235
VERSION     WP_102757235.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119538
     Region          34..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnfnlqfhwr nkigffamlc lmsismsnaq sqaitglvts egqplpgvsi iikgtsqgtv
       61 sdfdggyslr asansvlvfs yigyvtkevt vganttvnvs ldediaklde vvvigygkqk
      121 rlevsgsvvs vkgedvqkft snnfqdalqg rvagvsvmaa ggepggeaii qirgtntlss
      181 rrrgnsgepd pnlnllnpte nglaplyivd gvqletnpnl ssndieniei lkdaattsiy
      241 gtrgaagvii ittkkgevgk akidfnltta vkkvtsaint antadaflid rtvhdnnspn
      301 lryfsildrn kdaldydtdw qdfvindfaq slnanlrvsg gnkdinynvt ldnyqedgvy
      361 kksnlnrtnl rtnatlkkgk fslnvgtnis agkrrlapwg llydairlap fnrpfdigsg
      421 sintpegavq pdggvftstn nvvgdlarkf sadnqrkefn lganvtleyk lfeslrartt
      481 lsgfrantes ffytprqeir sqetgeltqd prpadltnyn ttyqvfnrdf ildydqyfgn
      541 hrialllgae srellweefr isgntfvspe qrtitsaeni srrestknps stnsyfsrlk
      601 yeyggkyfll anvrrngtsk finnkigyfg gvsgawivsk egffknanfl savsnlklra
      661 swgtvgndri pdfnfqsrll snanpvfggg pqfgaarldl gnsnlkwett esinygvdlg
      721 lfkgaltita dyytakkkdl lfqlptvpsa gvqerpigln iasltnegle lslgyrnnsk
      781 avkwsvaaty tkntntvdkl tgtstdviqg gfplrannnv iqtpvtfirp gysagaffli
      841 ptdgviknqe eldaydalvs erlgrgnqig dlrykdkite dllmpqldan gnpeidadgn
      901 vimvagqdgi ldsgdgiind ddrifmgnnl pdfeagfnln lnyknldftm qwfgmfghkv
      961 fngpknltya hgthkdiayq hsalnpnssi parrqngtqd pnyssasdlf ledgdfvrlr
     1021 niqlgyslpl dkmkdiglqk irifisaqnl ltitdysgyd peiggdglat rgvdtglqpv
     1081 taqgiiglqi gf
//
LOCUS       WP_102757262            1122 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102757262
VERSION     WP_102757262.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1122
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124052
     Region          136..1121
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkntigwvl aldplkislk mkltyfllfv sllqsyansy sqntkvtldm revtlrsvln
       61 eiehktdykf lyekgifqtd kivsisvkrk klssilnrll epfdvsveyl dkqiiikrkp
      121 dpvevekavi keslqqqikg qvkdgfglpl pgvsilikdt ttgtstdfdg nyeiranpgd
      181 vlvfsflgyt tqevvvaqsl vidvqlkesv gvleevivta qgirkekkal gyavstlegk
      241 qlenkaetdv arslqgkvag vqinvnsgst gnqasirvrg dlsvtngnsp livvdgapfn
      301 gglidinpnd ikdfsvlkgl nasllygsdg rngvilittk sgsgspgkek vsinfshtvy
      361 tnqvanlpey qnkygqgsdn rfrggvvgnw gaafseldvv phpyasnpaf pefanvevpy
      421 kpipnnvksf fntgigtvta infnssqekt sfnlsagytd etgiignndl krfnfniggs
      481 aqvtdklnvr atinystrkr nsqngadmfe illhiprnid afnlpfqdpv tganvyyrps
      541 enpnwvinnt grnddvvrif gtfranynfd dhwnlsyrvs ldnevqdefd fanrggvddp
      601 tgfleldydk fqtidqslil stsyqlnkki gldgqigvns qtinnksnsa sfedqvvfgf
      661 lrpdnfdtqs gdasrskenf agvfgqlefn ydkflyvtvs grndwsstle kenqslfypg
      721 vsvsflptsa ldfnsnivny lkirgayats sgfpgrfrtr ntlvsdpqrf itsegalrss
      781 rvsrvlanpd lraelhkeve vgvesklfnn rvsleasvfk riskdqivsr pldpalgfts
      841 ttvnigrvds egleidlgid ilksdsfiwn ltnvftaynt evvelnapis ldndrfaiqg
      901 qplgviqedy airdsegnll inpnngeliv sddigfpdki igdptpdwal ttinslsykg
      961 ftfsaqieyt hggdniseta ydllrrgvtr dtenregsfi ipgvlgdpst glpfldangq
     1021 tipntiqana nrtafsnyle andfrlfdts lfrirevals ytldgkknkl pfdniaftls
     1081 grnvffnapn ypkytnidpd vdrgsttipt tkryafgvsi sf
//
LOCUS       WP_102757326            1173 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102757326
VERSION     WP_102757326.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1173
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131334
     Region          134..1172
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meiklthpll itkralilim mrtfiflfct slfsltpnhv lsqkaritie sdmkvsvdev
       61 fdmittqtky afiyhenlfk dfpkvelkkg iislnrlfnk slpkkqdlni ivtkdntili
      121 rernknnnrl qtiitgtvtd agglpiagvt vlvkgtitgt atdfdggysi kvsstenvlv
      181 fsslgfktqe itvgnqstin vvlneqadvl devklvstgy qkisreratg sfekvseeil
      241 evktaqnils klegevtgvl fdndgnitvr gestinavne plivvdgfpi qqslstinpn
      301 dvqsitvlkd aaaasiwgir aangvivivt rkggrnqkia vdytsnfsit qkrdlndlpi
      361 tptnsllefe khradnawll atssfnsspv geayktflal dsgaltqgea daiisglrgi
      421 dvrnefanlf isnetwmqhn lsitgggenn sfrasityne nknlesstgn nrgdvianls
      481 nnitllpkls ldaninyvnt vsksngirwg evislpqyqr ivdangnyvt qprtidqslk
      541 dgfasdgypy swdynlkqel dnknnrtvnt qlrlqtslky ditdnlnvqg lyqyeygfsk
      601 tenlfnedty rvrdlvnrft tlngtsgale saipkgeild lgdsntesht grfqlnydqs
      661 fndglhqina iagyeirktl fksyqstlyg fdsrslahan lnykdefsts psggnsridd
      721 gvniendenr fisyyvnaay tydnkytitg strlddtnlf gadeeyknip lysfgvkwni
      781 snenffkskv vnnltlritn gsngnvdnst spfvllkldn nfnsdipfag insvknpelr
      841 lervfvnnig ldfglwnnrl sgsieyyerk sqdllsqvsf psilgfnsal inagemenkg
      901 feiglnalav ngksfkynts infsynknev tkvevpeetv vrflffsdpi lnkplrylys
      961 yryngldsng dpqflnenne vvnvegqlan gdnasinnve glvfegtttp kyygawvnrf
     1021 syknffiral ttfkfghvfr ntdnfldysd trlpfltnvh adfdnrwrnp gdenstnipr
     1081 lpdapgdldr egyryyrsgd hlvddashir lrevvlgynl sskvanklgl nslslsvqgn
     1141 nlalinfnkw nvdpenqlfg lrktftlsvn anf
//
LOCUS       WP_102757355             932 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102757355
VERSION     WP_102757355.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..932
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103843
     Region          14..931
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyyisllfv ativgfasaq qkndtikiqi edkitvafge ikkdklvgav dviegedllh
       61 ssdynvesil agqapglivf egsgspgldn twmrirglsr ggaedhplvv idgianrtls
      121 siaidevesi qilkdatakl lygskaangv imlttkrgyn gkrkvtffhe ygiktptrlp
      181 eylnsaqyar qynqarindg lspiytaddi nnysnnpsvl ypdvdfydel vkkstsfqrf
      241 naqliggset tkfflnlgyv genglenqgk tqefsrlnir gnldydvnet vsmfldiagr
      301 mdiwdradit nsdffgalss hrpndyplwa gdvgdtdnlg fsprvetnll gelsrsgyvn
      361 tknyyaqtnl gmnfdlskla kgltatgyvt fdvfnnvaig ksldysrirf ddpndlslit
      421 rigtdkyddn esrkgdnstq nlglvakidy skawgnhdlq idlvgvnqtl trkstldgpt
      481 tqqddksinf garvnytlkn kytiegsssy mgsdkftken rwglfgaggf awiisnedfl
      541 kgnktinylk lkgsygvmgy drqgafdyll yrdfyegwgn frtgpqnstv efgwragqig
      601 npdftfeksk eynigietsm fnnkvdlein yfnqlrsdmp vrlnnalpdf lgelkpignf
      661 nevsnsgvdl slsytdkigd lnfsvvtnvi yskavndvfd eineydhqnr tgrasdaiwg
      721 wladglyqnd aditnhgvis tygdiipgdv kllditnnkg dntidqfdtq vignwfprvn
      781 yalninleyh glefyalgqg tsgsdkilnn syywnvgenk ysvqalgaav pgsvagassp
      841 rltslsqshs yrnstywlvs gnffklrtae laynfseris gkfgadklrl fargndlfai
      901 skikkldpes lnsgvtdypm frtislglrl ty
//
LOCUS       WP_102757894            1203 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavivirga
            eckloniae].
ACCESSION   WP_102757894
VERSION     WP_102757894.1
KEYWORDS    RefSeq.
SOURCE      Flavivirga eckloniae
  ORGANISM  Flavivirga eckloniae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavivirga.
REFERENCE   1  (residues 1 to 1203)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1203)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Flavivirga eckloniae"
                     /db_xref="taxon:1803846"
     Protein         1..1203
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134309
     Region          134..1202
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meikltnvlf fslttgirkk lliiimrtfi flfcatvfgf spnnvlsqna kikidadktl
       61 svdevftlit dqtdyafiyq adlfkdspki vlkkgvikan ellkqslssg rfdfsftnan
      121 tivikktpit lqqitvsgkv inengaplag igvvvvvidp nnrnsdylir gtstdfdggf
      181 kiiaesgnnl vvsgigyety eekvvsnktt ynitliekan eldevvivhd gfqsksiekt
      241 tgaynhiktk eierqigssl tdalegltag ltintfgngl egdnniprff vrgvgtfgnt
      301 qplivldgfp idaerlelis nqdiesvtll kdaaaasiwg aggangvlvi tskkgkkgkt
      361 sfslrntitv qqrpdlsyln lvssqdaini erdifnrdpg glpvrsdfen nntpyspvyd
      421 alfsfnegti nqtqldsrla dlasynnske iensflnapi tnitnfsfsg atdklnyyga
      481 fnhikeeiaf vgdknktini nlktdyqvnd ktnikiatny vigkykesav pelrgrfriv
      541 pqvfnilpyq rlrdengnpl aisgnypnst idkiiglggk dltyrplddl ndydfknken
      601 ttrinatirr difnglsael sylyqktnnl eerlftdrsy ftrnflveta avetdittge
      661 ildytqalpd gsikrnvdnq sttnsfraql nfnksftngk hkvdailgte rrkmerqrnt
      721 yslfgfnegn lssipadlti vqnpnvflni spnlnqynsa fkqderlssy yfngsylfns
      781 kygftasgri drssqfslsk qflgsaglkw nidreaffnv kwinnldirg twgilgnapl
      841 igestlvntg rtgnhfltnd vfisitnpan kkltfevtet knlgldfvvf nnrisgsidy
      901 ynkvssdiis tnitdptsgf fnvseniadi tnkglelrln tvnvklkdfk wstdinlsyn
      961 kndvdhsnvn vnnvfgnnav nlegypaysi fgfrfaglnd aglaqafrtn engeqvtttn
     1021 rgdlvfedle hvgtaipktt igfgnnityk gfdlyfrfiy ngghilklee vggfnlnstg
     1081 elsntfnnse lnywqnpgde entsvpalgt difnytlrsr asdlgfapad ylklrqvils
     1141 ytldkkwlqk tpissvklhf qarnlwywak nnhnidpeay lpqtgqrtlp vepsysfgat
     1201 inf
//
LOCUS       WP_102792074             405 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Alcanivorax sp. MD8A].
ACCESSION   WP_102792074
VERSION     WP_102792074.1
KEYWORDS    RefSeq.
SOURCE      Alcanivorax sp. MD8A
  ORGANISM  Alcanivorax sp. MD8A
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Alcanivoracaceae; Alcanivorax.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Alcanivorax sp. MD8A"
                     /db_xref="taxon:1177157"
     Protein         1..405
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42575
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigvpkeic pgeqrvaitp anvsallkkq gveiiierga gdlagypdsa feaagaklvd
       61 rdevfsasqv vlqvqtpgsn tengtedlnk lkegqtligm tdplanpkfa qslaekkisg
      121 lalelvprit raqamdvlss mamvagykcv llaatesqrm fpmnmtaagt lnasrvfvmg
      181 agvaglqaca takrlgaive aydvrpaare qilsvgakpv eldldtgeae gtggyakaqg
      241 edflkrqrel mtevvkemdv vittaavpga kspilvtedm vkamkpgaii vdlaaerggn
      301 cevtesgktv vkhgvtivgp envpssvafh asqmfgknme nllnlllddn gdlqldfede
      361 ivvetvishd gdvpqarlrd llglpalakp eapaeeaaad skeek
//
LOCUS       WP_102768545             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Kinneretia
            aquatilis].
ACCESSION   WP_102768545
VERSION     WP_102768545.1
KEYWORDS    RefSeq.
SOURCE      Kinneretia aquatilis
  ORGANISM  Kinneretia aquatilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Kinneretia aquatilis"
                     /db_xref="taxon:2070761"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38966
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvprera agetrvaatp etvkklkaqg hsvqvereag laasitdeay laagadiveh
       61 aaalgadlvl kvrrpeaeel almksgatlv gmldpfdrag lqalaaaglt sfaleaaprt
      121 sraqsmdvls sqaniagyka vmmaaeryqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpavk eqveslgakf idvpyetqee reaaegvggy arpmppswld
      241 rqraevakrv aqadvvista lipgraapql isedmvrsmk pgsvivdlaa grgadgvggn
      301 cplteagrtv vkhgvtlvge tnlpalvaad asalyarnvl dflklvlakd gtlsvplddd
      361 ivaaclvsqg gevkrs
//
LOCUS       WP_102784778             387 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Thalassospira].
ACCESSION   WP_102784778
VERSION     WP_102784778.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40467
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,98,295,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,285..286,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpkeiw pgekrvavtp etvkklkslg fdvaieagag idaaipddrf vdagatiakt
       61 mkttvkdadv ifkvrppvid gktneltayk kgaavvalle pfdrkellda makagvdgys
      121 melmprisra qsmdvlssqs nlagyravle aahqfgriyp mmmtaagtla parvlvvgag
      181 vaglqaiata krlgavvsaf dvrpavkeqv qslggtfiev eddeadaaet sggyakemsd
      241 dykkkqadkl kevlaktdiv ittalipgrp apeivtadmv agmkpgsvii dlaaerggnv
      301 agvklgqtit tangvkligs enitsavatd atamyaknll nfitlsvdte kgalvfnged
      361 qiiaetrlth dgkivhpkfg geavang
//
LOCUS       WP_102774725             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter pulmonis].
ACCESSION   WP_102774725
VERSION     WP_102774725.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter pulmonis
  ORGANISM  Achromobacter pulmonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter pulmonis"
                     /db_xref="taxon:1389932"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38580
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkyvggk htvvvergag saarypdday eaagatlgta
       61 qdalgaglvm kvrapdaael ahmkagtvvv gmldpfdaeg lqrmaaaglv gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaarvvvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgrggy arpmppawma
      241 rqavlvaerc kqadivitta lipgrpaptl vsaetiaamk pgsvlvdlav erggncplse
      301 kgqivekhgv tligltnlpg lvatdasaly arnildflkl itdaegalai rrddeivaac
      361 lvceggnvtr rt
//
LOCUS       WP_102793205            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102793205
VERSION     WP_102793205.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113333
     Region          43..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfgnrklila affflgmkat lkaqesvhdi ivrdkstqqp lsnvsikntt tgkeivtdgn
       61 gkvaievnev sqtyaisleg yiaqdialsv gklpdsvyll petkqlegvv ltgytrqska
      121 kttgavssik aeaiaktpva sldqalqgqi pglyvaspsg qpgamgrvti rgigsvqddk
      181 tnplyildgm pispeifavl npldyenivv lkdasataqy gsrgangviq itskkgkdnd
      241 kghsqffyqn qfgissvnnq kwdmmnssqr lefeeilqdp nfpgwvysrk npykivngqk
      301 iaktdadyte gdqkladlra tntnwrklll rngvtnshyl smgggnqktn hysslsyfkq
      361 egvlpnsgve rfninsgvnh ksgrftssfn lnltggqtql sesdfdvset npvaslyfam
      421 pyekpydkdg nltpgvnrfg analtmyqdi srkekqlqgv lssnlsfeit knlkltstlg
      481 vnhqqtrftr iikpdtyfgs mvdpgeqgly erintqktsy manfgfnykk rwgsneveai
      541 vlaefnkyst nydgftgygl ipglentsgg itpgtpdnnf ipkisggase nilvsqlgml
      601 rysyanrftl sgsirrdgss rvptdnryky fyafgatwni kneeflknwg alstlrlrls
      661 hgltgnaggf asdfgyrqly kpqhyngyta fipispgnpn ynwemnkisd vglefglfkn
      721 riigevdlyn rvtsdlfinr slsmtsgfes iadnmgkirn rglefrlsgd lfrndnfswn
      781 lglnlaynqn rilslgsene ivtenysihk vgsalghfym vrwagvdpat gaplyydkng
      841 avtkeynpen avmvkgaydp pikggittsf tyknlqvnal ftfvkgmyrl ntaelyrtsa
      901 dpnyriynqs tdmlnmwqkp gdisqnpgaq yarymtdrel qsadyiklrn vsinyklkdl
      961 gslnkvfkei nifaqgqnll twtkwkgqdp eddnnwyqye yplprtitlg fnvlf
//
LOCUS       WP_102793259             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102793259
VERSION     WP_102793259.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108812
     Region          31..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltnsvlv vvlsssfvfv naqkkqdsak tkdiegvvvt algikrekks lgyasqevka
       61 dklfdgttnt gniasqlsgk vsglqvntss nfggssslvi rgikslqgan plividgspv
      121 nnsstydtkt nqdmgnllsd inqddiesin vlkgaaasal ygerglngvi vittksgkgk
      181 ddgswgitls ssvqagfidk stfpeyqnry gagyamsfse knangtpygn lgddaswgpe
      241 fnpnqlvyqw dafdpnsknf gkatpwvaak ngpikffetp ityvngitle kgkkgnnfml
      301 sydnmlsngl mpnsdlrknt fttkinydft pklhatvyst lvvqstkgrn danysgnlvg
      361 gfrqwwannv divdqknayf nsggkniswn lksganpvvg fwnnpyyqry qsygtddrtr
      421 sfsyalltyd fnknfsltgk vsydnastyf qnrlapgsvp kafgasqklv ssgysrqnlt
      481 ttetnfdlml nykfnitdni nvsgiaggnv rrnyynsiya stegglekdg lyalanskfp
      541 iippdeneyt tvtssayata sfdfykffyl datfradkts tlpkanrvyt ypsftgsfil
      601 sefvkpswls fwkvranyae vggtadpyql qyyytfagtf nnsivmqnsq tllpnpelkp
      661 qrskefevgt eahffkgrlt fdaayyktkt fnqiinlpis agsglltava nagridnegi
      721 elqigatpik tkdfswnvdv nwsknknkvv ellhnattdv snynltsvqg gasvnatege
      781 mwgairgsdy kylngqkvvd skgfyvlegn kvignttpdw iggvrnsfsy kgisfsflvd
      841 frkggdifst dmyyatstgl ykdtaigdyr tgkvvlpgvt adgqlnqtai dasvygnmgy
      901 qksptsryiy dgsfiklrea sisytlpkal lantfvneak isivgrnlwi ihknlpyadp
      961 estlgggvrs fgysigslpt trdigvnisf kf
//
LOCUS       WP_102793430             928 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102793430
VERSION     WP_102793430.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 928)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..928
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103186
     Region          28..927
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvnyqvfta slffmgvcvy sqkkdtllke nkidevivvg ygkstksrmt dnvakisaes
       61 ikeipnanfq nalvgkaagv qinqtngkle agfninirgs asisagtgpl yvidgiplin
      121 rdestnsapv nplvtlsase iesveilkda ssaaiygsrg sngvvlittk tgkkgkpkls
      181 fnisqgfsnp thkvrflnak eyvellleag rnvndedfvi rrfnrysnnt dwrngaidtd
      241 wqkyifrqga vrdadfsvsg gddnynymft asnndskgii rgndlgrnta rlnvsakvtd
      301 klklgmnlgf srtsidrvan dnafvtpmqa vaqapispaf idgepftgtt yanflledky
      361 anyntlikrl tgklsaeyki lknltfnsdl gydyynqkek nyrgrntpqm atdgyaynsw
      421 vdtenlvftn ylsynlrfgs nnisavagte ynknrrefgs vtgirfpsdd fqninsagei
      481 iegrgeasey tffsyfarvn ydykgkyllk gsirrdgssr fgqenrygvf pafsagwvis
      541 kesflsesnt isllklrasw gktgnaeigd faardqwqat kykqlpgiep iqpanpdltw
      601 ekstqtdisl dfglfsnris geidlynkkt ngllfqqnip ytsgyssiyr nigdmsnkgf
      661 evvlntqnfr rddftwntsf niarnnnkit alpdnnadqi igntilrvge rsasfyltey
      721 agvdpangda lyykntlksd gtldktttnq yseanrivag sftplwiggl tntleyknfd
      781 fsftlygefg asiynsggkf mstagswfdn qtadqmnrwq kpgditnvpq arlgeengtq
      841 estrylekrg fvrlrnfslg ytlnkdlmks lgvnklriyi sainlltftk ysgydpeala
      901 dtgrggggat fysappartf tfglnvnf
//
LOCUS       WP_102793632             969 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102793632
VERSION     WP_102793632.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 969)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 969)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 969)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..969
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..969
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106572
     Region          33..968
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvkfkvlsa gvlffigqsv laqntkrdsa tstksieevv ivgfgqkktv keltgalstm
       61 ngkaiednpv atsvdkmlqg rvagvqtgvs sgqpggfasv rvrgissing vkdpiyivdg
      121 vriksgnlsq gsvngvanqg nvlanlnpnd ienitvlkda vstamygada gsgviiittk
      181 kgkrgaakfn mnftqgitqd avkrqgvlsa dqykklltys imnayqgdpn ygdnfknyqs
      241 sydfvkgggl daedggyysg ilnspyntnw kkatqrdvay mrnveanmsg gndkmtyfgs
      301 vnyfdqnstv kgadfkrita ttsvayqate rlkistdiqm aysntnsqpe ggvytnpllg
      361 qyfnlptdpl rnpdgswylg qngrltngqf nnaaiqdyny qrnqtsrifa nlqaeyklak
      421 gltykfvfap efinllesay yspihgdgrs skgqktdiss ryfnfnlqni ltynfsadln
      481 nmsftalqea yrtqldlvsa tgmvvgspyl qtmdnfikpy svggqknids rwgyglvghy
      541 dydriillda syrrdvlsnf tpgkkagnfw svglgldvar fdfmkdwkam smlklrasyg
      601 kvgnqvlanp yalysyrgny ndlasadlrg vynpnlswet inplnigvdl gflnnritlt
      661 aeyynkkskd llfqmplqis qglpsywani gdmvnkgfef tvnadilkns dgfnwsvngn
      721 lstlknvitn lpggdivnpp vgingasmng tilrqgesmn syymrkwagv dptngdplwy
      781 ingkdgattn kyaeakeaiq gtslnkvtgg fgtnisykgi sldafftygf ggkildqwmg
      841 ytvsdgssig ntpgyesqmd fwtpenpnas npkpildlgn krsfamstrr lyksdyirls
      901 niklaytfkg dilektklts lqiyvlgnnv wthtfdknlr ldpeisvtgn ynlgipiqka
      961 ymlgvnigf
//
LOCUS       WP_102793634             913 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102793634
VERSION     WP_102793634.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..913
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=99701
     Region          32..912
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlsa gvlffigqsa maqkkkvdtt stksidevvv vgytakkkan vttavttvta
       61 kdlndlpits feqalagkap gvsinigtgq pgsaagviir gvgsinggtd plyildgvpi
      121 nsgvfaslnp ndfesvsilk daaakavygs qagngviiik tksgkkngrl tvnyngnvgv
      181 sllpqanfnm mdsqtqlgiq keigitpgnn paqfdalskv ntdwqkvflr egityqndls
      241 fsggfentdy rlslgyldqq givqnsglqr mtsnlslnmg ngknfrvgit gnfgfskktg
      301 anseaavala npisaaylal pyqslynadg slatgsgryg anayelavkq qrltqetkav
      361 vgihadydlt ddltlswkgn ldhtsqyfkg midpntfngs stnpgnsgsl srsynqytgl
      421 ntnlllrysk yfgdhsvsay agmdytgkfi dgfgftgygl nkllgnavss vqvttsllpv
      481 lsgtsrslhi lsyiasvdyg ykgkylisan vrrdggsffs sdykwgtfgg vsagwvvske
      541 nflagnriin dlklraswgk lgntgdlftr aaynneiymt qgqydgnatl fpsgpfnsty
      601 rwesesqydi gmdfglfnnr itgsfdyydr rtsdlyirrt lsyttgfdll gsfnggkmsn
      661 kgievelagd virtkdftln lwanyaynkn riedlgqvte yisgtsiirv glpygshyev
      721 kwggvdptng spiyldrdgn rmasynssqa qatygswvpp hqggfgmkln ykgfsleptf
      781 qfkagfyryn nmryfnenvr ninvygqydv vstywktpgq vtdiqgynya mqfssklied
      841 ssflrlrnvk igytfpkqtl gdfglngaqi ylnaqnlftw tkwtgmdpdd snnlssyeyp
      901 apriitvgvn ltf
//
LOCUS       WP_102793638             961 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102793638
VERSION     WP_102793638.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 961)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 961)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 961)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..961
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..961
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105175
     Region          15..959
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklcmlsa gvlffighsi aaqkvkkdts svrdiegvvv talgikrdek slgyaaskvk
       61 sedltqvanq nfvnslsgkv sglqvissgg apgqasrlvi rggnksltns neplyvidgi
      121 pisnandgna ntvsgiaspn raadinpddi envtilkgaa gavlygnrgs ngvvvittks
      181 gkvrggkpvv tfttrigtdn vlklpdyqtv yaqgnngvyv egtslsfgpe ingqtvqsvg
      241 agaiqgigpq avqlkvydpr keffetgitk ennislahtv nntnlffsag hnsqtsivpn
      301 qeyekvnfrf ngsfkltdrf sagvnttysr swgnvpfagq dgnnpifsil hvpvswnlsg
      361 ygyerpdngr qinfrggafd nplwsvyknf aktnsnrfil gvnlgydltd wlklsyrvgn
      421 dystdnrvlf rdifsggspn galsfddiar eeltstfmvn vnknitnnfn ltlnlgqdyn
      481 irklrnniig gsalvlpgia ntnnirtfnp gynynssrtl fgafadltlg yknylylnlv
      541 grqewsstlp etnrnyfypg gslsfiftda fninknimny gkvrvgasrt ardaspysiy
      601 ntyingvfnd gftsgitfpf iglpgytvan tinnaslkpe ftneyevgtn lrffkdritl
      661 dftyfrnint dgiipleisp tsgarrtiin sgktssngie vmfkatpvkt tdftwevgfn
      721 fsrirslvee iypgvdriyl ggfsgnpaiy avkgerygsi igtkyarndn geilvgnngi
      781 plredgadlg yvepdwtggv stsfkykgvy lnalldirqg gylyngteel ldvygvsakt
      841 lnrnedyifp gvnsttgnpn tvvvrrgsaw ygsaypneey iyknnwvklr elsvgysfkl
      901 pgidyirsvd lglygrnlyl wtkiphidpe sssfgtgnaq gvsrmafpst rsfgfslkvq
      961 f
//
LOCUS       WP_102793639            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102793639
VERSION     WP_102793639.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110307
     Region          15..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklfmfsa galffighsa maqkvkkdta svqdidevvv vgyskvsrss fvgtaskvdm
       61 ssvdnksvst vsqalageva gvrvinpsgq pgreatirir gigsvngnrd plyvvdgapy
      121 sgnisainpd diesmvilkd atataiygar gangvivlnt kkgrgksyvq iesrvgvnts
      181 llprysviks pedyiglswe alynqgffng nadpvsyans rlfsgggina yynmwnataa
      241 qlidpvkkkv rpgierrytp enwereafsp gfrtennfsi gggdaktkyy tnigylkdeg
      301 ysinsqyery tgrlnvshqa kpwlkgdfni gyaysktkng gqssdsgsif wfvdnipsiy
      361 plylrdangn lvpdpyyggn vsdygangrg fgaltnsigd atiskmgnik heinanffle
      421 akftdflkfe trlsgqyynd srdvlnspfy gssasqggri skskqemlsy tflqllrfnk
      481 kwgdhsveaf aaheanfyew qflsaartgl itpdipefnn attqqrgesy tndyglesyf
      541 gqanydydnk ylvsftirrd gssrflknkw gtfasagigw visrenflnn kslpylklra
      601 sygtngdqag vgyypgynvy dpgnmmgsia avfnrngypd ltwesanqaq igldyslfkt
      661 kliegtvdvy rkttknlifd srlapstgna vervndgqli nqgiefnlig hiikkkdfyl
      721 dlsingaler nkltkmpidr atgmpkvidl aasgygrvag rsmydyymre wagvnpdtga
      781 akwfvnyvda nnngafdage qisslyeyvq snpnakiseg ttevysqatq rfvgksampd
      841 isgaanlsvg ykgfslnvqm lysfggyayd gayaglmang qvggnnwstd ifnrwqkpgd
      901 vtdvprltsn rtgdtnytsv strfltkkny fllnnvtlgy nvpkqmlegl glnalqltls
      961 gdnlwlaskr rgfnpstset ggssmytysp lstftfgvkv nf
//
LOCUS       WP_102793646             958 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102793646
VERSION     WP_102793646.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 958)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 958)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..958
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107684
     Region          35..957
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktqiknfgk agvcfflmsg mvhaqttkkd slnekkieev vvvgykkqrk etltssvatv
       61 nseqlqdvts anfqtmlqgk mpgvvaavss gqpgskptmr irgiasisan ndplyvvdgv
      121 ivhgnadiap dqiedvtvlk daaatalygs rgaagvivit tkagkgnsin vrmnnsfnff
      181 nmgplkimns qqlkdhfmey ldnnpnlklf gadgvlsqqy gktlnswddi kndfnwkdla
      241 tqvgvvhnyd vsfnkssegs ktylnagyyn eegtikgykl erltvrlnhe tqlykwlkvs
      301 pklyfmydkt fdqqyslfdg fyklpwdspy npdgslyyvt ssnnaswfsr drgnylidrd
      361 ksyskantfn aqgnldfevk lmknlkfist nsltyynydg fsyndpsmls evttggrmsq
      421 snairwtsyt nqmlryentw ndkhrlnalv ayeyqdymyk angarvknii vgsevlsnsa
      481 eadgvptgqr neyafqsyls naeysyddky llqgsvrvdq ssrftsqnkt gvfwavstgw
      541 nvanerffqs lkstinkwkl rgsygaqgna ptnyyatynk stsvpyngni glyptqagnn
      601 nlkwetiyql dlgtdisfln nrinvvfdwy nkdtkdlits lqlpwitgfn sktvnigtir
      661 nrgielaida diirnsnvrw nvgfniaknk atyvdlyngs yksgmyrvav gekmytyelr
      721 ewagvdasng nplwnvyfds agkrianltd ymnanpgasv tskttnnydq atyvhlkdks
      781 rlpdftggfn tsvsykgftl aasayfsvgg ylyngqrssf ldadgtypyy nvmvpdkdwi
      841 rwspkntpeq nakathpsli yedtrkgrye strylekgdf lkirsislsy dvpksfipgn
      901 tfksarisvn aenmfmitgy sgqtpemdfl gsnsggdgfa ytgypaprti tvglnvsf
//
LOCUS       WP_102793863             942 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102793863
VERSION     WP_102793863.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103506
     Region          15..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknclkllsa gvvffagqdl liaqqrkdtv ktkeieevvm vgfgqkksvk evtgavstmk
       61 adkiekvpva svdkmmmgrv sgvqtgsasg qpggatnvrv rgitsvnggv spiyivdgvr
      121 issgdltaln ttanilanln sddiesltvl kdavstslyg adsgagvili ttksgksgkp
      181 rfsfhknfgi nkiafklpgt lnkeqwldla sqivtntysn dfptkedayk aitdpnidvl
      241 rkaaymgynt dwnkelsrns avqedlnfsa sggtdkfkyy ssfnyftqes vykasdfkrl
      301 tastkleyka terlnitsdf nfsngvintv anggafsnpl iaqyfnlpid pvrnpdgswy
      361 lgidnqlpsg nfnaaalqdm nynranttri fanlgvnyki ipnlsyrfvf apeyivieed
      421 qylsplhgdg ysykgqlsan trrffnfniq nileynfkvg tnhnfvarli qeayktngrn
      481 inavgsvval qrfqtldnfi kpnsvggtks vtsragyaaq inynykqifn ldasyrrdal
      541 snfmpgkkag nfysvgasvd vaeiflkdsn tfsaiklrss ygklgntits tpyatysfgl
      601 nyndnagavy agvynpdlkw etvkpfnigl dvgllkdrik vtaeyfnkkt edlvfsvpls
      661 nshglgsydr nighlvnkgm efsvdatilk aksnddlgln fdanlstldn kitslyggkd
      721 iinglsimre geivgsffmr kwagvdpang dplwyingvd gattndwnqa kravqgspfa
      781 kifggaglnv sykgfslnar ltysfgakvf dnwafytlsd gaytlyypgy asqldywtpq
      841 npnatnpkpy dggvnanqas trflykadyl rlsnvrlgyt frgdfikgap insftvyvmg
      901 nniwtkvfdn nlafdpesai saltnlnlpv lksyvigftl df
//
LOCUS       WP_102793999             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102793999
VERSION     WP_102793999.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109319
     Region          32..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqqckiga lalilfaeyg faqtrdsltk ensikevvvv afgkqkkeei tgsvqslktk
       61 dlanlqngni lqgiggkvag vqvissgqpg sqptirmrgi gsinassdpl ivldgipyng
      121 nlnsipgtdi esisfledas snalygsrga ngviivntkr gktnglhiea dvktginfrs
      181 iedypvytsp kdyytafynr arvgeiarlk qagavptgas phevgisaln klgynaynlp
      241 fnqlisqdgs fnpnaqllyq dnwkkllfkp alrreasvgi tanneqvksy tslnylddqg
      301 ylissgferf girsnldyai tsklkltsgl sythskqdfg etggfsnpfq farniapfyp
      361 vflrnnnyqi vydkngkaly dygdgqgpng aarsyavyen pvgnlqqdks qttsnitnin
      421 lglnyeiikg ldftynfgay lenikdlrfg ntiggtsasv ggnltmssif rntlnhqqll
      481 tyqkkigkhn fnilvgheln ktksdrfsgt kqqlvlpnsl sfdnavkitd lsgngyeyav
      541 egyfsrllyn ydnkyffnan irrdgssvfs pgsrwgnfyg lgaawniake dflkgnntin
      601 slklkvsygq qgndnillen sdrdyyayqd iyginnfgeg kpvlslrkqg nkdlkwetsk
      661 nlnagfeisl lknrislnad yferkvsdmi ytlplppsna gsyikygnig dminrgvqan
      721 lnidilrsde lqwsfyanat hyknkitklp aeqrstglvs glfilteggd rytyylkkfa
      781 gtdpnngdal wyrtninpnt kkeettitnn ykeatdyntg ksaipkvygg fgtdftykgf
      841 nlavnfayqf ggygyddiyr slfhsdtyas nystdldktw tpenpnaalp rvdlnstnqn
      901 gnstlyliks dyislqditl syqlpadftq higlsalkiy ltgnnlylws krkgydpras
      961 ltgvsnsyry sllssvslgf klnf
//
LOCUS       WP_102794121             991 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_102794121
VERSION     WP_102794121.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..991
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110497
     Region          32..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnknvkslla lvltgcitqa afsqktkdtv ktkvidevvv talgikrmnk slgyaaenkd
       61 skifedtqnn nwanalegkv aglkiqtaga gplgsaritl rgeksfdmds nsalividgv
      121 pmsnnttgtg asaygagagg dlpidygngi nsinpddias vtilkgasaa alygsraang
      181 aimittksga gskklrvsfs sdtsfdtvlk wpdyqyeygq gtlnkdksgk fyysygased
      241 gvntgstssa fgpkfngqsy fqydpniigp slerqlwrpy knnikgfwqa getysnnlsl
      301 ensndktsfr tslgyvknnw mmpntgfnrf nfstslthql neklkittkv myskmmsdnl
      361 patgynnqsi syfmifqnpn vdlawyrpiw kpgkegidqi hpfssyidnp ymiayemlns
      421 annnqlnani tlnykinnnf dvmfrsglew qndirsqrrp fssanypqgy yreehitnqe
      481 ynndilftyk nsqkdskigi saslggsiry neyryemtra tglrkpniyt lsnglslfsa
      541 ipspkdrqen siyglvslny gkyvyldlta rndwtstlrk gnnsffypsv stsfilsdif
      601 gikntfdfwk lrlsvagvgn gtkpyrldry ysigeisgsv vapntlnnin llpekntnye
      661 ggmdfsmfkn rlgfnftfyk nitknqivei paltesgfrs rfinsgsven kgleitlnat
      721 pikkpnfswn inanwsanrn kvlslpaefe gnpytvasvg dvlfyqvrig gslgdmygyk
      781 lqrtpdgqvi ydpstglptr padieyvgna fpewraglqn efkiknfris fsfdgqykgm
      841 aysqshhkms eqgklghtlw grenpdgmvi gegviknadg sfspntkkvl ltnyygdyyr
      901 ranvetnsfd tsfiklrdar vsytfpdasi gklklkelti alygknlwmw tkfplfdpea
      961 atlnnstitp gaevgqlpsa rtigmqlnvk f
//
LOCUS       WP_102794222             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bowmanella
            denitrificans].
ACCESSION   WP_102794222
VERSION     WP_102794222.1
KEYWORDS    RefSeq.
SOURCE      Bowmanella denitrificans
  ORGANISM  Bowmanella denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Bowmanella.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Bowmanella denitrificans"
                     /db_xref="taxon:366582"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55006
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipkeil tnetrvaatp ksveqllklg fevhveqgag elasfndqay ldagakiaar
       61 eeiwqadmif kvnapmkngr kkidefelik pgttiasfiw paqnpalleq laskqvnvla
      121 mdavprisra qsldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv qsmgaeflvv dvkgmeqssd gyaketsaef
      241 nqaaerlyae qakevdiiit talipgkpap klisqdmids mkpgsvivdl aaanggncay
      301 tkankivttp ngvkvigytd mpgrlpaqss qlyatnlvnl akllcknkdg qidldfddlv
      361 irgvtvikqg evtwpappik vsaqskpkvt pvkekqpdkp idprkkygll aagiaafawv
      421 ansappefls hftvfvlacv vgyyvvwnvk halhtplmsv tnaisgiivv gallqigkgd
      481 glvtflafia vliasinvfg gftvtrrmle mfrkggk
//
LOCUS       WP_102808502             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium sp. ENV421].
ACCESSION   WP_102808502
VERSION     WP_102808502.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium sp. ENV421
  ORGANISM  Mycobacterium sp. ENV421
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Mycobacterium sp. ENV421"
                     /db_xref="taxon:1213407"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52467
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgetrvaatp qtvgqliklg yevlvesgag vaasfsdeaf veagasigaa
       61 aqalateivl kvnaptsaei aalrdgatli slispalkpe lveelsrrpi tvlamdavpr
      121 israqsldvl ssmaniagyr avveaahsfg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaagslgai vratdprpev adqvkslgge ylsiespeae vsatgyakem gddykareaq
      241 lyaeqsedvd iiittalipg rpapriitad mvasmksgsv ivdmaaangg nvegtvkdqa
      301 vltdngvtii gytdlagrlp tqasqlygtn lvnllklltp dkdgtlvldf ddvvqrsvtv
      361 vrdgettwpp ppvqvsaapa paataapavq qtkqpmtmgr rlgitfgaav vlfllialsp
      421 aalqvhltvf alaivigyyv ighvhhalht plmsvtnais giivvgallq ighgdiivtt
      481 laavaillas inifggfavt rrmlamfsrs
//
LOCUS       WP_102820366             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas stutzeri].
ACCESSION   WP_102820366
VERSION     WP_102820366.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38849
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkligqg hrvtlqsgag llssvpdsay eavgatigda
       61 aaafaaelvl kvnapddael aqmqsgsvll gmlnpfdnec iarmaargit afameaaprt
      121 sraqsldvls sqaniagyka vlvgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhera lqsdivitta lipgrkaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvaadasaly arnlldflkl vidkdgqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_102826563             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas stutzeri].
ACCESSION   WP_102826563
VERSION     WP_102826563.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38731
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkligqg hrvtlqsgag llssvpdsay eaagaaigda
       61 aaafaaelvl kvnapddael aqmqsgsvll gmlnpfdnac iarmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vlvgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhera lqsdivitta lipgrnaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvaadasaly arnlldflkl vidkdsqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_102833374             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas kunmingensis].
ACCESSION   WP_102833374
VERSION     WP_102833374.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas kunmingensis (Pseudomonas kunmingensis)
  ORGANISM  Stutzerimonas kunmingensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas kunmingensis"
                     /db_xref="taxon:1211807"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38759
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkligqg hrvtlqsgag llssvpdsay eavgatigda
       61 aaafaaelvl kvnapddael aqmqsgsvll gmlnpfdnac iarmaargvt afaleaaprt
      121 sraqsldvls sqaniagyka vlvgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhera lqsdivitta lipgrkaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvaadasaly arnlldflkl vidkdgqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_102837185             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Stutzerimonas].
ACCESSION   WP_102837185
VERSION     WP_102837185.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas
  ORGANISM  Stutzerimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas"
                     /db_xref="taxon:2901164"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39012
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletr pgetrvaatp etikkligqg hrvtvqsgag vqasvpdsaf eaagatiada
       61 aaafaaeill kvnapsetel aqmqpgtvlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmvaanqypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpcetdee recaegvggy arpmpaswma
      241 rqaqavhera kqadiiitta lipgrkaptl lqeetvqqmk pgsvvidlaa sqggncplte
      301 adqvvvkhgv tlvgytnlat hvpadasaly arnlldflkl vidgeakfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_102839230             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas frequens].
ACCESSION   WP_102839230
VERSION     WP_102839230.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas frequens
  ORGANISM  Stutzerimonas frequens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas frequens"
                     /db_xref="taxon:2968969"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38869
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkligqg hrvtlqsgag llssvpdsay eavgatigda
       61 aaafaaelvl kvnapdeael aqmqsgsvll gmlnpfdndc iarmaargii afaleaaprt
      121 sraqsldvls sqaniagyka vlvgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhera lqsdivitta lipgrkaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvpadasaly arnlldflkl vidkdgqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_102841780             464 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylocella silvestris].
ACCESSION   WP_102841780
VERSION     WP_102841780.1
KEYWORDS    RefSeq.
SOURCE      Methylocella silvestris
  ORGANISM  Methylocella silvestris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Beijerinckiaceae; Methylocella.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Methylocella silvestris"
                     /db_xref="taxon:199596"
     Protein         1..464
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47226
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
     Region          <376..>451
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mriavqaetd phesrvaatp etvktfiglg aevavetgag rgsaiaddaf aaagatlapt
       61 aaaaaagadv vlrvrrpkaa elagvkpgai vlavldpyen vaalqslaga gvsafameli
      121 pritraqsmd vlssqanlag yravidaaas ydraipmmtt aagsiqpari fvmgvgvagl
      181 qaiatarrig glvtatdvrp atkeqvlslg akfiavedee faaaetaagy akpmspeyqa
      241 kqaeltashi akqdivitta lipgrkapvl itadmvasmq rgsiiidlav erggncelsr
      301 pgetviseng vkiignlnvp grvaasasal yarnlvnflk plidkethel aidwddeivk
      361 atlltrdgal phpnfqapap estteaavep qpeagagaqa qapesaadav aeapalveae
      421 pgaeiapppa agdeqpqpta egpepaakpr qrsksgrgsa qgkp
//
LOCUS       WP_102848846             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phaeobacter inhibens].
ACCESSION   WP_102848846
VERSION     WP_102848846.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter inhibens
  ORGANISM  Phaeobacter inhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Phaeobacter inhibens"
                     /db_xref="taxon:221822"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55570
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egearvamtp dsavqlqklg ytcaietgag aaagfadaty eavgveivkt
       61 paalwkaadi vakvrqptet elkrmtagkt lisffnpggn eagmeiarsk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigastslg aityafdvrp evaeqvesmg aefvyldfee sqqdgaatgg yaavsspefr
      241 eaqlakfrel apdvdivitt alipnreapk lwledmvaam kpgsviidla aekggnvegt
      301 vmdekvvten gvtiigytdf psrmaaqast lyatnirhmm tdltpekdgq lnhdmeddvi
      361 rgatvtfeke itfpppppkv qaiaaqpkke vkeltpeekr eqeveafkqq tknqvtllav
      421 ggalvlfvgl fapasfmqhf ivfalacfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl viflaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_102844998             170 aa            linear   BCT 07-JUL-2024
DEFINITION  aromatic/alkene monooxygenase hydroxylase subunit gamma
            [Methylocella silvestris].
ACCESSION   WP_102844998
VERSION     WP_102844998.1
KEYWORDS    RefSeq.
SOURCE      Methylocella silvestris
  ORGANISM  Methylocella silvestris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Beijerinckiaceae; Methylocella.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Rosenzweig,A.C., Frederick,C.A., Lippard,S.J. and Nordlund,P.
  TITLE     Crystal structure of a bacterial non-haem iron hydroxylase that
            catalyses the biological oxidation of methane
  JOURNAL   Nature 366 (6455), 537-543 (1993)
   PUBMED   8255292
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Cardy,D.L., Laidler,V., Salmond,G.P. and Murrell,J.C.
  TITLE     Molecular analysis of the methane monooxygenase (MMO) gene cluster
            of Methylosinus trichosporium OB3b
  JOURNAL   Mol Microbiol 5 (2), 335-342 (1991)
   PUBMED   1904125
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Fox,B.G., Liu,Y., Dege,J.E. and Lipscomb,J.D.
  TITLE     Complex formation between the protein components of methane
            monooxygenase from Methylosinus trichosporium OB3b. Identification
            of sites of component interaction
  JOURNAL   J Biol Chem 266 (1), 540-550 (1991)
   PUBMED   1845980
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Stainthorpe,A.C., Murrell,J.C., Salmond,G.P., Dalton,H. and Lees,V.
  TITLE     Molecular analysis of methane monooxygenase from Methylococcus
            capsulatus (Bath)
  JOURNAL   Arch Microbiol 152 (2), 154-159 (1989)
   PUBMED   2505721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF045805.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Methylocella silvestris"
                     /db_xref="taxon:199596"
     gene            1..170
                     /gene="mmoZ"
     Protein         1..170
                     /product="aromatic/alkene monooxygenase hydroxylase
                     subunit gamma"
                     /EC_number="1.14.13.25"
                     /GO_function="GO:0015049 - methane monooxygenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=19394
     Region          6..166
                     /region_name="MeMO_Hyd_G"
                     /note="Methane monooxygenase, hydrolase gamma chain;
                     pfam02964"
                     /db_xref="CDD:427082"
ORIGIN      
        1 mpnynihenp vrsdwlekia elksvkdata fiqdfrkknt spfrtcyald vdylfieaki
       61 eerlavlkss tfsaadlftk attgetaqav addwiakmda ekdkfaaeki litfrqlykp
      121 pvlpvnlffk vdtylgsrlm elrntdyyad sledlrkkrg vkvlrlgnva
//
LOCUS       WP_102854328             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phaeobacter inhibens].
ACCESSION   WP_102854328
VERSION     WP_102854328.1
KEYWORDS    RefSeq.
SOURCE      Phaeobacter inhibens
  ORGANISM  Phaeobacter inhibens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Phaeobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Phaeobacter inhibens"
                     /db_xref="taxon:221822"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55600
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egearvamtp dsavqlqklg ytcaietgag aaagfadaty eavgveivkt
       61 paalwkaadi vakvrqptet elkrmtagkt lisffnpggn eagmelarsk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigastslg aityafdvrp evaeqvesmg aefvyldfee sqqdgaatgg yaavsspefr
      241 eaqlakfrel apdvdivitt alipnreapk lwledmvaam kpgsviidla aekggnvegt
      301 vmdekvvten gvtiigytdf psrmaaqast lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgatvtfeke itfpppppkv qaiaaqpkke vkeltpeekr eqevetfkqq tknqvtllav
      421 ggalvlfvgl fapasfmqhf ivfalacfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl viflaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_102862522             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_102862522
VERSION     WP_102862522.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38699
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigna
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqsdivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_102893144             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas stutzeri].
ACCESSION   WP_102893144
VERSION     WP_102893144.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39093
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq aretrvaatp etvkkligqg hrvtlqsgag llssvpdsay eavgaaigda
       61 aaalaaevvl kvnapneael aqmqpgavll gmlepfddag iarmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswma
      241 rqaqavhqra lqadivitta lipgrkapvl lqeetvrqmk pgsvvidmaa shggncplsv
      301 vdqvvvdhgv tlvgysnlat wvpadasaly arnlldflkl vidkdgqfql nleddivrac
      361 lmcrdgqvvr sna
//
LOCUS       WP_102867198             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudovibrio exalbescens].
ACCESSION   WP_102867198
VERSION     WP_102867198.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio exalbescens
  ORGANISM  Pseudovibrio exalbescens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Pseudovibrio exalbescens"
                     /db_xref="taxon:197461"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55974
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigapkevl egelrvaltp esakqlqklg yevvvetgag aaasfndedy eaagvkivpd
       61 aktlwetani iskvrppvea elelaregqi lisffwpaqn eelmkkfadk kvtvlamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv liigagvagl
      181 aaigastslg aityafdvrp evaeqvesmg aefvyldfee eqqdgassgg yasvsspefr
      241 aaqlakfrel apevdivitt alipgrdapk lwledmvasm kpgsvivdla aekggncdlt
      301 kmdekvvsen gvtvigytdf psrmatqsst lyatnirhmm ddltpekdgq pnvnmeddvi
      361 rgatithegd itfpppppkv qaiaaqkkpe vkeltpeekr aaeiaefkkk trqqvallag
      421 ggilmllvgl vapasfmqhf ivfvlacfvg fqviwgvahs lhtplmaitn aissiiilga
      481 llqigsgswl vivlaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_102898736             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cenocepacia].
ACCESSION   WP_102898736
VERSION     WP_102898736.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39102
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiakgag saasypdepy vaagaeltdq
       61 saafaadlvl kvqaptdael pllkrgavlv gmlepfngeq aaklaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvdtaqsmk pgsvlvdlaa grgpeidgrk
      301 ggncpltvad qvivhhgvti agytnlasmv asdasalyar nlldfmkliv tkegtlnidl
      361 tddivaatll crdgelark
//
LOCUS       WP_102905604             376 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Variovorax].
ACCESSION   WP_102905604
VERSION     WP_102905604.1
KEYWORDS    RefSeq.
SOURCE      unclassified Variovorax
  ORGANISM  unclassified Variovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="unclassified Variovorax"
                     /db_xref="taxon:663243"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38698
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaett agetrvavtp etarklvgqg havrvqagag vaasvtdaay qaagaeitdl
       61 agaygvdivl kvrspddaea armkpgtvlv gmlnpfdgpg lqrlataglt sfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtpee keaavgvggy akpmppswla
      241 rqqvevakrv aladivlsta lipgraaptl vtedmvksmk pgsvivdiaa grgpdgvggn
      301 cplseadrtv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke gslkidledd
      361 ivaacrmtqd gqvtrk
//
LOCUS       WP_102912766             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Streptomyces cahuitamycinicus].
ACCESSION   WP_102912766
VERSION     WP_102912766.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces cahuitamycinicus
  ORGANISM  Streptomyces cahuitamycinicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Streptomyces cahuitamycinicus"
                     /db_xref="taxon:2070367"
     Protein         1..>382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          10..>382
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mvpaepqpqr igipaestag etrvaatpat vgrlaalgyd vvvepgagas srfsdtayee
       61 agaelgdpwq aeivlkvnap sseetgrlre gatlialisp alnpelveel arrpitalam
      121 davprisraq sldvlssman iagyravvea ahafgrfftg qvtaagkvpp akvlvagagv
      181 aglaaigaar slgavvratd prpevaeqvr slggeflavg veqevstdgy akatsedydr
      241 laaqlyaeqa advdiiitta lipgrpaprl itaedvarmk sgsvivdmaa aqggnvegtv
      301 agkavvtdnd vtiigytdlp grlpaqasql ygtnivnlmk lltpgkdgrl vldfddvvqr
      361 smtvvregek twppppvqvs aa
//
LOCUS       WP_102954536             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            diazotrophicus].
ACCESSION   WP_102954536
VERSION     WP_102954536.1
KEYWORDS    RefSeq.
SOURCE      Vibrio diazotrophicus
  ORGANISM  Vibrio diazotrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Vibrio diazotrophicus"
                     /db_xref="taxon:685"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54440
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp ssvqqlvklg fdvsieshag dlasfdnasy eqagakivsk
       61 devwnselil kvnaplsnde sdeialikeg atlvsfiwpa qnpelmekls tksinvlamd
      121 svprisraqs ldalssmani agyravveaa hefgrfftgq itaagkvppa kvfvagagva
      181 glaaigaags lgaivrafdv rpevkeqvqs mgaeflevdy qensgsgdgy akemsdefnk
      241 kaaelyaeqa kdvdiiitta lipgrpapkl vtkemvdsmk agsvivdlaa anggnceytv
      301 kdqvittpng vkvigytdmv grlptqssql yatnlvnllk llckekdgni nidfedvvlr
      361 gvtvvkegei twpappiqvs aqpqakpqkv dpkaakveep tspakkiigl avgvgafawv
      421 asvapaaflg hftvfvlacv vgyyvvwnvt hslhtplmsv tnaisgiivv gallqigqgn
      481 gfvsflafia vliasinifg gftvtkrmle mfrkd
//
LOCUS       WP_102960076             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mangrovicella endophytica].
ACCESSION   WP_102960076
VERSION     WP_102960076.1
KEYWORDS    RefSeq.
SOURCE      Mangrovicella endophytica
  ORGANISM  Mangrovicella endophytica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Mangrovicella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Mangrovicella endophytica"
                     /db_xref="taxon:2066697"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55623
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapqety pgenrvamtp dsaarliklg yecliqsgag erarfsdeay rtagvtvvpt
       61 aadlwreadi vakvrapsqd evaqaregqi lisflypaqn adlleqlrak gvtalamdmv
      121 prisraqkmd alssmaniag yravieagnn fdrfftgqit aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aqfvyldfke qqqdgattgg yaapsspefr
      241 ekqlekfrel apeidivitt alipgrdapk lwladmvaam kpgsvvvdla aerggncdlt
      301 vpdqaietpn gvkivgytdf psrmatqast lyatnirhmm ddltpakdgm pvvnmeddvi
      361 rgatvtkdaa vtfpppppki qaiakqaprk vveetaeqka vreaalarkn gqrqmallgl
      421 gavlllligs vapvsflqhf vvfalscfvg yhviwnvsha lhtplmavtn avssiiilga
      481 ilqvgstsav vaalaaiail iasinifggf mvtrrmlkmf qks
//
LOCUS       WP_102963619             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            diazotrophicus].
ACCESSION   WP_102963619
VERSION     WP_102963619.1
KEYWORDS    RefSeq.
SOURCE      Vibrio diazotrophicus
  ORGANISM  Vibrio diazotrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Vibrio diazotrophicus"
                     /db_xref="taxon:685"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54512
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp ssvqqlvklg fevsieshag dlasfdnasy eqagakivsk
       61 devwkselil kvnaplsnde sdeialikeg atlvsfiwpa qnpelmekls tksinvlamd
      121 svprisraqs ldalssmani agyravveaa hefgrfftgq itaagkvppa kvfvagagva
      181 glaaigaags lgaivrafdv rpevkeqvqs mgaeflevdy qensgsgdgy akemsdefnk
      241 kaaelyaeqa kdvdiiitta lipgrpapkl vtkemvdsmk agsvivdlaa anggnceytv
      301 kdqvittpng vkiigytdmv grlptqssql yatnlvnllk llckekdgni nidfedvvlr
      361 gvtvvkegei twpappiqvs aqpqakpqkv dpkaakveep tsptkkiigl avgvgafawv
      421 asvapaaflg hftvfvlacv vgyyvvwnvt hslhtplmsv tnaisgiivv gallqigqgn
      481 gfvsflafia vliasinifg gftvtkrmle mfrkd
//
LOCUS       WP_102966800             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            diazotrophicus].
ACCESSION   WP_102966800
VERSION     WP_102966800.1
KEYWORDS    RefSeq.
SOURCE      Vibrio diazotrophicus
  ORGANISM  Vibrio diazotrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Vibrio diazotrophicus"
                     /db_xref="taxon:685"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54510
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp ssvqqlvklg fevsieshag dlasfdnasy eqagakivsk
       61 devwkselil kvnaplsnde sdeialikeg atlvsfiwpa qnpelmekls tksinvlamd
      121 svprisraqs ldalssmani agyravveaa hefgrfftgq itaagkvppa kvfvagagva
      181 glaaigaags lgaivrafdv rpevkeqvqs mgaeflevdy qensgsgdgy akemsdefnk
      241 kaaelyaeqa rdvdiiitta lipgrpapkl vtkemvdsmk agsvivdlaa anggnceytv
      301 kdqvittpng vkiigytdmv grlptqssql yatnlvnllk llckekdgni nidfedvvlr
      361 gvtvvkegei twpappiqvs aqpqakpqkv dpkaakveep tspakkiigl avgvgafawv
      421 asvapaaflg hftvfvlacv vgyyvvwnvt hslhtplmsv tnaisgiivv gallqigqgn
      481 gfvsflafia vliasinifg gftvtkrmle mfrkd
//
LOCUS       WP_102967836             314 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Vibrio diazotrophicus].
ACCESSION   WP_102967836
VERSION     WP_102967836.1
KEYWORDS    RefSeq.
SOURCE      Vibrio diazotrophicus
  ORGANISM  Vibrio diazotrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Vibrio diazotrophicus"
                     /db_xref="taxon:685"
     Protein         1..314
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35989
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifelfssr qkkargdvpd vyqykeipnk lrvqiihiik atigtrenns hyggptasei
       61 iyqkiheilc keygvfslsk qqytsdfeav ytyflnsdnv eecldiielt fkyiefrvkp
      121 nqlqfsrend tkqkaddaie elnhrfkesg vgyeflsgei vkidsqfihs evvkpalmil
      181 qgeeayngar deflsahthy rnqrykealv dclksfesmm kaicekrgwq fgkndsakkl
      241 inicltnnli pgymqeqfsq frallesgvp tvrnkegghg qgveiknvse nmvsytlhlt
      301 atnivflgqc ekes
//
LOCUS       WP_102968456             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            diazotrophicus].
ACCESSION   WP_102968456
VERSION     WP_102968456.1
KEYWORDS    RefSeq.
SOURCE      Vibrio diazotrophicus
  ORGANISM  Vibrio diazotrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Vibrio diazotrophicus"
                     /db_xref="taxon:685"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54482
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp ssvqqliklg fevsveshag dlasfdnasy eqagakivsk
       61 devwkselil kvnaplsnde sdeialikeg atlvsfiwpa qnpelmekls tksinvlamd
      121 svprisraqs ldalssmani agyravveaa hefgrfftgq itaagkvppa kvfvagagva
      181 glaaigaags lgaivrafdv rpevkeqvqs mgaeflevdy qensgsgdgy akemsdefnk
      241 kaaelyaeqa kdvdiiitta lipgrpapkl vtkemvdsmk agsvivdlaa anggnceytv
      301 kdqvittpng vkiigytdmv grlptqssql yatnlvnllk llckekdgni nidfedvvlr
      361 gvtvvkegei twpappiqvs aqpqakpqkv dpkaakveep tspakkiigl avgvgafawv
      421 asvapaaflg hftvfvlacv vgyyvvwnvt hslhtplmsv tnaisgiivv gallqigqgn
      481 gfvsflafia vliasinifg gftvtkrmle mfrkd
//
LOCUS       WP_102972506             428 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. AFG20].
ACCESSION   WP_102972506
VERSION     WP_102972506.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. AFG20
  ORGANISM  Arthrobacter sp. AFG20
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Arthrobacter sp. AFG20"
                     /db_xref="taxon:1688671"
     Protein         1..428
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43879
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiarerr egerrvaatp etvkqlaglg levlvesrag vsaghaddey rqagaqivad
       61 ldpaaldila hvrplelpaa talkrgavtv glaspssela tvralaeggv tsfalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplymtaa gtvpparvlv lgvgvaglqa
      181 igtakrlgar vsandirpss aeevtsmggt fikldletae aaggyarelt adrgalqrql
      241 laphvadadv littaavpgr hapllvtrem vqgmrpgsvv vdlaaesggn vegsvagrdi
      301 hvptadgkgt vtvvglkdap samptdasrl yaknvanlla lmtrdgtvap dfdddviaga
      361 clthdgvvrh pptaealavl trenapdgas gepprgapee dtadeadsel adelangpvk
      421 asenegvv
//
LOCUS       WP_102976498             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. AFG7.2].
ACCESSION   WP_102976498
VERSION     WP_102976498.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. AFG7.2
  ORGANISM  Arthrobacter sp. AFG7.2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Arthrobacter sp. AFG7.2"
                     /db_xref="taxon:1688693"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39979
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiprerr egerrvaatp etvkqlaalg aevlceagag aaaghpdaay gqagahivge
       61 ldlaqldvla hvrpldpdta rslkrgavtv glaspsselp tvqaladagi tsfalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplymtaa gtvpparvlv lgagvaglqa
      181 igtakrlgar vfandirpas adevasmggt firldletae aaggyarqls sdagtrqrql
      241 laphvaqadv littaavpgr rapllvtrem vqgmrpgsvv idlaaesggn vegvvagqdv
      301 pmptadgsgh vmlvglkdap samasdasrl yaknvanllv lmvrdgelip dftdevvags
      361 clthegavrh qptadlvaer agsrqegvl
//
LOCUS       WP_102978493             992 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium].
ACCESSION   WP_102978493
VERSION     WP_102978493.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110093
     Region          29..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrketqklll lsvlglvsvn maaqqqvkkd tiknidevvv talgikrqdk slgyvaekvd
       61 aevfeniqnn nwaqglegrv aglkiqttga gplsssritl rgeksfnldg nyalivvdgv
      121 plsnsttgtg taaygagtgg dlpidlgngl nsinpddies vtilkgasaa alygsraang
      181 almvttksgk skngklkvsf nsslsfdsvl kwpdyqyqyg qgtlakntag effysygasa
      241 dgvstggtss afgpkfngqs yfqydpnllg qsaerqlwrp yednikgfwe tgvtssnnis
      301 vesstdrtsf rtslsyldnk wmmpntgfdr fnlafsldhk vtdkfkistk fnyantksdn
      361 lpatgynnqs isyfmifqnp nvdlawykpi wkpgqeqvdq ihpfssfidn pyliayqmln
      421 gvekkmitgn isgtydfnkn fslmlrsgie mldeerttkr pyssanylkg fyreqyiknn
      481 efnndllftf kkdygkfnvs anagasiryn eyvmndyrae glkvigdysl nnaislitkv
      541 pkpndqqtns vygllsanyd nlvfldvtgr ndwsstlpvq yrsffypsvs ssfilsdifk
      601 lssptfnywk lraswakvgv aglpyqldky ytpsdfigsv ltpgtypnpl lkpedntnie
      661 agmdfsvlkn rlsynvtlyq ndtdnqiiti ptllesgysn riinagkvrn rgvemsmnam
      721 pfktqnfswn isanwtlnrn kiltlpdefa gensytistv agvlyynavv ggslgdlygf
      781 klvrnadgqv vydattglps rpdrvekvgn afpkwragfq ndfkiknwqi sfsfdgqygg
      841 maysqthhkm seqgklentl mgrdnpsgti vgqgvvlnpd gtyspntkav glaayygdyy
      901 rranietntf dtsfiklrda riaysfskev iaplkltelt lavfgknlwm wtkfpmfdpe
      961 vaalndstit pgaeigqlpt artvgfqvnl kf
//
LOCUS       WP_102978850             970 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium].
ACCESSION   WP_102978850
VERSION     WP_102978850.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 970)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..970
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107163
     Region          44..966
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvltv gvlfftgqai faqedtttsk kereekieev vvlgynnkvv kslttsaqtt
       61 vlaeqienrp nismisslqg tapgmqisan sgspgsakin vlirgissls gstdplyvid
      121 gipvnstvfr slnpedvesf svlkdaqats iygnrgangv ivittkkgrf nnkisirysg
      181 ntgftelqkh rydiansket lrlekqwetg lggtltdaqi dnyaidtnwe dyffrkgfsq
      241 shnvsvaags qnlssytslg yleqegivnn tdfkrftlrq nvdgksndsk ftysvgigan
      301 ystrneleqe trtdidgnvl qnplqgllts apyidpnlyq ggqqlfdqfg apsfqivpym
      361 lmdylrpgsv pnrynefkll anmsakyqft delsasitsg tdftqnkrvf arapwsylai
      421 tsqasagaaf ggielqsvnq dfgfnsvakv nynktigdkh tidvgvysey ikahrrfqay
      481 qqsgldprtw slgagtgytp wsastptlyr ptvsaiqqda glfsyfatad ydydgkygvs
      541 gmirrdasyk fiednrwgtf wsagarwnln kenfladssf nllklrgsyg tmgnanlsss
      601 iagnnllyag gqvvrdlnss qsgyggqssi gvsnianrnf iwekisqani gvdydykngl
      661 itgsvdiyrk kttdmfntin isatngiytl tgnlgdmknd giealirysp fkgkdfnltv
      721 fangsynnnk itkmpytmpt egnpfltmny qrpsdgviya eghlayeyfm vpylgvnhen
      781 gnmlfldrfg natedptdld rrftgkspip kyqggfglet sykgfyldvl ftfaadvwrv
      841 dadlqglsnp qanlgafpvt rdllnawspt ntasdtpaid atnytqseaf sdrflrdasy
      901 lrlrniavgy svskdllkst pikglkvfat aenmytwtkw rgfdaesfsg styggyptpk
      961 iisfgveaef
//
LOCUS       WP_102979527            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium scophthalmum].
ACCESSION   WP_102979527
VERSION     WP_102979527.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium scophthalmum
  ORGANISM  Chryseobacterium scophthalmum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Chryseobacterium scophthalmum"
                     /db_xref="taxon:59733"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124225
     Region          22..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkafillpl laaqialaqe kktitgkidd gdtskviaga sikietqsvs tktnqtgiie
       61 svsigtitdk ngnftleips dtksvtvsyl gyepkiiqiy egqtsynitl isvvsddipe
      121 knniqeviit gyqkiekrkq tsavttvkmn diqqagvasv dqllagqiag vavtpetgap
      181 gspakirirg taslsgpqdp lwvidglple gndvpnfsdk dnidqlqnfs iaglnpndie
      241 ditilkdaaa taiygaraan gvisittkkg kkgslrvnfs adtfitarpd fgklnllnas
      301 ekvdlelmla nrtdltyrtd kgevmriltq ngqldayrng glgalnmltr qqidglrnsn
      361 tdwgkllyqn ainkqygvsi sggsdrsdyy fslgyydeeg ttigtgfery nltlknnyki
      421 ndklnfgvsv fgtqsertsf vtdadasisp inysrnanpy lspynadgsy rydkdidgfe
      481 dryipfnfle erentsytlk nqslkaifdl dyklakglki tsqlglqydg nktekfaaen
      541 tyftrkmkeg tryykdgayr yflpdggvkq nwdnsffqyn wklqgsystk insvheidlm
      601 agtelrkted nttvtrafgy dsvtrrstai vfpssnfaae rkyetyremp pienayasmf
      661 atasytydqk ytffgsvryd gtnlfgvnkk ykylpiwavs gswlvskedf mknlsaisnl
      721 rlrasyglqg nidrntspff igeysdstil pggkeniinv inppndklrw ekttnvnfgl
      781 dlgvfnnrin ltadvynrkg tdmismketp letgfeytmm nwgsltnkgf elavstknin
      841 kdnfkwstti nfahnksnvi seqprdnall psreglpvna vfalktagmd engnpmfwkg
      901 nekvkiedff alydvyadfl pgqlvdskls naelrslfty vgdrdpkftg giintfkisn
      961 fdftvsatfn ikqtvmqtps yrgmeldrgr nytkdiynag gslpgitspd metnpgwmgn
     1021 kwlsdnrsna yslldiwake isylrissir lgytlpkeft npmgisalrl svegrnlfvf
     1081 sngykgyfdp etygniyaqp itksvtvgfn vsf
//
LOCUS       WP_102980512             974 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium].
ACCESSION   WP_102980512
VERSION     WP_102980512.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 974)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 974)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 974)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..974
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..974
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107210
     Region          29..973
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttgvli lvlsssfvva qaqtkpgdtl ktqeiegvvv talgikrekk algyasqeik
       61 gdvisdagqt navsalsgnv agvqvtapst mggstritmr gissitgenr pliivdgvpl
      121 dnsnvndvdt qrgaggrdyg dasfdinpdd iesvtvlkgg paaalygsra gngailyttk
      181 sakkgktdvq fntgvafeei yirpklqnqy gggsqftlpt qsingttyni qeyqtdaswg
      241 pkydpnlmyl pwyafdpefs adylkpvpfv apkndvdsff ktgvaytnnl svaksfgdtn
      301 vrlsytntni sgivptskik kdnfsinlns klseklkada vlnyvhtegf nrpevgygdn
      361 svaqkfyqfg qrnldfvklm dykladgsqr twnrtswdna apkysdnpyw tifentsads
      421 rnrffgnagl tynidkhfyi tgkvyadlys qnissrvavg sqaisnytle krnvsefnye
      481 grahynnnfg dfslnafagf nirdnkmswl rgttvgglii pglynlnngi enslatnyds
      541 hssvksifgs vslgykdmlf veatgrndwf smlnddqfyp svtgsfvfsk vlnadwlsfg
      601 kiragwssia lgtdpynrlt yteiglpfng spqysnpnts ndpnikpelk vtqeigieas
      661 lfknrvsldf tyydtkskdl iialpidpat gylfkrinag emtnkgieam vnvvpirnen
      721 fswnvtwnfa rnrnrlvnly gdlqnyvltn apfraqlvaq vgqaygtilg tdfvydgngn
      781 kvvdengfyk asdlkslgsi lpeynmgfrn tlkykslsls flidiqqggk yfstthmwgm
      841 ysgmleesal ggnreagivl agvkedgtqn dilldaqtwg styyntvdaq nvfdasyikl
      901 rdvtigyelp kslignvfeg irisafarnv fawnlankgi dpentsygsg niqgmeggsl
      961 pstrtfgfnv nfkf
//
LOCUS       WP_102980544             934 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium].
ACCESSION   WP_102980544
VERSION     WP_102980544.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 934)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 934)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 934)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..934
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..934
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103301
     Region          35..931
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvkisrslg iiaalyftan fnaqttprdt vskeqkieev vvigygsvkk snltsavstv
       61 ksetfddrpi sniaqaiqgn aagvnvvqps gkpggtmevk irgntsltsn ttplyvvdgi
      121 qtndisginp ddivdmtilk datstaiygi ngssgvvlvt tkrakynksq lgfnafwgfs
      181 kqvdninvln ldqyktlmge inpsylttin npiyngintn wrekvyqtgf dqnynvnysf
      241 gnenvkayts lgyqgidgvi kpasfdrysf kvnldaniak wlklntslsy iktnlnntnd
      301 nlssgrggvv lsalntpsfl pvygtdvnsi ptdsngnvlp gylpgqfapn pfqsssenpv
      361 ayqsrldktw nnrfmsilgl dislaknltf kpsisldyid tnkmtftday qtsygraqfg
      421 tggdsnstwq nilyegtlny alksgksdwt fllggnirdy kyrssgrwgs rfsedvrefv
      481 ydlaeqkhyg ygpfgppedv reissfarai ytydnkytvm giikaqassa lapgkkwgyf
      541 pgvsaawvis nedflkdnni lsylklrggw gkagnatgip ayssfnyati sefgndsngn
      601 pmgnwqqnki gnedlswett tdtnigldfn llnnrikftv dafkrdtkdl ilnvpiftdk
      661 syfrnigsie nkglefsfss snvksssftw dtsfnisfik nkitkidyvp vvykannetv
      721 gesivrfspd favgafygyq vqgvdpqtgs lqykdlngng ffdaadrsvi gnpnpnftfg
      781 fsnqfkfknl yvdvlitgsq gndifnasrl dlelmndykn qssavinrwt tpgqitdipk
      841 andtealhis drfvedgsyv klkavtlgyn fknvfkgisn lnvyvtgqnl ytwtkysgfd
      901 pevnaysgtp giigidygty pqvrtfifgi kttf
//
LOCUS       WP_102980689            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium].
ACCESSION   WP_102980689
VERSION     WP_102980689.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110647
     Region          29..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknsyykigg iffglmltav stntkaqtrt isgtvtasnk plsgvsisqe gsdqvtttse
       61 ngtytlqvta enpillfrhp dydeekvsti nqtvvnisle hkvkgieevi lnagyykvkd
      121 kertgsiakv sakdienqpv tnvlsalqgr mpgvnitqns svpgggfdvq irgrnslrsy
      181 attgydgskp lyivdgvplp qvndfntgms anilpysetn plnsinpddi eslevlkdad
      241 ataiygskga ngvilittkk gkkektevnl rtsyglgemt nlpkmmnlqe ytamrkiafv
      301 ndgvavpsna ydingvwnst kttdwqkyfv gntaeftdvq lgvsggsgst qfsitgghne
      361 ettvfpgsyr ytrnnlgvsl nhssedrkfq iafngtaalq nnilpptdfn lvyaslapna
      421 pdlytsnnmi nwenntftnp mgpatqtytv rtknlnanit ssyiigggfs vnlnsgysty
      481 nsydqkifpk ttynpssnig ssnssirkgq kmnqswilep qlnyekkwtk hqfsallgas
      541 lqeqksdnlv ilgrnfpsdd mltniaaaas vtipsayesl yryqavyarf nyglnkryfl
      601 nltgrrdgss rfgserryan fgavgaawlf seenmfkgqs wlsfgkfrts ygvagndqig
      661 dyqyydtyqs tggsyggysg lapqrlynkn fgweltrkfe aalelglfkq rlnltvgyyh
      721 nissnqlvgi pmpatvgfss iqanldatvr nrglevslqs vniqgdnwkw ttglnftlpe
      781 nklmefpnld kstyasrfei gkstslvkly qytgidpitg lytfydanqd giintadrvv
      841 skeikeywyg glqnsvqykn wsldvllqfi sqsqyniysm ygnigymanm pavftdywtp
      901 dnpdaqfqkp sagystaaat asslfnnsda tvsdmftvrv knatlsytip saengrlrak
      961 vffsgqnlfv fsnykygnpe ftlagysspl rvlsfgfslt y
//
LOCUS       WP_102980751             941 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium].
ACCESSION   WP_102980751
VERSION     WP_102980751.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 941)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     Protein         1..941
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103689
     Region          35..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqtnlkysc liavlyfgmn vngqiapkdt vakeqkieev vligygtqkk envtgsigiv
       61 sakdladkpn anplssvqgk lagvnitnig tpggsprvdi rgvgsltgnt vfivdgmitt
      121 disylnpqdi esmsvlkdps slaiygaqaa ngaviiktkt gkgkpvynvn syigfkkvtn
      181 ipkmvntdqy ielyneklin dngssagsit ranfpadtdw fneifrtsii nandfsatgs
      241 lgklnyygsv gylqdqgnla agqginsgsg fnrfntklnl sykitdniti gnnfsfskmr
      301 tdvaqnplld aynappifsv mnpntgdyqf fngysipnpr akldmyrsqv rqerllnniy
      361 gelkflkdft frisystdny spsqyeytpt ltyvpaanqv pstlvtrnyr nrnyvwdnti
      421 nwkksfgnhn fdvlagfsrt rttlsqdyws srgvqydgtn gslnvgngtd qvyvsgidrd
      481 davvagvdqd qqriesffgr lnydykgkyl vnasirrdas sqinvdrarv fpavsagwvi
      541 sredfmseqn vfnllklras ygelgnpnvg rgfnqnisii gggayfgnsg ypaatidqfv
      601 dteigwettv gkdvglemal fnnklkidaa yfdkdsknvv ynvfqgtvsg aanwnafktn
      661 aysfnnrgfe vsvnynakln envsfgvygn ftslkneits vyggsyletg aslfgnsivr
      721 lqtgqpvgay ygydvagvfq tdaeaaasgq agakagwfkf tdqdgngvid srdktflgsp
      781 ipkgtygfgv nfniyavdia vdfqgvfgnk iynynrerrf gnetwdldmy enrwhgagts
      841 ntnsmitsnq liiapnsfyv edgsyirirn iqvgynlpks lanalsvtkl rlyvsaqnpw
      901 tsfkyngfsp einntdrvqm gidnniypis aiytmgmnlt f
//
LOCUS       WP_102986114             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            diazotrophicus].
ACCESSION   WP_102986114
VERSION     WP_102986114.1
KEYWORDS    RefSeq.
SOURCE      Vibrio diazotrophicus
  ORGANISM  Vibrio diazotrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Vibrio diazotrophicus"
                     /db_xref="taxon:685"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54498
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp ssvqqlvklg fevsieshag dlasfdnasy eqagakivsk
       61 devwnselil kvnaplsnde sdeialikeg atlvsfiwpa qnpelmekls tksinvlamd
      121 svprisraqs ldalssmani agyravveaa hefgrfftgq itaagkvppa kvfvagagva
      181 glaaigaags lgaivrafdv rpevkeqvqs mgaeflevdy qensgsgdgy akemsdefnk
      241 kaaelyaeqa kdvdiiitta lipgrpapkl vtkemvdsmk agsvivdlaa anggnceytv
      301 kdqvittpns vkiigytdmv grlptqssql yatnlvnllk llckekdgni nidfedvvlr
      361 gvtvvkegei twpappiqvs aqpqakpqkv dpkaakveep tspakkiigl avgvgafawv
      421 asvapaaflg hftvfvlacv vgyyvvwnvt hslhtplmsv tnaisgiivv gallqigqgn
      481 gfvsflafia vliasinifg gftvtkrmle mfrkd
//
LOCUS       WP_102994739            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudotamlana
            carrageenivorans].
ACCESSION   WP_102994739
VERSION     WP_102994739.1
KEYWORDS    RefSeq.
SOURCE      Pseudotamlana carrageenivorans
  ORGANISM  Pseudotamlana carrageenivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pseudotamlana.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Pseudotamlana carrageenivorans"
                     /db_xref="taxon:2069432"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117574
     Region          25..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskfsgilt lllalfvqlt faqektvsgm vlddyslplp gatvlvkgtt tgtstdfdgk
       61 ysiqanegdv ivfsfvgyst qeitvsssnt invtlqedae sldevlivgy gtstlrsftg
      121 satqieaeal drktvsnvsq alageasgvr vintsgqpge datvrirgfg svngnrdply
      181 vldgvpytgs inainptdie sttilkdaaa taiygsrgan gvivintkkg srgkdeield
      241 irtgqnfngl prystisspe eyigisweal knrgnaings ggedyanqrl fsssginpay
      301 nmwnvangae lidpatglvr ngvtrkynpe nwedyafqas lrteanlkis ggtdktryft
      361 sfgylndngy sinsdykrys vraniehkak dwlsgslnig ytnstanngg qsedsgsvfw
      421 fvdnipsiyp lflrdadgnt mpdphyggni ydygegrgfg gltnaiadah nsisrsfvhn
      481 lngsanidis fnddlklink fgwnyynsdy tnqegpfygp sagqngsifk rrtdifsynl
      541 lnmltfkkkl dghnfdalaa heindwnrqy lygsknyltd pdgtdwndai iqtpmssfne
      601 gyslesffgq lnynynetyf lagtirrdgs srfkkgnkwg tfysfsgawa lsnedfmskq
      661 niftflklka sygkigdqgg vgfypgldly svgnlddkpt lvfdskgnpd ltwetsnqfq
      721 tgvefslgky ldasvdyyik dtenlifdrq vgpslgyaii kvndgslrnk glefdlnahl
      781 vktkdfyldl gingeiasne ltrmpidpat geqkvldiqg rygravghsi ydfymrewag
      841 vdsetglgqw nqyyydannd gmvnsgeeik sltdylaqyp dragnisktt tttyadatqk
      901 fidksiipdv rgavnlatgy kgfqlnvqfl ygiggyayda vyaglmdndv iggnnwhtdi
      961 rnrwqkpgdi tdvprltsdl dpnvaststr fltkadylsl nnirlaynvs qdfvekmgms
     1021 nfsvslsgdn lgiwskragf npsssetgls dtytysplts vtlglnvrf
//
LOCUS       WP_102994970            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudotamlana
            carrageenivorans].
ACCESSION   WP_102994970
VERSION     WP_102994970.1
KEYWORDS    RefSeq.
SOURCE      Pseudotamlana carrageenivorans
  ORGANISM  Pseudotamlana carrageenivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pseudotamlana.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Pseudotamlana carrageenivorans"
                     /db_xref="taxon:2069432"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118517
     Region          25..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlknklalv vmllfsitai aqsgivlkgt vasvedgipi pgvnvivvgt trgtttdfdg
       61 kyeinveqge avqfsylgyv sqtklvngsd plnislsedv sqldevvvig ygdqkekdit
      121 saltkvdakd iqdysvarve dalqgkvagl riqvttseag gdpkitmrgp gsitgssapl
      181 ivvdgvvlgt dpdilgsidn nniaslsvlk dassvaiygs rgangvilvt lkegvegqtk
      241 fsyntftgyk fatknknfnt tiaqersrln slqgqvsaid psspryvdvn ryydtayael
      301 eamefiaslg ggetnwqdei fnggvisshs lsvrggtelt sytgsigyle degivltdnf
      361 kklnarikid sksknkkikf ganisanynd qvrvptrftd plrqyghlpl rlneehmkyv
      421 tqgdpgdagk qfenigvgsy gfsrafdhvf tvdpnnprai nrdpvtglpt vspltsgglt
      481 lsttknvhpl vhylerdrlk kklnlntsay mdfklakgln frqtisgvfr hgknnnndyf
      541 ygqenrdqea frlesrdeln qyaiesllky nrsfgkhsfn svlgfeftqr nfyfqsteav
      601 gytddfnnni aiadggisyt dngtdklvsy fgrvdysfde kylvqlsart dgstrfgtnt
      661 rfgffpaasv gwilskedfl snsdvisflk lrasygisgs neidnnifns lyrfeeafst
      721 isyngltgvk aitlanqdlg weqlvefnpg vdvtfgrsll nlgvdyytrs skdlilfapv
      781 sgvygtdnwl qnigevkneg veievssrly tsenmswkas gqfalnrnev vslgkndqil
      841 sridqdtrpt efiarvgqpi tsfygwvyek emplewvdnp fnrfnndfah vyvkdlngdg
      901 iidgedrtel gnpypdftwg fnsdfsyknl dfsfqwqgsh ggevrvadld qmyyasesav
      961 navsnfpdrd llvhrrytdd hiqdasfial rnitlgytip esftskysid rlrlyltgen
     1021 llfftaadye gfnpeaagqt sdnantplta gyqrgdgpvv rtisaginfq f
//
LOCUS       WP_102996498            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudotamlana
            carrageenivorans].
ACCESSION   WP_102996498
VERSION     WP_102996498.1
KEYWORDS    RefSeq.
SOURCE      Pseudotamlana carrageenivorans
  ORGANISM  Pseudotamlana carrageenivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pseudotamlana.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Pseudotamlana carrageenivorans"
                     /db_xref="taxon:2069432"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111524
     Region          26..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqnlqklfl fsflvfvvqf sfgqekeikg tvtskadgip lpgvnvtvqg ttngtqtdfd
       61 ghysltvnvg dvlnfsylgm ttvsktvaqq evinaqlved aqqlnevvvt algikkerka
      121 ltysaqevgg deltrvkqtn pinslsgksa gltitrsssg lggatkvvlr gntsttnndp
      181 lyvidgvpml nsgngsngne pgtdifgsqt gnrdggdals linpddiesm tvlkgasasa
      241 lygsqgangv ilittkkgke galsvnfnss ftvdnvmslp nlqadyqsds vgqpiaengr
      301 vadakswgak anglsndase fftmgytain alsltagnqk aqtyfsyant lgegvlpgnn
      361 lkrnnltlre takflndkis vsanvnlsdq risnrptngl ysnpltavyl qpvgisrdiy
      421 knkfeyfntq lnqmdqyass fdeniqqnpy wlinrnpsed iaqrvlanvs vkyqvteafs
      481 lqsrgsydkt fytfdkrqya gtdpvnsgdn gryvlekten tqqyidfias ynkdfsedft
      541 fsgllgtslt kyrigdqvyl dsgrdgagln ypnvftianf attnnirqtv gnrevqsifg
      601 sanfgfkdml fldvtgrtdw sstlvntdsn sffypsvglt avltemfdmg dgisfakvrg
      661 syaevgkdip vyatiplnai nntntgigta pfapiegetl eperqkgfel gtewrffgnr
      721 lgldftyyds ktenqifyiq aapnpngysq nivnageiss dgieivlngk plvsdkfewd
      781 tainfaqnnn kvvavhpslq dgeavitarg vngyeyalie gedfgsikar slirdengtp
      841 vintsgtlms tdfetvahaq pdftlgwnnn fvigdfnvnf lidgkfggdv msvteavndk
      901 ygvsqasada rngnggmvnv vdesgaasqi saqeyynaig grdgmlgeyv ydatnvslre
      961 vsvgyklllg esdfidninf siiannlffi ykdapfdpni aastgmglqg vdiynqpstr
     1021 svglninvnf
//
LOCUS       WP_102996228            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pseudotamlana
            carrageenivorans].
ACCESSION   WP_102996228
VERSION     WP_102996228.1
KEYWORDS    RefSeq.
SOURCE      Pseudotamlana carrageenivorans
  ORGANISM  Pseudotamlana carrageenivorans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pseudotamlana.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Pseudotamlana carrageenivorans"
                     /db_xref="taxon:2069432"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117892
     Region          42..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mneqkpkikp kikwnfsvpg ftillvills sfsvinldaq nkitgtvtgg ldnmplpgvn
       61 vvekgtrnga vtdfdgnfsl qltsvsrtlv fsyigyktqe vvigdstsia vqleedtatl
      121 devvvigfqq vkrekilgav dtvksesinq aapvdalqgi qgkvagvqit sdngpgegfd
      181 ikirgvstft agatgplyvv dgqqtfdidn idpsdiesle vvkdgataai ygaqagngvv
      241 iittkrgveg kikldvttit gmnqlvgdlp apnaaqrleq errqgitwgp iardslslvt
      301 rnspdlqklv trvgirhqtn valsggsdkm sfywnngffn eegiilnsdh krintrlkid
      361 atpndkfkfg tlinmsyeft nstnpgpvlg hllnrvaylp iyepdgsftp gspnkqslnp
      421 iqnallrknd rrryransfs yaqfqilpsl sirsqfgvdf syekfegftp aildarnyan
      481 ginsgserhl lrygiqqdnt lnfnqswgkh dvsaflgmqi qrdtyenlnl sanfandlie
      541 tfnnslfadv dgnpldivdr tggdrtqntq tglfslftgf nydynnkylv gatfrrdgss
      601 sfggnnkygy fpsatlgwri skegflknss iisnllvras ygivgndrig pydflttlap
      661 gynyegqtgf apfslgnedl rweetesinl gfdlslfkgr rlnlsldlwe kltdgllvnt
      721 elpeesgfsv vrenkavvkn rgldftlsgt ivqnkdfswr ssfnlgllen kvleleddiy
      781 qgrfvttegk pigniwgykn hgvfqydesn aftpegeqly pnydangffe gtynrangdq
      841 yplgadikql thgssgntlr ggdyywddvn gdfvidsdde qilgnglptv fggfshdity
      901 knwsfetlfd ysfgndiyrr ydhdrnslra avlsvspgrl dnawqnqgdi atypaleggn
      961 trvqnrfdft gatanstyvs dgsyikwryv rfgysfpqev lenlnigmtg lklnfsvnnl
     1021 ltwtnypgyn pefgsrgnpl tpsedslryp ndreilltlr aqf
//
LOCUS       WP_103002575             882 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Hoylesella timonensis].
ACCESSION   WP_103002575
VERSION     WP_103002575.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 882)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 882)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 882)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..882
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         <1..882
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          2..881
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 traafgvili qtkgahpaer ttvtynnnfs wdqatylpdf vdvptrlraa legmannnky
       61 eveafgmyfd kllpyaekwk qqnkgrldyq emrkyvddnn vgdylmmgnt pyyyanwdin
      121 kiyftkaaps qshqlsvqgs ssktnyylsl aydrkegllk lhpdkldryn asvnvtssvt
      181 dwlqvgarin ftrkqykhpd twnktyqylw rwdasflpsg singldhrtm ailkqasder
      241 vttdfsrlna flranltkem sfyadftyai qnmnsasedf svyginwggi kpgyivspsq
      301 tgvwrdnsks ntwtlnaymd ydkswgnhhf kamagvnaek sdyiylygkr sglfdegmpe
      361 lnlasqegqd ikwahsemas agyfgrlnyd ykgiylleln grydgssrfp hnahwaffps
      421 asagyrfsee ayfeplkkvv sngklrasfg eigneaigdy mfeelinqtn sryvywvgnn
      481 ianankltmf nmpklvansl twerirtidl gldlgffnne lmmgfdwfqr enrdmlapsq
      541 vlpdvlgtaa pyqnagtlrt rgwefninwn htfgevnvya nfnlsdsktt vqewrndakl
      601 lntnysgkvy gdiwgfetdr yfeesdftgq ntdgtwnyaq giasqkgleq gsfhygpgdi
      661 kykdldgsgv idggkgtadd hgdlkvigni lpryeysfhl ggswkgfdld lffqgvgkrd
      721 awtisslnfp lmrgadlavy shqnsynrvl yssdwktikg yeinqanryp rlfpdndvag
      781 tvsginngrn nyypqsryli nmsylrlkni tfgytlptal tqkayiqrar iyfsgnnlfl
      841 lhkghdlpvd pevntgegel yggwgrtapi trtfsfgvqv tl
//
LOCUS       WP_103002580            1159 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_103002580
VERSION     WP_103002580.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1159)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1159)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1159)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1159
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1159
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127169
     Region          43..1157
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkvincsas vlliavlaal nlpihasner fveavavaqq ngtcsgvvkd ntgevivgas
       61 vrvknsslga itdldgrftl pnvgkgtvvv vtylgykpyk fvydgsrkvi eitlvnddkt
      121 lnevvitayg mpkqakqvgy attkvstdei erinavnpvn alqgkvagvq intagasgvt
      181 sssaitirga ksidknnapi fvidgmiiqe pltgnlsgtd wgsqlknlnp adyesvtvlk
      241 gaaatalygs rgangavviv skggkfgkrg lgievsqsie mtdiykspid lqdvygagtt
      301 fngyqggfla dgslqrtpns fgprmdgqli nqympdgqkt pfspkpnnwk dlyktglnnn
      361 tnvaisggge kssfrlsygf mknngvfirn sfdrhnvsfk gmtelnkvfs leigfkyafs
      421 rslnggsqgg wdwgnnvgmi saynlprnmd iahyasmyrd pvthavests pwgslrgylh
      481 trdtsvrqrs eqsiladvtl ranimpwlka slkanynyyg vnyeerqygt gpdygptgag
      541 yygrsgsteg synflamlns pdnkftigte eltlsgivaa elygntprnn wakgtngglv
      601 ipgvfafsns tnkieptfdy mpanqrtfgi ygivnlgwrd qvfleltarn dwlstltypt
      661 yitngknnyt vfypsanlsw vfsdsfrkdl pkwftfgklr asiarvgmgt sayatsngyg
      721 vfdqrsiykp dksgsvlsat pnlgtmfndn lkpeiqqsie lgadlrffde rltldfayyk
      781 tntfnqimrv gsvseagass qlinagniqn sgveiqmdvt pirnkdwrwt vggnftlnrg
      841 kiveldehvk ewqlmggyda apeiwayegg kfgvltsyln spystpvahf egpsgdprng
      901 kmlirydqqy gkphsvamys pvtlydqgkr eryilgkvep dftlslntsl swkqldlyiq
      961 gdgrfggnyy snlwkytvpr gnlkstlvgr dkehggiari nykgetvydg lmldavfeeg
     1021 akapvqnadg tpgalvdvgg mtyadaiaqk nivpvmtgsw yawnygwgmp afpeaiqdnt
     1081 wfclreitlg yrlpekickk fganylrlgf tarnvcylin kltdglnpms issnnplqpm
     1141 digavpfyrt yafnltvrf
//
LOCUS       WP_103003006            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_103003006
VERSION     WP_103003006.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121273
     Region          25..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllflmvc fmscttamaq taihgrvlde gtnepligat vveqntsngt vtdvdgafrl
       61 tvaklpvsik vsyigysekv vtvtsaqplt irmqdisnel setvvigysg siirskmtns
      121 iakvkneslt tgmfsnpsqa lsgavaglkv vqgsgnpnas ptivlrggtd ydgsgaplvv
      181 vdgmirssma dvnpndiqsm evmkdagata iygsranngv ilittkkgkd gegkigfssk
      241 lswnyfnnpy kfldagdyly yqrrsylyak qkgtvtlssl sgnqpygtgn kyeadgnkss
      301 agiwgvyeyg alapdvqkel igkgwrtmtd pvtkktliyv nnhmedfnin tpsfsqdyni
      361 nfsggndrgh yytslgynns egnainnynr rlslllntdy kikkwltsys sfnfstakyq
      421 gispfagean yfsrnfsypp tfraynnkge lllgknsgdg nqkflenaid qdysrqkftf
      481 sqdfrfsivd gltldlkgdw yyqyytgqsf yhtylsspgr ystghksfae sekhltqtyn
      541 vllnynktlg khtvsgllgw eyfhqklfdl qasgsnpann yfrdleytvt degkrmvdtg
      601 hskfitqsyf arvnydydak ylagitvrrd gisklskdnr wgtfpglslg wvfshekfme
      661 ktagwlsfgk vraswgkngn vnsswvgdyt vqgayamdty hgttsyylnn iptayltwet
      721 srtlelgldl gflnnkiqan itwydrvtsd kyanivipas sgftsitsnn gklrnrgvel
      781 etnchilnta dwkvdwafni arntnkilql pdngrdknrq ggyevytgng dkkmwvggya
      841 enetpgdlwv fqaegiykty deipgnlidk stsnnggnnk ylygpaayqs tgkaagglai
      901 mpgdikwkdv ngdgvidnyd lvkvgnmtpk wtggttltas wkglaltarl dfalgfktyd
      961 yrtpwimgnm qgtyntltnv kdtwsednpn akypiyiwad qlnarnydry nsmfvyngdy
     1021 lsfreltlsy slprqwlskv siesltvsvt gqnlgylcaa pyvfspevas nwggyplprm
     1081 lvlglnltf
//
LOCUS       WP_103003232            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_103003232
VERSION     WP_103003232.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121453
     Region          24..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkktiymli allacvlqvq aqervitgvv ldgdlkdepl igatvgkgvg kvstgtvtdy
       61 egkfklsvgk dtkaisvsyv gyttqtislk pgvnhykill mpdahsinev vvtgyqridr
      121 rkltasvttv disdkavgav knidqalagq iaglstvsss gapgapvkir irgtasingt
      181 qeplwvldgi plegtdipsm enlndiddmy qtsiaginps dienitvlkd aaataiygar
      241 aangvivitt kkgkegrpvi nfsakytysp klnidrlnll nadekvdlel gllasdytyr
      301 ehkgevanil ktlnetevyk regrnalsal aqtqinalrn ihtdwndilf rhamnqeyna
      361 siaggsnrsg yytsvgyyde qgnvkgvdnk rfnmtlkady rinkmlklga svyanqrkqn
      421 syltdtngft npvyysrlan pyflpfvdgk yhydvnvqgk edssldfnif eerentshkr
      481 tdrslmaifd gelqftpdlk ltsqfglqyd nyslekyage nsfamrkehf natyaykdgk
      541 rsylpeggmh kttsynslqw twkalleyah rfnkvhdvel lagtevrhin sssvysaayg
      601 ydartltthp vifpnettae srplhrenqa ensyvswfat gsytlfyryt lggsvrfdgs
      661 dvfgvakkyr ylplysvsgl wrvhqerfak kakwlsnlsl rasygiqgni dkntspylig
      721 fydktsilpg kgeqmikaet apnpdlrwek tknvnfgvdl glwnnaitls adyyyrrssd
      781 ligmrmlpqe tgfsattinw asmensgwei algsrniytk nfkwttnlnl gfntnkilne
      841 svaenstyps regypvgalf ayktagldkd gyplfvnkeg hkvtaaellk lnnagastls
      901 aseqralyty mgttdpkvsg gfinhfeykd wqlginfifn lgmkvrvqps ynpttydrgl
      961 nvnrdilqrw tpnnnqttfp klmtkdvrvp ehiqyseynt ysmldtwvkd rsymrlqslr
     1021 lgyklpskwl nkvgvtnasl slegrnlfvv atdytnyldp etmgnpfaqp maksvifgln
     1081 mnf
//
LOCUS       WP_103003800            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_103003800
VERSION     WP_103003800.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123866
     Region          24..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrltmllv slflcvglan aqtqingtvt sgddgqpvig asvmitgtkt gvvtnvdgkf
       61 sltsnkknpm itvsyigmks qtlrgtqnmq ivlqsdaqkv devvvtgmqk mdkrlftgaa
      121 tkvdaekskl dgvadisrsl egraagvsvq nvsgtfgtap kirvrgatsi ygsskplwvv
      181 dgvimedvte vnadqlssgd aatvissaia glnaddiesf qilkdgsats iygaramsgv
      241 ivvttkkgta gkthinytge ftmrlkpsys qfnimnsqeq mgiyrelean gmisfgrthr
      301 astsgvygkm yqlmntydpt tgkfllpnte dgrikylqaa emrntnwfde lfsnavsmnh
      361 sisissgtek aqyytsfsmm ndpgwteqsn vrrytfstna lynmskhlsl nlignaayrk
      421 qkspgamnqh vdnvtgavtr dfdinpysya intsrtldan efyvrnyapf nihhelannf
      481 ndydvidtkv qaelkykpit kvelamlgay kfstttqanq ikdnsnvala framddatml
      541 ygnqrlytdp dvpnslpfsv lpnggfyret kykmnswdfr atasyndvya ndhivnlfgg
      601 mevnntdrnr syfngvgmqy emgllgsydy ryfkqsseen eiyydlsngh srevsffgtg
      661 tyswkgryti ngtvryegsn rlgkarsarw lptwnisgaw nmheepwfek afknslthat
      721 fkasysltgd kpavtnaavi iqsynpwrpf tvdkesglei wdfandelty ekkhelnlgm
      781 dlgflnnrin vtfdwyrrnn ydligpritn gtkgtiveya nvasmksnge elsisskniv
      841 skdftwntdf ifshvktevt slknrrniiq mitgsgftle gypyrslfsm dfqglnengi
      901 ptfinengek ttsgiyfqsr niehlkyegp vdptytgslg ntfsykgwhl ivfatyafgn
      961 kvrldpafys wysdldatpk efrnrwtkag demttnvpai pdlrqrqkdq rlsyaynayn
     1021 rstervakgd firmkeisls ydfpqrwany lhlnkvnlkl qgtnlfliya dkklngqdpe
     1081 ffnaggvavp marqltmtlr vgl
//
LOCUS       WP_103004041            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_103004041
VERSION     WP_103004041.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113887
     Region          25..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkalfilfl iflscvsira qqkaingnvv drngnpiewv svvvkhtnvh tttnqtgayn
       61 iiasvgdtls fsiigfdkeq rvvgksnrmd imlheskdvv ladlivtgys kqerrdltgs
      121 vasvklddnv sfrsvdqmlq gkapgvfmtt ssgalgsanv ltirglssii gdnnplyvid
      181 gvpiygtdrs anstdvsgga ipaasmmgmq tgggslqynt dlkysfeknp latlnpddie
      241 sieilkdafa taiygsrgas gvvlittkkg sqarprvtvn ytlgvdnplg klkllngkqy
      301 aqiysqyfng mnfpelydtd widavtrtav shnvsasfsg gtqktvyfls laasdndsyv
      361 innnmkrysa rlslttaiss kldlgvnvsi srldnnalqa peifasaikk apnlpiyded
      421 gayyygyapn skgdpetynp vaqayindeg sedtrtigna ylewhpmswl ilrseigtdl
      481 ynsfssirkg alpdhvkgva gnqaqetttl ntkyvvtntl nvnkvfgdhf mqgivgqsye
      541 ytrerlnava gddffspdlv gvgaarskrv isaysqqsal fsafarmnyq yrmkymlglt
      601 yridgssrfn rshrylgtps vsagwrmsne rffrkalpfi nqaklrasfg vsskdgnnsy
      661 ygaqatykln savnygdrny lqmsqpgndn lnwehtltwn ggldleafks rlkltldyyy
      721 kkttnmlfps nlplytgykk enqniadmmn sgldlqiise nivgknfgwq tvlnvstttn
      781 kilklnfegn qldqlnssfk yyqegkaaaq wylhrwagvd pdtgdplwty adgtqstvpp
      841 aannetsqln kfvcgtalpt vygsisnslt yrnfeldiff nyalgshmin atratmltyt
      901 qnatnlskem mnlwqvpgqi tdipklnnas iigaydytta vtsdrflenn sylrlktltl
      961 syhvspallr ryklcrqlri yatftnlftv tgysgldpev safgssvtas gydnctmpss
     1021 rsmqfgvsat f
//
LOCUS       WP_103004015            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hoylesella
            timonensis].
ACCESSION   WP_103004015
VERSION     WP_103004015.1
KEYWORDS    RefSeq.
SOURCE      Hoylesella timonensis
  ORGANISM  Hoylesella timonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Hoylesella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Hoylesella timonensis"
                     /db_xref="taxon:386414"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121982
     Region          31..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkallffc fclislaiva qnpqksdamv qvvttitdtd gnplggatvk vkgkpvgvia
       61 dmdgkislwv drgntitvsy lgmksktikv tsaltknivl endaslleqv vvtgytrttk
      121 rrttgsvsti takdlnknpt anldmllqgk magvdvkals grpgesakvr irgtntitgn
      181 adplwvvdgv alqkdlptis kaqmlsgnfs difsngiagi npndiesvtv lkdasaaaiy
      241 gsraaggviv vttkrgvagk lrinysanat mvtrppravd lmdskeklaw eqelwdeysk
      301 pyfekneryp vvgivgmirs gygqykgmnk eqqdaeiarl gshttnwfde lfrnsvsqsh
      361 nlslsggsek stfyvslgys enaglvkktd ysryninskl dikpnkrvkl glsldlgwqt
      421 snspslavdl fkyayfanpy ervydeqgny aadqtyynim langskstlp lpdngvnimr
      481 einntssktk nfsttvigni tiniidnlnf eglgsysytt nngdnindkd tytawqdrpf
      541 dlktltskrt yssiaqsssy nssynlrgql hyfntfndkh yisgllgsei rgqyaksifa
      601 krygydpvsg nsampvypeg ktfeyndlkn yallmdnlsg qnivedrfas fyfsadyvyn
      661 nryvfsftgr tdgsnnfgsk eqfnptgslg lswnvdqesf meklkpiiss lslrtaygft
      721 gninksvhpq vimdyrqsfr ktdtdyyrmg wikkapnpnl rwektkdmkv sidagflndr
      781 irmtgeiykr itsdavsevf ipystgfrnq sfntsklsnt gaeftlsanv ikqddwnlli
      841 sgniaynrnr lleyksivsg lgegiyvgyp igsifsgkva gidsrlglit yeprpdavfe
      901 tsadrnnaen ylfylgtsna ptnggysmsl sykrltlsls gtyslggkil nqinspvgyg
      961 slsgtpvekg lsqmndlyvn hlnvtrdvvn rwttknhrtd ahprildayg kyygldnyvv
     1021 sspkitkasl ledvsyfkig slnlaysfdt kliqriglss lsvsftadni ytftnysgid
     1081 pespgavypm arsfsmgvfv gf
//
LOCUS       WP_103015443            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_103015443
VERSION     WP_103015443.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114322
     Region          29..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrysvlllg vllgalcfsp tssaqdpatv rgvvtdstga plpganvrvq gtqtgvsada
       61 dgayelaavr pgrrtivfsf vgfekvsrtl elsagdtrtl ditlgtgtvg lenvvvtalg
      121 vdreerslgy svervsgsdv aeapepnvmn nlsgkvagln vtggsgglas tprvtirges
      181 slagsnrpli vvdgipidnt pntqgsdaqt tqvdfgngls qinaqnisem svlkgpsaaa
      241 lygsraadgv ilietkdgse tdgigatvrt svtasrplrl pdyqneysyg nggefayvdg
      301 tnapgwnwgv rmdegverpq wqgprneage liptevtsap nkvrnffntg tnvstdvavr
      361 gggenssfra slsrsdrtgi vpntnldrts tslsasydvt daltvdanan yanttsdnlp
      421 ssgygsesim yyftwgarhv endllkdywq eegtqqahyd rnwtnnpyfq vnentngler
      481 drlyggvsar yeftdnlnlr artgldysnq gtkqrkafss itapngwlqe adrtftewns
      541 nlllnytrev gdftfepsvg anfmrqtrrn vqltaqalsv pdvynignar snvqaderde
      601 aqeilgvfas gtvsyqdmlf ldltgrndws stlpldnnsy fypsaslsvi vsdlvevpef
      661 lplsfakvra swaqvgndtd pfrltntytf gdawgstqtv vseadlanan lqpeitssye
      721 fgtnlrfydg raqldvtyyr sttrdqilsv plaqstgyns rlvnageirn tgvetrlqls
      781 piqdwsgfgw dvslnwtrnr stvveladgi dtfvlgegpf ggsaqaregg rmgdiygrvf
      841 drvedpnsph tgeiiyedgl pqltddvekv gnynhdwrgg igstfsyenl qlnvlfdvrk
      901 ggllysntha tgieggsleg ttrarnetvv gdgvvqnddg tysenteeae yvtwlrtyyd
      961 rpnvesnsfd atyvklrels lrynftsdwl tragvqnvgv svtgrnlflw tdvphvdpet
     1021 tisggdgqip gfevqqipst rsfgmnvqln f
//
LOCUS       WP_103016555            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_103016555
VERSION     WP_103016555.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109419
     Region          27..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlipsvaf glallllpgl awaqqgtvtg tvteaetgep lpgatvqiad entgaasdae
       61 gqyritgvpa gentlrvsfv gyqdqertvn vpaggtvrvn fqlrtsqaql eevvvssyav
      121 eedarvtgas esvsgediat qdvqnvsgal qgrasgirit sqsgapgsaf dvqvrgqsti
      181 sggtqplyiv dgvqvgpeni seesnlspla gltpsdvesi qvlkdasata iygaraangv
      241 viietkdggg etqvnfnaev gsvsplqqfn ilsasewaeh eflkaenagi ppaavanafg
      301 ipstnpeevs gpnwydqstr tgitqsyqls vsggneqtnf risgtferdk gqviqsflnq
      361 agvranvqhd vtddltvssk lnaiqnksrg tigggafins pfwasylirp hlkvreedgd
      421 ynlpleggga fnrnivaqed fntqstdgvq llgdvsatwe itdwlsarti fglnfndlse
      481 kdrrdprlpn nagiggsafv sdtreldqnf sqtlnynlsp gerhditglf gaeyrrqktq
      541 fvgadgegfp lfvfqnlnna atpagvnefe tesrflgffg daqytyddry tgsltlrydg
      601 ssrfgedtry glfgsvggsw siseeafmee vgfvealelr gsygvlgnsd fqdafgnfaa
      661 rrlyggggey sgtagiqpss lgqseltwee stqinvgldy svfggrlsgs fnlfrndtdk
      721 lllgrdlpad sgfdtvldnv geirtegfei afntvnvdrg gfrwdtefni tfqrsevlsl
      781 fdgreelrnf qqpggglyrv geplgqyerv pwagvnpang rplykdedgn ltyfvggqsa
      841 eetygnnlsd yyggfgntfs yagltldvff qfdygrntfn ndryfidgnf nfnhtenvte
      901 dfwqkpgdvs erplpwfgnr pggtgynsgf fnssvymena syirlkqvrl syslpsslvr
      961 gigiqnatiy vngsnlatft nytgldpeiv gtaiaqypnn eritgginvt l
//
LOCUS       WP_103016559            1093 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_103016559
VERSION     WP_103016559.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1093
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117916
     Region          27..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfrkllsvlv glllllpatv laqdtgtvsg tvidsttsqt lpgvnvtvqg lnigaatgpn
       61 gqfeisgvpa geqvlqasfv gytrknipvd veagetttvn vrlapqavgl edvvvtalgv
      121 ereeravsss vqqvdgadld atnnanfvns lrgkvsgani rssstmggss nivlrgyssi
      181 sgdnqplivi dgivvsnrsr qsgggtvegn ggfdfgnaas slnpsniksv svlkgpsaaa
      241 lygsrgangv iqittkdgsn lddeigvsfs ssvsmsqaye fvdyqnkygg gapsstfstl
      301 dgdfkkpdgd qyvvqyavde swgprldgrp vrqwyswddv nglegeatpw eahpdaienf
      361 mdtgavftnn valsqqtesl nyrlgltsrn qgsvmpngsm dryqvnfngs vdlsddlrat
      421 tfvkysyqdv karsgmgygf eenpfaafnt ftqrqldygp dsymrdyqra ngqqrgwnya
      481 gvsgaqgpvt qfqytdnpyv nryanfqqdd eqrllgkaev aydivpnltg tatvstdfrt
      541 hrfsdrrsdi stgapgsfse dvieeqetrs slrfdysrsl tnqidltsfv agqvryetye
      601 qnlgstqngl aspdvftlqn svgrpdveet fqesmvysty glvslgyqdi vflegtlrnd
      661 wsstlpadnn sylypsisgn liftgldalq dqdilsfgkv raswarvgqd tnpyrlgvty
      721 pgstpfqgqa lqnvqrsann pdlkperttg iefgadlrff nervnlstty yrdvtkdqil
      781 avdvsgasgi esslinagev snrgleaslt vtpilqedlq wdvtanfnkn vnkvvdlaeg
      841 ldtynltagg vifgptiqar egkaygamvq pslrrdangd vvfqrngvpr ttsspqvvgn
      901 fqpdwtggls ttvsykgvtl savvdgqvgg dvyslsnkfg tysglvestv adnqretgvi
      961 pggvvvpeda tpnengnydv egtdfgeavg ripsasywkn wfsagggdqf iydathaklq
     1021 elaityslpq rwfndfalrr asvsltgsnl mflykeapni dpsvtlgagn vqgvesaqip
     1081 pqrqytfrvn lsf
//
LOCUS       WP_103017093            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_103017093
VERSION     WP_103017093.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109310
     Region          32..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnryrpafa lllagvlali svgpavaqte ytiegqvtde stsevlpgan vqiegtnfgt
       61 atetdgefsf taqlqpgeyr vrvsfvgyet atrmveltdq evvtldpfql gvsaarvdev
      121 ivtgqagpte rkelgnaiss ieaaelqdtp ksstlqslqg klagvrvqqs sgdpaggtdi
      181 rlrgtgtvlg aasplivvdg viisndspel iqvggttqnr lidinpndia rievvkgaaa
      241 aalygsrann gvvqiftksg qegetevtys trvktqavrk tldvnmaqne qgqfldnsgd
      301 plpegqrrfd fqdfifdray gteqylsisg ssgdtrffts ggylgsqgiv desgfqrfng
      361 tvrlqhtvnd wfnvsagary afsksddvpn gglntlygal tgfifgpntf dprpneagef
      421 pddaafsnpl evqsrfdfgq ttdrfigdiq ldltpfdgls idytlgldty dqtgtafipr
      481 gvstpgfetg fsrraelsnl qlnsdlnvry easirdglts tsliggtlqh eseesfnaqs
      541 qdlppiaetv gggtssrefg efrspltvyg vfgqqsfgla drlfvtgalr ldasssfgeg
      601 drwqlypkvs tsyviseqdf wrgaigsvlp sfklrgsvgw sggltsigaf drftvynaqs
      661 fdgnpglqpa sqlgaqgvrp erqreievga dfslisdrls veftyynqrt edllltksla
      721 pttgfntela nigtvenngi elrargvaln rsdvrwvstv tyarnrnevt gipgetgrvi
      781 ipssfrvsaa qngepigsyf ggafarnedg evidtegnpm redddgywrp kncdvsesgc
      841 sgiparaeqd qiignpqpdf tlawanqvev gdnlsirfqv dgefgqdvfn ftrrigafps
      901 fgtledyere legdlpsgyg sgvfnifenw vedgtyvklr evavnytirp galpvesvrf
      961 naagrnlfsi ddysgydpev niggqrtgvr gfdfvvppvp rtfslgatit f
//
LOCUS       WP_103017096            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_103017096
VERSION     WP_103017096.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108201
     Region          30..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhnrlirhag twlallvllg wpvsavaqtt vegtvidaea gsplpgvnvr vqdtqigart
       61 dsegrftvel pegqrtlvfs fvgfatqevt vpegeteiqv amesdvvgid evvvtglass
      121 vkrenlanav tkideediag tvepstldga lqgklagvni tsqsgapggg invqmrgist
      181 lgagssqply iidgvyvnna qistgrssvd gaggasqdna anrladlnpd eieslevlkg
      241 psaaaiygqr anagvviitt ksgeggdtrv nfsqdlgavs alnllgvasw sedkidriyg
      301 egtpaaarek erfnearrng nltnyeekly gntgltrntq leisggnqqt qfyvsgglkd
      361 eegiikntgf arktvranid hslsdrvrvs srsnyiqtss drgftgnqns tggsvgytla
      421 ytptyaqlqq redgsypdnp yfaenplrlv neatnnqevn rflqsfslna dllqtesatl
      481 sldlnggldy lnsnstvyfp pffqfqqaqs npgdviqgke dnlntnmqgl lvynqtlesg
      541 agtfnlttqg gfsrftqden rqlvrgrgla pgqtnplngq iqeifsqqfv eivdigyvgq
      601 qevnwddkli gtigarfdrs tlnakqqefy fypkgslavn lhnfdfwgfd pvgqmklrta
      661 ygetgglpqf gdtfsalnsv niggglglta sqrgidpdld perarelefg advsaldgrv
      721 aleatyyrkt vddiildren pvstgittia tnagtlrntg velglslspi rrsnfswfsk
      781 tlfwqndsei tdltipaftt ggfgaalgty ytgegfsptt ivgtpatpdq evpftvygna
      841 qpdfqmsfsn sftlfqdlev sflfhwsrgg dninlsrfls diggttadwn edhdndgvpn
      901 gldrtdqfgp gaaqfvedas yvklreasiy ytlpssvlet afngvlrnar iglsgsnlll
      961 fsdyssydpe vsvfgtqpva qsvevtpyps srrltfhlel ey
//
LOCUS       WP_103017423            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_103017423
VERSION     WP_103017423.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113812
     Region          39..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mppfvssyss fkivltavfg vllacglpgg vqavhaqdfe vtgtvvsadn qsplpgvnir
       61 eagtsrgtvt gpdggfslav dspqdtltfs figyqtktvp vdgrseirvv letesqeleg
      121 vvvtalgier qqrsvgyats sieaqdlvdv tesnpanllq gnvpglvlss nasgpnssss
      181 inirgvssia gnndplfivd gvpidntvig gagkfggrdg gsalsvvspe nisdisvlkg
      241 agaaalygtr ardgvvlitt ktgrtsapge vsvqysstvt akdvisgfsd fqnqygqgtq
      301 grapsnqdaa lsaglsswga plgevdeapq fdgtvrpydd vadrqgfyrt glsqrhslsi
      361 nagfentslr lsashqnteg vvpnsgyeqt ninlrgqtrl ggltadasvt yqneltdnrt
      421 flndaarnpn ylisflpnni pksalqpgat eegvekqfts dglptnpywa vneleadddk
      481 drilgnvnln ysindwlslq gqtgldwysl rrtnvdafgs afepggsmte dtyrvwesns
      541 kllatatpsl tdelslrldv ggslrhrqfe qvgvfgrnfs ipdletisnt anptrnydfs
      601 eqqirsffgs asftyrnylf ltlttrsdws stlpednnpf vypsvsgsfv ftdafdlpda
      661 lsygkvrasw aeiggdtdpy rtsltygiig qhqgqaleti tqlsvplldl kptstreiel
      721 gfetqffndr fgvdftwyrr stvdqildvt vssasgytar tansgeirnt gvellltsip
      781 fstadwtwds rvnfaanrsq veslapgldv rvgpenrlat aniaqvvgqp anaiygntyv
      841 rddqgrivhg edglplsgek evlgtgapdw tlgfsntisy qnvsldflid akwggkvfsg
      901 tnanaygngl hkatldaraa cdeqagsngr ypedcfvgeg vigsvngege vtvdrendvg
      961 vrpseyygri sgeiaeefvy danfiklrql rlsydlpssv msrvpvrsas vsvvgrnlfy
     1021 lydsvpnisp essynseatp gfeqagvpqs rsigasvnlr f
//
LOCUS       WP_103017477             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Salinibacter ruber].
ACCESSION   WP_103017477
VERSION     WP_103017477.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40308
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maltigvpre tepgetrval vpdvadrlla tvddldirve egagqgayht dadydaagcs
       61 vvgrdatfda diiakvapps ddevdrlgeg qvlvgflnpl erpetaqala drgvtalame
      121 lvprisraqk ldalsamssi ggyraaigaa erlpaffpll ttaagtvrpa rvlvlgagva
      181 glqaiatakr lgakvfgydi reptreeves lgasfvelev dieadqdesg yaeqvekekq
      241 erqpellqph laeadvvist alipgqpapl lineeavaam dpgsvivdla apnggncalt
      301 etgeeivahn vqilgptnlp aempvhasel yaktvaamie egleadafap dfddeifaes
      361 cltrdgtvqn drvqgllgta eeaka
//
LOCUS       WP_103018267             536 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Alicycliphilus denitrificans].
ACCESSION   WP_103018267
VERSION     WP_103018267.1
KEYWORDS    RefSeq.
SOURCE      Alicycliphilus denitrificans
  ORGANISM  Alicycliphilus denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Alicycliphilus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Alicycliphilus denitrificans"
                     /db_xref="taxon:179636"
     Protein         1..536
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55524
     Region          11..536
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtsptppvq rigvpretfp gekrvatvpd vvekliklgf tvavesgagd aanfsdeayc
       61 aagaevlpda aalwaasdiv lkvrppssee aalmreggtl igfvwpaqnp dlmqqlaakk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rqmyatqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti igytdlasrl akqsstlyat nllrlveelc kakdghavvn
      361 meddairglt vikdgsvtwp applkappap apkpaavapv eqkkgghghg stgplpattl
      421 avifavaavl fwfigayapa aflghftvfv lacfigymvv wnvtpalhtp lmsvtnaiss
      481 iiaigalvqi appeagasgr pdglilwlaf aalvltavnm fggfavtrrm lamfrk
//
LOCUS       WP_103020546             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Salinibacter altiplanensis].
ACCESSION   WP_103020546
VERSION     WP_103020546.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter altiplanensis
  ORGANISM  Salinibacter altiplanensis
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Salinibacter altiplanensis"
                     /db_xref="taxon:1803181"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40487
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maltigvpre tesgearval ipdvadrlla tvdglevrve egaghgayht dadyeaagca
       61 vvgraetfda dlvakvapps gdevkrlndg qvlvgflspl erpetarala dqgvttlame
      121 lvprisraqk ldalsamssi ggyraavlaa erlpkffpll ttaagtvrpa rvlvlgagva
      181 glqaiatakr lgakvfgydi reptreeves lgasfvelev dieadqdesg yaeevekekq
      241 erqpellkph laeadvvist alipgrpapl linetaveam dpgsvivdla apnggncalt
      301 etgeevmkhk vqilgptnlp aqmpvhasel yaktvaamie eglgdgafap dfedqifaea
      361 cltrdgevqn ervrdllapt ekea
//
LOCUS       WP_103020570            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            altiplanensis].
ACCESSION   WP_103020570
VERSION     WP_103020570.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter altiplanensis
  ORGANISM  Salinibacter altiplanensis
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Salinibacter altiplanensis"
                     /db_xref="taxon:1803181"
     Protein         1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117606
     Region          27..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfrkllsvla glllllpatv laqdtgtvag tvvdsttset lpgvnvtvqd lnigaatgpn
       61 gqfeisgvpa geqvlqasfv gytrksipve veagetttvn vrlapqavgl edvvvtalgv
      121 ereeravsss vqqvdgadld atdnanfvns lrgkvsgani rssstmggss nivlrgyssi
      181 sgdnqplivi dgivvsnqsr qsgggtvegn ggfdfgnaas rldpgniksv svlkgpsaaa
      241 lygsrgangv iqittkdgsn lddeigvsfs ssvsmsqaye fvdyqnkygg gapsstfstl
      301 dgdfkksgdd qyvaqyavde swgprldgrp vrqwyswddv nglkgqatpw eahpdavkdf
      361 mdtgavftnn valsqqtesl nyrlgltsrn qgsvmpngsm dryqvnfngs vdlsddlqat
      421 tfakysyqdv karsgmgygf eenpfaafnt ftqrqldyga dsymrdyqrt ngqqrgwnya
      481 gvsgaqgpvt qfqytdnpyv nryanfqqdd eqrllgkaev aydivpnltg tatvttdfrt
      541 hrfsdrrsdi stgapgsfse dvieeqetss slrfdysrsl tdqvdltsfv agkvryetye
      601 qnlgstqngl aapnvftlqn svgrpdveet fresmvysty glvslgyqdi vflegtlrnd
      661 wsstlpadnn sylypsisgn fiftgldalq dqeilsfgkv raswarvgqd tdpyrlgvty
      721 pgstpfqgqa lqnvqrsann pdlkperttg iefgadlrff nervnlstty yrdvtkdqil
      781 avdvsgasgi gsslinagev snrgleaslt vtpvlqedlq wdvtanfnkn vnkvvdlaeg
      841 ldtynltagg vifgptiqar egeaygamvq pslrrdangd vvfrrngvpr ttsspqvvgn
      901 fqpdwtggls ttlsyqgvtv savvdgqvgg dvyslsnkfg tysglvgstv adnqretgvi
      961 pegvvvddgt pnengnydve gtdfgeaegr ipaasywknw fsagggdqfi ydathaklqe
     1021 laityslpqr wfndfalqra svsltgsnlm flykeapnid psvtlgagnv qgvesaqipp
     1081 qrqytfrvnl sf
//
LOCUS       WP_103020840            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            altiplanensis].
ACCESSION   WP_103020840
VERSION     WP_103020840.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter altiplanensis
  ORGANISM  Salinibacter altiplanensis
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Salinibacter altiplanensis"
                     /db_xref="taxon:1803181"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114034
     Region          29..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrysvlllg lllsalclvp tsnaqdpati rgvitdstga plpganvrve gtqtgvsada
       61 dgvyelatvr pgrrtiifsf vgfentsrtl elsagetrtl dialgagtvg lddvvvtalg
      121 vdreerslgy svervsgsdv aeapepnvms nlsgkvtgld vtggsgglas tprvtirges
      181 slsgsnrpli vvngvpidnt pntqgsdaqt tqvdfgngls qinaqniaem svlkgpsaaa
      241 lygsraadgv ilietkdgse tdgigatvrt svtasrplql pdyqneysyg nggdfayvdg
      301 tnapgwnwgv rmdegverpq wqgprtenge ltptevtsap dkvrnffdtg tnvstdvavr
      361 gggenssfra sfsrsdrtgi vpntnldrts tslsasydis daltvdanan yantasdnlp
      421 ssgygsesim yyftwgarhv qtdlledywq egqegtqqah ydlnwtnnpy fqvnentngl
      481 drdrlyggvs aqyeftdnln lrartgldys nqgtkqrkaf ssitapngwl qevdrtftew
      541 nsnlllnytr eaggftfeps vganfmrqtq rnvqltaqal svpdvynign arsnvqader
      601 datqeilgvf asgtvsyqdl lfldltgrnd wsstlplgnn syfypsasls vivsdlvevp
      661 eslplsfakl raswaqvgnd tdpfrltnty tfgeawgstq tvvseadlan adlqpeitss
      721 yevgtnlrfy dgraqldvty yrsttrdqil svplaqstgf nsrlvnagei rntgvetrlq
      781 lspiqnwggf gwdvslnwtr nrstvvelad gidtfvlgeg pfggsaqare ggrmgdmygr
      841 vfdrvddpns phtgeiiyed glpqltddve kvgnynhdwq ggigstlsyd nlqlnvlfdv
      901 rkggllysnt hatgieggsl egttrarnet vvgdgvvqnd dgtfsentqe aryvtwlrty
      961 ydrpnvesns fdatyvklre lslrynftad wlaragvqnv gvsvtgrnlf lwtdvphvdp
     1021 ettisggngq vpgfevqqip strsfgmnlq ldf
//
LOCUS       WP_103026883             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Salinibacter altiplanensis].
ACCESSION   WP_103026883
VERSION     WP_103026883.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter altiplanensis
  ORGANISM  Salinibacter altiplanensis
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Salinibacter altiplanensis"
                     /db_xref="taxon:1803181"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40460
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maltigvpre tesgearval ipdvadrlla tvdglevrve egaghgayht dadyeaagca
       61 vvgraetfda dlvakvapps gdeverlndg qvlvgflspl erpetaqala dqgvttlame
      121 lvprisraqk ldalsamssi ggyraavlaa erlpkffpll ttaagtvrpa rvlvlgagva
      181 glqaiatakr lgakvfgydi reptreeves lgasfvelev dieadqdesg yaeevekekq
      241 erqpellkph laeadvvist alipgrpapl linetaveam dpgsvivdla apnggncalt
      301 etgeevmkhk vqilgptnlp aqmpvhasel yaktvaamie eglgdgafap dfedqifaea
      361 cltrdgevqn ervrdllapt ekea
//
LOCUS       WP_103026777            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            altiplanensis].
ACCESSION   WP_103026777
VERSION     WP_103026777.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter altiplanensis
  ORGANISM  Salinibacter altiplanensis
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Salinibacter altiplanensis"
                     /db_xref="taxon:1803181"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114205
     Region          29..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrysvlllg lllsalclvp tsnaqdpati rgvitdstga plpganvrve gtqtgvsada
       61 dgvyelatvr pgrrtiifsf vgfentsrtl elstgetrtl dialgagtvg lddvvvtalg
      121 vdreerslgy svervsgsdv aeapepnvms nlsgkvtgld vtggsgglas tprvtirges
      181 slsgsnrpli vvngvpidnt pntqgsdaqt tqvdfgngls qinaqniaem svlkgpsaaa
      241 lygsraadgv ilietkdgse tdgigatvrt svtasrplql pdyqneysyg sggafayedg
      301 tgapgwswgv rmdegvertq wqgprneegd liptevtsap dkvrnffntg tnvstdvsvr
      361 gggenssfra sfsrsdrtgi vpntnldrts tslsasydvs daltvdadan yantasdnlp
      421 ssgygsesim yyftwgarhv qtdlledywq egqegtqqah ydlnwtnnpy fqvnentngl
      481 drdrlyggis aqyeftnnln lrartgldys nqgtkqrkaf ssitapdgwl qesdrtftew
      541 nsnlllnytr eagaftfeps vganfmrqtq rnvqltaqal svpdtynign vrsdvqaner
      601 datqeilgvf asgtvsyqdl lfldltgrnd wsstlpvdnn syfypsasls vivsdlvevp
      661 eslplsfakl raswaqvgnd tepfrltnty tfgetwdnnp tvvseadlan tdlqpeitss
      721 yevgtnlrfy ggraqldvty yrsttrdqil qlpfaqstgf nsrlvnagev rntgvetrlq
      781 lspiqnwggf gwdvslnwtr nrstvvelad gidtfvlgeg pfggsaqare ggrmgdmygr
      841 vfdrvddpns phtgeiiyed glpqltnnie kvgnynhdwq ggigstlsyd nlqlnvlfdv
      901 rkggllysnt hatgieggsl egttrarnet vvgdgvvqnd dgtfsentee aeyvtwlrty
      961 ydrpnvesns fdatyvklre lslrynftad wlaragvqnv gvsvtgrnlf lwtdvphvdp
     1021 ettisggngq vpgfevqqip strsfgmnlq ldf
//
LOCUS       WP_103027001            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            altiplanensis].
ACCESSION   WP_103027001
VERSION     WP_103027001.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter altiplanensis
  ORGANISM  Salinibacter altiplanensis
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Salinibacter altiplanensis"
                     /db_xref="taxon:1803181"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110435
     Region          27..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlipsiaf gvlllllpgl twaqqgtvtg tvteaetgnp lpgatvqvve eetgaasdan
       61 gqyqitgvpa gertlrvsfv gyqkqertvd vpsggtvrvn fqlqsgtaql eavtvsayrp
      121 etdqrvegga aaavssedie saqvqstega lqgkasgvrv lstsgqpgag fdvsvrgavs
      181 vnagtdplyi vdgvqinked nlgfargnpl sslnsndies irvlkdaasa aiygaqaang
      241 vviietkdgr agetqinvss evgfreaitp fdpmtteqff efqdealnna iaaktpfesl
      301 ggatggatta rdfnrlafgt dtistdwkda ilrtgntqsy nasisgggea tqfrvsgsfe
      361 rseaqvissg frqgqlraki eneatdylsv nananlstnk yegvteaavn vgspffasfq
      421 lppntkiynt agdpgsglnf pglvfpnpva tqelntresg vnsvsvnveg nwdlpknlaa
      481 rsfagvqyed vqesffgdpr ipsnagsggt gtldtqrdis vnvsqslsyr nvfsdvhnvs
      541 llggaelrrv kesfsgadge efpnelfrtl ssaadptgvn sfstqfrqls ffgngaytyd
      601 ntyqlegtvr fdgssrfgee nrygvfwtaa gfwrisnesf ledvdflsnl klrasygvtg
      661 nsdgignfqs lqqyssggay dgaplvrasn ignssltwee kvstnigldy alfggrikgs
      721 adifrddres lllnrdlpss sgfgsildnv geirvegidl sistrniddw ngvtwttdfn
      781 isfqeaevrk llpdddliqg gafevgeqpg qqiltryagv npangvpmyk dangdltytg
      841 sdpvnekkvg nanpdffggl tntvslggls vsaffqydyg rrtyandlff tninvpfttn
      901 ksqqildrwk epgdissvpk aygtlfgnnl pfgadlqsya nglpeqetfs strfmtnasy
      961 irlkrvqvry dfpgsildnl pqvrslsifa rgsnlvtwdd ydgvevesvg nvsstvfpqa
     1021 rtitfgvdlg l
//
LOCUS       WP_103027709            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            altiplanensis].
ACCESSION   WP_103027709
VERSION     WP_103027709.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter altiplanensis
  ORGANISM  Salinibacter altiplanensis
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Salinibacter altiplanensis"
                     /db_xref="taxon:1803181"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109354
     Region          35..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdvrhrrfpv slllaalfvv ahglvlvspv qaqttvggvv tdaedgkvip gvnvrvkntt
       61 vgtttdlsge yeiqvptgre vllfsfvgyq erevqvpdge aqvdvalprd vvdmdevvvt
      121 glgsevkren lanavtsvda adlegttdve sidgalsgkv pgaqinsysg apgggvsvrl
      181 rgvstingna qplyivdgii vsnasiptnv navtqaasgg srsnqdnpvn riadlnpkdv
      241 qsieilkgps aaaiygaras ngvvlietkr geagetrvdf sqtlgvttir kklgmrdfta
      301 etaevafger grqefleaqn ergfidyeee lfgqegvlst tsisasggsq dtrfylsgaw
      361 qddegiiert gferrsvrln vdhtfsarss itgtvnyvns etrrgltgnd nsgttfgrsl
      421 tstpnfidir eredgtypdh pfnasnplqt rdlftneekl nrvmaganfn ydffntdtqr
      481 lrfvgeggvd ffqfetvglf prrlqfepnd dqpgtsilge tnslftnfrt llvheyaied
      541 paldlttqvg ftasdsdvns tnfvardlip geqnldqaas lsstqertfq ndrsffvqee
      601 anyddkvift agvrgdrssl ngdtdefflf pksslavrva nfdfwtydav dqlklrvafg
      661 etgnttnfgt kftsfeapnv ggqagtlvdr ergddsiepe rqseietgvd lglfnrranl
      721 sftvyrkait dqllrrevps stgfqletin agklvnrgle tsltvlpvsn ntvewestin
      781 fwtndaevrd lpvpsfravg ggfgatlgev riqegrsptq ivgvddrdgd gssdgvfqlg
      841 dtspefqmsf snevtlfdgl sasflahwkk ggdnlnlsel lfdlsrtspd fdededgdgt
      901 pdgverlnaq gvsaqqfvqd asyfrlrevg vfyefpdpll rdvfdgavrr vrvglsannv
      961 ftitpyksyd pevnnfgstp vangvevtpf psskkfffhl nvgl
//
LOCUS       WP_103029696            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            altiplanensis].
ACCESSION   WP_103029696
VERSION     WP_103029696.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter altiplanensis
  ORGANISM  Salinibacter altiplanensis
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Salinibacter altiplanensis"
                     /db_xref="taxon:1803181"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117212
     Region          27..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlipsiaf gvlllllpgl twaqqgtvtg tvteaesgsp lpgatvqivd egtgaatdsd
       61 gryritgvpa gertlqvsfv gyqeqersvn ipaggtarvn fqlrtsqael devvvtalgi
      121 eqeerslgya ssevdgaeie gageanltna lsgktagldi sqssgqpgsg tritlrgnns
      181 yqaggnqpli ildgvrisna sddnptgpgv ftggtanrla dldpnsiksv nvlkgasaaa
      241 lygqqasnga iiietkdgsg tdgieasytv sagyddaiid gfqdeylqgt qgcyqngvrn
      301 gregayselg dpnsgecfdv ggpdqssntq taqswgphkd slstavldsi gqpntvdpre
      361 qffedgtqle nsltvsgqgd fgtasvtvtd trndgivpst kfnktsisan ysadlsekfs
      421 advsaqytet rrdfmleang pnsyqwalqs apinfdlepa rfedgtnrsf sggsrdnplf
      481 ttdalnlasd vdrfigaatf tyqpiewltl kerigvdryd dnrkekinag tsaepngstf
      541 dqtirrrqid sdftvtadrq vtddlnvnfl vgnnirkrtf nslevigtdi nvrdffnisn
      601 fntldrgqfq neevligayg dlslnyndya ylsitgrndw sstlpeenrs ffypsanlsf
      661 iftealsgaf eevpisfgrv rlsasqvgnd tdpfqlrttf gqsgsgdgvr gnitfpfngv
      721 nafqqedtra npnlepastt eyeagldlrf fggranistt yynksttdqi fdvpasdatg
      781 fpsqsrnage ivnrgweiea dgtalqigdf swdiganwtk ntteikelap gvsniflfgf
      841 ttiqiraetg edgygiifar gfrrngdisp dnplplpggs qrtepyegfg ddakligpdg
      901 qgllsagpkn ignvqpdwqg gfntsiswkg lsvstqweys qggeilnfdr fymegngthe
      961 atanrgeeit rdgiqiatge snetsvvrdq efftgpansn ferfvedasy lklrqasisy
     1021 qfqipqrigr isgletvrvg atgrnlitfs dfsmgdpags lagtgngqgf yhgvtpstrt
     1081 yrfsvrlgf
//
LOCUS       WP_103030252            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            altiplanensis].
ACCESSION   WP_103030252
VERSION     WP_103030252.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter altiplanensis
  ORGANISM  Salinibacter altiplanensis
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Salinibacter altiplanensis"
                     /db_xref="taxon:1803181"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114123
     Region          29..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrysvllls lllsalclvp tsdaqdpati rgvitdstga plpganvrve gtqtgvsada
       61 dgvyelatvr pgrrtiifsf vgfentsrtl elsagetrtl dialgagtvg lddvvvtalg
      121 vdreerslgy svervsgsdv aeapepnvms nlsgkvtgld vtggsgglas tprvtirges
      181 slsgsnrpli vvngvpidnt pntqgsdaqt tqvdfgngls qinaqniaem svlkgpsaaa
      241 lygsraadgv ilietkdgse tdgigatvrt svtasrplql pdyqneysyg nggdfayvdg
      301 tnapgwnwgv rmdegverpq wqgprtenge ltptevtsap dkvrnffdtg tnvstdvavr
      361 gggenssfra sfsrsdrtgi vpntnldrts tslsasydis daltvdanan yantasdnlp
      421 ssgygsesim yyftwgarhv qtdlledywq egqegtqqah ydlnwtnnpy fqvnentngl
      481 drdrlyggvs aqyeftdnln lrartgldys nqgtkqrkaf ssitapngwl qevdrtftew
      541 nsnlllnytr eagdftfeps vganfmrqtq rnvqltaqal svpdvynign arsnvqader
      601 datqeilgvf asgtvsyqdl lfldltgrnd wsstlplgnn syfypsasls vivsdlvevp
      661 eslplsfakl raswaqvgnd tdpfrltnty tfgeawgstq tvvseadlan adlqpeitss
      721 yevgtnlrfy dgraqldvty yrsttrdqil svplaqstgf nsrlvnagei rntgvetrlq
      781 lspiqnwggf gwdvslnwtr nrstvvelad gidtfvlgeg pfggsaqare ggrmgdmygr
      841 vfdrvddpns phtgeiiyed glpqltddve kvgnynhdwq ggigstlsyd nlqlnvlfdv
      901 rkggllysnt hatgieggsl egttrarnet vvgdgvvqnd dgtfsentqe aryvtwlrty
      961 ydrpnvesns fdatyvklre lslrynftad wlaragvqnv gvsvtgrnlf lwtdvphvdp
     1021 ettisggngq vpgfevqqip strsfgmnlq ldf
//
LOCUS       WP_103035794             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Castellaniella caeni].
ACCESSION   WP_103035794
VERSION     WP_103035794.1
KEYWORDS    RefSeq.
SOURCE      Castellaniella caeni
  ORGANISM  Castellaniella caeni
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Castellaniella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Castellaniella caeni"
                     /db_xref="taxon:266123"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38648
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipketl agetrvaatp etvkklvaak hqvlvergag trarfpdsdy eqagasltda
       61 agalasalvl kvrrpdaael grmqagtvll gmldpfdaeg lksladaglt afaleaaprt
      121 traqsldvls sqanlagyka vllashyygr ifpmmmtaag tlkaarvvvl gagvaglqai
      181 atarrlgavv easdvrpaar eqveslggkf idvpyetdee reiaqgvggy arpmpaawma
      241 rqaalvaerc kqadivitta lipgrpapvl iqpetvaamk pgsvvvdlav erggncplsv
      301 pgeviehegv tlvgltnlpa llatdasaly arnlldflkl vidaegrfap padddivkac
      361 lvcqdgkvlr sa
//
LOCUS       WP_103029541            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            altiplanensis].
ACCESSION   WP_103029541
VERSION     WP_103029541.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter altiplanensis
  ORGANISM  Salinibacter altiplanensis
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Salinibacter altiplanensis"
                     /db_xref="taxon:1803181"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109451
     Region          35..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdvrhrrfpv slllaalfvv ahglvlvlpv qaqttvsgvv tdaedgkvip gvnvrvkntt
       61 vgtttdlnge yeiqvptgre vllfsfvgyq erevqvpdge aqvdvalprd vvdmdevvvt
      121 glgsevkren lanavtsvda adlegttdve sidgalsgkv pgaqinsysg apgggvsvrl
      181 rgvstingna qplyivdgii vsnasiptnv navtqaasgg srsnqdnpvn riadlnpkdv
      241 qsieilkgps aaaiygaras ngvvlietkr geagetrvdf sqtlgittir kklgmrdfta
      301 etaevafger grqefleaqn ergfidyeee lfgqegvlst tsisasggsq dtrfylsgaw
      361 qddegiiert gferrsvrln vdhtfsarss itgtvnyvns etrrgltgnd nsgttfgrsl
      421 tstpnfidir eredgtypdh pfnasnplqt rdlftneekl nrvmaganfn ydffntdtqr
      481 lrfvgeggvd ffqfetvglf prrlqfepnd dqpgtsilge tnslftnfrt llvheyaied
      541 paldlttqvg ftasdsdvns tnfvardlip geqnldqaas lsstqertfq ndrsffvqee
      601 anyddkvift agvrgdrssl ngdtdefflf pksslavrva nfdfwtydav dqlklrvafg
      661 etgnttnfgt kftsfeapnv ggqagtlvdr ergddsiepe rqseietgvd lglfnrranl
      721 sftvyrkait dqllrrevps stgfqletin agklvnrgle tsltvlpvsn ntvewestin
      781 fwtndaevrd lpvpsfravg ggfgatlgev riqegrsptq ivgvddrdgd gssdgvfqlg
      841 dtspefqmsf snevtlfdgl sasflahwkk ggdnlnlsel lfdlsrtspd fdededgdgt
      901 pdgverlnaq gvsaqqfvqd asyfrlrevg vfyefpdpll rdvfdgavrr vrvglsannv
      961 ftitpyksyd pevnnfgstp vangvevtpf psskkfffhl nvgl
//
LOCUS       WP_103045591             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Comamonas
            faecalis].
ACCESSION   WP_103045591
VERSION     WP_103045591.1
KEYWORDS    RefSeq.
SOURCE      Comamonas faecalis
  ORGANISM  Comamonas faecalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Comamonas faecalis"
                     /db_xref="taxon:1387849"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55431
     Region          11..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtnpvpvgq rigvpreifp gekrvatvpd vvekliklgf svaveagagd ganfsddayr
       61 aagaevlpda aalwtasdiv lkvrppssde valmreggtl igfvwpaqnp elmaqltakr
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee dgsggggyak
      241 vmsegfqaaq rqmyasqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti igytdlpsrl akqsstlyan nllrlteelc kakdgiavvn
      361 meddairglt vtrdgvitwp applkappap apkaaaapva ekksahgpge pmsakaltiv
      421 favlavlfwa igvyapeafl ghftvfvlac figymvvwnv tpslhtplms vtnaissiia
      481 igalvqiapp dtgasgrpdg lilwlafaal vltginmfgg favtrrmlam frk
//
LOCUS       WP_103063321             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces qiguomingii].
ACCESSION   WP_103063321
VERSION     WP_103063321.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces qiguomingii
  ORGANISM  Actinomyces qiguomingii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Actinomyces qiguomingii"
                     /db_xref="taxon:2057800"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53594
     Region          1..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgipcqpp drsmtaatpq tveqltrlgy dvvvqrgaga pahfpdtaye dagarladrd
       61 etwgcnvvvt ayapddaeld lmhpgatlig rldparrpel vqalqehslt alaidtvpri
      121 sraqsmdvls sqanlagyra vieaathfgr llngqvtaag kfppasvyvi gagvaglaai
      181 gtayslgavv kgtdvrpeva dqvksvgaef vpvptaqevs adgyakemst dqaalanaly
      241 aeqsaaadiv ittanipgrk apllldraav damqpgsviv dmaaanggnt eltvpgevvt
      301 teggviivgy tdlaerlpaq asqlygrnil nlltlvtpak dgnltldldd qvvraitvcq
      361 agellwpppp vavsaapkaa paapapersa aevqaqaese aaararsrrh lkigvalava
      421 alaalvlvtp aaatnhyivl alaiilgfhv isnvtpalht plmsvtnais giillgaisq
      481 vgndnpavsa vafiaimlas invfggfavt nrmlamfrke
//
LOCUS       WP_103051220            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hanstruepera
            neustonica].
ACCESSION   WP_103051220
VERSION     WP_103051220.1
KEYWORDS    RefSeq.
SOURCE      Hanstruepera neustonica
  ORGANISM  Hanstruepera neustonica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Hanstruepera.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Hanstruepera neustonica"
                     /db_xref="taxon:1445657"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113248
     Region          25..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lflafvvqlt faqektisgt isdenglplp gvniivkgtt tgtqtdfdgn
       61 ysitantgdv ltysflgytt kemtigtann isfamevdse aleevvitaf giarkkdeit
      121 tayqevqsee lvqaqnpnvv qglagkvsgl qinttnsgvn kstnirlrsl vtvsgnnsal
      181 vvidgvitdl dltdidpnii etvnvlkgan gaalygqqas ggavivttkk nigdgdkfti
      241 nvnsaidiet vafvpdrqlr ygqgwngvht syenggwgpe fdgqirptgl pledgtyryf
      301 pyspikdnik effkdgvttq ntvsisagnl dngyvffsan rldsefvven dklrrnsfnf
      361 kagkkvgkwt vegnvsyins rteqtngglf lellqtatni pveefsapnn athwtsyyrs
      421 pywirdnern dfrqdqfngv inlgyeindn idiryngnmf tsstdsqswv ngyvdtlnvg
      481 ggdhttqssy grrntmtsny ygdlianfny eltddislsa nignniqdry fsssqisgnn
      541 ltidgfynit nitgqadvng fgnngwsrrr syalygnlql dfkdyltlnv tgrndwtsil
      601 sednnsffyp svgvsfiptk afdfggdtln ylkiagnwvk vgndgafgay svnpvlaqtt
      661 gfpygtinsf sqttsitdpn lkpefiesie fnlsagffkd ritldasyyt tkttdlisnk
      721 avsyasgvtq vranigelss egfevdlglr piwskesdgf rwqanfsyat nkstveeleg
      781 daeqvainaf tgnanpvgiy aiegqefpli qgvgysrdpq grviidpttg tpvqtpdliv
      841 lgktnpdyii glntfmtfkg lrlaatfdyr tghqfwsggk swlswsghlv esaqngrtgf
      901 ifpnsavets pgsgeyvant gvitggtsys sflnyysndy ytntenfvld atafkcrela
      961 lsytlpskll entmmkgitv gvqarnpfmi lpkenrnynd petsqttnia ggglaaigqy
     1021 pvtrtfgfkl natf
//
LOCUS       WP_103070258            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            sediminis].
ACCESSION   WP_103070258
VERSION     WP_103070258.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sediminis
  ORGANISM  Aquimarina sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Aquimarina sediminis"
                     /db_xref="taxon:2070536"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119024
     Region          27..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvltkkili lltvlvtqls vaqessitgt vtdnngtplp gvniivkgsn sgtqsdfdgk
       61 yslqasqgsi lifsylgfae keatiglekt iniqleeaas qldeivvtal gisrdkkslg
      121 ystqevaged lntvktanfv nslsgkasgv qikrnnnlgg stnvvirgna slsgsnqalf
      181 vidgvpinnt ntnskiqgqa rggqydygna asdinpedie sinvlkgaaa salygsraan
      241 gvimittkkg knskgmgitv nsgmtfgsid kstfakyqkq ygagygpyyg pgedsyldli
      301 didndgnldf vtpltedasy gaafdpnllv yqwdafdids pnyrtptpwv nakngpitff
      361 etpititnsv sfdkglengs frlnytqfdq tglmpnssik rhnfsmsgnf kltdqltatg
      421 yanyiktdgl grnstgyndn iisnfkqwwq tnvdieqqrd iyfatrrnvt wnpastapgs
      481 vpiywdnpyw tryenyqtdm rnrflgnvsl nykvfdwfdi tgrvatdtys elqeerrang
      541 svatsfgvnp gggnvdnrsn vdsgygrkni qntetnydlm fnfykdlsde fnikgvigtn
      601 irrnhlqsih astsgglsvp rlyslqnsvg plplpeeidq kigvdgiyas tslgyketyf
      661 ldatirrdhs stlpkgnstf yypsvagsfv fsnlidaefi sfgklranya evgnsapfdf
      721 lydsfnvntp igsastsvgd tkknpnlkpe rttsteigle mkllsnrlgf dvayyknnsi
      781 dqilgvpvtt atgylfktln ageienkgie lslygtpiet qnfswginvn wsknenevis
      841 ledgidnlql gsfqggvtin arvgqpygii qgtdytying qrvvdpsngq yiktttsnnn
      901 igdtnpdwlm gianklnykn lsfsflidiq qggsifsldq yygqatglye etafindlgn
      961 pvrntiadgg gfinpgvnpd gsantsrira drfgafgyrr glpnaafvyd asfvklrevs
     1021 lgysfpkkii ektflnevsi svigsnlwii dknlphadpe sglsagnlqg ysvgslpttr
     1081 digfnlklqf
//
LOCUS       WP_103050994            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hanstruepera
            neustonica].
ACCESSION   WP_103050994
VERSION     WP_103050994.1
KEYWORDS    RefSeq.
SOURCE      Hanstruepera neustonica
  ORGANISM  Hanstruepera neustonica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Hanstruepera.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Hanstruepera neustonica"
                     /db_xref="taxon:1445657"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114367
     Region          25..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkttinsvlf llfilptfmf gqnlvtgtvt eqssslplpg vnviikgttt gtstdfdgiy
       61 qievsngdvl vfsylgyvtk eityngesnl nvaldedaaq ldevvvigyg tvkkedatgs
      121 vslvtdedfn kgnivstdql ltgkiagvri tnsggqpdsa pnirirggss lsannnpliv
      181 idgvplsnin aagvsnplsl vnpndvesfs ilkdasatai ygarasngvi iittkkgtsg
      241 apqfnfstdi svnsagegld mmdsatyvrf iqeyhpdlvd klgvpigsvq tnepisqiid
      301 tpngpraiyd tdwrdsvlrs aftsntnfsa ranlfdvlpf rgsigytnae givktddyer
      361 vtasinlspr ffdddlkvtl nakatyadkn svdtggalgg slvfdptkpv ynnapdnrfg
      421 gyyfntaqdg nrlildgqwn plalleqrer peratrflgn leldyslnfl pglravvnlg
      481 ldaskakite rffnnaaaty qfdvdgnylf npgenyaenq ditnttmdaf lqytklyddk
      541 fvtkidvqag ysyqnfkndg tkreyryhvd dpntpddddq vglrelifdp anpnnryyne
      601 ynlqsffgrt nidildrylf tfsvradass lfvlddvwds nawgffpaaa fawkvsseef
      661 mnnvnfvndf kirfgwgktg qndisqvvgy ypttplftpg spnsqylpga glysalpynp
      721 dltwekttty nlgvdfsffk ndliagsfdi fkretkdlla rvnvppgqgf sdtfvknvge
      781 segrgfelnl nlnaiqtddl svslngnlsy vyneitdigg qadinrggsl rgtgsfllsd
      841 vvgqqaqsay vfkqlydsng nvipgafadl ngdniinddd ryhvqiapnw tygfgmdisy
      901 kkwdfttvfv gqvggniynf skmnygftea avpannnsit nvlnfyngaa dpafenvngn
      961 iqfsdyfied atflrcnniv lgytfdnmik ngnvrmygav snpfiitdyd gidpqnfggi
     1021 drdfyprptt ftlgvnfdf
//
LOCUS       WP_103070624            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            sediminis].
ACCESSION   WP_103070624
VERSION     WP_103070624.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sediminis
  ORGANISM  Aquimarina sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Aquimarina sediminis"
                     /db_xref="taxon:2070536"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112024
     Region          26..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 minklliflm fvlfvssnva faqnkktvsg tvtgedgipl vgvnviekgt sngtstdfdg
       61 nynvvvsnss svlvfsslgf eekeivvnek tnidvvligs dellgevvvt algikkttka
      121 lgysltevgg delstiklpn avnslqgkia gvnvtqnstg aagssrviir gsstltgdnq
      181 plyvidgipi snvnngsagl wggsdggdgi ssinpddies vsvlkggaas alygsraagg
      241 viivttksgk eqkgfgvevs ssvtfdqvdt slqdfqteyg qgrrgakpvn qeealdvgls
      301 swgerldgss viqwdgvsrp ysyvgnnqeh fyrtgttfin svaltngged fnyrfsasdl
      361 tneditpnsg lnrktfslns gavmadkltt qvnvkyilee vnnrprlsda pgngnftvan
      421 lapnvdvrfm npganddlte rqyssnsfsq npyfaaynfr nedtknrvia stslrydvfd
      481 wlyvsgragi dhytirrtav epfgtaykpl ggieereiry sqidadlilg vekditdkfa
      541 tnvfigangn svsqetkilr gndfivpgle qfgntvnqsa ennfsgngng krkigslygs
      601 vefsyddfay ltftgrndwf stlsfpgknt snndfypsvn aslilsqmfe lpeaidflkl
      661 rggysevagg aqdpyqlalt yqifgqghlg qplgsingdr vpnanlvafs kseseigida
      721 rffnsrlsfd vayysnettn divpvgtsvf sgyntalani givenkgief lisgtpvkte
      781 nfswttsvng ahntgkvvat neeggeislg eprsrnveik qivgepygvi fgvpyvrddn
      841 gnivyeidgd gvplaqrger kilgegvppl tlgftntity knvtlnflid gkfggqifsg
      901 tntvtygngl hkgtlagren gltvtgvnae tgeqftttva pedlqtyygr isgiaeefve
      961 dsdyikfrql slgytfpnsi ldktfldsas isliasnlfy lmrtvdnidp esaynvgnaq
     1021 gleyfglpst rsyglnvnlk f
//
LOCUS       WP_103071004            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            sediminis].
ACCESSION   WP_103071004
VERSION     WP_103071004.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sediminis
  ORGANISM  Aquimarina sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Aquimarina sediminis"
                     /db_xref="taxon:2070536"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117545
     Region          25..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfsgilt lilafvvqls faqektisgn vsdnsglplp gvnivvkgta tgtqtdfdgn
       61 ytinanrgav ltfsyvgfav reiavgnddt invqlqedaa qleevvvtaq girrekkslg
      121 yavstvandk ieqkaeadlg rilsgkaagv nitatnglsg sgtniiirgy ssvtgsnqpl
      181 fivdgvpfdg gtntqssfld nvtessrfld ldpnsiesvn vlkglsattl ygqagrngvi
      241 littkngatg ssnekfevtf tqsifsseai lpkyqnnygg gfhqdygfff snwgpgfnsd
      301 lsanrnfigi apdgttlvng plgafgdqsl nvgvedqidi pyryqpynsv ddffrtgyts
      361 ttsvnvgggs ekgrfnlsyt hlndegvtpg ntlrrnnigl ggsaklankl tvngvlnfal
      421 tdfksppvap sfgsgtgfdg gsvfgdllyt prsvnlfglp fqaqdgrsvy yrsgndiqnp
      481 rwtvantqts qevrrifgnv alnyeikdwl nlayrvgidq ytesnrygqn rggvdgqqlg
      541 iyrttsvvnt iwdhtlslna nkdlsenlnl nvnlgvnpry enferegves vgqlafgvle
      601 hfnfesqssf nsftnlpigv kstqntigay fdatlayqdf lylnasgrnd wsstlerenn
      661 slfypaasis fiptsafdnl agnglnylkm rfgygssagf pftyntrnvl elqprafvtt
      721 dgsavpnnnv anrlgnpnlk pelvtefelg vdtklfnrln fnvsvfskkt tdlltdqsld
      781 fatgfniqtv nigelqtegi eidynldiik pngdgfkwni agnfyadene vtdlddsvdr
      841 illtgavigq aanyaiegkp ygiilgttvq rdangdrlvd adglyiedte prelgdpnpd
      901 wttnvnttlg ykgfsfymdw qyrhggdifs tttgsligrg vvdgddpinr ealyvvpgvv
      961 qqfdgdgnlt gtvpnttqit atnlgfdiyg fganefkmfd gstlrlnela vgykmpskfl
     1021 nntpfgslsi kasgfnlwyk afnfpddvrf dtnslstgvg nglgidfitg psvrrygvsi
     1081 qatf
//
LOCUS       WP_103071386             975 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            sediminis].
ACCESSION   WP_103071386
VERSION     WP_103071386.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sediminis
  ORGANISM  Aquimarina sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 975)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 975)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 975)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Aquimarina sediminis"
                     /db_xref="taxon:2070536"
     Protein         1..975
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108293
     Region          24..972
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktftkstlf lfwlipmsff aqstingtvt dagsgqpipg vniivkestn gttsdfdgny
       61 slnnvnngdi ivysyvgfvs qeitysgqat vdilfeedaa eldqvvligy gttkkkdltg
      121 avalvtsesf ntgnnitpen lfngrvagvs intnggpaan seirirggas lnasndpliv
      181 idglplndpg dlangsrsil ssinpndies fsilkdasaa aiygnrgang viiittkkgk
      241 rnlqinldsk tsatsvnktv dvfsadtyra fiadnfpdrv adlgtantdw qdeiyrtafs
      301 sdhnlsirgs liedlparla igrsdqegir ktsrfertts slslnprlfd shlkidinan
      361 lnfeknrfap gvegaaitfd ptqpvfdsss pyggffeyrd sstgfassnv qrnpvaqllq
      421 treianvrry fgnvkldyql hffpdlravl nlglddsetd rfqerstesa tgfnatqgef
      481 lgfksdtdll iknrlldayl tynktlgrld leatggysyq kfeldkfetg dqrdpinfpe
      541 rtidpdevll ayflrtnlkf ndkyfltasi rrdgtsrfge dnrwgyfpsa sfgwqiseen
      601 flrnsstvsn lrlrlgygit gqqdidqaya ylqryrrssp ltqyildgev inivqpqfrn
      661 ediewekite ynigldygfw ndritgaidi frkesddlls qapipdaanf snqgfqnigk
      721 fitegiefsi sadvirksdf nwnlsynttf idreieslaf gqdilttgig ggtgntiqiq
      781 rqgeapfsff tyaqiydtng kpiegayadl nqdgvinnnd ryisgkgapd limglqssmn
      841 yknfdfsfsm ranigneiyn nvassnaqlg nvfrtvfnnt ptsisdtnfq stpdvilsdy
      901 yiedgsflrm dnitvgytmr nlmkgisslr fwaglqnafi itdysgldpe iqnngvdnti
      961 fprgrtlllg lnyky
//
LOCUS       WP_103085243             179 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_103085243
VERSION     WP_103085243.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..179
                     /product="STM4504/CBY_0614 family protein"
     Region          <5..43
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 dkaiselnni fhehslkyry engrivrlrr ikrlknicyy lyspgeygfv eydlmkaynr
       61 lilndfacvv rechaafrsv llriherkgi vyheqdslnt lmanlmargv isaeyvhkfh
      121 flsdvlesei flpmapeksh hhyammlris eelacsiyyl tersiffltq raeedsvap
//
LOCUS       WP_103068206            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina
            sediminis].
ACCESSION   WP_103068206
VERSION     WP_103068206.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sediminis
  ORGANISM  Aquimarina sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Aquimarina sediminis"
                     /db_xref="taxon:2070536"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114284
     Region          23..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikyyyilv cillsatsfa qeivvqgnvs tkdgplpgas vvvkgsasgt qtdfdgnfsl
       61 ktdrnsilvf syigfitqet katssmniil vedaaqleev vvvaygtask ssftgsvnqi
      121 saaeildrpl tnvltaldga apgvritpan gqpgsspsir vrgvgsinas sspliivdgv
      181 efvgsfssin pndisslsvl kdaastslyg sraangvili ttkkgkkgkd tfsldvsqgv
      241 ssrsikeykr vnaseyymlm wealrngfsi sgttpvtdan qmasdqifdn lgvnpfnvpn
      301 dqivltdgai npsakllyed dldwqdqlir tgyrsnlnfs ysggsdntdy fasigylked
      361 gyiiksdfer itgrlnvnsn lkewfktgin lsvatstsnn aadgsssslv npfgtsrqia
      421 piypvflhnp ttgaflldda gnriydssta rvgsssgrnv iqetilnids dkifsfnart
      481 ygevkflqnf tftfnaaldk rffntegfdn pvvgdgspdg raerdaivnt tvnynqllkf
      541 nksfgdhtvg vllghenfet ernfltgfrs giiadgntel inftttldle sntrrltreg
      601 yfsnitydyn dkyylnvsar rdassrfdkd arwgnffavg gswrldqenf mngvdwlstl
      661 kirasygevg nddifrsnss rsdfyasqal lslgfnngae ggiissakgn pdlswetniq
      721 tdaaiefgfl nnrisgtvey ynresedllf fvplsvsegl ddfpdnigsm tnkglevdln
      781 vgifdtenfg wklninaatl nneitelpqk eiidgtkklv vggdifaywl rdwygvdptd
      841 gsglyvldte lgaigdddvr tasdgtavtt nqnkalfdfg gtatpdlfgs fsndlryknf
      901 elgftftyqi ggetydsayr rllhsgqygt alsndilnrw qkpgditdvp rldvnqtsaf
      961 gaasdrwlvk sdylalrqvn laynfnrelv nrlgvsgarl ymsgenlfli nkrqglessq
     1021 nfngttsnrf tpsriitvgf nvtf
//
LOCUS       WP_103112236             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microcystis aeruginosa].
ACCESSION   WP_103112236
VERSION     WP_103112236.1
KEYWORDS    RefSeq.
SOURCE      Microcystis aeruginosa
  ORGANISM  Microcystis aeruginosa
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Microcystis aeruginosa"
                     /db_xref="taxon:1126"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40132
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikesd qgearvalvp dtvarlvkag fevivqngag isanfadsay savgaalsen
       61 seyiyetadi ilkvvppsds eidrlkgggi ligfldplrq prriakladr gitalsmeli
      121 prssraqsmd alssqanlag ykavllaave lpkmfpmmtt aagtiapakv lvlgagvagl
      181 qacatarrlg avveafdirp qvkeevqsvg akfiemplee dtvadngyak evslstqeri
      241 cqalaepikr advvittaqv pgkqapllvt kemiatmkag svivdlaaeq ggncaytqpg
      301 reiivngvki vgavnlpatv atnasqmyak nlqmllqllv skegslnldf addiidsacv
      361 thageirnqr iksalseqls af
//
LOCUS       WP_103117139             262 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_103117139
VERSION     WP_103117139.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..>262
                     /product="STM4504/CBY_0614 family protein"
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechav frsvllrihe rkgivyheqd slntlmtnlm argvisaeya
      241 hkfhflsnvl eseiflpmap ek
//
LOCUS       WP_103119200             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_103119200
VERSION     WP_103119200.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53542
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa daraklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_103126313             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nostoc
            cycadae].
ACCESSION   WP_103126313
VERSION     WP_103126313.1
KEYWORDS    RefSeq.
SOURCE      Nostoc cycadae
  ORGANISM  Nostoc cycadae
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Nostoc cycadae"
                     /db_xref="taxon:246795"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41172
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvglnp dtvarlvkqg levwvekgag ersffsdsay qaagakiisd
       61 tvqlwneadi llkvsppqer edgrseidll regsilisfl nplgnplvaq hlanrkvtal
      121 smeliprstr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vtleeettaa ggyakeisea
      241 skqrtqevvt ehvknadvvi ttaqvpgrka pllvteemva qmkpgsvivd laaeqggnca
      301 ctdpgkdivw ngitiigpin lpssmpvhas qlyaknvtsl mqllikdkal qinfaddivd
      361 aacithagei rnqrvkdalq alssvgat
//
LOCUS       WP_103120735             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylopila sp. Yamaguchi].
ACCESSION   WP_103120735
VERSION     WP_103120735.1
KEYWORDS    RefSeq.
SOURCE      Methylopila sp. Yamaguchi
  ORGANISM  Methylopila sp. Yamaguchi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylopilaceae; Methylopila.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Methylopila sp. Yamaguchi"
                     /db_xref="taxon:1437817"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38767
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavaketd aaeprvaltp dvvkklkglg adisietgag vasgvtdaay eeagaqiaas
       61 radalsgadv lltvrrpspe slaglkpgal vigtmdpygq adaiaalata nvsafamelm
      121 pritraqvmd vlssqanlag yravidaaae fgrampqmmt aagtvppara fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedde fkqaetaagy akpmsaeyqa
      241 kqaelvaahi akqdivitta lipgrsaprl vtaamvksmk pgsvivdlav erggnvegav
      301 pgqvveidgv kivghlnvpg rlaasssaly aknlssflet lisketkela vnwddelvka
      361 taltrdgavi hpiakpaean
//
LOCUS       WP_103155060             195 aa            linear   BCT 07-JUL-2024
DEFINITION  cytochrome c nitrite reductase pentaheme subunit [Vibrio
            vulnificus].
ACCESSION   WP_103155060
VERSION     WP_103155060.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03146.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     gene            1..195
                     /gene="nrfB"
     Protein         1..195
                     /product="cytochrome c nitrite reductase pentaheme
                     subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=21737
     Region          7..194
                     /region_name="PRK11659"
                     /note="cytochrome c nitrite reductase pentaheme subunit;
                     Provisional"
                     /db_xref="CDD:183264"
ORIGIN      
        1 mgniklaivi mlksilafsf ygysfsaiad tsvateatds srfqvelird rdykcvqchk
       61 dsketlsgsh gedahkilgr evnctechnn igpdhregap lvtkyasaqs kqgtekvfmd
      121 tsailkanta ctdchqpqyl redswthdvh aknltcsnch dvhankakvl glerkekikm
      181 cvdchsdfnq keeer
//
LOCUS       WP_103164047             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            vulnificus].
ACCESSION   WP_103164047
VERSION     WP_103164047.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54506
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprell agetrvaasp ssveqliklg fdvvvetqag alasfddsay esagakmvsk
       61 eeawnselil kvnapiidee ksideitlik egatlvsfiw paqnpqlmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvfvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaeflsv dyqeaagsgd gyakemsddf
      241 nkkaaelyaa qakdvdiiit talipgkpap klitkemvds mkagsvivdl aaanggncey
      301 tvanqvitta ngvkvigytd mvgrlptqss qlyatnlvnl fkllckekdg ninidfedvv
      361 lrgvtvvkdg eitwpappiq vsaqpqakpk avekpapkvq epvspvkkla glavavgafa
      421 wiasvapaaf lahftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngavtflaf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_103171134             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Paracoccus].
ACCESSION   WP_103171134
VERSION     WP_103171134.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55648
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkegf egearvavtp ssaghlmklg hevfvesgag aragfsddsy raagvtvlps
       61 aaelirsvdv vakvrqpsea eigqmqpgqt lisffypaqn sellaqakeq gitaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 asigtavslg aqvyafdvrp evaeqiesmg aefvyldfee aqdgaatggy aapsspefre
      241 kqlakfrela pqmdvvitta lipgrdapkl wtrdmveamk pgsvivdlaa erggncelti
      301 pderhvteng vtiigytdfp srmgaqasel ygnnvrhfma dltpkkdgvi qhnmeddvir
      361 gatvtrdhdv twpppppkia aiaaqkpkek kreltveerr aaevaafkae trsqvtllva
      421 galvllviga vapasfmahf ivfvlacfig frviwnvahs lhtplmaitn aissiiilga
      481 lmqigsgsww vvllgalavl magvnifggf lvtrrmlamf qks
//
LOCUS       WP_103176583             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            vulnificus].
ACCESSION   WP_103176583
VERSION     WP_103176583.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54575
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprell agetrvaasp ssveqliklr fdvvvetqag alasfddsay esagakmvsk
       61 eeawnselil kvnapiidee ksideialik egatlvsfiw paqnpqlmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvfvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaeflsv dyqeaagsgd gyakemsddf
      241 nkkaaelyaa qakdvdiiit talipgkpap klitkemvds mkagsvivdl aaanggncey
      301 tvanqvitta ngvkvigytd mvgrlptqss qlyatnlvnl fkllckekdg ninidfedvv
      361 lrgvtvvkdg eitwpappiq vsaqpqakpk avekpapkvq epvspvkkla glavavgafa
      421 wiasvapaaf lahftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngavtflaf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_103187305             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            vulnificus].
ACCESSION   WP_103187305
VERSION     WP_103187305.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54478
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprell agetrvaasp ssveqliklg fdvvvetqag alasfddsay esagakmvsk
       61 eeawnselil kvnapiidee ksideiasik egatlvsfiw paqnpqlmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvfvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaeflsv dyqeaagsgd gyakemsddf
      241 nkkaaelyav qakdvdiiit talipgkpap klitkemvds mkagsvivdl aaanggncey
      301 tvanqvitta ngvkvigytd mvgrlptqss qlyatnlvnl fkllckekdg ninidfedvv
      361 lrgvtvvkdg eitwpappiq vsaqpqakpk avekpapkvq epvspvkkla glavavgafa
      421 wiasvapaaf lahftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngavtflaf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_103187859             474 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            vulnificus].
ACCESSION   WP_103187859
VERSION     WP_103187859.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     gene            1..474
                     /gene="nrfA"
     Protein         1..474
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52934
     Region          1..474
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmass vsvtalvmta llnitavsae ekglvdprnd afelnhpdqy qswkktsesv
       61 eiedalaedp nmvilwagyg fakdynkarg hfyalddvrq tlrtggpqda ksgpmpmacw
      121 sckspdvarv idergedgyf egkwarlgae ianpigcadc hdtrsekfkn gepelaltrp
      181 yverafqain kpfeqqsrld kqasvcaqch veyyftgptk avkfpwdmgt gvqqmeeyyd
      241 algfadwtha vskapmlkaq hpgfetwreg ihgknkvvcv dchmpkvkke dgtvytdhkv
      301 gnpfdrfedt caqchtqskd qlreivstrk aqvlnmklta ekqivaahfe sgaawkagat
      361 edemkpilqd irhaqwrwdy aiashgvhmh apevalevlg tavdraadar tklvrllatk
      421 gitepvqipd isskaaaqka lgmdmekmna ekqhflktvv pdwdkaaaer esky
//
LOCUS       WP_103190799             577 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103190799
VERSION     WP_103190799.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..577
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=63788
     Region          <4..576
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvfintyve gnffddkltw kstfggdfiy nkrhrftpst npsfimndnq laqaiinrsn
       61 nqeflnentl nysetfgdhs invlagasfq tqssesvtin asdipsdgvg vnaiqlapae
      121 svaisssyse vhnlgvfgrv syiykdryvf naslrrdgks slgvnekyen fpsasfawkv
      181 keesfmqnvd aisdlkfrin ygrtgnsgvs afstianygi dnntilvdgv svpgvyqdei
      241 akpnlgweit dqfdagleis lfkrrltaev dvyykkttdl llaedvpdft gktelltnig
      301 evqnkgidiv lsgiiidtnd fkwdaslnis tyknevidlg qstflstknl tapavdessr
      361 lmvgqpvgif wgakylgfdp etgdaifedi sgpdgvpdgv ysgeyddqvi gnanpdfygg
      421 fqtnfkyknf dlsaffafsv gnetyseeff rvnettlnsf asirnnmysv nntenalypa
      481 vgsnnydlss slylqdasyl rlstlqlgyt lpsnlikgls klrlyftgsn lflvksddyl
      541 gfdpdvntga tgqlqrgfda iaypqsrnll lgidvsf
//
LOCUS       WP_103190800             424 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103190800
VERSION     WP_103190800.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..424
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=45442
     Region          22..>390
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkllttifi imisvsafsq ekmvtgkvvd ntgmplsgtt liikgtnngt mtdfdgeysi
       61 eakstdvitf syvgmktqtv tvgqsstini tmeedaaald evvvigygtv kkkdlagsva
      121 vvdtentfaa pvanpqnalq graagvqvts ssgapgsspe iiirggnsit ggnsplyvid
      181 gfvgadniss lnpndiesmq vlkdasstai ygargtngvi iittkkgklg kpvvnfrass
      241 giqslpdeid vqntlelatw fnnispdqtn lpydldnlpd tdtnwqkelt reavmsdyql
      301 svsggteavk yyvsggllnq dgivkgsgfd ryslrsnidf klskvfkagv nialsrtdke
      361 nntisftqll redpskpiyd eegeywigtn pilgtetgnl madallnddn ttldksfyqy
      421 irrr
//
LOCUS       WP_103190935            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103190935
VERSION     WP_103190935.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111914
     Region          26..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqflrmtfl fsflflgiqh vsaqekeitg tvtslgdgmp vaganvlivg ttngtltdfd
       61 gnyiitanlg dvirfsylgm ttkevtiaas stynvelsed seqlnevvvt algikkekka
      121 ltysaqevgg deltrvkqtn pinslsgksa gltitrsssg lggatkvvlr gntsttnndp
      181 lyvidgipml nsgngsngse agtdifgsqt gnrdggdams linpddiesm tvlkgasasa
      241 lygsqgangv ilittkkgkd galavnfnss ftvdnvtslp elqseyqsls vgqaiaengr
      301 vadaqswgaq tdglsndakd ffqtgftsin alsltagnqk aqtyfsyant igegvipenr
      361 ltrnnitlre takfldekid vsasinlsdq riwnrptngl ysnpltgvyl hpvgisrdly
      421 kdkyeyfnte lnqmdqyats fdeniqqnpy wlinrnpskd iaqrvlanvs vkyqitdafs
      481 lqsrgsfdks fytfdkrqya gtdpvnsgdn gryilekten sqqyidlian yntdfsedft
      541 fsgllgtslt kykigdqvyl dsgrdgdgli ypnvftianf astnnirqsv snrevqsvfg
      601 sanfgykdml fldvtgrsdw sstlvntdsn sffypsvglt tvltemidmp dfisfakvrg
      661 syaevgkdip vyatvplnai nntntgigta tfaplegetl eperqkgfei gtewrflgnr
      721 lsldftyyns ntfnqifyiq aepnpngysq nivnageiss dgielvvsgk pvvtdkftwn
      781 ttvnfaqnsn kvvavhpslq dgeaiitarg vngyeyslie gedfgsikar slirdengtp
      841 vinssgtlms tdfetvahaq pdftlgwnns feignfnvnf lidgkfggdv msvteavndk
      901 ygvsqasant rntndgmvnv vdesgaasqi saqeyynaig grdgmlgeyv ydatnvslre
      961 lsvgyrlqle ntslvdninf sliannlfff ykdapfdpni aastgmglqg vdiynqpstr
     1021 siglninvnf
//
LOCUS       WP_103191004            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103191004
VERSION     WP_103191004.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113322
     Region          27..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lflafvvqlt faqeklisgt vsdeaglplp gvniiikgts qgtqsdfdgn
       61 ytisaasgdv lsfsfmgykt tavtvgasss lnltmaqdls eldevvvtal girreekalg
      121 yssqsvssee lttvrdaniv nslsgkvagi nvtnasgavg sesrivirgi ssisgntqpl
      181 iivdgvvmdn tsygdsgayg gnstpngiad lnqddiasmn vlkggaatsl ygmrgangvi
      241 vittksgttk stqlgieiss svsfenayvl peyqnsygqg fdttyfeyvd gvtgdggide
      301 swgapldagy efiqwdsfdg eakpwvshpd nvkdfyetgi ttnnniafsk sgdgyngris
      361 lgmtdqkgii yntdlrkynl ggklnfdlsd kwsagmsvny iktessnlps lgygdannqi
      421 gqlvwsgrnv dfqalkdwen lplgyaagsd tatpinwnla ynnnpywald tntntfdrnr
      481 llgninityq itddlsftaq tgidyfssld tkrrafgtye strgsyeetq rtryeinsqa
      541 ilnynidite kfntslslgg qtmvnnyhrl ymaaselqvp dvynisntrd gvtpsldqsq
      601 tdqkinsgfg iasfsyddvv fldltgrndw asvlpstkns ffypganlsa ivsdianmnn
      661 tflklragwa qvgssgplsp yslepaytfg tawgttpvas spttlwnpni knetteefei
      721 gfdarffsnr lrvdftyydk etsdvimake isgasgnlyf wdnaatltnk gyevtlgadi
      781 irndgdgfnl gfsanfarnr nkaqdidddp ttnngsivlg glwnvdiqan egeavgtiyg
      841 pafarnddga iiysnglpti dptnqvlgni npdwtgglni dmsyknirfs tlfdvkwggd
      901 iysqtnswgn yagvlaetlp gretgiigeg vksdgsggwv andivqtast yygtvygsni
      961 gesavydasf vkwrelalfy dfplkkwakt gvdqlslgvt vrnlailykk tpnidpesaf
     1021 snstgaqgle yaqvpstrsi ginlnvkf
//
LOCUS       WP_103191006            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103191006
VERSION     WP_103191006.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116274
     Region          27..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lflafvvqit faqekaisgt vsdpnglplp gvniivkgtt ngtqtdfdgk
       61 ysitsatgei lsysfmgykt ktvtvgasat idvtleedla qldevvvtal gisrekkslg
      121 yasqevdgea vskvkaqnfv nslsgkvagl nikpsgtigg stnvvirgns svagnnqalf
      181 vvdgipidng nsnsstqqag gggydygnaa sdinpddies invlkgaaas alygsrasng
      241 vimittkkgk kqkgigvtin ssvtvgtpdk etlptyqkky gagygayyss sdgyfdlvdv
      301 ngdgildetv vftedasyga efdpdrliyq wnsiypgldt yqqatpwvaa endpntvwtt
      361 sstlinsvdl tggnekgtfr lgytnmmqeg nlpnssikrn nisfngslnl tekltastsf
      421 nfsktdgkgr ygtgydsknp mqqfrqwfqm nvdlkeqkda yfstgenitw nsnsvsdtsp
      481 iysdnfywtr yenyetdtrn rywgnvvldy eitdwlsvlg rftfdtysel qeeriavgsv
      541 dvseysrynr nvseynydlm lsfnkdltek inlsgiagfn lrqnntnsiy avtngglnla
      601 glyalsnsvn sieapseyda tkvvdgeyvq aslgydnfaf iegtyrtdrs sslpidnnry
      661 dywsatgsli fsqlleadwl sfgklrgnyg kvgndtdayn vfntyaigtp fnggiatnps
      721 aksnpdllpe eqtnweigle mqffqkrfgf dvtyydalne nqitsvplsn stgytsalln
      781 agtisnkgwe vtlnvtpirt enftwdmnvn wskneslvee ltdgidnlel asfqggvsin
      841 atpgeaygti rgtdltynen gepivgtngy yvrtstsnnv igdinadwka glynsftykn
      901 fnlsflidmq kggdvfsldt wygyatglyd ftagtndlgn pvrnsvadgg gvilpgvqad
      961 gsvntvraea ntyanpwgya raansqhvyd agyvklreat fsyslkdldr lpftgvtfsv
     1021 igrnlwiidk svpysdpeag lssgnaqgyq sgaypsirev gasvklqf
//
LOCUS       WP_103191008            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103191008
VERSION     WP_103191008.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112949
     Region          25..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklrgilt lflafvvqlt faqektvsgt vtgedglplp gttisvvgts sgtstdfdgn
       61 ytikasagsk lkysfmgfis qeitlgmsnt idvvlkedat sleevvvvay gtttkeaftg
      121 sagvvstkdl dlrplsspig aiegkvtgvq flsssgqpgs spsivirgvg tlngntdplf
      181 ivdgiafegg lgtlnqddie smtvlkdaas tslygsraan gvviittkkg krgsgitvna
      241 tsqygvitkg ineydavnpg qyyelmwqsy knalggdeaa aieasasiyn rlgrnpfnva
      301 ndeivdvngn fnpnaqiiae dldwygaler tgsrssnsin vsgggekhsv flsvsnldek
      361 gyviesdykr vtsrlsgtfd aadwlslggn vnisnekdhg ppsrgtsvan vfafaknmgs
      421 iyspylldpt tgailrdesg dviwdrgesv aslgipsrpt svgrnaleea ilnneltttd
      481 nygyrfnadf kpldglkvsf iygqdyqdgv nqsyenaevg dgaptgrfdd nryqrttenf
      541 nqiisynksf gehnfdltag hesfsrnyss nrafkstqta tgiyeldnfs vvldasgsst
      601 dyklegylar lnydfgnkyy lsasvrrdgs svftnnkwgt fysvggawri dqedfmqnsv
      661 fnslklrasy gevgndqlgs yyisqplyai ysnagepgiy wdttgnadlq wesldsydva
      721 leyglfnnri sgsfeyykkt tsdllynvpi pasegqieap dnigdlyneg feisinaaiv
      781 qsdkfswnlg lqastlknei tflpdpfidv skrweagrsr fdfylydyag vdpsngdalf
      841 ymyeevgdev gvavlnedgt hattnswada gkgyvgatav pdligsisns fsyknfelnv
      901 llsyqiggdi ldygyadmmh sgtygaslhp dalkawknpg ditdvprlen sntdlspsls
      961 srwltdasyl sirnvnlays lsnntidkig ldklrlfvtg enlfmfaere glnpqynlag
     1021 tpsgndynpn rvisiglnva f
//
LOCUS       WP_103191010            1016 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103191010
VERSION     WP_103191010.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..1016
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111754
     Region          24..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkacgvlt lllffmhfty aqqktitgsi tgpddlplpg tsimvkgsts gtssdfdgny
       61 silaspgqti ifsfvgykpq ekivgtsnti nvtleedasa ldeivlmgyt ktsrteltgs
      121 tvqlnnedfe qvpvstidqv lqgkvagltf nvnsgtpgst sdirirgrss ltagndplyv
      181 idgvpvssta ansttsgstf splasinsnn vesitvlkda sataaygarg tngvivittk
      241 ngksgkttfn fnssygfsnd avdgpqvltg aeretlyyeg vfntygesyg fdlagaqafs
      301 eannldggvy tawnaagrpe anwedvitnk daplmeynis asggdetynf ftslgyydqe
      361 atvigsdfqr ftgqvnlskd fsdkitfttr nsgsysyqdg lletsayfss pravkffmpp
      421 tdqpyddvgn inldtslpnp lwiaqedidd skftritsnn slnwelpipn ltfnttvaid
      481 lqlynykryr nrvdgdgast ngygwqsnst rtnyvfqnnl dyllninedh slnfkalqef
      541 qknrynylea daenfaddgl tnlnsagtpt tansyftdwa vasytglmhy sgyqgkyvld
      601 gtirregnsr fdasdrwgtf wsvgaaynmq keaflanssw lstlklrgsy gltgnanisi
      661 nqyqsllgyd gdyngtsaiy ldtfgadgls wetsksldlg idlgffnnri ttnltyyrrv
      721 tedmllnvnl pytsgfssqi anvgemenkg fefelnadvy rsekvsisfg gnlatnenev
      781 lkmyednsge etvisgttqr vesghpaygw ymvtsagvdt etgdelyyid gkgsettndy
      841 naanqawqgg salptitagi yvnieaynff lnvssyyagg hkvyedwary tngtdlfttl
      901 yyqgvdaild rwqepgdear fgkmryatta wqqnskflyd gdffrikdit fgynlpesvn
      961 siaglqsari fvkatnpytw vksdylkydp eidsdgftgl etpptksiil glninf
//
LOCUS       WP_103191634            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103191634
VERSION     WP_103191634.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113224
     Region          9..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhssfaqsit vsgnvtekgs dlplvgvsvv vdgtstgavt dfdgnftikt eettgkslnf
       61 sflgfkpvsv sltganqvvn lsmeedatsl devvvtalgi krekkslgys itkvggedla
      121 evktvsavns lqgrvagvni stssggasas srvvirgass ltgdnqplyv vdgipiinnt
      181 sssvvgatnd gtgdggddis slnpddiesv svlkgssaaa lygslasngv imittktgkg
      241 qrnlgvefss sftfdrintn lqnmqtrygq ginnlkpgye lddngnavei anaedaidds
      301 flytlqswga lmdgslvynw dgvkreyeyt gnnldkfyet gttavntlal skggedynyr
      361 fsfsdldnkd ifpgttlnrk slslnasati npkltstina kyivekthnr inigdtpgna
      421 ntvayvlpss lditdlkpgs ndegtellfq psqfitnpyw avndfnndde knrftastvl
      481 rydvtdwlyv lgragidtyd lsrtnvtpyg tayqpagqmt qskstytsvn sdvmlgveka
      541 itskistnsi fgansrtntf eqlsatgynf ivvgledlnn ttlpeptnsy yetktnslyg
      601 sievdyekyl yltftgrndw fstlsypgke spnndfywsl sssllltdll nlpevfnytk
      661 vrasyaqvag gasdayslnl dyaitgsfqg qsygqinsss ipnpdltpfk kteyefgles
      721 nffqnrlgid fayysnnttn divtasasqa sgyssailni gelsnkgief lirgtpiqtd
      781 dfswntsfni gyndseivht ddedtsinvd gsesrsgtai iahivgenyg viygssyerd
      841 dagnivydns gsipkpvqge nkilgqgvap ytlgfynsfk yknfslgfli dakfggsvhs
      901 gtnrelmmrg lhkktlegre sglvvsgtds etgesfsttv dpenlrffyg yigaesagia
      961 eefvystdfi kfrelsfsys vprealssvf iddlrlsfia rnlfyiskai dnvdpeaaln
     1021 nlnsqgierf gvpstqslgf svnvkf
//
LOCUS       WP_103191640            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103191640
VERSION     WP_103191640.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112886
     Region          73..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvflfsllkl asfcilyail efvfyifnil tntiilmkkt nnlfslfkrt kfmfsfllfm
       61 lfgfglqsqt lytlkgsvkd nlgtpatgvt vqlkntnqgt itdfdgnyel svnlepgdyt
      121 lvfrllgltt qdvnvtlank tevvsdvemt mdilgldqvv itgagaltsk rqlgntissi
      181 kggeiseags vditgalsgk lagiqvsqns gdpaggisvr lrssstvngs sdplyiidgv
      241 ivnnnstdvl gstsvvqnrm sdispqdidr ievikgaaaa aiygsrasng vvqiftkkgq
      301 sgepvitiss svnfnslrkk rdyndepfew vssditvldk veatrydyqd mvfenstgtd
      361 nyasmsggkg ntnyfgsfsy lkndgilkst nyqrqsgrir vnqvindwvs asfgtyfsts
      421 ksqdqpnggy vagilptilf tnntidprpd edgnyptmtf ypnileyint fdfnqknnrn
      481 isdlqitltp vdglkvnyiv gydssestgn tyipigttti elgsagttii nttqfnsdln
      541 gsynfdindm ftsttttgfs wqqdetsyss isgtglalgv kttngaasid tyesrsertf
      601 wggflqqtfg ikdklfltga irldgssvfg edernqwypk asmsylvske dfwehtfgsa
      661 lnsfkfraaw gqagnltaig pfdrlsnysa isidgtsgli aptelgnadl kperqtevef
      721 gvdmglfnnr igveltyykq diedlllart lspstgfgsr venvgtmtnq gfealvtatp
      781 iqmndfswtv tgtfstnkne vndiegdqfs ignfgfsvak ngqplgvfyq gyyarnedgs
      841 llltegglpq reqgsydadg npvaerdasg qpsganlskv igdpnpdfia sltnefqykn
      901 fsfrvqldav qgvdllswdt rmfyrfggge qtakelrges vrgtgaanfn iaesyiedgs
      961 yiklrelsts yllkdplegv dsvkftitgr nlfsidnfsg ydpevnmdgq sngsrggvmg
     1021 lvpipsvvkf gvvatf
//
LOCUS       WP_103192137            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103192137
VERSION     WP_103192137.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112895
     Region          46..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkntfvnkvm rlliyvlcvt falepynvws ypltnsltin llqqkqeisg hildgngipv
       61 fgvnvlikgt qqgtytkedg tfsivaassd vlvisylgfk tieievglkk qltitleddi
      121 taldvvnina gyyavseker tgniakvdsk iiekqpvnnp lgamqgymsg vdiiqdtgvp
      181 gggydiqirg knfingstep lyivdgvpfg seslgvsevs aginngnisp lnalsptdie
      241 sievlkdada taiygargan gvvlittkrg eagttqfkmn vtsslgqvsh fldlmntsey
      301 lelrreavtn dgygalless afdfvwpdlk twdqdrytnw qkeliggtay rntaqlsvsg
      361 gsaqtqflis gayqkettvf pgdsnykkys ihsnlnhssd nekfsinmsa nyakehnymp
      421 rtdltnmayn lspnapelyt edgelnwenn twdnplavle deyyaeintl mtninlsyll
      481 lpslkvlgnl gynnyqitsy klllntsrnp sfgftpegys sittndssrd swiiepqlqw
      541 vkqwgninld vlvgttfqsq ttdqlvikgt gfpnnslvnn iaaaseleir nstnseynyq
      601 affgrinlkl kdryiinltg rrdgssrfgp gkqfgnfgav gvawvfkeea vlksnavlsf
      661 gklrgsygtt gsdnigdykf lstysvtgnd ydgtlvleps gisnpffgwe vnnkleigle
      721 lgffknrmll ntawyqnrss nqlvgiplaa ttgfssltgn fdatvqntgl efdvhvkniq
      781 genfqwttsf nmslpkskll efpnlensvf askyvvgqpi tiqklfnalg vdpdtgmyqf
      841 edynndgais sledrqwied lapefygglg ntfsyknlsl dvffqfkkqk synelkqqaa
      901 pglmnnasvs flnrwqepgd qtplmiatsg fdfnlipsrd nyrlsnrtis dasyirlrni
      961 tlnyslpkal tqklalnvyv qgqnlwtltk fkgpdpdqps yiilpplrqi aigaqihf
//
LOCUS       WP_103192364             797 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103192364
VERSION     WP_103192364.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..797
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=86117
     Region          122..>797
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkalfrnvfr ltlficfisa ypsygmsenm dstqvtlner gatlveilsk iskitdfnit
       61 ygdfiaknkh pydavytnta lhtvlsdlgk qahfsfkvng sdvlighptk qtaetavqek
      121 mtltgkvfdd mnlplpgani veqgttngvt tdydgnftit lsqanatiiv sylgyttqhv
      181 avngrsdisi tlevdaagld evvvvgygsv kksdltgavs svsaddlvaf pvvdatqalq
      241 graagvsvqa tngapgsdys iqirgntsin asndplivvd gfiggimppa ediqsievlk
      301 dasstavyga rgangviivs tkrgakgkpq fsfstsyssq teinrldlln anqftdyite
      361 ldpdfipelt gegtdwqdei yrtggvqnyq lsiaggsdai syyvsgaiyd qegvvkdsdy
      421 krysvttnld lqaseavkfg tslfvrrsyt ngvksqeggd aaqtgvisga ykfsptqsit
      481 dangdfalsi vgypidnpya lateyqnevi advfqgnvya eidllkdlkf kttlgtsihd
      541 srtgqyyptt ldrgnsvgge atlntykats fisenyltya ktfaevhefa amagyslqkd
      601 rtevttslas gfisdsfsfw nlgagsnass vdselyestf eavfgrinyt lngkylftft
      661 grregssvfa knnkygffps aafgwkisde nfladsntis llklrvsyge vgnqaispyq
      721 slasftdvft tvqgsavtai rpstisnndl twettaqtnv gidvellrnr fgltldyykm
      781 kttdllfdvp tpnytgf
//
LOCUS       WP_103192506             446 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103192506
VERSION     WP_103192506.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..446
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=49058
     Region          <4..445
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miifderyll tltyrrdgss kfgdgnkwgd fpaaalawnv hnedffksdl isqlklrtsi
       61 gitgndrfgv glgqstfsps asvttdgttl aigtissrvg nedlqweetk kfdlalemgl
      121 fnnaltmelg yyknnttnll ldktiapsng iesiltnage venrgyeigl nynktfnsgf
      181 nwttnlnfsq nenevinlel iegtdflpge earidgnvsg sysvlkeglp igtiygyryl
      241 gilkdgetsa tqptavagdp lfedlngdgq itgedkesig ngyakynlgf nntfsyknit
      301 lsvfltgvfd vdklngnnvi gyqyntleia kerwtpsnte gtlpqdlwqg dqwvndyfve
      361 dasyvrlqnv slsydfsrdv ldkigistlq lsligtnlat wnnysgfdpe vnstrtsgtn
      421 lntgaglday sypyqksftl gvkvgi
//
LOCUS       WP_103192507             575 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Formosa
            algae].
ACCESSION   WP_103192507
VERSION     WP_103192507.1
KEYWORDS    RefSeq.
SOURCE      Formosa algae
  ORGANISM  Formosa algae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Formosa.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Formosa algae"
                     /db_xref="taxon:225843"
     Protein         1..575
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=62162
     Region          25..>575
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlfkiic vlifgvvipv qaqeknikgt lvdtdgaplp gatitikgts kgvvsdfdgn
       61 fsttaspgnv lvfsflgyst kevkintetn lrvvlesevs qldetviigy gsvrkedltg
      121 svavideknf nqgpsvgven liqgrasgvq isttssepga dmlvrirgnn svnsnnnply
      181 vvdgfpmesl snsinpadis svsilkdasa taiygtrgan gvviittkrg kkgqssityt
      241 gsfsiqnani daydfidsad yatlqnqidi sngiapsytd eaiaridelg lqtnwldeaf
      301 rtgytsehql avrggnddtk mffsagvysw dgvvkntsfd rynirlnadq dllddrikvg
      361 vntslsates dflgfsassl qdnilrgifq tsplnptydv ydalstedka lifgnssptd
      421 pletleimdn ngtnyfvlan afleakifnd ftfktqggar ivnqkisqfl psysslvass
      481 ldpgsarqsh llykyytysn llsydksigk hsinavagyt hewsseeyfs agssdfttda
      541 lgyyslqsga tiltpssyia eselasylar vnynf
//
LOCUS       WP_103194064             474 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            vulnificus].
ACCESSION   WP_103194064
VERSION     WP_103194064.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     gene            1..474
                     /gene="nrfA"
     Protein         1..474
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52947
     Region          1..474
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmass vsvtalvmta llnitavsae ekglvdprnd afeqnhpdqy qswkktsesv
       61 eiedalaedp nmvilwagyg fakdynkarg hfyalddvrq tlrtggpqda ksgpmpmacw
      121 sckspdvarv idergedgyf egkwarlgae ianpigcadc hdtrsekfnn gepelaltrp
      181 yverafqain kpfeqqsrld kqasvcaqch veyyftgptk avkfpwdmgt gvqqmeeyyd
      241 algfadwtha vskapmlkaq hpgfetwreg ihgknkvvcv dchmpkvkke dgtvytdhkv
      301 gnpfdrfedt caqchtqskd qlreivstrk aqvlnmklta ekqivaahfe agaawkagat
      361 eeemkpilqd irhaqwrwdy aiashgvhmh apevalevlg tavdraadar tklvrllatk
      421 gitepvqipd istkaaaqka lgmdmekmna ekqhflktvv pdwdkaaaer esky
//
LOCUS       WP_103198127             195 aa            linear   BCT 07-JUL-2024
DEFINITION  cytochrome c nitrite reductase pentaheme subunit [Vibrio
            vulnificus].
ACCESSION   WP_103198127
VERSION     WP_103198127.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03146.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     gene            1..195
                     /gene="nrfB"
     Protein         1..195
                     /product="cytochrome c nitrite reductase pentaheme
                     subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=21704
     Region          7..194
                     /region_name="PRK11659"
                     /note="cytochrome c nitrite reductase pentaheme subunit;
                     Provisional"
                     /db_xref="CDD:183264"
ORIGIN      
        1 mgniklaivi mlksilafsf ygysisaiad tsvateatds srfqvelird rdykcvqchk
       61 dsketlsgsh gedahkilgr evnctechnn igpdhregap lvtkyssaqs kqgtekvfmd
      121 tsailkansa ctdchqpqyl redswthdvh aknltcsnch dvhankakvl glerkekikm
      181 cvdchsdfnq keeer
//
LOCUS       WP_103198128             474 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            vulnificus].
ACCESSION   WP_103198128
VERSION     WP_103198128.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     gene            1..474
                     /gene="nrfA"
     Protein         1..474
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52947
     Region          1..474
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmass vsvtalvmta llnitavsae ekglvdprnd afeqnhpdqy qswkktsesv
       61 eiedalaedp nmvilwagyg fakdynkarg hfyalddvrq tlrtggpqda ksgpmpmacw
      121 sckspdvarv idergedgyf egkwarlgae itnpigcadc hdtrsekfkn gepelaltrp
      181 yverafqain kpfeqqsrld kqasvcaqch veyyftgptk avkfpwdmgt gvqqmeeyyd
      241 algfadwtha vskapmlkaq hpgfetwreg ihgknkvvcv dchmpkvkke dgtvytdhkv
      301 gnpfdrfedt caqchtqskd qlreivstrk aqvlnmklta ekqivaahfe agaawkagat
      361 edemkpilqd irhaqwrwdy aiashgvhmh apevalevlg tavdraadar tklvrllatk
      421 gitepvqipd isskaaaqka lgmdmekmna ekqhflktvv pdwdkaaaer eaky
//
LOCUS       WP_103225342             527 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Roseibium
            marinum].
ACCESSION   WP_103225342
VERSION     WP_103225342.1
KEYWORDS    RefSeq.
SOURCE      Roseibium marinum
  ORGANISM  Roseibium marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Roseibium marinum"
                     /db_xref="taxon:281252"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55844
     Region          5..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpealkigtp ketfpgearv amtpdsakql qklgyscliq sgagaaagfs dkayedagve
       61 viktaaslwk ksdivtkvrq pdeketrhlt kgktlisffn pggneaglea arakganvia
      121 memvprisra qkmdalssma niagyravie agnnfgrfft gqitaagkvp pakvlvvgag
      181 vaglaaigta tslgavtyaf dvrpevaeqv esmgaefvyl dfeeeqqdga atggyasvss
      241 pefreaqlak frqlapemdi vittalipnr papklwledm iaamkpgsvi vdlaaerggn
      301 aegtvadekv vtangvtivg ytdfpsrmas qastlyatni rhmltdltpe kdgqvvhnme
      361 ddvirgatvt yqgeitfppp ppkiqaiaak pkekpkeltp eekrarevaa fkaqtkqqvs
      421 llagggllll lvgliapasf mqhfivfvla vfvgfqviwn vshslhtplm avtnaissii
      481 ilgavmqigs gsflvillag lsvfmagini fggflvtrrm lamfqks
//
LOCUS       WP_103231117             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103231117
VERSION     WP_103231117.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107168
     Region          29..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkavipvlf vfsisanaqe kksadttktn sieevvvtsl gikrqarslt yssqqiggde
       61 ltevktpnll nsingkvsnv qinrtngvgs svrvimrgnk svsnsqplyv vdgipiingt
      121 gksadisqys nmpdpgdvls sinpddiesi nflkgasasa lygsaggnga ilittrkgki
      181 gkssiaysts ltverayslp klqhsylsyd psvptqspgn nieswgakgs skdylkdflq
      241 tgttwvnsls fqsgnekstn yfsignttnk gvipmsyfdq ynisfrnssk flddkltlda
      301 nfigslqdsk nrqtpgasfs plaslywlpr gvdfdqyged nysfidkkrl lpgqnwwevn
      361 qdgsfkgnpe tqnpywilnk nqvtvknkna ysavslsyei npwltarvrg nyswnssdsq
      421 rdisaysaps llavkegvng rmlkniyens stygdvllig spklsesisl dftvggsvnt
      481 tsnkvtqvdn aylsipnlft innlqwnvdr spgdgyhniy wnlkkqvrsv fasasvgykn
      541 mfyvdmtfrn dwdstlaltg rsgfdyesvg anailssifk lpevinfwkv rgsyatvglg
      601 lpanisnamv ayynaysygv dagnivypks sfvtsrpdli prpelnktfe agtelrmfsn
      661 rlnfdltyyn snasnqllet tigsnfggip sgsyyinagk irntgfeasl sykvfgteqf
      721 gwtttvnasa nkntivelfp sslpisenql fsltgggdft klrlggsfgd lygvkfkrdd
      781 qgrvlvdeng vplgttgdpq ylgnpnpkfi igfnnsfnig klgisflidg kfggkvlslt
      841 ekandlygvs qatadardag gvsipnavya pgtplagqay ngvtdakayy krtggaggig
      901 tgideaylys attvrlrqas isysfniqsk ymrnatvslv gtnlfffykk apfdpeqvsg
      961 ntpggvgvds fglpvtrsig lslkanf
//
LOCUS       WP_103231203             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103231203
VERSION     WP_103231203.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110273
     Region          29..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknsyykigg iffglmlstv stnikaqtrt isgtvtafnk plsgvsisqe gsdqvtttse
       61 ngtytlkvsa enpillfrhp dyaeeritat nqtvvnisle qkvkgieevi lnagyykvkd
      121 kertgsiakv sakdienqpv tnvlsaaqgr magvsitqns gtpgggfdvq irgknslrsa
      181 gnaplyvldg ipvggemasq fsaqilpass inplnsinpn diesleilkd adataiygsr
      241 gangvilitt kkgksgklsl hfgtaysvss vinklkmlnt adythmrtta yqndgianyp
      301 pnaydingiw dlnrntdwgk tligntadaf nshlslsggn ertsflvsya hseqstvfsp
      361 eykyktnnls sslkhtssdn rfqlnvsnrf stqnnnvvse ditkrsllls pnapqlygen
      421 gninwenntf nnpiaiyttt ysnqniqfln ninaqyelld dlvlqlnggi nyqsfdersl
      481 kpntmynpat vqgqssaysq ssknnqdrfs filepqlnwq fkknkhkldv lvgttfqret
      541 neqgsvigvg fesnvfleni gaaqtkiisd qirteyryaa fygrlnyqfa gkyilnmtgr
      601 rdgssrfgpn nkfanfgalg aawifseenf lkgkkwlsfg klrssigsag sdnigdygyl
      661 dtytvsssty ntstglnpsr lynpsyswek tvkaeaalel gflknrinlv aawyrnrssn
      721 qlvgyqlpat tgfssvlanl datvensgwe felnikplag kdlqwemgfn isfpknklis
      781 fpglegstya nsyiigqpts ivklyqyegi npatgiyqfm dfngdgkiss pndrqsvani
      841 gvqyfggwtn slryknwnls fmfqfvkqkn wnynnimpip gsmnnqpsev lnvwslenpq
      901 gyympyssgs ngvknqaqvf ftgstasvsd asfirlknie lgyqlpldns ifksvkvyfq
      961 gqnlltftdy fgidpefrti gylpplktys lgilvsl
//
LOCUS       WP_103231874             963 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103231874
VERSION     WP_103231874.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..963
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105359
     Region          39..961
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlsa galfffggmv iaqqqtttkk kdtvkketsi devvllgysk sitkpkstva
       61 sntvgevffe nrpnvnmlts lqgsapgvim nggsgspgsa kfsllirgts singntdali
      121 viddipsnas eyrnlnpndi esttilkdaa ataiygnrga ngvvvirtkr gkynsgfkls
      181 ytgmtgmslr pldkynlant eqymgimkly gfsdtnseyi kakdalaqgi ntdwknyffk
      241 pemfqshdva lstgganiss ynsfgymeqg gavpttdfkr ftvrsnvqak skdnklnvns
      301 qislafsrrn elleetssgi rnnsvqnpll gvlqglpyls ptkfsngqdl fnsigtnfnn
      361 gnniyvlqnl ltrgnlpnmv dqvsiganlg atyainknft vgnklgidyr qsdrisgrap
      421 waylalatkg ankytgfedq tttrdlsinn vvsamysgkt gehsvdasvn meynkvyyra
      481 tsrrqngldp rtyvpgsgtg yvpfdntaas pyvpsvsgsr itagtlgvfg tvsydyagrf
      541 gfqgtlrrda tyrfkgdnkw atywsvagrw nidkesfmeg stfnslklra sygtngnqni
      601 vaaaagsnpl ltasqiirdl yttptgygnt lgigfnyanp fvqwedvaqa nigldftlln
      661 nklegtfdvy hkkttnlfgv ipisgfsgay svsgnngamt nkgvelglry niiktqdlnf
      721 sifangsynn nkineyiing dpepgttvnm aghtysewyv ykyagvnksn gnllfyskdg
      781 gvteapkved aqfldvspip kyagsfgfes gykgfffdal ftfqkgvkkf dnalywlanp
      841 eglgssavgs snmstdllna wtpqnqnsdv pslratnwgy tadsdyfikd asflkvrsvt
      901 igyqlrkeql qnlpitglri yvqgenlytw tkwrgfdpep itgsnlsvyp nprmytvgvk
      961 idf
//
LOCUS       WP_103231689            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103231689
VERSION     WP_103231689.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111782
     Region          30..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknfcslsh iqlafgftll asgvaigqmr vitgtvtdnt nnkpisgvsi fqegsdtvat
       61 tnssgiyrvq vsvenpvlvf khpdypdrkv slgdrvsvdv slgnengsgs enenrkgsen
      121 ekaieevvln agyykvrdke rtgsiakvsa kdienqpvtn vlasaqgrms gvsitqnsgt
      181 pgggfdiqir gknsirregn eplyiidgip ilsetpsvys aailpyssis plnainpndi
      241 esfevlkdad ataiygsrga ngviivttkk gkkgrselkl ntsysiskva nrlkmmntse
      301 ylgmrrqafq ndgiaipaia ydlntwsqer etdwqkelig nnsdasvvql slsggsdnts
      361 ylisyghqeq stvypagfqy ktnnltgnfs yrspdrklev nltntvsfqd nnvvnddltk
      421 rsltlspnap alynadgsln wenstftnpv asfvseylns ssfintgtqi ayklfpfvsl
      481 kfnggmtynn feeyslkpht mynpssglts ansnssknns ssfsyilepq ivgdyswndh
      541 svemlvgatl qqsetksgtl qgygfesnal irniaaaktk vigdqvnnqy nytavfarln
      601 ykylkryivn vtgrrdgssr fgpnnrfgnf gavgaawlvs eeswmknmsw lslakirgsi
      661 gtsgndrigd yqyldtytvs tniynnitgl npsrlynpnf swektlkkev aaefsffknr
      721 wnlsvayyen tssnqlvgip lpattgfpsi qsnlpakvqn tgweletsvq vfrnskfryd
      781 tsfnisipns kllefpnleg styanqyvig ypttlvkvyq feginpatgv yqftdfnndg
      841 kisspddnkv ierigmqffg gwsnnlsygp wsasflwyfv kqrnwnynrq mvipgsmnnq
      901 pvevldvwsa snpsgtympy ssgsvaakts ahsffqnsta aigdtsfirl kniqlnysip
      961 vrefgikeam iyvqgqnllt itkyfgldpe faltgylppl ktyslgfqii f
//
LOCUS       WP_103233018             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103233018
VERSION     WP_103233018.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107729
     Region          16..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltasllv lvmsssiava naqqkndtik tkeiegvvvt algikrekks lgyaseevka
       61 aeltggttnt gnvasllsgk vaglqvntnn nfggsanlli rgykslsggs plividgspv
      121 nnntvtgstf dygnflsdvn qediesvnvl kgaaasalyg ergsdgvili vtksgrgnnd
      181 gswgvtlnsg itagfidkst fptyqkkyga gyggqawned pgpggynyan fvddasygpa
      241 fnpnqlvyqw dsfdpsspny gkatpwvaak ngpikffetp vtyintitie kgnktsnlsl
      301 sysnmlsngl mpnselrknt isakfnhdft dklhasvftt ltlqdtkgrn etgysdnvvt
      361 gfrqwwqtnv dvlalrdayt nngnsnfswn rstaadgtpq ywnnpyfqry qnyqsdnrtr
      421 ifsyaqlkyd vsknfgitgk lsyddlqmvv eerlmngslp qafgasqlnv ssgyartnvk
      481 nteinfdlfa nykfditsdl svsgiaggnv rrnlvdnifm stegglskpg lfaisnsirt
      541 ilppdenyak wvtsslyata sfgyknflfv dgtyrvdqss nlpkgnnsyg ypsvtgaiil
      601 sefvkqpwls fwklranyae vgsstnnfrl vntfkargeg lfdqpyflan pnlkpqrske
      661 tefgmeaqff knrlgfdvai yktrtfdqii nlpvssatgy rtflvnagqi dnkgvevqln
      721 gtpfktdnft wdvnvnwskn enkvialngd sqnylmasyq ggvslnarvg esfgalvgsd
      781 yvynsngdrv idpatgrylr nnnqvignit pdwvggirns frykdftvsf lidvkkggdv
      841 fstdmyygla tglyaetady reggfvhpgv npngnvnttp ainpgsfgnv dgyrrmpnkr
      901 fvydasyvkl reasigyslp ksilantsir eakisivgrn lwiihknlpy adpeagtgng
      961 laskgnsigv lpttrdigid ltlkf
//
LOCUS       WP_103233020            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103233020
VERSION     WP_103233020.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109743
     Region          32..1008
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttsvli valsssffia naqekggdti ktktieevvv tgalgikkkv daitnaqqvv
       61 gtkelnqasa pnavqaltgk vsglqitqtd nsvgassriv irgnksisgg nealvvidnv
      121 issasvlaql ppevienvnv ikglqgaaly gqqgvngvii vttkkgakge kmqftltssi
      181 qmsqafkfpi iqkqygkgyp hepafsagdp nyngttyvpf enmswgpayn dpniggqmvp
      241 sglpqadgsf iyekyapvdn hfskffkngv ilqngvtins ggadsyamls inrlendfvv
      301 egdqlrqnsf llkagkkldk lridgtvnyi skvtnqssad lysdilqmps mndirkyrns
      361 gvagglsaft knpyyqleht rqntvndyls gilslqydfn kninltytgn lylnnsrsdn
      421 hddgfkasqv yngsglvldg gtlqdytgss nfdsyyinrt vstrsyygdl mlnfnydltd
      481 ninlklnign niqdsyrtar smggtnlvvp gwydirnvtn liqpgnsaga tvldnilfen
      541 tttrqrtvag fanldlsykd ylflnstfri eessvlstyy ngqvhnksyp yysvglsfvp
      601 tkafealkgn niinyikiap gytrvgntsg vlpydtsnvg iapagypfpn lpgygidatq
      661 tnrtirpefi stydlnvqlg flndritleg siyqsdtkdl itnanvsnas gisnlkdnfg
      721 ktrmrgfeid lgitpfksqn ftwnvrasfa ksrstvldlp ngldevalav pfttvgigvf
      781 avkgsdlqvi kattfqrddq grvivgadgv plqnttlssm grvtpdytlg fntslkfkgf
      841 tlsatmdyrk ggkfasfsks lltftgasee tagfdrskgy vipnsvqmvg gqyvqnntpv
      901 ggtadydgva gyfssqslqr lgepmvldat afkvreials ydvpksvlss tfvtgitvgl
      961 farnpffvys kenrnyadpe tsytsgngag ialaeqypsq rsfginlkat f
//
LOCUS       WP_103233302             950 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103233302
VERSION     WP_103233302.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 950)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 950)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 950)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..950
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104121
     Region          6..948
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklsvltv gvlfftgqtv laqekdskns kdketkleev vvlgysktat kakttsssvt
       61 vgaetlenrp nisvlnsiqg tapgivvnsa sgspgsgkfn ilirgtssln gstdplyvvd
      121 gvitsgsqfr nlnsydidtf silkdaqata iygnraangv vvittkggkf nsglkvsyda
      181 ltsfsklpts dynmsdarql lqiqktlgtg kggtltqdgi nnwgtntdws kqfthigisq
      241 qhnlsitggg eninnffslg yldsegtvrs tdfkrftmrn nlngktkdgk ltfgaimglg
      301 ysrrnqldde tntgisnntl qnplfggvls lpyiapspya ngldlynaik gdatnnrqwi
      361 lqdninggir nrftelsisa nanvnykitd ylsvgnrtgi eykqyernfa rsplgylais
      421 vakgdgstyg gfedfsttrd ltfnsitnis fnksfgdhti saaayldyik ahvtstsqrq
      481 nglnplqwef gagtgyipfn pdtpniyrps nsatkvtagt layfatvdyd ykdkygvsgv
      541 vrrdgsyrfl ptnrwetfws vaarwnvdke efmadsgfrl lklrasigtt gnqnlgiagd
      601 nqnplallpn nflnlyngvs gyqnllgynf vnlsnpslew eqvkqsnigl dfnykglieg
      661 sfdyyqkrtt rmfndlqlsa vtgtyafrgn dgildnkgie gmikynvirn entrfsvfvn
      721 gsynsnkivs mgsenlsgdv vnaiggpagq yqlysyvgvn rdngnlefld kngnvteapt
      781 sadrvltgks ryakftggfg fnvqhkgwfl dtlfsfqqgg wiydnlqswi mdpsaagtrn
      841 lsadllnawt pdnrdtdvpa lkasnlslgs sdrflhksdf irlknisigy nfsksqlgkl
      901 pvkgikvfvq aenlytwtdw kgfdpepits yslnvypnpk tvsvglnvdf
//
LOCUS       WP_103233364             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103233364
VERSION     WP_103233364.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109124
     Region          36..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkqcklgv lalllfaeyg faqskdslsk etsikevvvv afgkqkkeei tgsvqslkak
       61 dlsnlqngni lqgiggkvag vqvissgqpg sqptirmrgi gsinassdpl ivldgipysg
      121 nlnsiassdi esisfledas snalygsrga ngviivntkr gknkglsiea dvrtgvnfrs
      181 iedysvytsp qdyytayynr arigeiarlk qpgavpsgps phdvglaaln klgydaynip
      241 fnqliskdgs fnpdakllyq dnwkkllfrp alrreatvgi nansdqvksy tslnylddkg
      301 ylissgferf girsnvdysi tsklkltsal sytyskqdfg etggfsnpfq farniapfyp
      361 vflrddnyqr lydnngnaly dygdgqgpng atrsyavfen pvgnlqkdks qiisnitnln
      421 lglnyeiikg ldftynfgay lentrnlqfg nteggtsssv ggtisqgsnf kytlnhqqll
      481 tyqkklgshs fnilvgheln kikddgfsgs kqqlllpnsq sfdnavkitd lsgsgyeyav
      541 egyftrllyn ydgkyffnan irrdgssvfs pesrwgnfyg lglawniake dflkdntvin
      601 slklkasygq qgndnillsg ssrdyyayqd iyginnfgdd kpvlslkkqg nkdlkwetsk
      661 nlnagfeisl lknrinlnad yferkvsdmi ytlplppsna gyyvkygnig dmtnrgvqan
      721 isvdilrgde fqwsiyanat hyknkitrlp aeqrntglvs glfilaeggd rytyflkefa
      781 gvnpdngdal wyrtsinpvt qkeertvtnn ykeatdyntg ksaipkvygg fgtdfsyqrf
      841 nlavnfayqf ggygyddvyr slfhsdsygs nystdldktw tpenptaalp rvdlnatnqn
      901 gnstlyliks dyislqditl syqlpdgfaq qaglsglkiy vtgnnlylws krkgydprts
      961 ltgvsdsyry sllssvslgf klnf
//
LOCUS       WP_103233596            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103233596
VERSION     WP_103233596.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124210
     Region          22..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlillpl laanivmaqq kktitgkied gntshiitga sikietqsvs sktelegiie
       61 svsvgtvtdk dgkfileipe dtksvlvsyp gyesrviqln egqtnytirl tsevtdknki
      121 qeviitgyqk iekrkqtsav stvkmdnisq agvasvdqml agqiagvavt petgapgspa
      181 kirirgtasl sgpqdplwvi dglplegndv pnftdkdnid qlqnfsiagl npndiediti
      241 lkdaaataiy garaangvis ittkkgkkgs lklnfsadtf itsrpdfgkl nlmnasekvd
      301 lelmlakrad ltyradkgev mriltqnsql dafrnggfda lnsftrqqin glrnnnadwg
      361 kllyrnaink qyglsvsggs dradyyfslg yydeegttig tgfkrynltl knnyklsdkl
      421 nagisifgtq sertsfvtda dasinpvnys rnanpylkpf nadgsynydk dmdgyedryv
      481 pfnfleeren tnyslknnsl kaildleyka skslrftsql glqydtnkte kfaaentyft
      541 rkmrentryy kdgkynyflp agavkqnwdn dffqynwklq aaystkinsk heidlmagte
      601 irktedntti trafgydpkt rrataivfpn sgfaadkrye tyreaapien ayasmfatas
      661 ytydqkytff gsvrydgtnl fgvnkkykyl piwalsgswl vtkedfmknv savsnlrlra
      721 syglqgnidr ntspffigey ndatilpgmk egvinvispp ndklrwektt ntnvgldlgl
      781 fnnrvsltad vysrkgtdmi smretpletg feytmmnwgs ltnkgfelai strninhdnf
      841 kwtttinfah nksrvlseqp rdnsflpsre glpvnavfal ktagmdehgn plfwkgdqki
      901 saaeffklyd vyadflpgql vdtklsnael rslftyvgdr dpkftggiin tfkisdfdlt
      961 isatfnlkqt vmrtpsyrgm dldrgrnytr diyeaggslp gitspdmdan pdgwmankwf
     1021 asnrssaynl ldvwakeisy irissirlgy tlpkeftnpm gisslrlsve grnlfvfsng
     1081 ysgyfdpety gniyaqpitk svtvgfnvsf
//
LOCUS       WP_103234249            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103234249
VERSION     WP_103234249.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114830
     Region          153..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknvvvytai lvflnlsalc aqqhisdkrv nyrtgkisaa kavsdfltan qleyaysaea
       61 lekytiqgvq ctnesvqncm kkilkglpfe vlikfnsvii keikpgtskt nlsetgdpet
      121 ipqnkalvka eiqspndtik reqlikeivl nagyyavkdk ertgsiskvt akdienqpvt
      181 nvlstlqgrm agvnitqnsg vpgggfdiqi rgknslrtag naplyiidgv pmgsemtspy
      241 sgvimpgasi nplnsinpnd iesleilkda dataiygsrg angvvlittk kgksgklglh
      301 fttsyglsqv askmkmmnte qyldmrrqaf andgitnypa taydingtwg qnrntdwvkt
      361 ligntaassn sqlslkggse tttfllslgh neqttafgrd fkylsnniss nishrspdkk
      421 fqltisnlfs iqknnvlrsd itrqaywlsp napdlyhqdg slnwenntfa npvaaynsty
      481 sneskqfltn vntqyelfpn ikiklnggin yqifdelalq phtmynpsfa lgqssatsra
      541 sknnhdrfsf iiepqinwty kknehefdal vggtfqremn kqgtmtgvgf esnvfienig
      601 aaqtkiisdq irteyryaav fgrlnyqfkn ryilnitgrr dgssrfgpnk rfanfgaiga
      661 awlfskenll kdnkwlsfgk lrgsygsags dqigdyqyld tyavsssiyn gttgllpsrl
      721 ynpdyswekt tkletalelg ffknrlnlta awyrnlssnq lvgiqlpsvt gfpsvlanlp
      781 atventgfel elnarpfksg eiqwetgfni sfpknklisf pglegstyan qyvigqptsi
      841 ikvyqlegid pqtgqyrftd fngdgkissp ddnkviekig veyfggwnnt lhyknwdlsi
      901 lfqfvkqrnr nynsimpvpg gmtnqpleil nvwsaenqgg fympyrsgvs tahnlfqnst
      961 aavsdasfir lknlqlgyri plknsvfkdv kvffqgqnli twtnyfgidp eflgmgflpp
     1021 lrtysfgaqf nl
//
LOCUS       WP_103235329             917 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium viscerum].
ACCESSION   WP_103235329
VERSION     WP_103235329.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium viscerum
  ORGANISM  Chryseobacterium viscerum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Chryseobacterium viscerum"
                     /db_xref="taxon:1037377"
     Protein         1..917
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100599
     Region          30..915
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfttvlki apafllastv mhaqkkdslp qekkieevvl igygkqkksd ltgsitsvta
       61 kdfnggatsa gqliqgktpg vqitnnsgap gsgtkirirg tsslsgensp lividgvpqd
      121 fvgmngvsdp lslinpndie tfdilkdasa taiygnrasn gvilittkkg tagkfklnfs
      181 tvtsvstkmg kvdvlnaqef rdfvntyapa gyktklgnan tdwqdqiyqa awgtdnnval
      241 sggikglpyr lslgyneqng ivksnsfrrt svglnlnpkf fdnhlsvnvn akgtftdnrf
      301 vdggvikaat yfdptqpvys gnsnyggyye wldsgsatgy nvnansnplg mingvrdvss
      361 vlrglgniql dykfhflpdl hfnvnagydy tksdghkfkn anlrpgfedk gssnfysmek
      421 knklletyfn yvktisaint gvditagyay qdfnislpga vtyrgtgins qdlnfetqnt
      481 lisfygraif tiankyvisg svrkdgssrf fngtrdnvwg vfpgvslawk lneenfikni
      541 ssistlklra gwgktgqqel palngnkpnn ypafaaynps yqgagyqfgn efyfmfrpan
      601 ynpnltwett ttknlgldfg fnknritgsi dvfrkdtkdl lvyadepagg lsnaswqnvg
      661 dmknegiegs itvipvknqn ttwevsfnat hykpvitklk dradeffnme vggieggsgn
      721 riqahavgya pnsfwvyqqv ydtngkpvdg ayvdrngdgi intkdmyyyk sttpdailgf
      781 stkvshknwd falsaravlg nyvynnaasn sslqsastne ylqnvfstap qyqfgvpqyk
      841 sdiyvenasf lrldninigy nfgeiftkgs nlkvyamaqn ifvitkysgv dpevfggidn
      901 gyyqmpkiys lgfnfqf
//
LOCUS       WP_103244623             481 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Aeromonas].
ACCESSION   WP_103244623
VERSION     WP_103244623.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53316
     Region          27..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsydklf rpglaalllt allgagslaq aadeaqskgk iearselfak dhadqftswk
       61 gtseskertd alaedpqmvv lwagypfskd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meqyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfeqtcrnc htqskemlqg vvkqrkdaih dlklkvekql vhahfeakaa
      361 wdagtteaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakgish eiaipdissk ekaqaalgmd mqqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_103247082            1016 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium phosphatilyticum].
ACCESSION   WP_103247082
VERSION     WP_103247082.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium phosphatilyticum
  ORGANISM  Chryseobacterium phosphatilyticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Chryseobacterium phosphatilyticum"
                     /db_xref="taxon:475075"
     Protein         1..1016
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111837
     Region          35..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlsa galfflgqaa yaqqkpkdtt agetaieevv vigysqvpke syvgtaskvd
       61 aksidsknvs tvsqalagea agvrvintsg qpgtdatiri rgfgsmsgnr splyvldgmp
      121 ftgnvssinp edienmvilk datatsiyga rgangvvvin tkkgrsnksv iqleskvgfn
      181 msllprysti sspeeyagls wqalrnqgrl agnanptaya ntrlfstagi spdyniwgta
      241 aanlidpatg mvrpgigriy dpenwedyaf qtsartennl sisggsgktt yytnigylsd
      301 kgysinsnfe ryngrlnlth qarpwlkgef nlgyayskak rngqtsdsgs ifwfvdnips
      361 iyplftrdaa gnkipdpyfg gnqfdyglgd ygrgfggltn aigdatnnin nfykheinan
      421 mflkaditkn lsfetrvggq yynnsndqvd npyygnaasq ngyiskskte lmaynwlqll
      481 ryqkrfgdhn vmafaahesn sweqkylsag rptiidmipe lnqgvgesls esytynytle
      541 syfgqltydf kgkyffngti rrdgtsrflq nkwdtfwsag lgwlvtkedf lndnkivkhl
      601 klkasygtvg dqaivgstaa saqnmgyypg ynvynpgnfm glpgatyvqd gyprltweks
      661 nifqvgaeig lfknravele vdyyhrttnd lifdnrlaps tgngilkvnd gklvnqglef
      721 tlkthiinkd nmyldfging eilrnkltqm pldqstgnak iidlseagfg raegrslydf
      781 ymreyagvns atgaaqwtvn yvdtngngkf dageqinsly efqklnpnad irtgvtevys
      841 qatqkfldks aipairgafn ldfgykqftl gvqflyslgg ysydglyagl mgngvvgsnn
      901 whtdirqrwq npgdvtdvpr mssnaaidan qnarssrflv ksdylalnni rlgynlpqdf
      961 vkaigltgfn lfvsgdnlwi atkrkgfnps vsetgassty syaplstitf gakinf
//
LOCUS       WP_103247565             973 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium phosphatilyticum].
ACCESSION   WP_103247565
VERSION     WP_103247565.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium phosphatilyticum
  ORGANISM  Chryseobacterium phosphatilyticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 973)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 973)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Chryseobacterium phosphatilyticum"
                     /db_xref="taxon:475075"
     Protein         1..973
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107909
     Region          14..972
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklntsllv lvltssiavt naqqkkdtmk tkeiegvvvt algikrekka lgyasqeikg
       61 dvisdagqtn avsalsgnva gvqvtapssm ggstritmrg issvtgenrp liivdgipld
      121 nsnvngsdte rgaggrdygd atfdinpddi esvtvlkggp aaalygyrag ngaiiyttks
      181 akrgkteiqf ntgisfesiy irpklqnqyg gglqsslpta tidgktyniv efgtdeswgp
      241 kydpnlyylg wnsfdpefgn dymklkkwva pnkdvddffr vgttytnnfs vsrsfentnv
      301 rlsytntkin givpnseikk dnfslnvntq lsenlkadav fnyvrtvgfn rpeqgygdns
      361 vaqkfyqwgq rqldfselkd yklangmqrs wnrtswddgt pnfsdnpywt iyentsddsr
      421 nrffgnaglt ynfskklyvt gkvygdtysq mitsrvavgs aalskyniqk rnnsefnyea
      481 rihyndnfgd fslntfagfn imnrkwdvln gnsvggliip glynlanske aprssnasyn
      541 lgvrslfasv svgyrdflyl eatgrndwfs mlnddqfyps vtgsfvfski lnvdwlsfgk
      601 lragwsriag gsdpyirgty asietpfngs pvysmpntkg epmikpeikt tkeiglemnf
      661 fknrlgfdvt yydvkttdli iplpidpstg ygfkrinage mtnkgieamv nitpvknsnf
      721 swdmtwnftk nknklvelqg dlqnyiltna pfraqlaaqv sysygvilgt dfvydangek
      781 vvdntgryka seirslgsvl pnynmglrns fkyknfglsf lidmqqggky fstthmwgmy
      841 tgmleetalg gnreagvilp gvkengtpnd irlnaptwgk sfyntvdaqn vfdasyiklr
      901 ditlsydlpk slignslqgi rvsafarnlf awnldfkgid pentsygsgn iqgleggslp
      961 strmyginvn fkf
//
LOCUS       WP_103248665             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium phosphatilyticum].
ACCESSION   WP_103248665
VERSION     WP_103248665.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium phosphatilyticum
  ORGANISM  Chryseobacterium phosphatilyticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Chryseobacterium phosphatilyticum"
                     /db_xref="taxon:475075"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110741
     Region          35..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhketqkllv lsllglisvn laaqqkakkd tikgldevvv talgikrhdk slgystqtin
       61 sdeilqtqnn nwaqslegkv aglkiqtaga gplgtsritl rgdismnmgn ngalivvdgv
      121 plsdkrtgtg tsaygagsgg dlpidygdsf nsinpddies vsilkgpsas alygsrgsrg
      181 aimittksgk trkgkiqvtl nsyssydtvl kwpdyqyeyg qgtqqkdkng nyyysygasp
      241 dgintgstss afgpkfdgqy yfqydptveg qskerqlwkp yknnikdfwq tgatysnsis
      301 iahsnettaf rtsvsylkne wmmpntgfdr fngaisldhk lsnkvkigtk vnfsqttsdn
      361 lpatgynnqs isyfmifqnp nvsldwykpi wrkgqeqvdq vhpfssyidn pyliayenln
      421 atnkkiltgn invsyqfakn ldvafksgme wsnemrtqrr pwssanylkg yyreqyirym
      481 dlnndillty knkfgdfgvt asaggsiryy estmsdyrai glnkaglyql snatsldnrl
      541 pkpndnqvns ayalanfsyk dmvfldvtar ndwsstlprh nrsyfypsvs ssfvlsdifk
      601 lksdqfnfwk lrlswskvgn dtynymldky yenstfsgsv espllypnpn lkpemitnie
      661 ggmdftilkn rltfnftayq insknqsivi pvlyetgynk riinsgelrn qgielvlnay
      721 piknkdfswn vnanwsmnrn kilslpdefq gqpytmasvg gvvyynavvg gslgdmygyg
      781 lmyspdgqvi ygadgltakp temkkignay pkwraglqne fkyknftvsf sfdgqykgma
      841 ysqshhkmse qgklthtlvg rdnpgglivg qgvvqnadgt fspntkgipv atyygdyyrr
      901 anvetnsfdt sfiklrdari sysfpksvte slkmtditla lfgrnlwmwt rfplfdpeaa
      961 tlddstitpg veigqlptar tvgiqlnvkf
//
LOCUS       WP_103255284             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas caviae].
ACCESSION   WP_103255284
VERSION     WP_103255284.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53164
     Region          29..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsydklf rpglaalllt allgagslaq addsalkgki earselfakd hadqftswkg
       61 tsesrertda laedpqmvvl wagypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eeyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfdqtcrnch tqskemlqgv vkqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaemk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llaakgishe iaipdisske kaqaalgmdm qqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_103256049             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tabrizicola aquatica].
ACCESSION   WP_103256049
VERSION     WP_103256049.1
KEYWORDS    RefSeq.
SOURCE      Tabrizicola aquatica
  ORGANISM  Tabrizicola aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tabrizicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Tabrizicola aquatica"
                     /db_xref="taxon:909926"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54876
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaltevf pgenrvamtp dsavqlaklg hsaciqsgag akagfsdaay aaagvevlpd
       61 aaavvaaadv ivkvrgpeag elsamqdgqt lisffwpaqn pelletaakk nltvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtsvslg aivhafdvrp evaeqiesmg anfvflefeq aqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrpapkl wtedmvrmmk pgsvivdlaa erggncdltv
      301 pdqkivtdng vtivgytdfp srmaaqastl ystnirhmlt dltpkkdgvi lhnmeddvir
      361 gatvahvgav typppppkia aiaaakpkek akeltpeerr akevaafkaq trnqvgllai
      421 ggglmllagl yapasfmshf ivfvlavfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsvf maginifggf mvtrrmlamf qks
//
LOCUS       WP_103261138             480 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Aeromonas].
ACCESSION   WP_103261138
VERSION     WP_103261138.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53223
     Region          29..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsydklf rpglaalllt vllgagslaq addsapkgki earselfakd hadqftswkg
       61 tsesrertda laedpqmvvl wagypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eqyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfdqtcrnch tqskemlqgv vkqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaemk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llaakgishq iaipdisske kaqaalgmdm qqmnsykaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_103261921             481 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Aeromonas].
ACCESSION   WP_103261921
VERSION     WP_103261921.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53419
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt mlglaalllt tclgtsgwaq aadeaqskgk iearselfak dhadqftswk
       61 gtsesrertd alaedpqmvv lwagypfskd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvider gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meeyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg vvkqrkdavt eiklkvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakgish eiaipdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_103273503             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter sp. AONIH1].
ACCESSION   WP_103273503
VERSION     WP_103273503.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. AONIH1
  ORGANISM  Achromobacter sp. AONIH1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter sp. AONIH1"
                     /db_xref="taxon:1758194"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38638
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkytagk htvvvergag vaaryldeay eaagatlgsa
       61 qdalgaglvl kvrapsaeel phmkpgavva gmldpfdaeg lmrlaaaglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahyygr lfpmmmtaag tlkaaravvl gagvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgvggy arpmppswma
      241 rqaalvserc kqadiiitta lipgrpaptl vsaetvagmk pgsvlvdlav erggncplte
      301 rgqvvekhgv tlvglnnlpg mvatdasaly arnlqdflkl iinadgalqi qrddeivaac
      361 lvceggnvtr rt
//
LOCUS       WP_103277154             474 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            vulnificus].
ACCESSION   WP_103277154
VERSION     WP_103277154.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     gene            1..474
                     /gene="nrfA"
     Protein         1..474
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52975
     Region          1..474
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmass vsvtalvmta llnitavsae ekglvdprnd afeqnhpdqy qswkktsesv
       61 eiedalaedp nmvilwagyg fakdynkarg hfyalddvrq tlrtggpqda ksgpmpmacw
      121 sckspdvarv idergedgyf egkwarlgae ianpigcadc hdtrsekfkn gepelaltrp
      181 yverafqain kpfeqqsrld kqasvcaqch veyyftgptk avkfpwdmgt gvqqmeeyyd
      241 algfadwtha vskapmlkaq hpgfetwreg ihgknkvvcv dchmpkvkke dgtvytdhkv
      301 gnpfdrfedt caqchtqskd qlreivstrk aqvlnmklta ekqivaahfe agaawkagat
      361 eeemkpilqd irhaqwrwdy aiashgvhmh apevalevlg tavdraadar tklvrllatk
      421 gitepvqipd isskaaaqka lgmdmekmnv ekqhflktvv pdwdkaaaer esky
//
LOCUS       WP_103288935             962 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103288935
VERSION     WP_103288935.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 962)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..962
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105284
     Region          34..961
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkavipvll vlsfysnaqe rkaadttktt diqevvvtsl gikrqarslt yssqqiggde
       61 ltevktpnll nsingkvsnv qinrtsggig gavrvvmrgd kstrnsqpll vidgipvins
      121 igtskigsdg tissgggads yngsadagdi fssinpediq smtflkgasa aalygsqgsn
      181 gailittkkg aagkanlsft ssltfdkaya lpklqheflq shdaatntyg ddswgvagss
      241 kdylkdflrt gttwtnsltf sagnekstsf fsvanttnkg ivpvsnfdqy nvnfrnsskf
      301 fddkltldan imasmqeskn rltpgvyfnp iyqvavlprg vnfdqykdym yldserqipa
      361 qnwynltgir qnpywilnrn asvsknknvy ssvalsyqin nwltakvrgn ytystsnter
      421 dlyaftvpsi agsfgngkmy ynnletnayy gdalligspn isdnisfdft vgasisdkkd
      481 vvteiqserl svpnlfslsn iywsrgsgty tiftphrqdq svfasttigy kkmlyldltf
      541 rndwsstlfg snysgidyes vganailsdi fqlpqafsfw kvrasyatvg naleptyanp
      601 vpilnngvit gysayltklf ppkpefnktf evgteirlfk nrlnfdftfy nslvqnqylr
      661 qveaapglsd lsgtkidina geiqnrgfem slsydaikgg dlnwtttina sanrnkimkl
      721 fpsefysgdn sffdlvgggn ynklkaggsf gdiygtaflr ndagqiivda kgapmvdpns
      781 rkflgnpnpk filgfsnsfs yknfkldfli dgkfggkvls laeatydyng vsqrsadarr
      841 dggvaienav yqngtpytgk tdaktyytti ggqvapniae aymyeattvr lrqasasytf
      901 rvnskymrea tvsvigtnlf ffykkapfdp eqvsgvnpgg vgvdvfgmpi trslgfsvkl
      961 nf
//
LOCUS       WP_103289091             954 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103289091
VERSION     WP_103289091.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..954
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105252
     Region          33..952
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlsa galfflgqva faqtakkdtt skvkqieevv vlgygktatk akstaastti
       61 sekvledrpn asflnslqga apgitinsss gspgsgridv rvrgigslns amdplyvidg
      121 mstngtqfrn lnpediasis vlrdaaatsi ygnraangvv vittksgsfn sgmklsfgst
      181 igfstypnhk ynlvsgsqyr alqnefvfgp deqysqdevi napntdwrkq yfrtgmtqqh
      241 nlgltfggkn vsvysslgyy dmtgivkstd fsrftfrnni ngksndgrft ygsqlavgys
      301 krsqldqens vsallanplq nplfssilar pdlepspynr gsdfyrdyqn kysdripwvt
      361 qdiinggvqn kytetsvman vnfaykltdy ltvghksgid fkesdrafar apygylalia
      421 kagndpyggi eqlnntkdfn insitnltfn kswgehtlev gayldyikah yrakqyqqng
      481 lnpltwslgs gtgyvpystt tptlyvpnvq asavnagala yfataeydya gkygftgmvr
      541 rdgayrfske nrwntfwavs grwnidkeaf megsvfdmlk lrssygtqgn qnlgitvnni
      601 nplvnaattt lfrnvyttnt aylnqqglgl svlgnpdvrw etqkmfnvgl dfvlfnrkle
      661 gnvdyyiktt dnlfnklnis aastgtftid gnngkmrnng iegnlrynif nrsdfklsif
      721 angsfnknri lelpygyspt dnvnatgsla fqwnlvryag vnkdtgemqf ldkngaiten
      781 pndsdrvltg ksyypkyqgg fglngsfkgv fadvlfswqa ggwqydnlyt wlmdpnglgt
      841 gnnvsadlln swtpdnrntd ipsitanntg sdgssdryly ktdfirlkti slgysfpkas
      901 lanlpitglk lfvqgenlvt wsswkgldpe pvtdyslsvy pnpktfsvgf nvef
//
LOCUS       WP_103289600             946 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103289600
VERSION     WP_103289600.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 946)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 946)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 946)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..946
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104100
     Region          32..945
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqsnlkysc liavlyfgmn vnaqvtsdsa kvqkidevvm igygsrkkvd nttsissisa
       61 eevtrtkvln asqaiqgkaa gvqvtasdap gstptvmirg lgtvlggrtp lyvvdgmftd
      121 ninninsndi ltydilkdaa alaiygnraa ngviiittks gkgklsvsyd glvgfrtplk
      181 tikmanasef vnynnagsks dfispnqpyn tdwfkeitrt gvynqhnlsi sgsseaakyf
      241 lslgnydeqs ilngtnynrt tvrtnnefri tkgirlaqtl satftndtpk sfgaftnayk
      301 qasvvpvyyp ngkygqpiin katgelgyeg grfnnvanpv mqmaydnqra knfllqgglk
      361 ldidiikdlk ftsqfsgeyg nykyynfvns ralwldsdpm rteaqysats pktrltnksq
      421 nyynwlinny ltytkkvgdh dielvagtea svksglettv inrknvpvsp dywnlsgvdy
      481 ygdlfsegdt kaiesiqgnr nttisyfgrf qykfmnryll sgtirrdgss qfaagqrwgt
      541 fpsfgagwii sqenfmqdgf fdmlklrggw gkignqtvpl nylplslgss ynygygnpsv
      601 sngvtvnkgy dpdlgwevte esslgldfgi lnnrltgtfd vynrktknli lgvvpymstg
      661 iselnyshmg svvnkgfevs lnwadkvgqd fsysiganys ynkntlasmd tskpvsqivg
      721 gnlgngidtk lfnasavgya lgsfylyead gynekgelkf kdlngdgvid akdksflgsy
      781 ipkstlgvnv smsyknwdfa lngygsfgfk vyngkkaqrn ggenveasva nnfwtpnntn
      841 aanpvnpani pvastfyled gdffrinnis vgytfknvtd ymksiklyvs ainpfvfqky
      901 sgysselsgy nptdtttegd pykragield ayptlrsfvf gvnlnf
//
LOCUS       WP_103289961             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103289961
VERSION     WP_103289961.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109106
     Region          32..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkqcklgv lallfiaeyg faqtkdsltr entiqevvvv afgkqkkeei tgsvqslkak
       61 dlsnlqngni lqgiggkvag vqvvssgqpg sqptirmrgi gsinassdpl ivldgipysg
      121 nlnsiaasdi esisfledas snalygsrga ngviivntkr gknkglsidv dvktgvnfrs
      181 iqdypvytsp qdyytafynr arigevarlk qpgavpsgst phdvglaalt klgynaynvp
      241 faqlirqdgs fnpeaqllyq dnwkkllfkp alrreatvgi nangdqvksy tslnylddkg
      301 ylissgferf girsnvdysi tsrlkltsal sytyskqdfg etggfsnpfq farnispfyp
      361 vflrdnnyqr lydsygnaly dygdgsgpng aarsyavfen pvgnlqkdks qttsnvsnin
      421 lglnyeiikg ldftynfgay lenvrnlqfg nteggtsssv ggtitrasqf rytlnhqqll
      481 tyqkklgkhn fniligheln kiknenmsgt kqqlvlpnss sfdnavkitd lsgngyeyav
      541 egyfsrllyn ydgkyffnan irrdgssvfs pesrwgnfyg lgaawnvake dflkgnnvid
      601 alklkasygq qgndnillds strdyyayqd iyginnfgdg npvlslkkqg nkdlkwetsk
      661 nlnagfeisl lknkinlnad yferkvsdmi yalplppsns gsyikygnig dminrgvqan
      721 lnvdilhtdn lqwniyanat hyknkitrlp aeqrntglvs glfilseggd rytyylkefa
      781 gvnpengdal wyrtainptt qkeektitnn ykeatdyntg ksaipkvygg fgtditykrv
      841 nlsvnfayqf ggygyddiyr slfhsdtygs nystdldktw tpenpnaalp rvdltstnqn
      901 gnstlyliks dyislqdvtl syqlsddfar haglsglkvy ltgnnlylws krkgydpras
      961 ltgvsdsyky sllssvslgf kltf
//
LOCUS       WP_103290882            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103290882
VERSION     WP_103290882.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114922
     Region          126..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklcravll ililsiscqg lyaqeklstk rvnfeigktt aseavgkfis envkdkiysn
       61 ddlkdftvqp trcknelvld clnkilkdip vetlidnnsv iirpkknrsk aansewssls
      121 latkdtises sdihiideit lnagyykvsd kdktgsitkv sardienqpv tnvlstvqgr
      181 mtgvniiqns gvpgagfeiq irgqnslrtg sfteqngnvp lyvvdgvpft eispqksqis
      241 stiipggnin plntinpndi esievlkdad ataiygsrga ngvilittkk gksgkvrlnf
      301 stnygiseai snltllnkde ylnmrrtayk ndgiatypsn aydvngvwdq qngidwqkvl
      361 igkkattsnt qlsanggskt tsfllslghn eqttvygqdf kytsnnfssn lshrsednrf
      421 qinvsnlftq qknnviysdl takaftlspi spqlynadgs lnwanntftn plaaynasyn
      481 ndtklfqtnl nseyklfkdf kikinaglny tiidelalqp ntiynpnias glssansqar
      541 qkkqdifsfi vepqvnwtkg wgnhnlqllv ggtfqniird teeelgfgfe snqfisniaa
      601 aktvmmlens nieykyaaiy grlnyqfknk yilnltgrrd gssrfgpnnr fanfgaigaa
      661 wnfsrenllk nlswlstgkl rasygsagsd nigdfqflnn yivsssliyn nitglspsrl
      721 ynpdysweit kkletavelg ffknrlnlst slyrnrsssq lvgyqlsavt gfssvmanln
      781 atienkglei eitgrplskk dlqwessfni sfprnkllsf pglagssyan qyvigqptni
      841 vklyqfegid pstgqykfkd fngdgkitsp edrqvvadig vkffggwsns fhyknwdlsv
      901 lfqfvkkkgw nynsimslpg tmsnqptqvl dvwspenpsg yympystlnt nthnlfrtst
      961 aavsdasfir lkniqlgytl pltegvfrdv kiyfqgqnlw twtkffgvdp ealtsgflpp
     1021 lrtysfgiqf nl
//
LOCUS       WP_103291694            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103291694
VERSION     WP_103291694.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116231
     Region          39..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqlnigvpl tvsvfcfllg ttnhlnaqkt kkdttknkqi eevvvtalgi krdqrklgya
       61 itkvetkdit qagvvnpmea lqgklpgvei sagsggpqss ariqirgnts lgnnnqpliv
      121 vdgviidnsi tgadqwgsgy dfgnemknln tdvfesvtvl rgaaasalyg sraangvivi
      181 ttkkgkdkng lgvrinsslt tqhvyegpkf qnefgagtap tfstdvngnr fvdasnffrs
      241 ygpkfdgkpv kdidgrtilw npqpknyrnl yqvgfdrkns feisggdaks tfllsytnqe
      301 aegilprnkf iknayylrat hefnkylqid asfnynrsfg qnpvpqggns splfsfiygl
      361 prsfdaaywr nnyldpvkgg irqdtadpyg mastyfnifq ntrtqkenny igrldlksqi
      421 tdwlnllvsg nfnnynfvne skilgenpgf sggsytvleg tkeqymvkfl lngnfkltdh
      481 ltlnasvgge dfrskykask qwtngglnsp gvfqlsnsid pitnepsysd gqspkriqgl
      541 yafanfawkd qlfiditgrn dwsstlaypd ghgslsyfyp sfvgnwtfsn sfklpkwinf
      601 gslrgslawv grdtspynts sglyykpdps ayntpggtri pltgfnsnsl anlnlknels
      661 ksiefgvnma ffnnrldfdv sfyktnttnq lltlslpqes gisqqqinag nlqnqgieii
      721 vnavpvkssd frwnttwtfs qnrdkilely pgvteyvinw gmgndvksia ipgqqygliq
      781 tkyayaryqa ydangnkidd prngmkvlkp ngtylrsdsy qnqgyttvgk stpdfltsfr
      841 ntlryknlsl svlidarvgg dllsatynyg vqfgnlastl qyrdeekggi kyidnagntq
      901 fglipegvfa qgteikdkqg ntrqvggmty qevydkgwvn pvrtvgyynn lsswaggire
      961 haifentwvs lrearltyff kpemikplgl ntlnmsiigr nlfyiynklp dginpegkys
     1021 nsagsfaeyg gapmsryigf nldfsf
//
LOCUS       WP_103291727             968 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103291727
VERSION     WP_103291727.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 968)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 968)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 968)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..968
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..968
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106639
     Region          31..967
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnklivkigl lpslffglng lygqntdstk aakidevvvt aygvkkekkt lgysfqdvkg
       61 qtlvdaketn vtnalvgkva glqvikggfg passsrinlr gfnslkgdsq plivvdgvpl
      121 sngmgvkpkq nngyfnndfw npdldmgngl ndinaddies msvlkggaas alygsrggng
      181 vilittktgk rrggvgitys tslgfesifm kpdmqnsfgl glngignpan sdntsswgpa
      241 iegsnmkryd nlsnffrtgi nsqhtlnfqe nlgegtslyt svnylndnsq ipnskferfn
      301 fmakmnstfg aqkrwtsevk vqyisskakn rpsggrgdgn yysnillmpq nidirdyreg
      361 qtqnnvksnw itpnginpyw saynslnadk kdrmllngyl kyqfndwlsa dvrlgtdfya
      421 lnadakvwtg ssrrnayats eekfyennyi asitakkdnl fgkwggsvsv ygqmmesrtk
      481 alyfstqnli vpnvfsvtnt sdlagianse idlwkkinsv faaveinydg ywfinatarn
      541 dwsstlnaqn rsysypsvst slvltemlnk lngttskvlt faklraayav tgnsldpyel
      601 yntyrlaadp tghailgrek vlydpylqae qlntfevgad lkffnrlsld vsyfnntakk
      661 qlinlpmnpl sgyesrkins gkihnsgiei vlntdifkke nfswnmnanf sklksevkel
      721 dgtiskyplg gydnvtffae igkpygaiyg tkflrvedpg npnygkiivg englpqatpd
      781 qyylgdqtpr alfgftnsfn ykniglsfqi dgriggkfys atqsalqkvg laadtapggr
      841 rdnfvldavv qqsgggyasn tkeitpqdyw aavtagnlgi teqniydatn irlrniqvsy
      901 sfpkslfqkf alqsakvsft annvwmlysk akgidpesvf ainsnavgfe nlsfpttrsy
      961 lftitlgf
//
LOCUS       WP_103291735            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103291735
VERSION     WP_103291735.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119065
     Region          22..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtlatfav fllplyftaq einisgnvks engssvsgvn itdkntgkta ttdengnfti
       61 sanprdilef lspefsvytv evsskrqysv vlkktnekqi egvvitalgi akkkekigys
      121 tqevgtkqfe tittpsignl fsgqvsglsv snptgmqqap qftlrgnsnl vfvidgvive
      181 kevfqnldpn nieninvlkg atasalygsr grygailitt ksakkkgfsv efsqntmitg
      241 gftnlpktqt eygngshgky efwdgadggv ndgdmiwgpk fvpglqiaqw nspirdkvtg
      301 qvipwygavs gsqyndksry ervpidwkyh dnlstflkpa vinnnnfais yrndkdiyrl
      361 sgnfmnyddr vpnsylqkyg vnfssenhfg dkfvfdtkfn fnqaftpnip nydynpsghm
      421 ytiliwmggd vdgkalknhm wipgqegrqq anwnyawynn pwfgaeyykn qnrtdiinaq
      481 tgleykatkd fsvkgkisiv enhskteils pysyfnysap rsggyivkde ktwnlnydvl
      541 atykkkisen fdftinagas tfyyknnkde rstdglkvpe vysfensiga lknytylkek
      601 liysaystid iglynaffin isgrndwsst lpkanrsyfy psasisavis nlvkmpeavn
      661 mlkvsaswak vaydfqpyst rnyylnnkgi tfngnptyyy pttlniensl kpeqtksyel
      721 glsagflnnr itfdatyfrt ldynnilqfp saessgftsq yvngneyttk gfelslglvp
      781 vktsdftwka linwstyeqk ltsiydnmpn ynniklgerm dsyydyqwqk spdgkvilda
      841 ksgmptrann qtnlghfnpd wtfginnsfk ykkftlnigi dgsiggvmrs qvvekmwwgg
      901 khpnsvayrd leyanpgtyy fvpdgvnynp atglytphtk aisfqdwaqn ypyqarvtes
      961 eseefanvfd rtfvklrsvv leydfsylln pkgivksfta nisaynlamw kksknlysdp
     1021 dfqirsgrtg dvtndiqdps srwfgigfnl kf
//
LOCUS       WP_103291738             978 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103291738
VERSION     WP_103291738.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 978)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 978)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..978
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108455
     Region          40..977
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvfkipvsv tyltgrvlli gaisaspmfl aqkkdsikek sidevvvvgy gtqkkskvsg
       61 avseasldkv ssrslsgige vlqgkapgvt vvneggdpng spkvnirglg gvngetplyv
      121 idgvvfnggs snnpygrgaa lfketpninp ndiedisilk dasaaiygar ssggvilitt
      181 krgkkgkltv dfdvkyginq awklkeslna aefqdvmrqa ydnagklssl plafnadkys
      241 dgritrtnwm keifrtgtiq eynvnlsggs eksrffvgmn hrnlegilln tqakrynfrv
      301 nsehkvkdwl tigenmyyny sdgntadtkn gytgalvaam yyppnvsvyt ptgaysglpi
      361 dvaggygdmi npvaylkris iqnptheili npyievalak dlkfrsnfsq tfkignikef
      421 tsrvlevgki fdtnsleyqs ntvatslaeq lltykftlgk hnfdalagft fqkttedgfr
      481 akafdfrsea eafrylqnaa dtnkevfsyk ykqaltsyla rfnydyagky iisllgrrdg
      541 tsmvskqnqf anyysvsgaw vaskenflne iswlsnlklr gsygilgnlg gvsyqavnpl
      601 mtrdnniifg qdptqniayy attkanqnlk wgkseqtnfg vdasffrnsl slqfdyfvkn
      661 stdqifnvnl sstemyndry vnaglfqdkg felginynsk skgdftysig asisqlkntv
      721 kqlagvdeif vnsnnvrgvl kptrikvges lysyygyrtd gifqtqadid nykdangnli
      781 qpnakpgdik flkkdgntgt lnnndfvnlg npypkfsygl synmawknfd lnlffqgvyg
      841 nkifnglkfi slnpggtgqn ynmdrdilna wtpqnantni prvvqgdpsg nyskvsdfyv
      901 edgsylrlkn ltvgyslpke lynklnvski rvyvttnnlf titkytgfdp evgmetygvd
      961 tgrypqarsf ifglevgf
//
LOCUS       WP_103291991            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103291991
VERSION     WP_103291991.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110532
     Region          12..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttsllv lmltssvaia naqekkndtv ktkeiegvvv talgikrekr slgyatqevk
       61 gdavnknptt nflnnlsgkv agleikqstn fggsvnvvmr gfksllgnnq alfvvdgipi
      121 lnnnintssq ntggggydyg saisdinpnd ietmnvlkga aatalygsra qngvilittk
      181 kgkknkegig lefsssitms svdrstfpky qsqygqgyrg tsfagtldgs pivdfgndas
      241 ygspydgslv wqygaftpgs ptegqrtpwq makngpikff nvgatyvnni alsggddkat
      301 yrlsysntna sdilpnstlm knnfsgsasy kltdkltanf yanyvtqktk grnstgyndn
      361 imtnfrqwwp tnvdvkdlqy lystykknyt wningtddlt pafwdnpyfq ryenyqndsr
      421 drfagnfsln ydvskefnll lrmgtdgytm mtedrkavgs yigntfglnt vvqpsgyals
      481 nykfnetnyd liatykknvt edfnvtallg gnvnvqkafs nqqstsggly tpgiytians
      541 ksnpvrplis dvskyvygvf aqvslgyant yylegtirrd qstalpsvna vywypsvsgs
      601 ivfsnlvkan wlnfgkvrag ysqvgsdtta dllrdryfsq psygdvpvya ynavlrnfdl
      661 rsqglkniev gietkmfnnr fgfdiswfqn rafdqiialp vsygtgasak nqnagelttk
      721 gfevavnvtp ikttdfswdl nlnwsnpwtk vtelspgien isigrlqgga svnaplngdy
      781 gtlwtsdfvy dsngqkivgp ngaylvsdka iydqgsfqar wsaglnntin yknlslsfli
      841 dwrqggkvys ldqsygygtg lypnsvglnd lgnpvrntia ngggiiqpgv madpnnpghy
      901 ipntirldks qssqvlqtdl pgaayvydas fvklrevait ykfnknifns kfiqgmsmsl
      961 vgnnlwiihk nlpysdpeag lsagniqgyq sgplpttrni sfnvkinf
//
LOCUS       WP_103291995            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103291995
VERSION     WP_103291995.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109495
     Region          31..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklrtsllv avlsssiava haqqkkdtik tkeiegvvvt algikrekks lgyasqeikg
       61 stlsegttnt gniasqlsgk vaglnvttnn nfggssnlli rgikslsggn plividgspv
      121 nntytqaggi dygnalsdin qddiesinvl kgaaasalyg erglngvivi ttkngkgkdd
      181 gswgvtlssa vqvgfvdkst fpeyqtryga gysqeftaqg anglndvnfg ddaswgpkyn
      241 ssllvnqwdy ydptssnygk atpwvaakng pikffnhptt ftnsitlekg qkgkninftf
      301 dnmlvdglmp nsrinkntfs lkvnydltpk lhssfystmt iqnttgrsit gyndnivtgf
      361 rqwwqtnidv keqqraysqn iaspnadnyy gnvswnrksg tegnaaywnn pyfqayenyt
      421 sdsrfrtfty aqltydlldn vsvtgkvsyd rsnlfaenri avgsiaqsfg lsensvgsgy
      481 srrdvtrtet nydlmfnykf ditnninvsg vlggnvrrny vnsiyasteg glvvpkiyal
      541 snsvkgplap denewttqtn sgyvtasfdf ykmfyldgtw ridqsstlps gnnvynypsv
      601 tgsvilseif kiknwmnfwk lranyaevgg tadpyqltny yssagifsga qggigiynsl
      661 lkkansdlkp qrskefelgt evhflrdrit ldfayyktkt inqiiplais sgtgftskvi
      721 nagridntgy evqlglvpik sndftwnidv nwskntnkvi elnpgidnil lnsftggvsl
      781 narvgeawgt lvgndytyln gqkvinpktg kylqnsnqii gnttpdwigg irnsinykgf
      841 slsflidvrk ggnvfstdmy yglssglyke tamgdfrdkn vilpgvlpng tpnniplspl
      901 dngsstgykt qppsefvydg sfvklreasv gytlpkslla gtkiydakis ivgrnlwiih
      961 knlpyadpea miggglnsyg wsigsmpttr digvnvtfkf
//
LOCUS       WP_103291993             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103291993
VERSION     WP_103291993.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109204
     Region          28..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttgllv lvvsssvava haqekkdtlk tkeiegvvvt algikrekks lgyasqeika
       61 galsdgttnt gniaaqlsgk vaglnvttnn nfggssnlvi rgvkslaggn plividgspv
      121 nntstqansi dygnalsdin qediesinvl kgaaasalyg erglngvivi ttkngkgkdd
      181 gswgvtfssa vqvgfidkst fpeyqtryga gysqkfgsqa sdglnyanfs adaswgpkfd
      241 pnlmvyqwds fnplspnyqk atpwvaakng pikffenpas yinsvtlekg qkgknisfty
      301 enmmsdglmp nshlnknnfs lkinydltpk lhssfystmt lqdtkgrsit gysnniatgf
      361 rqwwqtnvdv ndlqnlyfan vdphvanasn nygnvtwsrk saangapayw nnpyfqayqn
      421 yssdkryrsf tygqvtydll dnisvtgkvs ydrsnlmaes rlavgslpqa fgqsnnsigs
      481 gygrrdilqt etnydlmvny kfditdninl sgvvggnirr nyynslyast egglvvpgiy
      541 alsnskkapl apdeteytvq tnswyatasf dfykkfylda tfrveetstl lkgnnvfnyp
      601 sitgslimse ildtkrwmnf wkiranyaqv ggsassyqlt nnyrsagilf ntgiynsiln
      661 qpypglqpqk anefevgtea hflrdritld vayyktkttp qilqplptsa aigytgkvfn
      721 agridnsgve vqlglvpikt kdftwnidan wsknqnkvve lypginnyll nsfqggvsln
      781 arvgeawgal igsdytyvng qkvidpntgk ylqnpnqvig nttpdwiggi rnsfsykgfs
      841 lsflidmrkg gdifstdmyy glssglyket aigdyrdkpi vlpgvlpdgt pnnialspvd
      901 nsgstgyktq pssafvydgs fiklreasig ytlpksllag tkiydakisi vgrnlwiihk
      961 nlpyadpeam vgggvssygw sigsmpttrd lginvtfkf
//
LOCUS       WP_103292463            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103292463
VERSION     WP_103292463.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118764
     Region          106..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktaisiam lgslylsqpl caseihfnlh iiytspppvt kvleklsktt ktqffysvsd
       61 lediqvddkd inynslhqtl eylqknypie fviqnntvti rrtskkvqrk nnvivvnnta
      121 kkdtiadrek kidevvlvgy gkqnkkdvsg siaslgekdl ksvatsnfge miagkatgiq
      181 ttsansspgs spnirirgig tltaganpli vvdgfplteg tnlnsidpns iasidilkda
      241 astaiygsrg angviliqsk egkkgklevv ldsyygiqtr sdnekfvnay dmatfmkesr
      301 dnnylskgsn rsisdntttr iskgatlrel vpdylipyln kqpglidndw yttvlkpapm
      361 sntslnvlgg sdntkysftg sylnqkgili gtdyekysgn inlathitdq lkfgvsmsps
      421 ysqgslfdmv nggrtynllq mattmypffa prdangnlii sqqikvngpt dgamvenpva
      481 iaemtrrkyt lfktfgnifg ewkflddfky kisaggdyts ydynffdpst vgsyrtaapd
      541 vttaskteyi tknylienll tydkkignht fnailgqsyq netsnqtttl atgfpdnsie
      601 nisggssfkv dvnqykwtli syftrfnyty nskyslmasy rrdgsskfga nskwgdfyal
      661 slgwtvskes ffpsnkwldp lklrfslgtn gnnqipnfgs lslmekenyv fggmmvpgyr
      721 sstaasfdls weksksvnag idfslfnkyl nvsadyyiln rnglllevpv pqqsgystll
      781 qnigkirnsg levqlsvkpl higddfeysn nfsfsfntnk vlalangqsq ivagannfav
      841 tkvggsiaem ygynilgiyk tqeqidnsph isgtlvgdyi medlnkdgki dandkksfgs
      901 gipkyvmgft nsfryknfdl sftlyselgk kiyngdqvss tesgegfgva tqnyfdnryn
      961 pvtnpdgiyg lpnmnfsnnr keartssiff kngdyvrlrs lrlaynlpqs lvsalkvksi
     1021 qlyfvgnnll titsykgqnl datsesvltq gydngyypva rvysfgmnmk f
//
LOCUS       WP_103292893             919 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103292893
VERSION     WP_103292893.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..919
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100969
     Region          33..917
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfttilkv apafllasti mhaqttdsvt kekkieevvl igygkqkksd ltgsitsvta
       61 kdfnggatsa gqliqgktpg vqitnnsgap gsgtkirirg tsslggensp lividgvpqd
      121 fvgvngvsdp lslinpndie tfdilkdasa taiygnrasn gvilittkkg sagrfkvnfs
      181 tvtslstkmg nvdvlnadef rqfvntyapd syktklgnan tnwqdviyqt awgtdnnvaf
      241 sggikalpyr lsigyneqng ivrsnsfrrt svglnlnpkf fdnhlsvnvn akgtftdnrf
      301 vdpgvikaat yfdptqpvys gnskyggyye wldgnspngy nvnassnpmg midglrdvss
      361 vtrglgniql dykfhflpdl hfnvnagydy tkseghkvkd gryrigyedk gsenfysmek
      421 knklletyfn ytknisaint gvdltagysy qdfniiipga ltnrgignnt kdvdfesrnt
      481 lisfygraif tiankyiisg sirrdgssrf ynltrdnvwg vfpglslawk lneenfikni
      541 saistlklra gwgktgqqel palgvngnkp nnypalgayn psnpgayyqf gneyyymfrp
      601 anfnpnltwe ttvtknigld fgfaknrvtg sidlfrkdtk dllvfadepa gglsnaswqn
      661 igdmknegie gsitvipvkn enttwevnfn athykpvvtk lkdrggesfn mevggieggs
      721 gnriqahavg yapnsfwvyq qaydasgnpi sggyvdrngd gvintkdmyy yksttpdail
      781 gfstklshkn wdfalsarav lgnyvynnaa snsslksast neylqnvfss aadykfsdfq
      841 yrsdiyvena sffrldnini gynfgevfsk gsnlkvygma qnvfviskys gldpevyggi
      901 dngyyqmpki ysigfnfqf
//
LOCUS       WP_103293190             931 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103293190
VERSION     WP_103293190.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 931)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 931)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 931)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..931
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..931
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103369
     Region          30..929
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklhvlsa galfflgqaa faqktkndsi lkenkieevi vtgyqkkkad eitqaqavvg
       61 gdeirrnspt tsignslqgr asgvfvqstt gqpgaaatiq vrgvagvggs septyvvngm
      121 ymtarqfsai npadvesisi lkdaaataqy gargangvvv vttkagkagk thysfetkfg
      181 fserlkdnny tmmnsrelmg fqnqlgylgf kprtqqemdr laafdhnwqk dllkpssiqs
      241 ylfsaqggsk estfyyslgy dsdngiirdi dglkrytgnf gftnrlsekl nvginlgvqy
      301 qvtqnfrdrn ntqnpfgamy kyapyepiyn pdgsynqtmr agsnvveqis tyrlddqrlr
      361 ipvtlfaeyk iidglkfktn fnglydwfmg tqwlkkgsnl dltvntiptg slnknsfygf
      421 nytwnnsiny kksfgshnfd flgfieyndn fnetmnggay glkspvisvp sittpsdrnt
      481 ftgiktrntl fslagllnyd yagkylvtgs lrrdassrfg mnnqsgvfws asaawniake
      541 dfmkggfind lklrgsygtt gndgtlpdyy nvsnvsygly gsngtlypgt yaqssyiign
      601 tnlkwesnai tnvgvdftmw nrrvrgsvev yknkrkdfvq lvpldkqegg yyqyinagdm
      661 sqkglevels vdvikkrdfn wnlhanisfq ksildkladg qternlgdty lkvgespysf
      721 ynvrfagvdp nngdalyydk agnitnvysa snavpltdks pfpksfggfg ttvqykgldf
      781 sadfafkmgs ytynnmyyaa vnptlavagr nmaqqaanvw qkpgdtnvfq kvdsngmrds
      841 dqwieksdyl rlrsltlgys fdkaflgeds pinklrvyvq gqnlftvtkf hgepevsvgs
      901 adstalfvpg synlytypav rtilmglqle f
//
LOCUS       WP_103293174            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103293174
VERSION     WP_103293174.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124484
     Region          22..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlillpl laaqvalaqe kktitgkied gntsgvitga sikietqsvs tktelegiie
       61 svsvgtvtdk ngkfileipa dtksvlvsyp gyesrviqln egqtnytirl vaevsdknki
      121 qeviitgyqk iekrkqtsav atvkmdninq agvasvdqml sgqiagvavt petgapgspa
      181 kirirgtasl sgpqdplwvi dglplegndv pnftdkdnid qlqnfsiagl npndiediti
      241 lkdaaataiy garaangvis ittkkgkkgs lklnfsadtf vttrpdfdkl nlmnasekvd
      301 lelmlakrad ltyradkgei mriltqngql dafrsgglda lnsmtrqqin glrnnntdwg
      361 kllyrnaink qyglsisggs drsdyyfslg yydeegttig tgfkrynltl knnyklsdkl
      421 nagisifgtq seresfvtda dasinpmnys rnvnpyltpf npdgsyrydr dmdgfddryi
      481 pfnfleeren tsytlknnsl kaifdleykv skslrftsql giqydankte kyaaentyft
      541 rkmrentryy kdggyhyflp agavkqnwnn dffqynwklq gmystkinsv heidlmagte
      601 mrktednttv trafgydptt rrgtaivfpn stfgsdkrye tyremppien ayasmfatas
      661 ytydqkytff gsvrydgtnl fgvnkkykyl piwavsgswl vtkenfmkni savsnlrlra
      721 syglqgnidr ntspffigey sdttilpgsk eniinvispp ndklrwektt nvnfgldlgl
      781 fqnrinltad vysrkgtdmi smketpletg feytmmnwgs ltnkgfelal strninkdnf
      841 kwtttinfah nksrvlseqa rdnsifpsre glpvnavfal ktagmdeqgn pmfwkgneki
      901 saveffklyd vyadflpgql vdtklsnael rnmftyigdr dpkftggiin tfkvhnfdlt
      961 isatvnlkqt vmrtpsyrgm eldrgrnytr eiyeagsslp gitspdmdan pdgwmankwf
     1021 agnrsnvysl ldvwakeisy vrissirlgy tlpkeltspm gisslrlsie grnlfvfsng
     1081 ykgyfdpety gniyvqpiak sitvgfnvsf
//
LOCUS       WP_103293192             947 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103293192
VERSION     WP_103293192.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 947)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 947)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 947)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..947
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..947
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106410
     Region          2..946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklsvlsa avlffmghgv vaqkvkkdtt ssklidevvv vgyrsttkkt avtsiatvdn
       61 ktienrpnsn vlniiqgqla gvnvtastgq pgakptviir gvgtyngntd plyvidgfps
      121 nsdnfrsinp ndietfsvlk dasaiaeygs rgangvimit tkrgnysekt svrystqfgv
      181 smlqdpkyny vnsrelltmq krfgagwgak mtdeeianyn intnwrkvff rpavtqshdf
      241 siesggknin sytsvgylnq dgilkttglk rftvrnning kssnnrlkys lvtgvgfskn
      301 neailtagai nrnyilgayq sapyvspdly qngkqlfdly qkdgtllytp lmlmdklvny
      361 nnsteeirld iasnlsykit ndltarvrts gqyldtkftq aeyplsfnaf lfkgaqefsg
      421 ledvnkrref lfnnlwqley sktldkhtfs ftgnleynys qvdvsnmrqr gldpktfvpg
      481 tgsgyisdtp dndyyvpqis vsklklnmis yfglfsydfd kkygiegvir rdgtsrfang
      541 rqwgnfwsvg grwnidqeaf mdnvkfvdtf klrasygtqg nqrivdgtiy dglnppgftn
      601 iysvtnnsyn anqgyainfg dgklrwettk qynigadfef fkrrlrgsfd yynkktvdly
      661 mpdptapvlg tlsivrntda sivnkgiels laydilknke kdisltfrvn gsintqkvdg
      721 iksgngripe ssdpqyvtan ggllrepfvy kylgvnpnng nllfedingn ptenptaadr
      781 rlygknnlpk yqggfgmdfn yknffasttf tfvarvvryd ydmsslynpn nlrnftvdka
      841 mlnawtptnt ntdipslkaa nlglqsnsdr fikdasylrl rnvqvgyrfp qrylkdtfin
      901 slsvilqaen lltisnwkgf dpesprisdq qkyptpriit lgfdikf
//
LOCUS       WP_103293342             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103293342
VERSION     WP_103293342.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110791
     Region          30..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklqiliglg lvvsweaygq kvsqigdadt lkahekkide vvitalgikk ekkaigyavq
       61 evkgdvleka kepnfinsls grvaglnikn stdlfqdpgi nlrgakpliv idgvpdrtad
      121 lwrvnaddid nisvlkgpta salygsvgkd gaimittkkg kkgkmtvsfn nstmfqtsfi
      181 riptvqtvyg ggnngkyaym ngegsgsegg gwiwgpkldq kdpttpsgyf etpqynspvd
      241 pvtgklvplp wisrgkdnik nffqtgliqs nnvsvdwgse katfrlsfsn iyqkgivpnt
      301 dlkttsisla gsvnpikdlm instltynke ytsnfpevgy gptnylynlv lwtgadvdvr
      361 dlrnywvagk egyqqrhynv syynnpyfqa yeylrpyykd nvlgnvnvey qivpnlsaka
      421 rvganiysln refrepksyi gygnkslgny tqvtgnyfdm tselglkyqn hysdnftlsg
      481 eayisnfyre lknseirtdg lvtpgwynlf nsigplflpt dgsrnrkeye qinsvygyvd
      541 mefyktffln mtarydkvst lpkgnneyfy psisgsllln qlltlpswin faklrgsfaq
      601 vstgkiadnt ygyisafeks nvnwngqssf yfgdilidgn ikpetvdswe vgtnigllkn
      661 risldvayfq trdynnlaki plsegvgyky yltngnvyqr rgveftlnad iikhsdfkws
      721 sqlnfsryrk ylkeayggkd yitvynpang renfvrvger mdkltampye tspdgqlvlk
      781 ngypvnstap feskmgysdp dwtygfshnf syrnfslsll fdgriggtmy sttnqkmwwg
      841 giapgtvnqy rddanaghnt yiapgvqvvs gsvtynqngt iksdtrifap ndiavnynay
      901 mqstsnafes nyhyykqtfi klrevtltyn feksfvnkln vssasislig rnlwlasdik
      961 nvdpdsgmdq lqtpatrsfg vnlnvkf
//
LOCUS       WP_103293588             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103293588
VERSION     WP_103293588.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110723
     Region          35..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrketqkllv lsllglisvn ltaqqkakkd tikgldevvv talgikrhdk slgystqtvk
       61 sdeilqtqnn nwaqslegkv aglkiqtaga gplgtsritl rgdismnmgn ngalivvdgv
      121 plsdkktgtg tsaygagsgg dlpidygdsf nsinpddies vsilkgpsas alygsrgsrg
      181 aimittksgk tkkgqiqvtl nsyssydtvl kwpdyqyeyg qgtqqkdkng nyyysygasp
      241 dgvntgstss afgpkfggqy yfqydptieg qslerqlwrp yknnikdfwq tgatysnsls
      301 iahsnettaf rtslsylkne wmmpntgfnr lnaaisldhk lsnkikigtk vnfsqttsdn
      361 lpatgynnqs isyfmifqnp nvdlewykpi wrkgqdqvdq ihpfssyidn pyliayenvn
      421 tsnkkiltgn lnisyqlakn feiayksgle wsnemrtqrr pwssanylkg yyresyiryl
      481 dlnndlllty knkfgdfgvt asaggsiryy estlsdyrai glnkaglyql snatsldnrl
      541 pkpndnqvns myalanfsyk dmifvdvtar ndwsstlpsh nrsyfypsvs ssfilsdlfk
      601 vksdnfnfwk lrlswskvgn dtynymldky yensvfsgsv espllypnpd lkpemitnie
      661 ggmdftllkn rltlnftayq insknqsivi pvlyetgynk riinsgelrn rgieltlnay
      721 piknknfsws vnanwsmnrn kiislpdefq gqpytmasvg gvvyynavvg gslgdmygyg
      781 lmyspdgkvi ygsdgltakp temkkignay pkwraglqne fkyknftvsf sfdgqykgma
      841 ysqshhkmse qgklvhtleg rdnpgglivg qgvvqnpdgt fspntkgipv styygdyyrr
      901 anvetnsfdt sfiklrdari sysfpksvte slkmtditla lfgrnlwmwt kfplfdpeaa
      961 tlddstitpg vemgqlptar tvgiqlnvkf
//
LOCUS       WP_103294125             917 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium lactis].
ACCESSION   WP_103294125
VERSION     WP_103294125.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lactis
  ORGANISM  Chryseobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Chryseobacterium lactis"
                     /db_xref="taxon:1241981"
     Protein         1..917
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102624
     Region          31..916
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkktnrltt ggyfflvcgv lsaqttvkkd tlqenkiedi vivgykaqkr ssltaavsvi
       61 sdkklkdsnt pdvagllqgk aagaqilpgg gnpgstasvk irgtstingp sqalwvvdgv
      121 mmngvpnldp nqiesinilk datstalygs rgangivqvf tksgtsgkgs lnisvnnsfn
      181 tfnngrfklm dgtqlydyft slknapsipg glrnpgynwl kdgtqtgavq nytidfrggs
      241 qnsktyisgn yydesgtvks ydynrlsfri nheqtvrpwl ilrpklslay terknrqgsl
      301 eemylnmpwd nprnsegnli npntfngtwy grdyanylyd lqwnysksnq ldlignfdae
      361 ikltdylkfi ttnnvtykny ddmsytdprs iagesikggl tesyvkdisk ffnqmlrfdk
      421 dfgvhnvnal aayeytdriy kiskagvygi vpgseifdng attgqkpsgk kydkaynafl
      481 fnaeyvydkk yfvqgslrse sssafglsqr nglfysysag wnihkekffq vkqinewklr
      541 asrglvgntp spnygwqdly altqvyngqi gatwnqlgnk dltwesiyqn nigtdirafn
      601 nrlsinvdyf nnktknllvl vtlpsltgvd rqylnvgdvk negwefnfny alikskavnw
      661 dvgfnistyk nrvlstrnns tqllsnnqva ivgndvtsfy mrkwmgvnpd ngaaqwevvn
      721 adgsksittn ynqatlqivg aatpdyygsf ttnlsinnfy lnaniyfsqg gqiynsyrel
      781 fdsdgaypyy nqmvlqngws rwekpgdvat hpvatfnnnt ltnkpssryl edasymklrs
      841 lrlgynfpqs lteklhvrsl slyimgenlf titkfsgvdp evgpsdadkr dgnpysgnag
      901 aiypiprrfs lglnfsf
//
LOCUS       WP_103306484             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. MPR-ANC1].
ACCESSION   WP_103306484
VERSION     WP_103306484.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. MPR-ANC1
  ORGANISM  Pseudomonas sp. MPR-ANC1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. MPR-ANC1"
                     /db_xref="taxon:2075548"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38833
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_103324443             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_103324443
VERSION     WP_103324443.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38707
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapndsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvviehgv tivgptnlag avaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_103321830             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chromobacterium sinusclupearum].
ACCESSION   WP_103321830
VERSION     WP_103321830.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium sinusclupearum
  ORGANISM  Chromobacterium sinusclupearum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Chromobacterium sinusclupearum"
                     /db_xref="taxon:2077146"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39869
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhiaipaerl agehrvaatp etvkklaaag htvaveagag kaaaipdaay reagasiveq
       61 rpallsgadi vlcvgspdaa dldalksgav lagmlspyhn pllpqlaakr vsafalellp
      121 rttraqsmdv lssqnniagy kavllacqfy prfmpmlmta agtvkaarvl vlgvgvaglq
      181 aiatakrlga vveaydvrpa treqveslga kfievpmsde ekaassgvya remtpeflar
      241 qnellakraa aadivittal ipgkpapvll paasvaamrp gsvivdlaae sggnceltra
      301 geawqsdngv hlvgltnlps mvaadassly arnlltflgl llsaeglkid leddllaatl
      361 ithqgelrfg ttakpaaqtn kepqhg
//
LOCUS       WP_103333170             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudotabrizicola formosa].
ACCESSION   WP_103333170
VERSION     WP_103333170.1
KEYWORDS    RefSeq.
SOURCE      Pseudotabrizicola formosa
  ORGANISM  Pseudotabrizicola formosa
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudotabrizicola.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Pseudotabrizicola formosa"
                     /db_xref="taxon:2030009"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54852
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egenrvamtp esalqliklg hacviesgag akagfsdaay ekagvevvas
       61 aqalydaadv vvkvrgpeae eakllrsgqt lisffwpaqn pdllaqvaaq gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aivnafdvrp evaeqiesmg asfvflefda selpdgaatg gyaapsspaf
      241 aakqlakfre lapdmdivit talipgrpap klwtadmvqm mkpgsviidl aaerggncdl
      301 tvpdekivtd ngvtivgytd fpsrmaaqss tlysnnirhm ladltpkkdg viahnmeddv
      361 irgatvthqg avtypppppk vaaiaaakpk pkaveltpae kraqeiaafk tqtrnqvgll
      421 aigavlllal glvapasfmq hfivfvlavf vgfqviwnvs hslhtplmai tnaissiiil
      481 galmqigsgs flvillaals vfmaginifg gflvtrrmla mfqks
//
LOCUS       WP_103343006             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis sp. CA-126428].
ACCESSION   WP_103343006
VERSION     WP_103343006.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis sp. CA-126428
  ORGANISM  Amycolatopsis sp. CA-126428
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Amycolatopsis sp. CA-126428"
                     /db_xref="taxon:2073158"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38311
     Region          10..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(24,79,98,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(53,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdseqsqql tvgvvaesrp gerrvamvpk lvgrlvqrgl rvvvepgags gahlsddayt
       61 qagaelgdaw gapivvkvnp pspaevgkls rgavlvgfld prgnpdglak leeaglrafa
      121 meavprisra qamdalssqa siggyravll aaqklprffp mlttaagtvp pakvlvlgag
      181 vaglqalata krlgaqttgy dvrpevaeqv kslgaqfldl gieavgeggy areltaeere
      241 eqqrrlteai trfdvvitta lvpgrkaptl vtadavkgmp agsvvvdlag etggnceltk
      301 pgedvvehdv tissplnlpa empshasely arnvtellel lvtkegalel nfedeivaga
      361 cvagregsas
//
LOCUS       WP_103348037             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis sp. CA-128772].
ACCESSION   WP_103348037
VERSION     WP_103348037.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis sp. CA-128772
  ORGANISM  Amycolatopsis sp. CA-128772
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Amycolatopsis sp. CA-128772"
                     /db_xref="taxon:2073159"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38343
     Region          10..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(24,79,98,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(53,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdseqsqql tvgvvaesrp gerrvavvpk lvgrlvqrgl rvvvepgaga gahlsddayt
       61 ragaelgdaw gapivvkvnp pspgevakls rgsvlvgfld prgnpdalak leeaglrafa
      121 meaiprisra qamdalssqa siggyravll aaqklprffp mlttaagtvp pakvlvlgag
      181 vaglqalata krlgaqttgy dvrpevaeqv kslgaqfldl gieavgeggy areltpeere
      241 eqqrrlteai tkfdvvitta lvpgrkaptl vtadavkgmp agsvvvdlag etggnceltk
      301 pgedvvehdv tvssplnlpa empshasely arnvvellel lvtkegalel nfedeivaga
      361 cvagregsla
//
LOCUS       WP_103368013             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_103368013
VERSION     WP_103368013.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38747
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael alikrgtvlv gmlnpfnndt iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyesdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_103381841             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudonocardia dioxanivorans].
ACCESSION   WP_103381841
VERSION     WP_103381841.1
KEYWORDS    RefSeq.
SOURCE      Pseudonocardia dioxanivorans
  ORGANISM  Pseudonocardia dioxanivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Pseudonocardia.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Pseudonocardia dioxanivorans"
                     /db_xref="taxon:240495"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37870
     Region          12..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(24,79,98,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(53,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msaeagapht svgvpreage gerrvalvpk vieklrgrgv evvvesgagl galipdelyt
       61 aagarigdpw sanvvvkvap ptseeigrls sgstligfla pltakettaa lkaagvtafa
      121 mesvprisra qsmdalssqa nvagykavll aasestrffp mlttaagtvk patalvlgvg
      181 vaglqalata krlgarttgy dvrpevadqv rslgaqwldl gieavgeggy arelteaera
      241 eqqkrleeai tgfdivitta nvpgrtaptl vtakavegmk pgsvvvdlag esggncelte
      301 pgrtvvkhdv tiasplnlpa tmpehasely srnvsallel mlddtgavap nwddevlaks
      361 cvtrevan
//
LOCUS       WP_103398689             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. FW300-N1A1].
ACCESSION   WP_103398689
VERSION     WP_103398689.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. FW300-N1A1
  ORGANISM  Pseudomonas sp. FW300-N1A1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. FW300-N1A1"
                     /db_xref="taxon:2075555"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38681
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg htvtvqsgag vnasvvdsay eaagavigsa
       61 qdafgaelil kvvapsdtel tliksgtvlv gmlnpfsnet iaklaergit afsleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvivahgv tiagptnlaa qvgadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_103393001             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas laurylsulfativorans].
ACCESSION   WP_103393001
VERSION     WP_103393001.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas laurylsulfativorans
  ORGANISM  Pseudomonas laurylsulfativorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas laurylsulfativorans"
                     /db_xref="taxon:1943631"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38528
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag vnasvvdsay aaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvivengv tivgptnlag avaadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_103409706             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae group genomosp. 3].
ACCESSION   WP_103409706
VERSION     WP_103409706.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 3
  ORGANISM  Pseudomonas syringae group genomosp. 3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae group genomosp. 3"
                     /db_xref="taxon:251701"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38840
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqrgag iqasvpdsaf eaagaligea
       61 seafagelil kvvapndnel alinsgsvvi gmlnpfnnel igkmadrgvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv egsdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera rladiiitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adevvvahgv tlvghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_103411527             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            campbellii].
ACCESSION   WP_103411527
VERSION     WP_103411527.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54520
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agesrvaasp ksveqliklg fdvaiesqag vlasfddaay eaagakivss
       61 eevwtsglil kvnaplvdee kgideiallq dgatlvsfiw paqnaelmeq lssqninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgkpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqvitta ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg nididfedvv
      361 lrgvtvvkeg evtwpappiq vsaqpqakpq epvkpqpkve eptspvkkfg alavglgafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_103410800             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            campbellii].
ACCESSION   WP_103410800
VERSION     WP_103410800.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53122
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmsap iavatlfasq lflvgaplaa edkglvdprn dvfeqnhpdq yhswkatses
       61 ehiedalsed pnmvilwagy gfakdynkar ghfyalddvr qtlrtgaptd eksgpmpmac
      121 wsckspdvar vidergedgy fegkwarlgs eivnpigcsd chdtrseefk kgepalavtr
      181 pyverafdai gknfdeqsrl dkqasvcaqc hveyyftgpt kavkfpwdmg ttvndmekyy
      241 dalnfkdwth avskapmlka qhpgyetwrd gihgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfed tcaqchtqtk eqlqgivstr kaqvlnmklt aekqivaahf eagaawkaga
      361 tekemqpilq dirhaqwrwd yaiashgvhm hapevalevl gtavdraada rtklvrllat
      421 kgitdpvqip distkakaqe algmdmekmn tdkkhfletv vpdwdkaaae reaty
//
LOCUS       WP_103414227             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            campbellii].
ACCESSION   WP_103414227
VERSION     WP_103414227.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54492
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agesrvaasp ksveqliklg fdvaiesqag vlasfddaay eaagakivss
       61 eevwtsglil kvnaplvdee kgideiallq dgatlvsfiw paqnaelmeq lsskninala
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgkpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqvitta ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg nididfedvv
      361 lrgvtvvkeg evtwpappiq vsaqpqakpq epvkpqpkve eptspvkkfg alavglgafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_103435409             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas putida].
ACCESSION   WP_103435409
VERSION     WP_103435409.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38758
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp dtlkklvgqg hqvtvqrgag lnasipdsay eaagatlgsa
       61 adafgaqlvl kvvapsdqel alinrgsllv gmlnpfnsel igkmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrptvk eqieslgakf ldvpfetdee recaqgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvlehgv tivgptnlpa qvaadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgnvir nng
//
LOCUS       WP_103438916            1131 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103438916
VERSION     WP_103438916.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1131)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1131)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1131)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1131
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1131
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124086
     Region          25..1130
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkihfflm altflclngv maqsktisgs vtdandgapl pgvsivvqgt tigtqtdfdg
       61 nfnieastgd ilvfsylgmk tqnvtignst svnvsmqeda sqleevvvta lgikreeral
      121 gyavseikgd diaqvaqinp inamqgktag vqisttsggt fggtritirg nstfdqntqp
      181 ifvvdgvild ndisgesgad wgnqlknlnp ddfesfsilk gaaasalygs ralngvvivt
      241 tksgkkskgl gvsvnqtvgv rtvydtpnfq nqygsgltag gfsfvtngpn trtrddahdt
      301 gqfftydldt glpsmafdsy eehaaswgpr fdgqeiidyd gsratwsaqp nnykdsfdtg
      361 firntnvaid ggsetssfrl sfsnfsesgv elrndfdkns lsfkgshdli kdkltvnavm
      421 hytrskaknp lqpggltswf hdgfprnydv nkwknnyldv dggvphpngd nynftrmsri
      481 wahaleddni rtegsfisni nlnykisdni tatldgninq ytynqetktf adnrdrlngs
      541 yyfgngekfq hsfsaklffd kqinddirmd lllggelwts keqgqysntt ggfkirdfys
      601 lanskdalra gggigprkki nsvyaffnts ykrelyfsat arndwssalv ypngkgnnsy
      661 fypsaslgwv ssetfelpdf isfaklrasy aivgndtdpy rlstgfvadn fsqnpdlnmf
      721 rfedntavsv nlkpekkysf etgldlrfwn nrigldvayy kdntknqiip lqvpsesgid
      781 nqlinagnlq nqgieaalnl kivdnpdfsw diganythnr dkiielapgi nefrlfgnpd
      841 dsnsatasya yvggnygdlv trrgydyydg tnsanqgipv lanrngwsva ypigiqnkds
      901 lfvmgnmqad wyggmntsvr ykrvrlsaiv dakfggeiys adaryglhqg vlesslpnrd
      961 asqggitwts egqgqnffgk tyedgyipng vfpdgttvts gpsdnrtnvd vggltyqqay
     1021 dqglvepthw sgyvyrwtsa stgtpitgvy tsswvalrev tltydvpsei ldkllvksas
     1081 laltgrdlgf lynslpdnin ptlssnaaan plqqksspyi rsvsfslkln f
//
LOCUS       WP_103439001             990 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103439001
VERSION     WP_103439001.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106391
     Region          26..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkfiktnm flfflvtpll llaqdvvkgk itdtglgdpl pgvnvvikgt ttgttsdfdg
       61 nyeisvdnfp atlvfsslgy apkemqvtgp ttlnvamees atgleevvvt glatsvkrsn
      121 sansvasvsa deltgrtppq tldgalagkf agaqitaasg apgggmsvkl rgvtsingqg
      181 qplyiidgvy vnnnsvyagg lneisnaagg gasstdsqdn asnriadinp ddiqnieilk
      241 gasasaiygs raaagviiit tkkgkagktk infsqavgfn eavnllgqrn wtaalaedvy
      301 gegalytaae sagrlrdyek eiygekgflt ntnlsisggs dktsffgsft nneedgivkr
      361 tgaskqslrl nvdhritdni klsltgnyle ssadrgffnn dnsnttigvs llftrpwdyl
      421 lpdadgnypd hpanssnqih trdimtnnes vsrliaggsl dvnlfsnenq slkmilkagl
      481 dtytlkttvf fprelqfmsp avggvdglss dgttqntdan fsgflvhnfr tdnelsfttq
      541 agvtneqfsq ntvrvtstgl iaseqnvdqa anvkvdqfrl eqedagffvq eevnfqdkiv
      601 gtlgirgdks snngdanklf yypkasaavn ihnfdfwnle qvnqvklraa ygeagnfapn
      661 galfttyins lidgnvgiit patlgdpsiq perqkefeig mdagffnnkv tleftwynkk
      721 vedlilqadn epssghtfrw anagalenkg aelginvnaf dtedfswesg iswfknksei
      781 teltvasfdt qgfgtglgtf rieegksatq ivgndengnv valgdaepdf qmsfnnnfky
      841 kdftlsflwh wkkggdnvnl srllsdfgnt sadydevsld psgalnngdy rksafgagfa
      901 gpfvedasyl klrevglyyn lpentlqklf kgtvsnvkig lsghniisif dynsydpevs
      961 nfgsgaagig ievapfpssk rfmfhlsigl
//
LOCUS       WP_103439632            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103439632
VERSION     WP_103439632.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111023
     Region          24..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkllksll lfgtflcfgi asaqevsgtv sdatgplpga svvvkgttng aqtdfdgnft
       61 isdvaagstl vfsyigyktq evavsnqttl niimeedaqa laevviigyg tttikdatga
      121 vsavtsedfn ggvisspeql iqgktagvqi sqgsgepgsg vsirirgtss vrsnndplfv
      181 vdgvplpsgg sssegtdigv gsssarnpls flnpndiesm silkdassta iygsrgangv
      241 viittksgkg gaqggtwefs sdlsfsspsn efdllnrsef lsavsafggs atdlgndtdw
      301 qslvtrnsss tnnnlaysqn ygsgnvratf nygkqfgivp kssqervtgr inltqrlfdd
      361 klrldlqsti srvndeappl sgsagstgdm lgsaysanpt wpanstfnpg drinplnllq
      421 nwqsltytdr flinfsasyd ivedltakvt vgydksestr eaelgsksfn vgrgaggngr
      481 galndlnlen rlleltlnyk kdfgnsvlea lggfsyqdfn tqgrnvegwg ygtsnlnnma
      541 rdltnaaskl esmitgsyqq ygyssggdad lfvnrlfptp vsdrlgevsi pvksvftntf
      601 dntdelqsff aranysiask ylftatvrad gssrfgennr ygifpsaafa wkineedfmg
      661 damstlklrl sygitgnqdg lgygrfarre rystttngdp nigdggavsv pgittvefan
      721 pdlkweettq ynagldfgfg ndrfsgsidv yrketrdlll nieaaqpspq ptffqnldav
      781 vlnqgaefsl nydilqgddf gwnagfnvsy nkneitdfdg eiaagtirga glsnafaqrl
      841 asgqplysfy lrkftgfdan gnpvheggvd nqqfvgksal pditggfsts anyknwsasm
      901 yfngqfgnyi ynntanafft ggaigsgnnv tqnvvelagq egrfaeasvs trflekgdfv
      961 rlqtasisyd vplkeglfks mrlsltgqnl fvitdysgld pevsvapasa allnglpiag
     1021 idysafprpr tytlgfnvtf
//
LOCUS       WP_103439824            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103439824
VERSION     WP_103439824.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119194
     Region          25..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskltwila pimglfmsfs yaqektitgt vtdqmglvlp gvnivvegtt igtqtdfdgn
       61 ytiqgsqgqs llfsyigqms vtkvigesst idvvmqedaq aleevvvtal gisrdkkslg
      121 ystqevqgee lstvksgnfv nalsgkasgi qikknnnlgg stnvvirgna sltgsnqalf
      181 vidgvpvnnt ntnskyqgea sgnyydygnt asdinpddie svnvlkgaaa salygsraan
      241 gvimittkkg kdsqgigvtv nsgisigsid kstfakyqnq ygagygpyyg pdeddffnme
      301 dvtgdgvadl tvpytedasy ggrfdpnlmv yqwnaldpds pnyrtatpwv nakngpitff
      361 etpitttnsv sfsrsyeddg sfrlnytqfd qsgimpnssi kkhnfsmsgt fkltdrltvt
      421 gyanyintka hgrnstgynd nqisnfkqww qtnvdlkelk diyfdtkrnv twnpatsdag
      481 sapifwdnpy waryenyqnd grnrfignvs ldykftdwln ftaraatdty seiqeerran
      541 gsvptsfgip dsagnrgnvd sgygrrnldv tetnydfmfn fqkdlsedfn lkgiigtnir
      601 rsefqsiysa tsgglsvprl yslqnstgpl alpveiaeki gvdgiyasas lgynsmlfld
      661 atirrdhsst lpadnstfyy psiatsfvft nllnadfitf gklranyaev gnsapfdfly
      721 dtynvnippg apstsvdnqk knpnlkpekt esfevglemk flhnrlsfdl ayyqtnsidq
      781 ifgvpvsrat gfeekilnag eienkglels isgnpvrtdn fswtamvnwt knknevvsle
      841 dgiqtlqlgd fqggvtlnae vgkpygviyg tdytylnger vvdpadgqyi ktstsdqtig
      901 dtnpdwlmgi snkfnyknls fsflidiqqg gsifsldqyy gratglyaet afindlgnpv
      961 rnsladgggf inegvnpdga tntsriradr fgafgyrrgl pdkafvydas yvklrevalt
     1021 ynlpsklltn tfltnaslsv igsnlwiidk niphedpegg lsagnlqgys vgslpttrdf
     1081 gvnlklqf
//
LOCUS       WP_103439925            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103439925
VERSION     WP_103439925.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112170
     Region          21..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnklililai fgtiitagaq ktisgqvlek dtntpllgvs vlvkgsmtgt ttdfdgnytl
       61 adlstdaiie fsyigyttqe ftigdqttin vfleinaeqm devvvtalni qrdkeslgys
      121 isqvsseevn varennvmns lsgkvsglqi tqsntgvdgs srvllrgitt ingnnrplvv
      181 vdgipisngs ggagasggid rgdalsdinp ddvetisvlk gagaaaaygs lgmngvilit
      241 tksgtkkagv gislnssfsf sdvaltpdfq neygagafgd fapinadgrp vldypfswsw
      301 gpkmegqtyt nwlgqqdnyt pnskrnpyke fyqtgftmsn tlafegrndk gsfrlsitde
      361 dgqgivsnnt ltkqtfslrg ssnltdrfsi dgkmtyitsk vsnrpqlaeg sgntalqlsl
      421 mprdirlddv rnntvnange eikwnldntf nnpywalena gnvdekdhfq gfisanweid
      481 dkfnitaksg mdyiindyts ygatgaqaiq nglgsynhdg dqssiwnsdi lgtystdlsd
      541 fnitlslgan yrneysnykn isgndakvpn fyrisnykns fssegiseka iysyyalgqf
      601 gyrgflylda tirndnssal pqannsywyh senmsllftk llginsnils qgklrgsfak
      661 vgndtspyrt qavysvdqtv tlpytvasis eslpsfdlrp etsesweiga dlgflknriq
      721 ldvtyyktnt tdqimavpis gttaysskvi nageienkgi eaqlnlipfd senfswdlgf
      781 nftksnskvi tlneglesis lgslwtasve arpgqefgti ygndflrdnf grkiigndgl
      841 akrgdrvalg ninpdwyggf tnkiryknft lsslisaqvg geyysygrgy rlffgtders
      901 lvgrenglve egineftgfe ndnetsallk qftdifsnei atdiildatn vklrevaltf
      961 dfpktmlrdt fiqsaslsav grnllflyna agdidpeaty ssgpastafe hsslpstrsy
     1021 gvnlkinf
//
LOCUS       WP_103440016            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103440016
VERSION     WP_103440016.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115500
     Region          58..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklrgcrlf lfkkpenqkl kinlvlflfa laaitmearv ilepmvdegl iegvfqdqev
       61 tgtildennv plpgatvvve gtvigatsdf dgnysisvpe natkltisyi gyetqiisin
      121 grseiniqlk vtanaldevv vtalgiersk rslaysvskv ggdefteare tnianglvgk
      181 vagvdvtrta sgpagtarvl irgnssltgn nqplyvvdgi pidnanrgsa gewggsdggd
      241 gigninpddi esmsvlkgns aaalygsqas ngvilittkr gktnhglqve vnsnyvlena
      301 inhldpqtqy gsgllgvkps tqaeawaage fswgakldgs svvqfdgvsr pysysgnnfd
      361 kfyrtggtst ntvslsggte nvgyrfsasn menedvmpns gmkrqtfsan lhgkafdnkl
      421 sfqtsaqyil qdvknraqla dspgnshytv wqlpvttnil dlrgdpnrlg anpedatdly
      481 gstfgkkgye llptssiwmq npywaayqqt dkdskdriia sasmqydvnd wvyvkgragi
      541 dqsdrlsesi nptgtghnln ggmsqsqnky qqtnfdlmlg srhefdngia ydflagankm
      601 rlqedgtsas gnnfalpffy sianginngg gssyvklgsh svygqaeisy nnwlfltgsa
      661 rndwfsvmdg rdvfypsigl savlsdvltl pevidfvkvr tswaqvgsvg digayslnqn
      721 yslgraqlgi prgaisgssv rnsnlspllv telelgfniq flnnrlgvdf syydkktedd
      781 ilnagisyts gyrstiinvg eltnkgvell ltgvpvrten fswnvsfnms hntskvvslv
      841 dpdndeesfn iglsrarhaw vthiegkpfg qitgsqylrg angeltldan glpqvdvaag
      901 tvafgtgvhp fvaglhnsfr ykdftlgvlv dmkdgavghs gtnaqlyrrg vhkntlvgre
      961 tglgvipasg isayyeriyn diaeefiyda gfvklreitl gynipsklla ktfiskanvs
     1021 lvgrnlwlih snvenidpes syasgnaqgl dffampqtss fgfnvnltf
//
LOCUS       WP_103440077            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103440077
VERSION     WP_103440077.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121193
     Region          25..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkfhyyll lasflfvqgm maqsktvtgt vsddlgtplp gvnvvekgtn ngtstdfdgn
       61 fsisvsnnat lvfsslgftk keiavgaqts vkvvleedae qlgevvvtgl gitrekkalg
      121 yatatisada ltetatpnfa talygkapgv sinttpggst sasnitirgv asitgrsqpl
      181 iildgvpird gevsnnnywg dqrlrgngll dinpedidni silkgasaaa lygseavngv
      241 vlittksgkn rkngmtvdls ssysfdnvay lpryqtvrgp gaplnvsngg qdaegfiyhd
      301 vdgngtaetr gvlgysinfg pkfdgkptig wdgivrpyea qddrygglfn tahntsvnms
      361 itnvtdnsnl rfsytrqdnq gisigaeeek nvfnlnatfk waedfstdvi vnyvnqsvfn
      421 rpysvdrltn nftgmmspfd sadwyldryk tsrgyryvtg tgqsltpeen iiypgfkgdi
      481 gdfvwrvken aleeqsnrii gtitnnwdia kglnlrgris tdftnrrsea sntterplaf
      541 gnsggfsmsn snynslygel llryetpitt dltlammagy natkqsesnl nrgtngglsv
      601 enwfdisasv ntpnsgssrn sivkdaflgt mnldykgyfy vegtirkdkt stmnpnnnsf
      661 vypsvnssfi lseafdlplf mnyfkirgsw givgnypdpy qaniaynqnt lgsqggnpvl
      721 ytnipssfgn dgirpeekhe yefgmelkff qgrlgldasy ynaqvvdqil pltlpnssga
      781 gsvltnigtl rnkgyefglt gtpidtgsfr wdvivnvakn eniveklapg ldellhadyd
      841 gnaaqlkslv gqpmgdlyah pvatdaqgrr ivdpngmyki dadkmekfgn ampkwtggvm
      901 nsfsyknitl dalvdgrigg hvmptalnwm tsrglteest kfmdtesggl syyeengtgt
      961 riqttpsata gpggevvyhd gilldgvtnd gqpndqiass adyywtvynw ggpqyspntr
     1021 yelyikenty fkmrelsigy kmprkvidki glsklqfsvf grnlfyiyrt ikdmdgeqtt
     1081 agsrwfqnvn nvgtnpstrs fglmvrasl
//
LOCUS       WP_103440079            1130 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103440079
VERSION     WP_103440079.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1130
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123346
     Region          25..1126
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkihyyfm ltaflvvqgl vaqnktvsgt vkddvgtplp gvnvvekgtt ngastdfdgn
       61 ysinvsnsat lvfsslgftt kemavsgqst inisleedse qlgevvvtal gikreskaig
      121 yamtevqgee larinvvnpv qslqgkapgv sigasdgglf gnskiqirgv stlnssnnqp
      181 ifvidgvile ngtsgasadw nsssndygni lknlnpddyk tvsilkgaaa talygsrgin
      241 gvvlittkdg sgtrgigvsv rqsvgfdivy kgpalqneyg pgtlagyvny gnqdssnnyy
      301 nwdtqqfsyn sdgqpsminh aggglsygpk fdgrpiedyd gnmvpyeaqk nnmldaystg
      361 vntntsvavs ggndkgnfyl sdsynertgt lpnnsfkrna lsfrgsynla pwlrasasvs
      421 ftdsnshnpr ndisqgffdg tfernyntsk ykqqqywqap hggvpnanfg deftnvpnrg
      481 lwfayennnn yrketvvrpi vslaadvtdw ltitaegnmn hyttefeakn lgsgfanegg
      541 syelrhdkdv aktgklifnf nkditpdlsa nlllggeiwd hkqsytrawt dgglivpgrf
      601 yignslrtqr gdggvsdtkq lnsayflahl eyrdqlfldv tgrndwssal vytdgtgnns
      661 yfypsvsssw vfseatgtsk wftfgklras waqvgsdtsp ytinrgygqg sidnggnfvy
      721 tntvnttlvd rsirpelkds yeigadvrff nnrlgidvay ydetiseqig nvplpsesgy
      781 nnlltnigtl tntglevsvt gtpiksnnfs wnttlnywdn ttkisevhpd fgeykslggd
      841 itygnfrvgs vafeggeygv lysdsapkkf estdpshpnn gknqliwvds rrgayyersg
      901 vpekvgkaqa dfegswnnef nignfnmsil ldarygghma syssrygtsy gytekslrgr
      961 dpehggltwa sgyadvqgtq fsdgvipdgv faegqmvtap sgtsvdvggm tyqeafdagh
     1021 vepthasyyn yrrnswgngv vnddwfsevk yialrnislg ynlpkmaask mgarnvylgi
     1081 narnvaylyn slpndinpes frgttssdsf rersfspyla sytfsiaidf
//
LOCUS       WP_103440565            1133 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103440565
VERSION     WP_103440565.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1133)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1133)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1133)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1133
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122842
     Region          36..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntylknkiq slgqlslmll vfcsasvmgq svqhmvsgnl tssedgmplp gvsvvlkgtt
       61 qgvssdfdgn ysinvpngng vlvfsyigfe aqevtvngrt sinvtlepga qaldevvvta
      121 lgikradksl gysvenvage eltrvaqenv lnslsgkvag vtlnstggtg ssvsmvirga
      181 islssdnqpl fvvdgvpian svnniggfgn dnkvdygnai sdldpnsien vsilkgpsaa
      241 alygsragng vvlittkkan ekekmkvsft sntvfdvpyk yleqqtrfas gyfsfspesq
      301 ggsnlmpava lsggnsgsel drgyfavqwn apldangvpi ptelrsypnn iknfvqtgit
      361 ttnsltvtns tkalnyrlgv tnmentglvp nsdvnrnsfs lsassnlndk leittnvnvv
      421 hsfadnrpas nrganplqwa yampanidil sikdydlpgt dvlslssdyn npyflanevn
      481 nsysryrifg nmaldwklsp sfnirtsynl nssnqtqetk mspgysgetn ngtygisktd
      541 gvetnvdlla tfskefgdfd msisgggnlm yqkssgisns aasrvglvvp dlftisniap
      601 talvyssfms erginsvyal gnfgfkdmly ldvtarndws stlpvdnrsy fypsaslsfl
      661 lseivdipkv dlfklrggwa rvgndtspyq lgayynnagq wdnailysap gglstptlep
      721 eeatskefgv dltmfnnrfr fegtyytven knqivpsvpi pgssgygsvs inagvleskg
      781 yelslgvtpi rtenfnwdln vnfttneskv laladgvdyi efwsenksvs rgyvanaatg
      841 edglvgnlys pkiqrvtdan spyfgypmlg egedaewlae eervkvgnyn pdfvmglqss
      901 fsyknftlnm tfdwrsggqy msqtsrymte dgysqqlldn lidpginetg pelkqwvldn
      961 adlllygenf isiggppgeg gfpeafsgtv vydgvfnagv vgyhdengnf ilenenlgld
     1021 gtafipfsva nawdfgtphm fdadyiklre islgydlprk fvekagldnv nlsvysrnim
     1081 lwtkdssfgv dperayqaea gqdkrgtqfk qgierynvdp wvvpvgfkig itf
//
LOCUS       WP_103441512            1122 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103441512
VERSION     WP_103441512.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1122
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122573
     Region          67..1121
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknllnvrsr rscppknnlk iklsilliyg alfnisahty enseyilfgp niisndfgal
       61 eitaqqieis gtvkdvdgev lpganivlkg tskgvvsdfd gnftiavpna qavlvvsyig
      121 metkevvvgn qtslevlldy aaekmdevvv talgmkrekk algyavavve aealnqqpnt
      181 nvlsglsgkm sgvqinemgg dinakmnvii rgqtsltsnn epllvidgsp vgntdamrdi
      241 ssldiasisv lkgasaaaly gsragngvil ittksgegak kgigvsftqs ttlsvpynyf
      301 elqntfttgq kgqfnesswq ywygpragve avqwntngqa qplvmydnsl qdffqtglst
      361 qtdasisgny drgsfnfsin hmksdgitpg melkrlgfsl atsykitdkv klttnitisk
      421 ptsdnlpltn ngsddiymdi fanaphvnin dlkdyweveg sqqrragalp nnpwfsayer
      481 drtldqirgf gnvrldidil pgltamgrvs fsannekies iypwsydgfg ssavkpfgay
      541 eqtklderes nvdflfsydk kvgdfrinps vggnylnsrn tslygggdvl tlpalytlsn
      601 varpglgyns gvfekeiysl yglaslsfke mvyldltarn dwsstlpken rsyfypsasl
      661 smlisemtqm pswvslvklr tgwaevgkdt dpysinpiln qtfwgndiqy svpgslpnta
      721 lkpevatsye vgadlgffnn rlgfegtwyk tqnrnqiigv ttspmsgfss atinagnven
      781 tgielalnsv pvrtanfewn lgfnftkqes rlvelvegid rigvgnagsl tqqtfvggii
      841 gdlystsvlr vesgeyegwp ilnnnggltf qtdnalkpkv gkstndfnvg mntsfkyknf
      901 tlsanldwrq ggnfysetmk rtsrsgwvdk wqgdagtfsg ilgsnsfngd gtalaneiks
      961 nptkyqadnv wvggrdaqtg gfpyngfdng sfwpgvvkns dgtytenfgg pgtrlfdayk
     1021 vvepggglwd vgssfmydls fiklrnitft ydmpqkfask isaqkvsfsv ftknimiwna
     1081 adigidpela yyqnngsydi gkekwnalpw vapvgftinl tf
//
LOCUS       WP_103440720            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103440720
VERSION     WP_103440720.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114057
     Region          25..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklngilt lflalivqls faqektisgt vtdqdglplp gvnilvegtt tgtqsdfdgl
       61 ytieanvgev lvfsyigqkn armtvgasst invqmeedaq aleevvvtal gikrnprslg
      121 ysvksveaea itensepdli kslngkvpgv nvnvstgvag asnkisirgt tsfqggnqpl
      181 fvvdgtpysn dqvtttsqit ggggyesgis sldpndianv evlkgavaaa lygsravngv
      241 iiittksgks gglsnkkfev slntgvyfek ianlpeyqnt ygngtnfnyn nangswgarf
      301 dsretiptwp nllnafpdqf gptvpyvaqp nnvkdlfktg fvadnsvnis sakensnfsl
      361 tisnidqqgy ipfnsykrtn isaggnfkld nglkvganls ysdsyqvgpf lgenqfvgaa
      421 ssfartlvlg rtwdlslpye dangapvipn ggwdhplwsw ehnqirtgvn rtvanvsfay
      481 dfnehinary qlginkydla rieitdkgsr gasgtgsvvt dnygseeies tfvvtfnydl
      541 aedlnmnflv gnnvnqissh rvgytgtnli adniftvnnt anvvsdvdnt trkrivgvfg
      601 dlglgykdfl flnatarndw sstlpqtdns flypsvstsf iftealginn dilsygkirg
      661 gwanvsrdad pyqinkiftv gtvysgqpsv fvpatlgnpn lspenteefe igmdlelfsk
      721 rvlvdftwyq ktttdlisev nvptssgyts lltnigemen kgievgltli pvrtdnfkws
      781 tftsftknkn vvnkliegld rfpidvdqia fvdegepfgv fygtafmrdd egnylieqse
      841 ggilqaldnq vvgdpnpdfk igftntfkyk tlslqaqldw keggdisssg iaallgrgvt
      901 kdtedrertf ilpgfygdpi tgepildgsg nkipnttqmt mnnlyfsptn sntfginsvd
      961 eatiydgtvf rlreialaye vpkkfldktf iggmtfsvvg nnlwyfapnv pkytnfdpdv
     1021 taygsgnlqg ietqsapssk rfgfklnvtf
//
LOCUS       WP_103441586            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103441586
VERSION     WP_103441586.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115959
     Region          35..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnlfknvrc rvlllltllc tlfsmnaygq dgfgvsgtvv defgvplpga siiekgttng
       61 vvsdfdgnfs fevasqnatl tisyigfeeq qipingnali dvtmqstast ldevvlvgyg
      121 avkkkdltga isqvdaaals dqstnsvtdv lrgnvaglsi glsaspkgts qirirgnnsl
      181 sagssplivv dgmiyngdls diapsdidkl dvmkdassaa vygargasgv ilvttkrgts
      241 dkptinints vgmasdayke rpydaqgyvn wrtevfksin pqntidnpgr yndpnnlpsg
      301 vsldqwlayd gsagdptraw lnrigfqdve ienylagnsi nwydrimqkg frndintsis
      361 grngglnyyw sigrtsnegi ingekfealr srlnldakit dwltvgmntq fakrnegfia
      421 adrgqierss pwgsefdddg nirlspqddn gagavnafla qkfndridld htfnsrvyak
      481 lklplgfsye vgytnrlefq eyynhssaas pqnvvgsaer qvtkinewql dnilrwdkti
      541 dkhsfnlmfl vygekyqsyl trarantfep sdalgysale lgtvqtvdse detstgdavm
      601 trlnynydsr ylltmtmrrd gysafgtnnk rayfpsiaga wtisnesffn sefvnflklr
      661 lsygengnrd igrftalsrl gankylnvda ggnvitvptf dngtqentel rwertkatnl
      721 gldfslangv vegsieayqn itndlivtre lpniigfnnv ttnlgeienk gleftlatqn
      781 ynrenfqwnt sfnfslnrne irklygdlde ngkeldditn qrfigqatdv iwgqeaigiw
      841 qtneaaqaae ygvfpgdwki ndvdnsgdft vddnvfqghr sprfswamsn rftmlknfdf
      901 sfevysnwgq krvfneaknr ngfidrtnsi qtpfwtpdnp indyarlfss dgssnfaiwr
      961 dasfirlsni tiayrfpkpl leklslqslr lyanarnvav yaphwdfydp eptnidgrns
     1021 ngstdpslpt prfftfgidl sl
//
LOCUS       WP_103441594            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103441594
VERSION     WP_103441594.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118012
     Region          46..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrktkllg llfsvgiaqi lsanmlnsni eakgtsslfi evsvqqqitg tvvdedglpl
       61 sgasvlvkgt tngvvadfdg nfsievasgs tlvisyvgfe tkeivlglen klkivltagn
      121 aleevvvtal girkekrrvg yatqevtges lqkaiapnvv esltgkisgv tvtsngsdff
      181 sdpqiylrge kplivvdgvp qpnsdfwnla sddienitvl kgaaasalyg slgangaiqi
      241 tmksgkgvdg tvisfnsstt fqggflriph gqtqygpgnt gryefgtgaa ggggvndfdy
      301 svwgpkfdgr lvkqfdspid petgeriptp wisrgddnlk nfmevgmvts nnvtvqsssd
      361 kgsfvisnsy kyakastpgq rldintfrlr gnlilsdavn idgslqynyq ysdnrirgty
      421 gptspiylls iwgganfdvr nfdgdniwlp gkegikqnfv enwrynnpyi lshywkkpwt
      481 kndiltylqg nfklsekvsa sirstlnsys ltnneeiskd iynydipdrg grfrynatry
      541 fenntdflis ynddffddev rlngtlggnq rylrienesa sttqliipei ftldnsvdqv
      601 tptsskeykg vysayaaidf syrnqlffgm tgrvdksstl psandtffyp svymsavlsd
      661 ifelpepisy lklrsayaqv ggdlgiyeat nsystgrlrd lptasypgtl enpnlkpsft
      721 nsfeygfemk lfkgrfgidf syyenefgpq iytqpfssss gydgirlngr tterrgmdfs
      781 inampvktdn fnwsmivnfd kskeylislp plpdgtpqen egrtrvgali gdywysewer
      841 tpdgqliiks nglpkitdfp vnqgntqpdf tasvnnslty knlslnflid grfggstydr
      901 yerdlwragg hpdaihpere lsniayvhgg daktmqidgv aivsgeatyd pdgnivtdtr
      961 ifepstykvd yqtwaggyka awqnvliekt faklrevslt ymlpskllek tfidsasisl
     1021 igrnllywtk ddtfgdldty tvstgdtnlq lpsqrsygfn lnfqf
//
LOCUS       WP_103441884            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103441884
VERSION     WP_103441884.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109600
     Region          23..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikklllffv lvlgtyplla qsktvtgtvt datdgsplpg vnvlvqgttt gsqtdfdgnf
       61 sieaasgnvl vfsflgmksq svtvgasnti nvsmqedaeq lgevvvtalg ikreektlty
      121 aqqtvradel tatrdpnfmn sisgkaagve ikksssgagg stkivlrgnk slsgdssplf
      181 vidgipmann kggqpgmwgg vdagdglsai npddiesisi lkgsnaavly gsqgangvvv
      241 ittkqgtsgk ttvslnsgyt fehfqelpdl qfkygaigna keswsttagd yaseyveeff
      301 qtghnfnnsv tisggtdktt ayfsyanita sgitpknkyq knnftfkqst kmfndkvtvt
      361 ssvimaleet knrlpagyyl npltglymfp rnrnfydfqn nyetfdtdrn lysqnwfvvd
      421 hhqsnpfwii nkepktdenk rvigslnvey eiteklklqv rgnydysvke feqqhaatsn
      481 stnvhpkgaw dyrkyddqlv ytdailsydt dlsdsfslng vlgasyqktv ygdgvsvgtg
      541 tvgllypnef kfqnlptnvq vnstydgsvi kqgafanlqf gykdmlfldl sgrndwastl
      601 altgndsyfy psvgvtalls emftmpevvs fgklrasytq vgnevpfnri npqnrissng
      661 gvdrntvkpf fdakpeiits lefgadwrff qnrlgldfty ysltstdqfi evpllqsese
      721 ggfttkfina geitnkgvei tlsatpvkte dlqwvtafnf tkntneivdi gpdddkvinl
      781 gssegyqskl veggafndly vlkflrdaqg rilfdagkpl rtpttelmgn ldpdwtlgwn
      841 nnisykrfnl gmqingkfgg kvfsqtesml dgagvsqrta dardaggvtv ngvdqtsgaa
      901 ittvaaetwf raigdrngvg eayvydrtni rlsqlslgyn idvsklglpi saaslsfign
      961 nlffiskdap fdpelamstn qnaqgldnfn lpstgtygfn lkvtf
//
LOCUS       WP_103442256             366 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Arenibacter].
ACCESSION   WP_103442256
VERSION     WP_103442256.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39693
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigilketl dgerrvaitp niakqliasg feiiaeegag eyssfkdsdy tnvqvavekr
       61 avvfheaevl lkinpfdeed lklvdegqil isklyhksnp eliqaiakkg vsafsmdaip
      121 risraqdmdv lssqnnlagy kavilgafem tkifplmmts agtiaparvl iygigvaglq
      181 aiatakrlga iveatdirse tkeqaeslga kfilvdnege eseggyakea sadyqkrqke
      241 avnkslflad lvittanipg rkapilitee qvmqmkngav iidlaaaqgg ncevsqinkt
      301 iirngvkvig tsidprsvst nasdlyakni ynyiihlteg gnfkwdlkee itdetlivqn
      361 gtirkn
//
LOCUS       WP_103442326            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103442326
VERSION     WP_103442326.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117784
     Region          24..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkplicllt lilsivhlaq aqnitvqgtv fddngvplpg asvvvkgttt gtqsdfdgnf
       61 yidikgpesi lavsylgfkp qeilvgnqtq vnitlapdat qlddvvligy qkvfkrdvts
      121 avssiksddi egipvmnvag liatqatgiq svnmtgapag rgaliirgnt siggdidadl
      181 ayssplyvid gvqtsledla gygvsnvdfl aslnpndias idvlkdasaa aiygsrgang
      241 viiietkkga aldkpefsfs tslglqpkpn lvpilvggae rstkmemiqr wwhtdelqng
      301 qtpmvlsdsl npsfnnnvdy qglfyktgid qqydfsvrgg sektnyrmsl gydnqegvik
      361 gtgvdrvtfs snlnftagek frnqlitrft htdlqtgqgn pyqgsfnlns slpvdpaglq
      421 sslfyltder rqslsgeleg klnedktvnf tisnfatydl lkglslnsql sfvydsnkkn
      481 fyepstirte rdgfasyaly nrknltaety lslfknigan ndhevtgvlg nridynkyed
      541 maltafgfgs daiqtinnry tqdqiggytd isanalvsyf grvsykfknr ymvggnfsid
      601 gssrfgkdvr wakfpsfnag wvisdepflk phissfidyl kvrgswging kqfpenylrf
      661 gkynlgyggn vhwanqmgvs syggitgvip nydqignasl sweetkqwni gfdldmfnrr
      721 vslafdaynk stdklffdva fpaysgynsa ptnvagvlny gwesmvryhv fprtndlrle
      781 lsvgfaqnkn yisklpngnq dyiggdygyv vgrpinlykm findyiiddl dqlpvnpftg
      841 eplkgksawa nirpgfpiwq dlngdyllne ehdlklttdy spipditgsf ninlqykkwy
      901 fqaysqfsfg adikntvlns ymdsydrggd nwarrgladl seytfwqqpg dgaagvdfpa
      961 lypqsptlga fygfrdsqtl wiesgdywkv nnasigytfd qndnfmknig lsrlriygam
     1021 lnpyqwqrsk kvvdasmvda kghtygngyp qartitigid tkf
//
LOCUS       WP_103448295             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas putida].
ACCESSION   WP_103448295
VERSION     WP_103448295.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38817
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqrgag lnasipdsay eavgaslgsa
       61 adaygaqlvl kvvapndqel alinsgsllv gmlnpfnsel igkmaergvn afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvqengv iivgptnlpa qvgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_103455558             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas stutzeri].
ACCESSION   WP_103455558
VERSION     WP_103455558.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38830
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkligqg hrvtlqsgag llssvpdsay eavgatigda
       61 aaafaaelvl kvnapddael aqmqsgsvll gmlnpfdnec iarmaargit afameaaprt
      121 sraqsldvls sqaniagyka vlvgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhqra lqsdivitta lipgrkaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvaadasaly arnlldflkl vidkdgqfql nleddivaac
      361 licrdgqvvr tng
//
LOCUS       WP_103470654             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas bestiarum].
ACCESSION   WP_103470654
VERSION     WP_103470654.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas bestiarum
  ORGANISM  Aeromonas bestiarum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas bestiarum"
                     /db_xref="taxon:105751"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53226
     Region          25..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tclgasgwaq aeeaaptgki earselfakd hadqfsswkg
       61 tseskertda laddpqmvvl wagypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvinekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eeyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfdqtcrnch tqskemlqgi vqqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaemk diqqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llaakgishe iaipdisske kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_103474276            1133 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103474276
VERSION     WP_103474276.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1133)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1133)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1133)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1133
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122990
     Region          35..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntylknkiq rlgqlfllml vvgttsvmaq saqhtvsgnl tssedgmplp gvsivlkgtt
       61 qgvssdfdgn ysinvpngng vlvftyigfe aqeaavngrt sinivmdpsa ealdevvvta
      121 lgikradksl gysvenvgge eltrvaqenv lnslsgkvag vtlnstggtg ssvsmvirga
      181 islssdnqpl fvvdgvpian svnnvggfgs dnrvdygnai sdldpesien vsilkgpsaa
      241 alygsragng vvlittkkan ekekmkvsft sntvfdvpyk yleqqtrfas gyfsfspesq
      301 ggsnimppva lsggnsgpel drgyfavqwn apldangtpi ptelksypnn iknfvqtgit
      361 ttnsltvtns tkavnyrmgv tnmentglvp nsdvnrnsfs lsassnlndk leistnvnvv
      421 hsfadnrpas nrganplqwa yampanidil kikdydlpgt dvlsvsedyn npyflanein
      481 nsfsryrifg nmaldwkisp sfnirtsynl nssnetqetk mspgysaesn ngtygisktd
      541 gvetnvdlla tfkkelgdfd msisgggnlm yqkgsgisns aasrvglivp dlftikniap
      601 talvyssyls erainsvygl anfgfkdmly ldvtarndws stlpidnrsy fypsaslsfl
      661 vselvdipkv dlfklrggwa rvgndtspyq lgayynnagq wnnailysas gglstptlep
      721 eeatskefgv dltmfnnrfr fegtyytven knqivpsvpi pgssgyssvs inagvleskg
      781 yelslgftpi rtenwnwdln lnyttnesqi kaladgvdyi efwsenksvs rgyvanaatg
      841 edglvgnlys pkikrvtdts spyfgypllg egedaewlae dervkvgnyn pdfvmglqss
      901 fsyknfslnm tfdwrsggqy msqtsrymte dgysqqlldn linpgigqtg pelkqwvldn
      961 adllifgenf isiggppgdg gfpealggsv vydgvfnagv vgfhdengnf ilenenlgld
     1021 gtnfipfsva nawdfgtphm fdadyiklre islgydlprk fveragldnv nvsvysrnim
     1081 lwtkdsafgv dperayqaes gqdkrgtqfk qgierynvdp wvvpvgfkig itf
//
LOCUS       WP_103474413            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103474413
VERSION     WP_103474413.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113961
     Region          25..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklngilt lflalivqls faqektisgt vtdqdglplp gvnilvegtt tgtqsdfdgl
       61 ytinasvgei lvfsyigqsn akmtigasnt invqmeedaq aleevvvtal gikrnprslg
      121 ysvksveaea itdnsepdli kslngkvpgv nvnvstgvag aankisirgt tsfqggnqpl
      181 fvvdgtpysn dqitttsqit ggggyesgis sldpndianv evlkgavaaa lygsravngv
      241 iiittkagks gglsnkkfev slntgvyfek ianlpeyqnt ygngtnfnyn nangswgarf
      301 dsretiptwa nllnafpdqf gptvpyvaqp nnvkdlfktg fvadnsvnis sakensnfsl
      361 tisnidqqgy ipfnsykrtn isaggnfkld nglkvganls ysdsyqvgpf lgenqftgaa
      421 ssfartlvlg rtwdlslpye dangapvipn ggwdhplwsw ehnqirtgvn rtvanvnfay
      481 dfnehinary qlginkydla rieitdkgsr gasgtgsvvt ddygseeies tfvlnfnydl
      541 aedlnmnflv gnnvnqissh rvgytgtnli adniftvnnt anvvsdvdet trkrivgvfa
      601 dlglgykdfl ylnatarndw sstlpqsdns flypsvstsf iftealgisn dilsygkirg
      661 gwanvsrdad pyqinkiftv gtvysgqpsv fvpttlgnpn lspenteefe vgidlelfnk
      721 raivdftwyq ktttdlisev nvptssgyts lltnigemen kgievgltli pvrtdnfkws
      781 tftsftknkn vvnkliegld rfpidvnqia fvdegeafgv fygtafmrdd egnylieqse
      841 ggilqaldnq vvgdpnpdfk igftntfkyk tlslqaqldw keggdisssg iaallgrgvt
      901 kdtedrertf ilpgfygnpt tgepildgsg nkipnttqmt mnnlyfsptn sntfginsvd
      961 eatiydgtvf rlreialaye vpkkfldktf iggmtfsvvg nnlwyfapnv pkytnfdpdv
     1021 taygsgnlqg ietqsapssk rfgfklnvtf
//
LOCUS       WP_103474707            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103474707
VERSION     WP_103474707.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115932
     Region          35..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlikkvrc ralllltflc tllsmsaygq dgfavsgtvv defgvplpga siiekgttng
       61 vvsdfdgnfs fevasqnatl tigyigfeeq qipikgiaqi nvtmqstast ldevvlvgyg
      121 avkkkdltga isqvdaaals dqstnsvtdv lrgnvaglsi glsaspkgts qirirgnnsl
      181 tagssplivv dgmiyngdls diapsdidkl dvmkdassaa vygargasgv ilvttkrgts
      241 dkptinints vgmasdayee rpydaqgyvn wrtevfksin pqntidnpgr yndpnnlpsg
      301 vtldqwlayd gsagdptraw lnrigfqdve ienylagnsi nwydrimqkg frndintsis
      361 grngglnyyw sigrtsnegi ingekfealr srlnldakit dwltigmntq fakrnegfia
      421 adrgqierss pwgsefddeg nirlspqddn gagavnafla qkfndridld htfnsrvyak
      481 lklplgfsye vgytnrlefr eyynhasaas pqnvvgsaer qvtkinewql dnilrwdkti
      541 dkhsfnlmfl vygekyqsyl trarantfep sdalgysale lgtvqtvdse detstgdavm
      601 trlnynydsr ylltmtmrrd gysafgtnnk rayfpsiaga wtisnesffn sefvnflklr
      661 lsygengnrd igrftalsrl gankylnvda ggniitvptf dngtqentel rwertkatnl
      721 gldfslangv vegsieayqn itndlivtre lpniigfnnv ttnlgeienk gleftlatqn
      781 ynrenfqwnt sfnfslnrne irklygdlde ngkeldditn qrfigqatdv iwgqeaigiw
      841 qtneatqaae fgvfpgdwki ndvdnsgdft vddnvfqghr sprfswamsn rfsllknfdf
      901 sfevysnwgq krvfneaknr ngfidrtnsi qtpfwtpdnp indyarlfss dgssnfaiwr
      961 dasfirlsni tiayrfpkpl leklslqslr lyanarnvav yaphwdfydp eptnidgrns
     1021 ngstdpslpt prfftfgidl sl
//
LOCUS       WP_103474699            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103474699
VERSION     WP_103474699.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118973
     Region          46..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrktkllg llfslgivqi lfanmlspni egnrkpsili gtnvqqqitg tvtdedgvpl
       61 sgasvmvkgt tngvvadfdg nftidvdsgs ilvvsyvgfe tkeitiglqn klnivliagn
      121 aleevvvtal girkekrrvg yatqevnges lqkaiapnvv esltgkisgv tvtsngsdff
      181 sdpqiylrge kplivvdgvp qpnsdfwnla sddienitvl kgaaasalyg slgangaiqi
      241 tmksgkgvdg tvisfnsstt fqggflriph gqtqygpgnt gryefgtgaa ggggvndfdy
      301 svwgpkfdgr lvkqfdspid pvtgeriptp wisrgednlk nfmevgmvts nnvtvqsssd
      361 kgsfvisnty kyakastpgq rldintfrlr gnlilsdavd idgslqynyq ysdnrirgty
      421 gptspiylls iwgganfdvr nfdgdniwlp gkegikqnfv enwrynnpyi lshywkkpwt
      481 kndiltylka nfklsdkvsa svrstlnsys ltdneeiskd iynydipdrg grfrynatry
      541 fenntdflls ynesffndei qlngtlganq ryvrlerena sttqliipei ftlnnsvdqv
      601 tpssskrykg vysaysaldf syknqlffgm tgrvdksssl peandtffyp siylsavvsd
      661 minlpepisy lklrtayanv ggdqignssd plddtynavs sydtgrnrnf ptasfpgtld
      721 npnirpsftn sfeygfemkl fkgrfgidfs yyenefgpqi ftqpfssasg ydgirlngrt
      781 terrgmdfsi natpvrtdnf nwsmivnfdk nkeylislpp lpdgtpqene grtkvgalig
      841 dywysewers pdgqliiqss gtpkvtdfpv nqgntqadft asvnnsltyk nlslnflidg
      901 rfggttydry erdlwraggh pdaihperel sniayvnggd aktmqiagva ivsgeatydp
      961 dgnivtdtrv fepsnykvdy qtwaggykaa wqnvliektf aklrevslty mlpsklldkt
     1021 fvdsasisli grnllywtkd dtfgdldtyt vstgdtqlql psqrsygfnl nfqf
//
LOCUS       WP_103475560            1131 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103475560
VERSION     WP_103475560.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1131)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1131)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1131)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1131
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1131
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124070
     Region          27..1130
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkihfflm altllcfngv maqskaisgs vtdandgapl pgvsivvqgt tngtqtdfdg
       61 nftieastgd ilvfsyigmk tqsvtigvsn sinismqeda sqleevvvta lgikreeral
      121 gyavseikgd diaqvaqinp inamqgktag vqisttsggt fggtritirg nstfdqntqp
      181 ifvvdgvild ndisgqngad wgnqlknlnp ddfesfsilk gaaasalygs ralngvvivt
      241 tksgkkrkgl gvsvnqtvgv rtvydtpnfq nqygsgltag gfsfvtngpn trtrddahdt
      301 sqfftydlat glpsmafdsy eehaaswgpr fdgqeiidyd gsrstwsaqp nnykesfdtg
      361 firntnvaid ggsetssfrl sfsnfsesgv elrndfdkns lsfkgshdli kdkltvnavm
      421 hytrskaknp lqpggltswf hdgfprnydv nkwknnyldv dggvphpngd nynftrmsri
      481 wahaleddni rtegsfisni nlnykisdni tatldgninq ytynqetktf adnrdrlngs
      541 ysfgngekfq hsfsaklffd kqinddfrmd lllggelwts keqsqyantt ggfkirdfys
      601 lanskdalna gggigprkki nsvyaffnts ykrelyfsat arndwssalv ypngkgnnsy
      661 fypsaslgwv ssetfdlpdf isfaklrasy aivgndtdpy rlstgfvadn fsqnpdlnmf
      721 rfedntavsv nlkpekkysf etgldlrfwn nrigldvayy kdntknqiip lqvpsesgid
      781 nqlinagnlq nqgieaalnl kivdnpdfsw diganythnr dkiielapgi nefrlfgnpd
      841 dsnsatasya yvggnygdlv trrgydyydg ansanqgipv lanrngwsva ypigiqnkds
      901 lyvmgnmqad wyggmntsvr ykrlrlsaiv dakfggeiys adaryglhqg vlesslpnrd
      961 asqggitwts egqgqnffgk tyedgyipng vfpdgttvts gpsdnrsnvd vggltyqqay
     1021 dqglvepthw sgyvyrwtsa stgtpitgvy tsswvalrev tltydvpsei ldkllvksas
     1081 laltgrdlgf iynslpdnin ptlssnaaan plqqksspyi rsisfslkln f
//
LOCUS       WP_103475804             990 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103475804
VERSION     WP_103475804.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106329
     Region          26..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhklikrni llfflvapll llaqdvvkgk itdtglgdpl pgvnvvikgt ttgttsdfdg
       61 nyeisvdifp ttlvfsslgy apkempvtgp ttlnvalees atgleevvvt glatsvkrsn
      121 sansvasvsa deltgrtppq tldgalagkf agaqitaasg apgggmsvkl rgvtsingqg
      181 qplyiidgvy vnnnsvfagg lneisnaagg gasstdsqdn asnriadinp ddiqnieilk
      241 gasasaiygs raaagviiit tkkgkagktk infsqavgfn eavnllgqrn wtaalaesvy
      301 gegalytaae sagrlrdyeq eiygekgfit ntnlsisggs dktsffgsft nneedgivkr
      361 tgaskqslrl nvdhritddi klsvtgnyle ssadrgffnn dnsnttigvs llftrpwdyl
      421 lpdadgnypn hpanssnqih trdvltnnes vsrliaggsl dvnlfrnenq slkmilkagi
      481 dtytlkttvf fprelqfmsp avggldglss dgttqntdan fsaflvhnfs tdnelsfttq
      541 agvtneqfsq ntvrvtstgl iaseqnvdqa anvkvdqfrl eqedagffvq eevnfqdklv
      601 gtigirgdks snngdanklf yypkasaavn ihnfdfwnle qvnqikvraa ygeagnfapn
      661 galfttyins lidgnvgiit pttlgdpsiq perqkelelg ldagffnnkv sleltwynkk
      721 vedlilqadn epssgysfrw anagalenkg veiglnvnaf dtedfswdsg iswfknksei
      781 tkltvasfdt qgfgtglgtf rieegksatq ivgndengnv valgdaepdf qmsfnnnfky
      841 kdftlsflwh wkkggdnvnl srllsdfgnt sadydemsld psgtlnngdy rkdafgagfa
      901 gpfvedasyl klreiglyyn lpentlqklf kgnvsnvkig lsghniisif dynsydpevs
      961 nfgsgaagig ievapfpssk rfmfhlsigl
//
LOCUS       WP_103476209            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103476209
VERSION     WP_103476209.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109299
     Region          23..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikklllffv lvlgtyplla qsktvtgtvt datdgsplpg vnvlvqgttt gsqtdfdgny
       61 sieaasgnvl vfsflgmksq sltvgasntl nvsmledaeq lgevvvtalg ikreektlty
      121 aqqtvradel tatrdpnfmn sisgkaagve ikksssgagg stkivlrgnk slsgdssplf
      181 vidgipmann kggqpgmwgg vdagdglsai npddiesisi lkgsnaavly gsqgangvvv
      241 ittkqgtsgk ttvslnsgyt fehfqelpdl qfkygaigna keswsttpgd yaseyveeff
      301 qtghnfnnsv tisggtdktt ayfsyanisa sgitpknkyq knnftfkqst klfndkvtvt
      361 snvilaleet enrlpagyyl npltglymfp rnrnfyefqn nyetfdtdrn lwaqnwfvvd
      421 hhqsnpfwii nkepktdenk rvigslniay diteklklqv rgnydyaike feqqhaatsn
      481 stnvhpkgaw dyrkyddelv ytdailsydt alsddfslna vlggsyqktv ygdgvsvgtg
      541 tvgllypnef nfqnlptnvq vsstydgsvi kqgafanfqf gykdmlyldl sgrndwastl
      601 altgndsyfy psvgvtalls emftmpeavs fgklrasytq vgnevpfnri npqnsvtgsg
      661 gvnrntvkpf ldakpeiits lefgadwrff qnrlgldfty ysltstdqfi nvpllssese
      721 ggfttkfina geitnkgvei tlsatpvkte dlqwvtafnf tkntneivdi gpdddkiinl
      781 gssegytskl veggafndvy vlkflkddqg rilfdagkpl rtatselign ldpewtlgwn
      841 nnisfkrfnl gmqingkfgg kvfsqtesml dgagvsqrsa dardaggvvv ngvdqtsgaa
      901 ittvdaetwf raigdrngig eayiydrtnv rlsqlslgyn idvsnlglpi saasisfign
      961 nlffiskeap fdpelamstn qnaqgldnfn lpstgtygfn lkvtf
//
LOCUS       WP_103476411            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103476411
VERSION     WP_103476411.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119027
     Region          61..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtgfkklf sllsiflkeg mplrvsilal mlcsagsyat svdnyefetk vyedlsqtvn
       61 isgtildneg nplpgasive kgttngtqad fdgnfsitvk dqnavlvvsy igfstqdvvi
      121 ngrsqleivl qedsakldev vvvgygtarr kdisgavstv rledspials pntnalqvlr
      181 gnvsgvnvgv qnspgttpgi lvrgqnsing nndplivldg iiylgsmtdi ntddistidv
      241 lkdasaaavy gsraangvvv ittkkgksdk pmityttsvg vntwqnkfdm mnrerwtqky
      301 iaqtpsidsp eqiifdaaya ttlweqkevd tkwmdlisrn gfnqnhqiav sgqsnrinyy
      361 fsggytnneg aivgddyqrv sirtkldadv tdwlkvgidg tynnndysgv ratlgnnvyq
      421 qqpwaypyry egmpvnpgan tgtllerypt gqsipnplwg tdgsikdvdd rnfyrlstya
      481 likvpqidgl tyrfnfsins nnnirdrfvy edyyvgeats spyldryspg elakrlsqan
      541 gynnrtnsyt yvmdhilnyk kvlgdhylda tlvatrdysy sklvsidgsd yssngntllg
      601 idgihkaavq ksnldveera nvgyvgrlgy aykdkyhlta tmrrdgasvf gedqkwgdfq
      661 slgvawtase edfisgsekl nylkikasyg kngnqgldpy qtlarvasgn dggiryefgd
      721 apstilygvd qtnlgspslg wetttafngg fqsiwfnnrv ffdldfyfse tsdqifsrqi
      781 pimtgfssil sslgqvdnkg ieislntvnv ssenfkwssg ltywknrnki vslygddvdg
      841 dgkedddian slfigeslqs iygydyigvv qeddteyien vgaepgdamf rdisgpdgvp
      901 dgiisadydr eilgnrkenf rlglsntfey knfslyvmis gifgggkdnf ylrenelsns
      961 fkdryatnei dhdwwtpenk sekylraday snrylglqsr gfikiqdinl syklprevlg
     1021 siglnslely tsinnqftft nwfgggdpea girpddntpp vpttytmglk lsf
//
LOCUS       WP_103476487            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103476487
VERSION     WP_103476487.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115557
     Region          58..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklrrcrlf lfkkpesqkl kinlvlflfa laaitmearv ilepmvdkgl iegifqdqvi
       61 tgtildennr plpgatvlve gtvigttsdf dgnysisvpe natklaisyi gyetqivsin
      121 grsdidiqlq vtanaldevv vtalgiersk rslaysvskv ggdefteare tnianglagk
      181 vagvdvtrta sgpagtarvl irgnssltgn nqplyvidgi pidnsnrgsa gewggsdggd
      241 gigninpddi esmsvlkgns aaalygsqas ngvilittkr gktnqglqve vnsnyvlena
      301 inhldpqtqy gsgllgvkps tqteawaage fswgakldgs svvqfdgvsr pyaysgnnfd
      361 kfyrtgstst ntvslsggsa dlgyrfsast mdnesvmpns gmkrqtfsvn lhgkalndkl
      421 sfqtsaqyil qdvknraqla dspgnshysv wqlpvttnvl dlrgdpdrlg anpndatdly
      481 gstfgqkgye llpsssiwyq npywaayqqt dkdsknrvia saslqydind wvyvkgragi
      541 dqsdrisesi nptgtgynld ggmsqsqnky qqsnfdimlg srhefdngia ydflagankm
      601 rlqedgtsas gsnfalpffy sianginngg gssfskigsh svygqaeisy dnwlfltgsa
      661 rndwfsvmdg rdvfypsvgl savlsdvlnl pevidfvkvr tswaqvgsvg digayslnqn
      721 yglgraqlgi prgsisgssv rnanlspllv telelgfnvq flnnrlgvdf syydkktedd
      781 ilnagisyts gynstivnvg eltnkgvell ltgvpirten fswnvsfnms nntskvvslv
      841 dpdndeerfn iglsrarhaw vthiegkpfg qitgsqflrg angeltldan glpqvdevag
      901 tvafgtgvhp fvaglqnsfr ykdfafsflv dmkdgavghs gtnaqlyrrg vhkntlvgre
      961 tglgvipasg isayyekiyn diaeefiyda gfvklreitl gynvpskyla ktfiskanls
     1021 lvgrnlwlih snvdnidpes synagnaqgl dffampqtss fgfnvnltf
//
LOCUS       WP_103476681            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103476681
VERSION     WP_103476681.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111869
     Region          21..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnklililav fgtiitteaq knisgqvlek dtntpllgvs vlvkgtktgt ttdfdgnytl
       61 anlsndaiie fsyigyttre itlgnqttin vfleinaeqi devvvtalni qrdkeslgys
      121 isqvsseevn varennvmns lsgkvsglqi tqsntgvdgs srillrgitt ingnnrplvv
      181 vdgipisngs ggagasggid sgdalsdinp ddvetisvlk gagaaaaygs lgmngvilit
      241 tksgtkkdgv gislnssfsf sdvaltpdfq neygagafgd fapinadgrp vldypfswsw
      301 gpkmegqayt nwlgrqdtys pnpnrdpyke fyqtgftvsn tlafegrsdk gsfrlsitde
      361 dgqgivsnnt ltkqtlslrg sskltdrfsv dgkmtyitsk vknrpqlaeg sgntalqlsl
      421 mprdirladv knntvnange eikwnldntf nnpfwalena gnvdekdhfq gfisanweid
      481 dkfnitaksg mdyiindfts ygatgaqavq nglgsynhdd sksniwnsdi lgtystnisd
      541 fnvtlslgan yrneyssykn isgndakvph fyrisnykns fssegiseka iysyyglgqf
      601 syggflyfda tlrndnssal pqannsywyh senmsllftk llginsnils qgklrgsfak
      661 vgndtspyrt qavynvdqtv tlpytvasis gslpsfdlrp etsesweiga dlgflknriq
      721 ldvtyyktnt tdqimavpis gataysskvi nageienkgi eaqlnlipfd senfswdlgf
      781 nftksnskvv tlneglesis lgslwtasve arpgqefgti ygndflrdnf grkiigndgl
      841 akrgervalg ninpdwyggf tnkirfknft lsslisaqvg geyysygrgy rlffgtdars
      901 lvgrengiie egineftgfe ndnstsallk qftdifsnev atdiildatn vklrevaltf
      961 dfpktmlrdt fiqsaslsav grnllfiyna sgdidpeaty ssgpastafe hsslpstrsy
     1021 gvnlkinf
//
LOCUS       WP_103476926            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103476926
VERSION     WP_103476926.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111183
     Region          24..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkllksll lfgtfmcfgi asaqevsgtv sdatgplpga svvvkgttng aqtdfdgnfi
       61 isdvdanstl vfsyigyktq evvvgnqttm nismeedaea laevviigyg tttvkdatga
      121 vsavtskdfn ggvisspeql iqgktagvqi sqgsgepgsg vsirirgtss vrsnndplfv
      181 vdgvplpsgg sssegtdigv gsssarnpls flnpndiesm silkdassta iygsrgangv
      241 viittksgkg gaqggtwefs sdlsfsspan efdllnrsef isavsafggn atdlgndtdw
      301 qslvtrnsss tnnnlaysqn ygsgnvratf nygkqfgivp kssqervtgr inlsqrvfnd
      361 klkldlqsti srvndeappl sgsagstgdm lgsaysanpt wpanstfnpg drinslnlle
      421 nwqsltytdr flinfsasyd ivedltakvt vgydksestr eaelgsksfn vgrgaggngr
      481 gtlndlnlen rlieltlnyk kdfgnsvlea lggfsyqdfn tegrnvegwg ygttnlnnma
      541 rdltnsanki eslitgsyqq ygyasggdad ifvnrlfpdp isdrlgdvsi pvksiftntf
      601 dntdelqsff aranysiask ylftatvrad gssrfgennr ygifpsgafa wkineedfmg
      661 damstlklrl sygitgnqdg lgygrfarre ryststngdp nisdgggvnv pgittvefan
      721 pdlkweettq ynvgldfgfa ndrfsgsidv yrketrdlll nieaaqpspq ptffqnldai
      781 vlnegaelsl nydilqgddf gwtagfnvsy nkneitdfdg eiaagtirga glsnafaqrl
      841 asgqplysfy lrkftgfdan gnpvheggvd nqqflgksal pditggfsts anyknwsasm
      901 yfngqfgnyi ynntanafft ggaigsgnnv tqnvvelagq esrfaeasvs trflekgdfv
      961 rlqtasisyd vplseglfkt mrlsltgqnl fvitdysgld pevsvapasa allnglpiag
     1021 idysafprpr tftlgfnvtf
//
LOCUS       WP_103477427             798 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103477427
VERSION     WP_103477427.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..798
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=87654
     Region          9..797
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlnlwvqsr aangvilitt kkgkegkltv aydfysgvqn atrltdyvtn sadmmelynl
       61 aiqnedptas pfftsaqise frtgtdpyiy pntdwndlly rtaqinshnv rigggnestr
      121 ysfsvgyldq dgvllgtsaq qynvrfnlds kvsekfnysv kisgrhddvy espmgsgtlt
      181 gwvnrakpyy talledgryg dtwigsasqn alaaaqngkn higednivln lsgeyeileg
      241 fkyrgtvgvs krnqfqkifr peiftydpkt fearplgfgg salsadnral qdtdltfist
      301 lsydktfaen hnigllggfq qetskfdylr gtkagipsna lqeinagsid ptaegylvef
      361 glqsffgrat ynykekylle anfrydgssn fgpgnkwgff psvsagwnis eesflrdsni
      421 vnslklrgsw gqlgnqaidp nqysatyalg qnysyggslv ggaaqtslpn tevtwetstq
      481 tdigvdllaf ggklglvvdy fhkltddilr pvsissvigg lspptvnlas vrnsgfefal
      541 thkntigdfn ygvgvnltti dnevtkipap aiggytriae gspidefyli kmigifqnea
      601 evtahgaqpt akpgdvkfed fddngiidag drqavgssip kltygvtlda gyngfdfsal
      661 fqgvegvdai teheqkpffn gagiptfwqd nawtaenpnn syprltrssn ynvnawqdss
      721 flledasflr ikniqlgysf pdqlleklsl drlrvyvnaq npyvktdyrg ldpeksvtag
      781 rgsytnvsiy slglnisl
//
LOCUS       WP_103477508            1130 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103477508
VERSION     WP_103477508.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1130
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123524
     Region          25..1126
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkfhyylm laaflvvqgv vaqnktvsgt vkddigtplp gvnvvekgtv ngastdfdgn
       61 ysinvsnsat lvfsslgftt kemavsgqst invsleedse qlgevvvtal gikretkaig
      121 yamtevqgee larinvvnpv qalqgkapgv sigasdgglf gnskiqirgv stlnssnnqp
      181 ifiidgvile ngtsgasadw ngssndygni lknlnpddyk tvsilkgaaa talygsrgin
      241 gvvlittkdg sgtrgigvsv rqsvgfdivy kgpalqneyg pgtlagyvdy gnqdssdnyy
      301 nwdtqqfsyn aagqpsminh aggglgygpk fdgrliedyd gnmvpyeaqk snmldayntg
      361 vntntsvals ggndkgnfyl sdsyndrtgt lpnnsfkrna lmfrgsynla pwlrasatvs
      421 ftesnshnpr ndisqgffdg tfernynttk ykqqqfwqap hggvpnsnfg ddftnvpnrg
      481 lwfayennnn ynketvvrpi vslaadvtdw ltitaegnmn hytteyenke lgsgfanegg
      541 yyelrhnkdv sktgklifnf nkditpelsa nlllggeiwd heqsytrawt dgglivpgrf
      601 yignslrtqr geggisdtkq lnsayflahl eykdqlfldv tgrndwssal vytdgtgnns
      661 yfypsvsssw vfseaigtsn wftfgklras waqvgsdtsp ytinrgygqg nidnggnfvy
      721 tntvnttlvd rsikpelkds yeigadvrff nnrlgidvay ydetiseqig nvplpsesgy
      781 nnlltnigtl tntglevsvt gtpiksnnfs wnttfnywdn ttkisevhpd fgeykslggd
      841 igygnfrvgs vafeggeygv lysdsapkkf estdpnhpnn gknqliwvds rrgayyersg
      901 vpekvgkaqa dfegswnnef nignfnmsvl ldarygghma syssrygtsy gyterslrgr
      961 dpehgglswa sgyddvqgtq fsdgvipdgv faegqmvtap sgtsvdvggm tyqeafdagh
     1021 vepthasyyn yrrnswgngv vnddwfsevk yialrnislg ynlpkmaask mgarnvylgi
     1081 narnvvylyn slpndinpes frgttssdsf rersfspyma sytfsiaidf
//
LOCUS       WP_103477510            1108 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103477510
VERSION     WP_103477510.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1108
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121117
     Region          25..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkfhyyll lsafllvqgm taqtktvsgt vsddlgtplp gvnvvekgtt ngtstdfdgn
       61 fsikvsnnat lvlsslgftk kevavgaqts ikvvlaedae qlgevvvtgl gitrekkslg
      121 yatatisaea ltetatpnfa talygkapgv sinttpggst sasnitirgv asitgrsqpl
      181 iildgvpird gevsnnnywg dqrlrgngll dinpedidni silkgasaaa lygseavngv
      241 ilittksgkn skkgmkvdls ssysfdkvay lpryqnvrgp gaplnvsngg qdaegfiyhd
      301 vdgngtaetr gvlgysinfg pkfdgkptig wdgivrpyea qqdnysglfn tahntsvnms
      361 itnvtdnsnl rfsytrqdnq gislgaeekk nvfnlnttfk wakdfstdvi vnyvnqsvfn
      421 rpysvdrltn nfggmmtrwd hgdwylnryk tskgyryvqg tdqsltpeen iiypgfrgdi
      481 gdfiwrvken mleeqsnrvi gtitntwdvt kglnlrgris sdftnrktea sssterplaf
      541 gnsggfsmsn dnfnvlygel llryetpitt dltlammagy natkqnesnl srgtngglsv
      601 enwfdisasv ntpnsgssrs sivkdailgt mnldykgyfy vegtirkdkt stmnpnnnsf
      661 vypsvnssfv lseafdlplf mnyfkirgsw givgnypdiy ganiaynqnt lgsqggnpvl
      721 yttipssfgn dgirpeekhe yefgmelkff qgrlgldasy ynaqvvdqil pltlpsssga
      781 nsvltnigtl rnkgyelgls gtpvdtgsfr wdiivnvakn enkveklapg ldellhadyd
      841 gnaaqlkslv gqpmgdlyah pvatdsqgrr ivdpnglykv dadnmekfgn ampkwtggvm
      901 nsfsyknitl dalvdgrigg hvmptalnwm isrglteesl nymdtehggl syyedvsgtr
      961 iqttpsatag pggevvyhdg illegvtndg qpndqiassa dyywtvynwg gpqyspntry
     1021 elyikentyf kmrelsigyk mptkvlekig lsklqfsvfg rnlfylyrti kdmdgeqtta
     1081 gsrwfqnvnn vgtnpstrsf glmvrasl
//
LOCUS       WP_103477698            1122 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103477698
VERSION     WP_103477698.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1122
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122271
     Region          67..1121
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlinvrsr rscppknnlk ikltillfyg alfnisahvy ensesilfgp eiisselgal
       61 eiaaqqieis gtvkdvdgev lpganivlkg tskgvvsdfd gnftiavpna qavlvfsyig
      121 metkevavgn qtslevlldy aaekmdevvv talgmkrekk algyavavve aetlnqqpnt
      181 nvlsglsgkm sgvqinemgg dinakmnvii rgqtsltsnn epllvidgsp vgntdamadi
      241 ssldiasvsv lkgasaaaly gsragngvil ittnsgegak kgigvsftqs ttlsvpynyf
      301 elqntfttgq kgqfnesswq ywygaragve avqwntdgqp qplvmydnsl rdffqtglst
      361 qtdasisgny drgsfnfsin hmksdgitpg melkrlgfsl atsykitdkv kfttnitisk
      421 ptsdnlpltn ngsddiymdi fanaphvnin dlkdyweveg sqqrragalp nnpwfsayer
      481 drtldqirgf gnvrldidll pgltamgrvs fsannekies iypwsydgfg ssavkpfgay
      541 eqtklderet nvdflfsydk kvgdfrinps vggnylnsrn tslygggdvl tlpalytlsn
      601 varpglgyns gvfekeiysl yglaslsfke mvyldltarn dwsstlpken rsyfypsasl
      661 smlisemtqm pswvslfklr tgwaevgkdt dpysinpiln qtfwgndiqy svpgslpnta
      721 lkpevatsye vgadlgffnn rivfegtwyk tqnrnqiigv ttspmsgfss atinagnven
      781 tgielalntv pvrtanlewn lgvnftkqes rlvelvegid rigvgnagsl tqqtfvggvi
      841 gdlystsvlr vesgeyegwp ilnnnggltf qkdnalkpkv gkstndftmg lntsvkyknf
      901 tlsanldwrq ggnfysetmk rtsrsgwvdk wqgdagtfsg ilgsnsfngd gtalaneiks
      961 nptkyqadnv wvggrdaqtg gfpyngfdng sfwpgvvdng dgtyaenfgg pgtvlfdayk
     1021 vvepggglwd vgssfmydls fvklrnitlt ydlpqkfask isaqrisfsv ftknimiwna
     1081 adigidpela yyqnggsydi gkekwnalpw vapvgftinl tf
//
LOCUS       WP_103477805             366 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Arenibacter].
ACCESSION   WP_103477805
VERSION     WP_103477805.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39704
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigilketl dgerrvaitp iiakkliasg fellveegag eyssfkdsdy knvavavekr
       61 avifheaevl lkinpfdeed lklvdegqil isklyhksnp eliqaiankg vtafsmdaip
      121 risraqdmdv lssqnnlagy kavilgafem tkifplmmts agtiaparvl iygigvaglq
      181 aiatakrlga iveatdirse tkeqaeslga kfisvdnege eseggyakea sadyakrqke
      241 avnkslfqad lvittanipg rkapilitee qvlhmkngav iidlaaaqgg ncevsqinkt
      301 ivkngvkvig tsidprsvst nasdlyakni ynyimhltle tnfkwdleee itdetlivqn
      361 gtirkn
//
LOCUS       WP_103478139            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Arenibacter].
ACCESSION   WP_103478139
VERSION     WP_103478139.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter
  ORGANISM  Arenibacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Arenibacter"
                     /db_xref="taxon:178469"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119140
     Region          25..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskltwila pimglfmsfs yaqektisgt vtdqmglvlp gvnivvegtt ngtqtdfdgn
       61 ytiqgsegqt llfsyigqms vskiiggsat idvvmeedaq tleevvvtal gisrdkkslg
      121 ystqevqged lntvksgnfv nalsgkasgi qikknnnlgg stnvvirgna sltgsnqalf
      181 vidgvpvnnt ntnskyqgea sgnyydygnt asdinpddie svnvlkgaaa salygsraan
      241 gvimittkkg kdtpgigvtv nsgitigsid kstfakyqkq ygagygayyd gpggywyeed
      301 itgdgnddqv avytedgsyg apfdpnllvy qwdsfdpdsp nyrtatpwvn akngpitffe
      361 tpvtttnsvs fsrayeddgs frlnytqfdq sgimpnssik khnfsmsgvf klterltvtg
      421 yanyintrah grnstgyndn qisnfkqwwq tnvdlkqqkd iyfdtkrnvt wnpatsdags
      481 apifwdnpyw sryenyqndg rnrfignvsl dykftdwlnf taraatdtyt eiqeerrang
      541 svptsfgipd sagnrgnvds gygrrnldvt etnydfmfnf qtdlsedlnl kgiigtnirr
      601 sdfqsiysat sgglsvprly slqnstgpla lpveraekig vdgiyasasl gyksilfvda
      661 tirrdhsstl pednssfyyp siatsfvftn llnadfltfg klranyaevg nsapfdflyd
      721 tynvnippga pstsvdnqkk npslkpekte sfevglemkf lrnrlsfdva yyktnsidqi
      781 fgvpvsratg feekilnage ienkgvelsi sgnpvrtdnf nwtvmvnwtk nknevvsled
      841 gietlqlgdf qggvtlnaev gkpygvlygt dytylngqrv vdpadgqfik tstsdqtigd
      901 tnpdwlmgis nkfnyknlsf sflidiqqgg sifsldqyyg ratglyeetv findlgnpvr
      961 nsladgggfi negvnpdgat ntarinanrf gafgyrrglp dkafvydasy vklrevafty
     1021 nlpsklltnt fltnaslsvi gsnlwiidkn iphedpeggl sagnlqgysv gslpttrdfg
     1081 vnlklqf
//
LOCUS       WP_103496302             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_103496302
VERSION     WP_103496302.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38734
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag lnasvvdsay eaagaaigna
       61 ndafgaelil kvvapsdsel tlikrgtvlv gmlnpfnnet laklaehgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag avaadasaly arnlldflkl vfnkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_103523670             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aquitalea
            palustris].
ACCESSION   WP_103523670
VERSION     WP_103523670.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea palustris
  ORGANISM  Aquitalea palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Aquitalea palustris"
                     /db_xref="taxon:2480983"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39017
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqiaipaerl agekrvaatp etvkkliamg htvvveqgag qfaaapdaay aelgasiaan
       61 raealaqadi vltvraldea giaelktgav ligqlapyqn ttfpqlaark vsafamellp
      121 rttraqsmdv lssqnniagy kavllathyy prfmpmlmta agtvkpakvl imgvgvaglq
      181 aiatakrlga vveatdvrps tkeqveslgg kfievpmtae ekaasdgvya kemsddykrr
      241 qaelvskhar aadiiittal ipgkkaptli sadivaamkp gsviidiaae aggncertqp
      301 gevvvtenhv tvvgqfnlpg elaadassly aknlltflsl mlskdgftln leddllaatl
      361 vthdgqvrfp aan
//
LOCUS       WP_103547312             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces populi].
ACCESSION   WP_103547312
VERSION     WP_103547312.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces populi
  ORGANISM  Streptomyces populi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces populi"
                     /db_xref="taxon:2058924"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53179
     Region          13..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpaqesahhp pqrigvvaes tpgetrvaat patvrqlvgl gyevvvesda gtasgftdga
       61 ygeagarigd awqtdvvlkv nspssseiar vpdgatligl ispaqradll aelasrpitv
      121 laldavpris raqsmdvlss maniagyrav veaahafgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvkslggeyl avdvaqeest dgyakatsad
      241 ydraaaelyh aqakdvdivi ttalipgrpa prlltaedva amkpgsvivd maaaqggnva
      301 gtvagrtvvt dnnvtiigyt dlasrlptqa sqlfgtnlvn llklltpgkd grlvvdfddv
      361 vqravtvvre geitwppppv avsaapqpap aaaaaqtekp keprltpavr faligagmla
      421 mfalvafapa qlaanftvft lavvigyyvi gkvhhalhtp lmsvtnaisg ivvigallqi
      481 ghesavvttl sfvailltsv nifggfavtr rmlsmfskg
//
LOCUS       WP_103663381             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium sp. CJ77].
ACCESSION   WP_103663381
VERSION     WP_103663381.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. CJ77
  ORGANISM  Microbacterium sp. CJ77
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Microbacterium sp. CJ77"
                     /db_xref="taxon:2079201"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52978
     Region          3..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msqigivaeg prekrvaatp atitklialg ydvvveagag aassfpdaay aasgatvvsa
       61 seawasmivl kvdaptpdev arladgatli allspalrsd lveslatrei taialdavpr
      121 israqsmdvl ssmanisgyr avieaanefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvasigge ylevvvpdea kevstdgyak attaaydrra
      241 aeiyseqaad vdiiittali pgraaprlit aadvarmkpg svivdmaaaq ggnvegsveg
      301 ervvtdngvv ilgftdlpgr lpqqasqlfa tnlvnlikll tpgkdgqlhl dfddvvqrtv
      361 tvvrrgevtw ppppvqvsaa pqktvaapsv aaelkkpmss rargwlvaag iavlfavcaf
      421 appplpqhfl vltlsvvvgf yvighvahal htplmsvtna isgiiivgam vqimapdltv
      481 qilaavgvll asinifggfa vtrrmlamfq kgqnr
//
LOCUS       WP_103627075             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_103627075
VERSION     WP_103627075.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53557
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdlqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_103663586             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Gracilimonas amylolytica].
ACCESSION   WP_103663586
VERSION     WP_103663586.1
KEYWORDS    RefSeq.
SOURCE      Gracilimonas amylolytica
  ORGANISM  Gracilimonas amylolytica
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Gracilimonas.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Gracilimonas amylolytica"
                     /db_xref="taxon:1749045"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40220
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mivgvlketa dferrvaltp eiseqlikkg levwvepgag tasnfpdqqy knagatiagg
       61 rneilskadi lltiqtpage elrqlkndav licflwalqh pelvdllkel gisalgmdav
      121 prisraqnmd alssmssiag ykaaliaane ldkylpmmmt aagtippaks lvlgagvagl
      181 qaiatlkrlg svveafdirp evkeqveslg akfvevelge eetqteggya keldeskqdl
      241 qrkvihehak ksdiivttal ipgrpapvli teamvkdmmp gsvivdiase nggncelteh
      301 gktvekygvn iigpnnlpsq lslhasklys knmyalldll iedgkpnfnf edeillktti
      361 thqgevispm lksg
//
LOCUS       WP_103664411            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gracilimonas
            amylolytica].
ACCESSION   WP_103664411
VERSION     WP_103664411.1
KEYWORDS    RefSeq.
SOURCE      Gracilimonas amylolytica
  ORGANISM  Gracilimonas amylolytica
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Gracilimonas.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Gracilimonas amylolytica"
                     /db_xref="taxon:1749045"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114867
     Region          27..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiqiphfit mivlfclpam afaqngtieg qvtdqsgeil igvnvtlrvd grtlgsstdi
       61 dgnyqitgvp agthevsarf vgfrtevvev tlqagqtlvq dfvlststln ldelvvtgtg
      121 gtvqrkslgh tissvefdgi envattsiqd altgkiagvn inaqsgaidq epkirirgts
      181 slsmtnqpli yvdgvrvngg ggfapgfgag glgspsglsn infdsierve ilkgpaaatl
      241 ygsqassgvi qiftkqgsqe sapqfdieyg ttlyqmpdrf rknagfaena teqqnisdil
      301 gldvdlyepf etpinlidly nigvgqevsa svqgggqsmt yfsnlrytft dgpfnpqpsd
      361 fnggevgeas dvykkiyftg nlnfmpsdkl tlraqtsytn sdisiyesgi tiytptstsr
      421 yakpervgqa sqydtfgipl fattregtyp tvtdltnqgr vvlkadyfpm eglsidasig
      481 ldykdqrsan ympfgynvdg vaptgdgqiq igtrqqmvks feskmnwikd inqdirstfv
      541 agfqayqetq ntasstgtgf sgpglevlga tasqtsdsyf qevvnagafl qeqidygewi
      601 yltaglrmda ssafgddfdy atypkfsasf ipatafnfei nnvssfrirg awgqsgqqpg
      661 afdrfttfvp vnsfegagvl pgnpgnqdlk pevatewevg felglfedri gveatywdri
      721 vkdalidrty apsggftsaq ltnagrlaan gweiglnsnv iqnqnltlni fanaaylsek
      781 veslggqppi kidasyirdr mfikegyapg syfgtmlpag iafpfdsnqd gvpdsqsele
      841 affanpidpg tfnsaimvag pngealpggs tyldhylgkp tpdwegsfgf tanikknvtv
      901 ssrfqyafgn yyhhnltdaf rrvngaigrn missatlesv lknpsstaqe ridaaqewvn
      961 nnvslspfdg lneiekadyi rwanlsisyr ipsdlvervg lnnasltlsg nnlalwskyg
     1021 gvdplatgea slgqgaslqe nfgggmdtyg tpllrtyalt lkfdf
//
LOCUS       WP_103665543            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gracilimonas
            amylolytica].
ACCESSION   WP_103665543
VERSION     WP_103665543.1
KEYWORDS    RefSeq.
SOURCE      Gracilimonas amylolytica
  ORGANISM  Gracilimonas amylolytica
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Gracilimonas.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Gracilimonas amylolytica"
                     /db_xref="taxon:1749045"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119576
     Region          35..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkkllissf mvlvsvsaaf aqtttvtgtv tdadtgepip qvaiyisdls tgaatnidge
       61 ytidgveygt ytfrvssvgy itierditvn annnsfdfel aqdiqlledv vvtafgvsre
      121 qkslgysvqd vnaedlarvd qnsvvgaltg kvagvqvvqs ptmggserir irgvnglsdg
      181 qplfvidgtp vdnssfevas ngssargrdl gnlasdidls svasvsvlkg aaasalygnr
      241 aangvilitt ksgqmgedqp vrvdytnsty fenvyilpnf qneyaggytq dflqytdpad
      301 gqtynglnya adeswgprmd gtqyrpwysw fdgdfdgdgv sdygktvpln pnpdnvrnfy
      361 dtgvriankl sisggsansa yraglnntnq sgvypnstld ktavtfngsl nhnnkltssv
      421 sfnyvntqgk grpatgysav qgnpaqnmsq wfqrqldmdk lktyrledgs iaswnirsnt
      481 nkrplywdsp yfsvyenvqq ddrdriygny nlsynvndnv eligklhlda ysftvedrig
      541 tggleedwyy iaqrsrrevn yeggakfnkd fedfsmsgyl ggniltqdys sviqqtvggl
      601 stpnffnida sinrpnvssy kqqkevrslf gtatvgyrdl ayidaslrnd wssalpsdnn
      661 sylyyglsgs lvftefdafs dqnilsfgki rasiaqvgnd ldpyrilqtf nsstpygsqp
      721 aqsipnvlsn pdlepaissd yelgldlrfl dgrvrtdvty ynsvreneil qldapgssgy
      781 satlvnagkf tttgwevalg ataieqrdlt vdmnlnwsks kgvvdelaeg idtrllesaf
      841 fgiqlfaveg eewgraitsg gyggtayhen gqpiinssgt sykleynkdl gnilpdwngg
      901 fnldvnyknf slgafvefqk ggqfysisrm fgaysglvee tvgnnalgnp qrdpvldsng
      961 nevistplnq aasnsggktl rgvdengnev aylvnaptyw lnmfynkeew ledasyvklr
     1021 elkltydlsa rtlerlpinr asvslvamnp lliyssvdgv dpsaiqnnan gfgfweggtl
     1081 pgtrsfgfnv nigf
//
LOCUS       WP_103668729             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudanabaena sp. BC1403].
ACCESSION   WP_103668729
VERSION     WP_103668729.1
KEYWORDS    RefSeq.
SOURCE      Pseudanabaena sp. BC1403
  ORGANISM  Pseudanabaena sp. BC1403
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Pseudanabaenales; Pseudanabaenaceae; Pseudanabaena.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Pseudanabaena sp. BC1403"
                     /db_xref="taxon:2043171"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40479
     Region          1..330
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikeie fgerrvalip evvsrlvkng levlieshag essffadaay eevgakiifd
       61 ksvlinesdi llkvgapree evsmfksgqi tigflnplgr pelirrlahq gvtamsmemi
      121 prssraqsmd alssqasiag ykavliaaaa lpkylpmltt aagtippakv vvlgagvagl
      181 qaiatarrlg aqveaydirp avceevqslg akfidvtlde dttadggyak eiseaakqha
      241 qvilakhike adivittaqv pgrkapvmvt damiahmkrg siivdmageq ggncegtiag
      301 kdvmchgami ispinlpssm pihasqkyak nllnllnhli kkgeldldfd ddiisstcit
      361 hageirnqrv kdalsqlava v
//
LOCUS       WP_103689265             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_103689265
VERSION     WP_103689265.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38856
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lrasvpdsay easgavigdt
       61 netyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivgqtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_103692277             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia gladioli].
ACCESSION   WP_103692277
VERSION     WP_103692277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia gladioli
  ORGANISM  Burkholderia gladioli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia gladioli"
                     /db_xref="taxon:28095"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38993
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,300,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetr anearvaatp etvkkyvaag hsvcvergag aaasfpdeay aaagamlger
       61 aaayaaeivl kvqapdsdel pqmkrgavlv gmldpfnaeq aarlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee reaaqgtggy arpmppswla
      241 rqaalvhera kqadivista lipgrpaptl iqadtvaamk pgavivdlaa grgpenadgr
      301 rggncpltva dqvvkvhgvt iaghtnlaaq vgadasalya rnladflkli vtkegalnid
      361 mnddivaatl lcrdgevvrk
//
LOCUS       WP_103696195             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_103696195
VERSION     WP_103696195.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38880
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lrasvpdsay eaagavisdt
       61 netyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adevvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_103702151             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia eburnea].
ACCESSION   WP_103702151
VERSION     WP_103702151.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia eburnea
  ORGANISM  Paraburkholderia eburnea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia eburnea"
                     /db_xref="taxon:1189126"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39563
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anesrvaatp etvkkyvaqg htvtiqsgag tgasfpdeay aavgaqiada
       61 aaafgaelvl kvqspsvsel afmkrgavla gmldpfntdn aqklaeaglt afaleaaprt
      121 traqsldvls sqaniagyka vlvaanlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaavgvggy arpmppswla
      241 rqsalvhera rqadivista lipgrdaptl lpsetvqamk pgsvvidlaa grgpiadqat
      301 grrggncplt vadqvvtqhg vqicgytnla smvaadassl yarnlldflk livtkegaln
      361 idladdivaa tllardgvvt rkt
//
LOCUS       WP_103705856             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia eburnea].
ACCESSION   WP_103705856
VERSION     WP_103705856.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia eburnea
  ORGANISM  Paraburkholderia eburnea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paraburkholderia eburnea"
                     /db_xref="taxon:1189126"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54490
     Region          3..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mamtiaipre ifpderrvaa tpesvahllk lgyvveveag ageqasymdd ayraagaciv
       61 ddalelwssa divlkvrpps ideaqhlkrg atligfiwpa qqdalldtla argatvlamd
      121 cvprisraqk ldalssmanm agyravieaa qyfgrvftgq itaagkmppa kvlvigagva
      181 glaaigaarg lgaivrafdt rpevgqqies mgaefltvei eeegggaggy akqmsakfie
      241 aemalfkaqa aevdiivtta lipgrpaprl ldaqtvaclr agsvivdlaa eqggnceltr
      301 agevvrahgv aivgytdlps rmanqssqly atnlrhllsd lttdkdgelk idmndvvqrg
      361 ttvmlngelc wpappvqtaa paasksearn sapplpagga aheeatavrr rgaggvlalv
      421 liaalllglg avappsfvah ftvfvlaifv gyqvvwnvtp alhtplmsvt naisgiivig
      481 allhpagtna lvsvlagval vvatiniagg flvtqrmlkm fqrt
//
LOCUS       WP_103711948             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium sp. V23].
ACCESSION   WP_103711948
VERSION     WP_103711948.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. V23
  ORGANISM  Methylobacterium sp. V23
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Methylobacterium sp. V23"
                     /db_xref="taxon:2044878"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39477
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd paeprvaavp etvkkfiglg advtvqsgag lkagvldvey eaagasivgs
       61 aadavssadl vlkvrrpspe eigllkrgas vvaimdpygh eaelgamaea gldtfamelm
      121 pritraqvmd vlssqanlag yravidgaae ygrampmmmt aagtvpaarv fvmgvgvagl
      181 qaiatarrmg avvtatdvrp atkeqveslg akfvavedee fkqaetsggy akemsaeykk
      241 kqadlvtthi akqdivitta lipgrpapql vseamvasmk pgsvlvdlav erggnvegak
      301 sgevvttekg vkivghlnvp grlaatassl yarnlyafve tlidkeaktl avkwddelvk
      361 atnltrdgqv shpsfqpks
//
LOCUS       WP_103719339             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Allobosea
            psychrotolerans].
ACCESSION   WP_103719339
VERSION     WP_103719339.1
KEYWORDS    RefSeq.
SOURCE      Allobosea psychrotolerans
  ORGANISM  Allobosea psychrotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Allobosea psychrotolerans"
                     /db_xref="taxon:1871628"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39159
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaetq gaetrvavtp etvrkfiglg aeivvekgag lasgindady eaagatiakn
       61 akealkgaai vlkvrrpaes eiaglpsgal vvgimdpygn eaavealaka kvaafamefm
      121 pritraqvmd vlssqanlag yravidgaae ygralpmmmt aagtvpaari fimgvgvagl
      181 qaiatarrlg aivtatdvrp atkeqveslg akflavedde fkqaqtaggy akemskeyqa
      241 kqaeltashi akqdivitta lipgrpapkl isaamvesmk agsvivdlav erggncelak
      301 pgevavtang vkivghlnvp grlaatssql yaknlfafve tlidksakal avnwddelvk
      361 ataltkdgav ihpnfvpka
//
LOCUS       WP_103725313             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            croceum].
ACCESSION   WP_103725313
VERSION     WP_103725313.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium croceum
  ORGANISM  Flavobacterium croceum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Flavobacterium croceum"
                     /db_xref="taxon:370975"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107716
     Region          27..976
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykkllf lllllpfgmy aqgnlegnvi dsktslplsg vnvkvqnvsn gtitdsegrf
       61 kltkikngdv isfssvgykk qtivfsnqgs vtikleeean tlqevvvqvg ygsvkkkdat
      121 gsvsvisakd fnkgaivtte nllngrvagv tinsgggapg tgstirvrgg sslfgsndpl
      181 ividglpien ntdknigsts ilasinpsti esisvlkdas ataiygsraa sgvilittkk
      241 gtkklavdyn fqygsgslvk kidvfnadqy rsliaqyrpl dvsklgnant dwqdeiyrrt
      301 dfvdnnisvr gnlfnaiptr ltvgntyqeg lrltnsfnrt taglalnptf fkdhlkvrln
      361 anytneknrf adgvegsair fdptqpvyds tsiyggffey ynhangeltt qtprnpvaql
      421 lqtydtgknn ryygnfeldy kfhflpalra vvnvgfdean gertklvgtn aataasnnni
      481 pygtneyses mrknkllday fvynkayndf nfdvtagysy qkwdsdyyys nnilnptytg
      541 ptkvvewdrv lisyfgrsni nfknkylltl taradksskf dssnrtgffp gaafawkmke
      601 dffknnntis dmklrlgvgt sgqqdvgnnn dyiqiynlgn pnsqyyfgss ataiavsakm
      661 ssglkwetty tynagidygl fnnrvtgsld vyykdsknli arvatadgsn fsntswqnig
      721 slsnrgvefn vnfeavkaen fnwnmnfnts ayqrkieelk kvsyirvgen lagtgtqgqa
      781 ymvgyapfsy lvykqlydna gkpiegayad lngdgvinas dkyiyrnadp kvtfgfasnm
      841 nyknldfsfn lrasvgnrvf nqvaaskaqy sqlstgnalg niptsvvdtn fnttsdvvls
      901 dlyvengsfl rmdnitlgyt fpkwlegkas lrlsagcqna flitkysgld peignngvds
      961 tiyprqrqll fgvnmkf
//
LOCUS       WP_103725470            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            croceum].
ACCESSION   WP_103725470
VERSION     WP_103725470.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium croceum
  ORGANISM  Flavobacterium croceum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Flavobacterium croceum"
                     /db_xref="taxon:370975"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117413
     Region          25..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklhvfla lfvalfvqls faqqrtvtgt vsddkgmpis ganvvvkgak sgvqtdldgk
       61 fsikaesdqt lvityvgfnk kevsassnnl kiklqsnave legvvvtaqg ikrekkslgy
      121 atqqitgndl nggatdgnva nllsgkaagv eirrnnnmgg stnvvirgsk sltgnnqalw
      181 vidgvpidns nsnftsqqqg gsgydygnta sdinqedies inilkgaaat alygsraang
      241 vvlvttkkgk qkadkgigvs vsssltvgtv dkstfakyqd kygagygpyy gdptgfldyf
      301 dvngdgiddl vaptyedasy gapfqgqmvy qwnaftpyss nfgkatpwra aengpitffk
      361 nsiitnnsvt lesatdksnl llsysnydek gilpnsglkk nqistrfsqk vtdkltvnsy
      421 asvtlqntig rnstgyndni mtnfrqwwqt nvdlkeledv yfnsggqnit wnwsdvsspd
      481 glvpifwdnp yftryknyss dnrnrligyt aatydinkwl natgrvsidt ykslqeerra
      541 igsiasgfgl spvdegsgyq rydqsfkein ydfmlnfnkk fgsdlslagv fgtnirrksv
      601 dnvlastigg lvvpelyals nsryelpfpi etkythgvng iyaqaslgik dtyfiegsir
      661 rdasstlpkg enayyypais gsvvlsnlik sdklnfaklr tnyaevgnda pplslintfq
      721 rntnfhgqpv ytlpnvnknp nlkpertksf evgleasmln krlgfdlsyy vnnsvdqivs
      781 gavssasgvt navvnggeiq nkgievqlta tplkardfqw dvtvnwsknk ntvislpggl
      841 enlqlgsfqg gitinatpge pygtikgtdy iyhangqpiv sqttgrylst stsdktigni
      901 tpdwvggirn kftyknislg flidmqkggd ifsldmyygl atglypetae gniretgvih
      961 pgvapdgtpn tvytiapdqy gnnygyrrep nksfiydasf vklreasity sfskkflges
     1021 fikdlklslv gtnlwiihkn lpyadpesgl tsgnlsrgys vgslpttrni glnlsfkf
//
LOCUS       WP_103754212             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_103754212
VERSION     WP_103754212.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38907
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lrasvpdsay eaagavigdt
       61 detyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaargit afaleaaprk
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmptswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_103755006             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_103755006
VERSION     WP_103755006.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53553
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfaphhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglk mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_103758684             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Mobiluncus
            mulieris].
ACCESSION   WP_103758684
VERSION     WP_103758684.1
KEYWORDS    RefSeq.
SOURCE      Mobiluncus mulieris
  ORGANISM  Mobiluncus mulieris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Mobiluncus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Mobiluncus mulieris"
                     /db_xref="taxon:2052"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53588
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkepd gqplvsatpd tvgklvklgy evvvetgaga tasypdqqyr eagaevvgpq
       61 evwqaeiits ldtppdskie qiregsvlia rlgvranpai aevfarrnvs aismdavpri
      121 traqsmdvls smaniagyra iieaanafgr lftgqvtaag kmppakvyvi gagvaglaai
      181 gtansmgavv qatdvraaaa eqvesmgatf vaipapaqes sdgyaremse dqakaalrly
      241 teqagaadiv vttaqipgrp apllltaeav agmkpgsviv dmaggncelt vpgqvittdn
      301 gvtiigytdl agrlpgqasq lygqnivnll klmtpgkdgq ivfnlndeiv rsitiahqkd
      361 vlwppppiav saapaggaga ggaggsgsas gagvpaslga svdiaapkgh aarnfwtgia
      421 ailgvaliai tphemlpyyi vlalaivagf yvitnvthsl htplmsetna isgiilvgai
      481 islaqstsiv vtvlaclail iasinifggf yvthrmlkmf qkgd
//
LOCUS       WP_103762391             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Roseovarius].
ACCESSION   WP_103762391
VERSION     WP_103762391.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius
  ORGANISM  Roseovarius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseovarius"
                     /db_xref="taxon:74030"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56011
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevm egearvamtp dsalqlqklg hecaietgag eragftdady keagveiiks
       61 paalwkacdi iakvrvptdt evkrltkgqt lisffnpggn eeqmkiaaek gatviamesv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvfldfee dqkdgsetgg yaapsspefq
      241 ekqlekfrem apdmdivitt alipnrpapv lwtkdmvemm kngsvivdla aerggncelt
      301 qkdekivtdn gvtivgytdf psrmatqsst lyatnirhmm tdltpekdgk vvhdmeddvi
      361 rgatvthgge itypppppkv saiaaapkke kpkeltpeek kaqevaafkk qtmnqvgllg
      421 vgaflvllvg tvapasfmqh fivfvlsvfi gfqviwgvah slhtplmavt naissiiilg
      481 almqigstsy litllaglgi fmaainifgg flvtrrmlam fqks
//
LOCUS       WP_103771857             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Citrobacter arsenatis].
ACCESSION   WP_103771857
VERSION     WP_103771857.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter arsenatis
  ORGANISM  Citrobacter arsenatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter arsenatis"
                     /db_xref="taxon:2546350"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53506
     Region          21..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mariksrvrr ffslllpllf isavhaeqtp vpaktvtvea knetfapqhp dqylswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntasad fakgkpeltl
      181 srpyaerame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmek
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegkiytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gateaemkpi ledirhaqwr wdlsiashgi hmhapeeglr mlgsamdkaa dartklvrll
      421 atkgitheip lpdistkeka qaaiglnmqq inaekqdfik tvipqwedqa rkngllsq
//
LOCUS       WP_103777768             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Citrobacter amalonaticus].
ACCESSION   WP_103777768
VERSION     WP_103777768.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter amalonaticus
  ORGANISM  Citrobacter amalonaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter amalonaticus"
                     /db_xref="taxon:35703"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53476
     Region          5..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 martkisarr ffsllmpflf istvyaeqtt apattvtvea knevfapqhp dqylswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc gdchntaspd fakgkpeltl
      181 srpyaerame aigkpfdkas rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmek
      241 yydtiafsdw tnslskapml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdsf sqtcanchtq dkaslqkvva erkqsihdlk ikvedqlvha hfeakaawda
      361 gateaemkpi lddirhaqwr wdlsiashgi hmhapeeglr mlgsamdkaa dartklvrll
      421 atkgitheip lpdistkeka qaaiglnvqq inaekqefik tvipqwedqa rkngllsq
//
LOCUS       WP_103778610             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. Ru71].
ACCESSION   WP_103778610
VERSION     WP_103778610.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. Ru71
  ORGANISM  Streptomyces sp. Ru71
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Streptomyces sp. Ru71"
                     /db_xref="taxon:2080746"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52996
     Region          13..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msaqepahhs sqrigvvaec lsgetrvaat patvrqllal gyrvvvepea gaasgfgdqa
       61 yldagaeige awdadvvlkv nspsdaeisr lrrgatvval lspahrpell raladagvts
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgavvr atdprpevad qvkslggeyl pvhvtqeast dgyakatsad
      241 ydraaaelyh eqakdvdivi ttalipgrpa prlltaedva vmkpgsvvvd maaaqggnve
      301 gtvpgravvt dngvtligyt dlasrlpaqa sqlfgtnlvn llklltpgkd grlvidfddv
      361 vqravtvvrd gdvtwppppv pvsaapaaqp tppeaepapa rakpagrfal iglgmlalfl
      421 lvafapaqla enftvfalav vigyyvigkv hhalhtplms vtnaisgivv vgallqtghe
      481 stlvtalsva ailltsvnif ggfavtrrml smfskg
//
LOCUS       WP_103787880            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103787880
VERSION     WP_103787880.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115130
     Region          35..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mssnnillkr iggkgvllll llnfcatilf aqnvvirgtv kgdvgeplag atvkqvgtnn
       61 vtvvtkngty elknvapgas lqvtfigykn evivlksgqt tanfvlrnni vtlkevtvnt
      121 glykrpvgnf tgsaksytge elkvvnpknv lqalsvvdps vritpnnqfg sdpnqlpnlq
      181 vrgannlplt tntsganpvs ngdfaasyls npnqpliimd gfettlqaly dmdisliani
      241 tvlkdaaatv aygskaangv ivvdtkqpam gklrvtysvn astelpdlss yhlldaagll
      301 eaqriagvys dknqyndiak kqwydyrlaq vksgvntywl sqplqvgygl nhslqlaggg
      361 sqfrysfsln ynnsegvmkd sgrdryalsy nigyvggrvk vnnntsvgyv kgnnspwgsf
      421 nsyssqfpff knnddsgnpi kvlepssgdl gfaisapgsl aflnpsynst lnvsdynssl
      481 smsnktnvev sltddlkltg slgwqgnspy aqtflpadht sfassvtssm mdlgsysqlk
      541 gnnnaidgki glnyrlsfgr stllaavggq lqktessstq ikvlgvpndy ldemglangy
      601 gltstkpsat vnltrnvsnf gsisynfadr ytaeftanqs gssqfgsnsk mspfyaagls
      661 wnitnekffk pndviqsakl rasmgttgnq nfssdmsqqv yqyklvnnyr llmgtvttsf
      721 anpdlefqkt lktnvalmlg mfknrinvsa eyynevtnnl ilpleiapst gfityqdnlg
      781 atknegfelg isanvikdpq rnifwtvgfn tghykniitr lspaveaink knnldsdpnd
      841 ptntryqssp lprfvvgest sriwavpslg idpatgkevf vkldgshtfe wdandkraia
      901 datpkfkgaf ssnlnyknfv lnlnltyqyg gymynqtlvd kvenvnlalg nadsrvlter
      961 wkqpgdissf kslvsdgtng lqttkatsrf vmedsyvdla sltigynfps tlkwvkaahl
     1021 saprlmitqn nlahfgtikt ergtsypfar slsfglstnf
//
LOCUS       WP_103787302             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103787302
VERSION     WP_103787302.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108161
     Region          30..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqlykmkyl lllvcmfsvl ianaqnkssi sgklidesgq plpgayigim gsstgtnsda
       61 ngnykltgia ngsvtlqvkf igykdlqrti nligdfvanf vmqpestalt evvvigygsq
      121 qkkdhtgsis tvnakdfqkg sittpeqlis gkmagvnvvs nggspgsgsv irirggasls
      181 asndplivid gvplsndvia gaanplnlin pndiatftvl kdaaataiyg srasngvvli
      241 ttkkgeegkp kinfssqlsv yevgkkldvl taeefrtyvn tngndaqkam lgststnwqn
      301 evyqtaigad nnlsiagswk qmpyrlsggy lsqkgvlvtd klnrstvaln lspsfldkhl
      361 kvdlnlkgaf sntrfanqsa igaaaafdpt qsvnvtnqyg nyfewtttan gvttlnpnas
      421 rnpvgllqmk adeskvqrsy gniqldyqmp fvaglranln lgydvskgeg tvfvpaeaaq
      481 syavggvnne ykqkvnnkvg efylnyakdf ksikstinat agygyydflt tkylyashka
      541 ngdvvsgsep sfpfdkpqar lisyygrfiy sydskytlag slrndgssky apenrwglfp
      601 slaftwrinq enflkssksi sdlklrlsyg stgqqdgipy ysylpvysys vaaasyqfgn
      661 tfyqmsspaa ydssikweqt dtynagidyg fadnritgav dvyykktkdl lnnipiapgs
      721 nftneiitnv gnvenkgvef sinaaairnk ttnwdlgfni tyndnkitnl taidnpdyag
      781 aptgaitggt gnkiqinsvn yptnsfyvyk qiyqdgkpve glyedlsgdg vinekdlyry
      841 kssnpkvimg fntqfthkkw svsavlrani gnymynnlaa glgvknniln pvgylgnstt
      901 eiyrsnfinn qyqsdyylqn asflrmdnlg ltynvghvlg adktanlrin ancqnvfvvt
      961 kyngqdpeiy tgidnnfypr pktfvlgvnl df
//
LOCUS       WP_103787882            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103787882
VERSION     WP_103787882.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114201
     Region          133..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkvyyllt fvwlicllcq sgyaqtksik gtrsnsqdta lfktvtvfvk dlgsskvlds
       61 vrvtlgqesk fttngqvvfe nnssrnlvly kpgfrrvaky vtsetvsiam vslnesegfl
      121 istgqsksvs plfsgstvtv kgndlrkvns isfidalkyy vpsltvtysn nngsnpnslp
      181 eirlrgannl pyattlassk nagsgvqknp sasdyvasnv tsnsspiill dgvqvtlqta
      241 mdidlnriqs vtvlqdavst asfglrggng viaiqtskpk gglnisfseq vqgskadiss
      301 fnslnakqkf elenaaglyp stsdavyqkr ydqvynkgnn tnwlqiplqn glglkhsiav
      361 stgtenifyg vtasyndiqg tmkgsnrknl dlstdfggnl ggfsfsnkfs ylgsdasnsp
      421 ygkfsdytkl npywnpydln tgkfqryleg dvylnpayns tlattdnaky arynnqtnls
      481 lllgagfqln giasitkqsd elnyflppsh tsfdnitaan ilsrgrydyt ansfldvqgg
      541 anlqyqknlg kheisasfge nisqassese lisvsgfaid rladisygta ykgekpvssk
      601 ivtryastfg nasysydkry qidlsgaldn ysglssaskf gavglswnvq nesflknvsw
      661 inqlkvkgsl gitgnqnfls yldrtaydyy tnqqyvpgts nsstigqglg ayliaygnkn
      721 lkapqtykqd agidaalfnn rlalnfnvyq qkssniimpt lsasstgyqs ysyydnyagi
      781 enkgfefgia gtvyrsqrnn lswnvmlnsl hntdkitsia pfieqvnans ntashqeqlq
      841 sqykvgysps aiwavrsagi dpetgneifi skdglwnadd kvfagnltpk wqgsfgtdvt
      901 frqfslgmyf dyqlgakvyn qtladrvena niafnvdsra asaqrwqqdm snplykalsv
      961 ngiatsptya ttrfvenddk iqcasmmigy ampksiaekl kaqsmgfkfi vndafewgga
     1021 nmergiyypf qrnytftlna nf
//
LOCUS       WP_103788073            1161 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103788073
VERSION     WP_103788073.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1161
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127461
     Region          118..1159
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkallyyrf yglkkrlfll vvfllslpgf aqskealysf klkampvqqv fqqienethl
       61 rfsynpldid lnrkidlevs nekiedvlsi vsekiyakcl ikgeivmvqa vkdkrepftl
      121 rgqvvdnkqv plagvpiyns tskkgtstde lgrfslsaen gdvivvrfig fitqnitans
      181 aqnnitivll ddvkkldetv vtalgikreq kalgysysev qgnelkkare tnvinslagr
      241 vpglvvnsta ggpagssrvt irgntsitgn nqplyvvdgm pidnsnygqv gsdkfsggvd
      301 mgdaisainp ddiekisvlk gpsasalygs raangvilit tkkgsankel gvefnssstf
      361 enqltsfdgy qylygqgsnq nipqdasqar ttlfanfgpr ldaglsapsf dgvvrpyalv
      421 kdnisgffrt gstftntisl tnstekssfr fsasnltnnd ivpgsdmkrn sftfngnsqf
      481 gsklnleara fymnekvtnr pamaddpsni gnsfvglann vdqaqfstgy kdelgnyvdw
      541 gggqyrinpy wvinementt kkdrilgalq anytftkwls lqgrastdit fldyskfspk
      601 ttpgaltgrl dkrdqrystt eadmllsyqq qlskdfnlav rlgaslsrvn sfgtstvynn
      661 mtmtdvvsgn sfaedfpvei pyekntnsfy lvastayknf lyldatvrrd asstlpeenn
      721 tyyypsvgas fvftdafkln nniisfgkvr asaaevgndt dpyqldlyys lnpitangns
      781 aggisssvlp nknlkptrtr sfelgtelkf lknrlgvdlt yynsesrdqi nrvpapissg
      841 ftyqiinagv isnkgvelll tgkpvvsknf twdigfnfar nvnnveslae gvpfltlsda
      901 rwmgvsvvam pgapygsila fdyqkdpsgn vildpvtltp ltsnnrelvg kgtfswtggl
      961 sntfayknfa lnaivdikqg adlfsmtnlf aairgslsst iegraewies eerrmsagkt
     1021 pdewkamgnv kgyvpqgvvq tgtdqqgnpi ytqnsqavdp svywgqiytd gngvarpyiy
     1081 datyvkmrel slsyslppal lskwkvkals valvsrnpfi iykdvpnvdp dsnynngngq
     1141 gfeygslpsr rswginlnlr f
//
LOCUS       WP_103788275            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103788275
VERSION     WP_103788275.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115673
     Region          59..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkncyekvit kkynpkacfr kksflalllm assinlmaqs epqqakeekt aatatrkkiq
       61 ingtitdenn nplirvtvge lgtkngtvtn ekghfhlivq dnavvlityl gmesqklrmd
      121 gkttfnivmk esstsikevv vtgipfnrka esftgsytki taqelqsagt qnifqslknl
      181 epslnfidnn atgsdpnkmp elqirgassf pdvnneyatk pnqplfivdg femaiekvad
      241 lplpriesvt ilkdasakal ygaraangvi vietvkpkgg alrisyngtl gieapdfssy
      301 nltnssekla lerqlgaynq kqpieglrfd slyyanlkav qngvntdwla qptqtgitnr
      361 htinieggde hwttgfslfs ngtqgamkgs ernnlggtls igyrqskilf rnqlsltksn
      421 stnspygdfs fyaqlnpywr pynddgsvrk vlglsplygq tvynpmfnat lngrstsayt
      481 dltnntqley aftdhfkvvg rvgftntvng sdefipgsnl kfiafvgdnl ynrgsydktn
      541 gksssvngdl nanysnrwgr hlifvnaaan irednsesys ysatgfpndk mdniifakqy
      601 assalkptgs eattrelgal gminysfder yvadfslrts tssqygadnr wgmfwsagag
      661 wnvhkekffg dnqyinllkl rgsmgntgsq nfnayqamll ynyfvdqsyq gmvgtylnnl
      721 nnpglkwqqr mdynvgldvd fmkrlslrld vykgvtnnll tdittppslg fatykanlgq
      781 lvnngfefrv nykmfvntan rqvlnvfvsg asnnnkitki snslqsltnl qdtksrtsnk
      841 plvrfqegqs lnsiwavrsn gidpatgkei yvkldgtltd vwdpadkvvv gdnlpkmmgt
      901 aganfaykgl tigvigryrv ggqtynqtlv dkvenaslnn nvdarayyds wkqagdnvlf
      961 rsigttqttt lassrfvqdl selsissvnl gydfysysfv kklklsalrm glnlndvyqi
     1021 stvkvergts ypfarncslt lnasf
//
LOCUS       WP_103788564            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103788564
VERSION     WP_103788564.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113371
     Region          23..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknlllvtw lvlfslvsva qnrtitgtvt dksdgqsvpg vtiqvkgtnl gsqtnqegky
       61 slsipsdakt ltfqyigyit revalgasnv vnialeqdsk qlgevvvtal gisrekkalg
      121 yavtdlkgde lkrsgevnii ealsaksagv qvtssagtpg asskvvlrap atitgevqpl
      181 iivdgvpidn tttqstagdy pfnqnlsgvn nsnraidlnp ddiesvtilk gpaaaalyga
      241 ragngaivyt tkrgknkkgl gvtlgqtiei anvtdlperq siyaqgtiqn gvptyvtadp
      301 gpdnlyntad dvsagtsasw gplissvagi ashdnastff etstsyttnv svdggsdkvt
      361 frfgvgntnq ngvvpgtdfk rtsfrltadg yikdwlkigg tanyiksagq rvqngstlgg
      421 vmlglmrmpa sfdinpytfn ngfqrtyfgl gydnpyytsy enpfndnvnr vlgniylsyl
      481 gkpwfnvtyk lgidsysddr rqvfaissfg ndaadqtgqv nyntitnrdi ysdliftgsg
      541 niakdwtlny taghnitnkn fgslysrgtv lsipnfydls naanlysstl ktrqytwalf
      601 gqldfsfrnm lfislagrne wsstfgtakn nffypsanls wvfsetfklp ewfsfgklry
      661 ayaqsgispe pyqaktylkv piltdgftng lsfpyggvsg fgyslsnigs sdlkperqia
      721 nelgvnlkfi dnrinlditg ynqeskdvll frplasssgf gsvygnsarl rnkgleieas
      781 gdlfkgdgfn wnlgitwskn ksevleladg vdqfeiesgf gdpgayaivg qplgmlygtk
      841 wardanknll vdesglpfld pqfgilgnpw pdwtggirnt fsykgvslnv lfdirhggai
      901 wngtrarlnr igrseasadr ertyivpgvk adgtpndisi safdyynfyl gdngaaaeqm
      961 iedvnwfrvr eltlsytfrp kpwekyvnsi gvnvtarnlf lntnyhgvdp etsltgagsn
     1021 iqgfdyfnnp gsrsfifgin igf
//
LOCUS       WP_103788566            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103788566
VERSION     WP_103788566.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114353
     Region          23..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslllvaw llmftfvsma qnrtitgtvt dkldgqpvpg vtiqvkgtnl gaqtnqegky
       61 sisipsgtki lvfqyigyit hevtigagnn ynvaleqdsk qlgevvvtal gvsrekktlg
      121 yavstvspdn llqksepdml kgmqgkvagv dirasqgtpg aatrinirgy tsfygdnepl
      181 ivvdgipysn dviessdpts gggayssgls sldpndiesi svlkgaaaaa lygsrasnga
      241 liiktksgss klsqkglevt fassaameei anlpnyqnty gagtlftyan angswgekfg
      301 sretiptwpa ylaafpdqfg ptvpyqaypn nvkdlfdkgs lyensisiqs gtektslsgt
      361 asyltqsgyv pesdfsrvsl sfgglskltn gltaagnfay snsnqaggvf genqvdgaas
      421 sfarnlflar nwnlaglpye dadgfpvsts paqydnplws wkhntvktgt dryvaslkls
      481 ydikpinlnv syqagantsn ffrrqiidlg sraegglgsi feqnykkqel esnlvftytp
      541 hkafnenftf ramggfnvnq rttntqgfdg sqiiapgiyt itntkditkd llntfyerqr
      601 lwglyaeltl gyknyafltv tgrndwsstl pennrsyfyp svsasviftd aiginwgpld
      661 fgkvraswak vgrdappysl qntyslgnnv vgqpsatqan talnpnlkpe ftedieigtq
      721 leflkklisv dfawyqrast nqiaavpvpt ssgfsnayvn vgkvtnkgve lelglnpirt
      781 adwnvnikgt ftknkatvny leegltrltl ngvldeispy iepgkpfgyl rgtvnyrdse
      841 gnlminpetg llirasgqqm igdpnpkyka gislgvtykg iffntlfdwt qggdmysvtv
      901 ssllgrgvtk dtenreggfv ipgyygdpnt geplldaggn kipnttvvsm nemffgesfa
      961 insatewnvy datvytlrel tlgydfpkky fqktpigsls lsftarnlwf lapnlpkntn
     1021 fnpdvnsfas stqgielsaa pttrrygvnl kvtf
//
LOCUS       WP_103788665            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103788665
VERSION     WP_103788665.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112117
     Region          24..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrllyfia vflfvastvm aqnrtitgtv tdksdggpip gvsvlvkgss igaqtdiegk
       61 ysiaapanst lvfkfvgyst kevtvgatst vnisleqdak qlgevvvtal gvtkvkrdlg
      121 yatqtvkgdq ladkgdvnii ntlqgkvagv ditgasgnag sssniilrgi ssftgnnspl
      181 fvvdgvpvsn dldqstttly gnqpanrald lnlnniesmn ilqgpaaaal ygsrasngai
      241 iittkrgsgv kgktavtfss sygvqnvygf adlqnkygqg aggafnsvsg nswgpafgst
      301 pslanglvva tgttpnvngv vyqpgssiay nnyknnlidy fnqgtsfenn lsinsgdakn
      361 nygltlgntn qtgilptsef kklnaqftan lsltdkltlg tsinyfntiq ngattqgnga
      421 nssmfgiwgv trstdfnyyk nnyinadgsn nwfiagrdnp yfaansnslt snlsrvmgnv
      481 nlgydvfswl nvgyrlgldt ytdrrkrsva igstqaassa gsvmndqffr sefngdllit
      541 akksnifvdg lnasvllgqn inqrvyqnat vkatglsipg ywnvangssf tesgeasskr
      601 rligyyaqms lgyknylfle ltgrvdqsst lptenntffy psvsssfvft dafniqsdil
      661 smgkvrasya kvgkdanpyv lsntysswsf gnnvatynfp sgsilgygad atianpllsp
      721 eftssyefgt nlsflkdrin ldltyynqss knqiiavglp assgydsryt nigeitnkgi
      781 eatlgvtaig kggfrwdvsa nfaknnnkvv siaegvpsfa vpgsafggvi psvvvgqpyg
      841 vimgstynrn engdllidpk tglyagttpn qvvanpnrdw tagltntfky knftlsalvd
      901 ykkggqlvsw tiatlrgngs laetgvdrem philpgvian sdgsfvpnni qipaqtywns
      961 gfggigggef avfdattfrm reltlsydlk gsmiktsain nirftvygrn lfyyapnspi
     1021 dpevntqgag nirglelqsa pntrnfgasi kvsf
//
LOCUS       WP_103788667            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103788667
VERSION     WP_103788667.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113318
     Region          24..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqlllklms llllittvas aqnrtitgtv tsaednqplp svtimvkgtt maaqtdidgk
       61 ysisaatgst lvfsfvgyai kevklgtqat vnvalvsdsk qlgevvvaal gikrekkalg
      121 ysvsevkgdd ltrvkdpnvv stlsgkvagl qikqngngpt gssrivlrgn sslgsnnqpl
      181 ivvdgvpidn fsgatadfwg nksidkgsgi ndvssddies vsvlkgpaaa alygsragng
      241 vimfttkkgk kggvslayna nltfdnpmqt peyqnvygqg vsgafdknaa aswggkmdgq
      301 kvtdytgksv ayspgannls dfiqtgttlt nsfematgne nttfraaltr ndnkgivpns
      361 gfnktsftlr gtgklnekfs vdakisfsnq ktenrtkvaa dpdnifrnyl imprsvhftd
      421 lkstanyafp sgtsvdgadv sgkplswtsn ysglvrnpyw aaynntnddr rnrsmgfvsf
      481 kydftqwfnv qvrqgldmyt gqynlrqatn tpyweqsgty nvtddkyses ntdvlfsvnk
      541 pisssvsfna taggntmyqr tdllfsnsng llipnffnlt nslvptvnda htlkrinsly
      601 gtasfgyknf lyldlsgrnd wtstlspenr sffypslsss wvfsemlern gknlgpisyg
      661 klraswaqvg ndaaayqlmn ymnitvknvt dqngniiqii nsnasntkal ydlknelves
      721 yefglelkal hnrigldlgy ynkdsknqil kvqssgsdgy efhyknaglv nnkgievvls
      781 anpvktekld wnvalnfakn tnkivklted tkvqllndns tngflqitak eggaygdlyg
      841 rkyvrddknn ivvddkglpt fgtefeklgn fnpkwmagln nnftygnfdl gfqvdmrygg
      901 evymgsinng mtagtlketl egrdkmlvkg vtaggtpntv etkaelywgr lgngtepwiy
      961 datnvrlrev slgyslpkgl mskspfssak lslvarnafm iysktkgfdp eagysnsnaq
     1021 giefgsmptl rsvgfnlnvi f
//
LOCUS       WP_103788669            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103788669
VERSION     WP_103788669.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109062
     Region          25..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkylrilll vllsgisata lsqqrtitgt vtseddkqpm psvtvvvkgt atatqtdldg
       61 kysikasdga tlaftyvgyv tkevklgssn vinvtlslns kqlgevvvta lgikkearsv
      121 gyatgqvkgd eltqarevnv analagkvag vsvatpasgp ggaanviirg sssltgssqp
      181 lyvlngvpmn nsnsgsaiit gtastegsag qyggadlgdg isninpddie sisvlkgaaa
      241 aalygsraga gvimittksg kaqkgigvdf nttyqvdein dftnyqyvyg sghqglkpts
      301 veqalndgas swgarldgss viqldgvsrp yvaqknnikd fyrtggtftn tlalnggtet
      361 aafrfsaskl dnngvipnss ldrwsfnlgs taklgkkvta nvvvnytied aknrpslsda
      421 pgnsnfgiaf vansiqasqv lapgyhpdgs eiqftgntft tnpyfasakf vndthrnrii
      481 anaslrynif dwlfvqgrvv qdayndrfts vtptgtayrd lgdmrdnssr fselnadvlv
      541 gvsraiakdl tldaniganm mkrdneitni sgssfsipfl ytipntankt nsyfdfrsri
      601 nsiyatadlg yrnflylnls lrndwystla spssdkvsyl ypavsssfvf seflksntls
      661 ygkvrvgyae vggggdspyq ttlnyniagt ingipigqit ngsipnaelk praitefeag
      721 tevkffqnrl gidltyynkk inddivpvtt svatgypsav lnvgrltnsg wellltgtpi
      781 rnndftwnvs lngsvnkskv eslagdltsi qigigrteta fiqqivgkea sqvmafdysr
      841 desgnilkgp ngvplrgnli aygsgnykyn tglsnefkyk nfnlsflidg kwgakifsgt
      901 nayatgaglt qetlvdrdka gfdaqsyyan fgsnvsgqfv edasfiklrq lvlgydfpls
      961 mfnnkiqglk isfvarnlav lmkhttnidp esnynntaaq glelggvpst rsfglnlnfk
     1021 f
//
LOCUS       WP_103788909            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103788909
VERSION     WP_103788909.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118837
     Region          31..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkllysyl llallsllgs qvtlaqtktl vsgtvledgt kipvagatvs ikgtrdaiqt
       61 dadgkfklnt kakfpfrlvi qyvgyitkev qvfdledgei nillrsrnql sevvvtalgi
      121 esnrksints iaridkkeil aaketnvvta lsgkvtgvqv qnsggspggs stirirgnns
      181 vlgnnsplfv vdgipvdnsv qdilptisna fslatpsnra idinsedidn vsilkgpaaa
      241 alygiraang aviintkkgs dvdkkfsvsy tgsasfdevn rrlqprqniy snglnglyvv
      301 pgqpgsdenw garidsltys evssgfdkng livgksspis ngkpvnyydn innffetgkt
      361 ynnnisvtgn ldkggyyfsy snldqtgiip ttnfyrntfr anadykvtda lklstglnyi
      421 nsgsdnralm ggfntnvvra lvnspanfdi tnglsdpann pdsyllpatn skpwgdsrsy
      481 angrgwdnpy wslnmnpqnd dvnrflgfaq adydflpwls gtfrfgydsy rdlrkggfsr
      541 gtsgvaagai ndvnffrrdl ntdvilkaqr titkgwdlsa ivgsnyydsy knqintrgdg
      601 liipglfnis nasttnsfnq tvrkrlaagy fslalnhkdy lfvnftgrne wtstlpdghn
      661 sffypsagas fvfsefldrd tkkwfslgki rasyaqvgnd adpysletyf tnssaggwiq
      721 sslsfpfnnt aglsygstlg nqglkperin twevgtdlgf fknrlgleat yysslskdqi
      781 ipvslpnstg snaalvntgr isnkgfelsl nvnpienkdf swdfnvlysk ndskveelap
      841 glnnisltgg fpfgdsraiv gqpfgalfgv dlqrnaegkp iiddqqflas gapnanygyp
      901 lidatpriig dpnpdfnlgf rnevrykfat lsffldyrsg fdianaprlq mvfngvaeet
      961 anrgqqvvfd gvkksdgaqn ditaiasqsw yrqtfnipgm yvekdlywlr irdinltfel
     1021 plkwiqkaki sraaltftgr nfllstnysg adpdlssrng lsnalgvdfw ttpntrsyat
     1081 tltltf
//
LOCUS       WP_103789191            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103789191
VERSION     WP_103789191.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119095
     Region          26..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkylltllmv fcvslpgraq tksylvkgrv vadgdflpla gasvqlkgss dgtstdgdgv
       61 fslnvtgnsa tllvsfigyq qrevsirvps tdlrivlken ssllkevvvs tgyqslpqer
      121 ttgsfskvdn ellnrvvatd vfskleyavp gltvnrssfg aptisirgqs timgnsqpli
      181 vvdnfpydgd lnninpndvl svtvlkdaaa asiwgtragn gvivittkkg radellsigf
      241 tsnlsigqkp dlgylpliss sdfidfeqhl fnkgyytsie qspshpalsp svelmikqrd
      301 glisgaeans qfealkgqkv qddmnryffq nsikqqyaln lkggsnsiry yfsggydhnq
      361 enetrnnykr vtlnssmvfn plkqlelqad inynqsnasl nnpgislmss ssaysgkkfy
      421 pyalladgng nalaiaksyd vsfvnsaien gyldwnyrpl eelqlsnnqs dqydlrsnag
      481 vkysfnsnfn aelkyqyera ftnstnlqse gayysrdlin qfsegtgasl vhhipvggil
      541 dqgsstlnsq nlrgqlnflk dwnqqhllsl iggvevkqld vtarqsrvyg ydsetlqtqq
      601 vdytsafrvt psgyynfips msgqssktdr frsfyangsy tfkerytlsa sgridqsnff
      661 gvstnqrsvp lwsaglswni skepfykpdw lpqlklraty gyngnidktv tayttaryty
      721 dwlkymqale iinppnpelr wekigitnfg ldfetknrvl ygsieyylkq gkdlignmnp
      781 dptsgvmnyr gnlasmrgsg vdlnlnsrim dkaftwnaal lfsyvtdkit hytkedlayn
      841 ytalstgiai fpmqgrpvys vysyrfagld tqsgdpmgyv ngekstdyas ilntkpeeli
      901 yngparptyq galrntfgyk qfqlsfnigy klgyffrrns isysqlaatw sghsdyalrw
      961 qqagdeqrts vpsvsgvlna srddfylkse alvengshir lqdinlsytl drkrvpglpf
     1021 qqlqlyvymn nvgilwrand qgidpdavpn ggalylpqar svafgvkvgf
//
LOCUS       WP_103789215             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Solitalea
            longa].
ACCESSION   WP_103789215
VERSION     WP_103789215.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55139
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgiptevs ptelrvaatp ktvkrlikqg fhvciqqnag akanftdkef eeagaqivqt
       61 ateiygqsdi vlkvkepsvd evdmmwgglv llsylwpaqh pellkklalk kvnavamdai
      121 prisraqkmd vlssmaniag yraviegsyh fgrflngqit aagkvepakv lvigagvagl
      181 aaigaanslg aivrafdtrk evaeqiesmg asfltvnine dgatasgysk emskefidae
      241 mqlfleqakd adiiittaqi pgkeapklil dyhvaamkpg svivdlaast ggncvltkpg
      301 evytttngvt ilgklnqlpn qasqlygnnl chllddmgka ehfkidmeda vvsramvtyn
      361 gsinwppqpl pvspakpkte saaekaeekk vneqqlakkq atsmfirltv iglfllligq
      421 fapaefmqhf tvfvlavfvg wqviwnvshs lhtplmavtn aisgiiivgg llqttndlss
      481 pltilafvai lvasinivgg flvthrmlkm fkk
//
LOCUS       WP_103789549             991 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103789549
VERSION     WP_103789549.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..991
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109758
     Region          28..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklylfkyg ltlclllvsl vtfaqngtls grvfddenlp mpfagvaikg ttlktgtnad
       61 gdfkftglpl gqttvivtvl gyellektvn vtantqvyft lkpltktlte vvvvgygtak
      121 kkdltgavgt lsnkdfnvga vnsvqdaisg riagvsvtsi sgapgntsti rirggaslna
      181 sndpliivdn vpidntamgg apnilssinp ndvenvtvlk dasataiygs rasngvilit
      241 tkkggdkfkl syglttslst vpnkvpvytg defralvnkv yagqtpvlsl lgtantnwqd
      301 aiyqnafgqd hnlafsgklk tmpyrvsfgy nntdgtlkty nferttlaln atpnflknsl
      361 kmtfnvkgmy nnnnfadqga ignaifydpt kpvyngnerw rgyttwtqdn tlngdpvpla
      421 tanpvaqlel tdntstvkrs ignaqadyem pflkelhanl nvgydyaksq ghnnvmdntq
      481 winspsvsgg rvnpyeetrr nqlldfylny skplqkiqsk vevmggysws hfyregadsa
      541 tnvsgtakte pniysseyyl vsffgrlnyt fkdrylvtft lrddatsrfs senrwglfps
      601 vavawkmndd ffkdsktisd lklrvgygtt gqqdlnngnn ypylakytis dnasryqfgn
      661 sfyntlrpdg ydanikwest ktanigldyg fwdnritgtl dfyqkktedl lsivdvpagt
      721 nfsarvltnv gdmenkgvef tvnakllsks alkwnvnyni synknkisnl sltddpnyev
      781 mvgniagtts gtiqvqkvgh pinsfyvyeq iydrdgkpme dvyvdrnkdg vvntsdlyvf
      841 hkpdatvlmg igttlnykrw dfsafgrwsl gnwnynnvaa nstyrgfyst lgylsnqtts
      901 asdtrfttal ktntsdyyiq dasyfrldnv slgyhlpamy hqkvnlrlnl nvqnvfvitd
      961 ykgldpeisg gldnnffprs rtfqlglncd f
//
LOCUS       WP_103789903            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103789903
VERSION     WP_103789903.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113614
     Region          25..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkekftkflv llfslatltt yaqqkkitgt vtskadgtpl pavtvtvkgs slgtqtdgdg
       61 kfsisvpena tlsfsyigfk akevsvgasq tinvsldade rllnevvvta lgiqrdakal
      121 gysapqlkge eltksreanv inslagkvag vrvssqsgtl ggsskiiirg esglggssqp
      181 lfvidgmpid ngaqqistva gavpqgsaga dfgnrvgdin pedietmtvl kgaaatalyg
      241 araksgaivi stkkgvkgna svtfnssvrm ddilkmpefq neyaqgvqgt yniastngwg
      301 pkisdvqdkt fpnflaqdvh lkaydnnikd ffqtgktyin slafsggnet gdyrfsyani
      361 sqtgiipnqk ysknnitlna gktigkdfni rtilnyansg gdgrpvqssn npnvimpliy
      421 gvprtvdmel lrnnsinpet gqqitltpar ngnnpfwvid nnnfsndlnr fygnailsyk
      481 ilnwltvann lgldyynefr qgntrngtig altgnfftan ifnrsfnndf iatadtkitn
      541 dlslkvigga nvfenyyqrn qsdaqtltvd qlynfsnaat vtttntsnkw rmvglygdig
      601 lsykdylfln vtgrndwsst lpaenrsyfy psvsssfvft elmpsnkwln ygklraswan
      661 vgsgtdpyql afvygpqsta faqygygsqf pfngllafsi psvipnfnlk pqnqitteig
      721 adlrflnnrv kldvtyynsk tddqiialtl pqstgftskk mnagsvtnkg fevalglvpv
      781 ktnrfdwnfd lnfsqnkqtt qlpsevtayt lqsgwsgliv ktrsnesfgi fgsawerdpn
      841 gnividpatg lrktkldqrl gsinpdwmlg innsinfksf nlsflidvrq ggvvysntas
      901 slrtsglake tlanrgnifi dkgvvlqgte yvpntvpvqs mqdfwgqfst tnteanifda
      961 syvklrevkf sykipssilg ksakfmkele igvegrnlwi isdhvphvdp evnffgpgsa
     1021 adgiefnsap strsfgfnlr vki
//
LOCUS       WP_103789940            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Solitalea
            longa].
ACCESSION   WP_103789940
VERSION     WP_103789940.1
KEYWORDS    RefSeq.
SOURCE      Solitalea longa
  ORGANISM  Solitalea longa
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Solitalea.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Solitalea longa"
                     /db_xref="taxon:2079460"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108910
     Region          30..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrirhlrkml laffctvlia plvtfaqvnv kgkvtdavtn eplagvsvti kgsttgtatg
       61 pdgsftisap sstsqlqfsl lgyrtqtfaa sgtldvklve dvakleevvi tglatnvkrs
      121 nlansvatis skeltgvsnp qtlegalngk lvganivsqs gapgggmsvr lrgltsvnsn
      181 tqplyvidgv vidnsaisgg intitqasrg gvatsnqdnp snrmadinpq dienvevlkg
      241 psaaaiygsq assgviiitt krgkegktti sftqdigtse airllgvrqw dedkiqqfyg
      301 snqanadaqk qlyraaaaan slhdyekemy getgflstss lslkggsekt sfflsglymd
      361 engiiknsgy qksairanid hkisnkfnis vnttytnsts drgltnndnt gvtygvalss
      421 tptyaqifpd eagryprnay gasnpletrd litnrekinr fvgglsitay lqqssnsvtk
      481 lllkggldyy tlntkaifpn tlqfesegqg tnganiegnt nnlntnasay fvnvfntser
      541 kytfttsaga dmfnydqnql lttsteiigs qtsqaqasav kvdqkvfprk irgmfaqeev
      601 nfedkvifta avrldkssdn advnkfeayp kasvavnlan fdfwksktvd hfklraayge
      661 sanfptfgsk ftafspfnig gnggtligvl npagnvqqgn dqvkqerqqe fetgfdltlw
      721 dgkvafeaty ykrqgkdlif aanipastgf aqkiinggtl enhgwelglt llpvntpnfk
      781 wtsrnsfwmn rskmkeldvp sfrigafsna lanylieegk spteivgpdd tngdgtadgv
      841 fvlgnsepkf qmsfsndffi yknfsvsfvl hwkykcdnin ltellndlgg tspdfdqddn
      901 gngvvngver psllgvsarp lvqdasylrm rdigiyysvs psvvknafng vvsgikfgvs
      961 atnlftitpy ksydpevsnf gsggfstave vmpypsakrm ffhltvdf
//
LOCUS       WP_103804223            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            alvei].
ACCESSION   WP_103804223
VERSION     WP_103804223.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium alvei
  ORGANISM  Flavobacterium alvei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Flavobacterium alvei"
                     /db_xref="taxon:2080416"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117352
     Region          45..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlknlqltcl isilfagsft eqlhaqiaqd stqtitaapk kiqgilvkgv vknaknkevl
       61 sginiavpgf saaitnndgs feigvphlea lltvsgqdfq tkvfplksrd agieiflfee
      121 yysplyqvan lpageqinya ttkassvvnf ktnqwsspvk esvgdflqgr vaglnsvrks
      181 gvpgagayls lrgfnslyat nkplivvdgm iyddedygsg iiknnssspl enidvkdien
      241 itvlkddasl ygtkgangvl iinttrptel ttkidftmyg avnqepdelp vmqsdayrth
      301 iyqleasrgl aqipltylpy andnpgsvgy ykyhnetnwq dkvfkssisq nyflkvrggd
      361 niakyglsvg ylnnkgiied tesnrystrl naslrltekl tvdanmsfin niqnqrdqgf
      421 ayltspmyla ltkapflgan vivddgsvsp nlsdvddfnv snpraiidna igvnknyrff
      481 gnmnfkyvin ntwnvntifg itynkeretf fipdrgvtdi ilpiaigknr sgsevqilnt
      541 lytdtyanys kkfknedkld frfgfrtqan ksetdlglgy nsptddftsv gsgsnllrev
      601 ggvlgqwnwl niyangnyny rdkyflsasy avdgssrfgd esstgdnqya lmtsitgawl
      661 vsaenflkns ntfnylklra tigtagnddi gnfaaqkyyi sqnllgvqgl vrgnianpdl
      721 qwetvkkfnl gadlalfner lnvsldlfan ktenmliyet vlastgfdya vsnsgsmktr
      781 gaelalnsri inspdftfdl gvnlatysnr vlslpngtiy sqfggatymt evgndanlfy
      841 glktngvyat tsdaqadgfs rrltngelvp fkggdmrftd sngdkviddn drmvignpnp
      901 dltgsitanf aykrfylqgl fnfsvgndly ngvrynlekm sgyenqsvav enrwraegqq
      961 tdmpkatwgd pmgnasfsdr wiedgsylrl ktlvlgydfn vekmnyikai kiyatannlf
     1021 tftdylgydp efsatssifg qgvdmgmtpq fktfqlglrl gl
//
LOCUS       WP_103804230            1093 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            alvei].
ACCESSION   WP_103804230
VERSION     WP_103804230.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium alvei
  ORGANISM  Flavobacterium alvei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Flavobacterium alvei"
                     /db_xref="taxon:2080416"
     Protein         1..1093
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121718
     Region          33..1090
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkitnlly cfsfalivla alptlaqnak ttvvrgkvvd ssdnlpipsa tvveqdsenr
       61 titgvlsdvd gnfaihvknp knkifvssig yksklvsidg rdnirialvs svetlsevvi
      121 tsqkkvetgl mnisernktt ssvtikasdl atsqaaside qlqgrvagvd iiassgdpga
      181 gmqikirgas sisgssapli vvdgmpyets ipadfnfgta ddegyaalln iapsdietit
      241 idkdaaatal wgsraaggvi iintkrggis apkinysfvg tysklpdaip mlngdqysql
      301 ipeefmnrng vplntqtvke fmydpqevyy yknysnntnw idevsqtgli gdhnlslqgg
      361 gqraryftsv gyynskgvtr gtgfervstr lnldyvvsdr ikfktdisyt hsdtqrnyvn
      421 gtgngdlirs vaygkmpnmg vyeyneegil tpnyfspaqn vqgrypgtyn pvamaeyatn
      481 dqvsdrivph fninvdiipk eliatfdlqf dfnstkakaf lpqnatgrpi tetvvnrasd
      541 advdtssitt ktnfiyspni gknqslqmlw siqsndfrye shqvltsnta sslltdpsnp
      601 srtqnsdlql ytnnsqarsv gsllnaqygl mdnryivnvg lradgnskfg penryglfps
      661 asarwrisde kfmkkltyid dfslrlsygk sgkaprydys ffnvygnfss dylgmngvyp
      721 qnielsnlrw etltgknlgf nlqmfkrrlt ldvdfyrntt edmifqnidl ttisgyskvd
      781 anvgtmdnqg wevglfttpy ksgkwkvefn fnissnenmi reiseyypnq sgntdrngef
      841 krflqidnpf gsfygykfkg vyvdkdatla rdgngnvitg pngqtvymrf nypntdyifq
      901 pgdaiyedin kdgnidsrdv vylgnsnpkl tggfgpniif nnqfklllyf nyrlnydivn
      961 gtdmlttnmy gwnnqstatl srwrnpgdvt dmpravygag ynwlgsdryv edasflrlrs
     1021 itfsytlgks mlkklkmdei rtyitadnly twtnyrgqdp evsmksgdpf giaidnsrtp
     1081 ptsrislgit trf
//
LOCUS       WP_103804360            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            alvei].
ACCESSION   WP_103804360
VERSION     WP_103804360.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium alvei
  ORGANISM  Flavobacterium alvei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Flavobacterium alvei"
                     /db_xref="taxon:2080416"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115183
     Region          27..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngilv lllvlvaqit faqeravsgv vsdntgmplp gvsvlvkgtk tgtqtdfdgk
       61 ysikatssqv lifsyvgmkt heakassatv nvkmestave legvvvtafg qkkqkravas
      121 atsvvsakdl tevtntnvfe slsgkvagvd itapaqvgas skviirgynt isgntsplyv
      181 vdgspivnss asgtgntrsy dsgngigdid pnnietmtvl kgaaaaalyg srasngvivi
      241 ttksaknksk lnveimtstd faevariphl qndfgqgwsg hswsswsgsp ntasnengsw
      301 gpafngevrl wgaiinsgqq ikpyvalenn vkdffelgnt ftndvrvsgg geksnfslyf
      361 sdvksdgivp tdadlykrrt lamnggiteg kmtikgtiny vkkdqnvvnt gqgadagegn
      421 tlsqellqvp rdisivdled ytnnpyntns nyfspytnnp ywsvkenati vngnrfygna
      481 yfsykiddhf sasyqiggdy ssedvksyga vvkflpgsaq alaganevvg gvtestrerl
      541 efdnnvilny sntfaedfgl nafvgfnanq rkssslfaqi tnldipnfye lsnssikpvv
      601 gqanserksy svfasfetsy knflyltltg rndwtstlpi gnnsyfypsa alsgivldtp
      661 dtflklrasy aqlgndtdpy rtesamipgn salgfgnill piggvngyef sgllgnselk
      721 pemtteyevg fesnffkkrv nldvalydks tadllvnrpl ptstgytsqv aniadinnkg
      781 ievslnlvpi rtenftwdft ttftknisev tdikgestkq llasnygvtf navegeplgv
      841 favkmplknd egkyivdaat gfykvsddeq iigtsqrdfv mgfnsrmtyk nlvftfgvdw
      901 kqggemysyt krlshftgng iettyndrnt fiipnsvvev vnsagvvtgy aentkavgle
      961 dvtdfyntsn npgienthvi dktfvrlrsv altynfpstv ikrmglqnas fsvygknlal
     1021 wtpaenpyid pelstfgtgl lseqgefgan ptqrtygasi kltf
//
LOCUS       WP_103805426             981 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            alvei].
ACCESSION   WP_103805426
VERSION     WP_103805426.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium alvei
  ORGANISM  Flavobacterium alvei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Flavobacterium alvei"
                     /db_xref="taxon:2080416"
     Protein         1..981
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107058
     Region          24..980
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykkllf lllflpfcvl aqntiggtvl dkitgqpipg vnvnvqgstt gastdldgkf
       61 rlsnvkkgdk vvfsfvgyks etivfssqqs isvqleedss qlkevviqvg ygtvkkkdat
      121 gavavlgakd fnkgvtvnad nlfngrvagv tvnagggapg sgstirirgg aslnasndpl
      181 ividglpien stgtgstsfl aslnpsties fsilkdasat aiygsrasng vilittkkgg
      241 knlsvefnsm lgignliktv dvfdaatlrk vvteqnpsll srlgnantdw qkeiyrqtty
      301 tdanvsvrgs llgvlptrlt vgktyqeglr ltnvfnrntv glalnptlfq dhlklrlnan
      361 ysnennsfad avessainfd ptqpvydnts kfanfyenyn hatgaltpqt trnpvaqllq
      421 tdntgysnrl fgnfeadykm hflpelravv nvgfdethgq tsryagldva ssgsnnnipy
      481 gtneisrghr kntlfdafla ynktfdklvf dltggysyqk fenntyiqgn lndpnlpttg
      541 vggfpqykva tpvvllgyfa rtnlnyndky lltlsyrrdg ssrfakenrf gnfpaasfaw
      601 kasndffkds etvsdlkvrv gwgitgqqdi gdaaniylqk yvtgsgssqy tfgttalpia
      661 issayneqik weetttynag vdyglfknri ngsvdvfykv ssdllvkgpl adgsnfsnai
      721 fqnvgqfttk gveftinadi iksdnfnwnv nfnathfdrk ideliyhtii rtgdniagtg
      781 tqakvyqegf apdsfwvykq lydvsgkpie gayadsngdg vinaddkyiy knqdaklvlg
      841 fttnlnynkf dlsfalrsni gnsvfnavna sraqygrlnt gaditnlpts vvntgfnnts
      901 tvvlsdiyve nasflrmdni slgytfpkwf ndkislrlta gcqnvfvitk ysgldpeinn
      961 gvdgaiyprq rsflfgtnik f
//
LOCUS       WP_103806019            1125 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            alvei].
ACCESSION   WP_103806019
VERSION     WP_103806019.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium alvei
  ORGANISM  Flavobacterium alvei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Flavobacterium alvei"
                     /db_xref="taxon:2080416"
     Protein         1..1125
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123295
     Region          31..1124
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqtikqvcg lllftllsls syaqqtnger iiitgkvidn tnlgmpgvni vekgaksstv
       61 tdidgnykis vnkgavlsfa figmnkvekt vgntatvinv tmkddatqle qvvvvgygtq
      121 kkgnltgaie tinaeklqdl pvsnlaeslr gqivglnvgg ngtrrpgets tlqirqtfgf
      181 tgatntipli viddqiqvdp qtglstldaf nrldpseies itvlkdgsaa iygsrasqga
      241 ivvktkrgka gkmrfsyinq fgindavshv ktmnayesgi ysnrvmqalg ndpatsskfy
      301 spaeleemks lnynwldkaw kpaeqqkhsl tisggdekat yfagltyftq ganlgeqdyq
      361 kwnfrtgmna kitkdldfta svsgnsgdie ksftksnssv anpygatnae qadyghllhm
      421 pkfvpittiv ngreyymspf nradgnlggt qnsnssiagw nyfallnngs ksvssdfsyn
      481 vnaainykvp fikglalrgs fartqtssst sqvalafpla ritnftaagh hlasaatdad
      541 ysiadnvrqa rvtydntnsk stqanffaty artfgnhdid amfsverset nydsailyfd
      601 rgtktskdly lgtsltagdl tpgfsnnfls esgtmsylgr vnysykskyl lqfivrrdas
      661 tkfapenywg tfpglqagwv vskedwfeka lpaidylkfr yslgktgndn igawrwatfy
      721 diisdkglqf gpnggtlgna iaprpnpnrn atwdthikhd lgidfnvfnn rlqvsadyyy
      781 dkgtdmlvsg agildvpisv ggafaeania gvnswgtefs lkwsdhikdn fsynigvnfg
      841 lfagnettay pdgaltdpsn nqqrtgassy npiwgfkvwk gtstgdgilr tdeditnywn
      901 yltanatasg vagakpnflg iidvinvkkg mlayqdlagt fvpatglkpg vdgkiarndd
      961 ygklvnsnrt ygfttnlgfk yssvylntqi gtswggirni dnveqrtstn daywaretfw
     1021 kdmygydnvn gkypnvafrd nvsnpsdfwq istfscsvrn ltlgyefpel ftsqlgisra
     1081 tfgvtgynlw yfnnpfpdhy rnmydsstag yptlrtwsln initf
//
LOCUS       WP_103806872            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            alvei].
ACCESSION   WP_103806872
VERSION     WP_103806872.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium alvei
  ORGANISM  Flavobacterium alvei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Flavobacterium alvei"
                     /db_xref="taxon:2080416"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111399
     Region          24..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkylilll ffagiittys qnltvkgkvt dtngyslpgv nilekgtkng sstggdgsfs
       61 intkngatlv itfigfetke vkvtgaklni iinessqvlk evvitgsmgr tldksslgys
      121 aqavkgqeia dtqrsnfana lqgriagltv tsstgapgas taiqlrgvns lsgnntplyi
      181 vdglpvsnet ldqglmisna pnrnqdytnr gadinpedie sitilkgpea aalygmqagn
      241 gaivittkkg kqgvgrvsys tntrldqvyr fpetqnvyqr gsggitntdy rrqfgeafap
      301 gtkfydnign ffrvgtstth nlsfeagten tsyrlslsnl kqegitpnts yerltaslna
      361 takispkfks egtfsftkse ndkaskggsg gltgsngyll tllgwpqnld vrdylntdgt
      421 rkkitsgald tetdnpfwdv nknlstdwnn rfvtnvgliy dpaswlnfta rvgwdvnsgq
      481 gfraihpesa aglstggfie tyynstsnln stllgtakks fgkfntkimi gnaindnyfr
      541 ilstsgskyf dpnfnsinnt dattqrsqer ivqsriigff telnfdydki vfvsltgrkd
      601 wtsvlpdpff ypsastsfmf tnlpglkdkk ilsygkiras yaeaanipsp ysavpiftsq
      661 lttnggyayg vtganpnlip efrksiefgt elkffndrlg ldvtvystkt vdpilknmrl
      721 sygtgfvlts anfgdlrneg leitlnatpv ktasfswdln lnfnktrsev lnlpaavtey
      781 ylsdtwlynn vrggvkvggp tttitavdyl rnnagqilid pstgyplknp nfviagdrnp
      841 dfvlgfqntf kyknvslsil ldirkggdif ngtefwmyqn gistrtldre qprvvqgvir
      901 dglensatpt qnnimvtpyl qneyyrtgga vdadfiekdv nwlrmrditl syrlpsetlk
      961 ktairslafn itmtdafmit nytgadpavn glnasaggag gvgfdfgtvs tprglnmgvk
     1021 lgf
//
LOCUS       WP_103807812             477 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Pectobacterium parmentieri].
ACCESSION   WP_103807812
VERSION     WP_103807812.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium parmentieri
  ORGANISM  Pectobacterium parmentieri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Pectobacterium parmentieri"
                     /db_xref="taxon:1905730"
     gene            1..477
                     /gene="nrfA"
     Protein         1..477
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53118
     Region          4..477
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvrismsvsy lwgmvaslfl lmpaysadvp apsspapiea rnstfinqhp dqfnswkats
       61 eqaerhdala edpmmvilwa gypfsrdynk prghayaltd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqegee gyfkgkwarg gpeiandlgc adchdtaspd faqgkpaltl
      181 srpyaerame aigkpfdqts rfgqqsmvcg qchveyyfsg kdkavkfpwd ngtkvedmek
      241 yydaisfsdw tnplsrtpml kaqhpeyetw sigihgknnv tcidchmpkv knadgklytd
      301 hkignpfdky getctnchtq dkaamqavva erktaiqelk lkaeeqlvha hfeakaawea
      361 gateadmqpi lmdirhaqwr wdlavashgi hmhapdeglr mlgtslsksa eartklvrll
      421 aqkgvtgevk lpdistkeka qqaiglnmqq ikaekqdfln tvvpqwneqa rkagrln
//
LOCUS       WP_103857754             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aeromonas
            sp. ASNIH8].
ACCESSION   WP_103857754
VERSION     WP_103857754.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas sp. ASNIH8
  ORGANISM  Aeromonas sp. ASNIH8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Aeromonas sp. ASNIH8"
                     /db_xref="taxon:1920113"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53300
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevaieagag lrasfddaaf eaagasvvpn
       61 vwqadlvfkv napteaeiaq ikdgatlvsf iwpaqnpelv kklserninv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vspakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggefl kldfggedga ssdgyakvms eefikaemel
      241 faqqakevdi iittalipgk papklitkem vdsmkpgsvi vdmaaqaggn ceytvpgelh
      301 vtdngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgnvaidfe dvvqrnmtvv
      361 qagevtfppp aisvsaapqk paaakpaakk eeakpsnkkf vfgalgiaaf gwvaavapaa
      421 flshftvfil acvvgyyvvw nvshalhtpl msvtnaisgi ivvgallqig qgstlvtvla
      481 fvavliasin ifggftvtqr mlkmfrkd
//
LOCUS       WP_103808920             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_103808920
VERSION     WP_103808920.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53556
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghasavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfeksg rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tvgihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_103853975             503 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Avibacterium].
ACCESSION   WP_103853975
VERSION     WP_103853975.1
KEYWORDS    RefSeq.
SOURCE      Avibacterium
  ORGANISM  Avibacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Avibacterium"
                     /db_xref="taxon:292486"
     gene            1..503
                     /gene="nrfA"
     Protein         1..503
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=55926
     Region          5..499
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mygviivnif rktlaslaia gltlvsaqpl maadnsvaek raptreelak pnpdlkiqai
       61 seqfaekypk qynswaatae steivpaiev dprmivmwgg yafskeynkp rghfytvtdv
      121 rnilrtgapf dansgpqpma cwtckgpdvp rliaewgeee yfngkwakgg aevvnsigca
      181 dchdttskdf aegkpalria rphvlralda igkdfahldk tdkrgaican chveyyfdkk
      241 vvnnvvfpwm kgvdvdsmeq yydniefydw ihsisktpml kaqhpdyetw lqgthgkngv
      301 tcvdchmpkv qgadgkvytd hkignpldsf entcanchdq sketltkvva ghkkdikdvm
      361 ikledqivka hfeakaawda gateeemkpa lqairhaqwr wdysaaghgg hihapdiilk
      421 tiatgldria dartklaiil tkhgvkqpin ypdistaena wkamgidiek eraakakflk
      481 evvpqwnkea lekglmekap pak
//
LOCUS       WP_103863679            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            I32.4].
ACCESSION   WP_103863679
VERSION     WP_103863679.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. I32.4
  ORGANISM  Aquimarina sp. I32.4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Aquimarina sp. I32.4"
                     /db_xref="taxon:2053903"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113641
     Region          25..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfsgilt lllafvvqft faqekmisgt vtddkglplp gvnvvvksta ngtqtdfdgn
       61 ytltanrgav lsfsyvgfet kdvvigdnts inaqlsasas eleevvvtaq gikakpksls
      121 yaiatvadde iensgevnlv ssltakapgv svvsssgsvg asanirirgn tsitrsnspl
      181 fivdgvpidn ssvgnatngv dqsnraidin qndiasisil kgiaaqtlyg lraangvvii
      241 ttkkgkigap tvsvsstvqm seitqtpelq refaqgingv ykgpesfngp swgprvstle
      301 ydgdssypfh rfgtlvptgd gngraaetyd hydffvkgll tdlnvsvrgg tesvryylsa
      361 gkldqtgvap teefgknsfr aditadlsek feisasgsfv nsggvrvqrg snisgimlgl
      421 lrttptfdng ngltgrsavg vtdvyelsdg sqrsyragvy dnpywtvskn patdnvnrft
      481 grlsfeyrpm dwltlqgrya ydrysdvrks afdlnsasnr tgrvfddavf neditanfla
      541 lfnkdisekl tfngllgyen ysndylrrnv qadgltipgf fdvsnsstqi ndvdifrkkt
      601 davfgelkfg yndtffvtgr arndwsstlp vdsndflsys vgasfvlsel yesdivnysk
      661 lrasygktgn dapiyasktf feagaaggdg finnspntfp lfgavalerd gesgssqiqp
      721 eettelevgg elkffnsrvg ldltyytket tgqvfavdva pssgfsgrnt nvgkienkgf
      781 eiganfnpvr tddfswnidv nwtsyttevv elapgvesft lagftstssr vlpgesygai
      841 fgnkwlrdds gniqiddkgf pivdpqsgvi gdpipdwqag irntvsyknl slsflfdire
      901 ggdiwcgtcg ildffgvsqe tadqreitdy vfdgvvqstg qpntravala dnatgvnrwt
      961 kygfggvsed nvydgswvrl reaslsynfg dkllngtpit sgsltvsgrn lwvdtaypgv
     1021 dpetnltgds ngvgleyfnq pntrsyavsl klnf
//
LOCUS       WP_103864782            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            I32.4].
ACCESSION   WP_103864782
VERSION     WP_103864782.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. I32.4
  ORGANISM  Aquimarina sp. I32.4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Aquimarina sp. I32.4"
                     /db_xref="taxon:2053903"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118054
     Region          35..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhlfiglal llvsfghaqn vitgtvttat dgttipfvni qvkntsqgts sdangnysis
       61 tqnndailvf sslgfktkev iinnnsiinv slvegstgld eivitalnrk renkelgyvv
      121 qsinhkdiae vksvnfldnl agklagvtvt pggatgvgss skivirgeqs ftnntplfiv
      181 dgtpinnstv fnntneaaag fqevdfgnga mavnpddien vsvlkgpsaa alygtrasng
      241 viiittknga nskglgisin sslfidtafr lpqfqnqygq gnsgqfeyvd glgggvndni
      301 tyswgprlnq gtlipqfdsp vtlsngtvvr ggdtalydnp stsitptpfi shpdnlkdfy
      361 qtgvttinni alsshfdkgn yrlsftdlrs esiipgvdld rktiathlgf lptkkttvna
      421 sinyvntgsd nrpsngygse nvnyslvawg prslntnnlk dywqsglegi qqysfnytff
      481 dnpyfilsen rnsfdrdrvf gnisiqqela tnlsltirsg mdysnekrqf lrnfstnrfr
      541 ngayaehdvt yreintdfll nytkkindfn fdislggnrl dqkaktsqtq ttqlaqpgif
      601 sfnnaaspie sfgfeskkri nslygllkfg yknylfldit grndwssala tpfsaentsf
      661 fypsastsfv vsnafklpkv isfakvrasi aqvgndtdpy qtsgafvsqt svnsqptftn
      721 qnfipnpnlk peqttsyefg tdihffkdrl nldityyhal tkdqilslpi pissgfnqqv
      781 vnggkvrscg veivlnaipi khenfkwntt infsknvsti tslpqqegrv tlaysrvynn
      841 pdqtvwfqve eggrigdfyg tgylrnengd fvitpegrfi adntlkklgn ytpdfivgin
      901 nqfqyknwdi nflldwrqgg klvsrtlsla avggqleeta yrpdagiiaq gvvntgtadt
      961 pvytpnttav tpesyyrqfy drnheennvy dasylklrqf sigysfaldk gavgflkega
     1021 dfnisligrn lfaisdishf dpeqlavqgq glvsgvedls yatsrsfglk iginf
//
LOCUS       WP_103865042             549 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            I32.4].
ACCESSION   WP_103865042
VERSION     WP_103865042.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. I32.4
  ORGANISM  Aquimarina sp. I32.4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Aquimarina sp. I32.4"
                     /db_xref="taxon:2053903"
     Protein         1..549
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=59339
     Region          26..>544
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknklkylff vftfmsfsst iiaqeikvtg kvtdgnglll pgvniiiknt ttgtqtdfdg
       61 nysltlssge tlvfsyigme tqsiiapssg tydvimqens neleeivvtg yskqsvrnit
      121 gsvavikaed laattpvdle qslqglasgv tvgseggpgg ramvrirgfg tinnndplyv
      181 idgtptttgi nqlnpsdies mqilkdassa aiygfraang vilittkggk ynsktkftfn
      241 tsigidniak snfpdllspq esanviwarf nndgvapahp qygtgntpil pnyltpagad
      301 sadlstydat tnkitranka gtdwfdeyfn dafvqnynlg vsggsenakf hvgmgalkqe
      361 gvalhtsynr ytlransefk vtntfriges fnlsysdkvg sagnqstagd isflyraqpi
      421 ipvydiagny agpqspglgn ginpvasatr nrnnltrryr tignvyaeld flkdftfktn
      481 mgvdydntns sfftflnpev aepntvnrlr ednfytisst wyntlsyskn ignhsfdavl
      541 gteahkins
//
LOCUS       WP_103865041             511 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            I32.4].
ACCESSION   WP_103865041
VERSION     WP_103865041.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. I32.4
  ORGANISM  Aquimarina sp. I32.4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Aquimarina sp. I32.4"
                     /db_xref="taxon:2053903"
     Protein         1..511
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=57779
     Region          <12..510
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnrstqnkf lrasrtsfli dnldyryidr geqtrdnrgy ggksayfssf gkldysyndk
       61 yllsfslrrd atskfarnnr sdyfpsysaa wrvsnegfmk nisfisdlki kagygelgne
      121 sipqgrifsq yindddrnyd lrgsnsviss gyslyiignp dlewettttk nigidaalfn
      181 nkltlgfeyy nsltenlliq dqaditlign aqakyinags venkgfdfsl gyqdqindnl
      241 kyyatvnvss ykntvkelsd npdhfltgnl aretrpsrtq agqpiasfhg fiidgiiqne
      301 aernatgdyl gkdigtfkyr dinndgvind ddrdfigsph pdftysanmg leyknfdftv
      361 ffqgsqgndi ynftkfftdf nsfpggksrd ylnswsptnt ggklpqlsnn paehyssass
      421 yyiedgsylr lkniqlgynl pesvlsklni tklrffiqak nlytwtkysg ldpeinlqqy
      481 gggdsvnldi gidrgaypva rtfimgvnlt l
//
LOCUS       WP_103865046            1256 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            I32.4].
ACCESSION   WP_103865046
VERSION     WP_103865046.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. I32.4
  ORGANISM  Aquimarina sp. I32.4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1256)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1256)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1256)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1256
                     /organism="Aquimarina sp. I32.4"
                     /db_xref="taxon:2053903"
     Protein         1..1256
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=143175
     Region          165..1255
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkpkvtfg ykklpinqpl vmkltisfff fsilqvfayd sysqnivtld aknislihvl
       61 sdiekqtdfl fvynhntiek hkvsikvkne klehvlflll knkgikykki kkqlvfysak
      121 edlntllkkl eytkentskd kntsayhtis atikkpiiqk kkivgkvltk nntplpgvsv
      181 iikgtkkgvt tdfdgvfsit lqqdqnilif sylgfetkev dtsnskyvti ilsestnale
      241 evvvtgyqki spervtgafh kvtsksldrk isptnslite legqltgfqq nldhdnpdra
      301 flirgvssll grnsplfiid gfpmeassid alnsnhiesv tvlkdagaas iygkqasngv
      361 ivivtkkgke gkgkfnyqss isitprpdls ylnyadtkth ielekltidq fiqpyieqgi
      421 pidreratrf gltspvhvtt lnqaqglitt tqlenqlanw kkidntqqfe elfyknqyst
      481 qhdfsfsggs ntsnylaafn yvkselntle ndaenyrfsf ngnhqlsnrt qirlianytk
      541 nsrkylninl snltsirpye lfadshknpl sisgieytna sinrdgripd diatnlfdlt
      601 ykpledvyet vntsnnnifr vqgglnykin dylnidlggv yeksnatfdt yysedsydmr
      661 lyfnafaeyk ndqltfhlpt tggrltqnsn dsdhyttrvq lnynytlfdk hningligte
      721 ireirrtdrv nslfgydpet ntsgivdfkr lfingieysa ilpeyytsvn ttfdelyarw
      781 rigdifsynq lfsnnksivr ntslfgnlsy tyhkryslts siridndnvi sqspkfknlp
      841 vwhigglwni hnesffnvdw vnnlkiryty gltanaspls ngagiflqgf rgtsiiynqk
      901 ptfditspin adlrfeftkn hnlgidfslf nnkisasldl ykknterlfg ngqidptkgf
      961 snvllnngii snkgfeitmn ttnittnnfs wntslvfshn kntvekvdhi estfhsrqir
     1021 nmvngrvpve gypadaifsy qfagldsndg filikdqdgl dyknfyfsph dgynindkel
     1081 tkdaltysgt lipiyngsit nrlryknldl sfmfvyrggn kfrgeyldrr ggnlrydrst
     1141 esawrnpgde antnitsihn rdylniptgv fadinihdad fiklrevils yqlnheflkk
     1201 tpftgvgfsi qgrnlwywaa ndigidpeaf stqrsgpgrr llpieptytf ginitf
//
LOCUS       WP_103866005             975 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            I32.4].
ACCESSION   WP_103866005
VERSION     WP_103866005.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. I32.4
  ORGANISM  Aquimarina sp. I32.4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 975)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 975)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 975)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Aquimarina sp. I32.4"
                     /db_xref="taxon:2053903"
     Protein         1..975
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107987
     Region          24..972
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktftksalf llwflpmsff aqsvvegtit dagnghpipg vniivkestn gtssdfdgay
       61 slsnintgdi ivfsyvgfva qeipyngqts ldialeedaa eleqvvvvgy gssrkkdltg
      121 svalitakdf ntgnnitaen lfngkiagvs intnggpaas seirirggas lnasndpliv
      181 idglplndsg dlangsrsil sainpndies fsilkdasaa aiygnrgang viiittkkgk
      241 kklqislnsk tsvtranetv dvfsadeyra fiaknlparv aqlgttntdw qdeiyrtafs
      301 tdhnlsvsgs lmdalptris igradqeglr ktskferttt slslnpklfd nhlkidvnan
      361 lnfeknrfap gvegsaitfd ptqpvfdvns pydgffeyrd attgfasgnv qrnplaellq
      421 treianvrry fgnikldyql hffpdlraiv nlglddsetd rfkeistqsa lgfnttqgef
      481 lgsktdtdll iknrlldayl tytktlgrls ieatggysyq kfdfdrfetg nqrdpgsape
      541 rtidpdqvll ayfartnlky ndkyflsasi rrdgtsrfgk nnrwgyfpsa sfgwqiseed
      601 flknstvlsn lklrlgygit gqqdinqaya yleryrrssp ltqyildgnv inivqpqfrn
      661 eniewekite ynigldygff knrisgaidv frkesddlls eapipdaanf snqgfqnigk
      721 fttqgiefsi naniiqksdf nwnvsynaty idreignlaf nqdilttdid ggtgntiqiq
      781 rqgeapysff tyaqiyddqg npiegayadl nndgiinnnd ryisgkgtpd fimglqsnln
      841 yknfdfsfsm rsniggeiyn nvnsknaqlg nafrtvfsnt pssivntnfq ntpdvilsdy
      901 yiedasflrm dnitlgytlt nimkgvsslr lwtgvqnafi itdysgldpe iqnngvdkti
      961 fprgrtllfg lnyky
//
LOCUS       WP_103866577            1108 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            I32.4].
ACCESSION   WP_103866577
VERSION     WP_103866577.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. I32.4
  ORGANISM  Aquimarina sp. I32.4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Aquimarina sp. I32.4"
                     /db_xref="taxon:2053903"
     Protein         1..1108
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120886
     Region          27..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklltqklli llcvlvtqla iaqegpiagk vtddsgmplp gvniivkgtn ngaqtdfdgi
       61 yslnassgst llftylgfad keiivgtqkk idvqlevaas qldeivvtal gisrdkkslg
      121 yatqevdged lnkvktanfv nslsgkasgv qikrnnnlgg stnvvirgna sltgsnqalf
      181 vidgipinnt ntnskiqgqa rggqydygna asdinpedie sinvlkgaaa salygsraan
      241 gvimittkkg gkstgmgvti nsgltfgsid kstfakyqkq ygagygpyyg pnedsyldlk
      301 didndgtldf vtpltedasy gaafdpnimv yqwdafdpds pnyrtptpwv nakngpitff
      361 etpititnsi sldkgfdkgs yrlnytqfdq tglmpnssik khnfsmsgni kltdkltatg
      421 yanyiktdgl grnstgyndn iignfkqwwq tnvdikqqkd iyfatrrnvt wnpantdigs
      481 lpiywdnpyw arhenfqtds rnrflgnisl nykvtdwfdi tgrvatdtys elqeerrang
      541 svatafgvns gggdtdnrgt vnsgyarkdl rntetnydlm fnfykdlsde fsikgilgtn
      601 vrrnhfqsih astsgglsvp klyslqnsag plplpverde klgvdgiyas aslgyketyf
      661 ldatirrdhs sslpkgnntf yypsvagsfv fsnlidadfi sfgkiranya evgnsapfdf
      721 lydsyvvntp iggastsvgn vkknpdlkpe nttsmelgle vkllqnrlgf dvayyknnsi
      781 dqifgvpitr aagfsskiln ageienkgie islygtpiet tnfswnvnvn wsknenkvvs
      841 ledgienlql gsfqggitin aqvgkpygii qgtdytylng ervvdgretl pqdedgdgqd
      901 dpnpaqgqyv ktstsnnnig dtnpdwlmgi snsftyknls fsflidiqkg gsifsldqyy
      961 gqatglyeet afindlrnpv rnsladgggf inqgvntdgs vnttriradr fgafgyrrgl
     1021 pdaafvydas fvklrevslt ysfpkqlikk tflndvsfsv igsnlwiidk nlphadpesg
     1081 lssgnlqgys vgslpttrdi gfnlklqf
//
LOCUS       WP_103867433            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            I32.4].
ACCESSION   WP_103867433
VERSION     WP_103867433.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. I32.4
  ORGANISM  Aquimarina sp. I32.4
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Aquimarina sp. I32.4"
                     /db_xref="taxon:2053903"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116975
     Region          24..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntiskltlg lllllsltkl taqinisgkv tdinneplpf anvlikgklk gattdnngnf
       61 tlnnvkkkdi lkvsmlgfkn ftvpisktvf fkivlredsq ileevvvtgv avgtpvkklp
      121 falskvnnre lkevpgrdlg nslrgkvagi tivqpngdpn avssirlrgs nsllrsqepl
      181 iiidgiitgs dmnlkdinme dvesveiikg aagssmygsl sgngviqiit krgknsggkp
      241 tivvrnetgf sqiakaypla nthryklrda ndfpwnlndl neqgrwhlsn ggirdydedg
      301 lldnpfpril dhqkkiyttq pysslytsis sgnenfkyha sfqntkngga iqgvkpsvrn
      361 narlnidylp ndkiaiktsv syaktkghna pfstretalf lepwvditer dlngdivptp
      421 kgsyylrnfl dnplyevgil edyfdrqrlm fspsitydin dnlqlgasys hdesrsetys
      481 ytpkeykfpd ptltnvgdyg ivsnisksdi vqlyasyakk ignfntrfta kflrenrnvn
      541 sfnakgfqll vsgvrnlsyt egssriigsi qseekvsnyf fdfnldykdk iifnglirkd
      601 gsslfgkdnr watfgrlsaa yivtkdfnip kvddlklrfs wgtsgqrpaf ntqyetyrst
      661 wrgtlrpdis gnknllpsrv seweaginar lfdrvnlevn yaktqvkddf lkvplpratg
      721 fkeqwqnlgs iassalevql gldiiknknf swnanlnwsk itqeitdlgg vepfsrssrl
      781 frveegkpyg lmygykvatn vneltldnng fvinslgnpn inergtlkpe dfeinehgyv
      841 iikgtkgsak eqvillsdet gedekmeign tnpdwnlgft snfsyknfnl yfvidhqqgg
      901 diynstkqrl yraerhgdqe kfakqgkhil ysgissnldr glsdtshfve dgtftkvrel
      961 slgytlgknv lgpkaskiik elkisligrn lftftnysgf dpevaygsgl pegsltakvs
     1021 nptndrldlr sypqsrtfta mvqltf
//
LOCUS       WP_103873517             394 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Allobosea
            lathyri].
ACCESSION   WP_103873517
VERSION     WP_103873517.1
KEYWORDS    RefSeq.
SOURCE      Allobosea lathyri
  ORGANISM  Allobosea lathyri
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Allobosea lathyri"
                     /db_xref="taxon:1036778"
     Protein         1..394
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40481
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaetq gaetrvaatp etvrkfiglg aevavekgag laagindady vaagatvtkt
       61 akealkgaai vlkvrrpaes eiaglpagal vigimdpygn eaalealska nvaafamefm
      121 pritraqvmd vlssqanlag yravvdgaae ygralpmmmt aagtvpaari fimgvgvagl
      181 qaiatarrmg aivtatdvrp atkeqveslg akflavedde fkqaqtaggy akemskeyqa
      241 kqaeltashi akqdivitta lipgrpapkl isaamvesmk pgsvivdlav erggncelak
      301 pgevavtpng vkivghlnvp grlaatssal yaknlfafve tlidktsksl avnwddelvk
      361 ataltrdgav ihpnfaakpv vapapvaegs vqng
//
LOCUS       WP_103893209             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_103893209
VERSION     WP_103893209.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53630
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtemdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_103887919             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinacidiphila yanglinensis].
ACCESSION   WP_103887919
VERSION     WP_103887919.1
KEYWORDS    RefSeq.
SOURCE      Actinacidiphila yanglinensis
  ORGANISM  Actinacidiphila yanglinensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Actinacidiphila.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Actinacidiphila yanglinensis"
                     /db_xref="taxon:310779"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53161
     Region          16..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msqsaqpvgv vgvvsesqpg esrvaatpat vkqlralgyq vvvetgaghg aslsdeafee
       61 agarigdrvq vwgadvvlav napsdeeial lsdgavlval lapatrpdlv dalaerpvta
      121 lamdavpris raqsldvlss maniagyrav veaahlfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aagsmgavvr atdprpevad qvrslggefl svesaeaqvs atgyakemsd
      241 dyntraaaly aqqaadvdii ittalipgrp aplliteemv asmrpgsvvv dmaavqggnv
      301 agtvagevvv tanqvsiigy tdlagrlpaq asqlygtnlv nlmklltpek dgrlvldfdd
      361 vvqrsvtvvr ggektwpppp vqvsaapapt aaappptpvt kekrpitpgr rytavgaaaa
      421 vlfvlagfap aqlignltvf vlaivigyyv ighvhhalht plmsvtnais giivvgallq
      481 ighahtavtv lsfvaillas inifggfavt rrmlgmfskd
//
LOCUS       WP_103901548             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chromobacterium alticapitis].
ACCESSION   WP_103901548
VERSION     WP_103901548.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium alticapitis
  ORGANISM  Chromobacterium alticapitis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Chromobacterium alticapitis"
                     /db_xref="taxon:2073169"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39971
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhiaipaerl agehrvaatp etvkklvaag havsvqagag laaaipdaay rdagasvvda
       61 rqpllanadi tlcvrqpead diaslkpgst ligmlspyhn pllpqlaarg vsafalellp
      121 rttraqsmdv lssqnniagy kavllacqfy prfmpmlmta agtvkaaral vlgvgvaglq
      181 aiatakrlga vveaydvrpa treqveslga kfvempmsee ekaassgvya remtpeflar
      241 qnellaaraa aadivittal ipgkpaprll saaavagmkp gsvivdlaae aggnceltra
      301 gearlsdngv hlvgltnlpa mlaadassly arnlltflgl llapeglkld ldddivaatl
      361 vahqgeqrfg asakpaaaaq tdkephhg
//
LOCUS       WP_103904902            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103904902
VERSION     WP_103904902.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112434
     Region          26..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskfyskccs ltvvmllcis tlfaqqtvtg rvtgengdal pgvsvtvvgt nraaqtnaqg
       61 sysiqanngd kirfssvgfa sqvinvsgtt hnvslaedag nidevvvtam gikrerkslg
      121 ysfqevkseq ladakennva nalvgkvagl qvikgsagpa sstkitlrgn nsltgdnqpl
      181 iivdgvpmnn flgakgsngq vnndfwnpgt dmgnglgdin pediesmsvl ksgaasalyg
      241 sragngaivi ttksgkaqkg tgitysstlg fetlfmipei qsefgqgkdg vfdavstdnw
      301 gaaidgstyq aydninnffn tglnhtqnvs fqqqvgestn vyssatylnd kskipgssls
      361 rlnlmskvst sfgpnkrwst evkvqymnnd atnrpisgqn nsnafatlfr mprtinildy
      421 knpvnnlnkm nwygtsnsin pywlaeynln ndvrnrflsn anikykitew ldvegragld
      481 tytsrlenkt yggsplspsg lystgktefa eknftlglha rqdainggkw gvsgsvfgqi
      541 mrsdetylgv gvgelevpny fnvtngkgnp tpsqyndrkq inslygtgel sydgywflnv
      601 tarndwssal skvnrsyfyp svstslvisd mirksggemp sfinflkvra syaiagndmk
      661 ayrlinqyei nrdpngntta glgdvrfnen vrseliksle vgfdtrmfdn rfgidfawyk
      721 nnathqllei ptdpmsgfka eninagniqn sgieialdgq ilrsenglnw nssvnfsknv
      781 nkiielsdki dyytlggfdn iavraienql ygqiigskfl rvddqnspyy gqmilngngl
      841 pqavdgqvlg nqspkalvgw tnsfnyknvg lsfqidgrfg geffsgtnvn lqangtaaet
      901 vvngkrdnfv vsgvvangds ytqntkevtp qqywtqvats gnmgigeani ydatnirlrn
      961 itlsynlpas vlkskvlqra riaftmnnvw miksyakgvd pesvfsinsn atgfenfatp
     1021 tsrsyfinlt lgf
//
LOCUS       WP_103904999            1156 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103904999
VERSION     WP_103904999.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1156)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1156)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1156)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1156
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1156
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126622
     Region          46..1155
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrlllfsla lgltmptyas fsgstgnsal gnyagwtkas svlqntvtgt vsgpdgpiag
       61 atvsvigtsv ktatddagkf tinaavgskl risfvgyest evtvtgstvn vtlqsssdvl
      121 devvvvgyga qrkgnltgav stisvkdnle grpiadigrg iqgttpgltv tvpsgevgsd
      181 ptikirgava slqaagnpli lldnveipsi qyvnpddies itvlkdaasa siygakaafg
      241 vilittktgs kgeklditys nnfsfqnpyk qyemgginal kytkdamerv gsnisgafyy
      301 vtpegyelak qwhdtygnsi gkddptvygr dwivdptnas rkiglrtydp ydymvrewap
      361 titnnaafng tvgktkftat fghiaqsgml kagdsdkfkr snaavrlstd vndyltlrag
      421 amfsqrkkly pyatnsttad pwyymyrwss vypmgndehg npirspwsey easneasmkr
      481 nyinlnagat vkmtknwsld vdynftnedy dwfrpgtrft aanswiapvl rldaqgnqvy
      541 vdntgavvsa gapgampayd llnqmytspg snpdhvyara ayeykhtlna fstynlnlen
      601 ghdfkfmvgs nlvsdygkyn wtqktnlldi tnpqfdlasg tvtgsggtfw tsqvgffgrv
      661 nyayknkylf eanarydgss kfvdeliwrw ftsasagwvv seenfmewak palshlkfrg
      721 sygvignqav ppslytpnmf pfettwiggs nkyyavptpt fslrdiswed letidvgvda
      781 rflnnklgfv fdyyvrntnh mftgfqgttw tiggsapqgn fgtlktkgye vavdfnhrfe
      841 nglginaran fddavsrfyn vttsrltgsy ydgsaygdiw gyetdrlyqm ddfnlgadgk
      901 pvlvnltedm tkyygrgdgk ayqlkdpngv yqpflestnt fnfgpgdvkf kdlngdgeid
      961 ngdgtvdnpg drkiignstp rynyglrlga dfkgfdfsif lqgtgqraiw gsgalaipgf
     1021 ntadgampat fvddywtaen tgafypaafn nagsndannm qvqsrylldl sytriknitl
     1081 gyvfpksfia paklsnvriy valenfftwd nlnglpidpe vvsgfsmfne dnyngsrtgv
     1141 gtptfksasf glqlnf
//
LOCUS       WP_103905227            1167 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103905227
VERSION     WP_103905227.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1167)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1167)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1167)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1167
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1167
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131666
     Region          81..1166
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myfylnlkry mqllgrlnqe apkslkwili lfllllysal lqakskshhk frtdehhdph
       61 trhgsvsdst rtattpvqli vkghvknssg qplsaatvvv kgtprsvstd rngnfeiqas
      121 gtetliirfv gfrtqeipig grseitvima ledkaieavd vvatgfqnid rriftgaatq
      181 vkaedaqrfg vpdvsrmleg qvagvsmqnv sgtfgaapki rvrgatsitg dnkplwvidg
      241 iiiedvvnis ndqlstgdan tllgssvagi npddiesfei lkdaaatsly garamngvii
      301 ittkkgkagt qsvsylnnmt sylrpsytqf dilnsydqms iyaelarkga idyalirnnm
      361 nsgifgnlsr alttwredgt plvqnthegr eeflsryvrq ntdwfntlfn nslmqehsls
      421 fsngtdkvqt yystsflqdn gwaksngvrr ytanirgnyn isdkltlgll ttgsirdqra
      481 pgtlgqdsnp itgvvsrdfd inpfsyamnt srviapyden gnhefvtmny apfnilhele
      541 rnymdlkmld lkvqgeinyk lpknirynfi gayryastgn ehkiyensnl anayragtny
      601 dvtgnesavi adanrflyrn lnnlearptt alpyggfyit senglksfyl rnslnwdlht
      661 dkhyftafgi qeiryldrms kesigygyqf ekggvpfidp rmftrnvesn fpyfkmnvfq
      721 drfvafasnl tysydgryqf sgtyrydgsn qlgrsrvarw lptwnlsgsw nidqeafmkd
      781 qqffnslalr gtygltasmg patnaslvlr snsvnrprlt dqepvirley lenkdltwek
      841 qyetniglda tflnrryqvv ldfynreafd ligplfisgi ggehmkfany anmrtrglev
      901 llkasifdse nwkwkvqltn afnrtritdl rnepniwnlv nsvgaakegf phrslfsidf
      961 vrlndelgtp lyvnqsgdvs dniflqsiqt dylnyegpvd ptinggffnn ftyknlqlgv
     1021 lvtysagnkv rlnpiyrnyy seldamshdf inrftlpyea lspsiptart nsrltgdqvy
     1081 naynytseri adggfirmkq itlgynlptk flqgtglkni slnlvannlf liyadprlng
     1141 qdpefyssgg valpmprqft fslkvgl
//
LOCUS       WP_103905430            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103905430
VERSION     WP_103905430.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113533
     Region          2..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msgrvtsssd gaplsgvsva vvgtsvatqt dgeggyslav penatlnfsy vgydsqripv
       61 gtqttinval vansesleev vvtalgvqrt rkslgysvqq vkgddltqak qvdlntalag
      121 kvsgvqirsg sgakfgtssl rirgvnnltg gnpiyvvdgv itspelvnnd dvenltvlkg
      181 paatalygqr gsegavvitt rrgkvsegig vevnqatsfe nvyglpkyqn eygggynktw
      241 qifeydparh peylkqmdgv kyynygades wgprmdgtmh apwyswdpth pkfgqlapfd
      301 pqpdnvknff etgstlntnv aiskaadnyn trvsytnlsr hgvmpntkqn khflgasagv
      361 dlsdkltvst nlnfiyedrf ntpidgyssg pqssfnqwfa rninmddlrd yqrpdgtyrs
      421 wnmtsptnsn paywnnpfve myknirgnln rtfygnvtas ykfneewkat avargnfags
      481 dqhsriasrt lsvaeyyqyq rtaqetnfvg sidytkqled fnisaaiyge trnnkiryte
      541 grtqgglavp dlytlsaskn rpltnsyvsd ykvnslfgyv tlgyrdflfl egnlrndwss
      601 slpdgqnsyl yggvsgsfif teflktdwls ygkvrasfak vgtdtdpyrv mqtyllnspy
      661 gsnplltvpn qipnaalkpt lstsievgte lrflndrltf dynyytrsak dqiipmtitg
      721 atgystqlin agqidnwghe fslggtpvrn dnvtwtmsan iginrnevve lyedpetgmr
      781 vsnlrvtvdg tqsnfgfvga piislnareg etfgmltgsg ytrnekgekv vgadgyyips
      841 asdvdlgtil pdftggfttn vnykgfnagf sldfqkggky msissmfgsg sglfeetagl
      901 ndkgnpkrdp vedgggvvle gvkedgtpnd iyvdvqelyr dklnsgsiwe hwvydasyvk
      961 lrevsigytf pdrifgktpf kkvslnliaq npwliyaknk nfdpsilegs wfeggqlpnv
     1021 rsfgfnlrfs l
//
LOCUS       WP_103905483             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103905483
VERSION     WP_103905483.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108986
     Region          24..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqklfsflf tclllisvsy gqdfqvsgrv tsqadgnpia nvtvrvqgkn lssqtdadgs
       61 ytiraaegnv ivfrslgyke rsitvekmst iniqleaeeg sidevlvvgy gsgnnigsvv
      121 gsqvtvrakd iagkpapnai ealqgkvpgl svmtsngeps ttqsirlhgs gslgasstpl
      181 fvidgipvgs gsilstnpdd wesitvlkda satsiygsra angviyfksk kgkaserati
      241 tasamkgynn latknmmdqm mnskelqayw letgfrtqaq ideinqtfgh netvwgdyyy
      301 kkntgldqyn lnisggsekm qyyissayyd qegimyrsnf drvtlrsnls atlndwikag
      361 lnlsggydkr msnpyggnsl ngalslmalp wyspfdengn eyyeeripgl dayspkylad
      421 knlnegvnkq fnptiflqvq pykgltlkst agmdyfdyri salrlpsylg nlnngsasee
      481 yqtgilktit ntidyrtlih nvhdismmig qeatdydess fsasgsgltd drltllgqti
      541 angrgvgssk seyaynsyfg rlgysynaky lldlslrtda ssrfgknnrk atfwaagvsw
      601 kaksekflqd vswltdltik asigtqgnsa ignyqslatv gsinydgapg wgvsspgnpn
      661 laweqqtktt lgvrasflnq inldvevykr vtdnmlvsvp ypytsgfssi tsnvgslenk
      721 gidvqfsana frsekfyftp yvnfnynqqk itelfqdkey wivpntglsw avgkpvefff
      781 pvqagvnpdn glmqwyvpge nisdsnfdpn nvtttfnavd lqqstglrrd apftggfgft
      841 sgyngfyldm dfafvkgkym inndlyffsn pyqfrgynqi rgvrdywkep gdqtrypkfg
      901 qvhqfdtgll edasflrlkg lrfgynipkk llsgqkffks asvyyvgrnl wtktkylgpd
      961 pevdsnlalg vnpntkqssl giqlqf
//
LOCUS       WP_103905721            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103905721
VERSION     WP_103905721.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115293
     Region          26..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkllcfiv afvcligqsi aqtqnvsgtv tssadgqpls gvsvrvvgtt naaqtdgsgk
       61 ytlsnvaags tlsfsyigft sqtvtlgnsn tinielsqag ealdevvvva ygtakksevt
      121 gsmatmgaed lekrtvtnvs nalagmapgi svssgngqpg sgasirlrgi gsmsassspl
      181 yvvdgavfdg nigdinsddi esisilkdat saalygsrag ngvimittkk grgatrfnvg
      241 ltqgitqrgi eeyetvgind yyptvfqaik hsrmfptsgt pateedanry avdnikrlla
      301 ynpfnvadne vvdlngvmnp naslkyndfd wfdaiqrvgk rtnanvnlsg sndktdyyvs
      361 lgylndegyi lnsdlqrfng rmnvnsqikd wlkagvnisg tmsegsmasd aatgnaasyv
      421 npfsfirglg siypvhafda ttgapvinev tgehyydygm hpgavnrpsg aspgrhviye
      481 tilntnynkr avlggrafve ikflkdftft psvsvdltnr nrdyswnnrv gdgvsynglg
      541 sfqnditksy tfnqvlqyrk sfdlhnltal aghenydyef strnttktgq itsgiteldn
      601 yvtplssggy knvnrlesyf gkasynydqk yyadasfrmd gssifdnekr wgkffsvgaa
      661 wainkeafla daswindlrl kasygqvgnn nlldvngnri yygyqalynl gwsngglpgt
      721 ilsslpnpnl twessntfnv gvnfaflnnr lrgemefykr gsdqlllsvp ralssavsse
      781 fmnvgsmynt gfelslsgdi vrnenftwtm tknittfkne itkmpvenpv itsgnkrrev
      841 grdyysfwlr eyagvdatdg sslytpadna pasalrtvdg kqyvtnqnfa kfvysgtsip
      901 dlmgsimnsf sykdfslsfl lnyqiggqiy dsqyaslmst naygksyhvd amnawttsnt
      961 gstiprldqa nnaninaast rwlidasyls itnvnfqykl ptslvnkidl ssarvfftge
     1021 nlalfskrtg mnptegfdgs vsttylptri fslginvgf
//
LOCUS       WP_103905827            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103905827
VERSION     WP_103905827.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115110
     Region          25..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlptcltia laslcslqvl naqqisvagk itnadgapiv gasvfikgtq qgtssnelgl
       61 ftlnvpanst lliravgyan qevavnnrnn lsiqlqeeds nieevvvtal giqrsekslg
      121 ygaqsvssea lnankqpnlv nalqgkvsgv tisstggapg qganiqirgi nsidptrpgq
      181 plfvidgilm dnststqgdg aelrgmsnra vdinpddiet inilkggaat alyglrgang
      241 vvmittksgk agtlkidyqg tygfenvnkf pkmqdtysqg wagvynkddf wpafgptvee
      301 aikldpthps alyksfedaf etgnqsrnsl sftggtekfn flsslsqlnq qgvlpstdfk
      361 nyqarintnf tiseklkggs sisvnnsggy rgnagryaeq liywsprhdi rdyleengtm
      421 ksygdtnnpi yvaesnrfkd dvlrliggvn ltysptkwld fmyrlgvdty rdnregtalg
      481 fqglsgerli sengvpgaeg qgfynvynqn frginstfia tlkhefnedf kgslrlgqdv
      541 ydqvikrssa eggkltvynw fdlsnasivk trsylekyrl mglfgelals yrdylfltit
      601 grnditstle kgnrsffyps atlsyvfsdh melpesisfg klrfsyaqig kdalpystsg
      661 glgpytnlpt gyigftrpel lgdkalkpef tdtyeagiem kfldsrlgvd lnlytstskd
      721 qiirvpvtsa tgyataaina gsirnrglei tlntvpiqre gfrwssdlnf slnrgkvlsl
      781 redlteitva seygylssnv ymklipgesy gtlygrtfkr yysaseieqg ldktpeldkd
      841 rplligangf pvlestalpk klgnvqpdwi agwnntfnyk dfslnflvda rvgqsrynql
      901 gnfmssfgla dytedrndhk vfagktadgn dntkevwlgq gvdpktgtdy gngfyrnyhr
      961 gnseffveda sfvrlrsvsv gynipnslla dkfiknaris vignnlalwt kysgydpess
     1021 ttasgsnieg fagmtypavr sflfslnlgf
//
LOCUS       WP_103905891            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103905891
VERSION     WP_103905891.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124038
     Region          32..1110
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpkelltrg hgswlllllf lfnlqlafaq tftikgrvld eegkpvagat vsvqdsdrkv
       61 lsdakglftl vadkgsmlri talgfttkrv evnqtemnvr leeetnvlde vvvtamgikr
      121 etkklgyavq evkgdevnkv rdanplnama gkvagltiga stemlgrpei vlrgskdllf
      181 vvdgvpinsd twnispddie sysilkgpna aalygsrgin gaivittkrg kgsefsgnnw
      241 rvdfnstnqm ensfivlpes qseygrgtrf mysygdklyd ndqrlptwgp rfegqliqqy
      301 dspwdaekkk rsatpwvsrg aknyenfvqt gllstnnlsf akagddfdmr vsyshtyqkg
      361 iypntklnad nfsltsgfdi ndkfrvegnl nlnlqytpni pdvsygpnsy aylfrvygsa
      421 dfdvrdlkdi ykgpqgvkdq mqyaheygrv nspwfmakew lrrhdktdiy gnlnlsykfn
      481 ddlkllartq ittwnqlrse kvppstnlng yvqwysfgwf gdyredqrrl fennsdltln
      541 ynkdlgnwsi salgglatrm fnfhsnwttt rglvipklys fsnsqspvle ynytanmmvy
      601 sgfysfdigy knyfnlnstg rvdklstlpd nnntffypsl slstvvndyi nmpnaidmlk
      661 frasvaevkg gltsptvksa itaitgvdlt spgrgvlgyg qdlqtvydgp syanqnaytv
      721 fsyyggmpav dfsstianqn lkpynrlsye fgmdlrmlkg rigldatyfr tvngpqiyal
      781 nvapstsyss rningittln qgleislnan pikkqdfnwd isanwstfre tlkeiyaged
      841 vltmnghnfv vgerldaiyg rklardgqgn vihnggllyp tpsgigqnal lghlnpdftf
      901 ginnnfrykn vslgfqfdgr vggsifdfay aqamnagtai etvqgamgea rrkeweslrd
      961 ngkitphyig egvkivsgtp ifeggeiknl delkfapndv pvalqsyitg sngllgstey
     1021 fmidrsfakl revsigytlp qkflrkgfir sasislvgrn llyfaqrkdm dldsyasgfn
     1081 ssdrrasgsk gtvglqsavp rrygfnlnls f
//
LOCUS       WP_103906474            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103906474
VERSION     WP_103906474.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123695
     Region          26..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrslfllll llacsfsigi amaqaqevkg rveaagaglr qvtvtvrgtg aqaatdekge
       61 ftvragigst lvfthfgyqt kevtlqnlny ltvtletlde aieqvvvtgi gmqvdkrlft
      121 gattkisgsa teiggnldps rglegrvsgv svsnptgtfg taprlrirga tsiygsskpl
      181 wvvdgmived vadvssdels sgdaltliss avaglnvndi esfqvlkdgs atsiygargm
      241 agvivittkr gavgrstiny taeftsravp rysefnimns qeqmsvykdi ydkgylrmaa
      301 tsnasnsgiy gkmyelintg kmindlnttq vemnkflreg efrntdwfge lfsnniqqnh
      361 aislssgnek sqyyaslsfi ddkgwskrsg vkrytanlna nynilknltl nllangssre
      421 qeapgtvgqs tdvvfgevkr dfeinpysya mntsrtldpn tfytrnfapf nilheldqny
      481 mdvnvnelkf vgdlkwkpie gmqlgafaay rissttqhhy ikdrsnqama hrwapttvir
      541 danpyfyrdp enplavpisi lpeggiynrt dhkisdqvfr lnaqydkvid khrmfaflgg
      601 evtslernnt wfrgwglqyd lgespfssym afkrgqqent pyfymgnsry rqvaaftsli
      661 ytyderytfk vdgryegtnr fgktrrsrwm ptwnvsglwn vhneeffkes qdlishlvlk
      721 asysltgerg pasvtnsrvv igpfnpwrpv stdnesglqi dqpenaqlty ekknelniga
      781 nigmlnnrln vefdyftrnn fdligiintq gtdgftskmg nvaemksngi elaiegriiq
      841 sdnfswlsrl nyshfntevt klktrsrmid litgtgfare gaperglysi pfvrltdegl
      901 pvfigsdnte tttgiyfqer dlldflkyeg ptnptdiggf sntftyknfs lgalisysfg
      961 nvvrlnpvfr ngysdlvatp kefsnrwmvp gdesqtnvpv ipsrrqnnvy ggdlqyayns
     1021 ynystvrtak gdfirlrdvy ltyslprdmv nrwklnnmsv rlnasnlfli yadkklngqd
     1081 pefvnsggva spiprqftmt lrvgl
//
LOCUS       WP_103906524            1172 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103906524
VERSION     WP_103906524.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1172)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1172)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1172)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1172
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1172
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127183
     Region          <70..129
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cl21470"
                     /db_xref="CDD:473874"
     Region          <108..221
                     /region_name="PRK10856"
                     /note="cytoskeleton protein RodZ"
                     /db_xref="CDD:236776"
     Region          187..1171
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmhylyrtlf itcafmlfsq igtadpirks nptplhvlta hstaldslei vgkitdsvgt
       61 avagvvvtek gttnsalsne ngeykisasp ngilvflksg fatkeehvnn qkqldiqltv
      121 ataateaqeq qenaagtdst atavdstatt pdstavvpds tqqtgtvppt ttaqdsagta
      181 pvptgqqvvs gtvtgpsgpl pgvtvrvvgt dlaantdeng kfqiaagpkn rlrfssvgfk
      241 tvtqavgtrk diqvvlatet ntiesvqvva vgygtmkrat lptavssiga neienevlps
      301 vtqaiqgkag gvqvtqksgs pgggisirvr gttsinassd plyvvdgipv nsatnftggs
      361 tfdfgggtqg inilsslnps dvqsievlkd aasssiygsr aangvvlitt kkgaagqsqf
      421 nfnmyegfsq vpkeryydfm nteqyqdymr dyydilkkek petvvpeqif snpgvstdwq
      481 daifrtsptr syelsasggs dktqyytsvg ymrqggvlly sdfdrlsgrl nlnhqhnekl
      541 rfstsmnitr atnkrvqeen skqgatkngi fappnlavfd gngnyvydnv slvrenpvam
      601 lelpvneant yrilanasae yniipslllk tsfgtdlsfi detffmpptg lrsytgqggi
      661 gasrstrdql winettltfd ktfgdhylna lggfsvqgsr lefthaqran fpnndipyiv
      721 aggvitgana ypeewaiasg faratyvykd ryilnanirt dgssrfgadn rwavfpslag
      781 awriseedfl kenktfsdlk lraswgitgn qnignyaars lysggynymg gagfvpnvlg
      841 drglkwettr qwnvgvdagf fndrisllad yyykktsdll iglpilqssg fvnrftnsgt
      901 ienkgfefei tsrnlvgefr wstslnmtfn rnkvldlpeg ltemrggvgd lnraipgqpl
      961 gvfygwqaag vnpetgminy igkngdmvrp nsmedhvmig dpnpdffggi tnnfeyknfd
     1021 lsvlgqftyg ndifnynlas glegfnpssn afvdfvdrwk kpgditdvpr papgnldnga
     1081 vssrfvedgs ffrlrnitlg ytlpegvaer ikmkrlrfyv tvqnayvftk yrgydpevss
     1141 shggantgli ygydygsypq prifttginl tf
//
LOCUS       WP_103907074            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103907074
VERSION     WP_103907074.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118442
     Region          43..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myrsskklsk vgillimgma mqgtatgsvp yypvethvvq eqinvritvk dqetgtalsg
       61 vnmlvdgkai gftndsgvfq gtvtkgttir lrmigytqts itveretyav glnsldesid
      121 evvvtalgik reekalgyat ttvkgeqltd amssnwmdal sgkvaglnlm rsnagpvgst
      181 kiilrgesnl tdnnealivv dgvvvnggsg rrsslgsdsp ygtssdnmpv dygsgmddin
      241 pddiesvtvl kgpgaaalyg sraangavii ttktgtkker gigvtinsnt sfesmnrspe
      301 lqyeygqgtg gaahysmgss idggstsgts saygpkfdgq nffqldpttq kvglertpwr
      361 aydgkqgvng ffdvgrtftn svsidgntdk tsarfsatnv qnkwivpntg ykrntfslav
      421 nskvseklti ntkvsynnrw sdnlpgtgyg nqslmywyif wqpsaniewl rdywvkgeeq
      481 rkifypysty penpyaisye finannrhtf tgnaqasyqf tkelslqvra amdfsaenrn
      541 qnrpydagsk laegsfrtqs ifsretnadf llryakklnd dfdfsatvgg atlnneyrrd
      601 dmtsdgltyp giynhgnaky giktqqlner fqtnsfyglf taaykeflfl dftgrmdwts
      661 tlaavkdpdk klnffypsvn asfvisevae mpsfinfakv rasvagtgsg vtkpymtnfa
      721 yqkppnlvgg gnimnptglv npmilplkts syevgmdvrm frkrvnldva lykantfsqh
      781 lnrivdassg vsrylinlge vqnsgveval ntdqikkdsg fnwssmltyt snkneikqla
      841 dssivlqqrs vgsgqivgfv ggslgdlygl gyerapdgqi iydestgyak itkeviylgn
      901 tipkgkmslg nnfsykgirl nvlfdaqwgg vahslthykl aeqgktvntl pgrysglign
      961 gviqnadgsf rpndviatnv deyyrshyga dnaegstfat dflkfrearl dytfnrnvvk
     1021 rlginratig vygrdlfiwt kwpafdpefg tldgsdivkg feiaqfpstr tfgfnlvvgf
//
LOCUS       WP_103907221            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium lactis].
ACCESSION   WP_103907221
VERSION     WP_103907221.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium lactis
  ORGANISM  Sphingobacterium lactis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Sphingobacterium lactis"
                     /db_xref="taxon:797291"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117500
     Region          27..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrtiylylv glffalsttt vqaqhlirgk vlnedgqpvs gatvtdvask kqtqtnasge
       61 fsfdlpsaar elavrflgfq dqtkifkage tlnfllvpss dvleevvvta lgisrekkal
      121 gyavqevkaa elqtrptnam aalsgkvagl qvvssggnmg gstrtllrgi nsiagnnqpl
      181 yvvdgtpidn sdlnsastvs gsvgkdvgnm iqdlnpddie nisvlkgpsa aalygsrasn
      241 gvilittkka gkgeqvnidv ntglelehiv rlpkrqqlyg qgysqtfqtv dingqsfkiv
      301 dyasdeswgp kldgtpvlhy ynlnpeqadd ylkpspwiyp ehdvhyffqt glantnnlai
      361 sgnsgntnyr fsytnknvrg tvpnaslgrn tlnfsggtkl gklqisstvn yihnnslgkp
      421 wtgasnrnii leafqwgavq vdykrlrdyk redgtplawn rtgwqntpaa eatrfidnpy
      481 wsayesylee krdrfygnig lqyevndwlq vgakvhgdiy qfdskdriav ysrstsyyee
      541 nsnklneyny eflatakknw dkfslvanag anlrnqsrqv nygttqggln vpnyynlkna
      601 nsvkienfky drriaslygs asfgyndlly ldatvrndws stlptdansf iypsftgsfv
      661 fsqlpavqel gwlsfgkvrl gwaqvgndtd pyqlykayev eqsfngrpss klpatlnnat
      721 lkpeitsswe tgvnlqffrn rlgldvtyyh ntsrnqilpi pvsaafgyea kvlnagkven
      781 kgleviltgt pirndnfewn ttlnwstnkn kvlklddlvn tltlssslin lvaregepyg
      841 qllgydfvyt dagervvked gtyqrtsqlv plgsvlpdyl fgfqngfryk nfnlgflieg
      901 rvggsfysqt ysvgmysgil ertaannvre ngvvlegvka dvafnpdgty ttsnirendt
      961 ritaqqwgrn esngpttfsi fdgtfvklre vtlgyqiplk nanlvkrvhv sayarniwni
     1021 ytkskyidpe fanssgnvqg ieaaniptpl tygfnlslkf
//
LOCUS       WP_103912467             911 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Halpernia
            humi].
ACCESSION   WP_103912467
VERSION     WP_103912467.1
KEYWORDS    RefSeq.
SOURCE      Halpernia humi
  ORGANISM  Halpernia humi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group; Halpernia.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Halpernia humi"
                     /db_xref="taxon:493375"
     Protein         1..911
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=99386
     Region          33..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnyntvlkv apaflllgam fsaqttdsig kekkieevvl igygkqkksd ltgsitsits
       61 kdfnggasta aqliqgktpg vqittnsgap gsgsqirvrg tsslsannsp lividgvpqd
      121 faginggadp lslinpndia tfnilkdasa taiygnratn gvilittkrg tsgrlkvdfs
      181 tvasvsekmg nvdvlsaddf rsfvnanasa sykarlgtad tnwqdqiyqq awgtdnnlal
      241 sgglkwlpyr lslgyndqng ivktntfrrt saglnlnptf fdkhlrvdva lkgtytdnrf
      301 adggvinaat yfdptqpvys gnsnyggfye hllngglnvn gtanplstlq airdissvyr
      361 glgniqldyk vhflpdlhin vnagydytkg eghktvdgnl ragyfnggss stysqekknk
      421 lletffnytk diaaistkvd ltggysyqdf etstpstytt lgnppadynp yslasktgyt
      481 lvsfygrgif tiadkyvlsa slrrdgssrf yngttnnlyg tfygfsgawk isdekflkds
      541 kvvsnlklrg gygltgnqei nsgdfpafas ynlsgpgaqy qfggsfynfy rpniynpnlk
      601 wetattknlg ldfgflndri tgsvdiyekd tkdligqviv aagdlsnqni lnignmnnkg
      661 iegsinfvpi knetvrwdlg fnathynpiv tklqeraddt ynipvggisg gvgntiqaha
      721 vgynpysfyv yqqvydangk pldgvyvdrn gdgnitaadk yfyksttpda ilgfntkvsy
      781 knwdlsmsgr avlgnyvynn aasnssiqsa ttndflqnvy ssavnyrfqs pqyfsdifie
      841 nasffrldni nigynfkdil stkgnmrvya maqnvfvitk ysgvdpevfn gidngyyqlp
      901 hvyslgfnfq f
//
LOCUS       WP_103913266             946 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Halpernia
            humi].
ACCESSION   WP_103913266
VERSION     WP_103913266.1
KEYWORDS    RefSeq.
SOURCE      Halpernia humi
  ORGANISM  Halpernia humi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group; Halpernia.
REFERENCE   1  (residues 1 to 946)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 946)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 946)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="Halpernia humi"
                     /db_xref="taxon:493375"
     Protein         1..946
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105193
     Region          32..945
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknicllgl lftsslifaq kskkdsaesr enkideviit ssygtkklke evvgsistit
       61 skeintaqpf esidkmitgl apgvqissgt evganvkini rglgsivaln nsnvgtstqp
      121 liivdgiilk edrpfdatff ngsagseyni nslaristdn iesinilkda aavalygada
      181 angvilittk kgrkgkpqys fstqygisqs inkmkylsgp qyaqvynayq snngvaagfp
      241 yngvdvnwfd imnqngdyyk tnfgvsggak yftyrmginy snnneskvln tfqkkgidts
      301 lgfnfdklki nlfgsytnlv knqpntyfnf ilaptfsvyn ddgtfhstgy ngipnplaaa
      361 nqninltenn svlssinvsy dllknlklss ifavdyshqk dvdwksglng sgrgngtfii
      421 dgvrypkngs srlyksdafk wnwsaqayye kdfaeknhid llagielrkt hqdkigflgd
      481 nfinadvyql pwqaaqyass sgtitngfrt veltdkdagr slftqinydf akkyfasfti
      541 rrdessafgs dknaavnggl glswnlsnen flknsnwvdf lrlrtsagit gnsrigsyrs
      601 sglyninftg fsydynyatp dtsappnkel sweknakyni gidfnifkkl eftievyrnn
      661 isdmivsrnv pletgynsaq ingasmynqg iefnakvdwf ktknftwssm fniskvvnkv
      721 tslvglgsdy stsenaraqk igtstsaiwg yvwdginpan gddtylidgv ktdgksvnks
      781 sdkwqiigns qpdayggfrn nfriakrftl gfqinfeigg ddlvmpelid hytillnrnm
      841 sinaldywtp qnpnainhap snkatfisns tkylydntnv klqnvslgys ipikkgvirt
      901 adlflnisnv aywykekspq drngirelqy lypemrtfsf gfnmnf
//
LOCUS       WP_103913513             970 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Halpernia
            humi].
ACCESSION   WP_103913513
VERSION     WP_103913513.1
KEYWORDS    RefSeq.
SOURCE      Halpernia humi
  ORGANISM  Halpernia humi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group; Halpernia.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 970)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Halpernia humi"
                     /db_xref="taxon:493375"
     Protein         1..970
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105488
     Region          30..969
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkiravsm aavfftgsll iaqkkdsltt tkidevvvva fgkqkkeait gsvttvdekv
       61 ianqqapsvt salqgtavgv nvitsggqpg nnpaiyirgi gsinsstqpl ivldgspyng
      121 ninnipqdqv esitvlkdas stalygsras ngvviittkk gransaprvt vtsligvsdp
      181 avklhetlna adymkydwqa lrnsniaags stpgadasgq litslgynpy dvatpidang
      241 nlapgakllw dtdwekalin kaafkqehrf nvsggdsktt yflgaeylnv dgtvktsnfe
      301 rtgvrlnves kvkdylkvgm nsaftasssn lpiqsgntyg ssiqwiyslp siypiyrrda
      361 ngalildgng ktiydygvqa ggplnsqrpv fqnenavgal ynnsdvakrn sfvvnafaea
      421 titkglslrs qlsyeqytyd eksfdaidvg aassvggrvs qerditktin ftnslnydkk
      481 fgdhslglqg ifevyqtsfd yllaqgtgfi qgtnvlntst tpeavggyyt aerlvrylgr
      541 atynyknkyf vegsysrdgs trfspdtrfg nfyglgaswi ltnenflqds ntfsllklrg
      601 sygelgnnnt snpfayqtlf qagynqlgqa gvvlgdpany nltwestits tigldfglfq
      661 nringsvdyf tkqskkliyn lptpasvgns siltnvgaie nrgwegnlnt vnfknknftw
      721 ttnfnistfk nkvtelgvds flngtkrfiv grsifdfflp ewagvdsatg mgtwfindvd
      781 angnvigrkt ttdynlannn dnkiyagssi pdfyggltny fkvgpvdlni lfnysfgsyv
      841 ldgtyqglms gfsapgrqqs vdvmnawqnp gdvtdvpini qtqnnnnats trflfkndyv
      901 rlksltlgyn inkdmlsqfg vnsfrifvqg dnvwtwqshk gidpeqgisg ttdsrsyqsr
      961 tlslgvtvgf
//
LOCUS       WP_103914627             927 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Halpernia
            humi].
ACCESSION   WP_103914627
VERSION     WP_103914627.1
KEYWORDS    RefSeq.
SOURCE      Halpernia humi
  ORGANISM  Halpernia humi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group; Halpernia.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 927)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Halpernia humi"
                     /db_xref="taxon:493375"
     Protein         1..927
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101581
     Region          34..925
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkklkfvs aiavfyftad lsaqqvqdtl tkenkieevv migygsrkkv dnttsistin
       61 seevnktkvl natqaiqgka agvtvvasdl pgstptviir glgtalsgrn plyvvdglfv
      121 dninninsnd ilsydilkda salaiygnra angviiittk tgrgkgihve ydgyvgvrmp
      181 lkevkmagsn lfsyytntal gatkfsqdqp vntdwfkeit rtgmysnnsi slsgasesak
      241 yflslsnyee ksilngtdyn rttvrtnnef kirkgivvtq nfsvtfnhtt pkplsaftta
      301 ykqspivpvf fpngeygvpi vgadgfasat gisqfnnvgn pvaqlafnde kqksylmqgg
      361 lkldidiikh lkftsqfsge ysnfksyifd gqqrligqta sqytntlann tqdyfnwtlt
      421 nyltyaqkfg ihdieatvgt eatvkdgins lymlrknvin dpnywdvsgt nyldqilqln
      481 svngnknttn syfaraqykl mnryllsati rrdgssqfsd gnkwgtfpaf glgwviseen
      541 flkdstffnl lklrggwgkl gnqniptnyl pfatgvnyny sfnnmpnssg ttidkifdpn
      601 lsweiteets agvdfevlnr kfkgsvdvyn rettniilas ipistsgisn sglshlgsvv
      661 nkgieatlsy dgrvnenfty niggnysynk neltslsdan vspirggglg ngqytkllda
      721 tavgqplgsf wlwevagkda ngnftyvdtn gngktgadda tdrkffgsyi psstyginvg
      781 fkyknidfsa ngygtigskv yngkkaqrfs genieysvat dfwsstntga anpapsntvp
      841 iasnyylesg dffrinnisv gytltkpvdy lksvrlyvsa inpiifqkfs gfspelnadg
      901 npygntgvel dayptlrsfv vglnlqf
//
LOCUS       WP_103914687             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Halpernia
            humi].
ACCESSION   WP_103914687
VERSION     WP_103914687.1
KEYWORDS    RefSeq.
SOURCE      Halpernia humi
  ORGANISM  Halpernia humi
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group; Halpernia.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Halpernia humi"
                     /db_xref="taxon:493375"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107621
     Region          30..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttsvla vvlsssfaia naqqkkdsan vqdiegvvvt algiqrekks lgyasqeika
       61 dalsdgttnt gniasqlsgk vaglqvntnn nfggtanlli rgvkslgggs plividgspv
      121 nnsttygsqt dygnalsdin qddiasvnvl kgaaasalyg erglngvivi ttkngrgkdd
      181 gswgvtlssa vqagfidkst fpeyqteyga gydpsfytgt gpngidyvnf pedaswgpkf
      241 dpnlqvygwd yfdpnspnyk kstpwvaakn gpikffdtpf sftnsvnlak gtkgkninig
      301 fdnlqqnglm pgskinkntl sakinydltd klhtsvyttl tlqktagrat tnygdnfitg
      361 frewwqvnvd vlqqkrayeq sghqniswnr nsaddataif wnnpyfqale nqttdsrtrs
      421 fsyasltydf skhvsltgkv sydntdlfie nrlaagsiaq gfgqsgnstt sgyarqninr
      481 netnydllln ykfditdkin vsgvaggnvr rnysssiyns tegglvvpgl yslsnsagat
      541 lapsesqatt esnslfatas fdfykifyld gtyrvdksst lpagnnvygy psvtgalils
      601 elfkpswlnf wkvranyaev ggtapsyyts naygstglfg ttglfgsqtt lpntdlkpqr
      661 skeievgtei hvlrdritld vaayktktld qiislpisrg sglytanina gqidnkgiev
      721 qlgltpiksq nftwqidanw sknenkvvsl lhnettdvsn illgsyqggv slnategyaf
      781 galvgsdyqy ingqpvisat tgrylksttn qiignttpdw lggvrntfdy kgisvsflid
      841 vrkggdifsl dqyyglatgl ypetaangvr engivwpgvn pngqvnqttt inpssfgsld
      901 gyarmpakrf vydggyvklr easigwtlpk sliagtfltd akislvgrnl wiihknlpya
      961 dpeavvggsv ngietgnpgf svgslpttrd igvnvtvkf
//
LOCUS       WP_103921182             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Venteria ishoeyi].
ACCESSION   WP_103921182
VERSION     WP_103921182.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Venteria ishoeyi
  ORGANISM  Candidatus Venteria ishoeyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Thiotrichaceae; Venteria.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Candidatus Venteria ishoeyi"
                     /db_xref="taxon:1899563"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39725
     Region          3..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,75,93,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpvivvpkgq vagehrvalv pdvarrlkal gaeiriekdm ggsaffhded ygddvslaqd
       61 saalydkadi vlsvqatled vekmpdgcil igfmaahkqp elvkklqqkk italamelvp
      121 risraqaida lssqasiagy kavlmgadma pvffpmltta agtirpasvl vigagvaglq
      181 aiatarrlga vveaydvraa tkeqceslga kfidmdvkae geggyarelt eaekqqqrdv
      241 ladhiakahv vittaaipgr aspkiilqnm varmrpgsvi vdlaaegggn celtqpgeti
      301 ehggvkihap ldvasqmplh asemysknlf nlltlmiaeg nlkldwedev itgsalthdg
      361 eikhtatrel legaa
//
LOCUS       WP_103915374             701 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Xylanibacter ruminicola].
ACCESSION   WP_103915374
VERSION     WP_103915374.1
KEYWORDS    RefSeq.
SOURCE      Xylanibacter ruminicola
  ORGANISM  Xylanibacter ruminicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Xylanibacter.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Xylanibacter ruminicola"
                     /db_xref="taxon:839"
     Protein         <1..701
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <3..700
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 dvykritgqv nadyniykwl qvgsnnsiek wdtksvsqrg ysssfeqmiq idpltpvywt
       61 tpdemslsvr tvydalqngt adqnyrlfrd ekgwfantky selegsplak rdtsdgtdgg
      121 wningtlfan lmpikgltit srlgyrlnfs nthsytapyw igdrgnqsny sisettntgw
      181 yyqwenfany nitlakkhni gamigmsyre snkdnssiss sgadilqsye pnfryisylk
      241 ddapkkvsns psksasvayf grltynydnr yffqfnirrd afdtsklskk nrwgtfpsfs
      301 ggwtvskekf ftdlvptsvv sflklraswg rngnisvlsn ypytaaiskg stwyqlhvde
      361 igsrygsapd klanpnltwe tseqvdlgld arfldnrlsf gvdyydkrtk dllfsisvps
      421 elgftsvmtn ggtvlnrgle lelgwkdrig dfsysvngnf stlknkvlal akganptyrt
      481 dagstnfqik tvfeeghsiw hlygyiyegm dadgnpiftd lngdgqigtd dmtdigrttp
      541 sftygvnvta awkgfdllin gygqggnkil pvihsngykn glkwyldnar tpenpdgtip
      601 hpgvimqpnv pfwsstgnlf sgnyfrvkql qlgytipani tkkaaisnlr lyvslddfft
      661 itsypgldpe tastnnfsga gldwgsyptm kklilgvnvt f
//
LOCUS       WP_103923030             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            boritolerans].
ACCESSION   WP_103923030
VERSION     WP_103923030.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus boritolerans
  ORGANISM  Algoriphagus boritolerans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Algoriphagus boritolerans"
                     /db_xref="taxon:308111"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107427
     Region          26..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfklyktils laflwgsvgw anaqytvsgt vadertgdam igasillkgt ttgtitdldg
       61 gfsitlptnd patlifssig yltqnvevap gvtilniklk qdatnleevv vtglatsvkr
      121 snlanavtsv sardltgttt iqttdgalyg kvpgatirsn ggapgggisi qlrgisslsg
      181 asqpliivdg vyisnasqrt gratvsgaga snqddgsnrl adinpadiet ieilkgpsaa
      241 aiygtranag viiittkrgq egkttvslsq digfaqplrl lgvddwsedk infffpesrr
      301 pielerfraa qssgnfidye dyfynnqatl lntrinvsgg tdktkffvsg nitdeegtvk
      361 ntgfnrysir anidhkitng irlgvssnyi rsntdrgftg nqnnsgasig ysiayvpnyf
      421 dlrrnadgty ptnpyfsenp vavtdngvnn tlvnrfiqaf tldvdllkte ksflkatfsg
      481 gldylqntsl vylpeflqfq raqanpgdvl kgkqesfntn fqaalvynwn lgavnmnssa
      541 glvrldfenn alfnrgrglv pgqrnlqqan iqeinqefss kiqdagiflq qeanwedkii
      601 gtvgirwdks tlngdpnqyy afprasvafn vanfdfwnvg finqlkpria ygetagpvnf
      661 gstftplggt niggllgsvv stqigntiil petakelefg vdagffnnrl aieatyyiks
      721 tqnnvqnlnl apstgvnttp sneaelenkg ielaisgtpi etanfrwfsr vmywknellm
      781 trlgiptyia gafgsglgtf lyaegysptt ivgtpaaadn pggftfwgda qpdfnmsffn
      841 tisllkglel sflidwkkgg dninltsflt dgggttngwf ndddgdgrpn grqrppapfn
      901 nagrwvqdas yvkireigly ynlpktsiae wfgtsvsnir vgtsvnnafl ftnyegydpe
      961 tstfgaqaia nnvdiapypt prriffhltv df
//
LOCUS       WP_103923328             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            boritolerans].
ACCESSION   WP_103923328
VERSION     WP_103923328.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus boritolerans
  ORGANISM  Algoriphagus boritolerans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Algoriphagus boritolerans"
                     /db_xref="taxon:308111"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108669
     Region          30..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnylpklkt lmlafaltlg atlaanaqsr tisgtvmdas lgdpvpgatv ivkgttrgta
       61 tdldgkftlp lqaedqvlvi sfvgymtqev eignqtnitv nleediqsle eavvigygsq
      121 dkkeitsavv gvkpedfnrg nvsnpaqllq gkvaglsitr pggnpnnafn irlrglstfg
      181 anssplivld gvigaslenv dpndiqsidv lkdgsaaaiy gargssgvil itttkqgsre
      241 gstnvtinsf atvdqatnli pilsaeefva rggtdfgsnt dwrnelidda lsyttnasvs
      301 gsfgnsnyma svnyrdnngi vngvgnerln trmnfsqgal nnrlrfninl sftnldsesi
      361 ndaafryati ynptapvfen tedaqnrfgg yfqrdlfdfy npvalanqqk fvgetktalt
      421 syrveydilp nltataqysq drrntlsggf wslqdfqvgl gatgsaernt fdrkqrifet
      481 tlryetdlsd klnmtllgga glqyttnqgf narvrqylfd lgwnnlgaga irlgnntnvs
      541 sfanedqlns vfgranfnwd nmiflsasvr aetysgfgpn nqtgyfpafs igsdftqifd
      601 mgvfsqfkpr vsfgvtgnlp psptlalgvf gngnridldg dpltqndifv ginqfsnpnr
      661 dlkwetkeel nfgvdfgmfn nkvtgsidyy trnisdllfn vpvatgapnp fdpgrfntag
      721 stwvnlanlr aagfefaasv nqigkgalkw tptfnftiyd kttieslsag elgfeelrfa
      781 tpgspgqnnn qiiynrvgqn lgdiygprln gltengeyil sttdpnefek lgnglpkgef
      841 gftnsfmygq wslnfflrga wghdlynsyr gfyenadgas ntwnsvvtak tptnplvsst
      901 ptfnssvved asfirldnae lgynfktnsp nlsslrvyfa aqnlftitny tgvdpevrtn
      961 dsengdafts alspgierrn tyfqtrsftl gvtvnfk
//
LOCUS       WP_103924007            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            boritolerans].
ACCESSION   WP_103924007
VERSION     WP_103924007.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus boritolerans
  ORGANISM  Algoriphagus boritolerans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Algoriphagus boritolerans"
                     /db_xref="taxon:308111"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116505
     Region          25..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkallfvva lftmtlsyev saqqrvitgt viseedglgl pgatvlvkgt tvgtttdldg
       61 nysinvpags dvlifsfvgl ktaeeaignr svvnitlttd asnlsevvvt aigierekka
      121 lgyavtsvdn aqlenrpead varvlqgkvp gvsitstngm sgsgtnmvir gyssatgsnq
      181 plfvvdgvpf ntstnaqngf ttggtatssr fldidpnnie smsvlkglsa tvlygdqgrn
      241 gvilittksg askrkaaevt inqsvftnea aslptygqiy gngfqqdrgf ffsnfggrmd
      301 egvtinhpya tssiasirna fpqfwvdgiv ggtpvqyeyk ayadpseiff rqglisntsv
      361 qiaggsdrtg fnasfgytde qgylpgnele kfnfglgins aisdkltvns sftfaitdll
      421 tppvngsfgs gsaipsvfgh vlftprsvdl aglpfenpid kssvyfrggn divnpnwlvr
      481 nyvnssdvqr ffnstslnyd ltddfsityr lgldtytelq elrynkggps gnlataqgyy
      541 rtininntiw nqdlilnwkk efsdkfsmsa llggnsrydn yaqngvasqg qlafglfrhs
      601 nfqtsssnda ysggtmtyte eqrrygvytn itldysdylf lnlsarndwt stvekenrsi
      661 lypgasisfi pttafdwsst tlndlklrlg ygtsagypsp ystrnilaqs arafdrggit
      721 qthsvsnalg npnlrpelhg elefgveavm fnnklrfdls lyekntrdli tqspidpatg
      781 ftstainigq iktrgaefqa tvtpistpsg fewtstvnws tyetevielg ggleevvvag
      841 ftdlgnfaip gqpfnvikgv gfdrapdgqp iilsngvhkp aadlvilgdp npdwtgswin
      901 gfsykgfnln vmmeyrhrgv iysstvtatl argvtkdpvv dreltfimpg vrqdgnnadg
      961 tpryipndyq itasdyffsg yqgatdepnv fdgsmvrlre vslsyqlpns lmaktpfkra
     1021 sfavsgtnlw flalnfppnm nydvdvlgtg vgnglgfdfv tgpssrrmgg tltltf
//
LOCUS       WP_103924770            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            boritolerans].
ACCESSION   WP_103924770
VERSION     WP_103924770.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus boritolerans
  ORGANISM  Algoriphagus boritolerans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Algoriphagus boritolerans"
                     /db_xref="taxon:308111"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115896
     Region          29..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miaqkinwkw tlsvfltlvf nfsfaqetqv sgkvsdlnnd plpgatilvk gtsrgtvtdv
       61 dgmylisafp gdtlvfsfvg fetlertvgn sntisvslse glalsevvit algikrdeka
      121 lgyatqnids qelldarsnn wsdalrgkva glnvlsagsg pmnssqvslr gnnslnpngn
      181 falivvdgvp mnsgltssgv gnaysagsgn dvpvdfgngi adinpddien itvlkgasat
      241 alygsraang aliittkggs rntkgigvti ntnigfndvl rwpdyqyeyg qgtgrafnsd
      301 gelyysygas edgagtggts safgpkfdgq syfqydptve gqslerqpwr pyldnikgfw
      361 rtgynvvnnv aiegsheggs arasfthnkn ewimpntgfe rfvaalslsq qisdklrlna
      421 kasytnkrsd nlpatgynnq siayfmifqn pnvdlnwyrp iweqgqtnis qvhpfssfid
      481 npyliayemt navnnnaflg nisanytfne kfelllrsgi tmsqeersqr rpyssanyqr
      541 gfykeqditn yeinsdflft yrdkigskfs lsssvganqm qrnfrltsae viglvipgvf
      601 klangvsnpt vttsdnnrvi nsvyglvsmd wdekifvdlt grndwsstlp vennsffyps
      661 vstsfilsdl iklpkpvsfa klrisgaqvg ndtepyrtsk yygqsefpgs asvpttlynv
      721 dfkpeitssf etgmelifld rrlsldvnyy isetenqiiq vpvdivtgfs sailnagtvq
      781 nkgwevvfna tpiskgafew nstltwarnr nkvlslpdev dgsqvigngg nasiiarvgg
      841 ttgdiygfgf vrspegeivy nknglplrpq eiqyignaya dwkgglrnef ayksirlsvl
      901 fdgqyggivy sqthhkmseq gklrhtlrgr edgfivgegv vqntdgtysp nttqvnlaty
      961 ygdyyrranv esnsfdasfv klremrveya vparilsrts irgasiafyg rdlalwskfp
     1021 vfdpetaaln gstllpgvem gqlptprtfg anltlkf
//
LOCUS       WP_103925172            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            boritolerans].
ACCESSION   WP_103925172
VERSION     WP_103925172.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus boritolerans
  ORGANISM  Algoriphagus boritolerans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Algoriphagus boritolerans"
                     /db_xref="taxon:308111"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118980
     Region          25..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkifytllly lglaitplia qtsytvsgvv tseqdnttlp gvsvlikgst tgtvtdetgr
       61 yklsittesa tlvfsylgft tkevslnssr seidvslapl dmelsqvevl atgyqeipre
      121 rangsfvgid kelvnrrvst gilerledvt pglifnregd efeaisirgr stiyanaqpl
      181 ivvdnfpydg pieninpndv esmtvlkdaa aasiwgarag ngvivittkr akagqsfrvs
      241 fnanttvaek pdlfynpkme vsslvdlhre lfergnfnsn insnnkprva pavevllkar
      301 ngeisqsead qllegfksrd frndldryfy qpsvnqqyal nlsgsgnvhq ynfalgydan
      361 ssevvgnsnn ritltqnnqw kllenrlelg agiywvqsnn ntttdlaqgw iydrmtdeeg
      421 nplaisrsys dryinsieae radllnwryv pldeiglldn rsrtndlrln anigyqlfpg
      481 fkaevryqyw nnqvetrnhs pqetffvrdl inqfsefdqa glltrriplg gildhstgrg
      541 dshslramls yekltktgnr inaiggyeik sltsyqdamr yfgyddqlgl ssavdpttrf
      601 rrlynnalat ipanqshrgn tdrfisyfan asyqidtrfn fsastrkdqs nlfgvnanqr
      661 gvplwsiggg ytiseekwyr fdalpylrlr mtygyngnfd nrvsafttar ysispsstip
      721 nlpiaaimsp pnpnlgweki rninlgldfg skngkisgtf efyqkngedl igdievpast
      781 gffnfrgnfa ntstvgydln lnaliidkgv kwrtdffwsf vkekvtrydf tlppanffnt
      841 sginpyvgrp lfgvygypwa glnpengnpm gfldgipsed hrgiltsitp etlhyagpgr
      901 pvhfgslrnt vswkgfefsa nisfrlgyyy rrssvsynni ltgtfehady errwremgde
      961 mvtsvpsmps vpnsfrdafy lnsevliekg dhirlqdirl aysfqesgla ggifrnlsly
     1021 syvnnlgilw katkdeldpd frttlpkrsi afgvnwnf
//
LOCUS       WP_103924937            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            boritolerans].
ACCESSION   WP_103924937
VERSION     WP_103924937.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus boritolerans
  ORGANISM  Algoriphagus boritolerans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Algoriphagus boritolerans"
                     /db_xref="taxon:308111"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109607
     Region          26..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkflsiafs lalllgisat aqsqqrvlkg kvtassdgla mpgvtildks nqtgtttdvd
       61 gmysipvteq svlvfsfigf tsqeftvgnr telnvvldes asdlsevvvv algltkekek
      121 lgysistvss dvmdkaretn vanslagqva glvvkgtngg pggssnivlr glpsisgtgs
      181 plfvingvpm dntqrgsagq wggsdngdgi gnlspddies mtvlkgqaas alygsrasng
      241 vilittkgaq kggdwtltyn lnvmgeqavd ftnfqdqygq gtgglrpqta tdarttgrfa
      301 wgermggnvi gfdgnqypya paseryidfy rtgsnitntv avskglgkdg afrmsisnln
      361 sksivpnsgv drlninlnvd qnitdklsvt aminyvdqqs tnipslsdgp knpnnflfla
      421 pnirpsifap gfnpdrseiv fsddifvtnp yfitnkgind lgrkrtisal sakyaftpkv
      481 yamlrvgndt snddfysvdp tglaysanlq gglggrglsn rselnvdalf gadlklnddi
      541 eidgliggtl rknrfetvgv ngsrfvipel yspfnlvnfg rsygfqerev qsgfysiglg
      601 ykdfltlttt grydvystlp tnnnsifsps vtgaflfdrf lnisaldfgk fraayavtsg
      661 epfgayqtqf yyssanayag vpagssplgl pnlslkpftt deielgfdls ffktrlsfdv
      721 ayftkttnne imnanysiss gfgsgvvatg strntgievl itgvpiqtan fswksslnft
      781 nvknevlstd pnnnpinlgq nratlgnavt ayvvglpgpq iraydyryda ngnvvvnsag
      841 ipergelknw gsvlptiygg wnnefnfkrl sfsflidynf gnkvlsatef yshfrglhqn
      901 tlegreggvt tneitanaen yyqglvqnvt rtsivdgdfv klrqltlgyt fpselfnsvp
      961 vlkgltasiv arnlailmrk aenidpeatf gsninylgie gtslpstrsi gfnlnfkln
//
LOCUS       WP_103925343            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            boritolerans].
ACCESSION   WP_103925343
VERSION     WP_103925343.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus boritolerans
  ORGANISM  Algoriphagus boritolerans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Algoriphagus boritolerans"
                     /db_xref="taxon:308111"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119035
     Region          24..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikrfmicil malvsmgafa qnsklqgvvl saedriplpg ttiriggtnq vaitdeegkf
       61 nlntpnqeir ltfsfigyqs qtldlilptd pltvlmelee tslqgvevfa tgyqeipker
      121 qtgsfvgldr elinrrists ildrledvtp glifnrtgst tdpisirgrs tifsnaapli
      181 iidnfpydgp ieninpndve sisilrdaaa asiwgaragn gvivittkkg vrgdsprvtl
      241 vanstwaerp dpfyqplmss sevvdmerrl fsenfylnqe nspfrtpltp vvesliqnre
      301 gllsnaelqt rlesfrnldi rndyrdylyq sswnqqynln vignsgkygy ylsagwdenq
      361 snlvgnqssr ytllsnqnln lldgklelgl ginyilstqs gsnngpsgir fngaqplyay
      421 gslvddsgns tafysgireg fartaesngl lswelnplee lrlvdrsnel edirlnlfgk
      481 ykilpqlsae vyyqywkgsg lnntvndpns favrdqinrf tqrgesgals yaipqgaird
      541 wsvrnsvshs vrglvrwngd lgksgvlnsl agyeikqlnf eglssraygy spetgntvpv
      601 dqvtlfsqyq npairaqipf glgvsggadn fisyfanaay tfknkftvst sarkdasnlf
      661 gvnanqrsvp lwsaglawti seenwqlpqw vsflrlrtty gvngnvnkgv talttarivg
      721 vsrysgfpva nltnppnlnl rweeikilnv gfdfdfwndr lggsfevfrk egndligdip
      781 fapntgveqf rgnfanslgk gfdfqlralp ikkalawrid yfhshvqekv ldyevkttvl
      841 nylgqatgan psspifpleg rpiyaiyslp faglnpdngd plglldgess sdyaailsaa
      901 tpedltfhgs arpthfgsfr ntftwkrwnl sanisyrlgy yyrrnsvryl pilsgeqghg
      961 dyslrwqnpg delttqvpsl patrntfrdn fysfssvlve kgdhvrfqdv rlgyshansn
     1021 gkrgnwqifa yannlgmiwk asndpldpdf rtmrplrsft lglqwdf
//
LOCUS       WP_103926611             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus boritolerans].
ACCESSION   WP_103926611
VERSION     WP_103926611.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus boritolerans
  ORGANISM  Algoriphagus boritolerans
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Algoriphagus boritolerans"
                     /db_xref="taxon:308111"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40671
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvlketk eferrvalsp dvvkllkkke fdvvietgag egsyfsdqdy lnagaivsgv
       61 aevfasdvll kvniptleei aqmkqgsaci symyayqhpe iiealnrksi ssfsmdavpr
      121 israqkmdal ssqanlagyk avilgsnylg kifplmmtas gtitpakvli fgagvaglqa
      181 iatakrlgai vevsdvrpet keqveslggr fltvegagvv kteggyarev saeflekqqq
      241 likdkikdad lvittalvmg rkspilvtee mvksmktgsv ivdmavdsgg ncaisekdkt
      301 vvkhgvtlvg esnlpsllpl nasqlyatni stlflhlfns fglipnleee itkgvmithe
      361 gqlvheftks ilnppakns
//
LOCUS       WP_103965071             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas ureae].
ACCESSION   WP_103965071
VERSION     WP_103965071.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas ureae
  ORGANISM  Nitrosomonas ureae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas ureae"
                     /db_xref="taxon:44577"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39376
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir sgetrvaatp etvkkytakg vhkvlvqlga gagasipdsa yqeagamivt
       61 dvaelyaqsq ivlkvrgpes gelammrkda vllgllsphq kdgvdalaqh gltafamekl
      121 prisraqnmd vlssqaniag ykavivaanv yqrffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avveafdvrp avkeqveslg akfvevplse eekaqaetag gyaaemsddy
      241 krrqgelvhe railadiiit talipgrpap vlikeetvqa mkqgsvivdm aveaggncpl
      301 selnknvikh gvhligianl pglvaadast lyarnlmnfl nlmldqenda lkidrsdeii
      361 agtllcagge vagks
//
LOCUS       WP_103967868             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Billgrantia desiderata].
ACCESSION   WP_103967868
VERSION     WP_103967868.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia desiderata
  ORGANISM  Billgrantia desiderata
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Billgrantia desiderata"
                     /db_xref="taxon:52021"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35593
     Region          5..171
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mpifelfskr qkklrgevpd vyqyesleqs frvqvvhiir dtigveqsyn natngvyrei
       61 hrvlckeygv fslkeytnsn feavfeyfln eknyekcldi ielafriidt hvrerewdfr
      121 naagasqkpd daiselnsrf kesgigyqfe sgelirvdsq fihsevvkpv lrllgkniky
      181 agandeflsa hehyrhkryk eclndclksf eslmkaihek hswsfnkddt akklinscla
      241 nglvpeylqn qfssvrtlle sgiptvrnke gghgqgaevt svpehlasyt lhltatnllf
      301 laqceekys
//
LOCUS       WP_103973128             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylovulum psychrotolerans].
ACCESSION   WP_103973128
VERSION     WP_103973128.1
KEYWORDS    RefSeq.
SOURCE      Methylovulum psychrotolerans
  ORGANISM  Methylovulum psychrotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylovulum.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Methylovulum psychrotolerans"
                     /db_xref="taxon:1704499"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54153
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeih rgekrvattp eaaaqiiqlg fsvmiesgag laanisdeay qaagvavvdq
       61 ktlwqdadiv mkvraperrp rlgidelaal hegqtlisfi wpaqnaelmq tladknatvl
      121 amdsvprmsr aqkmdalssm aniagyraii eaaqhfgrff tgqitaagkv ppakvlviga
      181 gvaglaaigt aksmgaivra fdtrpevkeq iesmdaeflm ldfkeegagv ggyaktmspe
      241 fiaaemalfa eqakevdiiv ttalipgkpa pklitaemvq smragsvivd laaeqggnce
      301 ltekdkvtva hdvtiigytn lpsrlanqss qlyatnlrhl ltelcpgkng vinvnmedev
      361 irgatvikeg kitwpppppt lsvaaakpaa vaeavikapp appsvlkqll plligglalf
      421 gigavapesf mthftvfvla cfvgyqviwn vspslhtplm svtnaisgii vigaivqvss
      481 pavgllagla iliasinigg gflvtrrmld mfrk
//
LOCUS       WP_103982116            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides chinchillae].
ACCESSION   WP_103982116
VERSION     WP_103982116.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides chinchillae
  ORGANISM  Parabacteroides chinchillae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Parabacteroides chinchillae"
                     /db_xref="taxon:871327"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114917
     Region          42..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlknfkpvsl ilfagalcfs gnayadlapv kqstnisqqs gkvtgtveda lgpvtgasvv
       61 vkgttngtit dfdgnfaleg vqkgdviqis figytsqeit yngqplgiin laedtqklde
      121 vvvtalgikr ekkalgyatq elkgdailds resnvtnals gkvsglqvvr ssggpgassk
      181 ivlrgnnsit gtnqplivid gipmdnfqgg vadawgnkgp dmgnglsdin pediesmnvl
      241 kgasaaalyg sragngvili ttksgkkqsg lgitvnagvt aetmfmqpdi qnsygqgstg
      301 iydvksrasw gpiadgsvni dswngknvpm ytydnvgnyf dtgvsfnegi sfqqanegts
      361 vfasinrsdd kgivpgakls ktsinlrgtm efgpdkrwkl dgkvnylnni ghnrplqgin
      421 qsnafstiyn lprsinildl kdcldedgnm iwwdtestpq enpywtkqyr tnedtrnrfl
      481 gtmslsykif dwwnvelkgg tdyyttttts klyaggnvtp kgnysegset fyennfsflt
      541 taqkdnllgk fggfvtfggn lmiqkrsvek istgdllipn lfsinnavdk nkmgleytlt
      601 qrkmnslygs fqinydgwmf lditarndws stmskvnrsy fypsvslsav isdmvqkngg
      661 slpewmtfak vrasfaevgn dldpyqlytv ysmskdpygn pvaspgsvlf npdvrselik
      721 sweagvdlkf lnnrlgidfa wyksnatrql ldlpldpfsg ysskkinagn iqnsgvelma
      781 yadifqnpkg fswnitanls fnrnkvidly egikemglsd gsfndevkvv ahtggmygdi
      841 ygkkfqrves gadagkiivd aqglplltsd lqylgnqqpk cmlgitntfn yknislsfli
      901 dariggkiys attakmyyng saagtvvnga reefvvpnsv tasgdgytan ntsvtpqlyw
      961 ervgtgnlgv geaflydatn vrlrnltlgy tfdkkllakt plerlrlsft annlwmiash
     1021 legidpesvs ttntnatgie lgaaptsrsy tfnvtvgf
//
LOCUS       WP_103982115            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides chinchillae].
ACCESSION   WP_103982115
VERSION     WP_103982115.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides chinchillae
  ORGANISM  Parabacteroides chinchillae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Parabacteroides chinchillae"
                     /db_xref="taxon:871327"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115685
     Region          42..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkkfrpvsl illlgalsft gslyaipgte npaasvpqqt skvsgtveda lgpvtgasvi
       61 ikgttngtit dldgnftldg vkkgdiiqis figyvpqdip ytgqstltvh lsedtqklde
      121 vvvtalgmkr dkkalgyamq elkgddllss repnlansls gkvsglqivr ssngvggssk
      181 ivlrgnnslt gsnqplvvvd gtpmdnftgg vddvwgnsga dmgnglsdin pediesmtvl
      241 kgasaaalyg sragngvili ttksgrkteg lgltvnagit aetiflkphm qddfgqgsvg
      301 iydnqsrlsw gpkaegqtvk dwlgrdvplh tydnidaffg tgtsfnegvs fqqdikgtsv
      361 fasvnrsdda sitpesklnk tnitvrattf ldeakkwkvd akvnyinmna hnrpiqgvnp
      421 snafntiynl prslnikefe nsvdengkmv wydasnnpqe npywvtkyrq nedtrnrllg
      481 nlslkyaptd wfdielrggt dyytttknek vyaggnttpr glysegsetf yennfsflat
      541 arkdnlidrl ggfitfggnl mqqqrskmna sagellvpdl fslnngvdkp tvtselirrr
      601 mnslygslql nwdgylfldi tarndwsstm skvnrsyfyp svslsgvisd mvpklggamp
      661 dwfsfakira syaevgndld pyqlynyfsv dkdqngntia kpgkvlfdss vrselikswe
      721 agfdfrffnn rlgidfawyk snatrqlldl pmdpfsgyas rkvnagniqn egvelslnge
      781 ifnnpqgfnw nataqfslnr nkiidlypgv tlyniktfda vqivavqgsl ygdiygqtfq
      841 rvtdensphy gkivvgedgl plistdkskv gnqnpdwmlg ltnnfsykgf nlsflidfri
      901 ggdiysatas glytrgnaag tvvngdrqsf vvpnsvvqkg ngyvmnevkv tpqnywerig
      961 stgnyglpem ytynatnvrl rnitlgydfn rqmlkktpfq rvrlsatcnn vwmihynlpg
     1021 idpesvaatn tnatgfenga aptsrsytfn vtigf
//
LOCUS       WP_103984042            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides chinchillae].
ACCESSION   WP_103984042
VERSION     WP_103984042.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides chinchillae
  ORGANISM  Parabacteroides chinchillae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Parabacteroides chinchillae"
                     /db_xref="taxon:871327"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113779
     Region          46..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msknvkqrkk lvqtalicgl lsgigtinan avipsegvtv sqqkeivvkg tvkdrngeti
       61 pganvvvkgt nigtttdfdg nfsmqapana ilevsfigyk ttdvavnnqn ninvvlsstv
      121 eeldevvvta lgikrekkal gyamqeikae smaevrsesv anmlqgkvag vqisqsatgv
      181 ggstrvilrg ttslsgnnqp lwvvdgmpis dkqtgdanqw ggidysgaas einpediesi
      241 svlkganaaa mygsraqngv iivttkkgqs gklqleyngn ihfskaydsy eyqnvygqgs
      301 ggtytvgate swgpkmtgqm vdnwrgpngi ykdsrydaqn allpqnsyid dfyrtgvnyt
      361 ntltasggse tatarfsfsd srnegitpgh slnkqyydlg aelkgkyidi sakvnymrqk
      421 genrpalgey gimrslitmp rgirlsdlkd pvgldgytvn wsgqsnehrn pytdtmseng
      481 nrddrnriig klqlvgkitd ylkitgrvgi dwyhdqirny gsytqtytst sythtmatnq
      541 efnadlmanf nkqfgdfsvt anlgaamtsf kwnnvngssg yfsiphlval sngnnqttse
      601 gysnkhvnsv lgnatvgwks klyldvtarn dwsstlpann rsyfypsvsl sgimseiltl
      661 peqisfwklr asyaqvgndt npyqllsvys lnktngeiln ataatvfllt nlkpedtrsf
      721 evgtefrmfn grlgfdltyy nantlnqilk vavpissgys eklinagkmk sygwevsltg
      781 tpiqtkdwtw dvtlnwglnr tkcieldpsl kqftigeetr igkvivkegg rygdimgngy
      841 erdangrlli gdnglpikes nkivgnmtpd wtgsfstslr wknlslnali dircggdfis
      901 ttdayataag tsartldren eivvngivks tgkentqtvs aqtywsavgg aygvaeeyly
      961 dasyvklrel sigytlpkaw lrnlpiqsvk lsavgrdlfy ifknapinpe ssfgrsdyaq
     1021 afeyaalpst rslgftlnvk f
//
LOCUS       WP_103983791            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides chinchillae].
ACCESSION   WP_103983791
VERSION     WP_103983791.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides chinchillae
  ORGANISM  Parabacteroides chinchillae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Parabacteroides chinchillae"
                     /db_xref="taxon:871327"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115405
     Region          25..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkkltfall clvmsigmam aqatkvtghv tsvedgepvi gasiivkgtt igtvtdfdgn
       61 fslevpangk ilvvsyigmt tqevpvssnv mvklksdtqn ldevvvtamg isrekkalgy
      121 avqdvkaekl tkgansnlag alqgkvsgmd ikpssgmpga ssqitirgar sftgdntply
      181 vvdgmpiass adidteasvt gtdianravd idpndiesin vlkgqaasal ygirasngvi
      241 vittksgkgi ekgkpqvsfn tnvsfdvlgr kpqlqqtfaq gtngtyspyn saswgpkisd
      301 landptyggn vankynggdt qkyagkyyvp qraaagidpw atpqvydnig gffqtgvtwn
      361 nslnvaqate kasyafslgs stqdgiipet gmdrynakit seiklheqwt tgvtanyins
      421 kikkmpaand allatvyptp vsydlngips htsqsiyeqn sfrsttfaia pwfvknnefi
      481 ektnrffgns flnfktkfgt dnhtlnakyq igvdsytthy qdiwgygnkg anmngqvedy
      541 gwsnvsfnsl ltvnydwtis pewtlnailg nevvhnqtkk yyefgssfnf pgwnhienat
      601 tlqsqerqrs krtvgffgsv sasyrnmlyl nvtgrndyvs smprnnrsff ypsvsagfil
      661 teleplknev vnyakirasy aevgqagdyy enyyytpvyg ggfyqidpvv ypingmgafv
      721 pypviydpnl kpqntrsyel gadlnffnnl vtlnytfsrq nvsdqifqvp lagstgasdl
      781 ltnggrihtn aheltinvnp irtknvdwni ganwtkidny vdelapgves iflggfvtpq
      841 vragigdkfp viygvgylrd dkgnlivden gvpqagkdqv igsvspdfil gfntdlrvwk
      901 fslsavfdwk kggqmyggtn glldyfgmsk ategrdtesf ivdgvkadgs kndieikgas
      961 awqnyfqsin nideasiyns sflklreial sypvlekkwm sitvnvfarn illwsefpnf
     1021 dpessqgnnn mtgaferysm pqtssygfgm nvkf
//
LOCUS       WP_103998317             978 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            urumqiense].
ACCESSION   WP_103998317
VERSION     WP_103998317.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium urumqiense
  ORGANISM  Flavobacterium urumqiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 978)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 978)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Flavobacterium urumqiense"
                     /db_xref="taxon:935224"
     Protein         1..978
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107562
     Region          24..977
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykkllf lllllplsil aqntvngtvl dqvsgqpipg vnvnvqgatn gvstdfdgkf
       61 qlsnikkgdk ivfsfigyka svvtydsqks vmvslieden qlkevviqvg ygtvkkkdat
      121 gavtvltakd fnkgpvnsad qmiqgkvagl qiingggspg esatirirsg sslsagndpl
      181 yvidgvpvnn ggieggknpl stinqnnies itvlkdasat aiygsrasng viiittkkgk
      241 ageiqvsyng nlqvsevtnr vdalsstqfk dfvtangtpa qikllgtadt nwqneiyrta
      301 igtdhnials ggvdnvvyra svgytnlngi lkrdnmerst lgvsvtgnfl dkhlkievnn
      361 ntsliksnys nrgaigaais fdptqsvrna ddtyfqwyas pteinqlagr nplslinqqn
      421 nfgnsyrsig niqteykmhf lpelkavanf gydqltgtgs ggtnadylng lkgsgysnty
      481 kniesrknkv mdlylnynkk vdaintqidv tggytyqdfq dsknksnynf qndvttiesf
      541 tpsrinlqsf fartnitiad kyiltasyrr dgtsrftpdy rwsnfpavav awklneesfl
      601 kdvssistlk lrggwgitgq qnigiypsip lylasnttaq yqlgntfytt yrpqkynsnl
      661 kweqtttvna gldyglfnnr ftgsvdvykr ttkdlllety npsffgfsnt dnynignidn
      721 kgiellaevi pvrtdnlewr iggnvtfqds kitkltttqp ntpgipegdi aggtgnkiqn
      781 hqvgyapnsf yvyeqaygan gkpldgvfvd rnkdgliteq dkyrfhkpaa dvfygfntsv
      841 tyknfdmgmt wrgswgnymy nnvdsnfgty nnvllrqtdl sngvanllet gftktddfql
      901 hsdyyiqdas firldnvnvg ytfnqkpnss slvkltlsaq nvllitkyng ldpeisngid
      961 nnlyprpitf tlglnvnf
//
LOCUS       WP_103998959             988 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            urumqiense].
ACCESSION   WP_103998959
VERSION     WP_103998959.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium urumqiense
  ORGANISM  Flavobacterium urumqiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Flavobacterium urumqiense"
                     /db_xref="taxon:935224"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105722
     Region          24..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknsllkglm vfltmlctsl tysqevsgtv sdssgplpga svlvkgttng aqtdldgkft
       61 iknvgsnpvl vfsyiglksq elnvagkssv rvilkedsae lkevvvigyg svkkkdatga
      121 vdqlsskkfd nvaatnpael lrgkvagvqi tsssgepgaa nsirirgngt lrggngpliv
      181 vdgvplaggd vsagganmnl gsmsakdpls finqndiesm silkdassta iygargangv
      241 iiittkkgks klpeltysts yttssyaskf dvlstdefia atpgqtanhf ggafdwkkqv
      301 lqtgstvnhd lsfssgtdns ntrvslgman tdgivrntgl dkitasfyns ndffdgkvkl
      361 etriaysnik drrglitndt gyignllsaa lywnptrsvy dptqpggftr vsgdylnpvh
      421 lmnsfsnngd lskllgsltt tvkltnslky nmvvgietsn ssvkqqatpd lniqdfatat
      481 npadlktyrg qatvsndqrv nktiehnltf tkditkdinl naivgysfyn yasngtyvsa
      541 kgfaatqanl lenmeggipt etrtgsykgl vemqsvfara slafynklnl dltvrrdgss
      601 ktaagkkygn fpslglaykl vdgkdglvnd lklrgnigkt gntefprnss vgtieyngpd
      661 qfnivnnans qltwetttsy gvgtdfalln nkltgsvdyf nknttdlivg ipstsgqpsp
      721 qgikytnlpa nlinkgvevs lsykvidtdd ltwdisgnva flsntienlg aanvynvgai
      781 hgqglsdayv qriqdgyply tyylptftgy dangisqyad ggavklldkq plpkmtagfs
      841 tslaykgfdf stslygnfgn ylfnntnval fyqnqlggkn vtpevansvq srsdantpst
      901 kylekgdfir mgnltfgytv kgnvlerfkv ksarfyvngs nlfiitkysg fdpevdtnks
      961 lngipsagid ylsypkartf svglnvtf
//
LOCUS       WP_103999650            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            urumqiense].
ACCESSION   WP_103999650
VERSION     WP_103999650.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium urumqiense
  ORGANISM  Flavobacterium urumqiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Flavobacterium urumqiense"
                     /db_xref="taxon:935224"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111332
     Region          25..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlkfkwifs lvlamsmqfm faqektitgv vsdgngtlpg anvlikgtka gvqtdfdgky
       61 sikaktgdvl vfsfvgmnds saivgasntv nmklasssqt leevvvvgyg qvkkkneitg
      121 nvvsvsgdvi kqapmvsvdq alqgkvvglq msassgtpgs vqdirirgrn sisagnsplf
      181 vidgvpving dftgsaniss lstlasispa diesmtvlkd agatsvygar gsngvilitt
      241 kkgkkgeakf sfsstvgfqn navaglrpft gaekkelyle aiyntfsnng ttftkdntya
      301 wmltsptsli sagnktalvn wvnageneyn wdelmknkda vfnsldfsvs agdekstlya
      361 sigynkteat vigsdfkrvn gvlnysrklt dkfelrtgmn vsnirqngvl eqgaffsnpn
      421 ltkafmspwn npynadgsls taitplhnal ytavnnvran dltrvlsnns lsyqiakdlk
      481 frtdvsfdyt lasykgfnna vhgdglsvgg natasvrknf nyvaqnsldy glslnedhrf
      541 dfkalveyqk nkqnfisafg eviplgftnv sntaankdas styddwsnlg yvgivnykfq
      601 nrflldltgr reassrfaad nrwgtfysag aawnvnnesf mknltfvdll rlrgsygtsg
      661 nnnidinsyq tllgttnynn qgglvpvqfg tadlgwetqk kldtglefgv wdnrikgtaa
      721 yynnksedll lslplslttg hssqnqnlgs lrnsglefel nvdiirsddf nwsiggnyat
      781 vknevvgmpt ingkqvtitg gttrtevgyp vagwymrkwa gvdpangnal wyidgvsgat
      841 ttsyntakve wqgdsalpkf tgglnthidv ynfyvdvsly aagghkvyed wagftqhsgr
      901 tslltyngse aildrwqnpg ditnvpkvey tatagnaqaa atstrflydg dymrlrditf
      961 gynfksavls qlkldglsas vrgtnlltwv kddrlkydpe vradgftrlt sppvksvvfs
     1021 lnvkf
//
LOCUS       WP_104000028            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            urumqiense].
ACCESSION   WP_104000028
VERSION     WP_104000028.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium urumqiense
  ORGANISM  Flavobacterium urumqiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Flavobacterium urumqiense"
                     /db_xref="taxon:935224"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118141
     Region          27..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngfll llvilvaqit faqeravsgt vsdnaglplp gvsvlvkgtk tgtqtdfdgk
       61 ysikasssqv liftyigmkt qeivagsssv nvklasgave legivvtalg ikrekkslgy
      121 asqeikgadl tsgagssnfl nelsgksagv nirkntnfgg stnvvsrgvk nltgdnqmli
      181 vidgmpinnt ntnssagsqt agarntydyg nnamdinpdd ieslnilkga aaaalygwqa
      241 gngvimittk kgkskkgmgv tisseltvgt vdkstfpdyq nkygqgygpt ydsagnpkgi
      301 pvgptgafft idsngqqvat tvddasygva fdpnlsvfqw nayttfsdny gkktpwqaak
      361 ngpitffnta qtlsnsvsie dgtdktnfvl nfnnfketgi lpnselkknt fsakinhkft
      421 dklstsvfan ytaqntvgrn ttgyggdnva glfrqwwgtn vdiqeqktvf drsggqnisw
      481 nmgapatgnt npkywdnpyf trfknfqsde rnrfigyvql dyklndwlsa sgkvstdsys
      541 elreerkaag slnstfginr lavpsgyqry ngmfseqnyq atltfkknit eqislsglag
      601 lnslrtrrts ilasteggli ipeiyalsns vaavpfpier eensgvnsaf astsfgfkdf
      661 lfldgtirnd afstlpkgnn avntfsasas yvftehvrqd wlsfgklras yaenpqgnid
      721 lyalqsvftk fnpfganqly srpdvganse lrpvktatke iglemqflkk rvgfdvsvyk
      781 slssdqifpv dystatgysk kyinagsven kgievqfnas piktadfqwd ifvnwsknkn
      841 tvvalapgie tltlgtfqgg vgiiatkghp ygdiigkdyt ysadgqrits ngsyvmtttt
      901 nnvignvtpd wigglrnkft ykqlslgfll dmqkggdifs ldqyygqdsg lykstagine
      961 lgnpvrntia ngggvilpgv nangtpnttr ttrpevagsi ygyeknpqka fvydagflkl
     1021 revnitysfp tnivsqinlt dlrlsivgsn lwtisknlpd adpesgitsg nlsagysggs
     1081 lpstrnigfn ltlkf
//
LOCUS       WP_104000030            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            urumqiense].
ACCESSION   WP_104000030
VERSION     WP_104000030.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium urumqiense
  ORGANISM  Flavobacterium urumqiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Flavobacterium urumqiense"
                     /db_xref="taxon:935224"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119167
     Region          27..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv llvvlvaqlt faqeravsgv vsdnaglplp gvsvlvkgtq sgtqtdfdgk
       61 fsiratssqi lifsyigmkt qevmassatv nvklagsave legvvvtalg ikrevkalpy
      121 aaqtvkaeql nvtqsvdvkg alagkvagiq ingqagskig atgkirirga isltgdddal
      181 yvldgiavdp nsidmdniad vtvlkgpnat alygqravyg viqltskkgv kgrmtvdins
      241 sttfdkvayl pkyqnlygtg yegndswsnf dyaaggfgga yptewsvmdg krylrednny
      301 adeswgpkfd dkdylpwysw skdspyfgqt akysaqpnni kdfydtgvtk rnsftlsggg
      361 dnfrarlsyt nldqqgiqps tgqrknyias tmsydlsdkl kvdfmmnyst gtirgefdds
      421 ysnqtsgsfn swfgrqldvt klrelkdlkn gagyqatwnw wgpeyytlgg syqkpafwyn
      481 pytyleqfdy nqktdnltfs lsptykindn lsvagtfsrn qnnydrkyyf ptelslsaap
      541 dlynpwqnaf giyksvsted nydarinynv dfnelklttt agasvrnnay dristeidqt
      601 srvgglvlpd vytfsnasvt pitrpfiydk svksiyalan lgyknffyld gtvrrdwssa
      661 mpstangntt gsigaslift elmgkndvls fgklragyai igtdanalai npnypilnsh
      721 pynstnvaff nkqtivdpnl kfaqnasfea gldlkflsnr isfsatyyne nrkdeiisin
      781 vpnstgsyff ltnagetkrs gielslsgdv vkasnkdgfn wntslnfaqn ktqivsireg
      841 lsaingpggt ddwnlatvtq qegeewgqir gsaikrdang tkivnadgly eietnhdfgs
      901 vlpdftggly nqisykgitl aasldfqkgg kffslsetwg tysglleeta alnnnginvr
      961 edvdlanpsk sggvhvvgvn aigtaidtyv sanpyfaqfk gnniaepfvh dasylklrdv
     1021 slsytfsgar fnnvlqsatv givgrnlwli avskdnknrw dpselsggfg engqlpgtrs
     1081 lglnvkltf
//
LOCUS       WP_104000970            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            urumqiense].
ACCESSION   WP_104000970
VERSION     WP_104000970.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium urumqiense
  ORGANISM  Flavobacterium urumqiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Flavobacterium urumqiense"
                     /db_xref="taxon:935224"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111432
     Region          44..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiislnkgv galwytlifg lyfcctpala nkvlrqnqsl lqqiqirgsi tdgnnplpgv
       61 tisvkgkltt aisdyngqyt iaaspddtlv fsfmgfktvl ihidgqktin iqlkedattl
      121 kevlvntgyy svkesertgs iakitaaaie kqpvtnvlav mqgrmagvni tqttgvpggg
      181 fdiqirgkns lrtdgnnply iidgmpyase nvgntllsst ilsaaginpl nginpsdien
      241 ieilkdadat aiygsrgang vvlittkkgk sgkttftlna ysgtgkvtrt lnlmntpqyl
      301 emrreafand gftqypdway dingtwdqnr ytnwqkelig gtaltqniet avsggtsntq
      361 flirgtrfke ttvfpgnfay gktalhfnin hiadnnkfsi slsgnyvadk nnllgtdltr
      421 easvlspnap elydpngnln wenstwdnpl rlleekylak tnnltassai gykimpglev
      481 kttlgytdnr leeskkspst vynpawglns sasyfllnqa kkqswsiepq ltyqqevglg
      541 tfkilagatf qeqtreqqal yasgfssnsl ltniasaahi ailnndnsty rynavfgrvn
      601 ynlqqkyiln ltgrrdgssr fgadkhfanf gavgaawlfg kedfiskaip clsfgklras
      661 ygttgndqig dyqflntyss sgisyqgitg lqptrlynpd fswetnkkle valetgflkd
      721 rvllstayys ncssnqlvgi plpsttgfts iqanlnatve ntgwelelrt vnfqnrqfkw
      781 stmanatiar nkliafpgia astyanqyei gqpldirkvy hftginpqtg iyqfedynhd
      841 gaitapedrq nivhtnpnff gglqnsltyk nwqldflfqf vtqlginfny tgvlpgvgnn
      901 qpvavldrwq qpgdtsafqq ytagfnndav nafynysssd avftdasfir lknlsisytl
      961 pdswskigrc rlylqgqnll titrfkgpdp enqsqgslpp lrvltmgiql nf
//
LOCUS       WP_104003469             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacterium lutimaris].
ACCESSION   WP_104003469
VERSION     WP_104003469.1
KEYWORDS    RefSeq.
SOURCE      Marinobacterium lutimaris
  ORGANISM  Marinobacterium lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinobacterium.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Marinobacterium lutimaris"
                     /db_xref="taxon:568106"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55508
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipreve egerrvaltp evatqlhklg fslaietqag aaanfddeqy ravgveived
       61 prelwktsdi imkvrppkeh pelgfygvel lgkgqtlisf mypamnpeml qdlskhgvta
      121 lavdsvpris raqkmdalss maniagyrav veaaqhfgrf ftgqitaagk vppakvlvig
      181 agvaglaaig aaksmgaivr afdtrpevke qvesmdaefl mldfpdedga gtggyaktms
      241 pefikaemdl faaqaaevdi iittalipgk papeliterm vanmkpgsvi vdlaaeaggn
      301 cklteankvv vkhgvtligy tnlpsrlaaq asqlyatnlr hlltdlcpek ngeivvnmed
      361 evirgatvvk egevtwpppa prislapked vgikskaele kaeqkkahpl aflvplalsg
      421 lalfglgsva ppeflghltv fvlscfigym viwgvshslh tplmsvtnai ssiivigali
      481 qissdsplvv ilatlavfit sinivggfav tqrmlrmfrk
//
LOCUS       WP_104014918             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas jandaei].
ACCESSION   WP_104014918
VERSION     WP_104014918.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas jandaei
  ORGANISM  Aeromonas jandaei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas jandaei"
                     /db_xref="taxon:650"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53380
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mmvsshnrqs rlglaalllt tclgtsglaq aadeaqpkgk iearselfak dhadqfiswk
       61 atsesrertd alaedpnmvv lwagypfskd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvideq gedgyfkgmw akggpevvnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meayydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfeqtcrnc htqskemlqg ivkqrkeavi etklkvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdyaias hgvqmhapev alkvlgsald kaadartkla
      421 rllarkgish eiaipdistk eqaqaalgmd mkqfnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_104008290             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Jhaorihella thermophila].
ACCESSION   WP_104008290
VERSION     WP_104008290.1
KEYWORDS    RefSeq.
SOURCE      Jhaorihella thermophila
  ORGANISM  Jhaorihella thermophila
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Jhaorihella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Jhaorihella thermophila"
                     /db_xref="taxon:488547"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56193
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevm kgenrvamtp dsarqlqklg yecliekgag haagfddaay eaagvtvikt
       61 aaalwkeadi iakvrpptet elkrlnkgkt lisffnpaen ekgleiarek ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaavslg aivyafdvrp evaeqvesmg aefvyldfed dqdgaetggy akpsspefre
      241 aqlakfrela pdmdivitta lipnqpapil wtkdmiqsmk rgsvivdlaa erggnvegtv
      301 kdekivtdng vtiigytdfp srmaaqasql yatnirhmis dltpnkdgqi vhdmeddvir
      361 satvayqgei tfpppplkvq aiaskkpqaq pkeltpeekr eqelaafrae tkqqvtllti
      421 gtvlmllvgl vapasfmqhf ivfvlsvfvg fqviwnvsha lhtplmavtn aissiiilga
      481 lmqigsgswl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_104018858             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseovarius nitratireducens].
ACCESSION   WP_104018858
VERSION     WP_104018858.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius nitratireducens
  ORGANISM  Roseovarius nitratireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseovarius nitratireducens"
                     /db_xref="taxon:2044597"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55583
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevm egenrvamtp dsalqlqklg ydcaietgag eragfsdaay eeagveiikt
       61 aaalwkasdv vakvrvptet elkrlreglt lisffnpggn eagletaakk gatviamemv
      121 prisraqkmd alssmaniag yravieaggn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqvesmg aefvyldfee eqqdgsasgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvksm krgsvivdla aekggncklt
      301 vaddkivten gvtiigytdf psrmatqast lyatnirhmm tdltpekdgq avhdmeddvi
      361 rgstvthkge itwpppppkv aaiaaapake kpkeltaeek raqeiaafka qtkrqvtllg
      421 iggalvlgvg lvapasfmqh fivfllavfv gfqviwnvsh slhtplmavt naissiiilg
      481 aliqigsssi fitilaalav fmaainifgg flvtrrmlam fqks
//
LOCUS       WP_104022418            1138 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gemmatirosa
            kalamazoonensis].
ACCESSION   WP_104022418
VERSION     WP_104022418.1
KEYWORDS    RefSeq.
SOURCE      Gemmatirosa kalamazoonensis
  ORGANISM  Gemmatirosa kalamazoonensis
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Gemmatirosa.
REFERENCE   1  (residues 1 to 1138)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1138)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1138)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1138
                     /organism="Gemmatirosa kalamazoonensis"
                     /db_xref="taxon:861299"
     Protein         1..1138
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122985
     Region          32..1135
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrflrthstf wlagvlvalg sagraaaqap atingrvtsd agvplpganv iitelnisvg
       61 tnaqggftiq ipgarvngqt vqlrvrsvgf qptsrpvvvr sgtqtmnfel ktdvlrlsev
      121 vvtgvaegte rakvpfsvgr vtaadlpvpa ldpmkalagk vaglrvantg sgrpgtepei
      181 qlrgptsina tgrsngplii vdgaimnvgs lselggldie svevvkgaag aslygtraan
      241 gvitittkrg ssagqgirfg vrseygfsdl nsisygmpln hqlqldetgt rfcvagsqnv
      301 apcsrtvdwm keimrinnvn adttrtpvsl qwnaltvggg eltnvfqsqi wpgryfnpla
      361 qalqrnpitl nqvdatgtlg avrfyvsgsy qdekgairgl dgaqqrrarv nvdydirpdl
      421 nvsvstlydn gatdnrngga dggsifgqil rgiaigtdmq ardtlgrllv rsgganlrsp
      481 tgnggatvly dtenrisdqt sdrylgsits rytpaewvtv egtyaydsrs rvqrayrikg
      541 yrttsisaan nagnlsfdnr ydrsmngslt atlrkqlrsd lfgkltfrgl fddyllrtng
      601 lsaeqfvvsg iyradnatan kdinssreqv knvgwvtgas ldfkdrytvd gyfrydgssl
      661 fgsgnrwapy grisgvwqfs kepfwhigli ddarvrasyg tagtpprfsa qyetyniaat
      721 gpslgqagns klrpevtaet evgldftllh kvglelthar gttknqilpv napaalgfat
      781 qwqnagtlqn itwelvanlp viqkkefnws mrgswdrtrt yitelfvpdf vmdagtsqgt
      841 aslfhvtanr aksngfpqnr lgniwgrkfy rtcgdlpqsv qgqcgdgkpf qrndqgyivw
      901 vgqgntwrdg itknlwstyl pkdqspwnwp lyfghpivdr plkgepnegv ginqvignal
      961 pdfrlqfsnt vqwkrltlyg lvdgtfghdv nnqgeawgll dlsssefdqa nktvetakpv
     1021 gyswragytd gagtggfydq lgpnnynved asfaklrevs ltyhlgkvrg vgdwtfgvig
     1081 rnlltltgys gldpevgats annggsgtng sgsglinqvd afnfptlrsf tftvstrf
//
LOCUS       WP_104022438             973 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gemmatirosa
            kalamazoonensis].
ACCESSION   WP_104022438
VERSION     WP_104022438.1
KEYWORDS    RefSeq.
SOURCE      Gemmatirosa kalamazoonensis
  ORGANISM  Gemmatirosa kalamazoonensis
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Gemmatirosa.
REFERENCE   1  (residues 1 to 973)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 973)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Gemmatirosa kalamazoonensis"
                     /db_xref="taxon:861299"
     Protein         1..973
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104172
     Region          29..941
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msgprvfvfv fatlalaapl gaqpptgivr grvtqvggip mdaaqvsivg ttrgartnaq
       61 gvyrivgvpa gaqqvrvqli gfaaqtravt lrggdsvvvd felrpaavsl dalvvtgtav
      121 esrkkevgns maaisarele vapvkntqdi lgarapgitv lqnsgqpgag gtirlrgtns
      181 vtqgnnpiiy vdgiriysda gpispgsrqa tasyndikpe dierievvkg aaattlygte
      241 aapgviqift krgaagtpew sieagggana mghigssedp tgvfvnkcrg pdlrdsrdsl
      301 wvdptcpasg swlrtgavaq asvavkggaq qmsyylsgty dgeqgvvptg saksggaran
      361 fqfsprpslt fnvntaynrn etrfipdgnf awgfmlnvgr gsfgnfkggk gecagitttc
      421 vtnkyildqq atnsadhfit gltanwsplq altnrvaigy dynnvdsqdv ipfgyinlpl
      481 grldktdwnh tklsldyagt fqhtllglas tsswggqmfd drdkfigetg ndfsgpgdpt
      541 lgsaarvtlg rvdrprvvna glfvqqmfgw rdrlfvtggl rmdgnsafgs nfglqsypkv
      601 saayviseeg fwpkqllstm klraalgesg kapgafdavr twdpiagdeg kpgftpnqig
      661 npnlgpertr elelgfdaga fedrvslelt mfraktldal igvtypptqg ftrtqlenvg
      721 tlqnrgvevq lsgdilrldk lqwsgrvsyt amnskaidlg griismgssv yvregypvps
      781 yfgrkvtnpd aiaepvveqd qflgsaypnh llgvsttvrl frnlaldvlg eyqgggmlgn
      841 fvgyqnenrs vwypcygtqk airanqlqgv tamqrakcai dptkinsdyw ieptdffkir
      901 sasvawtvpk rfvpgaasam lilsgrnlwk stdydgldpe lrdasdqgat larreyyqlp
      961 pskqfllsar vhf
//
LOCUS       WP_104022512            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gemmatirosa
            kalamazoonensis].
ACCESSION   WP_104022512
VERSION     WP_104022512.1
KEYWORDS    RefSeq.
SOURCE      Gemmatirosa kalamazoonensis
  ORGANISM  Gemmatirosa kalamazoonensis
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Gemmatirosa.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Gemmatirosa kalamazoonensis"
                     /db_xref="taxon:861299"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109138
     Region          35..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrcirawaf gliagqaala sgaravqaqp qptavvrgsv vdsatrqpip naqivvgsta
       61 rgqtdaagrf llrsvpagtv tiraqrigfq prsrqvtlva gstadvdfvl raqaaimsdv
      121 vvvgygtrsr aevssavaqv ggenvrntpv agvdaalqgk apgvqvtqna gnpgngitvr
      181 irgassisas nqplyvvdgv pmiqdnvsqi gfggqgitav tglnpdeidr idvlkdaaaa
      241 aiygsrasng vvmittkrgn asaprfsfdv yyggqksarr lpllnakeyv afmneaaknd
      301 dedpadfgft pgvddttntd wqsavlrrap vsnfnltang ggdrfsyiis gsrfgqdgiv
      361 mgsgynrgsg rvnvdltatp kltfrssvav srehfdrten dntivgaqan sqanqpnvpi
      421 ykpgttefst sseglayanp vaiatfnkap antlralgni eaafeatsrl ringrvgadv
      481 ydyqerrwds prvidtyavg aqgvarqant taskyvgeaf adldalrsna qkltvtvgtg
      541 tefnhneily lrgegfgndq fqypgtagki vnydgqatqa nllsaftran yslkdryllt
      601 aslrtdgssr fgksrrwgvf paaslgwnls derflsglrr fataklrasy gttgnqsipt
      661 lygyltsyar anygstagia paalgnedlr westresdig ldlsfldgrv sviadyyskn
      721 ttdllvsrpv pttsgfasiw dnvgsvknag aelqlttvnf rskgrggfdw ttdvnlshna
      781 nkvtalyqdq pfasgiggvn yvaigqpigv fftqkfvgvd pqtgdaqyqk kdgtitkspv
      841 sadrqyvgsp hpkyfggvrn tmtwrnldln vfvqfsqgak vfdlfreysd dsgynydnki
      901 snvlkrwqkp gdvtdvpras fdgtsgaqiv ssryvedgsy vrlqdvtfgv rlpsalmsht
      961 gvsnarlyva gsnlklwtky lgydpdvnsn gsnanislgq dfyayprart isvglsgnf
//
LOCUS       WP_104022846            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gemmatirosa
            kalamazoonensis].
ACCESSION   WP_104022846
VERSION     WP_104022846.1
KEYWORDS    RefSeq.
SOURCE      Gemmatirosa kalamazoonensis
  ORGANISM  Gemmatirosa kalamazoonensis
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Gemmatirosa.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Gemmatirosa kalamazoonensis"
                     /db_xref="taxon:861299"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109623
     Region          54..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msvhsappag rpagtrgvgr alalvlaapp vvaplallva papaaavqpa aqgvvagvvt
       61 tqsgralsda qvvvdgttlg attdaaghfr itgasgttvr vtarrigyap ttvtarvgat
      121 dvtiamaerv lelnqvvvtg tagvaekrav gnavstvkaa dvvatqpvrn vqdlltgraa
      181 gvaviassgq vgtgsrirvr gasslsland pliyvdgvrv dnaqatgptv qafgsapvsr
      241 wndfnpedie sievikgpaa atlygteasn gviqiitkkg aagrpvanit ahlgsswlpg
      301 wkdgygytny gavqrqgaaa gvldtisiti aqlndslnah fghdifragv nrdveasvsg
      361 gpaqlkyyma lnhneddgve ranrlnksgv ranltaspwr kvdittalgy ttgrtylpfe
      421 sggggatwat ffssptflyn npgaatqtpn npqlgfrsgp pdiyyasyte fqgvnrftgs
      481 mtianrptgw ldhrliigvd qvdednqdqe prndiignty asfsgltgpn agyleidtrs
      541 vrnltadyal nakvalpwsm qsvtslggqf ygrrthlrgd dafgfpaagf lsltsgatqq
      601 ifrddlydnn tlggfvqeql iwkdrlyltg avrrddnsaf gtnypavtyp klsasyvlse
      661 epalhlpsai ntlrvraayg gsglqpgafd airtynavgg lltpsnagnt nlgpeksyet
      721 eigadvglfa dklgaevtyy tgytrdails rtaapsngfp glqlfnagrv nrnglewlvr
      781 atpyssrpvt ldfsvtgsft hqkikslapg tnqvvvssnv vhvvnyapga wwdrrivsad
      841 ynpttkktsn llcddgkggt vacasaprvy lgnsiptheg sisggatffq nlrlnafvdy
      901 rggykkldgn yrvrcgafal crdlyypdeq pnkavlaaeq agtaytfhli kdadfvrfre
      961 lsltytlpqr farriggsaa altvagrnlh lwtnytglep easfnsgtrg gaygfweqnv
     1021 lpqtrqivtt lnlsf
//
LOCUS       WP_104022884             993 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gemmatirosa
            kalamazoonensis].
ACCESSION   WP_104022884
VERSION     WP_104022884.1
KEYWORDS    RefSeq.
SOURCE      Gemmatirosa kalamazoonensis
  ORGANISM  Gemmatirosa kalamazoonensis
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Gemmatirosa.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Gemmatirosa kalamazoonensis"
                     /db_xref="taxon:861299"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105936
     Region          55..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpkrnlmmsr taallaigtl algspalaqq grisgtvtsa ddarpvaavq vvvvgttngt
       61 vtredgryti tarpgtyrvr airigyapds atvtvtdggd atanftlhpt atilstvvsi
      121 gygtqekrdr tgavevvdss qfnkgriisp dqlikakvpg vqvvdnnepg ggvavrirgg
      181 tsinasndpl yvvdgvplqv gggvsagrnp lnflnpndie gisvlkdasa taiygsrgan
      241 gvviittkqg krgtqvdyas svsssvvtgq pdmldaaqir aavqqyapen lnqlgnastn
      301 wrdliernag gqehtlgisg mredmryrvs lgyldqggvl igtdtrrasl gvnyadqlfa
      361 krlevtaslk gsrsddkftp ggvlsgatlf sptlapytan ggftqyanil aaanplsela
      421 yisdagrtyr signvearyk tpwvpglsat vrggydvata erttftsslq hgqvgadnpg
      481 tfyrnspeqt glvletfgny vhdvgakstv dltagytyeq angdypsfta rglasnllgp
      541 ngvpaakqvd qfltqdeskl vsgfaranls ladrylltls vrrdgssrfg panqwgwfps
      601 aalawrvine pwfqnhagpf sdlklrvsyg vngnqafgny lqystytyan nlaqvqfgnt
      661 fvtpirpsav dpdikweqta stnfgvdygf ldnrftgsve vynkkttnli fnvpvaagtn
      721 lsnfvttnig smqnrgvefg ltaqvleggs rglsytasfn aatntnkllr itgagsdqia
      781 vggiaggvgt tiqvlqpgvp vnsffvyrhr tdasgnpvvg dkpdsalyvd qngdktinqa
      841 drvaykspqp kwilghtsnl ayrrvdlnft lrsylgnyvy nnvasnlghy dalkgiwpsn
      901 lqasvlkngf vkmqsfsdly vedasflrld nvtlgytfkq prgfralrly gsvqnvftlt
      961 gysgldpaag lngidnniyp lsrtfsagin vgf
//
LOCUS       WP_104023246            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gemmatirosa
            kalamazoonensis].
ACCESSION   WP_104023246
VERSION     WP_104023246.1
KEYWORDS    RefSeq.
SOURCE      Gemmatirosa kalamazoonensis
  ORGANISM  Gemmatirosa kalamazoonensis
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Gemmatirosa.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Gemmatirosa kalamazoonensis"
                     /db_xref="taxon:861299"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117949
     Region          43..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miresvrrsf rpaaavaava ltvasarvvs aqqpaprgsg saiegtvrdv asgrplanaq
       61 vlivnstlga atnengtyri anvpvgpavq vrvrligyga qsktvavtlg qtaradfdlq
      121 qsalqldqvv vtgtgaavet kklgntvati ntedlksapi qnpsellaar tpgvqvlpsg
      181 gttgsgarir irgnaslsqs nnpviyidgv radnggssag gasnssrled idpssierve
      241 vlkgaaaatl ygteasngvi qiftkkgsqg parwtvdlsr saitypdrva pnagfarnqa
      301 kadtlgrifg ltlqpfqpfe ynvtkqlwet gfnntasasv sggaekvnyf vsgryeyedg
      361 pftsnkianp tdvkadlaqd llkrnqatvs lnvlptdkit igfqthytvf rldgiqgqns
      421 iyspyaesmy akpdsascng pdgkhsldyi ggvarcqltg npfgnstfts lresvqqqay
      481 qdgthytgsl sarwapqekl nlaatvgldn tdvravsyyp fgnnvdlist qaplgtrsvn
      541 dlrtqnvtvd tkgnwtsrlg safesqltlg aqgymvtqks engsgrdfpg pglavtgaga
      601 tqsssegyir vvnagyfaqe qlgfhnwifg tvgarydyns afgesaggvl ypklsvsvvp
      661 sdrggwnwtt lsslrlraai gksgrqpgaf dkfttyapln astgsglvpd nlgnpdlkpe
      721 vtteieggfe aglfsnraql satywtrtlk daliskqfpv sggfssrqlt nigrldahgi
      781 elalngfvvn ranfavdlfa ngsylsqkvv slggappikv qgsyvrirgf ikegytpgal
      841 fgvkifqpcs syrnpatdak ggcyqagetp ydqnrdgkpd teaqlravla npinptnlvl
      901 lradddgnkl fddhyqgkpf pdwqgafggn vrlgkawrla nvfeykaghy tisdltdsfr
      961 nasptlgrnr ieaarveatl lnpastader faaaqqwlgl valspydgyn qnkpgdfvrw
     1021 revsltyttp hafaskigar elslvaaarn lvlwtrypgt dpevnyngts nslssaqtdn
     1081 nfyeasdvfg lpiprrftfs arlaf
//
LOCUS       WP_104023523            1016 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gemmatirosa
            kalamazoonensis].
ACCESSION   WP_104023523
VERSION     WP_104023523.1
KEYWORDS    RefSeq.
SOURCE      Gemmatirosa kalamazoonensis
  ORGANISM  Gemmatirosa kalamazoonensis
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Gemmatirosa.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Gemmatirosa kalamazoonensis"
                     /db_xref="taxon:861299"
     Protein         1..1016
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108167
     Region          31..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrntpwhva lvvllgsgla rqaaaqatgi vrgtvtdsat qrpvigaqvt vgsgargavt
       61 ndagiyvvrg vpagdallrv qrigyasaer rvavdangvt tvnvtitpva tvlstvvsvg
      121 ygtssratvt saiasvdsta irnapvaald nalqgkiagv qvvqnsgepg sgvsvrvrgp
      181 aslnagnqpl yvvdgipitq gafeqisqsg qdqtaisaln pdeiasidvl kdaaaaaiyg
      241 srgsngvili ttkrgtagrm rfslnayggt qrvekkigll naqqyvelmn esakndgyav
      301 sdydfvpgkd daqsfdwqda vfrraavsda qlamsggsdr fryflsgsnf dqrgivigsg
      361 yrrqagrvnl dlhagdrlll ttslgltred ddripgdlsl dgvvtnaigm qpmrpilgns
      421 fgfggttegl kysnpvaiar ynqnnyqtlr alghaeakys vadgfsltgr vgadvfnide
      481 lqwgspkvda tsakslngig rdghtaidky vmegfftaep lraannnlsi tggssleynr
      541 rylsylrgeg fptgfttyvr natnvtswdg srsdnnlvsf ftranwtlan rylvgaslra
      601 dgssrfgkdn rygifpaasv gwvvtdepal sglarigtlk lrgsfgvtgn qgigdyasln
      661 laagapyaga pgvagtqlgn anlkwettke tdigadfgff dgrisviadw yerntsdllv
      721 qrpipvtsgy ssiwdnigsi rnrgvdlglh tvnldgargs lglgwtsdln vtwnrntvte
      781 lyggqpvtft vssrvtsaaa vghplgefym ykvlridpqd gnvvfakasg getksptsad
      841 lmfvgspqpk yyggftnvlt wktldlrgfl qfsqgnkvfn mmriftddgg ysydnkstlt
      901 ltrwqkpgdi tdeprfsydg tsgarlmssr miedgsfvrl geitlgwklp trlvtstgld
      961 narlyvsgrn lktwtkysgy npdvsssgaa anvitgvdyy ayplartfsl glsagw
//
LOCUS       WP_104023526            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gemmatirosa
            kalamazoonensis].
ACCESSION   WP_104023526
VERSION     WP_104023526.1
KEYWORDS    RefSeq.
SOURCE      Gemmatirosa kalamazoonensis
  ORGANISM  Gemmatirosa kalamazoonensis
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Gemmatirosa.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Gemmatirosa kalamazoonensis"
                     /db_xref="taxon:861299"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106695
     Region          44..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpptaarrla patppilggw lllvtlalga pdlraqptsg ptgvvagtvt dgvahtpltg
       61 vavaldgtrf gaatgadgry ritgvpagty taiarrigyn ptrlsvtvta greatadfgl
      121 qasaialdqv visgtagetq rrevgnavat idaatalqqs aapnvaslln arapgvavrq
      181 rtgrlgagpt ievrgrssls lenspliyvd gvrvnnqtss gpqavagrlg gqgsqvggrl
      241 ndinpddies ievikgpaaa tiygteaang viqiitkkga agaapqisaq veegslefan
      301 avdrvqtnyf kdptsgqivt wnglqqeads grpiyktgqt rkftgslsgg rdalryylgs
      361 tyendlgiep nnslrqfslh tnlnssvrps telamsvnyv agdthlgady gaspllgaqv
      421 ghrllfagtr gffavppevp qqlydnstrv drftgsatit nrpaswftqr aivgldyags
      481 deralerfap peiaryltaa aaggaigqtl rhnsvftgdy ngsarvslts alsskssvgg
      541 qfyktalnss flggtafpap gvdivsgtta pvassqseti nttigayaeq qfgwhdrlfl
      601 sgalrvdnns afgedfkwvt ypkvsaswvv neepfwerwr navntlrlra aygesgrqpa
      661 afsalrtfaa ttgpggssav tpnslgnpdl kpergkevel gfeaglynrl tldftyynkk
      721 tydeivqqpv apssgfpgtq yrnlgqvdnk gvelsanlra varrtvswdi nanvatnkdv
      781 irdlgglpti iasygaanvv gypiggifvr hvisaernat tgqatnilce gpngtgvaca
      841 tapfvfwgtp tpkvtgavss tvtlwqrlsl ygladfrrgn klqnsvellr ctgavggalc
      901 ranyypqeyd plylaetnin avalgtvdqy iqdagftklr eisatytfpe ritrartslt
      961 iagrnlytwt kyrgidpesn innaatttat ldqavtpplr sfvatvrvtw
//
LOCUS       WP_104023557            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gemmatirosa
            kalamazoonensis].
ACCESSION   WP_104023557
VERSION     WP_104023557.1
KEYWORDS    RefSeq.
SOURCE      Gemmatirosa kalamazoonensis
  ORGANISM  Gemmatirosa kalamazoonensis
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Gemmatirosa.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Gemmatirosa kalamazoonensis"
                     /db_xref="taxon:861299"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110154
     Region          28..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mavvrylmla avggalwsaa ahaqatgtis grvvdstaqq pitnatiaiv gtqrgtltrn
       61 dggfvmsgip sgtirvraar igftaqeqev tvpsggtvsv sfalhpvaav lseivtvgyg
      121 tqrreaitgs vatvkaedan vgvvpnaqam lsarvagvnv tlnngepgag aqirirggts
      181 lsasndplyv vdgvplqndq tvatggangv ggslprspln aispddiasi tvlkdasata
      241 iygsrgangv vlietkrgat grnssnmeyd gyvaaaapss klgflsgney rafvtqqaaa
      301 givpqstvaa lgnantnwed eitrtslsqn hslsfsggsa atqyraslny fdqngvvidn
      361 glqryqarln aqnqslngkl qlganlmasr vnnrylafen tggftggvft nvavfnptfp
      421 vidpktgkyy elgagsqsvr npvalaaqvd drapenrvlg nvsgslslls sltakttvgv
      481 dyagsvrrtf lprdnpvgaq tnglarqedr dltninfqql ltwtphfsda heidvvggye
      541 ytkfdntgft aeshdfitna fsvynlgagv qasspppgsy reqsllasff grmnygyhnk
      601 yfltgvlryd gssrlakgne walfpavsas whlseegfmk gnffsnlnlr agwgrqgnqa
      661 vrpyatelll radngarypf gsgittglva aqvanpnlkw etaqqtnvgl dygfrnnrit
      721 gtldlyqkdt kdlllsvpvp qpavvtnqiq nvgsirnrgv eaqidadlwq sgqrslssgl
      781 vltvernevv slgtgtnfil tgvvsgqgqs gkfaqrlipg kpvgtfwgae yvgvnaqgqq
      841 lfnkydvtrd akgnetsrkl agtttapsad detiigdanp afslglrsnl twhkldaswl
      901 wrgefgrdvf nntalvystk saisqgrnfm rsalsdpigv kepaiysskw iedgsfvrlq
      961 nvtlgysfnl psmagsrpar lyvsgdnlll ftgysgydpe vfvragddit gsasrgidyl
     1021 vyprartftt gvriqf
//
LOCUS       WP_104023559            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gemmatirosa
            kalamazoonensis].
ACCESSION   WP_104023559
VERSION     WP_104023559.1
KEYWORDS    RefSeq.
SOURCE      Gemmatirosa kalamazoonensis
  ORGANISM  Gemmatirosa kalamazoonensis
            Bacteria; Pseudomonadati; Gemmatimonadota; Gemmatimonadia;
            Gemmatimonadales; Gemmatimonadaceae; Gemmatirosa.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Gemmatirosa kalamazoonensis"
                     /db_xref="taxon:861299"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110000
     Region          29..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvrprckisl lvggllvavr lgaqaptgtv sgrvidstsr lpvtnanvvi egsqrgtvtr
       61 adgayviagv pagpqrvrvs rigyaaqtrd vtvtaggtve aqfaiasaat altevvvvgy
      121 gtqrreaitg svatvnadda kvgritapte llqgrvagvt miqnngspga gvqvrirggt
      181 sisasneply vidgvplnnt aieptslgsg dnrntslprn plssidpsdi etitvlkdas
      241 ataiygsrga ngvvqittkh gregrtelty egyfssssps ktldvlngde yrafvqqqvt
      301 agnlaasrlt glgtsntdwe kevvrtahtq nhnlgfsgga astqyrgsln ymqqegivls
      361 sglerisgri nagqqafanr lrmglnlnas qvkndyvpse ntagftgttf tnmlimnptq
      421 pvrvtdpstg vsryyeigtg avtirnpvai tdqvkddgvs rrilgnftad ydlfssltaq
      481 lnvgtdrsng trsayypris plgastngda lygelanttn tlqtyltyra spgphslell
      541 ggyefnnyst vsenseaqgf itdafayynl gagatlqqgf vtsgrtdsrl vsffgranys
      601 lkdryfltgv vrrdgssrfg agnkwavfpa vsgswlmsae pfmkgllgsv vselrlkagy
      661 glngsqeisp ysslltlatg pkasfgettv lgvspnrnpn pdlkweqtaq tnvgldfail
      721 dgrfsgtvey ylkntrdlll tinvpqpavt dtvlanvgav rnkgleftld artisrprld
      781 ltlgvlgsve rnrvvslgkt afitsgnvsg qgqtgqvsqr impgfplgtf ygpeyvgvda
      841 ngrqlfnkyk vtknaagvit sreltaqttt ptaddynvlg nanpkfslgg hgqlragqld
      901 asflvrgvfg qkvlnntalv ystkgnalqd knflksalnd pigikepaif ssrwiedgsf
      961 vrlqnvtvgy tvrlpsgtha rqarvyvtgd nlimstnytg ydpeaftsag rasrgvdyln
     1021 ypnprtvslg vrvgf
//
LOCUS       WP_104024703             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            hyugaensis].
ACCESSION   WP_104024703
VERSION     WP_104024703.1
KEYWORDS    RefSeq.
SOURCE      Vibrio hyugaensis
  ORGANISM  Vibrio hyugaensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio hyugaensis"
                     /db_xref="taxon:1534743"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53102
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmstp iavatlfasq lflvgaplaa edkglidprn dafeqnhpdq yhswkatses
       61 ehiedalged pnmvilwagy gfakdynkar ghfyalddvr qtlrtgaptd eksgpmpmac
      121 wsckspdvar vidergedgy fegkwarlgs eivnpigcsd chdtrseefk ngepalavtr
      181 pyverafdti gkkfdeqsrl dqqasvcaqc hveyyftgpt kavkfpwdmg tsvndmekyy
      241 dalnfkdwth avskapmlka qhpgyetwre gihgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfdd tcaqchtqtk eqlqgivstr kaqvlnmklt aekqivsahf eagaawdaga
      361 teeemqpilq dirhaqwrwd yaiashgvhm hapevalevl gtavdraada rtklvrllak
      421 kgitepvqip distkakaqq algmdmekmn adkkdfleti apdwdkaaae reaty
//
LOCUS       WP_104025394             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            hyugaensis].
ACCESSION   WP_104025394
VERSION     WP_104025394.1
KEYWORDS    RefSeq.
SOURCE      Vibrio hyugaensis
  ORGANISM  Vibrio hyugaensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio hyugaensis"
                     /db_xref="taxon:1534743"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54677
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvaiesqag vlasfdnaay eaagativss
       61 devwqsglil kvnaphvgee ngideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgrpap tlitkemvds mkagsvivdl aaanggncey
      301 tekdkvitta ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg nididfedvv
      361 lrgvtvvkeg eitwpappiq vsaqpqaktq epvkkepkve eptspvkkfa plviglgafg
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_104037853             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            jasicida].
ACCESSION   WP_104037853
VERSION     WP_104037853.1
KEYWORDS    RefSeq.
SOURCE      Vibrio jasicida
  ORGANISM  Vibrio jasicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio jasicida"
                     /db_xref="taxon:766224"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53100
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmstp iavatlfasq lflvgaplaa edkglidprn dafeqnhpdq yhswkatses
       61 ehiedalged pnmvilwagy gfakdynkar ghfyalddvr qtlrtgaptd eksgpmpmac
      121 wsckspdvar vidergedgy fegkwarlgs eivnpigcsd chdtrseefk ngepalavtr
      181 pyverafdti gkkfdeqsrl dqqasvcaqc hveyyftgpt kavkfpwdmg tsvndmekyy
      241 dalnfkdwth avskapmlka qhpgyetwre gvhgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfdd tcaqchtqtk eqlqgivstr kaqvlnmklt aekqivaahf eagaawdaga
      361 teeemqpilq dirhaqwrwd yaiashgvhm hapevalevl gtavdraada rtklvrllak
      421 kgitepvqip distkakaqq algmdmekmn adkkdfleti apdwdkvaae reaty
//
LOCUS       WP_104034915             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            jasicida].
ACCESSION   WP_104034915
VERSION     WP_104034915.1
KEYWORDS    RefSeq.
SOURCE      Vibrio jasicida
  ORGANISM  Vibrio jasicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio jasicida"
                     /db_xref="taxon:766224"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53072
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmstp iavatlfasq lflvgaplaa edkglidprn dafeqnhpdq yhswkatses
       61 ehiedalged pnmvilwagy gfakdynkar ghfyalddvr qtlrtgaptd eksgpmpmac
      121 wsckspdvar vidergedgy fegkwarlgs eivnpigcsd chdsrseefk ngepalavtr
      181 pyverafdti gkkfdeqsrl dqqasvcaqc hveyyftgpt kavkfpwdmg tsvndmekyy
      241 dalnfkdwth avskapmlka qhpgyetwre gihgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfdd tcaqchtqtk eqlqgivstr kaqvlnmklt aekqivaahf eagaawdaga
      361 teeemqpilq dirhaqwrwd yaiashgvhm hapevalevl gtavdraada rtklvrllak
      421 kgitepvqip distkakaqq algmdmekmn adkkdfleti apdwdkaaae reaty
//
LOCUS       WP_104043783             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. ZGTC412].
ACCESSION   WP_104043783
VERSION     WP_104043783.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. ZGTC412
  ORGANISM  Arthrobacter sp. ZGTC412
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Arthrobacter sp. ZGTC412"
                     /db_xref="taxon:2058900"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40125
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiprerr egerrvaatp etvkqlaalg veilleagag apaghpdady rqagasivpe
       61 ldeaqldvlt hvrpldpqtv atlkrgavtv glaspsselp tvqalaeagv tsfalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplymtaa gtvpparvlv lgagvaglqa
      181 igtakrlgar vfandirpas adevasmggt firldletae aaggyarqls sdagtrqrql
      241 laphvaqadv littaavpgr rapllvttem vqgmrpgsvv vdlaaesggn vegavpgqdi
      301 piltadgsgy vtlvglkdap sampydasrl yaknvanlla lmirdgalap dfadevlaga
      361 clthdgavrh rptaellaar agsrregil
//
LOCUS       WP_104046639             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            jasicida].
ACCESSION   WP_104046639
VERSION     WP_104046639.1
KEYWORDS    RefSeq.
SOURCE      Vibrio jasicida
  ORGANISM  Vibrio jasicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio jasicida"
                     /db_xref="taxon:766224"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53101
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmstp iavatlfssq lflvgaplaa edkglidprn dafeqnhpdq yhswkatses
       61 ehiedalged pnmvilwagy gfakdynkar ghfyalddvr qtlrtgaptd eksgpmpmac
      121 wsckspdvar vidergedgy fegkwarlgs eivnpigcsd chdtrseefk ngepalavtr
      181 pyverafdti gkkfdeqsrl dqqasvcaqc hveyyftgpt kavkfpwnmg tsvndmekyy
      241 dalnfkdwth avskapmlka qhpgyetwre gihgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfdd tcaqchtqtk eqlqgivstr kaqvlnmklt aekqivaahf eagaawdaga
      361 teeemqpilq dirhaqwrwd yaiashgvhm hapevalevl gtavdraada rtklvrllak
      421 kgitepvqip distkakaqq algmdmekmn adkkdfleti apdwdkaaae reaty
//
LOCUS       WP_104062240             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. 4R501].
ACCESSION   WP_104062240
VERSION     WP_104062240.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. 4R501
  ORGANISM  Arthrobacter sp. 4R501
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Arthrobacter sp. 4R501"
                     /db_xref="taxon:2058886"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52969
     Region          3..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivael gretrvaatp ttvkqllglg yevvvekgag esasfrdeay aeagavivga
       61 deawgsevvl rinppteeei grlaegatli gslspglrpe lvaalaarpi talaldavpr
      121 israqsmdvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksiggt ylkvevaeem kssdgyakat seaynaraae
      241 iyseqaadvd iiittalipg rpapklltae dvagmkagsv ivdmaagqgg nvvgsvager
      301 vvtdngvvil gytdlparlp aqasqlygtn mlnllklltk dkdgqlridf ddvvqrsvtv
      361 vrdgektwpp ppvqvsaapa atahgpases tapkkkqgls aagkaglfaa giavlfvvna
      421 vapaplpqhf tvlmlsvvvg fyvigkvhha lhtplmsvtn aisgiivvga llqvtsenpv
      481 mqvlaavavl lasinifggf avtrrmlamf sagkars
//
LOCUS       WP_104062898             402 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. 4R501].
ACCESSION   WP_104062898
VERSION     WP_104062898.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. 4R501
  ORGANISM  Arthrobacter sp. 4R501
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Arthrobacter sp. 4R501"
                     /db_xref="taxon:2058886"
     Protein         1..402
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41224
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiprerh egerrvaatp etvkqlaglg ldvlieagag aaaghsdhdy adagarivqd
       61 ldpgelnvlv hvrpleppta aalkrgavtv glaspssela tvqalveagv safalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplymtaa gtvpparvlv lgagvaglqa
      181 igtakrlgar vsandirpas adevasmggt fikldletae asggyarels adrgalqrel
      241 laphvavadv littaavpgr rapllvsrqm vqgmrpgsvv vdlaaesggn vegvvpgedi
      301 lvptadgqgh vtlvglkdap samaqdasrl yaknvanlla lmvrdgtvap dfdddviaga
      361 clthdgdvrh lptaealaal vpalpdhapr vqddrvqneg gi
//
LOCUS       WP_104069711             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Albidovulum inexpectatum].
ACCESSION   WP_104069711
VERSION     WP_104069711.1
KEYWORDS    RefSeq.
SOURCE      Albidovulum inexpectatum
  ORGANISM  Albidovulum inexpectatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Albidovulum.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Albidovulum inexpectatum"
                     /db_xref="taxon:196587"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56068
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkeva kgearvaltp esathirklg hecfiesgag aaagfedaay eaagvtvikt
       61 aaalykavdv vakvrpptet evkrlrkgqi lisffypaqn kklmelaakq gatiiamdmv
      121 prisraqkmd alssmaniag yravieaann fdrfftgqvt aagkvppakv lvvgagvagl
      181 aaigasvslg aityafdvrp evaeqiesmg anfvyldfed snqdsastgg yaapqseefr
      241 qkqlekfrel apemdivitt alipgrdapk lwtedmvkam krgsvivdla aerggncelt
      301 rpdekivten gvtiigytdf psrmasqsss lysnnirhml sdltpnkdgq ivinmeddvi
      361 rsatvthege itfpppppkv kaiaapkpke kpreltpeer ramemaefre qtkrqaillg
      421 vggaallavg svapasfmqh fivfvlavfv gfqviwnvah slhtplmavt naissiiilg
      481 almqvgsgsa lvvilaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_104094930             412 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Terrimesophilobacter mesophilus].
ACCESSION   WP_104094930
VERSION     WP_104094930.1
KEYWORDS    RefSeq.
SOURCE      Terrimesophilobacter mesophilus
  ORGANISM  Terrimesophilobacter mesophilus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Terrimesophilobacter.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Terrimesophilobacter mesophilus"
                     /db_xref="taxon:433647"
     Protein         1..412
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41714
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvgvtreqr agerrvaatp etvqqltalg ldvvvekgag desgysdaay keagatiaak
       61 lalgaldvlv hvrplspata kalkkgavti glaspstelp tvaalaagkv tafalelipr
      121 israqsmdal ssqalvagyr avieavmryp rffplymtaa gtippakvlv lgagvaglqa
      181 igtakrlgar vsandiraas adevrsmggt finldldtaa egtggyakel aedrakrqrd
      241 llaphvaasd ilittaaipg raapllvtty mvkgmragsv vidlaaesgg nvegvvagad
      301 tpvavdggtv tlvglqdaps aipsdasrly aknvanllai mtadgtvspd ysdevvagac
      361 ltrdgtvvhe ptanalaqsk paptkkpasa akpatrkpat gkkpvttkkg ak
//
LOCUS       WP_104108309             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides sp. 616].
ACCESSION   WP_104108309
VERSION     WP_104108309.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. 616
  ORGANISM  Nocardioides sp. 616
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nocardioides sp. 616"
                     /db_xref="taxon:2268090"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52681
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigiprear pgetlvaata ktaeqltklg ydvvvesgag qaadlrdesy aeagirvgda
       61 devwssdvvv kvnaptdpei arlrrgatvv slmaparspe lveklaaagv talamdavpr
      121 israqsmdvl ssmanvagyr avieaahvfg rqftgqvtaa gkvpparvfv vgagvaglaa
      181 igaagsmgai vrafdvrpev aeqvesmggq fvtvdmesev ssdgyakemt aeqeaatalm
      241 ydeearnadi vittalipgr paptlitaet vaamqpgsvi vdmaaanggn caltqtgdkv
      301 vtdnlvtilg ytdlagrlaa qtsqlfgtnv vnlfklltpe kdgqmvldmd dvvqrgitvv
      361 fdgetmwppp pvqvsaapaa pvaaqpapae pkkpadprrk vfaaalaavl faalatvspp
      421 eflshftvla lavvvgyyvi snvahalhtp lmsetnaisg iilvggilqv gstnvlvsvl
      481 aviavlvasi nifggflvtl rmlemfrkd
//
LOCUS       WP_104124984             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter soli].
ACCESSION   WP_104124984
VERSION     WP_104124984.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter soli
  ORGANISM  Acinetobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter soli"
                     /db_xref="taxon:487316"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39838
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipteti agenrvaatp etvkklisag hrvliergag vraayidsay eqvgatited
       61 vysgsqlilk vrapqgdeiq klaahttvva mfdpyrnpdl dtfasqnvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak eqveslggkw ldvpmspeeq aradeaakng ygwapgeqyi
      241 kdqaaivdka vsnadivitt allpgrnapr likaetvakm kpgsvildma vetggnvegs
      301 kvgetvften gvkilgvpni pstlsteasa lyarnvfnfv etlfdqdknf ainpeeeiqk
      361 allvthgghv llkrg
//
LOCUS       WP_104139397             424 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. ZGTC131].
ACCESSION   WP_104139397
VERSION     WP_104139397.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. ZGTC131
  ORGANISM  Arthrobacter sp. ZGTC131
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Arthrobacter sp. ZGTC131"
                     /db_xref="taxon:2058898"
     Protein         1..424
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43419
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlgiprerr egerrvaatp etvqqlaglg levlvesrag aaaghsdedy rqagaqivpd
       61 ldpaeldvla hvrpidpata rslkwgavtv glaspstela avqalaeggv tsfalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplfmtaa gtvpparvlv lgvgvaglqa
      181 igtakrlgar vsandirpss aeevtsmggt fikldletae asggyarels adrgalqrel
      241 laphvadadv littaavpgr rapllvtrsm vqgmrpgsvv vdlaaesggn vegsmpgrdi
      301 hvptadghga vtlvglkdap sampadasrl yaknvanlla lmtrdgtvsp dfdddvvaga
      361 clthdgvvrh aptaealasl agqtaapeqg apeqspaeqa vpepasppks elsgekasen
      421 egva
//
LOCUS       WP_104150552             364 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium intracellulare].
ACCESSION   WP_104150552
VERSION     WP_104150552.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium intracellulare
  ORGANISM  Mycobacterium intracellulare
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Mycobacterium intracellulare"
                     /db_xref="taxon:1767"
     Protein         1..364
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37155
     Region          7..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdaqttvgv vsesgaderr valvpkavas lggsgvavvv esgagerall pdalyteaga
       61 tigdawaadi vvkvapptad evgklhsgqt ligflaprna ensigalkqa gvqafaleai
      121 prisraqamd alssqgnvag ykavllaase atrffpmltt aagtvkpatv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwlelgise titaageggy areltdeera
      241 qqqqalekai sgfdvvitta lvpgrpaprl vtaaaveamk pgsvvvdlag etggncelte
      301 pgktvvkhdv tiasplnlpa tmpehasely sknitalldl lltdgklapd fddeviadsc
      361 vtrd
//
LOCUS       WP_104155728             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pokkaliibacter plantistimulans].
ACCESSION   WP_104155728
VERSION     WP_104155728.1
KEYWORDS    RefSeq.
SOURCE      Pokkaliibacter plantistimulans
  ORGANISM  Pokkaliibacter plantistimulans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Balneatrichaceae; Pokkaliibacter.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Pokkaliibacter plantistimulans"
                     /db_xref="taxon:1635171"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55001
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeih hgearvattp evaaqlqklg yhislesgag eaakyrdedy aaagveivsd
       61 vqalwqsadi ilkvrapqhh phlstheadl lragqtlvsf mapgqnatll etlasknvna
      121 laidmvpris raqkmdalss maniagyrav veaaqhfgrf ftgqitaagk iapakvlvig
      181 agvaglaaig taksmgaivr afdtrpevke qvesmdaefl mldfkedgsg sggyaktmsk
      241 efieaemalf aeqakevdii ittalipgkp apelitedmv ksmkegsviv dlaaeqggnc
      301 klseadkvvv khgvtligyt nlpsrlasqa sqlyatnlrh lltdmtpgkd gilqinfddd
      361 vvrgatvvka geitfpppap klsakpaapk psvskaprqe ekkehkhssp lwliagalvf
      421 lllgmtapas fmghftvfil scfvgymviw nvtpslhtpl msvtnaissi iiigallqis
      481 apsgwvvffa aiavlltsin ifggfavtqr mlamfrk
//
LOCUS       WP_104163755             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cryobacterium sp. N22].
ACCESSION   WP_104163755
VERSION     WP_104163755.1
KEYWORDS    RefSeq.
SOURCE      Cryobacterium sp. N22
  ORGANISM  Cryobacterium sp. N22
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Cryobacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Cryobacterium sp. N22"
                     /db_xref="taxon:2048290"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38489
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvgigrerr egekrvaatp etvtqltalg vdvtveagag laagysdaay enagaqlvad
       61 fdatafdvlc hvrplspela atlpagiitv glaspaselp tvaalaaarv tsfalelvpr
      121 israqsmdal tsqalvagyr avleatirfp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsaydvrpas adevtsmggt fisldlaave gsggyasela edravrqrel
      241 laphvakadv littaaipgr papllvtrqm vagmpagsvv idlaaetggn vegvlpgvdq
      301 avptaagdgi vtlvgmrdaa samasdasrl yaknvanlla lmtsdgqvvp dfadeviaga
      361 cltadgevrh aptaaalegk n
//
LOCUS       WP_104175226             394 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. Y81].
ACCESSION   WP_104175226
VERSION     WP_104175226.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. Y81
  ORGANISM  Arthrobacter sp. Y81
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Arthrobacter sp. Y81"
                     /db_xref="taxon:2058897"
     Protein         1..394
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40579
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgivrerr dgerrvaatp etvqqliglg levlvesrag taaghsddsy vragarivpe
       61 ldpgsldvla hvrplepata avlrrgavta glaspstelp tvralaaagv tsfalelvpr
      121 israqsmdal ssqalvagyr cvleaamrlp rffplfmtaa gtipparvlv lgvgvaglqa
      181 igtakrlgar vsandirpas adevtsmggt fikldletae asggyarels adrgalqrrl
      241 laphvaqadv littaavpgr rapllvsrem vqgmrpgsvv vdlaaesggn vegsvpgqdi
      301 lvdtadgqgt vtlvgmkdaa sampadasrl yaknvanlla lmvrdgtlal dfsdevvagt
      361 clthdgevrh aptaealals ddpgnresen egvv
//
LOCUS       WP_104176257             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. Y81].
ACCESSION   WP_104176257
VERSION     WP_104176257.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. Y81
  ORGANISM  Arthrobacter sp. Y81
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Arthrobacter sp. Y81"
                     /db_xref="taxon:2058897"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53614
     Region          3..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivgel gretrvaatp vtvrqllelg yevvvekgag dsasfadday aaagamivga
       61 deawgsevvl rinpptedei grlaegatli gtlspglrpe lvealaarpi talaldavpr
      121 israqsmdvl ssmaniagyr avieaahefg wfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksiggt ylkvevdevm assdgyakat seaynrraae
      241 iyseqardvd iiittalipg rpapklltae dvagmkpgsv ivdmaagqgg nvegsvager
      301 vvtdngvvil gytdlpgrlp aqasqlygtn mlnllklltk dkdgqlridf ddvvqrsvtv
      361 vrngekiwpp ppvqvsaapa gqtdatragv saanktakkt glspvgkagl iaggiailfg
      421 inavapaplp qhftvlmlsv vvgfyvigkv hhalhtplms vtnaisgiiv vgallqvtsd
      481 nivmqiiaav avllasinif ggfavtrrml amfsrgnrad g
//
LOCUS       WP_104202083             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Billgrantia saliphila].
ACCESSION   WP_104202083
VERSION     WP_104202083.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia saliphila
  ORGANISM  Billgrantia saliphila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Billgrantia saliphila"
                     /db_xref="taxon:1848458"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55803
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela kgearvaltp esaqhirklg hecliesgag vaagfddday raagvtvles
       61 aealwheaev vikvrepsee eaerlregqt lisffwpaqs eallercrar gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfde nqdgsatggy aapsspefre
      241 kqlqcfreqa pdvdivitta lipgkpapkl wledmvkamk pgsviidlaa ekggncdltr
      301 pdervvsdng vivvgytdfp srmatqasll yatnirhmlt dltpekdgki vhdmeddvir
      361 gatvthqgei tfpppppkvk aiaaakpkpk ekeptpeekr ateiaafkaq tkrqatllgv
      421 ggllmlllgq vapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgiiilga
      481 ilqigsgngl vvfmaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_104184282             237 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Escherichia coli].
ACCESSION   WP_104184282
VERSION     WP_104184282.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>237
                     /product="STM4504/CBY_0614 family protein"
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtask
//
LOCUS       WP_104220065             391 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Kaistia
            algarum].
ACCESSION   WP_104220065
VERSION     WP_104220065.1
KEYWORDS    RefSeq.
SOURCE      Kaistia algarum
  ORGANISM  Kaistia algarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Kaistiaceae; Kaistia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Kaistia algarum"
                     /db_xref="taxon:2083279"
     Protein         1..391
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40312
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvpaeid avesrvaatp etvkkfialg ayvavqagag lasripdaey aaagatiapd
       61 aaaaladadi vlkvrrpaps elpaykagal vvatmdpygh eddvramaga gvtaiamefm
      121 pritraqvmd vlssqanlag yqavidaase ydralpmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedee fkqaetaagy akpmsaeyqa
      241 kqaalvaehv kkqdivitta lipgraapkl isaamvasmk pgsvlvdlav erggnvegsk
      301 agevaivdgk kivghlnvag riaatasqly sknlysflet lidkntkala vkwddelvka
      361 tvltrdgkvv hpafapkeep keilvaaega n
//
LOCUS       WP_104301044             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Caldimonas
            caldifontis].
ACCESSION   WP_104301044
VERSION     WP_104301044.1
KEYWORDS    RefSeq.
SOURCE      Caldimonas caldifontis
  ORGANISM  Caldimonas caldifontis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Caldimonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Caldimonas caldifontis"
                     /db_xref="taxon:1452508"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38538
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpletv agetrvavtp etakklkaqg htvrvqsgag vkasapdeay tavgaeitda
       61 agaygcelvl kvrapgadel almkpgttlv gmlnpfdaeg lqrlaaaglt sfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvggy arpmpqswld
      241 rqkvevakrv aladvvitta lipgrpapvl vteemvksmk pgsvivdlaa pqggncplte
      301 pgqtvikhgv tlvgetnlpa lvaadasaly arnvldflkl vitkegtlkv dleddivaac
      361 rmtqdgqvtr k
//
LOCUS       WP_104321321             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter maroccanus].
ACCESSION   WP_104321321
VERSION     WP_104321321.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter maroccanus
  ORGANISM  Marinobacter maroccanus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter maroccanus"
                     /db_xref="taxon:2055143"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55719
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeif ederrvaatp psvhkliglg ydviveggag eaanysdaay ekvgaaiaad
       61 tsslwkeadf ilkvrapmen palgkheadl mkegaflvsy iwpaqspell eklaarkits
      121 faidslpris raqkmdalsa maniagyrav ieaanhfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig aansmgaivr afdtrlevke qvesmgaefl vldfddedgs gsggyakqms
      241 defikaemal faeqaeevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgkva hhhgvtligy tdlpsrmakv aselyatnlv hllteltpek dgqplvnmed
      361 evirgltvvn enditwpppk pespvspkpa pgteepsaea kaaakkdadr rsligkgvll
      421 vvtalalygv gahapesflq hftvfvlacf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gailhlaqae niavgimafv avliasinvg ggfrvthrml kmfrk
//
LOCUS       WP_104357430             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Caldimonas
            thermodepolymerans].
ACCESSION   WP_104357430
VERSION     WP_104357430.1
KEYWORDS    RefSeq.
SOURCE      Caldimonas thermodepolymerans
  ORGANISM  Caldimonas thermodepolymerans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Caldimonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Caldimonas thermodepolymerans"
                     /db_xref="taxon:215580"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38758
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligipresl dgetrvavtp etakklkaqg htvrvesgag vaasapdeay vaagaeitdr
       61 agafgcdlvl kvrapqpdev glmkpgtvlv gmlnpfdaeg lqrlaaagit gfaleaapri
      121 traqsmdvls sqaniagyka viiaadryqr ffpmlmtaag tvkaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetdee reaaegvggy arpmpqswld
      241 rqkvevakrv aqadvvitta lipgrpaprl vseemvrsmk pgsvivdlaa aqggncelte
      301 pgatvvkhgv tivgetnlpa lvaadassly arnvldflkl iltkegtlki dlddeivaac
      361 rvtqdgqvtr k
//
LOCUS       WP_104359780             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            cyriacigeorgica].
ACCESSION   WP_104359780
VERSION     WP_104359780.1
KEYWORDS    RefSeq.
SOURCE      Nocardia cyriacigeorgica
  ORGANISM  Nocardia cyriacigeorgica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Nocardia cyriacigeorgica"
                     /db_xref="taxon:135487"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52205
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgilrear pretrvaatp atvtrlvrlg ydvvvdagag tmasfsdday reagatigna
       61 rtadivlgvn apadyqlddm rpgatlvsll gvlndpglit dlaerpital amdavprisr
      121 aqsldvlssm aniagyravv eaahtfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgavvra tdprpevadq vkslggeyls iesaeaevsa tgyakemsgd ykareaqlya
      241 eqcadvdiii ttalipgrpa priitadmva smkpgsvivd maaqnggnve gtvadhaivt
      301 dngvtilgyt dlagrlpaqa sqlygtnvan llelmtpnkd gtlvldfddv vqrsitvvrd
      361 gtvtwppppv avtakpaaep pappepapak kplsagrrlg lvliaaaalf gliaispsal
      421 qahltvfala ivigyyvigh vhhalhtplm svtnaisgii vvgallqigh gdpwitglsf
      481 aaillasini fggfavtrrm lamfsrs
//
LOCUS       WP_104369484            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            MGM1].
ACCESSION   WP_104369484
VERSION     WP_104369484.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. MGM1
  ORGANISM  Prevotella sp. MGM1
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Prevotella sp. MGM1"
                     /db_xref="taxon:2033405"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116397
     Region          25..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnenikrfvl clslsavftt dgfaqkltgr vvnsanqpia dvvitspgct ttrsasdgtf
       61 amdsvkagai vsfrhegfyt kteylknadv tglnvymvet dktrynetal lphgkyendm
      121 svagvsnvnr kdfalgsmsi dkalkgsvtg lnvvnksgmt gegaymqlrg ikslvaensp
      181 lvvingvpym pdmnmsqiin gysrsifqal ngqdirniti lkgadaaiyg slgsngvimi
      241 etdqatstdv ntrisfsaiy gfnwnnrrip vmnsnqyksy lsdmgltyyd nmeaffkdft
      301 flsdpnanka ylyqyntdwq deiyrnsntm dylfrveggd niakynislg ymgddgtlks
      361 tssqryntqv nasvlvskkl eiqaainaay ltgdyqeqgm syetnpmlaa yrrspllspw
      421 ksdmyghlin tyssykygai ekddffvsnp laivntlygk srqydmnaki qliynpianl
      481 tingvvgmyy nynqeeafip gknnndivpl fdqygkaens vrigtnhtfn myyganavyk
      541 wnlnpdnkfn fmagyqallt syeydaafgr nsnndyyqtl gdaqslgkyf sgynnkwnwm
      601 nlyahadytf anllkvglsa swdgassigk datrmsfypa gevvvmakql pglntfdfin
      661 klnlyanygl tgnsrysskl gkyyytsrpy qtiagivran vpntkleaet dytlnlgvet
      721 slwnnrvdlg vgyydinakn vlmtgvrssv lgtstyynnd aeisssglel slavapiytk
      781 dlkwtiggnl ttlknevksl gnindivtpl ndgaeiitrv genpyafygy ktngvfstta
      841 eaaaanlsnr sgvkyqagdm ryvdmnndni indddkvvig satpdffgsi ftrveyknfa
      901 ldvtmaysvg ndaynavrrv tesgsdfsnq sismvrrwsm egqvtdiprv mygdkvgnnd
      961 fsdrwiedas ylklrdvtls ytwnkplfnf iqggtlfvtg enlfcitdyl gldpefsysn
     1021 ssvyqgvdya kvsaprsikf gvnlkf
//
LOCUS       WP_104369489            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            MGM1].
ACCESSION   WP_104369489
VERSION     WP_104369489.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. MGM1
  ORGANISM  Prevotella sp. MGM1
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Prevotella sp. MGM1"
                     /db_xref="taxon:2033405"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121198
     Region          32..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnriksikin vrisllmvml vsfgmaasaq nvisgivsem vgntkepvlg anvvlvnsqn
       61 ryikgavtdf ngnytlqvpa nagklkvrvs yigmktktvn yngqttlnft lesdeankvk
      121 eikvvsrrsd rmgvsrleqt ssmqtlqvge iveqspigti eealqgqisg ldinlggdpg
      181 arssirirgt stldgdaepl ivvdgvpydv disndfsfqt aneedfgall niapsniesi
      241 dvlkdasata iygskgangv llintkrgsy gktqfsfstk ftvkkepasi pllngrqyts
      301 lmqdelwnaa nskgisnass emdmlfnade inynkaykyy deyncdtdwl davkqdavit
      361 dnnfsmsggg ekatyrfslg yyneqgttkg tgldrlstqf kitynfsdrl rvhtdfsftn
      421 tekeanvldn arsmaqkkmp nlspywiddv tglatgryfm qesdfqggyk dnynpvalvd
      481 lgfnkttmre ekmkvmleye fpfhlrfqgw valnmktnkn kkflpqeatg vlwtnsnanq
      541 atdatsdgft lqseakllyn nvlgkkhglt ataifrtyqs qsfnsssvty gnassnlsdp
      601 vvgsvvsssg sgnsearsvs figqavysyd eryvlkasvn yegnsamggr nrfgtypafg
      661 lawnidkehf wsesfhkwft egklrfglgw agkapsgaar yygaytslgq ymdmqaihai
      721 rmqlenlkwq streydfgvd lrlwdklnit fdyydkktsd lllkdtklps ttgydkiawi
      781 nsgvlsnkgf elrfdyqvlk kkdwfvsvna nisrnvnkve elpstykyen ytfgngnyal
      841 rilenapigs fygyrykgvy qnaedtyard kngtvmrdyn gnpiimrngs tqafpgdaky
      901 edinhdgvin endivylgna npkliggggf qvkwkdltlt tffygrfgqk iinkarmnle
      961 smygtgnqst avlsrwraeg dqtdipraly gmgynylgsd rfvedatfvr lktlslswnv
     1021 pkkllqklnw gisranvfvt gydlftwtgy kgqdpevslp satklvedna ttpvskrfaf
     1081 gltvnf
//
LOCUS       WP_104370034            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            MGM1].
ACCESSION   WP_104370034
VERSION     WP_104370034.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. MGM1
  ORGANISM  Prevotella sp. MGM1
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Prevotella sp. MGM1"
                     /db_xref="taxon:2033405"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121380
     Region          18..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mglcfcqgam aqkagdivsg tvtdafgpvm manvvevdaa nrivastvtd msgnfsfklk
       61 spknrlrvsf vgyktvtmpi nktrfvvkmt datqikevtv tsrrraqgsg lsipmdevss
      121 srqtinmsef dglsmttvde alqgriagld ivansgnlgs gssmrlrgvs tinssaepli
      181 vvdgnvwetn tndfdfqsan dekfaellnv npddiesisv lkdaaataiw gsqgangvie
      241 iktkrgirgr trvsysfrlt gtyqpngyem lngdeytmll keeyfnpkls datsdipeln
      301 ynpsfseyem ynnntdwlka vkqtgwrqnh slaltgggek arfriaagyd hetgsiikqq
      361 ldrftsrvnl dynvsdriai etnialtytk nkknaadlla tayirmpnvs iyeqdrygnd
      421 lgefynmlpt ispalrdqld hmnpvavahl aendetsyni vpefklkynl lglsddktrl
      481 tyegkvvfni fnkyedmfmp sslntrgwnd tdkkqsnrtt ansskslgvt tthtltftph
      541 frnedhsmmm llrgqltdgn stsqhtvtwg lpsgsitspg apaliaemnt gsgqwrsiyl
      601 tyslhyaykk ryafdfsvrr dgstkfgpdq rwgnfpavsl rwniskepwf ektfpwisml
      661 svrpgwgivg kqpnaeylyf skyangagym negsihpqni qlknlkweqt etynlgidfg
      721 ffnekltgnv eiyaqyvtdl lmqnrgipts sgfptlayqn vgkmknvgwe fningnrivk
      781 agkfgldfni tfannknqit emdetclasl nnefnrsngs ylsrvelnra lgsiygfkyk
      841 gvyqyseyse kevpgvsgpn apvvrdangk vfidesnrtk pmtfcygtsa eyefkggdai
      901 yedinhdgqi neldivylgs slpkvtggfg fklswgrlsw nnqfnfrfgn kiinaarmna
      961 enmytnnnqs ravnwrwrve gdmtevpral rqagynwlgs drfvedgsfv rlnytqlsys
     1021 fepkfvkkig lsmlnvylsa nnllcltkys gadpevgygn lgivtdnakt praksftfgl
     1081 tvqf
//
LOCUS       WP_104370217            1120 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            MGM1].
ACCESSION   WP_104370217
VERSION     WP_104370217.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. MGM1
  ORGANISM  Prevotella sp. MGM1
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1120)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1120)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1120)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Prevotella sp. MGM1"
                     /db_xref="taxon:2033405"
     Protein         1..1120
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125439
     Region          26..1119
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpkiklmlta illvmvqavm aqgqrisgti tdnfgpvmma nvverdannr ivtatvtdvn
       61 gnfsmvvknp knklvisyvg aktkvlsigt rtkfnenlss qttvqevkvv akrksnsggl
      121 sipkrevsva qqtmdmadve glsftsadea lqgkiagldi vvgsgnlgsg tqmrlrgvts
      181 ingnknpliv vddqiydapd fdvenatded yasllsvnve diqsitvlkd aastaiwgsr
      241 gangvieikt krgargktrv nfsykftgnw qpkgyellng dnysmlmkee iynptqqsda
      301 tininelnyv kswgdyenwn nntdwvdavt qfgqmhsynl nltgggskan frisagydhq
      361 tgtiikqtln rfttrlaldy fvserikfmt tfaftytnnn knysdllgla qkmapnmsiy
      421 rqnangedtn eyyimnpssg vrnpsseelk diralgnpva ianlafsken vyrvnpdfsl
      481 qyellgieeg ksrltyrgdv yfdiyanskp syypaelstd nmdsknynrs ynlesnsmgf
      541 tftndltftp hfknedwtat mkfryqikts tssqqyetgy ltppgldips lgvliddgts
      601 sstgksksqs wsytghfsyk sryslgvtlr adgdskfgpe hkwayfpsvs grwniidepf
      661 mkpirkvvsm lafrpswgkv gnapsseslf yeayntaagn ygtgsgaptt tmlrlkldnl
      721 kwetttsynl gfnlgllddk ieaefeyykk ttkdllmkdv ripstagyat laysnvgems
      781 negwelnvsl nniikagkfs asaninvsqn fneitemddk vlasvntews nknglylnrv
      841 qvgnplgsiy gyrykgvyky syeylinyrk ehpsefptna sfenwinqql aagntapvar
      901 dkngkvlmna dgtpmhmvfd yatrnyefkg gdaiyedvnh dgqinsldvv ylgnsmpkvn
      961 ggfgftfryd rftlrtnfny rfgnkvvnfa rmelekmsta ynqcatvnyr wrkdgddtpi
     1021 pramygneva fnwmgsdryv edgsfvrfqy vqltydmpkt mtkklglntf kiyasannly
     1081 cwtkysgsdp ehsasgwgfa edkaktprak sftlginvgf
//
LOCUS       WP_104370252            1091 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            MGM1].
ACCESSION   WP_104370252
VERSION     WP_104370252.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. MGM1
  ORGANISM  Prevotella sp. MGM1
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Prevotella sp. MGM1"
                     /db_xref="taxon:2033405"
     Protein         1..1091
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121371
     Region          56..1090
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksiifnikk sfhrnafcli avglampvfa qdelagdeva aapkrpkveq ekyqlktvkg
       61 vildevtkkp lggiqvkalg nsrytamsdd dgtftikvpv fttslyvyaq efsaqqvgid
      121 adkedglvvy mlsdkfrpmy ndgtsitasr dftatgghnf tidteienrl sgdlrsiqrs
      181 gsvgignnmf irglnsinas sqplvivdgv emdmqlgrem lhsgnvnnml anvmpsdiek
      241 vtvlknatal ygarggngvi lidtkrghsm atridanisv glslvprlqk mmnasqyrny
      301 ateilgtidg idkntpslnf lnddpngyyy htyhndfdwq davyhtaltq nysinvqggd
      361 dvgmynlsvg yvdgestakg ndynrmnvrf ntdidilknl ktkfnmsisr tttnsqndgv
      421 pedfskatpt sptflaaiks plvtpyqynt hlggfsslls esddlfdaig kgyslanpva
      481 ilekaegvnr nytentyfqa miaptlklgr dwsvtemfsy vlnrnsqryt rpstgvpgfe
      541 lknlgtvynq fstlfsnenn ivsdtrvdfs hifgahtlsa yagfrynyfs fdsdamstqy
      601 tsrqddknph isasssdint sggandvwkq iqwygnvdyn ymnryfltls llgeansrfg
      661 vecdgldmfg tkwelypsvq agwvatnekw fpknaginyl rinagydvsg nddimnnaar
      721 tvyamtkyng fpalqlvnig ndkiqsekth kfnvgfqsyl lhnrigvsfd yyihkttnll
      781 tmksfsdpis ginsywtngg elkntgfeaa vsvkpvvskn wnvelgasvg hyknevtklp
      841 dgdytssiyg nnniltsvgn pvamfygykt agvfaddaaa ksagnggyly iedntgqrhd
      901 fkagdvhfvd kdgngiidgn drfvigdpnp diygnifatv nwknftlsmn fnyslgndvf
      961 nyqrmifnsg snfynqqvam tnhwryegqv tdmprvmfnd pmgnnrfsdr wiedgsylrl
     1021 ktlklayrvp vnftwlqgls vwaeavnlft ltkylgndpe fsinngvmyq gidcgnlaqg
     1081 raftlgmkin l
//
LOCUS       WP_104377458             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            nova].
ACCESSION   WP_104377458
VERSION     WP_104377458.1
KEYWORDS    RefSeq.
SOURCE      Nocardia nova
  ORGANISM  Nocardia nova
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Nocardia nova"
                     /db_xref="taxon:37330"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37297
     Region          2..349
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(11,66,85,278,304,306)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(40,118..119,128..129,132..133,136..137,139..140,
                     142..147,149,151..153,156,179..180,268..269,311..312,316,
                     319..320)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(113..114,118,121,124,165..168,188..190,218,229,
                     246..248,255,257)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(115..116,118,128,171..172,179,195..196,198..201)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(148..152,155,158,181,183)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvretnader rvalvpkiip slvkqgvqvv veagagvgal ipdeayeaag atigdpwqae
       61 vvvkvappnd aeiaklsqgq tligflaprn adnkigalqn agvrafavea iprisraqvm
      121 dalssqanva gykavllaas estrffpmlt taagtvkpat vlvlgvgvag lqalatakrl
      181 garttgydvr pevadqvrsv gaqwldlgid aageggyare ltedekaqqq qaledaikgf
      241 dvvvttalvp grpaprlvta aavegmkpgs vivdlagetg gnceltepgk tvvkhgvtic
      301 splnlpatmp ehaselyskn iaallelmlk dgelepdfgd qvladscvag apsrpadsee
      361 qg
//
LOCUS       WP_104380913            1209 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104380913
VERSION     WP_104380913.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1209)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1209)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1209)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1209
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1209
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134182
     Region          158..1182
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myhfftkknv gdlfcvvptd eqstgeksvs riftnalmki slssllllgm mgvqantmaq
       61 rvninkknvs lrkilqeini qtgyhylwaa pnidpltcts vsfnnlplqe alktlekntp
      121 iffelekdmi mvkqrqseig giqlketill lnlknqskir gkvvdengnv lvganvmiqg
      181 skkgtitnan geftlenssv gtniiisyig yesitipvtn nlgvitlalk tgtlneatve
      241 vntgyqklpk drvtgsfsyv sgeklerkla tdlksalegq ttgltidkag kieirgvstf
      301 naqktplivi dgypvettid dinpmniasi tvlkdgvaas iygsraangv ivvttksgqn
      361 sepkisysgf vniiqkpqlk ylnkattsdy idaeidlfnl npngpstmdp ynmsrvtyll
      421 mqeregkisl edamaeingl rginalnqiq dlffrnkvth qhniniaggs pkssynfsvn
      481 yqqtkdnlin ndskrlitdf knewqlfpfl sagaaasfty nkgnstsfty stiygpelvg
      541 dnyqslagfs ggsmimpytn lldekgnpaa iwgisqykvn tykntpgmks wdyvpledmg
      601 kmpsysniyn frmsgflran ilkgltaevg gnwvkgtanv kniqqadsyn ariayndgts
      661 ksnpanhyip dgsildefkn inetwtlrtq lnysknfsdn khllhalvgn eirkitsdnn
      721 rlatragyne nagsfipvni kdftagiyna dmlfpdgsvs ltdglltygd nrfvswyang
      781 syeydnrfil sgsirldltn ffgtdkkyry kpmwslggty klsnekwwdk avfsklnirg
      841 sygingnisl rngpflilsv gnyspttggv sygissppnk qlrwektkia nvgldfglfn
      901 ntiegsfdyy nknssdllaa daadatlgfs sltknvgkmt nhgfelglnv haiknsrfsw
      961 dilpnisfnt nkvkyynvnr pyagsytvpg gimvagypsd glwgyrfagl nelgqtqvyt
     1021 gdnqvvlasn aevtdlvyqg tfrpkwdlal tnrfsyqnwd lsfmiiaklg hkyrkdtfsg
     1081 snyqnrhvae rwrkpgdekn tiypvleewn mdmfsfpfad vnvgnasyak lrditlsynl
     1141 eklsqkiglt narifiqgrn lfritakgvd idpettefnv sggtgagtdq gftslplpqe
     1201 ifiglrfgl
//
LOCUS       WP_104380919            1220 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104380919
VERSION     WP_104380919.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1220)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1220)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1220)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1220
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1220
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=137800
     Region          154..1187
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myknyaevcr alhgqaeimk nsdridfwgr shwrgnimrv slttimmscc llhvgaktyg
       61 qsvsiheksv slrkvfstin kqtgysyvwa aktidpntkv qlnvekgtln gtlekllnel
      121 nlsfeikgki ivvrekaeqg givsnynsls dqkilikgfv vddnnrplqg atirvkgvpq
      181 gtttdqngyf eissvsansl leitmvgfsp lslpvksdlg tirlhaidaq lqevnvtvnt
      241 gyqkiskera agsfaqvtak dmegrlqpnl ldridgllpg lnlirntssp qneknnlgie
      301 vrgrstinaq aaplivvdgm pyegdltain pndiasitvl kdasaasiyg vrssngvivi
      361 ttkigtagkt kvdysntlsf rglpsrkyln qmssselvdf qkqmfnyrsg dyaaidprks
      421 mndvyrilyn hkggviseae mekqldvyrn rdrfsqmeef lnttrfdqqh nlaisggsdr
      481 ytyhyslnyt qpgdynkgra tnkelgfslk nnfrvtdwfn franilgknq nregdigfnf
      541 ydnyigfnek yvgtkasyfl lrnedgspaq wygsksqfei drlnglgled etyiplnhvs
      601 avhekfynky infnfsanfk iikgldfdls yqnertegyk gtinrknsqs vagmvndatq
      661 igkdgvikrn ipqggqffeq rndvnsytlr gqfsyqnniq dkheivaiag aerrqihnry
      721 tniykygyde sslafkgine elfgimipnt qalfnsytis rnkdegfrdv idrfvsfyan
      781 gsytynkklt lsgsirmdqs nlfgtdiknq ykplwsigal yqlpklnwep ldrwairmty
      841 gvngnvpkdn gpylisrvgk svnpysgelq atidsppnpl lrwertsvwn agldfslfkn
      901 rlsgnidfyn kkttdllgnt pldptlgwdv vllnygdmqn rgielglngk iiqheqfswn
      961 stlnfsynkn eitnlfveqn tpyyyyympq nrvgvpmgsl ysidyaglne kgrplarkad
     1021 gslvestqql tvddliyegt tippynvsfr ngfkykdltl sfmfifnggh vmrgvhpefl
     1081 skyaelnyns nfdklwlnyw kkpgdennpd iapafisaas gnisdiynaa hkfvqkadyi
     1141 klrdislsyn fpskwiaptk lsyirltgqv lnawrwaank enldpeawvg yttatstnms
     1201 gpsrgitapv vynlgvsvgf
//
LOCUS       WP_104380948            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104380948
VERSION     WP_104380948.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119398
     Region          24..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrrsialla asvlvssavy aqtvlkgkvi dqdgkpipgv titlrdgtgt qtgqngefti
       61 nykqagvlnv saigydrkev nltnqttiqv tlqsdersld evvvtamgit rdkkslgyai
      121 qevkakdltd agqlnltssl agkmagvqvn qfggtvgasa risirgnssl qadqqplivv
      181 dgvpisndvq rsgdntyngv dygsgindin pediesvtvl kggsaalygm ragngvllit
      241 tksgkngadg vslsydgnft vdraltipky qnlygqggag deyhfkldgk gmtyqdyavk
      301 nafsyfdgtg ndgvndgvde swgprmdigl mipqfdsplv ngvrqstpwi shknnvkeff
      361 qtgysqnhnl sllaknarst traslsfrdq kgtvpntdqk rysaqinnty kvsdkfdydi
      421 ttnytrtqsn nlvsqgydgn npmnsliwfg rqvdmkslkn nwdekdakgd ytyynwnksy
      481 hvnpffnvhe ntnsyqrdri fgksslyyka medlkfegri gmdyynskmf qrnlfnydyk
      541 ngsfrdiqis ntelnldfia tytkivgdfn ilataganyr daqwqnstig adaltvpgiy
      601 tisnkqgaay nfmdhshirs nsiygngsig wkdqvyldfs arndwsstit ksffypsfsl
      661 swlptttfan lkgdvlsfwk iraswaeign attayrnray ylaqtnsfnd vaqiyksmvf
      721 pnenlepeki rtwevgtevg lfkerlhadl lyyykssrnq ilpvstsnvi gfnqmilnag
      781 eieskgvelq lrgdilksed gfnwtttinf skerskiiel ypelnvtsyr lgwtwgista
      841 anagekwgvl lgpgydrvtd gpmkgaikvt edgllagvdn qvignitpdf lasmrndfry
      901 kgfsfgfmld frkggdiwsq tmshgyatgi asvtaengir eraiiagkdv mpnerfamqn
      961 dkgewventi etnaqdwfkn aiapmavfdg sflklreahi tynipkefys rwkgikrani
     1021 tligsnlall wvhksntmrl dpetggvssd srgvgfeqas vptsrsiglk lgvtf
//
LOCUS       WP_104381360            1204 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104381360
VERSION     WP_104381360.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1204)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1204)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1204)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1204
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1204
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134849
     Region          148..1203
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnrsnlvsa lldkvahlas ingagknnsk kvqftwdkky pfdcivyslr qmmsartpvp
       61 mpksgkgmiq lalnlhflvf nviiclskal knkqallila cscfnkvicl skalknttml
      121 ltciavfhmf slsaqtprkd sgvdgllvlt gtvvssadgk piqglsirve gekgrtssnk
      181 dgsfslsvsn pkgtvsfshl gfrylelpyt agvsltvkli plenqleeve vvstgyqkip
      241 keratgsfef vdskmlnkrv gstiidrlen msnsvridke yrwldrsqye tvpnynfdmr
      301 gksallgaps rtiildnvvy egdlrdinpn diesvsilkd avatslwgiy ggggvlvltt
      361 kkgalnsptk lsfnsnltvq krpdiyalpf mnstdfieye tflfdkgyfn sklndtysyv
      421 tvspvvklld evrkgnvsav daqvqidkyk tydirddysk yvyrnavnqq yainlsggtd
      481 kvaynftdgy dgntnnkins nndrttlrss vkvkpiaale ittdvnfanv nahdasidqn
      541 iaygaldags gsgawpylkl vdangnpian davpisrayr dtagngklqd wsfnllnevd
      601 qnwqklsskn lmatiglnyk lrpdltlqlm ynyqynpvev kdwlglksfk mrnlinylsq
      661 wndvallktp ipvgdrlina htnnvnqtgr fqvnyasqfk dgihkidflg aaeirerrfe
      721 rdvktlygyd psnlniipvd pttifpflnq kfgggnipia dalqkttnry vsllananya
      781 flgrynlsas irkdasnlfg vksnqkwqpl wsigtawein kesflharfi dmlklrasyg
      841 ysghanadys aqpiiyyngt apltnlpyas itspanpsls wekirtinlg idygffknrl
      901 sgsiewyqrn srdlissvmi dpttgfesti knggelvgkg ieleinsani vgpifhwrsr
      961 lllnrnrtkv kkydykfayp ynyvmtsgst ntqyregydv gtvfayrsag ldpetgdprg
     1021 yldgevskny rgilyggmen ivdvgsgvpr yygslsndft igkfsltvnl qarwgfkffr
     1081 qsfnqqtaae nragykdykd rwqqpgdelh tnvpslkypi difrgrfssg stdwivnggn
     1141 vrlqdilisy rlgsfkyikd lsvygfvknm nvilwrenkv gidpeyrdai pfplsvsfgi
     1201 nmsl
//
LOCUS       WP_104381372            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104381372
VERSION     WP_104381372.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122884
     Region          32..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrkcklfyd vllalcvlfl sstllyaqek piklsglvld mdkkpisgai itdinsstkg
       61 vgstdvngkf tinttengii kisyigfasq tialrgrkel tvtlqaenrs leevvvtamg
      121 ikrdvrslts aqqsidvnsm tevrgsnlld mlsgkaagmq vvpgggplgs trivirgnns
      181 ltgnnqplfv idgvpmlnns gesgdldygs avnsinpdei enieilkgan asalygsdaa
      241 ngvvlittkk agrkqglgis ygfnamfgsl ysyptyqnly gagqngrfqr regvnyfgns
      301 nngvnfnpdl pygiwnpnqg nqdnrswglp mlgfdvvgrn gqvksyipqe stiknmyqts
      361 haltnsiald kltdqmsfrl sytnqhandi lekfnlydrh nfnlrstaki tnyfdvdasv
      421 rytledvknr gyrnasdrnp lyaianlprd asieelipwk qpdgtpfnfn gfrnpywlln
      481 etanaddknm fnanltlnlk lgnpfrlrlr gatdlqkskg wdftnlyspf dtdgdyskwn
      541 rswtnnnfda llsfnktlkk dfnisangga siqriegdri ssrnfmllfp dqrtlsntrg
      601 itssleeier kekqavfgmt sfsyknrvfl datvrnewss slpksnnsyf yysfgtglim
      661 tdllqlknsp lsywklrasy aqvgndtgfd rlltgyyrpd ggsflglpyy vgeevlknpn
      721 lkpeqtqswe agtefrlwnd ritadityys krtkdqivea daplasgyrr eilnageikn
      781 wgtevslnii piktklvtwt tgfnwsknns kvvslvagvn ryemgsgdni klyaevgksy
      841 gvfygndykr naegaiyvga dgkpkflpdq ylgeiqprwf ggwkntvnig rfsigtmldf
      901 qsggkvwsyt afrggidgst vqtldgrwey mlsdlilgen sderrgflqp gntvkpgany
      961 nenyvmypdy grskgiqlgn tvydpsvsdf wadkpalswv spmdhwthns assaaryiyd
     1021 asyiklrevs vgynfspqwf ratpikdarl slvgrnvail fqntpkgmdp qatsttgnaq
     1081 gfergfnlpm atwgfdlkls f
//
LOCUS       WP_104381407            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104381407
VERSION     WP_104381407.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124519
     Region          48..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnycklkqs hripsswllc lvafgsptta lkantalksi aglvvqnrei tgkisdsngq
       61 plsgvtvnvl gstmstasqa dgsysiavpq raeklvfkll gyqsqeislt qakilnvvln
      121 psadeldevv vvgygtmrkk dltgsvtqil pdrianenpk tvqdilrgta gmnigydasa
      181 kgggsievrg krsvydsnsg hnnpllvldg mifygelsei npddieqidi lkdasaaaiy
      241 gskaasgvii istkkgkqgk ptinmtmnag atqlsnyrkr fspaaymqhr edwytkntyg
      301 idpetglyea yqtrddngnl tvpygfylnp dqlpsslsld swralstnen gesdqsiwgr
      361 rlglqgnalq nflngkavdw adhtfrtgfn qdynasisga sdkvnyylsm gylknegavi
      421 sdtykavran mkinahvnkw lelganvnfq drsdgnidid ldqelrnspy adyadangna
      481 lqyplseqfs qrgynydflq nyleldkgyt vlnsifnaki klpfnitysf nasprlqyfh
      541 dryfmsaelp gsnpadrgan reqtkrfdws lnntinweht fvdkhrvmlt lvqeaeeqqs
      601 wkdriearni lpsdalgfhn tkngskenss fdsydshqta dallarlfys yddrymltts
      661 irrdgysafg tsnpyatfps valawnfske kffkwtdvld ygklrasygk ngnrqladpn
      721 lalanlysgs gkmhgylnsa gelvqyrylm vdrlanpnlq wekttawnfg ldfgflknri
      781 sgsleyylmq thdmimeqkl pnftgfgsit tnlgqvdnkg ieltlntvnl qkdnlkwstt
      841 fsfsynknqi vhlyknyedv ldangnvigr kemdeisngw figqpigaiw dyqvtgiwqa
      901 neaaeaaryg qapgdpkvan pytaddvvna dgrkpvynnn dkvflgqtdp rfrwamrnef
      961 tlwkdlsfsf niyssmghks lsgnylnndd dggrmaygla nlpakeywtp dnptdrygri
     1021 eakgpvgaeg arrlydrsfi rldnisvgyt lptaltsryh lnrvklygtv rnvatwtkdw
     1081 eygdpetfhp dnnpqgwasr vftfgvnlsl
//
LOCUS       WP_104381817            1290 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104381817
VERSION     WP_104381817.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1290)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1290)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1290)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1290
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1290
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=143723
     Region          107..970
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
     Region          1150..1283
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mkhsvkallf mlmhvngyaf gqhptnapdh ipfkqlvksi eqrsdyrfvy dpneinpdla
       61 lmvnlsdtdi ptllkqafsa kgirynivkn tivlqgslta ktqqmdvsgr vrntagltle
      121 gvslrvknkv lstvtdangr fslrglqlnd vvllssvgyr srevkitdag plelnleadp
      181 gnldevvvig ygtssirknt gsvssitske igaqpvldpl aalqgrvagl niasnsglpg
      241 ssfqvqlrgv nslsngsspl yiidgipfsd esmnqfnaan gkqsplslin pkdieridvl
      301 kdadataiyg srggngvili ttkkgnnngl kidfntnlga gkairnlkml ntdqylqirr
      361 eafqndnftp tidnapdllt wsptaysdwq rqfygasapf styqlsfsgg deytqylasa
      421 nfnrqgdplp gnlnyqrggg llnlstqskd qrfklhgsfn lnldrnnsvp tdiaqfynla
      481 pnyplydeqg ayywfqqslq npaaymerss lsksksllan fsaeyavlpe liaklsvgyn
      541 lksmdqtail plrgfnplts tgsmasygns dyqsyivepq lnysrsfgkh elkfllggtw
      601 qqrvsegkyl dgnsypsdsq lenigaagii vvrnnqyady ryqsafgrin yayddkylfn
      661 vsyrrdgssr fgpnnkygnf gsvgaawvfs sedflrnqti lsfgklrasw gltgndqigd
      721 yqyldtwgtg layqniagly ptrvfnpnfg weeikkkelg ldlgflkdri fltanyynnr
      781 sdnqlinivl apqtgfgsyf gnqpalienk glefelsssn iqkdkfiwkt nfnitfpsnt
      841 lldypglens sasrsyvige strivrgfqf tgvdtqtgia qfldvdgdgk isdfkdyvtl
      901 gslmpkyygg lsnnltygdl slgfmfqfvk qegpsigygp qaatigglan ldeyvlgrwq
      961 kpgditdvpr atanganaan layrnnyryf nlylldsian ypvsliryfp etgylvaydp
     1021 lkadkikavt aetmaiqgli tgqlnqrqta kawfiksvsd lksaplltai akcyqqwgdm
     1081 qhskplleaa ylqapfdpai kmllkadveq rgiqspsaqq ayfnnldkqw kqlyykdfdq
     1141 tigntafpke isivdmvkkp lsrtdfegki viidfwatwc kpciasfpyl hqvykkyaed
     1201 pkvkfvvlns gsgnswdday kwaqtnpqfd fpfyynqdkk lssklditsi pttlildgqg
     1261 nirfrkvgfe gekllqslda mieylkereq
//
LOCUS       WP_104382244            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104382244
VERSION     WP_104382244.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124136
     Region          113..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkffnntrh rccllffcsf ifvtnvfgqq pkitiqkkgi tvdellnelr kqsgldfvsl
       61 tskidhfqri danfkdeply qvldkyfnvr sgvvyvirnn siilldeqka qmrrisgvvh
      121 redtdremag vsltftdkai kantdlngkf iiqvpeyakv levsylgfkk ktvpltsatn
      181 yiihlsptse eldevvvtgi fnrsaesftg atttvsgeei kkintnsvla aisaidpafr
      241 lvasnqfggn inrlpevqmr gqnsfpnlsg elsnnpnepl fildgfqvnl qrivdldmnl
      301 iksitllkda sataiygsrg angvmvitti ppaagkvqvt ftndfriatp elgvynllna
      361 rekldfekra gfytstfnig qlgkdvlyns hlknilegvd tdwlkiptqi grsnrsslrv
      421 qggdeifryg lqftadmqeg vmkgqdrdny sgqvdlsynv dkfrfmnslr vfqnkanvsp
      481 ygrfsdyvta npyfspydae gnipllleev yyhpayqpyt tinplynttl hsvnksayfg
      541 vtnnfsvryn iipglfvesn fsitkqhdda dqfysaqdsr fasiaepsrr gsytartgks
      601 fgyeslttan ynvqfgksqi fsmlgfnakn atsefyqiva egfpydrldn llfanqyqmn
      661 grptgdestt rniglvysgn ysydnrylmd lsvrrdgssq fgtdrrfgtf wsaglgwnih
      721 nerffkdspi inklrlrany gstgslnipa ygaqfrysfg vgssyydqlg ailnnlgnyn
      781 lswqsvykln igmdasllnq rldlrmevyr ddtrnaltsv tlapstgfss ysenlgelrn
      841 tgmefsarya iinqkakgvm wsvnvngftn knilkklsnk lktanedlnt anagqiypnv
      901 lleegqsmnt ifavrslgid patgtemflk kdgtttydwd irdkvpvgvq qpkwngnfgs
      961 narykgfeln lifnyqfggk lynytlvdrv envdvaqnvd rrayelgwsk pgdvslykri
     1021 istpnatqat srfvqednnl kltsaslgyn fygkaflkrw glnslsital tndpiwwssv
     1081 qlergtenpf arnyslslra sf
//
LOCUS       WP_104382257             951 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104382257
VERSION     WP_104382257.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 951)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..951
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106081
     Region          48..950
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntysmikka tallfavwsg stslkaqqpg ewiapdstds qkvknygtvr gqelekipvs
       61 nltntlygrl nglmvsqtng qpgydqatll mrgratydqa alvcyvdgfq vdmsfyfqyl
      121 aageiasvti lkdpvslatf gmkgangvlw vttkrantdt fridaqvvsg iqqavkirkp
      181 ydayqyanly nqaisndaya lngnrfqwsp tysdealqqy kdgagtnvdw lneslrdngr
      241 ytntyvnmqg gmkevakynl yldymdqtgl fnipsgaeas rntglkrynl rsnvdlkffk
      301 iftgkidlgg riesysqpfs nntydnaqnf wkrlttypnn iypvrdaltg qwsgnalypn
      361 npvaelnalg myashdrtlq gnfslredls flteglyleq avsfntwsrv iqnktatyar
      421 fyegkqatad qntpivfgsn tpygqltwrq snlsagykrq fgkhrinavv nyyasdmipd
      481 anedaakiay hyqqfsgras yayqdkyfae lgwgysgsds yapghrwkly paaslswvls
      541 eedflkdnpv inyaklrlaa gktgndqtlq grylyqqyyr flpgsvtgnn slsfngglgl
      601 grlatpdita eqsmkyelgl dlrlvknvdf qatwfsdrrs giitrnnlva gylgytgadm
      661 lplqnigkvn nqgvelglsy qeqigalqln lgvmatyakn kivyqaeipn knafsnmtgr
      721 aigtpiglva dgfyqfedfn adgslkdgla kpgfgpvqpg dlkykdldqd glvdqsdvta
      781 igkptypkwy yalniglayk gidlsalfqg aagmdinllg atynqvvpfv gnttiypiag
      841 nawayypteg idtrnsatfp rltmqsnann ytnstfwmkn adflklrslq vgytlpsals
      901 kkmqlqkfrv fltavnpfvw ssfyrkykmd petpagypal ksynlgisft f
//
LOCUS       WP_104382176            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104382176
VERSION     WP_104382176.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121679
     Region          32..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkssiliylv llvffsiffc afevkaqdai igrilnastg kpmesinvdv rngkksifln
       61 sdnegrfllk inksddivik vsavgfakld tiigvsnlkd kqiilrlqea ntkldvvdvn
      121 vstgyqtlpk eritgsfswi dskkldeqis tdiirkldgt vnglvfdrst sstprlsirg
      181 lstlqpsmns plivldnfpy egdinnlnpn dienitvlkd aaaasiwgak aangvivitt
      241 kkrklnqplk idlmlntsvi dkpdlynkqq msssdfidve kmlfsngyye ndisssnkpv
      301 lspviellik rgaaspteiq eidntiellk qhdvrddfdk yiykkgvnqq yaismnggts
      361 kmgwksfign dinldnlgnk ykrinlrlqn tiiltdnlsl ssnltltkse nhsgrqgigq
      421 isskggflyp yamladaqgn slaipkdwry syidtfgngk lldwkyyple dyksneqkge
      481 vldilanvsl nykflkwfka dllyqyqrqg ssmnyyrsde syfvrdfing ftqfdaqgnm
      541 lrkvpeggiv dyqdgtmvfh ntrgqvsfdk ksgnhlinai lgtelrqsts sghgsrsygf
      601 dsntmtsgvv dfttaypnli tgaslfidng issnekvtrf lsvygnaayt fknkytlsas
      661 arrdasnlfg fktndrwnpl wssgvswlis dermyresfi gktipylkar ltygrsgnih
      721 pslaavttir yrgnsvytqs pyasfdryan pelkwettam lnigldfgsk nnrlsgsvey
      781 yrknsndlfa nvpidysggi gtsvvknaae ikgsgwdfvl ntinidksfk wrtefnfstn
      841 rdevvsyylp sdrgsnfmlv iptvtgivgk pvysmlsykw agldpltgap rgylkgevst
      901 ayseitgsgt aasdliyhga vnptmfgsvg nsfyfkgfsl avriqyklky ffrkptisyn
      961 slytnwnghs dyskrwkepg demrtdipal typasvqsea fyqfaepfvl kgdhirlqyl
     1021 nfaydfskgr srmpferfkv flsasnlgil wrankegldp dysydnlmmv psktwslgaq
     1081 itf
//
LOCUS       WP_104382274             959 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104382274
VERSION     WP_104382274.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..959
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107365
     Region          54..956
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkykklsial clglswiatt egmakeslnp tigqyknths tcsktglqds igkdsttlvq
       61 vafrkvqkkd lmgnvqsini pqlldksynt yslenldafi sgyngniwgm sgylvlvdgf
      121 prdannvmpt eidqisvlkg vnaialygsr aakgvisint krgkaggqqi kiransgint
      181 aisypqylgs aeymtlynea rqndglsaly gaetiyqhaa gtnpfrypnv dyyssdyikd
      241 hynrydatae isggnqraqy ytnfgfwseg smlnfgqakk ngganrfnmr gnidvkvnem
      301 islnvdasas fymlkgvnad ywgaaaiarp hrfsplipid mieegdinsm vyvnnsnfli
      361 dgkyllggsq ldqtnafani yaggtnryln rqfqfntgln fdlknilegl vfktnlavdy
      421 qsnynqaynn nyavyqaswn nydgkdriss ltkygddris glqnisgsty rqtiglngsl
      481 nfnrtydnnh hlsaillana fqiaasgsyh klsnanlglq lgynysgkyy vdfssayshs
      541 aklpqgnrqa lsptlalawr lskenflvns kvvndlrlsa sagilntdld isdyflyqgy
      601 ytynngawys wadgalvhsf drrrgdnpnm kfpkrkelni slegglynnl itfntsyffn
      661 rmsgglvqaa tqypmyfttg wpvysdlpfi nynsderrgv dfgvnlnkql nqtfvslgln
      721 gmyyttkaak rdelyqfsyq nkagkpldal wglqhdgfym sqsdidnsaf ssfgevkpgd
      781 ikykdqngdg tidtrdevyl gkggwsgapl tlglnltvkw nnftlfaaat gqfgakamkn
      841 ssyfwvdaed kysvvvrdrw testketaty prlttfnsdn nfrssdfwly ktdrinlskv
      901 qlsydfpkri lsskfihelg iyangsnllm iakeketmql nigqapqtrf fnvglkalf
//
LOCUS       WP_104382856            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104382856
VERSION     WP_104382856.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111758
     Region          33..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mivhihsnrt vavgtmlgcl flwtgiaaaq tttvkgrvss aadqtvliga tvsnlmnkla
       61 tktdkegnfn isanagdklk vsllgfktve iavpaagdlq itletesqqm eevvvtalgi
      121 krqvrgltya tqqldgaavn nardnsgnvl ssltgkvaga vvttaatgpg asarvvlrgn
      181 ksisgnnnal ivvdgvpydn ssaqqasgtt ynygtsdgaa ninpddiesi nvlkgpsaaa
      241 lygsraanga ilittkqgka gryqidyngs asldqvnlls kfqnsygrgn ggvtgtnvge
      301 swgprgttyk nnvrdffena asfnnsvsty ggtekvqgyv sytnnkiggi ipgndlkrns
      361 lnlrvnteli pklktdvkln yvnqqidnrp rlgdmgipve ayvmprdmdk aelqdyetid
      421 pvtgepqrky wsgsavydnp ywstnrtsvn evrdrvtamg sasyqltdwl nvmgrfsydk
      481 yidktdgsfy agtvslgdvr pggkyfetha ryqernfdll fngknsisea vkisynvgas
      541 slnrqyssfq nmanglsipn efslkmattp efllingyqr rlnsvygsaq laffdnifld
      601 mtarndwtst lksphsyfyp svgvsaifne wlklpawvsy gklrasytqv gndpdpyllq
      661 qlysfglgag kgfisrspik aipelkpelt ksyeagldmk ffanrlgfdm tiyksntinq
      721 llflglpmas gysrqyinag nienrgievq ltasplkken lewqttfnfa antnkvielh
      781 ektkratite ntkyasvvvn egerygdlyg ykwkrdgqtg kyvvdgsglp vveanqklgn
      841 fnpkallgws nsvryknftv nalidtrigg eivsgtsayl aafgvadyta dyrdgglvld
      901 avdasgaant kaitaqqlwt rvsqngrdaw gefftydmtn vrlrelsvsy kfnlnstaai
      961 ksaqlmltgr nlfffyrgks kldipgigkt anpidpeaal gagnfqgvev glpptvrsfg
     1021 lnvkltf
//
LOCUS       WP_104382921            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104382921
VERSION     WP_104382921.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120237
     Region          35..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkinalifll lqiiclssla qtklniriad desrpikgas lkmlgssnav msdqngfali
       61 tvsladryvv shlnyrtdtl agsrllaert ivlqplvrki eevlvqtgyq siskersags
      121 fqvlgkeqle rsnsanllsr lenittglaf irkdnngege gtpklrlrgm ttifgdgspl
      181 iildnfpfng sitdinpedi atvsvlrdas aasiwgarag ngvivlttkk gsqkpqsfqf
      241 ytgleaaskp nfdrspyhin agtfmdmekt ffdkgwyeqn dwtlnspyvd rlfdlkngki
      301 fetdlnswtt vmrqrdfvne mrkelyqvpi llryginstg gfakgsyyfs ianqadqiti
      361 rhnsnaktnv vanidyrltd altldietqv mhnvikndgm gisniiatgk syllpyasfg
      421 deygiqkrys lpyiesaesn gyldwrfype rdylwrenrd rdlsfrfngg lrykfpfgld
      481 igfkqlytvg ssasrkyyls nsyesrnlin qytspdgtra ipkgglshts sdsqrgyatr
      541 fflsfdrnfe dlhqlnlfag verneniieg tptmtvygin dqtlvgassi dyknpvqmsp
      601 qgnwgyipap dsrsmlktdr yeayyanvgy tfdrrytata svrvdqsnlf gvnfnqkrvp
      661 lwstglmwnv kaehwfksdl lsalklrati gengnvdktl taypiatygn dsfngltrgt
      721 lantgnpslr wekirtlnlg ldfglfnsri vgqvefynkw grdligdaiv dpttgidnqi
      781 lrnrinyana ltrgldvdlt vqaikrnqfs wtgnvilsyv nnkvtqyddg qngwaiatyl
      841 gqeqvfsppq vgkpqnylys ykwngldneg dpvvyltdgt vsknyaaylq glelsdlvya
      901 gstvptwfgs wrnsfniagr fnvsfllsfk agyvyrrpsl syysllnnwm ghiemvdrwq
      961 qsgdenhtsv pgipkdlasm sqrdmvyqms eqtiasaani rmediqfayt fpwknrlfkk
     1021 vdlsfnvknl gilwskskeh idpdmplsfy alplrasmll kidf
//
LOCUS       WP_104383586            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104383586
VERSION     WP_104383586.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120208
     Region          53..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfsinpiqin lrhssskvlf aalivacnld vasaavpmed shgvihnfnq gkikikgkvv
       61 dsktkeplas vsilsdgiak gttdrngnfe ieveagalir fqligyegqt ktfatgqsev
      121 kialdvtsea lnevvvtalg iqreekalgy sistvkgeel tnaisnnwtd altgkvagln
      181 lvksgagplg snkvilrget smtgendali vvdgiimggg trmtgngnsa yldgdspvdf
      241 gssladinpe diesvsvlkg pgaaalygyr gsrgaviitt kkgksiqnri gvtvnsntai
      301 gsinrwpdyq yeygqgaigq dlyysygqse dgastlstss awgpkfdgqy yyqydpanyr
      361 qtpaertlwr pyennrkdlf qteltstnsi svsgstektt arfsytnvtn kwiipnmgyn
      421 rhtiatqfss kitdklnlst kinfnnrgsd nlpnsgynnq symyfvrgiv pnidaawldq
      481 nwlpgkegie qmtpfsnlld nprtisydmv naqnknnlig nvqldykftn elslmlrtgi
      541 dmsydkrkqs rpfdtykyaf gyyreqsiya eernsdfllq ynnqrsenhr fgvsaggall
      601 nnkyikddas ansliypnqy kfanarervl ydpyraeyai hsvyglanys ykeryfidvt
      661 grvdwastla spkrnevkpf fypsvntsfi lsqifelprs inywklrasi agvggggtkp
      721 fnnfygyssv igfngglsnp stvpdenlqa entlsyelgt dfrmfkdrik ldltvyhtlm
      781 dkqlietpvd pssgyrrkft nggevktqgi eialsgdilk sqdklnwnmy gnfthydsev
      841 vsipaslegr lilstlfgsr gtieaipgrr fgdiwglgye rnpdgkiiya dgvpvlaqes
      901 ryignpnptt kfgwgnefky kgfrfnflfd gqfggvgysl thavlmeegk lkktlpgryt
      961 giigdgvvln pdgsyskntv vatagdyyar hfnrdnlesn tfstdfiklr evrldyslpk
     1021 sflsrykiek asiglygrdl fvftkwpafd pefasltgsg iekgaeiaqf pstrtmgvnl
     1081 sfsf
//
LOCUS       WP_104383650            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104383650
VERSION     WP_104383650.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111147
     Region          31..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnklyttlr mlsivptmlf sasllhaqsn qvkgtvvdak tkaplvgati kvlgtstass
       61 tdskgafqin vddknrvlni stigyenktv tlgpgettvt vsldeqtqql esvvvtalgi
      121 sraqksltys tqqvngdeln kvkstnlann lngkvagvni assssgpggs akvilrgnks
      181 asgnnqvlyv vdgvpinnqt lasqpdnvfg gqrdggdpis linpedieni svlkgasaaa
      241 lygsqaangv ilvttksgkq grttinfsss aqieqavstp kfqnqygqgs ggknsntsvf
      301 swgdktngan ydnageffrt gsnftnsltl sggneknqty fsyantlakg ilpendlmrh
      361 nfnlkesatf fddkltvegs anyitqkldn apssgfyynp lvgtyllprs lniadyknye
      421 tfntsrnlne qnwfslsdsp ttqqnpwwiv nrnptrstrn rlllngsaky kvapwisiqa
      481 rgsvdrtsev wdrkvyastp nplgkvngny nytnttitqq ygdvvanmnf nvsdkfqitg
      541 lvgtsitdwk tegvdfntgi dglkipnqff iqntttpvts tlsanrrqlq svfasanlay
      601 dnwiyldlta rndwsstlaf tgtksffyps aglgivlndk lnlpefvnma kvrgsyavvg
      661 ndlppytsll tnivnpyavl tvndiaflkt lkpektksfe igtewrmwnn rlnvdvtyyk
      721 tnttnqffkv aasqaslnkq yainagniqn qgvealvsld aikndnfkwt tsinftynkn
      781 kikeladavp efsltgenqn nfasklevgg sfgdiygqdf vrdeqgrili sedgipqkts
      841 aytklgnsnp iwqmgwnnsf nyknfnlsfl idgkfnydvm sitqsvmdgy gvseasgaar
      901 anggvsingv tpkgtpvsvv daekwytstg gigpvssqyi ydgtvvrlre ltfgydfnik
      961 dsffkklrvn avgrnlfyis kkapfdpevt mstgnalsgv difmmpatrn ygltlnatf
//
LOCUS       WP_104383656            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104383656
VERSION     WP_104383656.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116164
     Region          23..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrklllils gvmlssslwa qtktisgkvt sasdgtsmsn vtvtikgkai stqtnpdgtf
       61 tinaepgdil ifralgsses qklvgsanvi nvaltgreet ldevvvtamg ikkekkalgy
      121 avqdiggtel mknkspnlin slagkiagvn vtqtsggaga gasiilrggt slqrdnqplf
      181 vvdgliydnn tgingnsgfd gaqstnsvys nrvmdinped ienisvlkgp aaaalygsra
      241 asgvimittk rgkegtasis vtsrftsnwa nrlpeqqnmy krgeyqldgr llegdatktm
      301 gswgarfgag esvynnikdf frtgtawdns asvsggykng syyfsasdfr qkgiipnsdy
      361 nkttfrlnad qkygilkigt smtysiadql ssltssglyg angegavqga yiwprdldmk
      421 hylnedgsky rmfsydlvqn dfdnpywvin kmprtskvnr ftgtfnakld itswwdlvyt
      481 vgldryteng srltsagsgv efrylnglms qntttfqyln snlmtsfkkk vndfdfnlml
      541 gttaesmtrq fdglkawnfv lpnfyvptnt vntdrdiaqs inrnrlvgif gefrasykdi
      601 ayftatqrnd hsstlpvens syyypslsgs viftelmpks diltfgkvra swarvgkdas
      661 ayvtntytvg peftlfnqgq gvgfrndwlk gnnrlkpeit eaqeygvdlk flknrlgmef
      721 tyyknrsinq llqprssqat gyilmwtnag dinnkglels isatpiknen fkwdimlnas
      781 rnkgkvenll dgmdilyvtd vqvgtakaas fnkgnfmais gskwlrspdg qlvlnpetgm
      841 ptsdgldtye ignrepklfg glnnsfqykn wnlsflfdyr iggdiyngtd yymttmgmsg
      901 rsqqrdklsi tgvvktgvdn nqmpvysdlk tfeyeagkmy kigdkdvsgd yvinnyywqs
      961 aynlesanym tktnwlrlrs vtlsyslpes lvkrvkgvkg atatftgtnl wlltnykgmd
     1021 petsaagsga vgsssvgidy ngvpalsgvs fglnvtf
//
LOCUS       WP_104383807            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104383807
VERSION     WP_104383807.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120233
     Region          46..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnhfvfpkks sirlakllai gimvggafps fsyganssel nllffknitg kvvdqngkpl
       61 egvtisikgt ntatstdkdg tfrlnlpvgn eiliinhvgy krlefpagnq nvltirmeaa
      121 nqeldevvav gyttqkkahl tgavvdikae eieelpttni gaalagrllg vgvsggisrp
      181 gskasltvrq pinygkdvgs sdplyvidgv iqvngqnqpd vtlfnnldps eieslsilkd
      241 gaaavygvkg angvvlvttk rgkvgtpkis yngsyainde ayrtkmmnay qygmyfnimn
      301 gpnganvkst dasyvnrifs qdemdyfkdh synwlddawk ssyltrhsln vsggtevaty
      361 faniaynkqd gnlgtlnydr wnfragsdik vasnfkvglq vsgntgdlqk tfnkiggend
      421 endyknllma spyipayvdg lpvrlpgnsg dlsayhyfel qrlgnlatsn nrqftvnlng
      481 eyqapwlkgl tlrmsynknl mngrgtqvgt kyqtyeftrm genqhiydga inpkaltfsn
      541 gnrvyfsnss gdnyqlnfta fydkqwkkhn fsglfsveka eakssqedvw kedpidqtng
      601 qfstafgavd grtaayesgt lsylgrinyr ygekylaeil frsdastkfa penywgkfyn
      661 isagwvisee dffkvkgvdy lklrfshgkm grddftpwaw rqrytfqvgk gavfggngns
      721 ttgmrmekta nraatwsdey knnlgldarf lnnrlsatie gyytkgsnil iertgniait
      781 vggsvagenf gkvntygmel glgwqdkind fsygvssrfs wgdnkvvqmn fndtdilypw
      841 nakpgassdn gmwgydyigm fksqqdidny vsqynitevf gtkaqdlkpg mlyykdvrga
      901 mqadgsfaap dgiintndqv qlakrkdnhy gfgmtfrvgy kgitaeavia gsfggyaein
      961 drnklnndis rtytnlpviw gdiydpvlnp tgtmpnpnws diynvsssfw tvsafrmrmt
     1021 sfnvgyklpe kfikylkisn arafvsamnp mslynpygyk dgnggawdsy pnlrtysfgv
     1081 nltl
//
LOCUS       WP_104383891            1172 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104383891
VERSION     WP_104383891.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1172)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1172)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1172)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1172
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1172
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126975
     Region          52..120
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cl21470"
                     /db_xref="CDD:473874"
     Region          189..1171
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmhplnhtll facgfilfch sgqahtiein yrthratfak ppsfqrldti gisgkvtdsl
       61 gtaltgvvvt ekktgnsgls dqsgafrlsa dpngvlifik tgfaikevyv nnqktiavsl
      121 sagaakavtd stvqnrdsta tvaagrdsmt nvaagrdstt kidanqdstt ratgnpnsaa
      181 gvsagktsvt gtvtgpkgpl pgvtvavvgt nvsastdeag kfqiaagpkn qlrfsslgfe
      241 aitqlvgdrk diqvvlsget kvldsvqvva vgygtmnrat lpsavssiga neikdevlps
      301 itqaiqgkag gvqvtqksgs pgggisirvr gttsinassd plyvvdgipv nsttnftggs
      361 tfdfgggtqg invlssinps dvqsieilkd aasssiygsr aangvvlist kkgvagqsef
      421 nfnmyegfsq vpkeryydfm nteqyqdymk dyykilqqqd pkavipeqif anpnvntnwq
      481 daifrnaatr syelssrggs ektqyytsvg ymkqggvllg sdfnrlsgri nldhqhnekl
      541 rfstainltr avnhrvqeen skegatksgi fsppnlavyd aagnfvydqv rntrenpvam
      601 ltlptneaqt frvlanasae ynivpelllk tsfgtdisfi detffmppvg lrsyasqggi
      661 garrntrdql winettltyd kkfgdhsina lagfsvqesr lefvhgqrsn fpnndipyit
      721 aggvitgans ypeewaiasg faratyiykd kyilnanvrs dgssrfgadn rwavfpsfag
      781 awrlteedfl kdskviddlk lraswgitgn qnignyasrs lyssgnnymg lagfvpnvlg
      841 drnlkwettn qwnvgvdagf lgnrismlad yyykkttdll iglpiltssg yltrftnsgd
      901 ienkgfefel ttknlvgefk wttslnmtfn rnkvvalpeg ltemrggvgd lnraivgqpl
      961 gvfygwqang vnpqtgmidy lgadgsavtp tdykdqrmig dpnpsffggi tnnfayknfd
     1021 lsiqgqftyg ndifnynlas glegfnpssn qfvdfvdrwr apgditdvpr papgdlnnga
     1081 issrfvedgs ffrirnitfg ytlpssiaek ikmkklrwya tvqnafvftn yrgydpevss
     1141 shggantgli ygydygsypq prifttgvnv tf
//
LOCUS       WP_104384208            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104384208
VERSION     WP_104384208.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124768
     Region          22..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkflipltf mcvqmaqaqe skelkgkvld avtlkpvvga tvvvessava edigvpnqvq
       61 qsalgaltda sgefrlkvpg nlkyvtisyv gyqrmqipvf qdhktillqp ggesldeviv
      121 tgytdikkrk nttaynkinv adikqtgvas idemlagqva glqlsnfngg pnsapqirir
      181 gtvslngtqd plwvidglpi egtampnrie kdnlnsltnl piaginpddi aditvlkdaa
      241 atsiygaraa ngvivittkr gksgpaklqi santfvterp dfgklnlmna nekvdfellm
      301 adrtdlnyrt dkgavmriln nanaldayrs gglaalspev qqsisqlrtq qtdwgkelyr
      361 qalnqqysas isggndghry ylssgfydek gatkgadlrr ysltlnndfn indrfkagin
      421 llgsvsnrqn piqdadaftn psnyvrtvnp yltvrdqsgk ynydpdiegy ekdtyipfns
      481 veerentkyt ltnkalkaig yleytiipql slrtefglqf densmerfad qesyntrklr
      541 aatryydaat ktnkyflptg gkiendhnsi fqynwktylk ynktwnekhe lelmggtelr
      601 rskntivssk gfgynpatlt tqsivfpnsn yqddrrflqy skvfgensya sfygnatytf
      661 drkynvygsi rydgsnmfgv dpqyrflpiw slsgswnvle edfikdktkl sdlrvrasyg
      721 iqgnidrnty pfivglynna tllpgntest vvvempandk lrwertksyn agidlglwkn
      781 rlnitvdyyn rtstdligns elpmengfqn vqvnwasvrn qgieltissr qiqtdkfsws
      841 tdfniahnnn kllkvmdnpk ayspesqagr pingmyvlet agldkdgvmq frnqdgsvss
      901 medfyglydp wadflpgyts qtsmtaatyl skfrylgskd pkfiggmtnr fryanfdlai
      961 savfnldrwv srtptynpal vdrgqnysrd llmalqgnta fpalgsisse lndrwmaysw
     1021 mesndpiksf nmydvwakkm syvrinsirl gytlptavsk kigasnlrvn vegrnlfvfg
     1081 anyegyfdpe tygnnyaqpi sksfafglsa sf
//
LOCUS       WP_104384216            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104384216
VERSION     WP_104384216.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117309
     Region          26..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maknnidfvv maalclssst lyaqstikgk vvdnnnnpiq gatitetisk kqvqtdtngl
       61 felssngssi siqvqfigfd sktvqtnpgg lttiqlspts sqldevvvta lgisrekksl
      121 gyavqevksv elqtrptnal salsgkvagl qvttsggnmg gsshvllrgi nsiagnnqpl
      181 yvvdgtpidn tdlnssstin gsagkdvgnm iqdinpddid nisvlkgpsa aalygsraan
      241 gvilittkra skgekidisl ntgvdfeniv rlpkrqhlyg qgystvfqtq ningtdykiv
      301 dyaadeswgp kldgtpvlqw ynlnpedean ylnpspwlyp kndvsyffrt gvantnnfai
      361 agnsgntnyr fsytnknvkg ttpnsslgrn tfnfsggtql gklkinsnfn yirnasigrp
      421 wtgasnrnii leafqwgavq vdykilenyk redgtplawn rtgwqniptd eatrfidnpy
      481 wsayesymed nrdrfygnig lqydlnswls lgakvhgdiy sfqsqdriav ysrsasqyee
      541 tsnklneyny eflatakknw nqfslvgnig anlrdqqrkq dyaitqggli ipnyynlkna
      601 nsvkidnfky hrriasvygs fslgyndlly ldgtvrndws stlptdnnsf iypsltssfv
      661 fsqleafkql dwlsfgkirl gwaqvgndtd pyqlykvyep eqsyegqasy glpsikpnan
      721 lkpeitsswe tglnlqlfkn rlgfdityyn nnsrnqilpv pvsssfgyas kvfnagkinn
      781 kgleivlngt piknenftwd atinwaknkn kviklddqvn tlslsnslve lvaregesyg
      841 qflgydfvya angqrivqad gtymktsqlv plgsilpdft fgiqnsfryk nfslgflvsg
      901 rvggkffsqt ykvgmysgil dktaannire tgavldgvkg dvtfhsdgty tvenvqqntt
      961 nitaqqwarn eyngpttfsi fdatyvklre vtlgynfklt nskivknigv naygrnlwni
     1021 ytkskyidpe ftssggnvqg ieggaiplpv tygfnvnlkf
//
LOCUS       WP_104384299            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104384299
VERSION     WP_104384299.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116121
     Region          24..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqtllsflv ggmiltsvaf aqekkisgrv tsadgkglpg vtvvvqgtnq atqtdasgny
       61 slnvpagkvv vfrsvgfddk tiivnnnstv fnismenhdn aleevvvtam gqsrqkrals
      121 yatqevkgdk ltegansnla talqgkvsgv qvtpssgmpg asanitirga rsftgnnspl
      181 yivdglpiss tsdqstgnsv sgadyssrgl didpndiesi nilkgqaasa lygmrasngv
      241 iiittksgkg kqgkpqisyn snvsfdkvsv lpefqtkyaq gtngqyspls smswgqqiqd
      301 lyndpvyggn tdndytkkyg khegkyyvpq ranagmdpwa tpqaynnakd ffntgntynn
      361 sfnivqgfek gsyalslgat nadgivpstg mdrytaklsg eaklsdkwtt gftgnyvnsh
      421 iskqtganng iiatvfgapa sydlkgipsh nlnapttqnt yrstsgfdga ywavdhnkft
      481 edtqrffgng fgqyatnlge nqkltlkyqa gvdsyttnyt dlwgyghadg fgevenfnvs
      541 vtewnslgta aynwkinddl vldamvgnei vnrnrrrdya yganfnfpgw nhinnastvt
      601 teqtlrhtrt fgtfgslala yknmlflnat grndivssmp rnnrsffyps vsagfvftel
      661 davknsvltm gklrasyaev gqagdyydny fdkptygggf sngtpilypi nsdgvtsyts
      721 ypivydpnlk pqntqafelg tdltfwngli nlnytfsrqn vkdqifevpl aastgysslv
      781 tnggkihtna heltlavapf rsgdfkwdfa fnftkidnyv delkegvnsi fmggfvtpqv
      841 ragigskfpv iygvsylrnd agqiivdkng lplageekvi gsvspdfnlg fntnfeykki
      901 rlsavldwkq ggqmyhgtsg tldvygvtqk sadfrdgngf lfegaavkev spgqyapndi
      961 liapnptfga dgkvnnvsty dyfnrlsnis eagirgtsfv klrevavgyp vyqnskikvd
     1021 vnafarniil wselkgfdpe vsqgntnmsg aferfslpgt ssyglgvnvk f
//
LOCUS       WP_104384304            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104384304
VERSION     WP_104384304.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110947
     Region          24..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkllsffv gsmiltsvaf aqekkvsgrv tgadgkplag vtiavqgsnv atqtdangny
       61 slsvptgkvi vfrsvgfadk tlivkegqsa fnvtldgsdn alsevvvtgm gvskntkglg
      121 ysvskvsgdd lvksgeanii qglaakatgv qvtsssgtpg asskiilrgp asfsgdnqpl
      181 ivvdgvpldn slnnikagdd pynqnlagvq tanraldinp ddiesvtvlk gpaaaaiygq
      241 aagngaiiyt tkkgklgsgl givystgfea skvnklpemq tsygqgeggv skvsadswgp
      301 slagkqsydn vkeffqtgri fnnnlaitsg gekttfrfsv gshnnkgivp nssfnrytar
      361 lssesklnda itvggtlsyt nsntravqng snlagtmlal lrtpadfnla dyinedgsqk
      421 qyfpnydnpy wstefnpyte qnnrltgnay advklnnift iswktgldny stegkqiyai
      481 gsrgddngla ygeikrtnvn frniysdlll kfntkisedf svsgmlggnf nyaqytsnfg
      541 rgrnlampgy ynfasaqely vsnyeeykns kaifldatfd yrsilfltlt grnewsttfg
      601 kdskgffypk advsyvfshl lennsilnyg kvrfaysnvg ispnvysdrs yftvptiadg
      661 mtngfsfpya gqagfaksnv qvaeefrper nkgyeaglem kffnnrlgld ftyyqqhssd
      721 llisqpidpt sgyayyynnv gamkntgyev gitahvvkae kfnwhttvnw sknenevtel
      781 aegvdkmsig safsapqsya ivgqpfgvly aqkfkrnaeg kvlinptsgl piyedelgnv
      841 gspiptwlmn wnnefsykdf slsflwdfrk ggkiwggtqa glynrgkaae tadrermyki
      901 dgvfasgpde gkennkeida ltyfrnylgn snseiaiqng swarlrsvdf syrfknfsks
      961 iqyiqvgvnl rnvllitdyk gvdpetsltg snqnfagydf fnnpgtksys lnlrfgf
//
LOCUS       WP_104384492            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104384492
VERSION     WP_104384492.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117863
     Region          33..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 memdiytkrk wiriipllfs lmlfqlssfa qskitgkiln nnrplpgatv fiknnvknat
       61 ssnqtgafei qaksddiliv ksvgfetqei svggrqtlti nliessndlg eaivtgytti
      121 srkkstgsia svtskdienl paasidvllq gklpgvnvqn ftgqpgmkts lvirgntnip
      181 rsngdydadn ltsnplyvid giptsedeik sfnvtgtnfl aslnpndies vdvlkdasaa
      241 alygaranng viliktkrgq lgrpkfslnt yqgyvtkpak vatligaaer rkklaliyky
      301 gndaqladip qlltdslnpa fnnnndyqdl fyqsgyvqny dlsvsgaten lnyrvsggmy
      361 nekgivkstg lkrysftsnl ifnitkqlef ltnfkastnk rmdgkgntef lktnryrgif
      421 ainpvdmpts llgmsqddin sivnpydyqr ndninvdlsg vgelrytflk dfrlstrsii
      481 nystakndfa spsilnsdgl ayakstytqy rkylltnsll wtksyndvhn ftatavqeye
      541 srkneglyll gkdipndniq vvkgvssqnl ngysdqstya klsflgafhy dykskyllda
      601 vwradassrf gknnkwgyfp svgagwiise epfmeanewv defklraswg rtgdessigd
      661 ndrynafvag dgsypgnfgn tygggtaiip nysgitndni twqksdtwna gfdayllkgr
      721 ltvnfdtyvr tttgqmlqiw ipeysgylqt ftnaagvrns gveiniqgrv fdkekafqwt
      781 pqlnlsfnkn vvtalpngnr dlyydngvyv vgkplnmfyg ylvngaisss ndiivnpytg
      841 avgatkwgtl kpgypnwvdv ngdykisdai gendmtffgd pnpkvtggfi nnfsykdfsl
      901 qilttftfgr diinntfarr msngffygsa kdfskasigd ldkfdfweqe gdiarypaan
      961 pymglyawra aqsmfmepgw yvrikninla yrfnkgknpw mdrlginslr lygtmdnvhm
     1021 fqkfsgvdae mvdargfdyg dgyplpskyt lgvqfef
//
LOCUS       WP_104384495            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104384495
VERSION     WP_104384495.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114088
     Region          24..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 makkltllis svlactyman aqnrtvsgtv vdsqgkpiph vsvklknrsg gtttddqgrf
       61 sipvypqstl vlssvgflnk eqevneqssl sitlesgnte ltevvvigyg tasrkdvtgs
      121 iasvkaeqle nenpqsvadl lkgniaglsv sqntsakggg dllvrgkttl sastsplivl
      181 dgiiyngqls dinpndiqti dvlkdassla vygakaatgv vaittkkgts dkpiltantn
      241 wglatlarnq rvyngpeflk wradvgragg srpsyfyddp rnlsagvtld qwlsggnkdl
      301 dpvdiwldrl glvanekany vagktvdwyd eifrtgirqd htvsmsgrke dvnyymslgy
      361 nknqnliegg efstfrarln legkvtnflr mganvqyadr degaieadwa qltslspygd
      421 kynadgtlrr iptddnglna rnpflnmtyn drmnkqntlf aslfakvnlp fgityqfnfs
      481 pgidmyrtfn hnssanpnvt ipggsasrdq etrynwqidn llkwnrkfaq ihhvdvtlla
      541 nsekyqtwwt qaanqgfvpn dylgyhnlas gtlpsvnsed kvytgdalma rvnyslmdry
      601 nltlsvrrdg ysvfgmnskr atfpavaaaw tfteesflkn lswlnygklr lsygingnrd
      661 lrnpdngtvd pyaalsqlti nkyqtvkpdg tpaevntvvv nsrlgnpdlk weqttslnag
      721 ldfsvlkdrl sgsidvyskk tndllvkqsl ssvsgyqfvy snlaevknkg levsltsrnl
      781 vdgpvkwnsn vilslnrnki vrlatpsddr gngwfigqdi dviwdykvsg vwqeneieea
      841 kkytkasirp gdfkledlng dyvyndedkq figytsprft wsvrnefnlf knidfsfqli
      901 snwgqkkqfn qaknnpgsvg fmrstsyiqp ywtpenpind yarlgsgang tsfnvywkns
      961 firlnnisla yslpkqlaer fkvrnlkvym nvnnaavyap vwnywdpqnd gptpryytlg
     1021 lnvsl
//
LOCUS       WP_104384561            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104384561
VERSION     WP_104384561.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118795
     Region          21..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklvsilia llmvvaaeaq iqfkgtvknr dlkpipfati qtadkklvfi tdslgrfafs
       61 ygrgdfkivi samgyeskeq lfridkthvd iillakenil eeasvntgyq mlpkerstgs
      121 fgqiknkdln amttvnlmer legklagmqf dnrsgnsein irglntfneg ssrplivldn
      181 fpyegsleni npndiesvtv lkdaaassiw gsragngviv inskksglqd rtrinvsant
      241 mitempdvfy rpaisssdfi kvermlfekg yydtqyngss nkmfifspvv ellyankngs
      301 vssgeleqki eywsandyrk dyskyllrtg igqqyyadme snssnnsmrv svgfdrqsgt
      361 rimstdqrft fkvinetklg kkgkatssva ytesnntssa nfpdenlnpg gtrsriypya
      421 elvdatgkal aipkgfnqnf adsagagkll dwnyrplddv sksllenrlk hmvasmqlky
      481 qlleslsgel iygyehqsgn ttmsyseqsf ytrnlinrys qivnnqvkyi vprgdilnks
      541 vsnmqshrvr gqlyfnrtwd nnhslnmllg geisaakstt dsygvygydk dvmvskdvdy
      601 vtrfptyggl fgnqtipsfs kftdrinrfv slysnlqynf rdrynlslsa rrdasngfgs
      661 ntntrwnplw sagvawqisk epfiqnigwv nqlklrattg aggnaipsss setmityvsk
      721 apvsglpyav vvtppnpnlk wetvkmnnyg ldfevlnhki sgyveyyekr sydilsldvv
      781 dqtsgfvnmp knigeikskg ldlgltgtit igkfvwnpqv nfsyasntit qykggigesa
      841 fyvnggvsit piegnplypi fsyqfaglda qngdpvgyln gqrskdyiki iadslqylnf
      901 hgtalppyyg sfnnnfsygr lnlnvalmfk wghyfrkeal vysslfesws dhgdfekrwq
      961 ktgdehntti psmifpanad rdnfyskssa nidradlvrv qsirlsyglg ikqgkhting
     1021 svfiggnnlg ivwkktktdl dpdflgtpnp rmftagvnfq f
//
LOCUS       WP_104384694            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_104384694
VERSION     WP_104384694.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119625
     Region          19..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiilfffl isflegkaqi agkiigenni plsgatvalk earqtmlsde nghfsfgkvs
       61 fpdtlsvrfv gyieqkvavn sagrnlqirl vhatqaisev qvvntgfyqi pkeratgsft
      121 tinnellnrs vganilerld gvasgvqfvt pngtkpsdir vrglatiqsd aspliivdnf
      181 pydgditsin pndidnitvl kdgasasiwg aragngvivi ttkkgrynqk gvlsvnsnls
      241 igrkpdlmys rnrlpsetvm qiekekylhg gfyidtdnqv pfpryvemli ardngsmtee
      301 eflgqenmlk ktevrkeamr ylyqpsvvqq yalnarggge nytyflsggy dknrgevign
      361 tgnrvsfstq ntfrplrnle vmssvwysqq hgkengitln dlkghvtsvg lspytrlmde
      421 ngnrltlike yrqsyidrak adglldweyn plrerdlidk rrkseelrln aglrydflqd
      481 fhldityqyt kgssfrsvly drdsyfvrdm vnrftqddgk kiipyggifi nespesllsh
      541 sargqlnyng sygkdhqvsg liggeirefr rtitpgstly gynpdiamgl tnldysqgyn
      601 lrpdsygyis spdytnrifv drylsyfgnv gytfkkryil saslrwdgsn lfgvktnqkg
      661 tplyslgtsw disqenwfav rnleylrira tygsagnvnk svsvyptvrh mgadlttgvd
      721 naqilsvgnp slrwervntf nmgidfrsfg nrlsgtaeyf rknasdlige dilppntgii
      781 eggsannsrl inyadlvtng yelqlnsint dgrlkwtsal llnlvrnrvt ryaqnnnvvi
      841 sdyldgkvpv agmsrdamft lpwyglgntd glpivyvdgr esrdytkfys glafndltaa
      901 glsvppfygt lrnalnyngv gleftlswkt ghsfransmn sggeytldyn mdyfkrwqkp
      961 gdenstdvpa tqeigktipy sniiysnsai likrgdqirl qdirlfydlp isvakklkfn
     1021 nmrfyamarn lgvlwqsgdr svdpdysgae yvapktitlg mqldf
//
LOCUS       WP_104385018            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104385018
VERSION     WP_104385018.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111639
     Region          28..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfykktag lalctlfsat slfaqqgisg kvsdakgpls gatisvkgtn ratqsgtnge
       61 fsiqaaqget irislvgykp qeivvgatkt invnlsndes tlgevvvtam gikrekktlg
      121 ysfqdvkgdq lvdakennva nglagkvsgl qvikgsagpa sstkitlrgn nsltgdnqpl
      181 iivdgvplnn flgatngigq tnndmwnpgt dmggglgdin pediesmsvl kggaasalyg
      241 sragngaiii ttksgkaqkg agitysstlg letlfmtpkl qstygqgkdg vnnptstenw
      301 gekltsqayd nignffktgv nhtqnltfqq qfnktniyts atylndqski pgsslerlnl
      361 mtkvntsfgp ddrwttdvkv qymntnaknr pasgdntsnm ystlftmprs inildfknaa
      421 daqgnmnwyg ttnsinpywl akyklnqdir drflmngsiq ykfndwlnae arlgrdqytt
      481 nyenktyags pisatgqygl gkntffennf tlalnakkdn lvgkwggals lfgqimkqks
      541 tgldanagnl evpnlfyiqn sisnpvvnqs latkqinsly angeinydny wfinftgrnd
      601 wsstlgnnnr sffypsvsts lvisdmitkn ggqlpswlsf akvrgsyaqv gndlssfqly
      661 nvfnigkdpn gnttagmpnt kfnpdilsel iktiefgfda rffqsrmgid fawyknnatn
      721 qiinipadpf sgyefekina gniqnsgiev vldgrifdnr egfswtssin fsnnrnkiid
      781 lsaasdiypl gsydnvavra vkgslygdiy gtkflrveda nseyngqlil ngnglpqass
      841 gmvklgnqap kalvgwtnsf afknfglsfl idgrfggefy sgtnlnlqvn gsaavtapng
      901 qrdkflvdgv vtsgtgyakn tvettqqlyw nqvgttsgnf gigeanvyda tnirlrnlsl
      961 synfpstilk nsiiqrakis vtannvwmik shangvdpes vfainsnatg fenfstptsr
     1021 sfffnvtlgf
//
LOCUS       WP_104385337            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104385337
VERSION     WP_104385337.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115362
     Region          44..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrgsmhaqal mtlaltlnls ptiaksgnsi ssanygyssl glqqtirgki ldgkgqgiga
       61 vtvrnltagt taqsapdgsf siaakqgdql efssvgydrq tvsvngsgpl aitlankstv
      121 ledvtvtgyt nysrkqsanv sttvkakdle qvpmasvdqm lqgrvpgmsv massgqpgat
      181 asvvirgvgs ingisdplyv idgipiatse lknfsandfe svnvlrdatg kslygsrgsn
      241 gvivittkkg ksgqlnvnfn sqygiskltr pkfqmmntqq rlqfeeelga fvdpdnnegi
      301 gpgwtyspkn pdvvsgtpvy karaaqilds lrginvdwrd yffrngkfmd qqvnvsggge
      361 hvrfyssagy ykqegvairs gldrytlknn vdfdkgklsg ginvtlgytn skftegvgas
      421 rvgssmasvy yalpyeypya pdgtlihfgn eddyfildqr egsaglerll nssssselfn
      481 tnvglnlnyq llptlkvhtr lgidyntttg qdyidpdsyy gsrdrdptlg gkglfaednl
      541 rstnlisttg ltyqntfdek hnlelsayfe ylyrrnrafg ykgygidsrl penpngvtvs
      601 ptylpailgg rtkyalasym algrytydnr ysltasyryd gssrvaeanr whgfysfgan
      661 wnikeeeflk snefikglsl rasygttast ingdfnylat frkditygge tairpydpgn
      721 pnydweyvde fnagfdlelf pskrlrvamd yynkitknmf fdqpisltsg fldrklplst
      781 gkmrnrgvem svsgdvvktt dwgltlgvna synkntilyl sdaltevldg dtrimrvglp
      841 ygtyyapewa gvnpqtgdaq yynrdgsvtt eydetsqavt ksgsmfpkwv ggfnttvrwk
      901 slsldalfaf vsdvrrwnne dfynenssym tsnqsirmlt drwkqpgdna ilqridipre
      961 ytskdiqdas flrlrnvnlv yqfpktlfgd qkvikgarif fqgqnlltwt swrgldpens
     1021 egisrfnypa prtytagfsv nf
//
LOCUS       WP_104385022            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104385022
VERSION     WP_104385022.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122483
     Region          28..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfykktag lalctlfsat slyaqqsitg ivsdakgpis gatvsvkgtt rgtqtaangs
       61 ftiqasqget lrisivgyks qeivvgstkt lnitltedas aleevvvtam gikrapkelg
      121 yamstvdske ltktgspnfa galygkapgv risaapggat sgininirgt nsitgnsqpl
      181 viidgvpmrq tsfnnsdywg dqrargngle dlnpedieni silkgasaaa lygseamngv
      241 vlvttksgka gkgfsvdfna tythdqiayl prfqdvrgpg yskayndvkq addlffyygd
      301 edkvngvtrg lmntslnfgp kfdgkdiisw dgqvrpysaq nsynkffnnp nnsifnlaig
      361 ntsensnirf sltrqdnqmt aldsynkknv anlnasftlw nkfkndvvvn fvnqhthnrp
      421 fltdrlinnt agmistfdnp ewylnkyrts lgykyvikdp ntqsltpded ihyfgyrgdv
      481 lgflwdtkak qydeysnrli gsytatwsit ddlslrgrvs advtsqrtes rqpneiplef
      541 gnsggfslgn qnaniyytdl latynknine dikigviagy tatrsqdtyv qnetsggltv
      601 rdwfdvnasl nqpirndryn yrnymlrdav fgtlnfnlkq fwnvegtlrr eristmnpdn
      661 nvlyypsvns sfilsdaikl peffnyaklr aswgivgsyp diyksalayt vktlgpqvtn
      721 gasviystlp ttgfgnidik petkneiefg letkmlngrl gldvtyyngl vkdqiinytl
      781 pissgsnsil anvgslrntg wefaingtpi qkenfkwsst lnfsmnnnkv vslpgnastl
      841 llrdydgnaa qlvanvgqsm gdimvrptkm dengnrvvss nglyeidgdr wikagnalpk
      901 avgglinnfs yknfsldvlm dfrlggsvmp tgtnwmisrg lleeslnnmd aehgglsyyq
      961 aknangsivg iatnattgpn getvyhdgml ldgvladgss ntniisqaty yantynwggp
     1021 qysqsryely vkknnyvkmr eisigyrlpa svanklkakn iqlsafgrnl ffvyrsikdl
     1081 dpeqmtggsn winsvsnagt spatrtyglm lrasf
//
LOCUS       WP_104385370            1159 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104385370
VERSION     WP_104385370.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1159)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1159)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1159)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1159
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1159
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129503
     Region          172..1157
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkftltpftk kekdfhsfhl dadvasgvqr iyekqkplfa rplsrslmri nlitlliglg
       61 lsqvdahtya qqvslkkqks slesilknle kqsgysffyk kneinqiidl sadikeapfk
      121 qvlniifnka nlsydffdkt vvirrelmds hkksntlsfv lpsqinaiqq aiagrvvded
      181 gkpisgatlr lksdtkkavv samdgsfnlp ltaagetiiv tsigyepyef sakfsghllm
      241 vklkkieskv eevvvtgmmt rkkesfsgat asftgqelkm vnnqnviagl raldpsfiqi
      301 ennalgsnpn mlptielrgq tsistsalrd efsidpnqpl fildgfetnl rtimdldmni
      361 iqnvtilkda astaiygsra sngvivveti kpkagkimls yttdmqaqip dlssynmmna
      421 pekleferls grytaksnli eqqilldsiy narlqevlsg vdtywlkipv qtgfshrhsl
      481 sarggegalv fdagvnyknt kgsmkgsgrd dwsanlnlny ragklnianr afvtgytgne
      541 spygsfstwa ntnpyyrpls aaekfltyke dartsnyswn vfnpiydanl ssfnttknyv
      601 innnlmmtyd fntalrltas gqiskgmtnt dnflsplhss fegvenrkkg slahresstf
      661 gytanamlty skvlqdkhti tanlrgeise sqnrlngyka vgfpaasngn psfafgfeqd
      721 skpsastris rrtsilgsin ysydqrfnfd inynldgsts fgsnnlfspy ysfgtswnih
      781 nerfaktanw inmlrvrani gitgnqnfgn vsqsifdyns dvnrfgqgiv lsalgapdle
      841 wqrtrqtsvg vdatlfnnkl nfqinaydkf tdplvvavtl psstglsayp fnagtldykg
      901 leatinyspi yrpqnqfivt fgltgsmlka kyahfdnkls alnnemkqsn aliryrdgys
      961 pntlwavqsq gidpssgrev fltkageqtf nynaddlvav gnaqplaegi lrgtlsykgf
     1021 ttnvlvryil rkdnfnnaly dkvenmseee ivknnqdkra lydrwqnpgd iaqfrgisit
     1081 ditpmssrfi qrensfsges isfgyefrnk twldrlnlst vrinsilndi fysstvrrer
     1141 giaypfsrsv sfslnatfk
//
LOCUS       WP_104385379            1121 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104385379
VERSION     WP_104385379.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1121)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1121)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1121)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1121
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1121
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125845
     Region          121..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtnyylkl mggallfqsl alqsmasqfs tsegigkila rmeqkfnvkf gydasisdqk
       61 inaaanvdhl kkdqivqfiq tisngnlevk kiddklyvvs kknisaskde ngrtinaqee
      121 vrgkvvdqet glpiagvtvr vkgssvastt dqnglfklps vtegamlqis ylgyetvnip
      181 vsqagtikla kssealeevv vtalgikreq ralgyatqsv kgedltrvkg vdvgttltgr
      241 vsgvrvlnst efnktpeiqv rgltpilvid gvayenmdlr dvpvdniqdm nvlkgatata
      301 lygskgegga imittkkgla dkgteitvnt nnmffsgyla lpevqhsyss gesgkfnndd
      361 yvwgdkldig rtaeqwnpit kayevqelts rgknnfknfl epgfisnntv sftnqgehgs
      421 irtsinhiyn kgqypnqkln ltnisvtgtt kindkldlea rlgynrssss tnfgsgyndq
      481 gyiynilvwt gpeydlrdyk dywlvkdqsq nwmykgwydn pyliahekit pelinkmnaa
      541 vtlnykingw akfmlrsgyd yygksrtqrn pigiygtrgg fsdfrddlsv fggfdskgky
      601 vkandngfst tndailtgkk sfgdfgidgl lggsvfyssd qtlvagtmng lsipgfyslr
      661 nsigpvssve irprqmrngi ygrlslswrn alfleatgrn dwvstltken rsyfypslsa
      721 savvtdllas kpmwldmfkv raswavtksv ldpyevhsaf tvkgnvwngm ptasypniik
      781 dysisptqrd ltefgfdfai lknriygnyt ryyrllhnqi vkakiskttg feerlintke
      841 eemtkgheit lgttaikrvn fqwdatinls qnlryfhkld peyskdalyv kqglradyie
      901 ykdwerapdg qlvlnssgmp isaqyanqlv gytapkwfwg fsnqfrykdf tfgfsldgri
      961 kgmsystmna rlwqtgshpd sdtefryeev vngnktfiap gvkivsgtvk ydkygqited
     1021 trvfekndqv vsyegyykra ysgrwnywde tfiklrelsl syrvsdkfas klkakkasvg
     1081 ltgqnlllwt kefrfsdpdt gsedlnspsm ryigfnvnlt f
//
LOCUS       WP_104385469            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104385469
VERSION     WP_104385469.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115739
     Region          48..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfnhyiklsv vgvllviadk qtvqaswypr lreivsgyad gvigkfpkil deygkpisga
       61 kvfdaerqli getdengdfs ltggiiheal wveypgyyrk mikgdseksv slvpavlqra
      121 dslyisydkk kssellgavs vvynsqikdv ptplylnalt gripglftqe vsgfrspsmt
      181 aitandlags lpsdavkyrs sigdnteigf slrgqspitl idgvqrdiys idpeniesvt
      241 vlkdalssil lgqrssrgil qvttkkgqag pprisftaqt giqqslkmpq plnayqyayl
      301 yneallnagr qpvyssddfk afrdgtnslf fpdvnwydav vrdnnpitky nlgvkggikn
      361 aryalslsyl nqyglfksdd kfdyetnlqn krylinsaid vdvtddltig lqffgkiqdg
      421 rqpgaktgti lstlyntpnn aypifnpdqs yggssvyrsn lyqlttgsgy lldntrdlla
      481 nldfnykldk fvpglyakgk lnvsstsssl idrnrqqpvy dlsyneqkel vyvrygtiad
      541 qpnsfattst anffyfqgal gydkqvsekh rvgaklfmdr qtanyqfdlp aiytnfaata
      601 nyayqdkyfa evalnysgfn rfmpgnqygl fygfglgwdm mqedflkeka dwlsqlkwsa
      661 tfgrtgntne aalgyyswra sygqdgangy dfgseyaytn sliekglani egtwekgnkf
      721 nigldaafwh stlkltadyf rdtyfdllqq rgstidligi gypnenigkn ryegqeislt
      781 yqnnfgefny fitanasrmk tqvlymnevf qqynwnrrtg mpvgqtfgyr adgliqtqee
      841 adnapllsgn kvypgdvklv dlngdgiinq ydqtaigntk plvyfgttlg fnvagfdfsv
      901 llqgvlnrsy qqtdysfgnt gdgqgfdyml grwtpetgta asyprltlgp dptntqniss
      961 ywtrsgeylr vrnldvgytl pfnwtqrakl ssvrifanaq nlftftpygr ldpeissgta
     1021 ypaqriisfg vnvkl
//
LOCUS       WP_104385516             988 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104385516
VERSION     WP_104385516.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109219
     Region          28..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkqllrpfw alnmllgvsa safaqqatlq grvmdqkgns llgatvrfed iqkslstnan
       61 gdfsldrlqt gklhlkvsmv gyasldtliq vndgrnplnl ylksntsale evvvigygtq
      121 kksdltgsis tvtskdfqkg qisspeqlim gkvpgvqitt sggqpgagst irirtgasln
      181 asndplivvd giplagggis gvanplsmin pndietftil kdanataiyg srasngvimi
      241 ttkkgsragt qvnfstqnsl atvakkvdll sadqirdyvn angtdamkkl lgtantdwqd
      301 viygnafttd nniniaskva empyrvsvgy mdqngvlknd nmkrtatsla ltpnffdnhl
      361 klevnaratw skskfatqda igsaiqfdpt qpvyvddkns fggyyewiqg gkpnpnsprn
      421 plallelrkd igdvfrstgn akldysmhfl pelhvnlnvs ydlarakgnt ltpaiaarnf
      481 neggertqyk sdinnkvlef ylkydkelpa iksnidatlg ygyyknstks ynfdrtneag
      541 dvltsvnlpf dkpenllisy ygrmiysydn ryvlsgtlra dgssrfspdn rwgyfpsvgf
      601 twraknegfl kdhnaisdlk lrlsygktgq qdgianysym pnytiggdqs myrfgneyyy
      661 lyspvvydad irwestttyn agidfgfndn riygsvdyys kktkdllsti piavgsnfsn
      721 flltnvgnme nqglefnlhv lpiktenstl dlginltynr skvtnltlse dpnfmietgg
      781 irggtgnniq ahmvgytpys frvyqqvydd agkpveglyv drngdgvisd sdrymykspl
      841 pkyligfsaa ysykkwsast tlranldnyv ydnvssnfgs synvidqasl vinnapvdfl
      901 ntnfkekqll sdyyvknasf lkmdnlnvay qvghfirnsk atlsisatvq nvftiskykg
      961 vdpeisngid drfyprprty vlgvnvnf
//
LOCUS       WP_104385522             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104385522
VERSION     WP_104385522.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108071
     Region          27..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkllaqci mvptfmlvtl vamaqtrvlk gkvvdetqsp ltgatikvkg tatatttdpe
       61 gsfslnisnd akflevsyig yamkevpiag ndmtialeps tdqgleevvv igygtarkkd
      121 ltgsmvtiga knfnkgimts pdqliqgktp gvmvinntgq pggsttvrir gnssirasnn
      181 plfvldgvpm sgnsplpegr ggfssdrgnp ltylnpgdia smdilkdasa taiygsrgan
      241 gvviittkkg kvgspevsvg asagvstmre ypdvlnaarf realkyytps eaadsdfggn
      301 edafkaitrk aitqnyyadv aggteygkyr lsggylnqng iirgsqlkky tanftgnfrf
      361 lenkrlgldf avfltqmdnk yapinatvgs egnvisqalq wnptrplrde qgnltfvsst
      421 trnpltsiea frdlattntm vvnlapyyki tddleyrfiy samrqtgnre gmyraglidp
      481 savnneqafi snngetnlqm thmlsynkqi nedwnvnava gyeyldynfn nniafgggfr
      541 ymgldyfdyl qyssvstrev asyrsptnql qslflrggfn yldrylftat vrrdgstkfg
      601 snnkyavfps lavawnvaqe dflkssgifd qlklrlgwgk tgnqefpsga slnrlvfgnq
      661 svsqanygnp dlkwetstti nagidfgifg nrlygsidyf nkkttdalfe qtlaqpapag
      721 riwvnldgei vnkgveialt gtivkndnwt wdltgnatfl knsvsglvgy yetgalrgqg
      781 fsgvlgqrmv ngqplnvwyl adyqgidpqt gmsmyrgqdg sisttndpai nkfythspnp
      841 ttllgistnl nykqfslaan mngafghylf nntaattlgl snlssrnigs affdtsvkes
      901 tsnsaapstr flekgnylkm anltlsykvg dvgktlknln vsltgqnlfi itkytgfdpe
      961 vntdgatngi pslgieylpy pparnillgv nfsl
//
LOCUS       WP_104388800             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cuspidothrix issatschenkoi].
ACCESSION   WP_104388800
VERSION     WP_104388800.1
KEYWORDS    RefSeq.
SOURCE      Cuspidothrix issatschenkoi
  ORGANISM  Cuspidothrix issatschenkoi
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Aphanizomenonaceae; Cuspidothrix.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Cuspidothrix issatschenkoi"
                     /db_xref="taxon:230752"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40725
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeie vcerrvslip divaklvkqg levlvetgag ekafftdady eaagakivgd
       61 stqlwseadi llkvsppqdr edgrseidll kpgsvlisfl nplgnpeiaq klahrqvtal
      121 smeliprstr aqsmdalssq aslagyktvl laaaalpkyf pmlttaagti apakifimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkleeetvaa ggyakeised
      241 skkrtqelva ehvknsdvvi ttaqvpgrka pilvteemvk amkpgsvivd laaeqggnca
      301 ctepgkdivw ngvtiigpin lpssmpvhas qlyaknvtsl mqllikdkel qinfaddivd
      361 aacvthggei rnqrvkdalq avav
//
LOCUS       WP_104392919             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            nova].
ACCESSION   WP_104392919
VERSION     WP_104392919.1
KEYWORDS    RefSeq.
SOURCE      Nocardia nova
  ORGANISM  Nocardia nova
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Nocardia nova"
                     /db_xref="taxon:37330"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37328
     Region          2..349
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(11,66,85,278,304,306)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(40,118..119,128..129,132..133,136..137,139..140,
                     142..147,149,151..153,156,179..180,268..269,311..312,316,
                     319..320)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(113..114,118,121,124,165..168,188..190,218,229,
                     246..248,255,257)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(115..116,118,128,171..172,179,195..196,198..201)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(148..152,155,158,181,183)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvretnader rvalvpkiip slvkqgvqvv veagagvgal ipdeayeaag atigdpwqae
       61 vvvkvappnd aeiaklsegq tligflaprn adnkigalqn agvrafavea iprisraqvm
      121 dalssqanva gykavllaas estrffpmlt taagtvkpat vlvlgvgvag lqalatakrl
      181 garttgydvr pevadqvrsv gaqwldlgid aageggyare ltedekaqqq qaledaikgf
      241 dvvvttalvp grpaprlvta aavegmkpgs vivdlagetg gnceltepgk tvvkhgvtic
      301 splnlpatmp ehaselyskn iaallelmlk dgelepdfsd qvladscvag apsrpadsee
      361 qg
//
LOCUS       WP_104396825             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microcystis aeruginosa].
ACCESSION   WP_104396825
VERSION     WP_104396825.1
KEYWORDS    RefSeq.
SOURCE      Microcystis aeruginosa
  ORGANISM  Microcystis aeruginosa
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Microcystis aeruginosa"
                     /db_xref="taxon:1126"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40161
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikesd qgearvalvp dtvarlvkag fevivqngag isanfadsay savgaalsen
       61 seyiyesadi ilkvvppsds eidrlkgggi ligfldplrq prriaklaer gitalsmeli
      121 prssraqsmd alssqanlag ykavllaavq lpkmfpmmtt aagtiapakv lvlgagvagl
      181 qacatarrlg avveafdirp qvkeevqsvg akfiemplee dtvadngyak evslstqeri
      241 cqalaepikr advvittaqv pgkqapllvt kemiatmkag svivdlaaeq ggncaytqpg
      301 reiiengvki vgavnlpatv atnasqmyak nlqmllqllv skegslnldf addiidsacv
      361 thageirnqr iksalseqls af
//
LOCUS       WP_104402146             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            penaeicida].
ACCESSION   WP_104402146
VERSION     WP_104402146.1
KEYWORDS    RefSeq.
SOURCE      Vibrio penaeicida
  ORGANISM  Vibrio penaeicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Vibrio penaeicida"
                     /db_xref="taxon:104609"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54472
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpketl agerrvaatp ktveqllklg fdvsvesqag vlasfddaaf esagatvvsr
       61 dnvwksdlil kvnapqvdpe sgvdefdlik egaslisfiw paqnealmek lsskninvma
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv qsmgaeflev dfqensgsgd gyakemsdef
      241 nkkaeelyaa qakdvdiiit talipgrpap klitkamvds mkagsvivdl aaanggncey
      301 tvadevittp ngvkivgytd mvgrlptqss qlygtnlvnl lkllckekdg nidinfedvv
      361 lrgvtvvkeg eitwpappiq vsaqpevkpk aqsveavkae eptspvkkva alvigvgafa
      421 wvasvapasf lahftvfvla cvvgyyvvwn vshslhtplm svtnaisgii vvgallqigq
      481 gsgvvtflsf iavliasini fggftvtkrm lemfrkd
//
LOCUS       WP_104405265            1141 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroidales].
ACCESSION   WP_104405265
VERSION     WP_104405265.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 1141)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1141)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1141)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1141
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..1141
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126769
     Region          23..1140
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrikylltl alcfccsvaf aqkritghvw sssdngpvvm anvaeidksn raisatqtda
       61 ngnfslaikn pnntlqisyi gykterispi gsrtnfrvel hdkntiagae vvvtrktqsn
      121 glvipereis vakqtlnmdq meglsfetag ealqgqiagl divansgnlg agtsmrlrgv
      181 tsingnqepl ivvngqiled ydsedfdand mneekfatll qvnpediqti nvlkdaaata
      241 iwgargsngv ieittrrgar gktrvnfsyr fsgawqpegm nmlngdqykm mlqqayhnpn
      301 pqagnpadai velqdlptyt ayrynynknt dwidevtqfg qthnygiais gggdkatfrv
      361 sgsydhetgt vikqtldrfs srlaldyyvs drikfssdfs ltytkqnkni ddglmgrayq
      421 ampnmavtrw eydrqngryf dtgdyyqmpq aaaaagmvsn nsnkssyyls dmvsngnpva
      481 ianlswrrws tytitpqfkl eykllgkddd ethldytgev ymnaytetkn syrpsslspg
      541 swsdgintts ndefkslafn trhqlvfkpy fvnpdhslqv larlevgsqn strqslsssg
      601 igggitdptv pgyltgasts tgkghtmsgi gsfhysfgsk ysldftlrad gstkfgsgnk
      661 wgffpgvsgr wnisdeaffk plkkvvsmla frpgwgvtgn csfgegliyn qysafdsyng
      721 vaairpsnlr ltqiqwektk swnmgfnlhl fedllqfdln vykkkttdll nynvripstt
      781 gfstlsaanv gsmenegwel yintgklfev gkfstvlrfn iaqnintits mdasvlasnn
      841 kdfdyangne svmqrvqigh alggiygfry kgvyaydykh ngyflnqsdn eyylpepdan
      901 gnmyntakat gktapivrda qgnvvydkng nplqmvynyg gvnykfeggd viyedinhdg
      961 qideldivyl ggsnpkvngg fgvdfnfgqw tlktnfnfri gnkiinlarm yaedmrtnkn
     1021 qsaavnhrwr tngqvteipr amstkvangn tynalisdry vepgdylrfq yfqigynfka
     1081 dklkkyglss lrlaasgnnl ifwskykgvd pdhsssgfsp ctdssqtprs rsftvslnvg
     1141 f
//
LOCUS       WP_104418149            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104418149
VERSION     WP_104418149.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115256
     Region          22..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpittalgl lvllsgslsa qrtlsgsvtd dsgpligatv maqgttigtv tdldglfals
       61 vpegiesllv tytgyegrti pitaaseyei sldesaldls evvvtalgvk rekkslgyav
      121 qdldgeaieq trstnvingl sgkvaglqvs agnvpgggsq vvirgnssvl gnnqplyvid
      181 gvpmegdfaa pidgatdnnv ygggiseisp dniesitvlk ganaaalygs raangvilvt
      241 tksganaegl tisyagsysi enpfvvpefq niygggtggv twysdgrngg itdplaleqf
      301 rsvypnaplv gtagvdeswg apmdgrlvrh wwsgtevapl vpvpdswsnf wdtgntsnnt
      361 lsisnnygtg nfrfsfgrmd tkgimynndy ernnfrlnid qelapklkvs vsseyiksgs
      421 dnrqqpglwe lgtwhhrhdd wgvlrnyady mdvhivregd wypyanwqhs fasnrfyeqe
      481 nltnanekdr llgnvaftye flpslslmvr agtdmwtdtr rsvnryasik sgnelnesfs
      541 edvlrrqetn ldfiltynny fgedfsvnaq fggnhrsnyf krnyigvnda tinglynvsn
      601 nasqntnvsr ieekevnsff gaasfgyksf lyldvtarnd wsstlpvenn syfypsvsls
      661 gvitdalsis spilsyakvr agwaqvgsdt dpyrlrqvfa patpwnattp lfaeqatian
      721 sdlrperttg keagldlrfl ggrialdvta yeqttedqii niavsratgy gsklinagkv
      781 rnrgvevils gaivdlpkfg wdvslnyakn nntvlelytd esgneletiv ltslrglsle
      841 arvgqpfgtl fgsgfarvpd gelageiife ngipvkdpdl kvlgnvnpdw iggirntfrl
      901 gafsanvlvd arvggeiaeq stslgmqtgv ypmtaigree gvigngarni gdgetpiyvt
      961 ndvvaptrdv vgalspryan egaifdasfv klreagitya lpqallsnvs firaasisli
     1021 grnlamlysn hsqidpefnv sggnllgals yttipstrsf gvnlnvtf
//
LOCUS       WP_104418256             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104418256
VERSION     WP_104418256.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106743
     Region          25..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktrlyfvla lffsafavag aqslitgtvt dadnqpltgv tvsvaatgtg nvtdldgrfs
       61 veaavgdilr fsyigmaare ievestdelt vvlesdaaql deivvvgygs kkrsdvtgsi
      121 asvknenfnk gvvvnpgqll qgkiagvnvt aasgepgaaq diiirgvgsl rsgttplfvv
      181 dgfaldntvn gvptnplnfi npadiesidv lkdasaaaiy garaangviv ittkqgragq
      241 sqinvsasta itslarkidv fdaaafrnqi naiggvlndg gadtdwqdel trtantnrvn
      301 lsmsggagss syfasfsaen qegilrnndl erysarlnlt qralndrfkv dfnfsatrfe
      361 nsrpnttsvv tdmlqlnptf patvdgeptd lvgdninplv reriyddlsy nnrilanlap
      421 sieivdnlvy rfsvgvdyst tnrdvqfmpy psindfelgs lnsfttsntn tqaentltys
      481 idrgihdlsf laghsfqqie veqkgffteg fpnngvepry qvgaaseptr qsafatinel
      541 qsffgrinyg fndkylitat mradgsskfg annkygyfps valawnvtne pflassdvft
      601 nlkvraswgq tgnqeipski tqasftesns gndtypldpn asdlseypyg siytrlanpn
      661 iqwevstqtn vgldfalfny rltgnvdffn kvsenillev apvdpiqptd rfwtnipnme
      721 irntgvelal nynsdetraf vygiggnisv tenevrnspy silttgsvig agqsgating
      781 vlngepigtf fvqdfigige dglnqfadin gdgeildndr faagtalpsy iyamnvnfay
      841 knfdlginfn gvggnkifnh valslyskgn lsnslnttdl avqfpnedvs nsnrvstryl
      901 edgdylrlnn atlgynfdld rlgignvvkn irlsftgqnl llftnytgfd peintgssvg
      961 diqtfgidyf syprgrtflf gldvtf
//
LOCUS       WP_104417984            1091 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104417984
VERSION     WP_104417984.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1091
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119897
     Region          23..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkliyltllt cclagvtpla aqqtvtgrit dpnnepliga svlipgtnag tvtnfdgdfe
       61 ltvpslndtl lvtyvgyetl repingrtev mfllregald lnavtvtalg iereakalgy
      121 avqeidgeql drvkdpnlin nlagklagvr vtgggsgigs ssrivirges slsgdnqplf
      181 vvngvpinnd ngnngggngn maadygnsaa dinpddieti tvlkganata lygsraangv
      241 vlittksgag krgigasfss nttferplri peyqnsygqg aggqfafgdg fgagtndnid
      301 eswgpafagn plivqhnspt ssglragdfa vrprtedgqf adeatalpwt aapgniedff
      361 etgyttintv alyggdeqrn frlsysntan egilpntdls rnnltldvgq nfldqklrvr
      421 ananyinsss dnrpnnsygt envmylwvwf grqiqmnslr dywqpgqeni qqfnynynwh
      481 dnpyftmyen tnafdenrlf gnvnatydft delqlmvryg ldtydelrtg rrawstqrfp
      541 rgqyrednif fqernadfll tyapqigetf tatisaggnq mtqerrfrrt sanelavpgv
      601 ysfnnaaipl vnnqfnsrrr inslyatanl gfrnflyldl sarndwsstl paannsyfyp
      661 saslsavlse vidfpaavsf aklragygqv gadtdpyrll gyfqfssnty ggqllgtedn
      721 llananlkpe rlntlefgad lrflrgrlgl dltwynnvsr dqilqvpvsq ssgygaryfn
      781 ageieskgve lllngepvsr gnfdwrvnln ftrarstvne lapgiesyql ssnyltvlar
      841 pgermgdvyg tgfvlidtet nervtvddva dikdtyahly dangfpvrdp nlrrlgnynp
      901 dfqlglnndf rignvdfgfl wdwsqggvim srtlliggts gmmaetaeyd rettdfiggt
      961 trvtgvseld rngvvatgdg tyvpnttals ardfywshfn rdnetvgmyd atflklrear
     1021 igynlprewv sgigaqrirl sligrnlllf tenphfdpev fsyggggivp gvedmatpss
     1081 rsfgfnlnvv f
//
LOCUS       WP_104385910            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium sp. HMA12].
ACCESSION   WP_104385910
VERSION     WP_104385910.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. HMA12
  ORGANISM  Sphingobacterium sp. HMA12
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Sphingobacterium sp. HMA12"
                     /db_xref="taxon:2050894"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120277
     Region          28..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktfilmvlf lfisgianfa igqnlmakie gkvissdnkk piqgasisis rgksttksdq
       61 egrfviranh gdsvlvshig yhsetilykt gtssltimlv pvanvlnevi vssgyqqlrp
      121 nemtgsfqvl dkkildqqvg tnildrlnnl tpgfrkgtfe fkpnrnekln isirglstie
      181 askdplivld gfiyegdidn idptsiasvt vlkdaaatsi wgaragngvi vmnsintank
      241 sqktivnish ttttkritdy nrlyqpanld yilaeqelfn agyydgkleq spylaltptv
      301 evflarrrgl isaqdstdri aellamdgka ayrdaflkap flqqsfanis gastvirynf
      361 gvgntmdlse nrakdnkinl ylnnsfhwkd kfelnlnvnf ltqkqrsgts vldqfkyggk
      421 yvpffefmna egevlpfnrs yrgnylnely gdklldwnyy plhdyeldra ttrknelyai
      481 vqakynikpy ltaavsyqyq iqrkvteria qaesyyarnl inmfssidpq sglvarpipi
      541 ggiydlnngd issntwrgql nfnrsfgvhh ingilgaeir evlskgstss sygysadpir
      601 tkvvdyagfy ptlpaggfss iqgnislmks lnrfvshyan vaylfkqryg lsasirkdga
      661 nvfgintndk fnpfwsvgas wqirkekfad wkavdalqlr atygysgnid psrtplpvae
      721 ttsgrytnyp afvistlndp slrwekvrtl nlglqfglfk sritasfdyy vkkstdlygn
      781 slidytvfgk anttiknnas irsqgaelnl taeavrtpsf swrpavllsl nknkvleyyn
      841 tqfglinlvg ngsstipivg rplnsiaafn wggldehgdp qgflngelsn dyqkirnstv
      901 getddnqtiv fvgssvpqlf gnlintfsyr nfelsfnlsf kadyyfskqa ttsgnfylyg
      961 kaysdfdrrw qspgdenytq vprvkypida nrdafyqess vnvlkgdhvr veyinlswrn
     1021 lwqlgskkln trlffngsnl gliwkknkeg vdpdfpgrlt pnptyaigln vnf
//
LOCUS       WP_104418348            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104418348
VERSION     WP_104418348.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121368
     Region          20..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkftltlllv wsvvgislaq tvsgtitdea gnpliganil evgtdngtvt dvdgfysfep
       61 tgdnptlris yigfgaqelv lngrttldvt ltegnnidev vvtalgvsre rkalgyatve
      121 lqteditktq vtnfasalyg kapgvsirst pggatsgini nirgqasitg ntqplivldg
      181 vpirngefnn ssywddqriq gnglldinpe dianisvlkg asaaalygsd avngvilitt
      241 kkgkfnqglg vefnasyntd riaylpryqn vrgpgypvsl adagqgadrf igydtdgdee
      301 ndvrglints vnfgpnfdgq pvmawdgvvr pyvssensyg dlfqpanssn vnlavskgte
      361 afnfrvslsr qdnqmisfns knerniltft tnydinerls sslnvryinq stnnrpykvd
      421 rmvnnftgmm drfesadwyf dryktsdgyy frtgtqpstt peeniiyngf ksdiadyvwr
      481 vneyqsrenn nrvianftqr wnvigglnlq grlstdytaq eteswnstel psalynnpgg
      541 afsltnyten llygdvilny dldvtddisl gvlagytark ydyaltsigt vnglspenkf
      601 dlsasrdipq gratrateit dglftslsfg fktfwfvegt irrdristia pgnnsfsyps
      661 vnsslilnei fdlprsisya klrasygvvg nypgrylani nyiqntlgvq sgggsaviyt
      721 nlgnafgnel irperkkeve fginlnflnr frvdatyyng riidqilpvd vptssgattv
      781 ltnigvlrne gmefslgadi irnenfnwtt tinfarnint veqlandatq lihadfdgna
      841 aqvrsvvgrp mgdiyahpva tdandnrivg pnglyqldgd nwevygnalp dfeggflttl
      901 gykfltlnfv adfsyggsim ptgiywmtsr glteeslnym daesgglryy qnedgqgvqt
      961 tanegpngel vfndgilleg vningepntn vvsqaryyng tynwggpqyg nsryelyine
     1021 nnwvkvrela lgfnlpttwl sgvgmqnani svygrniffi yrsikdldpe qttagsrwyq
     1081 ninnagnnps frsfgvqfkt sf
//
LOCUS       WP_104418334             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104418334
VERSION     WP_104418334.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107506
     Region          43..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqktkstral pgasvscfsl phllsfgffl llsvtgraqt vevsgtvtdg ngealvgvsv
       61 fekdnasasg tvtdldgsys lsvppdavli fsyvgfgtee ipvqnrttid vtlgntstnl
      121 nevvvigygt terqqvtssv asideaqfnk gnvnnplqfl qgkvaglsin rsgsdpnggf
      181 avrlrglstf ganaspliii dgvqggnlel vdpndiasid vlkdgsaaai ygsrgssgvi
      241 ivttkkgreg trgvtfdayg tideiarsvp iasaerfvee ggtdlgydtd wldlvtrtgv
      301 sqtynlalng ssaessyrls vnyrdqegia rnsgfnqfnt rlnlnhsvld srlnftgnvs
      361 vnirnasfvp yealgfalis nptapvyvdn dpelgylepn ttefhnpvai meentregky
      421 ktmlgsirad yellegltas afyslqyrse iygayatsaq rfggfdglqg radrnsldeq
      481 nslfeltgsy kkrvgrvdln ivggytyqel itenfnvfnt gfitdelgyn nldfglgins
      541 edvtrrgfds gkgqsllasf fgralvsfed tysftaayrr egssrfgann rwgnfyslsa
      601 gvdlakalni pmdrlklrag ygvtgnlptp fyayrvllsn agtipfndgn aernirlfny
      661 asnpnpdlkw eqkaetnigi dfalfdyrlt gsidaytrns tdllfnqpvs qppnffgstl
      721 lnlgeleskg lelvvdynvi nqealayttg itfstnktti islnedsqvf fggnpgppgl
      781 ngtnviraav geelgqiqap rflgldadgn rqyeeltdld gngaierfnd wpivgnalpd
      841 felawnnslt fgnfdfsatf rgafghsian israyyevpd nvnnynlvit dfylpdmvgn
      901 eewsdyyvek adyvkldnaa lgynfdlgns sfrqlrvyva tqnpivissy tgvdpeprig
      961 dalypgveyr nnyfrsrsyt igvkvgl
//
LOCUS       WP_104418428            1145 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104418428
VERSION     WP_104418428.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1145
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125754
     Region          44..110
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          120..1144
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miatyrhsft rtiyrlcplc vlvaglvapv rgqgpspgla naafrdaplr qvldvieeqt
       61 dftfvydtrv lnpdqgftld atdepleavl dtlsergdle fevvdriiti rkkenaaeiv
      121 rgsvhdaegf plpgatvmeq gttngtttdy dgnfslavts adatlevsyi gygtrtveat
      181 agsvqdiils dnvnsfdavv vtalgikree kklgfsqatv kadnlaqavp nnwtsalqgk
      241 vaglnitsas sgpmgsqqit lrgnnsldpn gnyalivvdg vpvnqeltps gsssaymgad
      301 spidygnais dlnlediesv tvlkgpgata lygsraanga livttksgrq arglgvtyns
      361 svsfdhiqrw pdwqyeygqg tgksfddngd pyysfgssed gnntgstssa wgpafdgqty
      421 yqydpavegq saerrpwrgy pdnrkdfwrt gvtynnnvsl qggneqgsmr lsaghsknew
      481 impntgferl tasinanyqi sdrievgsvi nynnrtsdnl pstgynngsi ayfmifqnpn
      541 vdldwyrpiw qdgqnqiqqi qpfssyidnp yliayeatna lgsdqivgni farlelaprl
      601 elmlrtslnt yhqdreqkrp ysinryargf yekqnifkqe vnsdfllsyd nqlgdgfays
      661 aslggnaldy ryrrtdasvd alvvpgvykl angvnnpivq tydrnrkvns lygllslsye
      721 ekifldltgr ndwsstlpvq nnsffypsan vsvilselfe lpeavsflky rfsfaqvgnd
      781 tdpyrtskyy sqsafpssas lstnlynpnf rpeitrsyet gietrllksr ltldatvyet
      841 ttknqiisip ldittgyssa vlnsgevrnr gveltltgkp ikserlnwts tltfsrnwnk
      901 vlaladgiqg qqeigsagqa tiiakeggtt taiygaafvr spdgqivydn aglpaypddi
      961 syigdaapdw raglynsfrl gkatlnftld gqyggiiysq thhklaeqgk lrstftgree
     1021 gfivgegvvl nedgtyapnt tpavtpdwyt ryyrranves nsfdasylkl revslaytft
     1081 gswlqtlriq gleaslfgrn lavvsdfpiy dpetatlngd tilpgaeigq mpspatygfn
     1141 lkltl
//
LOCUS       WP_104418596            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104418596
VERSION     WP_104418596.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116471
     Region          24..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqllsllva llcsaaiygq nsvtvsgtit dpdglpliga tviaqgtsvg tvadidgnye
       61 ltvpatvtdl vysftgyetq titlsgqtiv dvvmsegval devvvtgyav tskrqttgai
      121 stvsaeelta ipsgnveqql qgraagvtvi tngqpgtqsi irvrgfgsfg gnnplyvvdg
      181 vpqtnidfls pddiqntsil kdaasasiyg araangvvvi qtkrgsqeas plkvtynglt
      241 gftdpgsgnp iltpqqdatk tweairntaa angvdpvfnh pqygtgetpv ipdyimvgat
      301 sgyvgeidve dertrynidp asgdyyqvvr ankegtdwyd aitrtamvnr htlgfsgstd
      361 atryyvslga qiqegillnn dferytarmn tefdlgskvr fgqnlqfthr kvlgltgggg
      421 gagsaneenq ilsafrlnpl ipvrdifggy agtaaqgfgn prnpvaereg lannqsfeni
      481 afgnlylefe pieslvlrss fggkyvgfng rsygrrtyen aenigsfsys efqgystdwi
      541 wsntatytmd fgahnlnvlg gvealeignf rssngsginp fsesvdfvsl nnvdsrvvts
      601 gftygsrfys lfgqvnynfn dkyyltgvlr rdgssrfgad nrygtfpais aawrvtaepf
      661 mqnqtffadl kirggwgqmg nsnnvsgdnr fnlfgtglgp ssydiggtns savagfyrsr
      721 igtetarwet svtsnigfda tllggnfdvi vdiwrketnd llvqlavpnv lgpsatppsi
      781 nvgsmlnegi daqliyrtki agdfgieati ngailnneit kftddvdffd snvasprisg
      841 tivrnqvgmp lssffgynvv glfqsdlevq napdqegaap grfrfednns rdengeltgi
      901 pdgqiteadr tflgsavpdf tggvnlrfdy kgfdlttffy tslggevyny gkwftdfygt
      961 fvgaavstrv ldswtpqnps tnvpiyenis nfststesss yyvesadylr lqnislgysf
     1021 pddsfrgfvs tlrvaisann lftisgydgl dpavggaadt lfgvdlgnyp vtrgynlalt
     1081 vgf
//
LOCUS       WP_104418764            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104418764
VERSION     WP_104418764.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114722
     Region          27..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpqkirgvl sllvlflats vwaqqlvtgt vtgddgepli gvsvriegtg tgtvtdvdgt
       61 yslttqegnt liysytgygt vsrevgtqti idvelvagaq ldevvvtalg isrerkalgy
      121 aveeieseqi ertqqnnlvn slqgqvagvq vtsagggpgq gariiirgin sldpsannep
      181 lfvidgipvs netltaggga ernvsnriad inpqdvesmt vlkggpatal yglraangai
      241 iittkrgqag klsvdfstty gteevnkfpe tqrvytqgye gvydpdsfwp swgptveear
      301 qyaeenglpr pndlfnnyen afqqgnqwrh tlsvsggdek atfrtsisrl ehegvlpfsd
      361 yentsfrina nyvasekfnf gggvnyirsg gnrvnadrfs trltywapqy dvndyinedg
      421 smigyqagrt agnnpiygea tnkfiddvdr yignlnfsya pfpsltfnyt igldqysdfr
      481 qnygrgsvyp gapnfednls ngngfvvetr mrsrdvtsni ngiftstvlp dinmrflagf
      541 dvfdssydrv tttgydldiy dlfslnnaad iqtesnlrnr rllglygdls fdyrnavylt
      601 vtgrndwsst lpaanrsffy psvslglimd elielpsais ffkirtsyag igkdtdpyrt
      661 sivyanptgf piegvtgwsr gsqkgandlk pertntfeig tnlrflqnrl sldftyydak
      721 svdqiipvpt slttgfssfv lnagsmrnrg velmlkgspv atenflwdvt lnytrnrnev
      781 leiyegiedi figdhfgyag asatirlieg qpygniygrs yaryganddd lfidysqpml
      841 igadgfpvie ttqkilgntq pdwfgaiinn ftykgltfsf qidtrqgvqk ynqqgnffsa
      901 fgiapytlnr eetivfegvt adgepntqav ylgqgtgpdg raygagyyrn tyrgstenfv
      961 edadwirlrn vsisyqlpat llenlfidnv slrvtgnnlw ldtpysgfdp egnrgngntd
     1021 tgfggftypg vrtvfftlnv gf
//
LOCUS       WP_104419378            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104419378
VERSION     WP_104419378.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115405
     Region          22..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlllvgal vcfafgiaia qrtvsgnvtd vdgqgligas ilvegttsgt vsdidgsfsl
       61 avpdggevli vsytgfttek vvleegrtty dialeenaaq lgevvvtalg ierrrdedls
      121 satlvkadvl qrsgetgvvq glagktsgin itrnsgdpgs gayiqirgqn tilgdaspli
      181 ildgvpisns nigggtggvv qqsrlndinp qdiesitvlk gasaaavygt gaangvlvin
      241 tkrgrtggkr ftvnagisyg ldevnreyek qgvfgqgspf ttenfeqfgs yvpntglswg
      301 driadrsgtd vvnenggfft gdqtgtvyyp itekgdrtvy ndvnrdqifq tgstldmnvg
      361 infrgdnsnt yvsfsnlqqe gllrgnsdyd rttirinqdf nltdkvsirv nssysgvesn
      421 riqtgsnlag lylgylrtsp dfdntdysgv ytdadgiarn ghrgyrnylg tgipaynnpg
      481 wtinrqlnps evdrflvape inynilpnlk ltarygldyy tderrtvfpv lsagdygqgg
      541 lfrdeitekt qniflilngn teisdafald ytvgynyydn dyqrlsgsat nllvpsdkfv
      601 ienaiasnng stqalsrnrk ngvfgvlnft ivenllvels graertaslp delffypsas
      661 lgykllddda ktvsfaklra sygevgiepp lyrnlstfvs tspgsggwgd vldglnyggt
      721 yarsavqgnp nltneivkef evggdfrffq nrlslgltyy dritedallq vetppssgft
      781 srfaniaeit ntgfeldfsy niindgearw rlfgnashne nivtklpdvs rlilngftst
      841 ssalvegapf galyggmylr dedgdfalne ngfptndvvq gvigdpnpdw rgglgsevty
      901 kgialsvlfe taqgqdmwng tkgvmqyfgi dpitanista psdiknaaga tipagtefrg
      961 nvidfgagpv aadaswylgn gggfgsideq yiedaswtrl revtlsynlp vtllagvgls
     1021 nvsvgitgrn lllwtpfega dpdtnltgas rgrglayfnn pgsrsvlfnl kfgf
//
LOCUS       WP_104420035             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104420035
VERSION     WP_104420035.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107227
     Region          27..953
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqpinrlcwl llpalflpcl aygqypvtgt vtdnegeplv gvtvlivgtt tgtvtdfdgs
       61 faidipeepa elrlsytgfa sqvievsrgi apleiilmpd vanleqvvvt glastikrtn
      121 sanavsvvsg eeltgvttqq tvdgalygkl tgvnitqtsg apgggyavrl rgvsslsgnn
      181 qplfivdgvy isnvelpngs rsasgangan eesssnriad inpddiesie vlkgasaaai
      241 ygtranagvv iittkkgvsg etrvtfnqdl gfntiirkvg rrsftpeqve aefggdepde
      301 iaagraeral yeaavargel fdyedilyge kgfitdsrlr vsggnertnf fvssgwrdea
      361 giikntgyer fsarlnlthr isdrlkiqsn tyyvrsqanr sfsgnenegg lsygytlayt
      421 rdwvnlfpde egnypdnpnf agnplqtrdq trneenvnrv leginvnynv lqtnnhslnl
      481 ifnggldfil sktfvyvpet fqsqrnrqng flaegkndlf nynysaiavh dyytesginf
      541 tsqagityln qsadqllsqt tqliplqtnl argsaqeidq fllnveefgy vlqeevnvnd
      601 rliatagvrf dksslngdpn kfyafprasv alnlhefdfw npsnpiqqvk lraaygqtgn
      661 sasfgrlftt ltnnsiggra gftvdgqqgd gdlvpetsse iefgtdlgfl dnkvnvtaty
      721 yirdvkdlly dravptssgf sneirndldl rnrgfefqlg llpvntanfs yrttlnfwln
      781 rseitrlgve dgtegedips fvpsgvafgl glgtfyineg spitglwenv ggvptqtgnt
      841 epdfqfgwnn nltlfqdldv nflfhwrqgs ellnltrllt ddgrttprey dnlegyiedg
      901 syfrlreagi tyrlplesdv frgirigvsg rniftltdys sydpeasvkg gsglstniev
      961 apfpsakqfy fhlgfdf
//
LOCUS       WP_104421400            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104421400
VERSION     WP_104421400.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111922
     Region          31..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhpiapgrp lrqlallvlf laaaglsaqv tvtgrvteaa ggealigvsv veqgtangtv
       61 tdidgnfrlt vsepeatlvt tyvgyepqev alagrsqlei tlregvnlde vvvtalglkr
      121 ekkalgyave evsgddidav rpvnmlsgls gkvagltvtn asngltsssr vvirgensln
      181 inangplivv dgipinneiy gvgggstsqs dlpsdygnga aeinpadias vsvlkgaaas
      241 alygsraang vllittksge rqeglginfs snttwssplv lpdqqtqygg gwglayasdf
      301 gtnfgpafde glqieqdgsp lpgaqpfvqr yniadffqtg ftttnqlais ggsdrgnfrl
      361 sygnsqsegi vpntdldrnt islnteyrpa dwltidlsgn yiksesgnvp vsgygsqglm
      421 yvllwnynna dmdwyrdywa eggedreqty iftwadnpyl iayenlngfe kdrlfgrisa
      481 taqitpdlsl llrggtdyfd dlrtsrrpvg aqryangmyr eqnvnfretn ldflltytkr
      541 fgefsavvsg ggnrrdeeyr enfiegrgla vpgiynlqni nvnpttrril lpkrvnslya
      601 fanlgyrdfl yldvtarndw ssalpeanns yfypsaslsf lpseifdlgd avdylklran
      661 iaqvgndtra fsliktyefa tlpnsvssps elpnanlkpe rtnsvevglt telferrlrf
      721 dftyynsltk dqiiragisp asgfnstvvn ageietngve valgvspfrn pegfswdlna
      781 nftrsrsvvn alapgietfi vangpdgttv earvggrmgd iygqvfnrte dgriiygsng
      841 lpevstdrrt ignynpdftv glstdlsyrg vfahalldir sggriysytn aigaetgllq
      901 hslpgrtegi vgdgvtrddd gnfvenatvv apetwyyggy yrrdnveans fdasfaklre
      961 vtlgyrlpqr wlegigvana siafvgqnva lwtdvpnidp eafalnggtl vpgfevtqlp
     1021 stksfgfrln lgf
//
LOCUS       WP_104421640            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104421640
VERSION     WP_104421640.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117637
     Region          25..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrfrawita gnlllpvfll sqvpisgtvt svdgpltgat vyeadhpgkg tvtdsigtft
       61 lliqdfpsil kinylgytsr sfpidattpl pldvhleagi tlddvevvvt algvrrsnst
      121 lgysvqevqs eeltdvqavn fvdnlsgqva glrvtagatg vgsssqvvir getsftnnnp
      181 lfvvdgipin nntiinrtne eaagfqevdf gngamdvnpa dvqsvsvlkg asaaalygtr
      241 aangvivitt krggkqpglg isfnssltld rpfqlprfqn efgqgqggef afvdglgggi
      301 sdnitysygp rldvgnqvpq fdspvtladg tvvrggdvav hgglpipstp fvsqpdnvrd
      361 fydsgttaih nlaisgggad gdfrlsvtdl rsdsyipgvn lkrktlagrf gfrpaerlhl
      421 daslnyintt sdnrpaggyg seninydlta wlgrqtdlei lrdywqpgle gtqqysynyt
      481 ffdnpyftll enrngldrdr lfgflsarye lldnlslqvr sgmdysnerr rflrnfssnr
      541 fpqggyaend vlfreintdf lldytqsfgd ftlnllaggn rltqlaennq snaltlaqpg
      601 ifrlsnaasp vvivdqaaek rinslyglar fgfrdylfld ltgrndwssa lanpasadnt
      661 sffypsasvs flasrlldlp eavsylqlra nvaqvgndtd pfrtsstfva rspyngqptf
      721 teqsvlaqpn lkpeqtttte lgadirlley rlgldftyft qrtenqilsl piaqssgynq
      781 qivnggtvss rgveailslt lvvtedfrwt srfnfsssra vvdelpagtd rftlaysrvy
      841 nsvnqtvyfi vepggeigdi wgtgyrktdd grfiltnqgq fiadntlrki gnanpdfilg
      901 aansfrfrnl elnllldwrq ggqivsrsls lagvagqlee tayrpeagiv vpgvvntgtd
      961 sepvyvdntt aisaesyyrs yydrnheenn lydasylklr elrltyrldr saladgplgg
     1021 fqgvsvslig rnlyawseip hfdpeqfaiq gqgivfgved mtypsarsfg lslgldf
//
LOCUS       WP_104421747            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104421747
VERSION     WP_104421747.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116341
     Region          24..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqrfslvlal viglagfala qesitgtitd asgepligas vlvagtttgt vsdfngyftl
       61 nvpegaeeli vsytgyatqn vplttddnyd ivlaegvqln dvvvtalgis reekslgyav
      121 sqidgaevnq aqetnlvsal ngrvagaqin nnnsglggss siilrgatsl tgtnqplfvv
      181 dgtpidnstf ggrnasearg gqdygnmaqd inpndiesis ilkggaaaal ygsrasngvi
      241 littksgkar rglgvtinsg iqfstvavlp dyqdeygggr rgnflpfefk egeypesyre
      301 fdgqliadya ydgswgpald gtlvrhwdsw fpgetfgelr pwvasensvr dfydtgvqyn
      361 nnvsiaggse tgnfrlsytn nsnngvypgs slnrntvnvs asqqlgskft asvnanyvnt
      421 agegrpgigy gnasatniqt nfnqwwqrql dldrlkdyqm pdgtprtwni rapndlrany
      481 wespywtinr dgnsddrdrv fgnlalrydi mpglslsgfa rtdyytfrtt qrvasgsnas
      541 ldyysevart arennfeall dysktfsdfs idgqlganlr qeqdqstggn tvdglnvpdy
      601 ytldasnsrp nlinyrsqke vqsvygrlgi gwrsmlyvdv tgrndwssal esgnnsyfyp
      661 svsgsfvfse liansdivsf gkirggfatv gndtdpyntr ntigsvgpfg afpgfaiptq
      721 qrnfdlrses ittwetglem rflndragfd ltyydiqsed lifdvsvsst tgfastfvna
      781 gllenkgiel rvygtpvqte nftwnvginy arnrnkvvel idgldqlsig stwyvnflae
      841 kgqpygqlng ggflrdstsg siildeeglp trvtnqnfgs aypdftggis nsftiygfni
      901 ntlvdfrkgg qiysvsnmwg nysgmfentv gvnalgapir dpaydedgnr lsggiliegv
      961 nedgtpnety vdvrnyyest fqiseqfvyd asfvklrevs isrplpaawf annfistatl
     1021 sltarnlail yknapnidpd aalsngniqg yengqnpsvr sygvnlnvsf
//
LOCUS       WP_104421816            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Neolewinella
            xylanilytica].
ACCESSION   WP_104421816
VERSION     WP_104421816.1
KEYWORDS    RefSeq.
SOURCE      Neolewinella xylanilytica
  ORGANISM  Neolewinella xylanilytica
            Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
            Lewinellaceae; Neolewinella.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Neolewinella xylanilytica"
                     /db_xref="taxon:1514080"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114456
     Region          33..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklrleflc hclllalslw astagaqaap tgvvtgtvld aetgdpligv tvqvqgtttg
       61 tvtdldgyye isanaddeli fsytgmetmv ipvgaqttvd vqmgassial dqvivtaygt
      121 skrgsftgsa tqinaealen raitnvtsal egaagiqysp gsgqpgatsp irvrgfgsvn
      181 asasplyvvd giifsgslns inpndieslt vlkdasstal ygskaangvv littksgkag
      241 qtrfnvnlsq gfsgraipey drvgpgqyye lqweayrnsl vygsglsmee anreasreiv
      301 dllgtnpynv adslvvgpdg qlnpnaqliy gddldwqdal trlgnrtqad isyqggtent
      361 tyftslgyid dtgwilasdf srlsgranvt ttprdwirtg fnanissstt nqaadggsts
      421 fvnpffstrn iapiyplyeh dpvtgefvld enggrifnlg ddrvgntngr nvvqetilni
      481 dqdrintiga rafvdlyfln dftftfnaal drrafnnegy gnrivgdaap ngrafrtntv
      541 tssitynqll nydhafgshn vsflaghesf eyeynylyay svgqiasgnt elrnfttisd
      601 adsyterytt egwlaraeyd fddryfvsas fradgssrfs esirwgnfys lglawrldee
      661 afvanlpwvd llkvrasyge vgndsnldtd pvsfyasqpl ftlgfnndte agiilgslga
      721 ptlewetnaq tdlavefglw dyrisgsvey ynrvtdnlif svplplstgs ddylanigsm
      781 ynrgveials asiintpnfn ftldfngsti knqftelpqe eiitgskklv vggslydywl
      841 rdfygvdped gaalyaldpa vnapesdiri lngdslttna nyaeyafvgt avpdffgsft
      901 pkfrignlrf gllftyqigg qtydtnhanl lengnygssl stdildrwqe pgditnvprl
      961 dagqannfga asdrflvssd fialrqanis yeipdglter igltnlrvya naenlwlnta
     1021 rtgmdvnqnf ngttanrftp srtitfgvnt sf
//
LOCUS       WP_104423351             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacter tundripaludum].
ACCESSION   WP_104423351
VERSION     WP_104423351.1
KEYWORDS    RefSeq.
SOURCE      Methylobacter tundripaludum
  ORGANISM  Methylobacter tundripaludum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylobacter.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Methylobacter tundripaludum"
                     /db_xref="taxon:173365"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54850
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeih pgekrvattp eaaeqiiklg fsvlvesgag vsanisdeay kevgveivdd
       61 aktlwksadi vmkvrapeqh pelaldeidl lpeggrlisf iwpaqndalm qklaaknatv
      121 lamdsvprms raqkldalss maniagyrav ieaaqhfgrf ftgqitaagk ippakvlvig
      181 agvaglaaig takgmgaivr afdtrpevke qiesmdaefl lldfkeegag tggyaktmsk
      241 efieaemalf arqamevdii vttalipgkp apklitegmv esmkpgsiiv dlaaeqggnc
      301 altekdqvvv khgvtiigys nlpsrlanqs sqlyatnlrh lltelcpekn gtinvnmede
      361 virgttvike gkitwppppp klsaspapqt eapacaevqe pkkpsvikqf iplviaglal
      421 fgigavapas fmthftvfvl acfigyqviw nvtaslhtpl msvtnaisgi ivigalvqvs
      481 sptlnisila gsailiasin iaggflvtrr mlemfrk
//
LOCUS       WP_104425270             168 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: aromatic/alkene monooxygenase hydroxylase subunit
            gamma [Methylobacter].
ACCESSION   WP_104425270
VERSION     WP_104425270.1
KEYWORDS    RefSeq.
SOURCE      Methylobacter
  ORGANISM  Methylobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Rosenzweig,A.C., Frederick,C.A., Lippard,S.J. and Nordlund,P.
  TITLE     Crystal structure of a bacterial non-haem iron hydroxylase that
            catalyses the biological oxidation of methane
  JOURNAL   Nature 366 (6455), 537-543 (1993)
   PUBMED   8255292
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Cardy,D.L., Laidler,V., Salmond,G.P. and Murrell,J.C.
  TITLE     Molecular analysis of the methane monooxygenase (MMO) gene cluster
            of Methylosinus trichosporium OB3b
  JOURNAL   Mol Microbiol 5 (2), 335-342 (1991)
   PUBMED   1904125
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Fox,B.G., Liu,Y., Dege,J.E. and Lipscomb,J.D.
  TITLE     Complex formation between the protein components of methane
            monooxygenase from Methylosinus trichosporium OB3b. Identification
            of sites of component interaction
  JOURNAL   J Biol Chem 266 (1), 540-550 (1991)
   PUBMED   1845980
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Stainthorpe,A.C., Murrell,J.C., Salmond,G.P., Dalton,H. and Lees,V.
  TITLE     Molecular analysis of methane monooxygenase from Methylococcus
            capsulatus (Bath)
  JOURNAL   Arch Microbiol 152 (2), 154-159 (1989)
   PUBMED   2505721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF045805.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Methylobacter"
                     /db_xref="taxon:429"
     gene            1..168
                     /gene="mmoZ"
     Protein         1..168
                     /product="aromatic/alkene monooxygenase hydroxylase
                     subunit gamma"
                     /EC_number="1.14.13.25"
                     /GO_function="GO:0015049 - methane monooxygenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=19362
     Region          6..166
                     /region_name="MeMO_Hyd_G"
                     /note="Methane monooxygenase, hydrolase gamma chain;
                     pfam02964"
                     /db_xref="CDD:427082"
ORIGIN      
        1 manykihdnp vrdewmqkid glrtlaqgaa flvdfrkkyt tplradysle ldwgwvevki
       61 eekvamlkhh efndqqflnn ntcgtnaqkv adavvakmaa ctdkyeaekl hidfriknkp
      121 pimpvnvfmd tdrilgtklm elrntdyyal sleqlrkerg vkvialqs
//
LOCUS       WP_104425735             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter sp. ACNIH1].
ACCESSION   WP_104425735
VERSION     WP_104425735.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. ACNIH1
  ORGANISM  Acinetobacter sp. ACNIH1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter sp. ACNIH1"
                     /db_xref="taxon:1636603"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39744
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaetv igenrvaatp etvkklisag hsvviergag vkaayidsay eqvgakitdd
       61 aytgsqivlk vrapkgeeiq klsanttvva mfdpyrntel dqfaaqnvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmspeeq aradeaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr liraetvakm kpgsvildma vesggnvegs
      301 kcgetvvten gvkilgvpni pstvsteasa lyarnvynfv etlfdadknf vlnqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_104434393             529 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Kineococcus xinjiangensis].
ACCESSION   WP_104434393
VERSION     WP_104434393.1
KEYWORDS    RefSeq.
SOURCE      Kineococcus xinjiangensis
  ORGANISM  Kineococcus xinjiangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kineosporiales;
            Kineosporiaceae; Kineococcus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Kineococcus xinjiangensis"
                     /db_xref="taxon:512762"
     Protein         1..529
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53941
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpresg pretrvaatp attrqltglg yevlveagag vrssapdday aaagarigsa
       61 adawgadvvl hvgkpspaei gmlregavli atlapafdpq lveelatrpi talavdavpr
      121 israqsldvl ssmaniagyr avieaahtfg rfftgqvtaa gkvppakvlv cgagvaglaa
      181 igtasslgai vratdvrpev aeqvrsvgge yvavpaaeqq lstdgyarem sedynrraaa
      241 myaeqardvd iivttalipg rpaprlitae mvagmrpgsv vvdmaaaqgg nvagsvpdel
      301 vvtpngvtii gytdlpgrlp aqasqlygtn lvnllklltp gkdgrlvldl ddvvqramtv
      361 vrdgrvlwpp ppvqvsaapa paaavpapap ppppepapar rqafavlgaa alftltalsp
      421 aqlagnltvf alavvvgfyv ighvhhalht plmsvtnais giivvgallq lghgsaaata
      481 lalvavllas invfggfavt rrmlamfttt gppatprppa tarpernar
//
LOCUS       WP_104429530             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacter tundripaludum].
ACCESSION   WP_104429530
VERSION     WP_104429530.1
KEYWORDS    RefSeq.
SOURCE      Methylobacter tundripaludum
  ORGANISM  Methylobacter tundripaludum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylobacter.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Methylobacter tundripaludum"
                     /db_xref="taxon:173365"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55127
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeih pgekrvattp eaaeqiiklg fsvlvesgag laanisdeay kevgveivdn
       61 aktlwksadi vmkvrapeqh pelaldeidm lseggrlisf iwpaqneevm qklaaknatv
      121 lamdsvprms raqkldalss maniagyrav ieaaqhfgrf ftgqitaagk ippakvlvig
      181 agvaglaaig taksmgaivr afdtrpevke qiesmdaefl mldfkeegsg tggyaktmsk
      241 efieaemalf arqamevdii ittalipgkp apklitegmv ksmkpgsiiv dlaaeqggnc
      301 altekdqvvv khdvtiigys nlpsrlanqs sqlyatnlrh lltelcpekn gtinvnmdde
      361 virgttvike gkitwppppp klsaapapqt eapaysaaqe qqkpsvikqf tplviaglvl
      421 fgigsvapas fmthftvfvl acfigyqviw nvsaslhtpl msvtnaisgi ivigalvqvs
      481 aqdqnisila glailiasin iaggflvtrr mlemfrk
//
LOCUS       WP_104453292             481 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Aeromonas].
ACCESSION   WP_104453292
VERSION     WP_104453292.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53295
     Region          27..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsydklf rpglaalllt allgagslaq aadeaqskgk iearselfak dhtdqftswk
       61 gtsesrertd alaedpqmvv lwagypfskd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meeyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg vvkqrkdavt eiklkvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakgish eiaipdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_104468189             309 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Enterobacteriaceae].
ACCESSION   WP_104468189
VERSION     WP_104468189.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35416
     Region          5..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maihdlfskr qkrlrgevpd vyqytelpys frvqvihiit etigdsyrag seseqiyeai
       61 snalcreygv fsltrssrgh fesirdffln eqnyercldv ielsfkcing yvkenywrfh
      121 gqyqksdaai eelnvrfkea gigyqfesge lvrvdsqfih sdavkpalqi lgsskefaga
      181 ndeflsaheh yrhqrfkecl ndclksfesl mkaihkkrsw eygstdtakk lissclsngl
      241 ipdymqnqfs slrillesgv ptirnkeggh gqgdevtnvp ehlasytlhl tasnllflak
      301 cdenftkkk
//
LOCUS       WP_104470085             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter indicus].
ACCESSION   WP_104470085
VERSION     WP_104470085.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter indicus
  ORGANISM  Acinetobacter indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter indicus"
                     /db_xref="taxon:756892"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39804
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklinag hsvviergag lkaayidsay ehvgakitdd
       61 aytgsqiilk vrapkgeeiq klapnstvva mfdpyrntel dqfaaqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmseeeq qkaadaakng ygwmpgeqyi
      241 kdqaiivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 qcgetvvten gvkilgvpni pstvsteasa lyarnvlnfv etlfdseknf visqddeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_104473598             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter indicus].
ACCESSION   WP_104473598
VERSION     WP_104473598.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter indicus
  ORGANISM  Acinetobacter indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter indicus"
                     /db_xref="taxon:756892"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39760
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklinag hsvviergag lkaayidsay ehvgakitdd
       61 aytgsqiilk vrapkgeeiq klapnstvva mfdpyrntel dqfaaqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmseeeq qkaadaakng ygwmpgeqyi
      241 kdqaiivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 qcgetvvten gvkilgipni pstvsteasa lyarnvlnfv etlfdgeknf aisqddeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_104475952             400 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microterricola pindariensis].
ACCESSION   WP_104475952
VERSION     WP_104475952.1
KEYWORDS    RefSeq.
SOURCE      Microterricola pindariensis
  ORGANISM  Microterricola pindariensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microterricola.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Microterricola pindariensis"
                     /db_xref="taxon:478010"
     Protein         1..400
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40093
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvgiarerr dgerrvaatp dtvrqltrlg ldvliesgag vaaghsdqsy adagatvvpa
       61 lelaeldvfa hvrpltpetv gllrrgavti glaspaselp tvralagagi tafalelvpr
      121 israqsmdal tsqaliagyr cvleaatrlp rffplymtaa gtippasvlv lgagvaglqa
      181 igtakrlgar vsandvrpas adevasmgak finldletae asggyakelg edkaarqral
      241 laphvaaadv littaaipgr papllvtram vqamkpgsvv vdlaaesggn vegavagadv
      301 lvptadgsge vtivgmkdaa samasdasrl yaknvanlle lmtadgvvap dfgdevvaga
      361 cltadgvvrh aptaealglp paaaadasap daqateggva
//
LOCUS       WP_104478685             361 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinokineospora auranticolor].
ACCESSION   WP_104478685
VERSION     WP_104478685.1
KEYWORDS    RefSeq.
SOURCE      Actinokineospora auranticolor
  ORGANISM  Actinokineospora auranticolor
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Actinokineospora.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Actinokineospora auranticolor"
                     /db_xref="taxon:155976"
     Protein         1..361
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37003
     Region          6..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(19,74,93,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtantvvgvp kesaagerrv alvpkvverl rarnlsvvve pgaglaalip ddayvhsgat
       61 lgdpwaadvv vkvappnete vgalragsvl igflapltdp gkakalrerg vtafamesip
      121 risraqsmda lssqanvagy raamlaaehl trffpmltta agtvppakvl vlgvgvaglq
      181 alatarrlga httgydvrpe vadqvrsvga qwldlgieaa gsggyaralt daereeqqrq
      241 lgkaitgfda vittaqvpgr taptlvtaea vegmragsvv vdlagesggn celtepgeiv
      301 vahsvtvasp lnlpatmpeh aselyarnvq allellvdad galsvdftde vvagacvtke
      361 a
//
LOCUS       WP_104484473             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter indicus].
ACCESSION   WP_104484473
VERSION     WP_104484473.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter indicus
  ORGANISM  Acinetobacter indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter indicus"
                     /db_xref="taxon:756892"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39848
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklinag hsvviergag lkaayidsay ehvgakitdd
       61 aytgsqiilk vrapkgeeiq klapnstvva mfdpyrntel dqfaaqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmseeeq qkaadaakng ygwmpgeqyi
      241 kdqaiivdka vsnadivitt allpgrdapr liktetvakm kpgsvildma vetggnvegs
      301 qcgetvvten gvkilgipni pstvsteasa lyarnvlnfv etlfdseknf visqddeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_104488225             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oceanisphaera arctica].
ACCESSION   WP_104488225
VERSION     WP_104488225.1
KEYWORDS    RefSeq.
SOURCE      Oceanisphaera arctica
  ORGANISM  Oceanisphaera arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Oceanisphaera.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Oceanisphaera arctica"
                     /db_xref="taxon:641510"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53639
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipretl sgetrvaatp ksveqlrklg fevsieqgag skasfddaay eaagatlvaa
       61 eqiwqaamiy kvnaptadei erlqagttlv sfiwpaqnpe lveqlknkgv tvmamdmvpr
      121 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvlv igagvaglaa
      181 igaagslgai vrafdtrpev keqinsmgge fleldyeeda dssdgyakem skafidaema
      241 lfmaqakevd iiittalipg kpapklitae mvanmhpgsv ivdlaaqngg nceltkpgel
      301 fvsdngvkii gytdlngrlp tqsstlystn lvnlakllck ekdgnikvdf ddvvlrnmtv
      361 vkdgevtfpp paisvsaapk aaaqaqpkae phakqpsnlk yylggvgvll fawlsavapa
      421 eflshftvfv lacivgyyvi wnvshslhtp lmsvtnaisg iivvgalsqv gaggfvtfla
      481 fvavliasin vfggftvthr mlkmfrkg
//
LOCUS       WP_104491143             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            denitrificans].
ACCESSION   WP_104491143
VERSION     WP_104491143.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus denitrificans
  ORGANISM  Paracoccus denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus denitrificans"
                     /db_xref="taxon:266"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55802
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkesf egearvavtp ssaahlrklg hevyvevgag vragfsdtay eaagvtvepn
       61 aaaligdvdv vvkvrppneg elrqmrrgqv lishfwpaqn pdllelareq gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaavslg aqvyafdvrp evaeqiesmg aefvyldfqd qvqdgaatgg yaapsspefr
      241 ekqlekfrel apemdivitt alipgrdapk lwtadmveam ktgsvivdla aerggncdlt
      301 vpderivten gvviigytdf psrmgaqase lygnnirhml sdltpgkdgv ivqnmeddvi
      361 rgstvafdgd vtwpppppri aaiaaakpke kpreltpeer rdkeiaefra qtrsqvtllg
      421 vgavlmllvg lfapasflsh fivfvlavfv gfqviwnvsh slhtplmait naissiiivg
      481 allqigsggw lvvllaalsv lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_104495460             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter indicus].
ACCESSION   WP_104495460
VERSION     WP_104495460.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter indicus
  ORGANISM  Acinetobacter indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter indicus"
                     /db_xref="taxon:756892"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39790
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklinag hsvviergag lkaayidsay ehvgakitdd
       61 aytgsqiilk vrapkgeeiq klapnstvva mfdpyrntel dqfaaqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmseeeq qkaadaakng ygwmpgeqyi
      241 kdqaiivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 qcgetvvten gvkilgipni pstvsteasa lyarnvlnfv etlfdseknf aisqddeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_104503608             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter indicus].
ACCESSION   WP_104503608
VERSION     WP_104503608.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter indicus
  ORGANISM  Acinetobacter indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter indicus"
                     /db_xref="taxon:756892"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39770
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklinag hsvviergag lkaayidsay ehvgakitdd
       61 aytgsqiilk vrapkgeeiq klapnstvva mfdpyrntel dqfaaqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mlpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmseeeq qkaadaakng ygwmpgeqyi
      241 kdqaiivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 qcgetvvten gvkilgipni pstvsteasa lyarnvlnfv etlfdseknf aisqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_104508152             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodoblastus sphagnicola].
ACCESSION   WP_104508152
VERSION     WP_104508152.1
KEYWORDS    RefSeq.
SOURCE      Rhodoblastus sphagnicola
  ORGANISM  Rhodoblastus sphagnicola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhodoblastaceae; Rhodoblastus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rhodoblastus sphagnicola"
                     /db_xref="taxon:333368"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39146
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaetr alegrvaatp dtvkkyvsfg aevvvqkgag akagitdadf ekagakivgd
       61 asatvagadv vltvrrpepq alvgvapdal vlsimepygq erllkalaga gvrafamelm
      121 pritraqsmd vlssqanlag yrsviegane fhrvlpmmmt aagtvpaakv fimgvgvagl
      181 qaiatakrlg avvtatdvrp atkeqveslg gkflavedde fkqaqtaggy akemskeyqa
      241 kqaeltashi akqdivitta lipgrpaprl itadmvasmr pgsvivdiaa erggnceltk
      301 pgeivvsang vrvvgslnia salsatasql yaknllafle tmidkekkai vvneedelik
      361 atlltrggav ihpnfag
//
LOCUS       WP_104513883             960 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Nonlabens
            xylanidelens].
ACCESSION   WP_104513883
VERSION     WP_104513883.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens xylanidelens
  ORGANISM  Nonlabens xylanidelens
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 960)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 960)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 960)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..960
                     /organism="Nonlabens xylanidelens"
                     /db_xref="taxon:191564"
     Protein         1..960
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103902
     Region          23..959
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqklqtvll lillpffafa qsvitgtvle snglpalgat vsvkgtsngt stdfdgkytl
       61 nnvpsdaviv fsfigymtqe iplngqtsin itlaenpsel dtivligygs tkkanvtaaq
      121 ttvkaeefnk gaitspgqli sgkvagvqvt aasgrpgdgp virvrpgstl ggnqdalyvv
      181 dgvpldqrna slntinpadi esftilkdas ataiygnras ngvvlittkk aklnsdlkig
      241 ydvqfavnqv qdyahvlnad efrqlvvdqg rdpavlgdan tdwqneiyqn gtraihnltv
      301 ekgyeatsir aslgytneng tllrsgyera tlglnvrqnf lkgdlklnft sqlaqeelrr
      361 adegavgaav vfdptqsifn ntgefggffe ytnstgpegn aprnplglln sldsqldnkq
      421 arlnlnaayn irqvpglkft gnagidynef deytirdfns gagargnnrs fgegfrrnql
      481 ldgrfeykrt lesldtdmdl tlggsfqdft rqstshstvn nelqenpiai ddsalvtafa
      541 rasfdikdlv vlsasasrng ssrfskenrw anfygasaai kltntdfvqn sgflsqlklr
      601 ggfgqtgqqd idasfaylsv ftpgqpqaav qfgdqfvtti rpegsidlkw ettdqwnagi
      661 digffddrit gsvdgfyret kdlllfgplp agglengsfq nagstlsrgi etsisgkiiq
      721 tenmnwtlsa natvqeieit dlagadnapv pvggisggtg ntiqewavgs dptsfhvfrq
      781 vydqdgnpld gvyvdtngdn iindadrvry kkanhdvyfg ltsnfnyknl dfsftfrgaa
      841 ggynynnvds nsasygsifp tntqtpiyvn stvdilntnf sqqrlqsdyy iqkadfikld
      901 nvslgynfpg envdirasit gtnlltitdy dgtdpevfgg idnnlfprnr glifglgfkf
//
LOCUS       WP_104520479             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodopila
            globiformis].
ACCESSION   WP_104520479
VERSION     WP_104520479.1
KEYWORDS    RefSeq.
SOURCE      Rhodopila globiformis
  ORGANISM  Rhodopila globiformis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Rhodopila.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Rhodopila globiformis"
                     /db_xref="taxon:1071"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39099
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavlkerr aaetrvaatp dtvkklialg ltvaveagag asasmsdaef aaagaeiapd
       61 akavlaganv vfavqmpeae qraliprgal lvcvagafgd kdlvpslaaa gidvaamell
      121 pritraqsmd vlssqanlag yravvesata fqrgfpmmmt aagtvpparl fvigagvagl
      181 qaiatarrlg aivsatdvrp aakeeikslg asfvgvedee takqtgayar emtdafrqkq
      241 aelmattvak ndivictalv mgrkapvivt kamvesmkag svivdlasda ggncestvpg
      301 qcittpngvt ilgfnnwpgr isvassslya rnlltflttf wdkeqkapkl petddivkgv
      361 mltrggsvvh pnflpsqaa
//
LOCUS       WP_104515667            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Nonlabens
            xylanidelens].
ACCESSION   WP_104515667
VERSION     WP_104515667.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens xylanidelens
  ORGANISM  Nonlabens xylanidelens
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Nonlabens xylanidelens"
                     /db_xref="taxon:191564"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112193
     Region          24..1017
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklngilt lllalvvqva faqqtvtgkv tdadggllga vvsvkggsan attdfdgnyt
       61 ilagpedtlv ftysgyetvs ilvgnqtvin ttlqasldtv vligyrnstk prsniasttv
      121 dskdivdrpn asviqrlqgq vagltvqtns gqpgansliq lrgissingn teplilvdgv
      181 pvdedafatf npndvenmti lkdaaataiy gnrgangvil ittkrgeyds plsisysgtt
      241 sftefidtdy nlyssrglla lenrrgagfg ntlteaeiaa ydiqtdwndv ffrtgvnqsh
      301 nlslssggkn srqftsinyt kqegtllatd lqrfnvrtnv sgksdnerft ynttaslgys
      361 qsnsqtetgn nrntlfffss ilganrglpy vdineytpdf ltginaftar napfvtfdni
      421 qfnsnrddel klivggdfay klnddftlay nigadygqtt glrvidpnsa larvrasfis
      481 ptavegaqte sflrdfrfns nlslrfkrsy gdkdqhtvia ngyveyvkgh ykdflyqqtg
      541 lnprtfspgn nggafigdta addnnvpfvt snkastglfs yfgefdydyd dkygfqatir
      601 rdassrftad nawgtfysva grwnlhkedf laevdwlntl klrasygttg ndrineadgl
      661 ggyygalnst rtlfatgqsy ndqqtfvrnq ignedlrwet iktvnigidf emfdnrlrga
      721 idayqrkted lffarstsli sgisqldanl gdisntgiel tasydllran nkdevnlrvy
      781 gniaynrnea dfidlpdglq dnsasgtviq egqrlneyfv vpyvgvnpan gnllyeding
      841 nltesptldd rrltgtssvp dffggfgfna syknffietq fsymtglqrf dnnlfnylnp
      901 aeigqlqlss dldrawtpdn rvtdipslda dnispgvatd rflidsdflr lrflqvgynf
      961 dqeildrtfl ksariyasge nlatwtgwlg sdpesqrtve enrfptprii svgldlkf
//
LOCUS       WP_104530256             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus saxobsidens].
ACCESSION   WP_104530256
VERSION     WP_104530256.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus saxobsidens
  ORGANISM  Blastococcus saxobsidens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Blastococcus saxobsidens"
                     /db_xref="taxon:138336"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53866
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mhigvpretr gretrvaatp ttvrqlvglg ydvvvetgag aassfpdeay aeaggrvgta
       61 deawqadvvl rvnapapdel prlrdgatli gllspaldpg lvdalaqrpi talamdavpr
      121 israqsmdvl ssmaniagyr avveaahvfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvavpageqe vsadgyarem gedfnrraae
      241 myaeqardvd iiittalipg rpaprlitee mvasmrsgsv ivdmaaaqgg nvagsvpdei
      301 vvtangvsii gytdlpgrlp aqasqlygtn lvnllklltp gtdgrlvldl ddvvqrsitv
      361 vrggekmwpp ppvqvsaggg agagaaaapp eprepapppe ppkpgrrfal vglgaallfl
      421 ltafspnelv qhftvfalav vvgfyvigkv hhalhtplms vtnaisgiiv vgallqlgsd
      481 dgvvralafv atlvasinvf ggfavtrrml gmfsrgpnpk aaar
//
LOCUS       WP_104544984             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chroococcidiopsis sp. TS-821].
ACCESSION   WP_104544984
VERSION     WP_104544984.1
KEYWORDS    RefSeq.
SOURCE      Chroococcidiopsis sp. TS-821
  ORGANISM  Chroococcidiopsis sp. TS-821
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Chroococcidiopsidales; Chroococcidiopsidaceae; Chroococcidiopsis.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Chroococcidiopsis sp. TS-821"
                     /db_xref="taxon:1378066"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41117
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavakeie vgerrvalvp dtvtrllkkg ievwveagag essfftdady etagakiihd
       61 tdtlwreadi llkvgipker edgrleidll regavlvsfl nplgepaiaq rlaqkqital
      121 smemiprttr aqsmdalssq asiagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vqlnedtvad ggyakevsea
      241 akqrtqevva ehvkqsdvvi ttaqvpgkka pllvteemva qmkpgsvivd laaeqggnca
      301 ctepgkdvqr ngvtiigpin lpssmpvhas qlysknlfsl vqllikdgnl evnfaddiin
      361 aacithagei rnqrvkeala tlssatag
//
LOCUS       WP_104630630             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. MH60].
ACCESSION   WP_104630630
VERSION     WP_104630630.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. MH60
  ORGANISM  Streptomyces sp. MH60
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces sp. MH60"
                     /db_xref="taxon:1940758"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53496
     Region          13..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtghqpahhp pqrvgvvaes lpgetrvaat pstvrlllgl gyevvvepga gaasgfgdea
       61 yaeagaspge awaadvvlkv naptdeeiar lragttlval vapaqrpell ealaardvtv
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvrslggeyl avdvaqeest dgyaratsad
      241 ydraaarlyh eqardvdvvv ttalipgrpa prlvtaadva amrpgsvivd maaaqggnve
      301 gtvpgrsvvt dngvtvigyt dlaarlpaqa sqlfgtnlan llrlltpgkd grlvidfddv
      361 vqrtvtvvra gtvtwppppv tvsaappsta peaaspaapv gakpsgitpa grfgliglgm
      421 latfllvafa paqlaenftv falsvvigyy vigkvhhslh tplmsvtnai sgivvigalv
      481 qighegtlvt vlssvaillt svnifggfav trrmlsmfsr gesr
//
LOCUS       WP_104663944             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ensifer
            adhaerens].
ACCESSION   WP_104663944
VERSION     WP_104663944.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55187
     Region          1..527
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaprert asearvaltp dsavqlaklg ygsiietgag vaagfpdday raagvevaps
       61 aealwassdv ivkvrppqha eiahlsaekt lisffypgqn aelldlanak ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigvatslg aqtyafdvrp evaeqiesmg aefvyldfad geggaqqdga atggyaapss
      241 pefrekqlak frelapqidi vittalipgr dapklwladm vaamkpgsvv vdlaaerggn
      301 cdltvadqri vsdngiivig ytdfpsrmaa qastlyatni rhmltdltpg kdgklvhnme
      361 ddvirgatvt fagdityppp ppkvaaiaaq kpkekvkept peekraseaa tfkaqtknql
      421 allavgtall llvgafappa fmghfvvfvl acfvgfqviw nvshslhtpl mavtnavsgi
      481 vilgallqig sgnwlvvlla alsvliatin ivggflvtrr mlamfqks
//
LOCUS       WP_104664607             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ensifer
            adhaerens].
ACCESSION   WP_104664607
VERSION     WP_104664607.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39595
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfvake tdpnegrvaa spdtvkklka lgfdvivead agflsripda eyekagarig
       61 aiadaktadv vlkvrrptsa eiagyksgai viaimdpygn eaaiaemasa glsafamelm
      121 pritraqsmd vlssqanlag yqavidaace ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsreyqv
      241 kqaalvaehi akqdivitta lipgrpaprl vtremlknmk pgsiavdlav erggnvegae
      301 agkvaqvegv kvighlnvps riaasasgly aknlvtflet mvsketkala lnmedelvka
      361 talthggqvv hpnfgaskgd k
//
LOCUS       WP_104704513             527 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Roseibium
            album].
ACCESSION   WP_104704513
VERSION     WP_104704513.1
KEYWORDS    RefSeq.
SOURCE      Roseibium album
  ORGANISM  Roseibium album
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Roseibium.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Roseibium album"
                     /db_xref="taxon:311410"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56099
     Region          5..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msealkigtp keifpgearv amtpesakql qklgyscliq sgagkaagfs ddaykeagve
       61 ivktapslwk qsdivakvrq pedkelgylt kgktlisffn pggneagmea akekganvia
      121 memvprisra qkmdalssma niagyravie agnnfgrfft gqitaagkvp pakvlvvgag
      181 vaglaaigts tslgaityaf dvrpevaeqv esmgaefvyl dfeedqqdga atggyasvss
      241 pefreaqlak frelapdmdi vittalipnr papklwledm vqsmkpgsvi idlaaerggn
      301 vegtvadkki vtdngvtivg ytdfpsrmaa qsstlyatni rhmmtdltpe kdgqlvhnme
      361 ddvirgstvt hggeitfppp ppkvqaiaak pkekpkeltp eekraqevaa fkqqtkqqvt
      421 llavgglfml lvglvapasf lqhfivfvla vfvgfqviwn vshslhtplm avtnaissii
      481 ivgallqvgs gsfliillag lsifmagini fggflvtrrm lamfqks
//
LOCUS       WP_104709907            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104709907
VERSION     WP_104709907.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117070
     Region          24..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkillatvm llstlvmhay gqdrvvigkv tssddgspip gvnvtlkgtn rgistnange
       61 yklnvganat lvftsigfvr qevgvdnrte vnvvlqvtnd dlqevvvtal nigrekkain
      121 savqevkgan laiarnnnva dalagkvagv qvfsqsgakf gtpsirirgv nsltggdply
      181 vvdgtvtdvn fvnmddvesl nvlkgpaasa lygnrasagv vvittkkgkn qqglgidvnh
      241 sttfdnvsll pkyqneyggg ysqefgtfey npaihpaswa afngqktidy sadeswgprm
      301 dgslyrpwys wipsdpdfgk evpfspqpnn vrsffqtgat vntnvaisks selfnarvsy
      361 tnynvkgtip nsqqhrdyls gklgvnitpk ftanlnvnys tektrnrpsd gyggqnqtig
      421 sfnqwfqrql dmtqlrtyrn pdgtyrswni tgpenttply wdnpytqvyq nisneknerl
      481 fgdfgltykf tddlsvsvva rrdflnryfd srvasntknt ayygtsndsr rednyealls
      541 ynkkfgkftl nanaggnirk ntrdyvamnt ngglsipnyy nivnsatpgt ftnynarrev
      601 rsvygfvsfd yndllfieat arndwsstlp vnnnsyfyps vtaglifsef lqnkrilsyg
      661 kirgsfaqvg sdldpyqiyt vfntgvkygs nttqsiptql pnqslkpgls sgyeggidlk
      721 flnnriglef tvyrqdntnq ilplavpgss gyntalvnag nirsegmelh inavpvktkd
      781 ftwdfdinld rsrskvvela aglktydllq nslfngvprf ggtslgfiar agsdwgtivg
      841 rqfqryqavd gngnkidnpn ngkiivdang lplstagqdl atvlpkmkgg flstfnykgv
      901 tlrfnidwll ggkfysttrm fsagsglsae taglndkgnp krddpanggg vlfpnsvyad
      961 gsanttyada qtlyesrlfd lnenwifdkt yvklrevnlg ynlpvawirn tpfktayvaf
     1021 mvrnpfliys kvgggidpse tqtfwgeggq qipvrsvgfn vkfgl
//
LOCUS       WP_104709968            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104709968
VERSION     WP_104709968.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115775
     Region          23..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqlllkvllp vllwvqvqaa laqqvtgvvr stadqqplag vtvqikgttr gtvtnaegty
       61 tvtaqpgetl rfsfigykae elavpetgvl nvnlnneesa lqevvvtalg iakekkslgy
      121 svqelkstei sqaretnlvn alsgkiagvn itnsqgnmgs srivirgets iagnnqplfv
      181 vdgipvdnsq fgstgtnrdy pnaiadinpd nietisvlkg pnaaalygsr aangvilikt
      241 kggkgnkglg vtlnaahtfe nllvlpdyqn vygqgtgglf sykdgkgggl ndgtdeswgp
      301 kmdgrllpqf fskgeavpfv phpdnvknff ktghtnnigv siagsdakfd yrfsfnntrq
      361 tgvvpntdit knnfsvngty hlndrltint sanfirsesd nlsalggrgs svmlqflwfg
      421 rqvdtgllrd yrangendfn wnhsyysnpy lllyentnaq rrdrfignvn lnykindwls
      481 amvrtgndfy tdrrkskisy gtngtpfgsy aedayvvnen ntdfalnfnr klsddfdleg
      541 lvggnirsnf feqnyqqapr lavaglytln nsrdplvsnn vfkrrrvysa yasaqlgfrn
      601 yaflnltarn dwsstlppgs nsyfypsvna svvltdafni rtnwlsfaki rggwaevgnd
      661 tdpyqltnty pfnqpfgsnp lltvsdvlln rnlkpeitqs seiglelalf ksrvradfsy
      721 ynsdsynqil radvspttgy kqkllnaghi nnhgfeaqls gtpvqtsggf kwnvivnfsr
      781 niskvvsldd qgllnqyilg sngttqvlag vgqrygalyg safqrdasgn vvvgangfpl
      841 knanlqtlgy ytpkwiggit nafsykgwnl svlidtkqgg qiysatnatg rytgvlestl
      901 pgrdaehggl syyyagnnts stpvqvagpd akapngeriy sdgiifngvt adgqanktiv
      961 paeryykniy snsagvneas vfdasfiklr evrlsyalpq nlvkrlslqg vnisligrnl
     1021 aflqkkapni dpetafntgn gqgleslqlp ttrsygvnln isf
//
LOCUS       WP_104713137            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104713137
VERSION     WP_104713137.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112119
     Region          31..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkisflrfqa rfgrlfallw lmslsamaqn itgkvtnvtd gsplpgvtvv ekgstkgtvt
       61 daqgqytlna aaeatlifsy lgyvsqeipv ggrttvdvam kedtkslnev vvtalgiqrd
      121 kkalaysvte vkgseftqar ennvanalsg kiagvnatgl stgpggssri iirgngsltg
      181 anqplyving mpidnttpgg satanggqgn vdrgdgiggi npddiesmsv lkggtaaaly
      241 gsraangvil ittkkgraqk gigvdfnstf taesiavvpd wqyeygqgdg avkpttqaqg
      301 iawgrrswga kidgsdfvaa dglthpyvaq rnnlknfyqt gktftntlav nggnenvnyr
      361 fsvsdldakg ilptqtynrk tgnlslngkf gpkiaveala qytieannnk tgagdalgnp
      421 nwtpymignt sdirwlapgy dannneiawn dasiasnsyf vinkykqndt knrfigqfgl
      481 tynildnlfv kgtvsrdffn yqykyilptg tlyvpngeyn elktdvsetn amvtanyntk
      541 iastiglsal vganrrdyny nqiniagsny vlpyfysstn lrtitttpln qrvrtnsvfg
      601 sldldykgia fltmtgrqdw fstlspknns ifypsiggsf vlsqaialpr aidfakvras
      661 waqvggatpd pyainltysm vpssgqplqn vtstaitnag lkpltsttye vgvdlqflnr
      721 rvgldltyyn rsttddivqt sisetsgyns vymnvgkmsn kgvealvtys pirrknfgwd
      781 isynvaynds kvikladgit slqmatsvgn wayinsiegr sygtivgttr qrdangniiy
      841 dpttgyalks nlhelgkgvp pltmgltnef hyknfsfnfl vdgkfgnkif svlevyanrm
      901 gklkrtldgr engltvtgvt asgdsftkti akenlrtyyd ndknytelfl hdasfvklrq
      961 amvsynipvk nfkllklqsa sisfvsrnil tlykntdnfd peqsftnssn qgfesiglpr
     1021 trsyglnlll kf
//
LOCUS       WP_104714402            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104714402
VERSION     WP_104714402.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110309
     Region          30..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrksvlpgkl lfyllfawta lagsvsaqvq lqgkvsdasg sglpfitvkl ssastgtttn
       61 asgtyqftps lkpgrytlif sgvgyksqqk sfdvnasqna vtldatleed vlgldevvvt
      121 gtmgatskre lgnsiatvga kdlqfsaaps ldaalqgkls gaqitqnsgn paggisirmr
      181 gpstivgssd plyivdgviv nndsrqlidl ggysqnrlvd inpadidrie vikgaaaaai
      241 ygsranngvv qiftkkgkeg kpsitfstqf rvsqlrkkma yneypfafan ttptdetqvp
      301 vtrydyqdki fqnafgteny lslsggtant kyfvsgsnyy nqgiikstdf nrngirlriq
      361 qkignkatis agsnyvysss keipnggise aygaltgfif snnsvnpepd pvtgvypsta
      421 pvsvvrrtnp leainrfkfg qrtsriisdf nfnlkpiegl nidytvgidn ytqsatayip
      481 pknttptydq glarradatv fqinndlnvs yntkvndwlt stsgiggtiq ydrtltfgat
      541 aqqlgafget inngtiiate frsersilga faqqsfgikd ryfitgaarv dassvygidn
      601 rwqffpkvsg syvlsnekfw segalgrvvn sfklraawgq sgnltaigay drftnyspvi
      661 yggqtgytsp aqfgnftvkp erqteteiga dfsllndrvs vefsyfnksv adlilnrtla
      721 pttgfnnrli nvgsmtnkgf evmvkavpvq tsrfrwittl tytsnkntvn gvegngvlpf
      781 aggfsqvaav ngyplgayys tffarnpdgs llltaptatn pnrypqrerg tqlangqytv
      841 qrdangqptg tilskvigdp npwgivgftn efeigkfnfr mqwdgmlgfe vfnftrrvge
      901 rdlyaslkgy epelrgdvpk gtsaalfsif enyiedgsfv klreisasyv ltpklwkmqn
      961 lrltligrnl lsidnysgwd petnaagqdn avrgfdfvev piprsflfgv svnf
//
LOCUS       WP_104713859            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104713859
VERSION     WP_104713859.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112657
     Region          22..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrlsilll llsslwataq drqltgvits sedgqplpgv sisikgtakg attnadgayq
       61 lavssgntlv fsyvgftske vvlgdestln iqlqmnassl sevvvtalgi trekkalgys
      121 vqeiggkqlt qaretnlvna lsgkiagvqv tnsngapgas srmlirgans igsnnqplfv
      181 vdgvpidnsn ygsgtgvdyg ngagslnpdd iesmsvlkgp saaalygsrg angvvlitlk
      241 sgrgskgigv svnsnttfdt pfrqpewqne ygqgakglfk fvdgrgagvn dgvdeswgpr
      301 ldgrlieqfd spvvngvrta tpwvahpdnv nqffrtgkty tnnvsvtggs dkgdfrlslt
      361 dlnqsgilpf tnykrqtvsl nagwnltpkl niratgnyvk dgsdnrtnwg lyfiwfgrqv
      421 dmenlknyta pgsiyqnnwn ynywtnpyyq lanskrenek drlygnisat ykltdwlslm
      481 artgtdyyad rrktknaart snlfdgynee qifvresnsd fllnathkfg efdltanigg
      541 nhrknfyqrd ymsaaelaip rvwnmgnsrl rpvtensysq kvvnslyasa nigfrnylfi
      601 dltarndwss alpssnrsyf ypsaavsavl tdmfnvqssf lsfakirggi arvgndtdpy
      661 nlmqtyeyan awgslaslke sngllnpelk peltssyeig telkffqnri gldltyydkq
      721 sfnqilkvdv snatgfsskl lnagrlqnrg ieiqltgtav ktnsfkwdia lnwarnqnkv
      781 velaqgltty tlgtvrgmgi earvgqpygt ffgqgfqrap dgqivydqsg ypvinpvrrv
      841 lgnftpkwig glqntftykn lslttlidmk qggdifsqti nigrytgvlk ettvgretgi
      901 vgqgvvnvgt aanpeyvpnt knisseewhh kyylltnnee tifdgsyvkl revrltyvfp
      961 gkvfkrlpfr ditisavgrn lallhsniph idpetsyynd gnlqgiengq ipttrsvgfn
     1021 islnl
//
LOCUS       WP_104714432             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104714432
VERSION     WP_104714432.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108679
     Region          41..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlsylhvsgp rrrwsglwll lpallvsysl mavprlaavp itgkvisnsg dplpgvsile
       61 kgtnngtltd aegnykinvq gassvltyty igfvkqeitv gnqpvinvtl eesssslnev
      121 vvvgygtldk kevtsaithv sgkdlltvgv tnpisalqgk vsgltitntg ggdpnsmpsi
      181 qlrgvssrda glgplvvvng vpggvlenin qndiesidvl kggaasaiyg trgsngviii
      241 ttkkgsqgsr vdyngygafd faamplktls aseflaqnrg tdfgaqtdwl ksitrasafs
      301 hkhslsfsgg darnnyrata dyrdaqgldl rsgreeygar lmlnhtsann lytltlnvap
      361 ryfksnnady dsfdqaltln ptlpifdpqn ptrynriqsg fsspfnpver lrteqsgteg
      421 kildynasll vnilptlttq ltfgqftrdy fdfffrpsts tyaaqyqgsm nsasraynky
      481 dqrslewvgn yswtkgahdv kvlggysyqy fqssglsgen rqmpsdalty nnigtglyqq
      541 vegrngmgty kndsrliaff grinyalqdk ylfsaslrre gsskfgynhk wgnfpaasvg
      601 wrlsqeafmk pltwiddlkl radygvtgnq dfgnylsldt ysgygyypln gsqyqvwgps
      661 qntnydlrwe taenlnfgvd fsifkerfsg sinyytrknk dllgfysvpl ppniqgstya
      721 nvgtmqnsgi elqlnaqvvs tsaftysvaf agatnsnkfv sfsnaayqgq nyidvvglps
      781 pgspgtaqrl qegqrigtfy mlhaagvgdd gkllvynqkg diipadkann ddkrvvgngl
      841 pkatlslnnt ftykkwdasv ffravvgykl fntqafytgt pgtqsnanvl tsaygggkya
      901 kltnqattvi lsdyfledgs flkldnvtlg ytpkvnlksi rsirlyaaar nlltftsftg
      961 gdpdryping lypginssrs yyptttqila giqlgl
//
LOCUS       WP_104715132            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104715132
VERSION     WP_104715132.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116176
     Region          24..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msksllsfll lfltggvlya qtivkgvvts sqegvplpgv svavkgtttg tvtnaegryt
       61 lsvprgqtil vfsnigftks eiditnkttv dvilqeesqv lnevmvvgyg tvskethvgs
      121 saqvkaidia krpvsnalna lvgaapgvqt sqsggapgsa ptirvrgfgs isasnsalyv
      181 vdgvpfnmnt sslnpddies invlkdastt aiygsrgang vilittkkgk nnrnnlnfna
      241 svgtisrglp eyetvsaqey yplmwevqrn tlqygslrip qevagsiaag qttqylgrny
      301 tgiydllkyn pfnvannqiv dangvlnpna qllypedlnw vkaiqrggqs rqnynisydg
      361 ganksdyfas vgytkeqgyl lksdferfta rvnmntqptk wfktginlng sysrsntdag
      421 tggtsfinpf yitrfmgpiy pvykhdpatg ayvldkdgnk vydmgdsrpf ssgrhavwen
      481 elndrkeetg iiggrayati nilpslkats nisfdlqdrh rrtydnpiig dgapagrsyh
      541 ylyrtmsstf nqlleydksf gkhnlnvlgg hesytykyny mvgaragiiv dgitelpnfa
      601 tvlnvssred nygiesyfar asydfdkkyv lnasirrdgn skfykdvrwa tfwslgaayn
      661 iekedflkni nwlsmlklra sygvvgnedl gdlgyypyqg lyelarnnna epgftqasia
      721 nyqltwetak nfdvgvdfsv lrnrvsgsve ffnratdgli fsvplalang gttsgefevn
      781 rnigslynrg velqltgevv rtqdfryavt lnltsfknki tkmpesqpli qtgtkaysvg
      841 hsiydfymre fhgidsetgl amyktntltt nakivgadtl trviseanyr ytgfssipkf
      901 ygsmnhnlsy kgvslsfvlt fqvggkvydn ayrqlmhggt ygtalhkdaf krwqkpgdit
      961 evprfdngdv anltgestrf ltdasflqln nitlgytlpv swlsgigaks aslyfagenl
     1021 alfstrrgmn vtgsfngtvd ntynfnrvls igarlgf
//
LOCUS       WP_104715102            1176 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104715102
VERSION     WP_104715102.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1176)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1176)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1176)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1176
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126844
     Region          53..115
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          133..1172
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mglllrrkss glvgllitgi vcsaagqtpa yfaraeaere erprpatpat kgltevfqql
       61 ekkyhvqfay qkklvqdkri qatvgagkrs leenlqqvls plnltyekig etyiiserir
      121 esveskktsk aeikvkgkvt akdgselpgv nvrvkgtgig avtngqgeyl itapsetsvl
      181 vfsfigytsq eiavagktti dvilenetkq ltevvvtaag ierkanalgy svstlsttdl
      241 aqknepdpvr alagkvagvn vqggggvagg atnitirgns slgnnnqply vvdgvpfdns
      301 tfapvtgnnq tqsnqstasr afdidpnniq smtvlkgaaa aalygsraan gaiiittkas
      361 akksrkgtei tyntsysaet iaglpeyqql ygqgtngdyr savygssgsa ystratiphp
      421 laragfsaad fpqfyeadgv tpvqvpyrsy agknqrdffr tgsvyenalt vnsgsekgnf
      481 tvglsrttnq givpgneiar tsinvggnar ldnkfyvrgt inyvmtdqks ppiggsgsim
      541 stmyylptsy dltgypyenp ntganvydya gvdnpywsir hspatsnvdr yygnfvlgfd
      601 plswlniqnt agfnaytdrr vsvlgkgssv yangtintdn iyrqeldntl lvtitktikq
      661 dfslraifgn ninqrmtdrs afvgtniita ginninntst itlgslpnnr amirqrfyaf
      721 ftditldykg faslnivgrn dvsstlppen rsylyggvng sfifteafgl nspilnfgkv
      781 rvgytqvgne aqpyqtvnvf nanasagdld apfsnpvqsn vstmtlgdvl snarlkpefi
      841 tefeagtelq ffnnrlsidl tyyhkrstsq iftvksapst gftdriinlg qtsnkgielg
      901 isatpvslas gfrwninanf trnrnnvddl ggfaqlvygn nihiagqpyg qiygsryard
      961 segnilvnpq takpiaaats gpignpnpkf ivglnnsfsy kritfdvlfd wkqggaiyst
     1021 nignalsrgv trdtenretl wvgpgvlgnv ntlepildes gnkipnntal tvidyffsgg
     1081 ygpggigegy vfdatvfrlr elslgyqlps nilqktpfgs vsislsgrnl wykapntpky
     1141 mnydpevstg aannagfdsl gvpttrrfgv nlrasf
//
LOCUS       WP_104715277            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104715277
VERSION     WP_104715277.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118607
     Region          29..96
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          102..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mitrvpgllv alwisfgiwn qagaqqltlr lqqaslttif seiekqagvq fhydaqdipl
       61 krrfdfnssg plpvilrdla slsnlaflqk gnrilvrkqa qrrvsgrvid rsektplpgv
      121 svrsstgrvl avtdaegyyt gtvsatdlsq arlefrmvgm kpilspplgs satldvemep
      181 esrqmnelvi tnaytngtpk eevigsisqi nakelqpyrp iesfdkmleg laagvyvept
      241 tqlgtpvkin irgqgtltpv ggtrttstqp lfvidgipim eqergdaaqi fsgetlinpi
      301 aginpqdias isilkdasat aiyganaang viiittkags agrtaahvsv srgvstfinr
      361 mkllsgpeyf tlkreallns gftesqaadq agsstidtdw lglttrnasy tainadvsgg
      421 kegttyrfst gyryqqasal kndlqqlnls lkvnsilnrk lklgvtlspt iikksgldnf
      481 knnaylppnl spydaegnft tllgvpnpla vlaqneaftd alafngnanl hyavtpnlti
      541 sgtigtnfsq skdvsydsak natgstkggq lqifdrqtlg wlgylqgtya ktfqqnhsvq
      601 viagleaqdq rtvllagsgt nftydrirei sqatrqsass skqenatvsy yaqatydfkk
      661 kylltssira dqssmfgsdf nlalnsavgl swiiskepfl qnhpaftflk lrtsygstgn
      721 srigsyaarg lynfsygnyn gyvaavpets sapnpnlswe knlklnlgld ltlfdrlsit
      781 aeyyqntihd lisnvevple tgygsisynt akmrnqgfdl tlqthfiqsk hfkwrstltt
      841 gfnrnrilqy nqgftsvysd pasttseana airegystta iwgirwagvn petgneqfya
      901 pdgsvvdrtt irtyprssyf vlgdrlpkaq ggwvndlsyk qfsltlnily nlgenrmept
      961 qfigdgrnlr hsnmsvnlld rwqkpgdvap vsklliekgl vtnssrylqd lthlklsnvt
     1021 lhyslasals krlrmqgvsa flnitnvayw ykdkspagrn gvretrfafp eartlslgln
     1081 lsl
//
LOCUS       WP_104715662            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104715662
VERSION     WP_104715662.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118151
     Region          49..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnekkaygsv spatslfpvl lkrfgilagl yavllgwgsq vqaqstpltl qgsvidrtsn
       61 eplpgvaisv nnkavdltna qgrfelqvev gstigftfig yqphqfkaek ndasltvyle
      121 ngqkdlnevv vtalgikree kalgysvsti kedqltqamp nnwsdalkgk vaglnilqsg
      181 sgplnsarin lrgdrsldpn knealvvidg vpmingkvss gvdqaygaga sgadkdipid
      241 fgnglgdinp ddiesvtvlk gaaatalygs ragngaliit tksgkrkgkg vgvtvnsnfs
      301 indvlrwpey qyeygqgsga kyysyglspd gsntgstssa fgpkfdgqey fqydpvvegq
      361 sperrpwrpy kdnikgfwrt ghtftnnvav egggenysar asltytnnew impntgfdrl
      421 vaslnssvsl skriklntkl sytsktsdnl pgtgynnqsi syfmifqnpn vdlawyeprw
      481 kkgqdqiqqi hpfssfienp yliayemtns lnstniigni qatytlspkw efmirsglns
      541 rqdrreqrrp wntsnfpqgy ykqqdvafle sntdflatyk skltrtidlt asvggnrmss
      601 dvkqnnavar glllpgvykl snaleqpiad nsliqrkins lyglinldwq nkifvditgr
      661 ndwsstlpag nnsyfypsvs tsyvlselmp lptvisfaka rlswaqvgtd tepyriakyy
      721 dkspfpgsan spsilyngtl kpeistswea glnvylfkkr vnadvnfysn ttvnqvltvp
      781 mdittgyssa finsgkvqnr gvevmlsvqp vqsknfnwtl tgtwsknqnr ilalsndies
      841 eqqiiassgn asiiatkggs tgdiwgfglv rnpegqvvfd aktglalrpa ditkignaya
      901 dwrgglqnef syknlrlnvl ldgqfggivy sqthhkmseq gklkhtlagr etgtivgqgv
      961 irnadgsyap nttpvaistw ygdyyrranv etnsfdasyl klrevrleyn lprslvnrwk
     1021 lsaasigffg rdlamiskfp ifdpetasln gativpgvem gqlptprtwg vnlnlkl
//
LOCUS       WP_104715686            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104715686
VERSION     WP_104715686.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120143
     Region          35..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqllpkpqr slgylsllta lwmvlfslts qaqdrtlsgt vrgqddqqpl agvavrvkns
       61 nqgtttnadg tyrlavpass etliftfvgy ttqeeaissr tqidvllatd qrlleevvvt
      121 slgitkakrd lsyatqtika qdlvkarepn pvnalvgkva glnigasael lrapqvllrg
      181 grplfvvdgv pivsdtynin pddiesydvi kgpsgsalyg sratngviii ttkkgskdkr
      241 gfsvevnsst mtengflaip kvqdeygpgn kgtysfvdgr ggglndgdyd vwgpkfegql
      301 iaqydspidp qtgkriptpw vargkdnlkr flrpgvlstn svaisatsgk tdlrfgitnq
      361 yqkgmvpnts lnsttfsatl gqnisdrvrf esnfnfsrqa sanypdvnyg pnsliyntvi
      421 wagadwnvdd mkqlwqpgke giqqiyaeyq rynnpwfvak ewlrghynnt yngyalmkfd
      481 llknlelqar tqvtgyelfr nekmpysatt ygreqakgdy redrrsllen ntdvllnynk
      541 tfahgislra vggfsgrffr ynsnyastdy lsvpgvytfd nslnptrans fnsrmqvlsa
      601 lysvdvnlgr yatlsttgrw dknstlpsdk nvyfypsagv stvvsdyvrt paaisfvklr
      661 asyanvkeaf tqqnvytafs pldgsnplgy gqtfaspyeg psygttvayt isrpynneaa
      721 asyanalvdp nlkpssrtsf eagldvrflk nrigldvayf syldgprifg ltlpeatgys
      781 slttngiksq krgleialtg talksargln wdvtlnwstf qeylkeiygs qtrlnqfykv
      841 gdrldayygs afartregqi indasgrpvv npvnqflgyt nadfafgfin kfnyrnffln
      901 vqvdgrvggv iedyiqkqtf rggrhietvq gkmgearyqd ykgvaswvgp gvvltngniq
      961 ydvdgnitnf eslsfspmsd anktylqdwi sryyntnean misrsfvklr evtfgyqips
     1021 qvlqgrlgfv ksasisfvgr nllywaekkd ldveqfvsys drgsslqtpt trrygvninl
     1081 if
//
LOCUS       WP_104716173            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104716173
VERSION     WP_104716173.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111700
     Region          22..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklifftfl mlfgwiaqaq drivtgtvta sedgapipgv tvvvkgsntg tntdakgtyr
       61 ltlpsngttl vfsavgfgrk eeeingrtti dvvlqssves lnevvvtaqg ierdtrslgy
      121 atqnvngsal aqrsepnvln tlqgkvagvn itsssgapga stninirgit sfngsnqpli
      181 vvdgiifnnd vdnsqntlfg sqpssrlsdi spesiesinv lkgpaasvly gsrasagviv
      241 ittksgkgln gktevtfnss vnwqnvaylp kfqnqygqgt qnnyvnnnta swgpafgtpg
      301 fetvqnfrge tvpyraypnn irdfyktgtm fqnalniagg dqnnnfaati sstiqngvvr
      361 esdfdrhsvq vggnsklkng iklggtityv ksaqkntlmg nggsafgqit riprsydlvn
      421 tpyldpltge dfyfvngqnh plwsiqntff nsnvdrvfgn lsvgyditnw lnvsyrvtad
      481 tytdnrkqvq rvgaarapqg qidedlrfrs elngdllita kkndlfvqgl nanlllgqnl
      541 nqrsyresgv vsqslaipgf dnvgvgsvft ssyastnrrr lvghygqlsl dyksylflel
      601 sgrvdqsstl pknqnayfyp saalsfvple afnvktdavs ylkvrgniar vgrdadpyrl
      661 qsfftsatfg nnvaditfpl nvggtslpgf qpdgrigssn lkpefvnsfe vglnvgffnn
      721 rlgvdftyfn trstsqifnv aisnasgydt rttnigemqn kgielqlsat pirtssfkwd
      781 vllnftrirn kviaisegvn nsnitgnsfs giapsiavgy pygviigtan artesgelli
      841 npntglfmpg iagqvisnpq kdwvagltnn fsykgftlsa lvdvnkggqi ysfsqvdmrn
      901 agqteitgvd rnqprilpgv irnadgttrp nniqisaqsy wqslgglase gavfdatayr
      961 lrevalnyal pssllsrtpf gnisigvsgr nlwmyapgfp sdpeintqga gniqgldlng
     1021 ipttrnygvn lrvtf
//
LOCUS       WP_104716139            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Siphonobacter
            curvatus].
ACCESSION   WP_104716139
VERSION     WP_104716139.1
KEYWORDS    RefSeq.
SOURCE      Siphonobacter curvatus
  ORGANISM  Siphonobacter curvatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cytophagaceae; Siphonobacter.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Siphonobacter curvatus"
                     /db_xref="taxon:2094562"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115604
     Region          34..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiliflwa lalpglgtcq litqgrvval phlqplagas vrlqdsnlgt ttdslgrftl
       61 rtaqqtgmli issvgyqskp vplgpnvgti alseeasqls evvisngfer ipkeratgsf
      121 vtvdqqllnr svstdlisrl advvpgltfv rqnsspnaqt pirirgqstl naraeplivi
      181 dnfafegdin tinpndvesv tvlkdaaaas iwgaragngv ivittkqgkf nqapvvslta
      241 nvtvgekpdp yyvslmssad fianeqqlft rgyyrsqets pnklvlspvv elliagrdgk
      301 lsaaqvaqql eqlktqdvrq dylrylyqps inqqyalnlt ggaaqhryrv aagwdenrst
      361 avgdgyrrlt lsakntwsll krkldlttef yltagrtlqn nggltpmnqv qllsknpyar
      421 ladeqgqpla ipkdyrvgvl tpqplpwdyk pleelrlady srrtqelrln lglsyqvlpg
      481 ltaslqyqya pgsslqrnlq kqesyetrkl insfrqadgs lpiplgdmld esnarstghn
      541 lrgqlayqrh wggkhelswl ggseiselrr yarsarlygy daehltskav nyllpyasai
      601 npasqlsyip ykdgstlqvd rflslytnas ytydrrysvs astrydqsnl fgvdanqrgv
      661 plyslglgwn lheetfyhls alpylklrlt ygysgnidks vsayttayyq sfdaasglpy
      721 amitnppnps lrwervgmtn vgldfqsknr rivgslewya kkgldlmats tlapqtgvas
      781 lkgnsantkg rgidltltsl nvnrrlkwet tflfsynkdw ltkylgpass tlsfvgsanv
      841 plegkpqyal ysyawagldp atgnpqgyln gevsqnysql vsvpltdlvy hgsrrplvyg
      901 alrntlsykr fslsanltyr lgyffrktsv vygnvlggka shgdyalrwq qpgdeawtqv
      961 psrpqtfsss rdsfyanaei laakgdhlrw qdmnlsyrfp kgqvylyaan lgllytadks
     1021 gldpefpdgf pparslalgm nftf
//
LOCUS       WP_104729349             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ectopseudomonas oleovorans].
ACCESSION   WP_104729349
VERSION     WP_104729349.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas oleovorans
  ORGANISM  Ectopseudomonas oleovorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Ectopseudomonas oleovorans"
                     /db_xref="taxon:301"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38736
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etvkklvgqg hqvtvqagag isasipdsaf eaagatigne
       61 saafgadlvl kvvaptdael ahmksgavlv gmlnpfcndt iarmnargvt afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpqswme
      241 rqakavhera kqadivitta lipgrkaptl lhestvaemk pgsvvidlaa aqggncplte
      301 adkvvvkhgv tlvghtnlaa lvpadasaly arnlldflkl vidkegqfql nleddivaac
      361 lmcnagevvr kng
//
LOCUS       WP_104735517            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hanstruepera
            ponticola].
ACCESSION   WP_104735517
VERSION     WP_104735517.1
KEYWORDS    RefSeq.
SOURCE      Hanstruepera ponticola
  ORGANISM  Hanstruepera ponticola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Hanstruepera.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Hanstruepera ponticola"
                     /db_xref="taxon:2042995"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113004
     Region          23..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqgyklffl fvffsicsya qeksitgtvs desglplpgv niivkgttng tqtdfdgnyt
       61 ltvnqgdvlq isylgytsle qtvgnnnvin vslepdvtai devvitalgi krkpkelaya
      121 ttelkketlv qaapvdvasa lsgkssglni ntsdngvnpt sqvvlrgfss ltgnngaliv
      181 vdgvpqsqgt lnnlnandie sinilkgass vtlygskgan gaiivttkrg gnnekininf
      241 nsvvtfeevk yfpetqtkfg sgstqnfeyd pieneswgpr ydglprrvgp iladgtyqvl
      301 pyapikdnkk dffdtgitlq naislsggse nssyffsaqr vdrtgvtpgd eyvrdnfrfn
      361 atrksgklet stsvsffqdk tdvagaspnd gsyyrillnt pghipisnyr nwrtdkfstp
      421 dtyfnayfkn pyqiidqnrn tarsnrlqgi arldyefndw itatytlggt wfnssfkntq
      481 eawqydptlt ytrpsdevna vqdgmtdnfr lnsdllvnfd rqltedisar lilgnhvetf
      541 rskqvnvggn nlftnviynv nvrtgeltgg egttqkrlys yfgdltlgfr dylyltgsyr
      601 qdisstlpid nnsygyysag lsfvptdaft slkegaldyl kfnvsyarvg ndagigqtne
      661 nfivpggfpf gtttglrptt iavdpelspe fstsieggfn veffkrritl ganyyfvkse
      721 dqinfsqasa gsgarsyltn igeiqnqgfe fdlglvplky enfqwdlgvt vttnksevis
      781 ladgadrlqv gtgfqntatl faqvgeaypa ifapgyvrdp egrvvidant gdplvtnefi
      841 nlgstvpdli igattrirfk dftlsavady ktghvfyntv vealefaglt vhsastnrqp
      901 fvfpnssyet spgsgvyven nnittsggnr nfwqtsynni kenyvvdasa ikireialdy
      961 nlpskflekt piealsfgiv annllmwrak enkytdpefs intggngvsg igssaqtppt
     1021 gtygfkmnvn f
//
LOCUS       WP_104754310             440 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Brucella
            oryzae].
ACCESSION   WP_104754310
VERSION     WP_104754310.1
KEYWORDS    RefSeq.
SOURCE      Brucella oryzae (Ochrobactrum oryzae)
  ORGANISM  Brucella oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Brucella oryzae"
                     /db_xref="taxon:335286"
     Protein         1..440
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45452
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke sdpsetrvaa saetvkkfia lgfdvvvekg ageksripda eftaagarig
       61 taadaktadv ilkvrrpvda elklyksgaa lfamldpygh edavaalaka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedde fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vskemvasmr pgsvlvdlav erggnvegav
      301 agqiadvngv rivghlnvsg riaasasqly arnliafvet lvdkeakvlk idpeeelvka
      361 tllthqgkil hpafakaeta aapaavekaa kpkaapkska ekptakaaap katakpakkv
      421 pakaaktpss pktpadggea
//
LOCUS       WP_104735684            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hanstruepera
            ponticola].
ACCESSION   WP_104735684
VERSION     WP_104735684.1
KEYWORDS    RefSeq.
SOURCE      Hanstruepera ponticola
  ORGANISM  Hanstruepera ponticola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Hanstruepera.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Hanstruepera ponticola"
                     /db_xref="taxon:2042995"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112348
     Region          25..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lflafvvqlt faqektisgt isdenglplp gvniivkgtt tgtqtdfdgn
       61 ysitantgdv lsysflgytt kemtvgtann isfamevdse aleevvitgy giarekreit
      121 yqteevdeql lnqaqttraa tglagkvagl qinvqnngvn pssqiilrgl rsitgnneal
      181 ividgsitsk gafddlnpnd iqdinvlkga taaalygsra gngaliittk kgklgetltv
      241 glnstvtfed vaympdlqde ygpgiaggyd pyentnwgpr fdgisrrvgp ifedgtfqsl
      301 pyapvkdnar nfydtgitsq ntiylsggne tstmylsign qdtkgivpkd rykrttlran
      361 atkkvgdfel alnstflrde snvvgnnigs qsrtlywfvl nqganiplen ysdwendlys
      421 spdgyyngyy qnpywaidnn rntdksnrlt anmsvtwdvf dwldltgrvg gnilngsgke
      481 wrnaqaynsi ngaprptnvt sflidnefqr tdytfdflan mnfdinddfs lkailgassv
      541 teqvrasnvq vnnlsipgly dvsngtgapv vgaaetekrt ygyfadltig fknflflnas
      601 grydftstlp vddnsyfyps iglsavltda ipsikgnvln yakvtvsnst vyndlapeqi
      661 ietygqnaaf pfgavngfei qnqaidssik kekinttevg lnlgffnnrl tldaayfkti
      721 ttdnivssts apssastsll tnigklegdg ieitlggtiv kagdfswdas lnftkyktvv
      781 keigngvsei nlastgevgv yaiegeefpv iqasayvrdp ngnvvidpss gnplnslevn
      841 grlknlgttv pdyilglnts fnykgirlag tfdyrtghvy yaqgsdamef tgrsiestvg
      901 nrqdfvwpns vietspgvyv qntnipitgg sqqfwtdvyn eikenyvrda tavklrelsl
      961 sytlssklle ntpvkklsvg iigrnlitwl peenrfsdpe fangngpngn aigiggyfqs
     1021 pptrsigfnl nvef
//
LOCUS       WP_104772515             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_104772515
VERSION     WP_104772515.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53602
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq iktekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_104767321             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_104767321
VERSION     WP_104767321.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54890
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrkagaevv
       61 ataadlwgrs divlkvrpps seevalmrdg stlvgfvwpa qnpelmqqla tkratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgti nvdfnddair
      361 gltvikegnv twppppiqqp aaapkpatpp vaaaaskghg hgsgapmsak slaitfavga
      421 lvfllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_104778054             518 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Streptomyces].
ACCESSION   WP_104778054
VERSION     WP_104778054.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53266
     Region          11..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mvpaepqpqg igipsestag etrvaatpat vgrlvalgyd vtvepgagas srfsdaayee
       61 agarlgdpwq teivlkvnap steeigrlrd gatlialvsp alnpdlveel arrpitvlam
      121 davprisraq sldvlssman iagyravvea ahafgrfftg qvtaagkvpp akvlvagagv
      181 aglaavgaar slgavvratd prpevaeqvr slggeflavg aqqevstdgy akatsddynr
      241 laaelyaeqa advdiiitta lipgrpaprl itaedvarmk pgsvivdmaa vqggnvegtv
      301 agkavvtdnd vtiigytdlp grlpaqasql ygtnivnlmk lltpgkdgrl vldfddvvqr
      361 smtvvregek twppppvqvs aapaaggake pepapaeqpa kparpawssy alvgagalal
      421 flvtafspse llghftvfvl aivigfyvig nvhhalhtpl msvtnaisgi vvvgallqig
      481 qgdtavtvls faaillasin ifggfavtrr mlgmfskg
//
LOCUS       WP_104792710             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cloacibacterium normanense].
ACCESSION   WP_104792710
VERSION     WP_104792710.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacterium normanense
  ORGANISM  Cloacibacterium normanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Cloacibacterium normanense"
                     /db_xref="taxon:237258"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40485
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,91,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigvlkeps fetrvsllae saaalikkgn klivesgagd ksfnnnqeye kvgaeiksra
       61 evleqadill sihplqdedf pkisskillg vyqplsngen viksierkit tfsldmlprt
      121 traqamdvls sqaniagyka vllaansygr yfpmfmtaag siapakmlil gagvaglqai
      181 atakrlgavv evfdtrpavk eevmslgakf vevegaadas taggyaveqt eeykqkqqqr
      241 iaesvaksdi iittaqipgk kapiliteem lnsmrngsvi idlaastggn tpftknnetv
      301 nyngvsiign sslqstmpsd asklygkniv nflqliidke anlnlnwedd lvkgacithn
      361 geiindrvks ilspsmnn
//
LOCUS       WP_104793189             952 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Cloacibacterium normanense].
ACCESSION   WP_104793189
VERSION     WP_104793189.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacterium normanense
  ORGANISM  Cloacibacterium normanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
REFERENCE   1  (residues 1 to 952)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 952)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 952)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Cloacibacterium normanense"
                     /db_xref="taxon:237258"
     Protein         1..952
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104485
     Region          33..950
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklkvltv galffiggqt vmaqkkkdsl gekkidevvi lgynksstkp kdvsanttit
       61 advldsrpnv sflnsiqgsa pgvtiasnsg spgsaridvi irgissinas teplvvidgv
      121 ptnanqfrnl npediesvsi lrdaaatsiy gnrgangvlv vktkqakfgs gfrftysgtt
      181 gvsfmpdnry niadarellt iqkrrnvllg rtltdaqiad ypidtnwkdv ffnadltqqh
      241 nltissggen lsnytslgyf qqgglvpntn fqrftlrnni nakssnnklt fnaqvglafs
      301 krnqlnqetn sgingntvqn pllgslmalp yleanrfknp gdlfntigtn sggvgnfvyi
      361 ledvlktghi pnrifdtnif tsttttykit ddlsltnrsg mdfkntdqwn arapwsylaq
      421 vvaasnstqy ggfetisnsk efnfnsvtsa nysktfgdhq idlgayleyt kvhylfssrt
      481 qnglnplnwa lgagtgyvpy naadpnkyvp svsaqkvnag alaffgtldy dykskygfga
      541 vlrrdasyrf aennkwatfw svagrwnidk enfmegsvfn llklrasygt qgnanvvapa
      601 agsnamllgt qivrdlntvn ngydnnvgya vssignlslq weevtqanig ldfkvfsnkl
      661 egnvdvyrkq tdklyndiks saitsfydyr gnlgglkneg vevalrynia ntkdlrfslf
      721 vngaynkntl tdlavpvltg slinevggtl nqwnlvryvg vnpangneqf ldangnlten
      781 pvdadrvktg knyfpkytgg fglnseykgf fldaifafqa dlwridnqmi waynpsymas
      841 gfnvsadlln awtptntitd ipsltaplrs stsdrflyda sflrfktlsf gysvpkellk
      901 gnfvkslkvy vqgenlavwt kwkgfdpegl gtfplsvypn prtvsigtni ef
//
LOCUS       WP_104793227             930 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Cloacibacterium normanense].
ACCESSION   WP_104793227
VERSION     WP_104793227.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacterium normanense
  ORGANISM  Cloacibacterium normanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 930)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Cloacibacterium normanense"
                     /db_xref="taxon:237258"
     Protein         1..930
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103364
     Region          35..929
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmnikkglg liavlyftss fqaqiksdss aikekkidev vligyggikk qnltsaistl
       61 ksdafdnrpi ynvgqalqgs vagvtvvqas gkpgvsidvk irgnnsissg vnplyvvdgi
      121 qtfdisglnt ddivsmtilk datstaiygi ngsggvvivt tkrgkggkpq lnfnaywgvs
      181 ksvdnidvln mdqyktlmne inpaflntin npryqgintn wrdeifrtgf dqnynvnysf
      241 gndkvrayta lgyqgiagii epaqfdrvsa kvnldaniak wlklnaslny intklnntnd
      301 nagvarggvv lstlntpafl piygsqvnfi nsdatvydqt tgevkdgykp gqfapnpfqs
      361 gwenpvafqs rknltntqrf lsnlglevtl aknltwkpqv sydiidsvnd qfidnyssvy
      421 grqekglgge ynylykdlni entlnyklkh eahdldllag lqvhernten hnytgnvfpa
      481 gttdfnydla tyqhevlqke qlrevsyfgr aiytfenkyt vmgvfryngs salapgnkwg
      541 ffpgvsaawt isnenflkdn ptiselklrg gwgktgnasg iptyshfnle rltelgpngt
      601 wythqwdssd lgwevttdtn fgvdlglmnn rikltadvyq rktddlilpi gmgslgnilk
      661 nvgsmenkgv efsintvnfk redfswnsgl nisftknkil smnymptidn afietvggyl
      721 vrfsaeqqis sffgyqfdkv dpttgdvlyk dlngngyfdt gdrtfignpt pdytlgftnn
      781 fkyknwyldv lvtasqgndv ynatrfdlel mndfknqstv vldrwttagq itnipkants
      841 tamyisdrfv edgsfvklkn vtlgynfnnp fkgvsklnvy ltgqnlytwt dytgfdpevn
      901 afnttngvfg idygtypqvr tvilglkanf
//
LOCUS       WP_104793552             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Cloacibacterium normanense].
ACCESSION   WP_104793552
VERSION     WP_104793552.1
KEYWORDS    RefSeq.
SOURCE      Cloacibacterium normanense
  ORGANISM  Cloacibacterium normanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Cloacibacterium normanense"
                     /db_xref="taxon:237258"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110626
     Region          34..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkrtqqiil laalglvsvt hlqaqskkak ldsvrnidev vvtalgikrq dkslgyvaek
       61 vsseefektq nnnwaqaleg kvaglkiqta gagplgsski tlrgsismnl dnnealivvd
      121 gvplggtntg tgnaaygags ggdlpvdygn nfnsinpddi envtilkgat asalygsrga
      181 ngaimittks gknkngkirv tlnsstsfdt vlkwpdwqye ygqgtlakns agqfyysyga
      241 sadgvstggt ssafgpkfdg qyyfqydptv egqslerqlw rpykdnvkgf wqmgttysns
      301 isiessndkt sfrtslsavn ntwmmpntgf drfnyalsfd hkvtkklrvv skfaynytks
      361 dnlpstgynn qsisyfmifq npnvdlawye piwkkdkyqv dqihpfstfi dnpyliayem
      421 lngvhkklit gnitatynfn nnfemmlrsg ieitdeertt krpyssanyl qgyyreqyik
      481 nseyntdllf tyknnfgkwg vsasaggnir aneyvlndyr aiglrvpgiy qltnaislnt
      541 riaqpndket nsvyglasfn ydniwfvdft arndwsstlp kanrsyfyps vatslilsdv
      601 lkmkskswny wklraswsqv gndtqpyklq qfyntsdfvg saenianfqn pnlkpemnqn
      661 ieagmdfsff knrltynvtv yqnstkdqiv nvpslietgy strtinagev rnrgiemtln
      721 afpvknknfq wnvtanwsmn knrimslpae fqgepytmgs vggvvffnav vggslgdmyg
      781 yklqyapdgq vifgsdglta ksteieyvgn ayakwrgglq nafkyknfsl sfsfdgqygg
      841 rvysqshhkm seqgklthtl vgrdnpngti vgvgviqnad gsyspntkav tltsyyadyy
      901 rranvetnsf dasyvklrea nitfyfpkqi vqslnmsdls lslfgrnlwm wtkfplfdpe
      961 aatlndssit pgveigqlpt artvgiqlna kf
//
LOCUS       WP_104798098             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. TS-CS-82].
ACCESSION   WP_104798098
VERSION     WP_104798098.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. TS-CS-82
  ORGANISM  Limnohabitans sp. TS-CS-82
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Limnohabitans sp. TS-CS-82"
                     /db_xref="taxon:2094193"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38567
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpaeis agetrvaitp etakkliaqg havrvqsgag vaasitdeay aavgvsivda
       61 aqawaselvl kvrvpeaaea tciqsgsavv gmlepfnaeg lqrlasagav gfaleaaprt
      121 traqsmdvls sqaniagyka vmlaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi eatdvrpsvk eqveslggkf idvpfetaee keaaegvggy arpmpqswld
      241 rqkvevakrv aqadvvitta lipgraapvl vtaemvqamk pgsviidiaa gkgtdgvggn
      301 cplteagktv ikhgvtlvge tnlpalvaad asalyarnvl dflklvinke galhidledd
      361 ivaaclvtrd gavvkk
//
LOCUS       WP_104800455             376 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Limnohabitans].
ACCESSION   WP_104800455
VERSION     WP_104800455.1
KEYWORDS    RefSeq.
SOURCE      unclassified Limnohabitans
  ORGANISM  unclassified Limnohabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="unclassified Limnohabitans"
                     /db_xref="taxon:2626134"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38492
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpvela agearvavtp etakkliaqg havrvqsgag vaasvpdeay aavgaelvna
       61 stawgsdlvl kvrapeaaea ssikagstvv gmlepfnaeg lqrlatagat gfaleaaprt
      121 traqsmdvls sqaniagyka vmlaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi eatdvrpsvk eqveslgakf idvpfesqde kdaaegvggy arpmpqswld
      241 rqkvevakrv aladivitta lipgraapvl vtedmvkamk pgaviidiaa gkgadgvggn
      301 cplteagktv mkhgvtivge tnlpalvaad asalyarnvl dflklvinke galhidledd
      361 ivaaclvtrd gavvkk
//
LOCUS       WP_104800575             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. TS-CS-82].
ACCESSION   WP_104800575
VERSION     WP_104800575.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. TS-CS-82
  ORGANISM  Limnohabitans sp. TS-CS-82
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Limnohabitans sp. TS-CS-82"
                     /db_xref="taxon:2094193"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38558
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvigvpaeta agesrvsitp etakkliaqg hvvrmqsgag vaasvpdday aavgvelvga
       61 qaawssdlvl kvrapeaaea ssiktgstvv gmlepfnaeg lqrlasagat gfaleaaprt
      121 traqsmdvls sqaniagyka vmlaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi eatdvrpsvk eqveslgakf idvpfesqde kdaaegvggy arpmpqswld
      241 rqkvevakrv aladivitta lipgraapvl vtedmvkamk pgaviidiaa gkgadgvggn
      301 cplteagktv ikhgvtivge tnlpalvaad asalyarnvl dflklvinke galhidmedd
      361 ivaaclvtrd gavvkk
//
LOCUS       WP_104808430            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            filamentus].
ACCESSION   WP_104808430
VERSION     WP_104808430.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter filamentus
  ORGANISM  Polaribacter filamentus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Polaribacter filamentus"
                     /db_xref="taxon:53483"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112826
     Region          25..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lllalvvqis faqdktisgt vsdqsgplpg vsilikgast gtetdfdgky
       61 tisasegavl vfrylgyktl ekrignsnvi nltmaedssv leevvivayg tstrealtgs
      121 asvvttkdla lrnvtspiaa iegkatgvqf vsasgqpgsd ptivirgvgt lngssdplyi
      181 vdgiqfeggl ntinqddias mtilkggast slygaraang vvlittktgt kgktqvnvtt
      241 qyglvtrgip eydylnpgqy yetmweaykn sltgataaad asvgiysrlg ynpfnvpndq
      301 ivgtdgtlnp aaqvtyksln wydvldqvgt rsnhsvnvas ggenhkvffs asyldeegyi
      361 itskfdritt rvngdfnvnk wlkiggsani siseskgpps rggsianpfg faknigsiyp
      421 vylndadgnl vldaagnrif dvgegdisln qgsrpnnpgr haiaeailnd elnrdntygf
      481 ryyadlnite glnlrlnygm dineginksy enpivgdgqp tgrygetrfr rdvinfsqvl
      541 dytksfknvh nfnatlghes yqrdfssndg lattqtasgi fefdnfaipv rlggstttkr
      601 iegyfarlky dydnkyyisg svrsdgtsvl stdarwgtfy svggawridq edfiknvsfi
      661 drlklrasyg qvgnddlndf fisqalyslt snagvpaivf tnpgnqllew etvgsweaal
      721 efglfnnfld gsveywekns tdllynlpip lsnginsapf niadvsnsgi elsltahlln
      781 ksdfkwdvtv qastfkneiv klpepfings krwevgrsry dfflfhsagv dpangdalyy
      841 myeddldgns vaildangvh ettndwndtq rayseantip dvlgsisntf sykgftadll
      901 ftygiggdll dngysammht gnygnsyhpd vlnawkqagd itdvprlevg sttqvqtqst
      961 rfltdasfla lknvnvgysf ndliteklgv snmkvyvsge nlfintartg lnpqfnlggt
     1021 gagndfnpar tvtfglnisl
//
LOCUS       WP_104808435            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            filamentus].
ACCESSION   WP_104808435
VERSION     WP_104808435.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter filamentus
  ORGANISM  Polaribacter filamentus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Polaribacter filamentus"
                     /db_xref="taxon:53483"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112395
     Region          25..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntkfnrilt lllafvvqis faqqktisgt vsdnsgsipg vsiivkgtti gvqtdfdgky
       61 aikaapgdvl vfrylgyktl ektvtasttl nvtlqeggei ldevvitafg ikkeekalgy
      121 svqsikgesl tearesnitn sisgkiagvq vtgtsgsvga ssrivlrgns sitgnneplf
      181 vvdgvpinns sfgsatsggg vdlpngaadi npddiesitv lkgpnaaaly glrasngviv
      241 ittkrgnpnk kfsvsmntnl tfsnplllpd yqnsygqggd tsffqyvnga sggigdgvde
      301 swgpaldagl efvqwdsqlt nngnptpwis hpdnvkdfln tginisnnvs itsgsfrlsi
      361 gnskeegmvp ftelkkftvg isgsldiadh tkvgislnyl nqdsdnlpis gynnenpfqq
      421 fiwsarqvnf tdlrdwrnfp sapvgtaaeg tplnwnhnfq nnpywiletn tntfekdrii
      481 gnvttetqlt dhltlstmlg vdmfsqrttn rqafgsnnaq sgsyqerirr feeinanfll
      541 synnnitedf gfsvslggnh mnrtgdnvng ylpnlelpnl yslsnlqtgs tavlsnyhad
      601 qqinsfyatg qlayknmvfl dftgrndwas ilptannsff ypsvaasvll sdvfegikes
      661 nvnllkirgg wsqvggtgal geyslnqtfg lsnsgfgnqa svpntqfnpn lkaetvtgie
      721 fgldlkmfsn rlrfsatyyd qksndllvpi gvsaatgfts vwdniadmqn kgfelqlggt
      781 iikkadftfd ldvnfaknvn evtslgdlds yvlggqwgvs learpgqpyg slvgrdfert
      841 adgqviyeng lplidetqqi igniapdwtg ganfafqyka fslstlidak iggdvhsmty
      901 awgryagtls esligretgi vgngvmadgn ggyvtnnvvv gaksfnqasy snsiessaif
      961 dasyvklrqv sigytlpqky lektiiqslk fsvvgrnlai lyknaphidp etgfsssngn
     1021 qgqefgqyps arnigfnvnl rf
//
LOCUS       WP_104810379            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Polaribacter
            filamentus].
ACCESSION   WP_104810379
VERSION     WP_104810379.1
KEYWORDS    RefSeq.
SOURCE      Polaribacter filamentus
  ORGANISM  Polaribacter filamentus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Polaribacter filamentus"
                     /db_xref="taxon:53483"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117683
     Region          20..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhffmwvll lfasnsfsqi kitgtitqkn tgekipyvsi sssirngtts dingeysiei
       61 lekntyltys slgyktqkia ignqtviniq ldeietnlne ivvtalgvnr ntkelgyvvq
      121 eikskdisei ktpnfldnla gklagvtisq gatgvgsssk itirgeasfs nnnplfvvdg
      181 tpinnntvfn ftneaaagfq eidfgngame vnaddiesvt vlkgpsaaal ygtrasngvi
      241 viktkdgtkk kglgisinss itfdtafrlp dfqneygqgn sdnfkygngl gngindnity
      301 swgprldtgn liaqfdspvn lpngtivrgg dtslynglpi tptlfksnpn nlkdfyqtgi
      361 ttsnnisind efdsgsyrls ftnldsesii pgvnldrktv alkmnfnpte ttkitssvsy
      421 vnsssdnrpa ngygsenvny slvawgprsl ninslrnywq pglegvqqys fnytyfdnpf
      481 filqentnsf nrdrlfgnva inhkftenls islrsgmdys sekrefkrnf ssnrfkngah
      541 aehdvfyrei ntefllnykn nfgyfsfdts fggnrldqka stkqsqttnl aqpgifslnn
      601 aaspievfqf nsqkrinsly giaklgykdy lyiditgrnd wssalatpfs vdgtsffyps
      661 isssfilsny tklpenisfa klrasaaqvg ndtnpyqtsg afvsqttfng qptfsnqnfi
      721 pnanlkpevt tsyefgadvr ffkdrlsvdf tyynattkdq iislpipiss gynqqvvngg
      781 kvnttgveii lggtpiknkn ftwntifnfa tnksvikdlp qengrltlay sriydsanqt
      841 vwfqveegge vgdfygtgyk knaegqflid dngsyiadnt lqklgnynpd ftlgwsnsfq
      901 yknwnasflf dwrqggeivs rtsalgnvgg qlaetsfrpd tgivaqgvnv ntgqpntiav
      961 saesyyrkfy drnheennvy dasflkvrqf sigytlnlne gflglqdvst mnfsfignnl
     1021 fvitenphfd peqlavqgng fvsgvedmsy atsrslgfkv afnf
//
LOCUS       WP_104811847            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aureitalea
            marina].
ACCESSION   WP_104811847
VERSION     WP_104811847.1
KEYWORDS    RefSeq.
SOURCE      Aureitalea marina
  ORGANISM  Aureitalea marina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aureitalea.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Aureitalea marina"
                     /db_xref="taxon:930804"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112742
     Region          27..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkllmkll fvpvlllfgg aalaqttvtg nvsdnlgpvp gvniivkgts ngaqsdfdgn
       61 ysldnvasda tlvfsyigya tqevavngqs tinvtlqddv qalnevvvig ygtttvkdat
      121 gavasvtaed fnkgvilsae qliqgktagv qvsqstgepg agidirirga nsvrsnnnpl
      181 fvvdgvplsg eatqaessdv gagsagaknp lsflnpndie sisilkdasa taiygsrgan
      241 gvvlittksg rgaqggrwdi sssisrakvr ktfdllsase ylaqtdrfgf dvasrnfrns
      301 tdwqdfiyrt avstdqnigy snnygdgnvr asfnygkilg vventaleri tgrlnanhkf
      361 iddrlrlsfq gtasrvnddg taigpsagfr gdligsaysa nptwptnadf ansggllspa
      421 talaysesrt ntnrfllnfs aefdiipelt akvnlgydys dsqrsnvasa narnfgrgaf
      481 gngvgaigql etqnqlleat lrynkqfgnv nldviggysw qdfnrngyna qawgfntedm
      541 rqmvrdmest idvlegrisg eyqqygyapn isdgifinrl gldnrdeagn pqpvtdfirn
      601 nsglqvrslv ndyfdntdel rsyfgrvnvd isdkylftat vradassrfg ednqtgvfps
      661 gafawkmhne dfigdsvstl klrlgvgvtg nqeglgygnq frrqrfsgvg isdggdvnip
      721 gisdvafanp dlkweetiqy aggidfgfnn drfygsvdvy yketndllfr vlsaqpaaqp
      781 fvflnlpdsk vvnqgiefsl gadivdsgdw ywgvnfniay neneitdlqg efdagtirgq
      841 glslafaqkl kagqplfsyf lrdfqgfdpt tgqpiqtdvq dfvgksalpd intglsttas
      901 yknwtlsayf agqfghyiyn ntanafftag afrsgrnvpl dvlnagesfd aaadvstrfl
      961 esgdfvrlqn vtlsydipla edsvfervgv sltsqnlfvi tdysgldpev ssapaggdll
     1021 nglpvfgidy gayprpttft lglnanf
//
LOCUS       WP_104812876            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aureitalea
            marina].
ACCESSION   WP_104812876
VERSION     WP_104812876.1
KEYWORDS    RefSeq.
SOURCE      Aureitalea marina
  ORGANISM  Aureitalea marina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aureitalea.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Aureitalea marina"
                     /db_xref="taxon:930804"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117949
     Region          25..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfsgilt lllafvvqlt faqektisgt vtdnsglplp gvniivkgts ngtqsdfdgn
       61 ysiqasvgqs lvfsyvgftt veqavtaaas nisiqmqeda aeldevvvta qgikkeakal
      121 gyavstveae dieqrtegdv arvlsgkasg vqitsqggts gsatnvvirg yssitgsnqa
      181 lfivdgvpfs sdtnaqgnfl dgnvgssrfl dldpnniesv nvlkglaaat lygtagrngv
      241 ivittksggg gatasvkkte itvsqsfffn eiaslpdyqd dygngfdqsf gwffsnwgpn
      301 fspngvdgyl ndpaglidgn gtlahpydts aflnnfnggn nelknkysga rypyqpynsv
      361 enffrtgavs ntsinirgns edgkvafnvn yghldeegft pgngirrntl avggraqlsn
      421 kftaqatlnf srndvksppv aasrgngtlg fstfanvfft prsvdlmgle feipenggsi
      481 yyrngndiin prwsvknags rqltnrvfgt aqlqyditdn lnvlyragid fynerntqyv
      541 nkngvnfnqa ingqyitydn nvriwdhyls vggdydltsd fglsftagat srsrefdqqg
      601 vqsdgqivfg vlrhfnfltq qpiqfttyrn iigvfgeali dfrdyafltl sgrndwvsnl
      661 ptennskfyp sisgsfiptq afpsirsngf nylkiraglg qsanfptgfp vvntvaqntn
      721 vnggaiggvt tnavsnfqan pdlkpelise fevgfdtrvw dnritlnfsy fdrqtkdliv
      781 nkplspstgf tntqdnigkv egdgfeadls vdffraeneg dfawnsrvnf tkseqivteq
      841 dedqilfags tasflganaa iegeqlgviv gdrvlrdeng nfvvnsagny vtesqvtldd
      901 grqitpiign pnpdyvmnfi nsfsyknfnl nfqvshtsgg diasstiavl lgrglieeta
      961 drkntfilpg vrqdngqpnd iqinnsqyyf snvlfgpkel qvydgsvirl qeislgytvp
     1021 kryldktpfg svsitasgfn lwydayntpd ganfdpnvag vgigngrgfd yingpssrrw
     1081 gmsikasf
//
LOCUS       WP_104824294             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. NXC24].
ACCESSION   WP_104824294
VERSION     WP_104824294.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. NXC24
  ORGANISM  Rhizobium sp. NXC24
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium sp. NXC24"
                     /db_xref="taxon:2048897"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40522
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnlvfvake tvadetrvaa sietvkkmks lgfdivveag agalsripdd eyeaigarig
       61 sardaaradv ilkvrrptse eiagyksgai viaimdpygn eaaladmara gltsfsmelm
      121 pritraqsmd vlssqanlag yqavieaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aqvsatdvrp aakeqvaslg arfvavedee fkaaetaggy akemskdyqv
      241 kqaalvaehi skqdivitta lipgrpaprl vsremlkamr pgavavdlav erggniegve
      301 fgtvadvegv kvigypnlag ripasasaly aknlvtflet mvdknsknlg lnradelika
      361 tmltdggevv hpnfvdpdqp tvnkgdl
//
LOCUS       WP_104827469             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Rhizobium].
ACCESSION   WP_104827469
VERSION     WP_104827469.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55088
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigavkera agearvamtp eaalqlqklg yecvietgag kaagfsdeay rgvgvtvvds
       61 aallyetsdv iakvrppeaa evdrlepgkt lisffypaqn kelldqasss ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfge eqqdgaatgg yaapsspefr
      241 ekqlakfrel apqidivitt alipgrdapk lwladmvaam kpgsvvidla aerggncdlt
      301 vpderivsdn gvivigytdf psrmaaqast lyatnirhml tdltpgkdgv ivhnmdddvi
      361 rgatvtkdga itypppppkv qaiaaakpke kvkeptpeek rarelaafka qtrnqgillv
      421 igtallllvg ayapssfmsh fvvfvlacfv gfqviwnvsh slhtplmavt navsgivilg
      481 allqigsgng lvvtlaalsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_104827955             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. NXC24].
ACCESSION   WP_104827955
VERSION     WP_104827955.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. NXC24
  ORGANISM  Rhizobium sp. NXC24
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. NXC24"
                     /db_xref="taxon:2048897"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55266
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgspreta pgelrvaltp eaalqlqklg yecvietgag rqagfsdeay ravgvtvvds
       61 aallyetsdv iakvrppeaa evarlapgkt lisffypaqn kelleqarsr ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avtyafdvrp evaeqiesmg aefvfldfge eqqdgaatgg yaapsspefr
      241 ekqlakfrel apqidivitt alipgrdapk lwladmvaam kpgsvvidla aerggncdlt
      301 vpderivsdn gvivigytdf psrmaaqast lyatnirhml tdltpgkdgv ivhnmdddvi
      361 rgatvtkdga itypppppkv qaiaaakpke kvkeptpeek rarelaafka qtknqgillv
      421 igtallllvg ayapssfmsh fvvfvlacfv gfqviwnvsh slhtplmavt navsgivilg
      481 allqigsgng lvvtlaalsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_104830322             412 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hyphococcus luteus].
ACCESSION   WP_104830322
VERSION     WP_104830322.1
KEYWORDS    RefSeq.
SOURCE      Hyphococcus luteus
  ORGANISM  Hyphococcus luteus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Parvularculales; Parvularculaceae; Hyphococcus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Hyphococcus luteus"
                     /db_xref="taxon:2058213"
     Protein         1..412
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42617
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavlketr sgetrvaatp etvkkfislg asvsvqagag daarfpdady aaagasisps
       61 aadaaqgada ilkvlapsse elrvfgrgvk liailsaynd pdsvasyarl gvdamamelm
      121 pritraqsmd vlssqsnlag ykavidaaay ygralpmmmt aagtiaaakv fvmgagvagl
      181 qaiatarrlg aivsatdvrf aakeqveslg atfvtvdeea mkeaeteggy akemsedfqk
      241 rqadfvadhi akqdivvtta lipgrpaprl vsadmvnsmk pgsvivdlav eaggnvelsr
      301 pgeaietggi tilgfknvpg rlaadassly arniynfiaa ffdketksmk adpedaiika
      361 vtltrggkiv hpafeaaeaa pettpepeap aeetppkgag adtpdetdge ed
//
LOCUS       WP_104839566             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium fredii].
ACCESSION   WP_104839566
VERSION     WP_104839566.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium fredii (Rhizobium fredii)
  ORGANISM  Sinorhizobium fredii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium fredii"
                     /db_xref="taxon:380"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39374
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msqivfiake ldsdeprvag svesvkklks lgfdvvveag agsrsrvpde efekagarig
       61 saadagsadv ilkvrrptae eiggyksgai viaimdpygn daaiaamaea gltafamelm
      121 pritraqsmd vlssqanlag yqavvdaahe ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg amvsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskdyqa
      241 kqaalvaehi akqdivvtta lipgrpaprl vtrqmldsmk pgsvvvdlav erggnvegae
      301 agrvveiggv kvvghlnvpg riaasaslly aknlvtflet mvskeekala vdmedelvka
      361 talthggavv hpafggangg dk
//
LOCUS       WP_104864347             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium parafortuitum].
ACCESSION   WP_104864347
VERSION     WP_104864347.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium parafortuitum (Mycobacterium parafortuitum)
  ORGANISM  Mycolicibacterium parafortuitum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Mycolicibacterium parafortuitum"
                     /db_xref="taxon:39692"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52730
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgetrvaatp qtvgqliklg yqvvvetgag aassfsdday aqagaeigst
       61 yqvlssdvvl kvnaptdaei aglrdgatli slispalkpe llealstrpv tvlamdavpr
      121 israqsldvl ssmaniagyr avveaahrfg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaagslgai vratdprpev adqvaslgge ylavtdpaeg vaevsttgya kemgedykvr
      241 eaalyaeqak dvdiiittal ipgrpaprii taemvasmkp gsvivdmaaa nggnvegtvk
      301 deavvtangv tiigytdlag rlpaqasqly gtnlvnllkl ltpekdgqlt ldwddvvqrs
      361 vtvvrdgeit wppppvqvsa apattpaaap vqkaepkapm smgrrlgitf taaaalfali
      421 alspaalqvh ltvfalaivi gyyvignvhh alhtplmsvt naisgiivvg allqighgna
      481 vvsavafiai llasinifgg favtrrmlam fsrs
//
LOCUS       WP_104852535             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter sp. SWBY1].
ACCESSION   WP_104852535
VERSION     WP_104852535.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. SWBY1
  ORGANISM  Acinetobacter sp. SWBY1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter sp. SWBY1"
                     /db_xref="taxon:2079596"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39831
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklisag hsvviergag vkaayidsay eqvcatmtdd
       61 ayrgsqmilk vrapkgeeiq klapnstvva mfdpyrntel dqfasaqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmseeeq qkaadaakng ygwmpgeqyi
      241 kdqavivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 qcgetvvtan gvkilgipni pstvsteasa lyarnvlnfv etlfdndknf alnpeeeiqk
      361 allvthngqv llkrg
//
LOCUS       WP_104872880             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Providencia].
ACCESSION   WP_104872880
VERSION     WP_104872880.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Providencia"
                     /db_xref="taxon:586"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53480
     Region          8..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 makiinrtly llslvagiwl ltpavhaqta skeasstint knesfaqahp dqyhswrats
       61 eqsqredala edprlvilwa gypfsrdynk prghayalid vretlrtgap kdaqdgplpm
      121 acwsckspdv arliqeqged eyfhgkwakg gpeivnvlgc adchktdspe faqgqpaltl
      181 trpyaarame aiskpfdkas rfdqqsmvcg qchveyyfag enksvkfpwd sgtkvedmev
      241 yydniafsdw tnslskapml kaqhpeyetw sagihgknnv tcidchmpkl qnekgelyts
      301 hkignpfdnf eqtcrnchtq skqelqavva erkqaiqemk ikvedqlvha hfeakaawda
      361 gatekemapi ladirhaqwr wdlaiashgi hmhapeeglr mlggamnkaa dartklvrll
      421 gakgitheia ipdistkeka qqaigldmqk inaekqeflk tvvpewdaqa rknnllsq
//
LOCUS       WP_104882319             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. SWI6].
ACCESSION   WP_104882319
VERSION     WP_104882319.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. SWI6
  ORGANISM  Pseudomonas sp. SWI6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. SWI6"
                     /db_xref="taxon:2083051"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38836
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqrgag lnasipdsay eavgaslgsa
       61 adaygaqlvl kvvapndeel aqinsgsllv gmlnpfnnel iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvmengv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_104884565             492 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Pasteurella multocida].
ACCESSION   WP_104884565
VERSION     WP_104884565.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella multocida
  ORGANISM  Pasteurella multocida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Pasteurella multocida"
                     /db_xref="taxon:747"
     gene            1..492
                     /gene="nrfA"
     Protein         1..492
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=54915
     Region          14..491
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mngviivntl kkrlfvattm iwglsvtlpv laeykpieqp vepanpslki esrndlfkek
       61 ypkqyqtwad tskstdldsv nyedprvivl wagyafakdy kkprghfyav tdvreilrta
      121 apmtldagpm pmacwscksp dvprliaerg eagyfgatwa sggsevvnpi gcadchdtts
      181 kdfaegkpal riarpyvlra lekidhkfdt sdrtdqraal canchveyyf agdlkqvtfp
      241 wdngitvdam ekyyddigfv dwthavskap mlkaqhpdye twmlgvhgkn gvtcidchmp
      301 kvqgadgkvy tdhqignpfn afehtcanch dqskeklqam vksrkteikd vmlrledqlv
      361 aahfeakaaw eagaskeemk ealqdirhaq wrwdyaaagh gghihapdvl lkvigtgldk
      421 ssdartklvr vlakhgitdp vqlpdistae nawkatgvdi ekerkakaef lktvvpqwdk
      481 earekgllpa ek
//
LOCUS       WP_104893172             507 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Devosia].
ACCESSION   WP_104893172
VERSION     WP_104893172.1
KEYWORDS    RefSeq.
SOURCE      Devosia
  ORGANISM  Devosia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Devosia"
                     /db_xref="taxon:46913"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51814
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlrerf egesrvaatp etvakyialg aeiavekdag tgsriadeqf keagatigat
       61 aattlkgadi vlcvrrpaaa dlkgvntgal ligaldpygn dkdvaalaka gvaaismefm
      121 pritraqvmd ilssqanlag yqavieaaav fdrampmmmt aagtvrpaka fvmgagvagl
      181 qaiatakrlg avvsatdvra aageqveslg gkfimtdalk dasgtggyar eltkdeqaaq
      241 aelvaghisk qdivvttali pgrpapklvt kamvesmapg svivdlaaer ggnveltqpg
      301 kvithngvti igytnlaghi pttasqlyar nllafidtlv dkkekklain wddelvkatv
      361 ltregavvhp afaapqadta hdpeakpapa nkpaakkapa kadlahdqea kpapvkkpat
      421 rkpaasksta sksaaapkpd vahdpeakpa prrtaarkpa akaaaaeahp qtdtaakapa
      481 akkpaarkpa akkpaakkpa apeggdk
//
LOCUS       WP_104898729             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nostoc sp.
            'Peltigera membranacea cyanobiont' N6].
ACCESSION   WP_104898729
VERSION     WP_104898729.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. 'Peltigera membranacea cyanobiont' N6
  ORGANISM  Nostoc sp. 'Peltigera membranacea cyanobiont' N6
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc; Nostoc cyanobionts.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Nostoc sp. 'Peltigera membranacea cyanobiont'
                     N6"
                     /db_xref="taxon:1261031"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41452
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dtvarlvkqg levwvetgag ersffsdpdy eaagatiisd
       61 taklwgetdi llkvsppqer edgrsevdll kegavlvsfl nplgnpivaq qlanrkital
      121 smemiprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkldeetvaa ggyakeisea
      241 skqrtqevva ehvknsdvvi ttaqvpgrqa prlvteemva qmkpgsvivd laadqggnca
      301 ctepgkdivw ngvtiigpin lpssmpihas qlyaknvtsl mqllikdkal qvdfsddivd
      361 aacvthagei rnqrvrdalq alstqqsavn
//
LOCUS       WP_104909212             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nostoc sp.
            'Lobaria pulmonaria (5183) cyanobiont'].
ACCESSION   WP_104909212
VERSION     WP_104909212.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sp. 'Lobaria pulmonaria (5183) cyanobiont'
  ORGANISM  Nostoc sp. 'Lobaria pulmonaria (5183) cyanobiont'
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc; Nostoc cyanobionts.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Nostoc sp. 'Lobaria pulmonaria (5183)
                     cyanobiont'"
                     /db_xref="taxon:1618022"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41026
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dtvarlvkqg levwveagag ersffsdsdy eaaggtiisd
       61 taklwgetdi llkvsppqer edgrsevdll kegavllsfl nplgnpvvaq qlanrkvtal
      121 smemiprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkldeetvaa ggyakeisea
      241 skqrtqevva ehvknsdvvi ttaqvpgrqa prlvteemva qmkpgsvivd laadqggnca
      301 ctepgkdivw ngvtiigpin lpssmpihas qlyaknvtsl mqllikdkal qvdfsddivd
      361 aacvthagei rnqrvrdalq alssvgag
//
LOCUS       WP_104912734             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Pontimonas
            salivibrio].
ACCESSION   WP_104912734
VERSION     WP_104912734.1
KEYWORDS    RefSeq.
SOURCE      Pontimonas salivibrio
  ORGANISM  Pontimonas salivibrio
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Pontimonas.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Pontimonas salivibrio"
                     /db_xref="taxon:1159327"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40032
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mivgvptesi sgenrvaqtp etvkqlvdmg lkvqvhkgag vaagypdkdy qdagasivat
       61 lnlekvdvlt hvrplsttvv nklpagtitv glgspasegp vvkalakkkv tsfalelvpr
      121 israqsmdal tsqalvagyr cvleaamrfp rffplymtaa gtvppanvlv lgagvaglqa
      181 iatakrlgak vqaydvraas adevrsmggq fieldldaqa dgqggyakel ssdrqarqqe
      241 lltpyvtqad viittaaipg rpaprlitkk mmadmkpgsv lidlaaetgg nvegsvagvd
      301 tpvkvqggkg hatlvgmkdv psamaydasr lyaknianll almnvdgtiq pdfedevvag
      361 aclthegeir heptrealas pkkga
//
LOCUS       WP_104916160            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Weeksellaceae].
ACCESSION   WP_104916160
VERSION     WP_104916160.1
KEYWORDS    RefSeq.
SOURCE      Weeksellaceae
  ORGANISM  Weeksellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Weeksellaceae"
                     /db_xref="taxon:2762318"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119348
     Region          21..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilmplil cssislmaqh tisgqvldql sqsplrnvti alknsstavi tdsngffglq
       61 tkenkielva svlgyeskti elnlpqsipv kimltakftd ietvniatgy qkiskeratg
      121 syshadnkll nqqvgtnvld rlsnmisgvt idrgtsgtaq lmirgistin gpksplvvvd
      181 nfpyegdign inpnmvesit vlkdasaasi wgaraangvi vittksgkls qplsleftan
      241 tsispkpdfn ylktisssdf idvetelfkr gyydsdinfs shpalspvvd llnkqkkglm
      301 seeevnrqig alrnidakdq yrrymylpse krqyflniag gapkfswtsg igyddnkgnl
      361 gekytrtnlr fqniwrpikq ltvntgiyyt dtrtesgris yggiimarns avpymqlads
      421 egnpsivtkg ydqnykdsfg lgklldwnyy plldwqndra ktngtevmin asvnykiirg
      481 feaefkyqyq rqnditenlh nsqsyfarny vnsfaqvdtn gntnfivpkg gildksgalt
      541 iinnvrgqln ytgkwhkhgv taiagaesrd avrsyeynry ygynensmas ssvdytrqyt
      601 llptgnmefi qrgqslgkrt trfvslfana aytfdnkyti sgsfrrdasn lfglntndqw
      661 npfwsvgtlw eiskenfyhv ewlpylklra sygfngnidp amvavstiaf dtdksrytgt
      721 svarfdnyfn prlrwetsrm inagvdfssr nsrisgsvey ftkkgtnlfg prqmdyttgi
      781 dymlsnvaet sghgidvelk tmnidrvvkw ntilnfstyr dkvtkyylad plasqfigng
      841 ssvpisgveg lpvysifayk wagldpktgd pqgylngqvs kdysqmvgvg tsvqdlefyg
      901 savptvygsf vnsfsyknfs mdigisykfg ywfrrnsiny tnlftswsgh sdyafrwqke
      961 gdeaftnvps nnyqsdanrd afysgssvlv ekgdhirlqy inltytfdkt lfgssvfenl
     1021 safvnlsnlg ilwranksgi dpdynlgvng lrppavytig lrakf
//
LOCUS       WP_104916584             975 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_104916584
VERSION     WP_104916584.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 975)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 975)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 975)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..975
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108042
     Region          26..974
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvklhmlsv gvlffigqgl laqkkkpdtt sikdieevvv vafgkqkkea ivgsvatvdk
       61 riietqqats ilgalqgtvt gvnviaaggm pgdnpsiyir gvssinastq pliivdgspy
      121 ggninsipqd qvesmsvlkd asanalygsr gangviiitt kkgrlnakpk vnvtsligvs
      181 ssavkfhevl kaedfmkytw qairnarivs ngqtpdaaaq yatnniintl gynpynvvnp
      241 iddkgnvvan akllwdtdwe relinnsalk qehrlnisgg senttyfiga dyldmygnik
      301 tsrferlgfr anvdskvntw lkvglntsfs assqnypmqs gsafqspiqw vytlsgiypv
      361 ymrdekgnii ldafgrsqyd ygdnavsgrp vnaqrpllan enalgalynn kirynrydtf
      421 ingyaevtlt dylklrsqgs fqlynydsys ythyaygaaa svkgrvsqsr dltktinwtn
      481 sldfnksfgk hnvnaqaife lmdyrfdals aqgtgflpev yvlngktvse gvggyinqer
      541 lvgylgrlgy nyankyfieg svrndgstrf asevrwgtfy svggawvvsq ekffknkivn
      601 ylklkssyge lgnngtdgyf pyvmsfatgw nqlgqtgvll ggardyfltw ektaslnaga
      661 eigflknrit vnvdyfnkrs idliyakplp gstgntsitt nvgalrnygw efdisslnis
      721 sdkfqwrtsl nltfeknrit kltqesfing tkrwevgssl ydfflvewag vdtktgmgtw
      781 wydkkdaqgn vtrekttdyn lanaeaskry mgsslpkfrg gftnsfkygs fdlnalfnfs
      841 fgsyiydssy aslmsgfssp gnqqsvdvkn awqkpgditn vpvnimannq nnalssrflf
      901 kndfirlksl tfgynvkedl letmgvssmr vflqgdnvwt wqshkgidpe qslagttnsr
      961 synlrtislg fsigf
//
LOCUS       WP_104916696             940 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_104916696
VERSION     WP_104916696.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..940
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104737
     Region          3..939
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkvlqvsc lvaafyfsad vhaqtkksdt itkekaieev vmigygsqkk envtgsigvv
       61 sakdladkpn pnpissiqgk vagvqiqnsg apggsprvdi rgisslsgkt vfivdgmitd
      121 disflnpqdv esmsilkdps slaifgaras ngaviiktks gknktvfnfs syigvktvtn
      181 vpkmansdqy velyneklrn egvtdptkfi sranypantn wfdevlktgf itsndfsasg
      241 tlakklnyfa sigylddggt laagrgvnsg nnfqrlntra nltykinnni svgnnftwsh
      301 intniasnpl laaygappvy ypvnpatgny dpfslislan pratldllrs kekqdrilnn
      361 vwaevkflkd fsfkvsytid htnsykyeyn ainnynpnqt ptrsnlitrd trtegyvwdn
      421 ilswkknfnq hhlevlggfs rtqnyyhgvy skvfdipytg hdrdlvlsng vdlvtftfnk
      481 dvdmvpyknr ieslfgrlny dyagkylvna svrrdgatgf ssnnrfktfp avsvgwvisk
      541 egfmsnqnlf nllklraswg klgnpdvrrd ydklttiins gayfggtgnp aetvtrvvnp
      601 nidwetttgr digvemalln nklkieatyf dkdsknvvya inqpsisgas nwndfvtnay
      661 sfnnrgfeas vnydtkisen irlgvyanit tiknkitsvy ldsfnepgah lfgstiirlq
      721 tgqpvgsyyg yqvagvfqnq aeingapqqt naavggfrfa dldgngvida rdktflgspi
      781 pkytygfgfn lsvydfdfam dfqgvqgnki ynynreqryg nenwdldfyk nrwqgagtsn
      841 sypmttnnqa iilpssffve dgsffrirni qlgytlpkef tkqlsvqklr lyfsaqnpwt
      901 sfkyngfspe imnsdrvqmg idnniypisa iytfgmnltf
//
LOCUS       WP_104919897             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Escherichia].
ACCESSION   WP_104919897
VERSION     WP_104919897.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53593
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta aptkpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdgkd gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tvgihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr ilgtaldkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_104965376             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            fluvialis].
ACCESSION   WP_104965376
VERSION     WP_104965376.1
KEYWORDS    RefSeq.
SOURCE      Vibrio fluvialis
  ORGANISM  Vibrio fluvialis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Vibrio fluvialis"
                     /db_xref="taxon:676"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54452
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp tsveqliklg fevalesqag slasfedtay eaagakvvsk
       61 ddvwqsdivl kvnapvsnee vdeisllkeg atlisfiwpa qnpelmeklt vkninvmamd
      121 cvprisraqa ldalssmani agyravveaa hefgrfftgq itaagkvppa kvfvagagva
      181 glaaigaags lgaivrafdv rpevkeqvqs mgaeflevdy kensgsgdgy akemsddfnk
      241 kaaelyaaqa kdvdiiitta lipgkpapkl vtkemvdsmk pgsvvvdlaa anggnceytv
      301 kdqvfvtpng vkiigytdmv grlptqssql yatnlvnllk llckekdgni dinfedvvlr
      361 gvtvvkggei twpappiqvs aqpqqqakaq pikekkveep vspikklagl vigvgafawi
      421 asvapaaflg hftvfvlacv vgyyvvwnvt hslhtplmsv tnaisgiivv gallqigqgn
      481 gavtflafia vliasinifg gftvtkrmle mfrkn
//
LOCUS       WP_104972607             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            diabolicus].
ACCESSION   WP_104972607
VERSION     WP_104972607.1
KEYWORDS    RefSeq.
SOURCE      Vibrio diabolicus
  ORGANISM  Vibrio diabolicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio diabolicus subgroup.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio diabolicus"
                     /db_xref="taxon:50719"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54574
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agesrvaasp ksveqliklg fdiaiesqag vlasfddaay eaagakivss
       61 eevwasglil kvnapivdee qgideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaefltv dfqedsgsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgkpap klitkemvds mkagsvivdl aaanggncey
      301 tvkdqvimtd ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 irgvtvvkeg eitwpappiq vsaqpqvkqe qpakpepkve epasptkkii gvaaavgafa
      421 wiasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvsflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_104973691             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            diabolicus].
ACCESSION   WP_104973691
VERSION     WP_104973691.1
KEYWORDS    RefSeq.
SOURCE      Vibrio diabolicus
  ORGANISM  Vibrio diabolicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio diabolicus subgroup.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio diabolicus"
                     /db_xref="taxon:50719"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54532
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agesrvaasp ksveqliklg fdiaiesqag vlasfddaay eaagakivss
       61 eevwasglil kvnapivdee qgideiallq dgatlvsfiw paqnaglmeq lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaefltv dfqedsgsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgkpap klitkemvds mkagsvivdl aaanggncey
      301 tvkdqvimtd ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 irgvtvvkeg eitwpappiq vsaqpqvkqe qpakpepkve eptsptkkii gvaaavgafa
      421 wiasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvsflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_104980689             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            alginolyticus].
ACCESSION   WP_104980689
VERSION     WP_104980689.1
KEYWORDS    RefSeq.
SOURCE      Vibrio alginolyticus
  ORGANISM  Vibrio alginolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio alginolyticus"
                     /db_xref="taxon:663"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54576
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agesrvaasp ksveqliklg fdvaiesqag vlasfddaay eaagakivss
       61 eevwasglil kvnapivdde qgideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaefltv dfqeesgsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgkpap klitkemvds mkagsvvvdl aaanggncey
      301 tvkdqvimtd ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 irgvtvvkeg evtwpappiq vsaqpqvkqe qpvkpepkve eptsptkkii gvaaavgafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvsflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_104999465             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. PGP41].
ACCESSION   WP_104999465
VERSION     WP_104999465.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. PGP41
  ORGANISM  Arthrobacter sp. PGP41
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Arthrobacter sp. PGP41"
                     /db_xref="taxon:2079227"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40197
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigiprerr egerrvaatp etvkqlaalg vevlleedag aaagypdlay tqagvrlvre
       61 ldlaqldvla hvrpldpeta rslkrgavtv glaspsselp tvealadagv tafalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplymtaa gtvpparvlv lgagvaglqa
      181 igtakrlgar vfandirpas adevasmggt fvrldveaae aaggyarqls sdagtrqrql
      241 laphvaqadv littaavpgr rapllvttem vqgmragsvv vdlaaesggn veavvpgqdv
      301 svptadgsgf vtlvglkdap samasdasrl yaknvanlla lmvrdgalip dfgdevlaga
      361 clthdgevrh rptaellaer agsrregvl
//
LOCUS       WP_105007384             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            leguminosarum].
ACCESSION   WP_105007384
VERSION     WP_105007384.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39145
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare itgeetrvaa saetvkkmks fgfdvvveag agaasripde efgaagarig
       61 sfadaasadv vlkvrrpsgs eisgyksgav iiaimdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsanyqa
      241 kqaalvaehi tkqdivitta lipgraaprl vshamlasmk sgavavdlav erggniegvv
      301 pgeiadvegv rvigfanmpg rvatsasaly aknlvtflet mvnketrsvv vnlddelvka
      361 tmltyagdvv hpafggakkg di
//
LOCUS       WP_105013492             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Salinibacter sp. 10B].
ACCESSION   WP_105013492
VERSION     WP_105013492.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter sp. 10B
  ORGANISM  Salinibacter sp. 10B
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Salinibacter sp. 10B"
                     /db_xref="taxon:1923971"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41242
     Region          4..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maftigipre teadetrvsl vpevasrllk mregldivve sgagakafhr ddayeeagct
       61 vvdradafda dlvakvapps edeldffseg qalvglldpl nrpeaaqtla ergvtsfame
      121 lvprisraqk mdalsamssi ggyraavlaa erlprffpll ttaagtvkpa qvlvlgagva
      181 glqaiatakr lgarvfgydi reptreeves lgakfvelev didgdqdesg yaeelekekq
      241 erqpellkph laeadvvist alipgrpapl linenavaam dpgsvivdla apnggncaht
      301 qagetvvkee vrimgptnlp aqmpvhasql yaktisatie efvedgtitp dfddeifdga
      361 clthdgevrn ervrealglg epateee
//
LOCUS       WP_105028184             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Limnobacter].
ACCESSION   WP_105028184
VERSION     WP_105028184.1
KEYWORDS    RefSeq.
SOURCE      unclassified Limnobacter
  ORGANISM  unclassified Limnobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Limnobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="unclassified Limnobacter"
                     /db_xref="taxon:2630203"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39579
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaetr sgetrvaatp etvkklisqk hevfvqagag iassitdqay sdvgativdr
       61 amdvisncdm ilkvrapaen elsayragqv vvgmlnpfdn asleamnkag ltafaleaap
      121 rttraqsmdv lssqaniagy kavmiaanvy qrfmpmlmta agtvkaarvl ilgvgvaglq
      181 aiatakrlga vieasdvrpa tkeqveslga kfvdvpfesd eereiaqgvg gyarpmpesw
      241 mkrqaaavhd kaiksdivit talipgrkap tllheetvra mkpgsvvidl aveqggncpl
      301 sklneivdvn gvkivgyanl aamvaadasa lyarnvidfl klvfdkegaf kidmeddiva
      361 aclmctggel krkna
//
LOCUS       WP_105038444             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Flavipsychrobacter stenotrophus].
ACCESSION   WP_105038444
VERSION     WP_105038444.1
KEYWORDS    RefSeq.
SOURCE      Flavipsychrobacter stenotrophus
  ORGANISM  Flavipsychrobacter stenotrophus
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavipsychrobacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Flavipsychrobacter stenotrophus"
                     /db_xref="taxon:2077091"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39470
     Region          1..359
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,89,284,310,312)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,122..123,132..133,136..137,140..141,143..144,
                     146..151,153,155..157,160,183..184,274..275,317..318,322,
                     325..326)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(117..118,122,125,128,169..172,192..194,224,235,
                     252..254,261,263)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,122,132,175..176,183,199..200,202..205)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(152..156,159,162,185,187)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigvlkeqa petrvslvpe vvaafvkmgv tvwieqgagd tsfygnqlyi nagaeiksgt
       61 diratadmvl tiqatnagev kpgavlmgiy qplfnpeqml awagkghtvf sldtiprttr
      121 aqsmdvlssq aniagykavl laafqysryf pmfmtaagsi ppakvlilga gvaglqaiat
      181 arrlgavvev fdtrpavkee vmslgakfve vegaadaska ggyaveqsed fqrkqkekih
      241 ehakksdiii ttaqipgkka pilittamie dmragslivd lasvtggnte ltqndkavmy
      301 ngvtiignsa laattpadas klysknvlnf akliinkegg inlnfeddiv kgtcitsegk
      361 ivnervgall tvas
//
LOCUS       WP_105053395             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychrosphaera saromensis].
ACCESSION   WP_105053395
VERSION     WP_105053395.1
KEYWORDS    RefSeq.
SOURCE      Psychrosphaera saromensis
  ORGANISM  Psychrosphaera saromensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Psychrosphaera.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Psychrosphaera saromensis"
                     /db_xref="taxon:716813"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53893
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkeil kgerrvattp dvvkkltklg fdvaietcag eaanytdday idagceivns
       61 akalwqqsdi vlkvqapeae esallksgqt licflwpaqn pkmlkelter gvtaiaidsi
      121 prisraqkmd arssmanisg yraiveaaqh fgrfftgqit aagkvapakv lvigagvagl
      181 aaigaaksmg aivrsfdsra evkeqiesmd aeflmldfkd edgsgeggya kvmsdeftka
      241 emalfaaqak dvdiivttal ipgkpapkli tsdmvasmkh gsvivdlaae qggnceltvp
      301 gevavvegvs iigytdlpsr laaqssqlys nnlhnllaem tpdkdgnlvi dmtndvvlga
      361 ticlegkttw pppaptlsva pkkpttktvt pvvvekkksi lgpiigatvg alallglgav
      421 apasfmshft vfvlacfvgy mviwsvspal htplmsvtna issiivigal iqisstdeti
      481 kwfavftvli asinivggfa vthrilkmfr k
//
LOCUS       WP_105054967             479 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aliivibrio sifiae].
ACCESSION   WP_105054967
VERSION     WP_105054967.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio sifiae
  ORGANISM  Aliivibrio sifiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Aliivibrio sifiae"
                     /db_xref="taxon:566293"
     gene            1..479
                     /gene="nrfA"
     Protein         1..479
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53373
     Region          1..471
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkkqwtrrsa aaiamvttll lsshsfaase ktervdprne ayakehaeqy kswratsdsv
       61 qiedalaedp nmvimwagyg fakdynkarg hfyaiddvre tlrtagptda nsgpmpmacw
      121 sckspdvgrv ieekgedgyf sgkwarlgse iqnpigcadc hdtrseefkn gepalaitkp
      181 hveramdaig kpfgdqsrld qqasvcgqch veyyftgktk avkfpwdkgt svdemeeyyd
      241 eigfsdwthk vskapmlkaq hpgyetwrdg ihgknkvtcv dchmpkvtne dgtvytdhkv
      301 gnpfdrfedt caschtqske mlqgvvasrk aqvlkmklta erqivaahfe agaawdagat
      361 ktemepilld irhaqwrwdy aiashgihmh apeialevlg tavdkaadar tklirllakk
      421 gitepvaipd istkaaaqka lgmdmegmea ekkhfletvv pkweheaker eskdyapie
//
LOCUS       WP_105062958             479 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aliivibrio sifiae].
ACCESSION   WP_105062958
VERSION     WP_105062958.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio sifiae
  ORGANISM  Aliivibrio sifiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Aliivibrio sifiae"
                     /db_xref="taxon:566293"
     gene            1..479
                     /gene="nrfA"
     Protein         1..479
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53318
     Region          1..476
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkkqwtrrsa aaiamvttll lsshsfaase ktervdprne ayakehaeqy qswrstsdsv
       61 qiedalaedp nmvimwagyg fakdynkarg hfyaiddvrq tlrtagptda nsgpmpmacw
      121 sckspdvgrv ieeqgedgyf sgkwarlgse iqnpigcadc hdtrsegfkn gepalaitkp
      181 hveramdaig kpfgdqsrld qqasvcgqch veyyftgktk avkfpwdkgt tvdemeeyyd
      241 eigfsdwthk vskapmlkaq hpgyetwreg ihgknkvtcv dchmpkvtne dgtvytdhkv
      301 gnpfdrfedt canchtqske mlqgvvasrk aqvikmklta erqivaahfe agaawdagat
      361 kaemepilld irhaqwrwdy aiashgihmh apeialevlg tavdkaadar tklvrllakk
      421 gitdpiaipd istkaaaqka lgmdmegmsa ekkhfletvv pkweneaker eskdyepik
//
LOCUS       WP_105062246             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Photobacterium angustum].
ACCESSION   WP_105062246
VERSION     WP_105062246.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium angustum
  ORGANISM  Photobacterium angustum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Photobacterium angustum"
                     /db_xref="taxon:661"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54868
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprevl ahetrvaatp ktveqilkmg fsvvveqgag rlasfddaay eaagatvvst
       61 devwqsdlif kvnapqvnpe tgvdefelik egaslvsfiw paqnpellek lsskninima
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaeflev dykedtstgd gyakemsdef
      241 nkaaerlyae qakdvdiiit talipgrpap klitkemvds mksgsvivdl aaanggncay
      301 teadkvvttp ngvkvigytd mvgrlptqss qlygtnlvnl lkllckekdg nidinfddev
      361 lrgltivkag eltwpappik vsaaaqqpka aakvepkvee paspvkkfgl mgagialfaw
      421 vanyapaefl ahftvfvlac vvgyyvvwnv shslhtplms vtnaisgiii vgallqigqg
      481 ngvvsflafi avliasinif ggftvtkrml emfrkdk
//
LOCUS       WP_105068757             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            jasicida].
ACCESSION   WP_105068757
VERSION     WP_105068757.1
KEYWORDS    RefSeq.
SOURCE      Vibrio jasicida
  ORGANISM  Vibrio jasicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio jasicida"
                     /db_xref="taxon:766224"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53094
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmstp iavatlfasq lflvgaplaa edkglidprn dafeqnhpdq yhswkatses
       61 eyiedalged pnmvilwagy gfakdynkar ghfyalddvr qtlrtgaptd eksgpmpmac
      121 wsckspdvar vidergedgy fegkwarlgs eivnpigcsd chdtrseefk ngepalavtr
      181 pyverafdti gkkfdeqsrl dqqasvcaqc hveyyftgpt kavkfpwdmg tsvndmekyy
      241 dalnfkdwth avskapmlka qhpgyetwre gihgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfdd tcaqchtqtk eqlqgivstr kaqvlnmklt aekqivaahf eagaawdaga
      361 teeemqpilq dirhaqwrwd yaiashgvhm hapevalevl gtavdraada rtklvrllak
      421 kgitepvqip distkakaqq algmdiekmn adkkdfleti apdwdkaaae reaty
//
LOCUS       WP_105066027             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            campbellii].
ACCESSION   WP_105066027
VERSION     WP_105066027.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54468
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agesrvaasp ksveqliklg fdvaiesqag glasfddaay eaagakivss
       61 eevwtsglil kvnaplvdee kgideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgkpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqvitta ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg nididfedvv
      361 lrgvtvvkeg evtwpappiq vsaqsqakpq epvkpqpkve eptspvkkfg alavglgafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_105072966             363 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Chromatium
            okenii].
ACCESSION   WP_105072966
VERSION     WP_105072966.1
KEYWORDS    RefSeq.
SOURCE      Chromatium okenii
  ORGANISM  Chromatium okenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Chromatium.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Chromatium okenii"
                     /db_xref="taxon:61644"
     Protein         1..363
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38232
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipretr lgetrvastp dvvkkliskg ftlnveagag isagypdtdy sqagaqltdr
       61 agaydvdlll kvrrpdaddv aamrsgglli alletcgadd ilsemlnknm rvlgmermpr
      121 tsraqsmdal ssqsnlagyr atleaaaryg rffpmmmtsa gsskparvvv lgagvaglqa
      181 iatarrlgad vhaydvrpet qeqirslgak pivldlgesg ageggyarel saeakaiqqi
      241 algdelakah viittalipc rpapvlvtae vvermrpgsv ivdlaaangg ncpltiadei
      301 vqhqgvtivg itnfpalipa dasafyarnl fnlieimfef saappqlkdl dadditaaml
      361 ikk
//
LOCUS       WP_105076419             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_105076419
VERSION     WP_105076419.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53588
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkli qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_105078064             274 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Escherichia coli].
ACCESSION   WP_105078064
VERSION     WP_105078064.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>274
                     /product="STM4504/CBY_0614 family protein"
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnkn
//
LOCUS       WP_105095488             104 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105095488
VERSION     WP_105095488.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..104
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11243
ORIGIN      
        1 mkqlvtkrsy kiglsamalv llmttaggat ahaskgtysv etrgdakvyr lleaptesfa
       61 qggivlkpvn nsttkpsetk swfdsfwssv ktfweafcrg vgwc
//
LOCUS       WP_105105417             104 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105105417
VERSION     WP_105105417.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..104
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11498
ORIGIN      
        1 mkqlvtkhsy kiglsamalv llmttagsat ahastgtysv etrdddkiyr llekpaesfe
       61 qgsvvlkpvn npitkpsepk swfasfwssv ktfweafchr vgwc
//
LOCUS       WP_105095489             108 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105095489
VERSION     WP_105095489.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..108
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11588
ORIGIN      
        1 mkhivtkrny kvgacamala llmttaggav vnadqrlesp agfvqrgdvl lklkesnqtf
       61 negevsnvep inspmpqvap svqkswfgsf wggvkkfwka lccgvgwc
//
LOCUS       WP_105103411             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbulbifer pacificus].
ACCESSION   WP_105103411
VERSION     WP_105103411.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer pacificus
  ORGANISM  Microbulbifer pacificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Microbulbifer pacificus"
                     /db_xref="taxon:407164"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54015
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miiaipketa pgearvaatp asvlrlqtlg fdvvieqgag eaasfpdaey ekagakican
       61 aadclsqagl vlkvqgptda elelipagat lisflkpaqn gellqkladk ninalavesi
      121 prisraqkmd alssmaniag yravieaahe fgrfftgqit aagkippakv lvigagvagl
      181 saigtaksmg aivrafdtrp evreqvesmg aefltveiee dgsgtggyak qmskefidae
      241 malfreqake vdivittali pgkpapklwl admvdtmang svvvdlaaem ggncdytead
      301 kkvvksgvti lgytnlasra atqsstlyat nlchllsdmt pekdgqinin fddeairgat
      361 vvkegsitwp ppapklsaap qkpkeaapqi kvepkpekks splslvafwa vagalllalg
      421 ksapadfvah ftvfvlsifi gwqviwnvsh alhtplmsvt naisgiviig allqvgatgs
      481 llvtvmafva vlfasinifg gffvthrmlk mfrr
//
LOCUS       WP_105115087             124 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105115087
VERSION     WP_105115087.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..124
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=13226
ORIGIN      
        1 mkhivtkrsy kvgacamala llmttaggav vnantdvian teqslksdyg fsngggsgsv
       61 lierkeltep vnkgvyhvep inhsesqmdp segqsswfgs fwggvktfwk klccavglpw
      121 ckvk
//
LOCUS       WP_105121471             108 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105121471
VERSION     WP_105121471.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..108
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11521
ORIGIN      
        1 mkhivtkcny kvgacamvla llmttaggav vnaeqdlkst gtisergnsv lvatpalnks
       61 fqnngvnqle sinqkmdpsv qkswfgsfwg hvktfwkalc cavgltrc
//
LOCUS       WP_105121472             104 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105121472
VERSION     WP_105121472.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..104
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11324
ORIGIN      
        1 mkqlvtkrsy kiglsamalv llmttaggtt ahastgtysv etrgdakvyr llektaksfa
       61 qgdivlksvn nsttkpsetk swfdsfwssv ktfweafcrg vgwc
//
LOCUS       WP_105121473             111 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105121473
VERSION     WP_105121473.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..111
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=12129
ORIGIN      
        1 mkrivtkrsy kvglcamalv llmstaggvt agaqghnfts sdssamrntq vlvkgntsnr
       61 sshdgpvkia mpraagsknq ktwyeslwst ikkffeqlrh gfhlerlfkn g
//
LOCUS       WP_105123720             105 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105123720
VERSION     WP_105123720.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..105
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11408
     Region          <13..88
                     /region_name="flgE"
                     /note="flagellar basal body protein FlaE; PRK06803"
                     /db_xref="CDD:235862"
ORIGIN      
        1 mkqlvkkrsy kiglsamala llmttaggat ahastdtysv ethgetkvyr llensagsft
       61 qgnvvlktvn npttepsetk swfasfwssv ktfweafcyg vgwck
//
LOCUS       WP_105123721             112 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105123721
VERSION     WP_105123721.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..112
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=12255
ORIGIN      
        1 mkrivtkrsy kvglcamala llmstaggvt agaqghkfts sdssamrntq vlvkgntsnr
       61 ssvktlkvat prmaltssgk astwhdyfqk tfknfckafr dgfglyrlfk fw
//
LOCUS       WP_105125910             122 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105125910
VERSION     WP_105125910.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..122
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=13463
ORIGIN      
        1 mkrivtkrsy kvglcamala llmstaggvt agaqdyhvts sgelkpmskg vfmklessst
       61 pientgvtel rsinsqnads anssdswfwn lwkkfktvfk tfidsgvrrg fgvknlfknk
      121 ww
//
LOCUS       WP_105134748             123 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105134748
VERSION     WP_105134748.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..123
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=13205
ORIGIN      
        1 mkhivtkrsy kvgacamala llmttaggav vnantdvnsn teqsltskyg fsdgggkhnv
       61 llerkeqtes fnhgvgdves inypsgsqmd qsswfgsfwk gvqrlwnalc gsvgltwckv
      121 qvk
//
LOCUS       WP_105132798             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. BE12].
ACCESSION   WP_105132798
VERSION     WP_105132798.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BE12
  ORGANISM  Burkholderia sp. BE12
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia sp. BE12"
                     /db_xref="taxon:2082394"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39113
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiakgag saasypdeay aaagaeltdq
       61 saafgadlvl kvqaptdtel pllkrgavlv gmlepfngeq aaklaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgvggy arpmppswlg
      241 rqaalvhera rqadivitta lipgrpaptl isvetaqsmk pgsvlvdlaa grgpeidgrr
      301 ggncpltvad qvvvhngvti agytnlasmv asdasalyar nlldfmkliv tkegtlnidl
      361 tddivaatll crdgevtrk
//
LOCUS       WP_105134749             112 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105134749
VERSION     WP_105134749.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..112
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=12283
ORIGIN      
        1 mkqlvtkhsy kiglsamala llmttaggav ahaethaety yyssdkgset htsnvqtnig
       61 gfsegvvtte sinnsnshre qnkslgsrfw dglkrfwssw ccgfglkwlk fe
//
LOCUS       WP_105135652             108 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105135652
VERSION     WP_105135652.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..108
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11889
ORIGIN      
        1 mkqlvtkrsy kiglsamalv llmttaggav ahaetyyyss dkgsethtsn vqtniggfsd
       61 gvvtiesinn snshreqnks lgsrfwdglk rfwsswccgf glkwlkfe
//
LOCUS       WP_105139413             104 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SSU0592/SSU0593 family protein [Streptococcus].
ACCESSION   WP_105139413
VERSION     WP_105139413.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     Protein         1..104
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11290
ORIGIN      
        1 mkqlvtkrsy kiglsamala llmttaggat ahastetysv etrgdtkvyr lleapaesfa
       61 qgsivlkpvn nsttkpsetk swfdsfwssv ktfweafcrg vgwc
//
LOCUS       WP_105139414             122 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SSU0592/SSU0593 family protein [Streptococcus].
ACCESSION   WP_105139414
VERSION     WP_105139414.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     Protein         1..122
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=13620
ORIGIN      
        1 mkrivtkrsy kvglcamala llmstaggvt agaqdysvks sgtlkpigyk vfmitehsps
       61 ytmnegvenl rsingqdads anssdswfwn lwkkfktvfq kfihsgvrrg fgvknlfnnr
      121 ww
//
LOCUS       WP_105140294             104 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105140294
VERSION     WP_105140294.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..104
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11206
ORIGIN      
        1 mkqlvtkhsy kiglsamala llmttaggat ahastdtysv etqgetkvyr llensagsft
       61 qgnvvlkpvn nsttepsetk swfvsfwssv kkfweafccg vgwc
//
LOCUS       WP_105140293             109 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105140293
VERSION     WP_105140293.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..109
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11692
ORIGIN      
        1 mkhivtkrny kvgacamala llmttaggav vnantdqhle ssvgfeqsge vllkqkelpk
       61 avdpgvqnle sinqkmapse pkswfgsfwg gvqrlwralc cglgfcpsr
//
LOCUS       WP_105142649             104 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105142649
VERSION     WP_105142649.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..104
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11330
ORIGIN      
        1 mkqlvtkrsy kiglsamalv llmitaggat ahastetysv etrgdakvyr lleaptesfa
       61 qgsivlkpvn nsttkpsetk swfdsfwssv ktfweafcrg vgwc
//
LOCUS       WP_105142944             118 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105142944
VERSION     WP_105142944.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..118
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=13049
ORIGIN      
        1 mkhivtkrsy kvglcamala llmstaggvt agaqghnfts sdssgmrntq vlvkgntsnr
       61 ssvktlkvat prvasltssk rsetwsdyiq ekfknlkkaf wlgfgikqlf kiswwrfw
//
LOCUS       WP_105142945             104 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105142945
VERSION     WP_105142945.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..104
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11453
ORIGIN      
        1 mkqlvtkhsy kiglsamala llmttaggat ahastdtysv etqgddkiyr llenptesfa
       61 qgivflkpvn npttkpsetk swfdsfwssv ktfweafcrg vgwr
//
LOCUS       WP_105147934             120 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105147934
VERSION     WP_105147934.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..120
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=13299
ORIGIN      
        1 mkrivtkrsy kiglcamala llmstaggvt agaqdysvks sgtlkpigyk vfmitehsps
       61 ytmnegvenl rsingqdads vnssdswfwn lwkkfktvfq tfiekgvrrg fgiqrlfgfk
//
LOCUS       WP_105152576             126 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105152576
VERSION     WP_105152576.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..126
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=13939
ORIGIN      
        1 mkrivtkrsy kvglcamala llmstaggvt agaqdysvks sgalkpigng tfmkmeysaf
       61 pkdtpienng vtelrainsq nadsanssds wfwnlwkkfr tvfqkfidsg vrrgfgvknl
      121 fknkww
//
LOCUS       WP_105152577             118 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105152577
VERSION     WP_105152577.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..118
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=12613
ORIGIN      
        1 mkhivtkrsy kvgacamala llmttaggav vnanteqslk sdygfsnggg sgsvlierke
       61 ltepvnkgvy hvepinhses qmdpsegqss wfgsfwggvk tfwkklccav glpwckvk
//
LOCUS       WP_105155228             106 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105155228
VERSION     WP_105155228.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..106
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11678
ORIGIN      
        1 mkqlvakrsy kiglsamalv llmttaggat ahahasrdty svetrgddki yrllenptes
       61 faqgsvvlkp vnnpitkpse pkswfasfws svktfweafc hrvgwc
//
LOCUS       WP_105155229             109 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105155229
VERSION     WP_105155229.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..109
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11756
ORIGIN      
        1 mkqlvtkrsy kiglsamalv llmttaggav ahaeeitvyi spkgsesfis vekpniggfa
       61 egvvttesin nsnshreqnk slgsrfwdgl krfwsswccg fglrglksk
//
LOCUS       WP_105155509             116 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105155509
VERSION     WP_105155509.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..116
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=12721
ORIGIN      
        1 mkqlvtkhsy kiglsamala llmttaggav ahaethaeth aetyyyssdk gsethtsnvq
       61 tniggfsegv vttesinnsn shreqnkslg srfwdglkrf wsswccgfgl kwlkfe
//
LOCUS       WP_105155907              78 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein, partial [Streptococcus suis].
ACCESSION   WP_105155907
VERSION     WP_105155907.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..>78
                     /product="SSU0592/SSU0593 family protein"
ORIGIN      
        1 mkhivtkrny kvgacamvla llmttaggvv vnaeqrlnsq fgfeqrdevl leikgpkqsf
       61 neggvgnles inspmpqv
//
LOCUS       WP_105156529             105 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105156529
VERSION     WP_105156529.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..105
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11399
ORIGIN      
        1 mkqlvkkrsy kiglsamala llmttaggat ahastdtysv etqgetkvyr llensagsft
       61 qgnvvlktvn npttepsetk swfasfwssv ktfweafcyg vgwck
//
LOCUS       WP_105157792             107 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein, partial [Streptococcus suis].
ACCESSION   WP_105157792
VERSION     WP_105157792.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         <1..107
                     /product="SSU0592/SSU0593 family protein"
ORIGIN      
        1 nykvgacama lallmttagg avvnanthqs fessygfsgr ggdggvllkl kgptesvnqg
       61 vgnvepvnpp vtqmapsepk swfgsfwggv qrlwralccg lgfcpsr
//
LOCUS       WP_105157361             104 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105157361
VERSION     WP_105157361.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..104
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11440
ORIGIN      
        1 mkqlvtkhsy kiglsamala llmttaggat ahastgtysv etrdddkiyr llekpaesfe
       61 qgsvvlkpvn npitkpsepk swfasfwssv ktfweafchr vgwc
//
LOCUS       WP_105157997              95 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein, partial [Streptococcus suis].
ACCESSION   WP_105157997
VERSION     WP_105157997.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..>95
                     /product="SSU0592/SSU0593 family protein"
ORIGIN      
        1 mkrivtkhsy kvslcamala llmstaggvt agaqdysves sgalkpigng tfmkmeysaf
       61 pkdtpienng vtelrainsq dadsanssds wfwnl
//
LOCUS       WP_105161423             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_105161423
VERSION     WP_105161423.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38700
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay eaagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklaehgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_105180823             312 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudoalteromonas sp. T1lg21].
ACCESSION   WP_105180823
VERSION     WP_105180823.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. T1lg21
  ORGANISM  Pseudoalteromonas sp. T1lg21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudoalteromonas sp. T1lg21"
                     /db_xref="taxon:2077095"
     Protein         1..312
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36781
     Region          5..174
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 meykiyskrq kelrgevhdv fqyhllpqsl riqikflldg llgdesnyny epnvrevytq
       61 iynflreelg rfdlnnqnsk iekynanayv elntflinek nielvlsyve yafilaeiyt
      121 seyefrnknl edkmeeslkt lnlrfrengv gfafeeshii rvdsmlmhee vikpalklln
      181 mkeyevtqdy flnayehyrh kkyneaivec nkafestmki icmnqkwelk gnesasklia
      241 aclknklipd ywqtqlssln smlssgipti rnkyshgqda lqeqapeelv gyiihttast
      301 iifliesqkr lh
//
LOCUS       WP_105182755             108 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105182755
VERSION     WP_105182755.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..108
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11891
ORIGIN      
        1 mkqlvakrsy kiglsamtlv llmttaggav ahaetyyyss dkgsethtsn vqtniggfse
       61 gvvttesinn snshreqnks lgsrfwdglk rfwsswccgf glkwlkfe
//
LOCUS       WP_105183187              98 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105183187
VERSION     WP_105183187.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..98
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=10651
ORIGIN      
        1 mkhivtkrny kvgacamala llmttaggav vnaeeitvyt spkgsesfis vektniggfs
       61 egdiktepmn kreepqmfpp sksgfdwfwg glktfwns
//
LOCUS       WP_105183188             102 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105183188
VERSION     WP_105183188.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..102
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11109
ORIGIN      
        1 mkqlvtkrsy kiglsamalv llmttaggat ahastdtysv vtegettkyi llenkvedpf
       61 nngqiknlss vnpsisskee cswisslwkg ligllnrifw ie
//
LOCUS       WP_105191651             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Amnimonas
            aquatica].
ACCESSION   WP_105191651
VERSION     WP_105191651.1
KEYWORDS    RefSeq.
SOURCE      Amnimonas aquatica
  ORGANISM  Amnimonas aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Amnimonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Amnimonas aquatica"
                     /db_xref="taxon:2094561"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38679
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaetl agetrvaatp etvkkfaalg cevlvqagag lassatdaay eaagakvvat
       61 aadalanadf vlkvaaptae eaalmkqgat vlaafaphan phfdayaarg ltcvamelip
      121 ritraqssdi lssqanlagy kavllaaney aglfpmmmta agtikpariv vlgvgvaglq
      181 aiatgkrlga vveasdlrpa akeqveslgg rwldvpmsde ekakalgtgg yawqpspeyi
      241 rdqaavvdka vsqanivitt aqipgrkapv lvkaetvakm kpgsviidma vgsggnvegs
      301 apdqtvvten gvrivgisni palvateasa lyarnllnfl apmhdkesgr ivlnreddmv
      361 kptlvvdsgt viykkpn
//
LOCUS       WP_105201749              87 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein, partial [Streptococcus suis].
ACCESSION   WP_105201749
VERSION     WP_105201749.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..>87
                     /product="SSU0592/SSU0593 family protein"
ORIGIN      
        1 mkrivtkrsy kvglcamala llmstaggvt agaqdyhves sgalkpigng tfmkmeysaf
       61 pkdtpienng vtelrsvnsq nadsvns
//
LOCUS       WP_105202294             116 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105202294
VERSION     WP_105202294.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..116
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=12094
ORIGIN      
        1 mkhivtkrny kvgacamala llmttaggav vnaeqrltst gnisergdsv llatpaqnqg
       61 fqnggvhnle sinspmhqva psgqksswfg sfwggvktfw nalccsvglt glkvsk
//
LOCUS       WP_105217339             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Pukyongia
            salina].
ACCESSION   WP_105217339
VERSION     WP_105217339.1
KEYWORDS    RefSeq.
SOURCE      Pukyongia salina
  ORGANISM  Pukyongia salina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Pukyongia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pukyongia salina"
                     /db_xref="taxon:2094025"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40012
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtigilketq kgetrvaisp niakqliekd fkviveedag ttssfkdsdy skvgaqiekr
       61 gvvfkdsdll lkinpfdqed lklvdkrhil msqlfhksnp elmkaiaatg atafsldamp
      121 risraqdmdv lssqsnlagy kavirgayem tkifplmmta agtitparvl vygvgvaglq
      181 aiatakrlga iveatdirpe tkeqteslga kfievegngd eeasvyakva seeymkkqke
      241 avnkslfqad lvittamvpg rkspvlitke qvgqmkngav iidlaaaqgg ncalskmnki
      301 vvkngvkiig ttispesvst naselfgknm ynfimhlten aafkwdleee itdatliiqn
      361 gtirkngvtt
//
LOCUS       WP_105219913             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Gloeocapsopsis dulcis].
ACCESSION   WP_105219913
VERSION     WP_105219913.1
KEYWORDS    RefSeq.
SOURCE      Gloeocapsopsis dulcis
  ORGANISM  Gloeocapsopsis dulcis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Chroococcaceae;
            Gloeocapsopsis.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Gloeocapsopsis dulcis"
                     /db_xref="taxon:2859516"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41038
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavareie vgerrvalip dtvarlvkkg ievwveagag essfftdtdy etagakivtd
       61 tdalwheadv llkvgipker edgrlevdll regavlisfl nplgepaiaq rlaqrqvtal
      121 smemiprttr aqsmdalssq asiagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vqlnedtvad ggyakevsea
      241 akqrtqevva ehikqsdvvi ttaqvpgkka pilvteemva qmkpgsvvvd iaaeqggnca
      301 ctkpgkdvqy ngvtiigpin lpssmpvhas qlyaknlfsl vqllikdsnl dvnfaddivs
      361 aacithagei rnqrvkeala tlssatag
//
LOCUS       WP_105235426             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Marivivens
            donghaensis].
ACCESSION   WP_105235426
VERSION     WP_105235426.1
KEYWORDS    RefSeq.
SOURCE      Marivivens donghaensis
  ORGANISM  Marivivens donghaensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Marivivens group; Marivivens.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Marivivens donghaensis"
                     /db_xref="taxon:1699413"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55613
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeil egenrvamtp asakdlqklg yecviesgag anagfsdemy keagvevvkt
       61 aaalfkavdi vakvriptda eikrlskgqt mitffnpgan eeglklaask gasviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlkkfrel apevdivitt alipnreape lwtedmvqam kpgsvivdla aekggncklt
      301 vkdekivtpn gvtiigytdf psrmaaqast lyatnirhmm tdltpnkdgv vvhnmeddvi
      361 rsstvthege itfpppplki qaiaaksqek pkeltpeekr aaevaafkaq tkqqvtllai
      421 ggaillaigl vapasfmqhf ivfvlsvfig fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgswl viilaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_105238028             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter spanius].
ACCESSION   WP_105238028
VERSION     WP_105238028.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter spanius
  ORGANISM  Achromobacter spanius
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter spanius"
                     /db_xref="taxon:217203"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38515
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkyvggk htvivergag aaaryldday vaagatlgsa
       61 qdalgaelvm kvrapapeel phmkpgtvvi gmldpfdaeg laqlaaaglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravil gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgtggy arpmppawma
      241 rqavlvserc kqadivitta lipgrpaptl vsadtvaamk pgsvlvdlav erggncplse
      301 kgqivekhgv tiigltnlpg lvatdasaly arnildflkl iinadgalai qrddeivaac
      361 lvceggnvtr rt
//
LOCUS       WP_105243429             124 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105243429
VERSION     WP_105243429.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..124
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=13666
ORIGIN      
        1 mkrivtkrsy kvglcamala llmstaggvt agaqdyhves sgalkpigng tfmkmeysaf
       61 pkdtpienng vtelrsvnsq nadsvnssds wfwnlwkkfk tvfqtfiekg vrrgfgiqrl
      121 fgfk
//
LOCUS       WP_105244937             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychrobacter sp. Marseille-P5312].
ACCESSION   WP_105244937
VERSION     WP_105244937.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter sp. Marseille-P5312
  ORGANISM  Psychrobacter sp. Marseille-P5312
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Psychrobacter sp. Marseille-P5312"
                     /db_xref="taxon:2086574"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40056
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvisadi asesrvaltp davkklrklg fevviqsgag qaayyadaly qaagadiass
       61 saeviaqsqi ittihdlpae vaehlssgqi vvgmldpyrn tqldtyaakg vtafamellp
      121 rtlsraqnmd vlssqanlag ykavllaane ysrpfpmfmt sagtvkpakv vilgvgvagl
      181 qaiatakrlg avveasdlrp aakeqveslg gkwldvpmsd deaqkakatg gyawtpseqy
      241 ikdqaavvdk alsnadivit taqipgrqap rlvhqatlak mkagsvlidm aagtggnveg
      301 sapnetvttd ngvrivgaan ipsqlaaqss dlyannlvnf ittliapaat ddasanklal
      361 nldmedeiqg alavthdnqv rltkr
//
LOCUS       WP_105248801              91 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein, partial [Streptococcus suis].
ACCESSION   WP_105248801
VERSION     WP_105248801.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..>91
                     /product="SSU0592/SSU0593 family protein"
ORIGIN      
        1 mkrivtkrsy kvglcamala llmstaggvt agakdyhvts sgelkpmseg vfmklesssn
       61 fienegivvk sisnqntnpn nlneswywkf w
//
LOCUS       WP_105250230             467 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella sp. WE21].
ACCESSION   WP_105250230
VERSION     WP_105250230.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. WE21
  ORGANISM  Shewanella sp. WE21
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Shewanella sp. WE21"
                     /db_xref="taxon:2029986"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52209
     Region          1..467
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mmkkmtgksf alsalvaasf maagamasdk teprnevykd kfknqynswh dtakseelvd
       61 aigqdpnmvi lwagyafakd ynaprghmya vtdvrntlrt gapknaedgp lpmacwscks
      121 pdvprlieeq gedgyfkgkw skggpevtnt igcgdcheks spklrisrpy adrafeaigt
      181 pfskaskqdk esmvcaqchv eyyfektddk knfvkfpwdm gttvekmevy ydsiqfsdwt
      241 halsktpmlk aqhpeyetwk mgihgmnnvs cvdchmpkvt saegkkftdh kvgnpfdrfe
      301 eicatchsqt keflvgvtne rkakvkemkl kaeeqlvkah feaeaawkag ateeemkpil
      361 tdirhsqwrw dlaiashgva ahapdealri lgtsvskaad arvklaqllg kkgitdpvai
      421 pdistkakaq aalgmdmkkm naekeafkkd mlpkwdeeak kreatyk
//
LOCUS       WP_105251577             508 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Shewanella].
ACCESSION   WP_105251577
VERSION     WP_105251577.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53358
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevvieanag qlssfddaaf eaagakvttn
       61 vwqadlifkv napsdaeieq ikdgativsf iwpaqnpelv aklskrkinv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggqfl kldfgneegg ssdgyaktms defiaaemal
      241 faeqakevdi iittalipgr papklitkam vdsmksgsvi vdlaaatggn ceytqsgelf
      301 vtpngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgtasinfd dvvmrnmtvi
      361 kegevtfppp pisvsaapak paakiepknt tpkapsklky vlaalgvagf aavasvappe
      421 flshftvfll scvvgyyvvw nvshslhtpl msvtnaisgi ivvgallqig qgstlvtvla
      481 fiavliasin ifggftvtqr mlkmfrkd
//
LOCUS       WP_105257263             124 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_105257263
VERSION     WP_105257263.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..124
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=13596
ORIGIN      
        1 mkrivtkrsy kvglcamala llmstaggvt agaqdyhves sgalkpigng tfmkmeysaf
       61 pkdtpienng vtelksinsq nadsanssds wfwnlwkkfk tvfqsfieng vrrgfgiqrl
      121 fgfk
//
LOCUS       WP_105259409             536 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodoferax
            sp. TS-BS-61-7].
ACCESSION   WP_105259409
VERSION     WP_105259409.1
KEYWORDS    RefSeq.
SOURCE      Rhodoferax sp. TS-BS-61-7
  ORGANISM  Rhodoferax sp. TS-BS-61-7
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Rhodoferax.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Rhodoferax sp. TS-BS-61-7"
                     /db_xref="taxon:2094194"
     Protein         1..536
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55680
     Region          12..536
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtsvptetg qrigvpkeif pgekrvatvp evvekliklg frvsvesgag alancdddsy
       61 raagaevvat avelwaqsdi vfkvrgpssd evgllreggt lisfiwpaqn pdllqqlaar
      121 katvlaidal prtlsraqkm daltsmagvs gyravieaan afgrffngqi taagkvppak
      181 vfiagagvag laaigtaasl gaivrandtr aevadqvtsl ggefvkvdye eeggggggya
      241 kvmsegfqqa qramyakqar evdiiittal ipgkpapkli taemvrsmkp gsvivdmaae
      301 qggnceltep gqavvkhgvt ivgytdlasr lskqsstlya nnlfrlseel ckakdgvani
      361 nmeddairgl tvikegsvtw papppklpaa paaaakaapv avkkpahghg gasepmsaks
      421 lailmavaav lfwligsyap aaflghftvf vlacfvgymv vwnvkpalht plmsvtnais
      481 siiaigalvq ispiagavgr pdslitwlaa aaivltainm fggfavtqrm lamfrk
//
LOCUS       WP_105262218             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodoferax
            sp. TS-BS-61-7].
ACCESSION   WP_105262218
VERSION     WP_105262218.1
KEYWORDS    RefSeq.
SOURCE      Rhodoferax sp. TS-BS-61-7
  ORGANISM  Rhodoferax sp. TS-BS-61-7
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Rhodoferax.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Rhodoferax sp. TS-BS-61-7"
                     /db_xref="taxon:2094194"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39008
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,300,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpteta vgetrvavtp etvkklvaqg hvvrvqsgag vaasvtdegy vaagagitda
       61 agalgselvl kvrtpsdaea tqmkpgttlv gmlnpfdteg lqrlataglt ayaleaaprt
      121 traqsmdvls sqaniagyka vmlaadtyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslggkf idvpyetdee rdaavgvggy akpmpaswle
      241 rqkvevakrv aqadivista lipgrpaptl itedmvqsmk pgsvivdiaa gkgaigphgs
      301 gggncplsea dktvvkhgvt ligetnlpal vaadasslya rnvldflklv inkegalhvd
      361 leddivaacl vahggevrrk
//
LOCUS       WP_105264274             114 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein, partial [Streptococcus suis].
ACCESSION   WP_105264274
VERSION     WP_105264274.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         <1..>114
                     /product="SSU0592/SSU0593 family protein"
ORIGIN      
        1 khivtkrsyk vgacamalal lmttaggavv naeqdlkstg tisergnsvl vatpapnqsf
       61 qnngvnhles inqfgsqmdp segqsswfgs fwgrvktfwn klccamgltw ckvk
//
LOCUS       WP_105263467             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [unclassified Escherichia].
ACCESSION   WP_105263467
VERSION     WP_105263467.1
KEYWORDS    RefSeq.
SOURCE      unclassified Escherichia
  ORGANISM  unclassified Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="unclassified Escherichia"
                     /db_xref="taxon:2608889"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53628
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ffsllvpfff ltsvhaeqta alakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghayavtd vretlrtgap knaedgtmpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekgg rfdqqsmvcg qchveyyfdg kdkavkfpwd ngmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkatlqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_105273166             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia sp. MOD1-EC7003].
ACCESSION   WP_105273166
VERSION     WP_105273166.1
KEYWORDS    RefSeq.
SOURCE      Escherichia sp. MOD1-EC7003
  ORGANISM  Escherichia sp. MOD1-EC7003
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia sp. MOD1-EC7003"
                     /db_xref="taxon:2093900"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53632
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mirikinarr ifslliplff ftsvhaeqta tsaktvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaeegplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyavrame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkli qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_105288242             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Escherichia].
ACCESSION   WP_105288242
VERSION     WP_105288242.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53571
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta aptkpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheip ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_105280905             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [unclassified Escherichia].
ACCESSION   WP_105280905
VERSION     WP_105280905.1
KEYWORDS    RefSeq.
SOURCE      unclassified Escherichia
  ORGANISM  unclassified Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="unclassified Escherichia"
                     /db_xref="taxon:2608889"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53601
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaaramd aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd ngmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkatlqklva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_105290461             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia sp. MOD1-EC6842].
ACCESSION   WP_105290461
VERSION     WP_105290461.1
KEYWORDS    RefSeq.
SOURCE      Escherichia sp. MOD1-EC6842
  ORGANISM  Escherichia sp. MOD1-EC6842
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia sp. MOD1-EC6842"
                     /db_xref="taxon:2093899"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53543
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaaramd aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd ngmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq lpdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_105295843             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacter virginiensis].
ACCESSION   WP_105295843
VERSION     WP_105295843.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacter virginiensis (Mycobacterium virginiense)
  ORGANISM  Mycolicibacter virginiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacter.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Mycolicibacter virginiensis"
                     /db_xref="taxon:1795032"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51924
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mnigvlseaq pgetrvsatp ttvaaltklg ydvvvdsgag eassfsdeay teagatigda
       61 raadivfgvn apsteqldgm kpgatlvsll apalnpdrve dlarrpital smdavprisr
      121 aqsldvlssm aniagyravi eaahvfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivra tdprpevadq vrslggeyls iestetevsa tgyakemsdd ykareaqlya
      241 dqcadvdiiv ttalipgkpa priitadmva smkpgsvivd maaanggnve gtvkdqavvt
      301 dngvtiigyt dlagrlpaqa sqlygtnlvn lmklmtpgkd gqlvldfddv vqrsmtvvrd
      361 gestwppppv qvsaapakva eapvvaqtnk epmsagrrlg vvvsaaavlf alvalapaal
      421 qvhltvfala ivigyyvigh vhhalhtplm svtnaisgii vvgallqigh gdpaitslaa
      481 aaillasini fggfavtrrm lamfsrs
//
LOCUS       WP_105348566             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium sp. ITM-2016-00318].
ACCESSION   WP_105348566
VERSION     WP_105348566.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium sp. ITM-2016-00318
  ORGANISM  Mycobacterium sp. ITM-2016-00318
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Mycobacterium sp. ITM-2016-00318"
                     /db_xref="taxon:2099693"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52358
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgetrvaatp qtiaqliklg yevvvesgag aassfsdeaf teaggtvgsa
       61 eqvwaadvvl kvnapddaei aalrdgatli glispalkpe lverlgtrpi tvlamdavpr
      121 israqsldvl ssmaniagyr avieaankfg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 vgaagslgai vratdprpev adqvkslgge ylsiespeaq vsatgyakem gddykareaq
      241 lyaeqagdvd iiittalipg kpapriitad mvasmnpgsv ivdmaaangg nvegtvkdev
      301 ivtdhgvtii gytdlagrlp atasqlygtn lvnllklltp ekdgklildf edvvqrsvtv
      361 vrdgevtwpp ppvqvsaapv tatapvetkp akehmstarr lgltfaaaav llalialspa
      421 alqvhltvfv laivigyyvi gnvhhalhtp lmsvtnaisg iivvgallqi ghgniaitav
      481 atlaillasi nvfggfavtr rmlamfsrs
//
LOCUS       WP_105361916             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium sp. ITM-2016-00316].
ACCESSION   WP_105361916
VERSION     WP_105361916.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium sp. ITM-2016-00316
  ORGANISM  Mycobacterium sp. ITM-2016-00316
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Mycobacterium sp. ITM-2016-00316"
                     /db_xref="taxon:2099695"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51880
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresq agetrvaatp qtvgqilklg ysvvvesgag aassfsdaay eeagasigsp
       61 wdaevvlkvn apddteidal ndgatlvsli spalrpelve klstrpitvl amdavprisr
      121 aqsldvlssm aniagyravv eaahafgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivka tdprpevadq vkslggeyvs vdpaaaevsa tgyakemgdd ykareaavya
      241 elarevdiii ttalipgrpa priitadmva smkpgsvlvd maaanggnve gtvkdqavit
      301 dngvtiigyt dlagrlpata sqlygtnlvn llklltpakd galtldfedv vqrsvtvvrd
      361 gqttwppppv qvsaapaaak aepvqapkvk epmstgrrlg ialtgaailf vllalspaal
      421 qmhltvfala ivigyyvign vhhalhtplm svtnaisgii vvgallqvge tdaviaalat
      481 vaimlasini fggfavtrrm lamfsrs
//
LOCUS       WP_105374196             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neorhizobium huautlense].
ACCESSION   WP_105374196
VERSION     WP_105374196.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium huautlense
  ORGANISM  Neorhizobium huautlense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Neorhizobium huautlense"
                     /db_xref="taxon:67774"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42561
     Region          14..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 makiihvsre gsdeprvsas petvkrlagl gftivvesga giasgipdgd feaagariga
       61 asdagsadiv lrvnrptaae aasyksgavv favmdpygne aalaamakag lttfamelmp
      121 ritraqsmdv lssqanlagy ravidashey grampmmmta agtvpaakvf vmgagvaglq
      181 aiatarrlga vvsatdvrpa akeqvaslga kfiavedeef kaaetaagya kpmseayqak
      241 qaalvaehia kqdivittal ipgrpapqlv tramlssmkp gsvavdlave rggniegsqk
      301 gkvanvegvt vigyanvagr iaasasalya knlfafietm vdktskefav npedelvkat
      361 mlthaghvvh pnfaaavaal vreapaapaa iaepvpakta rprkkavaes aakgeel
//
LOCUS       WP_105383178             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neorhizobium alkalisoli].
ACCESSION   WP_105383178
VERSION     WP_105383178.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium alkalisoli
  ORGANISM  Neorhizobium alkalisoli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Neorhizobium alkalisoli"
                     /db_xref="taxon:528178"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42595
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 makiiyvsre gsdeprvsas petvkrlsgl gftivverga glasgipdgd feaagariga
       61 asdagsadiv lrvnrptaae aasyksgavv favmdpygne aalaamakag lttfsmelmp
      121 ritraqsmdv lssqanlagy ravidashey grampmmmta agtvpaakvf vmgagvaglq
      181 aiatarrlga vvsatdvrpa akeqvgslga kfiavedeef kaaetaagya kpmseayqak
      241 qaalvaehia kqdivittal ipgrpaprlv tramlasmkp gsvavdlave rggniegsek
      301 gkvasvegva vigyanvagr iaasasalya rnlfafletm vdknskefav npedelvkat
      361 mlthggrvvh pnfasavaal vseapagpav vaepapakta rprkkavaes aakgeel
//
LOCUS       WP_105400137             427 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neorhizobium sp. T7_12].
ACCESSION   WP_105400137
VERSION     WP_105400137.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium sp. T7_12
  ORGANISM  Neorhizobium sp. T7_12
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Neorhizobium sp. T7_12"
                     /db_xref="taxon:2093832"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43461
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpkivfvcre gsdeprvaas pesvkrltgl glsvviesga glasgvrdad featgariag
       61 agevgsadii lrvnrptaae mtsykpgavv favmdpygne aalagmakag lttfamelmp
      121 ritraqsmdv lssqanlagy ravidashey grampmmmta agtvpaakvf vmgagvaglq
      181 aiatarrlga vvsatdvrpa akeqvaslga kfiavedeef kaaetaagya kpmseayqak
      241 qaalvaehia kqdivittal ipgrpaprlv tramlasmkp gsvavdlave rggniegsek
      301 gkvadvegva vigyanvagr iaasasalya rnlfafietm vdkgtkefav nledelvkat
      361 mlthggqvvh pnfaaaaaal aggetpvaas aatsapavis ieepaaakpv rarkkpvade
      421 aasngdl
//
LOCUS       WP_105412602             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_105412602
VERSION     WP_105412602.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38560
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarlaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_105421771             420 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neorhizobium sp. T25_27].
ACCESSION   WP_105421771
VERSION     WP_105421771.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium sp. T25_27
  ORGANISM  Neorhizobium sp. T25_27
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Neorhizobium sp. T25_27"
                     /db_xref="taxon:2093831"
     Protein         1..420
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42977
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpkivfvcre gsdeprvaas pesvkrltgl glsvviesga glasgvrdad featgariag
       61 agevgsadii lrvnrptaae mvsykagavv favmdpygne aalagmakag lttfamelmp
      121 ritraqsmdv lssqanlagy ravidashey grampmmmta agtvpaakvf vmgagvaglq
      181 aiatarrlga vvsatdvrpa akeqvaslga kfiavedeef kaaetaagya kpmseayqak
      241 qaalvaehia kqdivittal ipgrpapklv tramlasmkp gsvavdlave rggniegsek
      301 gkvadvegvt vigyanvagr iaasasalya rnlfafietm vdkgtkefav nledelvkat
      361 mlthggqvmh pnfaaaalad etpvaapapa aisikepaaa kpvrarkkpv adeaasngdl
//
LOCUS       WP_105423737             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus opacus].
ACCESSION   WP_105423737
VERSION     WP_105423737.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38006
     Region          13..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqsasta rptvgvvres ndgerrvalv pkivasliak gvdvvvesga glgalipdel
       61 ytevgakiad pwsadvivkv appsdeevgr lhagqtligf laprnqdnqv aalkaagvqa
      121 faveaipris raqvmdalss qanvsgyksv llaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrat gydvrpevad qvrsvgaqwl dlgidaageg gyarelteae
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvvvdl agetggncel
      301 tepgqtvvkh gvticsplnl patmpehase lysknisall elmlvdgala pdfsdevlaa
      361 scvtreegvs
//
LOCUS       WP_105423777             506 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus opacus].
ACCESSION   WP_105423777
VERSION     WP_105423777.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..506
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52164
     Region          1..505
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgvlkear agetrvsatp ttvaalqklg yqvvvepgag epagftdgay aeagaelrdp
       61 laadvvigvn pptlaqrdrl qpgatliaml nprlddgiva dlaqrpital smdavprisr
      121 aqsmdvlssm anvagyravv eaahefgrmf tgqvtaagki pparvfvvga gvaglaaiga
      181 asamgaivra fdvrpevaeq vasmgaefve idfeaevsad gyakemtaeq eiataamyde
      241 earaadivit talipgrpap kliteetiaa mrngsvivdm aaanggnaal tktdervvsd
      301 ngvrilgytd lagrlaaqas qlygtnivnl lklltpgkdg elvldfddvv qrgitvvrdg
      361 estwppppvq vsaapqvpaa atvpaaepke pmspgqrlgv vaaaaavlfl ligvapaqlq
      421 lnltvfalai vigyyvighv hhalhtplms vtnaisgiiv vgallqigkg dtaitvisfv
      481 avllacinif ggfavtrrml amfsrs
//
LOCUS       WP_105428570             420 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neorhizobium sp. T6_25].
ACCESSION   WP_105428570
VERSION     WP_105428570.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium sp. T6_25
  ORGANISM  Neorhizobium sp. T6_25
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Neorhizobium sp. T6_25"
                     /db_xref="taxon:2093833"
     Protein         1..420
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43014
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpkivfvcre gsdeprvaas pesvkrltgl glsvviesga glasgvrdad featgariag
       61 agevgsadii lrvnrptaae masykqgavv favmdpygne aalagmakag lttfamelmp
      121 ritraqsmdv lssqanlagy ravidashey grampmmmta agtvpaakvf vmgagvaglq
      181 aiatarrlga vvsatdvrpa akeqvaslga kfiavedeef kaaetaagya kpmsepyqak
      241 qaalvaehia kqdivittal ipgrpapklv tramlasmkp gsvavdlave rggniegsek
      301 gkvadvegvt vigyvnvagr iaasasalya rnlfafietm vdkgtkefav nledelvkat
      361 mlthggqvvh pnfaaaalae eapvaapapa visieepaaa kpvrarktpv adeaasngdl
//
LOCUS       WP_105438067             420 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neorhizobium sp. T25_13].
ACCESSION   WP_105438067
VERSION     WP_105438067.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium sp. T25_13
  ORGANISM  Neorhizobium sp. T25_13
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Neorhizobium sp. T25_13"
                     /db_xref="taxon:2093830"
     Protein         1..420
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43014
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpkivfvcre gsdeprvaas pesvkrltgl glsvviesga glasgvrdad featgariag
       61 agevgsadii lrvnrptaae masykpgavv favmdpygne aaladmakag lttfamelmp
      121 ritraqsmdv lssqanlagy ravidashey grampmmmta agtvpaakvf vmgagvaglq
      181 aiatarrlga vvsatdvrpa akeqvaslga kfiavedeef kaaetaagya kpmseayqak
      241 qaalvaehia kqdivittal ipgrpapklv tramlasmkp gsvavdlave rggniegsek
      301 gkvadvegvt vigyanvagr iaasasalya rnlfafietm vdkgtkefav nledelvkat
      361 mlthggqvvh pnfaaaaiad etpvaapapa viaieepaaa kpvrarkkpv adeaasngdl
//
LOCUS       WP_105434698             427 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neorhizobium tomejilense].
ACCESSION   WP_105434698
VERSION     WP_105434698.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium tomejilense
  ORGANISM  Neorhizobium tomejilense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Neorhizobium tomejilense"
                     /db_xref="taxon:2093828"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43479
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpkivfvcre gsdeprvaas pesvkrltgl glsvviesga glasgvrdad featgarias
       61 agevgsadii lrvnrptaae masykpgavv favmdpygne aalaamakag lttfamelmp
      121 ritraqsmdv lssqanlagy ravidashey grampmmmta agtvpaakvf vmgagvaglq
      181 aiatarrlga vvsatdvrpa akeqvaslga kfiavedeef kaaetaagya kpmseayqsk
      241 qaalvtdhia kqdivittal ipgrpapklv tramlasmkp gsvavdlave rggniegsek
      301 gkvaevegva vigyanvagr iaasasalya rnlfafietm idkgtkefav nledelvkat
      361 mlthggqvvh pnfaaaaaal aggetpvaas aatsapaais ieepaaakpv rarkkpvade
      421 aasngdl
//
LOCUS       WP_105465964             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_105465964
VERSION     WP_105465964.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53575
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkitfsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_105513802             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Albidovulum denitrificans].
ACCESSION   WP_105513802
VERSION     WP_105513802.1
KEYWORDS    RefSeq.
SOURCE      Albidovulum denitrificans
  ORGANISM  Albidovulum denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Albidovulum.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Albidovulum denitrificans"
                     /db_xref="taxon:404881"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55725
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkeif egenrvamtp dsalqlqklg heclieagag akagfsdaay eaagvkvvkt
       61 aaalfkeadl vakvrppsdt etkrlrkdqt lisffypaqn kellelankq gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvyldfte sqtdgaatgg yaapsspefr
      241 eaqlkkfrel apevdivitt alipgrdapv lwtrdmveam kpgsvivdla aerggncelt
      301 kadekivtdn gvtivgytdf psrmaaqast lysnnirhmm adltpgkdgv vnqnmeddvi
      361 rgatvthdga itfpppppkv qaiaaqkpke kareltveek ranevaafka qtrnqvtllg
      421 vgavlllavg lvapasfmqh fivfvlsvfi gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsy lvillaalsv fmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_105507270             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. BL21I4N1].
ACCESSION   WP_105507270
VERSION     WP_105507270.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL21I4N1
  ORGANISM  Paraburkholderia sp. BL21I4N1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia sp. BL21I4N1"
                     /db_xref="taxon:1938801"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39361
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqsgag tgasfpdeaf taagaeivda
       61 atafgadlvl kvqspteael pllkrgatlv gmldpfnaen aaslagagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmpaswls
      241 rqsalvhera kqadvvista lipgraaptl isvetvqamk pgsvlvdlaa grgaeyegqr
      301 ggncpltvtd qvvvkhgvqi vgytnlasmv padasslyar nlldflkliv tkegtlnidl
      361 addivaatll ardgevtrkt
//
LOCUS       WP_105528448             517 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Microbacterium].
ACCESSION   WP_105528448
VERSION     WP_105528448.1
KEYWORDS    RefSeq.
SOURCE      unclassified Microbacterium
  ORGANISM  unclassified Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="unclassified Microbacterium"
                     /db_xref="taxon:2609290"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52581
     Region          4..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mavigivrep agearvsatp atiaslgklg htvrvergag gaasypdrey eaagaalvdr
       61 aeawgseivl aitapgaeei allsddatli allspalrpd lveslaqrgi tavaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvtsiggs ylpvdvevaa stdgyakats adydrraaei
      241 yteqaadvdi iittalipgr aaprlitasd vaqmkpgsvi vdmaagqggn vegsvagerv
      301 vtdngviilg ytdlasrlaa qasqlygtnl anlvalltpa kdgqlvidfd dvvqrsvtvv
      361 rdgevtwppp avqvaaapaa kaaaapveia ppkkmstark vtlimvgiaa lfavnafapa
      421 plpqhftvlv lsvvigfyvi gkvhhalhtp lmsvtnaisg vivvgamlqi tsplpvvqvl
      481 aaiavllasi nifggfavtr rmlamftlgt sakvgqk
//
LOCUS       WP_105521459             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_105521459
VERSION     WP_105521459.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38691
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_105531275             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Solimicrobium silvestre].
ACCESSION   WP_105531275
VERSION     WP_105531275.1
KEYWORDS    RefSeq.
SOURCE      Solimicrobium silvestre
  ORGANISM  Solimicrobium silvestre
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Solimicrobium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Solimicrobium silvestre"
                     /db_xref="taxon:2099400"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38717
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaetk sgetrvaatp etikkylaak hqvlvqagag iassipdeay vaagaqivna
       61 adafgcelvl kvrapdsaer almksgsvlv gmlnpfdten taamaacgih afaleaapri
      121 traqamdvls sqaniagyka vmlaantygr fmpmlmtaag tvkaarvlim gvgvaglqai
      181 atakrlgavi easdvrppvk eqveslgakf idvpfitdee keiaqgvggy arsmpadwmr
      241 rqaelvhera kladiiitta lipgrkapil iseetvkamk pgsvivdmav eqggncplse
      301 cgttvtkygv hiigvpnlat lvpadasaly arnvldflkl iidkdaalai nredeivvat
      361 licsggevlk k
//
LOCUS       WP_105542482             445 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ochrobactrum vermis].
ACCESSION   WP_105542482
VERSION     WP_105542482.1
KEYWORDS    RefSeq.
SOURCE      Ochrobactrum vermis
  ORGANISM  Ochrobactrum vermis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Ochrobactrum.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Ochrobactrum vermis"
                     /db_xref="taxon:1827297"
     Protein         1..445
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45892
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke sdpnetrvaa saetvkkfia lgfdvvvekg ageksripda eftaagarig
       61 taadaktadv vlkvrrptdt elkgyksgaa lfamldpygh edavaalaka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedde fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vskemvasmr pgsvlidlav erggnvegav
      301 agkiaevngv rivghlnvsg riaasasqly arnliaflet lvdketkllk idpeeelvka
      361 tllthqgkil hpafakadaa paavaekpaa kpkaapkpkv akaeavgdaa kpaapkaakk
      421 tpakapkaaa ksssspkspv dggea
//
LOCUS       WP_105558452             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter sp. MYb9].
ACCESSION   WP_105558452
VERSION     WP_105558452.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. MYb9
  ORGANISM  Achromobacter sp. MYb9
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter sp. MYb9"
                     /db_xref="taxon:1827284"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38505
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkyvggk htvvvergag taaryldday eaagatlgsa
       61 qdalgaelvl kvrapspael sqmkpgavvi gmldpfdadg laqmaaaglv gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgtggy aramppdwma
      241 rqaalvserc kqadlvitta lipgrpaptl vsaetvaamk pgsvlvdlav erggncplse
      301 kgrvvekhgv tiigltnlpg lvatdasaly arniqdflkl iinadgalai qrddeivaac
      361 lmceggnvtr rt
//
LOCUS       WP_105579275             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_105579275
VERSION     WP_105579275.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38608
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaesfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_105562905             377 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Brevundimonas].
ACCESSION   WP_105562905
VERSION     WP_105562905.1
KEYWORDS    RefSeq.
SOURCE      unclassified Brevundimonas
  ORGANISM  unclassified Brevundimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="unclassified Brevundimonas"
                     /db_xref="taxon:2622653"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38397
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavaiavtre rregetrcav tpetvkklia lgatvsveag tgigssipda dyaeagamvk
       61 pdtravldga divlkvrgpt aqetaalkpg aiviamlday rekaavealk ganatafame
      121 fvpritraqv mdvlssqanl agyravieaa yafgkgfpmm mtaagtvapa kvfvmgvgva
      181 glqaiatarr lgavvtatdv rpatkeqves lgakflaved defknaqtag gyakpmspey
      241 qakqavltge hikkqdivit talipgraap vlvsaeqvas mkpgsvlidl aveaggnvag
      301 akagevvtta ngvsivgytn lpgriaadas alyarnlaaf vglmlkdgav tldlddeilk
      361 aavvthggav vhegvkg
//
LOCUS       WP_105621107             297 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Cronobacter malonaticus].
ACCESSION   WP_105621107
VERSION     WP_105621107.1
KEYWORDS    RefSeq.
SOURCE      Cronobacter malonaticus
  ORGANISM  Cronobacter malonaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Cronobacter.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Cronobacter malonaticus"
                     /db_xref="taxon:413503"
     Protein         1..297
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=33763
     Region          5..161
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mfykrfsrrr sealgkvddv ftydniprqa rvqiatawnt vvykagdlpr tlygfvceem
       61 gvhslpvtnr inswgdsdpf vdlvnffcdt rdcddelcid iidmvsfvih ktfspyrsdy
      121 iqpvvdkinf rlqshgigyr ieeghlirvd teythneiik psiatlgssk ryqsafdqfi
      181 lafdhfkank leeaiisack syeatlkiil kdngiqlsgn etisqlvpkl ftldhipafl
      241 qdgnlklsgm lqayvgtirn ksaahgsdqp rnidvelvnf mlnltgsnil fltrifr
//
LOCUS       WP_105671299             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium sp. MYb62].
ACCESSION   WP_105671299
VERSION     WP_105671299.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. MYb62
  ORGANISM  Microbacterium sp. MYb62
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Microbacterium sp. MYb62"
                     /db_xref="taxon:1848690"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52506
     Region          4..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mavigivrep agearvsatp atiaslgrlg htirvergag aaasypdaey eaagaalvdr
       61 eeawgsevvl aitapgveei allsdgatli allspalrpd lvdslaqrgi talaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvtsiggs ylpvdvevaa stdgyakats adydrraaei
      241 yteqaadvdi iittalipgr aaprlitasd vaqmkpgsvi vdmaagqggn vegsvagerv
      301 vsdngviilg ytdlasrlaa qasqlygtnl anlvalltpa kdgqlvidfd dvvqrsvtvv
      361 rdgevtwppp avqvaaapaa kaaaapveia ppkkmstark vtlivvgiaa lfavnafapa
      421 plpqhftvlv lsvvigfyvi gkvhhalhtp lmsvtnaisg vivvgamlqi tsplpvvqvl
      481 aaiavllasi nifggfavtr rmlamftlgt sakggrk
//
LOCUS       WP_105693189             398 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Arthrobacter].
ACCESSION   WP_105693189
VERSION     WP_105693189.1
KEYWORDS    RefSeq.
SOURCE      unclassified Arthrobacter
  ORGANISM  unclassified Arthrobacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="unclassified Arthrobacter"
                     /db_xref="taxon:235627"
     Protein         1..398
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40399
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkagiareal dgerrvaatp etvkqlvglg levelesgag lasghsdddy rqagasvvqs
       61 ldlgtldvyc hvrpmepsta aalrrgsvtv glgspsselp tvralaasgi tsfalelvpr
      121 israqsmdal tsqalvagyr cvleaatrlp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandirpas adevasmggt fikldletae asggyarels adrgalqral
      241 laphvaqadv littaavpgr rapllvtrqm vqgmrpgsvv vdlaaesggn vegsipgqdi
      301 piptgdgqgt vtlvgikdaa sampadasrl faknvanlla lvtrdgavsp dfsdevvagt
      361 clthdghvrh aptaealaal agetanpgsd rpgsegar
//
LOCUS       WP_105689748             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium sp. MYb64].
ACCESSION   WP_105689748
VERSION     WP_105689748.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. MYb64
  ORGANISM  Microbacterium sp. MYb64
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Microbacterium sp. MYb64"
                     /db_xref="taxon:1848691"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52792
     Region          4..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mavigivrep ggesrvaatp atiaslrklg hevvvergag sdasypdeay aaaeatlver
       61 eqawgseivl aitppdperi alladgatfi allspalrpd lveslaqrgi talaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvtsigge ylpvdvavek sadgyakats eaydrraaei
      241 yteqaadvdi iittalipgr aaprlitasd vaamkpgsvi vdmaagqggn vegsvagert
      301 vtangviilg ytdlasrlaa qasqlygtnv anlvalltpg kdgvlaidfd dvvqrsvtvv
      361 rdgavtwppp pvqvaaapak atpalrqaqg pdgaapakks msagrkalli vlgiaalfav
      421 nafapaplpq hftvltlsvv igfyvigkvh halhtplmsv tnaisgvivv gamlqitdsn
      481 pvvqviaaia vllasinifg gfavtrrmla mftkggqk
//
LOCUS       WP_105699077             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_105699077
VERSION     WP_105699077.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38686
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvvdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaehgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_105713150             306 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Acinetobacter].
ACCESSION   WP_105713150
VERSION     WP_105713150.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..306
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35417
     Region          5..166
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiidlfskr qkklrgempd vyqyeeipkq lrvqiihiik dtvgiennss ksaevydfvh
       61 kalcreygrf slgetfesns qalfnfflte knyeycldfi esffrliyrv vriqphafir
      121 tkqkpdeaie elnirfreag vgyqfeqgei irvdsqfihs evvkpvihll gkdkdyegat
      181 aeflaahehy rhrrykecln dslkafesvm ksihkkhsws ykasdssknl insclthnli
      241 pqylqtqfca ianllesgvp tirnkegghg qgaevkevpe hlasyalhlt asnllflikc
      301 eenyvk
//
LOCUS       WP_105717941             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingobacterium haloxyli].
ACCESSION   WP_105717941
VERSION     WP_105717941.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium haloxyli
  ORGANISM  Sphingobacterium haloxyli
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Sphingobacterium haloxyli"
                     /db_xref="taxon:2100533"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40235
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgvlketk vserrvalsp eivkllvkkd fkvqiesgag lgsnfadedy klagadivrk
       61 adifnadvvl kvnaptleea sqykkqavsi sllypytqpe lldmlnarqi tsfamdavpr
      121 israqkmdal ssqanlagyk avviganalg kifplmmtaa gtitpakvli fgagvaglqa
      181 vatakrlgav vevsdvrpet keqveslggr flvvesaeev kteggyakev sqeflakqqq
      241 likdkirdad lvittalvmg kkspilvtee mvksmragsv ivdmavesgg nceisefnkt
      301 vekhnvtiig esnipsllav nasqlyatni salllhlasn egfkwemdee itrgalithq
      361 gelvheftks ilsk
//
LOCUS       WP_105723890             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium sp. MYb66].
ACCESSION   WP_105723890
VERSION     WP_105723890.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. MYb66
  ORGANISM  Microbacterium sp. MYb66
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Microbacterium sp. MYb66"
                     /db_xref="taxon:1848692"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52444
     Region          4..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mavigivrep agearvsatp atiaslgklg htvrvergag aaasypdaey eaagaalvdr
       61 aeawgsevvl aitapgpeei vlladgatli allspalrpd lvdslaqrgi talaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvtsiggt ylpvdvevaa stdgyakats adydrraaei
      241 yteqaadvdi vittalipgr aaprlitasd vaqmkpgsvi vdmaagqggn vegsvageri
      301 vtdngviilg ytdlasrlaa qasqlygtnl anlvalltpa kdgrlvidfd dvvqrsvtvv
      361 rdgevtwppp avqvaaapaa kaasapveva ppkkmstarr vglivvgvaa lfavnafapa
      421 plpqhftvlv lsvvigfyvi gkvhhalhtp lmsvtnaisg vivvgamlqi tsplpvvqvl
      481 aaiavllasi nifggfavtr rmlamftlgt sakggrk
//
LOCUS       WP_105727688             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingobacterium gobiense].
ACCESSION   WP_105727688
VERSION     WP_105727688.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium gobiense
  ORGANISM  Sphingobacterium gobiense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Sphingobacterium gobiense"
                     /db_xref="taxon:1382456"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40205
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgvlketk inerrvalsp eivkmlvkkg fqvqiesgag lgsnfadedy klagagivsk
       61 teifnadvvl kvnaptreea sqykkqavsi sllypytqpe lldmlnarqi tsfamdavpr
      121 israqkmdal ssqanlagyk avviganalg kifplmmtaa gtitpakvlv fgagvaglqa
      181 iatakrlgav vevsdvrpet keqveslggr flvvetaeev kteggyakev sqeflakqqq
      241 likdkikdad lvittalvmg kkspilvtee mvksmkagsv ivdmavesgg nceisefnkt
      301 vekynvtiig esnipsllpv nasqlyatni salllhlann egfkwemdee itkgalithq
      361 gelvheftks ilsk
//
LOCUS       WP_105733031             439 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium myrsinacearum].
ACCESSION   WP_105733031
VERSION     WP_105733031.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium myrsinacearum
  ORGANISM  Phyllobacterium myrsinacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Phyllobacterium myrsinacearum"
                     /db_xref="taxon:28101"
     Protein         1..439
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45307
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke tdaneprvgg saetvkklig lgfsvivegg agvlsripdr efeaagatig
       61 ktadirtadv vlkvrrpsaa elksykkgav viamldpygn daavkelada gvtaftmefm
      121 pritraqvmd vlssqanlag yqavvdaage ydralpmmmt aagtvpaaki fimgvgvagl
      181 qaiatarrmg avvtatdvrp avkeqvaslg akflavedde fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdiiitta lipgrpaprl vsremyarmr pgsvivdlav erggnvegav
      301 agktvdvdgv kivghlnvag riaatasqly aknlvafvet lvdkdakaik infddelvka
      361 tvlthdgkvv hpnfaaaatt aaapaakpva kkvaakaapa apaeaeskka takaapkkaa
      421 aprktaakta tpkktegea
//
LOCUS       WP_105742781             425 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium phragmitis].
ACCESSION   WP_105742781
VERSION     WP_105742781.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium phragmitis
  ORGANISM  Phyllobacterium phragmitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Phyllobacterium phragmitis"
                     /db_xref="taxon:2670329"
     Protein         1..425
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43800
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifipre tdpaeprvaa spetvkkfig lgfsvvvekg agtlsripds efeaagakmg
       61 iagdaksadv ilrvrrpspa elkgykkgav liamldpygn eaevralasa glsaftmefm
      121 pritraqmmd vlssqanlag yqavidaaae ydrampmmmt aagtvpaakv fimgagvagl
      181 qaiatarrlg aivtatdvrp aakeqvaslg akfvavedde fkaaetaggy akemsgeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vskemlasmr pgsivvdlav erggnvegaq
      301 pgkvaeiggv kiighlnvpg riaatasqly arnlvafvdt mvdkesktlk infddelvka
      361 tlltrdgavv hpafagasdt kpaaaaakkp varkaaakpa sgtdaakapa kkgrkpaapk
      421 tggea
//
LOCUS       WP_105750408             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_105750408
VERSION     WP_105750408.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38578
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vsasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghnnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_105773327             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105773327
VERSION     WP_105773327.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38984
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvqaptdael pslkrgavlv gmlepfnaeq aaklaatgvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqamk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad evivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegvlnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105775431             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105775431
VERSION     WP_105775431.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38939
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrisvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvqaptdael pslkrgavlv gmlepfnaeq aaklaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isaetvqamk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad qvivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegvlnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105779080             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105779080
VERSION     WP_105779080.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38941
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvqaptdael pslkrgavlv gmlepfnaeq aaklaatgvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isgetvqamk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad qvivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegvlnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105782649             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105782649
VERSION     WP_105782649.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38913
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvqaptdael pslkrgavlv gmlepfngeq aaklaatgvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isaetvqamk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad qvivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegalnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105786587             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia ambifaria].
ACCESSION   WP_105786587
VERSION     WP_105786587.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55015
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagasia
       61 asaaelwsgs divfkvrpps adeaalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaidtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl ygtnllrvie elckakdgti nvdfdddair
      361 gltvikegni twppppikqa avapkpqaaa paaaapaksk ghghsgepms akalaivfal
      421 galafllvgq fapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapplge lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_105792023             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105792023
VERSION     WP_105792023.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39011
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvqaptdael pslkrgavlv gmlepfnaeq aaklaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isaetvramk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad qvivhndvti aghtnlasmv asdasalyar nlldfmkliv tkegvlnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105797555             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105797555
VERSION     WP_105797555.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38985
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaatg hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvqaptdael pslkrgavlv gmlepfnaeq aaklaatgvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqamk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad qvivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegalnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105814997             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium tuberculosis].
ACCESSION   WP_105814997
VERSION     WP_105814997.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37553
     Region          10..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdpqtqstr vgvvaesgpd errvalvpka vaslvnrgva vvveagager allpdelyta
       61 vgasigdawa advvvkvapp taaevgrlrg gqtligflap rnadnsigal tqagvqafal
      121 eaiprisraq vmdalssqan vsgykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwldlg isasgeggya reltdderaq
      241 qqkaleeais gfdvvittal vpgrpaptlv taaaveamkp gsvvvdlage tggnceltep
      301 grtvvkhdvt iaaslnlpat mpehaselys knitalldll ikdgrlapdf ddeviaqscv
      361 trgkds
//
LOCUS       WP_105817127             530 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_105817127
VERSION     WP_105817127.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54841
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taheerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ptaadlwgrs divlkvrpps seevalmreg gmligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfiagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akeadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvve elckgkdgti nvdfsddair
      361 gltvikdgnv twppppiqqp aaapkpatpp vaaaaskghg hgsgapmsak sltitfavga
      421 lafllvgqfa patflahftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgdaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_105819895             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia gladioli].
ACCESSION   WP_105819895
VERSION     WP_105819895.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia gladioli
  ORGANISM  Burkholderia gladioli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia gladioli"
                     /db_xref="taxon:28095"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38962
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,300,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetr anearvaatp etvkkyvaag hsvcvergag aaasfpdeay aaagatlger
       61 aaayaaeivl kvqapdsdel pqmkrgavlv gmldpfnaeq aarlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdke reaaqgtggy arpmppswla
      241 rqaalvhera kqadivista lipgrpaptl iqadtvaamk pgavivdlaa grgpenadgr
      301 rggncpltva dqvvkvhgvt iaghtnlaaq vgadasalya rnladflkli vtkegalnid
      361 mnddivaatl lcrdgevvrk
//
LOCUS       WP_105826852             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia gladioli].
ACCESSION   WP_105826852
VERSION     WP_105826852.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia gladioli
  ORGANISM  Burkholderia gladioli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia gladioli"
                     /db_xref="taxon:28095"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38923
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,300,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetr anearvaatp etvkkyvaag hsvcvergag aaasfpdeay aaagatlger
       61 aaayaaeivl kvqapgsdel pqmkrgavlv gmldpfnaeq aarlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr flpmmmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee reaaqgtggy arpmppswla
      241 rqaalvhera kqadivista lipgrpaptl iqadtvaamk pgavivdlaa grgpenadgr
      301 rggncpltva dqvvkvhgvt iaghtnlaaq vgadasalya rnladflkli vtkegalnid
      361 mnddivaatl lcrdgevvrk
//
LOCUS       WP_105832070             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia ambifaria].
ACCESSION   WP_105832070
VERSION     WP_105832070.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54952
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagasia
       61 asaaelwsgs divfkvrpps adevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqastl ygtnllrvie elckgkdgti nvdfdddair
      361 gltvikegni twppppikqa vvapkppaaa paaaapaksk ghghsgepms akalaivfai
      421 galafllvgq fapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapplge lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_105835686             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105835686
VERSION     WP_105835686.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38956
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvqaptdael pslkrgavlv gmlepfnaeq aaklaatgvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqamk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad evivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegalnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105838456             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105838456
VERSION     WP_105838456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38939
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvqaptdael pslkrgavlv gmlepfnaeq aaklaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isaetvramk pgsvlvdlaa grgpevdgrk
      301 ggncpvtvad qvivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegvlnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105844615             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105844615
VERSION     WP_105844615.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38984
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvqaptdael pslkrgavlv gmlepfnaeq aaklaatgvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isaetvqamk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad evivhngvti aghtnlasmv asdasalyar nlldfmkliv tregvlnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105841328             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105841328
VERSION     WP_105841328.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38941
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadvvl kvqaptdael pslkrgavlv gmlepfnaeq aaklaatgvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isaetvqamk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad qvivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegvlnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105854340             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_105854340
VERSION     WP_105854340.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38983
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvqaptdael pslkrgavlv gmlepfnaeq aaklaaagvt gfeleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isaetvqamk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad qvivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegvlnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_105856892             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia vietnamiensis].
ACCESSION   WP_105856892
VERSION     WP_105856892.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54845
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatgerrvat vpevveklik lgfavavqsg agaganfdda ayraagasia
       61 atagelwsgs divfkvrpps adevalmreg gmligfvwpa qnpdlmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqak slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvle elckgkdgti dvdfdddair
      361 gltvikegnv twpapplkqp avapkpaaaa paaaapaksk ghghsgepms akalaivfav
      421 galafllvgq fapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapptae lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_105861360             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Labrys
            okinawensis].
ACCESSION   WP_105861360
VERSION     WP_105861360.1
KEYWORDS    RefSeq.
SOURCE      Labrys okinawensis
  ORGANISM  Labrys okinawensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Xanthobacteraceae; Labrys.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Labrys okinawensis"
                     /db_xref="taxon:346911"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39069
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgiavpaeve pgeprvggtp dtvrkliglg atvrvasgag lasgftdedy aqagamvags
       61 nqealdgaav vlkvrrprad elgayrsgal vlgimdphgq healaalaqa gvsafamelm
      121 pritraqvmd vlssqanlag yravidasae fgrafpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfvavedee freaetsagy akpmsaeyqa
      241 kqavlvaehi kkqdivitta lipgrpaprl vsaamvdslk pgsvlvdlav erggnvegar
      301 pgevvvtpgg vkiighlnvp grlaasassf yarnllafve tlvdkkdkvl apnwedelvk
      361 atlltkdgav vhpafqpqpa
//
LOCUS       WP_105862620             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Labrys
            okinawensis].
ACCESSION   WP_105862620
VERSION     WP_105862620.1
KEYWORDS    RefSeq.
SOURCE      Labrys okinawensis
  ORGANISM  Labrys okinawensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Xanthobacteraceae; Labrys.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Labrys okinawensis"
                     /db_xref="taxon:346911"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39094
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipsete pgeprvgatp dtvrkliglg atvrvasgag lasgftdedy aqagatvags
       61 nqealdgaav vlkvrrprad elgayrsgal vlgimdphgq healaalaqa gvsafamelm
      121 pritraqvmd vlssqanlag yravidasae fgrafpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfvavedee freaetsagy akpmsaeyqa
      241 kqaalvaehi kkqdivitta lipgrpaprl vsaamvdslk pgsvlvdlav erggnvegar
      301 pgevvvtpgg vkiighlnvp grlaasassl yarnllafve tlvdkkekvl apnwedelvk
      361 atlltkdgav vhpafqpqpa
//
LOCUS       WP_105876774             503 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit, partial
            [Haemophilus influenzae].
ACCESSION   WP_105876774
VERSION     WP_105876774.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     gene            <1..503
                     /gene="nrfA"
     Protein         <1..503
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
     Region          1..496
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 kslivaasfa slslfnsata elvykpleqp vepakpdlki esvnekfaek ypnqynswrs
       61 tangdgenii yadeenprli vlwggyafak eynaprghfy avtdvrnilr tgapktandg
      121 pqamacwtck gpdvprliae wgekdyfnak wakggpeivn sigcadchdt tskdfaegkp
      181 alriarphvl raldalekat aekdkaegrp hnnlsfntaa htekraeica nchveyyfag
      241 dikqvtfpwd ngqtvddiek yyddigftdw thslskapml kaqhpdfeiw slgmhgkngv
      301 tcvdchmpkv qgadgkvytd hqiqnpfeaf dstcanchdq skeklrdivt srkkevkdvm
      361 grledqivka hfeakeawda gatkkemeaa lmdirhaqwr wdytaashgg hmhapevvlr
      421 vlasgldkva dartklavil tklgvktpvq ipdistadka wkvmgidiek erkakeeflk
      481 tvvpqweqqa rekgllvdpp aqk
//
LOCUS       WP_105885390             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Oligella
            urethralis].
ACCESSION   WP_105885390
VERSION     WP_105885390.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54263
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkeqf agetrvaatp ttvtqliklg ydvavesgag qlakfddaay teagasvvsr
       61 ddvfksdiiy kinapsdaei damdegtilv sfvqpaqnpv lveklrakki tamavdmvpr
      121 israqsmdvl ssmanisgyr avieaahhfg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igaagslgai vkafdtrlev aeqiesmgge flkldfpqea ggsgdgyakv msdefikaem
      241 alfaeqakvv diiittaaip gkpspklitk emvdsmkpgs vivdlaalgg gnceytvpge
      301 vvvtdnnvtv igytdlpnrl agqssqlyst nlvnlsklit pakdgqavld fddviirnmt
      361 vthagelmfp pppiqvsaap qqaapaaapa tkpekapkpl wqklalpvig vliylwashy
      421 apqeflnhlt vfmlscvvgy yvvwnvthal htplmsvtna isgiiivgav iqmsningfa
      481 sflafisvfl vsinifggfy vtrrmlnmfr kg
//
LOCUS       WP_105905936             415 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit, partial
            [Haemophilus influenzae].
ACCESSION   WP_105905936
VERSION     WP_105905936.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     gene            <1..415
                     /gene="nrfA"
     Protein         <1..415
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
     Region          1..408
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 akeynaprgh fyavtdvrni lrtgapktan dgpqamacwt ckgpdvprli aewgekdyfn
       61 akwakggpei vnsigcadch dttskdfaeg kpalriarph ilraldalek ataekdkaeg
      121 rphnnlsfnt aartekraei canchveyyf sgdikqvtfp wdngqtvddi ekyyddigft
      181 dwthslskap mlkaqhpdfe iwslgmhgkn gvtcvdchmp kvqgadgkvy tdhqiqnpfe
      241 afdstcanch dqskeklrdi vtsrkkevkd vmgrledqvv kahfeakeaw dagatkkeme
      301 aalmdirhaq wrwdytaash gghmhapevv lrvlasgldk vadartklav iltkhgvktp
      361 vqipdistad kawkvmgidi ekerkakeef lktvvpqweq qarekgllvd ppaqk
//
LOCUS       WP_105922764             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter baumannii].
ACCESSION   WP_105922764
VERSION     WP_105922764.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39722
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklisag hsvviergag vkaayidsay eqvgatitdd
       61 aytgsqiilk vrapqggeiq klaanttvva mfdpyrntel dqfanqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgaiv eatdlrptak dqveslggkw ldvpmseeeq qraadaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvvgs
      301 kvgetvvten gvkilgipni patvateasa lyarnvfnfv etlfdkeknf ainqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_105924561             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter baumannii].
ACCESSION   WP_105924561
VERSION     WP_105924561.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39738
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklisag hsvviergag vkaayidsay eqvgatitdd
       61 aytgsqiilk vrapqggeiq klaanttvva mfdpyrntel dqfanqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgaiv eatdlrptak dqveslggkw ldvpmseeeq qraadaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likadtvakm kpgsvildma vetggnvegs
      301 kvgetvvten gvkilgipni patvateasa lyarnvfnfv etlfdkeknf ainqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_105928858             281 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_105928858
VERSION     WP_105928858.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..281
                     /product="STM4504/CBY_0614 family protein"
     Region          1..145
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 ireqiillii ntlgncssfy dmtlycyhns hsdevyrric ktlrkeyglf tlyahstsyl
       61 demsnlllkt ddkrkhidti elafnyidty lrtyevtlgl epdkaiseln nifhehslky
      121 ryengrivrl rrikrlknic yylyspgeyg fveydlmeay nrlmlndfac vvkechavfr
      181 svllriherk givyheqdsl ntlmtnlmar gvisaeyahk fhflsnvles eiflpmapek
      241 shhhyammlr iseelacsiy yltersiffl tqraeedsva p
//
LOCUS       WP_105977278             312 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Vibrio sp. V01_P9A10T6].
ACCESSION   WP_105977278
VERSION     WP_105977278.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. V01_P9A10T6
  ORGANISM  Vibrio sp. V01_P9A10T6
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Vibrio sp. V01_P9A10T6"
                     /db_xref="taxon:2116368"
     Protein         1..312
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35933
     Region          5..173
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mgtfdlfskr qkklrgdvpe vytydslpnp lrvqiihiwn dslgdklqyf svddiretyk
       61 fivetlcrey glfelpsnkn grqriyidel anyfleennv ekqldvveit fkvintvtre
      121 yqymrkngas evadsaidel narlkehgvg fqftnneiir vdsellhsea vkpallllnq
      181 khykgaqeef llayehyrhg rykeslndcl kafestmksi cdnhdwkyeq satarsliqi
      241 cfdnglipsf wqqqmsslrs llesgvptgr nrlsghgqgs ntieipdylv aymlhmtast
      301 lvflttaesk ia
//
LOCUS       WP_105940806             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Gordonia
            iterans].
ACCESSION   WP_105940806
VERSION     WP_105940806.1
KEYWORDS    RefSeq.
SOURCE      Gordonia iterans
  ORGANISM  Gordonia iterans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Gordonia iterans"
                     /db_xref="taxon:1004901"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52107
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligiprese pgetlvaata ktvdqlrklg yqviieagag eraeqadeaf adagadigna
       61 davwaadvvi kvnaptddei akmgrgavli smmaparnpe lveklrqagv talamdavpr
      121 israqsmdvl ssmanvagyr avveaahefg rmftgqvtaa gkipparvfv vgagvaglaa
      181 igaasamgav vrafdvrpev aeqvesmgae fvqvdfeaev ssdgyakemt aeqeaataam
      241 ydeearaadi vittalipgr papklisaet vagmhngavi vdmaaanggn aagtvagekv
      301 vtaggvtilg ytdlagrlaa qtsqlygtni vnllklltpk kdgvltldmd dvvqrgitvt
      361 rdgegmwppp pvqvsaapka aaaapvpape pkapmapgkk vglalaaiil ygivvafapg
      421 dipqhftvlm laivigyyvi gnvahalhtp lmsvtnaisg vvvvgailql atnnttvlvl
      481 atiatlvasi nvfggfavtr rmlsmfskga
//
LOCUS       WP_105984625             429 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Brucella].
ACCESSION   WP_105984625
VERSION     WP_105984625.1
KEYWORDS    RefSeq.
SOURCE      unclassified Brucella
  ORGANISM  unclassified Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="unclassified Brucella"
                     /db_xref="taxon:2632610"
     Protein         1..429
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44485
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlyipke sdpnetrvag saetvkkfia lgfdvvvekg ageksripda efaaagarig
       61 tavdaktadv ilkvrrpgda elkayksgaa lfamldpygh edavaalara gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskdyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vskemvasmr pgsvlvdlav erggnvegav
      301 pgeiadvngv kivgylnvpg riaasasqly arnliafvet lvdkkskvlk idpeeelvka
      361 tllthqgril hpafakaeta paavtekaek pkaapkappk aaakpakkap akaakkpssp
      421 kspvdggea
//
LOCUS       WP_106001986             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Magnetospirillum gryphiswaldense].
ACCESSION   WP_106001986
VERSION     WP_106001986.1
KEYWORDS    RefSeq.
SOURCE      Magnetospirillum gryphiswaldense
  ORGANISM  Magnetospirillum gryphiswaldense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Magnetospirillum.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Magnetospirillum gryphiswaldense"
                     /db_xref="taxon:55518"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39094
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipkerr agetrvaasp dtvkkyvqmg fevqveagag sgasiadavy aeagasiaad
       61 aqaafdadvv lkiarptdde igllregavl iaglsaltnk dmveklaark vtafamelvp
      121 ritraqsmdi lssqanlagy kavldgvhvf kravpmmmta agtvaparfl ilgagvaglq
      181 aiatakrlgg vvyafdvrpa vkeqvqslgg kfvevdpeat kdaetaggya kemsedykak
      241 qaakiaevla ktdiaictal ipgkpapvli tedmvkgmrp gsvivdlave mggncplsef
      301 dqvvekhgvt lvghgnvpar lavdasalfa knllnfitpl vdkenktlaf nwddeilkgs
      361 cvtrdgqvvh palag
//
LOCUS       WP_106077975             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chromobacterium amazonense].
ACCESSION   WP_106077975
VERSION     WP_106077975.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium amazonense
  ORGANISM  Chromobacterium amazonense
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Chromobacterium amazonense"
                     /db_xref="taxon:1382803"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39807
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhiaipaerl agehrvaatp etvkklaaag htvaveagag kaaaipdaay reaganiveq
       61 rpallsgadi vlcvgspdaa dldalksgav lvgmlspyhn pllpqlaakg vsafalellp
      121 rttraqsmdv lssqnniagy kavllacqfy prfmpmlmta agtvkaarvl vlgvgvaglq
      181 aiatakrlga vveaydvrpa treqveslga kfievpmsde ekaassgvya remtpeflar
      241 qnellakraa aadivittal ipgkpapvll paasvaamrp gsvivdlaae sggnceltrp
      301 geawqsdngv hlvgltnlps mvaadassly arnlltflgl llsaeglnid leddllaatl
      361 ithqgelrfg aaakptaqtn kepqhg
//
LOCUS       WP_106107974             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Citrobacter freundii].
ACCESSION   WP_106107974
VERSION     WP_106107974.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter freundii
  ORGANISM  Citrobacter freundii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter freundii"
                     /db_xref="taxon:546"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53498
     Region          9..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marikscvrr ffsllvpllf isavhaeqtp vpaktvtvea knevfapqhp dqylswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc gdchntaspd fakgkpeltl
      181 srpyaerame tigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmek
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegkiytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvra hfeakaawda
      361 gateaemkpi ledirhaqwr wdlsiashgi hmhapeeglr mlgsamdkaa dartklvrll
      421 atkgitheip lpdistkeka qaaiglnmqq inaekqdfik tvipqwedqa rkngllsq
//
LOCUS       WP_106134077             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mongoliibacter ruber].
ACCESSION   WP_106134077
VERSION     WP_106134077.1
KEYWORDS    RefSeq.
SOURCE      Mongoliibacter ruber
  ORGANISM  Mongoliibacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Mongoliibacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Mongoliibacter ruber"
                     /db_xref="taxon:1750599"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39981
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigilkepq gesrvsmlpe avktllswnt evcieadags tayaedntyq dvgasiksrd
       61 ellrqadvli giqplspeei altkpsavim gqlnalynpd ltkllidqkr tafsmelvpr
      121 ttraqsmdvl ssmatvtgyk avlmaadllp rffpmfmtaa gsitpsrvli lgagvaglqa
      181 iatarrlgas vfafdvrqaa keevlslgak fvdvegated kgaggyaveq saeylqkqkd
      241 tihehalkad viittaqipg rkapllveer tvramkpgsv vidlaassgg ncalsqpdqt
      301 vningvrivg ienlaakmpq daskmygkny lnflkliikd gnlnlnfedd ivtgtcvchd
      361 gqavsprivq mqns
//
LOCUS       WP_106159907             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hasllibacter halocynthiae].
ACCESSION   WP_106159907
VERSION     WP_106159907.1
KEYWORDS    RefSeq.
SOURCE      Hasllibacter halocynthiae
  ORGANISM  Hasllibacter halocynthiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Hasllibacter.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Hasllibacter halocynthiae"
                     /db_xref="taxon:595589"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55098
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigapkeqs petrvamtpd sakairklgh dcliqagaga asgfsdaeye aagvevvkta
       61 palwnqsdvv vkvnkpteae akrlkegmtl isfvgpsedn almemaadeg ativamemvp
      121 risraqkmda lssmaniagy ratieaanqf grflngqvta agkvppakvl vvgagvagla
      181 aigtatslga qvyafdvrpe vseqiesmga efvfldfeea qdgsetggya apsspefrea
      241 qlakfrelap emdivittal ipgrpapelw tedmvqsmkp gsvvvdlaaa nggnctltkr
      301 gavvvkhgvr iigyddyasr mgaqastlya nnirhmladl tpekdgvivh dmeddvirga
      361 tvvhegaitw pppppktkai aaaprkekpp eqtaeerras evaafreetk rqvgllagag
      421 llvllvglva plsflqhfiv ftlacfvgfq viwgvahslh tplmavtnai ssivilgalm
      481 qigsgswlvl ilaalavfmc ginifggflv trrmlamfer s
//
LOCUS       WP_106163344             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tritonibacter scottomollicae].
ACCESSION   WP_106163344
VERSION     WP_106163344.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter scottomollicae
  ORGANISM  Tritonibacter scottomollicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Tritonibacter scottomollicae"
                     /db_xref="taxon:483013"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55592
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeia egearvamtp asaldlqklg feccieagag qaagftdaay seagvevvkt
       61 aaalwktadi iakvrqpnet elkrltkakt lisffnpggn kdglelaksk gatviamemv
      121 prisraqkmd alssmaniag yravieagnn fdrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg avtyafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yaavsspefr
      241 eaqlakfrel apevdivitt alipnreapk lwladmvaam krgsvivdla aerggnvegt
      301 vrdekiitdn gvtivgytdf psrmasqsss lyatnirhmm tdltpekdgq vvhdmeddvi
      361 rgstvthage itfpppppkv qaiaaqkkpe ppkeltaeek raqevaafkq qtknqvtlla
      421 vgaalllgvg lvapasfmqh fivfvlavfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsw lviflaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_106182645             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Pandoraea novymonadis].
ACCESSION   WP_106182645
VERSION     WP_106182645.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Pandoraea novymonadis
  ORGANISM  Candidatus Pandoraea novymonadis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pandoraea.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Candidatus Pandoraea novymonadis"
                     /db_xref="taxon:1808959"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39244
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaeti fgetrvaatp etikklvaak hqlivtrnag lnanvpdtaf esagatlgsk
       61 deafgadiil kvrapsaeel khiapgsvli gmlnpfdten nnrmaaagiq afsleaapri
      121 traqsidvls sqaniagyka vilaanlhqr fmpmlmtaag tvqaarvvil gagvaglqai
      181 atakrlgaiv easdvrpnvr eqieslgakf idvpfeseee rdisqgiggy arpmpaawla
      241 rqsklvhsri vqadvvitta lipgslaptl iaadtvkemk pgsviidiaa grgangggnc
      301 tlsvpdeivn ihgvhiagyt nlpsmvaada sslyarnvle flklitdkeg qlnidvnddi
      361 vaacliclng qvlrna
//
LOCUS       WP_106178536             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Prauserella shujinwangii].
ACCESSION   WP_106178536
VERSION     WP_106178536.1
KEYWORDS    RefSeq.
SOURCE      Prauserella shujinwangii
  ORGANISM  Prauserella shujinwangii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Prauserella.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Prauserella shujinwangii"
                     /db_xref="taxon:1453103"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38418
     Region          9..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpetdsppti gvvketkpge rrvalvpklv erlvkrglpv vvekgagaga hlpdelyeqa
       61 gasvgdawsa divlrvappt radierlarg tiligflapl snveevaale eagvrafave
      121 siprisraqs mdalssqssv agyratllga qrltrffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgaratgydv rpevadqvrs vgaqwldlgi eavgeggyar elteeeraeq
      241 qrrlteaitg fdvvittalv pgrtaptlvt adavrgmrpg svvvdmagea ggnceltepg
      301 kdvvvhdvti csplnlpaem pdhaselyar nlvelvellv dkegnvnldf sdeiiagacv
      361 agageevn
//
LOCUS       WP_106226213             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Jezberella
            montanilacus].
ACCESSION   WP_106226213
VERSION     WP_106226213.1
KEYWORDS    RefSeq.
SOURCE      Jezberella montanilacus
  ORGANISM  Jezberella montanilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Jezberella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Jezberella montanilacus"
                     /db_xref="taxon:323426"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39018
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigilretr dhetrvagtp etvkkyvtag hevlvepgag laahftdeay taagaklaas
       61 aqcldaelil kvrapspeei skiksgtvvv gmldpfdseg inalnaagit afaleaapri
      121 traqsldvls sqanlagyka vllaahyygr mfpmmmtaag tlkaaravvl gagvaglqai
      181 atakrlgavv easdvrpaak eqieslggkf idvpfetdee reiakgvggy arpmpaswma
      241 rqavlvaerc kqadivitta lipgrpaptl vsaetvfgmk pgsvivdlav erggncplsv
      301 kgevvehhgv klvgltnlpg mvatdasaly srnlmdflkl iidkdaklai nhedeivqac
      361 lmcangevkr kn
//
LOCUS       WP_106229938             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            ventosae].
ACCESSION   WP_106229938
VERSION     WP_106229938.1
KEYWORDS    RefSeq.
SOURCE      Halomonas ventosae
  ORGANISM  Halomonas ventosae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas ventosae"
                     /db_xref="taxon:229007"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55414
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapketa rgearvaltp esakqiqklg heclieagag vaagfndeay reagvsvvdg
       61 iealwteaev vikvrepsee earrlregqt liaffwpaqn eallelckaq gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 saigtatslg avvrafdvrp evaeqiesmg aeflfldfde sqdgsesggy aapsspefre
      241 kqlecfreqa pdvdivitta lipgkpapkl wledmveamk pgsvivdlaa ekggncdltk
      301 pdekvvsdng vtvvgytdfp srmatqasll ystnirhmlt dltpekdgkv vhdmeddvir
      361 gatvthqgev tfpppppkvk aiaaakpkpk ekeptpeekk aaelaafkaq tkrqvtllav
      421 ggalmlllgq vapasfmqhf ivfvlacfvg fqviwgvshs lhtplmavtn aisgiiilga
      481 ilqigsgsvv vgvlaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_106202766             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aliiruegeria haliotis].
ACCESSION   WP_106202766
VERSION     WP_106202766.1
KEYWORDS    RefSeq.
SOURCE      Aliiruegeria haliotis
  ORGANISM  Aliiruegeria haliotis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Aliiruegeria.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Aliiruegeria haliotis"
                     /db_xref="taxon:1280846"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55590
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigsprevf pgesrvamtp dsakqlqklg yecaiesgag laagfsdavy adagvevlgs
       61 aeelyaasdv iakvrppeea eislltpdkt lisffypasn ealmeaakek gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvylefde eqtdgaatgg yaapsspefr
      241 eaqlakfrem apemdivitt alipnrdapv lwtkdmvemm kpgsvivdla aerggncelt
      301 vkdekivtdn gvtiigytdf psrmaaqsst lyatnvrhmm tdltpekdga vnhnmeddvi
      361 rgatithage itfpppppki qaiaakpkpt vveltpeekr akeleefkaq tkrqvtllti
      421 ggalllgvgl vapasfmqhf ivfvlsifvg fqviwnvsha lhtplmaitn aissiiivga
      481 lmqigsgsfl villaalsif maginifggf lvtrrmlamf qks
//
LOCUS       WP_106262332             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Donghicola
            tyrosinivorans].
ACCESSION   WP_106262332
VERSION     WP_106262332.1
KEYWORDS    RefSeq.
SOURCE      Donghicola tyrosinivorans
  ORGANISM  Donghicola tyrosinivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Donghicola.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Donghicola tyrosinivorans"
                     /db_xref="taxon:1652492"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55928
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egerrvamtp dsalqlqklg yecaietgag eaagfsdeay kaagvevlpt
       61 aaqlfkavdi vakvrepnet eakrltkgqt lisffwpaqn kelmelcqsk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg aitlafdvrp evaeqiesmg aefvyldfee kaqdgaatgg yaapsspefr
      241 eaqlkkfrel apevdivitt alipgrdapv lwtkdmvemm kpgsvvvdla aekggnceit
      301 ekdqrvvsdn gvvvigytdf psrmaaqast lystnirhmm tdltpekngq tnhnmeddvi
      361 rgatithege itfpppppkv kaiaaqkpke kakeltpeek raaevaafkk etktqvtlla
      421 iggalllavg lvapasfmqh fivfvlsvfi gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsf lvillaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_106268485             530 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Isoptericola].
ACCESSION   WP_106268485
VERSION     WP_106268485.1
KEYWORDS    RefSeq.
SOURCE      Isoptericola
  ORGANISM  Isoptericola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Isoptericola"
                     /db_xref="taxon:254250"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53796
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigiplesr qgerlvaatp atvrqltalg ydvvveagag eranlpnkay veagariger
       61 advwacdvvt svnapspael dlltpgstli sqlapaarpe lvdalaerrv talaldavpr
      121 israqaldvl saqsnvagyr avieaadefg gmftgqvtaa gttppatvfv igagvaglaa
      181 igtasslgak vrafdvrpea aeqieslgat avraegasqe vsadgyasal tgdqeaatrr
      241 tyaaesagad vvittalvrg tapttitaem vaamrpgsvi vdlaaagggn celtvpgerv
      301 vsdggvivlg ytdlpgrmpq htsqlfgtnv vnlvtlltpa rdgslvidld dvvvrgmtlt
      361 rdgevlwppp pvqvsaapap tapppepaps stdpaaeaaa rrsrsrrngv ltvlaallag
      421 lavavsppda vghftvfala vvvgyyvisa vthalhtplm aqtnaisgii lvgallqigv
      481 ddwlvtslav vaatlasinv fggflvanrm irmfrkgsps gapvtsevar
//
LOCUS       WP_106281951             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. BL25I1N1].
ACCESSION   WP_106281951
VERSION     WP_106281951.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL25I1N1
  ORGANISM  Paraburkholderia sp. BL25I1N1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia sp. BL25I1N1"
                     /db_xref="taxon:1938804"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39431
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatli gmldpfnten ssklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswla
      241 rqsalvhera kqadvvista lipgraaptl isvdtvqamk pgsvlvdlaa grgaeyegqr
      301 ggncpltetd kvvikhgvti vgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_106276731             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Geodermatophilus tzadiensis].
ACCESSION   WP_106276731
VERSION     WP_106276731.1
KEYWORDS    RefSeq.
SOURCE      Geodermatophilus tzadiensis
  ORGANISM  Geodermatophilus tzadiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Geodermatophilus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Geodermatophilus tzadiensis"
                     /db_xref="taxon:1137988"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51903
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpaetr rnetrvaatp tsvgrlcalg hevlveagag sradspdeay vaagarigsa
       61 aqawgadvvl hvnaptldev allrpdavli sllapalape lldalvargv talamdavpr
      121 israqsldvl ssmaniagyr avveaahafg rfftgqvtaa gkvppakvfv agagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvgvpadege qagsgtgyas vtsedfnara
      241 avmyaeqard vdvvittali pgrpaprllt eemvagmkpg svvvdmaaaq ggnvagsvpd
      301 evvttpngvt iigytdlpar lpaqasqlfa tnlvnlltll tpgkdgqlvl dlddvvvrgm
      361 tvarageklw ppppvqvsaa pvaaapppap lpppakapap grraalvgla aallfllaaf
      421 spdqlignlt vfalavvvgf yvighvhhal htplmsvtna isgiivvgal lqlghvstvv
      481 tvlaflavll asinvfggfa vtrrmlgmfr ra
//
LOCUS       WP_106291025             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arcticibacter pallidicorallinus].
ACCESSION   WP_106291025
VERSION     WP_106291025.1
KEYWORDS    RefSeq.
SOURCE      Arcticibacter pallidicorallinus
  ORGANISM  Arcticibacter pallidicorallinus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Arcticibacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Arcticibacter pallidicorallinus"
                     /db_xref="taxon:1259464"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40268
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvavlkekk hpekrvaltp dvvktlvkag fkchiessag dgsgfydssy vaagaviekd
       61 rapllgdani llkvnapsld evsllkegav iisfmyayti peiveacnak kistfamdav
      121 prisraqkmd alssqsnlag ykavllgana lgkifplmmt aagtitparv lifgagvagl
      181 qavatakrlg avvevtdvrv etkeqveslg grflqvesdg vqteggyate vseeylkkqk
      241 eliskhvaea divittalvi gkkapvlite dmvktmkpgs vivdmavesg gncelsefnt
      301 tivkhgitlv geanlpglva vnaselyakn istlllhlad rehfkwdmdd eitkgslith
      361 naeivndftk eilnknka
//
LOCUS       WP_106285733             535 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. BL25I1N1].
ACCESSION   WP_106285733
VERSION     WP_106285733.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL25I1N1
  ORGANISM  Paraburkholderia sp. BL25I1N1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Paraburkholderia sp. BL25I1N1"
                     /db_xref="taxon:1938804"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55058
     Region          3..535
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligiple aaagerrvat vpevveklik lgfsvavqsg agaganfddd ayraagasia
       61 ataaelwsgs divfkvrpps teevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvr slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvesm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl ygtnllrvve elckgkdgti nvdfdddair
      361 gltvikegnv twppppikqa vvapkpaaaa paaaaaapak skghghsgep msakslaivf
      421 aigalaflcv gqfapasfls hftvfvlacf vgymviwnvt pslhtplmsv tnaissiiai
      481 galvqvappl gelanagvrp sglilglavg altltavnmf ggfavtrrml amfrk
//
LOCUS       WP_106298658             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Knoellia
            remsis].
ACCESSION   WP_106298658
VERSION     WP_106298658.1
KEYWORDS    RefSeq.
SOURCE      Knoellia remsis
  ORGANISM  Knoellia remsis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Knoellia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Knoellia remsis"
                     /db_xref="taxon:407159"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53936
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkesl agetrvaatp ktverliklg yavfvesgag qlssftdeay aeagadvvgp
       61 evwntdiilk inapspdeve klragqvlvs llspalkpel vdalaergvt alamdavpri
      121 sraqaldvls smaniggyra vieaanefgg mftgqvtaag kvppatvlvv gagvaglsai
      181 gtagslgavv rafdarpeva eqvesmgadf lhielpdgad dspssdgyak etgedfntaa
      241 ealyaqqaae vdiiittali pgkpaprlit eemvasmkpg svivdmaasn ggnvagsvad
      301 ekvvtengvt ilgytdlpgr lptqasqlfg tnlvnllall tpekdgeltl dledqvqrgm
      361 tvvrdgevmw ppppvqvsaa atglgapdat aksgteasgr htetvakqrd prlkylamai
      421 galvfalvas aspavflghf tvfalavivg fyvisnvaha lhtplmaetn aisgiivvgg
      481 llqidsddvv vralafvail vasinifggf avtgrmlqmf rkd
//
LOCUS       WP_106306153             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chamaesiphon polymorphus].
ACCESSION   WP_106306153
VERSION     WP_106306153.1
KEYWORDS    RefSeq.
SOURCE      Chamaesiphon polymorphus
  ORGANISM  Chamaesiphon polymorphus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Gomontiellales;
            Chamaesiphonaceae; Chamaesiphon.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Chamaesiphon polymorphus"
                     /db_xref="taxon:2107691"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40561
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaviketn pgeqrvalip dlvarlvkqg leiwvearag eksfwsneay tqagaeviad
       61 tdrlwgepdv vlkvappnpa eagklrsgat liscltplan eqlmsqlasq gvtslameli
      121 prstraqsmd alssqasiag ykavllaaaa lpkyfpmltt aagtiapakv fiigagvagl
      181 qaiatarrlg aiveafdirp avreevqslg akfievplne dtvgengyak evsqsakelt
      241 qatiaqhvrs advvittaqv pgkkapllvt aemvsqmrpg svivdlaaeq ggncayteag
      301 ksidrhqvmv igtinlpasv pvhasqlysk nistllqyli kdgvlnldft ddivsstcvt
      361 hegkichdrv rnfvkstsqp svva
//
LOCUS       WP_106310552             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. BL18I3N2].
ACCESSION   WP_106310552
VERSION     WP_106310552.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL18I3N2
  ORGANISM  Paraburkholderia sp. BL18I3N2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia sp. BL18I3N2"
                     /db_xref="taxon:1938799"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39461
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatlv gmldpfnten ssklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvetvqamk pgsvlvdlaa grgaeyegqr
      301 ggncpltetd kvvikhgvti vgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_106317312             506 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinoplanes italicus].
ACCESSION   WP_106317312
VERSION     WP_106317312.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes italicus
  ORGANISM  Actinoplanes italicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Actinoplanes italicus"
                     /db_xref="taxon:113567"
     Protein         1..506
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51820
     Region          1..505
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigvlrdpd pgerrvaatp atveqlaklg yqvvvepgag aaasfsdeay aeagasigdp
       61 lvadvvftin pppaqrldkl aegttligml nprldpglve dlarrpital smdavprisr
      121 aqsldvlssm aniagyravv eaahafgrff tgqvtaagkv ppakvlvaga gvaglaaiga
      181 agslgaivra tdprpevadq vrslggeyle vkaadvevss tgyakemsdd yndraarlya
      241 dqarevdivi ttalipgrpa pklitaemva amragsvivd maaanggnve gtvagevvvt
      301 angvtilgyt dlpgrlpaqa sqlygtnlvn lmklltpgkd gelvldfddv vqrsmtvvrd
      361 geltwppppv svsaapaava ekpaeaapkp akkpmnpllv tgigaaalfl ltaaapaalr
      421 ghltvfalai vigyyvighv hhalhtplms vtnaisgiiv vgallqlghg gpvvtglsfa
      481 aillasinvf ggfavtrrml amfsrs
//
LOCUS       WP_106313614             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. BL18I3N2].
ACCESSION   WP_106313614
VERSION     WP_106313614.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL18I3N2
  ORGANISM  Paraburkholderia sp. BL18I3N2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia sp. BL18I3N2"
                     /db_xref="taxon:1938799"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39880
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigvpketg alesrvaatp etvkklvakg hrvvvgegag tdafftdday viagaeivda
       61 kkaliadvvl kvgspteael hsmrrgtvlv gmlnpfdekn tarlagaglt afalesaprt
      121 traqsldvls sqanvagyka vlvastlyqq fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqveslgakf ldvpyetsee qeaahgvggy arpmpqtwld
      241 rqgalvhera kaadivista lipgrpaptl ipevtlqamr pgsvivdmaa grgavtnstt
      301 gqrggncplt qadkvvtrhg vqlvgytnlp smvshdssal yarnildflk liideegrlv
      361 vdtedeivaa tllclegala raa
//
LOCUS       WP_106334774             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Alsobacter
            soli].
ACCESSION   WP_106334774
VERSION     WP_106334774.1
KEYWORDS    RefSeq.
SOURCE      Alsobacter soli
  ORGANISM  Alsobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alsobacteraceae; Alsobacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Alsobacter soli"
                     /db_xref="taxon:2109933"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40160
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavitetd phedrvaatp etvkklvglg anvavqsgag lasgitdady qaagattept
       61 aeaaladadv vlkvrrptpa eagamkrgai vlaimdpygn eaalkalada gvsafamelm
      121 pritraqvmd vlssqanlag yravidgaae ygralpmmmt aagtvpaari fvmgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akflavedee flqaqtaggy akemskeyqa
      241 kqaalvashi akqdivitta lipgrpapkl vsedmiasmk pgsvlvdlav erggnvalar
      301 pgeivvtpng vkivghlnvp grlaatassl yaknlfnfle tmidkgskal avkwddelvq
      361 atnltrdgav vhpnfqpkpa epapaaapta
//
LOCUS       WP_106353588             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Yoonia
            maritima].
ACCESSION   WP_106353588
VERSION     WP_106353588.1
KEYWORDS    RefSeq.
SOURCE      Yoonia maritima
  ORGANISM  Yoonia maritima
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Yoonia maritima"
                     /db_xref="taxon:1435347"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55311
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpketf egenrvamtp asakdlqklg yeclietgag taagfsdqay adagvevvkt
       61 gaalfkaadi vakvrppsdt evkrlrdgqt lisffypaqn aelmdaankk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvfldfee eqqdgsatgg yaavsspefa
      241 aaqlakfrei apemdivitt alipgrdape lwtkdmvesm kpgsvivdla aerggncklt
      301 vkdekivten gvtiigytdf psrmaaqast lyatnirhmm tdltpekdgv pnhnmeddvi
      361 rgatathkge itfpppppkv aaiaaapkke apkeltaeek rakevadfka qtknqvtlla
      421 vgaalllgvg lvapasfmqh fivfvlsvfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsa lviilaalsv fmtginifgg flvtrrmlam fqks
//
LOCUS       WP_106355358             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia fungorum].
ACCESSION   WP_106355358
VERSION     WP_106355358.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia fungorum
  ORGANISM  Paraburkholderia fungorum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia fungorum"
                     /db_xref="taxon:134537"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39415
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqsgag tgasfpdeaf aaagaeivda
       61 atafgadlvl kvqsptdael pllkrgatlv gmldpfnaen ssklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvetvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvvkhgvti vgytnlasmv padasslyar nlldflklii skegalnidl
      361 addivaatll ardgevtrkt
//
LOCUS       WP_106367672             388 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chlorogloea sp. CCALA 695].
ACCESSION   WP_106367672
VERSION     WP_106367672.1
KEYWORDS    RefSeq.
SOURCE      Chlorogloea sp. CCALA 695
  ORGANISM  Chlorogloea sp. CCALA 695
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Entophysalidaceae;
            Chlorogloea.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Chlorogloea sp. CCALA 695"
                     /db_xref="taxon:2107693"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40989
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miiavakeie vgerrvalip etvgrlvkkg levwvetgag draffpdday eaagakvvad
       61 saalwgeadi llkvglpqer edgrqeidll kegavligfl nplgvpeiaq kladkkvtaf
      121 aieliprssr aqsmdalssq asvagyksvl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vqlneetvaa ggyakeissd
      241 srartqevva ehikqsdvvi ttaqvqgkka pllvteemva qmkpgsvivd laaeqggnca
      301 rtepgkdvqw hgvtiigtin lpssmpihas qmysknlatl vqylvkdnvi nldfaddiid
      361 sacithggei rnqrvrdalv ttsatvgn
//
LOCUS       WP_106375892             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Vreelandella songnenensis].
ACCESSION   WP_106375892
VERSION     WP_106375892.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella songnenensis
  ORGANISM  Vreelandella songnenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Vreelandella songnenensis"
                     /db_xref="taxon:1176243"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55380
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigapkets rgearvaltp esaqqiqklg heclietgag laagfnddty rdagvtvvds
       61 aealfeaaev vikvrepsea eaarlregqt liaffwpaqn ealleacraq gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfen sqdgsesggy aspsspefre
      241 kqlecfreqa pdvdivitta lipgrpapkl wledmvaamk pgsvivdlaa ekggncdltq
      301 pderivsdng vivvgytdfp srmatqssll yatnirhmlt dltpekdgvi nhnmdddvir
      361 gatvthqgdv tfpppppkvk aiaaakpkkk ekeptpeekk ateaaafkaq tkrqvgilai
      421 ggalmlllgq vapasfmqhf ivfvlacfig fqviwkvshs lhtplmavtn aisgiiilga
      481 ilqigsgsav vsvlaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_106380100             479 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Glaesserella parasuis].
ACCESSION   WP_106380100
VERSION     WP_106380100.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     gene            1..479
                     /gene="nrfA"
     Protein         1..479
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53676
     Region          1..477
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mlknslvatm amlgcfqaaw ageakefegp kpdvkiesan hkfaelyplq yqswaataes
       61 kevtsaleed prlvvlwtgy afskdynkpr ghfyavtdvr nilrtgapmd ensgpqpmac
      121 wackspdvpr miaekgevgy fdakwakygs eivnpigcad chdttsqefk dgkaalrvar
      181 phvlralevi gwkfdtldky gkraavcsnc hveyyfagke kavtfpwdkg vdvdsiekyf
      241 deikftdwvh glskapmlka qhpdfetwal gthgkngvtc idchmpkvet kdgkvytdhk
      301 ignpfdnfeh tcktcheqsk eslqarvkeh kkqikdvmir ledqlvkahf eakraweaga
      361 teeemkdalq airhaqwrwd ysaaghgghm hapdvilhvi gtgldraada rtklaviltk
      421 hgvqtpiefp distkakaqk vvgidfdkek aakeeflrtv vpqwekeake kgllpadak
//
LOCUS       WP_106388889             455 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit, partial
            [Haemophilus influenzae].
ACCESSION   WP_106388889
VERSION     WP_106388889.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     gene            <1..455
                     /gene="nrfA"
     Protein         <1..455
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
     Region          1..448
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 ekypnqynsw rstangdgen iiyadeenpr livlwggyaf akeynaprgh fyavtdvrni
       61 lrtgapktan dgpqamacwt ckgpdvprli aewgekdyfn akwakggpei vnsigcadch
      121 dttskdfaeg kpalriarph vlraldalek ataekdkaeg rphnnlsfnt aartekraei
      181 canchveyyf agdikqvtfp wdngqtvddi ekyyddigft dwthslskap mlkaqhpdfe
      241 iwslgmhgkn gvtcvdchmp kvqgadgkvy tahqiqnpfe afdstcanch dqskeklrdi
      301 vtsrkkevkd vmgrledqvv kahfeakeaw dagatkeeme atlmdirhaq wrwdytaash
      361 gghmhapevv lrvlasgldk vadartklav iltkrgvktp vqipdistad kawkvmgidi
      421 ekerkakeef lktvvpqweq qarekgllvd ppaqk
//
LOCUS       WP_106405079             479 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Glaesserella parasuis].
ACCESSION   WP_106405079
VERSION     WP_106405079.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     gene            1..479
                     /gene="nrfA"
     Protein         1..479
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53752
     Region          1..477
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mlknslvatm amlgcfqdaw ageakefegp kpdvkiesan hkfaelyplq yqswaataes
       61 kevtsaleed prlvvlwtgy afskdynkpr ghfytvtdvr nilrtgapmd ensgpqpmac
      121 wackspdvpr miaekgevgy fdakwakygs eivnpigcad chdttsqefk dgkaalrvar
      181 phvlralevi gwkfdtldkh gkraavcsnc hveyyfagke kavtfpwdkg vdvdsiekyf
      241 deikftdwvh glskapmlka qhpdfetwal gthgkngvtc idchmpkvet kdgkvytdhk
      301 ignpfdnfeh tcktcheqsk eslqarvkeh kkqikdvmir ledqlvkahf eakraweaga
      361 teeemkdalq airhaqwrwd ysaaghgghm hapdvilhvi gtgldrvada rtklaviltk
      421 hgvqtpiefp distkakaqk vvgidfdkek aakeeflrtv vpqwekeake kgllpadak
//
LOCUS       WP_106446364             532 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Simplicispira suum].
ACCESSION   WP_106446364
VERSION     WP_106446364.1
KEYWORDS    RefSeq.
SOURCE      Simplicispira suum
  ORGANISM  Simplicispira suum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Simplicispira.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Simplicispira suum"
                     /db_xref="taxon:2109915"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55321
     Region          11..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtsptpavq rigvptetfq gekrvatvpd avekliklgf kvavesgagd gahfsdetyr
       61 aagaevlpda aalwaasdiv lkvrppnsde valmrdggtl igfvwpaqnp elmqqltakn
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaaslg avvrandtra evadqvkslg gefvkvdyee dgaggggyak
      241 vmsegfqaaq rqmyatqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eaverhgvti vgytdlasrm akqsstlyan nllrlveelc kakdgvavvn
      361 meddairglt vtkdgaitwp applkaapvp apksaapvaa kkdshargap mpaknlaimf
      421 avaavlfwfv gayapaaflg hltvfvlacf igymvvwnvt palhtplmsv tnaissiiai
      481 galvqiappe agahgrpdgl ilwlafaalv ltsinmfggf avtrrmlamf rk
//
LOCUS       WP_106454514             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Zobellella
            taiwanensis].
ACCESSION   WP_106454514
VERSION     WP_106454514.1
KEYWORDS    RefSeq.
SOURCE      Zobellella taiwanensis
  ORGANISM  Zobellella taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Zobellella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Zobellella taiwanensis"
                     /db_xref="taxon:347535"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53528
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipretl sgetrvaatp ksveqlrklg fevcieqgag hsasfedaay vaagaslvet
       61 aqvwqsaily kvnaptadei erlqagttlv sfiwpaqnpe lveqlknkgv tvmamdmvpr
      121 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvlv igagvaglaa
      181 igaagslgai vrafdtrpev keqinsmgae fleldyeeds dssdgyakem sqafidaema
      241 lflqqakevd iiittalipg kpapklitae mvaamnpgsv ivdlaaqngg nceltrpgel
      301 fvsdngvkii gytdlngrlp tqsstlyatn lvnlakllck ekdgnikvdf ddvvlrnmtv
      361 vkdgeitfpp paisvsaapk akaaaqpaae phakkpsnlk yylggagvll fawlaavapa
      421 eflshitvfv lacivgyyvi wnvshslhtp lmsvtnaisg iivvgalsqv gaggfvsfla
      481 fvavliasin vfggftvthr mlkmfrkg
//
LOCUS       WP_106469878             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter radioresistens].
ACCESSION   WP_106469878
VERSION     WP_106469878.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39964
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv igenrvaatp etvkklinag hsvviergag vkaayidsay eqvgatitdd
       61 ayqnsqiilk vrapkgeeiq klsphttvva mfdpyrntel dqfasqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaneyqr mfpmlmtaag tvkparvvvm gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmsaeeq qraaeaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvakm kpgpvildma veaggnvegs
      301 kcgetvttsn gvkilgvpni patvateasa lyarnvfnfv etlfdqeknf tvnmedeiqk
      361 allvthngqv llkrg
//
LOCUS       WP_106474080             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pukyongiella litopenaei].
ACCESSION   WP_106474080
VERSION     WP_106474080.1
KEYWORDS    RefSeq.
SOURCE      Pukyongiella litopenaei
  ORGANISM  Pukyongiella litopenaei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pukyongiella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Pukyongiella litopenaei"
                     /db_xref="taxon:2605946"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55609
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egenrvamtp esaqalqklg hdclietgag aaagfsdaay eaagvevvkt
       61 aaalfkaadv vakvrpptet evkrlqpdqt lisffypasn ekllkkaaar gattiamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg aitlafdvrp evaeqiesmg aefvyldfee sqqdgaatgg yaapsspefr
      241 ekqlekfrel apemdivitt alipnrdapv lwtadmveam kpgsvivdla aerggncelt
      301 vpdekivten gvtivgytdf psrmatqsst lyatnirhmm tdltpekdgv idhdmeddvi
      361 rgatithdke itypppppkv qaiaarpqek pkeltpeerk aqelaefkaq tksqvtmlaa
      421 gglalllvga vapasfmshf ivfvlavfvg fqviwnvshs lhtplmaitn aissiiivga
      481 lmqigsgnwl vlllaalsvl magvnifggf lvtrrmlamf qks
//
LOCUS       WP_106486442             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_106486442
VERSION     WP_106486442.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53588
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnsegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_106506177             542 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brachybacterium timonense].
ACCESSION   WP_106506177
VERSION     WP_106506177.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium timonense
  ORGANISM  Brachybacterium timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Brachybacterium.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Brachybacterium timonense"
                     /db_xref="taxon:2050896"
     Protein         1..542
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55573
     Region          1..540
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligiprepd paqavvsatp dtvtklirlg yevqvqsgag draafpdqqy aqagaavvgd
       61 evwdadvlit ldvppqelre rirpgrvlis rmapgrhpel veelesrait glavdavpri
      121 sraqsmdvls smaniagyra vieaagvfgr lftgqvtaag kippaevyvi gagvaglaai
      181 gtansmgavv ratdlrpeva eqvasmgaef vpipaaaers edgyakemta eqaaaaarly
      241 teqsaatdiv ittanipgra aprlltaqdv agmrpgsviv dmaaasggnc eltvpgevit
      301 tdggvtivgh tdlagrlpaq asqlygqniv nlltlmtpek dgmlqidldd eiirgitvtr
      361 aridregerp rvvadvlwpp ppvqvsaapa tgatganana haagaaagsg daaqmgaddp
      421 eadaasgnrl grgvwaalgv llgaglilas plavagqyvv lllavvvgfy vitavthalh
      481 tplmsetnav sgiilvgail qvgssnwavs alaflaivva sinifggftv thrmlgmfrr
      541 da
//
LOCUS       WP_106510382             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_106510382
VERSION     WP_106510382.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53744
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdleiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_106521714             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Taibaiella
            chishuiensis].
ACCESSION   WP_106521714
VERSION     WP_106521714.1
KEYWORDS    RefSeq.
SOURCE      Taibaiella chishuiensis
  ORGANISM  Taibaiella chishuiensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Taibaiella.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Taibaiella chishuiensis"
                     /db_xref="taxon:1434707"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39626
     Region          2..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mltigvlkep gfeprvslnp diaaalvksn ikvvaetgag erafagdpvy taagvalasr
       61 qevlaqsdil lsinapaaed crqmkkgavl igvyqplfnq klmqewavsg ltifsldtlp
      121 rttraqamdv lssqaniagy kavlvaaaay pryfpmfmta agsippakal ilgagvaglq
      181 aiatarrlga vvevfdtrpa vkeevmslga rfvevegaad askaggyave qsedfqqrqk
      241 akiaehvaka divittaqip grqapvlitt dmidsmkpgs vivdlaavtg gntsltrnne
      301 tvvhkgisii gnsslaatlp adasklygkn vhnflkilld kesnlvlnfg ddlvkgaciv
      361 hggevvnerv aqllaapaqg
//
LOCUS       WP_106528167             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga niastensis].
ACCESSION   WP_106528167
VERSION     WP_106528167.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga niastensis
  ORGANISM  Chitinophaga niastensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Chitinophaga niastensis"
                     /db_xref="taxon:536980"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40336
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miagilkekn detrvslvpe ivkqlqqmsv tvwveqgaga hafynddaym dagalikqag
       61 eilsgadiif tlqppsrdli dqipprkiit gilqplyhvs eveywaskni tafsldtipr
      121 ttraqimdvl ssqaniagyk avllaaysys rylpmfmtaa gsiapakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevislgak fvevdgaada skaggyaveq sedykekqqq
      241 riaesiakad ivittaqipg kaapilittl mldqmragsv ivdlaaatgg ntsvtknnet
      301 vhyrgvsiig nsnlpatmpa dasklyaknv fnflkliltk egnlllnfed divkgacith
      361 ngeivndrvk svmqqla
//
LOCUS       WP_106542783             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Prolixibacter denitrificans].
ACCESSION   WP_106542783
VERSION     WP_106542783.1
KEYWORDS    RefSeq.
SOURCE      Prolixibacter denitrificans
  ORGANISM  Prolixibacter denitrificans
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Prolixibacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Prolixibacter denitrificans"
                     /db_xref="taxon:1541063"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40873
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigllketg sekrvamlpe vvsglierkv eifveegage tayqndesyk kagaqvvsrk
       61 evlekaevli qiqppetdlv eslkkeqiwi sqynplwntd lvkafiskgm vsfsldsvpr
      121 itraqamdvl ssmatvsgyk avleaasllp sffpmfmtaa gtirpanvli lgagvaglqa
      181 iaisrklgaq vqvfdvrsav keevmslgak fvevegared aaaggyaveq tddfkkrqqe
      241 ainekaikad vvigtaqipg kkapvlipnd vvekmkpgsv iidlaastgg ncelskdnei
      301 aehhgvrivg qsnypaqmpv daskmfgknl snflalmide egqlqldfed eiikgtcitr
      361 dgeiinervk smldskne
//
LOCUS       WP_106552701             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas hydrophila].
ACCESSION   WP_106552701
VERSION     WP_106552701.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas hydrophila
  ORGANISM  Aeromonas hydrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas hydrophila"
                     /db_xref="taxon:644"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53385
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tclgtsgwaq aadeaqpkgk iearselfak dhadqftswk
       61 gtseskertd alaedpqmvv lwagypfskd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meqyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg vvkqrkdavt eiklkvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakgish eiatpdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_106558499             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. WS11].
ACCESSION   WP_106558499
VERSION     WP_106558499.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. WS11
  ORGANISM  Variovorax sp. WS11
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Variovorax sp. WS11"
                     /db_xref="taxon:1105204"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38372
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetv pgetrvavtp etakklvaqg htvrvqsgag itaaitdaal qaagaeitda
       61 agafacelvl kvrspsdgea almkpgtavv gmlnpfdaeg lqrlaaaglt sfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetqee keaaegvggy arpmpqswmd
      241 rqkvevakrv aaadivvtta lipgraapvl vteemvramk pgsvivdmaa pqggncplte
      301 agrtvikhgv tlvgetnlpa lvaadassly arnvldflkl vlpkeggfki dleddivaac
      361 rmtqdgqvtk k
//
LOCUS       WP_106571901             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitratireductor sp. StC3].
ACCESSION   WP_106571901
VERSION     WP_106571901.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor sp. StC3
  ORGANISM  Nitratireductor sp. StC3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Nitratireductor sp. StC3"
                     /db_xref="taxon:2126741"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55225
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtprevl dgearvamtp dsarmlqklg fvcaietgag enagfsdaay eeagveivks
       61 aerlwadadl vakvrpptgt evallstgkv lisffhpaqn ealmrqaadt gatvvamdmv
      121 prisraqkld alssmaniag yravieagnn fgrfftgqvt aagkvpparv lvvgagvagl
      181 aaigtstalg aityafdvrp evaeqiesmg aefvyldfns dqqdgsasgg yaapsspefq
      241 akqlekfral apeidivitt alipnrdapv lwtkdmvaam kpgsvivdla aerggncelt
      301 vkddkivtdn kvtiigytdf psrmatqast lyannvrqfv gelapardgt lvhdmhddvi
      361 rgstvahqga vtypppppkv raiaaaprkd kpkepspeek ralevaafra qtrrqagllv
      421 agaalialvg avapasfmqh fivfvlacfi gfqviwnvsh alhtplmavt naisgivvlg
      481 allqigsgdw lvvtlaaism liasinivgg flvtrrmlam fqks
//
LOCUS       WP_106571951             435 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Nitratireductor].
ACCESSION   WP_106571951
VERSION     WP_106571951.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor
  ORGANISM  Nitratireductor
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Nitratireductor"
                     /db_xref="taxon:245876"
     Protein         1..435
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44390
     Region          4..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,289,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfvpre leagedriaa spdtakrlcg lgftvvvekg agtgsripde dfikagasig
       61 kagdagkadi vlkvrrpgaa elktykkgav vlatmdpygn eaaveamaka gvsalamefm
      121 pritraqsmd vlssqanlag yqavidaage ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvra aageqvaslg akfimtdalk dasgeggyar eltdaekkaq
      241 aelvaehiak qdivittali pgrpaprlvs gemvksmrpg svivdlaver ggnvegakag
      301 evvttangvk ivghlnvpgr vaasasllya knlfafletm idkdkqalsl nredelvkat
      361 llthdgavvh anfagaqtap atkkpaakkp astkqatkap aakkpaagkt ppkkapakkp
      421 aaaqpvsdak pkgda
//
LOCUS       WP_106576065             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. R9.37].
ACCESSION   WP_106576065
VERSION     WP_106576065.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. R9.37
  ORGANISM  Pseudomonas sp. R9.37
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. R9.37"
                     /db_xref="taxon:1390498"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38662
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag tkasvvdsay etagatigsa
       61 edalgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvivengv ticgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_106602096             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga ginsengisoli].
ACCESSION   WP_106602096
VERSION     WP_106602096.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga ginsengisoli
  ORGANISM  Chitinophaga ginsengisoli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Chitinophaga ginsengisoli"
                     /db_xref="taxon:363837"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40220
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miagvlkeqp genrvslvpd ivkqlgkqgv tvwiepdagt rayypdesyv qagavikpat
       61 eilqqadiil siqipdeqsw ksipagkvlt giyqpfsnsa imqqwadrql ttfsldsipr
      121 ttraqsmdvl ssqaniagyk avllaawsys rylpmfmtaa gsiapakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgar fievegaada saaggyaveq teaykqrqqe
      241 riaesiaksd ivittaqipg kkapilitee mldrmrpgav ivdlaaatgg ntaftennrt
      301 vvhkgitiig dsnlpssmps dasklyakni fnflqllvkd gdlvlnfsdd ivqggciths
      361 gvitnerlrq adsvkl
//
LOCUS       WP_106606611             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shimia
            abyssi].
ACCESSION   WP_106606611
VERSION     WP_106606611.1
KEYWORDS    RefSeq.
SOURCE      Shimia abyssi
  ORGANISM  Shimia abyssi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Shimia abyssi"
                     /db_xref="taxon:1662395"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55425
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf ggenrvamtp dsakqlqklg yecaietgag lnagfsdaty eaagvevvkt
       61 aaalwkasdi iakvrqpdat elkrlnkdkt lisffnpagn edgmaaaksk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaasgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvaam kpgsvivdla aekggncklt
      301 vmdekfvten gvtiigytdf psrmaaqsss lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgatvthqge itfpppppkv qaiaakpkev vpeltpeekr aaevaafkaq tkqqvtllgv
      421 ggalllgvgl iapasfmqhf ivfvlavfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsssfl vvllaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_106614985             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Saccharothrix carnea].
ACCESSION   WP_106614985
VERSION     WP_106614985.1
KEYWORDS    RefSeq.
SOURCE      Saccharothrix carnea
  ORGANISM  Saccharothrix carnea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharothrix.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Saccharothrix carnea"
                     /db_xref="taxon:1280637"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38062
     Region          1..358
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,284,310,312)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,274..275,317..318,322,
                     325..326)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,224,235,
                     252..254,261,263)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvgipvear paerrvaglp etvttligag ltvdvqagag rhahasdaay raaganviad
       61 hpagqsdviv svqpptpeqa aalregditi sflqpsgere lidvlvankv tafsldllpr
      121 vtraqsvdal ssqalvagyr avmeaasrlp kflpmfttaa gtippakvlv lgagvaglqa
      181 iatarrlgav veaydvraaa keevkslgar fleldletqq gvyaeaqset flerqrelia
      241 ervaasdvvi staaipgrka pvlvtndmlk amppgsvvvd laaesggnvt asspgeeiwv
      301 gevlvygakn mpssmpvhas rlyarnvanl lmmmtkdgqv vpdltdevla gcclthagel
      361 rrelp
//
LOCUS       WP_106639876             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Allosphingosinicella vermicomposti].
ACCESSION   WP_106639876
VERSION     WP_106639876.1
KEYWORDS    RefSeq.
SOURCE      Allosphingosinicella vermicomposti
  ORGANISM  Allosphingosinicella vermicomposti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomicrobiaceae; Allosphingosinicella.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Allosphingosinicella vermicomposti"
                     /db_xref="taxon:614671"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38860
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkeea egerrvaatp etirklialg atvsveagag qsasivdedy raagaeiger
       61 tailpgaaii lcvqgpdpai lqdaapgavl igtlnpiger arvdayaatg vealamewmp
      121 ritraqsmdi lssqsnlagy kavldaaaey grvfpmmmta agtvtaarvf vmgvgvaglq
      181 aiatarrlga vvsatdvrsa treqieslga kaifvddvqg iegegaggya temsedykar
      241 qaelvsahia kqdivittal ipgkpaprli tdaqiatmrp gsvivdlave qggnvegsel
      301 gqiverhgvr ivghrnvpsr laadasalya rnlynfiaaf wdaegkhlsl paddeivagt
      361 rvtqngkvvn srla
//
LOCUS       WP_106649597             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            sp. Pdp11].
ACCESSION   WP_106649597
VERSION     WP_106649597.1
KEYWORDS    RefSeq.
SOURCE      Shewanella sp. Pdp11
  ORGANISM  Shewanella sp. Pdp11
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Shewanella sp. Pdp11"
                     /db_xref="taxon:2059264"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53271
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevvieanag qlssfddaaf eaagakvttd
       61 vwqadlifkv napndaeieq ikdgatvvsf iwpaqnpelv aklakrkinv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggqfl kldfgneegg ssdgyaktms defiaaemal
      241 faeqakevdi iittalipgr papklitkam vdsmksgsvi vdlaaatggn ceytqsgelf
      301 vtpngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgtasinfd dvvmrnmtvl
      361 kegevtfppp pisvsaapak paakiapkdt tpkapsklky vlaalgaagf aavasvappe
      421 flshftvfll scvvgyyvvw nvshslhtpl msvtnaisgi ivvgallqig qgstlvtvla
      481 fiavliasin ifggftvtqr mlkmfrkd
//
LOCUS       WP_106664293             441 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium sophorae].
ACCESSION   WP_106664293
VERSION     WP_106664293.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sophorae
  ORGANISM  Phyllobacterium sophorae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Phyllobacterium sophorae"
                     /db_xref="taxon:1520277"
     Protein         1..441
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45514
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke idaneprvgg saetvkklig lgftvivetg agtasripdr efeaagatig
       61 kaanvkdadv vlkvrrpssa eltsykrgai iiamldpygn daavkelada gvtaftmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaalvndhi akqdivitta lipgrpaprl vtremvarmr pgsvlidlav erggnvegav
      301 agkvvevdgv kivghlnvpg riaatasqly aknlvaffet lvdkdsksvk infddelvka
      361 tvlthggkvv hpnfastasa aapalaakta tkkaapakap aakdapvkae askaapkksp
      421 tpkpakaaap kaaskktegd a
//
LOCUS       WP_106683962             532 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Melaminivora suipulveris].
ACCESSION   WP_106683962
VERSION     WP_106683962.1
KEYWORDS    RefSeq.
SOURCE      Melaminivora suipulveris
  ORGANISM  Melaminivora suipulveris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Melaminivora.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Melaminivora suipulveris"
                     /db_xref="taxon:2109913"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55379
     Region          11..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtpnapqaq rigipreifp gekrvatvpd vvgkliklgf avaieagage aanfdddayr
       61 aagaevlpda aalwaasdiv fkvrpptpee valmrqggil igfiwpaqnp elmqqltakn
      121 atvlaidslp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee dgsggggyar
      241 vmsegfqaaq rqmyaqqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg esvvrhgvti igytdlpsrl akqsstlyat nllrvaeelt rakdgvavvn
      361 meddairglt vtkdgsitwp ppplaappap apkaatpvae kksahgpgep msaktltivf
      421 avlavlfwai gayapeaflg hftvfvlacf igymvvwnvt palhtplmsv tnaissiiai
      481 galvqiappa mgvagrpdgl itwlafaalv ltavnmfggf avtqrmlamf rk
//
LOCUS       WP_106686243             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_106686243
VERSION     WP_106686243.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53550
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi dmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_106690411             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            methylarcula].
ACCESSION   WP_106690411
VERSION     WP_106690411.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus methylarcula
  ORGANISM  Paracoccus methylarcula
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus methylarcula"
                     /db_xref="taxon:72022"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55650
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkesy egearvaitp ssathlqklg hevfvesgag aragfmdsdy eragvtvekt
       61 aadlikavdv vakvrqpada eigqmregqt lisffypaqn aellekakeq gitaiamdmv
      121 prisraqkmd alssmaniag yrsvieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aqvfafdvrp evaeqiesmg aefvfldfee qaqdgaatgg yaapsspefr
      241 ekqlakfrel apdmdvvitt alipgrdapv lwtkdmveam kqgsvivdla aekggncelt
      301 vaderivten gvtiigytdf asrmgaqsse lygnnirhfm tdltpkkdgv inhdmeddvi
      361 rgatvahdhd vtfpppppkv aaiaaqkpke kpkeltpeer raqevaafka etrsqvtmla
      421 gggillllvg lvapasfmsh fivfvlacfv gfkviwnvah slhtplmavt naissiiilg
      481 almqigsgsa wvlilaalav lmagvnivgg flvtrrmlam fqks
//
LOCUS       WP_106694782             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter shengliensis].
ACCESSION   WP_106694782
VERSION     WP_106694782.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter shengliensis
  ORGANISM  Marinobacter shengliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter shengliensis"
                     /db_xref="taxon:1389223"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55906
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeif kderrvaatp psvhkliglg ydviveggag eaanysdaay ekvgaaiaad
       61 ttmlwkesdf ilkvrspmen palgkheadl mkegaflvsy lwpaqnpell eklaarkits
      121 faidslpris raqkmdalsa maniagyrav ieaanhfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig aansmgaivr afdtrlevke qvesmgaefl vldfenedgs gsggyakqms
      241 defikaemal faeqaeevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgkva hhhgvtligy tdlpsrmakv asdlyatnlv hllteltpek dgqpvvnmed
      361 evirgltvvh edditwpppk pespvspkpa pgteepsaea kaaakkkadr rsqigkgvlf
      421 vvtalalygv gahapesflq hftvfvlacf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gailhlaqae niavgimafv avliasinvg ggfrvthrml kmfrk
//
LOCUS       WP_106696174             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas chlororaphis].
ACCESSION   WP_106696174
VERSION     WP_106696174.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38619
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvvengv tiigptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_106702188             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ottowia
            oryzae].
ACCESSION   WP_106702188
VERSION     WP_106702188.1
KEYWORDS    RefSeq.
SOURCE      Ottowia oryzae
  ORGANISM  Ottowia oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Ottowia.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Ottowia oryzae"
                     /db_xref="taxon:2109914"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39737
     Region          1..381
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeta agetrvavtp etakklvaqg hqvvvqsgag lrasvtdeay qaagaqitda
       61 sqalgadmvl kvrlpsgdev armkpgavlv gmlepfnaeg lqrlaaanlt afaleaaprt
      121 traqsmdvls sqaniagyka vitaadhyak ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf idvpyetaee keaaegvggy akpmpaswle
      241 rqkvevakrv aqadvvista lipgraapvl iteemvksmk pgsvivdmaa gkgapnadgt
      301 vggncpltea dkivqkhgvt ivgdtnlaar vgadasalya rnvldflklv lppaakgepa
      361 sdfridmedd ivaatlmahq gavtrr
//
LOCUS       WP_106714230             433 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium brassicacearum].
ACCESSION   WP_106714230
VERSION     WP_106714230.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium brassicacearum
  ORGANISM  Phyllobacterium brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Phyllobacterium brassicacearum"
                     /db_xref="taxon:314235"
     Protein         1..433
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44996
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke idaneprvgg svetvkklvg lgftviveag agtasripdr efeaagatig
       61 kttdikgadv vlkvrrptsa eiksykqsav viamldpygn daavkelada gvtaftmefm
      121 pritraqvmd vlssqanlag yqavvdaaee ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaalvndhi akqdivitta lipgrpaprl vtremysrmr pgsvivdlav erggnvegav
      301 agkiievdgi kivghlnvag riaatasqly aknlvaffet lvdketktvk infddelvka
      361 tvlthggkvv hpnfasaaat paaapaakpa akkaatakap vakdapvkae akkaapkkta
      421 tpkaapkkte gea
//
LOCUS       WP_106706650             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas supralitoralis].
ACCESSION   WP_106706650
VERSION     WP_106706650.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas supralitoralis
  ORGANISM  Nitrosomonas supralitoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas supralitoralis"
                     /db_xref="taxon:2116706"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39466
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir eketrvaatp etvkkytakg vhkvlvqsga gagasipdsa yqeagasivn
       61 dvaelyaqsq ivlkvrgpes selammrkdv vllgllsphq kdgvdalaqh gltafamekl
      121 prisraqnmd vlssqaniag ykavimaana yqkffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avveafdvrp avkeqveslg akfvevplsd eekakaetag gyatemsddy
      241 krrqgelvhe railadiiit talipgrpap vlikeetvqa mkpgsvivdm aveaggncpl
      301 selnknvlkh gvhligianl pglvaadasa lyarnlmnfl nlmldqesda lkldrsdeii
      361 agtllctgge vigks
//
LOCUS       WP_106719479             436 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium endophyticum].
ACCESSION   WP_106719479
VERSION     WP_106719479.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium endophyticum
  ORGANISM  Phyllobacterium endophyticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Phyllobacterium endophyticum"
                     /db_xref="taxon:1149773"
     Protein         1..436
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45073
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke teaseprvgg spetvkklit lgfdviveag agvdsripda efvaagarig
       61 ktadikgadv ilkvrrpata elkaykqgai viamldpygn eaaiqaiada gitaftmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg gvvtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaalvaehi akqdiiitta lipgrpaprl vtremyarmr pgsviidlav erggnvegav
      301 agmvtevdgv rivghlnvag riaatasqly aknlvafvet lvdketksvn infddelvka
      361 tvlthggkvv hpnfanaaaa vapvakpakk aaptmesgak dapakavikk apapkakapa
      421 ksaaskstaa knegea
//
LOCUS       WP_106730542             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Zobellella
            endophytica].
ACCESSION   WP_106730542
VERSION     WP_106730542.1
KEYWORDS    RefSeq.
SOURCE      Zobellella endophytica
  ORGANISM  Zobellella endophytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Zobellella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Zobellella endophytica"
                     /db_xref="taxon:2116700"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53571
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipretl sgetrvaatp ksveqlrklg fdvcieqgag ikasfedaay eaagaslvga
       61 dqiwqsaiiy kvnaptaeei erlqagttlv sfiwpaqnpe lveqlkakgv tvmamdmvpr
      121 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvlv igagvaglaa
      181 igaagslgai vrafdtrpev keqinsmgae fleldyeeea dssdgyakem skafidaema
      241 lfmqqakevd iiittalipg kpapklitae mvaamnpgsv ivdlaaqngg nceltkpgel
      301 fvsdngvkii gytdlngrlp tqsstlystn lvnlakllck ekdgnidvdf edvvlrnmtv
      361 vkdgevtfpp paisvsaapk akaaakpaae phakqpsnlk yylggvgvll fawlsavapa
      421 eflshftvfv lacivgyyvi wnvshslhtp lmsvtnaisg iivvgalsqv gaggfvtfla
      481 fvavliasin vfggftvthr mlkmfrkg
//
LOCUS       WP_106724446             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudaminobacter soli (ex Li et al. 2025)].
ACCESSION   WP_106724446
VERSION     WP_106724446.1
KEYWORDS    RefSeq.
SOURCE      Pseudaminobacter soli (ex Li et al. 2025)
  ORGANISM  Pseudaminobacter soli (ex Li et al. 2025)
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Pseudaminobacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Pseudaminobacter soli (ex Li et al. 2025)"
                     /db_xref="taxon:1295366"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43532
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtqtifipke idpseprvaa spetvkrltg lgfdviveaa aglgsritda dfttagakig
       61 ktadaakadv vlkvrrptda elkgyksgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqatltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegav
      301 pgkvvttdng vkivghlnvs grvaasasll yaknlyafle tmvdkgtkql ainredelvk
      361 atmltdggkv vhpafanvvv aepaakaepe kaepakpkva kpaaakkpaa akkpavkksk
      421 gda
//
LOCUS       WP_106734208             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_106734208
VERSION     WP_106734208.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38857
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikklvgqg hqvtvqagag isasipdsay eaagatignd
       61 saafgadlvl kvvaptdael ahmrpgavlv gmlnpfcnet iarmnargvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarilil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpqswme
      241 rqakavhera kqadivitta lipgrkaptl lhestvaemk pgsvvidlaa aqggncplte
      301 adkvvvkhgv tfvghtnlaa lvpadasaly arnlldflkl vidkegqfql nleddivaac
      361 lmcnagevvr kng
//
LOCUS       WP_106738163             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ectopseudomonas mendocina].
ACCESSION   WP_106738163
VERSION     WP_106738163.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas mendocina
  ORGANISM  Ectopseudomonas mendocina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Ectopseudomonas mendocina"
                     /db_xref="taxon:300"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38811
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etvkklvgqg hqvtvqagag isasipdsaf eaagatignd
       61 laalgadlvl kvvaptdael ahikrgavlv gmlnpfcndt iarmnargit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpqswme
      241 rqakavhera kqadivitta lipgrkaptl lhestvaemk pgsvvidlaa aqggncplte
      301 adqvvvkhgv tlvghtnlaa lvpadasaly arnlldflkl midkegqfql nleddivaac
      361 lmcnagevvr kng
//
LOCUS       WP_106740059             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            iguanae].
ACCESSION   WP_106740059
VERSION     WP_106740059.1
KEYWORDS    RefSeq.
SOURCE      Neisseria iguanae
  ORGANISM  Neisseria iguanae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria iguanae"
                     /db_xref="taxon:90242"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54297
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl agetrvactp vtvsqlqklg fevvvehnag laaslddtay eaagatvadm
       61 etvwqspliy kvnaptetet grlnagqtlv sfiwpaqnpe lvqllsdkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvli igagvaglaa
      181 igtanslgai vkafdtrlev veqiesmggr flkldfpqet ggsgdgyakt mseefiaaem
      241 klfaeqakdv diiittaaip gkpapklita vmvesmkags vivdlaaaag gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnlskllr pnkdgeitld fddviirnmt
      361 vtrdgeitfp ppaiqvsaqp qatpsekaap vaksepklvl lwkkltpavi aaimilwiga
      421 vapaeflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqghgf
      481 vsllafiail iasinifggf yvtrrmlnmf rkg
//
LOCUS       WP_106744551             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Yoonia
            maritima].
ACCESSION   WP_106744551
VERSION     WP_106744551.1
KEYWORDS    RefSeq.
SOURCE      Yoonia maritima
  ORGANISM  Yoonia maritima
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Yoonia maritima"
                     /db_xref="taxon:1435347"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55474
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpketf egenrvamtp asakdlqklg yeclietgag taagfsdqay advgvevvkt
       61 gaalfktadi vakvrppsdt evkrlrdgqt lisffypaqn telmdaankk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvfldfee eqqdgsatgg yaavsspefa
      241 aaqlakfrei apemdivitt alipgrdape lwtkdmvesm kpgsviidla aerggncklt
      301 vkdekivten gvtiigytdf psrmaaqsst lyatnirhmm tdltpekdgv pnhnmeddvi
      361 rgatvthkge vtfpppkpki aaiaaapkke apkeltaeek rakevadfka qtknqvtlla
      421 vgaalllgvg lvapasfmqh fivfvlsvfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsa lvivlaalsv fmtginifgg flvtrrmlam fqks
//
LOCUS       WP_106749062             407 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phreatobacter cathodiphilus].
ACCESSION   WP_106749062
VERSION     WP_106749062.1
KEYWORDS    RefSeq.
SOURCE      Phreatobacter cathodiphilus
  ORGANISM  Phreatobacter cathodiphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phreatobacteraceae; Phreatobacter.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Phreatobacter cathodiphilus"
                     /db_xref="taxon:1868589"
     Protein         1..407
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41201
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaiprete ggeprvagtp dtvkrlmalg aevvvepgag lssgiidady aaagaslsad
       61 avkgadvvlk vrrpsaaelk gykagavvla tmdpygneaa lgamaaagvs afamelmpri
      121 traqvmdvls sqanlagyra vidgagefgr alpmmmtaag tvpaakifvm gagvaglqai
      181 atarrlgavv tatdvrpaak eqveslgakf vavmddefkq aetaagyakp msaeyqakqa
      241 alvaehiakq divittalip graaprlvta amvasmkags vivdlaverg gnvegakage
      301 ivvtengvki vghanvpgrl aatssslyak nlfafleimi dkaakalvvp wddelvkatl
      361 ltrdgavvhp nfqsaapppp apaaaapage dpapakpkpa pkkstka
//
LOCUS       WP_106751464             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pannonibacter carbonis].
ACCESSION   WP_106751464
VERSION     WP_106751464.1
KEYWORDS    RefSeq.
SOURCE      Pannonibacter carbonis
  ORGANISM  Pannonibacter carbonis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pannonibacter.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Pannonibacter carbonis"
                     /db_xref="taxon:2067569"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39601
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpresd avetrvaatp etvkklktlg fevtietgag ttsrildtey eaagaviakd
       61 aastfadadv vlkvrrpnad elklmkagal viatmdpygk eaevqamaea giaafamefm
      121 pritraqvmd vlssqanlag yravidaaae ydrafpmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp askeqveslg akfiavedde fkqaetaggy akpmseayqa
      241 kqaelvaahl tkqdivitta lipgrpaprl itaamlasmk pgsvvidlav erggnvegak
      301 agevatvsgv rivghlnvpg riaasassly aknlfaflet mvdktnkvlk pnwddelvka
      361 tvltrdgavv hpafapaks
//
LOCUS       WP_106758901             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Massilia
            glaciei].
ACCESSION   WP_106758901
VERSION     WP_106758901.1
KEYWORDS    RefSeq.
SOURCE      Massilia glaciei (Mokoshia glaciei)
  ORGANISM  Massilia glaciei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Massilia glaciei"
                     /db_xref="taxon:1524097"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38694
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qvivqsgagv masvvdeayv aagatigsaa
       61 dalgcevvlk vrapdagera qmrpnavlig mlnpfdleni aamaaaglsa faleavprit
      121 raqsmdvlss qaniagykav mvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpyltdeek eiakgsggya ktmppdwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlavs qggncplsel
      301 gktvvkhgvf ivgepdlatl vaadasalya rnvldflkli fdkddalvid redeilkasl
      361 vcfggealrk
//
LOCUS       WP_106805888             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_106805888
VERSION     WP_106805888.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53642
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavklpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheis lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_106774238             431 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Kumtagia
            ephedrae].
ACCESSION   WP_106774238
VERSION     WP_106774238.1
KEYWORDS    RefSeq.
SOURCE      Kumtagia ephedrae
  ORGANISM  Kumtagia ephedrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Kumtagia.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Kumtagia ephedrae"
                     /db_xref="taxon:2116701"
     Protein         1..431
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43818
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqvifipre tdsgeprvgg spdtvkrlkg lgfdviveag aglgsrivda dfeaagavlg
       61 rasdaakadv vlkvrrptaa elkgykpgaa vlaimdpygn daaladmaka gvtgfamelm
      121 pritraqvmd vlssqanlag yqavidgaae ydralpmmmt aagtvpaakv fvmgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl isaamvasmk agsvivdlav erggnvegak
      301 agevvttang vkivghlnvp grvaasasll yaknlfafle tlidktgkql sinrdddlvk
      361 atmltdggkv vhpnfakaad vphveppaip attlvadaaa gaeparpkka apkkaagaga
      421 aksagkpkgv a
//
LOCUS       WP_106814496             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium timonense].
ACCESSION   WP_106814496
VERSION     WP_106814496.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium timonense
  ORGANISM  Microbacterium timonense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Microbacterium timonense"
                     /db_xref="taxon:2086576"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52838
     Region          3..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivaep pgenrvaatp ttvpklialg ydvvvengag dassfpdaay taagaavvdg
       61 ptawaspivl kvnpptpaei erladgatli allspalrpd llealatrgi taialdavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvasiggk ylevvvpeea kqvsadgyak atseaydrra
      241 aeiyseqaad vdiiittali pgrpaprlit aadvasmrpg svvvdmaaaq ggnvegsvag
      301 ervvtengvv ilgytdlpgr lpqqasqlfg tnlvnlvkll tpakdgelsv dfddivqrtv
      361 tvvrdgtvtw ppppvqvsaa ttaqekaapa tpvapkktms rttrtvftva giaalfavca
      421 fappplpqhf lvltlavvvg fyvigqvaha lhtplmsvtn aisgiivvga mvqitvpdlt
      481 vqilaavavl vasinifggf avtrrmlamf qkgqar
//
LOCUS       WP_106817439             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Janibacter
            massiliensis].
ACCESSION   WP_106817439
VERSION     WP_106817439.1
KEYWORDS    RefSeq.
SOURCE      Janibacter massiliensis
  ORGANISM  Janibacter massiliensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Janibacter massiliensis"
                     /db_xref="taxon:2058291"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52792
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgvpkesr agetrvaatp ktverlvklg ydvviesgag aaaafsdaay eaagatvgsa
       61 eeawgadlvt kvnapspaei grlregatla sllapatspd lvqaltdrkv talamdavpr
      121 israqaldvl ssmaniagyr avveaahefg slftgqvtaa gkvppakvlv cgagvaglaa
      181 igtanslgai vrafdirpev geqvesmgae fleverdaae aeassdgyak eatedfnrka
      241 aalyaqqaae vdiiittali pgrqaprlit eemvasmkpg svivdmaags ggnvagsvad
      301 ekvvtangvt ilgytdlpar lptqasqlyg tnvvnmltlm tpekdgqlvi dlddvvvrgm
      361 tvtsggetlw ppppvqvsaa ataaspapaa ggasapepaa kapmspaarw gaigaaalvf
      421 llvmgfappa ilanvtvfml avvigyyvig nvhhalhtpl msvtnaisgi iligamtqit
      481 dddpiiqvia flavllasin vfggftvtqr mlsmfrka
//
LOCUS       WP_106844951             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pulveribacter suum].
ACCESSION   WP_106844951
VERSION     WP_106844951.1
KEYWORDS    RefSeq.
SOURCE      Pulveribacter suum
  ORGANISM  Pulveribacter suum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Pulveribacter.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Pulveribacter suum"
                     /db_xref="taxon:2116657"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38086
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl pgetrvaatp etvkklqaqg htvrvqsgag tgasitdaaf aaagaevvda
       61 agawgcelvl kvrapseaeg pllragstvv gmlnpfdaag lqrlaaagvt ayaleaaprt
      121 sraqsmdvls sqanvagyka vmiaadryqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslggkf idvpyetaee keaaegvggy arpmpqswld
      241 rqklevakrv aqadvvitta lipgraapvl vtqemveamk pgsvivdlaa aqggncpltq
      301 agrtvvhrgv tlvgetnlpa lvaadasaly arnvldflkl iigkdgalhi dqaddivvac
      361 lvahegkitr t
//
LOCUS       WP_106854766             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Caballeronia novacaledonica].
ACCESSION   WP_106854766
VERSION     WP_106854766.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia novacaledonica
  ORGANISM  Caballeronia novacaledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Caballeronia novacaledonica"
                     /db_xref="taxon:1544861"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39634
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkklvtqg hrvsvqsgag lpasyiddaf aqagadlvdv
       61 atafsaeivl kvqspsesel amlkpgavli gmldpfnten tarlagtgvt afaleaaprt
      121 traqsldvls sqaniagyka vlmacqyyqr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavv easdvrpavr eqieslggkf vdvpfetdee reaavgvggy arpmpaswla
      241 rqaaqvhera kaadivista lipgrpaptl isvetvkhmk pgsvivdlaa grgpefegkk
      301 ggncpltevd qvvmkhgvhi vghtnlasmv gadasalyar nlldflklvi tkegtlnidl
      361 addivaatlq crdgqvtrpa a
//
LOCUS       WP_106890365             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ahniella
            affigens].
ACCESSION   WP_106890365
VERSION     WP_106890365.1
KEYWORDS    RefSeq.
SOURCE      Ahniella affigens
  ORGANISM  Ahniella affigens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Ahniella.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Ahniella affigens"
                     /db_xref="taxon:2021234"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39220
     Region          3..359
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,72,91,284,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,274..275,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,224,235,
                     252..254,261,263)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgivisavke tvanekrvam tpeiakklka lgtqprievg agvsaafpde aykdadisna
       61 vlsdsdvvla vqpltdeaik qlkpgtvlis ilqphasver vkllrdgkit sfamellprt
      121 traqamdvls sqagmagyka vliaaqaspk ffpmlttaag tirpskvliv gagvaglqai
      181 atarrlgaqv egfdvrpevk eqieslgakf ldlgvsaaga ggyaraltpe eqaeqqkrlg
      241 dhvrnidviv ttaavpgrra priitkamve gmkagavlvd laaetggnce ltepgqtvvt
      301 sngvqvigpv nmpsmgavhs semyarnlfn ftslmikdgq lnldwtddli antcltfdge
      361 ikheatrkai ena
//
LOCUS       WP_106886639             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas rivipollensis].
ACCESSION   WP_106886639
VERSION     WP_106886639.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas rivipollensis
  ORGANISM  Aeromonas rivipollensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas rivipollensis"
                     /db_xref="taxon:948519"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53182
     Region          26..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgshnkpf rpglaalllt allgtsmlaq adeaapegki earselfakd hadqfsswkg
       61 tsesrertda laedpqmvvl wagypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eeyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqskemlqgv vkqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaemk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llaakgishe iaipdisske kaqaalgmdm kqmngdkamf lkttvpawda eakaagrlaq
//
LOCUS       WP_106906413             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_106906413
VERSION     WP_106906413.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53602
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdalt edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qkaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_106908896             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microcystis sp. MC19].
ACCESSION   WP_106908896
VERSION     WP_106908896.1
KEYWORDS    RefSeq.
SOURCE      Microcystis sp. MC19
  ORGANISM  Microcystis sp. MC19
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Microcystis sp. MC19"
                     /db_xref="taxon:1967666"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40223
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikesd qgearvalvp dtvarlvkag fevmvqngag isanfadsay savgaalsen
       61 seyiyetadi ilkvvppsds eidrlkgggi ligfldplrq prriaklaer gitalsmeli
      121 prssraqsmd alssqanlag ykavllaavq lpkmfpmmtt aagtiapakv lvlgagvagl
      181 qacatarrlg avveafdirp qvkeevqsvg akfiemplee dtvadngyak evslstqeri
      241 cqaltepikr advvittaqv pgkqapllvt kemiatmkag svivdlaaeq ggncaytqpg
      301 reiiengvki vgavnlpatv atnasqmyak nlqmllqllv skegslnldf addiidsacv
      361 thageirnqr iksalseqls af
//
LOCUS       WP_106910756             471 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Plesiomonas shigelloides].
ACCESSION   WP_106910756
VERSION     WP_106910756.1
KEYWORDS    RefSeq.
SOURCE      Plesiomonas shigelloides
  ORGANISM  Plesiomonas shigelloides
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Plesiomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Plesiomonas shigelloides"
                     /db_xref="taxon:703"
     gene            1..471
                     /gene="nrfA"
     Protein         1..471
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52200
     Region          1..471
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivklnttsi ttglalfltg tllcssalaq vearndkfad ahqpqyqswt qtqqsserad
       61 alaedpnmvi lwagypfakd ynkprghyya ltdvrdtlrt gapktaedgp lpmacwscks
      121 pdvarmiese gedayfkgmw akggpeivns igcadchatd sqefkdgkpa lhlsrpyasr
      181 amdaihmpfa kqgrfdqqaq vcgqchveyy fsgdnkavkf pwdngtsada maeyydelgf
      241 kdwvhglskt pmlkaqhpey etwqagihgk nnvgcvdchm pkvqgqdgkl ytdhkvgnpf
      301 drfdqtcatc htqskemlqg vvkerkeain tlklkveqql vhthfeakaa wdagateaqm
      361 qpilqdirqa qwrwdyaias hgvhmhapdi alktlgdaln laadartkla rllatkgitg
      421 eiplpdistk ekaqaalgmd mkqfisdkqq flkttvpawe keakdagrls q
//
LOCUS       WP_106914214             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_106914214
VERSION     WP_106914214.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53616
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhvpeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvilqweeqa rkngllsq
//
LOCUS       WP_106928952             315 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Adhaeribacter arboris].
ACCESSION   WP_106928952
VERSION     WP_106928952.1
KEYWORDS    RefSeq.
SOURCE      Adhaeribacter arboris
  ORGANISM  Adhaeribacter arboris
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Adhaeribacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Adhaeribacter arboris"
                     /db_xref="taxon:2072846"
     Protein         1..315
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36442
     Region          5..164
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
     Region          225..299
                     /region_name="Abi_C"
                     /note="Abortive infection C-terminus; pfam14355"
                     /db_xref="CDD:433897"
ORIGIN      
        1 mtihdlyskr nkglpdvfty dvisdkikvq iqyiwddffe qltkelrevi wqgiriillk
       61 ehgkrelpsk yvnytdtydi qvrtyldwst dvevcldiie lvfkfinnvp tilknggyys
      121 tklsyspeha iehlntrfle nglgyefren iiirsdnkll hkeiiiptlh flssakyqna
      181 neeylsahkh frhrrtkecl ndslkalest lkvicklngw ksekgetakh lldlcfqknl
      241 ipaylanhfa glrsslesgv ptlrnklggh gqgtekievp mhfasyimyl sgtsinflis
      301 cqqkfesass lnlkd
//
LOCUS       WP_106935986             376 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Variovorax].
ACCESSION   WP_106935986
VERSION     WP_106935986.1
KEYWORDS    RefSeq.
SOURCE      unclassified Variovorax
  ORGANISM  unclassified Variovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="unclassified Variovorax"
                     /db_xref="taxon:663243"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38539
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeil agetrvavtp etvkklsasg htvrvqsgag vaasvtdaay qaagaeitdr
       61 agafgadmvl kvrtptddet allksgavvi gmlnpfdaag lqrlaaagvt afaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmpaswla
      241 rqqvevakrv aladivista lipgraaptl itedmvkamk pgsvivdiaa gkgadgvggn
      301 cplseadktv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrmtqd gqvtrk
//
LOCUS       WP_106941985             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. MOS002].
ACCESSION   WP_106941985
VERSION     WP_106941985.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. MOS002
  ORGANISM  Bradyrhizobium sp. MOS002
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium sp. MOS002"
                     /db_xref="taxon:2133947"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39213
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag lksglpdsef tavgatvsad
       61 alkdadiiik vrrpeasela qykrgalvia imdpygneaa lktiadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvta dmvrsmkpgs vlvdlaverg gnvegvkage
      301 vaevdgikiv gytnvagrva asasslyarn lfnfietmvd kttkslavnw edelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_106948177             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. MOS003].
ACCESSION   WP_106948177
VERSION     WP_106948177.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. MOS003
  ORGANISM  Bradyrhizobium sp. MOS003
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium sp. MOS003"
                     /db_xref="taxon:2133946"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39267
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag iksglpdsef taagatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygneaa lktiadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegarpge
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 trdgavihpn fqpkv
//
LOCUS       WP_106955982             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            sp. MDA0666].
ACCESSION   WP_106955982
VERSION     WP_106955982.1
KEYWORDS    RefSeq.
SOURCE      Nocardia sp. MDA0666
  ORGANISM  Nocardia sp. MDA0666
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Nocardia sp. MDA0666"
                     /db_xref="taxon:2135448"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37243
     Region          2..349
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(11,66,85,278,304,306)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(40,118..119,128..129,132..133,136..137,139..140,
                     142..147,149,151..153,156,179..180,268..269,311..312,316,
                     319..320)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(113..114,118,121,124,165..168,188..190,218,229,
                     246..248,255,257)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(115..116,118,128,171..172,179,195..196,198..201)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(148..152,155,158,181,183)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvretgtder rvalvpkiip slvkqgvqvv veagagigal ipdeayeaag atigdpwqae
       61 vvvkvappnd aeiaklsqgq tligflaprn adnkigalqd agvrafavea iprisraqvm
      121 dalssqanva gykavllaas estrffpmlt taagtvkpat vlvlgvgvag lqalatakrl
      181 garttgydvr pevadqvrsv gaqwldlgid aageggyare ltddekaqqq qaledaikgf
      241 dvvvttalvp grpaprlvta aavegmkpgs vivdlagetg gnceltepgk tavkhgvtic
      301 splnlpatmp ehaselyskn iaallelmlt dgrlepdfgd qvladscvag apsrpadsee
      361 qg
//
LOCUS       WP_106984605             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Acinetobacter].
ACCESSION   WP_106984605
VERSION     WP_106984605.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39777
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaetv vgehrvaatp etvkklisag hnvviergag vnaayidsay eqvgakitdd
       61 aytgsqiilk vrapkgdeiq klapntavia mfdpyrnpel dqfaaqqvsa falellprtl
      121 sraqnmdvls sqanlsgyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptar dqveslggkw ldvpmspeeq qkaadaakng ygwmpgeeyi
      241 rdqaiivdka vsnadivitt allpgrdapr likaetvakm kpgsiildma vetggnvegs
      301 vcgenvmtan gvkilgipni pstvsteasa lyarnvlnfl dtlfdaeknf ainpeeeiqk
      361 allvthsgqv llkrg
//
LOCUS       WP_106998922             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. JAB6].
ACCESSION   WP_106998922
VERSION     WP_106998922.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. JAB6
  ORGANISM  Rhizobium sp. JAB6
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium sp. JAB6"
                     /db_xref="taxon:2127050"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40568
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msnlvfiake sladetrvaa svetvkkmrs lgfdvvveag agalsripda eyeaagarig
       61 likdakaadv ilkvrrptse eisgyksgai viaimdpygn eaalaemara gltsfamelm
      121 pritraqsmd vlssqanlag yqavieaatv ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aqvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsreyqa
      241 kqaalvsdhi akqdiiitta lipgrpaprl vgrdmlkamr agavavdlav erggniegae
      301 yskvaevegv rvvgypnmag riaasasaly aknlvtflet mvdkdtksla lnrtdelika
      361 tmltdggevv npnfvdpdqp tikkgdl
//
LOCUS       WP_107006720             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter sichuanensis].
ACCESSION   WP_107006720
VERSION     WP_107006720.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sichuanensis
  ORGANISM  Acinetobacter sichuanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter sichuanensis"
                     /db_xref="taxon:2136183"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39951
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv lgesrvaatp etvkklisag hnvviergag kkaayidsay eqvgakitdd
       61 aytgsqlvlk vrapqgneiq klapnttiia mfdpyrnpdl dqfasqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparivim gvgvaglqai
      181 atakrlgavv eatdlrptar dqveslggkw ldvpmsdeek qkaadaakng ygwmpgeqyi
      241 kdqaiivdka vsnadivitt allpgrdapr likaetvakm kpgsiildma vetggnvegs
      301 kcgenvvtdn gvtilgipni patvsteasa lyarnvfnfv etlfdqdknf klnqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_107024307             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. BBP2017].
ACCESSION   WP_107024307
VERSION     WP_107024307.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. BBP2017
  ORGANISM  Pseudomonas sp. BBP2017
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. BBP2017"
                     /db_xref="taxon:2109731"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38763
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqsgag inasvpdsay eaagatigsa
       61 adafgaqlvl kvvapddsel aqiksgtvlv gmlnpfnndi iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvaqgv tivgptnlpa qvgadasaly arnlldfmkl lfdkdnqlvi nleddivaac
      361 lmcrdgqiir kng
//
LOCUS       WP_107074003             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Micromonospora sp. MH33].
ACCESSION   WP_107074003
VERSION     WP_107074003.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. MH33
  ORGANISM  Micromonospora sp. MH33
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Micromonospora sp. MH33"
                     /db_xref="taxon:1945509"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52919
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipsesk qgalvaatak tvsqltnlgy dvivesgagd ladqpdsaft aagvrvgtte
       61 evwaadvvvk vnaptheeig rlrqgatiis mmapgrspel leelqaqgvt alamdavpri
      121 sraqpmdvls smanvagyra vveaahefgr mftgqvtaag kipparvfvv gagvaglaai
      181 gaasamgavv rafdvrpeva eqvesmgaqf veldrsvfka ekssdgyare mteeqqaata
      241 amydeearga divittalip grpaprllta etvagmkngs vivdmaaang gnvagtvadq
      301 kvvtqngvti lgytdlagrl aaqtsqlygt nvvnllkllt pekdgnltln fddvvqrgit
      361 vvkdgestwp ppavqvsaip aaatptvaap vkeekarlsa gakvglvlgg ialfwlvnat
      421 apdpiprhft tlmlsivigy yvigkvahal htplmsvtna isgvvvvgal iqvasedttv
      481 rilsaaatll asinifggfa vtrrmlgmfn kgv
//
LOCUS       WP_107106903             312 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Rhizobium].
ACCESSION   WP_107106903
VERSION     WP_107106903.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..312
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35061
     Region          6..176
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mavwglfskr qsqlrgevpd vytytsippk lrvqivhiis ealgnpgery qepqvnetyk
       61 tiveglcrey glfylpptnd rygvsygkel fdfllrvenv eqcldvveis fravdlvarq
      121 rdyihgssgg qicdgaieel nerfkengvg yqfvdgeiir vdsqllhaea vkpalnllnt
      181 reyrgpheef inayehykdg nnkealvdcl kafestmkai cdkrrwaydp kggakdliav
      241 mfdkglvpsf wqtqlsslrs llessvptgr nklaghgqgs tptevpdeit aymlhmtast
      301 lvflttaera lp
//
LOCUS       WP_107107338             530 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium].
ACCESSION   WP_107107338
VERSION     WP_107107338.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55611
     Region          4..529
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msnkvgvpre itagesrvgl tpesalqlvk lghdclvetg aglsagfsde ayraagvrvv
       61 atreavyaeg dviakvrppq adevallsag ktlisffypa qnkdlleqar etgasviamd
      121 mvprisraqk mdalssmanv agyravieag snfgrfftgq vtaagkvppa kvlvigagva
      181 glaaigtats lgaityafdv rpevaeqies mgaefvyldf ahsqgggqqd gaatggyaap
      241 sspefrekql akfrelapei divittalip grdapklwle dmvaamkpgs vvvdlaaerg
      301 gncdltvpdq kivspngvti vgytdfpsrm aaqastlyat nvrhmlsdlt pgkdgvlvhn
      361 mdddvirgat vtkageitfp ppppkiqaia aqkpkekvre ltleekraae vkafkaqtks
      421 qgillfvata lllvvgavap asfmshfvvf vlscfvgfqv iwnvshslht plmavtnavs
      481 givilgallq vgsshwlvva laalsvlvat inivggflvt rrmlamfqks
//
LOCUS       WP_107109233             387 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium].
ACCESSION   WP_107109233
VERSION     WP_107109233.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40199
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnlvfvake tvadetrvaa sietvkkmrg lgfdivveag agalsripdg eyeaigarig
       61 svhdaaqadv ilkvrrptgg eiagyksgai viaimdpygn eaaladmara gltsfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aqvsatdvrp aakeqvaslg akfvavedee fkaaetaggy akemskdyqa
      241 kqaalvaehi skqdivitta lipgrpaprl vsremlkamr pgavavdlav erggniegvg
      301 fgtvsdvegv kvigypnlag ripasasaly aknlvtflet mvdknskslg lnradelika
      361 tmltdagevv hpnfvdpdqp tvnkgdl
//
LOCUS       WP_107135362             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_107135362
VERSION     WP_107135362.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53573
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fvkgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_107140250             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudoduganella armeniaca].
ACCESSION   WP_107140250
VERSION     WP_107140250.1
KEYWORDS    RefSeq.
SOURCE      Pseudoduganella armeniaca
  ORGANISM  Pseudoduganella armeniaca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Pseudoduganella.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pseudoduganella armeniaca"
                     /db_xref="taxon:2072590"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38883
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qilvqsgags qasitdeafq aagativgaa
       61 ealgadivlk vrapsdaera qmrqgavlig mlnpfdadni armaasglsa faleavprit
      121 raqsmdvlss qaniagykav mvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqgia
      181 takrlgavie asdvrppvke qveslgakfi dvpfltdeek eiaqgvggya rpmpadwmrr
      241 qaelvherak ladivittal ipgrpapvli geetvkamkp gsvivdlave qggncplsel
      301 nktvlkhgvy ivgepnlacq vaadasalya rnvldflkli idkedqlaid redeiikatl
      361 vshggdvlrk
//
LOCUS       WP_107149356             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            symbiotica].
ACCESSION   WP_107149356
VERSION     WP_107149356.1
KEYWORDS    RefSeq.
SOURCE      Trinickia symbiotica
  ORGANISM  Trinickia symbiotica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Trinickia symbiotica"
                     /db_xref="taxon:863227"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39310
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaeth tretrvaatp etvrkfvaqg hrvtigsgag iaasfqdeaf aaagaeivda
       61 atafggdlvl kvqspteser sslkrgavli gmldpfnaen aqklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vlvaaslysr fvpmlmtaag tvkaarmlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee qeaaqgvggy arpmpqswlt
      241 rqaelvhera kqadivitta lvpgrpaptl isvdtvqsmk pgsvlvdlaa grgpdidgrk
      301 ggncpltvad qvivhngvti agytnlasmv asdasalyar nvldftrlii skegaltvdl
      361 tddivsatll crdgevtrk
//
LOCUS       WP_107148075             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_107148075
VERSION     WP_107148075.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53519
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwc wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_107150602             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            symbiotica].
ACCESSION   WP_107150602
VERSION     WP_107150602.1
KEYWORDS    RefSeq.
SOURCE      Trinickia symbiotica
  ORGANISM  Trinickia symbiotica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Trinickia symbiotica"
                     /db_xref="taxon:863227"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39498
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahearvaatp etikkyvaag hrvtvergag saasftdeaf aaagaelvda
       61 atafgadlvl kvqspvdsel atmkrgavlv gmlepfnten tarlaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vliaadlypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atarrlgavi easdvrpavk eqieslggkf idvpyetqee reaaegvggy arpmpaswla
      241 rqstavhera kqsdivitta lipgrdaptl isaetveamr pgsvivdlaa grgpglpgep
      301 gvrggncplt epdrvvtkhg vtivghtnlp amvaadassl yarnlldflk livtkegaln
      361 idmaddivaa tlltrdgala rsa
//
LOCUS       WP_107150740             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            symbiotica].
ACCESSION   WP_107150740
VERSION     WP_107150740.1
KEYWORDS    RefSeq.
SOURCE      Trinickia symbiotica
  ORGANISM  Trinickia symbiotica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Trinickia symbiotica"
                     /db_xref="taxon:863227"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39931
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaeir pgetrvagtp etvkrlaaqg havliersag erahfsdtay aqagatlvgt
       61 teawdadlvl kvqsptdgef ahlkrgrllv gmlnpfdadq aarigatgvr afalesiprt
      121 traqsmdvls sqaniagyka vllaatlyqr ffpmlmtaag tikaarvlvl gagvaglqai
      181 atarrlgavi easdvrptvk eqieslgakf ldvpyetdee reaahgvsgy arpmpaswla
      241 rqsalvhera rqadivitta lipgrtaptl ldedtvramk rgsvivdlaa grgavvngrc
      301 ggnctltgtd evvvrhgvhi agytnlpamv ateasslyar nvldflklii dadgqpkidt
      361 gddivaatll ghdastlkia
//
LOCUS       WP_107151650             535 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            symbiotica].
ACCESSION   WP_107151650
VERSION     WP_107151650.1
KEYWORDS    RefSeq.
SOURCE      Trinickia symbiotica
  ORGANISM  Trinickia symbiotica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Trinickia symbiotica"
                     /db_xref="taxon:863227"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55935
     Region          4..534
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mttiavprev hpgerrvaat pdtvaqlikl gyavtveaga gaaasfddda yrtagaeivs
       61 dtralwtgad vvvkvrppaf hprldvdesa liregatlig fvwpaqnpgl ltclaerrtn
      121 vlamdcvpri sraqkldals smanmagyra vieaahhfgr lftgqitaag kmppakvmvi
      181 gagvaglaai gaarglgaiv rafdtrpeve qqvqsmgaef lkvdveeegs gsggyakems
      241 arfieaemal faaqakeidi ivttalipgk aaptlitaem vesmrpgsvi vdmaaeqggn
      301 celtkpgevv nahgvtivgy tdlpsrmatq ssqlyatnir hlltdltpnk dgalridmnd
      361 evmrgatvvh egsivwpppa pkqpatekks sveragesan haarapgaaa qkengegarr
      421 kpgmgtlafi viaavallal gavapasfva hltvfvlavf vgyqviwnvt palhtplmsv
      481 tnaisgiivi gallqlgssn mlvttlggia lfvatiniag gflvtqrmlr mfqrn
//
LOCUS       WP_107152330             535 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            symbiotica].
ACCESSION   WP_107152330
VERSION     WP_107152330.1
KEYWORDS    RefSeq.
SOURCE      Trinickia symbiotica
  ORGANISM  Trinickia symbiotica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Trinickia symbiotica"
                     /db_xref="taxon:863227"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55770
     Region          11..535
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqptvvpkpq rigvpreifp gekrvatvpd vvekliklgf tvavesgage aanfdddayr
       61 tagaeiidsa aalwatsdiv lkvrppsdee vvlmreggll idfiwpaqnp elmrqlaaks
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvtvdyde dgaggggyak
      241 vmsegfraaq remyaqqakd vdiiittali pgkpaptlit dkmvqsmksg svivdmaaeq
      301 ggnceltvpg esvvrhgvti igytdlpsrl akqsstlyat nllrlaedlc kakdgvavid
      361 meddairglt vikngsitwp applkvapaa aprsaalpav ekksghahgs gapltakalt
      421 vifaiavalf wgvgtyapaa flghftvfvl acfigymvvw nvapalhtpl msvtnaissi
      481 iaigslvqia ppaagsngrl dglifrlafa alvltavnmf ggfavtrrml smfrk
//
LOCUS       WP_107152378             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            symbiotica].
ACCESSION   WP_107152378
VERSION     WP_107152378.1
KEYWORDS    RefSeq.
SOURCE      Trinickia symbiotica
  ORGANISM  Trinickia symbiotica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Trinickia symbiotica"
                     /db_xref="taxon:863227"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38707
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpaetv agesrvavtp etakklvalg hsvlvqsgag laaaaddaay eaagaqitdv
       61 agvfgcglil kvrapsarel emmrpgsalv gmlnpfdsag vgklaaagit afaleavprt
      121 traqsmdvls sqaniagyka vmiaadryqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgasi easdvrpsvk eqaeslgakf idvpyetdee reiaegvggy arpmpqswld
      241 rqkaavakrv aqadiaitta lipgraaptl iteemvrsmk pgsvivdlaa gkgpdgaggn
      301 cplteadrtv vkhgvtlvge tnlpalvaad asalyarnvl dfvklvlpkd adaisipddd
      361 eivaacliap qreteei
//
LOCUS       WP_107167641             477 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Pectobacterium punjabense].
ACCESSION   WP_107167641
VERSION     WP_107167641.1
KEYWORDS    RefSeq.
SOURCE      Pectobacterium punjabense
  ORGANISM  Pectobacterium punjabense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Pectobacteriaceae; Pectobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Pectobacterium punjabense"
                     /db_xref="taxon:2108399"
     gene            1..477
                     /gene="nrfA"
     Protein         1..477
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53044
     Region          4..477
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvrismsvsy lwgmvaslfl lmpaysadvp apsspapiea knstfinqhp dqfnswkats
       61 eqserhdala edpymvilwa gypfsrdynk prghayaitd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkegee gyfkgkwarg gpeitndlgc adchdtaspd faqgkpaltl
      181 srpyaerame aigkpfdsas rfgqqsmvcg qchveyyfsg kdkavkfpwd ngtkvedmek
      241 yydaisfsdw tntlsrapml kaqhpeyetw sigihgknnv tcidchmpkv knadgklytd
      301 hkignpfdny getctnchtq dkaamqavva erktaiqelk lkaeeqlvha hfeakaawda
      361 gateadmqpi lmdirhaqwr wdlavashgi hmhapdeglr mlgtslsksa eartklvrll
      421 aqkgvtgevk lpdistkeka qqaiglnmqq ikaekqdfln tvvpqwdeqa rkagrln
//
LOCUS       WP_107189678             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Photobacterium phosphoreum].
ACCESSION   WP_107189678
VERSION     WP_107189678.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium phosphoreum
  ORGANISM  Photobacterium phosphoreum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Photobacterium phosphoreum"
                     /db_xref="taxon:659"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54808
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkevl anetrvaatp ktveqllkmg fsvvvehgag alasfddaaf eaagaelast
       61 edvwqadlil kvnapqvnpa tgidefelik dgaslvsfiw paqhpellek lttkninvma
      121 mdsvprisra qaldalssma niagyravve aahqfgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaeflev dfkedtstgd gyakemsdef
      241 nkaaerlyae qakdvdiiit talipgrpap klitkemvds mksgsvivdl aaanggncay
      301 teankvitta ngvkiigytd mvgrlptqas qlygtnlvnl lkllckekdg nidinfddev
      361 lrgltvikag evtwpappik vsavpqqskt vekvqpkkae pmspvkkygm maagialfaw
      421 vghysppefl ahftvfvlac vvgyyvvwnv shslhtplms vtnaisgiii vgallqigqg
      481 sgivsalafv avliasinif ggftvtkrml emfrkdk
//
LOCUS       WP_107193363             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium tuberculosis].
ACCESSION   WP_107193363
VERSION     WP_107193363.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37573
     Region          10..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdpqtqstr vgvvaesgpd errvalvpka vaslvnrgva vvveagager allpdelyta
       61 vgasigdawa advvvkvapp taaevgrlrg gqtligflap rnadnsigal tqagvqafal
      121 eaiprisraq vmdalssqan vsgykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwldlg isapgeggya reltdderaq
      241 qqkaleeais gfdvvittal vpgrpaptlv taaaveamkp gsvvvdlage tggnceltep
      301 grtvvkhdvt iaaplnlpat mpehaselys knitalldll ikdgrlapdf ddeviaqscv
      361 trgkds
//
LOCUS       WP_107213073             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Photobacterium phosphoreum].
ACCESSION   WP_107213073
VERSION     WP_107213073.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium phosphoreum
  ORGANISM  Photobacterium phosphoreum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Photobacterium phosphoreum"
                     /db_xref="taxon:659"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54848
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkevl anetrvaatp ktveqllkmg fsvvvehgag alasfddaaf eaagaelast
       61 eevwqadlil kvnapqvnpa tgidefelik egaslvsfiw paqhpellek latkninvma
      121 mdsvprisra qaldalssma niagyravve aahqfgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaeflev dfkedtstgd gyakemsdef
      241 nkaaerlyae qakdvdiiit talipgrpap klitkemvds mksgsvivdl aaanggncay
      301 teankvitta ngvkiigytd mvgrlptqas qlygtnlvnl lkllckekdg nidinfddev
      361 lrgltvikag evtwpappik vsavpqqskt vekiqpkkae pmspvkkygm maagialfaw
      421 vghysppefl ahftvfvlac vvgyyvvwnv shslhtplms vtnaisgiii vgallqigqg
      481 sgivsvlafv avliasinif ggftvtkrml emfrkdk
//
LOCUS       WP_107236301             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_107236301
VERSION     WP_107236301.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53599
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkais
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dktalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekldfik tvipqweeqa rkngllsq
//
LOCUS       WP_107248865             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Photobacterium kishitanii].
ACCESSION   WP_107248865
VERSION     WP_107248865.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium kishitanii
  ORGANISM  Photobacterium kishitanii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Photobacterium kishitanii"
                     /db_xref="taxon:318456"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54793
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkevl anetrvaatp ktveqllkmg fsvvvehgag alasfddaaf eaagaelast
       61 ekvwqadlil kvnapqvdpa tgidefelik egaslvsfiw paqhpellek latkninvma
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaeflev dfkedtstgd gyakemsdef
      241 nkaaerlyae qakdvdiiit talipgrpap klitkemvds mksgsvivdl aaanggncay
      301 teankvitta ngvkiigytd mvgrlptqas qlygtnlvnl lkllckekdg nidinfddev
      361 lrgltvikag evtwpappik vsaasqqpkt vekvqpkkae pmspvkkygm maagialfaw
      421 vghysppdfl ahftvfvlac vvgyyvvwnv shslhtplms vtnaisgiii vgallqigqg
      481 sgivsvlafv avliasinif ggftvtkrml emfrkdk
//
LOCUS       WP_107252988             487 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Photobacterium indicum].
ACCESSION   WP_107252988
VERSION     WP_107252988.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium indicum
  ORGANISM  Photobacterium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Photobacterium indicum"
                     /db_xref="taxon:81447"
     gene            1..487
                     /gene="nrfA"
     Protein         1..487
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=54397
     Region          5..487
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mskkwtrnta amaailsalc lstnalatse qavtdenqtt tqqegmrfep rnekfaeaha
       61 eqykswkatq dseeredale sdpnmvvlwa gygfskdynk arghfyaitd vretlrtggp
      121 tddksgpmpm acwsckspdv arviddrged gyfegkwarl gaeinnaigc sdchntgsee
      181 fakggpalql srpyaerame aigkkfedqs rfdqqaqvcg qchveyyftg pkksvkfpwd
      241 kgtsvddmev yydeigfkdw thgvskapml kaqhpgyetw regihgknnv tcidchmpkv
      301 qnedgtvftd hkvgnpfdrf edtcaqchtq tkaalksvva trkasvlemk lraekqiiaa
      361 hfeakaawda gateaemepi lmdirhaqwr wdyaiashgv hmhapevalr ilgtaldkag
      421 darakvirll atkgiteeiq ipdistkvka qqalgmdmdk mnaekdeflk tivpewdkqa
      481 dareaky
//
LOCUS       WP_107272346             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Photobacterium sanctipauli].
ACCESSION   WP_107272346
VERSION     WP_107272346.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium sanctipauli
  ORGANISM  Photobacterium sanctipauli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Photobacterium sanctipauli"
                     /db_xref="taxon:1342794"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53523
     Region          1..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msnwtrntaa vaallsaifl stgvqaasee aekahiearn styakehvdq yltweatkes
       61 ediedalegd pnmvilwagy gfakdynkar ghfyalddvr ntlrtgspqd ensgpmpmac
      121 wsckspdvar vinergedgy fegkwarlgs eisntigcad chntnsedfk qgkpalalsr
      181 pyaerameai gkkfedqsrl dqqaqvcgqc hveyyfqkes hnavkfpwdl gtgvdemeiy
      241 fdnlgfadwt hglskapmik aqhpeyetwr dgihgkndvt cidchmpkvq nedgvvftdh
      301 kignpfdrfe dtcaqchtqd katlqgivst rkaqvlemkl raekqivaah feakaawdag
      361 ateeemkpil tdirhaqwrw dyaiashgvh mhapevalrv lgtaidkasd artqvvrlla
      421 tkgitepvei pdistklkaq qalgmdmeam eaekedflqn vipkweeeak vreasydk
//
LOCUS       WP_107286507             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Photobacterium kishitanii].
ACCESSION   WP_107286507
VERSION     WP_107286507.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium kishitanii
  ORGANISM  Photobacterium kishitanii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Photobacterium kishitanii"
                     /db_xref="taxon:318456"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54777
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkevl anetrvaatp ktveqllkmg fsvvvehgag alasfddaaf eaagaelast
       61 ekvwqadlil kvnvpqvdpv tgidefelik egaslvsfiw paqhpellek latkninvma
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaeflev dfkedtstgd gyakemsdef
      241 nkaaerlyae qakdvdiiit talipgrpap klitkemvds mksgsvivdl aaanggncay
      301 teankvitta ngvkiigytd mvgrlptqas qlygtnlvnl lkllckekdg nidinfddev
      361 lrgltvikag evtwpappik vsaasqqpka vekvqpkkae pmspgkkygm maagialfaw
      421 vghysppdfl ahftvfvlac vvgyyvvwnv shslhtplms vtnaisgiii vgallqigqg
      481 sgivsvlafv avliasinif ggftvtkrml emfrkdk
//
LOCUS       WP_107274313             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Photobacterium phosphoreum].
ACCESSION   WP_107274313
VERSION     WP_107274313.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium phosphoreum
  ORGANISM  Photobacterium phosphoreum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Photobacterium phosphoreum"
                     /db_xref="taxon:659"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54833
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkevl anetrvaatp ktveqllkmg fsvvvehgag alasfddaaf eaagaelast
       61 ekvwqadlil kvnapqvnpe tgidefelik egaslvsfiw paqhpalldk latkninvma
      121 mdsvprisra qaldalssma niagyravve aahqfgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaeflev dfkedtstgd gyakemsdef
      241 nkaaerlyae qakdvdiiit talipgrpap klitkemvds mksgsvivdl aaanggncay
      301 teankvitta ngvkiigytd mvgrlptqas qlygtnlvnl lkllckekdg nidinfddev
      361 lrgltvikag evtwpappik vsavpqqskt vekiqpkkae pmspvkkygm maagialfaw
      421 vghysppefl ahftvfvlac vvgyyvvwnv shslhtplms vtnaisgiii vgallqigqg
      481 sgivsvlafv avliasinif ggftvtkrml emfrkdk
//
LOCUS       WP_107299837             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Photobacterium rosenbergii].
ACCESSION   WP_107299837
VERSION     WP_107299837.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium rosenbergii
  ORGANISM  Photobacterium rosenbergii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Photobacterium rosenbergii"
                     /db_xref="taxon:294936"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53734
     Region          1..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msnkwtrnta avaallsaif lsgnalanee qpaekeriea rneafaaaha dqyksweatk
       61 esdhiedale gdpnmvilwa gygfakdynk arghyyaltd vretlrtggp qdansgpmpm
      121 acwsckspdv arviderged gyfegkwarl gseisntigc adchntnsed fkqgkpalal
      181 srpyaarame aidkkfedgs rldqqaqvcg qchveyyfqk qshnsvkfpw dmgtgvdeme
      241 vyfdnigfsd wthglskapm ikaqhpeyet wrdgihgknn vtcidchmpk vqnedgvvft
      301 dhkignpfdr fedtcancht qdketlqgiv strkaqvlem klraekqiva ahfeakaawd
      361 agateeemkp iltdirhaqw rwdyaiashg vhmhapeval rvlgtaldka adarakvvrl
      421 latkgitdpv eipdistklk aqqalgmdmd amnqekedfl ntvvpkweee akvreasyde
      481 k
//
LOCUS       WP_107291204             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Photobacterium sp. GB-36].
ACCESSION   WP_107291204
VERSION     WP_107291204.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium sp. GB-36
  ORGANISM  Photobacterium sp. GB-36
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Photobacterium sp. GB-36"
                     /db_xref="taxon:2022108"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54868
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprevl ahetrvaatp ktveqilkmg fsvvveqgag rlasfddaay eaagatvvst
       61 devwqsdlif kvnapqvnpv tgvdefelik egaslvsfiw paqnpellek lsskninima
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaeflev dykedtstgd gyakemsdef
      241 nkaaerlyae qakdvdiiit talipgrpap klitkemvds mksgsvivdl aaanggncay
      301 teadkvvttp ngvkvigytd mvgrlptqss qlygtnlvnl lkllckekdg nidinfddev
      361 lrgltvvkag eltwpappik vsaaaqqpka aakvepkvee paspvkkfgl mgagialfaw
      421 ianyapaefl thftvfvlac vvgyyvvwnv shslhtplms vtnaisgiii vgallqigqg
      481 ngvvsflafi avliasinif ggftvtkrml emfrkdk
//
LOCUS       WP_107312155             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia metallica].
ACCESSION   WP_107312155
VERSION     WP_107312155.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54781
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigvple taheerrvat vpdvveklik lgfsvavqsg agtganfsdd dyraagaevv
       61 asaadlwgrs dvvlkvrpps sdevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvve elcknkdgti nvdfnddair
      361 gltviqegnv twppppiqqp aavpkpaapp vaaaaskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa adgrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_107312167             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia metallica].
ACCESSION   WP_107312167
VERSION     WP_107312167.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39701
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaesv agearvaatp etvrklaaqg hevlvqagag eranftdday assgatlvda
       61 qraleadvvl kvqaptdtei allrtgavli gmldpfnaer aarlttagit afaleaiprt
      121 traqsmdvls sqaniagyka vliaaglyqr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrmgavi easdvrpavk eqieslgakf ldvpfetnee reaaegtggy arpmpaswla
      241 rqsalvrera saadiviata lipgrtaptl lpedivrdmk pgsvivdlaa grgaqtdgrr
      301 ggncpltepd rvvtrhgvhi agftnlpamv asdasslyar nvfdflklii dddgrlridt
      361 tddivaatlf ghdashqqsa
//
LOCUS       WP_107324192             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Phaeovulum
            veldkampii].
ACCESSION   WP_107324192
VERSION     WP_107324192.1
KEYWORDS    RefSeq.
SOURCE      Phaeovulum veldkampii
  ORGANISM  Phaeovulum veldkampii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Phaeovulum.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Phaeovulum veldkampii"
                     /db_xref="taxon:33049"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55003
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egearvamtp dsalqlqklg hecfvesgag akagfadaay aaagvtvlpd
       61 aaalfgavdv vakvrppvaa evdlmrkgqt lisffwpaqn aellerakar gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg anfvylefee aqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrdapkl wlddmvkamk pgsvvvdlaa erggncdltv
      301 pdqkvvsdng vtiigytdfp srmaaqastl ystnirhmma dltpkkdgvi vhnmeddvir
      361 gatvthdgai tfpppppkva aisaakpkek pkeltpeekk aaekaafrkq trdqvallvi
      421 ggglllaagl vapasfmqhf ivfvlsvfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsggfl alvlaalsvf maginifggf mvtrrmlamf qks
//
LOCUS       WP_107326533             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_107326533
VERSION     WP_107326533.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53748
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaecklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dsrtklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_107345789             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodopseudomonas palustris].
ACCESSION   WP_107345789
VERSION     WP_107345789.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39008
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeqd paeprvaatp dtvkklkalg aevavepgag lksglpdsdf taagatvsad
       61 alkdadvvfk vkrpeasela sykrgalvla imdpygndaa lksmadagia afamelmpri
      121 traqvmdvls sqanlagyra vidgaetfgr ampmmmtaag tvpaakvfim gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpaprlvta emvksmkpgs vlvdlaverg gnvegavpgq
      301 ivetngvkiv gytnvagrva asasalyarn llsffetlvn kekalavnwd delvkatalt
      361 rdgavvhpnf qpksa
//
LOCUS       WP_107340774             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agrobacterium pusense].
ACCESSION   WP_107340774
VERSION     WP_107340774.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium pusense
  ORGANISM  Agrobacterium pusense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Agrobacterium pusense"
                     /db_xref="taxon:648995"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55844
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtpkely egearvgmtp dsaqalqklg ydcvieagag kaagfsdday raagvtvvds
       61 aealytgsdi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qqqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvamm kpgsviidla aerggncdlt
      301 vpdqrvvsdn gvivigytdf psrmatqast lyatnirhmm tdltpakdgk vvhnmeddvi
      361 rgatvtyrge itypppppki qaiaaqkpke rakeltpeek hakekaefka qtksqvgllv
      421 agtavlllvg lyapasfmsh fivfvlacfi gfqviwnvsh slhtplmavt naisgiviig
      481 allqigsgnw lvvilaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_107348602             479 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Photobacterium lutimaris].
ACCESSION   WP_107348602
VERSION     WP_107348602.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium lutimaris
  ORGANISM  Photobacterium lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Photobacterium lutimaris"
                     /db_xref="taxon:388278"
     gene            1..479
                     /gene="nrfA"
     Protein         1..479
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53432
     Region          1..477
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msnkwtrnta avaallsaif lsgnafateq paekeriear neafaaehad qyktweatke
       61 seqiedaleg dpnmvilwag ygfakdynka rghfyavtdv retlrtggpk densgpmpma
      121 cwsckspdva rvidergedg yfdgkwarlg seinnaigca dchntnsedf kqgkpalals
      181 rpyaaramea igkkfedgsr ldqqaqvcgq chveyyfqkq sknavkfpwd mgtgvdemev
      241 yfdnigfsdw thgvskapmi kaqhpeyetw rdgihgknnv tcidchmpkv qnedgvvftd
      301 hkvgnpfdrf edtcanchtq dketlqgivs trkaqvlemk lraekqivaa hfeakaawda
      361 gateeemkpi ltdirhaqwr wdyaiashgv hmhapevalr vlgtaldkaa daranvvrll
      421 atkgitdpve ipdistklka qqalgmdmda mnqekedfln tvvpkweeea kareasydq
//
LOCUS       WP_107356777             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhodopseudomonas].
ACCESSION   WP_107356777
VERSION     WP_107356777.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas
  ORGANISM  Rhodopseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rhodopseudomonas"
                     /db_xref="taxon:1073"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39026
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeqd paeprvaatp dtvkklkalg aevavepgag lksglpdsdf taagatvsad
       61 alkdadvvfk vkrpeasela sykrgalvla imdpygndaa lksmadagia afamelmpri
      121 traqvmdvls sqanlagyra vidgaetfgr ampmmmtaag tvpaakvfim gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpaprlvta emvksmkpgs vlvdlaverg gnvegavpgq
      301 ivetngvkiv gytnvagrva asasalyarn llsffetmvn kekalavnwd delvkatalt
      361 rdgavvhpnf qpksa
//
LOCUS       WP_107402554             508 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Shewanella].
ACCESSION   WP_107402554
VERSION     WP_107402554.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53412
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevvieanag qlssfddaaf eaagakvttd
       61 vwqadlifkv napsdaeieq ikdgatvvsf iwpaqnpelv eklskrkinv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggqfl kldfgneegg ssdgyaktms defiaaemal
      241 faeqakevdi iittalipgr papklitkam vdsmkpgsvi vdlaaatggn ceytqsgelf
      301 vtpngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgtasinfd dvvmrnmtvi
      361 kegevtfppp pisvsaapak paakiepkdt tpkapsklkf vlaalgiagf aavasvappe
      421 flshftvfll scvvgyyvvw nvshslhtpl msvtnaisgi ivvgallqig qgstlvtvla
      481 fiavliasin ifggftvtqr mlkmfrkd
//
LOCUS       WP_107451447             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinacidiphila rubida].
ACCESSION   WP_107451447
VERSION     WP_107451447.1
KEYWORDS    RefSeq.
SOURCE      Actinacidiphila rubida
  ORGANISM  Actinacidiphila rubida
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Actinacidiphila.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Actinacidiphila rubida"
                     /db_xref="taxon:310780"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52292
     Region          8..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mseaaaqqig vvaesgtget rvaatpqtvk qllalgyevv vesgagtasg fsddaygeag
       61 aqvadawqad vvlkvnapsh eeiarlrega tligligagq spelveelaa rpitvlamda
      121 vprisraqsm dvlssmania gyravieaah vfgrfftgqv taagkvppak vlvagagvag
      181 laaigaagsl gavvratdpr pevadqvrsl ggeflaveva qeestdgyak atsedydrra
      241 aeiyheqaad vdviittali pgrpaprlvt aedvaamkpg svivdmaaaq ggnvagtvag
      301 ravvtengvt iigytdlagr lpaqasqlyg tnlvnllkll tpgkdgqlvl dfddvvqrsv
      361 tvvrdgektw ppppvkvsaa papalaaaaa papekkgltp aarfgligag maalflliaf
      421 spaqlvgnft vfvlavvigy yvigkvhhal htplmsvtna isgivivgal lqfghdrvav
      481 svlafaaill tsinifggfa vtrrmlsmft kg
//
LOCUS       WP_107497587             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassobius sp. I31.1].
ACCESSION   WP_107497587
VERSION     WP_107497587.1
KEYWORDS    RefSeq.
SOURCE      Thalassobius sp. I31.1
  ORGANISM  Thalassobius sp. I31.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Thalassovita.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Thalassobius sp. I31.1"
                     /db_xref="taxon:2109912"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55490
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapketf agearvamtp dsakqlqklg ydcaiesgag eaagfsnamy keagvevlkt
       61 gaalfkacdi vakvrqpdat elkrldkgqt lisffnpaan degmeaakak ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee eqadgassgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwteemvqam rpgsvivdla aekggncklt
      301 vmdekivtdn gvtivgytdf psrmaaqast lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgatvtfege itfpppppkv qaiaaqpkve vkeltpeekr aeevaafkke trnqvtligv
      421 gaafllavgl vapasfmqhf ivfvlsvfig fqviwgvahs lhtplmavtn aissivilga
      481 mtqigsgsfl villsalavf mcginifggf mvtrrmlamf qks
//
LOCUS       WP_107570545             508 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Solirubrobacterales].
ACCESSION   WP_107570545
VERSION     WP_107570545.1
KEYWORDS    RefSeq.
SOURCE      Solirubrobacterales
  ORGANISM  Solirubrobacterales
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Solirubrobacterales"
                     /db_xref="taxon:588673"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52038
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mnigvlkeaq agetrvaatp atvaqllklg yevvvepgag aaasfsdeay aeagatvgdp
       61 laadivfgvn tptaaqldgl kegatlisll spmlkpeive dlakrpital smdavprisr
      121 aqsldvlssm aniagyravv eaahvfgrff tgqvtaagkv ppatvlvagv gvaglaaiga
      181 agslgaivya tdprpevadq vaslggeyls vesdevevsa tgyakemsdd yntraaalya
      241 ekvpdvdili ttalipgrpa prlitaemva smkpgsvivd maainggnve gsvageavvt
      301 dngvtiigyt dlagrlpaqa sqlygtnlvn lmklmtpekd gqlvldfedv vqramtvvrq
      361 geltwpppkv evsaapaaap aaapapaaep papmtdekrl tivgvaalvf flivsqapna
      421 linqlfvfsl aivvgyyvig hvhhalhtpl msvtnaisgi ivvggllqig qgddaitivs
      481 alaillasin ifggfavtrr mlamftrs
//
LOCUS       WP_107606268             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium tuberculosis].
ACCESSION   WP_107606268
VERSION     WP_107606268.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37519
     Region          10..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdpqtqstr vgvvaesgpd errvalvpka vaslvnrgva vvveagager allpdelyta
       61 vgasigdawa advvvkvapp taaevgrlrg gqtligflap rnadnsigal tqagvqafal
      121 eaiprisraq vmdalssqan vsgykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwldlg isasgeggya reltdderaq
      241 qqkaleeais gfdvvittal vpgrpaptlv taaaveamkp gsvvvdlage tggnceltep
      301 grtvvkhdvt iaaplnlpat mpehaselys knitalldll ikdgrlapdc ddeviaqscv
      361 trgkds
//
LOCUS       WP_107608401             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium meliloti].
ACCESSION   WP_107608401
VERSION     WP_107608401.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39614
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfiake sdpnegrvag svesvkklks lgfdvvveag aglgsripdq eyekagarvg
       61 taadaktadv ilkvrrpsah eisgyrsgav viaimdpygn eeaisamaga glttfamelm
      121 pritraqsmd vlssqanlag yqavidaaye ydralpmmmt aagtvpaaki fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsreyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vtremldsmk pgsvavdlav erggniegae
      301 agkvtevggv rivghlnvag riaasaslly aknlvtflet mvsketkala lnmedelvka
      361 talthggavv hpafggamrg ek
//
LOCUS       WP_107649151             431 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium helmanticense].
ACCESSION   WP_107649151
VERSION     WP_107649151.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium helmanticense
  ORGANISM  Mesorhizobium helmanticense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Mesorhizobium helmanticense"
                     /db_xref="taxon:1776423"
     Protein         1..431
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44212
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgldvivesg agtasripde efakagaaig
       61 kagdaaradv vlkvrrptda elkgyrsgaa viaimdpygh daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvttang vkivghlnvp grvaasasll yarnlfafle tlvdkttkql ainrddelvk
      361 atmltdggkv vhpafakatv dphvepaaip attmvadasv kkaaprktad kkaatgksaa
      421 qksagkpkgi a
//
LOCUS       WP_107654392             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            suismassiliense].
ACCESSION   WP_107654392
VERSION     WP_107654392.1
KEYWORDS    RefSeq.
SOURCE      Nocardia suismassiliense
  ORGANISM  Nocardia suismassiliense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Nocardia suismassiliense"
                     /db_xref="taxon:2077092"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38256
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mettqsvgae sprgarvgvv resnagerrv alvpkiipsl lkqgvqvvve sgaglgalip
       61 dsayeaagat igdpwsaevi vkvappsdae vaklsdgqtl igflaprnae nqigklksag
      121 vqafaveaip risraqvlda lssqanvagy kavllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rttgydvrpe vadqvrsvga qwldlgidaa geggyarelt
      241 deekakqqqa ledaikgfdv vittalvpgr paprlvtaaa vegmkpgsvi vdlagetggn
      301 celtepgevv vkhevtiasp lnlpatmpeh aselysknis allelmlvdg klapdfsdqv
      361 ladscvtrev ea
//
LOCUS       WP_107670359             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Cyanothece
            sp. BG0011].
ACCESSION   WP_107670359
VERSION     WP_107670359.1
KEYWORDS    RefSeq.
SOURCE      Cyanothece sp. BG0011
  ORGANISM  Cyanothece sp. BG0011
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Gomontiellales;
            Cyanothecaceae; Cyanothece.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Cyanothece sp. BG0011"
                     /db_xref="taxon:2082950"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40754
     Region          2..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mlkiavpkes dlgelrvalv pdivarfikl gfevlvqsga ghgahftdse yeaagatiin
       61 sakelwesad illkvappge qqgeeemnwl kpgatlisfl nplanpeqiq alaqrkinaf
      121 smemiprtsr aqsmdalssq aniagyksal iaaaslprlf pmmttaagti ppakvlviga
      181 gvaglqaiat arrlgavvea fdvrpavkee vqsvgakfie ipieedtatt ggyakevgqs
      241 tqekirqvlt ehikksdvvi ttaqvqgkra plivteemvg qmnpgavivd laagqggnca
      301 cteagkdvyy ngvtiigpln lpatlpvdss kvyaknlltl vkyvvkdgai dfnfeddivd
      361 gtcvtyegev rnervknala tlvqa
//
LOCUS       WP_107673878             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudogemmobacter blasticus].
ACCESSION   WP_107673878
VERSION     WP_107673878.1
KEYWORDS    RefSeq.
SOURCE      Pseudogemmobacter blasticus
  ORGANISM  Pseudogemmobacter blasticus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudogemmobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudogemmobacter blasticus"
                     /db_xref="taxon:1075"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55213
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaltevf agenrvamtp esalaiqklg hscciqsgag dkagftdaay aaagvevlad
       61 akavlaaadv vvkvrgpeek eakalrqgqt lisffwpaqn pdlletvkaq gatvvamdmv
      121 prisraqkmd alsstanlag yravieaann fprfftgqvt aagkvppakv lvvgagvagl
      181 aaigasvslg aityafdvrp evaeqiesmg aefvyldfae qtqdgaatgg yaapsspefr
      241 eaqlkkfrel apdmdivitt alipgrpapk lwtedmvram krgsvivdla aerggncdlt
      301 vpdekivtdn gvtivgytdf psrmatqass lysnnirhml adltpkkdgv ivhnmeddvi
      361 rsatvahdga itypppppkv qaiaaakpke kareltpeer kaqeaaafkq qtrnqvvmla
      421 aggalmglvg lyapasfmsh fivfvlacfv gfqviwnvsh slhtplmavt naisgiivlg
      481 allqigsgnf fvlilaavsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_107675965             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agrobacterium sp. LAD9].
ACCESSION   WP_107675965
VERSION     WP_107675965.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. LAD9
  ORGANISM  Agrobacterium sp. LAD9
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Agrobacterium sp. LAD9"
                     /db_xref="taxon:2055153"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55740
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely egearvgmtp dsaqalqklg ydciletgag kaagfsdday raagvtivds
       61 adalyagadi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfae qqdgaatggy aapsspefre
      241 kqlekfrela pqidivitta lipgrdapkl wladmvammk pgsviidlaa erggncdltv
      301 pdqrvvsdng vivigytdfp srmatqastl ystnirhmmt dltpakdgkp vhnmeddvir
      361 gatvtyqgei tfpppppkiq aiaaqkpker akeltpeekh akeradfkaq tknqvgllvi
      421 gtavlllvgl yapvsfmshf ivfvlacfig fsviwnvshs lhtplmavtn aisgiviiga
      481 llqigsgnwl vvilaslsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_107688425             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            wadsworthii].
ACCESSION   WP_107688425
VERSION     WP_107688425.1
KEYWORDS    RefSeq.
SOURCE      Neisseria wadsworthii
  ORGANISM  Neisseria wadsworthii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Neisseria wadsworthii"
                     /db_xref="taxon:607711"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53846
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipketl aletrvagtp stvtqlqklg fevvvekgag laaslddaay eaagatvadt
       61 aevwscpliy kvnapsenei eylnagqtlv sflwpaqnpe lvqkltdqkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vkafdtrlev aeqiesmggq flkldfpqes ggsgdgyakv mseefiaaem
      241 klfaeqaqqv diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lfvsdngvki igytdmanrl agqssqlyat nlvnlsklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp ppaiqvsaap qqqaqaatva kpepkpvptw kklapaviga vlvlwmgava
      421 paeflnhfiv fvlacvigyy vvwnvshslh tplmsvtnai sgiivvgall qigqgngvvs
      481 llafiavlia sinifggfyv trrmlnmfrk g
//
LOCUS       WP_107693371             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Nitrosospira].
ACCESSION   WP_107693371
VERSION     WP_107693371.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nitrosospira
  ORGANISM  unclassified Nitrosospira
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="unclassified Nitrosospira"
                     /db_xref="taxon:2609267"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39399
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipveir ggetrvaatp etvkkftakg lhavlvqsga gagasipdea fqaaganiig
       61 saaelydqsq illkvrspea gelalipkda vllgllsphh vegieslarh gvtafamerl
      121 prisraqsmd vlssqaniag ykavlmaanv yqkffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avieafdvrp vakeqveslg akfvevplsd eeraqaetag gyaremsddy
      241 krrqgelvhq rasaadiiis talipgrpap vlikeetvra mkpgsvivdm aveaggncpl
      301 semdkivvkh gvhligisnl pglvaadasa lyarnlmnfl nlmldpkngd fvmnredevi
      361 agtlvctgge virkt
//
LOCUS       WP_107707330             380 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Paraburkholderia].
ACCESSION   WP_107707330
VERSION     WP_107707330.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paraburkholderia
  ORGANISM  unclassified Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="unclassified Paraburkholderia"
                     /db_xref="taxon:2615204"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39371
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvaqg hrvtiqsgag ggasfpddal aaagaeivda
       61 atafgadlvl kvqspteael pllkrgatlv gmldpfnaen aqqlaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlq
      241 rqsalvhera kqadvvista lipgraaptl lsvetvqamk pgsvlvdlaa grgadyegrr
      301 ggncpltead kvivrhgvti vgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll trdgevarka
//
LOCUS       WP_107748046             527 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Dietzia
            psychralcaliphila].
ACCESSION   WP_107748046
VERSION     WP_107748046.1
KEYWORDS    RefSeq.
SOURCE      Dietzia psychralcaliphila
  ORGANISM  Dietzia psychralcaliphila
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Dietzia psychralcaliphila"
                     /db_xref="taxon:139021"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53700
     Region          17..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mspqtevkdt aaapsvigvv aesdaaenrv aatpatvakl iglgyrvvve ngagtraefs
       61 daayaesgad lvsgdvawss dvvlkvavpt etevarlrsg atlvgllapa qnerllsvla
      121 ergvtalamd avprisraqs mdvlssmani agyravieaa hhfgrfftgq vtaagkvppa
      181 kvlvagagva glaaigaass lgaivrstdp rpevadqvks iggeylpvev pdeekevstd
      241 gyakatseay draaadlysa qaadvdivit talipgrpap rlltaadvas mkrgsvivdm
      301 aaaqggnveg svadevvvte ngvtiigytd lagrlpaqas qlygtnlvnl tklvtpdkdg
      361 rwaldlddvv qrgvtvakgg eimwppppvq vsaapaaaaa apleprpekk klsagarlgl
      421 iatgmallll ltavapgdip rhitvfvlai vigyyvignv hhalhtplms vtnaisgviv
      481 vgallqigid ntaglvlati ailvasinvf ggfavtrrml gmfskga
//
LOCUS       WP_107752126             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pararhodobacter aggregans].
ACCESSION   WP_107752126
VERSION     WP_107752126.1
KEYWORDS    RefSeq.
SOURCE      Pararhodobacter aggregans
  ORGANISM  Pararhodobacter aggregans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pararhodobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Pararhodobacter aggregans"
                     /db_xref="taxon:404875"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55220
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif pgenrvamtp dsalqlqklg hscvietgag aasgfedaay aaagveivps
       61 adalfaaadv vvkvreatae emgrlrpdqt liaffwpaqn aemlelakek gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqiesmg aefvyldfae aqqdgaatgg yaapsspefr
      241 eaqlkkfrel apevdivitt alipgrpapk lwtedmvamm krgsvivdla aerggncdlt
      301 vkdqkivtpn gvtivgytdf psrmgtqast lyannirhmi fdltpgkdgv inhnmeddvi
      361 rgatvakdga itfpppppki qaiaavkrek pkeltpeekr aqevaafkaq tkqqvtllav
      421 gggllllaga fapasfmahf ivfvlavyvg fqviwnvshs lhtplmaitn aissiiilga
      481 lmqigsgswl vmilaalsvl magvnifggf mvtrrmlamf qks
//
LOCUS       WP_107757892             527 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Dietzia].
ACCESSION   WP_107757892
VERSION     WP_107757892.1
KEYWORDS    RefSeq.
SOURCE      unclassified Dietzia
  ORGANISM  unclassified Dietzia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="unclassified Dietzia"
                     /db_xref="taxon:2617939"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53930
     Region          17..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mspqtevpdp aaapsvigvv aesdpserrv aatpatvakl iglgyrvvve ngagtraefs
       61 daayadagad lvdgdtawss dvvmkvavpt etevtrlrpg atlvgllapa qnerllsvla
      121 ergvtalamd avprisraqs mdvlssmani agyravieaa hhfgrfftgq vtaagkvppa
      181 kvlvagagva glaaigaass lgaivratdp rpevadqvks iggeylpvev pdeekvvstd
      241 gyakatseay draaaalysa qaadvdivit talipgraap rlltaadvas mrrgsvivdm
      301 aaaqggnveg svadevvvte ngvtiigytd lagrlpaqas qlygtnlvnl tklvtpdkdg
      361 rwsldlddvv qrgvtvardg evlwppppvq vsaapaaaaa epleppaekk klsprarlgl
      421 iatgmallll ltavapgdip rhitvfvlai vigyyvignv hhalhtplms vtnaisgviv
      481 vgallqigid ntvgqvlati ailvasinvf ggfavtrrml gmfskga
//
LOCUS       WP_107761452             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosospira multiformis].
ACCESSION   WP_107761452
VERSION     WP_107761452.1
KEYWORDS    RefSeq.
SOURCE      Nitrosospira multiformis
  ORGANISM  Nitrosospira multiformis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosospira multiformis"
                     /db_xref="taxon:1231"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39158
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaetr ggetrvaatp etvkkftakg lhvvlvqsga gagasipdae yqaagasivt
       61 dpgelygqsq ivlkvrapea aelalmrkda vligllsphq aegietlaah gitafsmekl
      121 prisraqsmd vlssqaniag ykavlmaani yqkffpmlmt aagtvkaarv lvlgagvagl
      181 qaiatakrlg avieafdvrp aakeqveslg akfvevslsd eekaqaettg gyaremsedy
      241 krrqgelvhq rasaadiiit talipgrpap vlireetvra mkpgsvivdl aveaggncpl
      301 selnkvvvkh gvhlvgianl pglvaadssa lyarnlmnfl nlmldaktge lninredeii
      361 agtlvcange vigkt
//
LOCUS       WP_107766306             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides terrigena].
ACCESSION   WP_107766306
VERSION     WP_107766306.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides terrigena
  ORGANISM  Nocardioides terrigena
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Nocardioides terrigena"
                     /db_xref="taxon:424797"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53353
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresr egetlvaatp ttagqlqalg yevvvergag iaaaqpddaf eaagirvgda
       61 eevwtsdvvv kvnaptpdei wrlragatvi slmaparspk lveqlqaqrv tglamdavpr
      121 israqamdvl ssmanvagyr avveaahafg rqftgqvtaa gkvpparvfv vgagvaglaa
      181 igaagsmgai vrafdvrpev aeqvesmgae fvtvdmeqev ssdgyakemt adqeaataam
      241 ydeearnadi vittalipgr paprlitaet vaamrtgsvi vdmaaanggn veltrtdekv
      301 vtdnlvtilg ytdlagrlaa qtsqlygtnv vnllklmtpg kdgelvldle dvvvrgitva
      361 rdgesmwppp pvqvsaapaa avaapaeaqk avekrppdpr rkwygaglaa vlfalvaays
      421 ppdflghftv fvlavfvgyy visnvahalh tplmsetnai sgiilvggil qvgsdntvvt
      481 vlaliavlva sinifggflv tlrmlemfrk d
//
LOCUS       WP_107773075             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides sediminis].
ACCESSION   WP_107773075
VERSION     WP_107773075.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sediminis
  ORGANISM  Nocardioides sediminis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Nocardioides sediminis"
                     /db_xref="taxon:433648"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53504
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresr egetlvaatp ttagqlqalg yevvvergag taadqpdaaf eaagirvtda
       61 devwssdvvv kvnapnpdei wrlragttvv slmaparspk lieqlqaqkv tglamdavpr
      121 israqamdvl ssmanvagyr avieaahafg rqftgqvtaa gkvpparvfv vgagvaglaa
      181 igaagsmgav vrafdvrpev aeqvesmgae fvtvdmeqev ssdgyakemt aeqeaataam
      241 ydeearnadi vittalipgr paprlitaet vagmrtgsvi vdmaaanggn veltradeev
      301 vtdnlvtilg ytdlagrlaa qtsqlygtnv vnlfklltpg kdgelvldld dvvvrgitva
      361 rdgesmwppp pvqvsaapaa pavappapvd gkevvakppp dprrkwyaag laavlfalva
      421 aysppdflgh ftvfalavfv gyyvisnvah alhtplmset naisgiiivg gilqvgsdnl
      481 avtvlalvav lvasinifgg flvtlrmlem frkd
//
LOCUS       WP_107801503             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Chromobacterium].
ACCESSION   WP_107801503
VERSION     WP_107801503.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium
  ORGANISM  Chromobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Chromobacterium"
                     /db_xref="taxon:535"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38598
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhiaipaerl agehrvaatp dtvkklvagg havtvesgag laaaqpdaay qeagaaiaad
       61 raaalaqadi vltvrplded giaalkdgaa ligqlnpyhn hslpalaakr vsafalellp
      121 rstraqsmdv lssqnniagy ravllatqhy prfmpmlmta agtvkparll ilgvgvaglq
      181 aiatgkrlga vveafdvrpa tkeqveslga kfievpmsee ekmansgvya kemsesyrqr
      241 qgelvakhak aadivittal ipgkpapkll sadvvaemkp gsvivdlaae tggncaltrp
      301 getvrldngv tvvgqtnlpg llaadassly aknlltflgl lltpeglnln ledeilsatl
      361 vthagqvrfp aad
//
LOCUS       WP_107802015             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas oligotropha].
ACCESSION   WP_107802015
VERSION     WP_107802015.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas oligotropha
  ORGANISM  Nitrosomonas oligotropha
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas oligotropha"
                     /db_xref="taxon:42354"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39159
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir ggetrvaatp etvkkytakg vhkvsvqsga gagasipdsa yqeagativa
       61 dvaelyaqaq iilkvrgpes telamirkda vllglltphh kesvdaltqh gltafamekl
      121 prisraqnmd vlssqaniag ykavimaanv yqkffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avveafdvrp avkeqveslg akfvevplsd eekakaetag gyatemsddy
      241 krrqgelvhe raiaadiiit talipgrpap vlikeetvqa mkpgsvivdm aveaggncpl
      301 selnqtvvkh gvhligianl pglvaadast lyarnlmnfl nlmldpasge lkidrtdeii
      361 agtllcggge iaats
//
LOCUS       WP_107814336             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            sicca].
ACCESSION   WP_107814336
VERSION     WP_107814336.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sicca
  ORGANISM  Neisseria sicca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria sicca"
                     /db_xref="taxon:490"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54011
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacplly kvnapsegel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafd rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkkltpavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_107816346             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Celeribacter persicus].
ACCESSION   WP_107816346
VERSION     WP_107816346.1
KEYWORDS    RefSeq.
SOURCE      Celeribacter persicus
  ORGANISM  Celeribacter persicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Celeribacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Celeribacter persicus"
                     /db_xref="taxon:1651082"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55769
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgvpkevf egearvaltp esarqlqklg ydcaiqsgag aaagfsdaay aeagvevieg
       61 akalwdacdi vakvrqpdet emgylrkgqt lisffnpggn aegmekaket ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgsatgg yasvqseefr
      241 naqlakfrel apemdivitt alipnrpapv lwtkdmveam kpgsvivdla aerggnvegt
      301 vkdervvtdn gvviigytdf psrmatqast lyatnirhmm tdltpekdgk vvhnmeddvi
      361 rgatvtydhe itfpppppkv aaiaakpkek pkeltpeekr aaevaafkkq trnqvtliav
      421 gailllgvgl vapasfmqhf ivfvlsvfig fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgswl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_107819930             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            bergeri].
ACCESSION   WP_107819930
VERSION     WP_107819930.1
KEYWORDS    RefSeq.
SOURCE      Neisseria bergeri
  ORGANISM  Neisseria bergeri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria bergeri"
                     /db_xref="taxon:1906581"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53915
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsegel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_107825715             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            sicca].
ACCESSION   WP_107825715
VERSION     WP_107825715.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sicca
  ORGANISM  Neisseria sicca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria sicca"
                     /db_xref="taxon:490"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54031
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qaagatvadk
       61 etvwacplly kvnapsegel pllkegqtiv sflwprqnea lvqkladkkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqtkev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fkdviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf yvtrrmlnmf rkg
//
LOCUS       WP_107842240             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            sicca].
ACCESSION   WP_107842240
VERSION     WP_107842240.1
KEYWORDS    RefSeq.
SOURCE      Neisseria sicca
  ORGANISM  Neisseria sicca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria sicca"
                     /db_xref="taxon:490"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53989
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacplly kvnapsesel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfitdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasvnifggf yvtrrmlnmf rkg
//
LOCUS       WP_107844788             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Litoreibacter ponti].
ACCESSION   WP_107844788
VERSION     WP_107844788.1
KEYWORDS    RefSeq.
SOURCE      Litoreibacter ponti
  ORGANISM  Litoreibacter ponti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Litoreibacter.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Litoreibacter ponti"
                     /db_xref="taxon:1510457"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55935
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkvgapketf agenrvamtp esalqiqklg htcliqsgag enagfsdaay keagvevvkt
       61 akalwdeadi vakvrqpdas emkrlrdgqt lisffnpaan ekmmesaaks ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvflefee ssqdsaatgg yaapsspefr
      241 ekqlekfrem apdidivict alipnreape lwtedmvqam kpgsvivdla aekggncklt
      301 vmdekivtdn gvtiigytdf psrmatqast lygnnirhml tdltpekdgv lnhnmeddvi
      361 rgatvtfdke itypppppkv aaiaaapkke kpkeltpeek raeeaaafak etktqvglia
      421 igaalvlgvg lipgmpasfm qhfivfvlsv figfqviwgv ahslhtplma vtnaissiii
      481 lgaliqigst sllitllaal gvfmasvnif ggflvtrrml amfqks
//
LOCUS       WP_107853196             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oceanimonas marisflavi].
ACCESSION   WP_107853196
VERSION     WP_107853196.1
KEYWORDS    RefSeq.
SOURCE      Oceanimonas marisflavi
  ORGANISM  Oceanimonas marisflavi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Oceanimonas.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Oceanimonas marisflavi"
                     /db_xref="taxon:2059724"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53537
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipretl sgetrvaatp ksveqlrklg fevcveqgag skasfedtay qaagaqlvsa
       61 devwqsaiiy kvnaptpeei erlqagttlv sfiwpaqnpe lveqlkskgv tvlamdmvpr
      121 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvlv igagvaglaa
      181 igaagslgai vrafdtrpev keqinsmgae fleldyeeds dssdgyakem sqafidaema
      241 lfmeqakevd iivttalipg kpapklitad mvaamapgsv ivdlaaqngg nceltkpgel
      301 fvsdngvkii gytdlngrlp tqsstlyatn lvnlakllck ekdgninvdf ddvvlrnmtv
      361 trdgevtfpp paisvsaapk akaaaqpaae phpkkpsnlk yylggagvll fawlaavapa
      421 eflshitvfv lacivgyyvi wnvshslhtp lmsvtnaisg iivvgalsqv gsggfvsfla
      481 fvavliasin vfggftvthr mlkmfrkg
//
LOCUS       WP_107853390             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            elongata].
ACCESSION   WP_107853390
VERSION     WP_107853390.1
KEYWORDS    RefSeq.
SOURCE      Neisseria elongata
  ORGANISM  Neisseria elongata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria elongata"
                     /db_xref="taxon:495"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54177
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkesl agetrvactp atvaqlqklg fdvvvengag lgasfddaay eeagatvaaa
       61 aevwkcpliy klnapngnec rrlkegqtlv gflypnqnee lvrkladkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapeaflnhf ivfvlscvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vsllafiail iasinifggf yvtrrmlnmf rkg
//
LOCUS       WP_107855609             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            weaveri].
ACCESSION   WP_107855609
VERSION     WP_107855609.1
KEYWORDS    RefSeq.
SOURCE      Neisseria weaveri
  ORGANISM  Neisseria weaveri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Neisseria weaveri"
                     /db_xref="taxon:28091"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53654
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl pgetrvactp atvtqlqklg fevvvergag laaslddaay eaagavaada
       61 aevwacpliy kvnapsesea grlnagqtlv sflwpaqnpe lvqkltdkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vkafdtrlev aeqiesmggq flkldfpqea ggsgdgyakv mseefiaaem
      241 klfaeqarqv diiittaaip gklapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvsdngvki igytdmanrl agqssqlyat nlvnlsklls pnkdgeiald fedviirnmt
      361 vtrdgeitfp ppaiqvsaap qqqaqaapva kpepkpvptw kklapaviga vlvlwmgava
      421 paeflnhfiv fvlacvigyy vvwnvshslh tplmsvtnai sgiivvgall qigqgngvvs
      481 flafiavlia sinifggfyv trrmlnmfrk g
//
LOCUS       WP_107860208             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            cinerea].
ACCESSION   WP_107860208
VERSION     WP_107860208.1
KEYWORDS    RefSeq.
SOURCE      Neisseria cinerea
  ORGANISM  Neisseria cinerea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria cinerea"
                     /db_xref="taxon:483"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53947
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrskkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_107863055             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            polysaccharea].
ACCESSION   WP_107863055
VERSION     WP_107863055.1
KEYWORDS    RefSeq.
SOURCE      Neisseria polysaccharea
  ORGANISM  Neisseria polysaccharea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria polysaccharea"
                     /db_xref="taxon:489"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53813
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwtcpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaas aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_107865062             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agitococcus lubricus].
ACCESSION   WP_107865062
VERSION     WP_107865062.1
KEYWORDS    RefSeq.
SOURCE      Agitococcus lubricus
  ORGANISM  Agitococcus lubricus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Agitococcus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Agitococcus lubricus"
                     /db_xref="taxon:1077255"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39426
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,125,128,131,172..175,195..197,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaeii agetrvaatp dtvkklitag hkvvvqagag vnasvpdasy savgasivda
       61 taayasdiil kvqaptaeei alikdgatvi amfdpyrnan laafaaknlq cfalellprt
      121 lsraqnmdvl ssqsnlagyk avimaadeyq rpfpmfmtsa gtvkparvvi mgvgvaglqa
      181 iatakrlgav veatdlrpta kdqveslggk wldvpmsdee kenakkaaas gyawmpgpqy
      241 iadqavivdk avsqadivit talipgrnap rlikaetvak mkagsvildm avetggnveg
      301 svvneivtta ngvkiigtpn ipaqlaaqss alyannvynf lvtilnkegq mvvnledeiq
      361 kallitqagq qlfppkra
//
LOCUS       WP_107874214             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            weaveri].
ACCESSION   WP_107874214
VERSION     WP_107874214.1
KEYWORDS    RefSeq.
SOURCE      Neisseria weaveri
  ORGANISM  Neisseria weaveri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Neisseria weaveri"
                     /db_xref="taxon:28091"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53736
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl pgetrvactp atvtqlqklg fevvvergag laaslddaay eaagavvvda
       61 aevwacpliy kvnapsesea grlnagqtlv sflwpaqnpe lvqkltdqkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vkafdtrlev aeqiesmggq flkldfpqes ggsgdgyakv mseefiaaem
      241 klfaeqaqqv diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnlsklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp ppaiqvsaap qqqaqaapva kpepkpvptw kklapaviga vlvlwmgava
      421 paeflnhfiv fvlacvigyy vvwnvshslh tplmsvtnai sgiivvgall qigqgngvvs
      481 flafiavlia sinifggfyv trrmlnmfrk g
//
LOCUS       WP_107878819             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            animaloris].
ACCESSION   WP_107878819
VERSION     WP_107878819.1
KEYWORDS    RefSeq.
SOURCE      Neisseria animaloris
  ORGANISM  Neisseria animaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Neisseria animaloris"
                     /db_xref="taxon:326522"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53822
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl pgetrvactp atvtqlqklg fevvvergag saaslddaay eaagavvada
       61 aevwsspliy kvnapsetei erlnagqtlv sflwpaqnpe lvqkltdkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vkafdtrlev aeqiesmggq flkldfpqea ggsgdgyakv mseefiaaem
      241 klfaeqarqv diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnlsklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp ppaiqvsaap qqqaqaapva kpepkpvptw kklapaviga vlvlwmgava
      421 paeflnhfiv fvlacvigyy vvwnvshslh tplmsvtnai sgiivvgall qigqgngvvs
      481 flafiavlia sinifggfyv trrmlnmfrk g
//
LOCUS       WP_107881666             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            morhuae].
ACCESSION   WP_107881666
VERSION     WP_107881666.1
KEYWORDS    RefSeq.
SOURCE      Shewanella morhuae
  ORGANISM  Shewanella morhuae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Shewanella morhuae"
                     /db_xref="taxon:365591"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53443
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevmvesnag qlssfddaaf taaganittd
       61 vwqadlifkv napndaeieq ikdgatvvsf iwpaqnpelv eklskrninv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggqfl kldfgnedgg ssdgyaktms defiaaemal
      241 faeqakevdi iittalipgr papklitkam vdtmksgsvi vdlaaatggn ceytqsgelf
      301 vtpngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgnahinfd dvvmrnmtvi
      361 kagevtfppp pisvsaapvk pavkiepknt tpkapsklky vlaalgvagf aavasvapae
      421 flshftvfvl scvvgyyvvw nvshslhtpl msvtnaisgi ivvgallqig qgstlvtvla
      481 fiavliasin ifggftvtqr mlkmfrkd
//
LOCUS       WP_107884195             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            elongata].
ACCESSION   WP_107884195
VERSION     WP_107884195.1
KEYWORDS    RefSeq.
SOURCE      Neisseria elongata
  ORGANISM  Neisseria elongata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria elongata"
                     /db_xref="taxon:495"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54245
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkesl agetrvactp atvaqlqklc fdvvvengag lgasfddaay eeagatvaaa
       61 aevwkcpliy klnapngnec rrlkegqtlv gflypnqnee lvqkladkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapeaflnhf ivfvlscvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vsllafiail iasinifggf yvtrrmlnmf rkg
//
LOCUS       WP_107893620             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodovulum
            imhoffii].
ACCESSION   WP_107893620
VERSION     WP_107893620.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum imhoffii
  ORGANISM  Rhodovulum imhoffii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rhodovulum imhoffii"
                     /db_xref="taxon:365340"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55115
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapketf agearvamtp dsalqlqklg yacvieagag vasgfddaay akagveivqg
       61 aqalwaaadi vakvrepsge evarlregqt lisffwpaqn eamlaqckdk ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfee sqdgaetggy aapsspefre
      241 kqlakfrela pdmdivitta lipgrpapkl wledmvaamk pgsvvvdlaa ekggncdltr
      301 pgekivsgng vtvvgytdfp srmaaqsstl yatnirhmmt dltpgkdgri vhnmeddvir
      361 gatvtfegdi tfpppppkvk aiaaapkkdk pkelspeekk mqeaaafrkq tisqvallma
      421 ggvlmllvga fapqsfmshl ivfalacfvg fqviwnvshs lhtplmavtn aisgiiilga
      481 llqigsgnwl vvilaavsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_107918534             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            elongata].
ACCESSION   WP_107918534
VERSION     WP_107918534.1
KEYWORDS    RefSeq.
SOURCE      Neisseria elongata
  ORGANISM  Neisseria elongata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria elongata"
                     /db_xref="taxon:495"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54215
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkesl agetrvactp atvaqlqklg fdvvlengag lgasfddaay eeagatvaaa
       61 aevwkcpliy klnapngnec rrlkegqtlv gflypnqnee lvrkladkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfitgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpetkpvp lwkklapavi aavlvlwvga
      421 vapeaflnhf ivfvlscvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf yvtrrmlnmf rkg
//
LOCUS       WP_107948153             308 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Shewanella].
ACCESSION   WP_107948153
VERSION     WP_107948153.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     Protein         1..308
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35599
     Region          5..170
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifelfskr qkkirgeved vyvyedipqs lrvqiihiir dtigqdkyed rargayefih
       61 kalckeygvf tlkqharsdd naifdcflnc ddyercldii eitfriinny vdenyynykq
      121 yttssqeped ainelnsrfk ecgvgyqfes gelirvdsqy lhsesvkpvl hllgsakeyq
      181 gandeflsah ehyrhkryke clndclksfe slmkaihekh swsygqndta kklinsclan
      241 nlvpeylqnq fssvrilles giptvrnkeg ghgqgaeist vpehlasytl hltatnllfl
      301 anceekfs
//
LOCUS       WP_107929011             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            animaloris].
ACCESSION   WP_107929011
VERSION     WP_107929011.1
KEYWORDS    RefSeq.
SOURCE      Neisseria animaloris
  ORGANISM  Neisseria animaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Neisseria animaloris"
                     /db_xref="taxon:326522"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53677
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl pgetrvactp stvtqlqklg fevvvergag laaslddaay eaagavaada
       61 aevwacpliy kvnapsenea grlnagqtlv sflwpaqnpe lvqkltdkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vkafdtrlev aeqiesmggq flkldfpqea ggsgdgyakv mseefiaaem
      241 klfaeqaqqv diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnlsklls pnkdgeiald fedviirnmt
      361 vtrdgeitfp ppaiqvsaap qqqaqaapva kpepkpvptw kklapaviga vlvlwmgava
      421 paeflnhfiv fvlacvigyy vvwnvshslh tplmsvtnai sgiivvgall qigqgngvvs
      481 flafiavlia sinifggfyv trrmlnmfrk g
//
LOCUS       WP_107960625             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            cinerea].
ACCESSION   WP_107960625
VERSION     WP_107960625.1
KEYWORDS    RefSeq.
SOURCE      Neisseria cinerea
  ORGANISM  Neisseria cinerea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria cinerea"
                     /db_xref="taxon:483"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53966
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qaagatvadk
       61 aavwacplly kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp ppqiqvsaqp qqtssekatp aakpepkpip lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_107967184             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingomonas oleivorans].
ACCESSION   WP_107967184
VERSION     WP_107967184.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas oleivorans
  ORGANISM  Sphingomonas oleivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Sphingomonas oleivorans"
                     /db_xref="taxon:1735121"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38673
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlreaa agerrvaatp etvkkltalg aqlavetgag ltasisdkgy aeagatvadr
       61 aatlagadii lgvqgpdpet lagakpgawl vaalnpfger arveayaaag lealamefmp
      121 ritraqsmdi lssqsnlagy kavldaasey grafpmmmta agtvsaarvf imgvgvaglq
      181 aiatarrlga qvsatdvrsa tkeqilslga kpifveevkg iegegsggya temseeykak
      241 qaelvsshia kqdivittal ipgrpaprli sdaqlatmkp gsvivdlave sggnvegava
      301 gaiverhgvk ivghrnvpsr laadasalfa rnlynflsaf wdkeagrpvl peddeigqai
      361 rltqdgkvvn trlla
//
LOCUS       WP_107970814             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            elongata].
ACCESSION   WP_107970814
VERSION     WP_107970814.1
KEYWORDS    RefSeq.
SOURCE      Neisseria elongata
  ORGANISM  Neisseria elongata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria elongata"
                     /db_xref="taxon:495"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54146
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkesl agetrvactp atvaqlqklg fdvvvehgag lgasfddaay eeagatvaaa
       61 aevwkcpliy klnapngnec rrlkegqtlv gflypnqnee lvkkladkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_107977288             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Allosediminivita pacifica].
ACCESSION   WP_107977288
VERSION     WP_107977288.1
KEYWORDS    RefSeq.
SOURCE      Allosediminivita pacifica
  ORGANISM  Allosediminivita pacifica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Allosediminivita.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Allosediminivita pacifica"
                     /db_xref="taxon:1267769"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56138
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeil pgearvamtp dsarqlqklg ydcaietnag kaagfadsay eeagveives
       61 adalwagsdi iakvrppted elgyldetkt lishfypgsn eelmklaask gasviamdmi
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqtdgsesgg yakpsspefr
      241 eaqlakfrel apemdivitt alipnreape lwtedmvkam krgsvivdla aerggnckmt
      301 vkddkivtdn gvtiigytdf psrmatqass lyatnirhlm tdltpekdgk vdhnmeddvi
      361 rgatiaheke vtfpppppkt kaiaaqkpkp kekeltpeek raqevaafkq qtkqqvtlla
      421 vgavlllavg lvapasfmqh fivfvlsvfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsf lvvllaalsv fmtginifgg flvtrrmlam fqks
//
LOCUS       WP_107986883             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. OK519].
ACCESSION   WP_107986883
VERSION     WP_107986883.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. OK519
  ORGANISM  Rhodococcus sp. OK519
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rhodococcus sp. OK519"
                     /db_xref="taxon:2135729"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37729
     Region          14..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsksaaqv rpsvgvvret sdgerrvalv pkvvaslaak gvdvvvepga glgalipdel
       61 ykeagatigd awacdvvvkv appsdgeigk lrtgqtligf laprnadnqi galtaagvsa
      121 faveaipris raqvmdalss qanvagykav lvaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrtt gydvrpevad qvrsvgaqwl dlgidaageg gyareltdae
      241 raqqqqalen aikgfdvvit talvpgrpap rlvtaaaveg mkpgsviidl agetggncel
      301 tepgqtavkh gvticsplnl patmpehase lysknvaali elmldesgal apdfsdeila
      361 gacvtgsken s
//
LOCUS       WP_107993098             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            elongata].
ACCESSION   WP_107993098
VERSION     WP_107993098.1
KEYWORDS    RefSeq.
SOURCE      Neisseria elongata
  ORGANISM  Neisseria elongata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria elongata"
                     /db_xref="taxon:495"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54089
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkesl agetrvactp atvaqlqklg fdvvvengag lgasfddaay eeagatvaaa
       61 aevwkcpliy klnapngnec rrlkegqtlv gflypnqnee lvqkladkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlscvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_107997131             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            cinerea].
ACCESSION   WP_107997131
VERSION     WP_107997131.1
KEYWORDS    RefSeq.
SOURCE      Neisseria cinerea
  ORGANISM  Neisseria cinerea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria cinerea"
                     /db_xref="taxon:483"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53900
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qaagatvadk
       61 aavwacplly kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk kmvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_108003401             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Mycoplana
            dimorpha].
ACCESSION   WP_108003401
VERSION     WP_108003401.1
KEYWORDS    RefSeq.
SOURCE      Mycoplana dimorpha
  ORGANISM  Mycoplana dimorpha
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Mycoplana.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Mycoplana dimorpha"
                     /db_xref="taxon:28320"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39616
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msgivfvare tdpaesrvaa svetvkkmka lgfdvvvetg aghasrisda dfegagarig
       61 saadgksadv vlrvrrptdk diksykpgai viaimdpygn dkalaamaka gltafamelm
      121 pritraqsmd vlssqanlag yqavidaaae ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskeyqs
      241 kqaslvadhi akqdivitta lipgrpaprl vtramlksmk agsiavdlav erggniegse
      301 agkvvdvdgv kvigylnvpg riaasaslly aknlvtflet lvnkeaktla vnpddelvka
      361 tmlthagqvv hpafaaapte ena
//
LOCUS       WP_108009565             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. VMFN-G11Ma].
ACCESSION   WP_108009565
VERSION     WP_108009565.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. VMFN-G11Ma
  ORGANISM  Streptomyces sp. VMFN-G11Ma
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces sp. VMFN-G11Ma"
                     /db_xref="taxon:2135609"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53193
     Region          13..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msadasshhp pqligvvaes asgetrvaat patvrlllkl gyeavvetga geasgfddqa
       61 yveagarigd awdadvvlkv naptgseitr lregatvagl lapaqnpell qelsragvta
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgavvr atdprpevad qvrslggeyl pvdvvqeast dgyakatsad
      241 ydraaaelyh eqaqdvdivv ttalipgrpa prlltaadva amkpgsvivd maaamggnve
      301 gtvagrtvvt gngvtiigyt dlasrlpaqa sqlfgtnlan lvklltpgkd grltvdfddv
      361 vqravtvvrg geitwppppv pvsaapvaqt aeaapvetep erprltpalr fgliglgmla
      421 mfllvafapa qlaenftvfa lavvigyyvi gkvhhalhtp lmsvtnaisg ivvigallqi
      481 ghennlvtal scvailltsv nvfggfavtr rmlsmfskg
//
LOCUS       WP_108027732             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodovulum
            kholense].
ACCESSION   WP_108027732
VERSION     WP_108027732.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum kholense
  ORGANISM  Rhodovulum kholense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhodovulum kholense"
                     /db_xref="taxon:453584"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55574
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeil egearvamtp dsavqlrklg ydclieagag eaagfadaay ekagvkvvqs
       61 aaalwqgadi vvkvrepvae evarlrkgqt lisffwpaqn ealleqckar gatviamdmv
      121 prisraqkmd alssmaniag yravieagsn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg amvyafdvrp evaeqiesmg aefvfldfed stadgsesgg yakpsspefr
      241 ekqlekfrel apdmdivitt alipgrpapk lwledmvaam kpgsvvvdla aekggncdlt
      301 rpgekivsdn gvtvvgytdf asrmatqsst lyatnirhmm tdltpgkdgq vvhnmeddvi
      361 rgatvthege itfpppppkv kaiaaaprke kpkeltpeek kaqeaaafrk qtitqvgmlv
      421 aggllmalig afapesfmsh fivfalscfv gfqviwnvsh slhtplmavt naisgiiilg
      481 allqigsgnw lvvilatfsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_108044052             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            cinerea].
ACCESSION   WP_108044052
VERSION     WP_108044052.1
KEYWORDS    RefSeq.
SOURCE      Neisseria cinerea
  ORGANISM  Neisseria cinerea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria cinerea"
                     /db_xref="taxon:483"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53955
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qaagatvadk
       61 vavwacpliy kvnapsegel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekatp aakpepkpip lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_108047012             398 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Allobosea
            sp. 124].
ACCESSION   WP_108047012
VERSION     WP_108047012.1
KEYWORDS    RefSeq.
SOURCE      Allobosea sp. 124
  ORGANISM  Allobosea sp. 124
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Allobosea sp. 124"
                     /db_xref="taxon:2135642"
     Protein         1..398
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40744
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaetq gaetrvavtp etvrkfiglg aeiavetgag lasgisdady qaagatvaas
       61 aadalagaai vlkvrrpaka eiaglpagal vvgimdpygn epelaalaka kvaafamefm
      121 pritraqvmd vlssqanlag yravidgage ygralpmmmt aagtvpaari fimgvgvagl
      181 qaiatarrng aivtatdvrp atkeqveslg akflavedee fkqaqtaggy akemskeyqa
      241 kqaeltashi akqdivitta lipgrpapkl isaamvesmk agsvivdlav erggncelak
      301 pgevvttpng vkivghlnvp grlaatssql yaknlfafve tlidktakav avnwddelvk
      361 ataltrdgav ihpnfaakpe akpepapapv vegsvtng
//
LOCUS       WP_108099127             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. GV071].
ACCESSION   WP_108099127
VERSION     WP_108099127.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. GV071
  ORGANISM  Pseudomonas sp. GV071
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. GV071"
                     /db_xref="taxon:2135754"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38598
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletf tgetrvaatp etikkliaqg hqvtvqsgag vnasvpdsay qavgasigda
       61 aaalgadlvl kvvapnaael aqlksgavlv gmlnpfnsen iaqmaergvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee reaaegvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkapvl lsaetveqmk pgsvvidlaa aqggncplte
      301 adqvvikhgv tivghtnlaa lvaadasaly arnlldflkl vidsegkfhv nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_108107280             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas mangrovi].
ACCESSION   WP_108107280
VERSION     WP_108107280.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mangrovi
  ORGANISM  Pseudomonas mangrovi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas mangrovi"
                     /db_xref="taxon:2161748"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38705
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikkliahg hqvtvqsgag vtaslpdhvy evvgaaigda
       61 atafaadlvl kvvapsdael almkpgavlv gmlnpfcnet iarvaargit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaegvggy arpmpaswmq
      241 rqagavhera kqadivitta lipgrkaptl lhaatveemk pgsviidlaa aqggncplte
      301 adqvvvkhgv tivghsnlaa mvpadasaly arnlldflkl vidsegkfhl nleddivaac
      361 lmcrdgqvvr sng
//
LOCUS       WP_108124983             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Saccharospirillum mangrovi].
ACCESSION   WP_108124983
VERSION     WP_108124983.1
KEYWORDS    RefSeq.
SOURCE      Saccharospirillum mangrovi
  ORGANISM  Saccharospirillum mangrovi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Saccharospirillum.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Saccharospirillum mangrovi"
                     /db_xref="taxon:2161747"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55471
     Region          3..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpltiavprd rqdgetriav tpdttrklie lgfhvriesg agaaaqyadt ayqdagadis
       61 tdvaqlyeqa dillkinapm aqhpvlnrse ldafpngktw vsflapaqne atlktfaqhn
      121 anaisldaip risraqkmdv lssmaniagy ravieaanqf grfftgqita agkvppakvl
      181 iigagvagla aigaakslga vvrafdtrke vkeqvesmgg qfltveleed gagsggyake
      241 msqafidaem alfmeqakev diiittalip gkpapklite emvkamapgg vvvdlaapng
      301 gncectvadq iveqhgikii gftnlaaraa tqasqllsnn vlrlfehlcp nkdgelvfdl
      361 ddaitrgctv vhagsviwpa pppqisaapk aepkaaetet apqtsaakra rpialywlia
      421 galmlglgav apadfishft vfvlavfvgw qviwnvshsl htplmsvtna issiiiigsl
      481 lqvsgsgstl vtvlaaigil vtsiniaggf yvtrrmlnmf rregqe
//
LOCUS       WP_108127116             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Gemmobacter caeni].
ACCESSION   WP_108127116
VERSION     WP_108127116.1
KEYWORDS    RefSeq.
SOURCE      Gemmobacter caeni
  ORGANISM  Gemmobacter caeni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Gemmobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Gemmobacter caeni"
                     /db_xref="taxon:589035"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55519
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreif egenrvaltp dsavqlqklg hvcvleagag akagfsdaay rtagveivtt
       61 aaelyaaadv vvkvrgpeps evamlrqgqt lisffwpaqn pelleaaker gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aitlafdvrp evaeqiesmg aefvyldfse aqtdgaatgg yaapsspefr
      241 eaqlkkfrel apdidivitt alipgrpapk lwtedmvqmm kpgsvivdla aerggncdlt
      301 vpdekivten gvtivgytdf psrmaaqast lyannirhmm sdltpkkdgv vdhnmeddvi
      361 rgatvtkdga itypppppkv qaiaaqkpke kakeltpeek raqeaaafrk qtrdqvlmla
      421 iggglillag lfapasfmah fivfvlsvyv gvqviwnvsh slhtplmavt naissiiilg
      481 almqigsgnw lvvilaaasv fmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_108131474             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Halomonas].
ACCESSION   WP_108131474
VERSION     WP_108131474.1
KEYWORDS    RefSeq.
SOURCE      Halomonas
  ORGANISM  Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas"
                     /db_xref="taxon:2745"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55771
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaprerh kgearvaltp esaghiqklg heclietgag elagftdaay eeagvtivds
       61 meavfeqadv vvkvrepqke esdllrqgqt lisffwpaqn eemletckdk gasvvamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv liigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfed sqdgsesggy aapsspefre
      241 kqlelfrqqa pevdivitta lipgrpapkl wledmvkamk pgsvvvdlaa ekggncdltk
      301 pdervvtdng vivvgytdfp srmatqssll ystnirhmlt dltpekdgki vhdmeddvir
      361 gatvthqgev tfpppppkvk aiaaakpkpk ekeptpeerk aaehaafmkq tksqvtmlav
      421 ggivmgllgl vapasfmqhl ivfalacfvg fqviwnvshs lhtplmavtn aisgiiilga
      481 vlqvgsgswl vallagisvl iasinvvggf lvtrrmlamf qks
//
LOCUS       WP_108178320             403 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phreatobacter oligotrophus].
ACCESSION   WP_108178320
VERSION     WP_108178320.1
KEYWORDS    RefSeq.
SOURCE      Phreatobacter oligotrophus
  ORGANISM  Phreatobacter oligotrophus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phreatobacteraceae; Phreatobacter.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Phreatobacter oligotrophus"
                     /db_xref="taxon:1122261"
     Protein         1..403
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40994
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaiprete ageprvagtp dtvkrlkglg advvvepgag laagitdadf eaagaslaad
       61 avsgadvvlk vrrpstaelk ayktgavvla tmdpygneaa lvamakagvs afamelmpri
      121 traqvmdvls sqanlagyra vidassefgr alpmmmtaag tvpaakvfvm gagvaglqai
      181 atarrlgavv tatdvrpaak eqveslgakf iavmddefkq aetaagyakp msaeyqakqa
      241 alvaehiakq divittalip graaprlvta amvasmkpgs vlldlaverg gnvegaqpge
      301 ivttangvki vghanvpgrl aatssslyak nlfafleimi dkatksvvvp wedelvkatl
      361 ltrdgavvhp sfaeaaaalp adasaaseap akpkaapkks tka
//
LOCUS       WP_108240565             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_108240565
VERSION     WP_108240565.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38777
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikkligqg htvtvqsgag itasvtdsay qtagasigsa
       61 adafgaelil kvvapsdsel aliksgtlvi gmlnpfnnei iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee reaaegvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkapvl lsaetvsqmk pgsvvidlaa aqggncpltv
      301 adqvviehgv tivghtnlpa lvaadasaly arnlldfmkl iftkegqlei nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_108243998             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Vibrio cholerae].
ACCESSION   WP_108243998
VERSION     WP_108243998.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35723
     Region          5..171
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mtifelfskr qkklrgevpd vyqyenieqs frvqvvhivr dtigierdyn natnnvynli
       61 hkilckeygv ftlkehtnsn feavfeyfls qkshekcldi ieltfriidt hvrenewdfr
      121 daigvsqkpd daigelnfrf keagigyqfe sgelirvdsq yvhsevvkpv lyllgkdkky
      181 agandeflsa hehyrhkryk eclndclksf eslmkaihek hswpynqndt akklinsclt
      241 nglvpeylqn qfasvrille sgiptvrnke gghgqgteit svpehlasyt lhltasnllf
      301 lgnceekys
//
LOCUS       WP_108255077             543 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. Hippo4].
ACCESSION   WP_108255077
VERSION     WP_108255077.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. Hippo4
  ORGANISM  Limnohabitans sp. Hippo4
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Limnohabitans sp. Hippo4"
                     /db_xref="taxon:1826167"
     Protein         1..543
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56369
     Region          21..543
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mttvhpsdnv ldgkaasspq rigvpkevfp gekrvatvpd vvtkliklgf svavekgage
       61 ladlsdqaye qagasiapsa ealwsssdiv fkvraptaee valmhegqtl igflwpaqnp
      121 dlmqqlaakk vtalsidalp rtlsraqkmd altsmagvsg yravveaaga fgrffngqit
      181 aagkvppakv fiagagvagl aaigaaaslg aivrandtra evadqvvslg gefvkvnfee
      241 egsggggyak vmsegfqaaq remyaqqake cdiiittali pgkpapklit aemvrnmkpg
      301 svivdmaaeq ggnceltepg kavvkhgvti vgytdlasrm arqsstlygt nlfrlteelc
      361 ktkdgvinvn meddairglt vikegtitwp applvvaakp apkpvaasva kkghghgeps
      421 gpmpagqlai vagiaavlfv lvglyaptaf lshftvfvla cfvgymvvwn vkpalhtplm
      481 svtnaissii aigalvqisp manaaarpnt liivlaslal vltainmfgg favtqrmlam
      541 frk
//
LOCUS       WP_108283799             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. Jir61].
ACCESSION   WP_108283799
VERSION     WP_108283799.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. Jir61
  ORGANISM  Limnohabitans sp. Jir61
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Limnohabitans sp. Jir61"
                     /db_xref="taxon:1826168"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39385
     Region          9..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(21,79,98,297,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(50,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,287..288,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 menpkslcig vpaevaagea rvavtpetak klmsqghtvr vqagagvaas vpdaayvsvg
       61 aevvdaasaw rcdlvlkvra peaaevayiq sgstvigmle pfnaqglqrl asagatgfal
      121 eaaprttraq smdvlssqan iagykavmla adkyqrffpm lmtaagtvka arvvilgvgv
      181 aglqaiatak rlgavieatd vrpsvkeqve slgakfidvp fesqdekdaa egvggyarpm
      241 pqswldrqkv evakrvalad ivittalipg raapvlvted mvkamkpgav iidiaagkgv
      301 dgvggncplt eanktvikhg vtivgetnlp alvaadasal yarnvldflk lvinkegalh
      361 idleddivaa clvtrdgavv kk
//
LOCUS       WP_108285339             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. T6-20].
ACCESSION   WP_108285339
VERSION     WP_108285339.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. T6-20
  ORGANISM  Limnohabitans sp. T6-20
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Limnohabitans sp. T6-20"
                     /db_xref="taxon:1100725"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54525
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpreif lgekrvatvp dvvtklvklg favsvergag eladlsdday veagatiaps
       61 aaelwrgsdi vfkvraptpd evalmhegqt llgflwpaqn pelmqqlaak kvtalsidal
      121 prtlsraqkm daltsmagvs gyravieaan afgrffngqi taagkvppak vfiagagvag
      181 laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya kvmsegfqaa
      241 qramyaqqar evdiiittal ipgkpapkli taemvqsmkp gsvivdmaae qggnceltep
      301 gkavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv nmeddairgl
      361 tvikdgeitw papplvaapk papkpaaapa akkghghgep sgpmpagklv ivaavtavlf
      421 alvgayapaa flshftvfvl acfvgymvvw nvkpalhtpl msvtnaissi iaigalvqis
      481 pmanaaarpn mliiilasva lvltainmfg gfavtqrmla mfrk
//
LOCUS       WP_108295081             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            taurinensis].
ACCESSION   WP_108295081
VERSION     WP_108295081.1
KEYWORDS    RefSeq.
SOURCE      Legionella taurinensis
  ORGANISM  Legionella taurinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Legionella taurinensis"
                     /db_xref="taxon:70611"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40759
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miivalneha rdtraaitpn slkhyqklgl tvhceqnvga acgftdsayq eagavivsdr
       61 alllqeadil acvsvpspad lpqlkrnall iapfdnepes plmqwcqqqs itafsmnlip
      121 risraqsmds lssqanlagy ravlegvahf nraipmmmta agmihpakvl ilgagvaglq
      181 aiatakrlga vvyafdvrra akeqveslga efievstded setsggyare mseeykkqqa
      241 elihqyatqa divvttalip grpapvlitr etvnqmkpgs vivdiatsrg gncelsqrde
      301 vihhqgvtiv gysnlagfip ataselyann vvnllkllvt spdaltfnae deivkqatlt
      361 hegryfpfqt tetkeaina
//
LOCUS       WP_108301282             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. JirII-29].
ACCESSION   WP_108301282
VERSION     WP_108301282.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. JirII-29
  ORGANISM  Limnohabitans sp. JirII-29
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Limnohabitans sp. JirII-29"
                     /db_xref="taxon:1835756"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38857
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpvett agetrvaitp etakklmaqg htvriqsgag vaasvtdvay aavgaelvda
       61 stawgcdlvl kvrgpseaet slikagstvv gmlepfnaqg lqrlafagat gfaleaaprt
      121 traqsmdvls sqaniagyka vmlaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi eatdvrpsvk eqveslgakf idvpfetqee kdaaegvggy arpmpaswle
      241 rqkvevakrv aqadvvitta lipgraapvl vtedmvkamk pgsviidiaa gkgaqgtdgn
      301 cplteagktv ikhgvtlvge tnlpalvaad ssalyarnvl dflkliinke gvlhidledd
      361 ivaaclmtrd gavvkk
//
LOCUS       WP_108302071             314 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Limnohabitans sp. JirII-29].
ACCESSION   WP_108302071
VERSION     WP_108302071.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. JirII-29
  ORGANISM  Limnohabitans sp. JirII-29
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Limnohabitans sp. JirII-29"
                     /db_xref="taxon:1835756"
     Protein         1..314
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35623
     Region          5..174
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mritdlfskr qaklrgevpd vfvydkmpqe lrvqvvhifk dylgnetevy rrnglvsgay
       61 efivntlcre ygifklpsar eygdrdyvte lfnfvlseks tervldavel gsriidvhsr
      121 kweyrhrqda adeadaalae lnarfqqhgf gfrfetgnii ridsevvhae vvkpalallh
      181 dtkyrgaeae fhkafehhrh grtkealadc lkslestmka vaahrkwkhd phatakplld
      241 lmfekqlipq lwsqhfsglr gmlesgvpta rnrlgghgqg pevvtvpqhf vafalhqtaa
      301 aivflanaea alpr
//
LOCUS       WP_108315436             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            paracholerae].
ACCESSION   WP_108315436
VERSION     WP_108315436.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53945
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg feicieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqdsgiv
      481 tflafiavli asinifggft vtkrmlemfr rn
//
LOCUS       WP_108312593             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans parvus].
ACCESSION   WP_108312593
VERSION     WP_108312593.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans parvus
  ORGANISM  Limnohabitans parvus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Limnohabitans parvus"
                     /db_xref="taxon:540061"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54966
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpreif lgekrvatvp davtklvklg fevavergag eladlsdday veagatiaps
       61 aaelwlssdi vfkvraptpd evalmhegqt ligflwpaqn pdlmqqlaak kvtalsidal
      121 prtlsraqkm daltsmagvs gyravveaan afgrffngqi taagkvppak vfiagagvag
      181 laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya kvmsegfqaa
      241 qrqmyaqqak ecdiiittal ipgkpapkli taemvqsmkp gsvivdmaae qggnceltep
      301 gkavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv nmqddairgl
      361 tvikdgeitw papplvvapk papkptvava ekksghghgs sgpmpaktla vvfglgalvf
      421 waigayapaa flghftvfvl acfignmvvw nvtpalhtpl msvtnaissi ivigalvqil
      481 ppeagtngrp dqliqwlafa givltavnmf ggfavtrrml dmfrk
//
LOCUS       WP_108324052             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Limnohabitans].
ACCESSION   WP_108324052
VERSION     WP_108324052.1
KEYWORDS    RefSeq.
SOURCE      unclassified Limnohabitans
  ORGANISM  unclassified Limnohabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="unclassified Limnohabitans"
                     /db_xref="taxon:2626134"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54091
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkeiy pgekrvatvp davtklvklg favvveqgag eladlsdaay vdagatiapn
       61 aaalwsgsdi vfkvraptad evalmhegqt ligflwpaqn pdlmqqlaak kvtalsidal
      121 prtlsraqkm daltsmagvs gyravvesan afgrffngqi taagkvppak vfiagagvag
      181 laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya kvmsdgfqaa
      241 qremyakqaq ecdiiittal ipgkpapkli taemvksmkp gsvivdmaae qggnceltep
      301 gkavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv nmeddairgl
      361 tvikngeitw papplvvapk papkpaaapa akkghghgep sgpmpvgqll ivsavaavll
      421 vlvgayapaa flshftvfvl acfvgymvvw nvkpalhtpl msvtnaissi iaigalvqis
      481 plaaagrpnt ligilaalal vltainmfgg favtqrmlam frk
//
LOCUS       WP_108331898             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. 2KL-1].
ACCESSION   WP_108331898
VERSION     WP_108331898.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. 2KL-1
  ORGANISM  Limnohabitans sp. 2KL-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Limnohabitans sp. 2KL-1"
                     /db_xref="taxon:1100699"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54902
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkeiy pgekrvatvp dvvtklvklg fevvveqgag aladlsdeay veagasvaps
       61 aaalwsgsdi vfkvraptld evalmhegqt ligflwpaqn pdlmqqlsak kvtalsidal
      121 prtlsraqkm daltsmagvs gyravveaan afgrffngqi taagkvppak vfiagagvag
      181 laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya kvmsegfqaa
      241 qremyakqak ecdiiittal ipgkpapkli taemvqsmkp gsvivdmaae qggnceltep
      301 gqavvrhgvt ivgytdlasr marqsstlyg tnlfrlieel cktkdgiinv nmqddairgl
      361 tvikdgeitw papplvvppk papkpaaava ekkgghghgs sgpmpvktla mvfgvgalaf
      421 waigayapaa flghftvfvl acfigymvvw nvtpalhtpl msvtnaissi ivigalvqil
      481 ppeagmngrp dqliqwlafa givltavnmf ggfavtrrml dmfrk
//
LOCUS       WP_108343122             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides currus].
ACCESSION   WP_108343122
VERSION     WP_108343122.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides currus
  ORGANISM  Nocardioides currus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Nocardioides currus"
                     /db_xref="taxon:2133958"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52921
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresr qgetlvaatt vtaaqleslg yevvveagag vaadqtdeaf aaagirvtda
       61 eevwtsdvvi kvnaptadei wklrqgativ slmapgrspk lieqlqaqrv tglamdavpr
      121 israqamdvl ssmanvagyr avieaahefg rqftgqvtaa gkvpparvfv vgagvaglaa
      181 igaagamgav vrafdvrpev aeqveslggq fvtvdmeqev ssdgyakemt aeqeaataam
      241 ydeearnadi vittalipgr papqlitadt vahmktgsvv vdmaaanggn valtqadekv
      301 vtdnlvtilg ytdlagrlaa qtsqlygtni vnlfklltpg kdgelvldhe dvvqrgitvt
      361 qdgeslwppp pvqvsaapaa paapvarpap vekppadprr kvyaaalgav lfalaaayap
      421 psflghftvf alaifvgyyv isnvahalht plmaetnais giilvggilq vgsdnpvitt
      481 lalvavlvas inifggflvt armlqmfrkd
//
LOCUS       WP_108360399             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. Rim8].
ACCESSION   WP_108360399
VERSION     WP_108360399.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. Rim8
  ORGANISM  Limnohabitans sp. Rim8
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Limnohabitans sp. Rim8"
                     /db_xref="taxon:1100718"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38653
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaett agetrvavtp etakklisqg htvrvqagag vpasvpdaay aavgvevvnv
       61 tqawgcdlil kvrapeasea ssikagstvv gmlepfnaeg lqrlatagat gfaleaaprt
      121 traqsmdvls sqaniagyka vmlaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi eatdvrpsvk eqveslgakf idvpfesqde kdaaegvggy arpmpqswld
      241 rqkvevakrv aladivitta lipgraapvl vtedmvkamk pgaviidiaa gkgadgvggn
      301 cplteagktv ikhgvtivge tnlpalvaad asalyarnvl dflklvinke aalhidmedd
      361 ivaaclvtrd gavvkk
//
LOCUS       WP_108351580             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. 2KL-51].
ACCESSION   WP_108351580
VERSION     WP_108351580.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. 2KL-51
  ORGANISM  Limnohabitans sp. 2KL-51
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Limnohabitans sp. 2KL-51"
                     /db_xref="taxon:1977911"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55113
     Region          12..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtgdnaptp qrigvpkeif pgekrvatvp davtklvklg favvveqgag eladlsdaay
       61 veagatiaps aaalwsgsdi vfkvraptpd evalmhegqt ligflwpaqn pdlmqqlaak
      121 kvtalsidal prtlsraqkm daltsmagvs gyravvesan afgrffngqi taagkvppak
      181 vfiagagvag laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya
      241 kvmsegfqaa qremyakqak ecdiiittal ipgkpapkli taemvqsmkp gsvivdmaae
      301 qggnceltep gkavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv
      361 nmeddairgl tvikdgeitw papplvvapk papkpaaapa akkghghgep sgpmpvgqll
      421 ivsavaavll vlvgayapaa flshftvfvl acfvgymvvw nvkpalhtpl msvtnaissi
      481 iaigalvqis plaaagrpnt ligilaalal vltainmfgg favtqrmlam frk
//
LOCUS       WP_108362112             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. Bal53].
ACCESSION   WP_108362112
VERSION     WP_108362112.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. Bal53
  ORGANISM  Limnohabitans sp. Bal53
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Limnohabitans sp. Bal53"
                     /db_xref="taxon:1977910"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55232
     Region          12..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtgdhaprp qrigvpreif pgekrvatvp davtklvklg favvveegag eladlsdaay
       61 veagatiaps aaalwsdsdi vfkvraptsd evalmhegqt ligflwpaqn pdlmqqlaak
      121 kvtalsidal prtlsraqkm daltsmagvs gyravvesan afgrffngqi taagkvppak
      181 vfiagagvag laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya
      241 kvmsegfqaa qremyakqak ecdiiittal ipgkpapkli taemvqsmkp gsvivdmaae
      301 qggnceltep gkavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv
      361 nmeddairgl tvikngeitw papplaaapk paakpaaapv akkghghgep sgpmpvgqll
      421 ivsavaavll vlvgayapaa flshftvfvl acfvgymvvw nvkpalhtpl msvtnaissi
      481 iaigalvqis pmaaagrpnt ligilaalal vltainmfgg favtqrmlam frk
//
LOCUS       WP_108372087             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. T6-5].
ACCESSION   WP_108372087
VERSION     WP_108372087.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. T6-5
  ORGANISM  Limnohabitans sp. T6-5
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Limnohabitans sp. T6-5"
                     /db_xref="taxon:1100724"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54898
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpreif pgekrvatvp dvvtklvklg fevdveqgag aladlsdesy veagaaiaps
       61 aaalwsgsdi vfkvraptpd evalmhegqt ligflwpaqn pdlmqqlaak kvtalsidal
      121 prtlsraqkm daltsmagvs gyravvesan afgrffngqi taagkvppak vfiagagvag
      181 laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya kvmsegfqaa
      241 qremyaqqak ecdiiittal ipgkpapkli taamvqsmkp gsvivdmaae qggnceltep
      301 gqavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv nmqddairgl
      361 tvikdgeitw papplvvapk papkpttava ekksghghgs sgpmpvktla mvfglgalvf
      421 wamgayapaa flghftvfvl acfigymvvw nvtpalhtpl msvtnaissi ivigalvqil
      481 ppeagtngra dqliqwlafa givltainmf ggfavtrrml dmfrk
//
LOCUS       WP_108378299             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. WS1].
ACCESSION   WP_108378299
VERSION     WP_108378299.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. WS1
  ORGANISM  Limnohabitans sp. WS1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Limnohabitans sp. WS1"
                     /db_xref="taxon:1100726"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55143
     Region          12..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtgdtaptp qrigvpreif pgekrvatvp davtklvklg favvveqgag eladlsdaaf
       61 veagasiapn aaalwsgsdi vfkvraptpd evalmhegqt ligflwpaqn pdlmqqlaak
      121 kvtalsidal prtlsraqkm daltsmagvs gyravvesan afgrffngqi taagkvppak
      181 vfiagagvag laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya
      241 kvmsegfqaa qremyakqak ecdiiittal ipgkpapkli taemvqsmkp gsvivdmaae
      301 qggnceltep gkavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv
      361 nmeddairgl tvikdgeitw papplvvapk papkpaaapa akkghghgep sgpmpvgqll
      421 ivsavaavll vlvgayapaa flshftvfvl acfvgymvvw nvkpalhtpl msvtnaissi
      481 iaigalvqis pmaaagrpnt ligilaalal vltainmfgg favtqrmlam frk
//
LOCUS       WP_108384711             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Yoonia
            sediminilitoris].
ACCESSION   WP_108384711
VERSION     WP_108384711.1
KEYWORDS    RefSeq.
SOURCE      Yoonia sediminilitoris
  ORGANISM  Yoonia sediminilitoris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Yoonia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Yoonia sediminilitoris"
                     /db_xref="taxon:1286148"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55523
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpneif agedrvamtp asakdlqklg ysclieagag lsagftdaay eeagvevvps
       61 aadvwktadv vakvrppees eikqmregqt lisffypaqn kelmeaansq gstviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqvesmg aefvfldfee eqqdgsatgg yaavsspefa
      241 aaqlakfrei apdidivitt alipgrdape lwtkdmvesm kpgsvivdla aerggncklt
      301 vkdekivtdn gvtiigytdf psrmaqqsst lyatnirhmm tdltpekdgt pvhnmeddvi
      361 rgatathkge itfpppppkv aaiaaapkke pikeltaeek raqevaafkq qtrnqvtllt
      421 iggallllvg lvapasfmqh fivfvlavfv gfqviwgvah slhtplmavt naissiiilg
      481 altqigsgsf lviilaamav fmtginifgg flvtrrmlam fqks
//
LOCUS       WP_108401995             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans curvus].
ACCESSION   WP_108401995
VERSION     WP_108401995.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans curvus
  ORGANISM  Limnohabitans curvus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Limnohabitans curvus"
                     /db_xref="taxon:323423"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38643
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaett agetrvavtp etakklisqg htvrvqagag vpasvpdaay aavgvevvnv
       61 tqawgcdlil kvrapeasea ssikagstvv gmlepfnaeg lqrlatagat gfaleaaprt
      121 traqsmdvls sqaniagyka vmlaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi eatdvrpsvk eqveslgakf idvsfesqde kdaaegvggy arpmpqswld
      241 rqkvevakrv aladivitta lipgraapvl vtedmvkamk pgaviidiaa gkgadgvggn
      301 cplteagktv ikhgvtivge tnlpalvaad asalyarnvl dflklvinke aalhidmedd
      361 ivaaclvtrd gavvkk
//
LOCUS       WP_108407625             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. 2KL-17].
ACCESSION   WP_108407625
VERSION     WP_108407625.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. 2KL-17
  ORGANISM  Limnohabitans sp. 2KL-17
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Limnohabitans sp. 2KL-17"
                     /db_xref="taxon:1100704"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54380
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpreif pgekrvatvp davtklvklg fdvvvergag eladlsdeay veagasiaps
       61 aadlwsgsdi vfkvrapape evvlmragqt ligflwpaqn pdlmqqlaak kvtalsidal
      121 prtlsraqkm daltsmagvs gyravveaan afgrffngqi taagkvppak vfiagagvag
      181 laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya kvmsegfqaa
      241 qremyasqar evdiiittal ipgkpapkli taemvksmkp gsviidmaae qggnceltep
      301 gksvvkhgvt ivgytdlvsr marqsstlys tnlfrlteel cktkdgvidv nmqddairgl
      361 tvikdgeitw papalvvapk papkpaaava akkghghgep sgpmpvgqll ivaavaavll
      421 alvgayapaa flshltvfvl acfvgymvvw nvkpalhtpl msvtnaissi iaigalvqis
      481 pmanaasrpn tligilaala lvltainmfg gfavtqrmla mfrk
//
LOCUS       WP_108414509             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. Jir72].
ACCESSION   WP_108414509
VERSION     WP_108414509.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. Jir72
  ORGANISM  Limnohabitans sp. Jir72
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Limnohabitans sp. Jir72"
                     /db_xref="taxon:1977909"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54700
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpreif pgekrvatvp dvvtklvklg favaveqgag eladlsdday veagasiaps
       61 aadlwsgsdi vfkvraptae evalmhagqt ligflwpaqn pdlmqqlaak kvtalsidal
      121 prtlsraqkm daltsmagvs gyravveaan afgrffngqi taagkvppak vfiagagvag
      181 laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya kvmsegfqaa
      241 qremyaqqak ecdiiittal ipgkpapkli taemvksmkp gsvivdmaae qggnceltep
      301 gkavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv nmeddairgl
      361 tvikdgeitw papplvvapk papkptvava ekkgghghgs sgpmpaktla lvfglgaltf
      421 waigayapaa flghftvfvl acfignmvvw nvtpalhtpl msvtnaissi ivigalvqil
      481 ppeagtngra dqliqwlafa givltavnmf ggfavtrrml dmfrk
//
LOCUS       WP_108419492             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. MMS-10A-178].
ACCESSION   WP_108419492
VERSION     WP_108419492.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. MMS-10A-178
  ORGANISM  Limnohabitans sp. MMS-10A-178
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Limnohabitans sp. MMS-10A-178"
                     /db_xref="taxon:1835767"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38553
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpaetr pgetrvamtp etakklkaqg htllvqsgag lsasvtdaay eaagaeitda
       61 agalacdvvl kvsapsaael ahmksgaalv gmlnpfdaeg laklaaaglt sfaleaaprt
      121 traqsmdvls sqaniagyka vmvaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslggkf idvpyetaee keaaegvggy arpmppswle
      241 rqkvevakrv amadvvista lipgraapvl vtedmvksmk pgsvivdiaa gkaadgvggn
      301 cllteagktv vkhgvtlvge tnlpalvaad asslyarnvl dflklvltke gefkvdiedd
      361 ivaaclmtqg gdvkrk
//
LOCUS       WP_108427281             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Limnohabitans sp. Hippo3].
ACCESSION   WP_108427281
VERSION     WP_108427281.1
KEYWORDS    RefSeq.
SOURCE      Limnohabitans sp. Hippo3
  ORGANISM  Limnohabitans sp. Hippo3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Limnohabitans.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Limnohabitans sp. Hippo3"
                     /db_xref="taxon:1597956"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54743
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkeiy pgekrvatvp dvvtklvklg fevvveqgag aladlsdeay veagatvapn
       61 aaalwsgsdi vfkvraptad evalmhegqt ligflwpaqn pdlmqqlaak kvtalsidal
      121 prtlsraqkm daltsmagvs gyravveaan afgrffngqi taagkvppak vfiagagvag
      181 laaigaaasl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya kvmsegfqaa
      241 qremyaqqar evdiiittal ipgkpapkli takmvqsmkp gsvivdmaae qggnceltep
      301 gkavvkhgvt ivgytdlasr marqsstlyg tnlfrlteel cktkdgvinv nmaddairgl
      361 tvikdgeitw papplpaaap kpaakpvaaa ekksahghgs sgpmpvktla mvfglgalaf
      421 waigayapaa flghftvfvl acfigymvvw nvtpalhtpl msvtnaissi ivigalvqil
      481 ppeagtngrp dqliqwlafa givltavnmf ggfavtrrml dmfrk
//
LOCUS       WP_108437052             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paragemmobacter aquarius].
ACCESSION   WP_108437052
VERSION     WP_108437052.1
KEYWORDS    RefSeq.
SOURCE      Paragemmobacter aquarius
  ORGANISM  Paragemmobacter aquarius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paragemmobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Paragemmobacter aquarius"
                     /db_xref="taxon:2169400"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55065
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egenrvamtp dsavalaklg htcviesgag lkagfsdaty eaagvevvkt
       61 aaalfkaadv vvkvrgpepk eakmlrqgqt lisffwpaqn aelletckaq gatviamdmv
      121 prisraqkmd alssmaniag yravieagsn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtsvslg aivhafdvrp evaeqiesmg asfvylefda selpdgaatg gyaapsspaf
      241 aakqlakfre lapdmdivit talipgrpap klwtadmvam mkpgsvvvdl aaerggncdl
      301 tvadqkivsd ngvtivgytd fpsrmaaqas tlystnirhm ltdltpkkdg vifhnmeddv
      361 irgatvthdg avtfpppppk iaaiaaakpk ekvkeltpee kraketaafk aqtrnqvgml
      421 lgggalilla glyapasfms hfivfvlsvy vgvqviwnvs hslhtplmav tnaissiiil
      481 galmqigsgn wlvvilaals vfmaginifg gfmvtrrmla mfqks
//
LOCUS       WP_108442962             312 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Klebsiella aerogenes].
ACCESSION   WP_108442962
VERSION     WP_108442962.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella aerogenes
  ORGANISM  Klebsiella aerogenes
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Klebsiella aerogenes"
                     /db_xref="taxon:548"
     Protein         1..312
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35960
     Region          5..176
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maihdiyskr qrrirgevsd vyiydnipqk fkiqfihiie eaigicttht rmsfssyqhn
       61 tkdnvykril ktllaeygrf klkndatsys deifsyfltt svtdhsldii elfciellsi
      121 fknppsiasr dravdalsgi ntrfkennig yqfeneeiir vdsqfihsev vkptlsllss
      181 ndeydgvmde flaahehyrl dnfkewlnec lksyesimka ihdkrkwqyn ktdtasklin
      241 sclehelips ylqgqftslk tmlesgipti rnknsghgqg tgvttvprel vsymlhltat
      301 nllflaqseq sl
//
LOCUS       WP_108440237             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Glaciimonas sp. PCH181].
ACCESSION   WP_108440237
VERSION     WP_108440237.1
KEYWORDS    RefSeq.
SOURCE      Glaciimonas sp. PCH181
  ORGANISM  Glaciimonas sp. PCH181
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Glaciimonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Glaciimonas sp. PCH181"
                     /db_xref="taxon:2133943"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38631
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaetr pgetrvaatp etvkklvaak hhvivqsgag tsssitdeay aaagaqigsa
       61 aeafgqetil kvrapaadey allksgtviv gmlnpfdaen ialmashglt afaleaaprt
      121 sraqsmdvls sqaniagyka vlmaantyqr fmpmlmtaag tvkaarmlim gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfitdee reiaqgvggy arqmpadwmr
      241 rqaeavhera kladiiitta lipgrkapil iseetvkamk pgsvildmav dqggncplse
      301 sgktvirhgv hiigegnlaa lvaadasaly srnvldflkl ivtpegglvi nleddivaat
      361 llcsagnvlr k
//
LOCUS       WP_108445901             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            denitrificans].
ACCESSION   WP_108445901
VERSION     WP_108445901.1
KEYWORDS    RefSeq.
SOURCE      Halomonas denitrificans
  ORGANISM  Halomonas denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas denitrificans"
                     /db_xref="taxon:370769"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55296
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela kgearvaltp dsakfiqklg hdcliesgag aaagfddaay rdagvtvvdg
       61 aealwteaev vikvreplee eaerlregqt lisffwpaqn eamleacrak gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnh fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgsesggy aapsspefre
      241 kqlecfreqa pdvdivitta lipgkpapkl wledmvaamk pgsviidlaa ekggncdltr
      301 adekvvsdng vivvgytdfp srmatqssll yatnvrhmlt dltpekegvi ehnmeddvir
      361 gatvthqgev tfpppppkvk aigaakpkpk ekeptpeekk aaehaafkaq tkrqvtllav
      421 ggalmlllgq vappsfmqhf ivfvlacfvg fqviwgvshs lhtplmavtn aisgiiilga
      481 vlqigsgsvv vgvlaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_108446993             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            denitrificans].
ACCESSION   WP_108446993
VERSION     WP_108446993.1
KEYWORDS    RefSeq.
SOURCE      Halomonas denitrificans
  ORGANISM  Halomonas denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Halomonas denitrificans"
                     /db_xref="taxon:370769"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40786
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlsvmrerh pgearvaltp anvsaladrg cqvfvetgag daagftnasy reagaeilet
       61 raqlldkgei ilcvdashae gladlreghv ciglmdplsq sdrfsdlarr gittlalelv
      121 prisraqsmd alssiatlag ykavllaaaq aprifpmmmt aagtlnpsrv fimgagvagl
      181 qaaatakrlg avveaydvrp aareqilsvg akpveldldt saaegqggya seqddafldr
      241 qraqmgavla qqdvvittaa ipgakapvli teemvkgmka gavivdlaae rggncalsqp
      301 gevvsvygvt iigprnlvat lphhasqmyg rnlenllrhl lddqgdlyld fedeildetv
      361 vthagevrat rirerlslpv kaseeva
//
LOCUS       WP_108451080             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_108451080
VERSION     WP_108451080.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53539
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfaphhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyesw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglk mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_108449794             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Halomonas].
ACCESSION   WP_108449794
VERSION     WP_108449794.1
KEYWORDS    RefSeq.
SOURCE      unclassified Halomonas
  ORGANISM  unclassified Halomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="unclassified Halomonas"
                     /db_xref="taxon:2609666"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55739
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaprerh kgearvaltp esaghiqklg heclietgag elagftdaay eeagvtivds
       61 meavfeqadv vvkvrepqke esdllrqgqt lisffwpaqn eemletckdk gasvvamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv liigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfed sqdgsesggy aapsspefre
      241 kqlelfrqqa pevdivitta lipgrpapkl wledmvkamk pgsvvvdlaa ekggncdltk
      301 pdervvtdng vivvgytdfp srmatqssll ystnirhmlt dltpekdgki vhdmeddvir
      361 gatvthqgev tfpppppkvk aiaaakpkpk ekeptpeerk aaehaafvkq tksqvtmlav
      421 ggivmgllgl vapasfmqhl ivfalacfvg fqviwnvshs lhtplmavtn aisgiiilga
      481 vlqvgsgswl vallagisvl iasinvvggf lvtrrmlamf qks
//
LOCUS       WP_108456382             512 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Colwellia].
ACCESSION   WP_108456382
VERSION     WP_108456382.1
KEYWORDS    RefSeq.
SOURCE      unclassified Colwellia
  ORGANISM  unclassified Colwellia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="unclassified Colwellia"
                     /db_xref="taxon:196834"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54001
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipkeal sgenrvasap tavvsllklg fevqiqkgcg tkasftdqef idagasvatk
       61 ktvwqsdiif kvnpptieei atmkdgayli gfiapaqned ilnalkeksi tslamemvpr
      121 mtrsqsmdal ssmaniagyr avieathhfg rfltgqitaa gkmppakvmi igagvaglaa
      181 igtasslgai vrafdtrpev keqiesmgae fleldyeepe dtgsgdgyak emskafidae
      241 malfaaqakd vdiiittami pgkpapklit aamvesmktg siivdlaaag ggncelteag
      301 kvvnangvki igytdlvsrl pnqssqlyan nlvsltkllc kekdgtlnid fddvvirnmt
      361 vvnqneitfp pppiqvsaap akpkvapvka aevkvekpms ptkkygmmaa gallfgwvas
      421 vapadflshf tvfvlacvig ynvvwnvshs lhtplmsvtn aisgiiivga ilqvgnsspl
      481 iqllagvail iatinivggf vvtkrmlkmf rk
//
LOCUS       WP_108469681             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter difficilis].
ACCESSION   WP_108469681
VERSION     WP_108469681.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter difficilis
  ORGANISM  Polynucleobacter difficilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Polynucleobacter difficilis"
                     /db_xref="taxon:556054"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39373
     Region          1..354
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpletr pgetrvaatp etvkklisqg hqfiiqsgag ngasvpdsay eavgatigsa
       61 adafaaemvl kvrspqadel kqiksgtvli gmldpfdnea iaamasqgit afaleaaprt
      121 traqsmdvls sqaniagyka vmlaaneyqr fmpmlmtaag tvkaarilil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpyetdee reiakgvggy arpmpeswmk
      241 rqaalvaera mqadiviata lipgrkppvl lhsetvakmk pgsvvidlaa grgengsgnc
      301 pltradqivd angvkivght nlpsmvaada salyarnvld fmkliinkea qlaipaaadd
      361 divaaclmcr dgqavrtn
//
LOCUS       WP_108481674             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas plecoglossicida].
ACCESSION   WP_108481674
VERSION     WP_108481674.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas plecoglossicida
  ORGANISM  Pseudomonas plecoglossicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas plecoglossicida"
                     /db_xref="taxon:70775"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38854
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqrgag lnasipdsay eavgaslgsa
       61 adaygaqlvl kvvapndqel alinngsllv gmlnpfnsel igkmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvhengv iivgptnlpa qvgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_108486663             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_108486663
VERSION     WP_108486663.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38764
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikkligqg hqvtvqtgag vsasipdsay eavgaaignd
       61 aaafgadlvl kvvapteael ahmktgavlv gmlnpfsnet iarmnargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpaswme
      241 rqakavhera kqadivitta lipgrkaptl lheatvaemk pgsviidlaa aqggncplte
      301 aeqvvikhgv tivghsnlaa mvpadasaly arnlldflkl vidgegkfhl nleddivaac
      361 lmcrdgnvvr tng
//
LOCUS       WP_108482093             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oceaniglobus ichthyenteri].
ACCESSION   WP_108482093
VERSION     WP_108482093.1
KEYWORDS    RefSeq.
SOURCE      Oceaniglobus ichthyenteri
  ORGANISM  Oceaniglobus ichthyenteri
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Oceaniglobus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Oceaniglobus ichthyenteri"
                     /db_xref="taxon:2136177"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55002
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligtpkeqf egerrvaltp dsakalaklg hsaliesgag aaagfsdaay aeagvevvkn
       61 agvvwskadv vakvrppses evaqmrsgqt lisffnpagn adlmeqakeq gasviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfee ssqdsaatgg yaapsspefr
      241 ekqlakfrem apeidiviat alipnreape lwtpdmvamm kpgsvivdla aekggncklt
      301 vpdekivtdn gvtivgytdf psrmaaqast lystnirhml tdltpdkdgk inhnmeddvi
      361 rgatvthqge itypppppkv aaiaaapkkd kpkeltaeek kakevadfka atksqvgllv
      421 iggvimaiig afapasfmqh fivfalacfi gfqviwgvah slhtplmait naisgivivg
      481 allqigsgnm lvvllslvsv liasinivgg flvtrrmlam fqks
//
LOCUS       WP_108495186             546 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Promicromonospora sp. AC04].
ACCESSION   WP_108495186
VERSION     WP_108495186.1
KEYWORDS    RefSeq.
SOURCE      Promicromonospora sp. AC04
  ORGANISM  Promicromonospora sp. AC04
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Promicromonospora.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Promicromonospora sp. AC04"
                     /db_xref="taxon:2135723"
     Protein         1..546
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54074
     Region          1..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipddgg plvpatpatt arlvglgyev avaagagaga gfpdaayeaa gavvvpdava
       61 waadivavtr apdelaapgp aglrpgargp dglrigavli aqiahatrpe lvralanrgv
      121 talaldavpr israqsldvl salsnvagyr avveaaaefg gmfsgqvtaa gttppanvfv
      181 igagvaglaa igaagslgaq vrafdvrpev aeqiesmgat vvraddaaqq vsadgyasal
      241 ttdqeaaalr aygvetaaad ivvttalvrg tapttitaem vanmrpgsvi vdlaapgggn
      301 celtvpgrrv vsdngvvilg ytdlpdrmpr htsellgtav anlvqlgtpa rdgrlaldpd
      361 dvvvrgmtva rggevlwppp pvavsapaea qslagssggp rsraeagspe srpggagars
      421 pritravlig lgavlgalav aaspadqaah ftvlalavvv gfyvishvsh alhtplmsqt
      481 naisgiilvg gmlqigsadp vvttlavlas avasinifgg flvthrmlam frrggpraga
      541 gegsar
//
LOCUS       WP_108497541             532 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Acidovorax].
ACCESSION   WP_108497541
VERSION     WP_108497541.1
KEYWORDS    RefSeq.
SOURCE      unclassified Acidovorax
  ORGANISM  unclassified Acidovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="unclassified Acidovorax"
                     /db_xref="taxon:2684926"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55474
     Region          11..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtspvpqpq rigvpretfp gekrvatvpd vvekliklgf tvtvesgagd aanfsddayr
       61 aagaeivgda aalwaasdiv fkvrppssde valmregttl idfiwpaqnp elmqqlaark
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rkmyaeqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti vgytdlasrl akqsstlyat nllrlteelc kakdgvavvn
      361 meddairgla vvkegsitwp applkqapap apkaaapvae kksshgtgap msaktltivf
      421 avlavlfwai gayapvaflg hftvfvlacf igymvvwnvt palhtplmsv tnaissiiai
      481 galvqiappd agvngrpdgl ilwlafaalv ltainmfggf avtrrmlamf rk
//
LOCUS       WP_108501706             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            indicus].
ACCESSION   WP_108501706
VERSION     WP_108501706.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus indicus
  ORGANISM  Paracoccus indicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus indicus"
                     /db_xref="taxon:2079229"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55351
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalketh tgearvaitp asaghlaklg hevfvqsgag tgagfadady akadvticqt
       61 aseligavdv vakvrqpsda eidqmregqt iisffypaqn sellakakdq gitaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aqvhafdvrp evseqiesmg aefvflefde ptadgaatgg yaapsspefr
      241 ekqlakfrel apqmdivitt alipgrdapv lwtadmvaam kpgsvivdla aekggncelt
      301 vmderivsdn gvvivgytdf psrmgaqase lygnnvrhfi adltpkkdgv idhnmeddvi
      361 rgatvardhd vtwpppppkv aaiaaqkpke kkkeptpeer raaeaaafka etrsqvgilv
      421 ggglllllig lvapvsfmsh fivfvlacfi gfrviwnvah slhtplmait naissiiilg
      481 almqigsqsw wvvllgalav lmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_108509002             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter acidiphobus].
ACCESSION   WP_108509002
VERSION     WP_108509002.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter acidiphobus
  ORGANISM  Polynucleobacter acidiphobus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Polynucleobacter acidiphobus"
                     /db_xref="taxon:556053"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39256
     Region          1..354
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpletr pgetrvaata etvkklisqg hqviiqsgag vgaslpdsay eavgasigsa
       61 adafaceivl kvrapqadel kqikagsvll gmldpfdnag isamaaqgit afaleaaprt
      121 traqsmdvls sqaniagyka vmlaaneyqr fmpmlmtaag tvkaarilil gagvaglqai
      181 atakrlgsvi easdvrpaak eqieslgakf vdvpyetdee reiaqgvggy arpmpeawmk
      241 rqaalvaera aqadivitta lipgrkppvl lhadtvekmk agsvvidiaa grgengsgnc
      301 pltradqvin hngvkivgyt nlpsmvaada salyarnlld fmkliinkeg qlaipaaadd
      361 divaaclmcr dgqairtn
//
LOCUS       WP_108511790             492 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Pasteurella multocida].
ACCESSION   WP_108511790
VERSION     WP_108511790.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella multocida
  ORGANISM  Pasteurella multocida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Pasteurella multocida"
                     /db_xref="taxon:747"
     gene            1..492
                     /gene="nrfA"
     Protein         1..492
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=54945
     Region          14..491
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mngviivntl kkrlfvattm iwglsvtlpv laeykpieqp vepanpslki esrndlfkek
       61 ypkqyqtwad tsksmdldsv nyedprvivl wagyafakdy kkprghfyav tdvreilrta
      121 apmtldagpm pmacwscksp dvprliaerg eagyfgatwa sggsevvnpi gcadchdtts
      181 kdfaegkpal riarpyvlra lekidhkfdt sdrtdqraal canchveyyf agdlkqvtfp
      241 wdngitvdam ekyyddigfv dwthavskap mlkaqhpdye twmlgvhgkn gvtcidchmp
      301 kvqgadgkvy tdhqignpfn afehtcanch dqskeklqam vksrkteikd vmlrledqlv
      361 aahfeakaaw eagaskeemk ealqdirhaq wrwdyaaagh gghihapdvl lkvigtgldk
      421 ssdartklvr vlakhgitdp vqlpdistae nawkatgvdi ekerkakaef lktvvpqwdk
      481 earekgllpa ek
//
LOCUS       WP_108514463             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium algeriense].
ACCESSION   WP_108514463
VERSION     WP_108514463.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium algeriense
  ORGANISM  Bradyrhizobium algeriense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium algeriense"
                     /db_xref="taxon:634784"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39223
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkyraig aevaiepgag iksglpdsef tavgatisad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygneaa lktiadagva afamelmpri
      121 traqvmdvls sqanlagyra vieaaesfgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa dmvksmkpgs vlvdlaverg gnvegakage
      301 vvdvdgikiv gytnvagrva qsasslyarn lfnfietmvd kpnkalavnw ddelvkatal
      361 trdgavvhpn fqpka
//
LOCUS       WP_108518031             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Homoserinimonas hongtaonis].
ACCESSION   WP_108518031
VERSION     WP_108518031.1
KEYWORDS    RefSeq.
SOURCE      Homoserinimonas hongtaonis
  ORGANISM  Homoserinimonas hongtaonis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Homoserinimonas.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Homoserinimonas hongtaonis"
                     /db_xref="taxon:2079791"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39390
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnvgvlrele pgerrvaatp esvrqlvgeg ltvtiergag eaagypdadf vaagatvvds
       61 iapgelevla hvrplsveli galregaitv glaspasslp avaalhdarv tafalelvpr
      121 israqsmdal tsqalvagyr cvleaamrlp rffplfmtaa gtippakvlv lgagvaglqa
      181 iatakrlgar vsandvreas adevksmggt fisldlgtad asggyakela edrarrqrel
      241 ltphvsesdi vittaaipgr aaprlitaem llgmkpgsvi idlaaetggn vegsvagedt
      301 aiplpgggti tivgmkdvas tmpfdasrly aknvanlisl mtvdgkvepd fadeivrgas
      361 lthdgavthe ptrealaaaa pkgdk
//
LOCUS       WP_108544914             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_108544914
VERSION     WP_108544914.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38657
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet itklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_108547882             394 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum humicireducens].
ACCESSION   WP_108547882
VERSION     WP_108547882.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum humicireducens
  ORGANISM  Azospirillum humicireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Azospirillum humicireducens"
                     /db_xref="taxon:1226968"
     Protein         1..394
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41014
     Region          1..378
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,105,302,329,331)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,138..139,148..149,152..153,156..157,159..160,
                     162..167,169,171..173,176,199..200,292..293,336..337,341,
                     344..345)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,138,141,144,185..188,208..210,242,253,
                     270..272,279,281)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(135..136,138,148,191..192,199,215..216,218..221)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(168..172,175,178,201,203)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiprerr pgerrvaasp etvkklktlg ldvvvesgag lgssitdsaf eaagaaiaad
       61 aasaladadi vlkvqrplia qeiekgegge delalirkga llfailnpyn srdhvkayad
      121 agvnafamef mpritraqvm dvlssqanla gykavvdaas eygrafpmmm taagtvppar
      181 afimgvgvag lqaiatakrl gaivsatdvr pavkeqvqsl ggsfvavene efkqaetagg
      241 yakemsddyk rqqaalvaeh ikkqdlvitt alipgrkapi lvtaehvasm kpgsvivdla
      301 veqggnvega klgevvttan gvkivghany asriaesasl lyaknllall tslhgkdtgv
      361 avnwddeivk aialtrdgai vhpafadare aqpa
//
LOCUS       WP_108548635             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum humicireducens].
ACCESSION   WP_108548635
VERSION     WP_108548635.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum humicireducens
  ORGANISM  Azospirillum humicireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Azospirillum humicireducens"
                     /db_xref="taxon:1226968"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40077
     Region          1..378
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,105,302,329,331)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,138..139,148..149,152..153,156..157,159..160,
                     162..167,169,171..173,176,199..200,292..293,336..337,341,
                     344..345)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,138,141,144,185..188,208..210,242,253,
                     270..272,279,281)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(135..136,138,148,191..192,199,215..216,218..221)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(168..172,175,178,201,203)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvaipkerr agelrvaasp etvkklkglg ldvvvesgag lgssitdsaf eaagaaiaad
       61 aasaladadi vlkvqrplia qeiekgegge delalirkga llfailnpyn srdhvkayad
      121 agvnafamef mpritraqvm dvlssqanla gykavvdaas eygrafpmmm taagtvppar
      181 afimgvgvag lqaiatakrl gaivsatdvr pavkeqvqsl ggsfvavene efkqaetagg
      241 yakemsddyk rqqaalvaeh ikkqdivitt alipgrkapi lvtaehvasm kpgsviidla
      301 veqggnvega klgevvttan gvkivghany asriaesasl lyaknllall tslhgkdtgv
      361 avnwddeivk aialtrdgav vhpafag
//
LOCUS       WP_108576542             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aeromicrobium chenweiae].
ACCESSION   WP_108576542
VERSION     WP_108576542.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium chenweiae
  ORGANISM  Aeromicrobium chenweiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Aeromicrobium chenweiae"
                     /db_xref="taxon:2079793"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53020
     Region          4..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msvigvvtes vagetrvaat patvtqlikl gyqvlvesga gekssftdea yveagasiga
       61 tadvwrseiv fkvnaptpae iglladgatl islispalnp dlveqlssrp itvlamdavp
      121 risraqsmdv lssmaniagy ravveaanvf grfftgqita agkvppakvl vagvgvagla
      181 aigtanslga ivratdprae vadqvkslgg eylavevete qstdgyakat seeydrraae
      241 iyseqaaevd iiittalipg raapvlitea dvasmkpgsv ivdmaaangg nvvgsrpgea
      301 vvtpngvtil gytdlagrlp tqasqlygtn lvnlmklltp akdgqlvldf ddvvqrtitv
      361 vrqgettwpp ppvqvsaapa aapvevaepk ppkaqltqra klglvglgvl alflvnafap
      421 dplpehftvl tlaivigyyv igkvhhalht plmsvtnais giivvgamlq igidgdgeng
      481 tviqvlafva illasinvfg gfavtrrmls mfsk
//
LOCUS       WP_108593993             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_108593993
VERSION     WP_108593993.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35915
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgngss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechav frsvllrihe rkgivyheqd slntlmtnlm argvisaeya
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vsp
//
LOCUS       WP_108596450             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Agromyces
            badenianii].
ACCESSION   WP_108596450
VERSION     WP_108596450.1
KEYWORDS    RefSeq.
SOURCE      Agromyces badenianii
  ORGANISM  Agromyces badenianii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Agromyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Agromyces badenianii"
                     /db_xref="taxon:2080742"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52833
     Region          3..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigviaeq spetrvaatp atvkqlialg hevavqagag aasafpdday reagaeivdg
       61 atalasdlvl kvnapteaei aqltpgatli gllapafkpe llqalaargv talamdavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksigge ylkveveveq stdgyakats eaydrraaev
      241 yseqaadvdi iittalipgr aaprlitaad vasmksgsvi vdmaagmggn vegsvageri
      301 vtpngvvilg ytdlasrlpt qasqlygtnv vnliklltpg kdgvlaldfd dvvqrsvtva
      361 kdgavtwppp pvqvsaaava aasapgagga khaaavpekk rpmspakkaa lvavgiaalf
      421 avnavapppl pqhftvlvla vvvgfyvigk vahalhtplm svtnaisgii vvgamvqits
      481 dvlvvqilaa vavllasini fggfavtrrm lamfsagktg adra
//
LOCUS       WP_108597930             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. HMWF013].
ACCESSION   WP_108597930
VERSION     WP_108597930.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. HMWF013
  ORGANISM  Arthrobacter sp. HMWF013
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Arthrobacter sp. HMWF013"
                     /db_xref="taxon:2056849"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53385
     Region          3..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivael gresrvaatp ttvkqllglg yevvvekgag esasfrdeay veagalivga
       61 deawgsevvl rvnppteeei drlapgatli gslspglrpe lvealaarpi talaldavpr
      121 israqsmdvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksiggt ylkveveeem kssdgyakat seaynaraae
      241 iyteqardvd iiittalipg rpapklltae dvagmksgsv ivdmaagqgg nvegsvager
      301 vvtdngvvil gytdlparlp aqasqlygtn mlnllklltk dkdgvlridf ddvvqrsvtv
      361 vrdgektwpp ppvqvsaapa ataqapvada aapkkkqgls tgakaglfaa giaalflina
      421 vapaplpqhf tvlmlsvvvg fyvigkvhha lhtplmsvtn aisgiivvga llqvtsdnpv
      481 mqvlaavavl lasinifggf avtrrmlamf srgdgark
//
LOCUS       WP_108598546             404 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. HMWF013].
ACCESSION   WP_108598546
VERSION     WP_108598546.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. HMWF013
  ORGANISM  Arthrobacter sp. HMWF013
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Arthrobacter sp. HMWF013"
                     /db_xref="taxon:2056849"
     Protein         1..404
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41462
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiprerh egelrvaatp etvrqlaglg levivesmag apagypdhdy aeagcrlvqa
       61 ldlseldvla hvrplepata kalhsgavtv glaspssela tvqaladagv tsfalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplfmtaa gtvpparvlv lgagvaglqa
      181 igtakrlgar vsandirpas adevasmggt firldletae asggyarels adrgalqrel
      241 laphvaqsdv littaavpgr rapllvsrqm vqamrpgsvv vdlaaesggn vegsvpgedi
      301 lvptadghgh vtlvgvkdap salasdasrl yaknvanlla lmtrdgvvap dfdddviaga
      361 clthdgavrh lptaealaal ipalpdhaph vpghapsvqd rger
//
LOCUS       WP_108599870             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. HMWF013].
ACCESSION   WP_108599870
VERSION     WP_108599870.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. HMWF013
  ORGANISM  Arthrobacter sp. HMWF013
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Arthrobacter sp. HMWF013"
                     /db_xref="taxon:2056849"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52436
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigivaera dgetrvagtp stvvqlmklg yqiviergag agsafpdrdy evagaeivdh
       61 rsawgadvvl tvnapsdddl alladgatlv swlspglnpg ivdklvalpi talavdtvpr
      121 lsraqsmdvl sstgniagyr avveaanqfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igtasslgai vratdprpev aeqvksiggt ylaveiaekm estdgyakat seaydrraae
      241 lyseqardvd iiittanipg raapklitaa dvasmksgsv ivdlaaangg nvegtvpgel
      301 ivtsngvtiv gytdlarrlp tqasqlygqn lvnllklltp gqdgllvldh ddvvqraitv
      361 vqngerlwpp ppvqvsaapt aaaagepsaa ppkaakkask lasaaltvag iaalfgliti
      421 apaplpqhit vlvlavvigf yvigkvhhal htplmsvtna isgivvvgam lqiaiddpvi
      481 kafsaaavll asinvfggfa vsrrmlrmfs kd
//
LOCUS       WP_108607020             433 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aminobacter sp. MSH1].
ACCESSION   WP_108607020
VERSION     WP_108607020.1
KEYWORDS    RefSeq.
SOURCE      Aminobacter sp. MSH1
  ORGANISM  Aminobacter sp. MSH1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Aminobacter.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Aminobacter sp. MSH1"
                     /db_xref="taxon:374606"
     Protein         1..433
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44276
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtifipre idaiesrvga spdtvkrlvg lgfdvivesg agtlsripda dftavggkig
       61 kaadagkadv vlkvrrpsea elngykpgaa vlatmdpygn daavaamaka gvtafamefm
      121 pritraqvmd vlssqanlag yqavidgaae ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrmg aivtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegav
      301 pgkvvttang akivghlnvp grvaasasll yaknlfafle tmvdkttkqi ainrddelvk
      361 atmltdagkv vhpnfanaaa aaaadkpkpv vagqnrgddp asdgaakaek paaakkttaq
      421 kttakkpakq gda
//
LOCUS       WP_108610205             433 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aminobacter sp. MSH1].
ACCESSION   WP_108610205
VERSION     WP_108610205.1
KEYWORDS    RefSeq.
SOURCE      Aminobacter sp. MSH1
  ORGANISM  Aminobacter sp. MSH1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Aminobacter.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Aminobacter sp. MSH1"
                     /db_xref="taxon:374606"
     Protein         1..433
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44273
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpgtifipre idaiesrvga spdtvkrlvg lgfevvvesg agtlsripda dftavggkig
       61 kaadagkadv vlkvrrpsea elkgykpgaa vlatmdpygn daavaamaka gvtafamefm
      121 pritraqvmd vlssqanlag yqavidgaae ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrmg aivtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegav
      301 pgkvvttang akivghlnvp grvaasasll yaknlfafle tmvdkttkqi ainrddelvk
      361 atmltdggrv vhpnfanaaa aaaadkpkpv vagqnrgddp asdgaakaek paaakkttaq
      421 kttakkpakq gda
//
LOCUS       WP_108616832             534 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. HMWF029].
ACCESSION   WP_108616832
VERSION     WP_108616832.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. HMWF029
  ORGANISM  Acidovorax sp. HMWF029
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Acidovorax sp. HMWF029"
                     /db_xref="taxon:2056863"
     Protein         1..534
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55609
     Region          11..534
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtspvpqpq rigvpretfp gekrvatvpd vvekliklgf tvtvesgagd aanfsddayr
       61 aagaeivgda aalwagsdiv fkvrppgsde valmregttl idfiwpaqnp dlmqqlaakk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rkmyaeqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg qavvrhgvti vgytdlasrl akqsstlyat nllrlteelc kakdgvavvn
      361 meddairglt vvkdgaitwp applkqapap vpkaaapvae kksshghgtg apmsaktlti
      421 vfavlavlfw aigayapvaf lghftvfvla cfigymvvwn vtpalhtplm svtnaissii
      481 aigalvqiap pdagvngrpd glilwlafaa lvltainmfg gfavtrrmla mfrk
//
LOCUS       WP_108620113             401 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Orrella
            marina].
ACCESSION   WP_108620113
VERSION     WP_108620113.1
KEYWORDS    RefSeq.
SOURCE      Orrella marina
  ORGANISM  Orrella marina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Orrella.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Orrella marina"
                     /db_xref="taxon:2163011"
     Protein         1..401
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41644
     Region          1..395
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipretr dgetrvaatp esvkklvqag htvlvehgag faaqfldeqy qdsgatlvta
       61 sealdaelvl kvrapdqiel aqmsagtvlv gmlepydavs merlaaaglt afalesapri
      121 sraqnmdvls sqanlagyka vilganafgk ifpmmmtaag tvkaarvvvl gagvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetele rqaaqgvggy aqpmppswma
      241 rqaekvaerc sqadivicta lipgrpapql vsvgtvkamk pgsvivdmav erggncplsq
      301 lgltvvehgv tiiglpnlpg llatdasaly arnlleflkl ilarpddkta kaeangtant
      361 nadtgaeksv nttapglain rddeivqacl vcedgqllkk a
//
LOCUS       WP_108626004             534 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. 107].
ACCESSION   WP_108626004
VERSION     WP_108626004.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. 107
  ORGANISM  Acidovorax sp. 107
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Acidovorax sp. 107"
                     /db_xref="taxon:2135638"
     Protein         1..534
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55568
     Region          11..534
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtspvpqpq rigvpretfp gekrvatvpd vvekliklgf avtvesgagd aanfsddayr
       61 aagaeivsda aalwaasdiv fkvrppssde varmregttl idfiwpaqnp dlmqqlaakk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsdgfqaaq rkmyaeqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti vgytdlasrl akqsstlyat nllrlteelc kakdgvavvn
      361 meddairglt vvkdgaitwp applkqapap apkvaapvve kksghghgtg apmsaktlti
      421 vfavlavlfs aigayapvaf lghftvfvla cfigymvvwn vtpalhtplm svtnaissii
      481 aigalvqiap pdagvngrpd glilwlafaa lvltavnmfg gfavtrrmla mfrk
//
LOCUS       WP_108627682             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_108627682
VERSION     WP_108627682.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53596
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw anslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_108629190             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_108629190
VERSION     WP_108629190.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35784
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkecg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnlfhehgl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf scvvkechaa frsvllrihe rkgivyheqd slntlmanlm argvisaeyv
      241 hkfhflsdvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 aap
//
LOCUS       WP_108637370             363 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium terramassiliense].
ACCESSION   WP_108637370
VERSION     WP_108637370.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium terramassiliense
  ORGANISM  Mycobacterium terramassiliense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Mycobacterium terramassiliense"
                     /db_xref="taxon:1841859"
     Protein         1..363
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37068
     Region          6..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(19,74,93,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miaqttigvv aesgtderrv alvpkavasl vgsgvavvve sgagegallp dalyieagat
       61 igdawaadvv vkvapptaee vgklrsgqal igflaprnae nsigalraag vqafaleaip
      121 risraqamda lssqanvsgy kavllaases trffpmltta agtvkpatvl vlgvgvaglq
      181 alatakrlga rttgydvrpe vadqvrsvga qwldvgidaa geggyarelt deeraqqqqa
      241 lekaisgfdv vittalvpgr paprlvtaaa veamkpgsvi vdlagetrgn celtepgqtv
      301 vkhdvtiasp lnlpatmpeh aselysknit alldllitdg klapdfddev iaescvtrag
      361 eds
//
LOCUS       WP_108638546             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_108638546
VERSION     WP_108638546.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53659
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfekas rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvra hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_108638925             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_108638925
VERSION     WP_108638925.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35911
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqilll iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlilndf scvvkechaa frsvllrihe rkgivyheqd slntlmanlm argvisaeyv
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 vvp
//
LOCUS       WP_108640579             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassorhabdomicrobium marinisediminis].
ACCESSION   WP_108640579
VERSION     WP_108640579.1
KEYWORDS    RefSeq.
SOURCE      Thalassorhabdomicrobium marinisediminis
  ORGANISM  Thalassorhabdomicrobium marinisediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Thalassorhabdomicrobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Thalassorhabdomicrobium marinisediminis"
                     /db_xref="taxon:2170577"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55622
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkety egenrvamtp asardlqklg hecvietkag laagfadady eaagvevvkt
       61 aaalwkaadi vakvrvpnet emkrlranqt lisffspvad edkmqaaakk gatviamemi
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqadgassgg yasvsspefr
      241 eaqlakfrel apemdivitt alipnreape lwtedmvkam kpgsvvvdla aekggncklt
      301 vkdekivtdn gvtiigytdf psrmatqast lyatnirhll tdltpekdgv idhdmdddvi
      361 rgatiahake vtfpppppkv qaiaaqpkaa vkeptpeeir anevaafkaq tkqqvtllgi
      421 gaalllligl iapasfmqhf ivfilsvfig fqviwgvahs lhtplmavtn aissiiilga
      481 liqigstgwl itilaalgif masinifggf lvtrrmlamf qks
//
LOCUS       WP_108644747             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudogemmobacter blasticus].
ACCESSION   WP_108644747
VERSION     WP_108644747.1
KEYWORDS    RefSeq.
SOURCE      Pseudogemmobacter blasticus
  ORGANISM  Pseudogemmobacter blasticus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudogemmobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudogemmobacter blasticus"
                     /db_xref="taxon:1075"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55238
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaltevf agenrvamtp esalaiqklg hscciqsgag dkagftdaay aaagvdvlad
       61 akavlaaadv vvkvrgpeek eakalrqgqt lisffwpaqn pdlletvkaq gasviamdmv
      121 prisraqkmd alsstanlag yravieaann fprfftgqvt aagkvppakv lvvgagvagl
      181 aaigasvslg aityafdvrp evaeqiesmg aefvyldfae qtqdgaatgg yaapsspefr
      241 eaqlkkfrel apemdivitt alipgrpapk lwtedmvram krgsvivdla aerggncdlt
      301 vpdqkivtdn gvtivgytdf psrmatqass lysnnirhml adltpkkdgv ivhnmeddvi
      361 rgatvahdga itypppppkv qaiaaakpke kareltpeer raqevaafkq qtrnqvvmla
      421 aggalmglvg lyapasfmsh fivfvlacfv gfqviwnvsh slhtplmavt naisgiivlg
      481 allqigsgnf fvlilaavsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_108678611             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            vulnificus].
ACCESSION   WP_108678611
VERSION     WP_108678611.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54506
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprell agetrvaasp ssveqliklg fdvvvetqag alasfddsay esagakmvsk
       61 eeawnselil kvnapiidee ksideialik egatlvsfiw paqnpqlmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvfvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaeflsv dyqeaagsgd gyakemsddf
      241 nkkaaelyaa qakdvdiiit talipgkpap klitkemvds mkagsvivdl aaanggncey
      301 tianqvvtta ngvkvigytd mvgrlptqss qlyatnlvnl fkllckekdg ninidfedvv
      361 lrgvtvvkdg eitwpappiq vsaqpqakpk avekpapkvq epvspvkkla glavavgafa
      421 wiasvapaaf lthftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigk
      481 gngavtflaf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_108648455             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter rarus].
ACCESSION   WP_108648455
VERSION     WP_108648455.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter rarus
  ORGANISM  Polynucleobacter rarus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Polynucleobacter rarus"
                     /db_xref="taxon:556055"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39323
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpletr igefrvaatp etvkklvssg hsvlieagag iaasvldsay eavgakissk
       61 eevyaaelvl kvrapfenel smmtsgsvli gmldpfdnam iaamathgit gfsleaaprt
      121 traqsmdvls sqaniagyka vmmatnsyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpfeteee keiaqgvggy arpmpaswmq
      241 rqsvlvaera kqadivitta lipgrkapml lssetvaqmk pgsvvvdlaa gkgdsgsgnc
      301 pltevdqivv khgvtiigls nlpslvaada salyarnvfd flkliinkea gltiptdddi
      361 vtaclmcsng qvirtna
//
LOCUS       WP_108679491             433 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aminobacter sp. MSH1].
ACCESSION   WP_108679491
VERSION     WP_108679491.1
KEYWORDS    RefSeq.
SOURCE      Aminobacter sp. MSH1
  ORGANISM  Aminobacter sp. MSH1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Aminobacter.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Aminobacter sp. MSH1"
                     /db_xref="taxon:374606"
     Protein         1..433
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44245
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpgtifipre idaiesrvga spdtvkrlvg lgfevvvesg agtlsripda dftavggkig
       61 kaadagkadv vlkvrrpsea elngykpgaa vlatmdpygn daavaamaka gvtafamefm
      121 pritraqvmd vlssqanlag yqavidgaae ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrmg aivtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegav
      301 pgkvvttang akivghlnvp grvaasasll yaknlfafle tmvdkttkqi ainrddelvk
      361 atmltdagkv vhpnfanaaa aaaadkpkpv vagqnrgddp asdgaakaek paaakkttaq
      421 kttakkpakq gda
//
LOCUS       WP_108683798             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methyloceanibacter sp. wino2].
ACCESSION   WP_108683798
VERSION     WP_108683798.1
KEYWORDS    RefSeq.
SOURCE      Methyloceanibacter sp. wino2
  ORGANISM  Methyloceanibacter sp. wino2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Hyphomicrobiaceae; Methyloceanibacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Methyloceanibacter sp. wino2"
                     /db_xref="taxon:2170729"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39839
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miaigvpaeg seeprigltp etvkklvkag akvtvrsgag lrshfsdedy keagasiaks
       61 dedavsgadv vftvrrpsvd lakamkkgas ligmldpfsd kaglealakt gvslfamefm
      121 pritraqsmd vlssqsnlag ykavvnaaaa feralpmmmt aagtvpaarv fvmgvgvagl
      181 qaiatarrlg aivtatdvrp avkeqvaslg akfiavedee fkqaetsggy akemsdeykk
      241 kqaelvaehv knqdivitta lipgrpapkl istamiesmk pgsiivdlaa erggnaeltk
      301 pgetaehkgv rifgqlnlpg qvpvnassly arnlqafiep fidketkela idwedelaig
      361 taiardgaiv nervaggkts
//
LOCUS       WP_108695059             195 aa            linear   BCT 07-JUL-2024
DEFINITION  cytochrome c nitrite reductase pentaheme subunit [Vibrio
            vulnificus].
ACCESSION   WP_108695059
VERSION     WP_108695059.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03146.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     gene            1..195
                     /gene="nrfB"
     Protein         1..195
                     /product="cytochrome c nitrite reductase pentaheme
                     subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=21597
     Region          7..194
                     /region_name="PRK11659"
                     /note="cytochrome c nitrite reductase pentaheme subunit;
                     Provisional"
                     /db_xref="CDD:183264"
ORIGIN      
        1 mgniklaivi mlksilafsf ygysfsaiad tsvateatds srfqvelird rdykcvqchk
       61 dsketlsgsh gedahkilgr evnctechnn igpdhregap lvtkyspaqs kqgtekvfmd
      121 tsailkanga ctdchqpqdl qqaswthdvh aknltcsnch dvhankakvl glerkekikm
      181 cvdchsdfnq keeer
//
LOCUS       WP_108691574             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pelagivirga sediminicola].
ACCESSION   WP_108691574
VERSION     WP_108691574.1
KEYWORDS    RefSeq.
SOURCE      Pelagivirga sediminicola
  ORGANISM  Pelagivirga sediminicola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pelagivirga.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Pelagivirga sediminicola"
                     /db_xref="taxon:2170575"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54781
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkevs egearvamtp dsaaqlqklg ydcaiesgag rlagfadady kaagvevvkt
       61 aaalwkgsdi iakvrpatgt elkrlvkgqt lisffdpsgn dagmeaarks gasviamemv
      121 prisraqkmd alssmaniag yravieaggn fgrfftgqit aagkvpparv lvigagvagl
      181 aaigtstslg avtlafdvrp evaeqvesmg aefvyldfde aqdgaatggy asvsspefre
      241 aqlakfrela pdidivitta lipnreapel wtedmvkamk pgsvivdlaa ekggnckltv
      301 kdekivteng vtiigytdfp srmaaqassl yatnirhmma dltpekdgqi hhdmdddvir
      361 gatvvhagei typppppkvq aiaakpkqta paptaaerka qelalfrkqt ktqatllaig
      421 aaimlligaf apesfmshfi vfvlacfigf sviwgvshsl htplmavtna isgiiilgal
      481 lqvgsgswlv vllaavsvfi asinivggfl vtrrmlamfq ks
//
LOCUS       WP_108698138             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas oligotropha].
ACCESSION   WP_108698138
VERSION     WP_108698138.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas oligotropha
  ORGANISM  Nitrosomonas oligotropha
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Nitrosomonas oligotropha"
                     /db_xref="taxon:42354"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39276
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir ggetrvaatp etvkkytakg vhkvsvqsga gagasipdsa yqeagativa
       61 daaelyaqaq ivlkvrgpes aelamirkda vllglltphh kesvdaltqh gltafamekl
      121 prisraqnmd vlssqaniag ykavimaanv yqrffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avveafdvrp avkeqveslg akfvevplsd eekakaetag gyatemsddy
      241 krrqgelvhe raiaadiiit talipgrpap vlikeetvqs mkpgsvivdm aveaggncpl
      301 selnqtvvkh gvhligiani pglvaadast lyarnlmnfl nlmldqesge lkidradeii
      361 agtllcsgge iavks
//
LOCUS       WP_108715514             509 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Actinobaculum].
ACCESSION   WP_108715514
VERSION     WP_108715514.1
KEYWORDS    RefSeq.
SOURCE      unclassified Actinobaculum
  ORGANISM  unclassified Actinobaculum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinobaculum.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="unclassified Actinobaculum"
                     /db_xref="taxon:2609299"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53815
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeps egqtlvaasp dtvgkliklg yqvcvetgag vaasyldqqy qavgaeivdr
       61 drawaadivt cldappdgel almregatli arldpgshpe rlekfsqrgi talsidavpr
      121 israqsmdvr ssmaniggyr avieaanrfg rlftgqvtaa gkvppatvyv igvgvaglsa
      181 igtanslgai vkatdvrpet aeqvhsmgge fvaipvqqes tdgyakamta dqeqlamkvy
      241 aeqaassdiv ittaaipgra aprlltaqai aamkpgsviv dmaassggnc eltvpgevvq
      301 tdngvtiigy ldlprrlpgq asqlygqniv nffklatpqr dgqltldedd vvvrsmtvtl
      361 nghimwpppp vkvsaapppt pkqeevaape pepekpawrr wwwriaaaav lvwliltapf
      421 gmrshfivfa laivvgfyvi tnvthslhtp lmsvtnaisg iivvgaiqqi gsssaaitvl
      481 afiamsvafi nvfggftvth rmlkmfrrs
//
LOCUS       WP_108717713             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Miniimonas
            sp. S16].
ACCESSION   WP_108717713
VERSION     WP_108717713.1
KEYWORDS    RefSeq.
SOURCE      Miniimonas sp. S16
  ORGANISM  Miniimonas sp. S16
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Beutenbergiaceae; Miniimonas.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Miniimonas sp. S16"
                     /db_xref="taxon:2171623"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53270
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigvpratv hgastvaatp ttvralralg ydvavehdag araslldpdy eaagarlvgp
       61 eeawqadvvi lvhtptlsdv arvrpgavlv smvapaqhpd lvqalaergv tslaldavpr
      121 lsraqaldvl stqsniagyr avieaaeeyg gmfsgqvtaa gktdpaavfv igagvaglaa
      181 igaasslgar vrafdvrpea geqiasmggt pvvapqaqqe iaadgyakpl tpeqqaaamd
      241 vyavetelad vvittalvrg tapttisham vaamrpgsvi vdlaasgggn cedtvpgerv
      301 vtangvsvlg etdltarmpr htsqllgtni vnllqlltpg kdgtlvldld dvvqrgmtva
      361 hagqilwppp pvqvsaapaa pagppapppp tpaevaaraa aaaeearrrg trrvvgyalg
      421 avllglaltl apvaflghmt vfalavvigf yvisnvshal htplmaqtna isgiilvgam
      481 lqlgssdwlv tglafvaaav asinifggfl vthrmigmfh kgada
//
LOCUS       WP_108726976             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Trueperella pyogenes].
ACCESSION   WP_108726976
VERSION     WP_108726976.1
KEYWORDS    RefSeq.
SOURCE      Trueperella pyogenes
  ORGANISM  Trueperella pyogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Trueperella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Trueperella pyogenes"
                     /db_xref="taxon:1661"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52840
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresg gqtlvaatpd tvgklsklgy evvvehdags aasfpdslye sagarivske
       61 eawaadivta ldapaladld lmrsgatlis rmapgrnpdi lqalssrsit glamdmvpri
      121 sraqsmdvls sqanvagyra vieaahhfgr lfsgqvtaag kvapanvyvi gagvaglaai
      181 gtansmgavv katdvrpeta eqvesmgagf vaipvaaees adgyakeigq eqaaaaekly
      241 teqaawadiv ittaaipgrr spvlltaeav agmkpgsviv dmgaanggnv vgsrpdevvv
      301 tdngviiigy selaarlpgq asqlygqnvf nffklatpdk dgvlhldldd eivrsmlvtl
      361 dervmypppp vkvsaapapv passeeptsa eakekswiak hwwkiaagav ftwliltapa
      421 gstthflvfa lavvigfyvi tsvthalhtp lmsvtnaisg iivvgalmqv sassvvvqil
      481 sfiaiavasi nifggflvte rmlkmfhrs
//
LOCUS       WP_108734407             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbulbifer sp. A4B17].
ACCESSION   WP_108734407
VERSION     WP_108734407.1
KEYWORDS    RefSeq.
SOURCE      Microbulbifer sp. A4B17
  ORGANISM  Microbulbifer sp. A4B17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Microbulbiferaceae; Microbulbifer.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Microbulbifer sp. A4B17"
                     /db_xref="taxon:359370"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54851
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miiaipreta egearvaatp dsvrrlrdlg fsvavekgag nrasftdeay aeagaeired
       61 iqqcladagi vlkvqaptdq elvlipkgat liaflkpaqn aeflqklaer dinalavesi
      121 prisraqkmd alssmaniag yravveaahn fgrfftgqit aagkippakv lvigagvagl
      181 saigtaksmg aivrafdtra evreqvesmg adfltveiee egsgsggyak emskefidae
      241 malfreqake vdivittali pgkpapklwl admvdsmpkg svvvdlaaem ggncdytvah
      301 ekvehngvti lgytnlpsra aaqssrlyst nlahllgelt pekdgeidln fddevirgat
      361 vvksgeitwp ppapkisaqp qpsakaaeev kivegkaekr ksplsifafw avaavlllwl
      421 grvappdfvs hftvfvlaif vgwqviwnvt halhtplmsv tnaisgiviv galvqlgvtg
      481 sglvsllafi gvlvasinif ggffvtyrml kmfrr
//
LOCUS       WP_108743567             391 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Salinivibrio sp. IB282].
ACCESSION   WP_108743567
VERSION     WP_108743567.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. IB282
  ORGANISM  Salinivibrio sp. IB282
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Salinivibrio sp. IB282"
                     /db_xref="taxon:1766122"
     Protein         <1..391
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          <1..390
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
       61 igaagslgai vrafdvrpev keqvesmgae flevdfkqdn sgsgdgyake msdefnqaae
      121 klyaqqaedv diivttalip gkpaptlitk emvdsmkpgs vivdlaaang gnceytekdq
      181 vittpngvkv igytdmvgrl ptqssqlyat nlvnltkllc kekdgniqid fddvvvrgvt
      241 vikegevtwp appiqvsaqp kaepkaepap kpapkktsra tkyglmaaaa gafgwianya
      301 pseflshftv fvlacvvgyy vvwnvthalh tplmsvtnai sgiiivgall qvgqgigfvt
      361 flafiavlia sinixggftv tkrmlemfrk g
//
LOCUS       WP_108781224             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pontivivens insulae].
ACCESSION   WP_108781224
VERSION     WP_108781224.1
KEYWORDS    RefSeq.
SOURCE      Pontivivens insulae
  ORGANISM  Pontivivens insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pontivivens.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Pontivivens insulae"
                     /db_xref="taxon:1639689"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55359
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalketw pgearvamtp qsiaqltklg htcvieagag eaarfddaly aeagaevlpd
       61 aaavyaaadv iskvrapema evahvrdgqt iisfiwpaqn aellealkak gattiamdmv
      121 prisraqkmd alssmanigg yravveasnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigaatsmg aityafdvrp evaeqiesmg aefvfldfde eqtdgaetgg yaapsspefr
      241 ekqlekfrel apeidivitt alipgrdapv lwtkdmveam kpgsvivdla aekggncelt
      301 vegekietan gvtivgytdl psrmatqsst lyatnirhmm ddltpekdgv inhnmeddvi
      361 rgatvthage itfpppppkt kaiaavkkek vpeptaeelr aaevaafkqq tktqvgllag
      421 gaalllligs ipgmpasfmq hfivfvlsvf igfqviwnvs hslhtplmav tnaissiiil
      481 galvqvgsss gliallaala ifmcginifg gfmvtrrmla mfqks
//
LOCUS       WP_108785640             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Falsiruegeria mediterranea].
ACCESSION   WP_108785640
VERSION     WP_108785640.1
KEYWORDS    RefSeq.
SOURCE      Falsiruegeria mediterranea
  ORGANISM  Falsiruegeria mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Falsiruegeria.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Falsiruegeria mediterranea"
                     /db_xref="taxon:1280832"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55740
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif egearvamtp asalqlqklg ydcaiesgag laagfsdaty eeagvevikt
       61 aaalwkevdi iakvrqpnet elkrlngdkt lisffnpagn eegmelaksk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvaam kpgsvivdla aekggncklt
      301 vmdekivten gvtiigytdf psrmaaqast lyatnirhmm tdltpekdgq inhnmeddvi
      361 rgatvthqge itfpppppkv aaiaaqkkpe vkeltpeekr eqevaefkaq tkqqvtllvv
      421 gavlllgvgl vapasfmqhf ivfvlavfvg fqviwnvshs lhtplmavtn aissiiilga
      481 vmqigsgsfl villaaisvf faginifggf lvtrrmlamf qks
//
LOCUS       WP_108811194             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingorhabdus sp. Alg231-15].
ACCESSION   WP_108811194
VERSION     WP_108811194.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. Alg231-15
  ORGANISM  Sphingorhabdus sp. Alg231-15
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sphingorhabdus sp. Alg231-15"
                     /db_xref="taxon:1922222"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39259
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkela dgeqrvsasp etvkkftalg atmaveegag lsasiadady eaqgasigtr
       61 aavlkdadiv lgvqgpepks lkgmrkgawl vaslnpfger arvdeyaalg idalamefmp
      121 ritraqsmdi lssqsnlsgy kavieagshy grafpmmmta agtvsaakcf vmgvgvaglq
      181 aiatarrlga qvsatdvraa tkeqiqslga kpifvedvag iegegtggya temseeyqka
      241 qaelvskhia kqdivittal ipgrpaprli sdaqiatmra gsvivdlaae qggnvegava
      301 gkvvekhgvk iygannmpst laadssalfa rnlynflsay wdeeakrpvl pdddevtigi
      361 rltkdgkvvn erllas
//
LOCUS       WP_108816065             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Loktanella
            sp. Alg231-35].
ACCESSION   WP_108816065
VERSION     WP_108816065.1
KEYWORDS    RefSeq.
SOURCE      Loktanella sp. Alg231-35
  ORGANISM  Loktanella sp. Alg231-35
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Loktanella sp. Alg231-35"
                     /db_xref="taxon:1922220"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55496
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpneif egedrvamtp asakdlqklg ydcvietgag vsagfsdqsy kdagvevvkt
       61 aaalykaadi vvkvrppeda eikrlsegqt lisffypaqn eklmeaankk gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqvesmg aefvfldfee eqqdgsatgg yaavsspefa
      241 aaqlakfrei apemdivitt alipgrdape lwtkdmvesm kpgsviidla aerggncklt
      301 vkdekivtdn gvtivgytdf psrmaaqsst lyatnirhmm tdltpdkdgt pnhnmeddvi
      361 rgatathage itfpppppkv aaiaaapkke apkeltaeek raaevaafqn etktqvglla
      421 agaalilgig lipgmpasfm qhfivfvlsv figfqviwnv ahslhtplma vtnaissiii
      481 lgaliqigst stlitilaal gifmaavnif ggflvtrrml amfqks
//
LOCUS       WP_108819494             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudovibrio sp. Alg231-02].
ACCESSION   WP_108819494
VERSION     WP_108819494.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio sp. Alg231-02
  ORGANISM  Pseudovibrio sp. Alg231-02
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Pseudovibrio sp. Alg231-02"
                     /db_xref="taxon:1922223"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55557
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigaakevl dgerrvaltp dsaqqlqklg yecaiesgag eaanfsdtdy kdagvkviad
       61 aktlwetadi vikvrppeas elelthegqt lisffwpaqn gellqqfadk kvnvlamdmv
      121 prisraqkmd alssmaniag yravmeagnn fprfftgqit aagkvppakv lvigagvagl
      181 aaigastslg aitlafdvrp evaeqvesmg aefvyldfee eqqdgastgg yasvsspefr
      241 eaqlakfrel apdvdivitt alipgrdape lwtedmvqsm kpgsvivdla aekggncklt
      301 kmdekivten gvtvigytdf psrmatqsst lyatnirhmm fdltpekdgq aninmeddvi
      361 rgatatkdge itfpppkpki aaiaaqkpka pektpeelal eeaaaakaag rkqlglligg
      421 gavmaligay apesfmqhfi vfvlavfvgf qviwgvahsl htplmavtna isgiiilgav
      481 lqlgsgswiv wflagisvli asvnivggfm vtrrmlqmfn ks
//
LOCUS       WP_108832450             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces sp. Marseille-P3109].
ACCESSION   WP_108832450
VERSION     WP_108832450.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. Marseille-P3109
  ORGANISM  Actinomyces sp. Marseille-P3109
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Actinomyces sp. Marseille-P3109"
                     /db_xref="taxon:2083009"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53412
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvprepv dqpraaaspq tvermirlgy evlvergaga raqfhddayq aagaqpagga
       61 qvwgcevvvs asspaeeqla lmsrgavlic rldptrrpel lealrergit claldvvpri
      121 sraqsldvls sqanlagyra vieaashfgr lfsgqvtaag kfppatvyvi gagvaglsai
      181 gtayslgaqv rgsdvrpeva dqvrsmgaqf vplpnaqevs sdgyakemsa dqaaaantly
      241 arqaaesdiv ittasipgrr apvlldrasi eamrpgsvii dmaaatggnt eltlpgevvt
      301 tdsgvtivgh tdlagllpsq asqlygrniv nlldlltpak dgtltldldd evvraitvth
      361 dgellwpppp iqvsaapapg rpaesttdda aaqeaaraaq arsrsrqwlg laaaslvaaa
      421 lvlvtppaat shyivlmlsv ilgfhvisnv tpalhtplms vtnaisgiil vgaisqvghp
      481 hpvisaisla avvlatiniv ggfavthrml amftkd
//
LOCUS       WP_108828826             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ascidiaceihabitans donghaensis].
ACCESSION   WP_108828826
VERSION     WP_108828826.1
KEYWORDS    RefSeq.
SOURCE      Ascidiaceihabitans donghaensis
  ORGANISM  Ascidiaceihabitans donghaensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Ascidiaceihabitans.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Ascidiaceihabitans donghaensis"
                     /db_xref="taxon:1510460"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55328
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egearvamtp dsalqlqklg hecvvetgag alagfddasy kdagvevvkt
       61 aaalwkaadv vakvrapdat evkrlrdgqt lisfinpaan eklldqaakk gstviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aavgtstslg aityafdvrp evaeqiesmg aefvfldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrem apeidivitt alipnreape lwtedmvaam kpgsvivdla aekggncklt
      301 vmdekivtdn gvtiigytdf psrmatqast lystnirhmm tdltpekdgv inhdmeddvi
      361 rgatvtheka vtfpppppki aaiaaqpkkd apkeltaeek raaetaafka qtknqvtlla
      421 vggiallavg lvapasfmqh fivfvlsvfi gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgsg lvillaalsv fmtginifgg flvtrrmlam fqks
//
LOCUS       WP_108841759             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Kushneria
            phyllosphaerae].
ACCESSION   WP_108841759
VERSION     WP_108841759.1
KEYWORDS    RefSeq.
SOURCE      Kushneria phyllosphaerae
  ORGANISM  Kushneria phyllosphaerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Kushneria.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Kushneria phyllosphaerae"
                     /db_xref="taxon:2100822"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55484
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkesa rgearvaltp esatqiqklg haclvetgag vaagfddqay rdagvtives
       61 aqalfddadi vikvrepseq eaerlrkgqt liaffwpaqn eamlekcrar gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfdn aqdgsesggy aspsspefre
      241 kqlecfraqa sdvdivitta lipgrpapkl wledmvaamk pgsvvidlaa ekggncdltr
      301 adervvsdng vvvvgytdyp srmatqssll yatnirhmlt dltpdkdgvi qhnmeddvir
      361 gatvthqgev tfpppppktk aigaakpkak ekeptaeekr alesaqfksq tkrqvgmlai
      421 ggalmlllge vapasfmqhf ivfvlscfig fqviwkvshs lhtplmavtn aisgiiilga
      481 vlqigsgsvi vgilasisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_108837523             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tateyamaria sp. Alg231-49].
ACCESSION   WP_108837523
VERSION     WP_108837523.1
KEYWORDS    RefSeq.
SOURCE      Tateyamaria sp. Alg231-49
  ORGANISM  Tateyamaria sp. Alg231-49
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Tateyamaria.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Tateyamaria sp. Alg231-49"
                     /db_xref="taxon:1922219"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55549
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif agehrvamtp esalalqklg htcvieagag aaagfadkay keagvevvkt
       61 aaalwkaadv vakvrvpdda emkrlradqt lisffspvad edkmqaaakk gatvvamemi
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqtdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnrdape lwtedmvkam kpgsvivdla aekggncklt
      301 vmdekivtan gvtiigytdf psrmatqass lyatnirhlm tdltpekdge inhnmeddvi
      361 rgatiahgke vtfpppppkv aaiaaapkke pakeltaeek raaedaafkq qtrnqvtllg
      421 vgaalvlgvg lipgmpasfm qhfivfvlsv figfqviwnv ahslhtplma vtnaissiii
      481 lgaliqvgss sllitllgal gifmasvnif ggflvtrrml amfqks
//
LOCUS       WP_108846137             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Dietzia
            lutea].
ACCESSION   WP_108846137
VERSION     WP_108846137.1
KEYWORDS    RefSeq.
SOURCE      Dietzia lutea
  ORGANISM  Dietzia lutea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Dietzia lutea"
                     /db_xref="taxon:546160"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54394
     Region          17..531
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtpetdlrdt adapsvigvv aesnpaenrv aatpetvakl iglgyrvvve rgagtraefa
       61 daayaeagge lvdgdsawsa dvvmkvavpt esevarvrsg atlvsllapa qnehlltvla
      121 ergvtalamd avprisraqs mdvlssmani agyravieaa hhfgrfftgq vtaagkvppa
      181 kvlvagagva glaaigaass lgaivratdp rpevadqvas iggeylpvev pdeekevssd
      241 gyakatseay draaaelyta qaaevdiiit talipgrkap rlitaadiaa mkrgsvivdm
      301 aaaqggnveg svpdevvvtd ngvtiigytd lagrlpaqas qlygtnlvnl tklvtpekdg
      361 lwsldmddvv qrgvtvtkgg eimwppppvq vsaapaapaa aapaaavpae paeekkklsp
      421 vaklgmiavg mallllltaa apgdiarhit vfvlaivigy yvignvhhal htplmsvtna
      481 isgvivvgal lqigidntlg lvlavvailv asinvfggfa vtrrmlamfs kga
//
LOCUS       WP_108856529             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aliiroseovarius pelagivivens].
ACCESSION   WP_108856529
VERSION     WP_108856529.1
KEYWORDS    RefSeq.
SOURCE      Aliiroseovarius pelagivivens
  ORGANISM  Aliiroseovarius pelagivivens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Aliiroseovarius.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Aliiroseovarius pelagivivens"
                     /db_xref="taxon:1639690"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55551
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkevf egenrvamtp esakmlqklg ydcvietkag aaagfsdavy keagvevvkt
       61 aaalwkaadi iakvrqpndt elkrlsadkt lisffnpggn edgmekakks ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yaavsspefr
      241 eaqlakfrel apevdivitt alipnreapk lwlkdmidam kpgsvivdla aekggnaegt
      301 vmdekvvten gvtiigytdf psrmaaqsss lyannirhmm tdltpekdgv vnhdmeddvi
      361 rgatvthqge itfpppppkv qaiaakpkev vpeltpeekr aaevaafkaq tkqqvtllav
      421 ggglmllagl ftpasfmqhf ivfvlavfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaaasvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_108852890             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Albidovulum aquaemixtae].
ACCESSION   WP_108852890
VERSION     WP_108852890.1
KEYWORDS    RefSeq.
SOURCE      Albidovulum aquaemixtae
  ORGANISM  Albidovulum aquaemixtae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Albidovulum.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Albidovulum aquaemixtae"
                     /db_xref="taxon:1542388"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55746
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspkevf egearvamtp dsavqlkklg hvcfieagag saagfadaay eaagvtvvkt
       61 aaalfkevdv vakvrppsea evkrltkgqt lisffypaqn ekllelakkq gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvyldfee qtqdgaatgg yaapsspefr
      241 eaqlkkfrel apemdivitt alipgrdapv lwtkdmveam kpgsvivdla aerggncelt
      301 kpdekilsdn gvtivgytdf psrmaaqsst lyannirhml fdltpakdgv inhnmeddvv
      361 rgatvahage itfpppppkv qaiaaqkpke kareltveek kaqeialfrq qtkkqvtmla
      421 aggallllvg ayspasfmqh fivfvlavfv gfqviwnvsh slhtplmait naissiiilg
      481 almqmgsgsf lvillaalsi fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_108862203             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ruegeria
            sp. Alg231-54].
ACCESSION   WP_108862203
VERSION     WP_108862203.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria sp. Alg231-54
  ORGANISM  Ruegeria sp. Alg231-54
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Ruegeria sp. Alg231-54"
                     /db_xref="taxon:1922221"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55571
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtprenf dgenrvamtp esalqlqklg yecliekgag aaagfsdasy eaagvevvkt
       61 aaslwkqadi vakvrqpnea elkrltkgkt lisffnpagn eggmeaakak ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfse dqqdgaatgg yasvqseefr
      241 eaqlakfrel apeidivitt alipnreape lwtkdmveam kpgsvivdla aekggncklt
      301 vadekivtdn gvtiigytdf psrmaaqsss lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgatvtfegd itfpppppkv qaiaaqkkpe vkeltpeekk aqevaafkaq tkqqftllgv
      421 ggalmllvgl iapasfmqhf ivfvlaifvg fqviwgvahs lhtplmaitn aissiiivga
      481 vmqigsgsil villaalsif maginifggf lvtrrmlamf qks
//
LOCUS       WP_108880943             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Anderseniella sp. Alg231-50].
ACCESSION   WP_108880943
VERSION     WP_108880943.1
KEYWORDS    RefSeq.
SOURCE      Anderseniella sp. Alg231-50
  ORGANISM  Anderseniella sp. Alg231-50
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Parvibaculaceae; Anderseniella.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Anderseniella sp. Alg231-50"
                     /db_xref="taxon:1922226"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38902
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavpseta agesrvavsp davkayvkkg ltvcveqgag agsfmsddaf kaagakiakg
       61 aavlkdadiv lavrrlpdas lkslkkgaiv aaqldpygdr knldamakqg vsafsmelvp
      121 ritraqsmdv lssqanlagy kavidaaehf srafpmmmta agtvpaarvf vmgagvaglq
      181 aiatarrlga vvsatdvraa ageqvaslga kfvfvegmad aateggyake lsaedkkkqa
      241 elvadhikgq divittalip grpapvlvtk qmvesmkags iivdmaverg gncplskpgq
      301 ivdhkgvaim ghenlpgkla gnastlyakn lqnfvdlmvs pegemkldwe deiitgcglm
      361 rdgeivhavl tekkgn
//
LOCUS       WP_108886432             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudoprimorskyibacter insulae].
ACCESSION   WP_108886432
VERSION     WP_108886432.1
KEYWORDS    RefSeq.
SOURCE      Pseudoprimorskyibacter insulae
  ORGANISM  Pseudoprimorskyibacter insulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudoprimorskyibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Pseudoprimorskyibacter insulae"
                     /db_xref="taxon:1695997"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55718
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeaf egearvamtp dsarqlqklg yacaiesgag vaagfsdaly eeagveiikt
       61 aaalwkdvdi iakvrqpnet elkrlnkdkt lisffnpggn eeglelakak ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlkkfrel apeidivitt alipnreapk lwladmiaam kpgsvivdla aekggnaegt
      301 vkdekivten gvtiigytdf psrmaaqssq lyatnirhmm tdltpekdgq ivhnmeddvi
      361 rgatvthqge itfpppppkv qaiaaqkkek pkeltpeekr aketaafkaq tkqqvtllav
      421 ggalllavgl vapasfmqhf ivfvlsvfig fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaglsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_108894138             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Palleronia
            abyssalis].
ACCESSION   WP_108894138
VERSION     WP_108894138.1
KEYWORDS    RefSeq.
SOURCE      Palleronia abyssalis
  ORGANISM  Palleronia abyssalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Palleronia.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Palleronia abyssalis"
                     /db_xref="taxon:1501240"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55805
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgvvkesq etearvaltp asaeqirklg hecvveagag aradisdaay rdagvevlds
       61 aqavfdaadv igkvrpptea evdrlregqt lisffypaen eellkkaadk gatliamdmv
      121 prisraqkmd alssmaniag yraviesann fgrfltgqit aagkvppaki lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqvesmg aefvyldfeg dtgsgeggya apsspefrea
      241 qlakfrelap didivittal ipnreapelw tedmvkamkp gsvivdlaae kggnckltvk
      301 ddrivtdngv viigytdfps rmakqsstly atnirhmltd ltpekdgtvn hnmdddvirg
      361 atithkndvt wpppkpkqaa qaapqkrekp kektpeekra eekaaftrqt rsqvmllaig
      421 avlmllvgay apesfmshfi vfalacfvgf qviwgvahsl htplmavtna isgiiilgal
      481 lqigagnwlv vilsfigvli asinivggfl vtrrmlsmfv ks
//
LOCUS       WP_108902092             453 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Limnobaculum parvum].
ACCESSION   WP_108902092
VERSION     WP_108902092.1
KEYWORDS    RefSeq.
SOURCE      Limnobaculum parvum
  ORGANISM  Limnobaculum parvum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Budviciaceae; Limnobaculum.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Limnobaculum parvum"
                     /db_xref="taxon:2172103"
     gene            1..453
                     /gene="nrfA"
     Protein         1..453
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=50815
     Region          12..450
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mgntalankp nvearnevfa kdhadqydsw ratselnklg ggldeypdmv ilwagypfak
       61 dykkarghfy aitdvreslr taapmkdtdg plpmacwsck spdvarlide ggedkyfegm
      121 wsrggaqivn pigcadchdt askdfaegkp alymsrpyta raleaigkpf dkashldqqa
      181 mvcsnchvey hfdgknkavk fpwdkgitve kmeeyydnia fsdwthllsk tpmlkaqhpe
      241 yetwsqgihg knnvtcidch mpkvqnaegk lytdhkignp fdrfnetcas chtqtkeqlq
      301 divasrkeav relkkkteaq lvhahfeaka awdagateee mkpilmdirh aqwrwdyaia
      361 shgihmhape vglkilgtal dkaadartkl arllatkgit heialpdlst kanaqkalgm
      421 dmqklesdkq eflktrvaew danakkeerl lsk
//
LOCUS       WP_108916245             169 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: aromatic/alkene monooxygenase hydroxylase subunit
            gamma [Methylosinus].
ACCESSION   WP_108916245
VERSION     WP_108916245.1
KEYWORDS    RefSeq.
SOURCE      Methylosinus
  ORGANISM  Methylosinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Rosenzweig,A.C., Frederick,C.A., Lippard,S.J. and Nordlund,P.
  TITLE     Crystal structure of a bacterial non-haem iron hydroxylase that
            catalyses the biological oxidation of methane
  JOURNAL   Nature 366 (6455), 537-543 (1993)
   PUBMED   8255292
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Cardy,D.L., Laidler,V., Salmond,G.P. and Murrell,J.C.
  TITLE     Molecular analysis of the methane monooxygenase (MMO) gene cluster
            of Methylosinus trichosporium OB3b
  JOURNAL   Mol Microbiol 5 (2), 335-342 (1991)
   PUBMED   1904125
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Fox,B.G., Liu,Y., Dege,J.E. and Lipscomb,J.D.
  TITLE     Complex formation between the protein components of methane
            monooxygenase from Methylosinus trichosporium OB3b. Identification
            of sites of component interaction
  JOURNAL   J Biol Chem 266 (1), 540-550 (1991)
   PUBMED   1845980
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Stainthorpe,A.C., Murrell,J.C., Salmond,G.P., Dalton,H. and Lees,V.
  TITLE     Molecular analysis of methane monooxygenase from Methylococcus
            capsulatus (Bath)
  JOURNAL   Arch Microbiol 152 (2), 154-159 (1989)
   PUBMED   2505721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF045805.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Methylosinus"
                     /db_xref="taxon:425"
     gene            1..169
                     /gene="mmoZ"
     Protein         1..169
                     /product="aromatic/alkene monooxygenase hydroxylase
                     subunit gamma"
                     /EC_number="1.14.13.25"
                     /GO_function="GO:0015049 - methane monooxygenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=19218
     Region          7..167
                     /region_name="MeMO_Hyd_G"
                     /note="Methane monooxygenase, hydrolase gamma chain;
                     pfam02964"
                     /db_xref="CDD:427082"
ORIGIN      
        1 makrepihen strtewegki aklnsvdqat kfiqdfrvay sspfrksydl dvdyqyierk
       61 ieerlsvlkt eklsvadlvt kattgedaaa veaawiakmk aaeskyaaer ihiefrqlyk
      121 ppvlpvnvfl rtdaalgtil melrntdyya tpleglrker gvkvlhlqa
//
LOCUS       WP_108917360             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylosinus sporium].
ACCESSION   WP_108917360
VERSION     WP_108917360.1
KEYWORDS    RefSeq.
SOURCE      Methylosinus sporium
  ORGANISM  Methylosinus sporium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae; Methylosinus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Methylosinus sporium"
                     /db_xref="taxon:428"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38700
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavqaetd knetrvaatp etvkkfknlg aevvvqsgag aisgfsdady aaagaaiaps
       61 aaaasdnaev vlrvrrpapg elsgiargaa ivaiadpfkh ekelaalaqt gatlfamefm
      121 pritraqvmd vlssqaniag yravidaaae ysraipmmmt aagtvpaaki fimgvgvagl
      181 qaiatarrlg givsatdvrp atkeqveslg akfiavende frqaetsggy akemspeyqa
      241 aqaelvaahi akqdivvtta lipgrpapvl isaaaarsmr agsviidlaa erggnceltk
      301 pgetivdngv kivgavnlag rlpatasgly aknllafvet lisketktla idwndelvka
      361 taltrdgavi dsrfaa
//
LOCUS       WP_108919412             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_108919412
VERSION     WP_108919412.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53529
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa daltklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_108919977             363 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium montefiorense].
ACCESSION   WP_108919977
VERSION     WP_108919977.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium montefiorense
  ORGANISM  Mycobacterium montefiorense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            simiae complex.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Mycobacterium montefiorense"
                     /db_xref="taxon:154654"
     Protein         1..363
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37888
     Region          4..354
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,71,90,283,309,311)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,273..274,316..317,321,
                     324..325)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,223,234,
                     251..253,260,262)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msaigvprei aagesrvalv pgvverlraa ghhlvvetga gegalirded ylragavigd
       61 pwsadvvvkv npptemeigr lkqgahligf laprtrpevs dqlrragvtg fameavpris
      121 raqtmdalss qanvagykav lcaaqcstrf fpmmttaagt vkpatvlvlg vgvaglqala
      181 takrlgartt gfdvrpevae qvrslgakwl elgvsaageg gyaraltpee qieqqqrlte
      241 aipgfdavit talvpgraap klvtaqavrr mrsgsvvvdl ageaggncel tvpgetvlrh
      301 dvtiaaplnl pasmpehase lyarnigall ehmldgtavr dlsdeildac cvtksdnelt
      361 gir
//
LOCUS       WP_108922024             364 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium montefiorense].
ACCESSION   WP_108922024
VERSION     WP_108922024.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium montefiorense
  ORGANISM  Mycobacterium montefiorense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            simiae complex.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Mycobacterium montefiorense"
                     /db_xref="taxon:154654"
     Protein         1..364
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37214
     Region          7..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdaqttvgv vaesgtderr valvpkavgs lvgtgvavvv eagagarall pdelyteaga
       61 tigdawaadv vvkvapptda evgklhsgqt ligflaprna ensigalkaa gvqafaleai
      121 prisraqamd alssqgnvsg ykavllaase strffpmltt aagtvkpatv lvlgvgvagl
      181 qalatakrlg grttgydvrp evadqvrsvg aqwldvgida sgeggyarel tdderaqqqq
      241 alekaisgfd vvittalvpg rpaprlvtaa avqamkpgsv vvdlagetgg nceltepgqt
      301 vvrhdvtias plnlpatmpe haselyskni talldllitd gklapdfdde viadscvtrd
      361 reds
//
LOCUS       WP_108923467             501 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Actinobacillus porcitonsillarum].
ACCESSION   WP_108923467
VERSION     WP_108923467.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus porcitonsillarum
  ORGANISM  Actinobacillus porcitonsillarum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Actinobacillus porcitonsillarum"
                     /db_xref="taxon:189834"
     gene            1..501
                     /gene="nrfA"
     Protein         1..501
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56015
     Region          1..487
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkrltkslam atiamlgcls ssawaeekaa esltdkalkh eklgvevesa nhkfaekypl
       61 qynswkatse stdrgsalal dpryvvlwag yafskeynkp rghyysitdv rdilrtgapk
      121 dendgpqpma cwtckgpdva rlieekgerg yfdpkwakyg aeivnsigca dchdtkskdf
      181 qegkpalria rphvlralet vgwkfedldk hgkraavcan chveyyfkdk kdvtfpwdkg
      241 vdvdsiekyy deiqftdwth klsrapmlka qhpdfevwaq gvhgkngvtc idchmpkvkd
      301 kdgkvytdhk ignpfdqfda tcktcheqsk etlqkrvaeh kkqvkdamik ledqlvkahf
      361 eakaawdnga teeemkdilt airhaqwrwd ysaaghgshi hapdvtlhvi atgidraada
      421 raklgvvlak hgvttpvaip distrekaqq aigldipkeq aakdeflktv vpqweaqare
      481 kgllpakeep kavaapkaea k
//
LOCUS       WP_108929310             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            johnsonii].
ACCESSION   WP_108929310
VERSION     WP_108929310.1
KEYWORDS    RefSeq.
SOURCE      Leptospira johnsonii
  ORGANISM  Leptospira johnsonii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira johnsonii"
                     /db_xref="taxon:1917820"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40974
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvlkeak eetrvavtpd vvdalkkiga sviiekgage gsyfsdedyk kagasiqsra
       61 dilkksdlvv sihladgasl skikkgafyl gmfqpavnpq vikklssgkv tvlsldaiar
      121 itraqsmdvl ssqatvagyk avllasthlt rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvqslgak fvevegashs aaaggyaveq teeykkrqqe
      241 aiekfaakad viittalipg rkapiiitkk ivdrmkagsv vvdlaspngg nceytqhgkv
      301 vltkngvsvi ghqnlagslp sdaskmfakn vlnylkllvk ekkinldlsd eilssttith
      361 dgeirhkltl dalggskqdg kkpaakkka
//
LOCUS       WP_108930888             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Agromyces
            badenianii].
ACCESSION   WP_108930888
VERSION     WP_108930888.1
KEYWORDS    RefSeq.
SOURCE      Agromyces badenianii
  ORGANISM  Agromyces badenianii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Agromyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Agromyces badenianii"
                     /db_xref="taxon:2080742"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52806
     Region          3..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigviaeq spetrvaatp atvkqlialg hevavqagag aasafpdday reagaeivdg
       61 atalasdlvl kvnapteaei aqltpgatli gllapafkpe llealaargv talamdavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksigge ylkveveveq stdgyakats eaydrraaei
      241 yseqaadvdi vittalipgr aaprlitaad vasmksgsvi vdmaagmggn vegsvageri
      301 vtpngvvilg ytdlasrlpt qasqlygtnv vnliklltpg kdgvlaldfd dvvqrsvtva
      361 kdgavtwppp pvqvsaaava aasapgagga khaaaapekk rpmspakkaa lvavgiaalf
      421 avnavapppl pqhftvlvla vvvgfyvigk vahalhtplm svtnaisgii vvgamvqits
      481 dvlvvqilaa vavllasini fggfavtrrm lamfsagktg adra
//
LOCUS       WP_108957262             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces fragilis].
ACCESSION   WP_108957262
VERSION     WP_108957262.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces fragilis
  ORGANISM  Streptomyces fragilis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces fragilis"
                     /db_xref="taxon:67301"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53192
     Region          13..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msaqepthnp pqrigvvaes apgetrvaat patvrqllkl gyevvvepga gelsgftdqa
       61 yaeagagtge awdadvvlkv napseaeiar lragatlvgl lapaqkpell rtlsdagvta
      121 laldavpris raqsmdvlss maniagyrav veaahtfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvkslggeyl pvhveqeast dgyakatsad
      241 ydraaaelyh qqaadvdivi ttalipgrpa prlltaedva vmkpgsvvvd maaaqggnve
      301 gtvpgrtvvt gngvtligyt dlasrlpaqa sqlfgtnlln lvklltpgkd grlaidfddv
      361 vqravtvvrd gdvtwppppv avsaapaaqp esapaeaapk kprttpavrf gliglgllam
      421 fllvafapaq laqnftvftl avvigyyvig kvhhalhtpl msvtnaisgi ivvgallqlg
      481 hesrivtvls ftailltsin vfggfavtrr mlsmfskg
//
LOCUS       WP_108960552             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            ellinghausenii].
ACCESSION   WP_108960552
VERSION     WP_108960552.1
KEYWORDS    RefSeq.
SOURCE      Leptospira ellinghausenii
  ORGANISM  Leptospira ellinghausenii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Leptospira ellinghausenii"
                     /db_xref="taxon:1917822"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40340
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikeps yenrvaitpd lidplkklgf svaietsagd saffsdqdyk dvgatvesrd
       61 silsgsdivi sihaldevsa kkigkdkmyi atlsplafpk kvkeiaaasf kifsmdtipr
      121 itraqsmdvl ssqatvsgyk avllaasnys rffpmlttaa gtitparvli lgagvaglqa
      181 iatsrrlgav vdvfdtrpev keqcmslgak fvevegaada sntggyaveq sedyqrrqke
      241 aiakfaekad iiittalipg krapllitke mvdkmrqgsv ivdlaavngg nceltendkt
      301 ivykgitiig nsnlqstqpm daskmyakni vnflklfvnk ekqfninled eiinacmiae
      361 ngsirhkptl allge
//
LOCUS       WP_108965761             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Alloyangia
            pacifica].
ACCESSION   WP_108965761
VERSION     WP_108965761.1
KEYWORDS    RefSeq.
SOURCE      Alloyangia pacifica
  ORGANISM  Alloyangia pacifica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Alloyangia.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Alloyangia pacifica"
                     /db_xref="taxon:311180"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55686
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpteif egearvamtp dsalqlqklg ydcliqsgag akagfadaay eaagvtvvqd
       61 aaalwaqadi vakvrppsee evahltpekl lisffypasn ealmkqaadv gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqadgsasgg yasvsspefr
      241 eaqlakfrel apemdivitt alipnreape lwtedmvkam kpgsvivdla aerggncklt
      301 vmdekivtdn gvtiigytdf psrmatqsst lyatnirhmm sdltpgktdg tvvhnmeddv
      361 irgatiahgk dvtfpppppk tkaiaaqkpk ekapeltpeq kraqevaafk aqtkqqvtll
      421 tigavlllav glvapasfmq hfivfvlsvf vgfqviwnvs hslhtplmav tnaissiiil
      481 galmqigsgn wlviilaals vfmaginifg gflvtrrmla mfqks
//
LOCUS       WP_108966245             518 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Actinomyces].
ACCESSION   WP_108966245
VERSION     WP_108966245.1
KEYWORDS    RefSeq.
SOURCE      unclassified Actinomyces
  ORGANISM  unclassified Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="unclassified Actinomyces"
                     /db_xref="taxon:2609248"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53169
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgipcqpp drsmtaatpq tveqlirlgy dvvvqrgaga paqfpdaaye eagaqladra
       61 etwgcnvvvt ayapddaeld lmhpgatlig rldparhpel vqslqdhslt alaidtvpri
      121 sraqsmdvls sqanlagyra vieaaahfgr llngqvtaag kfppasvyvi gagvaglaai
      181 gtayslgavv kgtdvrpeva dqvksvgaef vpvptaqevs adgyakemst dqaalanaly
      241 aeqsaaadiv ittanipgrr apllldraai damqpgsviv dmaaanggnt eltvpgevvt
      301 tdsgvtivay tdlaerlpaq asqlygrnil nlltlvtpak dgdltldldd qvvraitvcq
      361 agellwpppp vavsaapkap aaptpepapd asgdaeaqaa ararsrrrms iglalaavav
      421 avlvlvtpaa atshyivlal avilgfhvis nvtpalhtpl msvtnaisgi illgaisqvg
      481 nanpaisava fiaillasin vfggfavtnr mlamfrke
//
LOCUS       WP_108977868             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            ryugenii].
ACCESSION   WP_108977868
VERSION     WP_108977868.1
KEYWORDS    RefSeq.
SOURCE      Leptospira ryugenii
  ORGANISM  Leptospira ryugenii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Leptospira ryugenii"
                     /db_xref="taxon:1917863"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40114
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigalkeps fenrvsltpd vidalqklgf sisiesgagn qaffsdsdyq qagakvlpks
       61 ellgdsdilv sihqtdadtf skiaksklyi gtfsplaqpt kfkemanfgm kvfsmdmipr
      121 itraqsmdvl ssqatvsgyk avllaaanys rffpmlttaa gtitparali lgagvaglqa
      181 iatarrlgav vdvfdtrpev reqcmslgak fvevegaada sgsggyaveq sedyqrrqke
      241 aiakyaekad iivttalipg kkapvlitke mvesmrkgsv ivdlaavmgg nceltqndat
      301 ilhngvtiig nsnlpstqpm daskmyakni vnflklfvnk ekqfninled eiintcliad
      361 qgeirhkail sllt
//
LOCUS       WP_108986120             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Phycosocius bacilliformis].
ACCESSION   WP_108986120
VERSION     WP_108986120.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Phycosocius bacilliformis
  ORGANISM  Candidatus Phycosocius bacilliformis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacterales incertae sedis; Candidatus
            Phycosocius.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Candidatus Phycosocius bacilliformis"
                     /db_xref="taxon:1445552"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38745
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriailketr dgetrvaasp etikkisaag hqvvietgag agaaspdhmf veagaeiaad
       61 aksalkgael vlkvrrptea elklvpkgag vvafwtpygd kalieaaaka gvvalsmeft
      121 pritraqamd alssqanlag yraviegaal ygrgfpmmmt aagtvaaakc fvmgagvagl
      181 qaiatarrlg aivtatdvrp aakeqvaslg akfiavedee fkaaetaagy akpmsaeyqa
      241 kqaalvadhi akqdvvitta lipgrpapvl vtpemvakmk pgsvivdlav eqggncplsk
      301 pdqlvvtdng vtiagfanlp grlaadasal yaknllnllp lltdgdgkaf gphydddiiq
      361 gmlltrdgav vhpsltta
//
LOCUS       WP_108989836             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces coelicoflavus].
ACCESSION   WP_108989836
VERSION     WP_108989836.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces coelicoflavus
  ORGANISM  Streptomyces coelicoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Streptomyces coelicoflavus"
                     /db_xref="taxon:285562"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53082
     Region          13..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtghqaahqp pqrvgvvaes lpgetrvaat pstvrlllgl gyevvvepga gaasgfgdea
       61 yseagasvgg awaadvvlkv naptdeeiae lragttlval vapaqrpell ealaargvtv
      121 laldavpris raqsmdvlss maniagyrav ieaahafgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvrslggeyl avnvvqeesa dgyaratsad
      241 ydraaaalyh eqardvdvvv ttalipgrpa prlltaddva amrpgsvvvd maaaqggnve
      301 gtvagrsvvt dngvtligyt dlasrlpaqa sqlfgtnlvn llrlltpged grilidfddv
      361 vqrtvtvvra gtvtwppppv pvsaappata paappaagvs akprltpagr svliglgmaa
      421 vfllvafapa qlaenftvfa lavvigyyvi gkvhhslhtp lmsvtnaisg ivvigallqi
      481 ghenalvtal sfvailltsv nifggfavtr rmlsmfsrgg sr
//
LOCUS       WP_109009003             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nostoc
            commune].
ACCESSION   WP_109009003
VERSION     WP_109009003.1
KEYWORDS    RefSeq.
SOURCE      Nostoc commune
  ORGANISM  Nostoc commune
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Nostoc commune"
                     /db_xref="taxon:1178"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41461
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dtvarlvkqg levwveagag ersffgdsdy eavgatiisd
       61 taklwgetdi llkvsppqer edgrseidll kegavlvsfl nplgnpvvaq qlanrkvtal
      121 smemiprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkldeetvaa ggyakeisea
      241 skqrtqevva ehiknsdvvi ttaqvpgrqa prlvteemva qmkpgsvivd laaeqggnca
      301 ctepgkdivw ngvtiigpin lpssmpihas qlyaknvtsl mqllikdkal qvdfsddivd
      361 aacvthagei rnqrvrdalq alntqqpavn
//
LOCUS       WP_109021489             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            kobayashii].
ACCESSION   WP_109021489
VERSION     WP_109021489.1
KEYWORDS    RefSeq.
SOURCE      Leptospira kobayashii
  ORGANISM  Leptospira kobayashii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Leptospira kobayashii"
                     /db_xref="taxon:1917830"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40201
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigalqeps fenrvsitpd vidalqklgf tvqveskage kayysdadye kagakilsrn
       61 eilkdsdlvi sihpidpdsa kqipkdkiyi gtlsplafpq ktkelasfga kifsmdtipr
      121 itraqsmdvl ssqatvsgyk avllaaanys rffpmlttaa gtitparvli lgagvaglqa
      181 iatsrrlgav vdvfdtrpev keqcmslgak fvevegaada sksggyaveq tedyknkqke
      241 aiakfaekad iiittalipg kkapvlitke mvnsmrkgsv ivdlaaingg nceytendkt
      301 viqngvkiig dsnlpssqpm daskmyakni vnflkifvnk ekqfsinked eiidacliae
      361 sgnirhkgil sllg
//
LOCUS       WP_109032372             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces rubrogriseus].
ACCESSION   WP_109032372
VERSION     WP_109032372.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces rubrogriseus
  ORGANISM  Streptomyces rubrogriseus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            violaceoruber group.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces rubrogriseus"
                     /db_xref="taxon:194673"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53475
     Region          13..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtghqpahrp prrvgvvaes lpgetrvaat pstvrlllgl gyevvvesga gaasgfgdea
       61 yaeagasvge awaadvvlkv naptadetaa lregttlval lapaqrpell ealsargvta
      121 laldavprms raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaavg aasslgaivr atdprpevad qvrslggeyl avdvaqeesa dgyakatsad
      241 ydraaarlyh eqardvdvvi ttalipgrpa prlltaadva amrpgsvvvd maaaqggnve
      301 gtvagrtvvt gngvtligyt dlaarlpaqa sqlfgtnlvn llrlltpgkd grividfddv
      361 vqrtvtvvra gtvtwppppv avsaappata ppaaapaapv ggrprrltpa grfgliglgm
      421 latfllvafa paqlaqnftv falavvigyy vigkvhhslh tplmsvtnai sgivvigalv
      481 qighestlvt vlsfvaillt svnifggfav trrmlsmfsr gesr
//
LOCUS       WP_109037996             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aquabacterium olei].
ACCESSION   WP_109037996
VERSION     WP_109037996.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium olei
  ORGANISM  Aquabacterium olei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Aquabacterium olei"
                     /db_xref="taxon:1296669"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38658
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpletl agetrvavtp etvkklkaqg htlkvqsgag vaasvtdday vaagaeitda
       61 agalgadmvl kvrspsaeer tlmkpgavlv gmlnpfdkdg lqaltdtklt afaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr lfpmlmtaag tikaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyettee keaaegvggy arpmpqswld
      241 rqkaevakrv aaadivitta lipgraapvl vteemvrsmk pgsvivdlaa paggncplte
      301 agqtvvkhgv tlvgetnlpa lvaadsssly arnvidflkl vfnkegqfhv dleddivkac
      361 lmcrdgqllr a
//
LOCUS       WP_109044798             393 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudarthrobacter sp. AG30].
ACCESSION   WP_109044798
VERSION     WP_109044798.1
KEYWORDS    RefSeq.
SOURCE      Pseudarthrobacter sp. AG30
  ORGANISM  Pseudarthrobacter sp. AG30
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Pseudarthrobacter.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Pseudarthrobacter sp. AG30"
                     /db_xref="taxon:2249742"
     Protein         1..393
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40235
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiprerr egerrvaatp dtvrqltgmg ldvlletgag taaghsdhdy rqagaeivae
       61 ldhgaldilg hvrpldpdta aalkreavav glgspsselp tvqaladngv tsfalelvpr
      121 israqsmdal tsqalvagyr cvleaairlp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vfandirpas adevasmggt firldletae aaggyarqls sdagtrqrql
      241 laphvaqsdv littaavpgr papllvtrem vqgmrpgsvv vdlaaesggn vegsvpgqdi
      301 piptadgsgq itlvglkdpa samasdasrl yaknvanlla lmvrdgalal dfddevvaga
      361 clthggvvrh qptaallaar tgaaatarqd gal
//
LOCUS       WP_109046924             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum sp. TSA6c].
ACCESSION   WP_109046924
VERSION     WP_109046924.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum sp. TSA6c
  ORGANISM  Azospirillum sp. TSA6c
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Azospirillum sp. TSA6c"
                     /db_xref="taxon:709813"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39673
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiprerr pgerrvaasp etvkkfkalg ldvvvesgag lgssitdaay eaagaaiaad
       61 qasaladadi vlkvqrplia seggedelal makgtllfai lnpynsrdhv kayadvgvna
      121 famefmprit raqvmdvlss qanlagykav vdaaseygra fpmmmtaagt vpparafimg
      181 vgvaglqaia takrlgaivs atdvrpavke qvqslggsfv avendefkqa etaggyakem
      241 sddykrqqaa lvaehikkqd lvittalipg rkapilvtae hvasmkpgsv iidlaveqgg
      301 nvegaklgev vttangvkiv ghanyasria esasllyakn llalltslhg kdtgvavnwd
      361 deivkaialt rdgavvhpaf ag
//
LOCUS       WP_109083700             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_109083700
VERSION     WP_109083700.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36108
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieif fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel vsymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_109093536             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ancrocorticia populi].
ACCESSION   WP_109093536
VERSION     WP_109093536.1
KEYWORDS    RefSeq.
SOURCE      Ancrocorticia populi
  ORGANISM  Ancrocorticia populi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Ancrocorticia.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Ancrocorticia populi"
                     /db_xref="taxon:2175228"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53721
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipnepe qnlvsappds vrklvtlgyt vrvehaagna asfpdeqyla agaeiveske
       61 vwesdvvicl deppaeklel lrpgvtlisr ldpnsrpqlv ekltslkvna lamdavpris
      121 raqsmdvrss maniagyrav ieaanafgrv ftgqvtaagk vppanvyvig agvaglaavg
      181 aassmgaqvs gtdvrpevae qvesmggrfv pipvsqessd gyaramsedq aqqaqavytr
      241 eaigsdivit taqipgkpap tlitadavaq mrpgsvivdl gastggncel trpgevytta
      301 ngvtiigyed larrlpgqas qlygqnimnf lklatpqkdg nlvldqsdqv vrgvtvtfeg
      361 tlmwppppis vsaapqatpa ptaeqvpapi ppvrpsffkr twwkallvav ftwliltapp
      421 dmqghffvfa lavflgfyvi tavthslhtp lmsvtnaisg iiivgaitqi tsahvfvvva
      481 sfiaivvasi nifggftvth rmlkmfars
//
LOCUS       WP_109113271             448 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit, partial
            [Aeromonas caviae].
ACCESSION   WP_109113271
VERSION     WP_109113271.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     gene            1..>448
                     /gene="nrfA"
     Protein         1..>448
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
     Region          26..448
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tclgtsgwaq aadeaqskgk iearselfak dhadqftswk
       61 gtsesrertd alaedpqmvv lwagypfskd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvider gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meeyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg vvkqrkdavt eiklkvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakgish eiaipdissk ekaqaalg
//
LOCUS       WP_109114263             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_109114263
VERSION     WP_109114263.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53519
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqsecvdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_109142518             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. SUTN9-2].
ACCESSION   WP_109142518
VERSION     WP_109142518.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. SUTN9-2
  ORGANISM  Bradyrhizobium sp. SUTN9-2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium sp. SUTN9-2"
                     /db_xref="taxon:1167456"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39227
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiaiepgag lksglpdsef tavgatvspd
       61 alkdadivik vkrpeasevs qykrgalvia imdpygneaa lktiaeagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa dmvksmkpgs vlvdlaverg gnvegakage
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmid kkekklavnw ddelvkatal
      361 tkdgavihpn fqpka
//
LOCUS       WP_109148394             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Dietzia
            cinnamea].
ACCESSION   WP_109148394
VERSION     WP_109148394.1
KEYWORDS    RefSeq.
SOURCE      Dietzia cinnamea
  ORGANISM  Dietzia cinnamea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Dietzia cinnamea"
                     /db_xref="taxon:321318"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53903
     Region          17..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mspetdvret adapsvigvv aesnpaenrv aatpetvakl iglgyrvvve rgagtraefa
       61 daayaeagae lvdgdaawss dvvmkvavpt eaevarvrsg atlvsllapa qnehlltvla
      121 ergvtalamd avprisraqs mdvlssmani agyravieaa hhfgrfftgq vtaagkvppa
      181 kvlvagagva glaaigaass lgaivratdp rpevadqvks iggeylpvev peeekvvstd
      241 gyakatseay draaaklytd qaaevdiiit talipgraap rlitaadvas mkrgsvivdm
      301 aaaqggnveg svadevvvtd ngvtiigytd lagrlpaqas qlygtnlvnl aklvtpgkdg
      361 lwsldmddvv qrgvtvtkgg eimwppppvq vsaapaapaa aapaepaeek kklspaaklg
      421 miavgmalll lltaaapgdi arhitvfvla ivigyyvign vhhalhtplm svtnaisgvi
      481 vvgallqigi dntlglvlav vailfasinv fggfavtrrm lamfskga
//
LOCUS       WP_109161779             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_109161779
VERSION     WP_109161779.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35788
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehgl kyryengriv slrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechav frsvllrihe rkgiayheqd slntlmanlm argvisaeya
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vap
//
LOCUS       WP_109161859             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_109161859
VERSION     WP_109161859.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53686
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghaytvtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_109171002             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_109171002
VERSION     WP_109171002.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53700
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc ddchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_109176757             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_109176757
VERSION     WP_109176757.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53700
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmicg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_109181838             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_109181838
VERSION     WP_109181838.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53676
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignsfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_109187639             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_109187639
VERSION     WP_109187639.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35841
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iinalgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnlfhehgl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf scvvkechaa frsvllrihe rkgivyheqd slntlmanlm argvisaeyv
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 vap
//
LOCUS       WP_109210254             522 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Microbacterium].
ACCESSION   WP_109210254
VERSION     WP_109210254.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium
  ORGANISM  Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Microbacterium"
                     /db_xref="taxon:33882"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52826
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivaeg pgetrvaatp ttvpklialg ydvvveagag sassfpdaay aragatvvdg
       61 ptawsspivl kvnaptpaei drladgatvv atlspalrpd lveslatrgi taialdavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvasigge ylevvvpeea kqvsadgyak atsaaydrra
      241 aeiyseqaad vdiiittali pgrqaprlit aadvasmrpg svivdmaaaq ggnvegsvag
      301 ervvtdngvv ilgytdlpgr lpqqasqlfa tnlvnllkll tpakdgvltl dfddvvqrtv
      361 tvvrdgavtw ppppvqvsaa papaqaagtg paaaaapava akkpmskgar tglvvagiaa
      421 lfavcafapp plpqhflvlt laivvgfyvi ghvahalhtp lmsvtnaisg iivvgamvqi
      481 tvpdltvqil aaiavlvasi nifggfavtr rmlamfqkge tr
//
LOCUS       WP_109218701             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_109218701
VERSION     WP_109218701.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53622
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap kpaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_109227819             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Serinibacter arcticus].
ACCESSION   WP_109227819
VERSION     WP_109227819.1
KEYWORDS    RefSeq.
SOURCE      Serinibacter arcticus
  ORGANISM  Serinibacter arcticus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Beutenbergiaceae; Serinibacter.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Serinibacter arcticus"
                     /db_xref="taxon:1655435"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52951
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 milgvprata pgatavaatp atvvalrrlg ydvlveagag aaahltdday reagatvgtt
       61 eqawgadvva lvsapapadv erltpgatfa amlapaqrpd llealarrrv talaldavpr
      121 israqafdtl stqsniagyr avveaaqayg gmlagqvtaa gktdpatvfv igagvaglaa
      181 igaagslgar vrafdvrpev aeqieslgge fvrapqaqqe vaadgyatpl tpeqqaaamd
      241 vyavetarad ivittalvrg tapttitaam vaamrpgsiv vdlaasgggn cevtvpgstv
      301 vtpggvtvig etdltarmpr htsqllgtnv vnlltlmtpg rdgvlvldld dvvvrgltvt
      361 gpdgvlwppp pvqvsaapaa ppspppltpa evaaretaer derrrrgqrr tvaialgavl
      421 vafaltsapa svlphlmvfa lavvvgfyvi sqvshslhtp lmaqtnaisg iilvgallql
      481 gnesllvtvl aflaasvasi nifggflvts rmigmfaqgv rr
//
LOCUS       WP_109248536             467 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella algae].
ACCESSION   WP_109248536
VERSION     WP_109248536.1
KEYWORDS    RefSeq.
SOURCE      Shewanella algae
  ORGANISM  Shewanella algae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Shewanella algae"
                     /db_xref="taxon:38313"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51798
     Region          1..466
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvkklnqksf alsalvaasl maagafasdk teprnevykd kyknqyaswh dtaksseivd
       61 vlaedpnlvi mwagygfakd ynaprghiya vtdvrntlrt gapksaedgp mpmacwscks
      121 pdvprlieeq gedgyftgkw akggpevvna igcgdchekg spklrlgrpf aeramdtlgt
      181 pfdkasrkdk qsmvcgqchv eyyfekvegr kgfvkfpwdq gttvesmeay ydaiefadwt
      241 halsktpmlk aqhpgyetwq lgvhgknnvt cvdchmpkvt ndkgrkftdh kvgnpfdrfe
      301 etcaqchtqs kefmenltae rkakvnelkl kaedqivkah feaaaawkag atevemkpil
      361 tdirhaqwrw dyaiashgva ahapdealrv lgtavdkaan arvklaqlla kkgitepval
      421 pdistkakaq aalgmdmkkm vadkeefkkn vlpkwdaeak kreaayn
//
LOCUS       WP_109254406             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_109254406
VERSION     WP_109254406.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53544
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyakramg aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcancqtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_109251921             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinicauda salina].
ACCESSION   WP_109251921
VERSION     WP_109251921.1
KEYWORDS    RefSeq.
SOURCE      Marinicauda salina
  ORGANISM  Marinicauda salina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Marinicauda.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Marinicauda salina"
                     /db_xref="taxon:2135793"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38649
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlrerq sgesrvaatp dsvksliklg aelrvekgag agadlpddly kdagaklvtr
       61 aqalkdaeav favrrpdeet igkmpkgcll lgllephgde afakacaeag vnalameltp
      121 ritraqsmda lssqsnlagy ravieaaaly grafpmmmta agtiapakaf vmgagvaglq
      181 aiatarrlga vvsatdvrpa akeqvaslga kfvavedeef keaetaggya kemsdeykak
      241 qaelvaahla kqdvvvttal ipgrpaprli dtamvesmrp gsvivdiaav qggnceltrp
      301 devvehggvk iagftnlpgr laadasqlfa knlvslapll ldeegncaph wddeiikama
      361 ltrdgsvvhg e
//
LOCUS       WP_109259345             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hyphobacterium indicum].
ACCESSION   WP_109259345
VERSION     WP_109259345.1
KEYWORDS    RefSeq.
SOURCE      Hyphobacterium indicum
  ORGANISM  Hyphobacterium indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Hyphobacterium.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Hyphobacterium indicum"
                     /db_xref="taxon:2162714"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38834
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiailkerr dgetrvaatp esvkkliaag hdiqiekdag asasmpdsqy eavgaklgtl
       61 aatlkgadav favrapdaet laklpkgcll vgqlephgdk arakafaeag vnalameftp
      121 ritraqamda lssqsnlagy ravieasqiy rrafpmmmta agtiaaakvf vmgagvaglq
      181 aiatarrlga vvtatdvrpa akeqvaslga kfvavedeef kaaetaggya kemskeyqak
      241 qaelvashia rqdvvvttal ipgrpapkli tkamveamkp gsvivdlaap mggnceltka
      301 deivehkgvs iagfsnlpgr laadasslya rnlvnltpll vgedgalaph wddeiiigmt
      361 ltrdgkvvhe tlk
//
LOCUS       WP_109270207             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Allosphingosinicella humi].
ACCESSION   WP_109270207
VERSION     WP_109270207.1
KEYWORDS    RefSeq.
SOURCE      Allosphingosinicella humi
  ORGANISM  Allosphingosinicella humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomicrobiaceae; Allosphingosinicella.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Allosphingosinicella humi"
                     /db_xref="taxon:2068657"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38718
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlketa dgerrvaatp etikkfialg advaveagag vlasvddeam kgagatvssr
       61 advlkdadav lavqgpppgd lgaakpgalv vaalnpfger qrvdayaaag vealamefmp
      121 ritraqsmdi lssqanlagy kavldaasey grafpmmmta agtisaarvf imgvgvaglq
      181 aiatarrlga vvsatdvraa tkeqieslga kaifvesvag iegegaggya temsdeykka
      241 qaelvsghia kqdivittal ipgrpaprli sdaqlatmkp gsvivdlave qggnvegava
      301 geiverhgvr vvghrnvpsr laadtsalya rnlynflsaf wdaeakrvvl pdddeivqgv
      361 rltkdgkvvs erllas
//
LOCUS       WP_109273069             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_109273069
VERSION     WP_109273069.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35919
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iinalgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyvhsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaine lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlilndf acvvrechav frsvllrihe rkgivyheqd slntlmanlt argvisaeyv
      241 hkfhflsdvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 vap
//
LOCUS       WP_109284385             255 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_109284385
VERSION     WP_109284385.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..255
                     /product="STM4504/CBY_0614 family protein"
     Region          <12..119
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 yhnshsdevy rricktlrke yglftlyahs tsyldemsnl llktddkrkh idtielafny
       61 idtylrtyev tlglepdkai nelnnifheh slkyryengr ivrlrrikrl knicyylysp
      121 geygfveydl meaynrliln dfacvvrech avfrsvllri herkgivyhe qdslntlman
      181 ltargvisae yvhkfhflsd vleseiflpm vpekshhhya mmlriseela csiyylters
      241 iffltqraee dgvap
//
LOCUS       WP_109286947             508 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Shewanella].
ACCESSION   WP_109286947
VERSION     WP_109286947.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53327
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevvveanag llssfddaaf eaagakitae
       61 vwqadlifkv naptdaeiaq ikegatlisf iwpaqnpelv eklskrninv mamdmvpris
      121 raqsldalss maniggyrav veaahhfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggqfl kldftnedgs ssdgyaktms defiaaemal
      241 faeqakevdi iittalipgr papklitkam vdsmkpgsvi vdmaaqaggn ceytqpself
      301 vtengvkvig ftdlpgrlpa qssqlygtnl vnlmklmcke kngvasinfd dvvmrnmtvv
      361 kagevtfppp aisvsaapak paakveakaa eakkpsklky ilaalgaagf aavasvapae
      421 flshftvfvl scvvgyyvvw nvshslhtpl msvtnaisgi ivvgallqig qgstlvtvla
      481 fiavliasin ifggftvtqr mlkmfrkd
//
LOCUS       WP_109315413             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudovibrio ascidiaceicola].
ACCESSION   WP_109315413
VERSION     WP_109315413.1
KEYWORDS    RefSeq.
SOURCE      Pseudovibrio ascidiaceicola
  ORGANISM  Pseudovibrio ascidiaceicola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pseudovibrio.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Pseudovibrio ascidiaceicola"
                     /db_xref="taxon:285279"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55500
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigaakevl dgerrvaltp dsaqqlqklg yecaiesgag eaanfsdtdy tdagvkviad
       61 aktlwetadi vikvrppeas elelthegqt lisffwpaqn gellqqfadk kvnvlamdmv
      121 prisraqkmd alssmaniag yravmeagnn fprfftgqit aagkvppakv lvigagvagl
      181 aaigastslg aitlafdvrp evaeqvesmg aefvyldfee eqqdgastgg yasvsspefr
      241 eaqlakfrel apevdivitt alipgrdape lwtedmvqsm kpgsvivdla aekggncklt
      301 kmdekivtdn gvtvigytdf psrmatqsst lyatnirhmm fdltpekdgq aninmeddvi
      361 rgatatkdge itfpppkpki aaiaaqkpka pektpeelav eeaaaakaag rkqlglligg
      421 gavmaligay apesfmqhfi vfvlavfvgf qviwgvahsl htplmavtna isgiiilgal
      481 lqlgsgsriv wflagisvli asvnivggfm vtrrmlqmfn ks
//
LOCUS       WP_109327568             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum thermophilum].
ACCESSION   WP_109327568
VERSION     WP_109327568.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum thermophilum
  ORGANISM  Azospirillum thermophilum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Azospirillum thermophilum"
                     /db_xref="taxon:2202148"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40058
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvavpkerr agelrvaasp etvkklkglg ldvvveqgag lgssitdaaf eaagasivad
       61 paallrdadi vlkvqrplas gegeldelsl mkrgallfai lnpynsrdlv kayadagvna
      121 famefmprit raqvmdvlss qanlagykav vdaageygra fpmmmtaagt vpparafimg
      181 vgvaglqaia takrlgaivs atdvrpavke qvqslggtfv aveneefkqa etaggyakem
      241 sddykrqqaa lvaehikkqd ivittalipg rkapilvtre hvasmkpgsv ivdlaveqgg
      301 nvegaelgkv vtttngvkiv ghanypsria esasllyakn llallqvlhd keakgilvnw
      361 ddeivkaial trdgavvhpa fag
//
LOCUS       WP_109328580             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhodococcus].
ACCESSION   WP_109328580
VERSION     WP_109328580.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37966
     Region          13..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqsaaqp rptvgvpres negerrvalv pkivaaltgk gvdvvvesga glgalipdel
       61 yvgagakigd pwsadvivkv appsdeevgr lhagqtligf laprnqdnqv aalksagvaa
      121 faveaipris raqvmdalss qanvagykav llaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrat gydvrpevad qvrsvgaqwl dlgidaageg gyarelteqe
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvvvdl agetggncel
      301 tepgqtvvkh gvticsplnl pasmpehase lysknisall elmlvegrla pdfsdevlaa
      361 scvtreegvs
//
LOCUS       WP_109346028             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Massilia
            oculi].
ACCESSION   WP_109346028
VERSION     WP_109346028.1
KEYWORDS    RefSeq.
SOURCE      Massilia oculi (Telluria oculi)
  ORGANISM  Massilia oculi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Massilia oculi"
                     /db_xref="taxon:945844"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38810
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaarh qvlvqsgagl haaapdsaye aagasivdga
       61 aafgadivlk vrspdaderg lmrreavlvg mldpfdadnl aalagsglta faleaaprit
      121 raqsldvlss qaniagykai llaantygrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpyltdeer eiaqgsggya rpmpadwmrr
      241 qgelvherak ladivvttal ipgrkapili geetvramkp gsvivdmaia qggncpltel
      301 grtvvkhgvh iigepnlaal vaadasalya rnvldflklv idkddrffid redeivtatl
      361 vcangevlrk
//
LOCUS       WP_109355039             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingorhabdus sp. EL138].
ACCESSION   WP_109355039
VERSION     WP_109355039.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus sp. EL138
  ORGANISM  Sphingorhabdus sp. EL138
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sphingorhabdus sp. EL138"
                     /db_xref="taxon:2073156"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39224
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkela dgeqrvsasp etvkkftglg atmavekgag vsasiadsdy eaagasvgtr
       61 aavlkdadiv lgvqgpdpks lkgmkkgawl vaslnpfger krvdeyaglg idalamefmp
      121 ritraqsmdi lssqsnlsgy kavieaashy grafpmmmta agtvsaakcf vmgvgvaglq
      181 aiatarrlga qvsatdvraa tkeqiqslga kpifvedvag iegegtggya temseeyqka
      241 qaelvskhia kqdivittal ipgrpaprli sdaqiatmrt gsvivdlaae qggnvegava
      301 gkvvekhgvk iygannmpst maadssalfa rnlynflsay wdeeakrpvl pdddevtvgi
      361 rltkdgkvvn erllas
//
LOCUS       WP_109390058             436 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Salibaculum griseiflavum].
ACCESSION   WP_109390058
VERSION     WP_109390058.1
KEYWORDS    RefSeq.
SOURCE      Salibaculum griseiflavum
  ORGANISM  Salibaculum griseiflavum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salibaculum.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Salibaculum griseiflavum"
                     /db_xref="taxon:1914409"
     Protein         <1..436
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..435
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 tlisffnpgg neeglelars kgasviamem vprisraqkm dalssmanva gyravieagn
       61 nfgrfftgqi taagkvppak vlvvgagvag laaigastsl gavtyafdvr pevaeqvesm
      121 gaefvyldfe edqqdgaatg gyasvsspef reaqlakfre lapevdivit talipnreap
      181 klwledmvka mkpgsvivdl aaekggnveg tvmdekvvtd ngvtiigytd fpsrmatqss
      241 nlyatnirhm mtdltpgkdg qvvhdmeddv irgatvtheg eitwpppppk vqaiaaqkkp
      301 evkeptpeek raaevaafka qtrtqvtlla agaalilgvg lipgmpasfm qhfivfvlav
      361 fvgfqviwgv ahslhtplma vtnaissiii lgaliqvgss swlitvlaal gifmaavnif
      421 ggflvtrrml amfqks
//
LOCUS       WP_109384189             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseovarius carneus].
ACCESSION   WP_109384189
VERSION     WP_109384189.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius carneus
  ORGANISM  Roseovarius carneus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseovarius carneus"
                     /db_xref="taxon:2853164"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54821
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtptevl agearvamtp dsalqlqklg ydcvieagag akagfsdaay kdagvsvvkt
       61 aaalwkaadi vakvrppsda evkrlregqt lisffnpgan ekhmeqaaka gatvvamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvfldfee aqadgaatgg yaavsspefa
      241 aaqlakfrel apdidivitt alipnreape lwtedmvkam kpgsvivdla aekggncklt
      301 vmdekivten gvtiigytdf psrmaaqsst lyatnirhml adltpekdgv pvhnmeddvi
      361 rgatvahaga vtypppppkv aaiaaqpkke apkeltaaek raaevaafkk qtltqvglla
      421 aggvlvllvg mvapasfmkh fivfvlsvfi gfqviwnvah slhtplmavt naissiiilg
      481 aliqigsssf litllsavai fmasinifgg flvtrrmlam fqks
//
LOCUS       WP_109416362             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pararcticibacter amylolyticus].
ACCESSION   WP_109416362
VERSION     WP_109416362.1
KEYWORDS    RefSeq.
SOURCE      Pararcticibacter amylolyticus
  ORGANISM  Pararcticibacter amylolyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pararcticibacter.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Pararcticibacter amylolyticus"
                     /db_xref="taxon:2173175"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40521
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvpkesk lhekrvaltp diakqliakg feitieagag egsffsdecy rqagaktalt
       61 eevfdadivl kvdaptqeea nlmkegsaci smlyaytrpe lietfinrki tsfamdavpr
      121 israqkmdal ssqaniagyk avilaadqlg rifplmmtaa gtvtpakvli fgagvaglqa
      181 vatakrlgav vevsdvrpet keqveslggk fltvdgagdv kiqggyardv speflqkqke
      241 liankikead ivittalvmg kkspvlvtae mvrsmkngsv ivdlavesgg ncelseynkt
      301 vnkhgvtiig eanlpalvpv nssqlyavni stlllhlats egfnldpeee itkgtlitre
      361 gelvheftks ildkhtnlv
//
LOCUS       WP_109423081             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Maritimibacter sp. 55A14].
ACCESSION   WP_109423081
VERSION     WP_109423081.1
KEYWORDS    RefSeq.
SOURCE      Maritimibacter sp. 55A14
  ORGANISM  Maritimibacter sp. 55A14
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Maritimibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Maritimibacter sp. 55A14"
                     /db_xref="taxon:2174844"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55644
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeva kgearvamtp dsalqlqklg fdcaieagag taagfsdaay keagveiikt
       61 paalwkacdv vakvqpptdt eakrlregql lisffwpaqn etllelcksr sasviamdmv
      121 prisraqkmd alssmaniag yravieasnn fgrfftgqit aagkvpparv livgagvagl
      181 aaigtstslg avtlafdvrp evaeqvesmg aefvyldfee eqqdgsstgg yasvsspefr
      241 eaqlakfrel apevdilitt alipnreape lwtedmvksm krgsvivdla aekggncklt
      301 vkddkivtdn gvtiigytdf psrmatqsst lyatnvrhmm tdltpekdgk vvhdmeddvi
      361 rgatvthage itfpppppkv qaiaaapkke pakvptpqek raqelaafra dtrrqvgmla
      421 aggvlmlllg qvappsfmqh fivfvlacfi gfqviwnvsh alhtplmsvt naisgiivlg
      481 avlqigsgga lvvilaaisv liasinivgg flvtrrmlam fqks
//
LOCUS       WP_109448149             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. ICBB 8177].
ACCESSION   WP_109448149
VERSION     WP_109448149.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. ICBB 8177
  ORGANISM  Streptomyces sp. ICBB 8177
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Streptomyces sp. ICBB 8177"
                     /db_xref="taxon:563922"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53676
     Region          14..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msaqepahhp pqhvgvvres lagenrvaat pttvrqllgl gyevvvepga gaasgftdea
       61 yldagatvge awaadvvlkv napseaeigr lrqgatlagl lspaqrpell qalagagvta
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvkslggeyl pvnveqeast dgyakatsad
      241 ydraaaalyh eqakdvdivi ttalipgrpa prlltaadva amkpgsvvvd maaamggnve
      301 gtvageavvt eggvhligyt dlasrlpaqa sqlfgtnlvn lvklltpgkd grltldfddv
      361 vqravtvvra gevtwppppv svsaapaapp apasapaepe pkrarltpag rlgligigml
      421 amflvvgfap sqladnftvf tlavvigyyv igkvhhalht plmsvtnais givvigallq
      481 igheswivtt lsfvaillts vnvfggfavt rrmlsmfstf stsskg
//
LOCUS       WP_109447010             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum sp. TSH64].
ACCESSION   WP_109447010
VERSION     WP_109447010.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum sp. TSH64
  ORGANISM  Azospirillum sp. TSH64
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Azospirillum sp. TSH64"
                     /db_xref="taxon:652740"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40478
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiprerr pgerrvaasp etvkkfkalg ldvvvesgag lgssitdaay eaagaaiaad
       61 qtsaladadi vlkvqrplia aeggedelal irkgallfai lnpynsrdhv kayadagvna
      121 famefmprit raqvmdvlss qanlagykav vdaaseygra fpmmmtaagt vpparafimg
      181 vgvaglqaia takrlgaivs atdvrpavke qvqslggsfv avendefkqa etaggyakem
      241 sddykrqqaa lvaehikkqd lvittalipg rkapilvtae hvasmkpgsv ivdlaveqgg
      301 nvegaklgev vttangvkiv ghanyasria esasllyakn llalltslhg kdtgvavnwd
      361 deivkaialt rdgaivhpaf adareaqpa
//
LOCUS       WP_109440448             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter haemolyticus].
ACCESSION   WP_109440448
VERSION     WP_109440448.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39663
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv agesrvaatp etvkklinag hsvviergag vkaayidsay eqvgatitdd
       61 aytgsqiilk vrapkgdeiq klaanttvva mfdpyrnpel dqfatqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak eqveslggkw ldvpmsdeek qraaeaaksg ygwqpgeqyi
      241 kdqaaivdka vsnadivitt alipgrnapr likaetvakm kpgsvildma vetggnvegs
      301 kegetvvtan gvkilgipni pgtvateasa lyarnvfnfl etlfekekgf ainqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_109460312             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            album].
ACCESSION   WP_109460312
VERSION     WP_109460312.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium album
  ORGANISM  Rhizobium album
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium album"
                     /db_xref="taxon:2182425"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55331
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely pgearvamtp dsavqlqklg yacliesgag saagfsdedy raagvtvved
       61 pailfasadv iakvrppvag evdrlspekt lvsffypaqn pdlleqaknr gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigvatslg aqtyafdvrp evaeqiesmg aefvyldfdg gvqdgattgg yaapsspefr
      241 ekqlakfrel apqmdivitt alipgrdapk lwladmvaam kpgsvvvdla aerggncdlt
      301 vpdqrivsen gvivigytdf psrmaaqsst lyatnirhmm tdltpakdgt ivhnmeddvi
      361 rgatvthqga itypppppki qaiaaqkrqe kvkeptaaek raqevaafrk qtknqvllla
      421 igtallllvg ayapsafmsh fivfalacfv gfqviwnvsh slhtplmavt naisgivilg
      481 allqigsgsw lvivlaalsv liatvnivgg flvtrrmlam fqks
//
LOCUS       WP_109468456             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Albibacillus kandeliae].
ACCESSION   WP_109468456
VERSION     WP_109468456.1
KEYWORDS    RefSeq.
SOURCE      Albibacillus kandeliae
  ORGANISM  Albibacillus kandeliae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Albibacillus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Albibacillus kandeliae"
                     /db_xref="taxon:2174228"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55590
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif dgenrvamtp dsatalkklg hecvieagag lragfldeay aaagvevvad
       61 akalfaaadv iakvrppsda evamlrpdqt lisffypgsn eelmkkaadt gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvyldfte aqtdgaatgg yaapsspefr
      241 eaqlkkfrel apdidivitt alipnrpapv lwtkdmvelm kpgsviidla aerggncelt
      301 kpdekivsdn gvtivgytdf psrmatqsst lyatnirhmm tdltpekdgv inhnmeddvi
      361 rgatitheka vtfpppppki qaiaaqkpke kakeltpeer kaaeiaafka qtksqvtlla
      421 vgtivmllig iyapasfmsh fivfalacfv gfqviwsvsh slhtplmavt naisgivilg
      481 allqvgsgnw lvvilsfisv liasinivgg flvtrrmlam fqks
//
LOCUS       WP_109469183             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum sp. TSH58].
ACCESSION   WP_109469183
VERSION     WP_109469183.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum sp. TSH58
  ORGANISM  Azospirillum sp. TSH58
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Azospirillum sp. TSH58"
                     /db_xref="taxon:664962"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40498
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiprerr agenrvaasp etvkklkals levvvetgag lgsnlpdrvy qdagatiapd
       61 aasaladadi vlkvqrplla gegdldelal ikrgallfai lnpynsrdhv aayaaagvna
      121 famefmprit raqvmdvlss qanlagykav vdaaseygra ypmmmtaagt vpparafimg
      181 vgvaglqaia takrlgaivs atdvrpavke qvqslggsfv aveneefkqa etsggyakem
      241 sddykrqqaa lvaehikkqd ivittalipg rkapilvtre hvasmkpgsv iidlaveqgg
      301 nvegselgkv vvtdngvkiv ghanypsria esasllyakn llallqslhd kekgvtlnwd
      361 deivkaialt rdgqvvhpaf agqtv
//
LOCUS       WP_109469157             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum sp. TSH58].
ACCESSION   WP_109469157
VERSION     WP_109469157.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum sp. TSH58
  ORGANISM  Azospirillum sp. TSH58
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Azospirillum sp. TSH58"
                     /db_xref="taxon:664962"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41036
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiprerr agenrvaasp etvkkikglg ldvvvetgag lgsnlpdrvy qdagatiapd
       61 aasaladadi vlkvqrplla gegdldelal ikrgallfai lnpynsrdhv aayaaagvna
      121 famefmprit raqvmdvlss qanlagykav vdaaseygra ypmmmtaagt vpparafimg
      181 vgvaglqaia takrlgaivs atdvrpavke qvqslggsfv aveneefkqa etsggyakem
      241 sddykrqqaa lvaehikkqd ivittalipg rkapilvtre hvasmkpgsv iidlaveqgg
      301 nvegselgkv vvtdngvkiv ghanypsria esasllyakn llallqslhd kekgvalnwd
      361 deivkaialt rdgqivhpaf adavrevqtv
//
LOCUS       WP_109473671             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ornithinimicrobium cavernae].
ACCESSION   WP_109473671
VERSION     WP_109473671.1
KEYWORDS    RefSeq.
SOURCE      Ornithinimicrobium cavernae
  ORGANISM  Ornithinimicrobium cavernae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Ornithinimicrobiaceae; Ornithinimicrobium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Ornithinimicrobium cavernae"
                     /db_xref="taxon:2666047"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53030
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvptesa pgetrvaatp qtvgrlialg htvvvqagag arasypdeqy aeagaavdpg
       61 qgvwgadlvv tidapgptel eqlrpgayvv aqlgpgqhpe llddlarrgv talamdavpr
      121 israqsldvl ssmanlggyr avieaanvyg svftgqvtaa gnvpparvfv igagvaglaa
      181 igtasslgav vratdirpev aeqvesmgae fvpievedqa assdgyarem gedlqrrale
      241 vyarecaead ivittalipg rpaptlvtsg tvasmrpgsv lvdmaarngg nceltrpgev
      301 ltsdngvtiv gytdlparlp tqasqlygtn vanlielltp grdgrlvldl edevqrgltv
      361 thdgtvlwpp ppvavsagpg pvpeavpagg atpaapprar dprrgyvama laavlfalva
      421 slsppdflgh ftvfalaviv gfyvisnvth alhtpllaet naisgiilvg ailqvgnesl
      481 lvrglalaat vvasinvfgg favtgrmlrm frredva
//
LOCUS       WP_109477886             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. C35].
ACCESSION   WP_109477886
VERSION     WP_109477886.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. C35
  ORGANISM  Paraburkholderia sp. C35
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia sp. C35"
                     /db_xref="taxon:2126993"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39677
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdigvpaetr phesrvaatp etvkkyvsqg hrvlvqhdag laasftnesf stagaqivda
       61 atafaadvvl kvqsptdtev pllkrgavlv gmldpfnrdn atalaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaamlypr flpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaagvggy arpmppswla
      241 rqsalvhera kqadvvista lipgraaptl isvdtvramk pgsvlidlaa grgdefegrr
      301 ggncpltepd tvitrhgvqi agytnlasmv padasslyar nvldflklvi tkegtlnidl
      361 addivaatll ardvevvrkv
//
LOCUS       WP_109516692             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Teichococcus aestuarii].
ACCESSION   WP_109516692
VERSION     WP_109516692.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus aestuarii
  ORGANISM  Teichococcus aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Teichococcus aestuarii"
                     /db_xref="taxon:568898"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39446
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavlkerr sgetrvaatp etvrklidlg lgvvvetgag lasglpdaay reagaeiaqd
       61 asaalagaki vlkvraplga gegevnelal lprgalligt leavahpara qayaeaglea
      121 csmellprit raqsmdvlss qanlagyrav vegaaafdkg fpmlmtaagt ipaanvfimg
      181 agvaglqaia tarrlggrvs atdvrpaake eikslgaafv gyedeesraa qtaggyakql
      241 spefyakqae viaaavakad vvvctalvqg rkaptlltaa mvesmkpgsv vvdiaadagg
      301 ncaltrpgea ivteggvkil ghtnwpgrip aaasalyarn lltflstfwd keakapklpq
      361 edeiirgvtl trggavvhpq laaapaa
//
LOCUS       WP_109502213             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_109502213
VERSION     WP_109502213.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38609
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vfnkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_109521595             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas prosekii].
ACCESSION   WP_109521595
VERSION     WP_109521595.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas prosekii
  ORGANISM  Pseudomonas prosekii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas prosekii"
                     /db_xref="taxon:1148509"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38637
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vfnkegqfev nleddivvac
      361 lmcrdgqvir kna
//
LOCUS       WP_109532329             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pararhodobacter marinus].
ACCESSION   WP_109532329
VERSION     WP_109532329.1
KEYWORDS    RefSeq.
SOURCE      Pararhodobacter marinus
  ORGANISM  Pararhodobacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pararhodobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Pararhodobacter marinus"
                     /db_xref="taxon:2184063"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55712
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif pgenrvamtp dsalqlqklg hsciietgag aaagfedaay eaagveiaps
       61 aqalfeaadv vvkvreatte emnrlradqt liaffwpaqn aemlelakek gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqiesmg aefvyldfee qaqdgaatgg yaapsspefr
      241 ekqlekfrel apdvdivitt alipgrpapk lwtedmvrmm krgsvivdla aekggncdlt
      301 vkdekivten gvtivgytdf psrmgtqast lysnnirhml tdltpgkdgv inhnmeddvi
      361 rgatvahage itfpppppkv qaiaaqkrek pkeltpeekr aqevaafkaq trqqvtllgv
      421 ggallllagf fapasfmshf ivfvlacyvg fqviwsvshs lhtplmavtn aissiiilga
      481 lmqigsgswl vmilaalsvf maginifggf mvtrrmlamf qks
//
LOCUS       WP_109529230             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            aurea].
ACCESSION   WP_109529230
VERSION     WP_109529230.1
KEYWORDS    RefSeq.
SOURCE      Nocardia aurea
  ORGANISM  Nocardia aurea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Nocardia aurea"
                     /db_xref="taxon:2144174"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39570
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mettqsagds sprgarvgvv resnagerrv alvpkiipal lkqgvevvve sgaglgalip
       61 deayveagat igdpwsaevv vkvappsdte vaklskgqtl igflaprnsd nqiealtdag
      121 vqafaveaip risraqvmda lssqanvagy kavllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rttgydvrpe vadqvrsvga qwldlgidaa geggyarelt
      241 ddekaqqqqa lenaikgfdv vittalvpgr paprlvtaaa vegmkpgsvi vdlagetggn
      301 celtepgetv vkhevtiasp lnlpatmpeh aselysknia allelmlvdg kvvpdfedqv
      361 ladscvtrer glpsepikae vqs
//
LOCUS       WP_109554300             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_109554300
VERSION     WP_109554300.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53513
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfsf ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheie ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_109564701             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Jannaschia
            seohaensis].
ACCESSION   WP_109564701
VERSION     WP_109564701.1
KEYWORDS    RefSeq.
SOURCE      Jannaschia seohaensis
  ORGANISM  Jannaschia seohaensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Jannaschia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Jannaschia seohaensis"
                     /db_xref="taxon:475081"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55553
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkevl adearvaitp esaghlqklg ydviveagag ekagfldsay adagvevvsg
       61 adqlwkvadi vakvrpptee evarlehgkt lisffypasn etlmglakdk ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvflefed selpdgaatg gyappsspef
      241 qakqlekfre lapdmdivit talipnrpap vlwtkdmvea mkpgsvivdl aaerggncel
      301 tvkdekivtd ngvtivgytd fpsrmatqss tlygnnirhm madltpekdg qvvhnmeddv
      361 irgatithgg eitfpppppk vqaiaaqkke kpkeltpeek raqevaafka etkfqvslla
      421 vggvllllag lytpasfmqh fivftlacfv gfqviwgvah slhtplmavt naissiiilg
      481 allqigsgsm lvvilaaasv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_109580134             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus plantarum].
ACCESSION   WP_109580134
VERSION     WP_109580134.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus plantarum
  ORGANISM  Cupriavidus plantarum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus plantarum"
                     /db_xref="taxon:942865"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39445
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipletr agetrvaatp etvkkyvaqg hqvtvqtgag vrasqpdgay eavgarigsa
       61 aeaygaeivl kvrapddaer almkpgtvli gmlnpfdien narmtaasit afaleaaprt
      121 traqsmdvls sqaniagyka vliaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfltdee reiaqgvggy arpmpadwmr
      241 rqaelvhera rqadivitta lipgrkapvl lkeetvqqmk pgsvvvdlaa aqggncpltv
      301 adevverhgv ilvghtnlas mvaadasaly arnvldflkl vidkdgrytl nleddivaac
      361 lmcrdgqlvr qaa
//
LOCUS       WP_109591431             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychrobacter immobilis].
ACCESSION   WP_109591431
VERSION     WP_109591431.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter immobilis
  ORGANISM  Psychrobacter immobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Psychrobacter immobilis"
                     /db_xref="taxon:498"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40021
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvisads asesrvaltp davkklrklg fevviqsgag qaayyademy qaagadiass
       61 stevvtqsqi ittvndlpaa aidqltsgqi vigmldpyrn tqldtyagkg vtvfamellp
      121 rtlsraqnmd vlssqanlag ykavllaane ysrpfpmfmt sagtvkpakv vilgvgvagl
      181 qaiatakrlg avveasdlrp tareqveslg gkwldvpmsa eeaetakstg gyawtpseqy
      241 vkdqaavvdk alsnadivit taqipgrnap rlvhgatlak mkagsvlidm aagtggnveg
      301 svpdetitta ngvrivgaan ipsqlaaqss dlyannlvnf ittliapaat ndtsaktlal
      361 nldmndeiqg alavthenqv rlakr
//
LOCUS       WP_109594255             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            sp. 17 mud 1-3].
ACCESSION   WP_109594255
VERSION     WP_109594255.1
KEYWORDS    RefSeq.
SOURCE      Microvirga sp. 17 mud 1-3
  ORGANISM  Microvirga sp. 17 mud 1-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Microvirga sp. 17 mud 1-3"
                     /db_xref="taxon:2082949"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55107
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalreis pgenrvamtp dsaillnklg hacviqagag maagftdavy aaagvevfps
       61 aeavfaaadv vvkvrapemt eaemlrqeqt lisffwptqn pdlleqaraq gatviamdmv
      121 prisraqkmd alssmaniag yravieasna fgrfltgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aqfvflefeg aqdgaanggy aapsspefre
      241 kqlakfrela peidivitta lipgrpapkl wtqdmvaamr pgsvivdlaa erggnsdltv
      301 pdekvvteng vtiigytdfp srmaaqastl yannirhflt dltpnkdgii vhnmdddvir
      361 gatvthqgai typppppkvq aiaaakpkek vreltpeekr areaaafrsq trtqvgllva
      421 ggllialvga yapasfmahf ivfalacfvg fqviwsvshs lhtplmavtn aisgivvlga
      481 llqvgsghwl vvslaslsfl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_109599426             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            sp. 17 mud 1-3].
ACCESSION   WP_109599426
VERSION     WP_109599426.1
KEYWORDS    RefSeq.
SOURCE      Microvirga sp. 17 mud 1-3
  ORGANISM  Microvirga sp. 17 mud 1-3
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Microvirga sp. 17 mud 1-3"
                     /db_xref="taxon:2082949"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39321
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsesd qaearvaatp etikkykalg aevtvqagag gragfpdaey eaagaavaat
       61 aeeaakdadi vlkvrrpets elaalkpgal liaimdpygq daalkalada kvsafamelm
      121 pritraqvmd vlssqanlag yravidatae ygrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfiavedee fkqaetaggy akemsaeyra
      241 kqaalvashi akqdivitta lipgrpapkl vtremveamk pgsvivdlav erggnvelae
      301 pgrvaehngv kivghlnvpg rlaatassly arnlyafvet lvdkaaktla vkwddelvka
      361 tcltrdgaiv htafqpta
//
LOCUS       WP_109602321             505 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinoplanes xinjiangensis].
ACCESSION   WP_109602321
VERSION     WP_109602321.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes xinjiangensis
  ORGANISM  Actinoplanes xinjiangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Actinoplanes xinjiangensis"
                     /db_xref="taxon:512350"
     Protein         1..505
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51785
     Region          1..504
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigvlrdpd pgerrvaatp atveqlaklg yqvvvepgag aeasfsdeay aqagatigdp
       61 ltadivftin ppvqrldkla egttligmln prlapglved larrpitals mdavprisra
      121 qsldvlssma niagyravve aahafgrfft gqvtaagkvp pakvlvagag vaglaaigaa
      181 gslgaivrat dprpevadqv rslggeylav eaadvevsat gyakemsddy ndraarlyad
      241 qarevdivit talipgrpap tlitadmvat mkagsvivdm aaanggnveg tvagevvvta
      301 ngvtiigytd lpgrlpaqas qlygtnlvnl mklltpdkdg qlvldfddvv qrsmtvvrdg
      361 eltwppppvs vsaapaavap qpveatpkpv rrplnpllvt gvaaaalfll taaapaalrg
      421 hltvfalaiv igyyvighvh halhtplmsv tnaisgiivv gallqlghgg glvtglsvva
      481 illasinvfg gfavtrrmla mfsrs
//
LOCUS       WP_109622572             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sediminitomix flava].
ACCESSION   WP_109622572
VERSION     WP_109622572.1
KEYWORDS    RefSeq.
SOURCE      Sediminitomix flava
  ORGANISM  Sediminitomix flava
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Sediminitomix.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Sediminitomix flava"
                     /db_xref="taxon:379075"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40949
     Region          1..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(13,72,91,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(42,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvlkelh dqrvaitpdl vkklvksghe vvfesgagak afaqddayea agakaqnrea
       61 vvassdllmt ikpiakeeia qlkdgavlvs qfqpfqdaav cddfstknls tfsfdmiprt
      121 tiaqsmdils smasisgyka vlkatealpr yvpmlssaag tippskvlil gagvaglqai
      181 atakrlggqv eafdtraask eevmslgakf vevagaaddk gaggyaveqs eeykqkqqal
      241 ikekiqkadi vittaqlrgr paptliteem vqnmkpgsvi vdlasstggn cpltedkksv
      301 vkhgvtiigd selsdllpeq asqlysrnie nylkiflnee gisydfenqi iresclvfkg
      361 kkvygdtdql lpkkeevaes vea
//
LOCUS       WP_109613747             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudaminobacter salicylatoxidans].
ACCESSION   WP_109613747
VERSION     WP_109613747.1
KEYWORDS    RefSeq.
SOURCE      Pseudaminobacter salicylatoxidans
  ORGANISM  Pseudaminobacter salicylatoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Pseudaminobacter.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Pseudaminobacter salicylatoxidans"
                     /db_xref="taxon:93369"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42811
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifvpke vdaseprvaa spetvkrlag lgfdvvveag aglnsritda dyqavgakig
       61 kvsdaagadv vlkvrrptda elkgykpgaa viaimdpygn daavasmara gvtafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaki fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedee fkqaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpaprl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttang vrivghvnva grvaasasll yaknlyafle tmvdketkql ainrddelvk
      361 atmltdagkv vhpafaeaaa kaaaqpaadt dekpakpaak kpaaakkpaa skskgda
//
LOCUS       WP_109647658             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodohalobacter mucosus].
ACCESSION   WP_109647658
VERSION     WP_109647658.1
KEYWORDS    RefSeq.
SOURCE      Rhodohalobacter mucosus
  ORGANISM  Rhodohalobacter mucosus
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Rhodohalobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rhodohalobacter mucosus"
                     /db_xref="taxon:2079485"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39970
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miasvckete qhekrvaltp egvaalvklg vevhvesgag tassytdqmy teagatlsns
       61 rdslisgcdi llavqapaep virkmkagat lvsfiwplqn etyvellklq nitalamdti
      121 prisraqsmd alssmsniag ykaalmganq ldrylpmmmt aagtippakv lvlgagvagl
      181 qaiatakrlg avveafdirp avkeqveslg akfvdvplee aseteggyak elseknkqkq
      241 revihdhvrk sdivittali pgrpapllvt kamvedmspg svivdiaaeq ggncevtkpg
      301 etivhqgvri vapfnipssl afhasklysk nlmsllslli kegkpeynfe dqiivnatvt
      361 hqgelvspfv kdnln
//
LOCUS       WP_109665718             427 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium loti].
ACCESSION   WP_109665718
VERSION     WP_109665718.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium loti
  ORGANISM  Mesorhizobium loti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Mesorhizobium loti"
                     /db_xref="taxon:381"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43844
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglnsrivda dyasagaaig
       61 kasdvakadv vlkvrrpsda elksykpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafakadq qprvepaaip attmvadasv kpatakkaap kkaaapksps
      421 skpkgia
//
LOCUS       WP_109669540             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseicyclus mahoneyensis].
ACCESSION   WP_109669540
VERSION     WP_109669540.1
KEYWORDS    RefSeq.
SOURCE      Roseicyclus mahoneyensis
  ORGANISM  Roseicyclus mahoneyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseicyclus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseicyclus mahoneyensis"
                     /db_xref="taxon:164332"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55221
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeie agearvamtp dsalqlqklg ydcvietgag qaagftdaay eaagvevvkt
       61 aaalwkdadi vakvrpptta eakkfregql visffypgqn eklmetakaa gtniiamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvflefsa delpdgaatg gyappqspef
      241 qakqlakfre iapemdivit talipgrpap klwtkdmvea mkpgsviidl aaerggncel
      301 tkaderivtd ngvviigytd fpskmaaqss tlystnirhm mtdltpgkdg tvvhnmeddv
      361 irgatavfag aitfpppppk vaaiavqkre kpkeltpeek raaevaafka qtknqitlla
      421 vggalllgvg liapasfmqh fivfvlsvfi gfqviwnvah slhtplmavt naissiiilg
      481 almqvgsssv litvlaalgi fmasvnifgg flvtrrmlam fqks
//
LOCUS       WP_109671756             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Dyadobacter jejuensis].
ACCESSION   WP_109671756
VERSION     WP_109671756.1
KEYWORDS    RefSeq.
SOURCE      Dyadobacter jejuensis
  ORGANISM  Dyadobacter jejuensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Dyadobacter.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Dyadobacter jejuensis"
                     /db_xref="taxon:1082580"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40035
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkisvlketk pferrvaltp slvkslvksg ysctveagag elsyfsdasy qeagaqiagn
       61 vaetlaaadv vlkvnaptle evaamregiv lisylyayti pevleqlnek risafsmdav
      121 prisraqkmd alssqanlag ykavllgana lgkifplmmt aagtitpsrv lvfgagvagl
      181 qaiatakrlg avveatdvra etkeqveslg grfltvegae gvkveggyak evsadylqkq
      241 qelvkqrike adiaittalv igkkapvlit eemvrmmkpg svivdmaves ggncalsvfg
      301 etvvahgvti igepnlpsll pinaselyak nistlllhla taegfkwele eevtkgslit
      361 hqgalvhgft keilakvka
//
LOCUS       WP_109676266             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sediminicurvatus halobius].
ACCESSION   WP_109676266
VERSION     WP_109676266.1
KEYWORDS    RefSeq.
SOURCE      Sediminicurvatus halobius
  ORGANISM  Sediminicurvatus halobius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Sediminicurvatus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sediminicurvatus halobius"
                     /db_xref="taxon:2182432"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39677
     Region          3..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtirvavpke tasgerrval vpsvlkqydk lgvevlvqkg agaasgfadd eytgativdg
       61 aealyekadi ilrvqpptve eagklpegal llgfltpheg dsrirnlakr kvtsfamelv
      121 pritraqsid alssqaniag ykcallaaql spklfpmltt aagtvrpakv vvigagvagl
      181 qaiatarrlg aiveaydvrs atkeqveslg gkfietgvka egeggyarel tederrqqqe
      241 vladhiasad avvttaaipg rpapkiidka tvermrggsv ivdmaaetgg nceltqagke
      301 ithqgvvvag pknipsmaat hasemyarnl ynllalivkd geiqldwddq vladsclthd
      361 gevrhaptre rleggk
//
LOCUS       WP_109693307             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides silvaticus].
ACCESSION   WP_109693307
VERSION     WP_109693307.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides silvaticus
  ORGANISM  Nocardioides silvaticus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Nocardioides silvaticus"
                     /db_xref="taxon:2201891"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53413
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresk tgetlvaata ktaaqlqglg ydvvvesgag aladqadeaf tdagvtvgss
       61 edvwgsdivv kvnaptadei arlragatii smmaparspe lveqlaaqgv talamdavpr
      121 israqsmdvl ssmanvagyr avveaahefg rmftgqvtaa gkmpparvfv vgggvaglaa
      181 igaaaamgav vrafdvrpev aeqveslggt fvevdfesev stdgyakemt aeqeaatasm
      241 ydeearnadi vittalipgr papkliheet vaamrpgsvi vdmaaanggn vagtetdqrv
      301 vtdhgvtilg ytdlagrlpa qtsqlygtni vnlfklltpe kdgeltldld dvvqrgvtvt
      361 ratddgaesr sevmwpppav qvsatpktag apapeakepk paltargrma vvlggiaafw
      421 lvnatapdpi prhfttlmls ivigyyvigk vahalhtplm svtnaisgvv vvgallqles
      481 edvaiqvlaa iavlvasini fggfavtrrm lgmfskga
//
LOCUS       WP_109698558             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga deserti].
ACCESSION   WP_109698558
VERSION     WP_109698558.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga deserti
  ORGANISM  Chitinophaga deserti
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Chitinophaga deserti"
                     /db_xref="taxon:2164099"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39763
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milavlkekv genrvslvpe vvkqlvqqqv eiwveegaga aafypddsyr eagaalksrr
       61 dilqgadvll tirppeaady eqaaagktwa gvyqplyhpg lmqqlaarqf tvfsldsipr
      121 ttraqsmdvl ssqaniagyk avllaaftys ryfpmlmtaa gsippakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgak fvevegaada saaggyaveq sddfkqrqaa
      241 riaesaakad ivittaqipg kpapillpaa aveamrtgsv iidlaaatgg ntaltknget
      301 vlhkgvtiig nsdlagtapa dasklyaknm lnflklmigk egqwqpdykd divqgacitr
      361 egqvvnervk qlqpaav
//
LOCUS       WP_109707472             424 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Falsochrobactrum shanghaiense].
ACCESSION   WP_109707472
VERSION     WP_109707472.1
KEYWORDS    RefSeq.
SOURCE      Falsochrobactrum shanghaiense
  ORGANISM  Falsochrobactrum shanghaiense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Falsochrobactrum.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Falsochrobactrum shanghaiense"
                     /db_xref="taxon:2201899"
     Protein         1..424
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43956
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifipke sdpsetrvaa saetvkkfia lgfdvvveks ageksriida efsaagarig
       61 taadaksadi vlkvrrptda elknyksgsa lfamldphgh dgavaalaka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaaee ydralpmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedee fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vtremvaamr pgsvlvdlav erggnvegav
      301 agevadiggv kivghlnvpg riaatasqly arnlfaflet lvdketksfg fdpeeelvka
      361 tllthqgkiv hpafekvald aaggaeakae kpaakpktar kpaakapaka pktapktsad
      421 ggea
//
LOCUS       WP_109720280             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Abyssibacter profundi].
ACCESSION   WP_109720280
VERSION     WP_109720280.1
KEYWORDS    RefSeq.
SOURCE      Abyssibacter profundi
  ORGANISM  Abyssibacter profundi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Oceanococcaceae; Abyssibacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Abyssibacter profundi"
                     /db_xref="taxon:2182787"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39102
     Region          3..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtvklfvpke sasgekrvam apavvdrvvr lgtelsvqag agagsripda afeakgakiv
       61 ktkasplksa dvvlrvappt aadikgmkag silasfvytn rnpdvvkala eakvttlame
      121 lipritraqa mdalssqaaa agykaaliaa selerflpml ttaagtirpa kvlvigagva
      181 glqaiatarr lgamveaydv rtaakeqves lgakfvmadi kadaeggyar eltdeekaaq
      241 qamlekhvaa adavittaai pgrpspkiis kamvesmksg avivdlaaeg ggncelsepg
      301 stttagevti caplnvpsml sehasemyar nllnlmelfi kdgeltldle ddvikgallt
      361 hdgevvneqa kqilegsk
//
LOCUS       WP_109756548             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. 43mfcvi1.1].
ACCESSION   WP_109756548
VERSION     WP_109756548.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. 43mfcvi1.1
  ORGANISM  Pseudomonas sp. 43mfcvi1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. 43mfcvi1.1"
                     /db_xref="taxon:1761894"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38802
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvidsvy eaagatigsa
       61 sdafgaelil kvvapsdsel tliksgtvlv gmlnpfnnet isklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_109768586             392 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oceaniradius stylonematis].
ACCESSION   WP_109768586
VERSION     WP_109768586.1
KEYWORDS    RefSeq.
SOURCE      Oceaniradius stylonematis
  ORGANISM  Oceaniradius stylonematis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Ahrensiaceae; Oceaniradius.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Oceaniradius stylonematis"
                     /db_xref="taxon:2184161"
     Protein         1..392
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40347
     Region          3..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,76,95,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpltlfvake sqageprvaa spdtvkrlvk aghtvtvekg agilsripda dfegagasiv
       61 taaagsgkad vvlkvrrpts pelkkykkga aviavmdpyd aekalgemak aglsafamel
      121 mpritraqsm dvlssqanla gyqavieaaa aydrampmmm taagtvpaak vfvmgagvag
      181 lqaiatarrl gavvtatdvr paakeqvasl ggkfiavede efkaaetagg yakemskeyq
      241 akqaelvaeh iakqdivitt alipgrpapk lvskkmldam kpgsvlvdla verggnvega
      301 kanetvttrn dvkvigianm pgqvaasasl lyaknvlafl etlvdgesga lninrddelv
      361 aatllthdga lvhprfgges paaadkgeka dg
//
LOCUS       WP_109808380             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Stakelama
            portus].
ACCESSION   WP_109808380
VERSION     WP_109808380.1
KEYWORDS    RefSeq.
SOURCE      Stakelama portus
  ORGANISM  Stakelama portus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Stakelama.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Stakelama portus"
                     /db_xref="taxon:2676234"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38641
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlketa agerrvsatp etvkkfialg atvaveagsg dtascadasy tdagatigsr
       61 aevladadiv lgvqgpapds laglkqgawi vaglnpfger ervdayaqlg aealamefmp
      121 ritraqsmdi lssqsnlsgy kavldaasey grafpmmmta agtvsaarlf vmgvgvaglq
      181 aiatarrlga qvsatdvraa tkeqiqslga kpifvenvkg iegegtggya temsdeykaa
      241 qaelvsshia kqdivittal ipgraaprli tdaqvatmkp gsvivdlave qggnvegsva
      301 gevvekhgvk ivghknvpsr laadssalfa rnlynflsaf wdkdagrpvl pdgdeigdai
      361 rltrdgkvvn arll
//
LOCUS       WP_109760228             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Silicimonas algicola].
ACCESSION   WP_109760228
VERSION     WP_109760228.1
KEYWORDS    RefSeq.
SOURCE      Silicimonas algicola
  ORGANISM  Silicimonas algicola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Silicimonas algicola"
                     /db_xref="taxon:1826607"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55526
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigapkesa agearvamtp qsardlqklg yecliekgag ekagftdaay qeagvkvvtg
       61 anlwkeadiv akvqppseae akklkegqtl isffwpaqng almetakaqg anviamdmvp
      121 risraqkmda lssmaniagy ravieagnnf grfftgqita agkvppakvl vigagvagla
      181 aigtatslga ityafdvrpe vaeqiesmga qfvyldfeet sqdgaatggy aapsspefre
      241 kqlekfrela pevdivitta lipgrdapvl wtqdmveamk pgsvivdlaa erggnceltv
      301 kdqkivtdng vtivgytdfp srmatqssll ystnvrhmmt dltpakdgqv vhnmeddvir
      361 gatvthggdi twpppppkvp aiaaqpkkdk pkeltveerr akekadfada tkrqvtllvv
      421 gaavmlmiga yapesfmshf ivfalacfvg fqviwnvsha lhtplmavtn aisgiivvga
      481 llqigassll vvllsfvgvl iasinivggf qvtrrmlamf qks
//
LOCUS       WP_109795230             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Minwuia
            thermotolerans].
ACCESSION   WP_109795230
VERSION     WP_109795230.1
KEYWORDS    RefSeq.
SOURCE      Minwuia thermotolerans
  ORGANISM  Minwuia thermotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Minwuiales; Minwuiaceae; Minwuia.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Minwuia thermotolerans"
                     /db_xref="taxon:2056226"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55042
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkevh dgerrvaltp svarqiaklg yslavesgag ehadfsdeay reagvevles
       61 ardvwassdi vlkvrapeqh psgvheteml regqtlmsfv wpaqnpelme kmaarkasvi
      121 amdavprisr aqkldalssm aniagyravv eaanhfgrff tgqitaagkv ppakvmviga
      181 gvaglaaiga arglgavvra fdtrpevreq iesmgaefle ldfeeegsgq ggyakemske
      241 fidaemalfr eqcadvdivi ttalipgkpa pkliladmve tlkpgsvivd laaeqggnce
      301 ltepgqvvvr hgvtiiglvd lpsrlaaqss qlyasnlrhf lddltpakdg qpnhnmddvv
      361 irgatvikdg eitwpppave vaakpkaaap lpkpeakpek krpgagslva maagalallg
      421 lgtvapadfm ahltvfvlac fvgyqviwnv tpalhtplms vtnaisgiiv igallqvssp
      481 swivtalafv avliatinic ggfwvtqrml gmfrkdeake
//
LOCUS       WP_109811243             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Meridianimarinicoccus roseus].
ACCESSION   WP_109811243
VERSION     WP_109811243.1
KEYWORDS    RefSeq.
SOURCE      Meridianimarinicoccus roseus
  ORGANISM  Meridianimarinicoccus roseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Meridianimarinicoccus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Meridianimarinicoccus roseus"
                     /db_xref="taxon:2072018"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55197
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgvireve pgearvaltp asaaqlaklg ydcvvetgag aaagitdday seagvevlpd
       61 aaavfaaadv iakvrppqeg eidqlregqt ligffwpaan ealmeraker gatviamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aivrafdvrp evaeqiesmg aeflfldfed sqdsagsggy aapsspefre
      241 aqlklfreqa pevdivitta lipnreapel wtpdmveamk pgsvivdlaa erggnckltv
      301 kdekivtdng vtiigytdfp srmaaqssal ystnvrhmma dltpekdgkv vhnmeddvir
      361 gatithqgei tfpppppkvk aiaaapkkek akeltpeekr aaelaafkaq trqqvtllav
      421 gaalllavgl vapasfmqhf ivfvlsvfvg fqviwnvshs lhtplmaitn aissiiilga
      481 lmqigsgsfl vivlaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_109825948             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leucothrix
            arctica].
ACCESSION   WP_109825948
VERSION     WP_109825948.1
KEYWORDS    RefSeq.
SOURCE      Leucothrix arctica
  ORGANISM  Leucothrix arctica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Thiotrichaceae; Leucothrix.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Leucothrix arctica"
                     /db_xref="taxon:1481894"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53871
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpketh kgerrvattp dvatqllklg ftvsveagag aeasytdaay iaagceiies
       61 akdlwaksdi ilkvqapead evsllhsgqi licflwpaqa pellnklsel evtaiamdsv
      121 prisraqkmd arssmanisg yraiieaaeh fgrffagqit aagkvspakv lvigagvagl
      181 saigtaksmg aivrsfdtrp evkeqiesld aeflmldfkn eggsgeggya kvmsdefiqa
      241 emalfakqak dvdiivttal ipgkpapkli taemvksmkq gsvivdlaae qggncelavp
      301 gevtvkhgvs iiaytdlpsr maaqssqlyg tnlrhllhdm tpqkdgevvv nmedqvvrga
      361 vickegkitw pppaptlsvk pkkpvvapap ivaekkkspt gaiigaaiaa vallavgsva
      421 padfmahftv fvlacfigyt viwnvspslh tplmsvtnai ssiivigali qissedntik
      481 wiavftllit ginmvggfav thrmlnmfrk
//
LOCUS       WP_109835762             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leucothrix
            pacifica].
ACCESSION   WP_109835762
VERSION     WP_109835762.1
KEYWORDS    RefSeq.
SOURCE      Leucothrix pacifica
  ORGANISM  Leucothrix pacifica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Thiotrichaceae; Leucothrix.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Leucothrix pacifica"
                     /db_xref="taxon:1247513"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55777
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkisvpkevt sgerrvattp dvvtqllklg ysvevetkag epanfsdeay eaagasiapd
       61 tkscwdngdi ilkvnqptea eealmhegqt lisffwpaqn eeqlarfaek kvnviamdav
      121 prisraqkmd alssmaniag yravveasnh fgrfftgqit aagkippakv liigagvagl
      181 saigaatsmg aivrsfdtrp evkeqvesmg aeflllefee deaggteggy aktmskefid
      241 aemalfreqa kevdiiitta lipgrpapkl iladmvemmk pgsvivdlaa qqggnceltv
      301 pgevavkhdv tligytdlts rlatqssqly gtnlrhmltd ltpekdgkin idmeddvirg
      361 atvtkegkit wpppqisvsa appaaakpav epkpeptkee lraeakkkat itlatvfgli
      421 afilwigsva ppafmghliv fvlaifvgwq viwnvspslh tplmsvtnai sgiivigail
      481 qigspsgivv ilaaiavlia siniaggflv tqrmlrmfsr eed
//
LOCUS       WP_109868308             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_109868308
VERSION     WP_109868308.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53571
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqlmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_109872103             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Falsiroseomonas bella].
ACCESSION   WP_109872103
VERSION     WP_109872103.1
KEYWORDS    RefSeq.
SOURCE      Falsiroseomonas bella
  ORGANISM  Falsiroseomonas bella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Falsiroseomonas.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Falsiroseomonas bella"
                     /db_xref="taxon:2184016"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38244
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,279..280,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvavlrerr aaetrvaatp etvkkliglg ntvavetgag masgipdsay aeagaeiaad
       61 pgaalagagi vlavrapeaa elakiprgal ligtlqadaa aakayaeagi dacamellpr
      121 itraqsmdvl ssqanlagyr avieaaetfd rgfpmlmtaa gtipaanvfi mgagvaglqa
      181 iatarrlggr vsatdvrpaa keeikslgas fvgyedeesk aaqtaggyak qlsaefyakq
      241 aevvaghiak qdivvttalv qgrkaptlvt eamvhsmkpg svivdiasda ggnvaltkpg
      301 eavttangvk ilgwsnwpgr iagassalya rnlltflttf wdkegkkpal keddeivkgv
      361 altragavvh pslasa
//
LOCUS       WP_109895641             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium durans].
ACCESSION   WP_109895641
VERSION     WP_109895641.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium durans
  ORGANISM  Methylobacterium durans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Methylobacterium durans"
                     /db_xref="taxon:2202825"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39500
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsevd paeprvaavp etvkkfiglg advvvqsgag lkagvpdgey eaagatvaps
       61 aeetardadl vlkvrrpaae elpllkkgaa vvaimdpygh eaelkamada gvaafamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrsmpmmmt aagtvpaarv fimgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsaeyqk
      241 kqaelvkghi akqdivitta lipgrpapkl iseemvasmk pgsvlvdlav erggnvagak
      301 ageivttdkg vkivghtnva grlaatasal yarnlyafle tlidketkal aikwddelvk
      361 atnltrdgev vhasfqpkaa
//
LOCUS       WP_109907105             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Zavarzinia
            aquatilis].
ACCESSION   WP_109907105
VERSION     WP_109907105.1
KEYWORDS    RefSeq.
SOURCE      Zavarzinia aquatilis
  ORGANISM  Zavarzinia aquatilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Zavarziniaceae; Zavarzinia.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Zavarzinia aquatilis"
                     /db_xref="taxon:2211142"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39296
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaipkerr pnekrvaasp esvkklialg aeivietgag lasaitdaaf eaagakvapd
       61 aastiagadv vfhvqrpmpd elahfkrgav liaglnpyad rdsvkayada gidafamefv
      121 pritraqsmd ilssqanlag yravieaaae ysraipmmmt aagtvapara limgvgvagl
      181 qaiatakrlg aivsatdvrp atkeqveslg gtfvavmdde fknaqtaggy akemskdyqa
      241 kqaaliadti kkqdivitta lipgrpapvl vsaemvatmk pgsvivdlav eqggncplsk
      301 pgevvvtdng vkivgilnlp sricvdasql faknllnfit plvsketkql aidwedeiik
      361 asiltkggav vhpafvaa
//
LOCUS       WP_109912716             477 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Providencia].
ACCESSION   WP_109912716
VERSION     WP_109912716.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Providencia"
                     /db_xref="taxon:586"
     gene            1..477
                     /gene="nrfA"
     Protein         1..477
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53365
     Region          11..477
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 manirnnalc llslvagifl ftsvhaqtpt kdststinar netfeaahpd qyhswratse
       61 qsnredalae dprlvvlwag ypfsrdynkp rghayaiidv retlrtgapk daqdgplpma
      121 cwsckspdva rliqehgedg yfegkwakgg pevvnvlgca dchktdsedf akgkpeltls
      181 rpyaeramea igkpfdkasr fdqqsmvcgq chveyyfsgd kkavkfpwdn gtkvedmevy
      241 ydnigfsdwt nslskapmlk aqhpeyetws agihgknnvt cidchmpklq nekgelytsh
      301 kignpfdnfe qtcstchtqs kqqlqdvvae rkvaiqemki kaedqlvrah feakaawdag
      361 atedemkpil tdirhaqwrw dlaiashgih mhapdeglrm lggsmdkaad artklarllg
      421 skgitheiai pdistkekaq qaigldmqki naekqeflkt vvpqwddqar kndllak
//
LOCUS       WP_109922431             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Zavarzinia
            compransoris].
ACCESSION   WP_109922431
VERSION     WP_109922431.1
KEYWORDS    RefSeq.
SOURCE      Zavarzinia compransoris
  ORGANISM  Zavarzinia compransoris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Zavarziniaceae; Zavarzinia.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Zavarzinia compransoris"
                     /db_xref="taxon:1264899"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39486
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaipkerr pnenrvaasp esvkklialg aeivietgag iasavpdaaf eaagariapd
       61 aastiagadv vfhvqrplpe elqhfkrgav liaglnpyad rdsvkayaea gidafamefv
      121 pritraqsmd ilssqanlag yravieaaae yarafpmmmt aagtvapart limgvgvagl
      181 qaiatakrlg aivsatdvrp atkeqveslg gtfvavmdee fknaqtaggy akemskdyqa
      241 kqnaliadti kkqdivvtta lipgrpapvl vtpemvatmk pgavivdlav eqggncplsr
      301 pgevvvteng vkivgiinlp srisvdasql faknllnfit plvsketkql aidwedeiik
      361 asiltkggav vhpafaaa
//
LOCUS       WP_109951433             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium radiodurans].
ACCESSION   WP_109951433
VERSION     WP_109951433.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium radiodurans
  ORGANISM  Methylobacterium radiodurans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Methylobacterium radiodurans"
                     /db_xref="taxon:2202828"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39687
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd aaeprvaavp etvkkykalg advvvqsgag lsagvpdaey eavgatvaas
       61 aedaardadl vlkvrrpsae eakllkrgat vvaimdpygr edelkvlada gldtfamefm
      121 pritraqvmd vlssqanlag yravidgaae ygrsmpmmmt aagtvpaarv fimgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsaeyqr
      241 kqadlvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 ageivttang akivghlnvp grlaatasal yarnlyafle tlidkeskal aikwddelvk
      361 atnltrdgqv vhpsfqpkaa
//
LOCUS       WP_109961411             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium terrae].
ACCESSION   WP_109961411
VERSION     WP_109961411.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium terrae
  ORGANISM  Methylobacterium terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Methylobacterium terrae"
                     /db_xref="taxon:2202827"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39310
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd paeprvaavp etvkkykalg aevivqsgag lkagvpdaey eaagasiapd
       61 araaaegadv vlkvrrpgad elpalkrgai vvaimdpygh eaevkamada gvaaiamelm
      121 pritraqvmd vlssqanlag yravvdgaav ygralpmmmt aagtvpaari fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedde fkqaetaggy akemsaeykk
      241 kqaelvashi akqdivvtta lipgrpapkl vtadmvaamr pgsvlvdlav erggnvegvk
      301 adevveterg vkivgyanvp grlaatsssl yarnlyafve tlvdkaskal avkwddelvk
      361 atcltrdgav vhpnfqpkaa
//
LOCUS       WP_109973113             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium sp. 17Sr1-1].
ACCESSION   WP_109973113
VERSION     WP_109973113.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. 17Sr1-1
  ORGANISM  Methylobacterium sp. 17Sr1-1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Methylobacterium sp. 17Sr1-1"
                     /db_xref="taxon:2202826"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39346
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd paeprvaavp etvkkykalg aevtvqsgag lkagvpdaey eaagasiaad
       61 akaaadgadi vlkvrrpaed elpalkrgai viaimepygh eaevkamada gvsaiamelm
      121 pritraqvmd vlssqanlag yravvdgaav ygralpmmmt aagtvpaari fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedde fkqaetaggy akemsaeykk
      241 kqaelvashi akqdivvtta lipgrpaprl vtadmvsamr pgsvlvdlav erggnvegvk
      301 adevvetqng vkivgyanvp grlaatsssl yarnlyafve tlvdkgskal avkwddelvk
      361 atcltrdgav vhpnfqpkaa
//
LOCUS       WP_109987358             440 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Brucella/Ochrobactrum group].
ACCESSION   WP_109987358
VERSION     WP_109987358.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..440
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45465
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke sdpsetrvaa saetvkkfia lgfdvvvekg ageksripda eftaagarig
       61 taadaktadv vlkvrrptda elkgyksgaa lfamldpygh edavaalaka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedde fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vskemvasmr pgsvlvdlav erggnvegav
      301 ageiadvngv rivghlnvsg riaasasqly arnliafvet lvdkeakllk idpeeelvka
      361 tllthqgkil hpafakveta aapagvekaa kpkaepkpka ekpaakavap kaaakpakka
      421 pakapkttss pkspvdggea
//
LOCUS       WP_110017057             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Plasticicumulans acidivorans].
ACCESSION   WP_110017057
VERSION     WP_110017057.1
KEYWORDS    RefSeq.
SOURCE      Plasticicumulans acidivorans
  ORGANISM  Plasticicumulans acidivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Candidatus Competibacteraceae; Plasticicumulans.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Plasticicumulans acidivorans"
                     /db_xref="taxon:886464"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39755
     Region          3..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtlrlvvpke tfpgerrval dpsvagrfak lgaevqvers agksshfsdv qyeeasaslf
       61 ddaaqamsaa dvvvkvqppt leeverlheg avllgflaph rnpelvkrlr dkkitsfafe
      121 llprisraqs mdalssqasi agykvalmaa elasfffpml ttaagtirpa kvvvvgagva
      181 glqaiatckr lgamveaydi raaakeqves lgaklidtgv dasgqggyar eltkeeiakq
      241 aevlarhiaa asavittaai pgraapkivt kamvegmkag svivdlaaes ggnceltepg
      301 ktieyndvii hgplnvpsmi pvhasetysk nvfnflspfv kdgqltldwn devviksclt
      361 hdgairhept rkavgg
//
LOCUS       WP_110036959             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            neocaledoniensis].
ACCESSION   WP_110036959
VERSION     WP_110036959.1
KEYWORDS    RefSeq.
SOURCE      Nocardia neocaledoniensis
  ORGANISM  Nocardia neocaledoniensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Nocardia neocaledoniensis"
                     /db_xref="taxon:236511"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38084
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mettqnvgeg sprgarvgvv resgagerrv alvpkiipal tkqgvevvve agaglgalip
       61 daayveagat igdpwsaevv vkvappsdae vaklssgqtl igflaprnad nqigalksag
      121 vqafaveaip risraqvmda lssqanvagy kavllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rttgydvrpe vadqvrsvga qwldlgidaa geggyarelt
      241 eeekakqqqa ledaikgfdv vittalvpgr paprlvtaaa vegmkpgsvi vdlagetggn
      301 celtepgevv vkhevtiasp lnlpatmpeh aselysknia allelmlvdg klapdfsdqv
      361 ladscvtrev ea
//
LOCUS       WP_110057472             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga sp. S165].
ACCESSION   WP_110057472
VERSION     WP_110057472.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga sp. S165
  ORGANISM  Chitinophaga sp. S165
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Chitinophaga sp. S165"
                     /db_xref="taxon:2135462"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39997
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miagvlkeqp genrvslvpd ivkqlgkqgv tvwiepdagt rayypdesyv qagavlksat
       61 eilqqadiil siqipaeqaw ksipagkvlt giyqpfnnaa tmqqwadrql ttfsldsvpr
      121 ttraqsmdvl ssqaniagyk avllaawsys rylpmfmtaa gtiapakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevvslgar fievegaada snaggyaveq tdaykqrqqd
      241 kiaesiaksd ivittaqipg rkapllitae mlermragav ivdlaaatgg ntaftennkt
      301 vvhngvtiig dsnlsssmps dasklyakni fnflqllvkd gnlvlnfsdd ivqgaciths
      361 gnitserlrq adsvkl
//
LOCUS       WP_110069355             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            sp. A11-A].
ACCESSION   WP_110069355
VERSION     WP_110069355.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. A11-A
  ORGANISM  Halomonas sp. A11-A
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas sp. A11-A"
                     /db_xref="taxon:2183985"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55752
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaprela kgearvaltp dsaqfiqklg hdcliesgag vaagfddqay rdagvtvvdg
       61 aealwaeaev vikvrepeea evkrlrqgqt lisffwpaqn eellekcraq gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvpparv lvigagvagl
      181 aaigtavslg avvrafdvrp evaeqiesmg aeflfldfee sqdgsatggy aapsspefre
      241 kqlalfreqa pdidivitta lipgrpapkl wleemvaamk pgsviidlaa ekggncdltr
      301 pdervvtdng vivigytdfp srmatqasll yatnirhmlt dltpekdgqi vhdmeddvir
      361 gatvthagei tfpppppkvk aiaaakpkpr ekaptpeekr aaelatfreq trrqvtllgv
      421 ggalmlllgq iapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgiiilga
      481 ilqigsgsgi vmllaaisvm iatinivggf mvtrrmlamf qks
//
LOCUS       WP_110097302             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            vulnificus].
ACCESSION   WP_110097302
VERSION     WP_110097302.1
KEYWORDS    RefSeq.
SOURCE      Vibrio vulnificus
  ORGANISM  Vibrio vulnificus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio vulnificus"
                     /db_xref="taxon:672"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54522
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvprell agetrvaasp ssveqliklg fdvvvetqag alasfddsay essgakmvsk
       61 eeawnselil kvnapiidee ksideialik egatlvsfiw paqnpqlmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvfvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaeflsv dyqeaagsgd gyakemsddf
      241 nkkaaelyaa qakdvdiiit talipgkpap klitkemvds mkagsvivdl aaanggncey
      301 tvanqvitta ngvkvigytd mvgrlptqss qlyatnlvnl fkllckekdg ninidfedvv
      361 lrgvtvvkdg eitwpappiq vsaqpqakpk avekpapkvq epvspvkkla glavavgafa
      421 wiasvapaaf lthftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngavtflaf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_110124049             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            bronchiseptica].
ACCESSION   WP_110124049
VERSION     WP_110124049.1
KEYWORDS    RefSeq.
SOURCE      Bordetella bronchiseptica
  ORGANISM  Bordetella bronchiseptica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella bronchiseptica"
                     /db_xref="taxon:518"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38862
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpketr dgetrvaatp etvkkyiggk hsvivergag vaahypdsay eeagatlgta
       61 etalgcelvl kvrapadnel phmkrgavla gmldpfdadg lqrlaaaglt afaleaapri
      121 traqsldvls sqanlagyka vllaanyygr llpmmmtaag tlkaarvvvl gagvaglqai
      181 atarrlgavv easdvrpaak eqieslgakf idvpfetdee reiaqgvggy arpmppawma
      241 rqaelvaqrc kqadivitta lipgrpaptl ltaetvqamk pgsvvvdlav erggncpltq
      301 kglvadhhgv tlvgltnlpg mlptdasaly arnlldflkl ivdaegalai rrddeivtac
      361 lmceggqvtw rs
//
LOCUS       WP_110125942             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cryobacterium arcticum].
ACCESSION   WP_110125942
VERSION     WP_110125942.1
KEYWORDS    RefSeq.
SOURCE      Cryobacterium arcticum
  ORGANISM  Cryobacterium arcticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Cryobacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Cryobacterium arcticum"
                     /db_xref="taxon:670052"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38639
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvgigrerr dgekrvaatp etvtqliglg vdvtvesgag lasgysdaay ekagahlata
       61 fdatafdvlc hvrpltpela atlragtitv glaspaselp tvaalaaaqi tsfalelvpr
      121 israqsmdal tsqalvagyr avleatirfp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsaydvrpas adevtsmggt fitldldave gtggyatela edratrqrel
      241 laphvakadv littaaipgr papllvtrdm vaampagsvv idlaaetggn vegviagadq
      301 lvpttagdga vtlvgmqdaa samafdasrl yaknvanlla lmthdgevvp dyadeviaga
      361 cltaggevrh aptaaalegk n
//
LOCUS       WP_110143084             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            qingyii].
ACCESSION   WP_110143084
VERSION     WP_110143084.1
KEYWORDS    RefSeq.
SOURCE      Legionella qingyii
  ORGANISM  Legionella qingyii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Legionella qingyii"
                     /db_xref="taxon:2184757"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40505
     Region          10..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mmiatllapd netrvaitpg sakhfiklgf dvaieknagl aasfndrdye qvgvqirdkk
       61 niletanill cinepapqdl eglpqgalvi ghidndpqsk litwckekqv tlismnlipr
      121 israqsmdsl ssqanlagyr avleacsefh raipmmmtaa gmiqpakvlv lgagvaglqa
      181 iatakrlgav vyafdvrraa keqveslgae fievsqdqds etkggyasev seeykklqae
      241 lidqyaklsd ivistalipg rkapilvykk tveqmkpgsv vvdlatargg ncevsvldkt
      301 ikheevtivg lsnlaglvpa taselyannl vhlinllapt ppeitlnpnd eiiqqavlch
      361 qnqylpfqai ketqna
//
LOCUS       WP_110140559             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_110140559
VERSION     WP_110140559.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53603
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkndllsq
//
LOCUS       WP_110167269             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio sp.
            11986-1-5].
ACCESSION   WP_110167269
VERSION     WP_110167269.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. 11986-1-5
  ORGANISM  Vibrio sp. 11986-1-5
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Vibrio sp. 11986-1-5"
                     /db_xref="taxon:2211215"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54417
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkerl agetrvaasp ssveqliklg fevviesqag slasfedsaf qaagaiiess
       61 evvwncdivl kvnapiynqq idevsllkdq atlisfiwpa qhaqlmekla mksinvlamd
      121 cvprisraqa ldalssmani agyravveaa hqfgrfftgq itaagkvppa nvfiagagva
      181 glaaigaags lgaivrafdv rqevkeqvqs mgaefleieq lptvassdgy aremsddfnq
      241 kaaelyaeqa kksdiiitta lipgkpaptl itksmvdsmk pgsvivdlaa anggnceytv
      301 kdqlittdng vkiigytdmv grlptqasql yatnlvnllk llckekngvi nidfddvvlr
      361 gvtvikqgei twpappipvs aqqpaqskpm lektakqpas pwkklvglat gvgafawias
      421 vapaaflghf tvfvlacvvg yyvvwnvtha lhtplmsvtn aisgiiivga lvqigqgngi
      481 vtflafiavl iasinifggf tvtkrmldmf rkd
//
LOCUS       WP_110174173             395 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Luteitalea
            pratensis].
ACCESSION   WP_110174173
VERSION     WP_110174173.1
KEYWORDS    RefSeq.
SOURCE      Luteitalea pratensis
  ORGANISM  Luteitalea pratensis
            Bacteria; Pseudomonadati; Acidobacteriota; Vicinamibacteria;
            Vicinamibacterales; Vicinamibacteraceae; Luteitalea.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Luteitalea pratensis"
                     /db_xref="taxon:1855912"
     Protein         1..395
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40647
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,99,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,285..286,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvigvprelv pgedrvalvp asvapliksg aavlveqgag vragcpdday aaagatlvsr
       61 dqvfaqadil lqvrtaaaag tygaadverl ssrhtvigfa dplgapetar amaargatvi
      121 smelipritr aqsmdalssm aniagykavl laaatlprmf pmmmtaagti sparvfviga
      181 gvaglqaiat akrlgakiea ydvraavkeq ieslgakfve lpldtaaaeg qggyaaaqde
      241 sfyrrqretm arvvahsdvv ittaaipgkk spvlitadmv asmppgsviv dlaaerggnc
      301 eltvadetiv ahgvtihgpt nlpatvpfha sqlyaknltt llahlrtkqg dlvidpadei
      361 trevlvthkg eviaprlreq lglaplpapv aaaav
//
LOCUS       WP_110175869             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. RW409].
ACCESSION   WP_110175869
VERSION     WP_110175869.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. RW409
  ORGANISM  Pseudomonas sp. RW409
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. RW409"
                     /db_xref="taxon:2202895"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38591
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsndt iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_110177862             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            parahaemolyticus].
ACCESSION   WP_110177862
VERSION     WP_110177862.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54723
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvviesqag vlasfddaay eaagakvvss
       61 devwasglil kvnapivdee kgmdeiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaefltv dfqedsgsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgrpap klitkemvds mkagsvivdl aaanggncey
      301 tvkdqvimtd ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvikeg eitwpappiq vsaqpqakqa qpvkkepkve eptsptkkli glvaavgtfa
      421 wiasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvsflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_110180707             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides solisilvae].
ACCESSION   WP_110180707
VERSION     WP_110180707.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides solisilvae
  ORGANISM  Nocardioides solisilvae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nocardioides solisilvae"
                     /db_xref="taxon:1542435"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52791
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresr dgetlvaata ktaeqlvglg yevvvesgag qaadlrdety aeagirvada
       61 tevwssdvvv kvnaptadev armrrgatvv slmaparspe lldqlqaagv tglamdavpr
      121 israqsmdvl ssmanvagyr avveaahafg rqftgqvtaa gkvpparvfv vgagvaglaa
      181 igaagamgai vrafdvrpev aeqvqsmgae fvtvdmeaev ssdgyakemt aeqekatavm
      241 ydeearhadi vittalipgr paprlisaet vsrmkpgsvv vdmaaanggn veltvkdekv
      301 vtenlvtilg ytdlagrlaa qtsqlygtnv vnlfklltpg kdgelvldmd dvvqrgitvv
      361 rdgesmwppp pvqvsaapaa appapvepaa pkpppdprrk vfaaalaava faalatvspg
      421 aflnhftvfa lavfvgyyvi snvahalhtp lmsetnaisg iivvggilqv gsesllvsal
      481 avlavlvasi nifggflvtl rmlemfrkd
//
LOCUS       WP_110190114             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pokkaliibacter plantistimulans].
ACCESSION   WP_110190114
VERSION     WP_110190114.1
KEYWORDS    RefSeq.
SOURCE      Pokkaliibacter plantistimulans
  ORGANISM  Pokkaliibacter plantistimulans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Balneatrichaceae; Pokkaliibacter.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Pokkaliibacter plantistimulans"
                     /db_xref="taxon:1635171"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55067
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeih hgearvattp evaaqlqklg yhislesgag eaakyrdedy aavgveivtd
       61 aqalwqnadi ilkvrapqhh prlnvheadl lhagqtlvsf mapgqntall etlasknina
      121 laidmvpris raqkmdalss maniagyrav veaaqhfgrf ftgqitaagk iapakvlvig
      181 agvaglaaig taksmgaivr afdtrpevke qvesmdaefl mldfkedgsg sggyaktmsk
      241 efieaemalf aeqakdvdii ittalipgkp apelitedmv ksmkegsviv dlaaeqggnc
      301 klseadkvvv khgvtligyt nlpsrlasqa sqlyatnlrh lltdmtpgkd gilqinfddd
      361 vvrgatvvka geitfpppap klsakpaapk psvskaprqe ekkehkhssp lwliagalvf
      421 lllgmtapas fmghftvfil scfvgymviw nvtpslhtpl msvtnaissi iiigallqis
      481 apsgwvvffa aiavlltsin ifggfavtqr mlamfrk
//
LOCUS       WP_110215324             308 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Enterobacteriaceae].
ACCESSION   WP_110215324
VERSION     WP_110215324.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..308
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35615
     Region          5..168
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiydlfskr qkrlrgdvpd vyqytnlpqn frvqvvhivk stigrdsdys tpaskiykyi
       61 nntlcreygv fklqeyasen feyiynfflk ekdpekcldv ieltfkcidg yvrqntwefr
      121 dyqspddaie elnirfreag igyqfesgev vrvdsqfihs davkptlqil ghsqefagan
      181 deflsahehy rhqrfkecln dclksfeslm kaihkkrswe ygstdtakkl issclsngli
      241 pdymqnqfss lrillesgvp tirnkegghg qgdevtnvpe hlasytlhlt asnllflakc
      301 denftkkk
//
LOCUS       WP_110240508             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides gilvus].
ACCESSION   WP_110240508
VERSION     WP_110240508.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides gilvus
  ORGANISM  Nocardioides gilvus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nocardioides gilvus"
                     /db_xref="taxon:1735589"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52824
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipreaw pgeslvaata ktadqlvklg yevvvesdag qaadqpdhvy eeagitvvdr
       61 atawssdvvv kvnaptdeei gqmrrgatvi simaparnpe lidkftdagl talamdavpr
      121 israqsmdvl ssmanvagyr avieaanefg rmftgqvtaa gktaparvfv vgagvaglaa
      181 igaasamgav vrafdvrpev aeqvesmgae fvkvdmksev ssdgyaremt aeqeaatalm
      241 ydeearnadi vittalipgr papklitaet iaamrggsvi vdmaaanggn aaltvtgert
      301 vtdngvvilg ytdlagrlaa qtsqlygtni vnllklltpg kdgqltldfd dvvqrgitvt
      361 ldgesmwppp pvqvsaapaa aapaavapae pkkpanpmtk vyaaaggavl fgvlamfmgd
      421 qllqqltvlm lsvfvgyyvi snvahalhtp lmaetnaisg iilvggilqv gspnllvtll
      481 svvailvasi nifggflvtv rmlemfrkd
//
LOCUS       WP_110255113             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Undibacterium pigrum].
ACCESSION   WP_110255113
VERSION     WP_110255113.1
KEYWORDS    RefSeq.
SOURCE      Undibacterium pigrum
  ORGANISM  Undibacterium pigrum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Undibacterium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Undibacterium pigrum"
                     /db_xref="taxon:401470"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38773
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaesr pgetrvaatp etikkyvaak hqvivqsgag vassitdeay qaagaqigta
       61 adalgaelvl kvrapnaeer almksgtvlv gmlnpfdadn iaamathgls afaleaapri
      121 traqsldvls sqaniagyka vmlaantyqr fmpmlmtaag tvkaarvlim gvgvaglqai
      181 atakrlgavi easdvrppvk eqveslgakf idvpyetdee reiakgvggy arpmpaawme
      241 rqaalvhera kqadiiitta lipgrkapil iseetvkamk pgsvivdmav eqggncplse
      301 lnktvtkygv hiigepnlat lvaadasaly arnvldflkl iidkdaalai nredeivaat
      361 lvcsagevlk k
//
LOCUS       WP_110282098             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            sp. LBP4].
ACCESSION   WP_110282098
VERSION     WP_110282098.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. LBP4
  ORGANISM  Halomonas sp. LBP4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas sp. LBP4"
                     /db_xref="taxon:2044917"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55415
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaprela kgearvaltp esaqqiqklg heclveagag taagfddnay raagvtvvdg
       61 aealwreaev vikvrepsee eagrlrqgqt liafiwpaqn ealletcraq gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 saigtatslg avvrafdvrp evaeqiesmg aeflfldfde sqdgsesggy aapsspefre
      241 kqlecfreqa pdvdivitta lipgrpapkl wladmveamk pgsvivdlaa ekggncdltr
      301 adekvvsdng vtivgytdfp srmatqasll yatnvrhmlt dltpakdgki vhdmeddvir
      361 gstvthegei tfpppppkvk aiaaakpkpk epeptpeekk aaehaaflaq tkrqvtmlgv
      421 ggalmlllgq vapvsfmqhf ivfvlacfvg fqviwgvshs lhtplmavtn aissiiilga
      481 ilqigsssfl vvlmsaiavl iasinivggf qvtrrmlamf qks
//
LOCUS       WP_110280472             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Loktanella
            sp. PT4BL].
ACCESSION   WP_110280472
VERSION     WP_110280472.1
KEYWORDS    RefSeq.
SOURCE      Loktanella sp. PT4BL
  ORGANISM  Loktanella sp. PT4BL
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Loktanella.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Loktanella sp. PT4BL"
                     /db_xref="taxon:2135611"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55598
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif egenrvamtp asakdlqklg yeciietgag laagfsdqay kdagvevvkt
       61 aaalykaadi vakvrppsda evkklregqt lisffypaqn kelmeaanak gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqvesmg aefvfldfee eqqdgsatgg yaavsspefa
      241 aaqlakfrei apdmdivitt alipgrdape lwtkdmveam kpgsvivdla aerggncklt
      301 vkdekivtdn gviivgytdf psrmaaqsst lyatnirhmm tdltpekdgt pnhnmeddvi
      361 rgatathkge itfpppppkv aaiaaapkke kpkeltaeek ranevaafkk etktqvglla
      421 igaalilgig lipgmpasfm qhfivfvlsv figfqviwnv ahslhtplma vtnaissiii
      481 lgaliqigss nalitilaal gifmaavnif ggflvtrrml amfqks
//
LOCUS       WP_110285736             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_110285736
VERSION     WP_110285736.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53576
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgg adchnpasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_110318587             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium moriokaense].
ACCESSION   WP_110318587
VERSION     WP_110318587.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium moriokaense (Mycobacterium moriokaense)
  ORGANISM  Mycolicibacterium moriokaense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Mycolicibacterium moriokaense"
                     /db_xref="taxon:39691"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52212
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgetrvaatp qtvgqliklg yevvveagag aassfsdaaf teagagvgsa
       61 eqvwaadvvl kvnapdnaei aavrdgatli glispalkpe lvdqlatrpi tvlamdavpr
      121 israqsldvl ssmaniagyr avieaankfg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 vgaagslgai vratdprpev adqvkslgge ylsiespeae vsatgyakem gddykareaq
      241 lyaeqskdvd iiittalipg kpapriitad mvasmksgsv lvdmaaangg nvegtvkdqa
      301 ivtdngvtii gytdlagrlp atasqlygtn lvnllklltp dkdgklildf edvvqrsvtv
      361 vrdgeitwpp ppvqvsaapv ataapveakp akehmttarr lgltfaaaav lfalialspa
      421 alqvhltvfa laivigyyvi gnvhhalhtp lmsvtnaisg iivvgallqi ghgdvvital
      481 atlaillasi nvfggfavtr rmlamfsrs
//
LOCUS       WP_110313077             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aquitalea
            magnusonii].
ACCESSION   WP_110313077
VERSION     WP_110313077.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea magnusonii
  ORGANISM  Aquitalea magnusonii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Aquitalea.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Aquitalea magnusonii"
                     /db_xref="taxon:332411"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38840
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqiaipaerl agekrvaatp etvkkliamg hsvvveqgag qfaaapdaay aelgasiaan
       61 raealgqadi vltvrpldea giaelktgav ligqlapyqn ssfpalaakk vsafalellp
      121 rttraqsmdv lssqnniagy kavllathyy prfmpmlmta agtvkpakvl imgvgvaglq
      181 aiatakrlga vveatdvrps tkeqveslgg kfievpmtde ekaasdgvya kemsddykrr
      241 qaelvskhar aadiiittal ipgkkaptli sadivaamkp gsviidiaae aggncaltqp
      301 gevvvtdnhv tvvgqfnlpg qlaadassly aknlltflsl mltkegftln leddllaatl
      361 vthdgqvrfp aan
//
LOCUS       WP_110328010             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia tropica].
ACCESSION   WP_110328010
VERSION     WP_110328010.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54456
     Region          3..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mamtiavpre sqqderrvaa tpesvaqlik lgyeievetg agerasypdd ayrqagaclv
       61 ddalelwsna divlkvrpps tdevqrlktg atligfiwpa qngalleaca vrgvtvlamd
      121 cvprlsraqk ldalssmanm agyravieaa qhfgrlftgq itaagkmppa kvlvigagva
      181 glaaigaarg lgaivrafdt rpevgqqves mgaeflsvdv dedgggtggy akqmsakfie
      241 aemalfeaqa revdiiitta lipgkpaprl idaktaacmr agsvivdmaa eqggnceltr
      301 agevvqahgv tvigytdlps rmanqssqly atnlrhlltd ltplkngalt idmndvvqrg
      361 ttvmqqgnlc wppppvqtpa aqpqaapnap vhvaaaghaq pstqdarkhg awslgmliig
      421 allllalgav appafvahft vfvlavfvgy qvvwnvtpal htplmsvtna isgiivigal
      481 lhpggsstia svlagialvv atiniaggfl vtqrmlnmfq rt
//
LOCUS       WP_110339883             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitrosomonas sp. Nm84].
ACCESSION   WP_110339883
VERSION     WP_110339883.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas sp. Nm84
  ORGANISM  Nitrosomonas sp. Nm84
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Nitrosomonas sp. Nm84"
                     /db_xref="taxon:200124"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39453
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,95,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipaeir ggetrvaatp etvkkftakg vhkvsvqsga gagasipdsa yqeagativt
       61 dvaelyaqsq iilkvrgpes nelammrkda vllgllsphq kdgiealaqy gltafamekl
      121 prisraqnmd vlssqaniag ykavimaadv yqrffpmlmt aagtvkaarv lilgagvagl
      181 qaiatakrlg avveafdvrp vakeqveslg akfvevplsd eekakaetag gyatemsddy
      241 krrqgelvhe raivadiiit talipgrpap vlikeetvra mkpgsvivdm aveaggncpl
      301 selnetvvkh gvnligiani pglvaadsst lyarnlmnfl nlmldpesge lkidrgdeii
      361 agtlvcagge iiskps
//
LOCUS       WP_110342385             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Prauserella flavalba].
ACCESSION   WP_110342385
VERSION     WP_110342385.1
KEYWORDS    RefSeq.
SOURCE      Prauserella flavalba
  ORGANISM  Prauserella flavalba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Prauserella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Prauserella flavalba"
                     /db_xref="taxon:1477506"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38565
     Region          12..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtetesptgs tltigvvket kpgerrvalv pklierltrr glkvvvepga gagaqladdv
       61 fteagattgd awsadivltv vppsiadier lkpgtvligf lapltntdev aamkkagita
      121 favesipris raqgmdalss qanvagyrav llaaqrlpkf fpmlttaagt vppakalvlg
      181 vgvaglqala takrlgaqat gydvrpevae qvrsvgaqwl dlgieaageg gyarelteee
      241 rarqqqrlte aiggfdvvit talvpgrkap tlvtaeavrg mkagsvivdm agetggncel
      301 tdpgkdivah dvticsplnl paempvhase lyarnltell elivdtdgkl aidfsdevva
      361 gacvagrdee vn
//
LOCUS       WP_110350055             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium sp. B4].
ACCESSION   WP_110350055
VERSION     WP_110350055.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium sp. B4
  ORGANISM  Methylobacterium sp. B4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Methylobacterium sp. B4"
                     /db_xref="taxon:1938755"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39535
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavltetd pieprvaavp etvkkfiglg cdvvvqsgag tkagvpdgey eaagakiags
       61 aeealsgadl ilkvrrpnad elakiqkgat vvaimdpygh edelksaaea gvdtfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrslpmmmt aagtvpaari fimgvgvagl
      181 qaiatarrmg avvtatdvrp atkeqveslg akfvavedde fkqaetsggy akemsaeyqk
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 ageivtvgng vkivghvnvp grlaatassl yarnlyafve tlidkeaktl avkwdddlvk
      361 atnltrdgqv vhpnfqpka
//
LOCUS       WP_110356747             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arenibacter sp. ARW7G5Y1].
ACCESSION   WP_110356747
VERSION     WP_110356747.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter sp. ARW7G5Y1
  ORGANISM  Arenibacter sp. ARW7G5Y1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Arenibacter sp. ARW7G5Y1"
                     /db_xref="taxon:2135619"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39855
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigilketl dgerrvaitp iiakqlrasg fevlieegag enssfkdsdy knvevavekr
       61 avvfheaeil lkinpfdeed lklvdkgqil isklyhksnp qlvqaiankg vtafsmdaip
      121 risraqdmdv lssqnnlagy kavilgafem tkifplmmts agtipparvl iygigvaglq
      181 aiatakrlga iveatdirse tkeqaeslga kfisvnnege eseggyakea sadyqkrqke
      241 avnkslfqad lvittanipg rkapilitee qvmqmkngav iidlaaaqgg ncevsqinkt
      301 ivkngvkvig tsidprsvst nasdlyakni ynyimhltee thfkwdldeq itdetlivkn
      361 gtirkn
//
LOCUS       WP_110374729             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chelatococcus asaccharovorans].
ACCESSION   WP_110374729
VERSION     WP_110374729.1
KEYWORDS    RefSeq.
SOURCE      Chelatococcus asaccharovorans
  ORGANISM  Chelatococcus asaccharovorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Chelatococcaceae; Chelatococcus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Chelatococcus asaccharovorans"
                     /db_xref="taxon:28210"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38931
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mliavpaete qnegrvaatp etvkkflglg aevvvqsgag lrsgvtdady teagariaat
       61 pgetlsgadv vlkvrrpsas elplikrgal viavldpygd eaavkswada gisafsmefm
      121 pritraqvmd vlssqanlag yravidaaae ygralpmmmt aagtvpaara fimgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akqmsaeyqa
      241 kqaeltashi skqdivitta lipgrpapkl itaamvasmr pgsvivdlav erggnvegav
      301 pgevvvtang vkivghlnvp grlaatassl yaknlyafae tlidkaskal avnwddelvk
      361 ataltrdgai vhpaflpka
//
LOCUS       WP_110382509             311 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Nitrosomonas ureae].
ACCESSION   WP_110382509
VERSION     WP_110382509.1
KEYWORDS    RefSeq.
SOURCE      Nitrosomonas ureae
  ORGANISM  Nitrosomonas ureae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Nitrosomonas ureae"
                     /db_xref="taxon:44577"
     Protein         1..311
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35883
     Region          5..173
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 matfdlyskr qkalrgeihe vfkydslpst lrvqivhiwt dvlgtesqyh hyenvkfvyg
       61 eivrtlcrey glfqlptaek ykdrmyliel snyllqveei dnqldiiels fqcvemytqk
      121 ygylkrdkak esadeaiael ncrfkehgmg fqfvegeilr vdselihlev vkpalkllne
      181 nsysgaqqef lsayehyrhg nhkeslndcl ksfestmkai cekhkwpyee gatakslikv
      241 cfdnglvply wqqqlsslrs llesgistgr nklsghgqgv iptvvpdylv aymlhmtatt
      301 mvfltnaekn m
//
LOCUS       WP_110384562             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia silvatlantica].
ACCESSION   WP_110384562
VERSION     WP_110384562.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia silvatlantica
  ORGANISM  Paraburkholderia silvatlantica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Paraburkholderia silvatlantica"
                     /db_xref="taxon:321895"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54127
     Region          3..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 maltiavpre tyegerrvaa tpesvaqlik lgyvvevett agvsasypdd ayraagarvv
       61 ndahallsga divikvrpps seevqrlkpg atligfiwpa qnaalleqla areatvlamd
      121 cvprisraqk ldalssmanm agyravveaa qhfgrvftgq itaagkmppa kvlvigagva
      181 glaaigaarg lgaivrafdt rpevgqqves mgaeflsidi eeegggtggy akqmsakfie
      241 aemalfeaqa revdiiitta lipgkpaprl idaktvacmr sgsvivdmaa eqggnceltr
      301 pgevvnangv tvigytdlps rmanqssqly atnirhlltd ltpakdgels ldmddvvqrg
      361 ttvmqrgqvc wpppvqvsat pqaaaqpkpv avamgnakea aaqatrrngv gslavlvvaa
      421 llllalgava pgafvahftv fvlavfvgyq vvwnvtpslh tplmsvtnai sgiivigall
      481 hpgnagtivt vlagialvva tiniaggflv tqrmlkmfqr t
//
LOCUS       WP_110385328             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia silvatlantica].
ACCESSION   WP_110385328
VERSION     WP_110385328.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia silvatlantica
  ORGANISM  Paraburkholderia silvatlantica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia silvatlantica"
                     /db_xref="taxon:321895"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39633
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anetrvaatp etvrkyvaqg htvtiqagag agasyldeay tavgaqvada
       61 aaafgadlvl kvqsptvsel pfmkrgavlv gmldpfnaen aatlaeagvt afaleaaprt
      121 traqsldvls sqaniagyka vlvasdlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atarrlgavi easdvrpavk eqieslggkf levpyetdee reaavgvggy arpmppswla
      241 rqsalvhera kqadivista lipgrdaptl lpsetvqamk pgsvvidlaa grgpvadeas
      301 grrggncplt eadkvvthhg vqicgytnla smvaadasal yarnlldflk liltkegtln
      361 idladdivaa tllardgqvt rkt
//
LOCUS       WP_110391150             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rivihabitans pingtungensis].
ACCESSION   WP_110391150
VERSION     WP_110391150.1
KEYWORDS    RefSeq.
SOURCE      Rivihabitans pingtungensis
  ORGANISM  Rivihabitans pingtungensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Aquaspirillaceae; Rivihabitans.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Rivihabitans pingtungensis"
                     /db_xref="taxon:1054498"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38506
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqiaipaela agetrvaatp dtvkkyvalg havavqsgag rasavldday iaagatvvgd
       61 raallaaadi vltvralpae dipslkagav ligmldphrn ntlaelasrq isaftmellp
      121 rttraqsmdv lssqnniagy ravllatqfy prfmpmlmta agtvkaakvl vlgagvaglq
      181 aiatakrlga vveafdvrpa tkeqveslgg kfvevpmtde ekkandgvya kemsddykrr
      241 qgelvakhak aadivittal ipgkqapill eadvvagmkp gavivdiaae sggncpltrp
      301 gaafttdggv tvvgftnlpg mvaadassly aknlltflsl mltkegfsln leddllaatl
      361 ithqgalrfg qaa
//
LOCUS       WP_110402268             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphaerotilus hippei].
ACCESSION   WP_110402268
VERSION     WP_110402268.1
KEYWORDS    RefSeq.
SOURCE      Sphaerotilus hippei
  ORGANISM  Sphaerotilus hippei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Sphaerotilus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Sphaerotilus hippei"
                     /db_xref="taxon:744406"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38972
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpreva agetrvavtp etakklaaqg hqlvverdag rlasvpdsay eavgaqiada
       61 ahayradlvl kvrapqahel illragstmv gmldpfdreg lqrlasagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmlaantyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee qaaaegvggy arpmppswle
      241 rqqrevakrv aqadivista lipgrpaptl vteamvqamk pgsvivdiaa grgpggggnc
      301 pltvagqtvq ahgvtliget nlpalvaada salyarnvld flkliitkda tlqvpmdddi
      361 vaaclmtrdg qitrs
//
LOCUS       WP_110408192             390 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit, partial
            [Salmonella enterica].
ACCESSION   WP_110408192
VERSION     WP_110408192.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..>390
                     /gene="nrfA"
     Protein         1..>390
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
     Region          4..390
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi
//
LOCUS       WP_110421128             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia vietnamiensis].
ACCESSION   WP_110421128
VERSION     WP_110421128.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54843
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatgerrvat vpevveklik lgfavavqsg agaganfddd ayraagasia
       61 ataaelwsgs divfkvrpps adevalmreg gmligfvwpa qnpdlmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvle elckgkdgti dvdfdddair
      361 gltvikegnv twpapppkqp avapkpaaaa paaaapaksk ghghsgepms akalaivfav
      421 galafllvgq fapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapptag lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_110430287             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Glaciecola
            sp. KUL10].
ACCESSION   WP_110430287
VERSION     WP_110430287.1
KEYWORDS    RefSeq.
SOURCE      Glaciecola sp. KUL10
  ORGANISM  Glaciecola sp. KUL10
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Glaciecola.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Glaciecola sp. KUL10"
                     /db_xref="taxon:2161813"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56026
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif kgearvaitp esalalkklg yelaietkag elagfsdkay eeagveiikt
       61 aaalykevdi vakvrpptet eakrlrkdqt lisffypsan qalmelaqsk ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvflefed selpdgaetg gyappsspef
      241 qakqlekfre iaadmdivit talipnraap llwtkdmvel mkpgsvvvdl aaekggncel
      301 temdkrvvsd ngvviigytd fpsrmatqas tlygnnirhm madltpekng qvnhnmeddv
      361 irgatithqg eitfpppppk vaaiavqkke kpktltpeee kakevaefka qtknqvtllg
      421 igaalvlavg lvapasfmqh fivfvlsvfi gfqviwgvah slhtplmait naissiiilg
      481 almqigsgsy lviilsalav fmtginifgg flvtrrmlam fqks
//
LOCUS       WP_110414432             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Snodgrassella alvi].
ACCESSION   WP_110414432
VERSION     WP_110414432.1
KEYWORDS    RefSeq.
SOURCE      Snodgrassella alvi
  ORGANISM  Snodgrassella alvi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Snodgrassella.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Snodgrassella alvi"
                     /db_xref="taxon:1196083"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53996
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl agetrvaatp ktvtqliklg hevviehdag kaaslsdgly qeagatvsda
       61 gtvwqcplif kvnapnkeei aamqsgtilv sfimpaqqpe lvqqlqakki tvlamdmvpr
      121 israqamdal ssmanisgyr avieaaenfg rfftgqitaa gkvppaevlv igagvaglaa
      181 igtarqlgav vnafdtrpev adqiesmggn flqldyqeee sssgdgyakt msaayieaem
      241 klfaeqarqv diiittaaip gkpapklitr emvdsmregs vivdlaaatg gnceytepgk
      301 iittangvki igytdmanrl agqssqlygt nlvnlarllt pnkdgelaln fedviirnmi
      361 vthegnsmyp pppiqvsaap kaepkvaapa pvataqptsa nkkiiwaaia vilmlwigav
      421 apvaflnhfm vfvlacvvgy fvvwnvnhal htplmsvtna isgiivvgal lqigqghgfv
      481 sllafiavai vsvnifggfa vtrrmlnmfr k
//
LOCUS       WP_110449138             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phenylobacterium parvum].
ACCESSION   WP_110449138
VERSION     WP_110449138.1
KEYWORDS    RefSeq.
SOURCE      Phenylobacterium parvum
  ORGANISM  Phenylobacterium parvum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Phenylobacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Phenylobacterium parvum"
                     /db_xref="taxon:2201350"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38201
     Region          3..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,95,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maviaviret hpgetrvaat petvrkliaa gfevavqsga glsascpdad yaaagarlag
       61 saadavkgad ilfgirtpsa ealsalkkga ivaaslnphq draglealaa rgvdayalef
      121 ipritraqvm dvlssqanla gyravieast aygralpmmm taagtiaaak vfvmgvgvag
      181 lqaiatarrl gavvtatdvr patkeqvesl gakfiavedd efrnaqtagg yakemsaeyq
      241 akqaelvtgh igkqdivitt alipgrpapr lvtaaqvaam kpgsvlvdla veqggnvega
      301 ragetvetan gakilgipnl pgrvaadasa lfarnllafs gllldkdgal apdledeilk
      361 aalvvsggki vhpalags
//
LOCUS       WP_110455935             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            algidipiscicola].
ACCESSION   WP_110455935
VERSION     WP_110455935.1
KEYWORDS    RefSeq.
SOURCE      Shewanella algidipiscicola
  ORGANISM  Shewanella algidipiscicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Shewanella algidipiscicola"
                     /db_xref="taxon:614070"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41389
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgllkesq adekrvalip anvtrlikkn lqilvesgag esagfsdqqy qeagaiitpr
       61 eqvfeqadii tvvnckgsqf deiktlakan qlfigmmdpl ahpdnatala atgttaiale
      121 lvpritraqs mdilssmati agykavllaa hkaprmfpmm mtaagtlkpa rafimgvgva
      181 glqacatakr lgavveaydi rpaareqils vgakpveldl etentetkgg yateqsddfi
      241 krqqqamtnv laqqdivitt aaipgrkapv littamvegm kpgtiivdla aetggncelt
      301 rldetvvhng vtilgpsnvp gtaathasqm ygtnienllk llvdndgqlh ldfddeivrd
      361 tvvvhqgdvv narirsllgm pdiaapeeaq
//
LOCUS       WP_110457263             466 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella algidipiscicola].
ACCESSION   WP_110457263
VERSION     WP_110457263.1
KEYWORDS    RefSeq.
SOURCE      Shewanella algidipiscicola
  ORGANISM  Shewanella algidipiscicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Shewanella algidipiscicola"
                     /db_xref="taxon:614070"
     gene            1..466
                     /gene="nrfA"
     Protein         1..466
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52070
     Region          1..466
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvknltkktf avsalvaasl mtsgvmasdk teprnevykd kfakqynswh etaeseevvd
       61 mleqvpslvv lwagygfakd ynaprghmya vtdvrntlrt gapksdedgp mpmacwscks
      121 pdvprmieeq gedgyfkgtw hkggaeivnt igcsdchekg ssklrmsrpy adramntlgt
      181 pfdkasrkdk qsmvcgqchv eyyfektkdh kgfvkfpwdm gatveqmevy ydsieftdwt
      241 halsktpmlk aqhpgyetwq lgvhgknnvt ctdchmpkvk naegrkftdh kvgnpfdrfe
      301 eacgschtqs kefmvnltee rkvkvndlka raeaqlvrah feakaawdag aseaemkpil
      361 mdirhsqwrw dyatashgva ahaadealri lgtavdkagd ariklaqlla vkgvkqpiai
      421 pdvstkakaq aalgmdmkkm nadkeefkkt vlpkwdaeak qreaty
//
LOCUS       WP_110469407             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Williamsia
            limnetica].
ACCESSION   WP_110469407
VERSION     WP_110469407.1
KEYWORDS    RefSeq.
SOURCE      Williamsia limnetica
  ORGANISM  Williamsia limnetica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Williamsia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Williamsia limnetica"
                     /db_xref="taxon:882452"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37762
     Region          1..356
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,70,89,282,308,310)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,122..123,132..133,136..137,140..141,143..144,
                     146..151,153,155..157,160,183..184,272..273,315..316,320,
                     323..324)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(117..118,122,125,128,169..172,192..194,222,233,
                     250..252,259,261)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,122,132,175..176,183,199..200,202..205)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(152..156,159,162,185,187)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msvgvvrett agenrvalvp kvvatlvgkg vpvivesgag eaalipdqly adagasvgda
       61 wsadvvvkvd aptdaeigkl ssgssligfl aprnqenqig alkaagvqaf aveaiprisr
      121 aqsmdalssq gnvsgykavi laaekstrff pmlttaagtv kpatvlvlgv gvaglqalat
      181 akrlgarttg ydvrpevaeq vksvggqwld lgidaagegg yareltdder akqqqaleda
      241 iksfdvvitt alvpgrpapr lvtaaavegm kpgsvvvdla getggncelt epgenvikhd
      301 vlicsplnlp agmpehasel yaknilalie laldddgnfa pdfsdevlaa acvtreapts
      361 dvsgtdvkag a
//
LOCUS       WP_110572629             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinomonas alcarazii].
ACCESSION   WP_110572629
VERSION     WP_110572629.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas alcarazii
  ORGANISM  Marinomonas alcarazii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Marinomonas alcarazii"
                     /db_xref="taxon:491949"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55563
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeie dgelrvamtp siaskvkqlg fdivmesgag taasysdeay kavgveithd
       61 tkklwheanl likvrppveh pelgfygvel lgqnqtlisl ihpaqnmnkl qqlsergtnv
      121 valdavpris raqkmdvlss maniagyrav veaaqhfgrf ftgqitaagk vppakvlvig
      181 agvaglaaig aaksmgaivr afdtrpevke qvesmnaefl lldfkdedgs geggyaktms
      241 aefiaaemal faeqakdvdi iittalipgk tapelitedm vrsmkpgsvi vdlaaetggn
      301 crltqanevi dvhgvsiigy tnlpsrmaaq ssqlfatniy hlltelcpnk dgqidlnmed
      361 evirgatvvk dgsitwpppa prlsaapksd vseqlkpeka dvkakekkps afgfllpvli
      421 tgalllglgs iapaefmahm tvfvlscfvg ymvvwgvshs lhtplmsvtn aissiiviga
      481 itqvssdspi vsilaamaif itsinivggf avthrmlkmf rk
//
LOCUS       WP_110600947             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salinicola
            lusitanus].
ACCESSION   WP_110600947
VERSION     WP_110600947.1
KEYWORDS    RefSeq.
SOURCE      Salinicola lusitanus
  ORGANISM  Salinicola lusitanus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Salinicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Salinicola lusitanus"
                     /db_xref="taxon:1949085"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55368
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela kgearvaltp esaqqiqklg hecliesgag vlagfsdeay rdagvsvveg
       61 aaalwreaev vikvreplae eterlregqt litffwpaqn eenlercrak gatvvamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgagsggy aapsspefrd
      241 kqlalfreqa pevdivitta lipgrpapkl wledmvalmk pgsvivdlaa ekggncdltv
      301 pderivtdng vivvgytdfp srmatqasll yatnirhmlt dltpekdgvi vhdmeddvir
      361 gatvthagev tfpppppkvk aiaaakpkpk vkeptpeekk aadhaaflaq skrqigilva
      421 ggvlmwllgm vapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 imqigsgsgl vallaavsvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_110578086             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microcystis aeruginosa].
ACCESSION   WP_110578086
VERSION     WP_110578086.1
KEYWORDS    RefSeq.
SOURCE      Microcystis aeruginosa
  ORGANISM  Microcystis aeruginosa
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Microcystis aeruginosa"
                     /db_xref="taxon:1126"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40202
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikesd qgearvalvp dtvarlvkag fevivqngag isanfadsay savgaalsen
       61 seyiyetadi ilkvvppsds eidrlknggi ligfldplrq prriakladr gitalsmeli
      121 prssraqsmd alssqanlag ykavllaavq lpkmfpmmtt aagtiapakv lvlgagvagl
      181 qacatarrlg avveafdirp qvkeevqsvg akfiemplee dtvadngyak evslstqeri
      241 cqaltepikr advvittaqv pgkqapllvt kemiatmkag avivdlaaeq ggncaytqpg
      301 reiivngvki vgavnlpatv atnasqmyak nlqmllqllv skegslnldf addiidsacv
      361 thageirnqr iksalseqls af
//
LOCUS       WP_110634413             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Salinicola].
ACCESSION   WP_110634413
VERSION     WP_110634413.1
KEYWORDS    RefSeq.
SOURCE      Salinicola
  ORGANISM  Salinicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Salinicola"
                     /db_xref="taxon:404432"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55471
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela rgearvaltp esaqqiqklg hecliesgag rlagfddday rqagvsvvds
       61 aaslwqeadv vikvrepves eidqlragqt litffwpaqn eanlercraq gatviamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfee sqdgsgtggy aapsspefre
      241 kqlalfreqa pevdivitta lipgrpapkl wledmvaamk pgsvivdlaa ekggncdltv
      301 pderivtdng vivvgytdfp srmatqasll yatnirhmlt dltpekdgvi vhdmeddvir
      361 gatvthagei tfpppppkvk aigaakpkek vkeptpeekk aaehaafvaq skrqigilva
      421 ggvlmwllgm vapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 vlqigsgswv vallaglsvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_110644714             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_110644714
VERSION     WP_110644714.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38791
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag vkasvvdsay eaagasigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_110651023             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salinicola
            peritrichatus].
ACCESSION   WP_110651023
VERSION     WP_110651023.1
KEYWORDS    RefSeq.
SOURCE      Salinicola peritrichatus
  ORGANISM  Salinicola peritrichatus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Salinicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Salinicola peritrichatus"
                     /db_xref="taxon:1267424"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55301
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeia kgearvaltp esaqqiqklg hecliesgag vaagfddavy seagvevves
       61 adalwqtadv vikvrepdee eaerlhegqt lisffwpaqn eemlerckak gatvvamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgsasggy aapsspefre
      241 kqlalfreqa pdidivitta lipgkpapkl wledmvaamk pgsvivdlaa ekggncdltv
      301 aderiatang vivvgytdfp srmatqasll yatnirhmlt dltpqkdgvi vhdmeddvir
      361 gatvthagei tfpppppkvk aigaskpkek preptpeekr aaehaafvaq tkrqvgllaa
      421 ggvlmwllgl vapasfmqhf ivfalacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 ilqigsgswl vgllagisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_110655021             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salinicola
            halimionae].
ACCESSION   WP_110655021
VERSION     WP_110655021.1
KEYWORDS    RefSeq.
SOURCE      Salinicola halimionae
  ORGANISM  Salinicola halimionae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Salinicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Salinicola halimionae"
                     /db_xref="taxon:1949081"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55518
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela rgearvaltp esaqqiqklg hecliesgag klagfddety reagvsvigs
       61 aealwreadv vikvrepvet eidrlragqt litffwpaqn easlercraq gatvmamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv liigagvagl
      181 saigtatslg avvrafdvrp evaeqiesmg aeflfldfed nqdgsgsggy aapsspefre
      241 kqlalfreqa pdvdivitta lipgrpapkl wledmvaamk pgsvivdlaa ekggncdltv
      301 aderivadng vvvigytdfp srmatqasll yatnirhmls dltpekdgvi hhdmeddvir
      361 gvtvthagei tfpppppkvk aiaaakpkak vkeptpaekk aaehaafqaq skrqmgilia
      421 ggvlmwllgm vapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 vlqigsgswl vgllagisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_110659815             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_110659815
VERSION     WP_110659815.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38560
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelvl kvvapsdsel aliksgtvvv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_110665914             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salinicola
            halophilus].
ACCESSION   WP_110665914
VERSION     WP_110665914.1
KEYWORDS    RefSeq.
SOURCE      Salinicola halophilus
  ORGANISM  Salinicola halophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Salinicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Salinicola halophilus"
                     /db_xref="taxon:184065"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55295
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkvgavkera rgearvaltp esarqmqklg hdcliesgag vlagftdday reagvevves
       61 aealwtraev vikvrepldd evgrlrpgqt liaffwpaqn earleacrat gatvlamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfde gqdgagsggy aapsspefre
      241 kqlalfreqa aevdivitta lipgreapkl wlddmvaamk pgsvivdlaa ekggncdatv
      301 mdkrvvtdng vivvgytdfp srmatqasll yatnvrhllt dltpekdgqi vhdmeddvir
      361 gttvvhesqv tfpppppkvk aigaakpkar vkeptpeekr aaahagfvaq tqrqvgllaa
      421 gavtmwllgm vapasfmqhf ivfvlacfig fqviwsvshs lhtplmavtn aisgivilga
      481 ilqigsgssl vallaglsvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_110669121             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces tateyamensis].
ACCESSION   WP_110669121
VERSION     WP_110669121.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces tateyamensis
  ORGANISM  Streptomyces tateyamensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Streptomyces tateyamensis"
                     /db_xref="taxon:565073"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53727
     Region          13..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msaedptrhp pqrigvvaes vpgetrvaat pstvrqllal gyqvvvesea gaasgftdet
       61 yleagaeige awtadlvlkv napseeevar lnqgadlval lapaqrgdll evlaargvta
      121 laldavpris raqsmdvlss maniagyrav ieaahafgrf ftgqvtaagk vpaakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvkslggeyl pvnveqeast dgyakatsad
      241 ydraaaalyt eqakdvdivi ttalipgrpa prlltaadva amkpgsvivd maaamggnve
      301 gtvagravvt eggvtiigyt dlaarlpaqa sqlfgtnlvn llklvtpekd grltldfedv
      361 vqravtvvrd geitwppppv avsaapqaqa sapaavpaep agprltpaar fgliglgmla
      421 tfllvafapa qlaenftvfa lavvigyyvi gkvhhalhtp lmsvtnaisg ivvvgallqi
      481 gheswlvtal sfvailltsv nifggfavtr rmlsmfstsp err
//
LOCUS       WP_110680383             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aquipseudomonas alcaligenes].
ACCESSION   WP_110680383
VERSION     WP_110680383.1
KEYWORDS    RefSeq.
SOURCE      Aquipseudomonas alcaligenes
  ORGANISM  Aquipseudomonas alcaligenes
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Aquipseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Aquipseudomonas alcaligenes"
                     /db_xref="taxon:43263"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38752
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etvkklvgqg hqvtvqagag vsasipdsay eaagatignd
       61 aaafgadlvl kvvapteael ahmksgavlv gmlnpfcndt iarmnargit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpqswme
      241 rqakavhera kqadivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvkhgv tivghtnlaa mvpadasaly arnlldflkl vidkeaqfql nleddivaac
      361 lmckggevvr kng
//
LOCUS       WP_110687858             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salinicola
            aestuarinus].
ACCESSION   WP_110687858
VERSION     WP_110687858.1
KEYWORDS    RefSeq.
SOURCE      Salinicola aestuarinus
  ORGANISM  Salinicola aestuarinus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Salinicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Salinicola aestuarinus"
                     /db_xref="taxon:1949082"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55331
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela rgearvamtp esasqiqklg hecsveqgag alagftdday rqagvtvved
       61 aetlwshadv vikvrepvde eisrlrtgqt liaffwpaqn earleacrat gatvlamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfee sqdgagsggy aspsspefre
      241 kqlalfreqa aevdivitta lipgrpapkl wlddmvaamk pgsvivdlaa erggncdatv
      301 mderivtdng vvvvgytdfp srmatqasll yatnvrhlls dltpekdgql vhdmeddvir
      361 gvtvvresav tfpppppkvk aigaakpker vkaptpeekr aaehssfvaq trrqvgllga
      421 gavtmwllgm vapasfmqhf ivfilacfig fqviwsvshs lhtplmavtn aisgivilga
      481 vlqigsgsgl vvllagisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_110674336             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Salinicola].
ACCESSION   WP_110674336
VERSION     WP_110674336.1
KEYWORDS    RefSeq.
SOURCE      Salinicola
  ORGANISM  Salinicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Salinicola"
                     /db_xref="taxon:404432"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55458
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigapreia kgearvaltp esaqqiqklg hecllergag vaagfsdday qaagvtlvdd
       61 aealwetaev vikvreplda eiellregqt liaffwpaqn earlarcrek gatvvamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv lvlgagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfde sqdgsgsggy aspsspefre
      241 kqlalfreqa peidivitta lipgrpapkl wleemvaamk pgsvivdlaa ekggncdltv
      301 mderivtdng vivvgytdfp srmatqasll yatnirhmlt dltpekdgvi vhdmeddvir
      361 gatathagei tfpppppkvk aigaakpkak pkeptpeekr aaehasflaq tkrqvgllaa
      421 ggvlmwllgm vapasfmqhf ivfalacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 ilqigsgswl vgllagisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_110693768             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salinicola
            halophyticus].
ACCESSION   WP_110693768
VERSION     WP_110693768.1
KEYWORDS    RefSeq.
SOURCE      Salinicola halophyticus
  ORGANISM  Salinicola halophyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Salinicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Salinicola halophyticus"
                     /db_xref="taxon:1808881"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55436
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela kgearvaltp esaqqiqklg hecliergag alagfsdeay rdagvtvidg
       61 analwseadv vikvrepvea eieqlrkgqt litffwpaqn eenlercrak gatvvamdmv
      121 prisraqkmd alsstaniag yravieagsq fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgsgsggy aapsspefre
      241 kqlalfreqa pevdivitta lipgrpapkl wledmvalmk pgsvivdlaa ekggncdltv
      301 mderivtdng vivvgytdfp srmatqasll yatnirhmlt dltpekdgvi vhdmdddiir
      361 gatathggdi tfpppppkvk aiaaakpkpk tkeptseekk aaehaaflaq srrqigmlva
      421 ggvlmwllgl vapasfmqhf ivfalacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 vlqigsgswl vgllagisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_110710041             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salinicola
            sp. CR57].
ACCESSION   WP_110710041
VERSION     WP_110710041.1
KEYWORDS    RefSeq.
SOURCE      Salinicola sp. CR57
  ORGANISM  Salinicola sp. CR57
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Salinicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Salinicola sp. CR57"
                     /db_xref="taxon:1949086"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55383
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela kgearvaltp esaqqikklg hecliesgag vlagfsdeay rdagvsvveg
       61 aaalwreaev vikvreplae eterlregqt litffwpaqn eenlercrak gatvvamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgagsggy aapsspefrd
      241 kqlalfreqa pevdivitta lipgrpapkl wledmvalmk pgsvivdlaa ekggncdltv
      301 pderivtdng vivvgytdfp srmatqasll yatnirhmlt dltpekdgvi vhdmeddvir
      361 gatvthagev tfpppppkvk aiaaakpkpk vkeptpeekk aaehaaflaq skrqigilva
      421 ggvlmwllgm vapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 imqigsgsgl vallaavsvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_110717018             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salinicola
            acroporae].
ACCESSION   WP_110717018
VERSION     WP_110717018.1
KEYWORDS    RefSeq.
SOURCE      Salinicola acroporae
  ORGANISM  Salinicola acroporae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Salinicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Salinicola acroporae"
                     /db_xref="taxon:1541440"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55453
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela rgearvaltp esaqqiqklg hecliesgag vlagfsdeay rdagvsvved
       61 aaalwreaev vikvreplae eterlregqt litffwpaqn eenlercrak gatvvamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed gqdgagsggy aapsspefrd
      241 kqlalfreqa pevdivitta lipgrpapkl wleemvalmk pgsvivdlaa ekggncdltv
      301 pderivtdng vivvgytdfp srmatqasll yatnirhmlt dltpekdgvi vhdmeddvir
      361 gatvthagev tfpppppkvk aiaaakpkpk vkeptpeekk aaehaaflaq skrqigilva
      421 ggvlmwllgm vapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 imqigsgsgl vallaavsvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_110736298             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas mosselii].
ACCESSION   WP_110736298
VERSION     WP_110736298.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas mosselii
  ORGANISM  Pseudomonas mosselii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas mosselii"
                     /db_xref="taxon:78327"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38928
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvgqg hqvtvqrgag lkasipdsay eavgaalgea
       61 adafgaqlvl kvvapddqel tlinsgslla gmlnpfnnel igkmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera rqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvmhngv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgnlvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_110743590             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. LB-090624].
ACCESSION   WP_110743590
VERSION     WP_110743590.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. LB-090624
  ORGANISM  Pseudomonas sp. LB-090624
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. LB-090624"
                     /db_xref="taxon:2213079"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38745
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqrgag lnaaipdsay eavgaslgsa
       61 adaygaqlvi kvvapndqel alinsgsllv gmlnpfnnel igkmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvqangv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_110748572             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_110748572
VERSION     WP_110748572.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38532
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagaaigsa
       61 seafgaelil kvvapsdsel aliksgtvvv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlaa avaadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_110754412             414 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium leguminum].
ACCESSION   WP_110754412
VERSION     WP_110754412.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium leguminum
  ORGANISM  Phyllobacterium leguminum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Phyllobacterium leguminum"
                     /db_xref="taxon:314237"
     Protein         1..414
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42944
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifipke tdpveprvaa spetvkklig lgfsvvvekg agtlsripds efdaagakig
       61 satdaksadv ilkvrrpsls elksykkgaa liamldpygd datvrayada glssftmefm
      121 pritraqvmd vlssqanlag yqavidaaae ygralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg gkfiavedee fkaaetaggy akemsreyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vtkemlaamr pgsvvvdlav erggnvegaq
      301 pgkvveiggv kivghlnvpg riaatasqly arnlfafiet ltdkdskalk inlddelvka
      361 tllthdgsvv hpafaqaaaa saaepaamkp aekpvrkapa rktkadtpkt ggea
//
LOCUS       WP_110756336             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium/Agrobacterium group].
ACCESSION   WP_110756336
VERSION     WP_110756336.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium/Agrobacterium group
  ORGANISM  Rhizobium/Agrobacterium group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium/Agrobacterium group"
                     /db_xref="taxon:227290"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55740
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtpkely egearvgmtp dsaqalqklg ydciveagag kaagfsdday raagvtvvds
       61 adalyagsdi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qqqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvamm kpgsviidla aerggncdlt
      301 vpdqrvvsdn gvivigytdf psrmaaqast lystnirhmm tdltpakdgk vvhnmeddvi
      361 rgatvayqge itfpppppki qaiaaqkpke kareltpeek hakeraefka qtknqvgllv
      421 agtailllvg lyapasfmsh fivfvlacfv gfqviwsvsh slhtplmavt naisgivilg
      481 allqigsgnw lvvilaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_110778406             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas frequens].
ACCESSION   WP_110778406
VERSION     WP_110778406.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas frequens
  ORGANISM  Stutzerimonas frequens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Stutzerimonas frequens"
                     /db_xref="taxon:2968969"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38901
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigvpaesq psetrvaatp etvkkliaqg hqvvveagag iaacipdday laagaslgta
       61 gdalaadlvl kvtapnsdel grmqpgsvlv gmlnpfddag iarmakagit afaleaaprt
      121 sraqsldvls sqanvagyka vmlavdhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vevpyeteee recaegvggy arpmpeswmk
      241 rqaqavheka rqadivitta lipgrkaptl ltedtvaqmk pgsvivdlaa aqggncpltr
      301 adqvvvkhgv tivghsnlpa mlaadasaly arnlldflkl vidkdgqfql nreddivaac
      361 lmceggnvvr tnar
//
LOCUS       WP_110778529             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas frequens].
ACCESSION   WP_110778529
VERSION     WP_110778529.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas frequens
  ORGANISM  Stutzerimonas frequens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas frequens"
                     /db_xref="taxon:2968969"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38842
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkligqg hrvtlqsgag llssvpdsay eavgatigda
       61 aaafaaelvl kvnapddael aqmqsgsvll gmlnpfdnnc iarmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vlvgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhera lqsdivitta lipgrkaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvpadasaly arnlldflkl vidkdgqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_110781024             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodopseudomonas faecalis].
ACCESSION   WP_110781024
VERSION     WP_110781024.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas faecalis
  ORGANISM  Rhodopseudomonas faecalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rhodopseudomonas faecalis"
                     /db_xref="taxon:99655"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39122
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeld paeprvaatp dtvkklkalg advavepgag iksgipdadf tavgatvsad
       61 alkdadvvfk vkrpeasela kykrgalvla imdpygndaa lksmadagvv afamelmpri
      121 traqvmdvls sqanlagyra vidaaesfgr ampmmmtaag tvpaakvfim gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpaprlvta emvksmkpgs vlvdlaverg gnvegakpge
      301 vveidgvkiv gytnvagria asasglyarn llsffetmvn kekalavnwe delvkatalt
      361 rdgavvhpnf qpkta
//
LOCUS       WP_110784926             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodopseudomonas palustris].
ACCESSION   WP_110784926
VERSION     WP_110784926.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39080
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeqd paeprvaatp dtvkklkalg aevavepgag lksglpdsdf taagatvsad
       61 alkdadvvfk vkrpeasela sykrgalvla imdpygndaa lksiadagia afamelmpri
      121 traqvmdvls sqanlagyra vidgaetfgr vfpmmmtaag tvpaakvfim gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpaprlvta emvksmkpgs vlvdlaverg gnvegaqpgq
      301 vveidgvkiv gytnvagrva asasalyarn llsffetmvn kekalavnwd delvkatalt
      361 rdgavvhpnf qpksa
//
LOCUS       WP_110795294             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Litorivita
            pollutaquae].
ACCESSION   WP_110795294
VERSION     WP_110795294.1
KEYWORDS    RefSeq.
SOURCE      Litorivita pollutaquae
  ORGANISM  Litorivita pollutaquae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Litorivita.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Litorivita pollutaquae"
                     /db_xref="taxon:2200892"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55351
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevl egearvamtp dsarqlqklg ydcvietgag alagfsdaly keagvevvkt
       61 aaalfkasdi vakvrvptea evkrltegqt lisffnpaan eplmtlaask ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yaavsspefa
      241 aaqlakfrel apemdivitt alipnreape lwtedmvksm kpgsvivdla aekggncklt
      301 vmdekivtdn gvtiigytdf psrmaaqsst lyatnirhmm tdltpekdgq inhnmeddvi
      361 rgatvtfdke itfpppppki kaiaaqkkea pkeltpeekr aqetaafkaq tkqqvgllai
      421 ggalllavgl vapasfmqhf ivfvlsvfig fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsal villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_110805150             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodobacter viridis].
ACCESSION   WP_110805150
VERSION     WP_110805150.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacter viridis
  ORGANISM  Rhodobacter viridis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Rhodobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhodobacter viridis"
                     /db_xref="taxon:1054202"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55501
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egearvaltp dsavqlqklg htcfveagag haagfedtay eavgvtvvkg
       61 aealfdavdv vakvrppvea evarlksgkt lisffypaqn kdlleaakat gatviamdmv
      121 prisraqkmd alssmanisg yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigastalg aityafdvrp evaeqiesmg aefvyldfee qaqdgaatgg yaapsspefr
      241 daqlkkfrel apemdivitt alipgrdapi lwtkdmvekm krgsvivdla aerggncelt
      301 kkdekvvtpn gvtvigytdf psrmaqqssq lystnirhmm tdltpgkdgv vvhnmeddvi
      361 rgatvtfega itfpppppki aaiaaqkpke kakvltpeei raaekaafrk etrnqilmlg
      421 iggalllsig lvapasfmah fivfalscfv gfqviwnvsh slhtplmavt naissiiilg
      481 allqvgsssf lvillsgvsv fmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_110818255             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_110818255
VERSION     WP_110818255.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38860
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lrasvpdsay eaagavigdt
       61 netyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgtvv easdvrpavk eqieslgakf idvpyetdee hecaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_110826312             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_110826312
VERSION     WP_110826312.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53571
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyktw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_110855392             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia silvatlantica].
ACCESSION   WP_110855392
VERSION     WP_110855392.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia silvatlantica
  ORGANISM  Paraburkholderia silvatlantica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Paraburkholderia silvatlantica"
                     /db_xref="taxon:321895"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54160
     Region          3..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 maltiavpre tyegerrvaa tpesvaqlik lgyvvevett agvsasypdd ayraagarvv
       61 ndahallsga divikvrpps seevqclkpg atligfiwpa qnaalleqla areatvlamd
      121 cvprisraqk ldalssmanm agyravveaa qhfgrvftgq itaagkmppa kvlvigagva
      181 glaaigaarg lgaivrafdt rpevgqqves mgaeflsidi eeegggtggy akqmsakfie
      241 aemalfeaqa revdiiitta lipgkpaprl idaktvacmr sgsvivdmaa eqggnceltr
      301 pgevvnangv tvigytdlps rmanqssqly atnirhlltd ltpakdgels ldmddvvqrg
      361 tivmqrgqvc wppppvqvsa tpqaaaqpkp vavavgnake aaaqatrrng vgslavlvva
      421 allllalgav apgafvahft vfvlavfvgy qvvwnvtpsl htplmsvtna isgiivigal
      481 lhpgnagtiv tvlagialvv atiniaggfl vthrmlkmfq rt
//
LOCUS       WP_110856659             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia silvatlantica].
ACCESSION   WP_110856659
VERSION     WP_110856659.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia silvatlantica
  ORGANISM  Paraburkholderia silvatlantica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia silvatlantica"
                     /db_xref="taxon:321895"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39588
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anetrvaatp etvrkyvaqg htvtiqagag agasyldeay tavgaqvada
       61 aaafgadlvl kvqsptvsel pfmkrgavlv gmldpfnaen aatlaeagvt afaleaaprt
      121 traqsldvls sqaniagyka vlvasdlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atarrlgavi easdvrpavk eqieslggkf levpyetdee reaavgvggy arpmppswla
      241 rqsalvhera kqadivista lipgrdaptl lpsetvqamk pgsvvidlaa grgpvadeas
      301 grrggncplt eadkvvthhg vqicgytnla smvaadasal yarnlldflk livtkegtln
      361 idladdivaa tllardgqvt rka
//
LOCUS       WP_110861383             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Prochlorococcus marinus].
ACCESSION   WP_110861383
VERSION     WP_110861383.1
KEYWORDS    RefSeq.
SOURCE      Prochlorococcus marinus
  ORGANISM  Prochlorococcus marinus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Prochlorococcaceae; Prochlorococcus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Prochlorococcus marinus"
                     /db_xref="taxon:1219"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40465
     Region          6..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvsflipfes algetrvsat petvkkfldl gckvffekga gkaagflddt ykdagaelve
       61 iendevkkiv divlcvqppn ekflshlkpg sflvgllnpy gnkllaetlk sknisaiale
      121 llprisraqs sdalssqani agyksvllaa saldryfpml mtaagtiqps kivvlgagva
      181 glqaiatakr lgavvyvsdi reavkeqves lgarfielpk idetpsesgg yakqvsdefi
      241 vaqrkelakq lseadvaict aqvpgkkapk lidekmlddm rpgsvvidla vlsggncacs
      301 kpgetivreg vkiigasnlp csipnhassl ysrnllsllq pmfkegkfli dnddeliags
      361 liskdgvilk seiienggtr s
//
LOCUS       WP_110951792             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas bohemica].
ACCESSION   WP_110951792
VERSION     WP_110951792.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas bohemica
  ORGANISM  Pseudomonas bohemica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas bohemica"
                     /db_xref="taxon:2044872"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38643
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikkligqg hkvtvqsgag itasvtdgay eaagasigsa
       61 adafgaelil kvvapgdgel aliksgtvvi gmlnpfnnei iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee reaavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkapvl lsaetvsqmk pgsvvidlaa aqggncpltv
      301 adqvviehgv tivghtnlpa lvaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_110960879             534 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. ST3].
ACCESSION   WP_110960879
VERSION     WP_110960879.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. ST3
  ORGANISM  Acidovorax sp. ST3
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Acidovorax sp. ST3"
                     /db_xref="taxon:2219062"
     Protein         1..534
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55639
     Region          11..534
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtspvpqpq rigvpketfp gekrvatvpd vvekliklgf avtvesgagd aanfsddvyr
       61 aagaeivsda aalwaasdiv fkvrppssde varmregttl idfiwpaqnp dlmqqlaakk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rkmyaeqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti vgytdlasrl akqsstlyat nllrlteelc kakdgvavvn
      361 meddairglt vvkdgaitwp applkqapap apkaaapvve kksghghgtg apmsaktlti
      421 vfavvavlfw avgayapvaf lghftvfvla cfigymvvwn vtpalhtplm svtnaissii
      481 aigalvqiap pdagvngrpd glilwlafaa lvltainmfg gfavtrrmla mfrk
//
LOCUS       WP_110965727             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas putida].
ACCESSION   WP_110965727
VERSION     WP_110965727.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38673
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag inasvvdsay eaagakigna
       61 ndafgaelil kvvapsdnel aliksgtvvv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlaa svgadasaly arnlldfmkl lfdkdgqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_110969945             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas huaxiensis].
ACCESSION   WP_110969945
VERSION     WP_110969945.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas huaxiensis
  ORGANISM  Pseudomonas huaxiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas huaxiensis"
                     /db_xref="taxon:2213017"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38625
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvgqg hqvtvqrgag lnasipdsay eaagavmgsa
       61 adafgaqlvl kvvapddsel gqiksgtvla gmlnpfnnel iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqviqvngv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgalti nledgivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_110995050             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sichuanensis].
ACCESSION   WP_110995050
VERSION     WP_110995050.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sichuanensis
  ORGANISM  Pseudomonas sichuanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sichuanensis"
                     /db_xref="taxon:2213015"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38794
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvsqg hqvtvqrgag lnasipdgay eavgatlgea
       61 tdafgaqlvl kvvapndqel alissgsvla gmlnpfnnel igkmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvqangv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgalmi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_111000322             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Taibaiella
            soli].
ACCESSION   WP_111000322
VERSION     WP_111000322.1
KEYWORDS    RefSeq.
SOURCE      Taibaiella soli
  ORGANISM  Taibaiella soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Taibaiella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Taibaiella soli"
                     /db_xref="taxon:1649169"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40402
     Region          1..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,90,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,275..276,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,225,236,
                     253..255,262,264)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtigvlkeqh petrvslvpe vvqalvkmnv qvqveqgvgl tsfysdkmya dagatlqdre
       61 aviknsdlll siqpenissg mkanavllgv fqplynvpqm qswaekgftv fsmdniprtt
      121 raqsmdvlss qaniagykav llaafqysry fpmfmtaags ippakvmilg agvaglqaia
      181 tsrrlgavve vfdtrpavke evmslgakfi evegaadask aggyaveqsa dfqqrqkdki
      241 qehirksdiv ittaqipgkk apilitkpmi eemragsviv dlaaatggnt eltqndttvm
      301 yhdvaivgns alaatapada sklysknvln flklitdkeg nlqlnfeddi vkgtciahgg
      361 kitndrvqsf isqptta
//
LOCUS       WP_111015285             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. JP2-270].
ACCESSION   WP_111015285
VERSION     WP_111015285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. JP2-270
  ORGANISM  Burkholderia sp. JP2-270
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia sp. JP2-270"
                     /db_xref="taxon:2217913"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39178
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiakgag vaasypdqay aaagaeltdq
       61 saafdadivl kvqaptdael pslkrgsvlv gmldpfngeq aaklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetaqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qvivhngvti agytnlasmv asdasalyar nlldfmkliv tkegtlnidl
      361 tddivaatll crdgeltrk
//
LOCUS       WP_111158030             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            tubonense].
ACCESSION   WP_111158030
VERSION     WP_111158030.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium tubonense
  ORGANISM  Rhizobium tubonense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rhizobium tubonense"
                     /db_xref="taxon:484088"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55878
     Region          3..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mglkigtpke vvvgearvam tpdsaqqllk lgyeclieag agreagfsdd ayrssgvsvv
       61 dspdalyaav diiakvrppe lheaerlrdg qtlisffypa qkkellercr esganviamd
      121 mvprisraqk mdalssmani agyravieag nnfgrfftgq vtaagkvppa kvlvigagva
      181 glsaigtats lgaltyafdv rpevaeqies mgaefvflef etaqdgaatg gyaapsspef
      241 rdkqlakfre lapqmdivit talipgrdap klwlgdmvam mksgsvvvdl aaerggncdl
      301 tvadqrivsd ngvvvigytd fpsrmaaqss tlyatnirhm mtdltpnkdg rlnhdmgddv
      361 irgatvtyks eitfpppppk vraiapaksk kkepelspae krtqeraifa sqtrsqvall
      421 aivtllmliv gayapasfmn hlvvfvlacf igfqviwnvs hslhtplmav tnaisgivil
      481 gallqigsgs llvdilaals vliatvnivg gflvtrrmla mfqks
//
LOCUS       WP_111068530             394 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum ramasamyi].
ACCESSION   WP_111068530
VERSION     WP_111068530.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum ramasamyi
  ORGANISM  Azospirillum ramasamyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Azospirillum ramasamyi"
                     /db_xref="taxon:682998"
     Protein         1..394
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41116
     Region          1..378
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,105,302,329,331)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,138..139,148..149,152..153,156..157,159..160,
                     162..167,169,171..173,176,199..200,292..293,336..337,341,
                     344..345)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,138,141,144,185..188,208..210,242,253,
                     270..272,279,281)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(135..136,138,148,191..192,199,215..216,218..221)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(168..172,175,178,201,203)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiprerr pgerrvaasp etvkkfktlg ldvvvesgag lgsslpdaay eaagaviaad
       61 aasaladadi vlkvqrplia qevekgegge delalirkga llfailnpyn srdhvkayad
      121 agvnafamef mpritraqvm dvlssqanla gykavvdaas eygrafpmmm taagtvppar
      181 afimgvgvag lqaiatakrl gaivsatdvr pavkeqvqsl ggsfvavend efkqaetagg
      241 yakemsddyk rqqaalvaeh irkqdivitt alipgrkapi lvtaehvasm kpgsvivdla
      301 veqggnvega klgevvttan gvkivghany asriaesasl lyaknllall tslhgketgv
      361 avnwddeivk aialtrdgai vhpafadtre aqpa
//
LOCUS       WP_111069935             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum ramasamyi].
ACCESSION   WP_111069935
VERSION     WP_111069935.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum ramasamyi
  ORGANISM  Azospirillum ramasamyi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Azospirillum ramasamyi"
                     /db_xref="taxon:682998"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40129
     Region          1..378
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,105,302,329,331)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,138..139,148..149,152..153,156..157,159..160,
                     162..167,169,171..173,176,199..200,292..293,336..337,341,
                     344..345)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,138,141,144,185..188,208..210,242,253,
                     270..272,279,281)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(135..136,138,148,191..192,199,215..216,218..221)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(168..172,175,178,201,203)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvaipkerr agelrvaasp etvkklkglg ldvvvesgag lgsslpdaay eaagaviaad
       61 aasaladadi vlkvqrplia qevekgegge delalirkga llfailnpyn srdhvkayad
      121 agvnafamef mpritraqvm dvlssqanla gykavvdaas eygrafpmmm taagtvppar
      181 afimgvgvag lqaiatakrl gaivsatdvr pavkeqvqsl ggsfvavend efkqaetagg
      241 yakemsddyk rqqaalvaeh irkqdivitt alipgrkapi lvtaehvasm kpgsvivdla
      301 veqggnvega klgevvttan gvkivghany asriaesasl lyaknllall tslhgketgv
      361 avnwddeivk aialtrdgvv vhpafag
//
LOCUS       WP_111195930             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aestuariivirga litoralis].
ACCESSION   WP_111195930
VERSION     WP_111195930.1
KEYWORDS    RefSeq.
SOURCE      Aestuariivirga litoralis
  ORGANISM  Aestuariivirga litoralis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aestuariivirgaceae; Aestuariivirga.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Aestuariivirga litoralis"
                     /db_xref="taxon:2650924"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38170
     Region          1..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,275..276,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,225,236,
                     253..255,262,264)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiptetm vgesrvaasp dtvkafikkg aevtvqagag rgasipddaf aaagakieps
       61 vgrdadivlt vrrpsgells tlkrgailmg glepygdkag leaiaasgat afamelmpri
      121 traqsmdils sqanlagyka vidaafhftr afpmmmtaag tvpaakvfim gvgvaglqai
      181 atarrlgaiv satdvrkate eqvkslgakf vyadiadaat sggyakelsa edkakqaalv
      241 anhvktqdvi ittalipgrp apvliteemv esmkpgsiiv dlaverggnc plskpdqive
      301 hkgvkivgtv nlagklagna splfaknlan fldlmitkeg alkiddadec ikgtmiardg
      361 alvhpmftsk
//
LOCUS       WP_111163760             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            tubonense].
ACCESSION   WP_111163760
VERSION     WP_111163760.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium tubonense
  ORGANISM  Rhizobium tubonense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium tubonense"
                     /db_xref="taxon:484088"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40106
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnlvfvake iaadetrvaa svetvkklis lgfdvvveag agalsripda dynaigahig
       61 sfadaakadv vlkvrrpasa eiagyqhgai viaimdphgn edalaemara gltsfamelm
      121 pritraqsmd vlssqanlag yqavveaaat ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvsatdvrp askeqvaslg akfiavedee fkaaetsagy akemskeyqa
      241 kqaalvadhi skqdivitta lipgrpaprl vsramlasmk pgavavdlav erggniegst
      301 sggiaevegv rvigfanmag risasaslly aknlvnflet mvnkdtktlg lnlddelira
      361 tmlthsgvvv hpnfsdpdqa ivkkgev
//
LOCUS       WP_111251584             542 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Xylanimonas oleitrophica].
ACCESSION   WP_111251584
VERSION     WP_111251584.1
KEYWORDS    RefSeq.
SOURCE      Xylanimonas oleitrophica
  ORGANISM  Xylanimonas oleitrophica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Xylanimonas.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Xylanimonas oleitrophica"
                     /db_xref="taxon:2607479"
     Protein         1..542
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55317
     Region          1..540
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresr egqrlvaatp atvtrlcrlg ydvvvehdag taahltdtay teagatlgda
       61 tqvwtsdvvv avdapgpgql dllrpgavlv aqlapatrpd llealadrgv talaldavpr
      121 israqaldtl stmsnvagyr avieaaaeyq gmfagqvtaa gktppakvfv igggvaglaa
      181 igtavslgad vrafdvrpea geqiesmgat fvqaqgaqqe vstdgyarel tgeqeaatmr
      241 tyaqetarad ivittalvrg raprtvtaem vaamrpgsvi vdlaasgggn aeptvpgerv
      301 vtdggvvvlg ytdlpgrmpa qtsqlygtni anllalltpg edgvlaldld dpvqrgmtvt
      361 lapapagdgr hggdgggaar rgevlwpppp vhvsatpaga apagptpaqq eaaartasrd
      421 eaararlrrq rlavggalga vlvvlaltls pasfvghftv ftlavivgfy visnvshslh
      481 tplmaqtnai sgiilvgall qlgnenlvvt vlallaasva sinifggflv srrmiamfrk
      541 dv
//
LOCUS       WP_111276815             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phenylobacterium kunshanense].
ACCESSION   WP_111276815
VERSION     WP_111276815.1
KEYWORDS    RefSeq.
SOURCE      Phenylobacterium kunshanense
  ORGANISM  Phenylobacterium kunshanense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Phenylobacterium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Phenylobacterium kunshanense"
                     /db_xref="taxon:1445034"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38863
     Region          3..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,95,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpviavtker ragetrvaat petvkkfiga gysvvvesga gdgasipdad yeaagatlak
       61 svkdavgkad ilfkvrgpea deikalkpga ivaatlnpyq dratldalaa qgatafamef
      121 vpritraqvm dvlssqanla gyraviegae aygralpmmm taagtvapak vfimgvgvag
      181 lqaiatarrl gavvtatdvr patkeqvesl gakfiavede efqnaqtagg yakemskeyq
      241 akqaaltssh iakqdivitt alipgrpapr litaeqvasm kpgsiivdla veqggntega
      301 kpnetvvtan gvkilgftnl pgriaadssa lyarnlvafs elfktkegaf apdledeilk
      361 aacvthggav vhpslka
//
LOCUS       WP_111280442             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter radioresistens].
ACCESSION   WP_111280442
VERSION     WP_111280442.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39994
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv igenrvaatp etvkklinag hsvviergag vkaayidsay eqvgatitdd
       61 ayqnsqiilk vrapkgeeiq klsphttvva mfdpyrntel dqfasqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaneyqr mfpmlmtaag tvkparvvvm gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmsaeeq qraaeaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvvkm kpgsvildma vesggnvegs
      301 kcgetvttsn gvkilgvpni patvateasa lyarnvfnfi etlfdqeknf tvnledeiqk
      361 allvthngqv llkrg
//
LOCUS       WP_111293942             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Hydrotalea
            sandarakina].
ACCESSION   WP_111293942
VERSION     WP_111293942.1
KEYWORDS    RefSeq.
SOURCE      Hydrotalea sandarakina
  ORGANISM  Hydrotalea sandarakina
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hydrotalea.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Hydrotalea sandarakina"
                     /db_xref="taxon:1004304"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40151
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miagilkept genrvsflpe hlagllklni eiwvqenaga aayatnevyq qagasihsrs
       61 eilqnaqiif silpltnddl qiikpgtvvi gvyqplynya emqlwanknl itfsldtipr
      121 ttraqsmdvl ssqaniagyk avllaaanyg ryfpmfitaa gsippakvlv lgagvaglqa
      181 iatakrlgav ievfdtrpav keevmslgak fvevegaada skaggyaveq saeyqqkqqq
      241 riaeaakkad iiittaqipg kkapllltea miqqmrngsi ivdlaaatgg ntpltknnet
      301 vvtengvtim gysnlpgtmp fdasklygkn vfnflqliis kegklnisfd ddivkgccit
      361 yngkivnerv lalnn
//
LOCUS       WP_111312411             504 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus parahaemolyticus].
ACCESSION   WP_111312411
VERSION     WP_111312411.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus parahaemolyticus
  ORGANISM  Haemophilus parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Haemophilus parahaemolyticus"
                     /db_xref="taxon:735"
     gene            1..504
                     /gene="nrfA"
     Protein         1..504
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56231
     Region          1..489
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkrltktlam atiamlgcfh saqaeekasg aqtetltqka lkheklgvtv esanhlfadk
       61 yplqynswka tsestdrgsa leadprsvil wagysfskey nkprghyyav tdvreilrtg
      121 apkdendgpq pmacwtckgp dvprlieekg ergyfdpkwa kygseivnsi gcadchdtks
      181 edfkegkpal rvarphvlra lesvgwtfen ldkqgkrvai canchveyyf kdkkdvtfpw
      241 kngvdvssie kyyddiefad wthalskapm lkaqhpdfei wsqgvhgkng vtcidchmpk
      301 vkdkdgkvyt dhkignpfdq fentcktche qsketlqkrv aehkkqvkda mikledqivk
      361 ahfeakaawe agatpdemkd ilkairhaqw rwdytsashg gymhapdatl hviatgidra
      421 adaraqlgvv lakhgvttpv aipdistrek aqkaigldip kdqaakdefl rtvvpqweat
      481 arekgllpav eapkevttpk aeak
//
LOCUS       WP_111322612             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus chordae].
ACCESSION   WP_111322612
VERSION     WP_111322612.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus chordae
  ORGANISM  Algoriphagus chordae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Algoriphagus chordae"
                     /db_xref="taxon:237019"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40269
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvlkeak egenrvalsp dvikqlikke favvvelgag lgsnfsdedy kaagatvass
       61 eevftadvll kvnpfskeei skmktgtacm simyaynhpd lldemnkksi msfsmdavpr
      121 israqkmdcl ssqanlagyk svilganhle kifplmmtac gtitpakvli fgagvaglqa
      181 iatakrlgav vevsdvrpet keqveslggr fltvegaeev kveggyasev saeflqkqke
      241 liqtkikdsd lvittalvmg kkspilvtee mvksmkkgsv ivdmavesgg nceisekdqi
      301 vqkhgvtiig esnlpsllsn nasqlyatni stlllhlatk dgfnldreee itkgvlitye
      361 gqvvheftnk ilnk
//
LOCUS       WP_111366890             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aquicoccus
            porphyridii].
ACCESSION   WP_111366890
VERSION     WP_111366890.1
KEYWORDS    RefSeq.
SOURCE      Aquicoccus porphyridii
  ORGANISM  Aquicoccus porphyridii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Aquicoccus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Aquicoccus porphyridii"
                     /db_xref="taxon:1852029"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55367
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevi egearvamtp dsalqlqklg yeclietgag laagftdaay keagvtikkt
       61 analwkdadi iakvriptde emgrltknkt lisffnpggn eagleaakak ganviamemv
      121 prisraqkmd alssmaniag yravieagnn ygrfftgqit aagkvpparv lvvgagvagl
      181 aaigaavslg avvyafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apemdivitt alipnreapk lwledmvkam krgsvivdla aekggnvegt
      301 vadekvvtdn gvtiigytdf psrmaaqass lyatnirhmm tdltpekdgq vnhnmdddvi
      361 rgatvafdge itfpppppkv aaiaarpqek vkeltpeekr aaevaafkaq tkqqvtllav
      421 gaalvltvgl vapasfmqhf ivfllsvfvg fqviwgvshs lhtplmavtn aissiiilga
      481 lmqigsssvl itilaalavf maginifggf lvtrrmlamf qks
//
LOCUS       WP_111353984             500 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus paraphrohaemolyticus].
ACCESSION   WP_111353984
VERSION     WP_111353984.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus paraphrohaemolyticus
  ORGANISM  Haemophilus paraphrohaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Haemophilus paraphrohaemolyticus"
                     /db_xref="taxon:736"
     gene            1..500
                     /gene="nrfA"
     Protein         1..500
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56061
     Region          1..485
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkrltktlam atiamlgcfh saqaeekate tltqkalkhe klgvtvesan hlfadkyplq
       61 ynswkatses tdrgsalevd prsvilwagy sfskeynkpr ghfyavtdvr eilrtgapkd
      121 endgpqpmac wtckgpdvpr lieekgergy fdpkwakygs eivnsigcad chdtksedfk
      181 egkpalrvar phvlralesv gwtfenldkq gkrvavcanc hveyyfkdkk dvtfpwkngv
      241 dvssiekyyd diefadwtha lskapmlkaq hpdfeiwsqg vhgkngvtci dchmpkvkdk
      301 dgkvytdhki gnpfdqfent cktcheqske tlqkrvaehk kqvkdamikl edqivkahfe
      361 akaaweagat pdemkdilka irhaqwrwdy tsashggymh apdmmlhvia tgidraadar
      421 aqlgvvlakh gvttpvaipd istrekaqka igldipkdqa akdeflrtvv pqweatarek
      481 gllppvevqk evttpkaeak
//
LOCUS       WP_111358153             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodoplanes elegans].
ACCESSION   WP_111358153
VERSION     WP_111358153.1
KEYWORDS    RefSeq.
SOURCE      Rhodoplanes elegans
  ORGANISM  Rhodoplanes elegans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodoplanes.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rhodoplanes elegans"
                     /db_xref="taxon:29408"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39185
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaicaead aaeprvagtp etvkkmmalg advavepgag vksgildady qaagatvtrd
       61 aardadivlk vkrpnemelt gykkgaivia imdpyghqaa lealaragvi afamelmpri
      121 traqvmdvls sqanlagyra vidasaeygr afpmmmtpag tvpaakcfim gvgvaglqai
      181 atarrlgaiv tatdvrpavk eqvaslgakf iaveddefkq aetaggyake mskeyqakqa
      241 alvaehikkq divittalip grpaprlita emvasmkpgs vivdlaverg gnvegakpge
      301 vvevggvkiv ghlnvagrla asssalyskn llaflevlid kktkaialnw ddeivkatal
      361 tkdgaivhpn fvpktaa
//
LOCUS       WP_111373492             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arcticibacterium luteifluviistationis].
ACCESSION   WP_111373492
VERSION     WP_111373492.1
KEYWORDS    RefSeq.
SOURCE      Arcticibacterium luteifluviistationis
  ORGANISM  Arcticibacterium luteifluviistationis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Arcticibacterium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Arcticibacterium luteifluviistationis"
                     /db_xref="taxon:1784714"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40170
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlketk dyenrvaltp dvvkslvkkg fdvcvetgsg lkssfsdqgy idagasiakn
       61 tkeacqsdii lkvnsfteee vsmfpdasvc isfmyaytip evlevmkkkn issfsmdavp
      121 risraqkmda lssqanlagy ktvllganal gkifplmmta agtitpskvl ifgagvaglq
      181 aiatakrlga vvevtdvrpe tkeqveslgg rfltvegvea vkveggyake vsaeflqkqk
      241 eliqekikda divittalvi gkkapvlvte dmvksmktga vivdmavesg gnceiaemnk
      301 tvvkhgvtii gesnlpsllp inasqlyatn istlllhlad kdafkwemee eitkgslith
      361 kgeivhgftk qilgi
//
LOCUS       WP_111388375             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodoplanes serenus].
ACCESSION   WP_111388375
VERSION     WP_111388375.1
KEYWORDS    RefSeq.
SOURCE      Rhodoplanes serenus
  ORGANISM  Rhodoplanes serenus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodoplanes.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rhodoplanes serenus"
                     /db_xref="taxon:200615"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39179
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaicaead aaeprvagtp etvkkikalg advavepgag lksgildady eaagatvsrd
       61 avrdadivlk vrrpnemelt aykkgalvia imdpygheaa laalaragvv afamelmpri
      121 traqvmdvls sqanlagyra vidaaaeygr afpmmmtpag tvpaakafim gvgvaglqai
      181 atarrlgaiv tatdvrpavk eqvaslgakf iavedeefkq aetaggyake mskeyqakqa
      241 alvaehvkkq divittalip grpaprlita emvasmkpgs vivdlaverg gnvegakpge
      301 vveingvkiv ghlnvagrla asssalyakn lyaflevlid kktkaialnw ddeivkatal
      361 tkdgavvhpn fapktaa
//
LOCUS       WP_111388862             500 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus sputorum].
ACCESSION   WP_111388862
VERSION     WP_111388862.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus sputorum
  ORGANISM  Haemophilus sputorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Haemophilus sputorum"
                     /db_xref="taxon:1078480"
     gene            1..500
                     /gene="nrfA"
     Protein         1..500
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=55952
     Region          1..486
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkrltktlam taiamlgcfq saqaeekaae sltdkalkhe klgveiesan hkfaekyplq
       61 ynswkstses tdrgsalsad pryvvlwagy sfakdynkpr ghyyavtdvr eilrtgapkd
      121 endgpqpmac wtckgpdvpr lieekgedgy fnakwakyga eivntvgcgd chdtkskefe
      181 egkpalrvar phvlraletv gwkfedldkh gkrvavcanc hveyyfkdkt hvtfpwdkgv
      241 dvasiekyyd eiefadwtha lskapmlktq hpdfeiwsqg vhgkngvtci dchmpkvkdk
      301 dgkvytdhki gnpfdqfdas cktcheqske tlqkrvaehk kqvkdamikl edqlvkahfe
      361 akaawdagat qeemqdilka irhaqwrwdy saaghgshmh apdvmlhvia tgidraadar
      421 aklgvvlakh gvttpvaipd istrenaqka igldipkeqa akdeflrtvv pqwekqarek
      481 gllpaeeapk evttpkaeak
//
LOCUS       WP_111391873             374 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Algoriphagus].
ACCESSION   WP_111391873
VERSION     WP_111391873.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus
  ORGANISM  Algoriphagus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Algoriphagus"
                     /db_xref="taxon:246875"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39974
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvlketk enerrvalsp dvvkllrkke feviiesgag egsyfsdedf kaagaevgpa
       61 savyqadvll kvnlfsldei armkeksaci symyayqfpq iiealnaksi tsfsmdavpr
      121 israqkmdal ssqanlagyk avllganhlg kifplmmtas gtitpakvli fgagvaglqa
      181 iatakrlgai vectdvrpet keqveslggr fltvegaegv kveggyakev saeylekqqq
      241 lirdkikdad lvittalvmg kkspilvted mvksmktgsv ivdmavesgg ncalseknat
      301 vvkhgvtiig eanlpsllpv nasnlyavni stlllhlask nglnldleee itkgvlithq
      361 gelvhsftks ilnq
//
LOCUS       WP_111407109             508 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Haemophilus].
ACCESSION   WP_111407109
VERSION     WP_111407109.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus
  ORGANISM  Haemophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Haemophilus"
                     /db_xref="taxon:724"
     gene            1..508
                     /gene="nrfA"
     Protein         1..508
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56737
     Region          1..501
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnafkksliv aasfaslslf nsavadmvyk pveqpvepvk pdlkiesvne kfaekypnqy
       61 nswrstangn gekiiyadee nprlivlwgg ysfakeynap rghfyavtdv rsilrtgapk
      121 tandgpqpma cwtckgpdvp rliaewgekd yfnakwakgg peivnsigca dchdttskdf
      181 aegkpalria rphvlralda lekataekdk aegrphnnls fntaartekr aeicanchve
      241 yyfagdikqv tfpwnkgqtv ddiekyydei gfsdwthsls kapmlkaqhp dfeiwslgmh
      301 gkngvtcvdc hmpkvqgkdg kvytdhqiqn pfdafdrtca nchdqsrekl rdivtsrkke
      361 vkdvmgrlee qvvkahfeak aawdagatke emeaalmdir haqwrwdyaa ashgghmhap
      421 evvlrvlgsg ldkaadartk laailtkhgv ktpvqipdis tadkawkvmg idiekerkak
      481 eeflktvvpq weqqakekgl lvdppaqk
//
LOCUS       WP_111413781             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Billgrantia lactosivorans].
ACCESSION   WP_111413781
VERSION     WP_111413781.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia lactosivorans
  ORGANISM  Billgrantia lactosivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Billgrantia lactosivorans"
                     /db_xref="taxon:2185141"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55703
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela kgearvaltp dsaqfiqklg hecliesgag vaagfddday raagvtvves
       61 aealwqqaev vikvrepsea eaerlregqt liaffwpaqn eallekcraq gatviamdmv
      121 prisraqkmd alssmaniag yravieagnq fgrfftgqvt aagkvppakv liigagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed nqdgsgtggy aapsspefre
      241 kqlalfreqa pevdivista lipgrpapkl wledmvkamk pgsvivdlaa ekggncdltv
      301 pderivtdng vvvvgytdfp srmatqasll yatnvrhmlt dltpekdgri vhdmeddvir
      361 gatvthqgei tfpppppkvk aiaaakpkpr ekeptpeerr aaelaafkaq tkrqvtllga
      421 ggllmlllgq vapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgiiilga
      481 vlqigsgnwl vvlmaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_111420739             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodoplanes roseus].
ACCESSION   WP_111420739
VERSION     WP_111420739.1
KEYWORDS    RefSeq.
SOURCE      Rhodoplanes roseus
  ORGANISM  Rhodoplanes roseus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodoplanes.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rhodoplanes roseus"
                     /db_xref="taxon:29409"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39246
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaicaead taeprvagtp etvkkikalg advavepgag vksgildady eaagatisrd
       61 aardadivfk vrrpnemelt gykkgalvva imdpygheaa laalaragvt afamelmpri
      121 traqvmdvls sqanlagyra vidasaeygr afpmmmtpag tvpaakafim gvgvaglqai
      181 atarrlgaiv tatdvrpavk eqvaslgakf iavedeefkq aetaggyake mskeyqakqa
      241 aliaehvkkq divittalip grpapklita emvasmkpgs vivdlaverg gnvegakpge
      301 vvdvngvkiv ghlnvagrla asssalyskn llaflevlvd kktkqlalnw ddeilkatcl
      361 trdgavvhpn fapktaa
//
LOCUS       WP_111432847             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodobium
            orientis].
ACCESSION   WP_111432847
VERSION     WP_111432847.1
KEYWORDS    RefSeq.
SOURCE      Rhodobium orientis
  ORGANISM  Rhodobium orientis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhodobiaceae; Rhodobium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rhodobium orientis"
                     /db_xref="taxon:34017"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39283
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavplesd pvearvaltp etakrfvglg aevvvqkgag alsrfpdeay ekagaklakd
       61 akatlsgadv vlkvrrpnad elklikkgtl vvatmdpfgh eddvkamaea gitavtmdfm
      121 pritraqvmd vlssqanlag yqavidaael fdrampmmmt aagtvsaakv fvmgagvagl
      181 qaiatakrlg aivsatdvrp aakeqveslg grfvavedee fkeaetaggy akemsddykk
      241 kqaelvashi akqdivitta lipgrpapkl vtkdmlasmq pgsividlav erggnvegsv
      301 agevatvgdv kvagylnvpg riaataslly aknlyafvet lidkeakala vdwedelvka
      361 tvltrdgsiv hpafag
//
LOCUS       WP_111456341             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phenylobacterium hankyongense].
ACCESSION   WP_111456341
VERSION     WP_111456341.1
KEYWORDS    RefSeq.
SOURCE      Phenylobacterium hankyongense
  ORGANISM  Phenylobacterium hankyongense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Phenylobacterium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Phenylobacterium hankyongense"
                     /db_xref="taxon:1813876"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38679
     Region          3..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,95,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maviavtker ragetrvaav petvkkliaa gfavtveaga gsaasypdad yaaagatiak
       61 tlkdalakad ilfkvrapea deiaalpkga ivaavlnpyq dkaqlealak agatafamef
      121 vpritraqvm dvlssqanla gyraviegae aygrampmmm taagtiaaak vfvmgvgvag
      181 lqaiatarrl gavvtatdvr patkeqvesl gakflavede efknaqtagg yakemsaeyq
      241 akqaelvssh iakqdmvitt alipgrpapk lvsaaqvasm kpgsvivdla ieqggnvega
      301 klgevavtqn gvkilgvanl pgriaadasa lyarnlfafa glflnkegqf apdyedeilk
      361 aalvtqggav vhpqlks
//
LOCUS       WP_111460702             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. URMO17WK12:I2].
ACCESSION   WP_111460702
VERSION     WP_111460702.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. URMO17WK12:I2
  ORGANISM  Pseudomonas sp. URMO17WK12:I2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. URMO17WK12:I2"
                     /db_xref="taxon:1261623"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38420
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikkligqg hqvtvqtgag vaasitdtay vaagasigda
       61 aaafgaelil kvaapsdtel almnsgavlv gmlnpfsnet iarlnaagvt afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recavgvggy arpmpaswme
      241 rqakavhera kqadivitta lipgrkaptl lheatvaemk pgsvvidlaa iqggncplte
      301 ldkvvtkhgv tlvghgnlpa lvaadasaly arnlldflkl vidpsgafhl nleddivaac
      361 lmckggeivr vnk
//
LOCUS       WP_111467267             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cereibacter changlensis].
ACCESSION   WP_111467267
VERSION     WP_111467267.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter changlensis
  ORGANISM  Cereibacter changlensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cereibacter changlensis"
                     /db_xref="taxon:402884"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54884
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaakesf agearvamtp dsalqlqklg htcvietgag akagfsddsy aaagvtvlps
       61 aqalydaadv vvkvrgpepa eaemlragqt lisffwpaqn aelleqckak gatviamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfae aqdgaatggy aapsspefre
      241 kqlekfrala pemdivitta lipgrpapkl wladmvsmmk pgsvvidlaa erggncdltv
      301 pdekvvspng vtivgytdyp srmaaqsstl yatnirhmlt dltpkkdgvi vqnmeddvir
      361 gatvthdgai tfpppppkia aiaaqkpkek akeltpeekr aketaafrka tvsqvtllav
      421 gtallmlvgi yapasfmshf ivfalscfig fqviwnvshs lhtplmavtn aisgivilga
      481 llqigsgnwl vvilaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_111472131             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Roseicella
            frigidaeris].
ACCESSION   WP_111472131
VERSION     WP_111472131.1
KEYWORDS    RefSeq.
SOURCE      Roseicella frigidaeris
  ORGANISM  Roseicella frigidaeris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseicella.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Roseicella frigidaeris"
                     /db_xref="taxon:2230885"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39227
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,295,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,285..286,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavlkerr paetrvaatp etvkkliglg csvavetgag lasgipdaey aaagaevapd
       61 aaaalngagi vlkiraplgt gegavdelsl iprgalllgq lgadakaagt yaqlgidaga
      121 mellpritra qsmdilssqa nlagyravve aagafdrgfp mlmtaagtip aasvfimgag
      181 vaglqaiata rrlggrvsat dvrpaakeei kslgasfvgy eseeskqaqt aggyakqlsa
      241 efyaeqakvv aahiakqdiv vttalvqgrq apqlvsaemv ramrpgsiiv diaadaggnv
      301 altrpgemit tengvkilgy hnwpgriaga asalfarnll tflttfwdke akapklpaed
      361 eivkgvlltr ggavvhpnfa pakaa
//
LOCUS       WP_111494518             522 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Marinobacter].
ACCESSION   WP_111494518
VERSION     WP_111494518.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter
  ORGANISM  Marinobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Marinobacter"
                     /db_xref="taxon:2742"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55329
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkecy pgenrvaatp asvgkliklg htvvvetgag aaatyhdday rqagaeiadn
       61 aqdlwsaaef ilkvrgprfn eqadldetsl lkddsyllsf lwpaqnpell etlasrnvta
      121 fsidalpris raqkmdalsa mgniagyrav veasnrfgrf ftgqvtaagk vppakvmvig
      181 agvaglaaig aarsmgaivr afdtrlevke qvesmgadfl eldfeedgsg sggyakqmsk
      241 efieaemalf meqakevdii ittalipgkp aprlitadmv ramkpggviv dlaaeqggnc
      301 eltqpgevai engvsivgyt dlpsrmasvs sdlyatnlwh llseltpekd geiqvdmedt
      361 virgvavthe gkvtwpapqp ekpapkpaqp qaaaqpaaed adsgksgaka fwkgallvat
      421 vaalygigay apksflshft vfvlacfvgw qviwnvtasl htplmsvtna isgiivlgai
      481 lhlaqaqnlv igiiafvavl iacinigggf rvtyrmlkmf hr
//
LOCUS       WP_111501340             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptacidiphilus pinicola].
ACCESSION   WP_111501340
VERSION     WP_111501340.1
KEYWORDS    RefSeq.
SOURCE      Streptacidiphilus pinicola
  ORGANISM  Streptacidiphilus pinicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptacidiphilus.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptacidiphilus pinicola"
                     /db_xref="taxon:2219663"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53091
     Region          13..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msaqepahhp pqrigvvaes asgetrvaat patlrqllgl gyevvvesea gaasgftdea
       61 yleagarige awdadvvlkv napseaeiar lregatvvgl lapaqkpell ralaaagvta
      121 lsldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvkslggeyl pvnvvqeqst dgyakatsad
      241 ydraaaelyh qqaadvdivv ttalipgrpa prlltaedva amkpgsvvvd maaamggnve
      301 gtvagravvt dngvtiigyt dlasrlptqa sqlfgtnlvn llklltpgkd gqltidfedv
      361 vqravtvvqa gdvtwppppv svtaapaaqp aaappkpepk qpkltpagrl gliglgmlam
      421 flvvafapaq laenftvfal avvigyyvig kvhhalhtpl msvtnaisgi vvigallqig
      481 heswivttls cvailltsvn ifggfavtrr mlsmfskg
//
LOCUS       WP_111505171             311 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Paenibacillus odorifer].
ACCESSION   WP_111505171
VERSION     WP_111505171.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus odorifer
  ORGANISM  Paenibacillus odorifer
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Paenibacillus odorifer"
                     /db_xref="taxon:189426"
     Protein         1..311
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35989
     Region          12..170
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mysyeiytkr qkrlldqpvd plqytempkt friqvlhiwt saigafntyv dspqyllweq
       61 vqnilsrelg lfhlgdnrdn gpqsnckefl lrespenvln iidvsfnlln ikyrklnstd
      121 lddyiiiqsp dsaiselnkr frehnlgyqf enghiirvds lmihenitkp sltllhnnef
      181 kgaeeeflka yehfrhgrnk esiaealkaf estikticdr rrwvynpnkd tsstlidiif
      241 keglvpsylq shftslkstl tagvptlrnk tsghgqgent ielpehftay alhltatnil
      301 flvecylese e
//
LOCUS       WP_111509805             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium kyogaense].
ACCESSION   WP_111509805
VERSION     WP_111509805.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium kyogaense
  ORGANISM  Mycobacterium kyogaense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Mycobacterium kyogaense"
                     /db_xref="taxon:2212479"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52205
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgetrvaatp qtvgqllklg yevavesgag aaasfsdaay teagatigdp
       61 wagdiilkvn apndyeiall rdgatlisli spalkpelve klsarpvtvl amdavprisr
      121 aqsldvlssm aniagyravv eaahrfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivra tdprpevadq vkslggeyla vdpaaaevsv tgyakemgdd ykareaalya
      241 dqakdvdiii ttalipgrpa priitadmva smrpgsvivd maaanggnve gtvkdqavvt
      301 dngvtiigyt dlagrlpata sqlygtnlvn llklvtpekn gelrldfqdv vqrsvtvvrd
      361 geltwppppv qvsaapaaka aepvaqkpvk kpmsmgrrlg itfaaaavlf alialspaal
      421 qvhltvfala ivigyyvign vhhalhtplm svtnaisgii vvgallqigh gnpvitavaf
      481 aaillasinv fggfavtrrm lamfsrs
//
LOCUS       WP_111513434             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phenylobacterium deserti].
ACCESSION   WP_111513434
VERSION     WP_111513434.1
KEYWORDS    RefSeq.
SOURCE      Phenylobacterium deserti
  ORGANISM  Phenylobacterium deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Phenylobacterium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Phenylobacterium deserti"
                     /db_xref="taxon:1914756"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38518
     Region          3..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,95,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpviavtqer ragetrvaav petvkkliaa gfsvvverga glaaacpdad yeaagasvaa
       61 saqealaaad vafkvrapad eeiaalkpga lvvgllnphq drvvldalat kgvsafamef
      121 vpritraqvm dalssqanla gyravieaaq aygkalpmmm taagtiaaak vfvmgagvag
      181 lqaiatarrl gavvtatdvr paakeqvesl gakfvavede efkqaetaag yakemsaeyk
      241 akqaalvsdh irkqdivitt alipgrpapr lvsadqvasm kpgsvlvdla veqggnvegs
      301 rvgevfdtag vkivgypnlp grvaadasal yarnltafat llmnkegqfa pdledeilka
      361 alvthggavv hpslka
//
LOCUS       WP_111529909             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phenylobacterium soli].
ACCESSION   WP_111529909
VERSION     WP_111529909.1
KEYWORDS    RefSeq.
SOURCE      Phenylobacterium soli
  ORGANISM  Phenylobacterium soli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Phenylobacterium.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Phenylobacterium soli"
                     /db_xref="taxon:2170551"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38573
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,95,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 masiavtker ragetrvaav petvkkliaa gfsvtveada glaasylddd ykaagatiak
       61 takdavgaad ilfkvrapea deiaalksga ivvallnphq dkasldalak kgatafamef
      121 vpritraqvm dalssqanla gyravieaae aygkampmmm taagtvaaak vfvmgvgvag
      181 lqaiatarrl gavvtatdvr patkeqvesl gakfvavede efkaaetaag yakemsaayq
      241 akqaelvsgh iakqdivitt alipgrpapr lvsaaqvasm kpgsvivdla veqggnvega
      301 klgevavtkn gvkilgipnl pgriaadasa lyarnlfafa glfldkegkf apdyedeilk
      361 aalvtqagai thpalka
//
LOCUS       WP_111544931             431 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium kowhaii].
ACCESSION   WP_111544931
VERSION     WP_111544931.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium kowhaii
  ORGANISM  Mesorhizobium kowhaii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Mesorhizobium kowhaii"
                     /db_xref="taxon:1300272"
     Protein         1..431
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44267
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvvetg agtrsripde efakagavig
       61 kadavakadv vlkvrrptda elkgykpgta vvaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaaki fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegae
      301 agkvvttang vkivghlnvp grvaasasll yarnlfafle tlvdktaktl ainrdddlvk
      361 atmltdagki vhpafikadq qppkgqsvep aaipattmva daspkpaaak kaatkkpaas
      421 kspsskskgi a
//
LOCUS       WP_111535427             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Palleronia
            aestuarii].
ACCESSION   WP_111535427
VERSION     WP_111535427.1
KEYWORDS    RefSeq.
SOURCE      Palleronia aestuarii
  ORGANISM  Palleronia aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Palleronia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Palleronia aestuarii"
                     /db_xref="taxon:568105"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56023
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgvigets egearvaltp asaeqlqklg hdcvieagag gkadftdeay rdagvdvldn
       61 aqavfeaadv iakvrppsea evdmlregqt lisffypsen ealmkraaer gatliamdmv
      121 prisraqkmd alssmaniag yravveaann fgrfltgqit aagkvppaki lvvgagvagl
      181 aaigtatsmg aivrafdvrp etseqiesmg aeflfldfdd sdagsgeggy akpsspefre
      241 kqlalfkeqa pdvdivitta lipnqeapel wteemvkamk pgsvivdlaa erggnckmtr
      301 kdekfvtdng vtiigytdfp srmatqastl yatnvrhmma dltpekdgki vhdmeddvir
      361 gatithgkev twpppkpktk aqaapqkrek kkeltpeekr aqeveafkkd tqfqvgvlva
      421 gavvlllvga yapesfmshf ivfalacfvg fqviwgvahs lhtplmavtn aisgiiilga
      481 llqigasswi vvflsfvsvl iasinivggf lvtrrmlsmf qks
//
LOCUS       WP_111549655             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salipiger
            aestuarii].
ACCESSION   WP_111549655
VERSION     WP_111549655.1
KEYWORDS    RefSeq.
SOURCE      Salipiger aestuarii
  ORGANISM  Salipiger aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Salipiger.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Salipiger aestuarii"
                     /db_xref="taxon:568098"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55094
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkela hgenrvamtp dsaralhklg heclvesgag aaagfadaay eaagvtvvds
       61 aevlyaqadv iakvqppsda evdrlgqgkt lisffwpaan ealmqraadt gasviamdmv
      121 prisraqkmd alssmaniag yravieagsn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee dqadgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtpdmvaam kpgsvivdla aerggnckmt
      301 vkdekivtdn gvtivgytdf psrmatqsst lyatnirhmm tdltpdkdgv vnhnmdddvi
      361 rgatiahggd vtwpppppkt kaiaaqkpke kapeltpeek raaetaafka qtktqvtlla
      421 vggalllavg lvapasfmqh fvvfvlsvfi gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgnw ivivlaalsv fmtginifgg fmvtrrmlam fqks
//
LOCUS       WP_111554090             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Kitasatospora sp. SolWspMP-SS2h].
ACCESSION   WP_111554090
VERSION     WP_111554090.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora sp. SolWspMP-SS2h
  ORGANISM  Kitasatospora sp. SolWspMP-SS2h
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Kitasatospora sp. SolWspMP-SS2h"
                     /db_xref="taxon:1305729"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52069
     Region          13..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msgndssarp pqrvgvvaes vpgetrvaat patvrgllgl gyevvvesga gaasgfddaa
       61 yaaagatvgd awaaevvlkv napseaevgr lregavlvgl lapaqrpell aalaargvta
      121 lsldavpris raqsmdvlss maniagyrav ieaahafgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvrslggeyl aveavqeasa dgyakatsad
      241 ydraaaalyr aqaadvdivv ttalipgrpa prlltaedva amkpgsvvvd maaaqggnva
      301 gtvpgrtvvt dngvtligyt dlasrlpaqa sqlfgtnlvn llklltpgrd grlaidfedv
      361 vqravtvvre gettwppppv avsaapaapp aappaavgag aarvtpavrf gliglgmlal
      421 flliafapaq laenftvfal avvigyyvig kvhhalhtpl msvtnaisgi vvigallqig
      481 hesalvtvls availltsvn vfggfavtrr mlsmfskg
//
LOCUS       WP_111559392             300 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Paracoccus sediminilitoris].
ACCESSION   WP_111559392
VERSION     WP_111559392.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sediminilitoris
  ORGANISM  Paracoccus sediminilitoris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Paracoccus sediminilitoris"
                     /db_xref="taxon:2202419"
     Protein         1..>300
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..>300
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkenh pgearvaitp asaghlaklg hevfvqtgag tgagfsdddy gkadvticqs
       61 aseligavdv vtkvrqptea elnqmregqt visffypaqn sellarakek gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aqvhafdvrp evseqiesmg aefvflefdq ptedgaatgg yaapsspefr
      241 ekqlakfrel apqmdivitt alipgrdapv lwtadmvaam kpgsvivdla aekggncelt
//
LOCUS       WP_111576346             400 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Falsochrobactrum ovis].
ACCESSION   WP_111576346
VERSION     WP_111576346.1
KEYWORDS    RefSeq.
SOURCE      Falsochrobactrum ovis
  ORGANISM  Falsochrobactrum ovis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Falsochrobactrum.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Falsochrobactrum ovis"
                     /db_xref="taxon:1293442"
     Protein         1..400
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41255
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msqiifipte rssgetrvaa spdtvkllaa lgfdvvvesg agqlsriide dyakagatig
       61 stsaaasadv ilkvrrpsad elktykagai vlaamdpygn ddaiaamaka gisafsmefm
      121 pritraqsmd ilssqanlag yqavidaaae ydralpmmmt aagtvpaakl fvmgagvagl
      181 qaiatarrlg avvtatdvrp avkeqvaslg akfiavedee fkaaetaggy akemsaeyqa
      241 kqaaltadhi akqdivitta lipgrpapkl isadmvasmk agsvivdlav erggnvegsv
      301 pdqvvttang vkiighlnvp grvaasasll yarnlfafle tmvnketktl svdpedelvk
      361 atllthggrv vhpafakael dqpqptapkk staskaqggv
//
LOCUS       WP_111577702             376 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Chitinophaga].
ACCESSION   WP_111577702
VERSION     WP_111577702.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga
  ORGANISM  Chitinophaga
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Chitinophaga"
                     /db_xref="taxon:79328"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40048
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miagilkekn getrvslvpe vvkqlqqmsv tvwveqgagd hafynddaym qagaeiktaa
       61 silagadiif tlqppskeit dqippgkiia gilqplyrvn eveywasrni tafsldtipr
      121 ttraqvmdvl ssqaniagyk avllaaysys ryfpmfmtaa gsiapakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgak fvevegaada ssaggyaveq setykqqqqq
      241 rigesiakad ivittaqipg kaapvlvsne mldrmrpgsv ivdlaaatgg ntsatknnet
      301 vqykgvtiig nsnlpatmpa dasklyaknl fnflkliltk egalhlnfed divkgacith
      361 ngeivndrvk nlmqpa
//
LOCUS       WP_111588284             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas salmonicida].
ACCESSION   WP_111588284
VERSION     WP_111588284.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53201
     Region          22..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrlt rlglaalllt tcfgasglaq adeatpkgkl earselfakd hvdqfsswkg
       61 tsesatrtda laedpqmvvl wggypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eqyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqskemlqgi vqqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaqmk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llatkgishe ialpdistke kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_111590511             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga dinghuensis].
ACCESSION   WP_111590511
VERSION     WP_111590511.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga dinghuensis
  ORGANISM  Chitinophaga dinghuensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Chitinophaga dinghuensis"
                     /db_xref="taxon:1539050"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39722
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mivgilkekn retrvslvpe vvkqlqqmsv tvwveqgaga saffddqqyv aagavirses
       61 eilsqadiic aihppgaell atippgkivi galqplyrpr eveqwasssi talsldaipr
      121 ttraqsmdvl ssqaniagyk avllaaytys ryfpmfmtaa gsiapakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgak fvevegaada saaggyaveq sadyqrlqqq
      241 riaestakad iiittaqipg kkapvlitae mldnmragav ivdlaaatgg ntaatrnnen
      301 ylhngvtiig dsnlaatmps dasklyarnl lnflkliltk egkldinfnd divagacith
      361 ngeivnervk gmlqpa
//
LOCUS       WP_111599439             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga skermanii].
ACCESSION   WP_111599439
VERSION     WP_111599439.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga skermanii
  ORGANISM  Chitinophaga skermanii
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Chitinophaga skermanii"
                     /db_xref="taxon:331697"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40191
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgvlkekl nenrvslvpe vvkqlaqlkv nvwveagagk qawytdeayl eagatiqsre
       61 kilqeadill sihqpdkpew eqvtagktwi gvyqplykaa lmqdlaaknf tvfsldsipr
      121 ttraqsmdvl ssqaniagyk avllaantys ryfpmfmtaa gsippakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevlslgak fvevegaada skaggyaveq tseykqqqea
      241 kitqaiakad ivittaqipg kpapilvttg mleamkpgsv iidlaaatgg ntsqtknnts
      301 vvynnvtivg nselpssmpa daskvyaknv ynflqllidk tgqftlnfed divkgacith
      361 ggqvtnervl qslgvta
//
LOCUS       WP_111602092             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. Amel2xB2].
ACCESSION   WP_111602092
VERSION     WP_111602092.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. Amel2xB2
  ORGANISM  Streptomyces sp. Amel2xB2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Streptomyces sp. Amel2xB2"
                     /db_xref="taxon:1305829"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53600
     Region          8..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msdshpqqvg vvaesraget rvaatpdsir kilklgyetv vesgagaasg fsdeqyteag
       61 atigdawqad vvlkinepsr eeigrlrdga aligmiapgl ntslldelaa rpltvlsmda
      121 vprisraqsl dvlssmania gyravieaah vfgrfftgqv taagkvppak vlvagagvag
      181 laaigaassl ggvvratdpr pevadqvrsl ggeylavdve qeqsadgyak qtsedydrra
      241 aeiyseqaad vdiivttali pgkpaprlit aedvasmksg svivdmaasq ggnvegtvpg
      301 kaivtdngvt iigytdlpgr lpaqasqlyg tnvvnllkll tpekdgqftl dfddvvqrav
      361 tvvrdgektw ppppvqvsaq aapakgaega ggqgagaaan epkkprltpa arftligvam
      421 aamfaliafs paqlaanftv falavvigyy vigkvhhalh tplmsvtnai sgivvvgall
      481 qighvgpavt vlsfiaillt svnifggfsv trrmlgmfsk g
//
LOCUS       WP_111613337             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus yeomjeoni].
ACCESSION   WP_111613337
VERSION     WP_111613337.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus yeomjeoni
  ORGANISM  Algoriphagus yeomjeoni
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Algoriphagus yeomjeoni"
                     /db_xref="taxon:291403"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40265
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvlketk egenrvslsp dvikqlikke fsvivesgag igsnfsdedy kqsgatvgna
       61 adiytadill kvniftkeei aqmkngsacm simyaynhpe ilaelnkksi tsfsmdavpr
      121 israqkmdcl ssqanlagyk svilganyle kifplmmtas gtitpakvli fgagvaglqa
      181 iatakrlgav vevsdvrpet keqveslggr fltvegaeev kveggyasev saeflqkqke
      241 liqskikdsd lvittalvmg kkspilvtee mvktmkkgav ivdmavesgg nceisekdqi
      301 vkkhgvtiig esnlpsllst nasqlyatni stllmhlatk dgfnldrdee itkgvlitfe
      361 gqvvheftnk ilnk
//
LOCUS       WP_111624707             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arenibacter echinorum].
ACCESSION   WP_111624707
VERSION     WP_111624707.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter echinorum
  ORGANISM  Arenibacter echinorum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Arenibacter echinorum"
                     /db_xref="taxon:440515"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39616
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigilketl dgerrvaitp niakqliasg feliveegag eyssfmdsdy knvgvavekr
       61 avifheaevl lkinpfdeed lklvdkgqil isklyhksnp eliqaiankg vsafsmdaip
      121 risraqdmdv lssqnnlagy kavilgafem tkifplmmts agtiaparvl iygigvaglq
      181 aiatakrlga iveatdirse tkeqaeslga kfisvdnege eseggyakea sadylkrqke
      241 avnkslfkad lvittanipg rkapvlitee qvmqmkngav iidlaaaqgg ncevseinkt
      301 ivkngvkvig tsidprsvst nasdlyakni ynyiihlteg tnfkwdleee itdetlivqn
      361 gtirks
//
LOCUS       WP_111642924             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinimicrobium alkaliphilum].
ACCESSION   WP_111642924
VERSION     WP_111642924.1
KEYWORDS    RefSeq.
SOURCE      Marinimicrobium alkaliphilum
  ORGANISM  Marinimicrobium alkaliphilum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Marinimicrobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Marinimicrobium alkaliphilum"
                     /db_xref="taxon:2202654"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40422
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,323,325)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,330..331,335,
                     338..339)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipkerr aherrvaatp etvkkyialg ytvavetgag egsripdaay eevgaslapd
       61 aatlladadi vlkvqrpila gedgpdelal ipkgalvlal mapydapdsl kayaqagita
      121 valelvprit raqsmdvlss qsnlagyrav leacnvynra fpmmmtaagt iaparvmvlg
      181 agvaglqaia takrlgavvs atdvrpvake qveslggkfv mveseetaea etaggyakam
      241 sedyqrrqaa lvaetlkkqd ivictalipg rkaptlvnda mvhsmrpgsv ivdmaaeqgg
      301 nctlttpgei tqvggvtiig lfnlpsrlat dasglygknl fnylaplyde atkqlaidwa
      361 deivtasvlt rdgrivhsaf aaqdggq
//
LOCUS       WP_111653886             504 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinoplanes lutulentus].
ACCESSION   WP_111653886
VERSION     WP_111653886.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes lutulentus
  ORGANISM  Actinoplanes lutulentus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Actinoplanes lutulentus"
                     /db_xref="taxon:1287878"
     Protein         1..504
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51311
     Region          1..503
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigvprdph pgerrvsatp atvaqlvklg ydvvvesgag agssfsdday aqsgatigdp
       61 laadivfain pppaeqldrl apgttvigml nprldpdlva dlarrpital smdavprisr
      121 aqsldvlssm aniagyravv esahafgrff tgqvtaagkv apakvlvaga gvaglaaiga
      181 agslgaivra tdprpevadq vrslggeyls veaadvevss tgyakemsdd yteraarlya
      241 tqagdvdiii ttalipgrpa pklitapmva smkpgsvivd maaanggnve gtvpgevvvt
      301 angvtiigyt dlpgrlpaqa sqlygtnlvn lmklmtpekd gqlvvdfedv vqrsiavvhe
      361 geltwpppvv avsaaapaav avappvkavk kpinplaivg ggaaalfllt alapaalrgh
      421 ltvfalaivi gyyvighvhh alhtplmsvt naisgiivvg allqighgda vvtglafvat
      481 llasinifgg favtrrmlam fsrs
//
LOCUS       WP_111672420             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus litoralis].
ACCESSION   WP_111672420
VERSION     WP_111672420.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus litoralis
  ORGANISM  Algoriphagus litoralis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Algoriphagus litoralis"
                     /db_xref="taxon:2202829"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40475
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigviketk eferrvalsp dvvkllkkke feviiesgag dgsyfsdedy qnagatvsgl
       61 advfssdill kvniptleei aqmkpgaaci symyayqhpd iidalnaksi tsfamdavpr
      121 israqkmdal ssqanlagyk svilganhlg kifplmmtas gtitpakvli fgagvaglqa
      181 iatakrlgai vevsdvrpet keqveslggr fltvdgaesv kteggyakev saeflekqqq
      241 likdkikdad lvittalvmg kkspilvtee mvksmkagsv ivdmavesgg ncaiseknkt
      301 vvkhgvtlvg esnlpsllpv nasqlyatni stlllhlftp lalnpnleee itkgvlithe
      361 gklvheftks iinsqpknl
//
LOCUS       WP_111708474             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Lutibacter
            citreus].
ACCESSION   WP_111708474
VERSION     WP_111708474.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter citreus
  ORGANISM  Lutibacter citreus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Lutibacter citreus"
                     /db_xref="taxon:2138210"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39928
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvlkeqk igekrvaltp kiakqliekg feiiveegag essanknsdy kaigasietr
       61 gvvfkeatil vkinpfdeed lklidkrhil msqlyhisnk dlieaiaakg atafsmdamp
      121 ritraqdmdv lssqnnlagy kavikgayem tkifplmmta agtitpsrvl iygigvaglq
      181 aiatakrlga iveatdirme tkeqaeslga kfisvdntge qkaeggyake asedyvkrqk
      241 eavneslfka dlvittamvp grkspvlitk dqveqmknga viidlaaaqg gncelsklne
      301 tiikngvkii gttiapesva tnasdlyakn mynflvhlvn dtnefnwdle deitdgtliv
      361 qegkirkn
//
LOCUS       WP_111720810             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Homoserinimonas sp. OAct 916].
ACCESSION   WP_111720810
VERSION     WP_111720810.1
KEYWORDS    RefSeq.
SOURCE      Homoserinimonas sp. OAct 916
  ORGANISM  Homoserinimonas sp. OAct 916
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Homoserinimonas.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homoserinimonas sp. OAct 916"
                     /db_xref="taxon:2211450"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38861
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqvgvlserv dgerrvavtp esakqliaag levlveagag vkaglpdsay teagaivqns
       61 vdlsvldvlc hvrpltaaqv aelhrgaitv glaspstela tvkalaaggi tsfalelvpr
      121 israqsmdal tsqslitgyr avleaatrfs rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsaydvrpas adevtsmggt fvhldldave gqggyarels edralrqqql
      241 ltphvagadv littaaipgr aapllvttem vagmrpgsvi vdlaaetggn vegvlpgvdh
      301 qvpttvgdga vtlyglkdaa sdmatdasrl yaknvsnlie lmtaegevap dfddelvagt
      361 clthdgqvrh aptaaalegd
//
LOCUS       WP_111727304             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            cinerea].
ACCESSION   WP_111727304
VERSION     WP_111727304.1
KEYWORDS    RefSeq.
SOURCE      Neisseria cinerea
  ORGANISM  Neisseria cinerea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria cinerea"
                     /db_xref="taxon:483"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53905
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsegel pllkegqtiv sflwprqnea lvealcakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfitdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqq qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_111732059             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseovarius amoyensis].
ACCESSION   WP_111732059
VERSION     WP_111732059.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius amoyensis
  ORGANISM  Roseovarius amoyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseovarius amoyensis"
                     /db_xref="taxon:2211448"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55640
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeil egenrvamtp dsakalqklg ydcvietgag vgagfrdady eaagveivkt
       61 aaalfkeadi vakvrvptea elkrlrkgqt litffnpaen etglelaakk gasviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfee tgqdsaatgg yaapsspefr
      241 ekqlekfrel apdmdivitt alipgrpapk lwtedmvaam kpgsvivdla aerggncdlt
      301 kpderivtdn gvtiigytdf psrmaaqast lyannirhmm ddltpekdgk pvhnmeddvi
      361 rgatvthgge vtypppppkv kaiaapakkp aekeltpeer karelaefqa qtkrqvtlla
      421 igaalvlgvg liapasfmqh livfvlsvfi gfqviwnvsh slhtplmavt naissiiivg
      481 allqigsgaw lvvllaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_111750628             485 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Glaesserella].
ACCESSION   WP_111750628
VERSION     WP_111750628.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella
  ORGANISM  Glaesserella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Glaesserella"
                     /db_xref="taxon:2094023"
     gene            1..485
                     /gene="nrfA"
     Protein         1..485
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=54209
     Region          1..483
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkrvskmlkn slvatmamlg cihsavagea kefepakpev kiesanhkfa elyplqyqsw
       61 aatgeskeit saleedprlv ilwtgyafsk dynkprghfy avtdvrnilr tgapmepdag
      121 pqpmacwack spdvprmiae kgevgyfdak wakygseivn pigcadchdt tsqefkdgka
      181 alniarphvl raldvigwkf dgldkhgkra avcsnchvey yfagkekavt fpwdkgvdvd
      241 siekyfdeik ftdwvhglsk apmlkaqhpd fetwalgthg kngvtcidch mpkvetkdgk
      301 vytdhkignp fdnfehtckt cheqskeslq arvkehkkqi kdvmgrledq lvkahfeakk
      361 awevgateee mkdalqairh aqwrwdysaa ghgghmhapd vilhvlgtgl draadartkl
      421 aviltkhgvq tpiefpdist kekaqkvvgi dfdkekaake eflrtvvpqw ekeakekgll
      481 padak
//
LOCUS       WP_111771460             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_111771460
VERSION     WP_111771460.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36074
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafkyid tylrtyevtl
      121 glepdkaise lnnifhdhgl kyryengriv rlrrikrlkn iryylyspge ygfveydlme
      181 aynrlmlndf acvvrechav frrvlirihe rkgivyheqd slntlmanlm argvisaeya
      241 hkfhflsnvl eseiflpiap ekshhhyvmm lriseelacs iyyltersif fltqraeedd
      301 vap
//
LOCUS       WP_111769563             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_111769563
VERSION     WP_111769563.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35845
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnlfhehgl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf scvvkechaa frsvllrihe rkgivyheqd slntlmanlm argvisaeyt
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 aap
//
LOCUS       WP_111779358             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Shigella
            flexneri].
ACCESSION   WP_111779358
VERSION     WP_111779358.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53628
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhh dqylswkats
       61 eqservdala edprlvilws gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_111785241             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agrobacterium tumefaciens].
ACCESSION   WP_111785241
VERSION     WP_111785241.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium tumefaciens (Rhizobium radiobacter)
  ORGANISM  Agrobacterium tumefaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Agrobacterium tumefaciens"
                     /db_xref="taxon:358"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55655
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely egearvgmtp dsaqalqklg ydciletgag kaagfsdday raagvtivds
       61 adalyagsdi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfae qqdgaatggy aapsspefre
      241 kqlekfrela pqidivitta lipgrdapkl wladmvaamk pgsviidlaa erggncdltv
      301 pdqrvvsdng vivigytdfp srmatqastl ystnirhmmt dltpakdgkp vhnmeddvir
      361 gatvtyqgei tfpppppkiq aiaaqkpker akeltpeekh akeraefkaq tksqvgllvi
      421 gtavlllvgl yapasfmshf ivfvlacfig fsviwnvshs lhtplmavtn aisgiviiga
      481 llqigsgnwl vvilaslsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_111779712             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Shigella
            flexneri].
ACCESSION   WP_111779712
VERSION     WP_111779712.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53622
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhh dqylswkats
       61 eqservdala edprlvilwa gypfprdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_111793418             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agrobacterium tumefaciens].
ACCESSION   WP_111793418
VERSION     WP_111793418.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium tumefaciens (Rhizobium radiobacter)
  ORGANISM  Agrobacterium tumefaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Agrobacterium tumefaciens"
                     /db_xref="taxon:358"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55742
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely egearvgmtp dsaqalqklg ydciletgag kaagfsdday raagvtivds
       61 adalyagadi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfae qqdgaatggy aapsspefre
      241 kqlekfrela pqidivitta lipgrdapkl wradmvammk pgsviidlaa erggncdltv
      301 pdqrvvsdng vivigytdfp srmatqastl ystnirhmmt dltpakdgkp vhnmeddvir
      361 gatvtyqgei tfpppppkiq aiaaqkpker akeltpeekh akeraefkaq tksqvgllvi
      421 gtavlllvgl yapasfmshf ivfvlacfig fsviwnvshs lhtplmavtn aisgiviiga
      481 llqigsgnwl vvllaslsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_111783495             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Agrobacterium].
ACCESSION   WP_111783495
VERSION     WP_111783495.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55701
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely dgearvgmtp dsaqglqklg ydciletgag kaagfsdday raagvtivds
       61 adalytgadi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qsqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvaam kpgsviidla aerggncdlt
      301 vpdqrvvsdn gvivigytdf psrmatqast lystnirhmm tdltpakdgk vvhnmeddvi
      361 rgatvtyqgd itfpppppki qaiaaqkpke rakeltpeek hakeraefra qtksqvgllv
      421 igtaalllvg lyapasfmsh fivfvlacfi gfsviwnvsh slhtplmavt naisgiviig
      481 allqigsgnw lvvilaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_111812472             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter soli].
ACCESSION   WP_111812472
VERSION     WP_111812472.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter soli
  ORGANISM  Acinetobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter soli"
                     /db_xref="taxon:487316"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39882
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipteti agenrvaatp etvkklisag hrvliergag vraayidsay eqvgatited
       61 vysgsqlilk vrapqgdeiq klaahttvva mfdpyrnpdl dtfasqnvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak eqveslggkw ldvpmspeeq aradeaakng ygwtpgeqyi
      241 kdqaaivdka vsnadivitt allpgrnapr likaetvakm kpgsvildma vetggnvegs
      301 kvgetiften gvkilgvpni pstlsteasa lyarnvfnfv etlfdqdknf ainpeeeiqk
      361 allvthgghv llkrg
//
LOCUS       WP_111819075             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces sp. Z5].
ACCESSION   WP_111819075
VERSION     WP_111819075.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces sp. Z5
  ORGANISM  Actinomyces sp. Z5
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Actinomyces sp. Z5"
                     /db_xref="taxon:2250216"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53155
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgipcqpp drsmtaatpq tveqlirlgy dvvvqrgaga paqfpdaaye eagaqladra
       61 etwgcnvvvt ayapddaeld lmhpgatlig rldparhpel vqslqdhslt alaidtvpri
      121 sraqsmdvls sqanlagyra vieaaahfgr llngqvtaag kfppasvyvi gagvaglaai
      181 gtayslgavv kgtdvrpeva dqvksvgaef vpvptaqevs adgyakemst dqaalanaly
      241 aeqsaaadiv ittanipgrr apllldraai damqpgsviv dmaaanggnt eltvpgevvt
      301 tdsgvtivgy tdlaerlpaq asqlygrnil nlltlvtpak dgdltldldd qvvraitvcq
      361 agellwpppp vavsaapkap aaptpepapd asgdaeaqaa ararsrrrms iglalaavav
      421 avlvlvtpaa atshyivlal avilgfhvis nvtpalhtpl msvtnaisgi illgaisqvg
      481 nanpaisava fiaillasin vfggfavtnr mlamfrke
//
LOCUS       WP_111827030             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter sp. HZ01].
ACCESSION   WP_111827030
VERSION     WP_111827030.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. HZ01
  ORGANISM  Achromobacter sp. HZ01
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter sp. HZ01"
                     /db_xref="taxon:1416886"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38543
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkyvggk htvvvergag saarypdday eaagatlgta
       61 qdalgaglvm kvrapdaael ahmkagtvvv gmldpfdaeg lqrmaaaglv gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaarvvvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgtggy arpmppawma
      241 rqavlvaerc kqadivitta lipgrpaptl vsadtiaamk pgsvlvdlav erggncplse
      301 kgqivekhgv tligltnlpg lvatdasaly arnildflkl itdaegalai rrddeivaac
      361 lmceggnvtr rt
//
LOCUS       WP_111833819             310 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Agrobacterium tumefaciens].
ACCESSION   WP_111833819
VERSION     WP_111833819.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium tumefaciens (Rhizobium radiobacter)
  ORGANISM  Agrobacterium tumefaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Agrobacterium tumefaciens"
                     /db_xref="taxon:358"
     Protein         1..310
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35083
     Region          5..171
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mavfdlyskr qkrirgevpd vytydqlsns lrvqigylik qglnpsdsls agrvrstfkf
       61 ivdtlraeyg vhslvatgyq eyapdfellh flanetdidr cldvvelsmr vidkltrtid
      121 ycyygaynen adeviqdlnt rfkesgvgyq fidgeiirvd selihteavk pairllntkd
      181 yagpheefls ayehyrhgnn kealneclka festmkavcd krgwtykttd takalidvcl
      241 snglippfwq qqmtslrsll essiptgrnk lsghgqgavp qevpdyltay mlhmtastlv
      301 flttaekelk
//
LOCUS       WP_111834176             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Agrobacterium].
ACCESSION   WP_111834176
VERSION     WP_111834176.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55740
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely egearvgmtp dsaqalqklg ydciletgag kaagfsdday raagvtivds
       61 aealyagadi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfae qsqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvaam kpgsviidla aerggncdlt
      301 vpdqrvvsdn gvivigytdf psrmatqast lystnirhmm tdltpakdgk pvhnmeddvi
      361 rgatvtyqge itfpppppki qaiaaqkpke rakeltpeek hakeraefka qtksqvgllv
      421 igtavlllvg lyapasfmsh fivfvlacfi gfsviwnvsh slhtplmavt naisgiviig
      481 allqigsgnw lvvllaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_111848386             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter baumannii].
ACCESSION   WP_111848386
VERSION     WP_111848386.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39810
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklisag hsvviergag vkaayidsay eqvgatitdd
       61 aytgsqiilk vrapqggeiq klaenttvva mfdpyrntel dqfanqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgaiv eatdlrptak dqveslggkw ldvpmseeeq qraadaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 kvgetvvten gvkilgipni patvateasa lyarnvfnfv etlfdkeknf ainqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_111859394             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter sp. CFCC 10889].
ACCESSION   WP_111859394
VERSION     WP_111859394.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. CFCC 10889
  ORGANISM  Acinetobacter sp. CFCC 10889
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter sp. CFCC 10889"
                     /db_xref="taxon:1775557"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39978
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgesrvaatp etvkklisag hnviiergag vraayidsay eqvgakitdd
       61 aytgsqlilk vrapkgeeiq klapnttiva mfdpyrnpdl dqfalqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptar dqveslggkw ldvpmsdeek qkaadaakng ygwmpgeeyi
      241 rdqaiivdka vsnadivitt allpgrdapr likaetvakm kpgsiildma vesggnvegs
      301 kcgenvvtdn gvtilgipni patvsteasa lyarnvfnfv dtlfdqdknf klnqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_111872601             485 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas bivalvium].
ACCESSION   WP_111872601
VERSION     WP_111872601.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas bivalvium
  ORGANISM  Aeromonas bivalvium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Aeromonas bivalvium"
                     /db_xref="taxon:440079"
     gene            1..485
                     /gene="nrfA"
     Protein         1..485
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53781
     Region          35..485
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivssckkpt wlglaallmt tllcapvqad eaqpkgkeaq pkgkietrse lfakdhadqf
       61 sswkatgesr ertdalaedp qmvvlwggya fakdynkprg hfyaltdvre tlrtgapksa
      121 edgplpmacw sckgpdvarv ideqgedgyf kgmwakggpe ivntigcadc hdtaskefke
      181 gkpalhlsrp yadramsaig kpfkeqgrfs qqsqvcgqch veyyftgptk avkfpwdkgt
      241 tveqmeqyyd eigfadwtha lsrtpmlkaq hpeyetwrag ihgqnnvacv dchmpkvqne
      301 qgkvytdhkv gnpfdrfdqt crnchtqske mlqgvvkqrk davteiklkv ekqlvhahfe
      361 akaawgagat eaqmkdilqd irhaqwrwdf siashgvqmh apevalrmlg taldkaadar
      421 tklarllaak gisheiaipd istkekaqaa lgmdmkqmns dkaqflktti pawdaeakaa
      481 grlaq
//
LOCUS       WP_111885447             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Acinetobacter].
ACCESSION   WP_111885447
VERSION     WP_111885447.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39654
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaetv vgenrvaatp etvkklisag hsvviergag vnaayidsay eqvgakitdd
       61 aytgsqmilk vrapkgdeiq kltagttvvg mfdpyrntel dqfasqnvsa falellprtl
      121 sraqnmdvls sqanlsgyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptar dqveslggkw ldvpmspeeq qkaadaakng ygwmpgedyi
      241 rdqaiivdka vsnadivitt allpgrdapr likaetvakm kpgsiildma vetggnvegs
      301 vcgenvvtan gvkilgipni pstvsteasa lyarnvlnfi etlfdseknf ainpeeeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_111893199             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter sp. MB5].
ACCESSION   WP_111893199
VERSION     WP_111893199.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. MB5
  ORGANISM  Acinetobacter sp. MB5
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter sp. MB5"
                     /db_xref="taxon:2069438"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39779
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipmetv agesrvaatp etvkklvgag hsvviekdag vqaaylnday tqvgatiadd
       61 ayqgsqiilk vrapqgdeis kisanttvia mfdpyrntel eqfatqqisa falellprtl
      121 sraqnmdvls sqanlsgyks vllaaneyqr mfpmlmtaag tvkparvvvm gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmseeeq qraadaakng ygwtpgeqyi
      241 kdqaaivdka vanadivitt allpgrnapr likaetvakm kagsvildma vetggnvegs
      301 kvnetvttan gvkilgvpni patvateasa lyarnvfnfl etlfdkdknf linqedeiqk
      361 allvthggtl lfkrg
//
LOCUS       WP_111900098             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas veronii].
ACCESSION   WP_111900098
VERSION     WP_111900098.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas veronii (Aeromonas ichthiosmia)
  ORGANISM  Aeromonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Aeromonas veronii"
                     /db_xref="taxon:654"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53019
     Region          5..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mgsqhrhinl glaallltsw lgasgwaqad dattkgkiea rselfakdha dqftswqats
       61 eskertdala edpnmvvlwg gypfakdynk prghfyaltd vretlrtgap ktaedgplpm
      121 acwsckgpdv arvidekged gyfkgmwakg gpevvntigc adchdtaske fkegkpalhl
      181 srpyadramt aigkpfkeqg rfdqqsqvcg qchveyyfsg ptkavkfpwd kgttveqmea
      241 yydeigfadw thalsktpml kaqhpeyetw ragihgqnnv acvdchmpkv qneqgkvytd
      301 hkvgnpfdrf eqtcrnchtq skemlqgivk qrkeavietk lkvekqlvha hfeakaawda
      361 gateaemkdi lqdirhaqwr wdyaiashgv qmhapevalk vlgsaldkaa dartklarll
      421 askgisheia ipdistkeka qvalgmdmkq fnsdkaqflk ttvpawdaea kaagrlaq
//
LOCUS       WP_111903093             409 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter globiformis].
ACCESSION   WP_111903093
VERSION     WP_111903093.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter globiformis
  ORGANISM  Arthrobacter globiformis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Arthrobacter globiformis"
                     /db_xref="taxon:1665"
     Protein         1..409
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41978
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiarerr egerrvaatp etvkqlaglg levliesrag vsaghaddey rhagahivdd
       61 ldpagldila hvrplelpta talkrgavtv glaspssela tvralaeggv tsfalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplymtaa gtvpparvlv lgvgvaglqa
      181 igtakrlgar vsandirpss aeevtsmggt fikldletae aaggyarelt adrgalqrql
      241 laphvadadv littaavpgr hapllvtrem vqgmrpgsvv vdlaaesggn vegsvagrdi
      301 hvptadgkgt vavvglkdap samptdasrl yaknvanlla lmtrdgtvap dfdddviaga
      361 clthdgvvrh pptaealavl agengtadse ladelandpv kasenegvv
//
LOCUS       WP_111912928             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas media].
ACCESSION   WP_111912928
VERSION     WP_111912928.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas media
  ORGANISM  Aeromonas media
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas media"
                     /db_xref="taxon:651"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53279
     Region          26..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgshnkpf rpglaalllt allgtsmlaq adeaapegki earselfakd hadqfsswkn
       61 tsesrertda laedpqmvvl wagypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf ngptkavkfp wdkgttveqm
      241 eeyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfdqtcrnch tqskemlqgv vkqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaemk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llaakgishe iaipdisske kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_111932491             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia bryophila].
ACCESSION   WP_111932491
VERSION     WP_111932491.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia bryophila
  ORGANISM  Paraburkholderia bryophila
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia bryophila"
                     /db_xref="taxon:420952"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39484
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvrkyvtqg hrvtiqsgag tgasfpdeaf taagaeivda
       61 atafaadlvl kvqsptdael pllrrgatlv gmldpfnadn aaklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgarf ldvpyetdee reaaqgvggy arpmpaswlt
      241 rqsalvhera kqadvvista lipgraaptl isvdtvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltvad qvvvkhgvqi vgytnlasmv padasslyar nlldflkliv tkegtlnidl
      361 addivaatll ardgevtrkt
//
LOCUS       WP_111941289             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_111941289
VERSION     WP_111941289.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54803
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ataadlwgrs divlkvrpps seevallreg stlvgfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgti nvdfnddair
      361 gltvikegnv twppppiqqp vaapkpaaap vaataskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_111997084             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_111997084
VERSION     WP_111997084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54833
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ataadlwgrs divlkvrpps seevalmrdg stlvgfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq ardadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgti nvdfnddair
      361 gltvikegnv twppppiqqp aaapkpatpp vaaaaskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_112019197             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112019197
VERSION     WP_112019197.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53473
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtgikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112016051             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112016051
VERSION     WP_112016051.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53507
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv asliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigktfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112025026             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112025026
VERSION     WP_112025026.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53584
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchiq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112039110             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112039110
VERSION     WP_112039110.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53614
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakvkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112046851             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112046851
VERSION     WP_112046851.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53586
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rknallsq
//
LOCUS       WP_112054509             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Onishia
            taeanensis].
ACCESSION   WP_112054509
VERSION     WP_112054509.1
KEYWORDS    RefSeq.
SOURCE      Onishia taeanensis
  ORGANISM  Onishia taeanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Onishia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Onishia taeanensis"
                     /db_xref="taxon:284577"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55503
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeqa pgearvaltp esaqqiqklg hdclietgag vaagfadaay rdagvsvvdd
       61 aktlweqadt vikvrepsde eadrlhdgqt lisffwpaqn eallercraq gatvvamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgaesggy aapsspefre
      241 kqlacfreqa pdvdivitta lipgkpapkl wledmveamk pgsviidlaa ekggncdltv
      301 pderivtdng vivvgytdfp srmatqssll yatnirhmlt dltpekdgvv nhnmeddvir
      361 gstvthdgei tfpppppkvk aigaakpkpk ekeptheekk aaehaafvaq tkrqvgmlvv
      421 ggalmwllgq vapasfmqhf ivfalacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 vlqigsgnwl vgllagisvl iasinivggf qvtrrmlamf qks
//
LOCUS       WP_112056326             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112056326
VERSION     WP_112056326.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53601
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta vpakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheie ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112063197             479 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Glaesserella parasuis].
ACCESSION   WP_112063197
VERSION     WP_112063197.1
KEYWORDS    RefSeq.
SOURCE      Glaesserella parasuis (Haemophilus parasuis)
  ORGANISM  Glaesserella parasuis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Glaesserella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Glaesserella parasuis"
                     /db_xref="taxon:738"
     gene            1..479
                     /gene="nrfA"
     Protein         1..479
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53708
     Region          1..477
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mlknslvatm amlgcfqaaw ageakefegp kpdvkiesan hkfaelyplq yqswaataes
       61 kevtsaleed prlvvlwtgy afskdynkpr ghfyavtdvr nilrtgapmd ensgpqpmac
      121 wackspdvpr miaekgevgy fdakwakygs eivnpigcad chdttsqefk dgkaalrvar
      181 phvlralevi gwkfdtldkh gkraavcsnc hveyyftgke kavtfpwdkg vdvdsiekyf
      241 deikftdwvh glskapmlka qhpdfetwal gthgkngvtc idchmpkvet kdgkvytdhk
      301 ignpfdnfeh tcktcheqsk eslqarvkeh kkqikdvmir ledqlvkahf eakraweaga
      361 teeemkdalq airhaqwrwd ysaaghgghm hapdvilhvi gtgldraada rtklaviltk
      421 hgvqtpiefp distkvkaqk vvgidfdkek aakeeflrtv vpqwekeake kgllpadak
//
LOCUS       WP_112067566             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Herbaspirillum rubrisubalbicans].
ACCESSION   WP_112067566
VERSION     WP_112067566.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum rubrisubalbicans
  ORGANISM  Herbaspirillum rubrisubalbicans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Herbaspirillum rubrisubalbicans"
                     /db_xref="taxon:80842"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55119
     Region          3..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 maltvgipke ifpeekrvaa spemvaklia lgfpvlmesq agalanmpde afraagasia
       61 aspqqvwqaa dlifkvraps laevalmkeg stlisfiwpa qnadlmaala akratvlamd
      121 ciprisraqk cdalssmani agyravieaa nqfgrfftgq itaagkvppa kvfvigagva
      181 glaalgtavs lgavvrandt rqevadqiks mgaefigvny eeegsggggy akvmsagyqq
      241 aqrqvfaeqa kdvdiiitta lipgkpapkl itsemvqsmr pgsvivdlaa eqggnceltv
      301 pgevvvrhdv tiigytdlps rlskqsstly atnllrltee lcktkdgill vnmddemirg
      361 atvlkdgtvt wpppaikpav apakpapnap aaapqakaap vkkpasrwgp vifgglaavl
      421 lwlvgsyapt eflehftvfi lacfvgymvv wnvtaslhtp lmsvtnaiss iiaigamtqv
      481 spalgssgtp tsylmfalai agivltavnm fggfavtgrm lamfrkqg
//
LOCUS       WP_112068072             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Herbaspirillum rubrisubalbicans].
ACCESSION   WP_112068072
VERSION     WP_112068072.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum rubrisubalbicans
  ORGANISM  Herbaspirillum rubrisubalbicans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Herbaspirillum rubrisubalbicans"
                     /db_xref="taxon:80842"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38866
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaipvesr hgetrvaatp etvkklvaar hevmvesgag ikssipdeay vavgasigha
       61 eavysaeill kvrapnaaer ariqagtvvi gmlnpfdadn taamaaaglt afaleaaprt
      121 traqsldvls sqaniagyka vlmaantyqr fmpmlmtaag tvkaarmlim gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfltdee keiaqgvggy arpmppdwmk
      241 rqaelvhera kqadiiitta lipgrkapvl iseetvkamk pgsvildmav dqggncplse
      301 pgktvikhgv hiigegnlaa lvaadasaly arnvldflkl iidaegklvi nkeddivaat
      361 llcqggeilr k
//
LOCUS       WP_112073079             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Hyphomonas
            sp. GM-8P].
ACCESSION   WP_112073079
VERSION     WP_112073079.1
KEYWORDS    RefSeq.
SOURCE      Hyphomonas sp. GM-8P
  ORGANISM  Hyphomonas sp. GM-8P
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomonadales; Hyphomonadaceae; Hyphomonas.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Hyphomonas sp. GM-8P"
                     /db_xref="taxon:1280945"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38859
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkisvlrerr sgetrvaatp etvkklvasg hsvtiesdag ktagfldsay eeagasiakd
       61 aaatvqgadi vfkvrgpeeg eiaalpdgaa lialmepfam dpkviaglna kkiaalsmef
      121 tpritraqsm dalssqsnla gyraviegaq ifgrampmmm taagtvapak tfimgagvag
      181 lqaiatarrl ggvvtatdvr paakeqvasl gakfiavedd efeaaetagg yakqmspeyq
      241 akqaeltash iakqdivvtt alipgrpapv liteemvksm kpgsvivdma vaqggncpls
      301 kpdeivdvgg vkvagfsnlp arlpadsssl ysknllaflp lvtaedgsln ldtddevvva
      361 mlltrggetv neriqs
//
LOCUS       WP_112096976             425 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium hawassense].
ACCESSION   WP_112096976
VERSION     WP_112096976.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium hawassense
  ORGANISM  Mesorhizobium hawassense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Mesorhizobium hawassense"
                     /db_xref="taxon:1209954"
     Protein         1..425
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43963
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqiifipre idpneprvaa spetvkrlag lgfdvivekg aglgsripdq dfataggtig
       61 taadarkadv vlkvrrptda elkgykpgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaage ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsviidlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkaakql airrddelvk
      361 atmltdggkv vhpnfakaae eprtepaavp aktmvadate kkparksatg ksaakspssk
      421 segta
//
LOCUS       WP_112128302             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium atlanticum].
ACCESSION   WP_112128302
VERSION     WP_112128302.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium atlanticum
  ORGANISM  Mesorhizobium atlanticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mesorhizobium atlanticum"
                     /db_xref="taxon:2233532"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43099
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqivfipre ldpneprvaa spetvkrlag lgfdvivekg aglgsripdq dfaavgaaig
       61 taadakkadv vlkvrrptda elkgyksgaa viaimdpygn daavaamara gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkttktl aikrddelvk
      361 atmltdggkv vhpnfakaae eprtepaavp attmvaeaad pkpaarkkaa akpkgta
//
LOCUS       WP_112110599             494 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Mannheimia varigena].
ACCESSION   WP_112110599
VERSION     WP_112110599.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia varigena
  ORGANISM  Mannheimia varigena
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Mannheimia varigena"
                     /db_xref="taxon:85404"
     gene            1..494
                     /gene="nrfA"
     Protein         1..494
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=55361
     Region          1..486
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkflaksliv atisilgclq palaeeakke sltdkavkhe klgvtvesan hlfaekyplq
       61 ynswkatsqs tdrgsaleyd pryvilwagy afskdynkpr ghyyaitdvr dilrtgapkg
      121 eddgpqpmac wtckgpdvpr lieekgergy fdpkwakygs evvnsigcad chdttsedfk
      181 vgkpalrvar phvlralnti gwkfedldkh gqrpavcanc hveyyfkdkk dvtfpwdkgi
      241 dvdsiekyyd eikfadwtha lskapmlktq hpdfevwaqg thgkngvtci dchmpkvkdk
      301 dgkvytehki gnpfdnfeat cktcheqske tlekrvkqyk hdvkeamirl edqlvkahfe
      361 akaawdagat eeemknilta irhaqwrwdy saaghgnhfh apdvmlrtia tgidraadar
      421 aelgvvlakh gvttpvaipd istkekaqla igldipkeqa akdeflktvv pqwekearak
      481 gllpaedapk adak
//
LOCUS       WP_112145211             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paramagnetospirillum kuznetsovii].
ACCESSION   WP_112145211
VERSION     WP_112145211.1
KEYWORDS    RefSeq.
SOURCE      Paramagnetospirillum kuznetsovii
  ORGANISM  Paramagnetospirillum kuznetsovii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Magnetospirillaceae; Paramagnetospirillum.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Paramagnetospirillum kuznetsovii"
                     /db_xref="taxon:2053833"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55035
     Region          1..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkiaiprevf pnekrvatvp evvekliklg fevivesgag dlancsdday kaagatiaas
       61 akeawsagdi vfkvraptmd evallkdgat lisfiwpaqn pdlmqalsar kvtilamdcv
      121 prqlsraqkm dalssmania gyravveaan qfgrfftgqi taagkvppak vfvagagvag
      181 laalgtavsl gaivrandtr aevadqvksm gaefvkveye eegsggggya kvmsegfqaa
      241 qremyaqqar evdiiittal ipgkpaprli taemvqsmrp gsvivdmaae qggnceltvp
      301 gevvvrhgvt ivgytdlpsr lskqastlyg nnllrlaedl cktkdgtidv nmgddairgl
      361 tvikdgeitw papplvlpap paakpaaapv aakksghghg agepmsaksl aitfgigala
      421 fwfvganape aflghftvfv lacfvgymvv wnvtpalhtp lmsvtnaiss iivigalvqi
      481 spplgegisr pgfwigllav isiiltsinm fggfavtkrm lamfrk
//
LOCUS       WP_112171912             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia unamae].
ACCESSION   WP_112171912
VERSION     WP_112171912.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia unamae
  ORGANISM  Paraburkholderia unamae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia unamae"
                     /db_xref="taxon:219649"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39594
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anetrvaatp etvkkyvaqg htvtiqagag tgasypdeay tavgaqvada
       61 atafgaelvl kvqsptvsel pfmkrgavlv gmldpfnaen aaklaeagvt afaleaaprt
      121 traqsldvls sqaniagyka vlvaanlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaegvggy arpmppswlt
      241 rqsalvhera kqadivista lipgrdaptl lpsetvqamk pgsvvidlaa grgpvadqas
      301 grrggncplt eadkvvmqhg vqicgytnla smvaadasal yarnlldflk livtkegaln
      361 idladdivaa tllardgavt rka
//
LOCUS       WP_112174792             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia unamae].
ACCESSION   WP_112174792
VERSION     WP_112174792.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia unamae
  ORGANISM  Paraburkholderia unamae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Paraburkholderia unamae"
                     /db_xref="taxon:219649"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54204
     Region          3..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtiaapre thegerrvaa tpesvaqlik lgyaveveag agvnasypdd ayraagariv
       61 ddaqallsga divakvrpps seevqrlkpg atligfiwpa qhaalleqla areatvlamd
      121 cvprisraqk ldalssmanm agyravveaa qhfgrvftgq itaagkmppa kvlvigagva
      181 glaaigaarg lgaivrafdt rpevgqqves mgaeflsidi eeegggsggy arqmsakfie
      241 aemalfeaqa revdiiitta lipgkpaprl idaktvacmr agsvivdmaa eqggnceltq
      301 pglvvnangv tvigytdlps rmanqssqly atnirhlltd ltpakdgelk ldmddvvqrg
      361 ttvmqrgqic wppppvqvsa apqaaaqtkp vvvangqakd esvqaarrng vgslaalvia
      421 allllalgav appafvahft vfvlavfvgy qvvwnvtpsl htplmsvtna isgiivigal
      481 lhpgnagtvv tvlagialvv atiniaggfl vtqrmlkmfq rt
//
LOCUS       WP_112192873             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. LG1E9].
ACCESSION   WP_112192873
VERSION     WP_112192873.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. LG1E9
  ORGANISM  Pseudomonas sp. LG1E9
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. LG1E9"
                     /db_xref="taxon:2219057"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38737
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag lkasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklagqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adetvvendv iicgptnlag avaadasaly arnlldflkl vfnkegqfel nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_112205202             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter paneuropaeus].
ACCESSION   WP_112205202
VERSION     WP_112205202.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter paneuropaeus
  ORGANISM  Polynucleobacter paneuropaeus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Polynucleobacter paneuropaeus"
                     /db_xref="taxon:2527775"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39270
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpletk agetrvaatp etvkkligqg hqvliqkdag lqasqpdsay vavgatigsa
       61 adafaselvl kvrapqasel sqiksgsvli gmlepfdnnn iaamaaqgit afsleaaprt
      121 traqsmdvls sqaniagyka vmiaaneyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpfetdee reiakgvggy arpmpeswmk
      241 rqaalvaera qqadivitta lipgrkppvl lnsdtvanmk agsvvidlaa gkgdngsgnc
      301 pltqadkiid vngvkivgyt dlasmvgada salyarnlld flkliidkea klviptdddi
      361 vaaclmcrdg qairkns
//
LOCUS       WP_112251754             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_112251754
VERSION     WP_112251754.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38791
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqrgag lnasipdsay eavgaslgsa
       61 adaygaqlvl kvvapsdqel alinsgsllv gmlnpfnsel igkmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvqengv iivgptnlpa qvgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_112281196             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Prauserella muralis].
ACCESSION   WP_112281196
VERSION     WP_112281196.1
KEYWORDS    RefSeq.
SOURCE      Prauserella muralis
  ORGANISM  Prauserella muralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Prauserella.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Prauserella muralis"
                     /db_xref="taxon:588067"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38426
     Region          8..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpdtdapltv gvvketrpge rrvalvpklv erltkrglqv vvepgaglra qladelyeea
       61 gahlgearss divltvtppa padierlkag tvligflnpl snvdgvaamk kagirafave
      121 siprisraqa mdalssqanv agyravllaa qrlpkffpml ttaagtvppa kalilgvgva
      181 glqalatakr lgaqatgydv rpevaeqvrs vgaqwldlgi eaageggyar eltdeeraeq
      241 qrrlteaitg fdvvittalv pgrpapklvt aeavrgmrpg svivdmaget ggnceltepg
      301 qdtvahdvti csplnlpaem pvhaselyar nltelieliv dsegrlaldf sdeivagacv
      361 agadeevn
//
LOCUS       WP_112298705             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus wratislaviensis].
ACCESSION   WP_112298705
VERSION     WP_112298705.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus wratislaviensis
  ORGANISM  Rhodococcus wratislaviensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus wratislaviensis"
                     /db_xref="taxon:44752"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37907
     Region          13..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqsasta rptvgvvres ndgerrvalv pkivasliak gvdvvvesga glgalipdel
       61 yteagakiad pwsadvivkv appsdeevgr lhagqtligf laprnqdnqv aalkaagvaa
      121 faveaipris raqvmdalss qanvsgyksv llaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrat gydvrpevad qvrsvgaqwl dlgidaageg gyarelteae
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvvvdl agetggncel
      301 tepgqtvvkh gvticsplnl pasmpehase lysknisall elmlvdgala pdfsdevlaa
      361 scvtreegvs
//
LOCUS       WP_112300036             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus wratislaviensis].
ACCESSION   WP_112300036
VERSION     WP_112300036.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus wratislaviensis
  ORGANISM  Rhodococcus wratislaviensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus wratislaviensis"
                     /db_xref="taxon:44752"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38072
     Region          13..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdisrsvalp pptigvvres ndgerrvalv pkivasliak gvdvvvesga glgalipdel
       61 yteagakiad pwsadvivkv appsdeevgr lhagqtligf laprnqdnqv aalkaagvaa
      121 faveaipris raqvmdalss qanvsgyksv llaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrat gydvrpevad qvrsvgaqwl dlgidaageg gyarelteqe
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvvvdl agetggncel
      301 tepgrtvvkh gvticsplnl pasmpehase lysknisall elmlvdgala pdfsdevlaa
      361 scvtrdpegh
//
LOCUS       WP_112310016             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudogemmobacter bohemicus].
ACCESSION   WP_112310016
VERSION     WP_112310016.1
KEYWORDS    RefSeq.
SOURCE      Pseudogemmobacter bohemicus
  ORGANISM  Pseudogemmobacter bohemicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudogemmobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudogemmobacter bohemicus"
                     /db_xref="taxon:2250708"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55191
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkeif agenrvamtp dsalqlqklg hsclietgag anagftdeay kaagvtvlss
       61 asavaeladv vvkvrgpepq eldllheget lisffwpaqn pelleqakak gvtavamdmv
      121 prisraqkmd alssmaniag yravieaann fprfftgqvt aagkvppakv lvvgagvagl
      181 aaigasvslg aityafdvrp evaeqinsmg aefvyldfse tqtdgaatgg yaapsspefr
      241 eaqlkkfrel apeidivitt alipgrpapk lwtedmvglm krgsvivdla aerggncdlt
      301 vpdqkivtan gvtivgytdf psrmatqasn lysnnirhml adltpgkdgv inhnmeddvi
      361 rgatvakage vtypppapki aaiavqkpke aakeltpeek raaevaafka qtrnqftlla
      421 vgggllllag lfapasfmsh fivfvlscfi gfqviwnvah slhtplmait naissiiilg
      481 allqigsgnw lvivlaalsv lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_112315799             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodovulum
            viride].
ACCESSION   WP_112315799
VERSION     WP_112315799.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum viride
  ORGANISM  Rhodovulum viride
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhodovulum viride"
                     /db_xref="taxon:1231134"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55526
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeil egearvamtp dsavqlrklg ydclieagag eaagfadaay ekagvkvvqs
       61 aaalwqgadi vvkvrepvae evarlrkgqt lisffwpaqn ealleqckar gatviamdmv
      121 prisraqkmd alssmaniag yravieagsn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg amvyafdvrp evaeqiesmg aefvfldfed stadgsesgg yakpsspefr
      241 ekqlekfrel apdmdivitt alipgrpapk lwledmvaam kpgsvvvdla aekggncdlt
      301 rpgekivsdn gvtvvgytdf asrmatqsst lyatnirhmm tdltpgkdgq vvhnmeddvi
      361 rgatvthege itfpppppkv kaiaaaprke kpkeltpeek kaqeaaafrk qtitqvgmlv
      421 aggllmalig afapesfmsh fivfalscfv gfqviwnvsh slhtplmavt naisgiiilg
      481 allqigsgnw lvvilatvsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_112319985             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus pyridinivorans].
ACCESSION   WP_112319985
VERSION     WP_112319985.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus pyridinivorans
  ORGANISM  Rhodococcus pyridinivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rhodococcus pyridinivorans"
                     /db_xref="taxon:103816"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38533
     Region          17..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(30,85,104,297,323,325)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(59,137..138,147..148,151..152,155..156,158..159,
                     161..166,168,170..172,175,198..199,287..288,330..331,335,
                     338..339)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(132..133,137,140,143,184..187,207..209,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(134..135,137,147,190..191,198,214..215,217..220)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(167..171,174,177,200,202)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mstegsntgs gahrrptvgv vretndgerr valvpkivps ligkgldvvv esgagqgali
       61 pdaaykeaga tvgdawsadi vvkvappsda eiahlksgqr ligflaprna dnqigaltqa
      121 gveayaveai prisraqvmd alssqanvag ykavlvaase strffpmltt aagtvkpatv
      181 lvlgvgvagl qalatakrlg grttgydvrp evadqvrsvg aqwldlgida ageggyarel
      241 teaeraqqqq aledaikgfd vvittalvpg rpaprlvtaa avegmkpgsv ivdlagetgg
      301 nceltepgqt vvkhdvtics plnlpatmpe haselysknv yalielllde sgalapdssd
      361 eileaacvtr skens
//
LOCUS       WP_112320202             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Enterobacteriaceae].
ACCESSION   WP_112320202
VERSION     WP_112320202.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53558
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfenag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112320906             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Oceanibium
            sediminis].
ACCESSION   WP_112320906
VERSION     WP_112320906.1
KEYWORDS    RefSeq.
SOURCE      Oceanibium sediminis
  ORGANISM  Oceanibium sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Oceanibium.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Oceanibium sediminis"
                     /db_xref="taxon:2026339"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55475
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkell egearvalsp qsalqlqklg ydviveagag aksrftdday reagvevlds
       61 aeafyaaadi vlkvrppega eldhfregqt lisfiwpaqn ealmntlkdk gvnaiamdmv
      121 prisraqkmd alssmanigg yravveasnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aasgtatamg aityafdvrp evaeqiesmg aefvyldfee aaqdgaatgg yaapsspefr
      241 ekqlekfrem apdmdivitt alipgrdapi lwtkdmveam kpgsvivdla aerggncelt
      301 vkdqlieten gvkvigytdl psrmatqsst lyatnlrhml ddltpekdgk pfinmeddvi
      361 rgatvvnage itypppppkt qaiaaakpkp keptaeekaa tevaafkqqt rnqvtllavg
      421 aalllgvglv apasfmqhfi vfvlavfvgf qviwgvahsl htplmavtna issiiilgal
      481 tqigsgsffv illaalavfm tginifggfm vtrrmlamfq ks
//
LOCUS       WP_112335164             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. BK312].
ACCESSION   WP_112335164
VERSION     WP_112335164.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. BK312
  ORGANISM  Rhizobium sp. BK312
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium sp. BK312"
                     /db_xref="taxon:2587080"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40651
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msnlvfvake svaeetrvaa svetvkkmrs lgfdvvveag agalsrilda eyeavgarig
       61 sikdakaadv vlkvrrptsk eisgykngai viaimdpygn eaalaemarr gltsfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aqvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdiiitta lipgrpaprl isrdmlkamr pgavavdlav erggniegae
      301 ygkvaevegv rvvgypnmag riaasasaly aknlvtflet mvdkdmksla vnrtdelika
      361 tmltdggevv npnfvdpdqp tikkgdl
//
LOCUS       WP_112343419             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            tropici].
ACCESSION   WP_112343419
VERSION     WP_112343419.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium tropici
  ORGANISM  Rhizobium tropici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium tropici"
                     /db_xref="taxon:398"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40552
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msnlvfvake svteetrvaa svetvkkmrg fgfdvvieag agvssripda eyeaagarig
       61 svkdakaadv ilkvrrpttk eiagykngai viaimdpygn eaalaemara gltsfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg alvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsreyqa
      241 kqavlvadhi akqdiiitta lipgrpaprl vgrdmlkamr qgavavdlav erggniegae
      301 ygkvaevegv rvigypnmag riaasasaly aknlvtflet mvdkdskslg lnrldelika
      361 tmltdggevv npnfvdpdqp tvnkgdl
//
LOCUS       WP_112353208             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            benthica].
ACCESSION   WP_112353208
VERSION     WP_112353208.1
KEYWORDS    RefSeq.
SOURCE      Shewanella benthica
  ORGANISM  Shewanella benthica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Shewanella benthica"
                     /db_xref="taxon:43661"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54655
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipreil aqesrvaatp atviqlkklg fsvvvqsgag elanfkdeay reagaeivsl
       61 eeafqadlil kvnapainsd tgvdeadllk sgatvasfvw paqnpellek fkakginlla
      121 mdmvprisra qsldarssla nvdgyravve aanhfgrfft gqitaagkvp pakvliigag
      181 vaglsalgaa gsmgaivraf dtrpevkeqi nsmgaeflel dfeeesgsgd gyakvmskaf
      241 idaemelfrq qakevdiiit talipgkpap kliledmvyl mkpgsvivdl aaanggncel
      301 tvpgevivvn nvtiigytel srrlptqasq lygtnlvnll kimvpkkdgn yeinfddevi
      361 rgltvvkege itfpppviqv saqpkakeea vvevveakpk npwvkpalal vaaglfglva
      421 hsapldfiqh fsvfvlscvv gyyvvwnvsh slhtplmsvt naisgiivvg alvqmdsdnt
      481 avlvlsgiai liasiniagg ftvtqrmlkm frkd
//
LOCUS       WP_112352000             466 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella benthica].
ACCESSION   WP_112352000
VERSION     WP_112352000.1
KEYWORDS    RefSeq.
SOURCE      Shewanella benthica
  ORGANISM  Shewanella benthica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Shewanella benthica"
                     /db_xref="taxon:43661"
     gene            1..466
                     /gene="nrfA"
     Protein         1..466
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51893
     Region          1..466
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvrtltkksf vlsamvagsl masgvmadnk teprnevykd kfskqynswh etseskeiid
       61 vleadpnlvv lwagygfakd ynkarghmya vtdvrntlrt gapksdtdgp mpmacwsckg
      121 pdvprmieeq gedgyftgkw ykggaeivnt igcsdchvsg ksklrisrpf avrameaigt
      181 pfdeasrkdk qsmvcgqchv eyyfektkdk kgfvkfpwdq gitvdaaeay ydgiqfsdwt
      241 hkisktpmlk aqhpgyetwk lgvhgqnnvs ctdchmprvk naegrkytdh kvgnpfdrfe
      301 etcgscheqs kefmvdltnq rkakveelkm aaeghlvkah feagaaweag ateaemkpil
      361 tdirhaqwrw dyatashgva ahapaealri lgtavdkaad arvklaqlla kkgvkqpisy
      421 pdistkakaq aamgmdmkkm nadkaefkkt vlpkwdaeak kreaty
//
LOCUS       WP_112356148             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agrobacterium tumefaciens].
ACCESSION   WP_112356148
VERSION     WP_112356148.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium tumefaciens (Rhizobium radiobacter)
  ORGANISM  Agrobacterium tumefaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Agrobacterium tumefaciens"
                     /db_xref="taxon:358"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55713
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely egearvgmtp dsaqalqklg ydciletgag kaagfsdday raagvtivds
       61 aealyagadi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfae qqdgaatggy aapsspefre
      241 kqlekfrela pqidivitta lipgrdapkl wladmvammk pgsviidlaa erggncdltv
      301 pdqrvvsdng vivigytdfp srmatqastl ystnirhmmt dltpakdgkp vhnmeddvir
      361 gatvtyqgei tfpppppkiq aiaaqkpker akeltpeekh akeraefkaq tksqvgllvi
      421 gtavlllvgl yapasfmshf ivfvlacfig fsviwnvshs lhtplmavtn aisgiviiga
      481 llqigsgnwl vvllaslsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_112400458             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. CNPSo 3464].
ACCESSION   WP_112400458
VERSION     WP_112400458.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. CNPSo 3464
  ORGANISM  Rhizobium sp. CNPSo 3464
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. CNPSo 3464"
                     /db_xref="taxon:3021406"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55539
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigsprerl egearvamtp dsatqlqklg yqcaietgag klagfsdday raagvrivds
       61 vealfasvdv iakvrppeps diaklssnkt lisffypaqn kelleqakat ranviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsvslg aityafdvrp evaeqiesmg aefvfldfke qqqdgattgg yaspsspefr
      241 eaqlkkfrei apdidivvtt alipgrdapk lwladmvaam kpgsvvvdla aerggncdlt
      301 vpdqkivsen gvtvigytdf psrmaaqast lystnirhmm tdltpkkdgv lvhnmeddvi
      361 rgatvafege itypppppki qaiaaqkrqe kakeltpeer raaeasafks atrqqvgllv
      421 vggllmalig ayapsafmgh fivfalacfv gfqviwgvsh slhtplmavt naisgiiiig
      481 allqvtaggw lvtalaavsv aiatinivgg fmvtrrmlnm fqks
//
LOCUS       WP_112400690             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            miluonense].
ACCESSION   WP_112400690
VERSION     WP_112400690.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium miluonense
  ORGANISM  Rhizobium miluonense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium miluonense"
                     /db_xref="taxon:411945"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40621
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msnlvfvake svaeetrvaa svetvkkmrs lgfdvvveag agalsrilda eyeavgarig
       61 sikdakaadv vlkvrrptsk eisgykngai viaimdpygn eaalaemarr gltsfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aqvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdiiitta lipgrpaprl isrdmlkamr pgavavdlav erggniegae
      301 ygkvaevegv rvvgypnmag riaasasaly aknlvtflet mvdkdtksla vnrtdelika
      361 tmltdggevv npnfvdpdqp tikkgdl
//
LOCUS       WP_112437136             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. AN80A].
ACCESSION   WP_112437136
VERSION     WP_112437136.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. AN80A
  ORGANISM  Rhizobium sp. AN80A
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. AN80A"
                     /db_xref="taxon:3040673"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55533
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkell agesrvamtp esasqlqklg yiclieasag slagfsdkay raagvevvet
       61 aealfeqadi iakvrppepr elerlragqt lisffypgqn atlleqakat ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfkg dsqdgaatgg yaapsspefr
      241 ekqlekfrel apeidivitt alipgrdapk lwlsdmvalm kpgsviidla aerggncdlt
      301 vadqkivsdn gvivigytdf psrmaaqast lystnirhmm tdltpakdgk lvhnmeddvi
      361 rgatvafega vtypppppki qaiaaqkpre ktkeptaeek kareaaafka qtksqgflll
      421 igtallllvg ayapasfmnh fvvfmlacfi gfqviwnvsh slhtplmavt naisgivilg
      481 allqvgsgnw lvvilaalsv lvatinivgg flvtrrmlam fqks
//
LOCUS       WP_112437953             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces cadmiisoli].
ACCESSION   WP_112437953
VERSION     WP_112437953.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces cadmiisoli
  ORGANISM  Streptomyces cadmiisoli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            aurantiacus group.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces cadmiisoli"
                     /db_xref="taxon:2184053"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53178
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligivsear sgetrvaatp atvvqlvklg yevvvepgag vlssfpdday aeagarvgdp
       61 laadvvlgvn alttsqldel kpgttvmgim spafdpelve dlatrpital amdavprisr
      121 aqsldvlssm aniagyravv eaahvfgrff tgqvtaagkv ppakvlvcga gvaglaaiga
      181 agslgavvya tdprpevadq vrslggeyls aeaadsaeve vsatgyakem sddyntraaq
      241 lyrdritemd ivittaqipg rsaptlitad mvasmrpgsv ivdmaaatgg nvegtvrdea
      301 vvtangvtvi gytdlpgrlp aqasqlygtn lvnliklmtp dkdgllvldf ddvvqrsmtv
      361 vrdgestwpp ppvqvsaapa aapataspav kpvaaqaqpm strrrstmvg igatvlflca
      421 alspaallgh ltvfalaivi gyyvighvhh alhtplmsvt naisgiivvg allqighddt
      481 pngtvvmvls afaillasvn ivggfavtrr mlsmfsrs
//
LOCUS       WP_112478058             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            variabilis].
ACCESSION   WP_112478058
VERSION     WP_112478058.1
KEYWORDS    RefSeq.
SOURCE      Vibrio variabilis
  ORGANISM  Vibrio variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio variabilis"
                     /db_xref="taxon:990271"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54029
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpketl agetrvaatp ksveqllklg fdvsvesqag vlasfddaay eaagatiiss
       61 qevwqsdlvl kvnapndeei eslkegasli sfvwpaqnpe lmeklsskni nvmamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvesmgad flevdyqent gsgdgyakem sddfnkkaae
      241 lymeqakdvd iiittalipg rpapklvtke mvdamkpgsv ivdlaaangg nceytvadqv
      301 ittengvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkegevtwpa ppiqvsaqpe apkaeapkpa ekveeptspv kklaglvaav gvfgwvasva
      421 paaflshftv fvlacvvgyy vvwnvthalh tplmsvtnai sgiivvgall qigqgngvvs
      481 flafiavlia sinifggftv tkrmlemfrk dk
//
LOCUS       WP_112479892             471 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            variabilis].
ACCESSION   WP_112479892
VERSION     WP_112479892.1
KEYWORDS    RefSeq.
SOURCE      Vibrio variabilis
  ORGANISM  Vibrio variabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Vibrio variabilis"
                     /db_xref="taxon:990271"
     gene            1..471
                     /gene="nrfA"
     Protein         1..471
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52627
     Region          1..471
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnkhwiissv aalailgtas vsafaaseke lmdprnqaye qdhpdqyhsw kqtsesveie
       61 dalahdpnmv ilwagygfak dynkarghfy alddvrqtlr tggptdpksg pmpmacwsck
      121 spdvarvide rgedgyfegk warlgaeisn pigcadchdt rsekfkngep elaltrpyve
      181 rafeaigkkf deqsrldkqa svcaqchvey yftgptkavk fpwdmgttvg emeqyydaln
      241 fkdwqhavsk apmlkaqhpg yetwrdgihg kngvvcvdch mpkvtkedgt vytdhkvgnp
      301 fdrfedtcan chtqskdqlq givstrkaqv lnmkltaekq ivaahfeaga awdagateee
      361 mkpiltdirh aqwrwdyaia shgvhmhape maleilgtsv dkaadarakl irllakkgit
      421 dpveipdist kekaqaalgm dmdkmnaekk hfletvvpew dkeaaerean y
//
LOCUS       WP_112484820             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Thiomonas
            sp. X19].
ACCESSION   WP_112484820
VERSION     WP_112484820.1
KEYWORDS    RefSeq.
SOURCE      Thiomonas sp. X19
  ORGANISM  Thiomonas sp. X19
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Thiomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Thiomonas sp. X19"
                     /db_xref="taxon:1050370"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38401
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvvaesl ggerrvaatp etvkklvaqg htllvqsgag lgagatdady qgagaqmvda
       61 aaalgaelvl kvrrpqphel aqmqpgaavv gmlepfdaag lqalagaglt afaleaaprt
      121 sraqgldvls sqaniagyka vllaanlypr fmpmlmtaag tvkaarlvvl gagvaglqai
      181 atakrlgavv easdvrpaak eqveslgakf idvpfetdee rqiaqgvggy arpmpkawle
      241 rqaalvaerv kqanivitta lipgrrapvl vseamvqgmr pgsvlvdmaa aqggncplte
      301 adqtvvrhgv tivgdtnlpa qvaadasqly arnvldflkl vldkdrglvv nldddivaac
      361 lmtqggevrr ksa
//
LOCUS       WP_112528894             461 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium sp. P30BS-XVII].
ACCESSION   WP_112528894
VERSION     WP_112528894.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium sp. P30BS-XVII
  ORGANISM  Phyllobacterium sp. P30BS-XVII
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Phyllobacterium sp. P30BS-XVII"
                     /db_xref="taxon:2587046"
     Protein         1..461
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47409
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke tdavesrvgg saetvkklig lgfsvivesg agvssripdr efeaagatig
       61 ktadirnadv vlkvrrpssa elksykkgav viamldpygn daavkelada gvtaftmefm
      121 pritraqvmd vlssqanlag yqavvdaaee ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdiiitta lipgrpaprl vtremygrmr pgsviidlav erggnvegav
      301 agkivdvdgv kivghlnvag riaatasqly aknlfafvet lvdkdakaik vnfddelvka
      361 tvlthggkvv hpnfagaaps aaapaakpaa kkpakakaap aetvgvaaep kkapvkaapn
      421 kaaapkaavk ktapkpaatk taasktvtpk taapkttege a
//
LOCUS       WP_112556555             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium sp. GF69].
ACCESSION   WP_112556555
VERSION     WP_112556555.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium sp. GF69
  ORGANISM  Mycolicibacterium sp. GF69
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Mycolicibacterium sp. GF69"
                     /db_xref="taxon:2267251"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52009
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl egetrvaatp qtvgqllklg ysvvvesgtg aassfadaay veagaeigda
       61 waadivlkvn apsddeiakl qdgatlvsli spalnpelvk klsarpitvl amdavprisr
      121 aqsldvlssm aniagyravv eaahsfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivka tdprpevadq vrslggeyvs iesadsevsa tgyakemged ykareaalyt
      241 elasevdiii ttalipgkpa priitadmva smkpgsvlvd maaanggnie gtvkdqaivt
      301 dhgvtiigyt dlagrlpata sqlygtnlvn llklltpekd gqltldfddv vqrsvtvvrd
      361 gettwppppv qvsaapaaaa sapaeqkpak tpmttgrrlg itfaaaallf alialspaal
      421 qvhltvfala ivigyyvign vhhalhtplm svtnaisgii vvgallqigh gdwvitaiat
      481 aaillasinv fggfavtrrm lamfsrs
//
LOCUS       WP_112556965             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Agrobacterium].
ACCESSION   WP_112556965
VERSION     WP_112556965.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium
  ORGANISM  Agrobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Agrobacterium"
                     /db_xref="taxon:357"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55742
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtpkely egearvgmtp dsaqalqklg ydcvieagag kaagfsdday raagvtvvds
       61 aealytgsdi iakvrppets eidrlsadkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qqqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvamm kpgsviidla aerggncdlt
      301 vpdqrvvsdn gvivigytdf psrmatqast lyatnirhmm tdltpakdgk vvhnmeddvi
      361 rgatvtygge itypppppki qaiaaqkpke kakeltpeek harekaefka qtknqvgllv
      421 agtavlllvg lyapasfmsh fivfvlacfv gfqviwnvsh slhtplmavt naisgiviig
      481 allqigsgnw lvvilaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_112632087             382 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Mycobacterium].
ACCESSION   WP_112632087
VERSION     WP_112632087.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium
  ORGANISM  Mycobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Mycobacterium"
                     /db_xref="taxon:1763"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39315
     Region          7..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtnaqttvgv vaesgtderr valvpkavas lvnsgvavvv esgagerall pdalyteaga
       61 sigdawaadv vvkvapptqa evaklhsgqt ligflaprna ensigalkqa gvqafaleai
      121 prisraqamd alssqgnvsg ykavllaase strffpmltt aagtvkpatv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwldigida sgeggyarel tdeeraqqqk
      241 alekaisgfd vvittalvpg rpaprlvtaa aveamkpgsv vvdlagetgg nceltepgqt
      301 vvkhdvtias plnlpatmpe haselyskni talldllltd gklapdfdde viaescvtrd
      361 raaddaersd aeerrktage ds
//
LOCUS       WP_112663894             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            flavescens].
ACCESSION   WP_112663894
VERSION     WP_112663894.1
KEYWORDS    RefSeq.
SOURCE      Microvirga flavescens
  ORGANISM  Microvirga flavescens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Microvirga flavescens"
                     /db_xref="taxon:2249811"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39407
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mliavlsetd aveprvaatp etvkkykslg adivvqagag vragvpdaef eaagasiakd
       61 aksagkdadv vlkvrrptea elkvikpgal viaimdpygq daalkalaea kvaafsmelm
      121 pritraqvmd vlssqanlag yravidatae ygrampmmmt aagtvpaarv fimgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfiavedee fkqaetaggy akemsaeyra
      241 kqaalvashi akqdivitta lipgrpapkl vtrdmvesmk pgsvvvdlav erggncelsk
      301 pgevaehngv kivghlnvpg rlaatassly aknlyafvet lvdketkala vkwddelvka
      361 tcltrdgaiv hsafqptt
//
LOCUS       WP_112686439             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacter senuensis].
ACCESSION   WP_112686439
VERSION     WP_112686439.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacter senuensis (Mycobacterium senuense)
  ORGANISM  Mycolicibacter senuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacter.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Mycolicibacter senuensis"
                     /db_xref="taxon:386913"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51860
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mnigvlseaq pgetrvsatp ttvaqliklg yevvvdagag eassftdaay veagatigda
       61 raadivfgvn apateqldam kpgatlisll apalnpdrve dlarrpital smdavprisr
      121 aqsldvlssm aniagyravv eaahvfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivra tdprpevadq vkslggeyls iedpeaevsa tgyakemgds ykareaelya
      241 eqckdvdiii ttalipgkpa priitadmva smspgsvivd maaanggnve gtvkdqavvt
      301 dngvtiigyt dlagrlpaqa sqlygtnlvn lmklltpgkd gqlvldfddv vqrsmtvvrd
      361 gestwppppv qvsaapakaa eapvvkqesk apmaagrrlg lvvaaaavlf alvalapaal
      421 qvhltvfala ivigyyvigh vhhalhtplm svtnaisgii vvgallqigh gdpvitalat
      481 aaillasinv fggfavtrrm lamfsrs
//
LOCUS       WP_112707252             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium colombiense].
ACCESSION   WP_112707252
VERSION     WP_112707252.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium colombiense
  ORGANISM  Mycobacterium colombiense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Mycobacterium colombiense"
                     /db_xref="taxon:339268"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38940
     Region          7..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtnaqttvgv vaesgaderr valvpkavas lvnsgvavvv esgagerall pdalyteaga
       61 sigdawaadv vvkvapptqa evaklhsgqt ligflaprna ensigalkqa gvqafaleai
      121 prisraqamd alssqgnvag ykavllaase strffpmltt aagtvkpatv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwldigida ageggyarel tdeeraqqqk
      241 alekaisgfd vvittalvpg rpaprlvtaa aveamkpgsv vvdlagetgg nceltepgkt
      301 vvkhdvtias plnlpatmpe haselyskni talldllltd gklapdfdde vvadscvtra
      361 gddaersdae errqtsgevs
//
LOCUS       WP_112712144             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Moritella
            yayanosii].
ACCESSION   WP_112712144
VERSION     WP_112712144.1
KEYWORDS    RefSeq.
SOURCE      Moritella yayanosii
  ORGANISM  Moritella yayanosii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Moritella yayanosii"
                     /db_xref="taxon:69539"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54260
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl kgetrvaatp atveqlqklg fsvlvesnag qlanfndatf eaagatisgd
       61 tkqvwasdiv lkvnapandk eikllqkgts lisfiwpaqn eelleklakr einvlamdsv
      121 prisrsqsld alssmaniag yravieaane fgrfftgqit aagkvppakv liigagvagl
      181 saigaagslg aivraydtrp evkeqitslg aefltvdfde ssgsgdgyak vmsedykaqe
      241 qkmlaeqvad adiiittali pgrpaprlis qemvdgmkag svivdlaavn ggnvepsvvd
      301 kvittdggvk vigynemarr lpaqasqlyg tnlvnllkll tpekdgemii nfddvvqrgv
      361 tvikdgkitw pappiqvsaa pqaakkeevk eapakpekkk tgiykallag ggiwaysala
      421 syvpaeflnh lmvfalacvi gyyliwdvaa slhtplmsvt naisgivilg affqmgaesg
      481 lvtllaflgt fiatiniagg favtermlkm frk
//
LOCUS       WP_112712513             479 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Moritella yayanosii].
ACCESSION   WP_112712513
VERSION     WP_112712513.1
KEYWORDS    RefSeq.
SOURCE      Moritella yayanosii
  ORGANISM  Moritella yayanosii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Moritella yayanosii"
                     /db_xref="taxon:69539"
     gene            1..479
                     /gene="nrfA"
     Protein         1..479
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53658
     Region          26..479
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 masvyktlkp asgvavllat lllgvssstv faadqvsakl eprnekfqqa hpdqyktwka
       61 tseskeieda lqgdpnmvim wagygfskdy nktrghfyai ddirntlrtg gptnakngpm
      121 vmscwscksp dvarfieeng edayfsgkwa kggaeivnai gcadchdtrs dafkngepal
      181 kltrpyvera mevigkpfke qgrldqqaqv caqchveyyf tgptkavkfp wdkgttvdqm
      241 eeyydeigfk dwthavsktp mlkaqhpgye twregihgkn nvtcvdchmp kiknadgtvf
      301 tdhkvgnpfd rfqdtcanch tqskemlqdv vktrkdqvte lkllaekqii aahfeakaaw
      361 eagatqaemd eiqlnirhaq wrwdyaiash gihmhapeva lrvlgtaldr atdartqlir
      421 llakkgitdp ieipdistke laqqalgmdm dkmrkekaef lktlvpkwea eaeqreaty
//
LOCUS       WP_112712515             201 aa            linear   BCT 07-JUL-2024
DEFINITION  cytochrome c nitrite reductase pentaheme subunit [Moritella
            yayanosii].
ACCESSION   WP_112712515
VERSION     WP_112712515.1
KEYWORDS    RefSeq.
SOURCE      Moritella yayanosii
  ORGANISM  Moritella yayanosii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Moritellaceae; Moritella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03146.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Moritella yayanosii"
                     /db_xref="taxon:69539"
     gene            1..201
                     /gene="nrfB"
     Protein         1..201
                     /product="cytochrome c nitrite reductase pentaheme
                     subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=22247
     Region          44..193
                     /region_name="cyt_nit_nrfB"
                     /note="cytochrome c nitrite reductase, pentaheme subunit;
                     TIGR03146"
                     /db_xref="CDD:132190"
ORIGIN      
        1 mgnvklairt tisfllfici ygfnvsaaae spdhavinan tdsrhevtfn rdsdyaciqc
       61 hkdsketrqg thgekvvaei grdlkcvech ntigpnhred apqvtkffaa qskigthknl
      121 ldfgailkat gnctdchtpe klqektwvhd vhakkatcss chmihadgek egmqalerke
      181 qiaqcvdchk dfnlikedkg e
//
LOCUS       WP_112774280             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus alkaliphilus].
ACCESSION   WP_112774280
VERSION     WP_112774280.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus alkaliphilus
  ORGANISM  Cupriavidus alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus alkaliphilus"
                     /db_xref="taxon:942866"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38829
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvvvqagag lnasqpdgay eavgatigsa
       61 adalgaqlvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaasit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrqapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vvdkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_112775520             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus alkaliphilus].
ACCESSION   WP_112775520
VERSION     WP_112775520.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus alkaliphilus
  ORGANISM  Cupriavidus alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus alkaliphilus"
                     /db_xref="taxon:942866"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53920
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvkellk lgyqvavetg agleasfsdd dyraagaaiv
       61 daaslwasvd vvvkvrppqv hpslgveeaa llkkhatlig fvwpaqqmam lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyakems
      241 pafieaemrl faeqarqvdi iittalipgk papklleagt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpgk dgqlvvnmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevpvpaea apprsragtt lialalaaaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_112777287             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus alkaliphilus].
ACCESSION   WP_112777287
VERSION     WP_112777287.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus alkaliphilus
  ORGANISM  Cupriavidus alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus alkaliphilus"
                     /db_xref="taxon:942866"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39085
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipqetr vgetrvaatp etvkkyvaqg hhvtvqsgag vrasvpdgay eavgarigtm
       61 aealgaelvl kvrapddael aqmkrgatlv gmlnpfdten nvrmaatgit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfftdee reiaqgvggy arpmpadwmk
      241 rqaelvhqra lqadivitta lipgrkaptl lheatvqemk pgsvvvdlaa aqggncpltv
      301 adevverhgv ilvghtnlas mvaadasaly arnvfdflkl vldkeakltv nleddivaac
      361 lmcaggeltr an
//
LOCUS       WP_112829377             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            cremeum].
ACCESSION   WP_112829377
VERSION     WP_112829377.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium cremeum
  ORGANISM  Rhizobium cremeum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium cremeum"
                     /db_xref="taxon:2813827"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55395
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspkeif agearvamtp dsavqlqklg yeclieagag ksagfsdeay raagvtvvdg
       61 aealyagadv iakvrppeta eaerltagkt lisffypaqn kdllelckek ganvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfad qqqdgaatgg yaapsspefr
      241 ekqlekfrel apdmdivitt alipgrdapk lwladmvaam kpgsvvidla aerggncdlt
      301 vadqrivsdn gvivigytdf psrmaaqsst lystnirhmm tdltpakdgv lvhnmeddvi
      361 rgatvtyqge itfpppppkv qaiaaqkpke kpkeltpeek raqevaafka qtrnqaglla
      421 igtalllivg ayapasfmsh fivfvlacfi gfqviwnvsh slhtplmavt naisgivilg
      481 allqigsgnw lvvilaalsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_112861583             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brevundimonas vesicularis].
ACCESSION   WP_112861583
VERSION     WP_112861583.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas vesicularis
  ORGANISM  Brevundimonas vesicularis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Brevundimonas vesicularis"
                     /db_xref="taxon:41276"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38567
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavaiavtre rregetrcav tpetvkklia lgatvtveag tglgssipda dyaaagatvk
       61 pdtravldga dillkvrgpt aqetsalkpg avviamlday rdkaavdala gagatafame
      121 fvpritraqv mdvlssqanl agyravieaa yaygkgfpmm mtaagtvaaa kvfimgvgva
      181 glqaiatarr lgavvtatdv rpatkeqves lgakflaved eefknaqtag gyakpmsaey
      241 qakqaeltag hvvkqdivit talipgraap vlltaahvaa mkpgsviidl aveaggnveg
      301 sklnevvtta ngvtivgwsn lpgriaadas alyarnltaf vgllvkdavl avdledeilk
      361 aavvthagav vheglkgth
//
LOCUS       WP_112866207             471 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Plesiomonas shigelloides].
ACCESSION   WP_112866207
VERSION     WP_112866207.1
KEYWORDS    RefSeq.
SOURCE      Plesiomonas shigelloides
  ORGANISM  Plesiomonas shigelloides
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Plesiomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Plesiomonas shigelloides"
                     /db_xref="taxon:703"
     gene            1..471
                     /gene="nrfA"
     Protein         1..471
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52287
     Region          1..471
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivklnttsi ttglalfltg tllcssalaq vearndkfad ahqpqyqswt qtqqsserad
       61 alaedpnmvi lwagypfskd ynkprghyya ltdvrdtlrt gapktaedgp lpmacwscks
      121 pdvarmiese gedayfkgmw akggpeivns igcadchatd sqefkdgkpa lhlsrpyasr
      181 amdaihmpfa kqgrfdqqaq vcgqchveyy fsgdnkavkf pwdngtsada maeyydelgf
      241 kdwvhglskt pmlkaqhpey etwqagihgk nnvgcvdchm pkvqgqdgkl ytdhkvgnpf
      301 drfdqtcanc htqskemlqg vvkerkeain tlklkveqql vhahfeakaa wdagateeqm
      361 qpilqdirqa qwrwdyaias hgvhmhapdi alktlgdaln laadartkla rllatkgitg
      421 eiplpdistk ekaqatlgmd mkqfisdkqq flkttvpawe keakdagrls q
//
LOCUS       WP_112871021             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112871021
VERSION     WP_112871021.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53571
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwn dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112874987             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            endophyticus].
ACCESSION   WP_112874987
VERSION     WP_112874987.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus endophyticus
  ORGANISM  Paracoccus endophyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus endophyticus"
                     /db_xref="taxon:2233774"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55297
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigalkett egearvavtp ssaghlqklg hevhvesgag aragfsdaay eragvtvhpt
       61 aaaliaavdv vakvrppsda emaamregqt lisffypgqn aelleaarnr gvnaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv livgagvagl
      181 aaigaatslg aqvyafdvrp evaeqiesmg aefvyldfkd elqdgaatgg yaapsspefr
      241 gaqlakfrel apemdivitt alipgrpapk lwtedmvaam kpgsviidla aerggncdlt
      301 vpdekivtdn gvtiigytdf psrmgaqase lygnnvrhml adltpakdgt lvhdmdddvi
      361 rgatvtkdrd vtwpppppki qaiavqkpke kpreltpeer raqelaafra qtrsqvtllg
      421 vgalvmllig lfapasflsh fivfvlacfv gfsviwnvah slhtplmait naissivilg
      481 allqigsgsa wvvilgalav lmtavnifgg flvtrrmlam fqks
//
LOCUS       WP_112885937             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_112885937
VERSION     WP_112885937.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35635
     Region          5..170
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifelfskr qkklrgevad vyqytnipna frvqvvhivr dtigedsdye teasklyrlv
       61 hktlckeygv fslkqypesn fgaifdyfla erdhekcldi ieicfklidg yirsnewkfr
      121 glvkqspdds ieelnirfke aglgyqfesg elvkvdsqfi hsdvvkptlq ilgknksyng
      181 andeflsahe hyrhqrykec lndclksfes lmkaihkkhs wqfndtdtak klinsclann
      241 lvpeylqnqf ssirillesg iptirnkegg hgqgaeitkv peylasytlh ltatnllfla
      301 kceesytkk
//
LOCUS       WP_112905173             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            leguminosarum].
ACCESSION   WP_112905173
VERSION     WP_112905173.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39154
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare itgeetrvaa spetvkkmks fgfdvvveag agaasripdg efeaagarig
       61 sfadaasadv vlkvrrpsgs eisgyksgav iiaimdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgraaprl vshimlasmk sgavavdlav erggniegvv
      301 pgeiadvegv rvigfanmpg rvaasasaly aknlvtflet mvnketrsvv vnlddelvka
      361 tmltyagdvv hpafggakkg di
//
LOCUS       WP_112914337             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112914337
VERSION     WP_112914337.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53557
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwn dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqwdeqa rkngllsq
//
LOCUS       WP_112913829             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112913829
VERSION     WP_112913829.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53600
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnvegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112918667             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112918667
VERSION     WP_112918667.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53573
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqesmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112920954             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112920954
VERSION     WP_112920954.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53600
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvev knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112921746             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_112921746
VERSION     WP_112921746.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53553
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag hfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_112932005             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium sp. PM5].
ACCESSION   WP_112932005
VERSION     WP_112932005.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. PM5
  ORGANISM  Microbacterium sp. PM5
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Microbacterium sp. PM5"
                     /db_xref="taxon:2014534"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51740
     Region          3..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 marigivrer pgetrvaasp ttvgkiralg ydvsveagag aassfpdaay taagaaiatr
       61 deawgadvvl svaaptdaei allqpgatlv gilspalspd llaalaargv talamdavpr
      121 israqsmdvl ssmaniagyr avveaanefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvasiggt ylevvvpdeq kevsadgyak atsaaydaaa
      241 aklysdqaad vdivittali pgraaprllt aadvaamkpg svivdmaagq ggnvegsvag
      301 qrivtdggvi ilgytdlagr lpqqasqlyg tnlvnllall tpgkdgqlai ddtdvvqrav
      361 tvtrdgavtw ppppvqvsaa ltkpgtdaaa stpapaakkg lsagaktgli vagvaalflv
      421 cavapaplpq hilvltlsvv igfyvigkva halhtplmsv tnaisgiivv gamsqivvpn
      481 pvvqvlaaia vllasinifg gfavtrrmla mfqkgdqk
//
LOCUS       WP_112939037             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Massilia
            sp. YMA4].
ACCESSION   WP_112939037
VERSION     WP_112939037.1
KEYWORDS    RefSeq.
SOURCE      Massilia sp. YMA4
  ORGANISM  Massilia sp. YMA4
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Massilia sp. YMA4"
                     /db_xref="taxon:1593482"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38928
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qilvqsgags qasitdeafq aagativgat
       61 ealgadivlk vrapndaera qmrqgavlig mlnpfdadni armaasglsa faleavprit
      121 raqsmdvlss qaniagykav mvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpfltdeek eiaqgvggya rpmpadwmrr
      241 qaelvherak ladivittal ipgrpapvli geetvkamkp gsvivdlave qggncplsel
      301 gktvvkhgvh ivgepnlacq vaadasalya rnvldflkli idkedqlkid redeilkatl
      361 vshagdvlrk
//
LOCUS       WP_112950363             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp.].
ACCESSION   WP_112950363
VERSION     WP_112950363.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp.
  ORGANISM  Rhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp."
                     /db_xref="taxon:391"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55513
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeli agesrvamtp dsalqlqklg yiclieagag slagfsdkay raagvevvet
       61 aealfgqadi iakvrppepr elerlragqt lisffypgqn atlleqakat ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfkg dsqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvaam kpgsvivdla aerggncelt
      301 vadqrivsdn gvivvgytdf psrmaaqsst lyatnirhmm tdltpakdgk lvhnmeddvi
      361 rgatvafega vtypppppki qaiaaqkrqe kakeltpeek raketaafka qtksqgflll
      421 igtallllvg ayapasfmnh fvvfmlacfi gfqviwnvsh slhtplmavt naisgivilg
      481 allqiasgnw lvillaalsv lvatinivgg flvtrrmlam fqks
//
LOCUS       WP_112985060             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ensifer
            sp. ENS03].
ACCESSION   WP_112985060
VERSION     WP_112985060.1
KEYWORDS    RefSeq.
SOURCE      Ensifer sp. ENS03
  ORGANISM  Ensifer sp. ENS03
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Ensifer sp. ENS03"
                     /db_xref="taxon:2769283"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55198
     Region          1..527
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaprevt asearvaltp dsavqlaklg yssiietgag vaagfsdday ravgvevaps
       61 aealwasadv vakvrppeps evaylsadkt lisffypgqn aellelarek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigvatslg aqtyafdvrp evaeqiesmg aefvyldfad gegggqqdga atggyaapss
      241 pefrekqlak frelapqidi vittalipgr dapklwladm vaamkpgsvv vdlaaerggn
      301 cdltvadqrv vsdngvvvig ytdfpsrmaa qastlyatni rhmltdltpg kdgklvhnme
      361 ddvirgatvt fegaityppp ppkiaaiaaq kpkekvkept peekrateaa afkaqtksql
      421 tllavgtall llvgafappa fmshfvvfvl acfvgfqviw nvshslhtpl mavtnavsgi
      481 vilgallqig sgnwlvvlla alsvliatin ivggflvtrr mlamfqks
//
LOCUS       WP_112992831             532 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Herminiimonas fonticola].
ACCESSION   WP_112992831
VERSION     WP_112992831.1
KEYWORDS    RefSeq.
SOURCE      Herminiimonas fonticola
  ORGANISM  Herminiimonas fonticola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herminiimonas.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Herminiimonas fonticola"
                     /db_xref="taxon:303380"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55577
     Region          5..531
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mslvigvpre sfpgekrvat vpevveklik lgfsvsvesg agddanfsdd tyraagaqiv
       61 qgaanlwsgs divfkvraps adevglireg stligfiwpa qnpelmqqla akrvtvlamd
      121 slprtlsraq kmdaltstag vsgyraviea anafgrffng qitaagkvpp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvv slggefvkvd feeegsgggg yakvmsegfq
      241 aaqremyaqq akecdiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 epgkvvvkhg vtivgytdlp srlpkqastl ystnllrlte elckdaegkk ttdgiinvnm
      361 edeairgltv ikegnitwpp pppkqvaapa akpvvaptps hghgpstkvs sptrvatmfa
      421 faillfglig ygaptaflgh ltvfvlgcfi gymvvwnvtp alhtplmsvt nsissiivig
      481 alvqvappla dgmarpelli kclaaagial tainmfggfa vtrrmldmfr kn
//
LOCUS       WP_113044615             530 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_113044615
VERSION     WP_113044615.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54815
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ataadlwgrs divlkvrpps seevallrdg stlvgfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgti nvdfnddair
      361 gltvikegnv twppppiqqp vaapkpatpp vaaaaskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_113062747             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Oligella
            urethralis].
ACCESSION   WP_113062747
VERSION     WP_113062747.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54421
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkeqf agetrvaatp ttvtqliklg ydvavesgag qlakfddaay teagasvvsr
       61 ddvfksdivy kinapsdaei damdegtilv sfvqpaqnpe lveklrakki tamavdmvpr
      121 israqsmdvl ssmanisgyr avieaahhfg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igaagslgai vkafdtrlev aeqiesmgge flkldfpqea ggsgdgyakv msdefikaem
      241 alfaeqakvv diiittaaip gkpspklitk emvdsmkpgs vivdlaalgg gnceytvpge
      301 vivtdnnvtv igytdlpnrl agqssqlyst nlvnlsklit pakdgqavld fddviirnmt
      361 vthagelmfp pppiqvsaap qqqaapaaap atkpekapkp lwqklalpvi gvliylwash
      421 yapqeflnhl tvfmlscvvg yyvvwnvtha lhtplmsvtn aisgiiivga viqmsningf
      481 asflafisvf lvsinifggf yvtrrmlnmf rkg
//
LOCUS       WP_113070642             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas caviae].
ACCESSION   WP_113070642
VERSION     WP_113070642.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53236
     Region          27..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsydklf rpglaalllt allgagslaq aadeaqskgk iearselfak dhtdqftswk
       61 gtsesrertd alaedpqmvv lwagypfskd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkagkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meqyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg vvkqrkdavt eiklkvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakgish eiaipdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_113083310             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agrobacterium tumefaciens].
ACCESSION   WP_113083310
VERSION     WP_113083310.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium tumefaciens (Rhizobium radiobacter)
  ORGANISM  Agrobacterium tumefaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Agrobacterium tumefaciens"
                     /db_xref="taxon:358"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55788
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkely egearvgmtp dsaqalqklg ydciletgag kaagfsdday raagvtivds
       61 adalyagsdi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qsqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvamm kpgsviidla aerggncdlt
      301 vpdqrvvsdn gvivigytdf psrmatqast lystnirhmm tdltpakdgk pvhnmeddvi
      361 rgatvtyqge itfpppppki qaiaaqkpke rakeltpeek hakeraefka qtksqvgllv
      421 igtavlllvg lyapasfmsh fivfvlacfi gfsviwnvsh slhtplmavt naisgiviig
      481 allqigsgnw lvvllaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_113117252             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. BK512].
ACCESSION   WP_113117252
VERSION     WP_113117252.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. BK512
  ORGANISM  Rhizobium sp. BK512
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium sp. BK512"
                     /db_xref="taxon:2587010"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39308
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 manivfvake itgdetrvaa svetvkkika lgfdviveag agalsripds efeavgaaig
       61 tfadaasadv ilkvrrpses eiagyktgav viaimdpygn deavaamara glstfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtipaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemsadyqa
      241 rqaalvaehi akqdivitta lipgrpaprl vsramlasmk pgavavdlav erggniegvv
      301 tgqiadvegv kvigfpnmag rvaasasaly aknlvtflet mvnketksvv lnledelika
      361 tmltyagdvv hpafggakkg dn
//
LOCUS       WP_113136080             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ensifer
            sp. ENS07].
ACCESSION   WP_113136080
VERSION     WP_113136080.1
KEYWORDS    RefSeq.
SOURCE      Ensifer sp. ENS07
  ORGANISM  Ensifer sp. ENS07
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Ensifer sp. ENS07"
                     /db_xref="taxon:2769274"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55269
     Region          1..527
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaprevt asearvaltp dsavqlaklg yssiietgag vaagfsdday ravgvevaps
       61 aealwasadv vakvrppeps evaylsadkt lisffypgqn aellelarek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigvatslg aqtyafdvrp evaeqiesmg aefvyldfad geggaqqdga atggyaapss
      241 pefrekqlak frelapqidi vittalipgr dapklwladm vaamkpgsvv vdlaaerggn
      301 cdltvadqri vsdngvviig ytdfpsrmaa qastlyatni rhmltdltpg kdgklvhnme
      361 ddvirgatvt fqgaityppp ppkiaaiaaq kpkekvkept peekrateta afkaqtksql
      421 tllavgtall llvgafappa fmshfvvfvl acfvgfqviw nvshslhtpl mavtnavsgi
      481 vilgallqig sgnwlvvlla alsvliatin ivggflvtrr mlamfqks
//
LOCUS       WP_113156011             445 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitratireductor sp. OM-1].
ACCESSION   WP_113156011
VERSION     WP_113156011.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor sp. OM-1
  ORGANISM  Nitratireductor sp. OM-1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Nitratireductor sp. OM-1"
                     /db_xref="taxon:1756988"
     Protein         1..445
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45902
     Region          5..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,289,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqsifvpke vdvtegrvai spetvkrlag lgfdivvekn ageqsrivds efekagakig
       61 kasdaskadv vlklrrptpa evktykkgal vlasmdpygn egdvaamaaa gvtafamefm
      121 pritraqsmd vlssqanlag yravidaaae ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvra aageqvqslg akfimtealk dasgdggyar eltdeekkaq
      241 aelvaehiak qdivittali pgrpaprlvs tdmvksmkpg siivdlaver ggnvegakag
      301 evvttangvk ivghlnvpgr vaasasllya knlytfletm vdkekkelav dmedelvkat
      361 mlthdgkvvh pnfvdtvkpv akaaaprkap arktparkpa akaaagaatk ktaaqktaaq
      421 ktadkpagas saadkpaaak sgges
//
LOCUS       WP_113231955             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            sp. BK591].
ACCESSION   WP_113231955
VERSION     WP_113231955.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium sp. BK591
  ORGANISM  Rhizobium sp. BK591
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium sp. BK591"
                     /db_xref="taxon:2586985"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55551
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigsprerl egearvamtp dsatqlqklg yqcaietgag klagfsdday raagvrivds
       61 vealfasvdv iakvrppeps diaklssnkt lisffypaqn kelleqakat ranviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsvslg aityafdvrp evaeqiesmg aefvfldfke qqqdgattgg yaspsspefr
      241 eaqlkkfrei apdidivvtt alipgrdapk lwladmvaam kpgsvvvdla aerggncdlt
      301 vpdqkivsen gvtvigytdf psrmaaqast lystnirhmm tdltpkkdgv lvhnmeddvi
      361 rgatvafege itypppppki qaiaaqkrqe kakeltpeer raaeaaafks atrqqvgllv
      421 vggllmalig ayapsafmgh fivfalacfv gfqviwgvsh slhtplmavt naisgiiiig
      481 allqitaggw lvtalaaisv aiatinivgg fmvtrrmlnm fqks
//
LOCUS       WP_113257378             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseovarius sp. TE539].
ACCESSION   WP_113257378
VERSION     WP_113257378.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. TE539
  ORGANISM  Roseovarius sp. TE539
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseovarius sp. TE539"
                     /db_xref="taxon:2249812"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56128
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeir agearvamtp dsatqlqklg yecaietgag klagfsdady eaagveiikt
       61 gaqlwkaadi vakvrqptdt evkrlregqt lisfftpaen eeqmqmaaek gatviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvpparv lvvgagvagl
      181 aaigtstslg aitfafdvrp evaeqiesmg aefvyldfee esqdgaatgg yaapsspefq
      241 qkqlekfrem apemdivitt alipgrpapk lwtedmvkam kagsvvidla aerggncemt
      301 rpdekivtdn gvtivgytdf psrmatqssm lyatnirhmm tdltpekdgk pvhdmeddvi
      361 rgatvahggd vtypppppkv qaiaaapkke pekeltpeer rarelaefrk qtrnqvtlla
      421 igavlvlavg lvapasfmkh fivfvlsvfv gfqviwnvsh slhtplmavt naissiiilg
      481 aliqigsssv litilaalav fmasinifgg flvtrrmlam fqks
//
LOCUS       WP_113260987             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agrobacterium cavarae].
ACCESSION   WP_113260987
VERSION     WP_113260987.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium cavarae
  ORGANISM  Agrobacterium cavarae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Agrobacterium cavarae"
                     /db_xref="taxon:2528239"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55548
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgapreiy esearvamtp dsaqalqklg yeclietgag ksagfsdeay raagvtvven
       61 adalysgsdi iakvrppeas eidrlspdkt lisffypaqn qtllqqakdk gaaviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv liigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfae qqdgaatggy aapsspefre
      241 kqlakfrela pqidivitta lipgrdapkl wladmvaamk pgsvivdlaa erggncdltv
      301 pdqrivsdng vivigytdfp srmaaqastl yatnirhmma dltpgkdgqv vhnmeddvir
      361 gatvaykgei typppppkik aiaaqkpkek aneltpaekr aqeitlfktq trnqvallav
      421 gtallllvgv yapasfmshf ivfvlacfig fqviwnvshs lhtplmavtn avsgivilga
      481 llqvgssnwl vvilaalsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_113270965             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Vreelandella sulfidaeris].
ACCESSION   WP_113270965
VERSION     WP_113270965.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella sulfidaeris
  ORGANISM  Vreelandella sulfidaeris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Vreelandella sulfidaeris"
                     /db_xref="taxon:115553"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55697
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkesa qgearvaltp esakqiqklg heclvetgag laagfnddty rdagvtvveg
       61 adalwnetev vikvrepseq eaerlregqt lisffwpaqn eallekckaq gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfed sqdgsesggy aspsspefre
      241 kqlecfreqa pdvdivitta lipgrpapkl wledmvaamk pgsviidlaa ekggncdltk
      301 pdervvsdng vvvigytdfp srmatqssll yatnirhmlt dltpekegvi nhnmdddvir
      361 gatvthqsei tfpppppkvk aigaskpkkk ekeptpeekk atelanfkaq ttrqvgllav
      421 ggvlmlllgq vapasfmqhf ivfvlacfig fqviwkvshs lhtplmavtn aisgiiilga
      481 ilqigsgsiv vsvlaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_113280911             435 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium pellucidum].
ACCESSION   WP_113280911
VERSION     WP_113280911.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium pellucidum
  ORGANISM  Phyllobacterium pellucidum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Phyllobacterium pellucidum"
                     /db_xref="taxon:2740464"
     Protein         1..435
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45137
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke tdanearvgg spetvkrlig lgfnvvvetg agtasripda eftgagasig
       61 kaadvkdadi vlkvrrpasp elksykkgav viamldpygn dsavkelada gltaftmefm
      121 pritraqvmd vlssqanlag yqavidaaee ydralpmmmt aagtvpaakv fvmgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaalvndhi akqdivitta lipgrpaprl vtremyarmr pgsvlidlav erggnvegav
      301 agkiteidgv kivghlnvpg riaatasqly aknlvafvet lvdkeakvlk infddelvka
      361 tmlthdgkvv hpnfaqaaaa vavpaetraa rpvakkaapa kpaapkdaav kpaakkaapk
      421 kaaaskaapk tegea
//
LOCUS       WP_113287928             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodosalinus halophilus].
ACCESSION   WP_113287928
VERSION     WP_113287928.1
KEYWORDS    RefSeq.
SOURCE      Rhodosalinus halophilus
  ORGANISM  Rhodosalinus halophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodosalinus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhodosalinus halophilus"
                     /db_xref="taxon:2259333"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56158
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevm egearvamtp qsardlqklg hdclieagag ekagfndsay eeagvtvvpd
       61 aealwkeaei vakvrpptda evertregql lisffwpaqn edhmkalaek gssviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee dmedgsasgg yakpsspefr
      241 eaqlakfrel apemdivitt alipnqeape lwtedmvkam kpgsvivdla aerggncklt
      301 vpddkivtdn gvtivgytdf psrmatqsst lyatnirhlv tdltpekdgk ivhdmeddvi
      361 rgatvahage vtfpppppkv qaiaaqkpke kpkeltaeek rqqeiaefrk qtrnqvtllg
      421 gglvlmgllg lvapasfmqh fivfvlacfv gfqviwnvnh alhtplmavt naisgiivlg
      481 ailqigsgnw lvillaaisv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_113328846             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_113328846
VERSION     WP_113328846.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53630
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta tpakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkleltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdisikeka qkaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_113341356             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_113341356
VERSION     WP_113341356.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53492
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dactklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_113354955             387 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium].
ACCESSION   WP_113354955
VERSION     WP_113354955.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40449
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msnlvfvake svaeetrvaa svetvkkmkn lgfdvvieag agalsripdt eyeavgarig
       61 sikdakaadv ilkvrrptsk eisgyksgai viaimdpygn eaalaemara gltsfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg alvsatdvrp aakeqvaslg akfvavedee fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vgrdmlkamr pgavavdlav erggniegae
      301 ygkiadvegv kvvgypnmag riaasasaly aknlvtflet mvdkdtksla lnrtdelika
      361 tmltdggevv npnfvdpdqp tikkgdl
//
LOCUS       WP_113396674             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_113396674
VERSION     WP_113396674.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53584
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vreilrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_113419861             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_113419861
VERSION     WP_113419861.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53599
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntpspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheie ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_113485620             433 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Brucella
            pseudogrignonensis].
ACCESSION   WP_113485620
VERSION     WP_113485620.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudogrignonensis (Ochrobactrum pseudogrignonense)
  ORGANISM  Brucella pseudogrignonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Brucella pseudogrignonensis"
                     /db_xref="taxon:419475"
     Protein         1..433
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44934
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
     Region          <375..428
                     /region_name="valS"
                     /note="valyl-tRNA synthetase; Provisional; PRK14900"
                     /db_xref="CDD:237855"
ORIGIN      
        1 maqtifipke sdpnetrvaa saetvkkfia lgfdvvvekg ageksriidt efsgagarig
       61 ttadakaadv ilkvrrpnda elkgykpgaa lfamldpygq eaavaalaka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaadv ydrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedee fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgraaprl vskemvaamr pgsvlvdlav erggnvegav
      301 agqvadvngv kivghlnvpg riaatasqly arnlyaflet lvdkeakllk ldpqeelvka
      361 tllthegkvv hpafakaeve aapavvaekv akpkaapkvk apavkaeaek pvakktrkap
      421 akaaktsadg gea
//
LOCUS       WP_113505630             381 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Ensifer].
ACCESSION   WP_113505630
VERSION     WP_113505630.1
KEYWORDS    RefSeq.
SOURCE      unclassified Ensifer
  ORGANISM  unclassified Ensifer
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="unclassified Ensifer"
                     /db_xref="taxon:2633371"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39528
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfvake tdpnegrvaa spdtvkklkg lgfdvvveag agflsripda efeksgarig
       61 ttadaraadv vlkvrrptsv eiagyrsgai viaimdpygn eaaiadmana gltafamelm
      121 pritraqsmd vlssqanlag yqavidaaye ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskdyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vtremlksmk pgsiavdlav erggnvegae
      301 agkvaevegv kvighlnvpg riaasasgly aknlvtflet mvsketkala lnmedelvka
      361 talthggqvv hpnfgaskgd k
//
LOCUS       WP_113543189             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            leguminosarum].
ACCESSION   WP_113543189
VERSION     WP_113543189.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55874
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msivgvpkei aphearvalt pesalqlqkl gyeclieags gnaagfsdda yraagvtvvg
       61 daselyvrad ivakvrppee vevnrlgpqq tlisffypaq nkellescke kganviaidm
      121 vprisraqkm dalssmania gyravieags nfsrfftgqv taagkvppak vlvigagvag
      181 laaigtatsl gaityafdvr pevaeqiesm gaefvfldfn eeqqdgaaag gyaapsssef
      241 rekqlakfre lapqidivit talipgrdap klwladmvaa mkpgsvivdl aaerggncel
      301 tvpeqrlvsd ngvivigytd fpsrmatqas tlyatnirhm lsdltpgkdg vivhnmeddv
      361 irgatvlyrg eitypppppk vqaiaaqkpk dkvkeltpee kraaelfafr mqtrnqgmll
      421 avgtalllfv gafvpasfms hfvvfvlacf igfqviwsvs hslhtplmav tnavsgivil
      481 gallqigsgh wlvvalaals vliatinivg gflvtrrmla mfqks
//
LOCUS       WP_113545394             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            leguminosarum].
ACCESSION   WP_113545394
VERSION     WP_113545394.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55309
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligsprerf egearvamtp dsatqlqklg yqcaietgag kragfsdday raagatvvds
       61 aealfasadv iakvrpaess evarlssgkt lisffypaqn kdlldqakat ganviamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsvslg aityafdvrp evaeqiesmg aefvfldfee qqqdgaatgg yaapsspefr
      241 eaqlkkfrei apdidivvtt alipgrdapk lwladmvamm kpgsvivdla aerggncdlt
      301 lpdqkiisdn gvtvigytdf psrmaaqsst lystnirhmm tdltpkkdgv ivhnmdddvi
      361 rgatvafqge itypppppki qaiaaqkpke narklapeek raaeaaafka atrnqvglli
      421 vggllmllig afapqvfmgh livfalacfv gfqviwgvsh slhtplmavt naisgiiiig
      481 allqitvggw lvtalaaisv aiatinivgg fmvtrrmlnm fqks
//
LOCUS       WP_113593346             512 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Vibrio].
ACCESSION   WP_113593346
VERSION     WP_113593346.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53873
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr rn
//
LOCUS       WP_113599717             512 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Vibrio].
ACCESSION   WP_113599717
VERSION     WP_113599717.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53826
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsh
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_113601223             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            paracholerae].
ACCESSION   WP_113601223
VERSION     WP_113601223.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53848
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 deiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgad flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 fttdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq pkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr rn
//
LOCUS       WP_113609414             312 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Vibrio].
ACCESSION   WP_113609414
VERSION     WP_113609414.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     Protein         1..312
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35934
     Region          5..173
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mgtfdlfskr qkklrgdvpe vytydslpnp lrvqiihiwn dslgdklqyf svddiretyk
       61 fivetlcrey glfelpsnkn grqriyidel anyfleennv ekqldvveit fkvintvtre
      121 yqymrkngas evadsaidel narlkehgvg fqftnneiir vdsellhsea vkpallllnq
      181 khykgaqeef llayehyrhg rykeslndcl kafestmksi cdnhdwkyee satarsliqi
      241 cfdnglipsf wqqqmsslrs llesgvptgr nrlsghgqgs ntieipdylv aymlhmtast
      301 lvflttaesk ia
//
LOCUS       WP_113604764             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            tarriae].
ACCESSION   WP_113604764
VERSION     WP_113604764.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tarriae
  ORGANISM  Vibrio tarriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio tarriae"
                     /db_xref="taxon:2014742"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53872
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay iaagatigsh
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavfi asinifggft vtkrmlemfr kn
//
LOCUS       WP_113617512             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga flava].
ACCESSION   WP_113617512
VERSION     WP_113617512.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga flava
  ORGANISM  Chitinophaga flava
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Chitinophaga flava"
                     /db_xref="taxon:2259036"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40426
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miagilkekn getrvsltpe ivkqlqqmsv tvwveqgage qafynddaym qagaliktaa
       61 evlsqsdiif tiqppsrela eqiaagkill gvlqplfrpe evgywasqni ttfsldsipr
      121 ttraqvmdvl ssqanisgyk avllaaysys ryfpmfmtaa gsiapakvli lgagvaglqa
      181 iatakrlgav vevfdtrpav keevmslgar fvevegaada sagggyaveq neeyqkkqqq
      241 kiaesiakad ivittaqipg kpapvlvtqp mldqmhsgav ivdlaaatgg ntaltrnnet
      301 vhyrgitiig nsnlpatmpa dasklyaknv fnflkliltk egnlhlnfed divkgacith
      361 ngeivnerlk sakpatsti
//
LOCUS       WP_113639886             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia albertii].
ACCESSION   WP_113639886
VERSION     WP_113639886.1
KEYWORDS    RefSeq.
SOURCE      Escherichia albertii
  ORGANISM  Escherichia albertii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia albertii"
                     /db_xref="taxon:208962"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53688
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtriktnarr ffsllipfff ftsvhaeqta spakpvtvea knetfapqhp dqylswkats
       61 elservdala edprlvilwa gypfsrdynk prghayaitd vretlrtgap knaedgtmpm
      121 acwsckspdv vrliqkeged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaeramn aigkpfekgg rfdqqsmvcg qchveyyfdg kdkavkfpwd ngmkvenmeq
      241 yydkiafsdw tnalsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkatlqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gataaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qraiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_113642417             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Prauserella sp. PE36].
ACCESSION   WP_113642417
VERSION     WP_113642417.1
KEYWORDS    RefSeq.
SOURCE      Prauserella sp. PE36
  ORGANISM  Prauserella sp. PE36
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Prauserella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Prauserella sp. PE36"
                     /db_xref="taxon:1504709"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38685
     Region          12..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtetesptgs tltigvvket kpgerrvalv pklierltkr glrvvveqga gagaqladev
       61 fteagatmgd awsadivltv vppsvadier lkpgtvligf lapltntdev aamkkagita
      121 favesipris raqamdalss qanvagyrav llaaqrlpkf fpmlttaagt vpptkalvlg
      181 vgvaglqala takrlgaqat gydvrpevae qvrsvgaqwl dlgieaageg gyarelteee
      241 raeqqrrlte aiggfdvvit talvpgrkap tlvtaeavrg mkagsvivdm agetggncel
      301 tepgkdivah dvticsplnl paempvhase lyarnltell elivdtdgkl aidfsdevva
      361 gacvagrdee vn
//
LOCUS       WP_113650669             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia albertii].
ACCESSION   WP_113650669
VERSION     WP_113650669.1
KEYWORDS    RefSeq.
SOURCE      Escherichia albertii
  ORGANISM  Escherichia albertii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia albertii"
                     /db_xref="taxon:208962"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53563
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtriktnarr ffsllipfff ftsvhaeqta spakpvtvea knetfapqhp dqylswkats
       61 elservdala edprlvilwa gypfsrdynk prghayaitd vretlrtgap knaedgtmpm
      121 acwsckspdv asliqkeged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaeramn aigkpfekgg rfdqqsmvcg qchveyyfdg kdkavkfpwd ngmkvenmeq
      241 yydkiafsdw tnalsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkatlqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gataaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_113668358             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodovulum
            sp. BSW8].
ACCESSION   WP_113668358
VERSION     WP_113668358.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum sp. BSW8
  ORGANISM  Rhodovulum sp. BSW8
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhodovulum sp. BSW8"
                     /db_xref="taxon:2259645"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55506
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeil egearvamtp dsavqlrklg ydclieagag eaagfadaay ekagvkvvqs
       61 aaalwqgadi vvkvrepvae evarlrkgqt lisffwpaqn ealleqckar gatviamdmv
      121 prisraqkmd alssmaniag yravieagsn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg amvfafdvrp evaeqiesmg aefvfldfee atadgsesgg yakpsspefr
      241 ekqlekfrel apemdivitt alipgrpapk lwledmvaam kpgsvivdla aekggncdlt
      301 rpgekivsdn gvtvvgytdf asrmatqsst lyatnirhmm tdltpakdgq vvhnmeddvi
      361 rgatvthege itfpppppkv kaiaaaprke kpkeltpeek kaqeaaafrk qtitqvamla
      421 vgaalmllvg afapasfmsh fivfalscfv gfqviwnvsh slhtplmavt naisgiiilg
      481 allqigsgnw lvvilatvsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_113693439             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis albispora].
ACCESSION   WP_113693439
VERSION     WP_113693439.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis albispora
  ORGANISM  Amycolatopsis albispora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Amycolatopsis albispora"
                     /db_xref="taxon:1804986"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37475
     Region          8..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvaesgpvtv gvvkeslpge rrvalvpkal grllarglrv vvesgagdga litdsdyeaa
       61 gasigdawaa dvvlkvappt aaevtrlapg tvligflapl snverikela eagvtafave
      121 sipritraqa mdalssqssv agyravllaa erltrffpml ttaagtvapa kvlvlgagva
      181 glqalatarr lgaqttgydv rpevaeqvrs vgaqwldlgi eavgeggyar eltaeeraeq
      241 qrrlteaitr fdvvittalv pgrqapvlvt aeavegmpsg gvivdlages ggncelteag
      301 qdvvrhgvti ssplnlpagm pahaselysr nltellgllv ndegalaldf sdevvagacv
      361 tgegrd
//
LOCUS       WP_113705715             189 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_113705715
VERSION     WP_113705715.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..189
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=21316
     Region          <15..51
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mislspptic nsaielnerf rehgvgyqfe seeiiridsq lihadvvkpt lillsgeplf
       61 egandeflaa hehyrhkryk eclndclksf esimkaihdk nnwkyspndt asklinscls
      121 qnlipaylqs qftslktmle tgiptirnkn aghgqgadik evpeelasym lhltatnllf
      181 llkceknik
//
LOCUS       WP_113719732             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter dokdonensis].
ACCESSION   WP_113719732
VERSION     WP_113719732.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter dokdonensis
  ORGANISM  Arthrobacter dokdonensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Arthrobacter dokdonensis"
                     /db_xref="taxon:2211210"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53462
     Region          3..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivael gretrvaatp ttvkqlfglg yeivvekgag esaafrdeay teagamivga
       61 deawgsdvvl rinpptedei grlaegatli gmlspglrpe lvealaarpi talaldavpr
      121 israqsmdvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksiggt ylkvevaeem kstdgyakat seaynaraae
      241 iyseqaadvd iiittalipg rpapklltad dvagmksgsv ivdmaagqgg nvegsvager
      301 vvtdngvvil gytdlparlp aqasqlygtn mlnllklltp ekdgvlridf ddvvqrsvtv
      361 vregektwpp ppvqvsaapa vktdagtaae stapkkkqgl saagkaglfa agiaalfgin
      421 avapaplpqh ftvlmlsivv gfyvigkvhh alhtplmsvt naisgiivvg allqvtsdni
      481 lmqvlaavav llasinifgg favtrrmlam fsrgekars
//
LOCUS       WP_113720456             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas salmonicida].
ACCESSION   WP_113720456
VERSION     WP_113720456.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53358
     Region          22..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrlt rlglaalllt tcfgasglaq aeeatpkgki earselfakd hvdqfsswke
       61 tseskertda laedpqmvvl wggypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eqyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqskemlqgv vqqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaqmk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llatkgishe ialpdistke kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_113721016             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aeromonas
            salmonicida].
ACCESSION   WP_113721016
VERSION     WP_113721016.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53119
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevaieagag qlasfddaaf eaagasvvps
       61 vwqadlifkv naptdaeiaq ikdgatlvsf iwpaqnpelv kklserninv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggefl kldfgsedga ssdgyakvms defiaaemal
      241 faqqakevdi iittalipgr papklitkem vdsmkpgsvi vdlaaatggn ceytkptelf
      301 vapngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgqvaidfe dvvqrnmtvi
      361 qagevtfppp aisvsaapqk paaapikkae akqpsnkkfv fgalgiaafg wvaavapaaf
      421 lshftvfila cvvgyyvvwn vshslhtplm svtnaisgii vvgallqigq gstlvtalsf
      481 vavliasini fggftvtqrm lkmfrkd
//
LOCUS       WP_113722936             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arcanobacterium haemolyticum].
ACCESSION   WP_113722936
VERSION     WP_113722936.1
KEYWORDS    RefSeq.
SOURCE      Arcanobacterium haemolyticum
  ORGANISM  Arcanobacterium haemolyticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Arcanobacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Arcanobacterium haemolyticum"
                     /db_xref="taxon:28264"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53009
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkeph aqqalvattp dtaaklvklg ydvvieqgag nrasypdsqy eaagarivgg
       61 pdawgadivl tldtppaeqr nlmkngatli srmapashpd tlndlaergi tglamdmvpr
      121 israqsldvl ssmanlagyr avieaaanfg rlfngqvtaa gkvppatvyv igagvaglaa
      181 igtansmgai vnatdvraev aeqiesmgas figipapaqe ssdgyakems qeqahaaekl
      241 yaeqaavsdi vittanipgr kapillsaea vagmkpgsvi vdlaaanggn celtvpgsvi
      301 ttdngviivg htdysvklpa qasqlfgqni vnffklttpn kdgqlhldld dvivrqmtvt
      361 ldgkimfppp pvkvsaapav kpapaevpas epvhekswla kywwmlaaag vfialiyaap
      421 agmtshfmvf alacvvgfyv itsvthslht plmsvtnais giivvgaltq masasilvqi
      481 lafiavivas inifggfmvt drmlkmftrs
//
LOCUS       WP_113743526             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Anaerobiospirillum thomasii].
ACCESSION   WP_113743526
VERSION     WP_113743526.1
KEYWORDS    RefSeq.
SOURCE      Anaerobiospirillum thomasii
  ORGANISM  Anaerobiospirillum thomasii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Succinivibrionaceae; Anaerobiospirillum.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Anaerobiospirillum thomasii"
                     /db_xref="taxon:179995"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54001
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipkesl rgetrvaatp dtvgkliklg fevavqsnag adasfddasy eqagakvlkg
       61 reiwnsdiif kvnapsdaev ellkegqtlv sfirpaqnse lveklnakkv nvlamdmvpr
      121 israqsldal sstanisgyr avveaahtfg rfftgqvtaa gkvppakvlv igagvaglaa
      181 igaahslgai vrafdtrlev adqiksmgge flkldfkned ggssdgyakv msdefikaem
      241 elfaaqakdv diiittaaip gkaaprlitk emvesmksgs vivdlaaatg gnceltqegk
      301 ivttangvki igysdlaarl paqssqlygt nlvnlakllc kekdgninid fedvvlrnmt
      361 vskdgeitfp ppkisvsaap aakpadapaq kveqkqvsnk fkitcvamlv vafaliglya
      421 pekflphftv fvlscvvgyy vvwnvthslh tplmsvtnai sgiivvgavl qissgsfivg
      481 lfafigvlia sinifggfav trrmlamfrk q
//
LOCUS       WP_113751226             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            trematum].
ACCESSION   WP_113751226
VERSION     WP_113751226.1
KEYWORDS    RefSeq.
SOURCE      Bordetella trematum
  ORGANISM  Bordetella trematum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella trematum"
                     /db_xref="taxon:123899"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38851
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipretr dgetrvaatp etvkkyvaag havvlergag laahyrdedy eaagaalgda
       61 aqalgaelvl kvrapseqel pamkrgavlv gmldpfdreg lqrladaglt afaleaapri
      121 traqsldvls sqanlagyka vllaashsar lfpmmmtaag tlkatrvvvl gagvaglqai
      181 atarrlgavv easdvrpavk eqieslgakf idvpfetdee reiaqgaggy arpmppawma
      241 rqaelvaqrc rqadvvitta lipgrpaptl vtaetvaamk pgsvvvdlai erggncplse
      301 kgqvtvkhgv tligltnlpg mlatdasaly arnlqdflkl iigdgaalav rrddeivaac
      361 lmcedgqlvq rt
//
LOCUS       WP_113776575             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhodobacterales].
ACCESSION   WP_113776575
VERSION     WP_113776575.1
KEYWORDS    RefSeq.
SOURCE      Rhodobacterales
  ORGANISM  Rhodobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhodobacterales"
                     /db_xref="taxon:204455"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55375
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkesf pgenrvamtp asakdlqklg ytclietgag saagfadqay vdagvevvkt
       61 gaalfkaadi vakvqppsdv evkrlreeqt lisffypaqn aalmeaankk gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtatslg avtyafdvrp evaeqvesmg aefvfldfne eqqdgaatgg yaavsspefa
      241 aaqlakfrei apdidivitt alipgrdape lwtkdmvdsm kpgsviidla aerggncklt
      301 vkdekivten gvtiigytdf psrmaaqsst lyatnirhmm tdltpekdgr pnhnmeddvi
      361 rgatathkge vtfpppkpki aaiavapkke apkeltaeei rakeladfka qtknqvtlia
      421 vgaalllgvg lvapasfmqh fivfvlsvfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsf lvillaalsv fmtginifgg flvtrrmlam fqks
//
LOCUS       WP_113773020             449 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Yersinia
            enterocolitica].
ACCESSION   WP_113773020
VERSION     WP_113773020.1
KEYWORDS    RefSeq.
SOURCE      Yersinia enterocolitica
  ORGANISM  Yersinia enterocolitica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Yersinia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Yersinia enterocolitica"
                     /db_xref="taxon:630"
     gene            1..449
                     /gene="nrfA"
     Protein         1..449
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=50107
     Region          3..449
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msaaptppie arndkfaqqh vdqftswlkt kesgpredal aedpnlvilw agypfakdyn
       61 kprghayavt dvretlrtaa pktaedgplp macwsckspd varlineqge egyfkgtwak
      121 ggpevvnqlg cadchdtasa dfaagkpalv lsrpyieral qsinkpfeha srldqqsmvc
      181 sqchveyhfa gkdkavklpw dqgtdvesme kyydeiafad wvhplsktpm lkaqhpeyet
      241 wragihgknn vscidchmpk iqnaegkvyt dhqirnpfds fettcvncht qdkktlqdiv
      301 aerkasiqel klnvekqlvh ahyeakaawd agateqemkp ilqdirhaqw rwdyaiashg
      361 ihmhapdvgl rvlggalnka adartklarl latkgishei plpdistkln aqkalgmdmd
      421 klnsekqefl qqvvpawdeq akkagrlsq
//
LOCUS       WP_113796574             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus sp. TF02-8].
ACCESSION   WP_113796574
VERSION     WP_113796574.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus sp. TF02-8
  ORGANISM  Blastococcus sp. TF02-8
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Blastococcus sp. TF02-8"
                     /db_xref="taxon:2250574"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53589
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mhigvpretr aretrvaatp atveklvglg ydvvvesgag aassfpdday aaagarvgta
       61 eeawgadvvl rvnapaveel prlrdgatli gllspafnpe lvealaqrpi talamdavpr
      121 israqsmdvl ssmaniagyr avveaahvfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvavpageqe asadgyarem gedfnrraae
      241 myaeqagdvd iiittalipg kpaprlitee mvasmrsgsv ivdmaaaqgg nvtgsvpdev
      301 vvtdngvsii gytdlparlp aqasqlygtn lvnllklltp ekdgrlvldl edvvqrsitv
      361 vhegektwpp ppvqvsaapa paaappaake papppepprp grrfalvgvg aavlflvtal
      421 spdeliqhlt vfalavvigf yvighvhhal htplmsvtna isgiivvgal lqighddavv
      481 talafvaill asinvfggfa vtrrmlamft rgpgqkgaar
//
LOCUS       WP_113811939             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus sp. TBT05-19].
ACCESSION   WP_113811939
VERSION     WP_113811939.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus sp. TBT05-19
  ORGANISM  Blastococcus sp. TBT05-19
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Blastococcus sp. TBT05-19"
                     /db_xref="taxon:2250581"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53565
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mhlgvpretr aretrvaatp ttvqklvalg yevvvetgag aassfpdeay aeagarvgsa
       61 eeawqadvvl rvnapaaeel prlrdgatli gllapafnpd lvealaqrpv talsmdavpr
      121 israqsmdvl ssmaniagyr avveaahvfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvavpageqe vssdgyarem gedfnrraae
      241 myaeqardvd ivittalipg rpaprlitee mvasmrsgsv ivdmaaaqgg nvagsvpdei
      301 vvtgngvsii gytdlparlp aqasqlygqn lvslltlltp gkdgrlvldl ddvvqraitv
      361 vrdgektwpp ppvqvsaapa paqppavkep apppepprpg rqlavvglga allflvaals
      421 pdelvghftv falavvvgfy vigkvhhalh tplmsvtnai sgiivvgail qlgsddavvr
      481 tlafvatlla sinvfggfav trrmlgmfsr gpsaevaar
//
LOCUS       WP_113817836             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychromonas sp. B3M02].
ACCESSION   WP_113817836
VERSION     WP_113817836.1
KEYWORDS    RefSeq.
SOURCE      Psychromonas sp. B3M02
  ORGANISM  Psychromonas sp. B3M02
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Psychromonadaceae; Psychromonas.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Psychromonas sp. B3M02"
                     /db_xref="taxon:2267226"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54326
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipreiq enenrvaatp stvallikqg ftflveqnag saasfsdssy qeagaeiste
       61 aeailqsdii fkvnaptqae iqlikegatl vsfiwpaqnp ellkqleakn isviamdsvp
      121 rtsraqalda lssmaniagy ravieaanqf grfftgqita agkvppakvl ivgagvagla
      181 algaagslga ivrafdtrpe vkeqiesmgg eflevdyvee tevsttgyak tmsegyqkaq
      241 aemmaeqakd vdiiittali pgkpapkiis edmiksmkpg svivdlaaaa ggnaaltvkd
      301 evfetengvk iigytdlpsr lptqssqlya tnlvnlmkll cknkdgqidi dfedevirga
      361 tvvkegeisw pppainvsaa ptpkaeekve evveekepnk wikpaaavva aglfgwlasv
      421 aptdflahft vfilacivgy gvvwnvahsl htplmsvtna isgiiiigal lqvgsdnnvv
      481 talstiaili atinivggft vthrmlkmfq kdk
//
LOCUS       WP_113824890             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Roseobacteraceae].
ACCESSION   WP_113824890
VERSION     WP_113824890.1
KEYWORDS    RefSeq.
SOURCE      Roseobacteraceae
  ORGANISM  Roseobacteraceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Roseobacteraceae"
                     /db_xref="taxon:2854170"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55092
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif dgearvamtp dsalqlqklg ydcaiesgag aaagfsdaly eaagvevvkt
       61 aadlwatadi iakvrqpdan elehltdakt lisffnpaan tegmdaakak ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtadmvaam kpgsviidla aekggncklt
      301 vmdekivten gvtivgytdf psrmaaqass lystnirhmm tdltpekdgq inhdmeddvi
      361 rgatvthkge itfpppppkv aaiaakpket vpeltpeekr aaevaafkaq tknqvtllav
      421 ggallllvgl vapasfmqhf ivfvlavfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsvf mtginifggf lvtrrmlamf qks
//
LOCUS       WP_113830412             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus sp. TF02A-30].
ACCESSION   WP_113830412
VERSION     WP_113830412.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus sp. TF02A-30
  ORGANISM  Blastococcus sp. TF02A-30
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Blastococcus sp. TF02A-30"
                     /db_xref="taxon:2250580"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52873
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipretr aretrvaatp ttvaqlvglg yevvveggag eassfpdeay aaagartcsa
       61 geawgadvvl rvnapaveei grlrdgatli sligpalnpe lvdalaarpi tvlamdavpr
      121 israqsldvl ssmaniagyr avveaahvfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvavpageqe vsadgyarem gedfnrraae
      241 myaeqardvd iiittalipg rpaprlitee mlasmrsgsv ivdmaaaqgg nvagsvpdei
      301 vvtpngvsii gytdlparlp aqasqlygtn lvnllklltp gkdgllvldf ddvvqramtv
      361 vregektwpp ppvqvsaapa paapaprepa pppeppkpgr rfalvgaaaa vlfllagfap
      421 nelvqhltvf alavvvgfyv ighvhhalht plmsvtnais giivvgallq ighddavvtt
      481 lafvailvas invfggfavt rrmlgmftrg par
//
LOCUS       WP_113832360             531 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus sp. TF02-09].
ACCESSION   WP_113832360
VERSION     WP_113832360.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus sp. TF02-09
  ORGANISM  Blastococcus sp. TF02-09
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Blastococcus sp. TF02-09"
                     /db_xref="taxon:2250576"
     Protein         1..531
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54474
     Region          8..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 migatlhigv pretrpretr vaatpttvgq lvalgydvvv etgaggpssf pdeaytgaga
       61 rigtadeawq advvlrvnap sveeigrlrd gatliglisp afnpelveal aarpitvlam
      121 davprisraq sldvlssman iagyravvea ahvfgrfftg qvtaagkvpp akvlvagagv
      181 aglaaigaas slgaivratd vrpevaeqvr slggeyvavp ageqevssdg yaremgedfn
      241 rraaemyaeq ardvdiiitt alipgrpapr liteemvasm rsgsvivdma aaqggnvags
      301 vpdevvvtpn gvsiigytdl parlpaqasq lygtnlvnll klltpgkdge lvldmddvvq
      361 rsmtvvhdga ktwppppvqv saatapaaaa paakepappp eppkpgrrla lvglgaallf
      421 llagfspsel vqhltvfala vvvgfyvisg vhhalhtplm svtnaisgii vvgallqigh
      481 ddalvtalaf vailvasinv fggfavtrrm lgmftrgpst avrpstgsaa r
//
LOCUS       WP_113837855             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus sp. TF02A-26].
ACCESSION   WP_113837855
VERSION     WP_113837855.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus sp. TF02A-26
  ORGANISM  Blastococcus sp. TF02A-26
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Blastococcus sp. TF02A-26"
                     /db_xref="taxon:2250577"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52704
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvprets pgetrvaatp ttvraliglg hevvvesgag agashpdeay aeagarigta
       61 aeawgaglvl hvakpareel drladgavlv sllapafdae lvaalaarpi talamdavpr
      121 israqsldvl ssmaniagyr avieaahafg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdvrpev adqiaslgge yvgvpaddag epgggtgyas vtsedynara
      241 avmyaeqard vdivittali pgraaprllt aemvasmkpg svivdmaaaq ggnvegsvad
      301 qvvttangvt iigytdlpgr lpaqasqlyg tnlvnlvkll tpgkdgqlvl dlddvviram
      361 tvakdgevlw ppppvavsaa pstpappppa alpkpeqpam tagrrsalvg laaallflat
      421 afapnqlvgn ltvfalsvvi gfyvighvhh alhtplmsvt naisgiivvg allqlghvsg
      481 vvtvlaflav llasinvfgg favtrrmlgm fsrgparsta gsar
//
LOCUS       WP_113846515             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_113846515
VERSION     WP_113846515.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34890
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel vsymlhltat
      301 nlr
//
LOCUS       WP_113861660             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter pelagius].
ACCESSION   WP_113861660
VERSION     WP_113861660.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter pelagius
  ORGANISM  Marinobacter pelagius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter pelagius"
                     /db_xref="taxon:379482"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55814
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipreif qderrvaatp psvhkliglg ydviveggag eaanysdaay ekvgaaiaad
       61 tsslwkesdf ilkvrapmen palgkheadl mkdgaflvsy iwpaqnpdll eklaarkits
      121 faidslpris raqkmdalsa maniagyrav ieaanhfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig aansmgaivr afdtrlevke qvesmgaefl vldfenedgs gsggyakqms
      241 defikaemel faeqakevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgtva hhhgvtligy tdlpsrmakv aselyatnlv hllteltpek dgkpvvnmed
      361 evirgltvvh edditwpppk pespvspkpa pgteepsaea kaaakkdadr rsligkgvll
      421 vvtalalygv gahapesflq hftvfvlacf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gailhlaqae niavgimafv avliasinvg ggfrvthrml kmfrk
//
LOCUS       WP_113879529             385 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Marinobacter].
ACCESSION   WP_113879529
VERSION     WP_113879529.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter
  ORGANISM  Marinobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Marinobacter"
                     /db_xref="taxon:2742"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40947
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mmigiprerq dgenrvaiip sgvstlleag yevvvesgag saahftdddy rhagaiiadn
       61 adalyrqatv ilkvrapsse earliqqdat liclldpwfn qplleqlagq nvqafaldlv
      121 prttraqsmd vlsamagisg yravlsgama lpryfpmlmt aagtihparv lvigagvagl
      181 maiatarrlg avveaydlrp evkeqveslg adfieievpa sdttgdsgya kaqseafyta
      241 qrqqladcva radlvittaa vpgkpapkli dqemihrmks gsvivdlaad kggnvegtvl
      301 nqkvdvdgvt lvghanhpsr vpvhasqllt rnitafllnm tedgrvvpkl edeivaatlv
      361 vqhgsvrhna etrdtpqtst qkdtd
//
LOCUS       WP_113889867             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Roseiarcus
            fermentans].
ACCESSION   WP_113889867
VERSION     WP_113889867.1
KEYWORDS    RefSeq.
SOURCE      Roseiarcus fermentans
  ORGANISM  Roseiarcus fermentans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Roseiarcaceae; Roseiarcus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Roseiarcus fermentans"
                     /db_xref="taxon:1473586"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38551
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,289,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvaaetd paetrvaatp etvkkfiglg aevavaqgag vkagvpdaef qaagarivsn
       61 aealgadvvl kvrrpdaaet aalksgalvi avmdpyghtd avealagsga safamelmpr
      121 itraqvmdvl ssqanlagyr avidaaaeyg ralpmmmtpa gtvpaarmfi mgvgvaglqa
      181 iatgrrlgai vtatdvrpat keqveslgak fvavedeefk qaetaggyak emsdaykakq
      241 aaliathiak qdivvttali pgrpaprlvt admvrsmrpg svlvdlaver ggnvemakag
      301 evvttengvk ivgssnvtrl aatasalyar nlfafvetli dkankalavn wddelvkatc
      361 ltrggaivhp aflpk
//
LOCUS       WP_113913421             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseovarius dicentrarchi].
ACCESSION   WP_113913421
VERSION     WP_113913421.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius dicentrarchi
  ORGANISM  Roseovarius dicentrarchi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Roseovarius dicentrarchi"
                     /db_xref="taxon:2250573"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54798
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkear egearvamtp dsavqlqklg ydcaieagag aragfmdady aaagvelvet
       61 aqalwsgsdi iakvrppsta elghlkdgqt litffdpgtn dagmeaaras gasviamemv
      121 prisraqkmd alssmaniag yravieassn fgrfftgqit aagkmpparv lvigagvagl
      181 aaigtstslg avtlafdlrp evaeqvesmg aefvyldfde aqdgaatggy asvsspefre
      241 aqlakfrela pdvdivitta lipnrdapel wtedmvkamk pgsvivdlaa ekggnckltv
      301 kdekivteng vtiigytdfp srmaaqassl yatnirhmls dltpekdgqi vhdmeddvir
      361 gatvvhagei typppppkvq aiaakpkqta paptaeekka qevalfrkqt ksqvtllavs
      421 aavmvligaf apasfmshli vfvlacfigf sviwnvshsl htplmavtna isgiiilgal
      481 lqigsgswlv vllaavsvfi asinivggfl vtrrmlamfq ks
//
LOCUS       WP_113924365             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cognataquiflexum aquatile].
ACCESSION   WP_113924365
VERSION     WP_113924365.1
KEYWORDS    RefSeq.
SOURCE      Cognataquiflexum aquatile
  ORGANISM  Cognataquiflexum aquatile
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Cognataquiflexum.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Cognataquiflexum aquatile"
                     /db_xref="taxon:2249427"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40124
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigilkepq desrvallpe avktllswkv svwvethaga rayasdelyk eagaeihsrq
       61 eivtqsdlvi giqpisqsei sglkpeavlm gqmgalfnpe ltkyliqqkk tafsmelvpr
      121 ttraqsmdvl ssmatvtgyk avlmaanllp rffpmfmtaa gsitparvli lgagvaglqa
      181 iatsrrlgas vfafdvrqaa keevlslgak fvdvegaked kgaggyaveq tpeyiqkqkd
      241 tihehatkad iiittaqipg rkapqlveer tvramkpgsv iidlaassgg ncalsqpdqt
      301 vevngvrivg vgnlassmpq daskmygkny lnflkliikd gnlnlnfedd ivtgtcvcha
      361 gnpispriiq mqnn
//
LOCUS       WP_113935253             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Eoetvoesiella caeni].
ACCESSION   WP_113935253
VERSION     WP_113935253.1
KEYWORDS    RefSeq.
SOURCE      Eoetvoesiella caeni
  ORGANISM  Eoetvoesiella caeni
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Eoetvoesiella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Eoetvoesiella caeni"
                     /db_xref="taxon:645616"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38586
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipresl qgetrvaatp etvkkyisak hqvvvetgag aaahypdday vaagatlgta
       61 eqalsaalvl kvrtpsagel tsmkpgsvlv gmldpfnpeg lqslataglt afaleaapri
      121 traqsldvls sqanlagyka vllaanqygr lfpmmmtaag tlkaarvvvl gagvaglqai
      181 atakrlgavv easdvrpaak eqieslgakf idvpfetdee reiaqgvggy arpmpaawma
      241 rqaalvserc kqadiiitta lipgrpaptl vseetvqamk pgsvivdlav erggncplse
      301 kdkvvvkhgv sligytnlpa mvatdasaly arnvldflkl itdaegqlai qredeivaac
      361 lmssdgnllr sa
//
LOCUS       WP_113939112             467 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Shewanella].
ACCESSION   WP_113939112
VERSION     WP_113939112.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52130
     Region          1..467
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mmkkmtgksf alsalvaasf maagamasdk teprnevykd kfknqynswh dtakseelvd
       61 aigqdpnmvi lwagyafakd ynaprghmya vtdvrntlrt gapknaedgp lpmacwscks
      121 pdvprlieeq gedgyfkgkw akggpevtnt igcgdchekg spklrisrpy vdramdaigt
      181 pfdkaskkdk qsmvcgqchv eyyfekkedk kgfvkfpwdm gitvdqmevy ydgiefsdwt
      241 halsktpmlk aqhpeyetwk lgihgknnvs cvdchmpkvt spegkkftdh kvgnpfdrfe
      301 etcatchsqt keflvgvtne rkakvkemkl kaeeqlvkah feaakawelg ateaemkpil
      361 tdirhaqwrw dlaiashgva ahapeealrv lgtsvnkaad arvklaqlla kkgitdpiai
      421 pdistkakaq aalgmdmdkm naekeafkkd mlpkwdeeak kreatyk
//
LOCUS       WP_113945124             441 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudochrobactrum asaccharolyticum].
ACCESSION   WP_113945124
VERSION     WP_113945124.1
KEYWORDS    RefSeq.
SOURCE      Pseudochrobactrum asaccharolyticum
  ORGANISM  Pseudochrobactrum asaccharolyticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Pseudochrobactrum.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Pseudochrobactrum asaccharolyticum"
                     /db_xref="taxon:354351"
     Protein         1..441
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45960
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msqvifipve tdpvetrvaa tpetvkklis ygfkiivesa agtqsritdq ayaeagatig
       61 kttdiktadi ilklrrpsqt elknykigav liamldpygh edsvaaiaqa gltaftmefm
      121 pritraqvmd vlssqanlag yqavidaase ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfvavedee fkaaetaggy akemskdyqa
      241 kqaalvadhi akqdivitta lipgraapkl vsaamvasmk pgsvlvdlav erggnvegav
      301 agqvttkdgv kivghmntag riaasasqly arnlfaflet lidketkqvv inledelvka
      361 talthqgaiv hpafanvavv aekaepvkka eaaakpapkk apvkkaapkk pvtaketakp
      421 avkttvrkkt gteagnkgde a
//
LOCUS       WP_113946092             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudochrobactrum asaccharolyticum].
ACCESSION   WP_113946092
VERSION     WP_113946092.1
KEYWORDS    RefSeq.
SOURCE      Pseudochrobactrum asaccharolyticum
  ORGANISM  Pseudochrobactrum asaccharolyticum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Pseudochrobactrum.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Pseudochrobactrum asaccharolyticum"
                     /db_xref="taxon:354351"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55374
     Region          1..527
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigtlkeny pgesrvamtp esaiqlmklg hacaieagag lsagisdday lavgvkvleg
       61 atalaatsdv ivkvrqptka evdllssdkt lisffypgqn aellelakek ganviamdmv
      121 prisraqkmd vlssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigvatslg aqtyafdvrp evaeqiesmg aefvyldfad geggghqdga atggyaapss
      241 pefrekqlak frelapqidi vittalipgr dapklwladm vaamkpgsvi vdlaaerggn
      301 cdltvadqri vsdngviiig ytdfpsrmaa qastlyatni rhmltdltpg kdgklvhnme
      361 ddvirgatvt fegaityppp ppkiaaiaaq kpkekvkept peerrateaa afkaqtksql
      421 tllaigtall llvgafappa fmshfvvfvl acfvgfqviw nvshslhtpl mavtnavsgi
      481 vilgallqig sgnwlvvlla alsvliatin ivggflvtrr mlamfqks
//
LOCUS       WP_113952735             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Arenicella
            xantha].
ACCESSION   WP_113952735
VERSION     WP_113952735.1
KEYWORDS    RefSeq.
SOURCE      Arenicella xantha
  ORGANISM  Arenicella xantha
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Arenicellales; Arenicellaceae; Arenicella.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Arenicella xantha"
                     /db_xref="taxon:644221"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53874
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miisipkesy kgekrvaltp esalqiqklg htlrieagag knaefsdady kdagvdvvts
       61 daiwsdtdii mkvrgvtsae adkvaagttl isffwpaqne ellkqladak vnviamdcvp
      121 rlsrsqkmda lssmaniggy raiveaanqf grfftgqvta agkvppakvl vigagvagla
      181 aigaaksmga ivrafdtrle akeqveslgg eflvlefeed gsgdggyakt mskefidaem
      241 amfreqakev diiittalip grpapelitk dmvesmksgs vivdlaaeqg gncklskadk
      301 ivthkgvkii gytdlpsrla tqssqlystn lrhmltdltp dkdgkvlinm ddavirgata
      361 ahdgkvtwpa papalsaapk aapkpvampe papelsaask akmtfgamgl gllallgvgs
      421 vappdfmshf tvfilacfig yqviwsvtps lhtplmsvtn aisgiivvga llqissgsgl
      481 vvflafvatl iasiniaggf lvtqrmlkmf nkg
//
LOCUS       WP_113995750             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas hydrophila].
ACCESSION   WP_113995750
VERSION     WP_113995750.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas hydrophila
  ORGANISM  Aeromonas hydrophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas hydrophila"
                     /db_xref="taxon:644"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53401
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tclgtsgwaq aadeaqskgk iearselfak dhadqftswk
       61 gtsesrertd aladdpqmvv lwagypfskd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meqyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg vvkqrkdavt eiklkvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakgish eiaipdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_114010044             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cohaesibacter intestini].
ACCESSION   WP_114010044
VERSION     WP_114010044.1
KEYWORDS    RefSeq.
SOURCE      Cohaesibacter intestini
  ORGANISM  Cohaesibacter intestini
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Cohaesibacteraceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cohaesibacter intestini"
                     /db_xref="taxon:2211145"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55739
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtprelf egearvamtp ssakllqklg ydcvleagag alagfsdqay veagveivad
       61 aqalwqtadi vakvrqpepa elkyllkgkt lisffnpagn eegmeaakta eanviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv livgagvagl
      181 aaigtsvalg avtyafdvrp evaeqvesmg aefvyldfee eqqdgsstgg yasvqseefr
      241 naqlakfrei asdmdivitt alipnrpapk lwledmvaam kpgsviidla aerggnvegt
      301 vkdekivtdn gvtivgytdf psrmaaqsse lyasnirhmm tdltpekdgq vvhnmeddvi
      361 rgatvtfegd itfpppppki aaiaaqpkke vkeltpeekr aaeieafkqq tksqikllag
      421 ggllmlfiga fapasfmqhf ivfvlacfvg fqviwnvshs lhtplmaitn aissiiilga
      481 lmqigsgssl vivlaalsif maginifggf lvtrrmlamf qks
//
LOCUS       WP_114045213             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acidipropionibacterium virtanenii].
ACCESSION   WP_114045213
VERSION     WP_114045213.1
KEYWORDS    RefSeq.
SOURCE      Acidipropionibacterium virtanenii
  ORGANISM  Acidipropionibacterium virtanenii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Acidipropionibacterium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Acidipropionibacterium virtanenii"
                     /db_xref="taxon:2057246"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53162
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mmigipresa agenrvaatp stvprllklg yevvveqgag agasfpdqay qdagaqlgda
       61 arawgadlvl avnppsdgei aamrpgaalv tflaprqden ltrklasagv tgmsmdmvpr
      121 israqsmdal ssmanisgyr avveaafayg rtfggqvtaa gkvppakvfv igtgvaglaa
      181 lgaansmgae vfatdvrpet aeqvesmgar flhvrtsdad qgvssdgyak etsddyntra
      241 aelymeqart cdvvittaai pgrpspklit aemvaamrpg svivdlaalg ggncvlthpg
      301 ekyvtdggvt iigytdlpsr lpgqssqlyg tnlvnlvtla tpakdgqlvi dfedevirqa
      361 tvsrdgevtf ppppvqvaaa papvkkaaae pvlaakkepr pwpqtfamig vlavaliall
      421 tfapssflgl fgtfavavvv gyyvvwnvsh alhtplmsvt navsgiimvg aitqlgsgsl
      481 viqiiaaitv liasinvfgg ftvtqrmlkm frka
//
LOCUS       WP_114047433             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_114047433
VERSION     WP_114047433.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53582
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgv hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_114049113             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_114049113
VERSION     WP_114049113.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36165
     Region          6..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfkpyslr hsdllyedip leireqiivl iintlgscss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldeisnlll kiddkrkhid aielafkyid tylrtyevtl
      121 glepdkaise lnnifhdhdl kyryengriv rlrrikrlkn iryylyspge ygfveydlme
      181 aynrlmlndf arvvsechav frrvlirihe rkgivyheqd slntlmanlm trgvisaeye
      241 rkfhflsnvl eseifppiaq ekshhhyvmm lriseelacs iyyltersif fltqraeedd
      301 vvt
//
LOCUS       WP_114061061             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chromobacterium phragmitis].
ACCESSION   WP_114061061
VERSION     WP_114061061.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium phragmitis
  ORGANISM  Chromobacterium phragmitis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Chromobacterium phragmitis"
                     /db_xref="taxon:2202141"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40300
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhivipaerl agehrvaatp dtvkklvaag havtvergag laaalpdaay laagaaiaeq
       61 rqpmlaaadt vlavrmpdag diaalkpgaa lvgmlapyqn ellpqlaeqk vsafalellp
      121 rttraqsmdv lssqnniagy kavllacqyy prfmpmlmta agtvkaarvl vlgvgvaglq
      181 aiatakrlga vveaydvrpa treqveslga kfvevpmsde ekaandgvya remtpefqtr
      241 qnaliaqraa vadivittal ipgkpaprll sadavadmkh gsvivdlaae aggncaltra
      301 geaclspngv hvvgllnlpa mlaadassly arnlhtflgl llapeglkid ldddlvaatl
      361 ithqgerrfg aaarpaapaa qhdkepqhg
//
LOCUS       WP_114064387             303 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Salmonella].
ACCESSION   WP_114064387
VERSION     WP_114064387.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35887
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechav frsvllrihe rkgiayheqd slntlmanlm argvisaeya
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vap
//
LOCUS       WP_114070244             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Runella
            rosea].
ACCESSION   WP_114070244
VERSION     WP_114070244.1
KEYWORDS    RefSeq.
SOURCE      Runella rosea
  ORGANISM  Runella rosea
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Runella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Runella rosea"
                     /db_xref="taxon:2259595"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39747
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiailketk aferrvaitp divksllkag ftcaiqsgag enssllnady ekagatvaad
       61 tqtlladadv vlkvnaptld evaqmregai sisflyaytq pelvkalnak kisafsmdav
      121 prttkaqsmd alssqanlag ykavllgana lgkifplmmt aagtikpskv lifgagvagl
      181 qaiatakrlg avvevsdvrp etkeqveslg gkflsvegme ankseggyak evsaeflqkq
      241 qdlikqrikd adivittalv mgkkapilvt eemvqsmktg svivdmaves ggncalsean
      301 qtvvkngvti igesnlpall stnasdlyak nistlllhla nkdgfkwele eeitkgslit
      361 hqgtsvhaft kgilekk
//
LOCUS       WP_114073562             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chromobacterium phragmitis].
ACCESSION   WP_114073562
VERSION     WP_114073562.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium phragmitis
  ORGANISM  Chromobacterium phragmitis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Chromobacterium.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Chromobacterium phragmitis"
                     /db_xref="taxon:2202141"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40270
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhivipaerl agehrvaatp dtvkklvaag havtvergag laaalpdaay laagaaiaeq
       61 rqpmlaaada vlavrmpdag diaalkpgaa lvgmlapyqn ellpqlaeqk vsafalellp
      121 rttraqsmdv lssqnniagy kavllacqyy prfmpmlmta agtvkaarvl vlgvgvaglq
      181 aiatakrlga vveaydvrpa treqveslga kfvevpmsde ekaandgvya remtpefqtr
      241 qnaliaqraa vadivittal ipgkpaprll sadavadmkh gsvivdlaae aggncaltra
      301 geaclspngv hvvgllnlpa mlaadassly arnlhtflgl llapeglkid ldddlvaatl
      361 ithqgerrfg aaarpaapaa qhdkepqhg
//
LOCUS       WP_114076713             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            suum].
ACCESSION   WP_114076713
VERSION     WP_114076713.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus suum
  ORGANISM  Paracoccus suum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus suum"
                     /db_xref="taxon:2259340"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54785
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkvgalreva egearvavtp ssaahlkklg hevlveqgag sragfsddey raagvevlpt
       61 aaalteavdv lakvraptda elnrmhegqt lisyitpasn pelleaarar gvttiamdmv
      121 prisraqkmd alssmaniag yravieaaan fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aqvyafdvrp evaeqiesmg asfvyldfag aaqdgaatgg yaapsspefq
      241 akqlekfrel apqmdivitt alipgrpapk lwtadmvaam kpgsvivdla aerggncelt
      301 vadekivten gvtiigytdf psrmgaqase lyannirhfl sdltpakdgv inqnmdddvi
      361 rgatvthagd vtfpppppkv qaiavqkpkd kpkeltaaek raaeitafka qtrsqvtlia
      421 igavlmllvg ltapasflsh fivfvlavfi gfqviwnvsh slhtplmait naissiiilg
      481 almqigsgsa lvvilaalsv lmaginifgg flvtrrmlam fqks
//
LOCUS       WP_114081013             388 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Nostoc].
ACCESSION   WP_114081013
VERSION     WP_114081013.1
KEYWORDS    RefSeq.
SOURCE      unclassified Nostoc
  ORGANISM  unclassified Nostoc
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="unclassified Nostoc"
                     /db_xref="taxon:2593658"
     Protein         1..388
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41094
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dtvarlvkqg levwvekgag ersffsdtdy eaagatiigd
       61 taklwgetdi llkvsppqer edgrsevdll kegavllsfl nplgnpvvaq qlanrkital
      121 smemiprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkldeetvaa ggyakeisea
      241 skqrtqevva ehiknsdvvi ttaqvpgrqa prlvteemva qmkpgsvivd laaeqggnca
      301 ctepgkdivw ngvtiigpin lpssmpihas qlyaknvtsl mqllikdkal qvdfsddivd
      361 aacvthagei rnqrvrdalq alsgvgag
//
LOCUS       WP_114087811             392 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassospira profundimaris].
ACCESSION   WP_114087811
VERSION     WP_114087811.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..392
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41190
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,98,295,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,285..286,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpreiw pgekrvaitp dtvkkytglg fevviesgag ehasiaddry veagatiakt
       61 akaatgdadv ilkvrppmve gktnelaayk kgatviglie pydraeligk maeagltsfa
      121 melvprisra qsmdvlssqs nlagyravid aahefgrifp mmmtaagtla ptrivvvgag
      181 vaglqaiata krlgavvsaf dvrpavkeqv qslggtfiev edddaasaet aggyaremsd
      241 dykkkqaakl kevlaktdiv ittalipgrp apeivtadmv agmkngsiil dlaaerggnv
      301 agvkpgestm tengvkimgp snivssvaad atamyaknll nfvtlmvdge kkemvfnred
      361 qiiaetmltr dgkmvhpkfg geadketeae ng
//
LOCUS       WP_114092269             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            harveyi].
ACCESSION   WP_114092269
VERSION     WP_114092269.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54575
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvaiesqag vlasfddaay eaagakivss
       61 eevwtsglil kvnaplvdee kgideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgrpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqvitta ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvvkeg evtwpappiq vsaqpqakpq epvkpqpkve eptspvkkfg alalgvgafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_114094842             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassospira xiamenensis].
ACCESSION   WP_114094842
VERSION     WP_114094842.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40191
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,98,294,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,284..285,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpkeiw pgerrvavtp dtvkkliglg fdvaieagag inaaipddrf adagatiakt
       61 mkttvkdadv ilkvrppvvd gktdelaayk kgaavialld pydrkdliek maaagvssfa
      121 melmprisra qsmdvlssqs nlagyravld aahefgriyp mmmtaagtlp parvvivgag
      181 vaglqaiata krlgavvsaf dvrpavkeqv qslggtfiev eddaadgeta ggyakemsde
      241 ykakqaaklk evlaktdivi ttalipgrpa peivtadmva gmkpgsviid laaerggnva
      301 gaklgetvvt dngvkiigpe nitssvatda tamyaknlln fitlsvdkek gtlafnaedq
      361 iiaetmltrd gkvvhpkfgg eevang
//
LOCUS       WP_114099169             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassospira profundimaris].
ACCESSION   WP_114099169
VERSION     WP_114099169.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira profundimaris
  ORGANISM  Thalassospira profundimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Thalassospira profundimaris"
                     /db_xref="taxon:502049"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40470
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,98,295,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,285..286,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpkeiw pgekrvavtp etvkklkslg fdvaieagag idaaipddrf vdagatiakt
       61 mktavkdadv ifkvrppvid gktneltayk kgaavvalle pydrkeliea maqagvdgys
      121 melmprisra qsmdvlssqs nlagyravld aahefgriyp mmmtaagtla parvvvvgag
      181 vaglqaiata krlgavvsaf dvrpavkeqv qslggtfiev eddsasdaet sggyakemsd
      241 dykkkqaakl kevlaktdiv ittalipgrp apeivtadmv agmkpgsvii dlaaerggnv
      301 agvklgetvm tengvkligp anitssvatd atamyaknll nfitlsvdkd kgalvfnged
      361 qiiaetrlth dgkvvhpkfg geevang
//
LOCUS       WP_114101528             387 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Thalassospira].
ACCESSION   WP_114101528
VERSION     WP_114101528.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira
  ORGANISM  Thalassospira
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Thalassospira"
                     /db_xref="taxon:168934"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40483
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,98,295,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,285..286,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,235,246,
                     263..265,272,274)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpkeiw pgekrvavtp etvkklkslg fdvaieagag idaaipddrf vdagativkt
       61 mkatvkdadv ifkvrppvid gktneltayk kgaavvalle pydrkdlina maaagvdgys
      121 melmprisra qsmdvlssqs nlagyravld aahefgriyp mmmtaagtla parvvivgag
      181 vaglqaiata krlgavvsaf dvrpavkeqv qslggtfiev eddnasdaet sggyakemsd
      241 dykkkqadkl kevlaksdiv ittalipgrp apeivtadmv agmkpgsvii dlaaerggnv
      301 agvklgetvm tengvkligp anitssvatd atamyaknll nfitlsvdkd kgalvfnged
      361 qiiaetrlth dgkvvhpkfg geevang
//
LOCUS       WP_114105257             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Hyphomonas
            sp. CACIAM 19H1].
ACCESSION   WP_114105257
VERSION     WP_114105257.1
KEYWORDS    RefSeq.
SOURCE      Hyphomonas sp. CACIAM 19H1
  ORGANISM  Hyphomonas sp. CACIAM 19H1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomonadales; Hyphomonadaceae; Hyphomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Hyphomonas sp. CACIAM 19H1"
                     /db_xref="taxon:1873716"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38488
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkisvlkerr pgetrvaatp etvkkliglg htvtveggag tvagfldaaf teagasiags
       61 aaeaakgadi vfkvrrpepg eigalpdgaa lialmepfay paeelaalna kkiaalsmef
      121 tpritraqsm dalssqsnla gyraviegaq iygrampmmm taagtvapak vfimgagvag
      181 lqaiatarrl gavvtandvr paakeqvasl gakfiavedd efkaaetsgg yakemspeyq
      241 akqaaltash iakqdivvtt alipgrpapv liteemvrsm kpgsvivdma vsqggncpls
      301 kadeivdvgg vkvagfsnlp arlpadassl yaknllaflp litaeggalt ldtedevvva
      361 mlltrngatv serlk
//
LOCUS       WP_114111826             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassospira xiamenensis].
ACCESSION   WP_114111826
VERSION     WP_114111826.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xiamenensis
  ORGANISM  Thalassospira xiamenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Thalassospira xiamenensis"
                     /db_xref="taxon:220697"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40107
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,98,294,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,284..285,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpkeiw pgekrvavtp dtvkkliglg fdvaieagag tdaaipddrf adagatiakt
       61 mkttvkdadv ilkvrppvvd gktdelaayk kgaavialld pydrkdliek maaagvssfa
      121 melmprisra qsmdvlssqs nlagyravld aahefgriyp mmmtaagtlp parivvvgag
      181 vaglqaiata krlgavvsaf dvrpavkeqv qslggtfiev eddaadgeta ggyakemsde
      241 ykakqaaklk evlaktdivi ttalipgrpa peivtadmva gmkpgsviid laaerggnva
      301 gaklgetvvt angvkiigpe nitssvatda tamyaknlln fitlsvdkek gtlafnaedq
      361 iiaetmltrd gkvvhpkfgg eevang
//
LOCUS       WP_114115453             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Thioglobus sp. NP1].
ACCESSION   WP_114115453
VERSION     WP_114115453.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Thioglobus sp. NP1
  ORGANISM  Candidatus Thioglobus sp. NP1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Candidatus Pseudothioglobaceae; Candidatus Thioglobus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Candidatus Thioglobus sp. NP1"
                     /db_xref="taxon:2508687"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55788
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkeis tgelrvaltp dsavqlqklg hecliekgag qaagfndeqy kavgveistn
       61 aadlseasdv ivkvsppnkv eieklssskt lisffypgan eelmelaksr kanviamdmv
      121 prisraqkmd alssmanisg yravieasnn fgrfftgqmt aagkvppaki lvvgagvagl
      181 aaigastslg aityafdvrp evaeqvesmg akfiflnfad devdssstgg yaavsspeft
      241 aaqlakflei apemdivitt alipnheape lwtkdmvesm ktgsviidla aekggncklt
      301 vvderivtdn gviiigytdy psrmaaqasm lyasnirhmi tdltpekdgv imhdmeddvi
      361 rgatvvhsge itypppppkv qaiatppker ipektteeir adeisafkkq tktqvillav
      421 ggalmflvgs yapasfmqhf ivfilavfvg fqviwnvshs lhtplmavtn aissiiilga
      481 ilqisstssl vvilagisvf faginifggf lvtrrmlamf qks
//
LOCUS       WP_114123546             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassospira xianhensis].
ACCESSION   WP_114123546
VERSION     WP_114123546.1
KEYWORDS    RefSeq.
SOURCE      Thalassospira xianhensis
  ORGANISM  Thalassospira xianhensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Thalassospiraceae; Thalassospira.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Thalassospira xianhensis"
                     /db_xref="taxon:478503"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40175
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,98,294,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,284..285,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavpkeiw pgekrvavtp dtvkkliglg fdvaieagag inaaipddrf adagatiakt
       61 mkttvkdadv ilkvrppvvd gktdelaayr kgaavialld pydrkdliek maaagvssfa
      121 melmprisra qsmdvlssqs nlagyravld aahefgriyp mmmtaagtlp parivvvgag
      181 vaglqaiata krlgavvsaf dvrpavkeqv qslggtfiev eddaadgeta ggyakemsde
      241 ykakqaaklk evlaktdivi ttalipgrpa peivtadmva gmkpgsviid laaerggnva
      301 gaklgetvvt angvkiigpe nitssvatda tamyaknlln fitlsvdkek gtlafnaedq
      361 iivetmltrd gkvvhpkfgg eevang
//
LOCUS       WP_114132616             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus necator].
ACCESSION   WP_114132616
VERSION     WP_114132616.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus necator (Ralstonia eutropha)
  ORGANISM  Cupriavidus necator
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Cupriavidus necator"
                     /db_xref="taxon:106590"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54109
     Region          3..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvrellk lgyqvvvetg agqeasfsda dysaagaaiv
       61 daaslwasvd vvikvrppqv hpslgveeaa llkkhatlig fvwpaqqmam lerltqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgn ggggyakems
      241 pafieaemrl faeqarevdi iittalipgr papklleagt vglmragsvv vdlaaeqggn
      301 cvltvpgeav rqhgvtiigy tdlpsrmaaq asqlygtnir hllteltpgk dgqlvvdmdd
      361 emirgatvlh qgtvtwpppp ltvaipqqqa paappplqae aepprsrtga tlialaiaaa
      421 allglgavap pafmahftvf vlaifvgyqv vwnvtaalht plmsvtnais giivvgalvq
      481 lgkpslvtav iagsavllat iniaggflvt qrmlkmfqrd
//
LOCUS       WP_114134890             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus necator].
ACCESSION   WP_114134890
VERSION     WP_114134890.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus necator (Ralstonia eutropha)
  ORGANISM  Cupriavidus necator
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus necator"
                     /db_xref="taxon:106590"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38936
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvpveth ayesrvaatp etvkkyvaqg hkvvvqagag vrasqpdsay eavgatigsa
       61 aeafgadlvl kvrapeagel aqmkqgavlv gmlnpfdaes karmaaagit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfitdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra vqadivitta lipgrkapvl lqeatvqqmk pgsvvvdlaa aqggncpltv
      301 adevvnhngv iiightnlas mvaadasaly arnvldflkl vidkdgqfvi nkdddivtac
      361 lmtrreeeal ac
//
LOCUS       WP_114150326             307 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Acinetobacter baumannii].
ACCESSION   WP_114150326
VERSION     WP_114150326.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..307
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35557
     Region          5..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 msifelfskr qkklcgevpd vyqyenipnq lriqvihivk dtigsetqsn kagevykfih
       61 ktlckeygrf fliheyltsf sedifdfllq eknhencldv ieaffkvidh fvrankrefy
      121 gtkqepddai delnirfkea gvgyqfeqge lirvdsqfih sevvkpvlql lgkdkdykgs
      181 faeflsaheh yrhgrfkecl ndslkafesl mkaihkkhsw tfnqndtskk linscltkgl
      241 iplylqnqfs svntllesgi ptirnkeggh gqghevkevp eylasyalhl tatnllflvk
      301 ceenynk
//
LOCUS       WP_114155800             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia graminis].
ACCESSION   WP_114155800
VERSION     WP_114155800.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia graminis
  ORGANISM  Paraburkholderia graminis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia graminis"
                     /db_xref="taxon:60548"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39445
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvaqg hrvtiqsgag agasfpddal aaagaeivda
       61 atafgadlvl kvqspteael pllkrgatlv gmldpfnaen aqqlatagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlq
      241 rqsalvhera kqadvvista lipgraaptl lsvetvqamk pgsvlvdlaa grgadyegrr
      301 ggncpltead kvivrhgvti vgytnlasmv padasslyar nlldflklii tkegtlnidl
      361 addivaatll trdgevarka
//
LOCUS       WP_114176135             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia pyrrocinia].
ACCESSION   WP_114176135
VERSION     WP_114176135.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39152
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiakgag iaasypdeay aaagaeltdq
       61 saafdadivl kvqaptdtel pslkrgsvlv gmlepfngeq aatlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee rdaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetaqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qvivhngvti agytnlaamv asdasalyar nlldfmkliv tkegtlnidl
      361 tddivaatll crdgevtrk
//
LOCUS       WP_114183506             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter baumannii].
ACCESSION   WP_114183506
VERSION     WP_114183506.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39766
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vaenrvaatp etvkklisag hsvviergag vkaayidsay eqvgatitdd
       61 aytgsqiilk vrapqggeiq klaanttvva mfdpyrntel dqfanqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgaiv eatdlrptak dqveslggkw ldvpmseeeq qraadaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 kvgetvvten gvkilgipni patvateasa lyarnvfnfv etlfdkeknf ainqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_114184873             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            aerophila].
ACCESSION   WP_114184873
VERSION     WP_114184873.1
KEYWORDS    RefSeq.
SOURCE      Microvirga aerophila
  ORGANISM  Microvirga aerophila
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Microvirga aerophila"
                     /db_xref="taxon:670291"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39325
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd raetrvaatp dtvkkykalg advavqagag aqagvpdqdf eaagatiaas
       61 aaealrdadv vlkvrrpaeg eltgaksgal viaimdpygq eaalkslada dvaafamelm
      121 pritraqvmd vlssqanlag yravidavae ygrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg gkfvavedee fkqaetaggy akemsaeyra
      241 kqaelvashi akqdivitta lipgrpapkl vtremvesmk pgsvivdlav erggncevaq
      301 pgqvvdhngv kivghlnvpg rlaatassly aknlyafvet lvdketktla vkwddelvka
      361 tcltrqgaiv htafqptv
//
LOCUS       WP_114188642             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            aerophila].
ACCESSION   WP_114188642
VERSION     WP_114188642.1
KEYWORDS    RefSeq.
SOURCE      Microvirga aerophila
  ORGANISM  Microvirga aerophila
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Microvirga aerophila"
                     /db_xref="taxon:670291"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55049
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalreis agesrvaltp dsalqlqklg hacvieagag ekagfsdaay taagvdvlas
       61 ahavfetvdv vvkvrapepa eaamlregqt lisffwpaqt pellefcrek gatviamdmv
      121 prisraqkmd alssmaniag yravieasnh fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aqfvflefeq aqdgaatggy aapsspefre
      241 kqlakfrela peidivitta lipgrpapkl wtqdmveamr pgsvivdlaa erggncdltv
      301 pdekvvmeng vtiigytdfp srmaaqastl yannirhmla dltpskdgvi vhnmdddvir
      361 gatvthqgai typppppkvp aiaaakpkek vteftpeekr ageaaafkaq trnqvgllva
      421 ggllialvga yapasfmahl ivfalacfvg fqviwsvshs lhtplmavtn aisgivvlga
      481 llqvgsshwl vvslaslsfl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_114202564             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Janibacter
            anophelis].
ACCESSION   WP_114202564
VERSION     WP_114202564.1
KEYWORDS    RefSeq.
SOURCE      Janibacter anophelis
  ORGANISM  Janibacter anophelis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Janibacter anophelis"
                     /db_xref="taxon:319054"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52887
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgvpkesk rgetrvaatp ktveqliklg ydvvvesgag easaypdqay vdagatlepa
       61 dqvwaadvva kvnapsdeev prlasgaila sllapalnpd kvealraqgv talamdavpr
      121 israqsldvl ssmaniagyr avvesahefg glftgqvtaa gkvppakvlv cgagvaglaa
      181 igaagslgai vrafdvrpev aeqvesmgae fleidieqev stdgyaketg edfnrkaael
      241 yaeqakdvdi iittalipgk paprliteem vasmkpgsvi vdmaagsggn vagsvaderv
      301 vtdngvriig ytdlagrlpt qasqlygtni vnllklvtpd kdgqpvldme dtvvrgmtvt
      361 kdsetlwppp pvqvsaapka paaaaapvep kpekvvdpnr kfwliggaal lfliaaafmp
      421 taflshfivf alavvigfyv ignvahalht plmsvtnais giivvgallq vtssniviqv
      481 iaaaaiffas invfggftvt nrmlnmfrkg
//
LOCUS       WP_114212514             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_114212514
VERSION     WP_114212514.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53644
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prehafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_114216198             439 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Ochrobactrum].
ACCESSION   WP_114216198
VERSION     WP_114216198.1
KEYWORDS    RefSeq.
SOURCE      unclassified Ochrobactrum
  ORGANISM  unclassified Ochrobactrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Ochrobactrum.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="unclassified Ochrobactrum"
                     /db_xref="taxon:239106"
     Protein         1..439
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45358
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke sdpnesrvaa saetvkkfia lgfdvvvekg ageksripda efaaagarig
       61 taadaktadv ilkvrrptdt elkgykpgaa lfamldpygh edavaalaka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vskemvasmr pgsvlvdlav erggnvegav
      301 agqiaevngv kivghlnvag riaasasqly arnliafvet lvdketkllk idpqdelvka
      361 tllthqggiv hpafakteaa paavaekvak pkvapkpkae kpatktaapk aaakpakktp
      421 akavktpssp kspvdggea
//
LOCUS       WP_114224860             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia hospita].
ACCESSION   WP_114224860
VERSION     WP_114224860.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia hospita
  ORGANISM  Paraburkholderia hospita
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia hospita"
                     /db_xref="taxon:169430"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39682
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligiptetr pyetrvaatp etvrkyvsqg hrvrvqsgag taasyldday aaagaelvda
       61 ptafgaeivl kvqsptdsel pllkrgavlv gmlepfkven asrlaaagit afaleaaprt
      121 traqsldvls sqaniagyka vllaadlypr fmpmlmtaag tvkaarvlil gvgvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpyetdee reaavgvggy arpmppswla
      241 rqsalvhera kqadivista lipgraaptl isvetvqamk pgtvlvdlaa grgpeyegqr
      301 ggncpltead kvvvkhgvti agytnlasmv psdasalyar nlldfmklii tkegtlnidl
      361 addivaatlv ardgevarka
//
LOCUS       WP_114230473             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_114230473
VERSION     WP_114230473.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38580
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagamigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegaggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_114256119             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. Go-475].
ACCESSION   WP_114256119
VERSION     WP_114256119.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. Go-475
  ORGANISM  Streptomyces sp. Go-475
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces sp. Go-475"
                     /db_xref="taxon:2072505"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53436
     Region          10..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mvpaepepqr igipaestag etrvaatpat vgrlaalgyd vvvepgagas srfsdeayee
       61 agarlgdpwh aeivlkvngp sreeigrlrd gatlialisp alnpelveel arrpitvlam
      121 davprisraq sldvlssman iagyravvea ahafgrfftg qvtaagkvpp akvlvagagv
      181 aglaaigaar slgavvratd prpevaeqvr slggefltvs aeqevstdgy akatsedynr
      241 laaqlyaeqa advdiiitta lipgrpaprl itaedvarmk pgsvivdmaa aqggnvegtv
      301 pgkavvtdnd vtiigytdlp grlpaqasql ygtnvvnlmk lltpgkdgrl vldfddvvqr
      361 sitvvregek twppppvqvs aapapatakn aaapapeapa kptrpawasy alvaagalal
      421 flvtafspse llghftvfvl aivigfyvig nvhhalhtpl msvtnaisgi vvvgallqig
      481 qgntavtvls faaillasin ifggfavtrr mlgmfskg
//
LOCUS       WP_114272509             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Klebsiella pneumoniae].
ACCESSION   WP_114272509
VERSION     WP_114272509.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35948
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssnv rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspggaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel asymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_114284263             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Halocynthiibacter alkanivorans].
ACCESSION   WP_114284263
VERSION     WP_114284263.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Halocynthiibacter alkanivorans
  ORGANISM  Candidatus Halocynthiibacter alkanivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Halocynthiibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Candidatus Halocynthiibacter alkanivorans"
                     /db_xref="taxon:2267619"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55510
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkeif egearvamtp dsatqlqklg ydcaietgag alagfsdaty eaagveiikt
       61 paalfkavdi vakvrppset etkrlkagqt lisffwpgqn ealmelarsk ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvflefde qqqdgaatgg yaapsspefr
      241 ekqlakfrel apeidivitt alipgrdapk lwledmvaam kpgsvvvdla aekggncdlt
      301 vmdqkivsdn gvtiigytdf psrmaaqast lysnnvrhmm sdltpekdgq vahnmeddvi
      361 rgatvtyake itfpppppki raiavqkkev vkeltaeekr aaevaafkkt tkqqvgllvg
      421 gavlmlivga fapasfmqhf ivfvlacfig fqviwnvsha lhtplmavtn aisgivvlga
      481 llqigsgnwl vvvlasisvl iatinvvggf lvtrrmlamf qks
//
LOCUS       WP_114287213             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Halocynthiibacter alkanivorans].
ACCESSION   WP_114287213
VERSION     WP_114287213.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Halocynthiibacter alkanivorans
  ORGANISM  Candidatus Halocynthiibacter alkanivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Halocynthiibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Candidatus Halocynthiibacter alkanivorans"
                     /db_xref="taxon:2267619"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55586
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtlkevf agearvamtp dsalqlqklg ydcviesgag qaagfsdaty ldagveviqt
       61 aaalieicdi vakvrpptgd eanslragqt lisffypgqn dalmelcrdk ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aafvyldfee dqrdgaetgg yaapsslefr
      241 ekqlekfrel apemdivitt alipgrdapk lwledmvlam kpgsviidla aerggncdlt
      301 vadektvskn gvtivgytdf psrmaaqsst lysnnirhmm fdltpekngq vhhnmeddvi
      361 rgatvtfare itfpppppki aaiaaqkpkv tvieltpeek raaeveafkt atkqqvgllt
      421 vggilmlaig afapasfmqh fivfalacfv gfqviwnvsh alhtplmait naisgivvlg
      481 allqigsssf lvtvlaaisv liasinvvgg flvtrrmlam fqks
//
LOCUS       WP_114291422             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudosulfitobacter sp. DSM 107133].
ACCESSION   WP_114291422
VERSION     WP_114291422.1
KEYWORDS    RefSeq.
SOURCE      Pseudosulfitobacter sp. DSM 107133
  ORGANISM  Pseudosulfitobacter sp. DSM 107133
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Pseudosulfitobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudosulfitobacter sp. DSM 107133"
                     /db_xref="taxon:2883100"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55407
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif kgerrvamtp dsalmlqklg hecivetgag aeagfsdady aaagveiakt
       61 aaalwkasdv vakvrapeev eakrlrdgqt lisfinpgan selletaakk gstvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aavgtstslg aityafdvrp evaeqiesmg aefvyldfee eqqdgsasgg yasvsspefr
      241 eaqlakfrel apemdivitt alipnreape lwtedmvkam ksgsvivdla aekggncklt
      301 vkdekivten gvtiigytdf psrmatqast lyatnirhmm tdltpekdgv inhnmeddvi
      361 rgatvthake vtfpppppki aaiaaapkke avkeltpeek raaeiaafka qtksqvtllv
      421 vgavlllgvg lvapasfmqh fivfvlsvfv gfqviwgvah slhtplmavt naissiiilg
      481 alvqigsgsf lvvvlaavsv fmtginifgg flvtrrmlam fqks
//
LOCUS       WP_114320994             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            harveyi].
ACCESSION   WP_114320994
VERSION     WP_114320994.1
KEYWORDS    RefSeq.
SOURCE      Vibrio harveyi
  ORGANISM  Vibrio harveyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio harveyi"
                     /db_xref="taxon:669"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54533
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvaiesqag vlasfddaay eaagakivss
       61 eevwtsglil kvnaplvdee kgideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgrpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqaitta ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvvkeg evtwpappiq vsaqpqakpq epvkpqpkve eptspvkkfg alavgvgafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_114325946             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Colwellia aromaticivorans].
ACCESSION   WP_114325946
VERSION     WP_114325946.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Colwellia aromaticivorans
  ORGANISM  Candidatus Colwellia aromaticivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Candidatus Colwellia aromaticivorans"
                     /db_xref="taxon:2267621"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53749
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mnigipkesl ggenrvsgsp ssvsaliklg ftvqvqkgag akasftddey sasdaeivtk
       61 nicwqsdiil kvnpptleev asmkdgatlv sfiapaqspe llealkdksi ttlamemvpr
      121 mtrsqsmdal ssmaniagyr avieasnlfg rfftgqitaa gkmppakvmv igagvaglaa
      181 igtagslgai vrafdtrpev keqiesmgae fleldyeepe dtgsgdgyak emskafidae
      241 malfleqakd vdiiittami pgkpapklit eemveamkpg svivdlaaag ggncdctvpg
      301 kvvsahdvkv igytdlvsrl pnqssqlysn nlvnlakllc knkdgtldid fedvvirnmt
      361 vvkegeitfp pppiqvsaap aqkaaepvev veeepaspvk kyafmavgia lfgwvasvap
      421 adflthftvf vlacvigyyv vwnvshslht plmsvtnais giiivgallq igsdnmlvqi
      481 laafatlvat inivggfrvt srmlkmfsk
//
LOCUS       WP_114338372             519 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Corallincola].
ACCESSION   WP_114338372
VERSION     WP_114338372.1
KEYWORDS    RefSeq.
SOURCE      Corallincola
  ORGANISM  Corallincola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Psychromonadaceae.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Corallincola"
                     /db_xref="taxon:1775176"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54752
     Region          1..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvprevm sgeqrvaltp dtaeklqklg felaieagag aaasftdday saagvevitd
       61 taalwrgadi ifkvnppmvd patgndeael lkpeqtlisf fwpaqnedrl kvlaekninl
      121 lamdsvpris raqsldalss manisgyrav veaahefgrf ftgqitaagk vppakvlvig
      181 agvaglaaig aagslgaevr afdtrpevae qiesmggtfl rldyeeedtg agdgyakems
      241 kafieaemkl faeqaaevdi iittaaipgr papklilaem vesmkpgsvi vdlaaltggn
      301 celtepgeav vkhdvtiigy tdipsrlpaq ssqlygtnlv nlmkllclek dgnidinfdd
      361 evlrgvtvak agevtwpapp ikvsaqpqqp aaevaapepv eeakpkpwlk pamlavgagl
      421 fgwvaqnaps dflahftvfv lacvvgyyvv wgvahalhtp lmsvtnaisg iiivgglvqm
      481 nsdsplilal sgfailiati nivggftvtq rmlkmfqrd
//
LOCUS       WP_114349420             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            lutimaris].
ACCESSION   WP_114349420
VERSION     WP_114349420.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus lutimaris
  ORGANISM  Paracoccus lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus lutimaris"
                     /db_xref="taxon:1490030"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55414
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkeny egearvavtp ssaahlkklg hevhvesgag vragfsdaay eaagvavean
       61 agaligaadv vikvrppsda eigqmrrgqt visyfypaqn aellekareq gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv livgagvagl
      181 aaigaatslg aqvyafdvrp evaeqiesmg aefvyldfke qqtdgaatgg yaapsspefr
      241 eaqlkkfrel apqmdivitt alipgrdapk lwtadmveam ktgsvivdla aerggncdlt
      301 vpderivten gvviigytdf psrmgaqase lygnnvrhml adltpgkdgv lvqnmeddvi
      361 rgatvtydgd vtwpppppki aaiaaqkpke kvkeltpeer rakevaefka qtksqvtllg
      421 vgavlmllvg mfapasflsh fivfvlsvfv gfqviwnvsh slhtplmait naissiiivg
      481 allqigsgsw lvvilaalsv lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_114351253             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Saliterribacillus persicus].
ACCESSION   WP_114351253
VERSION     WP_114351253.1
KEYWORDS    RefSeq.
SOURCE      Saliterribacillus persicus
  ORGANISM  Saliterribacillus persicus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Saliterribacillus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Saliterribacillus persicus"
                     /db_xref="taxon:930114"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55437
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesy pgetrvaaip ktveqlkkfg fdisveagag eeasftdeqy lkagainast
       61 tdvwqsdiif kinppneeei vkmnegatlv sfifprqnse likhltekri nvlamdmvpr
      121 israqsvdvl ssmaniggyr avmeathafg rflngqitaa gkvppakifv igagvaglaa
      181 igtgrslgai vrafdaraev aeqvesmgge flsvaieedg ttasgyakem seafikaemd
      241 liaeqakevd iiittaliqg mpapklitke mvdsmkpgsv ivdmaaltgg nceytvpnel
      301 tvtdsgvkii gytdlpgrmp aqasdmyatn lvnltkllck ekdgnididf ddvilrnmav
      361 tregkvtfpp peisvsaapv kkedskakte pitketknrs glkymfgiaa illfgwigqv
      421 sppeflshft vfalaivvgy yviwkvtsal htplmsvtna isgiivvgai lqinsdilav
      481 kilsfigili asinifggfm ithrmlnmfr kdqev
//
LOCUS       WP_114359276             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhodopseudomonas].
ACCESSION   WP_114359276
VERSION     WP_114359276.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas
  ORGANISM  Rhodopseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rhodopseudomonas"
                     /db_xref="taxon:1073"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39027
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeqd paeprvaatp dtvkklkalg aevavepgag vksglpdsdf taagatvaad
       61 alkdadvvlk vkrpeapela gykrgalvla imdpygneaa lksmadagit afamelmpri
      121 traqvmdvls sqanlagyra vidgaeqfgr vfpmmmtaag tvpaakvfim gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpaprlvta emvksmkpgs vlvdlaverg gnvegaqpgq
      301 vveiggvkiv gytnvagrva asasalyarn llsffetmvn kekalavnwd delvkatalt
      361 rdgavvhpnf qpksa
//
LOCUS       WP_114365118             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ciceribacter lividus].
ACCESSION   WP_114365118
VERSION     WP_114365118.1
KEYWORDS    RefSeq.
SOURCE      Ciceribacter lividus
  ORGANISM  Ciceribacter lividus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Ciceribacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Ciceribacter lividus"
                     /db_xref="taxon:1197950"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55424
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigsprevf egearvamtp dsatqlrklg ydciiesgag kaagfsdday raagvdvvds
       61 aealyatadv iakvrppeta eaerlgagkt lisffypaqn kalldlckgk ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsvslg aityafdvrp evaeqiesmg aefvfldftd qqqdgaatgg yaapsspefr
      241 eaqlkkfrei apeidivitt alipgrdapk lwladmvaam kpgsvvvdla aerggncdlt
      301 vadqrivsdn gvivigytdf psrmaaqast lystnvrhmm tdltpgkdgk lvhnmeddvi
      361 rgatvtfege itypppppki qaiaaqkpke kpkeltpeek raqevaafka qtrnqvamla
      421 gggalillag lyapasfmsh fivfvlscfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgnf lvivlgalsv fmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_114374693             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Elioraea
            thermophila].
ACCESSION   WP_114374693
VERSION     WP_114374693.1
KEYWORDS    RefSeq.
SOURCE      Elioraea thermophila
  ORGANISM  Elioraea thermophila
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Elioraeaceae; Elioraea.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Elioraea thermophila"
                     /db_xref="taxon:2185104"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40623
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavpkerr pgearvaatp etvkklrglg ltivvesgag agaaipdaey laagaelapd
       61 pattfadani vfcvqaplgp gegeidqlsl iprgalligg lniwsdpkra eayaqrgida
      121 camellprit raqsmdilss qanlagyrav ieaameypra fpmmmtaagt vapaavfvig
      181 agvaglqaia tarrlgakvs atdvrpaake eikslgatfv gveteetkqa qtaggyakem
      241 sedfkrrqae lmaetvkkqd viictaltmg raapkiitae mvasmkpgsv ivdiaadagg
      301 ncvltrpger vvtengvsil gwrnwparip vaasalyarn lltfltafwd keakapklda
      361 ndeivrgvll trggavvhpq fapkpaeaa
//
LOCUS       WP_114388541             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter baumannii].
ACCESSION   WP_114388541
VERSION     WP_114388541.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39748
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklisag hsvviergag vkaayidsay eqvgatitdd
       61 aytgsqiilk vrapqggeiq klaanttvva mfdpyrntel dqfanqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgaiv eatdlrptak dqveslggkw ldvpmseeeq qraadaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 kvgetvvten gvkilgipni patvapeasa lyarnvfnfv etlfdkeknf ainqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_114390307             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Notoacmeibacter marinus].
ACCESSION   WP_114390307
VERSION     WP_114390307.1
KEYWORDS    RefSeq.
SOURCE      Notoacmeibacter marinus
  ORGANISM  Notoacmeibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Notoacmeibacteraceae; Notoacmeibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Notoacmeibacter marinus"
                     /db_xref="taxon:1876515"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55595
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mklgspkesa pgerrvaltp asakdlaklg heamvekgag alagfsdedy raagvevvds
       61 addlfrqadi iakvqppsde eiarlsddkt lvsffypaan perleavkat gasiiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvpparv lvigagvagl
      181 aaigastslg aityafdvrp evaeqiesmg aefvyldfse eqtdgaetgg yakpsspefq
      241 kaqlekfrel apdidivist alipgrdapv lwtadmveam kpgsvivdla aerggncelt
      301 vkdekivteh gvtiigytdf psrmatqsss lyannirhlm tdltpdkdgv vnhnmdddvi
      361 rgatvahqgd itfpppppkv kaiaaqkpke kaheltaeek kaaelaafka qtrqqvtlla
      421 igaalvlavg liapasfmqh fivfvlsvfi gfqviwnvsh slhtplmavt naissiiilg
      481 aliqigsfsi pikvlaaasi fmasvnifgg flvtrrmlam fqks
//
LOCUS       WP_114395248             394 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oleisolibacter albus].
ACCESSION   WP_114395248
VERSION     WP_114395248.1
KEYWORDS    RefSeq.
SOURCE      Oleisolibacter albus
  ORGANISM  Oleisolibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Oleisolibacter.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Oleisolibacter albus"
                     /db_xref="taxon:2171757"
     Protein         1..394
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41148
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,103,300,327,329)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,290..291,334..335,339,
                     342..343)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,240,251,
                     268..270,277,279)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkicipkerr pgelrvaasp etvkklvalg levavergag vgasitdaaf eaagaaivad
       61 petllktadi vlkvqrplta adtaegglde laamkrgall failnpygsr elvpayaaag
      121 inafamefmp ritraqvmdv lssqanlagy kavvdaasvy grslammmta agtvpparaf
      181 imgvgvaglq aiatakrlga ivsatdvrpa vkeqvqslgg sfiavendef kqaetaggya
      241 kemsddykrq qaalvaehik kqdivittal ipgrkapilv trehvasmrp gsvivdlave
      301 qggnvdgsal nqivttdngv kivgfgnyas riaesaslly aknllallqa lhdkesksir
      361 lnwddeivka ialtrdgavv hpafadpvrq apta
//
LOCUS       WP_114395941             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oleisolibacter albus].
ACCESSION   WP_114395941
VERSION     WP_114395941.1
KEYWORDS    RefSeq.
SOURCE      Oleisolibacter albus
  ORGANISM  Oleisolibacter albus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Oleisolibacter.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Oleisolibacter albus"
                     /db_xref="taxon:2171757"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42875
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,323,325)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,330..331,335,
                     338..339)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaiprerr ahelrvaatp dtvkkykglg fdvvvesgag lgsaltddaf aaagaeiapd
       61 aatalrgadi vlkvqrplla gegqidelal lkrgavlvsg lnpyqapesv tayaaagida
      121 famefmprit raqsmdilss qsnlagyrav ieaaaefgra fpmmmtaagt vpparalimg
      181 agvaglqaia tarrlgamvs atdvrpatke qveslgatfv avmdeefqqa qtaggyakem
      241 saeykakqaa liaetirkqd ivittalipg rkapvlvsde mlrsmkqgav lvdlaveqgg
      301 nvegsvpgev vekygvkivg rinmpsriav dasalyaknl lnfltpfvak dspgtlafng
      361 edevvkgtal trggavvhsa fapkeapaap vaaaappapp vpaaspvpge ppatptv
//
LOCUS       WP_114403369             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Parvibium
            lacunae].
ACCESSION   WP_114403369
VERSION     WP_114403369.1
KEYWORDS    RefSeq.
SOURCE      Parvibium lacunae
  ORGANISM  Parvibium lacunae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Parvibium.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Parvibium lacunae"
                     /db_xref="taxon:1888893"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40359
     Region          1..380
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,296,331,333)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,286..287,338..339,343,
                     346..347)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigifkets pgearvaatp etvkklsagg khqflierga gaaayipdaa yeaagaevle
       61 adaiyqradl lltvrtpsps dlgklrqgqi vvgmlnpfdv dgpnglkaln argvtafale
      121 aaprttraqs ldvlssqani agykavmlaa nlyqrffpml mtaagtvkaa rvvilgagva
      181 glqaiatakr lgavieasdv rpavkeqies lgakfidvpf etdeerecaq gvggyarpmp
      241 aswmqrqaqk vaeriaqadv vistalipgr taptliteam vqsmkpgsvi idmaagkgln
      301 kdgqigggnc pltvadqvtt qhgvqlvgyt nlpamvaada salyarnlld fmklivdaeg
      361 kftlnleddi vaaclmchag elkrna
//
LOCUS       WP_114412546             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinomonas foliarum].
ACCESSION   WP_114412546
VERSION     WP_114412546.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas foliarum
  ORGANISM  Marinomonas foliarum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Marinomonas foliarum"
                     /db_xref="taxon:491950"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55557
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeie dgelrvamtp siaskvkqlg fdivmeggag taasysdeay eeagveitqd
       61 tkklwhevdv likvrppveh pelgfygvel lgksqtlisl ihpaqnmnkl qqlsergtnv
      121 valdavpris raqkmdvlss maniagyrav veaaqhfgrf ftgqitaagk vppakvlvig
      181 agvaglaaig aaksmgaivr afdtrpevke qvesmnaefl lldfndedgs geggyaktms
      241 aefiaaemal faeqakdvdi iittalipgk tapelitedm vrsmkpgsvi vdlaaetggn
      301 crltqanevi dvhgvsiigy tnlpsrmaaq ssqlfatniy hlltelcpnk dgqidlnmed
      361 evirgatvvk dgsitwpppa prlsaapksd vseqlkpeka dikakekkps afgfllpvli
      421 tgalllglgt iapaefmahm tvfvlscfvg ymvvwgvshs lhtplmsvtn aissiiviga
      481 itqvssdspi vsilaamaif itsinivggf avthrmlkmf rk
//
LOCUS       WP_114414910             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Enterobacteriaceae].
ACCESSION   WP_114414910
VERSION     WP_114414910.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53600
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 vtkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_114433119             454 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium bourgognense].
ACCESSION   WP_114433119
VERSION     WP_114433119.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium bourgognense
  ORGANISM  Phyllobacterium bourgognense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Phyllobacterium bourgognense"
                     /db_xref="taxon:314236"
     Protein         1..454
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46173
     Region          4..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke ideprvggsp etvkkltalg favvveagag vasripdsef vaagaaigra
       61 gdiaradvvl kvrrpssael kayrkgavvi amldpygnda avkaladagv taftmefmpr
      121 itraqvmdvl ssqanlagyq avidaaseyd ralpmmmtaa gtvpaakvfi mgvgvaglqa
      181 iatarrlgav vtatdvrpav keqvaslgak flavedeefk aaetaggyak emskeyqakq
      241 aalvadhiak qdivittali pgrpaprlvt rqmvarmrpg svlidlaver ggnvegavag
      301 kitevdgvki vghlnvagri aatasqlyak nllafvetlv dkesktvkid fddelvkatv
      361 lthggkvvhp nfasaataap apaasvakpa avkkaapakp aatkpapaak aatakaapgk
      421 aaapkaktaa ktaaaqpaaa pspktapktt egea
//
LOCUS       WP_114463322             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Runella
            aurantiaca].
ACCESSION   WP_114463322
VERSION     WP_114463322.1
KEYWORDS    RefSeq.
SOURCE      Runella aurantiaca
  ORGANISM  Runella aurantiaca
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Runella.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Runella aurantiaca"
                     /db_xref="taxon:2282308"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39675
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiailketk aferrvaitp divksllkag ftctiqsgag enssllnady ekagatvaad
       61 tqtlladadv vlkvnaptld evaqmregai sisflyaytq pelvkalnak kisafsmdav
      121 prttkaqsmd alssqanlag ykavllgana lgkifplmmt aagtikpskv lifgagvagl
      181 qaiatakrlg avvevsdvrp etkeqveslg gkflsvegme ankseggyak evsaeflqkq
      241 qdlikqrikd adivittalv mgkkapilvt eemvksmktg svivdmaves ggncalsean
      301 ktvvkngvti igesnlpall stnasdlyak nistlllhla nkdgfkwele eeitkgslit
      361 hqgtlvhaft kgilek
//
LOCUS       WP_114471818             536 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudorhodoferax soli].
ACCESSION   WP_114471818
VERSION     WP_114471818.1
KEYWORDS    RefSeq.
SOURCE      Pseudorhodoferax soli
  ORGANISM  Pseudorhodoferax soli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Pseudorhodoferax soli"
                     /db_xref="taxon:545864"
     Protein         1..536
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55785
     Region          11..536
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtastqppq rigvpreifp gekrvatvpe vvekliklgf tvsvqsgage aancsddayr
       61 aagaeivada aalwrtadiv fkvrpptpee vglmreggtl idfiwpaqnp dlmqqlaarr
      121 asvlaidclp rtlsraqkmd altsmagvsg yravieaana fgryfagqit aagkvppakv
      181 fiagagvagl saigtaaslg aivrandtra evadqvtslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rdmyakqakd vdiiittali pgkpapklit aemvqsmkpg svivdmaseq
      301 ggnceltvpg eavvrhgvti vgytdlasrl akqsstlyat nllrlteelc kakdgvavvn
      361 meddairglt vvkdgtitwp applaqvakp paaakpavap aakkgghghg ssgplpaktl
      421 aivftvaala fwfigsfapa aflghftvfv lacfigymvv wnvtpalhtp lmsvtnaiss
      481 iiaigalvqi appdataggr pddlirwlaf aalvltavnm fggfavtrrm lamfqk
//
LOCUS       WP_114440522             433 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phyllobacterium salinisoli].
ACCESSION   WP_114440522
VERSION     WP_114440522.1
KEYWORDS    RefSeq.
SOURCE      Phyllobacterium salinisoli
  ORGANISM  Phyllobacterium salinisoli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Phyllobacterium salinisoli"
                     /db_xref="taxon:1899321"
     Protein         1..433
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44785
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifipre tdpteprvaa spetvkklvg lgfsvavekg agtlsripdd afetagakig
       61 tpgdaksadv ilrvrrpstv elkgyrkgav lvamldpygh eaevrelasa gisaftmefm
      121 pritraqvmd vlssqanlsg yqavidaaae ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfvavedde fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vskemlasmr pgsivvdlav erggnvegaq
      301 pgkvveiggv kivghlnvpg riaatasqly arnllafiet mvdkesktlk infddelvka
      361 tlltrdgaiv hpafagvatd akpitpavkt paapkaraka apgasaaeaa ktptnkaptk
      421 grkpaasktg gea
//
LOCUS       WP_114477376             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Billgrantia montanilacus].
ACCESSION   WP_114477376
VERSION     WP_114477376.1
KEYWORDS    RefSeq.
SOURCE      Billgrantia montanilacus
  ORGANISM  Billgrantia montanilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Billgrantia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Billgrantia montanilacus"
                     /db_xref="taxon:2282305"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55325
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela kgearvaltp dsaqliqklg heclietgag taagfddaay raagvtvves
       61 gealwreaev vikvrepsda eadllregqt liaffwpaqn eallerckar gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrsfdvrp evaeqiesmg aeflfldfed sqdgsgtggy aapsspefre
      241 kqlalfreqa pdvdivitta lipgkpapkl wledmvkamk pgsvivdlaa ekggncdltr
      301 pdekvvsdng vtvvgytdfp srmatqssll yatnirhmlt dltpgkdgvi vhdmeddvir
      361 gatvthqgev tfpppppkvk aiaaakpkpk ekaptpeekk aaelatfkaq tkrqltllgv
      421 ggalmlvlgq vapvsfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgiiilga
      481 vlqigsgnwv vvflaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_114481484             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_114481484
VERSION     WP_114481484.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53562
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhaseeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_114482758             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Extensimonas vulgaris].
ACCESSION   WP_114482758
VERSION     WP_114482758.1
KEYWORDS    RefSeq.
SOURCE      Extensimonas vulgaris
  ORGANISM  Extensimonas vulgaris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Extensimonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Extensimonas vulgaris"
                     /db_xref="taxon:1031594"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38201
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpaetm pgetrvaatp etvkklcaqg hqlcvqagag iaasvpdaay qaagaeivda
       61 atafgadvvl kvrapsaael allrpdavlv gmldpfdrag lerlaqagvs afaleaaprt
      121 traqsmdvls sqanvagyka vllaanayqr ffpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvggy arpmpaswle
      241 rqkaevakra aladvlitta lipgrpapvl vtedmvramk pgsvivdlaa hqggncplte
      301 pgrtvlkhgv tligetnlpa lvaadasaly arnvldflkl vlpkeggvqi dlqedivaac
      361 lvahqgavtr k
//
LOCUS       WP_114484472             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_114484472
VERSION     WP_114484472.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53544
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtaea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_114487546             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Vreelandella rituensis].
ACCESSION   WP_114487546
VERSION     WP_114487546.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella rituensis
  ORGANISM  Vreelandella rituensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Vreelandella rituensis"
                     /db_xref="taxon:2282306"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55652
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreta kgearvaltp esavhiqklg heclvesgag aaagfsdeay keagvtvids
       61 aeklwadaei vikvrepsqv evgylregqt liaffwpaqn eslleecrak gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv liigagvagl
      181 saigtatslg amvrafdvrp evaeqiesmg aeflfldfde nqdgagsggy aapsspefre
      241 kqlecfreqa pqvdivitta lipgrpapkl wledmvkamk pgsvivdlaa ekggncdltk
      301 pdekvvsdng vtivgytdfp srmatqssll ystnirhmlt dltpkkdgev vhdmeddvir
      361 gatvthqgei tfpppppkvk aiaaakpkek vkeptpeekk vaelaairtq tkrqvtllgv
      421 ggllmlvlgq iapasfmqhl ivfvlacfvg yqviwnvsha lhtplmavtn aisgiiilga
      481 vlqigsgnwv vvilaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_114494097             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_114494097
VERSION     WP_114494097.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53599
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta appkpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheie ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_114500078             314 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_114500078
VERSION     WP_114500078.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..314
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36239
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel vsymlhltat
      301 nllfllkwvm lpty
//
LOCUS       WP_114509810             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassococcus profundi].
ACCESSION   WP_114509810
VERSION     WP_114509810.1
KEYWORDS    RefSeq.
SOURCE      Thalassococcus profundi
  ORGANISM  Thalassococcus profundi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Thalassococcus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Thalassococcus profundi"
                     /db_xref="taxon:2282382"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55844
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egearvamtp dsarqlqklg ydcaiesgag ekagftdday aeagveiikt
       61 aaalwkvadi vakvrppsea evkrltqgkl lisffwpaqn kdlmeeaakk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvfldfee eakdgaetgg yasvsspeft
      241 aaqlakfrel apdmdivitt alipnreape lwtkdmvdam kpgsvivdla aekggncklt
      301 kmdekivtdn gvtiigytdf psrmatqsst lfatnirhlm tdltpdkdgk vkhnmeddvi
      361 rgatiaheke vtfpppppkt kaiaaqkpke kvkektpeek raeeiaafkq qtknqvtlla
      421 iggalvlgag liapasfmqh fivfvlsvfi gfqviwgvah slhtplmavt naissiiilg
      481 aliqigsssm lvtalaalgi fmaainifgg flvtrrmlam fqks
//
LOCUS       WP_114523130             480 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Aeromonas].
ACCESSION   WP_114523130
VERSION     WP_114523130.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas
  ORGANISM  Aeromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas"
                     /db_xref="taxon:642"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53147
     Region          29..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsydklf rpglaalllt allgagslaq addsapkgki earselfakd hadqftswkg
       61 tsesrertda laedpqmvvl wagypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eqyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfdqtcrnch tqskemlqgv vkqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaemk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llaakgishe iaipdisske kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_114530475             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces parvulus].
ACCESSION   WP_114530475
VERSION     WP_114530475.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces parvulus
  ORGANISM  Streptomyces parvulus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Streptomyces parvulus"
                     /db_xref="taxon:146923"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53132
     Region          13..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtghhathhp prrvgvvaes ipgetrvaat patvrpllgl gyevvvesga gtasgfadda
       61 yaeagasvge awaadvvlkv nppsveeiae lregaalval iapaqhpdll ealaarnvtv
      121 laldavpris raqsmdvlss maniagyrav ieaahafgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgavvr atdprpevad qvrslggeyl avdasqeast dgyaratsad
      241 ydraaaelyh eqardvdivv ttalipgrpa prlltaadva vmrpgsvvvd maaaqggnve
      301 gtvpgrtvvt dngvtligyt dlasrlpaqa sqlfgtnlvn llalatpgkd grlvvdfddv
      361 vqravtvvra gavtwppppv avsaapaaaa paasasepvp arksrltpag rfgliglgma
      421 amflliafap aqlaenltvf alavvigyyv igkvhhslht plmsvtnais givvigallq
      481 lghesalvtv lsfvaillts vnifggfavt rrmlsmfsrg es
//
LOCUS       WP_114536334             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            versutus].
ACCESSION   WP_114536334
VERSION     WP_114536334.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus versutus
  ORGANISM  Paracoccus versutus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus versutus"
                     /db_xref="taxon:34007"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55569
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigglkeif egearvaitp ssaghlrklg hdvhvetgag vragfsdaay eaagvtvhpn
       61 aaalvgavev vvkvrppsea elrqmrrgqt lishfypaqn pdllelareq gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaavslg aqvhafdvrp evaeqiesmg aefvyldfqd qvqdgaatgg yaapsspefr
      241 ekqlekfrel apemdivitt alipgrdapk lwtrdmvaam ktgsvivdla aerggncelt
      301 vpderivten gvviigytdf psrmgaqase lygnnirhml sdltpgkdgv ivqnmeddvi
      361 rgstvahdgd vtwppppprv aaiaaqkpre kpreptpeer raqeiaafra qtrsqvtllg
      421 agaaamllvg lfapasflsh fivfvlavfv gfqviwnvsh slhtplmait naissiiivg
      481 allqigsggw lvvflaalsv lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_114573355             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            sp. DQ26W].
ACCESSION   WP_114573355
VERSION     WP_114573355.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. DQ26W
  ORGANISM  Halomonas sp. DQ26W
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas sp. DQ26W"
                     /db_xref="taxon:2282311"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55564
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkela kgearvaltp dsaqliqklg hecliesgag iaagfdddty rtagvtvves
       61 aealwreaev vikvrepsne eadllrdgqt liaffwpaqn ealmerckar gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 saigtatslg avvrsfdvrp evaeqiesmg aeflfldfed sqdgsgtggy aapsspefre
      241 kqlalfreqa pdvdivitta lipgrpapkl wledmvkamk pgsvivdlaa ekggncdltr
      301 pdekvvsdng vtivgytdfp srmatqssll yatnirhmlt dltpekdgvi vhdmeddvir
      361 gatvthqgev tfpppppkvk aiaaakpkpk ekaptpeekk aaelasfkaq tksqltllgv
      421 ggalmlvlaq iapasfmqhf ivfvlacfvg fqviwnvshs lhtplmaltn aisgiiilga
      481 vlqigsgnwv vvflaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_114601260             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Gordonibacter sp. 28C].
ACCESSION   WP_114601260
VERSION     WP_114601260.1
KEYWORDS    RefSeq.
SOURCE      Gordonibacter sp. 28C
  ORGANISM  Gordonibacter sp. 28C
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Gordonibacter.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Gordonibacter sp. 28C"
                     /db_xref="taxon:2078569"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53222
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkepf egqtlvaasp dtvakliklg yeiaveegag aragyfddqy laagaeivgk
       61 eeawgsdivt cldtppaeel slvkkgatll armnpgaspe ligrlavknv talaldmvpr
      121 lsraqsldvr ssmmnvagnr avieaanrfg rlfagqvtaa gkvppakvyv igvgvaglaa
      181 igaagsmgae vsatdvraev adqveslggt fveipvrqes sdgyakelae eqqkavlevy
      241 keqaaksdiv ittaqvpgrp apllltaqav agmrpgsviv dmgasglgsn celtrpgeay
      301 ttengvtiig ygdlpsrlpg qssqlfgqnv vnlfklatpk kdgvpiwdae devirgmlvt
      361 vegkvmwppp pakvsaaqqp aqaapadeap eaaeapawkk wwwkvalgvl gvalvltapt
      421 emaghfivfe lavvvgfyvi tsvthtlhtp lmsvtnaisg iivvgailla gssnpivaal
      481 sfvamviasi nvfggflitn rmlkmferss e
//
LOCUS       WP_114609191             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Intrasporangium calvum].
ACCESSION   WP_114609191
VERSION     WP_114609191.1
KEYWORDS    RefSeq.
SOURCE      Intrasporangium calvum
  ORGANISM  Intrasporangium calvum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Intrasporangium.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Intrasporangium calvum"
                     /db_xref="taxon:53358"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52711
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpretr pretrvaatp ktvgqlialg ydvvvergag vgasfddaay vaagarvvda
       61 seawgsdivh kvnapsdaei tmlrpgavlv slmapalspd lveklraanv tamamdavpr
      121 israqsldvl ssmaniagyr avveaahqfg sfftgqvtaa gkvppakvlv vgagvaglaa
      181 igtagslgai vratdarpev aeqvesmgge flhvqvgelq assdgyarem gedynrkaae
      241 lyaeqckdvd iiittalipg rpapllitde mvatmragsv ivdmaaangg nvagsvadel
      301 vvtdngvkii gytdlagrlp tqasqlygtn lvnlmklvtp gkdgqlvadl edtvvrgmtv
      361 ardgellwpp ppiqvsaapa pvaaaplaka pppppnpnrk fvmmgvgaav faliaafspa
      421 sflshftvfa lavvvgfyvi gnvhhalhtp lmsvtnaisg iivvgaliql gvsesadvai
      481 lalafvatlv asinifggfl vtrrmltmfr kg
//
LOCUS       WP_114612272             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter vulgaris].
ACCESSION   WP_114612272
VERSION     WP_114612272.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter vulgaris
  ORGANISM  Marinobacter vulgaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter vulgaris"
                     /db_xref="taxon:1928331"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55894
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipreif tderrvaatp psvhkliglg yevtveggag eaanyadeay ekvgatiatd
       61 ttslwqeadf ilkvrapmen palghhevdl mkegaflvsy iwpaqnpdll eklaarkits
      121 faidslpris raqkmdalsa maniagyrav ieaannfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig aansmgaivr afdtrlevke qvesmgaefl vldfdneegs gsggyakqms
      241 defikaemal faeqarevdi iittalipgk papklitaem vksmkpgsvi vdlaserggn
      301 celtepgkva hhhgvtligy tdlpsrmakv asdlyatnlv hllteltpek dgkpfvnmed
      361 dvirgltvvq dnnitwpppq peapvstapp pgteepsaad kaaakkvadr raligkgvlf
      421 avtalalygv gayapesflq hftvfvlacf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gailhlaqae nlavgimafv avliasinvg ggfrvthrml kmfrr
//
LOCUS       WP_114636356             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter necessarius].
ACCESSION   WP_114636356
VERSION     WP_114636356.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter necessarius
  ORGANISM  Polynucleobacter necessarius
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Polynucleobacter necessarius"
                     /db_xref="taxon:576610"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39299
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpletr pgetrvaatp etvkkligqg htvviqkdag vkasqpdsay eavgasigsa
       61 sdalgaeivl kvrapetsel qqikagavll gmldpfdndm ivamaaqgit afsleaaprt
      121 traqsmdvls sqaniagyka vmvaaneyqr fmpmlmtaag tvkaahvlil gagvaglqai
      181 aiakrlgaii easdvrpaak eqieslgakf vdvpyetdee reiaqgvggy arpmpeawmk
      241 rqaalvaera qqadivitta lipgrkppvl lhsdtvanmk pgsvvidlaa gkgdnssgnc
      301 pltqadkvid vngvkivgyt nlasmvgada salyarnlld fmklivdkea klvipsdddi
      361 vtaclmcrdg qairkn
//
LOCUS       WP_114639155             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter necessarius].
ACCESSION   WP_114639155
VERSION     WP_114639155.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter necessarius
  ORGANISM  Polynucleobacter necessarius
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Polynucleobacter necessarius"
                     /db_xref="taxon:576610"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39190
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpletr pgetrvaatp etvkkligqg htvviqkgag vqasqpdsay eavgaaigsa
       61 adafgaeivl kvrspeasel kqiqsgsvll gmldpfdndn iaamaargvt afaleaaprt
      121 traqsmdvls sqaniagyka vmvaaneyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpyetdee reiaqgvggy arpmpeawmk
      241 rqaalvaera qqadivitta lipgrkppvl lhsdtvanmk pgsvvidlaa gkgdngsgnc
      301 pltqadkivd vngvkivgyt nlasmvaada salyarnlld fmklivdkea klvipsdddi
      361 vtaclmcrdg qairkn
//
LOCUS       WP_114646748             477 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pelagibacterium lacus].
ACCESSION   WP_114646748
VERSION     WP_114646748.1
KEYWORDS    RefSeq.
SOURCE      Pelagibacterium lacus
  ORGANISM  Pelagibacterium lacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Pelagibacterium.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Pelagibacterium lacus"
                     /db_xref="taxon:2282655"
     Protein         1..477
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47963
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavmrera ggetrvaatp etvakligfg atvsvekgag dasrildgqy eaagasleat
       61 aaaavkgadv ilavrrpevg alsgaakgal vlavadpygn eaalaalaga gfsvlamelm
      121 pritraqvmd vlssqanlag yqavieaala ydrampmmmt aagtvraakv fvmgagvagl
      181 qaiatarrlg aavsatdvra aageqveslg akfimtdalk dasgsggyar eltpeeqaaq
      241 aelvaghiak qdivvttali pgrpaprlvt kamvesmapg svlvdlaaer ggnveltrpg
      301 evvvhngvti igllnragki aatasqlyak nllafletmi dkdakalkvd wedelvkatl
      361 ltrdgavvhp nfaeaasaaa kaepkpvead kpvakapakt gaaakaaeak vatagavsva
      421 gekparkrtp aktgaaskta eaapeaakpa arkaparkpa akkpaakktv iksdgea
//
LOCUS       WP_114653953             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter necessarius].
ACCESSION   WP_114653953
VERSION     WP_114653953.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter necessarius
  ORGANISM  Polynucleobacter necessarius
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Polynucleobacter necessarius"
                     /db_xref="taxon:576610"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39457
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpleir pgetrvaatp etvkklisqg htvviqkdag vtasqpdsay eavgatigsa
       61 sdafgaeivl kvrapeaael kqikygsvll gmldpfdndn iaamaaqgvt afsleaaprt
      121 traqsmdvls sqaniagyka vmvaaneyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpyetdee reiaqgvggy arpmpeawmk
      241 rqaalvaera qqadivitta lipgrkppvl lhsdtvanmk pgsividlaa drgdngsgnc
      301 plteadkive kngvkiigyt nlasmvaada salyarnlld fmklivdaea klviptdddi
      361 vtaclmcrdg qairkn
//
LOCUS       WP_114663063             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter necessarius].
ACCESSION   WP_114663063
VERSION     WP_114663063.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter necessarius
  ORGANISM  Polynucleobacter necessarius
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Polynucleobacter necessarius"
                     /db_xref="taxon:576610"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39104
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpletk pgetrvaatp etvkklvgqg htvvvqkgag vnasqpdsay eavgasigsa
       61 adafgaeivl kvrapetsel kqistgsvli gmldpfnndn iaamaaqgit gfsletaprt
      121 traqsmdvls sqaniagyka vmvaaneyqr fmpmlvtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpyetdee rktaqgvggy arpmpeawmk
      241 rqaaliaera qqadivitta lipgrkppvl lhsdtvanmk pgsvvidlaa gkgdngsgnc
      301 pltqadkvvd ingakivgyt nlasmvaada salyarnlid flkliidkea klvipndddi
      361 vtaclmcrdg qairkn
//
LOCUS       WP_114683858             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Citrobacter].
ACCESSION   WP_114683858
VERSION     WP_114683858.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53532
     Region          21..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mariksrvrr ffslllpllf isavhaeqps vpaktvtvea knetfapqhp dqylswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspd fakgkpeltl
      181 srpyaerame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmek
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegkiytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gateaemkpi ledirhaqwr wdlsiashgi hmhapeeglr mlgsamdkaa dartklvrll
      421 atkgitheip lpdistkeka qaaiglnmqq inaekqdfik tvipqwedqa rkngllsq
//
LOCUS       WP_114690101             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter necessarius].
ACCESSION   WP_114690101
VERSION     WP_114690101.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter necessarius
  ORGANISM  Polynucleobacter necessarius
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Polynucleobacter necessarius"
                     /db_xref="taxon:576610"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39350
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletr pletrvaatp etvkkligqg htvviqkdag vrasqpdsay eavgatigsa
       61 adafgaeivl kvrapeaael kqiksgavll gmldpfdndm iaamaaqgvt afsleaaprt
      121 traqsmdvls sqaniagyka vivaaneyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpyetdee reiaqgvggy arpmpeawmk
      241 rqaalvaera qqddivitta lipgrkppvl lhsdtvanmk pgsvvidlaa gkgdngsgnc
      301 pltqadkvid vhgvkivgyt nlasmvgada salyarnlld fmklivdkea klviptdddi
      361 vtaclmcrdg qairkn
//
LOCUS       WP_114694454             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Motiliproteus coralliicola].
ACCESSION   WP_114694454
VERSION     WP_114694454.1
KEYWORDS    RefSeq.
SOURCE      Motiliproteus coralliicola
  ORGANISM  Motiliproteus coralliicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Motiliproteus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Motiliproteus coralliicola"
                     /db_xref="taxon:2283196"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55169
     Region          1..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkeih sgekrvaltp plvkqlqqmg ydvaieagag ldsnftdqay vdagvevidg
       61 aealwsasdi vlkvrppeqn ealgkheadl lnegailtsf iwpaqnpelm erltarkanv
      121 lamdsvpris rsqrcdalss maniagyrav veasnhfgrf lngqitaagk vqpakvliig
      181 agvaglaaig cagrmgaivr afdtrpvvke qvesmdaefl tveieedgsg gggyakemsk
      241 efidaemalf reqarevdii ittalipgkp apkliledmv emmaegsviv dlaaeqggnc
      301 eltvpgevvv rhgvsiigft dlpsrlptqs sqlyatnvrn vlseltpekd gkpdfnmedt
      361 iirgttvihe geviwppppp elsvapppka apepvpepep msagkraait fgsmgvamll
      421 llmlgsvapa afmshlivfv lscfvgwqvv wavtpalhtp lmsvtnaisg iiiigallqa
      481 gssssvvgfl afvailiasi niaggfyvtq rmlkmfvred
//
LOCUS       WP_114697676             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter necessarius].
ACCESSION   WP_114697676
VERSION     WP_114697676.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter necessarius
  ORGANISM  Polynucleobacter necessarius
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Polynucleobacter necessarius"
                     /db_xref="taxon:576610"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39307
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpletr pgetrvaatp etvkkfigqg htvviekdag vkasqpdsay eavgatigsa
       61 adafgaeivl kvrapeavel kqiksgavll gmlepcdndm iaamatqgvt afsleaaprt
      121 traqsmdvls sqaniagyka vivaaneyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpyetdee reiaqgvsgy arpmpeawmk
      241 rqaalvaera qqadivitta lipgrkppvl lhrdtvanmk pgsvvidlaa gkgdngsgnc
      301 pltqadtvvv vngvkivgft nlasmvgada salyarnlld fmklivdkea klviptdddi
      361 vtaclmcrdg qairkn
//
LOCUS       WP_114701664             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psychrobacter proteolyticus].
ACCESSION   WP_114701664
VERSION     WP_114701664.1
KEYWORDS    RefSeq.
SOURCE      Psychrobacter proteolyticus
  ORGANISM  Psychrobacter proteolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Psychrobacter.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Psychrobacter proteolyticus"
                     /db_xref="taxon:147825"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39841
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,127,130,133,174..177,197..199,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvisads asesrvaitp davrklrklg fevviqsgag qaayyadely qaagadiass
       61 rtevitqski ittvndlpae ateslssgqi vigmldpyrn tqldtyaakg atvfamellp
      121 rtlsraqnmd vlssqanlag ykavllaane ysrpfpmfmt sagtvkpakv vilgvgvagl
      181 qaiatakrlg avveasdlrp tareqveslg gkwldvpmsa eeaetakstg gyawtpseqy
      241 vkdqaavvdk alsnadivit taqipgrnap rlvhsatlak mkagsvlidm aagtggnveg
      301 svpnetittd ngvrivgaan ipsqlaaqss dlyannlvnf ittliaatgd dasaslalnl
      361 dmedeiqgal avthdsqvrl akr
//
LOCUS       WP_114706653             289 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Vibrio cholerae].
ACCESSION   WP_114706653
VERSION     WP_114706653.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         <1..289
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          <1..288
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 dgyakemsde fnrkaaelya aqakdvdiii ttalipgkpa pklitkemvd smkagsvivd
       61 laaanggnce ytvkdqvitt dngvkvigyt dmvgrlptqs sqlyatnlvn llkllckekd
      121 gnidinfedv vlrgvtvvka geitwpappi qvsaqpqqka kvqptkaqkk epeptspvkk
      181 lvglavgvgl fawvasvapa aflghftvfv lacvvgyyvv wnvthalhtp lmsvtnaisg
      241 iivvgallqi gqgsgivtfl afiavliasi nifggftvtk rmlemfrkn
//
LOCUS       WP_114708383             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_114708383
VERSION     WP_114708383.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53814
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq pkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_114709059             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_114709059
VERSION     WP_114709059.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53873
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp aqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqdsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_114717041             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_114717041
VERSION     WP_114717041.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53845
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplii kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_114714417             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            grahamii].
ACCESSION   WP_114714417
VERSION     WP_114714417.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium grahamii
  ORGANISM  Rhizobium grahamii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium grahamii"
                     /db_xref="taxon:1120045"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39367
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnvvfvake ttgdetrvaa svetvkkmvg lgldvvveag agtkskipda efeavgarig
       61 svgatatadv vlkvrrptdd eiggyksgai viavmdpygn deaiaamaka glssfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vsremlksmk pgavavdlav erggniegvk
      301 pgkvadvdgv rvigyanmag riaasasaly aknlvtflet mvnketktia lnledelika
      361 tmlthvgnvv hpafggtkkg dn
//
LOCUS       WP_114721528             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_114721528
VERSION     WP_114721528.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53881
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp psveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev qeqvqsmgae flevnfqeta glgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_114731837             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_114731837
VERSION     WP_114731837.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53829
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpt lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta glgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvgsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgvv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_114741478             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_114741478
VERSION     WP_114741478.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53773
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 ediwacplil kvnapsdgei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_114750463             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pleomorphovibrio marinus].
ACCESSION   WP_114750463
VERSION     WP_114750463.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphovibrio marinus
  ORGANISM  Pleomorphovibrio marinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Pleomorphovibrio.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Pleomorphovibrio marinus"
                     /db_xref="taxon:2164132"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39549
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgllkeps petrvslhpe avkaltgtgn kilvekgagd taflndtlyq eagaqiaerk
       61 evlqqaemlf qitpiskqer qtlttgklvf giyqplvekd lmkeiatqgv tllsmdaipr
      121 itraqsmdvl ssmstvsgyk avllaaaqlp rffpmlmtaa gtiapakvlv igagvaglqa
      181 iatakrlgav veafdtrpsv keqveslggk fvevpgaved kaaggyaveq seeykqkqae
      241 mmeksivksd vvittalipg rkapllitkd mlvqmkpgav vvdlaavngg ncegtineet
      301 vtiegvtiig tsalpstmpe datrmysknv hnllkimlke dqlnlnfedp iikgtcithn
      361 gevvyeplkq
//
LOCUS       WP_114750987            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pleomorphovibrio marinus].
ACCESSION   WP_114750987
VERSION     WP_114750987.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphovibrio marinus
  ORGANISM  Pleomorphovibrio marinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Pleomorphovibrio.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Pleomorphovibrio marinus"
                     /db_xref="taxon:2164132"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122878
     Region          48..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksiskgkg vffvlcccll fisgffspih atensinrta ldigefditi tgvvtdenge
       61 plpgasille gsttgtvtdi dgnysltvpd dsqtlivsyv gyqqqrvqig grseinvqls
      121 pdaeqlsevv vtafglkree rslghavgkv dtdqlaqnpe invanslsgr vagvqvdgag
      181 gadgssrvvi rgfsslggnn qplyvvdgip idntsrvqag rwggrdggdg iqnlnpndie
      241 emsvlkgpna aalygergan gvimittksg asrdgigvei nsnmrvgnpl vwpdfqneyg
      301 lgsngqhryf sdgqgnifsr seaqamgnmd qltpqvttnr dgpqhpkswg prmdghtvyg
      361 wdgemvpfsp qpnnvrdffq nqltfdnsvs lsggnetsnf rlsvgdirnr gmqpsnnltr
      421 ntfniraehk fnerltvssk vnyvrqsven rvgladdqrn aiyqfrglpr ntslesfqry
      481 eltqgdldnp nalhdylsnq rqvgwsrhws ngthtenpyw itnnvrnedr rervmafmdi
      541 hyqindwlst sllagtdfyt dnrhthdaig trvnqiggms ettqqfredn vqfllmankk
      601 ltddldfsan iggnymrndf qnsgfdgsrl svpnlyvitn aavqnpilni qqreiqsvfa
      661 fgqlgwrdyl yldwsirndw sstlpeqnns fmypaissnf vwtdafdfys stlsygslra
      721 swaqagnsad pynvlgvynl tnnphlgqpg avfqntvpfs dlqseltssw eigadlrffe
      781 grlrldatwy hastvnqiln iavapssgfa nrsvnageiv ntgvevmidg vvveredlmw
      841 slnlnvahny nevvslvdgi drfmlgdsrn vrvyadpgqp ygaiyspiar wlrdddgnri
      901 vgqdglpvre ngefrignvm plftggfsst lnyknwtlft lfdmryggdi fslsnvyeal
      961 ygtttrtleg rdgtyiadgv vgvqnedgqw vstgepnttq isaeqywnhv vpaqdqsvge
     1021 eflnsstfvk mrelrlgynf prafterlgv nqlnlsfvgq nlfyfvrhtd gfspevasfn
     1081 lgqegmgies fawplmrnlg fniriaf
//
LOCUS       WP_114752554            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pleomorphovibrio marinus].
ACCESSION   WP_114752554
VERSION     WP_114752554.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphovibrio marinus
  ORGANISM  Pleomorphovibrio marinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Pleomorphovibrio.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Pleomorphovibrio marinus"
                     /db_xref="taxon:2164132"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115443
     Region          26..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkplwimma lvgliffnqe gmaqtrtltg tvldvndgmp ipgvtvfekg tnrgistdid
       61 gtfsieadnn tvlvfsfigy htqeievgnq stlevlmsed vsdmqevvvt algiekerrs
      121 laysisevkg ddliearein lgdqlqgria gvnvsnigsg vagssrvvir gntsltgnnq
      181 plyvidgvpm dnsqlgsagm wggvdwgdgl sslnpddies lsvlkgntaa alygsrasng
      241 vvlittkkgt krqgigvevn sqytaerifn lfdfqqeygh gsagmvptnp gqgrefggis
      301 wggrldgspv yqfdgeqrpy eyagdnferf yrtgstltnt valtggsdkq tfrfsmsdlr
      361 nasitpnsgm nrqtatlstt anyvekltvs akiqytredv tnrarlsdsp gnsnatlavl
      421 ppninvdnlr gdpnkfgarp dgrelqyndn tfsqnpwwaa yqfensnvrd riigsglary
      481 dvndwlyaqa rvgmdwytsr rrslepfgta yrqlgalnee qirvrevnme yiigankefg
      541 dfginaffgg nmmersyenl ggraenfnvp flhtlqngan qslifdfnee ginslfgste
      601 fsyrnflfln vtarndwfst lpvnsnsily psvggsfvfs dafilpswis fgkvrgswae
      661 vgggappyql elnyglvgqg hlgaalarin qtsvpnnmlq pltagefevg fdirfmedrf
      721 gidyayykrt trndiiqtti pqtsgygqat vnvgevsnmg hevlltanli espnftwssn
      781 lnmsynindv eslfedsrvl svdeartgga fiqhripytd pgtgmfmpgg ysvimgrkhq
      841 rvdgqkvyde nglplftddl hylgsgispw aggwnnnfri gsislgmlid ykfggsiysg
      901 tnarayatgn hkntlegree gvtvtgvden geagewfisp ndpsnqgitt vqdyysryae
      961 itenfvydsd fiklrqisig yniptrlldr tpitgmnvsl iarnlfilhs kvdnidpest
     1021 fnslngqgie yygvpqtrsy gfnismkf
//
LOCUS       WP_114752401            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Pleomorphovibrio marinus].
ACCESSION   WP_114752401
VERSION     WP_114752401.1
KEYWORDS    RefSeq.
SOURCE      Pleomorphovibrio marinus
  ORGANISM  Pleomorphovibrio marinus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Pleomorphovibrio.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Pleomorphovibrio marinus"
                     /db_xref="taxon:2164132"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118221
     Region          23..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlllivcl gllisfssfa qaqtvtgkvt dskdgtslpg vsvlikgtst gtatdvdgny
       61 sisvdgsetv lvfsylgfqt lelpvgnrnt invsleeaaa eltevvvtal giernvkalq
      121 ysvttvggdn ltearennla nqlagrvagv nvtnvasgpa gssrviirgn tslqgnnqpl
      181 yvvdgipmdn tnfgqagvwg gpdrgdgmss inpddiesis vlkgasaaal ygaraangvi
      241 nivtkrgtar kgigvefnsn fvfeqindqt elqrtfgsgr tigpnmleav gtrpatiqqg
      301 ynwgtqawge rldggnvthf hglqrpyqya gdnwqrfyqt ataltnsisl agggenqtfr
      361 fnltdlrsna vipnsgfdrl naslatngkf gkkltfdaki lysnesaknr pflsdspnna
      421 fqsifalppd vnvldgrgdp nkpgaiapvi spywgqmgit dpqllldtwg fvegeemlmv
      481 nnpwgqnpyw athqvsvndv rnrilgsgsm ryditdniya sgrigmdwfn rrdtqiipqg
      541 tghtrggnmy egadivqetn leamlgfnke fgligvnafv ganrmhrsfn riratgqnfn
      601 vpffhamnna airnfdygfn elginsvfgs aeisynnvlf ltgtmrtdwf svlnpennqi
      661 typsiggsfv fsdalselps wlsfgkvras waqvgnvtvq pyqvenfysl lsapatdhsg
      721 qqipmasfaa aqgnagtipn rdlvpltste qefgidmrff qnrlgldlty ysqkttndil
      781 natisrssgf gstlvnvgem rnrgiemlft gtpvakrgft wevslnlarn rnevvslipg
      841 ndilvvdepr trtvfiqhrv gqpfgsivgw vqkrtpdgip ifepngapvq sdamevigng
      901 ipdwtggfsn tvsfkgfnlg alidfriggh iysgtnlrlt qwglheqslq gregeepltv
      961 sgvvqagtda ngnpiyedfn rtlspgeaqn ywaqtgnrvq dhfiydgsfa klrqinfgyn
     1021 fpqrllektp fgnlnlsfvg rnlsilwknv enidpesnys sgnaqgldyf gmpqtrsygf
     1081 nlratf
//
LOCUS       WP_114763799             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_114763799
VERSION     WP_114763799.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53865
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqsq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 aptaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_114757906            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. AG291].
ACCESSION   WP_114757906
VERSION     WP_114757906.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. AG291
  ORGANISM  Flavobacterium sp. AG291
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Flavobacterium sp. AG291"
                     /db_xref="taxon:2184000"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110320
     Region          44..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkifsankgl rvlfyslila slpisalara hasptgkayf qqilsgtisd atgplpgaiv
       61 lvkgttrsva adsqgkytia avtgdvllfs ftgyknlevi vtaqsvidvs leedstqlke
      121 ltinagyysv kqkeatgsia ritskdietq pvtnmlaamq grmagvsitq stgvpgggfs
      181 ikirgtnslr qdgndplyii dgmpfnaaay gasntglilp gsgtnplnsl npsdiesiev
      241 lkdadataiy gsrgangvvl ittkkgkggk tafsiesytg fgtitkksrl mktpqyiamr
      301 kqafyndgvt eypayaydin gtwdqnrytd wqkeliggps vinslqstis ggneqtqfli
      361 sntiygettv fpgdfdfrkv amnfnlnhts rdkrfrlsfs gnyitdrnnl patdltkaal
      421 tlspnapely dssgglnwen stwsnpvavl nepyenknnt ligntalqyl ladglelkta
      481 lgftqnrfke sratpstiyd pafglgteys slslssvdar swnfepqlny kkqlgqstvq
      541 alagmtfler kstqegliaq gyssnsliyn pamasmvfal ptndveyryn avfarlnydy
      601 agryilnltg rrdgssrfgp gkkfanfgav gaawifsken wfdrlpalsf gklrasygtt
      661 gndqigdyqf lnlygysgns yngipglqpv rlfnpdfswe tnkkleaaie iglfqdrvfv
      721 ssawyrnrss dqlvgiplpg ttgfssiqsn ldavvqnsgw efelrlqpvq kkhfgwnanl
      781 nvslpktkll sfpglessty rnqyiigepl diiqaynyeg vdtetglyrf tdfdgdgtit
      841 angdrkavvr rnpkyfaglq nslrfknwnl dfllqfvdqm gtksahigyl pgsvsnlpvq
      901 ngsvwtqpgd vasvqkyatg ldnaattafy rflasngsyt dasylrlknv slsymlpasf
      961 sesvaskvyv qaqnlftits yknadpetqf sgylpplriv sfgmkltf
//
LOCUS       WP_114772095             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_114772095
VERSION     WP_114772095.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53855
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp psveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_114771480             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            subterranea].
ACCESSION   WP_114771480
VERSION     WP_114771480.1
KEYWORDS    RefSeq.
SOURCE      Microvirga subterranea
  ORGANISM  Microvirga subterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Microvirga subterranea"
                     /db_xref="taxon:186651"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39480
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd raetrvaatp etvkkykglg advvvqagag lragfsdsef evagaaiaas
       61 aeeavrdadi ilkvrrpsng eltgvksgal ligimdpygq daalkslada hvaafsmelm
      121 pritraqvmd vlssqanlag yravidatae ygrampmmmt aagtvpaarv fvmgagvagl
      181 qavatarrlg avvtatdvrp aakeqveslg akfiavedee fkqaetaggy akemsaeyra
      241 kqaalvashi akqdivitta lipgrpapkl vtremvesmk pgsvvvdlav erggncelak
      301 pgevvehngv kivghlnmpg rlaasassly aknlyafvet lidkdsktva vkwddelvka
      361 tcltrdgaiv htafqpta
//
LOCUS       WP_114777470            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Botryobacter
            ruber].
ACCESSION   WP_114777470
VERSION     WP_114777470.1
KEYWORDS    RefSeq.
SOURCE      Botryobacter ruber
  ORGANISM  Botryobacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Botryobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Botryobacter ruber"
                     /db_xref="taxon:2171629"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116957
     Region          32..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrfkrftvyr khllatlfll lvcscgllaq sqtisgvvsd sqgqplpgvt vllkgstvat
       61 stnmggaysl tipgalttgd vlvfsfigyk tsevaysgka tinvklqvnd hvlsevvvta
      121 lgiereqkal gyatqtvsse slndarsnnf aqalsgkvag lsltspgsgp vnstrislrg
      181 dnslnpdgnn alivldgvpm ssemtssgvs saygagsgnd vpidfgngia dinpddiesi
      241 tvlkgpsaaa lygsraanga liittksgsr rqkgigvtvn tnisfndvlr wpdfqheygq
      301 gtenlnkegk pyysyrased gantgstssa ygpkfdgqyy yqydptlegq saerqlwrpy
      361 kdnvkgffrt gstitnsvav eggnekgsar asvthsknew impntgferl taalslnyka
      421 sdklrlnskv nfthkksdnl patgynnqsi syfmifqnpn vdlawyeprw ksgqeqidqi
      481 hpfssyidnp yviayemtna lnnystignl satyifspkf dlmvrsgvdm saedreqrrp
      541 fstanfqygy ykeqsifdye vntdalltyr dkigslvdvr asvggnmmnr kykgtngvvd
      601 glvipgvykl sngistpmmt tlhrnkrvns lyalasfsye dkifvdvtgr ndwsstlpvq
      661 nnaffypsis ssfvltdlfa lptqvsfakl rlsaaqvgnd tdpyktrkyy gqsdfagsgs
      721 vpttlhnvnf kpeittsyea gleymlykgr igmditlyks ftrnqildvp ldpttgysra
      781 vmnagkvrnq gvelvlnarp idnaffkwks slvwskndnk vlelaegmdd qqiigsggqa
      841 tiiakvggtt gdiygygfvr spdgqivyda aglpaypdet qyignayadw kggfsnefsy
      901 knfrfsflld gqyggiiysq thhkmseqgk lkhtlmgree gyiigegvvd ngdgtyspnt
      961 tkvspmeyyk ryyrranves nsfdasylkl remrleynlp ksllnrarfl qgasvalygr
     1021 dlamltnfpi fdpetaalng stilpgveig qmptprtygm nvtlkf
//
LOCUS       WP_114778425            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Botryobacter
            ruber].
ACCESSION   WP_114778425
VERSION     WP_114778425.1
KEYWORDS    RefSeq.
SOURCE      Botryobacter ruber
  ORGANISM  Botryobacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Botryobacter.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Botryobacter ruber"
                     /db_xref="taxon:2171629"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121317
     Region          33..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksintlilc vlvgtaillg ntawaqtkag plirgtiidk qtkesligvv vmevdsdqrv
       61 ingantdlng kfalktsdak nsirisyigy ititqpigns telniqlqpd sktlgtvevv
      121 aqqavrtgml dvaerdltta iakidarela evqatsidqa lqgrlagvdi vansgdpgag
      181 mairirgtss inqgsdplvv vdgmpyditi sddfnfatad eqgyaqllni aptdikdiav
      241 lkdaaatamw gprasngvlv intkrgakgk ptvsysfkgv vskqpdaipm ltgdqysmli
      301 peaymnrdgr plntnsikef qydpydpywy ynysnntnwi eeitrtghqq dhnislqggg
      361 dkatyfaslg ynntvgttig sdlsrinari nldykvsdri rfrtdlayth vdnnmnyssn
      421 lrsiaytkmp nmsvieyden gvptgnyfsp elnvqgrysg tynpvamame gksnnvgdri
      481 rptfnlqydl ipsrllttfd vafdinnskt trflpqtatg lpsdntnvnr aedidndrfn
      541 vqtktniiyt pelgenhnlq alfslqtndd rnvsyavtta nsastyfqdp tapsriqnpd
      601 lrlesgmaqs rtvgavinaq yslldryiin gglrldgnsk fnennryglf psisgrwris
      661 gesfmqdisq indlslrvsw gstgnpprns yshfaqyrsf dwnymglsgv ypmdlelrnl
      721 kwetviqtny ginlrafdnr leldaeiykk rtldmfypgl qissisgfns vdmnvgvmdn
      781 ngweimagvt pirskdltvr fdfnisrnfn iiqeiseyyp rergniyqng qykifmqegn
      841 pfgsfygfry kgvykdaeat vardkdgnqi idangapiym rfnyptfdyl fqpgdaiyed
      901 inhdgninym dvvylgnanp kltggfgpni twkdfrlnvf fnyrygyqii nqtkistenm
      961 sgynnqstav lrrwrdigde tdmpravigp nynslgsdrf vedgsfirik yitlryslpa
     1021 vlanqvhmkd lalfttieni ytftnytgqd pevsyrgndp frvgydtsmt ppvktltlgl
     1081 narf
//
LOCUS       WP_114778489            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Botryobacter
            ruber].
ACCESSION   WP_114778489
VERSION     WP_114778489.1
KEYWORDS    RefSeq.
SOURCE      Botryobacter ruber
  ORGANISM  Botryobacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Botryobacter.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Botryobacter ruber"
                     /db_xref="taxon:2171629"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112309
     Region          29..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiykkvvl gaiatvlpvm mhaqttdkin iqavvrdakg nplrgvvvkn eldnsitavt
       61 dslgaftlst spnailtvga sgyksksvva ssdlseitia ldqynrpvqv ahrkvdqkdl
      121 ttevtvvdvs emleknytts slqnmeglan gfhgniwgmd eylvlvdgvp rdagsvmpte
      181 idqitflkgv savalygsrg akgivyittk rgvvgdlqir grvnsgihvp ksypkylgsa
      241 eymtlynear rndglsdlys estiynhaig enpyrypsid fyspeylkkt ynrhdatvei
      301 sggnqkaryy tnigfntegs llnfgealkh nsndrlnvrg nvdvsitdni yakvdaaaiy
      361 ynqrgvntny wqsaatlrpn rfaplvpism ieandeasli lannssniid grfvlggtql
      421 eqtnpfatiy aggnsqftsr qfqfnttvga nlsnvlqgls festigldya tsytqsfnnd
      481 yavfaptwns yagydqitsl tqfgtdartg nqnvsgstfr qnlafsgqfn ylntindnhn
      541 isamlvangf qlsnsgvyhr tsnanlglhl gydfknkyya dfngalvhsa rlpeanrqaf
      601 sptvslgwri seedflqgss vvdnlkltas agrlytdmsi ndyylyteny nqtegswfgw
      661 rdgslsrttd srrganpdlt fakrdevnvg ldaslfnnlv nfegsvfank mtgnvvqtpv
      721 lypsyfvtgf pnanflpyin ynddqrvgfd ynlrlnnkln elewtvgfvg syykttaikr
      781 aeffedeyqy regkpldaiw glqsegffts qdeiesspkq sfgpvqpgdl kykdqngdgi
      841 inaqdevflg rggwygsplt lglnltakwk nftffalglg rygayamknn syfwiagedk
      901 ysevvrgrwt eetketatfp rlttlgrnnn frnsdfwlyk nnrfdlakiq vsydlpqrvf
      961 gnsfiremgv yasgfnlltv skerelmemn vggapqtrfy nlgvkalf
//
LOCUS       WP_114779364             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Botryobacter ruber].
ACCESSION   WP_114779364
VERSION     WP_114779364.1
KEYWORDS    RefSeq.
SOURCE      Botryobacter ruber
  ORGANISM  Botryobacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Botryobacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Botryobacter ruber"
                     /db_xref="taxon:2171629"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39996
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mniavlketr vpesrvaltp dvvksltkag fkcgiesgag vasgfydkay eevggvifad
       61 kaallenaav llkvnaptve evlllpdgsa visflyayti pevvdicvkk kisafamdav
      121 prisraqkmd alssqanlgg ykavimgana lgkifplmmt aagtitparv lifgagvagl
      181 qavatakrlg avvevtdvrp etkeqveslg grflevqaeg vkteggyake vsaeylqkqk
      241 eliskhiaea dlvittalvi gkkapmlvte emvksmkpgs vivdmavesg gncalsqfnk
      301 tvvehgvtiv gkvnlpalvp vnaselyakn istlllhlan kdgfkwemee eitkgslith
      361 qgalvhqftk dilqtqkv
//
LOCUS       WP_114782341            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Botryobacter
            ruber].
ACCESSION   WP_114782341
VERSION     WP_114782341.1
KEYWORDS    RefSeq.
SOURCE      Botryobacter ruber
  ORGANISM  Botryobacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Botryobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Botryobacter ruber"
                     /db_xref="taxon:2171629"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117042
     Region          32..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpftkftifs khliatlfll lvcccsllaq sqtitgvvsd skgqplpgvt vvlkgttvat
       61 stnmegaysl tipkaltsqd ilsfsfigyk tsevayngka tiniklqvnd hvlsevvvta
      121 lgiereqkal gyatqtvsse slndarsnnf aqalsgkvag lslispgsgp vnstrislrg
      181 dnslnpdgnn alivldgvpm ssemtssgvs saygagsgnd vpidfgngia dinpddiesv
      241 tvlkgpsaaa lygsraanga liittksgsr kqkgigvtvn tnisindvlr wpdfqheygq
      301 gtenlnkegq pyysyrased gantgstssa ygpkfdgqyy yqydptlegq saerqlwrpy
      361 kdnvkgffrt gstitnsvav eggtdkgsar asithsknew impntgferl taalslnyka
      421 sdklrlnskv nfthkksdnl patgynnqsi syfmifqnpn vdlawykprw ksgkeqvdqi
      481 hpfssyidnp yviayemtna lnnystigni satyefspkf dlmvrsgvdm saedreqrrp
      541 fstanfqygy ykeqsifdye vntdalltyr dkigrivdvr asvggnmmnr kykgtngvvd
      601 glvipgvykl sngistpmmt trhlnkrvns lyalasfsyd dkvfvdvtgr ndwsstlpmq
      661 nnsffypsis ssfiltdlls lptqvsfakl rlsaaqvgnd tdpyktrkyy gqsdfagsgs
      721 vpttlhnvnf kpeittsyea gleymlyngr igmditlyks ftrnqildvp ldpttgysra
      781 vmnagkvcnq gielvlnvkp idnrffkwks svvwskndnk vlelaegmdd qqiigsggqa
      841 tiiakvggtt gdiygygfvr spdgqivyda aglpaypdet myignayadw kggfsnefsy
      901 knfrfnflld gqyggiiysq thhkmseqgk lkhtlmgree gyiigegvvd ngdgtyspnt
      961 kkvsplqyyk ryyrranves nsfdasylkl remrleynlp kslltkakfl qgasvalygr
     1021 dlamladfpi fdpetaalng stilpgveig qmptprtygm nvtlkf
//
LOCUS       WP_114782930            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Botryobacter
            ruber].
ACCESSION   WP_114782930
VERSION     WP_114782930.1
KEYWORDS    RefSeq.
SOURCE      Botryobacter ruber
  ORGANISM  Botryobacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Botryobacter.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Botryobacter ruber"
                     /db_xref="taxon:2171629"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121371
     Region          64..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktvyplkrl llpclllgtw qlslgqglas agnlasdnqd kitaflvqrd traaailaaq
       61 qnmtvvgkik deqgqglpgv tvvlkgtskg tatdvngnfs ltvsdgsgtl visflgyktq
      121 evpinkrssi dvtlspdaka leevivvgyg gtttrgattg avdainakei edlplgnlga
      181 alqgrvlglg vsggtdrpgs qaqlsirnpg sfsnaqnnnp lyviddviqv nsqnapdptl
      241 fnsldpseve sitilkdaaa amygsrgang vvivttkrgk egppritysg syavndeayr
      301 tkmlsaydma ryvnimngpn ganrdagdnr yffgddeleh fkninydwld eawqasyntr
      361 htlnvsggtn kstyfanvay ftqngnmgkl dydkwtfrag advnvmagmk vglqvagnfq
      421 ntlkmnskig genaendynn lllapryvpm yidglpvrlp gsgnnlsayh ffeldkgdny
      481 mdnddkgtli nlyaeyeapf lkglkakvsy arnmtsgrsa riggqyylys ftrtgsrghi
      541 yegatdpvat kftndnrirf mnenalstql nfalnynqtf gkhtvggfft vergetesnm
      601 eevwkedpia gtngqfgtaf geidgrtygy qsgnmgyigr lnynfdgkyl mdfmfrsdas
      661 tkfapenywg kfyslgtgwv iseenffnmd ainmlklrys vgllgkddtk mwewrqrytf
      721 qggkapvfgd ntpkgtgikm easpnraavw sdelkqnigl darflnsrls atvegfynka
      781 tnmlmvvtgn vpvtlggtsa aqnfgamntf gyevslgwdd nigkdfrygi egrfswydnk
      841 iikhnfiend llypwktprp gqstdngvwg ydylgmfrdq aeidayveqy nikqvfdqta
      901 nnlrpgmlyy rdvrgplqad gtfagpdgvi ddndqiqlak rasshnnfgv tlklgykgls
      961 fdavitgsfg gwseidarsr mqgdisnlyq nmpaywnniy dpelnpggtl pnphfssvsl
     1021 sprstfyqvn afrlrmpnfn lsytlptkla damhvqnari altsinpitf ynpysyksae
     1081 gswenypvlr tyslgvnltl
//
LOCUS       WP_114782913             989 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Botryobacter
            ruber].
ACCESSION   WP_114782913
VERSION     WP_114782913.1
KEYWORDS    RefSeq.
SOURCE      Botryobacter ruber
  ORGANISM  Botryobacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Botryobacter.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Botryobacter ruber"
                     /db_xref="taxon:2171629"
     Protein         1..989
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106168
     Region          32..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqllskelk yllvlpflll tittalaqal evrgkitddk gvgmpgvtvl qkgtsngtit
       61 dtdgsfrlsv tdgnavllvs yvgyqnqeip vnrrsainvs lktdaqalee vvvvgygtak
      121 vkdvtgsvar vgakdfntgi naapeqliqg kiagvnivnn sgapggevtf rirgtssvrs
      181 gnqplfvvdg vpldgrntkp satagelggt agsnplnfln pndiatidvl kdasataiyg
      241 argangvvii ttkkgsqgap tvsldmstgi stltrkpdim dgntfrqala hrqienrdgg
      301 qsvdafdaim rtahtqmvna slsggndrss yrislgyhdq egiikesglk kytgnysgty
      361 kflpedrlkv dlnlvvantv engapiaens nvngsligna iewnptvpfr dadgkfvqrt
      421 ygtsvaglpt npvalleyyn dvanvtnvlg saaatfnivk gldyraslgi nqskgnrivd
      481 vsgnlflsti tdiglavvnn atltsstlth tlnynsklsd ninldvlggy eyqtyksntf
      541 ditargftsf dlkgtdilqn artdqvriss ykdptnelqs yfgranlnia ekylltatmr
      601 adgstkfgen nkygyfpsfa aawimseedf lkgieklsml klragwgqtg nqefpagasq
      661 eryafglqsi alsnvanpnl kwettetvnl gldfglfknr itgtveffdk strdllfrlp
      721 alqpapaasy wtnlpatvkn tgvevllnsi lvenanwtwe fgvnatylqn kligyegapv
      781 ltgqingngl gggsnsqqla dgqplfafkm lefmgfdeqg katysdeqkf vgdpnpnyll
      841 gintnvsrgk fsfsmnmnga fghhlynnta nalitaanfg lgrnasseig lgneslsnan
      901 vvstrflesg nfmrlqnatl gytfgnitpv lknariylag qnlllltnys gfdpevntnr
      961 svngvpsfgi eytpypmars ftlglnasf
//
LOCUS       WP_114783025            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Botryobacter
            ruber].
ACCESSION   WP_114783025
VERSION     WP_114783025.1
KEYWORDS    RefSeq.
SOURCE      Botryobacter ruber
  ORGANISM  Botryobacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Botryobacter.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Botryobacter ruber"
                     /db_xref="taxon:2171629"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120432
     Region          34..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrliqlpfy gslavallll lnfgsyaqnt gvgktikgnv sdkesgitii gavvteidke
       61 grivngantd ldgnfvlkva npanklavsf igykkivqei ggrtvfnfkl essanqlqev
      121 vvvarqtssn glmevekrss tvsvakidar eleemssssi dqaiqgrlpg vdiaansgdp
      181 gagmqirirg tstingssdp livvdgmpfe teipsdfnfg taddqgyatl lniapsdime
      241 iavlkdaaat avwgsrasng vllittkrgr vgkpavtytf rgtmakqpqp ipmltgdqfs
      301 mlipeavmnr ngaplnteqv keflydisdp yyyynygtnt dwldlitqtg ykhdhnlsls
      361 gggekaryya svgyldetgt tlgtglsris trinldydvs srlrfrtdia ytntdtdrny
      421 snnarsiayd kmpnmsvyey dlqgnntgly lsplrniqge yprtynplal ltmginnvrs
      481 eriipkfnlq ydivpdllrt tfdvqfdidn tksstflpql atgrpmsetv vnraydgdvd
      541 rfgiqtktnl iytpklgenh sliglvsfls ddnkvssvql qssnsasafl qdpsaaariq
      601 gmssgyshgr svallgnvqy syldryifna alrgdgnskf gpdnryaafp slstrwrvsg
      661 epfmqqfgfi ndlslrasfg qsgraprnny sfysvygnyd wdyiggpavy pqnmelstlr
      721 wetvtghnag fnlimfknrf dvdvdfyrmr ttdlyfpdlq lpgisgyssi nmnvgtmdnq
      781 gwevniqgtp iktkdwtvdl nfnisrnvni ireisefypr ekgnsaangq yksflqentp
      841 fgsffgyryk gvysdaeatv ardkdgnaiv gldgeplfmr fnypytdyif qpgdamyedi
      901 nhdgnidyrd vvylgngnpk figgfgptit yksrlkltaf fsfrtkyqiv ngtqmnttnm
      961 ygydnqstav lrrwrnpgdq tdmpralwns gynwlgsdry vedasfvrlr altaryalgk
     1021 nalskikmkn asvyvtaenl ltftnytgqd pevstrgtdp frvaidnsmt pptknivlgf
     1081 svgf
//
LOCUS       WP_114783021            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Botryobacter
            ruber].
ACCESSION   WP_114783021
VERSION     WP_114783021.1
KEYWORDS    RefSeq.
SOURCE      Botryobacter ruber
  ORGANISM  Botryobacter ruber
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Botryobacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Botryobacter ruber"
                     /db_xref="taxon:2171629"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116424
     Region          50..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myivtrsikr lmllglvvit vpamaqettt egrsgadava vrknisykgi katgtvrdaa
       61 tgvplagini svpgysaaft deqgnfsiev psykatlhvs spdfqtrqva lkgenvvvvg
      121 lheksfntvy eaavlpsgar aksqvpyavt sintagswqn pmafpdsylq gkaagvdvir
      181 ksgtpgqgae illngynsly gsnkpliivd gmiyehesfg sslikehsnn plsnidikdi
      241 dnitiikdga slygtkgang vilistsrak elatkidfaa yggvnfapkn lpvlnngdfr
      301 lylsdllrts gmtdaqlqaq pymnddpsnp eyaryhantd wqrevmsnsy nqnyylkvtg
      361 gdniakyals vgflenqglt ketslqryst rfnadlnlsp kltgntslsf tsnqqslrnq
      421 gldfgtnpll aalvkapflr vqqvtdegve spnladtdif nrsnptalin stqgqdqnyr
      481 ffgsakfnya lstystissl igltfdkvre difiprlgva peeldnaiay srlgnrvqry
      541 nslfndtyya ynrnwsgghs ftgragfrfs nikseedrsy gynspsddfv tlgtgvnslr
      601 yitgdmgear wlnsyvsady gwlskyllsv nmsvdassrf gpaipdafsv ngmklavlps
      661 vaaawlisse dfmagisavn llklrasygl tgnddignyt akqyyitqnl fgaqgtrrgn
      721 ianpeimwet trklnfglda svlnerlsls ldvfnsrttd mlvyepvpaq tgldymltnn
      781 ggmknsgina glfsrvvntg dlkldlglnl styrneltqi pgnrlltnfa gatilseagq
      841 panllygykt dgiftteaea aqanlktkap ngdlipfrgg dvkfldlnnd hiidendrtv
      901 ignpnpdfyg sfssnlswkr fsvnalvtfr sgndvyngvr anleamnstq nqlgsvnnrw
      961 qfdgqntdmp ratygdpagn arfsdrwied gsyirlrtls vayelpvkpg fikgtsvyas
     1021 annlltrssy igydpefsaa srpvaqgidv gleplyksfm vgvrlgl
//
LOCUS       WP_114786202             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            tetraodonis].
ACCESSION   WP_114786202
VERSION     WP_114786202.1
KEYWORDS    RefSeq.
SOURCE      Vibrio tetraodonis
  ORGANISM  Vibrio tetraodonis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio tetraodonis"
                     /db_xref="taxon:2231647"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54276
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp ksveqllklg fsvnieskag elasfgddaf tasganivtq
       61 devwlsdiil kvnapsdkei elikegatlv sfiwpaqnte lmeklsskki svlamdsvpr
      121 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvlv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfkees gsgdgyakem seafnkkaee
      241 lyaeqakdvd iivttalipg kpapklitkk mvdsmrpgsv vidlaaangg ncaytkpdkv
      301 vttkngvkvv gytdmvgrlp tqssqlyatn lvnllkllck ekngninidf ddvvlravtv
      361 vkngeitwpa ppiqvsaqpt qqqtkevskn tekkdqpvsr tkklaalgvg lcsfawvasv
      421 apasflshft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgngav
      481 sflafiaili asinifggft vtkrmlemfr kd
//
LOCUS       WP_114789037             976 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114789037
VERSION     WP_114789037.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..976
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108951
     Region          21..972
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgtfiaiil iamsvtqlya qtikgtvrdn kgaplsgisi lvkgsnigts tnadgaytlt
       61 lsetakagtl ifsgigykqt disinnrtei nvileandvg leevvvmgfs evdrkhiass
      121 vsqmdmekik nrpifkmqda fsgtipgvtm mrgsslpgsv pgtisirgis tlgaadplvi
      181 vdgmeqsihd idpnqvksit vlkdaasasm ygsrgangvi iietdrgqtg qfkvytnnwy
      241 alnkpidlpk fvggaefmkl rnetllhqgq pavysqeeit rfesgerkdv nwldeimqrn
      301 stalnnnvsv sggggvgtfn lmlghikeng lndiegtqkf sarfntnini adkfvlmadf
      361 yahrlqvdrl manddghgly klawrmnptq avfydvdrpd pyilhnninp vasitrggiq
      421 nnmydrstin lrpkynisrn lnieanvsym inksaekler ktfkffdenn apvtiwtnsv
      481 satqgvsesq ltaralinyn kklrkdkdki yltagsevmn ytytdyreis kssffgklny
      541 sfdnryilel tgrsdgsskf apghrwgffp sggfawnvhn etfftglles gaitnlklra
      601 syglignenv gpylwqesvn nygwmirvpn pefswekqkq wnlgldltal ndrlsftaev
      661 yrkmsydliy dqfsvppltg sntlvsavni gsvenkgwel sanwsdkagd fsykiggmlf
      721 dnrnkmlkag ytdmdslifk gnndriwykg ipinnyygfe tdgffqtree idataakmpn
      781 tlpgdiryvd qngdglindq drvyladplp hfnyainldl hykswdfsal gqgigkrtgr
      841 lmgqeaypvy vdgnsnnlga prveyvashw spenpdsrfp rlwtgptsnt llsdvwlsna
      901 affrvkslql gytfpkigrs fknfriylna qdvftitkwe gldperidvd spgtndgngn
      961 yprmatysfg istsiy
//
LOCUS       WP_114789101            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114789101
VERSION     WP_114789101.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114184
     Region          30..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mllistlfkr tssflivllm yniccaqagk mlrgkvldef ghplekirve dkgshktves
       61 nedgifeinv svpatlyfsg tsidaaiynv sgsaddivlr lqnrylvksd sldvlygrqk
      121 kelflgaaat vhtpqlsttp atlypyaltg rlaglyteqi qgyrtfsgts dansvsdlag
      181 tlartglepf sdnneislkl rgqnsvvvvd giqrnifsld pqsiesvsvl kdglsaialg
      241 qrssrglllv ttkkprmgpp qfsftaevgt qqplsqpqpl dafnyaylvn ealqnegrkt
      301 lytvgdlegf ksganayryp nvnwydqvik ksaplyrynl nlgggskvar ymvslsymnq
      361 egllnvqnpd aklqleryli nskvdidvtk yfnigvqlfg riqdgnqpga tvgsilgnll
      421 ttpnnaypvy npdgsfggnn sfqqnlrsml dnsgymmntd rdimanvdmk ysfdkwtkgl
      481 wvklkgnlsv qsatitdrsm rvpvylmqvg gdngdttyar ygsanaqvnn fyavsnaryw
      541 yaqgelgysk iinqhsftgs vmadsrrvtl nfdlpgtatn ymaklqynym ekymlegaln
      601 ysgydryppg qqfglfyaag agwniakenf iknnatwidl lklratyart gsgvdnsgyf
      661 twrqtyassn dqtgiagidh vraqiavaen glantgitwe kgnkfnagld valfknhlsl
      721 nadfyrdvys dllqirgksi aligtgypwe nmgknlytgg elqityqnni aafnyfftan
      781 gsleknrvlf mdeqqrdypw nvatgkpvnt rfgyiadgff qtdeeaqsga viagyeikag
      841 dikfkdlngd gmidqfdqta igtdkpllyy glttgfnykg lgfsillqgv knrdlyidnw
      901 nteilrangq vygqmyehll nrwtpetaai asyprlkang gfgdgyslss stfwmhsgdy
      961 wriknvnlqy tfpfswtsrf kvsaitafan aqnlftwaay drvdpevgyg aypiqkvynm
     1021 ginikf
//
LOCUS       WP_114789122            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114789122
VERSION     WP_114789122.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114391
     Region          34..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntklllgpy flctlfiflf ipmlvgaqdg rtdvrgvvrs eggdllrgvt vviknaradf
       61 tvstqtdslg ifrfsqlpag egysfsissv gfepqeltgy qlkananftl siklketgqs
      121 lnevvvigyg tqrkgditss vasvkaedfi kgavkdagql iqgkvagltv inpsgdptgs
      181 tqlilrgqst lmgvnqnplv lidgvpgdlr mitpqdiesv dvlkdgsaaa iygtrgtngv
      241 ifittkraga nnrtsveyst yagiqkiarq ltmstaadmr aqiesgqrkn elidqgaatd
      301 wlkeitrtpv iqdhnltirg gngvtnylas lnydnaqglf lksfnqifsg rfdinhsmfd
      361 nklklnvnaf sssrrlngfn sniyrqalmq nptaplkned gtwfqeltkf dyqspvsdim
      421 esdgetsesl sryngtisfl pvkglkfsal fsyskwmqky gyaetkqhas tlrdgrngya
      481 ndggaqsidr lteltgeytk sfnrhnltal agysyqendy tnhymenwdf ptdifswhni
      541 glgraissge fvglirnykt etnlvgffgr lsynydqryl lmaslrreka sqlwgtrnpw
      601 gvfpavsagw risrekfmqn qnvfddlklr vgygvtgsqp sdlfrgvall gysgfvlsdg
      661 kwvqtiiptq nanpdlkwee kretnigldf smlkgrlsgs idlynrqihn llylfevpsp
      721 pnlynrtlan vgtlenkgle vlvnftpvmr knfqwnsmvn fstnsnklks lsndlyrtst
      781 dylrvgaifp piqtfshllr vggsvgdfyg ykvvdigndp adaanygqwi yegrdgtpvk
      841 yadfahafed kkvignglpr yyltwnnnlq ykswdlgitq rgafkfqvan lqrmmfenpt
      901 qaqynllkna ydpvygkavl kspvefnsyy iengdfwkid nitlgysikt dkikyiksar
      961 iyiatlntfi itgykgidpe vslrngtssa qsgvlqvpts gldpgmdspy kypttrtfsi
     1021 glnvnf
//
LOCUS       WP_114790038            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114790038
VERSION     WP_114790038.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118866
     Region          22..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrlllvllt vffchvlkaq tkiitgtvld edeapisgvn istqdskkta qtnaqgkfti
       61 tipaeenill tftstgyksq taagldgmti tmvknvvsee dvvvvvdygy gkikksdltg
      121 svatlsgkdl akipmasaas altgrlpgvr vlttdgapda dvsirvrggg sitqdnsplf
      181 vvdglivssi rdipptdies vnvlkdasat aiygaaaang vivvttkqpr agrvsvsyng
      241 fyqmkklped rklkvlspye fvlanyehnr lqsdaavrsf etffgayddl elyknkpand
      301 wqdilfgspr asqyhnltls ggtamtkvfl sltnnkdegl linngfkrna lnfkldqkin
      361 eklsvglatr itksvvdgag tssaqlsikd avqtrptngl ademviapgn idpnddfaqf
      421 iqslvspsel vkqdwrkrtt qdyvlnptle ykilsnltfk snysyaktfd enlrfygplt
      481 gesfnnggnm plgektdqen fsyrwfntln yrfrnlknqt ldvllghets ssggkstfir
      541 sedfrlsitp eelfanmafg rtdrlqtgna tngnrvsgfg ridyqllnky matftfrgda
      601 ssrfskenrl affpaaavgw kisnekflsg vswikelklr asygatgndk ipttasqflf
      661 tgttnrgpgf gnvdnvyytp egsvlfnpnl kwettinrni gldftlfrst itgsldfykn
      721 tvkdllfqta iptntgfgaq wanigsnsne gielglnadi ikrkdllvsa nfnigrnvgk
      781 iveldgtnsr fqqsnwastd lrdrddfyfe vggrignvyg yvtdgyyqts dfesydevsr
      841 ryilkegvpn sggtvgngnv rpgflklkdl ngdgvinsed rqvigntlpk aqggfgfdvt
      901 yksfdlsiff dwtygndvyn agkiqysqfr rvtygnllda mslenrfsyl dvdgsytgtp
      961 ggivtdltql aemnankniw shashgvaqa vihswaiedg sfirlnnlnv gyslpkkwis
     1021 kigmnqfrvy ftgnnlklwt kysgydpevs trgngltpgv dnsgfprsrs ftfgvnvtf
//
LOCUS       WP_114790145            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114790145
VERSION     WP_114790145.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117115
     Region          25..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgkilsfff vvfccyplvl paqtrqvtgt vrnsagepvv natvsqkgsn nstvagedgr
       61 ftltvtgvnv iltlsavnyq nteinagtqs afevtllest gtkmdevfvv aygtakksty
      121 tgaatvinas kikdvpttsf enalngrvag lqitqtsgqa gsapalrirg igsmnasndp
      181 lyvldgvpiv sesvgqmgsy lnttnniman inpddiesit vlkdaaassl ygsraangvv
      241 iintkkgkig apvisfktsl gitptwatdn yeaagvqeqi nmlyqvfydl nitggktpea
      301 antdalsrln srfnrhgyrf etsgtdryqn vailgmtdgi enregryfnw ddvlfrtgff
      361 ttndlsvsgg tdktkyyssl sytqdksrva vnefqriagr lnltqkigsr lelesnigis
      421 kndksgfnds rstgsnymlq srnllwpvyw ptdyktglpf tarfgslaqn nvyydnewdn
      481 tagtlnisav ealtvnilsg ltaksifsyn nsqikehlyy salhfsgvap vngqvhelst
      541 ninkmvsstt lnynkaihqh sigvlagyea eknltdfmrs sgnnlpsssl ptvvtagttn
      601 asaynwgynm qsflsraeyn fsekyffsas yrrdgnsrfg pvnrwanfws vggawnifke
      661 dflkenelln elrirgsygt nattpsanyg wrtllsftdk ymeqpggsiv siadsglawe
      721 tnyntnlaie fgllerrvtg sieyfnrdsr nllmdvpism vtglpstlkn vgeinnrgie
      781 wnlgvdivrk ehlkwsvgln gtimnskvtk lnrqegasvg qdiiwndptg ndaraqfiyr
      841 egqsmlafyg fewagvdptn gknvwyindp nspttgdfef ngrgatytys kanriiigng
      901 tpkmfggfts dleykgisln lnfiyklggd lydgaykdva ddgyywerir sqdyydnmwt
      961 dnntsgtlpk lsgndltdpm qystrqlhda sflrlknatl ayrlpgnllg gigvrnarvf
     1021 vngtnlftaa kykladpevn qfatrgweip faktytfgie vsf
//
LOCUS       WP_114790408            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114790408
VERSION     WP_114790408.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120176
     Region          28..94
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          112..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklsllflgl alqvsatnyg qsislreehv slneifkkie kkspyrfyfs sdvlpqkhft
       61 svyadkasle dvmnkiltgv nlswkqlsgn rvvitenlpl saaattakti tglvtdntga
      121 alegvsvvik gtstgvvtsa tgrfsinane gdvlvfsrvg yqeqeiavga qdiidlilqa
      181 tqgslseviv vgygvqkkgs ltgalqtvtg nqlrdittps venmlngkvs gafvapgsgr
      241 pgsrgavvir gqatlsgtts plwvidgviv gsgagdlnpd dietmtilkd aastaiygsq
      301 gangvvvvtt kkaragktsl nystrmgvst ltngnlkmmn gaelydyyas fanagtisfp
      361 rwnanlrnsn fdwwdlavqn gftqnhnvsi asgteklqsy lsvgyydekg avkgydytry
      421 narltqvykp lkwlqvkpai vgsyrhvknr eysttamysn fpwdspydsa gnlvghrssl
      481 wvnsagtnyl ydlqwdhsen knyelmgnld fevkltnwlt fssvnsyryn tysasgysdp
      541 rsnsglnvkg rltdyrdeya rrytnqmftv nktwdrhvly avagyefndy yaktldvygt
      601 gfipgfevld vvakpertkg ninewavqsy lskanytydn rylleaslrr dgasnfgdna
      661 kygnffsvsa gwninkerwf nadwvnvlkl rasygsagnr pntlypqysl ysvstaasyn
      721 edpgalisqi gnkdltwert yttgvgvdga ffsnrlrltl dyynkntdni lymvpisglt
      781 gvtsiwrnig emnnkgievs lggdiirned wlwsldvnlg hntnqltkly ptknadgtys
      841 vkpviigdgl giagsaqrvl epgrpvdtyy lkewagvnpe ngsplwykvq rdangnetar
      901 dttsryaqat feklyrasps ffggfstalq ykqfdlnavf gyavggkiyn ysrqeydadg
      961 tytdrnqmkl mpewsrwqkp gdiathpvar ynnnsqanqm ssryledrdf lrlrsltvgy
     1021 nvklsrfhvn nlrvffagen lfvitnysgv dpeipandga vlsstgpsvy patrrymfgl
     1081 nvsf
//
LOCUS       WP_114790531            1211 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114790531
VERSION     WP_114790531.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1211
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131683
     Region          161..1210
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mllklnrvll fiaifiscsn lskaqningk vigktgigls dtylyktgsa dtaktdmdgi
       61 fslkankgds iqirnsllnl nlffvapatd svlinikdns eievgpwkks ssikdtiagq
      121 aqtvvdsakk qaatltdsta agknsvattp avtnngdtvf ikgtvtnsag eplpsasiey
      181 pdgklytaga dgsfsipfip nakvrfsavg vaaqermltt adaltiqlqq tapeqleevt
      241 vtalgiskks ravgyavsev dgsdiqtake tnfvnnlagr vagvqiatnt gsmggsskvt
      301 irgpksilgd nnalfvvdgi pfsnlntnsy gqqiggggfd ygspiqdinp ddidqisvlk
      361 saaatalygs rgqngvvlvt tkktnggknk igvnyslnvq tdkvyvlpky qnsygggskt
      421 tfdtlfynkn peqflsgnsp tyndpvlggy dllpeygvde swgpaldgrl vrhywsfdre
      481 kgnpdfgrta pwspnpdnik sffetgltvt nsvsvggsnd kgairigfad trqrfvlpns
      541 rlsrtnlgln gtykiadnli asagvrysyt kakgrpgtgf tgqnvmnlfs eygqrqwdme
      601 rmkdyqyadg sqiswnrtrf dnpkplfann pywtrfmeyq nddrsrlfgs vgleykpldw
      661 lsfnaqafmd syntlqeers akdyfvgsya rntidfrevn ymfttnikkd lgerfnlgat
      721 vggnimkqtv rlftgstpag aglitpgvyt lgnisappti iesmprkqin slfgttslgy
      781 nntifleltg rndwssalys annsyfypsa stsvifsewi qdakwlsfgk iragiaqvgs
      841 dtepyrilqt ysspqlfngv pyltaddikn sinllpektt ekeagielkm fnsrlgvdft
      901 yydritrnqi ipvnvsptsg ynqfvinags vsnkgielri dgtpiqtenf kwnigvnfsk
      961 nrnkvvdlaq ngrevvdkit igterrlnqv sivavkgqpl gtlvgfdyty lngqkvidtl
     1021 ghyvktstvv plgsvypdyv ggvsntfayk nvtlsalvdf sqggkffsyt nmygqysgll
     1081 eetaagnire ngvnvsgvlk dgtpysktis andhfknnfg rninaanvyd asyvylrevt
     1141 lgyqlpdswa qkisannitl slygrnlwli ksnapnvdps aitngtgniq gleggalpsi
     1201 rsmglnlnig f
//
LOCUS       WP_114790613            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114790613
VERSION     WP_114790613.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116120
     Region          42..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmyksfkpvl tvamtlllfa tgsaqttdsl nqkkvpvale ervvtgvvrd aatrwginga
       61 rlqvqgfsat iadsvgqyti kvpaptaiil veadgydpqv vsvkhrdqie vvllsrstks
      121 fnetmvtptg rlvrkfitsn aeqvmakgwq qpmetvdaml qgevaglnsi rrsggqgaga
      181 nlflnginsl yatnrpliiv dgmpfeandy gqslvannyt nplsiidvkd idritvlkda
      241 agiygakgsn gtiiittvsa egrqatqida gvfasfnvap qnlpllnvsd yrshlsrmla
      301 tsgmtaeeia aqpfmvdnvs spdyykyhnn tdwqrkvfnn smnqngyvri tggdniatyg
      361 ltvgylkntg iikntelery htrfnadfnf tekltgkvnl sfsyneqnlk dqgiadktgp
      421 lfnalvkspf ladreraadg tespnleavd ilglsnpvvl tdllqasnky yrffgsygfk
      481 feinkymaas tligiqfdkv retffvpseg vvrdtlwnav annrmgsqvk qlfslfndtk
      541 leynrnfnyn hsvtarlgir yqnnranqis vttansatdd lvsvqnglaa lrlvtgdmge
      601 wnwmnaylga dygfknkifl slnmamdgss rfgvkaangl siagrqfplf pslgaawlls
      661 sekfmsasdi nllklrasyg iagnddigny tglflytgqn llgaqgfvrk gianpslqwe
      721 tvhklnggvd lafwnervtf sldafsnrtt nmlvyrplqs pagfstvltn dgelknngve
      781 gsfnvrvvnt kdvkwdfgan iatyknkivs vpggeiftef agatirtaag qpanqfygyq
      841 tngifssnae atsaglsmvn ekggttafkg gdvrfvdmng dklidendrt vigdanpdff
      901 ggisnrliyr gfelsality svgsevfnyl ryrlesqsgp enqlqsvlns wrtdgqqtnm
      961 pranwgdpmg nnrfsdrwie dgsylrlrsl nltynfkmkp gapfksiavs atgnnlftvt
     1021 kylgydpefs pfpsplaqgi dtgmdpvfkn vvlgvrlgl
//
LOCUS       WP_114790839            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114790839
VERSION     WP_114790839.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122538
     Region          31..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrfdmknif vlcatlllmv vgekafaqda ivltgkvidk qgapvsgvsv setdneqrtv
       61 rgtttdidgn faikvsdvkh rltfsaigyk sredmaintr rifnitleqs sndmeevivv
      121 ssartdngml piperyntla tskinakdle emqatsidqa lqgrmagvdi aansgdpgag
      181 mqirirgtss inssttpliv vdgmpfetdi ptdfnfgtad dqgyanllni aptdikditi
      241 lkdaaataiw gskaasgvlv intkrgvrgk psltytfkgt isprpeaipm lsgsqytsli
      301 peafmnrngi plntqtvnef kfdpndpyyy ynysknsnwv deitrtgyvm dhnlsmtggg
      361 skakyftsvg ylnqdgvtvg tylkrltari nldydvsdri nirtdvsyat tdnnrnyaen
      421 lrdvayrkmp nmsiyeydey gnltpnyfsp fsniqgqyng lsnnkvsgtv npvamanaai
      481 nkvlqeriip kffmrysiip rtlvatvdvq fdmnstksks flpqtatglp wtntnvnlay
      541 dgdndnfnvq tksslvwtpq fenknhnftg lvnmmtydgt svsyqartsn tpsselqdps
      601 vpsrvngals nlsartnkta nanvlvngvy afmdryiina glrgdvtskl arseryglfp
      661 tlsarwrvsg ekflenvkqi ddlslrfsyg rsgnapkddy tfynlydnfd wdfmgesgiy
      721 psrmgltqlk wetvvgtnlg lslamfknrv nldvevyrnr tidlffkdlq issingykav
      781 nmnvgtmdnq gwelnintkp ytsktwqvdf nfnissaqnm ireiseyypl ekgnsaangq
      841 yitymqinnp fgsfygyryl gvyqdrdatl ardaagnviv rpngeqvymr fnypivdyvf
      901 qpgdamyedv nkdgtidyrd ivylgnsnpk vfggfginlg yknklrlstf fnfrtgyeii
      961 ngtemattnm fgydnqstav qrrwrkegdv tdipralyqa gynwlgssry vedgsflrfr
     1021 tvtlrynfdk tlltkmglkn lsayvtgenl ltltkytgqd pevsmrgsdp frvatdnsmt
     1081 ppvkmftlgl tasf
//
LOCUS       WP_114790961            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114790961
VERSION     WP_114790961.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121314
     Region          30..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrflakiilp ffvlmaccvq vaaqdgavtv vrgkvtdkrt klplegasvs eqdkegrivt
       61 sastdvegnf vlrvsnrnds isvtyigyks fleairgrti inaqlesdat sqeevvvisq
      121 rrtsnglndi nerdlttavg rinasqmeem aaasidqalq grlagvdita tsgdpgaamn
      181 irirgissls angnplivvd gmpyeteips dfnfgaadeq gyatllnisp adinditvlk
      241 daaatsvwgs raangvlvit tkrgrrtkpt lgyvfrgnta frppaipmln gdqystlipe
      301 afmnrlgttl npidvqefny dpynpywyhn ysnntnwvne itrqgylqdh tvslsgggdk
      361 aryfssigyf nqtgsvignd lkrmnarvnl dyvvsnklki ftsiaytytd rnrnytsnne
      421 gairnvaylk mpnmsvfeyd efgnlttnyf spaeniqgqy sriynpvama sqaiysvlgn
      481 rivprfqady siikgvlrat fdvqfdinst nnssflpqia tgrpntetvv nrsysgdidv
      541 fnvttrtsln ytpkfknkdh vfmafanlft ndgsantqev mksnafssll vdvsaggrtq
      601 neelraasrl tqtrslgavv qaqynlkdky lvnaslrgdg ssrfgpayry gffpgasirw
      661 risgekplqk laflddlsfr asyaqsgnap rtdysfynty styqwsyqgq savfpssmel
      721 knlrwetvhg mnaginislf kgrirsdidv yrnrtsdlfs rglqiasytg yssvdmnvgt
      781 leskgwefal wtqplktkdw lvgfdfnisq nenvireisp lypsqrgnlt nngtylallq
      841 tnnpfgsfyg ykhkgvykdk datiardang npivgpngqt iymrfsyptv dyifqpgdam
      901 yqdinydgni dhkdvvylgn nnprfyggfg pniswkgtwr lsaffsyryd vdvvngtkms
      961 ttrmsnydnq stavlrrwra egditdiprg migggynwlg sdryvedasf lrfrtitlry
     1021 tvppmrlqrv gikslsaylt genlytftny tgqdpevsmp gsdpfrivtd nsmtpptknf
     1081 tlglvvgf
//
LOCUS       WP_114791244             924 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114791244
VERSION     WP_114791244.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..924
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102690
     Region          50..923
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekltgilff krvmvvslal mlpylsfsqd edtvtsvqyk spfqtflppt gsldsvngsr
       61 llsfpvtnie talhgllsgl dirmssgerf sggalnlrgq tplvvidgiv rswssinpeq
      121 vehvtvlkda vslsrygmrg angvllittr rggiskpris ataqagvqqq lfqakylday
      181 nyslllneai vnqggtaryt qsdldlyksg adkfghpnvd wrdlltnrna gmqrynvnid
      241 gggaaaryhl dfdylnqngf lksgkdlnsy etndyaeryl iranvdvkat ktttlgvnif
      301 trirelnqpg atvatiynnl yytpnsaypv fdprdslagt lqyrdnlygs afnsgyrrtf
      361 drilysdval rqelpfikgl yakgiasfny sfgqtinrsk tfpvysmsig tvndttysqi
      421 atagaqansi tyngqnrqfy megglgydws gdkhqlhsel lynidrsdig gfgdlpvlnk
      481 nilntysyny sdkyfgdvsi aysyfnrlpe anqwglfpsv glgwklssen wftsnaidll
      541 klrasygkvg nnlnignfty lveyaesgpl fytgtsttpt ssatirepal vnkdlrwess
      601 cnlnlgvdmg llnnrlslsa dyfnntitdn lilrrsgast vlgsaltven lgelkysgvd
      661 isadynngae kkfnyfinan vgiaqsklvf ddelpvsysy martgqpvnq afgyvadgfy
      721 ntqsdldnap viegytpqlg dikykdlnnd gcidifdeta lgnkgprffy glsfmarwsg
      781 iefsmlwngs qnnnvwtnvl nnlefqtgan nsigqasemh lnrwtaataa tatyprlslg
      841 ynpnnhrass fwlkdgsyir lknvelaynl pqnwintikl kgarifingl nlltftklen
      901 mdpevtasll pntrvfncgl nlkf
//
LOCUS       WP_114791277             937 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114791277
VERSION     WP_114791277.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..937
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103253
     Region          52..936
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 misfrqtlal kavvvmiccl plgllaqsdt taintmsend saqtiyplif ykikksgsta
       61 sasvvpgtsi rhtpvmsfpa glagqlpglk inqtngqpln egismllrgr splvlidgip
      121 rsiteigiee iesvtvlkda valamlgvrg aggaisvvtk kgapmksein fsgqwgtqqp
      181 tqnlignpld ayqyallyne alkndglsva nngfsdaaiq aykdgsdpyl ypnvnwrdev
      241 trksapvary ninarggnef fkyfvnlehf nqdgffktdn snnystnaga kgyfvrsnvd
      301 vkitdrldgg iyimgrimdl napgsdgann ifqailntpa saypirnpng sfggssrfqn
      361 nilgqsqysg yfightrtvl tdfylrrdld dvlpglwaka rvsffsdmre nytrsktfav
      421 fqimnndant pvygqygtns eqgnsnavsf qnrsnfqefs igysrnkglh dldllllanr
      481 dnliagsnlk ltvqgisaha symydkrfia efagayngan rypsdggfky glfpsiglgw
      541 nlhnesflkn knwlnelkvh gsygmsgldn gsyftyiqsy nnapttyfgt satstttiae
      601 sflanpnity ekakmlnigf dsrflnnrls fdvdyyfnky sdlsiirgtn sgtlgiaypn
      661 enigkqhnsg ieavlgwket rgkfgysvai naaiqqtnlv yngepaqiye wmqrtghpvg
      721 ltygyvaegl yqtqaeldsr attegyipql gdikfkdlnn dgainqydmt iigsekpsvl
      781 lganlglqws rfdlstllva elnrqvypsg nsyreflegv gqafevhldr wtpanpnasy
      841 prlttnggpf ngefnnaatn sfwlrngnfl rvrslelgys ipasilnrik lkstrvfvng
      901 ynlfslsskt fngadpenyr glypiqkvvs fgihvkl
//
LOCUS       WP_114791867            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114791867
VERSION     WP_114791867.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116210
     Region          27..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkqfflcm lcffasmhav laqttpitgk vhdgkgnpip gatviqqgts qgiptgedgs
       61 fsmnvtgtkp tlevtavgfa rkivpidgkt eidigldadl gnleevvlig yqkvtrkkst
      121 asiasisgke ienlpmssfd qlmqgrlsgv nvqnfsgdpg araavsvrgs slvssqwdqn
      181 nvissplyvv dgvpqsneey vtpgsgtgin ylaginpndi esidvlkdas aaaiygsraa
      241 ngvilittrk grsgaprvtl sgftgyterp klrevtlgtt errqkltvlq eqltyiqqqq
      301 lpylltdsln pafngntdwq dlfyqsgait nvdlgisggs engstyrfst gyydeqgiik
      361 atgfkrysar lnmltkalkg kleinpilff trttrsrglg adprlenlni npfslgagnm
      421 psslfnlsda kkesilasyd esldknlsni fnmnlnlsya fnehlklnsl ssykystsrr
      481 nynrtsames flgnysytys dqtediltsn ylsyvntwgd hnfsgvigqd iqfnvfents
      541 asggfgasdn ikvvqgvllk nlgaysdyqa ygllsyysrl sydfkdrylf sfagrwdgss
      601 rfgagnkwgf fpsasaawil seekffqdfs sainlfkirg slgtsgslps rnylqynlyt
      661 vnagaypgni gsssyngvia itpnlrdgaa qsslsweksk qwnigldfev ekgkysgsid
      721 vynkesslql fsvnlpvttg yskaltnaig vrnagveltl aanplpqssp vkwfsrlnis
      781 ynknaimnlp ngnrdlvmdg drfdkshils vgspinsfyl yrtlgvfate ddipvnpftg
      841 akyrnsngtf tagsfyiqdv dgdyftdvfn sginpdkipm gdpnpritgg wtnnftwknf
      901 tvglffnfvf krdilnlfla dqfsnstsgd pqnnfaqfst pnldainiwr qpgdnatyak
      961 ydlgtylyyy tsaqsffltk gdfvrlknin lqynipapii kkwglgsfki fgtldnaarw
     1021 qaskllpdae nvnsygeyag dgypipkkyt lglqvlf
//
LOCUS       WP_114792004            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792004
VERSION     WP_114792004.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116564
     Region          60..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtlivyekkg sllpflrsms ktgaiacfsl llvfqakaei nlkndfdlkt nisytkkafk
       61 tvtgqvinad gspvesavvs vkgrntvttt andgsfsiea negdeliish asyitqtiiv
      121 gstsaitvtl rqnignldqi vvtgyteyak rnspsastqv saadinkvpm stldqilqgr
      181 vpgmsvisss gqpgqsasvv irgmgsitgt ttplyimdgi piesgyfqti npediesvtv
      241 lkdasakaly gsrgsngviv vttkkgkkgr lnigyssqyg fstltqpgfe mmdtrerlrf
      301 eeevgletgr digpgwtlss knpdyatlsp ieqqqrnsil dslgrintdw rdlffqnasf
      361 mqqqlslsgg nenvqtynai glwreqgivk etgldrfslr sntnmnygkf tagfninlgy
      421 sssrftyneg gtsvgspmas vyyalpyeyp ytpdgvfhat ddglgfydtr egsrgidvly
      481 gasdkteqfk tilgvnlaye iikglkistr ngidyrnsvd qvfinplsyi gsrqpgekga
      541 fgegfrryfn lvstsgityk kragihdfea sgfveyvynn trsfsyrgyg vddrlpetpa
      601 gitvstdflp disgtrrnsa lfsymglgry tlnnkytlta syrydgasvs svplknrwhg
      661 fysfganwdv kqedflattd iitalnlras ygqtassfdk yfeylplygv gttyggqqai
      721 vptfignpdy dweyvdelni gfdislfktq rvkltadwyn kitrnmfidl rpsatagagt
      781 dgdiplssar mankgiewsl sgdviqkpdf nwnigvngay nkneilrvsd vtdfiqegdt
      841 rwievgrpyg tyyaprwagv dpangdalyy nrdgsvtnvy saeaqsvpls anmfpkltgg
      901 ittavrwksi tvsallafvs dvqrwnnidf ynenetymgs nqsrrmlydr wkkpgdnttl
      961 qridvprnft skdiqdasfm rlrnlqlnys ipatllqstr ilksvdvfvq gqnlftwtnw
     1021 rgldpennrq ygrfeypnar kytaginvnf
//
LOCUS       WP_114792279            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792279
VERSION     WP_114792279.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112971
     Region          23..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkillllam fmgfsflafs qtrtvtgtvl deaaapvpfa svsvkgtsvg vsadadgkyt
       61 inakdgavlv fsatgyntae vtvrngiana vlkkgdgevi devvvtalgi qrppkslgya
      121 takvddkvlt qgkavnvang lqgkvsglni ttinsgvfee vkinlrgirs llgsndpmll
      181 ldgvpvalny lsslspndie nvnvlkgssa aaiygadarn gviivttrkt sdrpvvtlss
      241 saqmsnisff pkfqtsfgsg gygdyipyen wswgpaynge mvligdelpd gskqmvpysp
      301 nnsrkdffnk gitlqndvsf atkdfymsls danikgivpd dvnrrtglri ntgkefgrfk
      361 vqtnlnyvqs nydifdddam gdyhasqnvg lnnglmnlif ntpahipits ykdfennpfa
      421 qynnyfnhyg lnpyfaidnw rqkgriqdll gnlelsykat dwlnftyrag ltsrsevytr
      481 tskgeqvndf gesrdltsip amvreysnss lrlssevfas vnkdlsddfk ltavlgnyir
      541 atesrntnvg atnlvipgly nishrtgqlv gaspfeqtrl vaayasaglg ykgwanieft
      601 grnewvsmla qnhnsyfypg vsaafvatda inglksdvls flklrtawnr vgsadiapyq
      661 listytqpag fpfgsipgyt andraftdql kpefvtstev gveagffknr inveatyfvq
      721 dnsdqiipiq lssgtgytsy ltnaaafknk giemdlrltp ivkfreggve franatyidn
      781 kvtkvadnld evgiggfnnf amnyvvagqp afiwkavdyl rddqgrviid aetgrpkadp
      841 ilktfgrtqp lwivgltpsv ywkgfnlsil aeyraghyay hdigqamawt gvsaytarnn
      901 rypfvfpnsv yedpnnpgsy lpntdialnd vndfytgeyr dvasnfltsa aswrlreasl
      961 syeipvsqll gnsvikgasf altgrnlflw lpktnvysdp dfnfttgntg gvgtsqinpp
     1021 irtfganltl rf
//
LOCUS       WP_114792340            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792340
VERSION     WP_114792340.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123062
     Region          44..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkykyvvipi ariivlslig vlllpsvmra advvaesiak lvpikgtvrs ndgkplsgas
       61 vsvkgssnat ltdadgrfti daqvgqtlei tfvgyatkev vvadaeelni nltalesnle
      121 nvvvvgygtm rkkdltgait qlkpdkiade nprtvqdilr gtpgltigld asakgggsin
      181 irgqrsvyta gnhnspllvl dgmifygels einpddieqi dvlkdasaaa vygaqsangv
      241 liittkkgkq gkpkinftsn lalstmgvdr pvwgpegyik yredwytagt yglntatgky
      301 epyqmagdps lgkpgyyekp tadmlsrygi tadqwrayst neagasddli faqriglght
      361 vltnylagrt fdwydhsfre ginqdynlsv sgasdrinyy msagylsnqg vivgdnyrav
      421 rsnlkvdgki tnwlnigani nfqdrsdgni atnwgdaitf nspfasykde ngnlvvhpqg
      481 stltglvrgy nydynrqfqd lesgftvlns iftakvklpf ninysfnvap ryqwfyrryf
      541 asskhpdwnp ltnnagvdre nkkrfdwsln ntinwehtfa gkhrvnvtlv qeaeerelwe
      601 dyirarnitp tdalgfhets tgdkllsefd sydarqtadg mlgrlfysyd drymftgsvr
      661 rdgysafgts npratflsaa lawtftnekf fkwdalsngk lrlsygqngn rslenpyial
      721 adlalgtgtq gyingtgdyi qfyylrisrm anknlqwekt asfnvgldlg flnnritttl
      781 dyfnmsttdm imnqslpdfs gfssitsnlg evqnngieis insrnivrpd fnwnttfgfs
      841 yyknkikhly yqyedvldan gniisskevd ditnkwfigq pigaiwdykv tgiwqvneie
      901 eakkygqrpg dpkvensyta ddvkkadgtt tpvysnddkq flgqtqapvm wslrndftyk
      961 nfnlsfniys ymghksthga ylnqdngtst isqglantye kpywtpdnps dfwarleskg
     1021 pqglnapqrv fsrsfarlen vtlgytlpnk ltssvniekl rvfgairnva vwkkdsnwry
     1081 wdietgamap rtfalglnlt f
//
LOCUS       WP_114792283            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792283
VERSION     WP_114792283.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118604
     Region          24..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgklkvafvg ilsfltslaf gqaktvtgtv tddkgapipg atvtvsqtni gtatdpngrf
       61 tinlpegkrv ievtavgrss qavdldgkst vtivlsmien pleeivvtay grqtrravtg
      121 aiasinskdl ekraltsatg alegvapgvm vnntygqpgt apsirirgfs singnntplv
      181 vvdgviyggs iadlnsndie disvlkdaaa galygnkasn gvvlittkka ksgkpvfnaa
      241 inqgfytrgm keyttmspdq ymeamwlgyr nnllstsaty ntvekanaka nesaitdnir
      301 yniynksnte lfdangklvs darirdgylg dldwfepilq tghrqdynin ggtkndkssl
      361 ffstgyldek gyfkrsgfqr ftgringdit pvswfkagvl lngthqinnn ysdgntsfnn
      421 piynariiap vfpvhlhdma tgeyildeeg kvqyddgsty nrgqyvarha iwenelntrk
      481 niigsmqgqa yanvkflkdf sftilgdltt kntelrnyen pvigdgsgng grvsrdmyry
      541 kvytfqqqln wnryfndhnf dvlvghenys yfysrlqgsk gsqaftglen lddftsiisl
      601 geyedvvkte sylsrvryny sqkyflegsf rrdgssrfaa anrwgsfwgl sgawlissen
      661 flagsktvnn lklragygqv gndasaayya sqtlytfnqn anlmavylsq ngsqnlvwek
      721 vgtwgaaleg qlfnrfnfsv eyfdkrsidl ifpfnyplsa ggtsstsaqa tvlrnigtls
      781 nrgwelaady fiinkkdftl nlganatflk neivklpnen kkdgiidgtk klfeghgiyd
      841 fwlyqyagvd qmtgtglyva ddviynggnp dnagstipaa nlvkindkyy vnnvtyakrd
      901 wsgssipkvy ggvslranwk slsfqtlfty glggkmmdys yldlmsvsgt phslhtdllk
      961 awngapegmt essvnrldpn gipaidyarn aqatqtstrf lqdasygvlk nisigyglps
     1021 ttlerislrs cqinftienl atftklqgmd pqqsfngvhy nyfmtprifs lglnigl
//
LOCUS       WP_114792354            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792354
VERSION     WP_114792354.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112272
     Region          27..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktivsvll lwmascclpy iasaqtktvt gtvtssaktp ipgvtvmvkg ttratstnpn
       61 gkfsiavepg qtlefssigf egksvtlgne siievvlieg egkqeeevvv ttefgmkrig
      121 ravgssvqvv dgatiaesgr esfisalagr vpglnvtsts glpgasntvv lrnltsisgn
      181 nqplyvidgv pmnnstydpi smaggetysv rnqdyssrgn dvnpediasi tvlkgaaaaa
      241 lygsdasnga iiittkkgra gsgrvtynnf fkwdkaygwp dmqtkysnga ygttnyynta
      301 kfgglypdnv aqydniaail qtgtqqrhnl sveagsdkat irggvsylgq kgvikmtdyd
      361 rfnvslsgqa kitdwlkfea aiqytrtenn kalrgtdgpl yramiwpmvd ditnyqtldg
      421 lmrkpdyyld ldllnplfam nknknfdrtn rftsnmafti tptahtflrg qvgwdvgmqt
      481 fetswhpyya arnaglgryd lvqsnfsdpt vnilagynnk ffnnklsfag qvgyhqleng
      541 iirlatngsk yiipdfqsin ntdpvsitsr qrntkrriqa vsaqfefgyn nlafvtlrgr
      601 ndwsstlpvn nnsyfypaie gsliltefea ikrikaisyf klrgsiaqvg kdagpleiyp
      661 qleptnltgg gwkygftgpn pqlrpemtta revgfdarfl nnrintyfty fttrnedqiv
      721 kgfrlsyatg fvlntlnvga fktwgweasi dgdiiknakg ltwnvgmngs sgrskvlylp
      781 anvseyynay twnsgnirng iavgnpittl sgrgfernsa gqvlidpstg lpivsalwtv
      841 igdrepklrf gattsltykg irlsglfagr ygatvvngtk rsmmtqglsw esvalresrp
      901 vvfngvvrdg kqntanptvn tiavdpglaa asiyaggded wlekdvnyvr lqelrlsytl
      961 pkslfsrmri isgmdvyvvg ndlatwtnys gidavgntvs aaaggtggeg ydvwsipnpr
     1021 gitvgislnl n
//
LOCUS       WP_114792424            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792424
VERSION     WP_114792424.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120094
     Region          31..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknnrgfsr sglclllflc isylsfaqst ktisgsvmdd kqqplrgvsv vvknsklgav
       61 tnergiytlk gvpadatlvf sytgftdqei rvtdqsaini tmsttavdln evvvigygtt
      121 rrkdltgava svqtskleke aprsvqdllr gnaagiiigq snpgntargd adilvrgsgt
      181 lkagssplnv vdgvifdgtf adinpndiqs idilkdasat avfgakaang vilittkkga
      241 agkpritfna nlgivekagm prvmnaeefl nwrhdyevgk rtdaflnqyp emfidprklt
      301 nvtqldwyny dqktpvtsvt eeqltrawlt rlelkapeid nylankitnw qdlvfqkgfq
      361 qdyttsvsnk nenssyyfsl nyvdregiiv gnrftnfrtr lnleskitsf lkvgantnfa
      421 vrnegflqsd wgqsaiispy gsnnlddtas iyrrlptgda tpvnpfhdnl yrdrknmynt
      481 lnssiygiit lplgfefqsn ftpsftwhdy yshessknpq wtatggster tnektynwqi
      541 dnvlrwkrrf ddhnievtll qnaekgqfwr tkatttnyyg adilswhriq agtnpfnese
      601 dtyrtgdalm arlyyslkdk ymltasvrrd gysafgaqnp ratfpaiala wdfseekfmk
      661 ntsswldygk lrlswgkngn rdigqyeals dmvsglhpfi dqngkvylfp qlyvdrmanl
      721 glkwegktsy nigldfslfk rrlsgsiday tattvdllvd ralpeiigfn svaanlgqln
      781 nkgfeislsg nviqktdfnw nsgfifmlnr rkivhlygdm idvkddsgnv igqkeaddik
      841 nkwfigrdpd qfwdyerigv wqrgeeavak kyndsapgdf kykdqngdsv mtdadrvflg
      901 yksprfrwtw rndfdykrft lsifiysnwg qreqfnrasn nssfpdrttd yvqprwtsdn
      961 pindyarigs knigtnyver sfvrldnvsl syglpqplln kisvqsaris favrnvafwa
     1021 phwkygdpes ggyrtrnseg neytpgqpmp rtynlsfnlt l
//
LOCUS       WP_114792635            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792635
VERSION     WP_114792635.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119596
     Region          29..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnenffykgi lvlallvagl gsqaqdaavl kgvvydkkgg kpltdvsvmi vnannlalng
       61 nktneegkfe vvnskggski vfsnmgyqtq ekeigdktff tiylsedsss meivkvvstv
      121 qkkadlgfls idkrelssav asvdlentek mpvvnveqll qgmapglqvv sasgdpgaaa
      181 sirirgissi sgmndplwiv dgaeiignny qvasitdfgf spigdldpsd iasidilkda
      241 satalygsrg angviviqtk rgkkgkaqlq vntkftltev prtipmlsgd eqriyyiekt
      301 tggldngtsf pelrgdltrs dawifnnntd wtdaitrkgi fqqyntalsg ggdrinyywg
      361 lgyanqygtt kgtgydrfnt rfnlnykvsd rfkvtadlny tnsltdkrgq ehpitngnqe
      421 lnplllarqi payfpvysrn glnyfldrni tisshsrynp lalidystyf tranrfmast
      481 svdfkirsni dfraqvstdf resadeyflp gyatdalpge ilynaglqte gyqlminsnn
      541 rltwsaikrk dhrltftgvl tynidrnnst eiqyynsasp qlksadaaai isaatgnygt
      601 skylgmfvqg hyamkdryfi tvtgktegds rygadnpysi fpaiggawei sresfladae
      661 witfikprfa ygvtgnlprl nnlydiaygt gtgylgqtyt ypskfandni reertteynm
      721 gidwsffkdr ltgqldfysr ttnnlllqer lsstlgyssq yinfgtvrns gwelgvtgii
      781 lkgsdtklrw ksffniatnr nriiklpelf danaftvsqs gftsklqegd vvgafygyqa
      841 lgvysrddda ilkdaegnti yeadgitpky mrygsstgrq fkggdmiysd ingdgvinel
      901 drvqigdasp qffggwnntf nyrnwivtln lqyqtgndii natrqymerm tvshnqsqsv
      961 larwrrqgdv tdmpraqpdn swnsaastrw vedgsylrlk tvsltytagk elvrkiglgv
     1021 rqlsffvtgy nlytwtrylg ldpevpitgs vylfgidnat tapprqytlg lnigf
//
LOCUS       WP_114792572             935 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792572
VERSION     WP_114792572.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 935)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 935)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 935)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..935
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..935
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103622
     Region          60..934
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkysskyfrm ltwsgvails nwfsdanaqt addslnivkm dqlgilapag sikfprqnda
       61 vsfaellpgt pgvqvtetgi iaaapllmir gintinlktg ptiyidgipv kysrelssfl
      121 snyeptrfgf lnindirsin vlkdakdlsa lggrgangai ylttdrgefg gtkieftant
      181 gflrasyktn kmggnqfkty laaylkenga sdddiaanpi fnpssapynn ntdwvdmvtr
      241 pgryndyhvk lkggsgdany mfsvghmgrt gtieeskfnr ttmrfnldyk lssrfeisnn
      301 lsysntgsry seegynwgvh pfftavtkap fmnsysynde gvqtrllanv dvlgksnpla
      361 lvqnmrnsne enrvdgiisg lwhiekglsl ntslsvsyyn mresqyrpal givadrnrmr
      421 qnanrnssef tfiwnsyllk tgswsgniny kgqigawfet yedkalyark inagtddyet
      481 lkqgivdsas nirfrsnlnr lyfdgnldff nrlsisanvn aegssnfgpk grwalyggad
      541 llldlldrsk pnqlalraav grtgnndvrg yyqdnlyyai syfgyggvyl gnvanelikp
      601 eftnaieagi rlslfrrrld idagyyhrtt knlitfrnyp ielgidpqfe nsgtisakgi
      661 elsvmgriid nskitwrlyg nlstlkntvd qlengdiirs mynvsgiare aetigsfygy
      721 rikgvfqsaa dvslkkadgt aykpgdyive dlngdgkine ldrqiigkpl pdlyggfgtg
      781 frykhislda gfsfaygqdi ynsfkqqmnw mgdysnqspd vagrwksasd pgnglsrasy
      841 gdpssngmaa dlwvedggyt rlkyltlgyd lplktkwtfi kgikvnitge nlltltsysg
      901 ldpevisssd pllrgvdfga splpksiilg vkvsl
//
LOCUS       WP_114792647            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792647
VERSION     WP_114792647.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116834
     Region          44..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkyssswfq ikndltsvyf qkrllitalv illntvfala qtsikvtgkv ldqkgepmig
       61 asitqqggsi stssdkngsf tlnvkntdsd livtsvgytt knvsikntqt nivvrlelnd
      121 pqaledivvv gygkqkkesv lgavsqitse vleraggvtn lgmaltgtlp glvttassgm
      181 pgeespqivi rgqtswnssa plvlidgier dmnaidissv esisvlkdas atavfgvkga
      241 ngvilittkq gkagkaniri rsnmtmkvas klpekfdsyd allirnqvir nellynanaw
      301 ggykpleiid kyrnplntde wdkypnvdwv kelfkshama yntsanvsgg tnfvtyfagv
      361 dfvtegdlfk vvgnnrgyqa gysynrinar snldfnltkt tklttrlfgs ngarkfprta
      421 sdpwrsayrt spdamrpiys ngiwgyydpr nfdvpntvye lstsgtsktt snqlttdfvl
      481 qqdlkmltng lslrlnysvd ntfqetnrgv ddannpaqri wynpdtdvfe vilqtkpvdg
      541 welplnkvtw alnegsvnsg atyrrlnyaa qlnyarkfgk hdvtgtgvfm rerfvtgsaw
      601 ntfredwvfr atygydnryl ldangayngs ekfgpgyrfd ffpsvalgwn isnekfmksa
      661 tfinflklrg swgligddra gerwlyqsii nsggnalmgt ppantpysff sygrfgnpdm
      721 awenaekrni gleysvwnrk isgsvdffne drtdiinttp lvpsyfgasl pplnwgrvks
      781 sgyefelrfn hsfvngirvw antnythamn kviirndtel eptyqkdagy pigqvrshld
      841 ygylrswddi ygstaklsps tqnklpgdfn iidynadgii ddndvvpygy tgtpqntyna
      901 tigaewkgls ffvqfygvnn vtryvefpsl hnasnivyve gdywnkntga gtplprwsvl
      961 gstggngtry qydgsyirlk naelgytfsg nvinkmgmrs cklflngnnl llwtkmpddr
     1021 esnfatggns sngayptmrr fnlgidinf
//
LOCUS       WP_114792724            1013 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792724
VERSION     WP_114792724.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1013
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111491
     Region          36..1012
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miqtyrrcqc tgylfsaltv iilifsglsa taqqsqisgs vtddkgaalp svtvsvkgkg
       61 istktneegh faiaarindv lvfsavsylt reviitaate yqvvlatnav amsdvvvvgy
      121 gknskrtlss aitsikpedl nrgaigdvgq llqgkvpgln vtasgdpnrp aamilrghst
      181 inspggpfyv idgipgadin gvapddiasm dilkdasata iygnrasngv imvttkkgra
      241 gklqaayngy igfenvsssl dlmdaaalra ysqknnytps tnddkgantn wmeaiqkksa
      301 lshnhnisfs ggteksmysa slnylkkegi ilqsdlervi grisaehhal ndrltlglni
      361 mssnskasnv plqnmvfqqa vkynpmspvy nedgtffenf nntqyfnpvs iiknavddtk
      421 ygslqgnftl eaklpfnlty nanlsyqrst wlhgeyynsy ysqnystgsf ytngdpgggr
      481 slrnfysngl ayrnyyqnts ktfetfltwg kklglhnlka vlgyswqrnt nndglqtsqt
      541 nfindyttyy nlrlgnyqtv kgfavdyggs iyeetnfisd ffrlnydfne rillqasirr
      601 dgssvfgknk ewgyfpaasi awrisesafi knagfisdlk lrlsygatgn afglgaynaq
      661 rlydksgtyy sdgvfaasfr stqgsnpdlq wevtatknag ldygflknri tgaidiyekt
      721 ttdmlfrynv aqsidpsgwl wlnvgkirnr giefnvniaa vnkknftwtt glnlasnknv
      781 ildlkgpeqy gvnadstyyt qldgpgatgs rlqiltvggp lgqfysfqyl gkdasgnslf
      841 lkgdgtettn ptqvsdyhyl gsphpklmyg fnnsfryknf dlnlflrgvi gnkifnatra
      901 dlsyvftagq tnispyaadd artdsrnnny ssryvengsy lrfdnatlgy rfnlksdyfs
      961 nlrlygtvnn lfvitkykgi dpeinqggas lgvdynsfyp ktrtvligvs vgf
//
LOCUS       WP_114792798            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792798
VERSION     WP_114792798.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123031
     Region          28..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnakhvlrfa flfvlpllit mtavaqtrtv tgtvvddstk apiagvtikv kdgpqtaitn
       61 dqgnftlnap angaviqysh vnyefgevsv kldgpmnisl krvenslddv vvvgygtqsr
      121 rditgsvatv dlkkltempv asvtealrgq ipglnvsggs nrpgnmatls irqqfnwgkd
      181 ggsdlplvvi ddviqldpqs gkssldrfnq ldlseiesit vlrdaaaaiy gsrasqgaii
      241 vktkrgktgp prvsynakfq tndaishgkv mnarqygefa nsfgralgtw tadhffsdae
      301 laemgttnyd wlmndwrsan amqhsldlsg gseratyftg asyftqganl gnqdfsrwty
      361 ragtdvkvls glkfgatiaa sntnseksft kinfsdgfav ggeqndysvl lhmpkyipwv
      421 yningvdqyi spalgpnklg nmsgnnslsn wnyyaflnng skttdqqfny nanfnlqydl
      481 pfikglsfkl nygisqasvk teqnqfpitl vrdslgnkag qhlynestvw saplvnrsga
      541 rvsylgttsk neqsnffiny drkfgdhnis amasveratt eledrrmlyd npnadiyngt
      601 svsagslntg nsityryqgg tlsylgrlny nykgkylfqf vyrtdastnf apenywgqfp
      661 gvsagwvmsd ekffknnisw vnflkirasl antgnnnvnp wkwlqlytaa tdkgfgfgsn
      721 ggiyttgftp gvtpnraltw dktlqrnfgl dlaflnrrls vtfdqyfnst rdmltdmsaa
      781 inspisvgga faeqnfagvn swgselsinw kdnigdfsys igvnggmnny ktvkyfdlpf
      841 nypsiastrr aegnygifpv ygfttwkets sgdgmlrtda didnywnylt nlasnsgieg
      901 aapnflgite ksglrkgmlv yedvagnldv agktiggqng rimadedyvk lkksnrtygl
      961 ttnismgwkg islltqiats wgganyldyi kqgtssnnam wshpvyltdm ydaesnpngk
     1021 spnlayfdsf ggtrsdfflm ptfrmfvrsl svgytlpksw vqsinlenar iylsgqnlwd
     1081 fynpypkkyr nmyddprvsy ptlrtwalgl svgf
//
LOCUS       WP_114792805            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792805
VERSION     WP_114792805.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116560
     Region          28..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myfkhilkfa clliaivllq tqamaqtktv vgtvvsdsas tplagvtisi kggrqststd
       61 ktgnfslkip dgkvilewsy igyengedlv pesgamnitm kkldlsmdei vvvgygtqkr
      121 skltgavatv ksedivdlpv qniaaalrgr vaglgvssas grpgasitln vrgasssegv
      181 ggasaeplyv idnmivgkst fdnldpsmie disilkdasa aiygasgakg vilvttkkgk
      241 pgpprlsysg fvgiedavrk atmlsaydha kllnetyrik gvkeedhfsd edleylknnq
      301 yeswfdqiwq palmqrhsln lsggsdkmtf fvgggyqnqn anyagqksdk ynfrggltak
      361 lisnlrmevn fnidnnvrys rngwsendqn fletliqvpr wtpiqfgdky vnyiggatan
      421 fnpfaldnsg mynesknksy glnaglvyap ekgplkglni rfqasttass gkseeyrpey
      481 lqynfarwgn nnlfyrdsii gnpvivnggd narlsqgkse ssnyrvflni syartigahd
      541 fsimvggeqs ensgsgmgyy ysgqqipeqn yywafnpipt vntpsaslgg krsffgnfny
      601 tyagkytleg tarldassnf aveniwgffp rlgagwvvsq etffkdhaps fisylklran
      661 igltgddrvg atywreryki nvgsylynnt smaglrpdvy pnpditwern rtfnfgvdls
      721 lfnnklnlgf etfqtknfev fdkgndqnfp myagfaapvv nyrtiyrwgt efsigynanl
      781 akdlrfrast nfgfgrsila kmfynrfqlw edpytedwgn laqfgtdpti ynggnygmiv
      841 egmfrsqqev defmsahpgy tmfgaipeag wlkykdidgn givtdrdltl mfkkgtdpal
      901 stglqlglty ksfdwrvnig ariggkvfyd tkarrsiatp tknianfwnd twsvenpdaq
      961 fprfddpgis mesdfwavdg ttirvndmtl syaapkqvvn rvglssarfl isannlwlik
     1021 nplkykdpen syiydyptlr tisvglnlgl
//
LOCUS       WP_114793046            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114793046
VERSION     WP_114793046.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115437
     Region          23..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrksificcl ilflssisfa qsqtisgtvr yardssilpg vnvqekntkn tvqtnsegyy
       61 tinvkgastl iftaagmaqq evftspgiid iylrdaqttd lsevvvttal gikkqqkalg
      121 yavqevkget lektrtptai gslagkvagl nisnttdlfr npgielrgkt plividgipd
      181 pnadpykina ddiesitvlk gpaagalygq igingaimyt tkrgkkgivs vdlnsstmfq
      241 gsytvipkvq slygggdagk yayvngsgsg vegggwlwgp kldqrdpnta sgfvelpqyn
      301 spytpdqsyt vtylngdtht gnykpipwis rgknnirnff qtgilstnsi sasagndkgs
      361 yrlsaghiyq kgvvpntgvn nssfsiggny dlsknltvda kltynreysd nyptigygpp
      421 nilynlilwi gtdvdvrdlk nywvpgkegl qqrnynvswy nnpyfvanel lngykknnaf
      481 gqitfdykft pdlslkfrng fnqysensdi kepysyvnys fiskgnysvt ntnyfditsd
      541 lilnynrrfs smfavnasvg ganayrnlks tssstdglti pgfynlsntt npltgsnslq
      601 errtssaygt ldleafkfly anftgrydks stlpvadnay fypsaglsav isdavdlpka
      661 isflkartsw akvntgfvss tnpyehilty siggkwnnvp svvwpgsait pqlipstves
      721 telgmvigfl rnrinvdaty frnkeyngft tvrqseasgy tgvvqnanvy vrkgwefvlg
      781 gtpivnhhfk wettfnfsns hlwlkkatdp dsegfvdnik egdrndrifi sysqtadgrp
      841 ifnsngslal dtephffgyg dskwiygwqn aftyknigls fsfdgrlggl iysttnqkmw
      901 wggaaietan syrddaiagk ntyvapgvvi kdgsvdydrr geiisdtrqy ednttpvnyi
      961 sfmqsdagha lnnyfyysgt ylkmrelvls ynvpgkwskg ifkgasvsvi gnnlfilsrl
     1021 pnvdpdaesd nlqtpsvrsl gfninlkf
//
LOCUS       WP_114792936            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114792936
VERSION     WP_114792936.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118822
     Region          24..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkkiailai avsvttaals qtkftvsgti tsattgealv satvksiksn litisalggs
       61 ylmhlhylpd tllvthtgyi sqtfvvsqpg ifniqmsvdn eelegvtint gyqrikpnev
      121 ngsfavidnk tlneqtgtni lerlngvtng lifnsdklss agqpnpisir glstingnla
      181 pliivdnfpy dgdinninpn dvasvtvlkd aaaasiwgar agngvivitt krgqlnqrlk
      241 inanastlft sapdlfyapr intidllave eslftrgyyd dwimddynht plpslvsmll
      301 nrrnglitaq dsaaamhsfa qqdtrkeyar hfqqtaltqq yslsisggta nyswllggny
      361 nrvtgtnaat adkinihldn qlkitqqltl nlsayytssr sktgkpdfna vsringhyip
      421 ylqyvdelgq ptaldqyrre yidtagggrl lnwdyypltd yqhrytstqm qdilvragmd
      481 ykitsnlsan lqyqfqqqkv etgttsdles fytrnlinrf tiipgnaaaa lsyrvpigdi
      541 ltrsntpvqs qnlrgqfnyn qiwrkhqvsl iaggelrdav sgpgegftvy gyrkdplsnt
      601 qvdvtqpypi iingsyqyip ggaglsstis trfvsfygng sytllkrysi ngsfrkdasn
      661 ifglatndkw nplwsagigw lissepfykt swlpyvklra tygysgnvdv grtplpvsla
      721 adniisrlpy qriselnnps lrweksrqvn igldfespgk riagsveyyq kkgtdlyget
      781 pydytawgrr qfitanvagm egkgwdvsin tinikktmvw tssfiynynt skttayytat
      841 skgvfdinsg nnispiigqp lyaitayqwg glnskgdpqg ylngelttdy lditqkvrid
      901 glsagaltmm gssapvhfgs finriewkgl sfsanlmyka gyyffknsfs sveltgssrg
      961 hadyynrwqq pgdelhtdip afvysdytqy rerdnfyrys tvnvikgdhi rlhyinlgyl
     1021 lplnkgkivc svygnmsnig ilwrankegi dpdaptgspa prqytiglka df
//
LOCUS       WP_114793248             953 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Niabella
            yanshanensis].
ACCESSION   WP_114793248
VERSION     WP_114793248.1
KEYWORDS    RefSeq.
SOURCE      Niabella yanshanensis
  ORGANISM  Niabella yanshanensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Niabella.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Niabella yanshanensis"
                     /db_xref="taxon:577386"
     Protein         1..953
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105057
     Region          38..952
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miqkyrplla vlgwlcsvgv akaqtvtang tgqeqfkdst elnrlvdlgl rkeknwrnta
       61 atftlsgkel ekmfsgnlln tlqgripglt vntgsgepgy dnpnlfmrgr ttwnsgaaqq
      121 lilldgfqvd lnalsafspy eiesitllkd aaataiyglq gasgvinvat kkgrvsskne
      181 ltinarygiq tpvklpevmn aydytrlynq alandglpqk ypnpdlykvs ndpfhpnvnw
      241 ydellkknsa iqnynlsfrg gnrtaryyvl mdymnydgly knatainkdf gtnakyskin
      301 lranveldlt kslyvaanvs giiedrntps gftasqvfdn lmripaaafp vknpngtwgn
      361 ssvynfnpiq llqqngiysa htrtiqtnfk vrekldlitp glaaiggvsf nnqytgtrqt
      421 lysvmsyell kdnndqpild gggnptyrti gtntpqttne ggnghwnrnt fqagldynrg
      481 fgkntfsgml lgrrvnytri gqtyavrvqg iagnftydyd kkyivdfsss ymgsadfapg
      541 nkygffpals agwilsnedf lkhnevinfl klrasygsag sindayrfly qeraggasgw
      601 itgtsntgrg gmaigafanp datwelkktl nigveatlwd klsatidvfs etrsgiyeip
      661 yanvaaytgf nlpylntgkv nnkgfeaalt ynnqadafky fvtgtatfar nkiiekseta
      721 qpadrlyerg faigqvkglv fdgfyqssdf eangnlkqgi ttssyaqvrp gdlkfkdldg
      781 ngvineydra pwgynnvpev tlgfnlgfny kgfdfsafvq gvmnrtisml gaaynythpf
      841 vnnnnisvfs nnawtpetaa tatsprlstl anlnnnvgad fwfrngnffk lrsielgyti
      901 pqtgvlkkvg airvfangtn lfvsnmidgl epenlsmgyp vtkvvdfgfn vkf
//
LOCUS       WP_114796759             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Gaiella
            occulta].
ACCESSION   WP_114796759
VERSION     WP_114796759.1
KEYWORDS    RefSeq.
SOURCE      Gaiella occulta
  ORGANISM  Gaiella occulta
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia; Gaiellales;
            Gaiellaceae; Gaiella.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Gaiella occulta"
                     /db_xref="taxon:1002870"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37433
     Region          1..359
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrivvprega pgesrvalvp dsigrlapag feiavergag aaagfaddey aaagavlpdg
       61 gslydgadav vrvarpspde vakmapgtvv igflapltda egierlrarg vvafamesvp
      121 ritraqsmda lssqatvagy kaviiaadrv pkmfpllmta agtvtpakvl vmgagvaglq
      181 aiatarrlga vvsafdvrpa vkeqveslga tfldlgvrge eteggyakel tseqqaaqqa
      241 aleervpefd vvittalvpg rpaprlipas avaemrsgsc ivdlaaeagg ncelthpgee
      301 ivrdgvtivg ftnvpslmas dasrlyarnv tallqhlapg geldldfdde itagacvarp
      361 paevts
//
LOCUS       WP_114799278             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Meiothermus sp. QL-1].
ACCESSION   WP_114799278
VERSION     WP_114799278.1
KEYWORDS    RefSeq.
SOURCE      Meiothermus sp. QL-1
  ORGANISM  Meiothermus sp. QL-1
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Meiothermus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Meiothermus sp. QL-1"
                     /db_xref="taxon:2058095"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39545
     Region          2..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvqiavpket apgerrvalt pevvarlvke gcrvrletga gaqayfsdea yrnagaevvs
       61 retlfqeaqv vftvqpleva dlrrlaagtl vvglmyphrd pervramaeg gitalameli
      121 pritraqsmd vlssqatvag ymaaliaare ssrffpmltt aagtirparv mvmgvgvagl
      181 qaiatarrlg anvwaydvrk aaaeqalslg akvielpisa egeggyarel teeekriqhe
      241 alakevgsmd avittaqvpg rkapllitpd mvermgpgsv ivdlaaesgg ncaltrpget
      301 vevngvrivg plnlpsalav hasemyaknl ynlskllike kalapdwsde ilagallthq
      361 geiahaptra llgg
//
LOCUS       WP_114808664             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_114808664
VERSION     WP_114808664.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54003
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta glgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptkv qkkepeptsp vkklvglavg vclfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqdsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_114818005             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brevundimonas bullata].
ACCESSION   WP_114818005
VERSION     WP_114818005.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas bullata
  ORGANISM  Brevundimonas bullata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Brevundimonas bullata"
                     /db_xref="taxon:13160"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38514
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavaiavtre rregetrcav tpetvkklia lgatvsveag tgvgssipda dyaeagatvk
       61 pdtravlega divlkvrgpt aqetsalkpg aiviamlday rekdtvealk gagvtafame
      121 fvpritraqv mdvlssqanl agyravieaa yafgkgfpmm mtaagtvapa kvfvmgvgva
      181 glqaiatarr lgavvtatdv rpatkeqves lgakflaved eefknaqtag gyakpmspey
      241 qakqaaltge hirkqdivit talipgraap vlvsaeqvas mkpgsvlidl aveaggnvag
      301 akagevvtta ngvsivgytn lpgriaadas alyarnltaf vglmlkdgvv tldledeilk
      361 aavvthggav vhegvkg
//
LOCUS       WP_114813355             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia kururiensis].
ACCESSION   WP_114813355
VERSION     WP_114813355.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia kururiensis
  ORGANISM  Paraburkholderia kururiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia kururiensis"
                     /db_xref="taxon:984307"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39562
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anetrvaatp etvkkyvsqg hrvtvqagag taasftdeay vavgaeitda
       61 atafaadlvl kvqspsvsel pfmkrgavlv gmldpfnaan aaqlaeaglt afsleaaprt
      121 traqsldvls sqaniagyka vlvaasvypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atarrlgavi easdvrpavk eqieslgakf ldvpyetqee reaaegvggy arpmppswla
      241 rqsalvhera rqadivista lipgrdaptl lpaqtveamk pgsvvvdlaa grgpvadqat
      301 grrggncplt vadevvtkhg vtivgytnla amvaadassl yarnlldflk livtkegtln
      361 idladdivaa tllardgavt rka
//
LOCUS       WP_114806381             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_114806381
VERSION     WP_114806381.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53797
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklssknv nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa psiqvsaqpq qkakvqstka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgvv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_114819031             944 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114819031
VERSION     WP_114819031.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..944
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105839
     Region          15..943
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvkscvlsa galffigqiv agqklkkdtv kvrdideviv lgyrsmtkkn aatsvatids
       61 ktienrpnan vmniiqgqla gvnvtastgq pgakptvvir gvgtysgnsd plyvidgfps
      121 nsdnfrsinp ndidtfsvlk daaaiaeygs rgsngvilit tkkgkfnqnm rvrysnqfgi
      181 sflqdpkynl sdskeflslq kiygvgagak mtdeqiasyn intdwkkvff rpaitqshdl
      241 slesggrnin sytsigylen egilrttglk rftvrnning ksenerfkys lvtglgfskn
      301 neaildagav nrnfilgayr sapylspdly qngqqlfdly skdgtllytp lmlmdklvny
      361 nnlteemrld maanlsykit ndltakarts gqylntwfnq aeyplsfnaf lfkgaqefsg
      421 fedmnqrref lfnnlwqley fkafgkhtft lqgnaeynys qlntnnnrqk gldpktfvpg
      481 tgsgyiadts nndfyvsats asklkwamis yfasldydfs kkygitgvlr rdgtnrffgd
      541 kqwgtfwsvg grwnideeef mqnvkfvdaf kirasygtqg nqrivdgsiy aglnppaytn
      601 iysvtnntyn gnqgyaiafg dkelrwettk qynigsdfef fkrilrgsfd yyvkdthdly
      661 lpdptapvsg tlsivrntdv vlqnkgieln laydvirnke ndisltfrvn gsinnqkisg
      721 iqsgngritd glvvtenggl lreyflykyl gvnpsdgnll fedadgnpte spkdsdrkrm
      781 gvnklpkyqg gfgfdfsykn ffvsstftfv aklkridgdm sdiynpnnla sfnvdrdlln
      841 awtttntntd vpslkaanvg lqgnsdrflv dasylrlrnv qlgyripkrf lkgtfisdms
      901 ftlqgenllt ftkwrgydve spngsdqqry psprvvtfgf dvkf
//
LOCUS       WP_114819033             931 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114819033
VERSION     WP_114819033.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 931)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 931)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 931)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..931
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..931
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103252
     Region          30..929
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklhvlsa galfflgqaa faqkskndsv lkenkidevi vtgyqkkkad eitqaqavvg
       61 gdeirrnspt tsignslqgr asgvfvqstt gqpgaaatiq vrgiagvggs septyvvngm
      121 ymtarqfsai npadvesisi lkdaaataqy gargangvvv vttkagkagk thysfetkfg
      181 fseklrdkny tmmnsrelmd fqnqlgylgf kprsqqeida lagydhnwqk dllkpssiqs
      241 ylfsaqggsr estfyyslgy dsdngiirdi dglkrytgnf gftnklsekl nvgvnlgvqy
      301 qetqnfrdrn ntqnpfaamy kyapyepvyn adgsynqtmr agsnvveqir tnrsdeqrlr
      361 ipvtlfaeyk iidglkfksn fnglfdwymr trwmqkgsnl ditvnkvptg slnkdsfytf
      421 nytwnnsiny kksfgghnfd flgfieyndn ynetmnggay glkspvinvp sittpsdrnt
      481 ftgvkvrntl fslagmlnyd yegrylvtgs lrrdassrfg annqsgifws asaawniake
      541 dfmkggfind lklrgsygtt gndgtlpdyy nvnnisygly gangtsypgt asqgyyiign
      601 snlkwesnai tnlgvdftmw nrrvrgsvev yknkrkdfvq lvpldkqegg yyqyinagdm
      661 sqkglevels vdvikkkdfq wnlhanisfq ksildkladg qtqrnlgdty lkvgetpyvf
      721 ynvrfagvdp sngkalyydk egnvtdvysa snavpltdks pfpksfggfg ttvqykgldf
      781 sadfsfklgg ytynnmyaaa vdptlavagr nmaqaaaqvw knpgdtgvfq kvdsngmrds
      841 dqwieksdyl rlrsltlgyt fdkaflgegs pinklrayvq gqnlftvtkf hgepevsvgs
      901 destalfvpg aynlytypav rtilvglqle f
//
LOCUS       WP_114819049            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114819049
VERSION     WP_114819049.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124177
     Region          22..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlillpl laaniamaqq kktitgkied antsqmitga sikietqsvs tktelegiie
       61 svsvgtvtdk dgkfileipa dtktvlvsyp gyesrviqln egqtnytirl tseisdknki
      121 qeviitgyqk iekrkqtsav stvkmdnisq agvasvdqml agqiagvavt petgapgspa
      181 kirirgtasl sgpqdplwvi dglplegndv pnftdkdnid qlqnfsiagl npndiediti
      241 lkdaaataiy garaangvis ittkkgkkgs lklnfsadtf vtsrpdfdkl nllnasekvd
      301 lelmlakrad ltyradkgev mriltqnsql dafrnggfda lnsftrqqin glrnnntdwg
      361 kllyrnaink qyglsvsggs dradyyfslg yydeegttig tgfkrynltl knnyklsdkl
      421 nagisifgtq seresfvtda dasinpvnys rnanpylkpf nadgsynydr dmdgfedryi
      481 pfnfleeren tnyslknnsl kaildleyka skslrftsql glqydankte kfaaentyft
      541 rkmrentryy kdgkynyflp agavkqnwdn dffqynwklq aaystkinqh eidlmagtei
      601 rktednttit rafgydpktr rataivfpns sfaadkryet yreaapiena yasmfatasy
      661 tydqkytffg svrydgtnlf gvnkkykylp iwavsgswlv tkedfmknis avsnlrlras
      721 yglqgnidrn tspffigeyn datilpggke siinvlsppn dklrwekttn tnlgldlglf
      781 nnrvsltadv ysrkgtdmis mketpletgf eytmmnwgsl tnkgfelais trninhdnfk
      841 wtttinfahn ksrvlseqpr dnallpsreg lpvnavfalk tagmdeqgnp lfwkgdqkis
      901 aaeffklydv yadflpgqlv dtklsnaelr slftyvgdrd pkftggiint fkvsnfdlti
      961 satfnlkqtv mrtpsyrgme ldrgrnytre iyeaggslpg itspdmeanp dgwmankwft
     1021 gnrsnaysll dvwakeisyi rissirlgyt lpkeftnpmg itslrlsveg rnlfvfsngy
     1081 kgyfdpetyg niyaqpitks vtvgfnvsf
//
LOCUS       WP_114819351             998 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Chryseobacterium].
ACCESSION   WP_114819351
VERSION     WP_114819351.1
KEYWORDS    RefSeq.
SOURCE      unclassified Chryseobacterium
  ORGANISM  unclassified Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="unclassified Chryseobacterium"
                     /db_xref="taxon:2593645"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109038
     Region          19..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltasllv lvlsssiava naqqkndtik tkeiegvvvt algikrekks lgyasqeika
       61 salsdgttnt gnigaqlsgk vaglnvttnn nfggsanlli rgvktlgggn plividgspv
      121 nntytqeksi dygnalsdin qediesinvl kgaaasalyg erglngvivi ttkngkgkdd
      181 gswgvtlsss vnvgfidkst fpeyqtryga gysqkfgsqg pgglnnanfg adaswgpkfd
      241 pnllvyqwds fdptspnygk atpwvaakng pieffnnpat ytntvtlekg ekgknisfty
      301 dnmmsdglip nshinkntfs lkvnydltsk lhssfystmt lqdtkgrsit gysdntvtgf
      361 rqwwqtnvdv kdlerayfan vnpsiasaln nygnvtwnrk sasngapayw nnpyfqayqn
      421 ytsdrrhrnf tyaqltydll dnisvtgkvs ydrsnlfaen rvavgsvaqp fgqsgndvss
      481 gyarrdvlrt etnydlmvny kfditddinv sgvlggnirr nyfnsvygst egglvvpgiy
      541 alsnskkapl asdeseyttq tnsgyitasf dffkkfyidg twrvdqsstl pagnnvynyp
      601 svtgslimse ilntkswmnf wklranyaev ggtadpymlt nnyrsagils gvgiyssiln
      661 qanpdlkpqr skefevgtea hflkdritvd fayyktktid qiitlpvssg tgytgkvina
      721 gridntgfev qlglvpiktk dftwnidanw sknknevvsl ypgitnllln sfqggvslna
      781 rvgeawgtli gsdyvylngq rvidpdtgiy qtnsnqiign ttpdwiggir ntfsykgfsl
      841 sflidmrkgg difstdmyyg mdtglyketa igdyrdkdvi lpgvlpdgtp nnialsqfst
      901 gsnygyetqp akefvydgsf iklreasigy mlpksllagt kiydakisiv grnlwiihkn
      961 lpyadpeami ggginsygws igsmpttrdi gvnvtfkf
//
LOCUS       WP_114819353             993 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Chryseobacterium].
ACCESSION   WP_114819353
VERSION     WP_114819353.1
KEYWORDS    RefSeq.
SOURCE      unclassified Chryseobacterium
  ORGANISM  unclassified Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="unclassified Chryseobacterium"
                     /db_xref="taxon:2593645"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109328
     Region          28..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltasvfa vvlsssfvmm saqntkdtlk tknieeivvt galgikkkqd avtaasqvvg
       61 tkelnaasnp navqsltgkv aglqitttnv gvnssnrivl rgtrsitsdn qalividnvi
      121 sssavfqqlp pdaienvnvi kglqgaalyg sqgvngvivv ttkkgsnnqk iqfnltssve
      181 lssvyklpki qtkygqgvqd etfssvdyng tnhvpwents wgpafddpni ggqyvetglp
      241 qadgkflfak yspvkdhfak ffktgvtfqn gismnvggsd ayaylnlnrm ssdfmvegdq
      301 mlknsflfka gkkfgkfrid gdinyiyrst tetshdlyge mlqmpsnidi rnyrnsgleg
      361 nysvyalnpy wtiqneryna ktnfistiig lqyefndhin vtykgglqnt mgdfdnynng
      421 fkftrqyngt gtgidgtyfs dygtgdvtsl frqslsktsn yygdllvnfd ynltdnivlk
      481 lntgintqdn nyrinevgge nlkiakwyny anvlnpylay qlnnyqlrsr vfavlgnldl
      541 syknylylng tyrqewnsvf svrptgtyeq dlrsygyfsa glsfiptnaf eslkgdilny
      601 akislsytsv gnapiaayav dqigsfptgy pfgtntayia nqnptselir penvytkean
      661 lylgffkdrl tltgsysqsd tkrlitrvts ssttglaslq nnfgrmvnnt yelelgitpi
      721 kskdielnir gfysssiari kelpegvdev nllsystpgv gifaikgekm pmikgtkyqr
      781 dpngniivds ngnplttstf eilgkanpdy ilgmnlnfri kgftlsgtmd yrkgasfism
      841 skrllmftga dpmtadydrs kgyvipnsvq lvngnyvtnn tpvgntpeyg gavsyftgag
      901 rnigenlvvd gtalkvreia lsyslpksll astfvnsatl gvfarnpfik yadnnlnynd
      961 petasgngna ngialdtqyp nyrtfgfnln vtf
//
LOCUS       WP_114820966            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114820966
VERSION     WP_114820966.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115982
     Region          36..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqlnkglpl aagvfcflls tnqinaqkiq kdsvknkeid evvvtalgik rdqrklgyai
       61 tkvetkditq agvvnpmeal qgklpgveit agsggpqssa riqirgntsl ggnnqplivv
      121 dgviidngvt gadswgsgyd fgnemknlns dvfesvsilr gaaasalygs raangvivit
      181 tkkgkgtngl gvrvnssltt qhvyngpifq nefgagfssg fstdangdrf idpnnffysy
      241 gpkfdgkpvq didgrtilwn pqpnnykdiy qvgfdrknsf elsggndkst illsytnqea
      301 dgilprnkfi knayfirath qyskylqvda sfnynrsfgq npvpqggnes plfsfiygtp
      361 rsfdavywkn nyldpvkggm kqdnadpygm astyfnlfqn trtqkennyi grielksqlt
      421 dwlnllvtgn fnnydfines kilgenpgft gggysilegr keqyttkfll nanfkltenl
      481 tlnasigged frskykatrq wtngglnspg vfqiqnsidp vgsetyyadg nqspkriqgl
      541 yafanfawkn qlfiditgrn dwsstlaypd ghgnisyfyp sfvgnwifsn slqlpkwins
      601 gslrgslawv grdtspysts sglyyrpdps aynspdgtri plvgfnsnsl anlnlknels
      661 rsiefglnma flnnrldfdv sfyktnttnq lltlslpqes glsqqqinag nlqnqgievi
      721 vnaipvkssn fkwnttvtfs qnrdkliely pgvteyvlnw gmgtdvksia ipgqqygliq
      781 tkyayaryqa ldangnkidd prngmkvlka dgsylrsdsy qnqgyttvgk ltpdflasfr
      841 ntfryknlsl svlidarvgg dilsatynyg vqfgnlsstl qyrdeerggi kytdsngniq
      901 fgvipegvfn qntsikdkqg vtrdvsgmty qeayekgwid pvstasyynn lgswsrgire
      961 qsifentwvs lrearltysf kpemikslgv ntlnlslivr nlfyiynklp dginpegkys
     1021 nsagsfaeyg gspmsryfgf nldfsf
//
LOCUS       WP_114820533             912 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114820533
VERSION     WP_114820533.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 912)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 912)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 912)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..912
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100226
     Region          33..910
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfttvlki apafllastv ihaqtkdtls kekkidevvl igygkqkktd ltgsissits
       61 kdfnggaata dqlivgktpg vqitgnsgap gsgstirvrg gssfinndpl ividgvpidf
      121 nslsgatnpl slinpndiet fdilkdassa aiygnrasng vilittkkgt agkfkvnfnt
      181 nfsvstkmgn vdvldadqfr sfvntfgtnv qksylgtant nwqdkiyqqa wgtdnnvafs
      241 ggvkglpyrv slgyneqngi vrtnefrrts lglnfspkff dnhltvngnf kgtfsenrfp
      301 dagaigasiy fdptqpvysg nskyggyyew ldpantatgl nvngtrnplg llygkrdiss
      361 vfrvipslql dykfhflpdl rlsitgsydy aksdgsvnty keyaqgigtl gsyrsysqei
      421 ksklfesyln yvkkinaint tvdiiggysy qdtrsitpea ptyygngqkt dfstagdtqr
      481 tllsfyargi ftiadkyvin gsirrdgsst fwngadksql wgnfpavsva wkineesflk
      541 nisaikslki ragwgktgqq etgnfypafg sysysnssta qyqfgnsfyt llrpdvynpn
      601 lvwettttkn lgldfailnn risgsidyfd kksenliakv ptwagdlsnf niknvgvian
      661 kgfeanlnlv pvknemvtwd vnlnatrfnp rvtslsqyvd ssykiqvgtl tginnyiqai
      721 tvgqplnafy vyqqvydsng kplegayvdr ngdgkstedd kyfykspnpd vilgfstkvs
      781 vkkwefstsl ravlgnyvyn nsasnssian iqannflsnt nssvlttqfa atqlfsdmfi
      841 edasflrmdn fsiaynagef mgkgtnlrvn amaqnvfvit kykgidpevf ggidngfyqr
      901 pkvysvgfnf qf
//
LOCUS       WP_114819881             948 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Chryseobacterium].
ACCESSION   WP_114819881
VERSION     WP_114819881.1
KEYWORDS    RefSeq.
SOURCE      unclassified Chryseobacterium
  ORGANISM  unclassified Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="unclassified Chryseobacterium"
                     /db_xref="taxon:2593645"
     Protein         1..948
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103598
     Region          29..946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklsvlta gvlffsgqav faqtdttknt kqieevvvlg yskkstkaks taasvtidsk
       61 alenrpnvsf inslqgnapg isinstsgsp gsgkinvmvr glssinastd plyvidglit
      121 sasqfrnlnp edidnisilk daqataiygn rgangvvvin tknakynsgl rvtydmltsf
      181 svlpktkynm lgakdllnle hqygvgdggd mtqdeinawk tdtdwnkqff qtamlqqhtl
      241 gitaggknin nytslgylnt dgtfrstdfq rftlrnnltg ksdngkltfg mqmavgyskr
      301 hqldqetndn isaniiqnpl fgslrtpgyl epypfingqd mfnqiggagt nypgwvladi
      361 vrggivnlft etsilananv nykitdwlsv gnrtgmdfre sdrtfarnpt gylslaaras
      421 gaqyggfeqm tntkdltfns vsnitfdkkf gehsltvaay ldylkahylf ksntqngldp
      481 fnwafgagtg yipfnpatps lyvpqvsagk inagtlavig tleydyagky gvsatvrrdg
      541 syrfpkenrw etfwsvggrw niekesfleg stavnmlklr gsygttgnqn liqpanngnp
      601 lfvgtniytd liasntgymn svgynavign pnvkwekvsq anigvdfglf rnfvegtvdv
      661 yrkkterlfn sitlsavtgq ytingnngel enkgieaslr fnilknqdys vsifangayn
      721 knkilsfdga dlsddnvnaa ggpigqwnly hyvgvnpatg eqqfigkdgq vtespspddk
      781 vltgksyvpk ftggfgvnan ykgwfadvlf syqaggwmyd nvyswlmdps slgtganfag
      841 dilnswtpdn pntnipsmta nntglegssd rflfktdfir lknitfgynf nkdllknlpi
      901 tgikvfvqge nlatftkwkg ydpepmfays lgvypnpkti svglnvqf
//
LOCUS       WP_114821180             912 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114821180
VERSION     WP_114821180.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 912)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 912)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 912)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..912
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102347
     Region          31..911
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqknltts vcfflmtgfm aaqttkktds leekkiddiv iigykaqkks sltaavsvis
       61 dkklqdsntp svsgllqgka agvqvmpnsg aagssatvki rgnstingps salwvvdgvv
      121 mpyapnldpn qiesinilkd aastalygsk aangivqvft ksgnsgkgtl saslnnsfnv
      181 fnngrfklmn gtqlydyfts lkgapeipkt lrndgynwlk ggtqtgvvqn ytidfrggsd
      241 hsktyisgny ynetgtikgd eynrlsfrin heqtikpwli lkpkvslsyt tgkdtqasly
      301 qmylnmpwdn prdangnlir vdedyadwyg rdkssylydl qwnygksnql dlignldaev
      361 rftdylkfit tnnvtyknyd dmyytdprsi sgtsnkgelt enyqkdiskf fnqmlrfdkd
      421 fgnhninala ayeytdrfyk ssragvygvv pgtdifntga stgqkptgrk fdraynaflf
      481 nteyvydkky fiqgslrses ssafgannrn glfyaysvgw nihkenffkv kpvnewklra
      541 srglvgntps pdygwqdlyr ltekydgqig atwyqlgnpg ltwesiyqnn igtdikafnn
      601 rltlnidyfn nktknllmlv plpsltgvdr qyvnigdvrn kgwefnvnys iirsedinwd
      661 lgfnistykn nvlstrnngt qvldnyhvai qgydvnsfym rkwlgvnpen geaqweiinp
      721 dgsrsatsky nlatvqvvga atpdyygsvs tnlniknfyl aanlyfsqgg qvynsyrelf
      781 dsdgaypyyn qmvlkdgwtr wekpgdiath paavynnnsl tnkpssryle dasfvklrsl
      841 rigynlpasl tekmkiksan iyimgenlft itkfsgvdpe vgnadsqsvy sgnagaiypi
      901 prrfslglnf sf
//
LOCUS       WP_114821783             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114821783
VERSION     WP_114821783.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108899
     Region          36..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkqcklgv lalllfaeyg faqskdslsk etsikevvvv afgkqkkeei tgsvqslkak
       61 dlsnlqngni lqgiggkvag vqvissgqpg sqptirmrgi gsinassdpl ivldgipysg
      121 nlnsiaasdi esisfledas snalygsrga ngviivntkr gkskgvsiea dvktgvnfrs
      181 iedysvytsp qdyytayynr arigeiarlk qpgavpsgps phdvglsalt klgynvynvp
      241 fnqliskdgs fnpdakllyq ddwkkllfrp alrreatvgi nangdqvksy tslnylddkg
      301 ylissgferf girsnvdyai tsklkltsal sytyskqdfg etggfsnpfq farniapfyp
      361 vflrdnnyqr lydsygnaly dygdgqgpng atrsyavfen pvgnlqknks qivsnvtnln
      421 lglnyeiikg ldftynfgay lentrnlqfg nteggtsssv ggtisqssnf kytlnhqqll
      481 tyqkklgnhs fnllvgheln kikddgfsgs kqqlllpdsq afdnavkitg lsgsgyeyav
      541 egyftrllyn ydgkyffnan irrdgssvfs pesrwgnfyg lglawniake dflkdnsvin
      601 slklkasygq qgndnillgg ssrdyyayqd iyginnfgdd kpvlslkkqg nkdlkwetsk
      661 nlnagfeisl lknrinlnad yferkvsdmi ytlplppsna gsyvkygnig dmtnrgvqan
      721 isvdilrgde fqwsfyanat hyknkitrlp aeqrntglvs glfilteggd rytyflkefa
      781 gvnpengdal wyrttinpat qkeertvtnn ykeatdyntg ksaipkvygg fgtdfsykrf
      841 nlavnfayqf ggygyddiyr slfhsdtygs nystdldktw tpenptaalp rvdltatnqn
      901 gnstlyliks dyislqdvtl syqlpegfaq qaglsglkiy vtgnnlylws krkgydpras
      961 ltgvsdayry sllssvslgf klnf
//
LOCUS       WP_114822193             965 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114822193
VERSION     WP_114822193.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 965)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 965)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 965)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..965
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106082
     Region          29..964
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktifkvgl lqslfffggl yaqsdstkts kidevvvtay gvkkekkalg ysfqdvkgqt
       61 lvdakennvt nalagkvagl qvikgsfgpg ssskinlrgf nsftgdnqpl ivvdgvplsn
      121 slgskakqng kdsnndfwnp dldmgnglsd inpediesls vlkggaasal ygsrggngvi
      181 littktgkrk gglgitysts lgfenifmkp dlqhsfaqgs nglpnpqgtd nttswgpafe
      241 gsnmtvhdnl knffktgtta qhtlsfqeni gegsslytsa nylssnsqip nskyerfnfm
      301 akmnsnfgan krwttevkaq ymsvkgtnrp sagqgdgnhy paillmpqni dvrdyregqm
      361 qngvtsrwit snginpywta ynalnddkkd rfllngylky qfnnwlsadv rlgtdfysln
      421 tnarvwtgsr rnnsystgqe kfyennyiis lnakkdnivg kwggslsvyg qmmesrdkal
      481 yfstqnlvia nvfstsntsd lasvtttevd mwkkinsvfa aaeinydgyw flnatarndw
      541 sstlninnrs yfyssvstsl vltdmlkkln gttlnaltfa klraayaivg nslppqslyn
      601 tyiastdpng hivlarnkil fnpdlhaekl ktfevgadmk ffdrvsldvs yfnnnatdql
      661 iaipinplsg yermminsgg lhnkgfefvm ntdilkkesf vwnvnanfst lkskidkidg
      721 ivskyplsgf dnvaffaevg kpygaiygtk flrvedtssp yygklivdqn glpqatsdqy
      781 ylgdqtpral fgftnsfvyk niglsflidg riggkffsat qaalqangla adtapggkrd
      841 nmildavveg nggytantke itqqdywgav tsgnlgiteq niydatnirl rniqltynfp
      901 ksifqklalq sakvaftann vwmiyskakg idpesvfain snatgfenla fptsrsylft
      961 itlgf
//
LOCUS       WP_114822202            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114822202
VERSION     WP_114822202.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118232
     Region          22..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlatfav fllplyfsaq einisgnvks engssvsgvn itdkntgkta ttdengnfti
       61 sanpkdilef fapdfsvytv evsskkqysv vlkrpnekqi egvvitalgi akkkekigys
      121 tqevgtkqfe tittpsignl fsgqvaglnv snptgmqqap qftlrgnsnl vfvidgvive
      181 kevfqnldpn nieninvlkg atasalygsr grygavlitt knakkkgfsv efsqntmita
      241 gftnlpktqt eygngshgky efwdgadggv ndgdmiwgpk fvpglqiaqw nspirdkvtg
      301 qvvpwygavt gtqyddksky ervpidwkyh dnlstflkpa vinnnnfais yrnnkdvyrf
      361 sgnfmnyddr vpnsylqkyg infssenhlg eklifdtkfn fnqaftpnip nydynpsghm
      421 ytiliwmggd vdgkalknhm wipgkegraq anwnyawynn pwfgaeyykn qnrtniinaq
      481 tgleykatqd lsvkgkislv enhskteils pysyfnysap rsggyilkdn ktwnlnydvl
      541 atykkkisen fdftinaggs afyyknnnne rstdglkipe vytfensiga lknytylkek
      601 liysaystid iglynaffin vsgrndwsst lpkanrsyfy psasisavis nlvkmpesin
      661 mlklsaswak vaydfqpysi rnyylnnegi tfngnptyyy pttlnvensl kpeqtksyel
      721 glsagflnnr itldatyfrt ldynnilqfp aaessgftsq yvngneyttk gfevslglvp
      781 vktsdfswkt linwstyeqk ltsiydnmpn ykniqlgerm dsyydytwqk spdgkvilda
      841 ntgmptrana psnlghfnpd wtfgfnntfk ykkftlnigi dgsiggvmrs qvvekmwwgg
      901 khpnsvayrd leyanpgtyy fvpdgvnynp atgtytphtk aisyqdwaqn ypyrarvtqd
      961 eseefanvfd rtfiklrsvv leydfsslln prgmvkgfta nisaynlamw kksknlysdp
     1021 dfqtktdndi qdpssrwfgi gfnlkf
//
LOCUS       WP_114822301             988 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114822301
VERSION     WP_114822301.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107601
     Region          19..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkavipvlf vfsltanaqe kkaadttktt sieevvvtsl gikrqarslt yssqqiggde
       61 ltevktpnll nsingkvsnv qinrtngvgs svrvvmrgdk svnsaqplyv idgipiingt
      121 gksadigqys nmpdpgdvls sinpddiesi nflkgasasa lygsaggnga ilittkkgra
      181 gkssitysss ltidrayslp klqhsylsyd pavsgsqpgq steswgakgv skdylkdflq
      241 tgttwvnsls fqsgneksts yfsignttnk gvvpmsyfdq ynvsfrnssk flddkltlda
      301 nfigslqesk nrqtpgasfs pltslywlpr gvdfdqygpd nytylnkerf lpaqnwwevn
      361 pdgsfkgnpp tqnpywilnr npvtvsnknt ygalslsyqi npwltarvrg nyswnisdsq
      421 rdiaafsapt llavneging rilkntyens stygdvllig spkisesfsl dftlggsint
      481 trnkigqidn ayltnpnlft vsnlewgkkr spgdgyhniy tnmkkqvqsv fasatvgykn
      541 mfyvdmtfrn dwdsslaltg rtgfdyesvg anavlssvfk lpevisfwkv rgsyatvglg
      601 lptnisnami eynkgytfgv dagtlvfpks sfitdpkykd lfpkpefnkt fevgtelrmf
      661 snklsfdity ynsntsnqll etkidsyfgg iapgsyyina gkirntgfes slsykvfsse
      721 kfgwtttlna sanknkivel fppslpisen qlfsltggge ytklklggsf gdlygikfkr
      781 ddqgrilvne kgiplaegtp sylgnpnpkf imgfnnsfni gklgisflid gkfggkvlsl
      841 tekandiygv sqstadarda ggvsipnavy apgtpnagqa ytgltdakdy ykavgttegf
      901 gkgideayly sattirlrqa sisytfdiqs kymrnatvsl vgtnlfffyk kapfdpeqvs
      961 gntpggvgvd sfglpvtrsi glslkanf
//
LOCUS       WP_114822479             946 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Chryseobacterium].
ACCESSION   WP_114822479
VERSION     WP_114822479.1
KEYWORDS    RefSeq.
SOURCE      unclassified Chryseobacterium
  ORGANISM  unclassified Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 946)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 946)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 946)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="unclassified Chryseobacterium"
                     /db_xref="taxon:2593645"
     Protein         1..946
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104475
     Region          32..945
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqsnlkypc liavlyfgmn vnaqvtqdsa kvqkidevvm igygsrkkvd nttaissisa
       61 eevtrtkvln asqaiqgkaa gvqviasdap gstptvmirg lgtvlggrtp lyvvdgmyad
      121 ninninsndi ltydvlkdaa alaiygnraa ngviiittks grgklsvsyd glvgfrsplk
      181 tikmangsef atynnagkts tylnpnqpyn tdwfkeitrt giynqhnlsi sgsseaakyf
      241 lslsnydeqs ilkgtnynrt tvrtnnefri tkgirlaqtl satftndtpk sygaftnayk
      301 qsplvpvyyp ngkygqpiyn ktngnidyeg grfnnvgnpv mqlaydnqrg knfllqgglk
      361 ldidiykdlk ftsqfsgeyn nykyynfvns kafwldsdpm rvdsgydtsl pltrltnknq
      421 nyynwvlnny ltytkkvgnh dieivagtea svangletlt inrknvpvsq dywnldgvdy
      481 ygnlfsdntt kaiesikgnr nttisyfgrl qykfmnryll sgtirrdgss qfaeghrwgt
      541 fpsfgagwii seesfmqdgf fdllklrggw gklgnqkvpl nylplssgat ynygfgtspv
      601 sngvtvnqgy dpelgwevte etslgldfai ldkrlsgsfd vynrktnnli lgvvpylatg
      661 isdvnyshmg svvnrgaevs lnwsdkvged fsysvganys ynknklarid tskpvsqiig
      721 gnlgngvdtk lfnasaigya lgsfylyetd gydangnlkf kdlngngtmd ggdrrffdsy
      781 ipkstlgvnf smsyknwdfa lsgygafgfk vyngkkaqrn ggenveasva ndfwtptntn
      841 aanpvnpsni pvasnfyles gdyfrinnis vgytfknvtd ymrsiklyvs ainpivfqky
      901 sgysselsgy npadttaegd pykragield ayptlrsfvf gvnlnf
//
LOCUS       WP_114822576             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. KLBC 52].
ACCESSION   WP_114822576
VERSION     WP_114822576.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. KLBC 52
  ORGANISM  Chryseobacterium sp. KLBC 52
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Chryseobacterium sp. KLBC 52"
                     /db_xref="taxon:1862702"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109416
     Region          35..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrketqkllv lsllglvsvh laaqqkakkd tikgidevvv talgikrhdr algyvaekvd
       61 aktfeetqnn nwaqsmegkv aglkiqtaga gplgtsritl rgeksimmdh nyalivvdgv
      121 plgnsttgsg taaygagsgg dvpidlgngl nsinpddies vtvlkgasaa alygsraang
      181 almittksgk tkngklrvtf nssssfdsvl kwpdwqyeyg qgtlatntag nfyysyglsp
      241 dgpstggtss afgpkfagqy yfqydpnvig qsterqlwra yennikgfwr tgstysnsis
      301 vessnektsf rssltylnne wmmpntgfdr fnfalsfahq ltqklkistk fayntttsdn
      361 lpatgynnqs isyfmifqnp nvdlewykpi wkpgqeqvdq ihpfssyidn pymiayemln
      421 gvrkktitgn itadyqfnkn fslmlrsgie ilnekrttkr pwstanylkg fyreqfiknq
      481 eynndllfsy kadwnkfsis asaggsiryn eylqndyqai glktageysl tnalsipvky
      541 paprdkhvds vyglltlgyd nkifvdftgr ndwsstlpkq nrsffypsvs tsfilsdlfn
      601 lksnnlnlwk lraswakvgi dsdpylldny ytasnitgsv tgpttfnnpt lkpekntnie
      661 agmdfslfrn rlnlnltayq nlsenqiipv slpteagysk riinagkirn rglelsadil
      721 avkgkdfswk vggnwstnen rvmtlpegfd givsnvgdvv fykmevggsl gdmygfkllr
      781 tpdgkviygd nglparpadi ekvgnafpkw raglqndfki knftisfsfd gqyggiaysq
      841 shhkmseqgk lkstlpgrdn pggmivgdgv vqnpdgsfst ntkgvlvssy ygdyyrranv
      901 etnsfstdfi klrdariays fpketiksig lddltiaifg knlwmwtkfp mfdpevatld
      961 natitpgvem gqlptartvg fqlnlkf
//
LOCUS       WP_114832765             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Allobosea
            caraganae].
ACCESSION   WP_114832765
VERSION     WP_114832765.1
KEYWORDS    RefSeq.
SOURCE      Allobosea caraganae
  ORGANISM  Allobosea caraganae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Allobosea caraganae"
                     /db_xref="taxon:2763117"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38874
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaetq gaetrvavtp etvrkfiglg aevavqagag lasgitdady taagatvtas
       61 aaealagaai vlkvrrpsea eaaalpagal vvgimdpygn eaaveglaka nvaafamefm
      121 pritraqvmd vlssqanlag yravidgage ygralpmmmt aagtvpaari fimgvgvagl
      181 qaiatarrlg aivtatdvrp atkeqveslg akflavedde fkqaqtaggy akemskeyqa
      241 kqaeltashi akqdivitta lipgrpapkl itaamvesmk pgsvivdlav erggncelak
      301 pgevavtang vkivghlnvp grlaatssql yaknlfafve tlidkgekkl avnwddelvk
      361 ataltrdgav ihpnfapka
//
LOCUS       WP_114834362             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aquicella
            lusitana].
ACCESSION   WP_114834362
VERSION     WP_114834362.1
KEYWORDS    RefSeq.
SOURCE      Aquicella lusitana
  ORGANISM  Aquicella lusitana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Aquicella.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Aquicella lusitana"
                     /db_xref="taxon:254246"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41533
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipkeiv peesrvaavp etvakmikag wevvvesgag arsyiedqdy ekvgakiaas
       61 pemlfdqaei vlkvqrplfn dkkslheldl mkansillap lfptrhpell aklnakkits
      121 fsldmvpria raqsmdilss msniagyksv imaanylgkl fpmmttaagt ilpakiivig
      181 agvaglqaia tarrlggvvl afdtrpiaee qvqslgaefv clqtshaeaq daggyakeqs
      241 adfyqqeqav iqqhlkeadv vistalipgk papllitaem vktmkqgavi vdlaveqggn
      301 caltkpgeii ikhgvtligv lnvpgtlpih asqlysrnlf aflnhinpqr hvnewdftde
      361 iiksclithq getvhpsvqq vklpag
//
LOCUS       WP_114862161             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Azospirillum brasilense].
ACCESSION   WP_114862161
VERSION     WP_114862161.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum brasilense
  ORGANISM  Azospirillum brasilense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Azospirillum brasilense"
                     /db_xref="taxon:192"
     Protein         1..>381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiprerr agenrvaasp etvkklkals levvvetgag lgsnlpdrvy qdagaeiapd
       61 aasaladadi vlkvqrplla gegdldelal ikrgallfai lnpynsrdhv aayaaagvna
      121 famefmprit raqvmdvlss qanlagykav vdaaseygra ypmmmtaagt vpparafimg
      181 vgvaglqaia takrlgaivs atdvrpavke qvqslggsfv avendefkqa etaggyakem
      241 sddykrqqaa lvaehikkqd ivittalipg rkapilvtre hvasmkpgsv lidlaveqgg
      301 nvegselgrv vvtdngvkiv ghanypsria esasllyakn llallqslhd kekgialnwd
      361 deivkaialt rdgqvvhpaf a
//
LOCUS       WP_114880919             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_114880919
VERSION     WP_114880919.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38817
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnndt iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv tivgptnlag evaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_114880581             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfitobacter sp. SK011].
ACCESSION   WP_114880581
VERSION     WP_114880581.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter sp. SK011
  ORGANISM  Sulfitobacter sp. SK011
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sulfitobacter sp. SK011"
                     /db_xref="taxon:1389004"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55116
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif egearvamtp dsaqqlqklg hecvieagag aaagfddasy kaagvevvkt
       61 aaalwkaadv vakvrapdaa emkrlregqt lisffspvan ekemkqaadk gvtvvamemi
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkmppakv lvvgggvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee eqadgsasgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvaam kpgsvivdla aekggncklt
      301 vmdekivtkn gvtiigytdf psrmaaqast lyatnirhlm tdltpekdgv inhnmeddvi
      361 rgatiahdna vtfpppppkv aaiaaqpkkp aakemtpdek kaaetaafka atksqvtlla
      421 vggavmllig afapasfmqh fivfalacfi gfqviwnvsh alhtplmavt naisgiviig
      481 allqvgsgsf lvillsfisi liasinvvgg flvtrrmlam fqks
//
LOCUS       WP_114885516             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfitobacter sp. SK012].
ACCESSION   WP_114885516
VERSION     WP_114885516.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter sp. SK012
  ORGANISM  Sulfitobacter sp. SK012
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sulfitobacter sp. SK012"
                     /db_xref="taxon:1389005"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55336
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkety sgerrvamtp esatqlqklg hdcvietgag leagfddasy kaagvsvvkt
       61 atalwkaaev vtkvrapsea evkklrdgqt lisffnpagn adlmeasakk gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqadgsasgg yasvsspefr
      241 eaqlakfrel apeidivitt alipnreape iwtedmvkam kpgsviidla aekggncklt
      301 vmdekvvtdn gvtiigytdf psrmsaqasa lystnirhml tdltpekdgv inqnmeddvi
      361 rgatithakk vtfpppppkv aaiaaapkkd kpkeltpaek ranevaafka atksqvtmla
      421 iggavmllig tfapasfmqh fivfalacfv gfqviwgvsh slhtplmavt naisgivilg
      481 cllqigsgsw lvvllsfigv liasinivgg flvtrrmlam fqks
//
LOCUS       WP_114891118             508 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus haemolyticus].
ACCESSION   WP_114891118
VERSION     WP_114891118.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     gene            1..508
                     /gene="nrfA"
     Protein         1..508
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56753
     Region          1..501
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnafkksliv aasfaslslf nsavadmvyk pleqpvepvk pdlkiesvne kfaekypnqy
       61 nswrstangk gekiiyadee nprlivlwgg yafakeynap rghfyavtdv rsilrtgapk
      121 tandgpqpma cwtckgpdvp rliaewgekd yfnakwakgg peivnsigca dchdttskdf
      181 aegkpalria rphvlralda lekataekdk aegrphnnls fntaartekr aeicanchve
      241 yyfagdikqv tfpwnkgqtv ddiekyydei gfsdwthsls kapmlkaqhp dfeiwslgmh
      301 gkngvtcvdc hmpkvqgkdg kvytdhqiqn pfdafdrtca nchdqskekl rdivtsrkke
      361 vkdvmgrlee qvvkahfeak aawdagatke emeaalmdir haqwrwdyaa ashgghmhap
      421 evmlrvlgsg ldkaadartk laailtkhgv ktpvqipdis tadkawkvmg idiekerkak
      481 eeflktvvpq weqqakekgl lvdppaqk
//
LOCUS       WP_114898672             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aquirhabdus parva].
ACCESSION   WP_114898672
VERSION     WP_114898672.1
KEYWORDS    RefSeq.
SOURCE      Aquirhabdus parva
  ORGANISM  Aquirhabdus parva
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Aquirhabdus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Aquirhabdus parva"
                     /db_xref="taxon:2283318"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39283
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaesv agetrvaatp etvkkliaag htivvergag vkasyidsaf eqagakitdd
       61 ayqgsqiilk vrapkaeeiq kisantivig mfdpyrnpdl dafaaqgvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaneyqr mfpmlmtaag tvkparivim gvgvaglqai
      181 atakrlgavv eatdlrptak eqveslgakw ldvpmsdeek akalgtggya wipseqyvqd
      241 qavivdkavs nadivittal ipgrnaprli kaatvakmkp gsvildmave tggnvegsvv
      301 getvmtengv kilgipnipa tlatessaly arnvfnfvst lfdkegnlql nqeeeiqkal
      361 lvthggqvll krg
//
LOCUS       WP_114900952            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Kordia sp.
            SMS9].
ACCESSION   WP_114900952
VERSION     WP_114900952.1
KEYWORDS    RefSeq.
SOURCE      Kordia sp. SMS9
  ORGANISM  Kordia sp. SMS9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Kordia.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Kordia sp. SMS9"
                     /db_xref="taxon:2282170"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117678
     Region          25..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfngmlt lllalmvqla laqektvkgt vsdesgiplp aasvvvketn sgtttdfdgn
       61 ysiqvnqgqt lvfsyvgykk keivvggnnt idtslepdnq leeviitaqg ikkekkalgy
      121 avttvdskdl eqkadtdigk ilrgkasgvr itgsggvsgs gsniiirgqs sitggnqplf
      181 ivdgvpfdgs sgsanqsass gafqsgnvas rfadidpnni esvsilkgls atalyggegr
      241 ngvilittks gkdankkmev tvnqsiffnd iilpdyqntw gngfqnvyga ffsnwgarfd
      301 sqatidnafr tsilnnfgve psvlfpnrpe ldnpnvtyra ydsqeaffkt gtiastsvnv
      361 agsfgdkgsf nasyahvddq sfipnnslrr dnfsvggtfk msnkftlsgk islaktdirs
      421 pftdastgsd vtsstagtgg iasiwnilyl prsvditlpn qhpitgesiw yrggndrtnp
      481 awalnntqdk qstdrvftnf vamyeaadwl nisyrlgids qntkgrrvin kgsndglhpn
      541 gylqttsqrf tiwdqsllig idkelsedfg lqatigattk rqiferdgse srdqiiyglw
      601 nhlnfsnsst iiegtvfadn nttyqtfseq nnvaayvsgt lsyknflyln tslrnewnst
      661 leqenrsqfs pgvsmsfipt safeglrskn lnflklragy gtspgfpgpy ttrsvislvp
      721 nifqtaggns ttttsipnfl pnpdlkpels kefevglear lldnrigfdf tyynrdtenq
      781 iiqrplapet gytstftnig nvinegfeig fditpirted fefkltgsft qnessvkgld
      841 dgeqiqfggl fsgttnaain dqplgvivgg qilrdadgnr lvdengywiq dpnngiigdp
      901 npdwfttvnt gitwknwtvn mqweyqqggd iyattvgalv grglvedtdf drtqsivlpg
      961 vrqstgqpnd iqvtateayf nnigfgidev liydathvrl reasisyrlp kkwldktpfg
     1021 nvsltlsgqn lfvkafntpd svnydpelns lgvgnsqgfd yltswnsrry gmsvkvtf
//
LOCUS       WP_114900955            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Kordia sp.
            SMS9].
ACCESSION   WP_114900955
VERSION     WP_114900955.1
KEYWORDS    RefSeq.
SOURCE      Kordia sp. SMS9
  ORGANISM  Kordia sp. SMS9
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Kordia.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Kordia sp. SMS9"
                     /db_xref="taxon:2282170"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112549
     Region          25..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfsgilt lflalfvqil faqqqtvsgt vtddtgmplp gatvsikgtt sgkttdfdgn
       61 ysiqanngqt lvfsyvgyta qeikvtstti nvqlkqgeal eavtvvaygg avnsakvass
      121 iatvdgstie qvpinsldqv lqgaaagvnv ntgsgqpgqs atiiirgrgs lngdieplfv
      181 idgvpvdqdn frslnqndie tlsvlkdaaa taiygnrgag gvvivttkkg kkgsgvniqy
      241 ralygvavkp ktrfqvmntt qlltwqrdll pgtqfgdgqs daqiariagq antnwediff
      301 qqgttvshel sistgnents sytsmqyfkq egitlgsdlt rfsfrnnfng ssenkkfnyg
      361 ttltlnrsvs nfivdaargn ntggqldnpf ivpyignpym spynpdgsln ifgtrrsgal
      421 nddgtvgdpn gflntpflal ntarlntdqe tefkavgsin adynfaknlt iggqigidyt
      481 niellqitap gsirglitpn qgsevkgdqa etyfrdanfi lnaylryqnd itdklslsas
      541 lygeynysnt qsagfrafgl npalptssag ftsgntqege dengdgilda atelalnyvp
      601 tvfssesela lasifgtldl dydgkygfsg tirrdqtsrf pknptgtfws vagrwnidre
      661 dfmsdvdiin alkirasygv vgnqtvggry qglqtvfadp tsyqlgtgyg lgglvdeeiq
      721 wettnqlnvg lsfglwnnrl sgefdyydfl tdrlfsddap lsvaqtgynt vitnigsmrn
      781 sgvdlqlayd vlrksqtnpw aitvrangny nknrveelpv gftgntlrvt egrqaftwfd
      841 vrwagvdpsn gqplyydidg nitnvfdpsn avyldknfdp tytggfgadi sykgfalnal
      901 fsfaadrwrr ngslaiveda slagfanqsv tmlnawttpg qvtdiprlsf qgraevgdry
      961 iedasflrlr nlslsytvds kilektnvfs girvfvqgtn lvtwtkwrgf dpegnqsggf
     1021 fdypvprtfs lgfdlnf
//
LOCUS       WP_114906941             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ornithinimicrobium murale].
ACCESSION   WP_114906941
VERSION     WP_114906941.1
KEYWORDS    RefSeq.
SOURCE      Ornithinimicrobium murale
  ORGANISM  Ornithinimicrobium murale
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Ornithinimicrobiaceae; Ornithinimicrobium.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Ornithinimicrobium murale"
                     /db_xref="taxon:1050153"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53079
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreat pgetrvaatp qtvgrlialg htvtvesgag elasypdely aeagatigps
       61 pevwgadlvv aidppdpeql dqlrpgayla aqlgpgqhpd llealaergv talamdavpr
      121 israqtldvl ssmanlggyr avieaanayg svftgqvtaa gsvppakvfv igtgvaglaa
      181 igtasslgav vratdirpet aeqvesmgae fvpialdpna tstdgyarem geelqrrale
      241 vcaqecaaad ivittalipg rpapklvtad tvaamrpgsv lvdmaarngg nceltepgav
      301 rtsdngvqiv gytdlparlp tqasqlfgtn vvnlialltp nqdgqlvldl ddevqrgltv
      361 thehqvlwpp ppvsvsstpp papseppapa aepetgatrd prrgyvamgl aavlfalvas
      421 vsppsflghf tvfalavivg fyvishvtha lhtpllaetn aisgiilvga ilqvgnedll
      481 vrslalaatv vasinvfggf avtgrmlamf rreesa
//
LOCUS       WP_114913209             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acidibrevibacterium fodinaquatile].
ACCESSION   WP_114913209
VERSION     WP_114913209.1
KEYWORDS    RefSeq.
SOURCE      Acidibrevibacterium fodinaquatile
  ORGANISM  Acidibrevibacterium fodinaquatile
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acidibrevibacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Acidibrevibacterium fodinaquatile"
                     /db_xref="taxon:1969806"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39337
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavlrerh afetrvaatp etvkklialg lavvvetgag hgaaiaddef raagaeigad
       61 aaatlaeadi vfavqmpead iraqmrrgtl lvaianafad tslvpalaea gidavamell
      121 pritraqamd vlssqanlag yravteaavt fqrgfpmmmt aagtvpparv fvigagvagl
      181 qaiatarrlg aivsatdvrp aakeeikslg aafvgvedee taaqtgayar emseafrqkq
      241 aelmaatvak ndivictalv mgrkapvivt apmvaamrpg svivdlaaes ggncaqtvag
      301 eshvtengvt ilgwrnwpgr iavaasnlya rnlltflsmf wdkeakapkl pesddiikgv
      361 lltrggavvh sqfqppkaa
//
LOCUS       WP_114922022             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            elongata].
ACCESSION   WP_114922022
VERSION     WP_114922022.1
KEYWORDS    RefSeq.
SOURCE      Neisseria elongata
  ORGANISM  Neisseria elongata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria elongata"
                     /db_xref="taxon:495"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54206
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkesl agetrvactp atvaqlqklg fdvvvengag lgasfddaay eeagatvaaa
       61 aevwkcpliy klnapngnec rrlkegqtlv gflypnqnee lvkkladkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fkdviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapeaflnhf ivfvlscvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_114926932             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ornithinimicrobium avium].
ACCESSION   WP_114926932
VERSION     WP_114926932.1
KEYWORDS    RefSeq.
SOURCE      Ornithinimicrobium avium
  ORGANISM  Ornithinimicrobium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Ornithinimicrobiaceae; Ornithinimicrobium.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Ornithinimicrobium avium"
                     /db_xref="taxon:2283195"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52947
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpaetv pgetrvaatp rsvarlvalg hevlvetgag qrasfpdehy vdagarvgpa
       61 qdawaadlvv kveaplveev pllrrgavla tqlspaqrph lladlaergv talamdavpr
      121 israqsldvl ssmtnlggyr avveaaheyg svftgqvtaa gsvpparvfv igagvaglaa
      181 igtaaslgav vrafdvrpet aeqvesmggq fvrialpega ggadgyarem dadlqarame
      241 vyarecaead ivittalipg rpaprlvtaq tvsamrpgsv vvdmaarngg nceltepgqv
      301 vttpggvkvv gytdlparlp iqasqlygtn vanlvalltp gkdgelvldl edevqramtv
      361 thdgevlwpp ppvsvsaapp pspapepaap avrkaapqpa lagrrgvfgi algavllvll
      421 asvsppallg hltvfvlavi vgfyvitdvs halhtpllae tnaisaiilv gailqvgsqd
      481 pvvravavaa vavasinvvg gfavtgrmlr mfrregas
//
LOCUS       WP_114936342            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114936342
VERSION     WP_114936342.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116375
     Region          25..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrlllilc sfvfavtqlf aqnhtvtgtv takedglplp gvsvkikgtt tgtqttvdgk
       61 fslsvpnnav lsfsfigyat qdvpvgasan lkvvleasak glnevivtal gisrqqkslg
      121 yaaqqvkgdd ltvtkqsdln talagkiagv qvlggsgakf gtstirirgv nslsganpiy
      181 vvngvvtdpn avnnddiesl tvlkgpaata lygqrasega vvvtlkkgad kgigvslnqs
      241 ttfekvyqlp qyqneygggt stqwdtytyd pnngspasfa kfngvkiydy gvdeswgpkm
      301 dgtlyapwyf wdpsnpdfgk lkpfvaqpnn vrdfyrtgvt yntnaafska adnynfrvsy
      361 tnidrtgitp nsnqkrnnvg lngelkltkk ltvsanfnfs qinsnnvpqe gygtqtagsf
      421 sqwfhrdvei dklknyrrad gtytswnits pddltphywd npyteayvnt sqsnnnrvfg
      481 nltasyqftk dlslsliare dllnrddnsr vgsgtvntds ysqsqytyke nnyvanlays
      541 hnfkdlsvka glyaetrqdr ylytsgntng glsipelytl tnslnaptsf sykalsrins
      601 yygftsfgyk dflyldfnar ndisstlpin nnsywyggls gsfvftelmp kndiltfgkl
      661 rlsaaklgsd apiysiyqty nltttpygpt kvgnaaiqtv pntlpnpnlk pslstsyeig
      721 telhfikdrv rfdfnyytrt qkdqilplpv ngtsgystav inagqirnng ieitlggtpi
      781 kskeftwnsd fnisfnrnkv islypglnnl kvtpdglggy tasggnqaag tqsfgfvgsp
      841 sfgvngivgk sygqiigsgf trdkngniiv gddglpivnn tvnlgsmlps ftggftnsfn
      901 yknfilafsl dfqkggkfvs vtqqnlngsg lgietvgnna kgnpkrnpva dgggvlvagv
      961 hedgtpntty vetrtlyeqs ysqiwekwty dasyiklrev svgysfpkkm lgrlpfqtay
     1021 fgitsqnpwm iysklkgvdp sqlqtsfyeg gqlpntrnlg fnikltf
//
LOCUS       WP_114935696             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_114935696
VERSION     WP_114935696.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53741
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_114936717             945 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114936717
VERSION     WP_114936717.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..945
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104522
     Region          57..944
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkdyknfla wmltfcsfsa vnaqtavkap adtikkassy kdfvdgglri dkawrntgav
       61 ftlsgedltr mtsgnllntl qgripgltvv tgsgepgydn ptfymrgvss wnlqgnqvli
      121 yldgfqvdmg aisglsayei esvtllkdaa alavyglegg sgvlsirtkk gavlnktqvf
      181 vngkygilsp idlpkvmday gyttnynnal tndglpikya npelykaand pfhpnvnwyd
      241 ellkktsaiq dynfgfrggn ntakffvlmn ytnfeglykn adiidkdfgt nakytklnlr
      301 anielqlnkn lvvtanisgi tedrntpsgf taaqvfnnim aipaaafpvk npngtwgnss
      361 vykfnpiqll qqngvyqsht rnlqtnfsfv qkldkltkgl dlkgevsfan qyvgiyqkqf
      421 svnsfeitgq daqgkaiygs tpvtpisqss sdgggahwnr ttvrvgfdyd rtfgkstftg
      481 miqarrqgyt hdgivyqvrt qgiagnvtyd ydkkyivdls gsysgsadfa pgnrygwfpa
      541 lglgwiaske dflkdnstin flkvrasygt vgnvneayrf lyqqfavsap gwvtgtgntg
      601 hggltegpfa nlnfawekkt tlnlgldftl wknlsgtldv ftekrtgile vptasvpdyt
      661 gfnlqyantg evhnkgleas lkyeqndnkf kyyvggsfay arnkivkrse npqpynylyt
      721 qgypigqmkg lvytgfyqqs dfdangnlkp givassytnv kpgdlkfkdq dgngiindyd
      781 kvpmkysvlp eitlgfnlgf kyagfdfday lqgvlhrtvs lldaaytyth pfvfnnnise
      841 fsanswtpqn aatatsprls tlanpnndqq sdfwmrngnf lklrsvelgy tlpqrgflrk
      901 ldavrvfvng tnlftwdkie gleaerlsmg yplvkavtfg mkvkl
//
LOCUS       WP_114936949            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114936949
VERSION     WP_114936949.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113700
     Region          73..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrylwlcfvv faaittnalt glakgnegkk skvkrpfygk tyvrrdttak dsllkdsini
       61 iirhtlynkf adsvtkkpyd lskfpavslq qllkgqfagl yvqepsgepg svqymfirgv
      121 pmpllsprdv yqsqplvvld giplvtehpf afdiqlydyn rmgtatnpfa aidmnniasv
      181 evlkdlsata iygpravngv ivltsktpva aksitfdsyi glaqrphvtt ingkyenafr
      241 qrfydlyttn grysddenyp iylsdslnnv ysgksdwsdl yyrnavvygi nfgisggtdr
      301 anfrfslgdl knngiadgtv lnrysamfni nmkplkwllf stmvnanrld rqrnrylrdr
      361 faqinyfpdl saplppnkey yadylaqykk gfdnnktniv dgyakigidl gkfkfvttfn
      421 vdynegyrdv fyartllqgn syasnyfgfs qrimadnrat ydltinkvnd fhfelgqstq
      481 wdiykysnay aykgvndyik idlldsnpkn pdgsdnpnyl nptafprelt frfldkikhn
      541 lvsfyaktdy sfkqkyflsa tvradgssna qptsrwfysp vvsaawnikk ellanntiin
      601 dlilrasagr lgrlnafdny aqgpqytasv gytgnltvpg ynafgvltrp ystgwigygi
      661 pwsysnqlni gtdagflnnr lhlsvdwylk qeknlligip afaeygykqs iesgmavnns
      721 gvdvsvsani iqntkfgwss slnlnhnink lkalprglnq itidnkllkv gspvdqywll
      781 indgiykses eipvvngqpl kyngiamhag dpkwrdingd nvidnndkvl kghslpkisg
      841 gydnnfrygn wnlninlyfn lgrdlihqem anrfdfinre gnsdvnsvke itfwekrgdy
      901 skyplynpws tvipyrvdqd lflenasflk lrtvsigydl tkamrlkkik ltrfyvyata
      961 nnvftitpyt gqdpelvnyd gydtgyglpi prtytlgvkm el
//
LOCUS       WP_114936947            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114936947
VERSION     WP_114936947.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116407
     Region          29..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkhilfyiv lvvctifcct evdaqaqnit vtgtvvekat nkilpgvniy mgskgltqtd
       61 ykgkftisvp anstltftfv gfvtekvkle pgqknitvtl tedkkglnev iivayqnrnk
      121 estpgasvti takdiqdvpt snvesllqgk vaglniqnnt gapgfrgsvq vrglstlsvs
      181 gsgsesflqp tsplyiidgv pldadkaaef gfqtqgpgvs plslipvedi qsiqimkdaq
      241 atsmygsrga ygviiittkr gnskvprvry tgnffvnatp qlratiggna errakiqqil
      301 snatvidelr klgqtgflad slnaywnnst nwqsifygtt hnqshnvald ggndrfnykv
      361 nmgyysekgv ikntgfdryn lnmnmefkpn dkfrffgslf gslgsqakgn gvgllqqgva
      421 qngqastllp ppsfylspdg vtsalqtqns nstrnirtni dgryefirgl alsssisydy
      481 tsdaestftp aaanaqfaqm ydyegrnftl ynrnaltyak tfnadhtifi ntfneiykqg
      541 gqsgiirqsr ipndqlqgpv gsdsynsrgg gvlsnfknat iasfagsfny dykkkyvlel
      601 syrldgtssn glenpysknp aaglrwnyyk enwfknwdwl tsgglrltwg qnivptgslq
      661 siyglynlng nfnnnptigi nyefvpnpal kpttttqynl gfdmtilqgk vdlsfdtyyk
      721 kvdnllfdrf lpnstgfqkk ssndvsiady gyelmvtvrp ltakdfnwtv sfngainrdy
      781 llrlpaeyng qyikfdynny qhivfrvgkn tlsnyllvnq gvyptdanvp vdpvtgkkyq
      841 tnglafkggd pifkdvngdy ilddrdyeit gnsqplitgg vstninyknf glniyasyta
      901 krtilnnals drlsimkdpy allaavpldd mdiwrkpgdh akypnpysfs rfnqirplrs
      961 dqslwqeegs ylkintvtls ymfdrkfvrr fgfnnvrvyf stnnlitfsg yngpnpenvt
     1021 slgrdissgy pvprtynlgl nielntsk
//
LOCUS       WP_114936957            1144 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114936957
VERSION     WP_114936957.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1144
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127038
     Region          135..1140
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkltflynav cairrvkfkf llvlklttil lligalhlsa asysqtvtis gknkslesvf
       61 kdikrqtgyl ffysekvnik gktvdadfrd tqlvdvlnvc lkdfdlsfti vsktiviqnk
      121 ipeprpapvv amskipvsgr vldsvskttl pgvniavkgs rgvigqtndk gefnvqadag
      181 qtlvfsfmgy ksaevkvvag qsivvkllpd innikdivvt gyqvikkdny tgnaitisga
      241 dlkrnnpqnv iksiasfdps fkvldnnlag sdpnklpkin vrgttaipsi sddildrnnl
      301 ssnynlpafi ldgfevtlqk vvdldinrie svtllkdgaa tavygsraan gvmvittkap
      361 vagklqlsyn yeltfngpdl sdyhvlnakq kvayeqlvgl yntqtstsgd tkqdeldaql
      421 ftrlknvasg vntywlsqpl rnayqqkhsv yaqggdqsfr ygidlryqtq pgvmkgsdnt
      481 rysggvnfty npnskliirn dltitqvnqv nspygdfsty vnanpyfpir dstgrlvqel
      541 anwrvntgrt gtdqyvtenv fnplyeasls sfnkaaytei lesfsadyki skslrlralm
      601 svnktnsttd nyvsplssvf ynyasdklnn rgtydygtna slnldgnvti nynkqlgdhy
      661 fnlvlganil askadvksfs aegfsndrft nigfariyke nsgpygdvtk srtagaffsg
      721 nyafqnkyll dasvrvdgss afgadrryap fgslgigwni hkesffqgsk visqlrlkgs
      781 iatlgsisfp ayqsrsiysy dtqnwystgi gatilgygns nlewqktrts digmdiglfk
      841 drivispryy ykltkglitd inlapstgfn tykdnlgdms nkgyelylva qvfhttdwni
      901 nvtgnlahnv nkivsisdal kafnnnidnf qtnkdnnafs tpltryvegk slntiyavks
      961 lgidpengke ilvkkdgtlt yvwdvkdvqd vgnttpkaeg ffgstvsykr fmlsfsfhyr
     1021 fggqafnqtl idrvenadpr fnvdsrvleq rwkqpgdhtf fknitdltdt yvssrfvqkd
     1081 nlielqslyl sydfkpkair rlglqnlrla atandvfras tiqaerginy pfarsltfsl
     1141 lgsf
//
LOCUS       WP_114936976            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114936976
VERSION     WP_114936976.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115314
     Region          25..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkitlifv llitiltrtf aqdvtvkgiv kdsqglpipg atvknkstga vtvtdvkggy
       61 sitansnatl vfsfvgsatq eqqikgrtti dvtladankq leevvvigyg travkdvtga
      121 issvkaekle nehpasatdi irgnipgisv alntsakggg tgdlqirgka slsgnvqpvi
      181 vldgviypgq ladinpndid rvdvlrdpsa lavygaqsag gvvaittkkg kkggtqitln
      241 anfgiaqllq nqkyytgdgf lnwradgars sntsnpyyyy snpnklpdgv tlaqflngat
      301 gdpttiwlqr lglfpneian yqagkmtdws klifrngfrq dytgsfsgss etvkyyvsgn
      361 ytknqnliqg gqytdgrfrv nlegkaakfl tlgvnaqfas rdegaastpl sgqaidatea
      421 dwtqiinssp ygdmynadgs lrridtddsg lnqrnpflgn rynqnvavqn tlfsvlfarl
      481 dlpfgikytv nyaptiesyr nfffrpvanp nelsggtair sqenryrynl dnilswnktf
      541 gihsfdatfl lnkekyqtwy tnasntqltp tdilgyhnig agtlpvessd driynadaim
      601 grinytllgr yiltatvrrd gfsafglehp revypsaava wvfsdesfmk gdafkwldyg
      661 klrfsygang nrtstttadp sislavlggi kyptannsgt vtnnsgiyvs tlqnaqlkwe
      721 rtvgpnigld ftilhnrlsg sidvydrktt dllvkrsild vqgynssgdl pggannsnpy
      781 tnigqvnnkg feisldgkim ksenfnwnas gtfflnrnki vhlygafpvt dangvttnve
      841 kddigngwfi ghdinavwdy kiqgvwktte adqaakygak pgdfklqdvn gdfkftnddk
      901 qflgsqnpsf swslrndfni fkhfdvsfll vssigalkqy nqalnnpgsv gfarmnsyvl
      961 pywtpdnqid dyarlnsgss gttinvwrka sfvrlqtasi gytfspqlik rlgissaklf
     1021 vnasnaavfs swplwdpqng gptprylsag fnvvf
//
LOCUS       WP_114937279            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114937279
VERSION     WP_114937279.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118043
     Region          24..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllaswc lfmlfisvvh aqnktvtgrv tskddglplp gvsvrvvgtt lgtqtnadgk
       61 fsltapasak slsfsfigft sttveitsap ldvkllssan klsevvitga ygtkqssrsa
      121 syaaqvvksd alntirqpnv nnalagkvag vqvrsqsaaa lgrntnirlr gatgfgsgnn
      181 plyvvdgtim pnaddlsndd idnisilngp aasaqfgsqg aygaivistk kgkkskgvgv
      241 elnlganfdk ayilpnyqnt ygggasadfi qyhwkdgdpe gwkaldgkfy pdytddsswg
      301 pkmvgqeyip wyawaagtky sfktakwtpq pdnakdffrt gvalnnsvaf tkaaddynir
      361 msynnqhttg ivpetwlnkn nftlnanfdl nkhltagasi nysgtqlhgq isdayasass
      421 gsfnswfhrd ldmgimkelq dlkspdgtyv swnhqnpnsy dpsnpaafyg gnywynpylw
      481 qkqwqnlntr drlygniylq ykinndlsfk vtyrrnqtnt wnenkissei qasgtqtgqk
      541 atygtsntys nrenyetlln ydkqikdfhv nvnagsdfyn wsykdnsant nnglsvpdly
      601 tlansvdpis asngrtqeqy ravfakasan ykrivyvdat lrndwfstis tvndansvls
      661 ksfggsfvfs evlpefkdwl sygkvrgswg qvplalgtst etfgayrnnt lygiaankwn
      721 gsllqggptq fvdpalhgtt ttskeigldl gffndrltfg atywaaddkd iplglavnaa
      781 sgvssiltnv glikrrglei tasgtpirlp nfswtintnf aqlldntvve isnkygvdrv
      841 qvagvwgtdm pylinqkgkw wgqiygngik rnsagipilt ssgayindpn vyfgsalpky
      901 tgglqntftl fkdfvlsani dyqfggkfvs lsnrwgqysg ltantaalnd kgmsvrdpva
      961 dgggvkvtgv dadnkpvtyy vdaksyyqgl tnnktydpyv ydltfiklre vavgynlpik
     1021 kwglgnvfqs aridltgrnl lliyakskdf dpseisateg etaqypgtrg igfnlkvtf
//
LOCUS       WP_114937347            1146 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114937347
VERSION     WP_114937347.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1146)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1146)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1146)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1146
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1146
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123803
     Region          70..123
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          136..1142
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkldssnff rcccflmvll gqsvygfaqm altsnnrvha ksfgytapqa veskillkda
       61 ldnlkkqfni qiayqeglld nkfvpanlts nvsqltlddn lkqllsafql tyrkindnqi
      121 siftvkdvnv avaavtltgk vvdagdgqpv igasvylkmd nkvgattdls gnfkliipdk
      181 yagkpltlvv ayvgynqeev pvsdpasplq iklaqnnkal nevvvtalgi skqkkslgys
      241 vtevkgteft qarennvana ltgkvagvna aglstgpggs srvvirgngg lagdnqplyv
      301 vngmpidnsv pggaatvngi tnnvdrgdgi aainpddies isvlkggtaa alygsraang
      361 vilittkkgr iqkgvgvefn statydnvav fpdyqyeygq gdggvkpttl aaaqasgrrs
      421 wgakidgstd yvavdglahp yvaqknnlkn fyqtgstytn slafvggnea ftyrfsaadl
      481 nskgilpgtt ydrktfnlal ngklsnklsi ealaqynvet ghnrtgagda lgnpnwtple
      541 vantvdvrwl kpgydamgne mvwndasias ngyfvinkyk eddvknrfig qgsiiyspik
      601 dltfkatisr dffnynytni lptgtlytpn gqyagiksdv setnelatvs yrtkiisdln
      661 vgvlggvnsr knatnqltfs gsqftipyfy sftnlavsst tpynakivtn svfgsadfdy
      721 kslvflsftg rkdwfstlsp ksnsifypsi ggsfilsdav klpeffnmak lrgswaqvgg
      781 gapdpyvinl tysnvpsagq plqnvtsnni tnsnlkpyts ttfeggfelq mlrnrlgldv
      841 tlydrkttnd ivntaissts gynnvilnvg evsnrgievl lngtpvktan fnwtvsynva
      901 yndnkvvkla pglntiqlat svgnwgildn iegkpfgmlv gtrmqkdang nvvfnattgl
      961 pvqtplqqlg ksvapltmgl tnefrykrfs lnflvdgkfg nkvfsvmevy atrlglmkst
     1021 lpgrenglvl ngvdqtgapy trtvpvsglr syydnyktys dlflhdgsfv klrqvilsya
     1081 lptnllnkvk iqsasisfva rnlwtiykkt dnfdpeqsft nsnaqgfesi glprtrslgv
     1141 nlavkf
//
LOCUS       WP_114938358            1124 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114938358
VERSION     WP_114938358.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1124
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122915
     Region          31..1123
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqnllkisr lllvmivcmf tysslqaqtl tirgivlddn nqplpgvsvt ikdtkqgglt
       61 neggrftisa skgqtlvfht igfttqevvv gtevyisvnl ksdtkalsev vvtalgvkke
      121 fqklgysqsq vrgdamttar danplnslsg kiaglsigan aefagaptvv lrgskdvlyv
      181 vdgepvnsdt ydynaddvet ytvlkgpnaa alygfrging aiiittkrgs kdkkgwqvdf
      241 nsttelekgf lvlpksqtey grgsnfayty gnvlydntqr lpewgprfdg vfqtqqydsp
      301 ydpatgirqk tpwlargakn fenfvqtgvt stnslsiaas gsnydmhisy ghtyqkgdfp
      361 ntklnidnfk iaagyditpk lrvegdlnln qlyspnipdv dyspqsyvym fkvygsadyd
      421 vnalkniyqg pqgvpglqqy aqeygrlnnp wfiadkwlkg rtkqtiygsl klnykitqdl
      481 nvslrealnt ydeqnteqvp aganlnqyls wytfgwygdy rqddrnlldn ntdltftynh
      541 kfgdwnisgl lggnarsfsy ksdwgttqvl alpgvynlnn sagkpyiynf dskmqvysay
      601 ysfdfgykny fsinttnrvd hlstlpsgnn tffypsvais svvgdyiklp efisflkirg
      661 sfadvkgglt sptigtsyna lnstalgtgw nskpvtgllg ygtelytpyn gptylnaspi
      721 atgtfyngtp svtlsntisn dkikpfdvks yeagfdakfl gnrlglngty fttengpnif
      781 plgvatstgn tnqlvngvtt rkrgfevelm gsvlknpngl nwdvnvnyst yketiksiyp
      841 gvstlqqnnh nyvvgdrpda iygtkfvrdg ngnivntysv dasgkvsggv plsspggisn
      901 qgllgyanpd fsfgitntft ykgfilsfqf dgriggkiyd rtyyqamngg tdletatgay
      961 gaarlaewns tkegtvgatp syigpgvhiv sgtpifvggq ianlkdltfa pntipvtvqs
     1021 yissgiagsf deyymisrsy aklreaslgy slpasilrgs fikkvtfsvv grnllyfaar
     1081 kdidldqfas gynasdrslt ggnggsdles ptarrfgfnl hltf
//
LOCUS       WP_114938540            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114938540
VERSION     WP_114938540.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113356
     Region          44..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maycyikrcl tgitllllll atagyavaqq dttavaparp gqasgivlde ygnplqgvkv
       61 tnkgknstqt tgkdgafain aikgdilsft aanynarqvt vkntagirvr lldtyiqkpk
      121 tinvlydtvs taksvgavst iytnrltttp stlytyalpg qlpglytqqy sgfaapqtgv
      181 qtvndfigav vqhnnysand nsefglflrg qapvtiidgv qreiasldpe siesvsvlkd
      241 alsnimlgin ssrgtllitt krgqvgaphi sftaqtgiqq plglpnplpa yqyaylynea
      301 lqndgkpaly saadfnayrn htdpirhpdi nwfntilrdn spitsyklnv nggtqvarys
      361 vslnyldqag mfrqdpsvay ntnndlnryi insdlavnvt kkftvdlqlf grvqqstqpg
      421 agygnilstl yslpnnayal rnpngsfagt ttytnnllsq tefsgyqrtn sndvlanldl
      481 nynlnsitpg lsakakgnla fssqsflnrs lqnnaysfna dssysavgss vaqsnsystv
      541 ssarysfaqa svnydrtfgk hnitgmalyd vrsvvlnydl sqvttnralk agynydgkyf
      601 ieaaanssgy nryppgnqyg lfyaggigwq mgkesfikdn fswisswkwr atygktgnnn
      661 vdnygyynfl qtygatngys ystgtskspv qgfyentlan pyirwekark ldvgtdislf
      721 ndhfnitadv yrdryydllq vrgnsiallg taypyenlgi nlykgaeltl tyqnhiqnfn
      781 yfisgnasiq sskiifsdee pypypwlkht grsttaiygy taigyfkdaq daatsatttg
      841 ytaqagdvky kdlngdhiin qfdvsaiggn rplvyyglss gfnykgfsls fllqgvanre
      901 lmfnnsqvng fagvgflglt ysgqayetil grwtpetaat ataprlslgn anntanstly
      961 lrkgnyvrlk naelgynlpy ewarklrlsg lrvfvngenl ytmygykdfd peiygtaypi
     1021 qrvinagvni kl
//
LOCUS       WP_114938792            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114938792
VERSION     WP_114938792.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109950
     Region          30..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfkqllkrf ilpllsvfvf cystyaqtvt lkgkvtdekg epiagasvki kgtnagsvtn
       61 gsglfslnyn gqgtlivtai gftahevklt gqaqvnvtla ednkvlnevv vtalgikrdk
      121 riltyssqei kgesltqske pnlvnaiagk vagvqvtsss gtpgssariv irggssffgt
      181 neplmvidgv pvdnsetgnl ntgpgtnria didpsiiasm nvlkgaaata lygskgangv
      241 viittkngal nkkplitfss dfsaekpllp qiqnkyslgt ngiyydgvtn ktstswgarm
      301 dtlkingqpa kvynqsdlff ktghtynntv niggggnnst ylvsysnfnq qgtvpttkfl
      361 rntffakysa qvlknlnttf qlnysnsqnd rlpegyales pvwtvftapv synlqpylna
      421 dgtqrlyrfs rnnpywvldn iknhssvnrf lptftadykp lswltiterf gadvytemdr
      481 yhestqsvsn pngrlvdnnt tfrqynndll lsatkqfgdf nidvilgnnl istygentya
      541 ngvgltvpgl ynmasastvn ysesstlqrk igfylqsnie ykrflllslt grydgnsvls
      601 tdhnfypygs aagsfifsef fspelskvmn lgkirvsygt vgndgsigay slltpynkat
      661 irnlafpynq qagflisdvl gnpnlkneri nefeagfeag ffnnrislea sfyskktidg
      721 iipnvaiaas tgyastgvns avmrnrgiei llnatpiksr dfnwdltlnf trnrnkvlsi
      781 ygdqqvlgng ftnivvgqpy gviygtryar naagkllidd tglpyaddtq givgninpnw
      841 lgginnnfry kqfnfsfffd ikrggdiqnn vdgygyfygt pkvtenrgpr vvdgvnattg
      901 qpntiavngq ayyqransvl esviqdgsyv klrnvslgyt lkpswlsksp fksatfsvtg
      961 rnlwihaphf tggdpevssf gssngsqgiy sfstptsksv dfslkvtl
//
LOCUS       WP_114938806            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114938806
VERSION     WP_114938806.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113899
     Region          27..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkiyklfla illpfilvqt vagqsvkisg vvtaksdglp lpgvsisvkg tttgaqtnvd
       61 gkftinakvn dvlrvsyigf tsqdvtvtgs stlnivlvea pnslnevvit alniskdkks
      121 lgyavqglks kdiseaketn fvnalagkia gvqvtnsqgd mgssrivirg etsisgnnqp
      181 lfvvdgvivd nsqflgnngs rdfanaisdl nsediesvsv lkgpnaaaly gsraaagvil
      241 irtktgkgak glgvtinsnt sfsnvqilpd yqnqygqgsn gkfsyvdgkg ggvndgvdes
      301 wgpaldgsli pqfysngqav pfvahpdnvk dffktgvtln ngiaiasssd ksdfrlsynn
      361 lhqtgivpnt sqgrnsfaln ssyrinpklt vntivdyskd dadnlpgtyg kratstmlqf
      421 twfgrqvdin rlknykdang ntfnwnnsyy snpywlayen tvgqhknhli gsielnykii
      481 dglsanfrtg tdyyndrrki kvaygtngtp fgsyeedays vnenntearl qytkklnndf
      541 tldvfgggni avrttenndq lapklavagl ytlsnsrdpl vstnyygklk tysyfgsaql
      601 gfrnyaflnf ttrndwsssl padalsyfyp svngslilse algiksdvls yaklrggwsk
      661 vgkatdpfql invytssnlf gsnpqqsisn idlndhlkpe tttsaeagfe lgffhdrvhl
      721 dvsayntnst nqiltvqvss stgfgqkvin ggrlnnkgie vqlgitpiks ngftwdittn
      781 yslnrskvas ldadgrlqsv vlgtdrtvqv laalgqpyga lygtaytrda agnividang
      841 tpvfnttkry lgkftpnwlg sinnsfsykg inlsvlvdar fggsiysntn rtgtytgvla
      901 stlpgrgaan gglsyyypgn ntsaaavqvt gaapagvtvy ndgmifkgvk adgspnttii
      961 paqsyykgft nideafvyda syiklrevkl gyslpakwvn kigfqgatfs vvgrnlwiih
     1021 knapnidpet afnagngqgl edltlptvrn igfnvnlkf
//
LOCUS       WP_114938844            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114938844
VERSION     WP_114938844.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114958
     Region          23..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklflllsv llclgsalka qdrnitgtvt dekgaplpgv avqvkgsntg tltnadgkys
       61 lkatnlqaiv vgvkflgyny qekalkigem nadfkmlpsq naleevvvvg ygtqkkvhlt
      121 gavaavdmkt iqdipttnla aalrgtnaav svtggiarpg qsgtitirnp vflaknggst
      181 tplyiidgvq rtesdfnlld qsevenisil kdaaaaiygi lgangvivvt tkrgqagapk
      241 vsfsssvgva daiqlpkmms gvqmatylnd ieqtrynhti tpegyingdl snkdlkyytp
      301 deleyfknnn qnfleqafkp avttrnalsi tggndkvtyf aganyvnqns nfkgvntnrf
      361 gfrasvdakv akglklslsl sedlakskiy wyklastses pdndflslnq appwqkyfid
      421 ghpvylgtsn ndnlnffavq nsnnytgnnn tvfnglanls yeipginglt anvsynrnin
      481 nafnkqygst fyynqysgeg dnnhipggtv vgvkaikngd kvrltpslad nyqfnanlty
      541 hkrfgaheit alalyeqyes ysegvaaead gvivggkdnq tftigdqssn qatlvkeygr
      601 kavagrinya yadkylvela mradantnfa pghqwgyfps asagwviske nffksvsfvd
      661 llkfrgsvgl lgsdntpsfl yavnyqfgtg nkggavfggn gdrglgalln iaipnvnltw
      721 dhdlktnygl daaflnnrls vsadyfwehr ydmlaslnts vpvtigaaps aenygiintf
      781 gyeisvswkd kigsnfsynf spffswsdnk yikydiaaaq vgtiqdltgk sgdpgtlgyk
      841 slgiirtqad adaiiaeraa aaggaqnvki fgftptpgmi nyvdkngdgi ikqndindqf
      901 ylghkannhy nlglnlggsy ktlslnvvmg mswggtqsie saaikqgtan qnrpvfwadh
      961 wtptntnary pdpyysddvs atsdfwfvsp ftwnissanl sytlpagltk rlgmssiray
     1021 vvatnpinfv npfpdhyrdi sspfgaypnl rtvsfglnlg f
//
LOCUS       WP_114939305            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114939305
VERSION     WP_114939305.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112363
     Region          25..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqiylrcfa fllfsvitmt ayaqktvtgt vteksgqvlp gvsvaekgta ngtttnadgk
       61 ysirvkqgav ltfsfigfks aevtvgtqaa invtldeken altevvvtal gikrekkslg
      121 yaiqevkget ltaskepniv nalsgkvagl qitrsgngpg gsskitlrgn nsltgsnqpl
      181 ivvdgipldn ftgaanndyy npsldmgngl sdinpedies lsvlkgpsaa alygsragng
      241 ailittktgk tqkglgitis ssigsesifa rpglqqdfgq gsnnvydats ssswgpkatg
      301 qdvkkwdgtt aplhtydnik nyfgkglnan qsisfqqqyk stsvytsynr lddksvipga
      361 klirnnlmgr tvskfgegdk wtvdtkvqyi natalnrpqg gsnvsnnfya lsllptsidi
      421 rdfkgrtdns gnmlwwrqnn elnpywasky nlnedirnrf llnasikyqf ntwlnaelkg
      481 gadtyttnte nktyagatpt stgayglgka nftetnysgl ltakkdnifg klggtatfgg
      541 nlmnrqsssl sasanplqvp nlfsinngtt spsvsqtisk hdiysvygsl glnydgylfl
      601 dgtfrndwss alnannrsyf ypsvstsflf tefmtkngnt lpswltygki rgsfasvgnd
      661 mdpyqlynty tigkdpngnt tasrndvlyd pnvkseliks yeaglemrff nsrlgfdfav
      721 yksnatrqli nlpmdglsgy tarkinagdi qnkglelmvd gkiiqgqgfn wntsvnfsin
      781 rntvkylypg vsqyslggfd dlsvvaetgq lygeiygsrf lrvkdasspy ngqllldang
      841 lpqvdpertk lgnqqassll gvtntfsykn fdlsflvdar fggqifsgti anmeqygtsn
      901 ktvvggsred mlvngvvlnt ttnqyqpntv ktsaqnywtv vaghgnigvt eanlydasni
      961 rlrnvqlnyn lpqkfvrsig mqrakvgvsa nnvwlisshm ngmdpessya tgtnatgfes
     1021 gsfpttrtll fnltvgf
//
LOCUS       WP_114940634             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114940634
VERSION     WP_114940634.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108122
     Region          27..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mykklllwlg acalcfiftg kvlaqdktis gtvtdaadss plpgvsvvvt gmsvgtttna
       61 kgvytlkvss saktisfsyi gystrevplt geatlntslt asskslqevv vvsvgygtld
      121 krevssaith vsskdllpva snsplmslqg kvaglsitnt agadpnsspk vqlrgvssrn
      181 aglgplyvin gipggnidni nqndiesidv lkggaasaiy gtrgsngvii ittkkgssqa
      241 rtfyegyasf dyltnelqnl tpdefiadrv knnqgqdyga ktnwmgavtn spafaqkhti
      301 qlsggsgktn yfasadyrna dgidlrahkk eygarinvnh atdngifvas lniaprymnt
      361 knsdqgnfnn altlnptypi ydtahkynyi ntgffsnnpv enanviksea eikemdings
      421 lrvnilknls ttvtiseisr sarslnftps tlssivhank itqtnfasqr qeendqknve
      481 wtgnysldlg rnhfkvlggy sytlynyntf yaqnydfpfd sylwnnlgsg lynggaagqg
      541 qsavsstqng stlisffgra nydfnnryil tasvrregss kfgtnnkwgs fpaasaawrv
      601 seenfmkgal pwvndlklra dygvtgnqdf dsylslllyg gagyfpyngq vyqvygptsn
      661 vnpdlrweks infnvgldfs ildnrisgsl dyyirknkdl lgyynvplpp nsqtqtfanv
      721 gtmknyglel alngavvrnt dfsynltftl aynrnkfisf sndiykgapf velaglpapg
      781 spgniqriqe grsigefytl rsagvnkdga lqvykkdgti vqanqasadd kqfvgnglpk
      841 ftgsmgntfr ykrfdlgifl rgtfgykifn taafyigtps sqsdanvlks aydskskysl
      901 ltnsattaia sdyflengsf vkidnvalgy tqpfkskylk sirvyatgrn lhtftsftgg
      961 dpdlvdvngl tpgvntslny ypatlqlilg lqatf
//
LOCUS       WP_114939989            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter endophyticus].
ACCESSION   WP_114939989
VERSION     WP_114939989.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter endophyticus
  ORGANISM  Mucilaginibacter endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Mucilaginibacter endophyticus"
                     /db_xref="taxon:2675003"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121213
     Region          29..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkiyqrlra vitvllfcva psilfgqtki sgtvtddkhl plpgvsvkik eqnkgtvtdi
       61 eghysitata gqtliysfvg yapvyvvvdn kttvnvsmig dskalnevvv talgvkketr
      121 rigystqsvs gadvttardp npitgltgkv aglsvgpsae llgnpsvlir gnsvtlyvvd
      181 gfpintdtyn ispddietyt vlkgpsaaal ygsraqngai littkkgekn krgltvdins
      241 stvmntgfla fprtqntfgp gentfytfvd gkggapggvd sdydvwgpyf agqlipqyds
      301 pvvngvrqgt pwvargkdnl knflktgyqt nnnislgsvg etyvtrfsvs qqhqtsyips
      361 qyldiananf ygqftpskrw kfeanvdfnr qstdnfpdvq ygpnsiiyni avwtgadwni
      421 napdikaiwq pgkegvqsvf aeytryhnpy lltekwtrgh ykndiygyls gnfkindnln
      481 vtlrsqidty nilrtedlpf sahpygregn qgdyredrrn lfdnntelfv nynytiknfv
      541 nlsglvgsnl rsfnynsswt stdylnvpev yafsnsknav qstnfssqer vlsgyysida
      601 tfgkyatlss tgridkssaf qnvttyyyps isaatvisdy vklpeiisfl karasystvk
      661 adassatigp apfnaisvyg gstttsnpns nplflnplgy gstynspyng psyqlnpfyl
      721 tskpynsqpa asasdflyqp niktstrvny eegfdikflq nrlglsattf qyidgpqila
      781 nsistatgyt tlylnalktk ktgyefsleg tpiknlggfg wnvlvnvstf kdiyeelppn
      841 qqtyqtffkk gdrvdklygt afartpqgqi indaagkpla lpvpqylgne nakyqwsfan
      901 klhykninfg fqfdgsvggv iidymhnktm rggsnietat galgdarykd wqnfgkagyn
      961 gsyvgegvtv sngaainydp atgkitnyga lqyapnkqta lvqdyvskyy nvdesnlmsk
     1021 tfsklrevti gydfpktwld ksfikkasvs vygrnllyfy gdkrfkdvdl dqynyatsst
     1081 vlqsptvrsy gfnlnvsf
//
LOCUS       WP_114946473             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            calopogonii].
ACCESSION   WP_114946473
VERSION     WP_114946473.1
KEYWORDS    RefSeq.
SOURCE      Microvirga calopogonii
  ORGANISM  Microvirga calopogonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Microvirga calopogonii"
                     /db_xref="taxon:2078013"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39087
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd gaetrvsatp etvkkykslg advvvqagag akagipdaef eaagasvatt
       61 agdalkdadi vlkvrrpaeg eltgvkpgal viaimdpygq eaalkalada qvsafamelm
      121 pritraqvmd vlssqanlag yravidgsae ygrampmmmt aagtvpaarv fvmgagvagl
      181 qavatarrlg avvtatdvrp aakeqveslg akfiavedee fkqaetaggy akemsdayka
      241 kqaelvashi akqdivitta lipgrpapkl vsramvesmk pgsvivdlav erggncelaq
      301 agqvvehngv kivghlnvpg rlaasassly aknlyafvet lvdketkala vkwddelvka
      361 tcltrdgaiv htafqpta
//
LOCUS       WP_114947890             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            calopogonii].
ACCESSION   WP_114947890
VERSION     WP_114947890.1
KEYWORDS    RefSeq.
SOURCE      Microvirga calopogonii
  ORGANISM  Microvirga calopogonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Microvirga calopogonii"
                     /db_xref="taxon:2078013"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39641
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd gvetrvaatp etvkkykglg advvvqagag akagipdadf eaagasragt
       61 agealkdadi vlkvrrpaeg elkgakpgal viaimdpygq daalkalada qvsafsmelm
      121 pritraqvmd vlssqanlag yravidatae ygrampmmmt aagtvpaarv fvmgagvagl
      181 qavatarrlg avvtatdvrp aakeqveslg akfiavedee fkqaetaggy akemsaeyra
      241 kqaalvashi akqdivitta lipgrpapkl vtremvesmk pgsvvvdlav erggncdlae
      301 pgqvvehngv kivghlnmpg rlaasassly aknlyafvet lidkdsktva vkwddelvka
      361 tcltrdgaiv hpafgqaafq paa
//
LOCUS       WP_114949578             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Trueperella pyogenes].
ACCESSION   WP_114949578
VERSION     WP_114949578.1
KEYWORDS    RefSeq.
SOURCE      Trueperella pyogenes
  ORGANISM  Trueperella pyogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Trueperella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Trueperella pyogenes"
                     /db_xref="taxon:1661"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52860
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresg gqtlvaatpd tvgklsklgy evvvehdags aasfpdslye sagarivske
       61 eawaadivta ldapaladld lmrsgatlis rmapgrnpdi lqalssrsit glamdmvpri
      121 sraqsmdvls sqanvagyra vieaahhfgr lfsgqvtaag kvapanvyvi gagvaglaai
      181 gtansmgavv katdvrpeta eqvesmgagf vaipvaaees adgyakemgq eqaaaaekly
      241 teqaawadiv ittaaipgrr spvlltaeav agmkpgsviv dmgaanggnv vgsrpdevvv
      301 tdngvviigy selaarlpgq asqlygqnif nffklatpdk dgvlhldldd eivrsmlvtl
      361 dervmypppp vkvsaapapv passeevtsa eakekswiak hwwkiaagav ftwliltapa
      421 gstthflvfa lavvigfyvi tsvthalhtp lmsvtnaisg iivvgalmqv sassvvvqil
      481 sfiaiavasi nifggflvte rmlkmfhrs
//
LOCUS       WP_114952525             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingosinicella terrae].
ACCESSION   WP_114952525
VERSION     WP_114952525.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella terrae
  ORGANISM  Sphingosinicella terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Sphingosinicella terrae"
                     /db_xref="taxon:2172047"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38533
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkeae sgerrvaatp dtvkklaglg atlaveagag aganiadady eaagakvggr
       61 aevlgdadia lvvqgpdpaa lngvkpglil vgalnpfgrr dridayassg iealamefap
      121 ritraqsmdi lssqanlsgy kavldaaaey grafpmmmta agtipaarlf vmgvgvaglq
      181 aiatarrlga vvsatdvrsa tkeqilslga kpifvenvag iegegaggya temseeykka
      241 qadlvsshia kqdvvittal ipgrpaprli sdaqlatmrp gsvvvdlave qggnvegava
      301 geiverhgvr iighrnvpsr laadasslya rnlynflsaf wdaegkklal pdddeivkgv
      361 rltrggqvvs erllg
//
LOCUS       WP_114961757             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tritonibacter mobilis].
ACCESSION   WP_114961757
VERSION     WP_114961757.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55427
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtprela tgesrvamtp lsaldlqklg fecciesgag eaagftdaay aeagvevikt
       61 aaglwkaadi iakvrapnet elkrlnkskt lisffnpggn eeglelaksk gatviamemv
      121 prisraqkmd alxsmaniag yravieagnn fdrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg avtyafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreapk lwladmvaam krgsvivdla gerggnvegt
      301 vrdekvvtdn gvtiigytdf psrmasqsss lyatnirhmm tdltpekdgq vvhdmeddvi
      361 rgatvthage itfxppppkv qaiaaqkkpe ppkeltaeek raaevaafkq qtknqvtlla
      421 vgaallltvg lvapasfmqh fivfvlsvfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsw lviflaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_114962845             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tritonibacter mobilis].
ACCESSION   WP_114962845
VERSION     WP_114962845.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55583
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeia egesrvamtp lsaldlqklg fecciesgag eaagftdaay aeagvevikt
       61 aaglwkaadi iakvrapnet elkrlnkskt lisffnpggn eeglelaksk gatviamemv
      121 prisraqkmd alssmaniag yravieagnn fdrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg avtyafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreapk lwladmvaam krgsvivdla gerggnvegt
      301 vrdekvvtdn gvtiigytdf psrmasqsss lyatnirhmm tdltpekdgq vvhdmeddvi
      361 rgatvthage itfpppppkv qaiaaqkkpe ppkeltaeek raaevaafkq qtknqvtlla
      421 vgaallltvg lvapasfmqh fivfvlsvfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsw lviflaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_114964420             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Alkalilacustris brevis].
ACCESSION   WP_114964420
VERSION     WP_114964420.1
KEYWORDS    RefSeq.
SOURCE      Alkalilacustris brevis
  ORGANISM  Alkalilacustris brevis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Alkalilacustris.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Alkalilacustris brevis"
                     /db_xref="taxon:2026338"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55036
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigcpseif egerrvaltp esagqlaklg hecliesgag egagfsdady kaagvevvkt
       61 aaalwkaadi vikvrepnet eakrlrkgqt lisffwpaqn ealleqcrak gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtsvalg avthafdvrp evaeqvesmg aefvyldfae stqdgaatgg yaapsspefr
      241 eaqlakfrel apemdivitt alipgrpapk lwtedmvaam kpgsvvvdla aekggncdlt
      301 radekvvsdn gvtvigytdf psrmatqsst lyatnirhml tdltpekdgv vvhdmeddvi
      361 rgatvthage itfpppppkv aaiaaakpke kkpeptaaek raaeaaafqa qtkaqvtlla
      421 vggglmlllg qiapasfmqh fivfvlacfv gfqviwgvsh slhtplmavt naisgiivlg
      481 ailqigsgnw iivvlaaisv liatinivgg fvvtrrmlam fqks
//
LOCUS       WP_114968070             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodoferax
            ferrireducens].
ACCESSION   WP_114968070
VERSION     WP_114968070.1
KEYWORDS    RefSeq.
SOURCE      Rhodoferax ferrireducens
  ORGANISM  Rhodoferax ferrireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Rhodoferax.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rhodoferax ferrireducens"
                     /db_xref="taxon:192843"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37836
     Region          2..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(5,63,82,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(34,114..115,124..125,128..129,132..133,135..136,
                     138..143,145,147..149,152,175..176,271..272,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(109..110,114,117,120,161..164,184..186,221,232,
                     249..251,258,260)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(111..112,114,124,167..168,175,191..192,194..197)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(144..148,151,154,177,179)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgetrvavtp etakklkaqg htlriqagag vaasvpdeay laagaditda agafqcelvl
       61 kvrspsdvea almrpgtclv gmlnpfdleg lqqlaaaglt gfaleaaprt sraqsmdvls
      121 sqaniagyka vmmaadryqr ffpmlmtaag tvkaarvvil gvgvaglqai atakrlgavi
      181 easdvrpsvk eqieslggkf ievsydtpee keaavgvggy akpmpqswld rqkievakrv
      241 aladivista lipgrpaptl itedmvksmk pgsvivdlaa gkgpngggnc plseadqtvv
      301 khgvtliget nlpalvaada sslyarnvld flkliltkeg slnidlnddi vaaclmtqgg
      361 evkrk
//
LOCUS       WP_114968072             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodoferax
            ferrireducens].
ACCESSION   WP_114968072
VERSION     WP_114968072.1
KEYWORDS    RefSeq.
SOURCE      Rhodoferax ferrireducens
  ORGANISM  Rhodoferax ferrireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Rhodoferax.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rhodoferax ferrireducens"
                     /db_xref="taxon:192843"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37817
     Region          2..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(5,63,82,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(34,114..115,124..125,128..129,132..133,135..136,
                     138..143,145,147..149,152,175..176,271..272,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(109..110,114,117,120,161..164,184..186,221,232,
                     249..251,258,260)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(111..112,114,124,167..168,175,191..192,194..197)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(144..148,151,154,177,179)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgetrvavtp etakklkaqg htlriqagag vaasvpdeay lavgaditda agafqcelvl
       61 kvrspsaqea glmkpgtclv gmlnpfdleg lqqlaaaglt gfaleaaprt sraqsmdvls
      121 sqaniagyka vmmaadryqr ffpmlmtaag tvkaarvvil gvgvaglqai atakrlgavi
      181 easdvrpsvk eqieslggkf ievsydtpee keaavgvggy akpmpqswld rqkievakrv
      241 aladivista lipgrpaptl itedmvksmk pgsvivdlaa gkgpngggnc plseadktvv
      301 kfgvtliget nlpalvaada sslyarnvld flkliltkeg slnidlnddi vaaclmtqgg
      361 evkrk
//
LOCUS       WP_114983521            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclonatronum
            proteinivorum].
ACCESSION   WP_114983521
VERSION     WP_114983521.1
KEYWORDS    RefSeq.
SOURCE      Cyclonatronum proteinivorum
  ORGANISM  Cyclonatronum proteinivorum
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Cyclonatronaceae; Cyclonatronum.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Cyclonatronum proteinivorum"
                     /db_xref="taxon:1457365"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115523
     Region          25..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkkllltim llafplalla qtgslsgvvt dsdtreelpg atvflvelnr gtatnidgef
       61 slenipvgqy svlvtfvgyq rferritina gansldvalr vdrfglediv vtgvlgdtea
      121 rrtpftvgrv sardlemvpg sspvaalrgk vagvnivqgs gqpgsspsvv lrgitsises
      181 neplyivdgv ilaesavdie sldiesievi kgaaaaslyg sraasgvini rtnrganlae
      241 gttrivvrne fgvssvenpi rtnqshafqm sgnaelpwld sdgnptadkt ervlvgptnt
      301 tfldqaypve tfdnfdtffn pgnfytnyva isqrvgnvny lasfnntqqd gvldaldgyg
      361 rrnvrlnids rvsdmltlsa sgyyavstld qiqtgpgspf fglafsapdi dlgatdpvtg
      421 rlliqpneas ieenplyeat yndrtdnrtr imgsfegrft pftnfelaan lsydrsnref
      481 trfwptfweq idqntyaggg llrdarfnea lnasvnatyt hdfgrlrtrt qarmlietqe
      541 fsqfsaegrn fgvdrvptlg ntssdnqilg sstsevkseg yylitnfdyd gryifdalvr
      601 rdgsslfgpd erwhtyyrls aaylineedw fdvngidelk inasvgtagg rprfsaqyet
      661 wsvsgdavik nvlgnrtlkp efsreieagl evgflnrflf nftyaqtetk dqllllplvs
      721 yfgfssqwqn agtvesntie mslrtfaiqr rdmslsfnvl fdrsvseite fnrpaqlhgp
      781 dvqqgaafyr ragervgtfy gigwatgvss lpdnmrqhad ffqrnddgyf vpvgqggswr
      841 danwgetvtl pdgtvlnwgi pvrqvneegq nfvklgnalp dfsmsfstnf ryknfsvfal
      901 ldaqiggeiy nqtrqwayrd lmhfdqdqrg kaddrkkpia yyetlyaqnl tsghfvedgt
      961 ylklrelalr ysfdssqlqp vfgnavnrin isligrnllt ftnysgfdpe vgresatvlr
     1021 fdsfdypnfr titgsiefqf
//
LOCUS       WP_114984213             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cyclonatronum proteinivorum].
ACCESSION   WP_114984213
VERSION     WP_114984213.1
KEYWORDS    RefSeq.
SOURCE      Cyclonatronum proteinivorum
  ORGANISM  Cyclonatronum proteinivorum
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Cyclonatronaceae; Cyclonatronum.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Cyclonatronum proteinivorum"
                     /db_xref="taxon:1457365"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40134
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigipketr pgetrvafnp etaqkwvdkg levrieksag lasfftdeay keagcvitdn
       61 aiegadiilk vnrptpdeik rmksgavfag flwpaqnrdt veallksgit slgmesvpri
      121 sraqkmdals smgsiagyka vligadalak ympmmmtaag tiapakvlvl gagvaglqai
      181 atakrlgavv eafdvrasvk eqveslgatf vdvplaeedq qaetaggyak elseaskklq
      241 eeaiqervkq sdlvittali pgkkapvlvr asavegmkpg avivdlaaeq ggnceltkad
      301 evtevhnvri fgptnitaal plhasqlyar nlnnllelii kegkltldfe deivkgstvt
      361 hagevvspfv raqlglnada
//
LOCUS       WP_114984754            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Cyclonatronum
            proteinivorum].
ACCESSION   WP_114984754
VERSION     WP_114984754.1
KEYWORDS    RefSeq.
SOURCE      Cyclonatronum proteinivorum
  ORGANISM  Cyclonatronum proteinivorum
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Cyclonatronaceae; Cyclonatronum.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Cyclonatronum proteinivorum"
                     /db_xref="taxon:1457365"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112894
     Region          62..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdhllmskek lqdagfqrss lqsdsglrkc lkptglmtai ltalfllfvv qvqtaeaqqr
       61 vqvsgvvtda sdgepligvt vivqgsleat gttigtstni dgeytlnvps dlntlifssv
      121 gyqtlsvnid grtrvdvaln advreldnvv vvgygtqres eitsavstit aadfqsgnin
      181 dsqqllqgkv aglsvsrpgg dpnadfdirl rglstlganq splvvidgia gadlntvdpn
      241 diesmtvlkd asaaaiygtr gangvilvtt rsgvgdqpis vqytgqvsis tvgnklevls
      301 aeqyrnfvsa dpdalpndlg netnwfdevt qtgvtqthsl nisggnnqtt ysvsgsyrdi
      361 qsiqigsgrq qlntrlnlth ralnnrlrln ttvavtdrde kiglgevfry aalfnptapi
      421 rnadgsffqq tffdyfnpva ineqstleae strmnlgfra eymfddyvpg lsgslfyarq
      481 sfsrlygeyy ektalfrgag rnglairesf dsrndlfegv lnydrsfgnv rfeattgysw
      541 qdfqddvffa eggdfindsf gwnnifeare fgrgegtvst frnenrligf fgrtnfvidd
      601 tyflsaavrr egssrfgvdn kwgtffavsg gleitnlvsi egvdqlkarv sygetgtdap
      661 fnglsqqrfs sgsaflvdgn fvpsigpvtn anpdlkwevk relnagvdfa fldarlrgsl
      721 dyyrsttddl lleinvpvpp nqapttwina aevsnngfea avsydairsr dltwttgitf
      781 atntstlery aagrqtianv gapglndtpm irvdegrkig diwgwkfsri gengewlflt
      841 pdgeeldtdg mralgdasrq vignglpdfe lswtnnvryn nwdfsmfwrg afghdmvnsf
      901 difhrnaffi tsrnvmrstl dipelvespq fssfqvedas ffrlenvtig ytvptspesv
      961 frslriyaaa nnlltltnys gvdpdvrfad tgntdnasra gapnplapgi errdqwftqr
     1021 sfvfgvslgf
//
LOCUS       WP_114987252             477 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Pragia
            fontium].
ACCESSION   WP_114987252
VERSION     WP_114987252.1
KEYWORDS    RefSeq.
SOURCE      Pragia fontium
  ORGANISM  Pragia fontium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Budviciaceae; Pragia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Pragia fontium"
                     /db_xref="taxon:82985"
     gene            1..477
                     /gene="nrfA"
     Protein         1..477
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53254
     Region          7..474
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mgvltvgkik aklsagllil faslmmsnvv aakseiearn evfakdhaaq ydswratsel
       61 dtlgggldey pdmvilwagy pfakdykkar ghfyaitdir eslrtaapmk dsdgplpmac
      121 wsckspdvar lideggedsy fegmwskgga qvvnpigcad chdtastdfa egkpalymsr
      181 pyteraleai nkpfekasrl dqqsmicsnc hveyyfsgkn kavkypwdng itvekmeayy
      241 dniefsdwkh qlskapmlka qhpeyetwsq gihgknnvtc idchmpkvqn aegkvytdhk
      301 ignpfdrfne tcanchtqsk qalqdvvasr keavrelkkk aerqlvhahf eakaawdaga
      361 teaemkpilq dirhaqwrwd yaiashgihm hapevglkvl gtsldksana rtklarllas
      421 kgitheielp dlstkanaqk algmdmqkle sdkqnflktr avewdenakk egrllsk
//
LOCUS       WP_114998056            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Empedobacter
            falsenii].
ACCESSION   WP_114998056
VERSION     WP_114998056.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110922
     Region          23..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrrltslgl laflglgtma faqvtgvvnd annfpesdve vtvkgtdkva ytdengnfni
       61 dakvgdtiii ngkefkvtst nlgalkydte skdislgevt ilggikldpa qkigsyetvk
      121 keafentpva svdevlngrv aglnfstggg qpgsaniiai rgagsfvgtt nplyvidgvv
      181 vgkgadnagl mtsfnplssi dpnqienvtv lkdasataly gargangviv vttkrgkfnq
      241 atkfnistdf avqdeaynen kymnaqefiq wggllrynsg latsreagee yfktytgwdg
      301 vtdtdwrdav qrntstvkty nfsaqgggen tsfragfsyy ennpltlysg fdrlstslaf
      361 dhkasekfkl ganvnfttvk nntymdggaf snpwltqwtv rpitpiynad gsynvnlgga
      421 gghnpvavqe yshiqgnint flasvygtyn ftkdltfdtn fgaqyqtlae eqwnnpwygd
      481 gvsvngrlye tdskyfdwnw vntlgyrkvi nevhdfqanv gmeyqehkmk yafahgtdfl
      541 iakpqmsnag timtatsydr kwiqysyfar lnyifnnrlt vsgqvrndnn stlgennkgg
      601 wfwsagasyn fakdinssai dvltirgnyg elgnipyads wgsvyngvsf mgvssiyngd
      661 kgfivsnvgn pdlkwettkq lnigleygfg nglisgsvdv yrklttdaif pseisydtps
      721 pvnssftnig eienkgieai ltvrpfnkgd frwsltanas ynksevgkml dpdarylagg
      781 mkaiqegref geyytygwag vdkatgagly wtdetktatt sdrtkaqqff qgttpfpkwm
      841 aglrsdmswk nitlsaffag sfdyqvydsw qsyalsdgas vtynqlssal ydswtpentd
      901 asnpiqlwgn gtnsraassr ylkdgdfirl kelklaysfg dklknagidn ltiylkgqnl
      961 itwvfddtlt fdpesnsnay sygwqgkgvf dytspimksy siglsidf
//
LOCUS       WP_114998206            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Empedobacter
            falsenii].
ACCESSION   WP_114998206
VERSION     WP_114998206.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113656
     Region          25..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkltslsl faflgfaafs ygqtkgiind gngfpeadvq itikgsdkva ytdengefdi
       61 dakigdilii ngkeyvvssn hlgviklqsn stvdlaetvv tafgvqkket vvgsvgtisa
      121 edienrplsn vakaldgava gvqvstgsgq pgsglsvqvr gvgsynlsss plyvvdgviy
      181 tgslqdlnpn diqsltvlkd aastslygas aangvvmitt kkgkkgkgsf rlssntgvvt
      241 ratpeysrvg agdyyvatwe smrngylasn ssatlaqana yastnlitnn lknniygvan
      301 dqvvvdgvlt ssdalyndfd wqdyisrtgs fqkydidysg gdekttyfag fgynketgyv
      361 iksdferyna rvnvdsqvtd wlklgtnltg sliksnqads sggssyinpf yftramgpiy
      421 spylydangq rvydtegnpv ydgnesrgrg ssassgrnvl qetllnnqyq dtnsinsrfn
      481 aeiklakglt fttnlsydvr nykykeygnk eigdasgtaa leiteykytg ttfnqilnyr
      541 ksfglhnfda ilghesferk tdysnvrktg etvsgiyeli nflnttsatg ynyiirkegy
      601 farvnydyas kyllsasarl dkssrfsden nqgifwsvga gwnihkedfl kdssvinelk
      661 lrasygqvgn dggideepgy qvdldlyslg ynngtesgvl lgqvgnsnlt wesknsfdvg
      721 ldfalfrnri sgsleyylqd vkdmifavpv pnsagvpgns iyqnigkmrn qgvelslnfg
      781 ivrnekfswd lgliaahnen emlkmangad daiingtkri aeghslydfw lrqwygvdss
      841 dgaalyvqdp tkaddsntrt vngtkvttny analydysgs slpdvygsit nnfkvgnfda
      901 simlnyqlgg ktydsnyall mssypqgqai stdmlsawkn pgdvtnvpim stanttnasa
      961 astrwlvssd yltiktvqlg ynfdkraieg iglsnlrvyv sgenlyswta rqglepaqsf
     1021 ngtttyrytp srtvslglnv sf
//
LOCUS       WP_114998823             972 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Empedobacter
            falsenii].
ACCESSION   WP_114998823
VERSION     WP_114998823.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 972)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 972)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..972
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107540
     Region          25..971
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrilkqslla lvlsspails aqtaikgtvq dsanntvlag advsnittge stvsdekgnf
       61 tleandgdii visffgyddq eitfagqtql qlrmsktten lkevvvigyg takkedvtgs
      121 vnqlnsedfn kgsitsaqel mtgkiagvvv tsaggapgdg qniiirgnss lslnsqplyv
      181 vdgvplsevn iggsrnpldf lnpndietmt ilkdasatai ygsraangvv mvttkkgkgk
      241 kfrfnynsit siyqpegyid vmnadqfrel vksvgtadei srlgnantdw qkeiyrtavg
      301 fdhnfsatgn iggkmpsrfs isntdqdgil kgdninrtta smnlspsfld dhlkfelnar
      361 gsyienqfan rgaigaaley dptqpvysga nifggyhtwm dgsvkhnlap tnpvalinen
      421 rdtsevrrfv gnakmdyklh flpsvtatvn vgydisnang rnvttanmpn ssltwdgskt
      481 tfsaqfynkl fdayltfnkd fgqhgltvvg gysyqyfnty ntnydseleq qgsdqftfvd
      541 rdhysllsyf grlnynfdnr yiltatmrad assklshdnq wgyfpsaaia wniskeeflk
      601 gssvvndlkl rvgygkvgnv nglgnfqflt ryqgsestay yqfgstfyqt yrpqpfngdl
      661 kweisstlna gidyslfknr iygtldvykk ktsdliasvy vdpftnfgnm idknigdmen
      721 kgiefsvnad iiktkdfdws fgyniafndn kivnlptdnl tgsidggtgn niqiqregee
      781 pfsfyvykqi ydangkpieg ayedlnndgi inekdryihk spfakvtmgf ntffryknwd
      841 lsataranig nyaynnmass kgyskkatgn gqnylsnvls syyntgftsi tetnllsdhf
      901 iedasffrid nitlgynlkq aikgldirly gavqnvavft nysgldpeiy rgidnsfypr
      961 prtyvfglnv nf
//
LOCUS       WP_115000285            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Empedobacter
            falsenii].
ACCESSION   WP_115000285
VERSION     WP_115000285.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter falsenii
  ORGANISM  Empedobacter falsenii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Empedobacter.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Empedobacter falsenii"
                     /db_xref="taxon:343874"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124675
     Region          22..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlillpl faasiafsqe krvitgsvqd ekslvgiaga svkieaqsis tktdqkgiie
       61 svtvgtvtde dgffslevpa gtksvlisyl gydsklvels tdlatyhvsl kstsgevlpe
      121 nndlkevvvt gyqkiekrkl tsavstvkmd diqqagvasv dqllsgqiag vavstetgsp
      181 gspskirirg taslsgpqdp lwvidglple gndvpnfsdk dnidqlqnfs iaglnpndie
      241 ditilkdaaa taiygaraan gvisittkrg kkgamtvnfs antfvtarpd fgrlnllnas
      301 qkvdlelmla srddltyrtd kgevmrilqk ngqlnalrng gfnsldlitq nqinslrnnt
      361 tdwgkllyrn aintqyglsi sggndrsdyy fslgyydeqg ttigtgfery nltlknnykl
      421 ndkldvgisi fatssdkksf vtdadasinp inysrnanpy lspfnadgsy rydndidgfe
      481 drsvpfnfie erentnytlk nrslkgiidl nyqlakglkl tsqfgiqyds nktekyaeqe
      541 tyftrkmreg tryyksgqyl yflpdggvkq nwdneffqyn wklqgtystt innrheidlm
      601 agteirhtqn ettltrafgy nkitktgtpi vfpnssfasd kryetyremp tdenayvstf
      661 atasytldrk ytvfgsvryd dtnlfgvnkk ykylpiwavs aswlvskesf menvdfisnl
      721 rlrasyglqg nidrntspff igdyndatil pgnkediina inlpndllrw ekttntnvgl
      781 dlglfknrin lavdvynrkg tdmismretp letgfeytmv nwgeltnkgf eialttrnid
      841 kknfkwstti nfahnkskvl keqqrenslv psreglpvna ifalktagfd eygnpmfwkg
      901 dekvsakeff alydlyedfl pgeivdsklt seekrklfty igdrdpkftg giinnfkihn
      961 fdltisaafn lkqtvmktps yrgmeldpgr nytqdifeag stlpgitspi kgdndswman
     1021 kwfagnnana ynlldiwake isymrissir lgytlpnkya evvgfksarf slegrnlfvf
     1081 sngykgyfdp etygniyaqp iaksvtvgln vsf
//
LOCUS       WP_115015931             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus lacunae].
ACCESSION   WP_115015931
VERSION     WP_115015931.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus lacunae
  ORGANISM  Cupriavidus lacunae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus lacunae"
                     /db_xref="taxon:2666307"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38898
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipieiq ageqrvaatp etvrkfvaqg hqvlvqagag vrasqtdaay eaagarigta
       61 aealgadlvl kvrapdivel aqmrpgaalv gmlnpfdvqn qarmaaagit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaarhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra iqadivitta lipgrkapvp lqeatvqqmk pgsvvvdlaa vqggncpltv
      301 adevvnhngv iiightnlas mvaadasaly arnvldflkl ildkdgklvv nqeddivaac
      361 lmtgrdemal as
//
LOCUS       WP_115019838             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Synechococcus sp. UW140].
ACCESSION   WP_115019838
VERSION     WP_115019838.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. UW140
  ORGANISM  Synechococcus sp. UW140
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Synechococcus sp. UW140"
                     /db_xref="taxon:368503"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39460
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(18,79,98,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(47,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milprllipv etaaaetrva vspetikkfi glgcsvaieq gagasagfvd ssyaeagael
       61 vavgdaqawg qadlllcvqt pqqqalaklr ngalvvglls pysnesltts lkncglsama
      121 lellprisra qsadalssqa niagykavll gaaaldryfp mlmtaagtvq pakvvilgag
      181 vaglqavata rrlgavvfvs dirpavkeqv eslgarfiep pemddkpaes ggyakqasea
      241 flaaqrqqls dqlaeadvai ctaqvpgrra prlisddmld rmrpgsvvvd lavaqggnca
      301 dtqpsqtvdr kgvkligand lpcsvpnhas alyarnllal lepmfkdgqf sldtedelia
      361 gcliaqdgsi rrgdvltpga n
//
LOCUS       WP_115030927             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Dermatophilus congolensis].
ACCESSION   WP_115030927
VERSION     WP_115030927.1
KEYWORDS    RefSeq.
SOURCE      Dermatophilus congolensis
  ORGANISM  Dermatophilus congolensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Dermatophilus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Dermatophilus congolensis"
                     /db_xref="taxon:1863"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53162
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipqett pgetrvaatp stvttliklg hnviiesgag eradicdday leagahigdt
       61 attwaadiia kinppndeel dnirdgatli sllnprtdpa mvdklatrni talamdavpr
      121 israqsidvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakili agagvaglaa
      181 igtagslgai vratdtrpev aeqvqsmgae fvavntnekt tstdgyaret ssayetaaaa
      241 vyaeqakdvd iiittalipg rpaprlitad mvnsmkpgsv ivdmaaangg nvegvipgek
      301 tttpngvtii gytdlagrlp tqasqlygtn ivnllnlltp hkdghlaldm ddsvirgmtv
      361 ihngnlmwpp ppvnisantp ptnttptppt qppptpnpir ryigigvasa lflalaaftp
      421 apllshtvvf alavvigfyv igsvhhalht plmsvtnais giiiigaitq ittnntlist
      481 lafiavlvas invfggftlt hrmlamfhkd ps
//
LOCUS       WP_115061792             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Oligella
            ureolytica].
ACCESSION   WP_115061792
VERSION     WP_115061792.1
KEYWORDS    RefSeq.
SOURCE      Oligella ureolytica
  ORGANISM  Oligella ureolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Oligella ureolytica"
                     /db_xref="taxon:90244"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54278
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkeqf agetrvaatp ttvtqliklg fevavesgag llakfddasy veagakvmsr
       61 eevfnsdiiy kinaptdaei damqegtilv sfiqpaqnsd lidklsakki tamavdmvpr
      121 israqsmdvl ssmanisgyr avieaahhfg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igaagslgav vkafdtrlev aeqiesmgge flkldfpees ggsgdgyakv msdefikaem
      241 alfaeqakvv diiittaaip gkpspklitk emvdsmkpgs vivdlaalgg gnceytvpge
      301 vvttnnnvtv igytdlpnrl agqssqlyat nlvnlsklit pkkdgnveld fddvivrnmt
      361 vthhgegmfp pppiqvsaap aqaasapapv qvkkepkplw qrlalpvigv aiylwasnya
      421 pqeflnhltv fmlscvvgyy vvwnvthalh tplmsvtnai sgiiivgaiv qmstisgfas
      481 flafisvflv sinifggfyv trrmlnmfrk g
//
LOCUS       WP_115067565             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            mucosa].
ACCESSION   WP_115067565
VERSION     WP_115067565.1
KEYWORDS    RefSeq.
SOURCE      Neisseria mucosa
  ORGANISM  Neisseria mucosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria mucosa"
                     /db_xref="taxon:488"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53915
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacplly kvnapsegel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiatem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpdpkpvp lwkklapavi aailvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vsllafiail iasvnifggf fvtrrmlnmf rkg
//
LOCUS       WP_115074197             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Oligella
            urethralis].
ACCESSION   WP_115074197
VERSION     WP_115074197.1
KEYWORDS    RefSeq.
SOURCE      Oligella urethralis
  ORGANISM  Oligella urethralis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Oligella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Oligella urethralis"
                     /db_xref="taxon:90245"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54291
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkeqf agetrvaatp ttvaqliklg ydvavesgag qlakfddvay teagasvvsr
       61 ddvfksdivy kinapsdaei damdegtilv sfvqpaqnpe lveklrakki tamavdmvpr
      121 israqsmdvl ssmanisgyr avieaahhfg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igaagslgai vkafdtrlev aeqiesmgge flkldfpqea ggsgdgyakv msdefikaem
      241 alfaeqakvv diiittaaip gkpspklitk emvdsmkpgs vivdlaalgg gnceytvpge
      301 vvvtdnnvtv igytdlpnrl agqssqlyst nlvnlsklit pakdgqavld fddviirnmt
      361 vthagelmfp pppiqvsaap qqaaapaaap vkvekapkpl wqklalplig vliylwashy
      421 apqeflnhlt vfmlscvvgy yvvwnvthal htplmsvtna isgiiivgav iqmsningfa
      481 sflafisvfl vsinifggfy vtrrmlnmfr kg
//
LOCUS       WP_115079872             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas fluorescens].
ACCESSION   WP_115079872
VERSION     WP_115079872.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38860
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hrvtvqtgag vkasvidsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnndt iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv tivgptnlag evaadasaly arnlldflkl vftkegqfev nlkddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_115091864            1124 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Myroides
            odoratus].
ACCESSION   WP_115091864
VERSION     WP_115091864.1
KEYWORDS    RefSeq.
SOURCE      Myroides odoratus
  ORGANISM  Myroides odoratus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Myroides odoratus"
                     /db_xref="taxon:256"
     Protein         1..1124
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125787
     Region          26..1123
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkivlhfff viaallmvne gfaqsrkvtg rvsdgdgypl pgasvlikgt qegvgtdldg
       61 nfsinvkddn avlvfsfvmm nsvekkvgka svinvvlked stldeinivt tgyesvnkrt
      121 ftgavsrise kelkvdgvpd vsrmiegkaa gvtvqnvtgt fgaapkitvr gsssifgdtk
      181 plwvidgmvq eeiinvsfed lasgnastml ssavaglnan dvlsieilkd aaatsiygar
      241 amngvvvitt ksgrkntplt vnynmentir eipnygsfdi lnsqstmgil lemedkgllt
      301 dptisqgryg giynlwfksy ntydplgged hkggyreint pgnkydflrq yeyantdwfk
      361 hlfrpsimqn hslsfsggse natyyasvgy mkdpgwtiad qvqritanlk ttfyfndrmn
      421 lglstvfssr kqdapgsfdr qddpvggsvs rdfdinpfny alntsralrp ydndgfyety
      481 rqnwapfnil neldnnnmtl dvkdiklqad feyklmdglk fnssaalryv isdrdhdvre
      541 gsnvvqafra aettvvkdqn iylyqdpdhl dgekevvlkd ggiwyryqnk mtainwrnsf
      601 sydkifgkng qheinafggs eirvidrdfs aqdtygimyd ngylgnpnhk lyrklfaegd
      661 alfkrgyeke rnvgffarvn ytydgkytas ltgrydasnq qgqsgamwlp twtasgkwni
      721 iqeewmmnqt tfsdlslrgs ygltatagpa snssavfkna ltvsrfdpnt revgmqienl
      781 kngdltwekq yeanigldmg lfknriylst diyqrqafdl vdqvrtsgig getykwgnna
      841 dmttkgvels lttrnidtks fkwtsnlnvs yydqkikkls ytprafdlia ktggnvvgkp
      901 rnvlysyeft glnseglpty vmadgetdnv gganfqdtqd vvgylkyegt vepnktigfn
      961 ntfqyenwsl dvmtvaawgn vvrldpnfss qyndtqiftk amnnrwviag denttnvpvi
     1021 asadmidkyg rsldraynty nysdqriakg dfiriknitl gyefpelvkk qmrvsslgvk
     1081 lsvtnpflly sdkklngqdp effrvggvam pvtrqytltl nlsi
//
LOCUS       WP_115094298             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            gonorrhoeae].
ACCESSION   WP_115094298
VERSION     WP_115094298.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53486
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igadvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldflqes ggggdgcakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaatgg nceltrpgel
      301 svtgngvkii gytdmanrla gqssqlyatn lvnltkllsp nkdgeitldf edviirnmtv
      361 trdgeitfpp ppiqvsaqpq qtpsekaapa akpepkpvpl wkklapaaia avlvlwvgav
      421 apaaflnhfi vfvlacvigy hvvwnvshsl htplmsvtna isgiivvgal lqigqgngfv
      481 sllsfvaili aginifggfa vtrrmlnmfk kg
//
LOCUS       WP_115103751             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia lacunae].
ACCESSION   WP_115103751
VERSION     WP_115103751.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia lacunae
  ORGANISM  Paraburkholderia lacunae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia lacunae"
                     /db_xref="taxon:2211104"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39448
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqsgag tgasfpddaf taagaeivdg
       61 atafgadivl kvqsptdael pllkrgatlv gmldpfnaen alklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppgwlq
      241 rqsalvhera kqadvvista lipgraaptl isvetvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvtrhgvqi lgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll arngevarka
//
LOCUS       WP_115118525             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Synechococcus sp. UW105].
ACCESSION   WP_115118525
VERSION     WP_115118525.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. UW105
  ORGANISM  Synechococcus sp. UW105
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Synechococcus sp. UW105"
                     /db_xref="taxon:337067"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39475
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(18,79,98,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(47,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milprllipv etaaaetrva vspetikkfi glgcsvaieq gagasagfvd ssyteagael
       61 vavgdiqawg qadlllcvqt pqqqalaklr ngalvvglls pysneslats lkscglsama
      121 lellprisra qsadalssqa niagykavll gaaaldryfp mlmtaagtvq pakvvilgag
      181 vaglqavata rrlgavvfvs dirpavkeqv eslgarfiep pemddkpaes ggyakqasea
      241 flaaqrqqls dqlaeadvai ctaqvpgrra prlisddmld rmrpgsvvvd lavaqggnca
      301 dtqpsqtvdr kgvkligand lpcsvpnhas alyarnllal lepmfkdgqf sldtedelia
      361 gcliaqdgsi rrgdvltpga n
//
LOCUS       WP_115107292             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia lacunae].
ACCESSION   WP_115107292
VERSION     WP_115107292.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia lacunae
  ORGANISM  Paraburkholderia lacunae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Paraburkholderia lacunae"
                     /db_xref="taxon:2211104"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54800
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligiple vapgerrvat vpevveklik lgfavavqsg agaganfgdg dyraagaevv
       61 ataaelwars divfkvrpps seevalmreg atligfvwpt qnpelmqqla arratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akffiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq ardadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl ygnnllrvve elcktkdgti nvdfdddair
      361 gltvikegsv twppppikqp avapkpqpaa aaaasapkkg hgssepmsak slaivfgiga
      421 lafllvglfa patflshftv fvlacfigym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplggsa agdrpsglil glavgalalt avnmfggfav trrmlamfrk
//
LOCUS       WP_115123264            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Marinirhabdus
            gelatinilytica].
ACCESSION   WP_115123264
VERSION     WP_115123264.1
KEYWORDS    RefSeq.
SOURCE      Marinirhabdus gelatinilytica
  ORGANISM  Marinirhabdus gelatinilytica
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Marinirhabdus gelatinilytica"
                     /db_xref="taxon:1703343"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115439
     Region          26..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkkrlfll lllvsssivl aqesytlsgt vvsaadqipv pganvilegt srgtttdfdg
       61 nyeiqvqngd vvqfsyigyv sqsveitgqt tlnialaeea ssldevvvvg ygtrkksqvt
      121 gavakiggee vaaiqstrvd ealggklagv liqnqdgapg adpkiqvraa ssingnsnpl
      181 ivvdgypisg tlatvnpndi qsievlkdaa saaiygsrga ngvilvttkk gktgdptfsy
      241 dtyssissry rsdrrkltag ewaneleqgi asgrfdvsel dpafvnykin ayrnapdvvp
      301 vedylfrngy stshnfsmsg gsenanyfas vgyqntegvv itqafervna rlnvdarlgd
      361 kfetgvsfng fasdrdivgh dirdllrayn ihpiyhtaas iayvqqldqq aqalgldpfd
      421 dgyrggdapf nnsiytlepg dtaqdwhygr sgngiggsgd agpatkldnt dryqktffan
      481 vssylqyqiv kglniktvlg gdirdtqdyf wrglefdsra rpnqtaldqv dvkrssilse
      541 ttlnysgeig nheisavagv efqtlytrgt alngtnvpfs diinynllqp ediavtevde
      601 tivrksifgr inyafdnryl lsvsvrrdgd srfgannkye tfpafsigwn vhneafynfd
      661 aistlkprfs ygslgttsdl gaynslslln pqstalgtgf lipsdiense ltwqtntetn
      721 ygldlgfinn rvrlsadyyt sdiedilinq svsevfgtps irlnsgdvrs tgielelssa
      781 ivrnenfswd fggnfstvet eitdlgglde lpqtiygqsg rgpvfrnyvg geigemwgle
      841 tigivedeyi edptraigin sseyyvvdqn gdgvidntkt veeggdlvki gqntpdfyyg
      901 vnsnfrykdf dlsfqlqgae ggevfnvdpl yynsefggrl rdsfdadndg iadhnglhyt
      961 qsrnqtdaqi qdasylamrn ltlgytikpe fitrvginsa rvylaatnlf yifgddytsd
     1021 npegvettnt gylgpttygv qvgaspivrs ftfglnvnf
//
LOCUS       WP_115125414             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Synechococcus sp. GEYO].
ACCESSION   WP_115125414
VERSION     WP_115125414.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus sp. GEYO
  ORGANISM  Synechococcus sp. GEYO
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Synechococcus sp. GEYO"
                     /db_xref="taxon:2575511"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38437
     Region          2..359
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(9,70,89,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(38,122..123,132..133,136..137,140..141,143..144,
                     146..151,153,155..157,160,183..184,275..276,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(117..118,122,125,128,169..172,192..194,225,236,
                     253..255,262,264)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,122,132,175..176,183,199..200,202..205)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(152..156,159,162,185,187)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 metaagetrv aaspetvkkf aalgcsvvle qgagqpsgyl dqayaeagae lvtrgdssaw
       61 sqadvllcvq spstqalsql rrgallvgll apyanaelaa glqqaglsam alellprisr
      121 aqsadalssq aniagyksvl lasaaldryf pmlmtaagtv qparvvilga gvaglqavat
      181 arrlgavvyv sdirpavkeq veslgarfid ppemedkpae sggyakqasd aflaaqrqql
      241 sdqlaeadva ictaqvpgrr aprlisedml drmrpgavvv dlavaqggnc adtiasktvd
      301 rngvkligan dlpctvpnha samysrnlla llqptlkdgq ltldsedeli agclisqdgt
      361 irrgdvltpg an
//
LOCUS       WP_115133440             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            zoodegmatis].
ACCESSION   WP_115133440
VERSION     WP_115133440.1
KEYWORDS    RefSeq.
SOURCE      Neisseria zoodegmatis
  ORGANISM  Neisseria zoodegmatis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Neisseria zoodegmatis"
                     /db_xref="taxon:326523"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53778
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl pgetrvactp stvtqlqklg fevvvergag laaslddaay eaagavvada
       61 aevwacpliy kvnapsesea grlnagqtlv sflwpaqnpe lvqkltdkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vkafdtrlev aeqiesmggq flkldfpqes ggsgdgyakv mseefiaaem
      241 klfaeqarqv diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lfvtdngiki iaytdmanrl agqssqlyat nlvnlsklls pnkdgeiald fedviirnmt
      361 vtrdgeitfp ppaiqvsaap qqqaqaapva kpepkpvptw kklapaviga vlvlwmgavv
      421 paeflnhfiv fvlacvigyy vvwnvshslh tplmsvtnai sgiivvgall qigqgngvvs
      481 flafiavlia sinifggfyv trrmlnmfrk g
//
LOCUS       WP_115149604             471 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Plesiomonas shigelloides].
ACCESSION   WP_115149604
VERSION     WP_115149604.1
KEYWORDS    RefSeq.
SOURCE      Plesiomonas shigelloides
  ORGANISM  Plesiomonas shigelloides
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Plesiomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Plesiomonas shigelloides"
                     /db_xref="taxon:703"
     gene            1..471
                     /gene="nrfA"
     Protein         1..471
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52166
     Region          15..471
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivklnttsi ttglalflag tllcssalaq vearndkfad ahqpqyqswt qtqqsserad
       61 alaedpnmvi lwagypfakd ynkprghyya ltdvrdtlrt gapktaedgp lpmacwscks
      121 pdvarmiese gedayfkgmw akggseivns igcadchatd sqefkdgkpa lhlsrpyasr
      181 amdaihmpfa kqghfvqqaq vcgqchveyy fsgdnkavkf pwdngtsada maeyydelgf
      241 kdwvhglskt pmlkaqhpey etwqagihgk nnvgcvdchm pkvqgqdgkl ytdhkvgnpf
      301 drfdqtcanc htqskemlqg vvkerkeain tlklkveqql vhahfeakaa wdagateeqm
      361 qpilqdirqa qwrwdyaias hgvhmhapdi alktlgdaln laadartkla rllatkgitg
      421 eiplpdistk ekaqaalgmd mkqfisdkqq flkttvpawe keakdagrls q
//
LOCUS       WP_115153291             914 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            buccae].
ACCESSION   WP_115153291
VERSION     WP_115153291.1
KEYWORDS    RefSeq.
SOURCE      Segatella buccae (Prevotella buccae)
  ORGANISM  Segatella buccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Segatella buccae"
                     /db_xref="taxon:28126"
     Protein         1..914
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=99391
     Region          51..912
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 minirsftvl flfgasssmf plhaqttalt ssvqdslrke fmggistgkg gsvdvvdqsr
       61 mkkglitssl dalsgqavgv niasagndrm amlssvrvrg ttsltggndp lviidgvysd
      121 lstlsgiypa diasfailkn aaetapygsr gasgviqvtt kkghgsqfhi sydgnmgfes
      181 vydkirmlnr ngyistakal gldyndggfd tdfqkaitrt gfiqnhhvaf sgggesssyr
      241 aslgfmdhnt viknseydnf vakidltqka fdnlltidlg vfgssqnnkn ifdtqqlfys
      301 aatqnptypd gmnatggwdr nalasqicnp lsllhkqdhd kllnfnthiq lsfalsqdla
      361 lkafgsysyn stekaqylpt wvwaqgqayr aevknedwlg nlsltyhhdf rghvidalll
      421 geyqsrlqrg ffttvkgfts nafgydnlaa gatipyggtg shydnpklas ammqvsydcq
      481 glftltanar adgssmfgkg nkwgffpsls aswnllhtfs alqqlhrldk ltlrsgygvs
      541 gntggiesyn smlllnpngl vswngtpaat lgiasnanpn lkwelrstfn igtdiglfdn
      601 rlvltaeyyy skttdmlymy nvpvppftyd kllanigsms nsgfevglgl tpllkkdmel
      661 ninvnlsfqk nkllslsgny ngtylstsdi tpighltgag fhggdnnivy qivgqplgvf
      721 ylphctglsk nangqytydi adldgnkvvd iadgadryia gqatpkmtlg snisfryrdf
      781 disvqmngaf ghkiyngtal tymnmtsfpa ynvmegasea niadqtatdy wlesgdylni
      841 dyvtvgwnvp vkkhcryins lrlslsinnl atltgysglt pminsyvvgs tlgiddkrsy
      901 ppyrsyslgv siqf
//
LOCUS       WP_115153787            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            buccae].
ACCESSION   WP_115153787
VERSION     WP_115153787.1
KEYWORDS    RefSeq.
SOURCE      Segatella buccae (Prevotella buccae)
  ORGANISM  Segatella buccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Segatella buccae"
                     /db_xref="taxon:28126"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118201
     Region          38..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrqvilfli stllmlfpls ggsvlqqsei aaqtpratgv vvdtgnepii gasvmvkgak
       61 tgtvtdmdgr fgldaadnat lvvsyigyvt qevkvakgrp mrvvlkedvh qinevvital
      121 gikrdrkalg yslgevkgee lqkakevnvv nslagkvagl tvsktatgpa gstrvilrgs
      181 teltgnnqpl yvvdgvpmdn tnfdssdqwg gfdlgdgiss inpddiesls vlkgpaasal
      241 ygsrashgvi littkkadgk kdfsvelnst ttfetqltkw nnvqyefgqg segrislsdd
      301 ryssnrnwgp ridpglylty fdgkarpyvv iknnidgffr tgintsnsli vskkmgktgi
      361 ratytdmrdk dlipkthmar niinmrantn iagtldldfk mtytrenvkn rpavadhran
      421 iaknlmtlst tfdqawlrdn yedengryyn wnngdvynin pywvlnkmsn dtkkdnykga
      481 avirykvmkq ltlqttlgad innlvfndfa ypsspgrelg qlvtkdyknr mynaeflaiy
      541 kdryrkwdyg atlggnlykv dnkttvvtaq nmimtdaqap qsfmekkirl dtyrkqinsv
      601 ygslnlaydn fafmdmtlrg dysstlprnn nmywypsvsg sllfsellkt gkrilpygkv
      661 raswakvgnd tapymmtlsy emtpnsfgky pmamissdvi pnrnlkptmt gsvelgfelr
      721 flknrigldf tyynqhskdq ilrmntsyas synyqlinag dienkgveiv lntrpielkd
      781 fswdlnlnfa knsnkvkela ngidefelas arwlgvkvva kvgenygcim gkdflrneng
      841 diiidgtsgl pkmtddlkvl gnaswdwtgg ittnlryknf slgaifdvkv gadlysmsar
      901 sayatgkhkd tlegrdawyq seekrleagv tpaawkatgg yvakgviqqd dgtykpndiy
      961 vdpqvywayv stqtarpfiy dnsyvklrel tlsyvfprkl lgkslnaltl sfvarnlfni
     1021 yknvpnidpd snynngtgmg lefgslpsrr sfglnvnlkf
//
LOCUS       WP_115153681             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            buccae].
ACCESSION   WP_115153681
VERSION     WP_115153681.1
KEYWORDS    RefSeq.
SOURCE      Segatella buccae (Prevotella buccae)
  ORGANISM  Segatella buccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Segatella buccae"
                     /db_xref="taxon:28126"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110468
     Region          26..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkkilvpl fatcalqama qtagsitgvv vdqwnkpisg avvmdandpl navptrkdgs
       61 ftisgsktlk vqapnrsekv veagdgkvvv kmdyasrpvy tgtgkvltek estasvagaw
      121 gsdlnhrstk digqslfgqv lglqtlqqsa rfagvsttny vrglqstnss pliivdgier
      181 eitditpeev dhvsvlkdaa aaalygykga ngvlvittkr glydkreisa sydhsfnwqa
      241 rrpkfvdgft yagavneara negatavyde nalnaykngt lpynfpnvdw vgetmrdvss
      301 tdnfnltfrg ggmkfryytl fnlinsngyi kqpnlndgys tqekymkani rsnwdidlsp
      361 ktklavnllg tlaesnypgd naniwnaiys mpsgavpvkt edglwggssq fagtlnpval
      421 atgaaysknh rrtfdadltl tqnldafldg lygsfrlayd ntslitenrs klynygmntv
      481 tgwntdgtva svnkykqtvt sesmaensdl tsynrlfnfy aqlaydktfg khsiyaqgrw
      541 eyeyknyqgl nttnyrmtas lfthygflsr yffdtswaya gsnklalghk wtlsptfsaa
      601 wvasdeawak dlgwldflkv rasygvqntd aipyedyweq lykysgvgyr vgsefglgna
      661 ryemsrlasq aslheradkf nigldatlfg gldvtmdffs qqrnniwvea sgkytavlgv
      721 eapyeaaeki sshgfelgln yiknvtsdlt vnvggnftyn knkvkemlee prafenlvmt
      781 gkpygqltgl qaiglfkdea diaasprqnf gpvypgdiky kdvngdnvid andvtsigyn
      841 tlcpeiyysf klgadyknfg ftalfqgagn fsammssslv rpsasgnsis teyynnrwtp
      901 enptakyprl syesssnnnr nssfwlvdrs flklryveay ynlpqsvlnr ikfiskakvy
      961 vrgidllcfd kvkvadpetp ntlyptsrsi vaglsldf
//
LOCUS       WP_115153815             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            buccae].
ACCESSION   WP_115153815
VERSION     WP_115153815.1
KEYWORDS    RefSeq.
SOURCE      Segatella buccae (Prevotella buccae)
  ORGANISM  Segatella buccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Segatella buccae"
                     /db_xref="taxon:28126"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111158
     Region          23..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrhilltia lmtglaassq nnvtgvvvdk agnpvsgakv eakgglikay tdrqgsftis
       61 tgtdqltvda pdlsrkivsi egtgplrivm dyasqpinig fgirqtvges tmsvagaanr
      121 dfnnrsakni gnslfghvlg lttlqgtgdy ssyeptfyir glqsmsgnsp ivlvdgiern
      181 isyitpeeve nvivlkdapa valygykgin givniitkrg kyksneinfs fdhaitwear
      241 rpkfvdayty anamneafan dgkaprysal eldafksgky pysypnvdwi ketfrdngan
      301 silnlsfrgg germryytli nytddrgfia hpnkndgyst qnkyskanlr snldidltat
      361 tkvqvnidgv lleslrpgls sdnlwgkiyt vpatafpikt qnglwggnat wdgyynpval
      421 tegrayskah tralfadmtl tqdlssltdg lsawtrlayd nisaywenht reyrygmdvv
      481 sewangepsa ydhftggkdg alskdskldw qnknfnfgig anydrrfglh sissllmwny
      541 eyrnwnginn twyrtaasly nhygykdryf adlsltlags nklapshkws fsptlsaawv
      601 iskenfmrsl sfvnflklra swgiintdni ptegyweqaf vseggyslgg nnqwsggwre
      661 grlastnvth erdnkynvgf datifnslnl tmdgyyrrrs diwvnasgrn savlgienpy
      721 vnggivdswg leagadytkk vgddlllnag akftlaknki veeyetpray kyqertglpl
      781 gqifglqaig yftdqadidh spaqqfsevr pgdikykdqn gdnvinadde vkmgynsycp
      841 eiyysfhiga eykgigfnam fqgagnytai lnaqsmfwpt lgttnisqyy ydnrwtpetp
      901 nakfprltse gnqnnfrtns vwlanrsflk lrnvelyykl pkgllratky ingakfyvrg
      961 idllcfdhik evdpeqygtt ypltrsvvig lalnf
//
LOCUS       WP_115153826             943 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            buccae].
ACCESSION   WP_115153826
VERSION     WP_115153826.1
KEYWORDS    RefSeq.
SOURCE      Segatella buccae (Prevotella buccae)
  ORGANISM  Segatella buccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 943)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 943)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 943)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..943
                     /organism="Segatella buccae"
                     /db_xref="taxon:28126"
     Protein         1..943
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105129
     Region          35..942
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikktyint mlvagllgsa tatqaqalas dsakvnvafr svdkedlmgg vsavdmtdlt
       61 rknystysld nmqayvggyn gqlwnmgeal vvvdgvprda nnvlpteieq itflksasav
      121 vlygsraakg avlittkrsr vdglqvsvrg natlftpkry pkylgapqym tlynealand
      181 gkspvysded iynyasgvnp yrypnidffs sdyvkksfqr yegiaefqgg grfahfyani
      241 glynvndlmk fgegkdnhtt rlnirgnvdl rlndwitgwv danatfydar ndnsdfwsqs
      301 atlrptsqyp ltplipleyi nksvpsmktm iensnyvidg kyliggtqsl qtnpfasmya
      361 agyhtytsrq lqfdagvkmd lasvlkglsf ktqfavdyat syttnlkney acfepvwsnv
      421 ngkdeiidlk kygtdkrtgi qniegstsrq tilysaqfdy drqfgdhgva asllahgyqr
      481 tvsteyhkvt nanlglqmny nylhkyyadl smaaihspkl apghreavsp vlsvawrlgk
      541 erfmkdaewi kdlkltasyg ivnedldien yymydqifta tgtwwgwses ansmqtsdsq
      601 rganndltfv krkefrlgln anlwdglitl eanyfnvatn gllttpstsy psyfmtywpk
      661 stflpyinyn nqrrtgfdft vnvhkrvgev dlqagltgml ysskntrvse nveydwlkae
      721 ggridalrgy qclgfigeed vvrgadgkvt gyadgvavvn nntkpgdlky kdqngdgkid
      781 skdavvlghw tpdfnlgfhf takykgftlf lnmtgnfgat aiknnayawa ygdrkysdmv
      841 lgrwtpataa tatyprltte ggelnfvtsd fwtystdavr lnkvqltydl pgslfsgkfv
      901 kgatvyvsgg nlltiakerk ymetavgsap qtraynlgvk vnf
//
LOCUS       WP_115153879            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            buccae].
ACCESSION   WP_115153879
VERSION     WP_115153879.1
KEYWORDS    RefSeq.
SOURCE      Segatella buccae (Prevotella buccae)
  ORGANISM  Segatella buccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Segatella buccae"
                     /db_xref="taxon:28126"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123240
     Region          24..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrftlflv glflsvgmaf aqtkisgtvv sqedgepiig asvlvqgskv gavtdvdghf
       61 tldvpagkkl visyigmqtq tinasanmkv aliqdnktlq evvvtglttm dkrlfsgatt
      121 kldasttkld gmadisrsle graagvsvqn vsgtfgtapk irvrgatsif gsskplwvvd
      181 gvimedvvdv daddlssgda ntlissaiag lnsddiesfq ilkdgsatsi ygaramagvi
      241 vvttkkgrag qahvsytgey tmrlkpsysn fnimnsqdqm evyqelqqkg flnyaetata
      301 mnsgvygkly qllsqydatt gqfavantee aklaylraae yrntnwfdql fsnavmhnhs
      361 vsvsggtdks qyyaslsamf dpgwtkaskv qrytanlntt ynvskyidin lignasyrkq
      421 kapgtlnsev dpvngevkrd fdinpysyai ntsrtldpne fytrnyapfn ilheldnnyl
      481 dlnvndfrvs asidykpirk lkltllgamk gastsqehyi rdesnqalay ramptaaird
      541 rnpflykdpd nvyalpisvl pyggiyertd nrsfgwdtri sasyndviad khiinfyagm
      601 etnytdrhtt wfrgwglqyk kgevplyayq vfkrgleegs dyfnmknthy rsaaffgtat
      661 ysyqgryqvt gtmryegtny lgkatsarwl ptwnvssawn aheekwfant fkdvlthgtf
      721 rlsysltgdr ppvtnalpiy ksenpwrpft svqesgltqt lgnpeltyek khefnvgldl
      781 gflknrinfs idaywrnnyd ligyantqly gegqvanvas mksngvefsl stqniktadf
      841 swntnlifsy ahneitdlys pariidlvqg tgyplvgypv rsifsipfkg lnrdglptfl
      901 dqdgnitttg iyfqtrdqsk tkflkyegpv dptvtgslgn vfkyknwtln vfltysfgnv
      961 vrlddvfksk yddlssmtke frnrwthagd ekrtdvpvia srwqntqden lkyaynayny
     1021 sdvrvakgdf irmkeialty dfpkpwlnpm gvnnlslklq atnlfliyad kklngqdpef
     1081 fntggvavpv pkqftltvrl gl
//
LOCUS       WP_115168663            1161 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115168663
VERSION     WP_115168663.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1161
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126720
     Region          49..135
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cl21470"
                     /db_xref="CDD:473874"
     Region          178..1160
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mihylyhalf ltcgllffcq tgradlienk yhssyslshs yfasdsieir gkvtdsagma
       61 iegvvvtekg tsnsgltdqn gefkiaadpn gilvviksgf knkevhvnnq rlveislssg
      121 kaeaetetda dsvvirqdsa tvvqtpdsag tvkpavtdss avkqdssvqi vpgkqaavsg
      181 lvngpqgplp gvtvtvvgtn qatntdengk fqiaagpknk ikfssigyrs ltqtvgnrkd
      241 iqvvlssetn vldsvqvvav gygtmnratl psavssigan eikdevlpsi tqaiqgkagg
      301 vqvtqksgsp gggisirvrg ttsinassdp lyvvdgipvn sttnftggst fdfgggtqgi
      361 nvlssinpsd vqsieilkda asssiygsra angvvlittk kgvagqsefn fnmyegfsqv
      421 preryydlmn teqyqdymkd yykilqqkdp natipdqifs nsnvntdwqd aifrnagtrs
      481 yelssrggse ktqyytsvgy mkqggvllgs dfnrlsgrin lnhqhndklr fstainltra
      541 vnkrvqeens kegatksgif sppnltvyda sgnfaydqvr ltrenpvaml tlptneaqtf
      601 rvlanvgaey niipelllkt sfgtdisfid etffmppvgl rsyasqggig arrntrdqlw
      661 inettltydk vfgdhalnal agfsvqesrl efvhgqrsnf pnndipyita ggvvtgansy
      721 peewaiasgf aratyifkdk yilnanvrsd gssrfgadnr waifpsfaga wrlseeeflk
      781 dskilndlkl raswgitgnq nignyasrsl ysgnsnylgm agfipnilgd rdlkwettrq
      841 wnvgidvgfl nnrisllady yykktsdlli glpiltssgy inrftnsgdi enkgfefelt
      901 tknlvgefkw ttslnmtfnr nkvlalpegl nemrggvgdl nraivgqplg vfygwqangv
      961 npqtgmidyl gqdgsavspt dykdhrmigd pnpsffggit nnfayknfdl siqgqftygn
     1021 difnynlasg legfnpssnq fvdfvdrwra pgditdvprp apgdlsngav ssrfvedgsf
     1081 frlrnitfgy tlpptvaeki kmkklrwyvt vqnayvftky rgydpevsss hggantgliy
     1141 gydygsypqp rifttginmt f
//
LOCUS       WP_115168859            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115168859
VERSION     WP_115168859.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113546
     Region          24..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikflllml gvvwncailf aqqqtvtgkv tdddgkslqg vtvmekgksn qvitdgsgny
       61 kitvspratl iyryvgmnti eqavgnktnl nitlssssss idevvvtayg idrskkslgy
      121 stpvvsgdev setqreaffn glqgrvpgls instsgapga saqivlrgfv svsgdnsali
      181 vvdgvpidns tlnendlasg sanraldysn rgmdlnpedi esytimkgpe atalfgsqga
      241 sgailittkk akagrtavty nfsgrmetvn kfpevqniys kgtnglydgt spyslgpkyk
      301 egvqlydnir sffrtgynqk hnlsfeggne aftyrwsney ndntgitpnt rytrissrla
      361 atakfgekln intsfsytns dndkarkgad gymvtllrfn pmadvrqwid ekgnrvlhsg
      421 tiysefdnpf wdvyrntsfd kvnrmmansn imyrpskwls ingilgldys fthgesvyhn
      481 qsylgsgseg dptggqisvy drtsriltgs ltarsshkfd dfslqgvlga sfndynyvtn
      541 aqygkkffdp dfysinntlp etrlskstin nyrnvgffgq avlgyktily ltlsgrldgs
      601 srlmpnnpff gypsgsiafn fsdikgfhdm fpfvdegklr ssvsltgkep wrtyytkssf
      661 egqystgggf aygvnggnln lkvertrdfe tgiefslfkk rvsfdftyyt rlssdqiilp
      721 rlsygtgyil kmlnggevkn hgieiqtmvr pvekrdfnwd vtfnftknrg kvlslaeelp
      781 elyesdtwvl sglrtsvhpg ysigalsgtr fkrnangdvl intatglpvt gdgvyypigd
      841 ripdftlgti nkfryksisl sflwdlrvgg dvfnglenrm fnlgvsaktl nredprviqg
      901 vlqdgleesa nptinniavt pfynsnyyft nvepsmfier diytfrlrdi slayelpksl
      961 tsrigkntsm svfftgtdll lftnytgldp esnlntpgvg giggygidyg nmakprgfnl
     1021 glrlkl
//
LOCUS       WP_115168862            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115168862
VERSION     WP_115168862.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112657
     Region          24..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkllllff wlmlisvnlm aqqktisgkv tnsadgapls svtvlvkgks vttktdadgs
       61 ftiqaspgdv lifrsvgske vqqtvgasnt vsvsmsgsee aleevvvtam gikkekralg
      121 yavqdiksde lmrnknpnvi nslngkiagv nvtnsggspg asasiiirgg tslerdnqpl
      181 fvidgmpmdn stgqgdnsaf dgntnisttn gnraldlnpe diesisvlkg paaaalyglr
      241 aaagavvitt krgkegsati gvnsrfganw vnrlpelqsk ykqgsnykgn kitdntylsw
      301 gdafaqgeti ynnledfyqt atsfdnsfnv sggnangnfy lsgsnldqsg ivpttdfkrt
      361 tfrfngeqkv gvftfganas yshsttqktl tgsglwggsg mgymesilaf prnvdmknwi
      421 dpsgkqilll pnvalqdnvd npywtinknp qndktnrflg nvyanvkitd wldatyklgv
      481 dnyttnfrsi ltpgsavkea wqkgmlsenv rqynyinsnf mlnfhkefar dwdlnfllgt
      541 taedtriqan smraeqfsip nfesinnadp knrylnevit nkrllgvygd lrigyknllf
      601 lsatgrndws stlpiqnrsf fypsfsgsli ftelmekndi lsygklrasw aqvgkdappy
      661 qtntylkdiq ltigggfrne wtrgndqlkp etttsfevgt dlrlfsnklg leftyyknns
      721 kdqilqprvs natgyilsyv ntgeienkgi evsintspik kenfkwglal nfshnngvvk
      781 slpaalpily vtdvqvgngk aasfgngdfm gisgsiwqkd angnllldwn tgypltstta
      841 typignrepd figglnntft yknwelsflf dfrkggdiln steylltang mskntenrge
      901 kisftgmgln pntkqyeqit revlateeyy rdiyslntph fvekvnwlrl rslsltyslp
      961 sallnrskif kaasvtaigt nlwlltnysg mdpevsaaga gvigsgsvgv dyagvpatag
     1021 vtfglnlkf
//
LOCUS       WP_115168855            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115168855
VERSION     WP_115168855.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111501
     Region          33..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mglttikfhe llkatlivll lslgssqvfa qtrqikglvl dgqnqspiag atiklvgteq
       61 aassdqngtf tinttstsnt lsvssvgyet ktataganga qvtivltpsm qelesvvvta
      121 lginraqksl tystqqvnse elnrvkspnl intlngkvag vniapsssgp ggsakvvlrg
      181 nksasgnnqv lyvidgvpin nstlgtqpsn vfggerdpgd pialinpedi enisilkgas
      241 aaalygsqaa ngvilvttks gkqgrtvvnf sssatletpa ytpefqnkyg qgsngvastt
      301 gssswgeeis gqnydnvgkf frtgnnftns itlsggnekn qtyfsysntq aqgitpnndl
      361 srhnfnfkes anffndklkv egganyitqk lenapqtgfy fnpivglyll prsidispyk
      421 dfekfnpqrn lydqnwfsit dnettqqnpw wivnrnqnss vrnrlllsgs akytatpwls
      481 vqargsldrt sevyerkvya gtqsilsrpn grydytntti tqqyadlvan vnfdvtdkfk
      541 isgvvgtsit dwktegvdyn sgqeslkipn vftlqnsttp rpstlsamrr qlqsvfasan
      601 lsydnwlyld ltarndwsst laftgnksff ypsaglgvvl ndklnlpsfi nmakirgsfa
      661 qvgndlppyt tlltnrldpy avltlndiaf lrelkpemtn sleigtewrm wnnrlsvdvt
      721 yyktntknqf fkiaasqasf ynqyainagn iqnqgieali sldavksedf nwttsinysy
      781 nknkileldd rikdfsltge srnnyaskfe vggsfgdiyg qdfqkddqgr iivsdgipqk
      841 nsnytklgna nplwqmgwnn nfsyknlsls flidgkfdye vmsvtqavld gygvskasgd
      901 areaggvain gvtpagvpvt sidankwyts tggigpvtsn yiydgtvvrl reltlgydfn
      961 ikqgfikklk vsavgrnlfy iskkapfdpe vtmstgntls gvdifmmpat rnygltlnat
     1021 f
//
LOCUS       WP_115168865            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115168865
VERSION     WP_115168865.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110175
     Region          25..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkhllllla mlvclldvvt aqeltisglv tsqedgkpil gasikvvgta vgavtdaggk
       61 ykikaakgqt lsfsyigmla vtrvvgesst idialspdmk gldevvvtam giernkkslt
      121 ysvqtvkged lrdanqsnvl nalqgqiaga qisssggspg lpteiilrgs stltgdnqpl
      181 mivdgirvsn ssangtvnri adfnpadied isilkgaaaa alygidaasg aiiittkkgk
      241 agamqingsy kafvetmgrt prqqgiyttg tggvydessg sswgrkfryd etvynnidrf
      301 fqtalthdvn lnvnggsekl nyymsggyrn agsmvpnteq ekinfllkgt aklssklelt
      361 tsanyiknni qeglggvnsg gwinsiltyp lrydilsyqk pngeplysyi eaeddgrnam
      421 ispmwgvmrn prnndverfv vngridykva dwvrlsyqlg qdftaskyri ittpgtpgty
      481 fdgrvsesnt ntkyttsifn atfdrkfynd fratlilggt sdyfdskgvg ymgesllvrd
      541 ifspnvvere nlsltdtwsr rqryaiygdf kleyknivsv gvtgrndwss tlpknarsfy
      601 spsysgsfsy selfdhdswf gkvrvsyakv gkdapiyrtn tnlvqaqtqg ggfvtsatgg
      661 npdlrpekts efeigselsl fknrlnldlt yyerksidmi mtprvplpsg yvimtfnags
      721 lrnrgieasl sgtpikkddf twsstlnawr ntskmlefag divtfkytna qltagtaatt
      781 lndavlgivg tdykrtdegy vvvnadgypi idskekyign repefnigwm nkfrykdisl
      841 sflwdfrfgg dilnasrqrm msvgtaydig ewrdkefvfn gvvqqndgty vkneksvvmd
      901 ysyfannyyq vgtnfvekvn warvryitls yalpkmwskr lgvnnlslel saqnpfvitn
      961 ysggdpevns agpnaggsga stmgvdngai plpksysfgf nisl
//
LOCUS       WP_115168914            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115168914
VERSION     WP_115168914.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116794
     Region          24..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkllsflv gtmiltsvaf gqekkisgkv tsatgqalpg vtvvvqgttl atqtdangny
       61 tlnvpagktl vfrslgfnek tivvspsats fnvsledqdn alaevvvtan aikrekrtlg
      121 ysaptlnnee ltsgknasai nslagkvagv nitstsnspg sssrvvlrgg ssiagnnqal
      181 ividgvpidn ssviggassl ssvdfgnrgn dinpddiasm tvlkgpaaaa lygsrasnga
      241 liittksgkq gsdkteitfn stntlssilk lpdfqneygq gysyydnagn vlfendpken
      301 wswgapftge tqewgqaing vrqtkpysav knnvrdffdl gvasdnnlsl sgggekttfy
      361 lglnslnsng vypgkkdtyn rygvrfngta efsnkfyagi sanynkinsn nigggqgggs
      421 vynnllqtpr dipvsdmsdl tnpyngygqv rdadgnlred lygyygaysm npywvldnyn
      481 nfndvnrimg nvnvgykpfe wldikerigv dhysdrrrse spkftyspad nttdnysqsa
      541 nkqtevgqyr idqfnvteii hdfmvtanhk fnddfeaslm lgnnirqrqt tnnstatnas
      601 aglvmpgwyn lansngpldl iedswskrrl vgvyadlnls yknylflqat arndwsstlp
      661 kannsffyps vsgsfvfsel mspearqils ygklraniak vgndtdpyql ittfsrgein
      721 ggfgtttfpf gnvsalmsss tignallkpe ittsyevgte lgffanrlsv dfsyyknssk
      781 dqilsipipn stgygfsvin agkvensgie lslrgtpvkt adfswelmgt ftknnskvve
      841 lmegvdqvsl ggfsgmsiva akgkpygefy avtnatdaqg rtivdaetgl pvitdepqyl
      901 gsynpkfqas lgtnvnyknw slnalfdmkh ggvffsrtrd imaftgtsae tggdrfgqif
      961 pnsvylddag nsientsvky dkvdyfptre aglnvvdasy iklrslaisy kftknqlknt
     1021 pfgsasvglf gnnlfiwtps enkyadpevn sagagnaqgf dytaqpslrn yginvkvsf
//
LOCUS       WP_115169122            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115169122
VERSION     WP_115169122.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122567
     Region          51..1117
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknrlfvpg mgltfhlwik rpslnpklsy alamsmligv svaeaqtnas vsglvrdeqg
       61 akisgatiti enkltafrks sttdaegvfv fegipagegy tfvisslgys kkeltgyaik
      121 sndklaisvt lesrndvlee vvvtalgikr ekkalgytva elkgneltqg keanvanals
      181 gkvagvqvsr aasgaggssk viirgnnsli gnsqplyvvd gvpidnqnyg aagssggtdy
      241 gdgisninpe dietisvlkg pnaaalygqr gsngvilitt ktgkagrgln infnsdfsig
      301 talvlpdfqn vygqglngnf thfrktdgki vtmadaiann ysgmpkmsag rdrlmrsswg
      361 akmegqqyed qfgnvlsftp kpntygdffd tekqfvndls vdggnekiny rfsyantnik
      421 gyvptntinr nslnlrtqak itdkfsidvk anyimqegvn rptlsdasdn payllisqpr
      481 smgmdvlady kwtkhdidnq lgfsnlfegl ektyatnsst anpywtiren rntdrrdrli
      541 gllrlsyefa pwlrltatgg tdlytdqrfr yrpigtyqsl nrkgdireei irsrennlda
      601 llsssfsate dikislnaga shlsrfmrnt gntgnqfivp dlyvinnttt nsyifnlies
      661 einsvygsgq isykdyafld fsarndwsst lsknnnsffy psvsgslils diwkfnpkal
      721 sflkvraswa qagssgnpyq ltgayslnqy thggvplatf tevipdpdlk nelttsvefg
      781 adlrflnnrm nfsftyynan tknqildipi apssmfkvnr inageisnkg iefvlggtpv
      841 ktsggfqwet sfnfnrnrnm vkslapgvdv fllgsdrgin vvaevgkpfg qligtqfawi
      901 kdengnrlid pntglplrta grvttdlgna qpkwlggfsn tfrykgialy alvdirqggl
      961 ifsqsnreqi iygvsnktve grdgtyvasg ylgtlqpdnt wknsgvqntm qvraqdywnv
     1021 vagekevmvs eemlndgsyi amreislsys lpkgilppky iqgakvgvyg rnlfyfqrkt
     1081 dgfspesasf ntnnssigie stslpmmrni ginlsvnf
//
LOCUS       WP_115169251             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115169251
VERSION     WP_115169251.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111742
     Region          81..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklyvvatv fsliggcltg ivsaspgtks rskgvtgfgi tnfskglvdt tqvdsvliyd
       61 lsaakpylgk dslameaarl rpfvsvqqml kgnlsgvyiq essgepgtik qgvtvrgist
      121 pvlhatdfnk nkplivvngi pltedpaivy diqnytiqpv gsatnintvl dpdniesiyv
      181 lkdystaaiy gpraangviy ittknasage rrisvnghfg fatpsnvsti ngefeknfrk
      241 pfydryadil qqasypayls dssnvnyygp snwtdlyykt spiysvngsl vgggnrsnfr
      301 ffaghtsdag aadaakfkry qgafyinmvp lpwltissmi hatrldrdrn ksiierfget
      361 ryvpdlstpi spnkdmygly lkeydktide nfnnsiigyf alnfailknl sfspklmmdy
      421 nentrnvfwp stlmsgnnyv snyfgynerm vfdntlnyfy dvndkdrlsf aggfnyqadv
      481 qkynyaqgyr gpndfikvnv vegnsqyany lksvgfipyy ysdkiqhrla sfygklnytr
      541 kdewnvaali rndgssavqp serwflsyav nadynlnhvi ksdffdyfkv lasygrlgni
      601 pttdrdaagp qyaselgwdg nkavfsyngl gtlsrpyqsg wvgydlpwsy temlnvgldv
      661 sllknmltar idfynkdnkd aifnvpivae sgyqferksg mvvnnkgvdl tlnfnlpskn
      721 dfswnsslni synnnklkal pnglqeieig trklavgeri dhfwllqnrg ifnndldvpv
      781 npstykilty ngtdmkggdp rwvdvngdyd innkdrqlmg nifpkytggf ynqfryksfd
      841 isallyfnlk kdilnsqaas yydfanqdes naigavrdit fweknfddka yplynpwspv
      901 spyqaeqdmf ledgsflklr nltlgydmtk lmnrskdrfs kfyvyvsgsn lwtltkytgr
      961 dpelvdfygy dtglglripk tfilgvkmdl
//
LOCUS       WP_115169620            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115169620
VERSION     WP_115169620.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117753
     Region          34..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miikifelfr rsgplvltll fsayfhygva qtgvsgkvts gttplagvtv nvksnpktaa
       61 gtdmngqysi nagpsdvlvf klighnpvev svngrsridv imeessdels evvvtgytti
      121 nrkkatgsia sitskdienl paasidillq gklpgvnvqn ftgqpgvkts lvirgntkis
      181 nstegfntdd lysnplyvid gipvsddevr afnttgtnyl aslnpndies vdvlkdasaa
      241 alygsraang viliktkrgs sgkprlsvnt yhgyistpsk vgtligaaer rkkldliyqy
      301 asdtqlkngl pqmltdslnp sfnnsndyqd lfyqsgkvhn adiaisggne nlnyrvsggy
      361 ydekgvvlnt glkrysftsn ilfkinkdle lltnlrasts rrfdgkgstd fskvnnyrdi
      421 ftvspvnmps sllqltqkdl nsilnpyeyq rddnvdvsln gvgelrytfl rdfristrni
      481 isystakndf aspseinsdg lavakssysq ykkyvltnnl mwnrtfedkh afsvnliqef
      541 etrrnesmfl lgrgipsdni qvvkgvqgtn lqgntnlsty sklsflgalh ydykskylfd
      601 avwradassr fgknnkwgyf pslaggwlls eeefvkdlgw vnelklrasw grtgdessit
      661 dydrynayla gngrypgsea psyggvasvi pnyngitndd itwqesnewn lgldayllnn
      721 rinlnvdvyk rettgqmlri lfpeytgydn tftnaagvrn tgleinllgk vfsqssafqw
      781 npsinisinr nmvtqlpngn rdlyygsavy vvgmplnmyy gylvngaiss qqdiitnpyt
      841 gavgstkwgt lkpgypnwvd vngdykisdn igeddktfyg nanpkvtggl tnffsykdft
      901 lqvlttftfg rdimnrtfaq rmsngffygn pedfakasvv dlnaydfwqr egdqakypaa
      961 npymglyvwr tgqsmfmepg wyirirnisl aynfkpanhe wmqrlklnsf rlygnmdnva
     1021 lfqkfsgida ervdgqgndy gdgypipkkf tlglqfdf
//
LOCUS       WP_115169761            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115169761
VERSION     WP_115169761.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124481
     Region          51..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mriflskkhq lltmlllrfk sprtncplrl gilgvlcvss havlaqsaas vhgvvrdaan
       61 npitgatvsi enpttkykqv nttnmegifs fdripegqgy mitvsylgfk tktlsnynid
      121 akdkvaitva leqdqeslee vvvvgygkqr kanitgsvas vnaeqlknia psnlsntlag
      181 raaginvtnt sgmagasssl rirgsfaepl yvidgivrdk aafdaleane vdqmsflkda
      241 ataavygtra gngvvvvttk kgtaqepvfn vqsnynfgap tqtlladitt aadeltyqnr
      301 vsqflwengs rsqpwvapng qeefdyfkdk vysvndviwr npfshrqsis vsgggdrity
      361 ynlvsyrken gsykslnhek fnlrsnvsak itddftidvn isanqinsqr fywpfstssn
      421 dddfdvsdfy rvtfnwpkmy pfylnkdgsp sntateypvq tpmgswqawn vidqvvgnry
      481 idrkvrqvnp imtlnykldk lveglstkvv gsylaedymr krfmtfqkny tftslnpdgn
      541 rfipappsed kvniftfsqa qpfmdyapqr eweyqvnwfl nynrrfnkha idalvvyeqf
      601 kaggtyvtsr aenpivsidq mfiyptdrtf rstdayesin srrgfigran ynyadkyiae
      661 fsfrydgspl fpgdkrwgff psmsaawris eeqffsgikn tfsdlklras ygttgndlnv
      721 naerigqfly qekyrpaggy mfgdryyngi aygatptqnl twttsksini gvdfglinnk
      781 ltgvldvfsr ketnilgprs lkvpdnygre lapenyaars ykggefslnw ndrlgevsyg
      841 ltanigyakd rwdiydeepa favggtrnfe srvgrpenri vgleaidlvr tqaqldalkn
      901 qgfktygrdp ylgmilykdi rganysdtpd gkiddndmml lsddntprin ygfglnaswk
      961 gltvsallqg vmaydrvisn qegggirqhg gtfrpyypiw agdvwtaenp daayprvvgs
     1021 nwqesgtgvs sfwirngayl rlrdlnisys lpqsvtnamk iknvsvffng tnlfvfspmt
     1081 efhdpeqkmy dsypvmktfa lgldvkf
//
LOCUS       WP_115169866            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115169866
VERSION     WP_115169866.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120901
     Region          26..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqfyqtcct iillsilsit gvfaqqtvtg kvtnangnlp gvnvaikgts rgtqsgsdgn
       61 ysiqaapgek lrfsmvgyis qeisvgstkt invtlqpdes tldevvvtam gikrdqrklg
      121 yavstvkaed iqegspsiga slygkapgvr iqtspggqia asgitirgqn sisfarqpli
      181 ildgipirng eantqgmwde srimgnglld vnpndiesis ilkgapasal ygseavggvl
      241 vittkkgsqk tglgidfnmn mqserlaflp efqhefgpgy gwtgpngllt agadadgffk
      301 ttgrdgksyi rpsmgswgny gpkfdnrdvm wwdgeirqys aqpngmkdly dkgntnnysl
      361 svsnsgdlgs frfsynrndf kgispgtkqn rnnfnfngtl nvskkitfdl ttsyintytl
      421 nrpylinnvn aygynlaeka dvvrskykts kgyqftnnkt wdpeeyilyg tsatqymqni
      481 lwnnlvnkdm lrenrfitsa tlnykpidpl sfrirlgndi tsnnnetenp ntqnvsfans
      541 gyygtrngnq rvtygdflgs ynksfndfev gislgamlkq eknqytsiat agglvqenff
      601 slnnsldrvs tgfgrgkvtr tgifgiatlg yknqlfgels vrressstlp pannsftyss
      661 mslswiises lanrpdwlny tklrtaygfv gndlsayaan naykqeting vivnfwptvy
      721 gndyirperk refevglesk lfdnrigldi tyynnaikdq ityidvpgss gvtsmlsnla
      781 kmtnygleig lnanpvrtet wnynvgvnfs fnrnriselp tggqylklad idnnavmvva
      841 spnaaygdim tysykrdqng nklvddegyy ikentpsvrg nvtpkgvggi tnnvsfdtgh
      901 gkiaftalid yriggdifsl snyqntasgk lastlqgrda arggisyyva adgtnkaiqq
      961 gtpvpgdarf ggrifddgii adgyredgtk nntimlasyy ylfnnywnsg iydnqiydns
     1021 yvklremtls ytlparlaar lkarnvtlsl igrnlfyiyk nvpnidpesa igttpremgl
     1081 drygiptsrs ygfslkfgi
//
LOCUS       WP_115169869            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115169869
VERSION     WP_115169869.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121201
     Region          15..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mllsilsits vfaqqtvtgk vtdasgnvpg vsvsvkgtsr gtqtaadgsy siqaaqgetl
       61 rfsmigytsq eivvgstkti nvtlkadega leevvitamg ikrapkelgy amstvdskel
      121 tktgspnfag alygkapgvr isaapggats gininirgtn sitgnsqplv iidgvpmrqt
      181 tfnnsdywgd qrargngled lnpediesis vlkgasaaal ygseamngvv lvttksgkgg
      241 kgfaidfnat ythdqiaylp rfqdvrgpgy ttayqndgqa ddmfyyypns saingvnrgl
      301 laatvnfgpk fdgkdviswd gqvrpyvaqn aynklfnnpn ntifnlalsn ttensntrfs
      361 vtrqdnqmts ldsynkknia nlnstiklwd klttdvvvny vnqhthnrpf ltdrlinnft
      421 gmistfdnpe wylnkyqtsl gykyvvqsad aqsltpdeni ryngyktdvl dyiwntkakq
      481 ydeysnrvig svtntyqits dlsvrarfsa dmtslktedk epnavplqfn nsgyfglgnq
      541 naniyytdll atynkqinkd iklgvmagyt atksqdtyvq retagglsvr nwydinasvn
      601 tiggntryny rrnmlrdavf gtlnfnlkef wfvegtlrre ristmhpdnn vlyypsvnss
      661 lilseafqlp eifnyaklrg swgivgnypd iyksalsytq qslgvqipng asviynnvpt
      721 tgfgnenikp erkkeiefgl etrllnnrlg fdityyngli qdqildytlp ismgassiia
      781 nvgtlrnkgw efaitgtpiq henfkwntvl nfsmnknvve elpggvqell hrdydgaaaq
      841 lvskvgqpmg dimvhpiktd angnkivqen giyqldadkw ikagnampka vgglintfty
      901 knftldalid frwgghampt ginwmtsrgl teesltamda engglsyyrv gtqgiatnaa
      961 tgpngekvyh dgmlmdgvla dgsrnnniis qatyynqtyn wggpqysnsr yelyvqknny
     1021 ikmreislgy ripahlaskl raknvqisaf grnlfflyrs ikdldpeqmt ggsnwvnnvs
     1081 nagtspatrt iglmlrasf
//
LOCUS       WP_115169875            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115169875
VERSION     WP_115169875.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121744
     Region          27..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiytscci ivlvfitisn lyaqqyvngk vttatgnlag atvtvrgtsr atqsqedgsy
       61 siqaekgqtl rfsivgyvpq eiqignnkti nvvlkadegs leevvvtgft erkrsqigsa
      121 vttisgedir rtgsinpita lqglvpglqv qpgiggpqst plfrirgsas ldpynnqpli
      181 vidniimddn mvlpnrgndq dfgnllkdln pddienitvl rggavtalyg sraqsgvili
      241 ttksgfsrrg lgvsvtqntq wdqayktldf qnefgpgtts sdldfikkpd gqiqvanpgy
      301 nygprftgqk vmdydgreii ysanpknvle ayriapstnt svsltggsdq gsfrlsysnn
      361 sskgvtpnnn fkrnsinfrg tqrllgkviv danvsyvksq arnaadvggg namlsgntsa
      421 gsvlvnfagg ipryydtkyw idnymqplgg wnradrtgft svlynlyenn riadddnfrg
      481 vidvqvpftd ylkfqgfvnm nylgnnfenr trgrdsaftn pgyststvnr ftsqyrgsln
      541 ftkkikdfni fligggeyys ftskgqaani ngaiypdiyr lsnsrnaitv teekprkrnl
      601 gslfyqasfd yrnditlnfy grndwnsslv yndghgtysy fypgadviwk fnetfknkls
      661 sifdygairl syveagngtg aytantgayg anpnyldylg nqvinygfss ntlpnqalip
      721 ertakyeagl evrmlknrlr adfayysqds knqiisfptp spsgvtaall nggtvrnrgi
      781 elsvsgvpvk tenfswdtrf nytrnrntvi slpfgleyts lgggdgyqav akvggeygtv
      841 iapyayaryq svdgngnpvd splngkkvll lsgtttlyer aanykegldk apvlgsilpk
      901 flgnwrntfn yktvqlvval dakfgglays atkdfgswlg tlkstlpgrs pefggiaytt
      961 aagvartdgv iydgiykqgs tvniggkvid vsgmthqevv dagylrpisa aayyanshsw
     1021 frgirersmy tsswvsvqqv slnydlpstf akklkmnglr vgvygndlff lynsapdnfn
     1081 pynlndsgsg amnegsampy vrrfgfnina sf
//
LOCUS       WP_115170099            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115170099
VERSION     WP_115170099.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118065
     Region          25..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksiyiilcf vctfcssvaf aqnvtvrgiv knsangetls dvsilietpr raigtsgrdg
       61 sfavtvpans tllftfqgtq vrqkieagrt vyninmaike nvinevevtv gyqarkktsf
      121 tgsavvisgk eiqdqpaanf tdllqgkvag lnvqlnngtp gvrgsmairg isninvqgsg
      181 dnafltptsp lfvidgipie dnanyeygfq sagpgispia miptediedi tvlkdaqata
      241 lygskgaygv ilvttkrgrs kvpivsyesk lfinavpglr nviggkgery lrlqqilgyd
      301 stynsalqhi ndspmladsl nafynnstdw qsyfyrptvn nsqnvnisgg dqafnykvnt
      361 gyydengiik ntgftryslq mnmqympssk frlmaylnss laknstgsgn alqqsgvgss
      421 antssllpsp slftgssdal aalnvlndsk tgnlssqvei qyepipgvra sstlnynylr
      481 gtqdrftqga lnadksevys yndrtntlyn rnllaynktf aekhnlsvyg faefevvnkr
      541 gdemsitgtp ndqitvglgy dtrnqkggtl ykitqekrtv gyagsfsyny dekyyidfty
      601 rvdgtsttgg lnpwtylptg glrwnfsnek faenwdwlsl gsirgtwgkn iipvgtiydv
      661 ygkyfqdgrt ynnqptvsid lgaipnvnlq pqtkttlnla tdwaffnnnl tftyeyyysq
      721 sdkmlrkkli stenafeavn snetsvvnrg hefqfnyrpl nnktwslsfn gnfainqdit
      781 aalpdgvrql likdesnyyq dilyqlgtnt lsnvlfhyrg vyrtdddvpv dprtgmkyrt
      841 ggifgadref ragdpiwtdl ngdyildekd lvvvgnsqpk vtggfgafik ykqfslqtnf
      901 vftikrdiln naladrfrsy snprglvtyd sngkpimpga lvplsqyniw trpgddayyp
      961 npfdfirnel ndfyrynqtl fqedgsylkf nsatfsynfd rewtrrmgis garvyfsgnn
     1021 iytfskysgp dpelvsdlgr dsskgyprar nytlglsvqf
//
LOCUS       WP_115170103             970 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115170103
VERSION     WP_115170103.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 970)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..970
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110123
     Region          75..968
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkrfycfli lvfpvsflqa adfpegytan tnryllqdtv stdtlllqrl nptavklgta
       61 dsvhiqtvst fpfhsvaqyl kgevagvyvq entaepgtnr nivlrglaap lfsnkdinas
      121 qptifvngvp ltqennfsyg iqkydynrlg pgtdfasifn inaiesievi kdpaklaalg
      181 plaangaiwi ttkggksgps eislnsyygm ntrksvtpvn aqyenmfrqq fyskygteqd
      241 rltypsylgd stnvnyygps nwseeyyknq plysidlslr ggsdranfnf lgghtsniss
      301 adaanfkryn atfnvnmapa ewfnftayvn asrverkrnr slrdrisetg ylpdlsipms
      361 pnrdvytryl kefdknvdgn vmnavqafis adfsilsnlr yttkfsidyn eglrdvfyas
      421 slmddnnyvs nyngynqryk fdhalnynlg kdtdhqldlt agmeymedly rftytktydg
      481 pndfiklnlk estlptyryt nredlrvysf ygnakykfkn lldlnavlry dgsstvqkdn
      541 rwlftpavsa kwnvknqfft tndgindlsi kagwgrigkl ltisrfatgp qyatdlnwst
      601 eaglvsyngf aaisrpytlg wvgydvewpy tdhfnidleg sffsnrlsag islynkndkn
      661 qiasipvpae ygytgrymng lnvnnkgvdv alglnlltnp dklqwsssfn fninkntlka
      721 lpnnlqtliv gdrklevgks vdqfwiyqna giynaeseip vnpntgrkmm fqgvemnagd
      781 akwidqngdy dvneddkila gnampkfvgg wsnqfryknf dlgfqwyfal ghkalnqrvs
      841 nrydfinnes nntinsvkei fhwqqdfdit kypiynpwss svpyrvdqdl flenasflkl
      901 rsvsvgyeia glkekvkrlr kayvyvtgtn lltitkftgv dpelidfngy ysgyglplsp
      961 tftlgfkldl
//
LOCUS       WP_115170150            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115170150
VERSION     WP_115170150.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125291
     Region          124..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktnyylkl mgsllflqlc vqktiaaenq qnreigpvis kiekklnirf gydtgighlk
       61 ikddtdlknl kkdnlnafim eisydqlqvs qvdnmlfvls rkheqkqkgt ntgfqkitvh
      121 adqkilkgei idqetkakia gvtvrvkgtd kvtttdnngv fsieevapga ilvvsslgyr
      181 tveipadqaa qieltrssee lqevvvtalg ikrekralgy avqeikgddl qkvkgvdvgt
      241 tltgrisglr vfnstefnkm psitlrgmdp ilvidgvlye nmnlrdipvd nieninvlkg
      301 atatalyger gaggaimvtt kkglkskgte isvstnnmff sgylalpsvq ssysagyggk
      361 fntddevwgd kldigrryqq wnpitkqlee selvskgknn fknflepgfi snnsvsftnq
      421 gengsittsi shvynkgqyp ntklnmtnis vsgetkitek lnlesrfgyn rrntpndfga
      481 gynaqgyiyn ilvwtgpeyd lsqykdywiv knekqnwnyn awydnpylsa yekisaelin
      541 klnaaitlny qvtdwgklvl rsgydyygnt qeqtnpmgiy gtrggfsgyd nrgkywtrkq
      601 dgfstnndli ftakktfgdf gidgllggav fyrrnntlta stvnglaipg fyslrnsvgp
      661 vssveskike mtnsvygrls lswrnlifle atgrndwsst lpkenrsyfy pslsgsvvvs
      721 dlfekpqwln llkvrgsqav tkqildpyei nqaftvtanv wdglstgsyp nsikdfsisp
      781 tqrdltevgl dfsvlnnrly gdytryyrre hnaitsatis gatgftsrli ntkeetmtkg
      841 heitiggtpv kkehfqwdis gnlsqnlkyy hkldpdysad alyvkvgert dhyvtrdwer
      901 spdgqivhna sgmpisavhe srlfgytapk wiwgltnnfr yhdfalsfsl dgrikglsys
      961 smnarlwqtg ahpdsdsper yeevvngnkt yigqgvkivs gnvtydkygq ivtdtrqfaa
     1021 ndktvsyesy wkraysgtrn iwdetfiklr eislsyylpa evaakfkakr asvgvtgqnl
     1081 flwtkeyrfs dpdvgsedln spsmryigfn invsf
//
LOCUS       WP_115170190            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115170190
VERSION     WP_115170190.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118685
     Region          46..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkefyisnlk kalflllfcf gafqdgiaer isanavpvka veqelfdikg vvkdavngnp
       61 vegvtilagn ksigktdeng kfsfsvlkgt qvsfrgigyt thnqtinken nnltislqpn
      121 etalsevvvt algikrdeka lgysatvvkg eqftdalsnn wtdalsgkva gvnlmrsnsg
      181 ptgstkiilr gesnlngdpg aliivdgivv sngsgrktai ggesaygtaa dnmpadygsg
      241 iddinpedie nvtvlkgpga aalygargas gaiiittksg skgkkgigvt vnsntafesv
      301 nrwpdmqyey gqgldgsdyy sygttadgts tsgtssaygp kfdgqmffqy dpltnttgke
      361 rtpwipyknq irdifevgrt ytnsvsidgg tdrttarfsa tnvnnswilp ntgfkrntva
      421 lsvnskvsdk ltisskinyt nkwsdnlpga gygnqslmyw fifwqpnadl nwlkdywrpg
      481 eeglkirypf ssypenpyai snefinrsnr qgvtgnvqas yqfnkewslq lrsaidfaye
      541 draqerpfda gskltqgsfr tqsifsnent idfllkydkk inkdwnvsat fggsrmqnky
      601 kkeelradsl tfpgvytfan akgpldarpy sskfevnsly alltasykdy lffdvtgrqd
      661 wsstlasvdm pdknlgffyp svnlsfiase yftlpkqiny akfrasiagv gsggtdpylt
      721 gysyetagsl ysgglqmptt lgngglkplk tnsyevgadl rffksrlgid valyksetkd
      781 qhllryvdps tgyrryvina gavsnrglei glngkpvqnk egfnwnmfat ftrntnridn
      841 lpdssiviqt gpvaggqlva kvggsmgdly gygykrspdg qvmydantgy allsdeiiyl
      901 gntipkgras igsdfsykgf klsvlfdaqf ggvshslshy klaeqgkttn tlpgryngii
      961 gngviqnpdg tyrkndviak nideyyrshy gqdnaegsvf stdfikfrea rfdytlnkdl
     1021 tkrlkiqrat vgvygrnlfi wsdwpifdpe fgtlsgtdiv kgfevaqfps trtfgfnivv
     1081 gf
//
LOCUS       WP_115170245            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115170245
VERSION     WP_115170245.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112764
     Region          27..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkkyfsill liwvsvyate ssaqthitle grildqksde pisgvsvsvk enprsgsvit
       61 gsqgsfrira hrgqtlvish igyiateavv ntsqsdlifr ltedphvlse vlvtgalgik
      121 rqsrelgtsa qsvsneelnl gkvvnpllal sskvaglrvn atdlttgktd pgiqirlrgt
      181 rslnrskndp lyvvdgvplp ditrinpndi qditvlkgan aaalygsegv ngaimittks
      241 grsergqinf snsttfsnvf llppaqtvfg qgqngvyspv aneswgdkfn getrdfglpi
      301 ngvqptkvys apskdnrlgf fdtgitaqnd lsfsggdekg ayfvslqdvr ikgvipgdks
      361 srtgarfngs rrfnklntsf nmnyvffknn ttsdgpwlsv ytqpanidyk earnwedpas
      421 pnhplnwynp vastrnpifm adnnrnmydq htlnsklefn yeftdwfdat yrtglyfqse
      481 pgrvtnrklv snvatrning svndthrgft rfnndlilnf hkkfgdfstk llvgqnvrmd
      541 dsklinvsaa nllfedifnq gsrtgeltgg stitkyrsla tygeftagyr nylfltltgr
      601 ndqvsvldpn nnsyfspgis ssfvftdaie slknssilsy griytsynkt gnvtldpyrl
      661 nltysqtggf pfgslvgftp slsepnllik pefvksfevg tqlaffndrl rtdiayaysd
      721 sdgqifnagi ssatgfnsti vnagqiinkt levmingtai knrdvrlefg vnfsytdtka
      781 knlyagnefn ifrqayaikg eqyptlrmtd flkengkivl dkdgnvipsk dekilgtmvp
      841 pylfgfntkf syksltvgfq idsrlgswmy sevvprmyaa gthpetvkyd rqpfimpnsm
      901 vrladgsive ntnvyskgdk awwtaygniq tttaakgdyl klrelyigyd lpekwltgqk
      961 likkasigfv gnnlfiirhs sntigdpeal ynqtdgynsf rqipsarsmg fnvnmtf
//
LOCUS       WP_115170725             628 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115170725
VERSION     WP_115170725.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..628
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=71107
     Region          <18..627
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maakdlygnw hadsdipiaq sgvntsknln lvsqtsftvt pvkhmditsd fnfkwdfggs
       61 taiqnlikty radnslmprd pnssyfaign ssnfyftpni yvnydfvdfl pkdhhvkvlm
      121 gyqqeynryd ysyakrnnli tdaipalnta igsqqvdqna yewatqslfa rlnydyqeky
      181 llelngrrsg ssrfangakw gnfygaslgw nmakedffkn aineklisll klrlsygglg
      241 nqnvgdnayp ylatmgfspt gqwlfdnvqq aqigapgatp skftwerpvt knialdvmal
      301 knrlsltiea fdrttydmlg pqnqlpllvg vgaprvnnat lstkgfelsv dwndkigddf
      361 synvrfllad nqskilkyyn ptgtlassyn egrkvgeiwg ytsvglfkda aqvtdwlskn
      421 dqsfisgepw ypgdvmykdl ngdgkvnngk ntvsdhgdls vignsnpryq fsfnlgatwk
      481 nfsvstfwqg iakrdlpisg pyfygtfvdv fesaafkehm dywtptntta yyprpsfdks
      541 wrndliqtry lqngaylrlk nvtlnyslpt sflkkihvnk lnlfvtgenl ftytklskif
      601 dpevtawynw gevyplskvy smgvninf
//
LOCUS       WP_115170787            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115170787
VERSION     WP_115170787.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119833
     Region          55..107
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          111..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrfrfiiwmk ltlimmliac lhvsagvysq qkvtldvnkt klskvlkiie qnsdyyfvyn
       61 stnqllnkei slsvketkvv dvldrlfkrs dlqysvsgdg lvvitprqql kvrgivtdaq
      121 gvalsgatvr lkgtaigkat dlngrfeldv nsgsvllisf agylsqevtv qnnneikval
      181 qednqllnev vvtalgvtre krtlgysvtq ingetltqar ennianslvg kvagldvsat
      241 sggvgsatsv virgasslsq tnqplyving vpmenapvgf gntnpngnkg sqwdnapdmg
      301 daignlnpdd iesisvlkga aasalygsra kagvilittk sgkgsgidfs snyvveqvmd
      361 rtdwqyvygq gtngekpvsa aaaaqvggss wgakldgssv pqfdgvsrpy vaqqnniknf
      421 ykdghtwtns lalnksfdgg alrfsvsdvs nksimpnsgl drqsfnltgt fepvkrlaid
      481 aranyiieka knrpmlsdga gsanynavfl ptsldirdlk pwktdkgaei pyntgntwdt
      541 npwfaayeiq nntdrnrlis sisarytfdn glfiqgragq dfytnsylsv lppglayvpp
      601 nnlvsqkmrf sdinadvlvg ksfkvnddis ltpnvgasyr ntktdltinq gsgvlvpgvy
      661 niaglknksv ayaeteqetq svygtmefay rdilyltgsa rsdwfstlaa pgkdnklnvv
      721 ypsisgsfvf teflnssain fgklragyav vgqatrpyqt altyrvmses lngaslgqin
      781 nleipnsglk askaseleig tdlrffnnrl nvdltwykkr sddeitavtt sstvgydgai
      841 lnsgsienkg vealitgvii kkedfnwtss inmtynkntv isladgvpeq liatsrsgvg
      901 flknipgkal gqivaydyky dangeivrla dgspdrgelk dygsaynkwf agwnndftyk
      961 rfnfgflidg kfggklfsgt dylgyikglh ketlenretl gntapkfyen tanntsfrfv
     1021 ndasfikfrq ltfgysfpak mfnnkinsln vslvarnlfi lmkktdnidp essynatfpg
     1081 lelggmppar tfgvnlnvkf
//
LOCUS       WP_115170898            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115170898
VERSION     WP_115170898.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117576
     Region          26..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkihhfli livgillpsy lhaqnitvsg kvtdeqnqpl sgvtiteiag thttqtdqng
       61 afslqissae aklritfvgy esqtqtvksg qqlaislkse ntqltevvvt algisrekka
      121 lgyavqevks telqtrptna lsaisgkvag lqvvssggni ggstrvllrg insiagnnqp
      181 lyvvdgtpmd nsdlnssati ngsagkdvgn miqdlnpddi enisvlkgps aaalygsraa
      241 ngvilittkr aakgervdis lntglefeni vrlpkrqkly gqgyattfpt atingteyki
      301 vdyasdeswg prldgtpvlq wyslnpedea nylkptpwsy pkndvnyffk tgvsntnnls
      361 iagtsgstny rfsytnknvs gtipnssldr ntlnfsggtq lgnlkitstl nyiknssvgk
      421 pwsgasnrni mleafqwgav qvdykileny kradgtplaw nrtgwqntpa aeatrfidnp
      481 ywsayesyme esrdrfygnf glqydvnnwl tvgakvhgdi ysfnyqdria vysrsasqye
      541 essnklneyn yeflatakkn wdkfslvani ganlrdqqrk vdyaitqggl ivpeyynlkn
      601 assvkvdnnr fhkrvsslyg sfslgyndll yidgtvrndw sstlpvddns fiypsftgsf
      661 ifsqlegvkn ldwlsfgklr lgwaqvgndt dpyqlykvyg vdlsfdglps tslqnqlnnp
      721 llkpeittsw etglnlqflk nrvgidvtyy nnssrnqiip lpvspafgye ykiinagkin
      781 nkgieitlng tpvksenlew nstlnwsrnr nkviklsdda ntytlsnslv slvaregqqy
      841 gqllgydfvk tedgrrvvqa dgtymrtsql vplgsvlpdy ifgfqnqfry knlslgflid
      901 grvggsffsq tykvgmyagi ldrtaennir etgvvldgvk gnvvfnpdgs ytvsnisend
      961 tritaqqwar neyngpttfs ifdgtfiklr evtvgytfkl knntffknlg vsvygrnlwn
     1021 iytkskyidp eftnsggnvq gieggniptp vtygfnvnlk f
//
LOCUS       WP_115171012            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115171012
VERSION     WP_115171012.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116602
     Region          34..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfrpnsalk kslwllcvmc visiksfgqt kvtkgkivds rtqeaivgas irnlsngrit
       61 ssgssgsfsi pttgndtlqi afigylsakv eassqqdllv slsanqeslg evvvtalgik
      121 kekqaigysv qevkgqdmvk arepnaianl agrvsgltit astnlfgdpg itlrgrsnvl
      181 ivvdgmpvnt dswnlspddi esysvlkgan aaalygsrgq ngaivittkr aksndrgfqv
      241 efnsstqvqt gynaipkiqt eygpgsnyey afkdgrgggv ndndyniwgp rfegqpitqy
      301 nspvdpvtge liplpwtarg knnltnflqn gilstnnlal stkgengdir isvsqmyqkg
      361 ttpntklggt nvsisggina geklrfdasi nynkqyspny pnlsygphnp iyiltlwgga
      421 dydindlkny wqpgkeqvqq ynreytiydn pwmtayenlr tydkddiygh ltmnyklsnk
      481 lsagartsvs twnrnrtiki pisanlygyd iggsrvggyh etydtfwenn tevslkyqdr
      541 lhediglnas vfgnlrtvgv kslfartdrg ltvpgvydls nsvmptiakn drasrqvasv
      601 ygfadidykn mlylsltgrv dksstmplkn ntyfypsasl savvsemvdl pavfsslkvr
      661 gayadvasdf vnendqyniy kllpfysnyg rwansytgvt ytdvlpnpdl vaervrtfel
      721 glearffngr lgldaavfrn legpriiels tsissgvrar qtngltllrk glevsitgtp
      781 vkkehfswdl ilnastnhaw lhnidgvqtr ygnirvgerw dsyyvrdfqk dnqgnlivgt
      841 nglpaynpyl skigysdnnf alslnnsfry ktiglsflvd grfgglinnv qdakqwgsgt
      901 hpesaneyry kdwqnrdvdn ykgsvmtngq kivsgqlstd qdgnvisdsr ifapndipvl
      961 wqswatnyyq sgpvaakdrt fvklrevvls ynlpasflqr skffrsasvs lvgrnllyft
     1021 gkgtknmdld qftsassdyq tpsvksfgln inatf
//
LOCUS       WP_115170811            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115170811
VERSION     WP_115170811.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114569
     Region          46..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkmhmhal lilglsfqlq hpldsfakes aaikssppvl svyqttlrgk vvnekgegia
       61 gvtiknlsan htvqssadgt fsiqgkvsdk laftyvgyda lqytvsdtgp mtitlsnssv
      121 vledititgy tsyskklssn vattiqakai eqvpmasldq vlqgrvpgms vlassgqpga
      181 nasviirgvg singvttply vvdgipisas elknynsndf envtvlrdas akslygsrgs
      241 ngvivittkk gkagglsvny tsqygfsklt rpkfqmmnse qrlrfeeevg lemdddigpg
      301 wkyssknpan anwtpaeaan agrildslrg lnvdwrdyff qtgkfmeqqa slsggnenvr
      361 ffnsvgyykq dgvavrsgle rytlrsnvdf nmnkfsggvn vtigysnssf tegvgesrvg
      421 ssmasvfyal pyeypyapdg tlihfgnedd ynildqregs aglerllnss skselfstni
      481 gmnlayqitp qlrahtrlgi dykntvtqdy inpdsyygsr nraptiggkg lfgegyartt
      541 slistsglty qntfadehnv efsgyfeyly dryrafgyqg ygidgrqpet pagvnvsavf
      601 lpginggrtr saltsflgag rysyankysl tasyrydgst kvarenrwhg fyslganwnv
      661 kgedflqgst liqglniras ygttasqfas dflylatylt disyggetai rpatagnpqf
      721 dweyvdefna gfdlelfpkk rlrisadyyn kltrnmfidq ppsltsgfdi lslssgkmrn
      781 rgvefsvqgd iinkddfgft lgvngaynkn kilfisdvtd emldgdtril kvgmsygtyy
      841 apewagvnpd tgepqyynrd gsitttydes sqsvtksgtl ypsfiggftt glrwkdltld
      901 alfsfvtnvq rwnnedfyne nadymtsnqs irmlenrwkk agdqailqri diprqytskd
      961 iqdasflrlr nvnlsynlpq salskigfvk gvriffqgqn lltwtswrgl dpenseargr
     1021 fqypaprtyt aglnvkf
//
LOCUS       WP_115171104            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115171104
VERSION     WP_115171104.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110494
     Region          23..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksalllls tflllaqaia qqitvsgkvt sggtpvagvs vsvkntkeat ltdqqgdysv
       61 kakqgdvlif shigyvrqeq tvgtstnisv qlqsdavgld evivtgtsqg ttrkqlgsyv
      121 ssvkgddlnk apsgnvlasl qgktagaqis qnsgdpaggi svrlrgissv nssseplyii
      181 dgvivsnntt rvtntsanyd ggdfvgsigq nrmvdinpad ierievlnga aaaaiygsra
      241 nagviqiftk rgasgapqin fgtsltlghl rkqvevnesp vkfggspnvf tqdviatplq
      301 ttttpvqryn yqdyifrsst gtdntlsisg gndntkyyts agyfsnqgii rntnfrrynf
      361 rtnldqklnd wakfsaglny vkssanekpd gnsffspmns vtiignfhdi fardengnlm
      421 avgergrvnp vsviedikqr qetdriiana nlkltpvknl tldftmgvdn saqngttyip
      481 pfaynvntdf fgggagldgt vngyastann nafqfnneln atyeakisdi lssttqvgys
      541 yqyerskyal isgrglapli etvnaastpl pgvdgrtels vsggyiqqnf kyrdhlfvtg
      601 alridqssvf gkdfrtqkyl kgsvsyvlss teywkklgvs swwdtfkirg aygesgnltg
      661 igayarfnay etqsflgras lfssatlane nvkperqrel elgtdlsffk nrlglqfnwy
      721 nkkvddlllr sviapsvgfs nlldnigslr nkgievvlng tpvkgekwnw ntsfiysrnr
      781 nealdvgglr lfptnsgapv siingqpigv fygtffarnp dgslltnaag ipmiergiqn
      841 sattftpqrd angmptgttl rkvlgnpnpd ytfsfvndis ykklslhvql davrggdvwn
      901 adwrtrqgvg ngkvaeqeqk gelprgyvsg vyaieewrid ngsfvklrev slsynvgrvk
      961 yikdltinvs grnliswdny kgydpelnag gqstilrnid fgavpiprtf siglltkf
//
LOCUS       WP_115171352            1152 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115171352
VERSION     WP_115171352.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1152)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1152)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1152)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1152
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1152
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129476
     Region          68..133
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          145..1151
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkinqlpkgl ghrkdcsylv pamertrhyi yqhrivimkl klfvlfacia igqskatvfa
       61 qkftlherkv plkvvfdkie kssnyvffyd rkeleeigri nvnaigmpld qllsilakdn
      121 gftfrivknn iaikksdkpr rqetipisgi vrdstgiiqg vsvqvknkpt iatstdvngr
      181 filmvptdav ltismigykr qeiqinkqta fdiflekdda qldevvvigf gtqkkqslvs
      241 svatvkgeel kgsnrslsns lagklpglia vqrsgepgyd nsefwirgts sfsggtspli
      301 lvdgiprtmn diepdeietf tllkdaaata vygaegangv vlitskrgia qkttiayrge
      361 yttlrptrip kfassadyls iyneglmneg ksamfsdeli akyrsgedpd lypnsqwwdl
      421 lmkentnntr htlsfrgggd rmkffvsgay fgesglykvs ndynnnagik rynlrsnidl
      481 dvtkttslrv dlsgqylqgn ypynsatnif erfsrippyl fpakysdgtl aghpaqdank
      541 vnpynqlmey gyrkewrsfi qsrvdlnqkl dflteglkvr gtisydsegf fnmsrykapk
      601 tfyatgrddt gklifkqisn ettigepqet ssglkkiyme aainydrlfg nkhqvngmll
      661 tyqkeqqsns dalavrkqay igrgvytfdn ryaieanfgi tgsekfaegy rygffpavgi
      721 aynisnepff gnelkkvinn lkvrasvgkt gnddtggarf lyrptfsdaa dngyswgigs
      781 tgtlnkingi vegrfaspsl sweieikrny gidlgffnns itlqvdyfdn rrsnilmqrr
      841 tisgvagfrq apfqnfgvvt nkgieggmni nhtfgefkig algnftfarn kiiemdeipq
      901 lhpwmnttgt rinalngmwi sdglyrendf nvtlgtdgkk qytlkdgipt attmpsplpg
      961 dlkfkdlngd givnefdrsq dvanpivpei iygfglnlqy kgiyasvffq gannvstnln
     1021 nqgnaflpfq wgltesnvrq eilesrwteq npsdnvffpr vrvenlgntn tattwwvrda
     1081 sflrlknvei gytlpkslie rlkfrntrly imgqnlyvwd kvkmydpelg nsaagtkypl
     1141 prtwtfglei tl
//
LOCUS       WP_115171749            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium spiritivorum].
ACCESSION   WP_115171749
VERSION     WP_115171749.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium spiritivorum
  ORGANISM  Sphingobacterium spiritivorum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Sphingobacterium spiritivorum"
                     /db_xref="taxon:258"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124091
     Region          22..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrillfllf scaqllyaqd vitikgrvld assqnpisgv tillgssavs edtgvpgqiq
       61 qsalgtltds ngafelkvpk ntafitvsfv gyesqnvkvn ggektiylrt enqsleeviv
      121 tgytdiskrk nttaynklkv aeirqagvss idqllegkva glqlsnlngg pnsapqirir
      181 gtvslngtqd plwvidglpi egtalpnsfd kdnlnnltnl piaginpddi editvlkdaa
      241 atsiygaraa ngvivittkk gkkgpaqvqi sansfvsqrp dynklnlmss sekvdfelam
      301 anradldyra drgavarila tgneldafrk ggfsalssas qqaintlrnq qtnwgdelfr
      361 nainqqytas vsggtdahty yisggfydek attkgvdmrr ysltfsnnfn insklkggls
      421 llgsatdrhn liqdadgfsn pskyartanp ylqvrdaqgn yvydrdiegf ekntyipfnv
      481 ieerentsys lanksmkaia nleyqiipsl svrtelglqf eevgterfgd kesyftrkfr
      541 entryydsqt kqykyflpdg giienssksd fqynwksfvq ynktfnsrhe ldvmagtelr
      601 rskntlistk gfgfnpvtlt tqnivfpnsn yqnnglyrqy akaigetaya sfyanasytl
      661 drkynvygsi rydgsnmfgv dpkyrflpiw slsgswnase edfikdieai smlkirgsyg
      721 iqgnidrnty pfivgnysna tllpgnnept ivvtapandk lrwertaswn agfdlglwkn
      781 rlvvtvdyyn rdskdlignn dlslengfdl vqrnwasvkn dgielsissk nisrehftws
      841 tdfniahnrn kltrvvanpk aympdgragf pinsmfvlet agldkdgvpq fygdngqvvs
      901 fedfyklydp wadflpgynv atnmtaskyq skfkykgsld pefiggmtnr fryhdfdlav
      961 saifninklv rrtptynpss ldrganntre mlavvkgesi lpalgssnie lndrwmaysw
     1021 mmdndpinsf qfldiwskkm syarinsirl gytlpqsvsr kirssnlrvs vegrnlfvfg
     1081 sdytgffdpe tygnnyaqpi sksiafglsa sf
//
LOCUS       WP_115172258             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_115172258
VERSION     WP_115172258.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109110
     Region          30..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkltksila vvlsssfvmi saqkmdttka keiegvvvta lgikrdqkai gyaaqeikgd
       61 litasrqtsa vgalsgniag vqvttssasm ggsarivlrg igsingenrp livvdgipfn
      121 nanfntgstl nnsgttarga ggvdygdass dinpddiesv vvlkggpaaa lygarainga
      181 ivyttkkgkg gktqivlnsg vsfesiykmp rlqneygqgs eqsalptqii ngktyniaey
      241 tvdeswgpky npnikylpwy afdpefkddy mkevpwvapq hdvdsffktg vtynnnisis
      301 rafektgirf sygnvktegi fpnsslkkns mninitsqls drlkldagit ynltegfnrp
      361 eqgygnnsva qkffqfgprs ldfakardyk lengkqrtwn riawdnanpk ysdnpywtvf
      421 enyttdkrqr vygnatltyn ligkslyavg nlygdiysfs ndgrvavgsq aqssyfitkr
      481 nfseynyelr lhfdhrfgdf sinsfvgtnm rqsksdmlyg ktngglvipn fynlkngygv
      541 stvlqnfadr rvyslyesvs lgykdtffid atnrtdwsst ipqsynypsi sgsfvfsnli
      601 kanwlnfakl rggwaniasd adpyqlvnvy dvslpflglp rfsntnaskn rnllnerkit
      661 seigldanmf nnrlginfty ytskvkdqii elpvdggtgr dtkvinvgem ankgieltln
      721 gkilksenfs wdvnlnfskn nnklvtlspd aknlllanap frvgvyaveg mrygqiygtd
      781 ytyddkgnkv igangyyvpt stpvylgsyl pdynaglrnt iryknftlsa lidrqkggky
      841 fstthmfgmy sgmlekttan nmrevglvlp gvvkqtdgsy iqntkniday tyaishynvv
      901 daanvfdssy wklrevtlty tlpkgllnna iqdisitafa rnlftwglaw didpetasya
      961 sgnvqglegg slpstrtygl niqfkf
//
LOCUS       WP_115172331            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_115172331
VERSION     WP_115172331.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112333
     Region          27..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkffcrgpl slvftiaivs ssyaqtkrvt gvvtdgntpi tgvtitqegq nkqvttnkng
       61 eftlevtgpk pvlvftreff yprreeigtq svldiklspr drtiegivln sgyykvkere
      121 stgsiakvtg iqienqpvnn vlsavqgrva gvsiiqnsgv agagfdiqir grnslrsyns
      181 gssyeanvpl yivdgvvlsq gndfktglsg gllvyqetnp lnflnpndie sieilkdada
      241 taiygsrgan gvilittkrg kkgeltvqyt ssyalgevgn lpkmmntqey lnlrkeaykn
      301 dginkypana ydvngvwnpn kytdwqkyfv ggnsertsne frisggtsqt qlmlsaghde
      361 etpifpgdyr ykktktgfnv shqsddkkfk lqfssfytlq nnllpptdfm rvyaslspna
      421 pdlykpdgsi nwenstfsnp iaaatsnyks kerqllssln lsyqlakgls fqvssgyttg
      481 ekterkitpk tindpiynig serssldige iksmswiiep qlnyrwkken heidmlvgss
      541 fqhrqteinq lygsnfpsde llenigsaae lkvensgniv yryaaiygrl nyqyknryiv
      601 nitgrrdgss rfgpgnrfan fgavgaawif skesfmknil wlnfgklras ygtagsdnig
      661 dyqfydtykn tgtiydgsqg mvpsrlfnpn fgwevtrkle ialeagflnd rlyltashyr
      721 nrsgnqligv plpgitgfss iqanlnavvq ntgweftvsa kpfrnsdfkw essinlsipk
      781 nklisfpgle astyankfvi gkstvlqkly hylgidpvtg myqfedvnkd grldindrti
      841 vkeietkwyg gfqntfrykn wsldvlfqfs rqsginllsq isgsvgyinn nlpvefldyw
      901 tpdnptakyq kptsgadyal atagrnmmis davvttstyl klknvqlsyq lpeatfnrlk
      961 ariffqgqnl wmwtnykgld peynligytp alrtwslgft vty
//
LOCUS       WP_115172381             991 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_115172381
VERSION     WP_115172381.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..991
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110453
     Region          32..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnknvkslla lvltgcitqa afsqktkdtv ktkvidevvv talgikrmnk slgyaaenkd
       61 skifedtqnn nwanalegkv aglkiqtaga gplgsaritl rgeksfdmds nnalividgv
      121 pmsnnttgtg asaygagagg dlpidygngi nsinpddias vtilkgasaa alygsraang
      181 aimittksga gskklrvsfs sdtsfdtvlk wpdyqyeygq gtlnkdksgk fyysygased
      241 gvntgstssa fgpkfngqsy fqydpniigp slerqlwrpy knnikgfwqa getysnnlsl
      301 ensndktsfr tslgyvknnw mmpntgfnrf nfstslthql neklkittkv myskmmsdnl
      361 patgynnqsi syfmifqnpn vdlawyrpiw rpgkegidqi hpfssyidnp ymiayemlns
      421 annnqlnani tlnykinnnf dvmfrsglew qndirsqrrp fssanypqgy yreehitnqe
      481 ynndilftyk nsqkdskigi saslggsiry neyryemtra tglrkpniyt lsnglslfsa
      541 ipspkdrqen siyglvslny gkyvyldlta rndwtstlrk gnnsffypsa stsfilsdif
      601 gikntfdfwk lrlsvagvgn gtkpyrldry ysigeisgsv vapntlnnin llpekntnye
      661 ggmdfsmfkn rlgvnftfyk nitknqivei paltesgfrs rfinsgsven ngleitfnat
      721 pikkpnfswn inanwsanrn kvlslpaefe gnpytvasvg dvlfyqvrvg gslgdmygyk
      781 lqrtpdgqvi ydpstglptr padieyvgna fpewraglqn efkiknfris fsfdgqykgm
      841 aysqshhkms eqgklghtlw grenpdgmvi gegviknadg sfspntkkvl ltnyygdyyr
      901 ranvetnsfd tsfiklrdar vsytfpdasi gklklndlti alygknlwmw tkfplfdpea
      961 atlnnstitp gaevgqlpsa rtigmqlnvk f
//
LOCUS       WP_115172557            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_115172557
VERSION     WP_115172557.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113183
     Region          43..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfgnrklila affflgmkat lkaqesvqdi ivrdkstqqp lsnvsikntt tgkeivtdgn
       61 gkvaievnev sqtyaisleg yiaqdialsv gklpdsvyll petkqlegvv ltgytrqska
      121 kttgavssik aeaiaktpva sldqalqgqi pglyvaspsg qpgamgrvti rgigsvqddk
      181 tnplyildgm pispeifavl npldyenivv lkdasataqy gsrgangviq itskkgkdnd
      241 kghsqffyqn qfgissvnnq kwdmmnssqr lefeeilqdp nfpgwaysrk npykivngqk
      301 iaktesdyte gdqkladlra tntnwrklll rngvtnshyl smgggnqktn hysslsyfkq
      361 egvlpnsgve rfninsgvnh ksgrfissfn lnltggqtql sesdfdvset npvaslyfam
      421 pyekpydkdg nltpgvnrfg analtmyqdi srkekqlqgv lssnlsfeit knlkltstlg
      481 vnhqqtrftr iikpdtyfgs mvdpgeqgly erintqktsy manfgfnykk rwgsneveav
      541 alaefnkyst nydgftgygl ipglentpgg itpgtpdnnf ipkisggase nilvsqlgml
      601 rysyanrftl sgsirrdgss rvptdnryky fyafgatwnm kneeflkncg alstlrlrls
      661 hgltgnaggf asdfgyrqly kpqhyngyta fipispgnpn ynwemnkisd vglefglfkn
      721 riigevdlyn rvtsdlfinr slsmtsgfes iadnmgkirn rglefrlsgd lfrndnfswn
      781 lglnlaynqn rilslgsene ivtenysihk vgsalghfym vrwagvdpat gaplyydkng
      841 avtkeynpen avmvkgaydp pikggittsf tyknlqvnal ftfvkgmyrl ntaelyrtsa
      901 dpnyriynqs tgmlnmwqkp gdisqnpgaq yarymtdrel qsadyiklrn vsinyklkdl
      961 gslnkvfkei nifaqgqnll twtkwkgqdp eddnnwyqye yplprtitlg fnvlf
//
LOCUS       WP_115172622             955 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Elizabethkingia anophelis].
ACCESSION   WP_115172622
VERSION     WP_115172622.1
KEYWORDS    RefSeq.
SOURCE      Elizabethkingia anophelis
  ORGANISM  Elizabethkingia anophelis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Elizabethkingia.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Elizabethkingia anophelis"
                     /db_xref="taxon:1117645"
     Protein         1..955
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106438
     Region          62..954
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksytsigg iscvlmltva gssfpaqvqn nsdmisrknt seasilrtks dtispsnkla
       61 lekvshieev vlnagyykvk dkertgsiak vsakdienqp vtnvlsaaqg rmsgvsitqn
      121 tgtpgggfdi qirgknsirr egneplyiid gvpqasetps lystkilpws sinplnainp
      181 ndiesfeilk dadataiygs rgangviivt tkrgkkgrse lklntsysls ritrpmemmn
      241 teqyismrrq afqndnaayp atmydingtw dqsrhtdwqk eligsmaday gvqlsmnggs
      301 enfsyqisyg hneqttvlpa dfkyitnnin anfsyltpdr rmefnlvntf sfqqnnvqnd
      361 dltlksimls pnapalytsd gsinwengtf nnpvasllse ysnktaffnn glnvsyklfp
      421 flslkmnagi syqnfeersi kphtinnpsf gqtsmnstss rnnqvnfsyi lepqlvgayk
      481 tgnhqfefll gatlqktqse qgaiqgkgfe snalidniga asvktisdqv rsqynytavf
      541 arfnyqlkkr yivnltgrrd gssrfgannr fgnfgaigaa wlfseepflk evkwlsmgkl
      601 rgsigatgnd kigdyqylnt yiissgiyng qtglnparly npnfswektl kkelalevgl
      661 wngrfnfsga yyentssnql vgiplpattg fpsvqsnlpa kirntgwefd tsvqvvrkgk
      721 fryetsfnls ipkntlvefp nlegstysnq ymigypttia kvyqyegidp atglykftdf
      781 ngdgkitspd dnkaveklgv rffggwstqf rlgnwsasfl wqfvkqrnwn ynrqmllpga
      841 lsnqpvevld awspsnpggs ymeysagynp qklslhgffq nstaavsdas yirlknvqln
      901 yripmqkmgi keamiyvqgq nlltitnyfg mdpefylvgy lpplktyslg fqvtf
//
LOCUS       WP_115175489             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            feeleii].
ACCESSION   WP_115175489
VERSION     WP_115175489.1
KEYWORDS    RefSeq.
SOURCE      Legionella feeleii
  ORGANISM  Legionella feeleii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Legionella feeleii"
                     /db_xref="taxon:453"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40076
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miiaalnesk ndtrvaitpn avkhylklgl evaceadagk asgfrdadye eagasivadk
       61 kdllkktkil vtvnepspkd lqglpagsll igpldneqeg elltwcckek vsafsmnlip
      121 risraqsmds lssqanlagy ravlegvnhf nraipmmmta agmihpakil ilgagvaglq
      181 aiatakrlga vvyafdvrra akeqveslga efievseeds etsggyaget seeykrrqae
      241 lidqyarqsd ivvstalipg rkapvlltkk tvegmkpgsi ivdlatargg ncelsqrdkv
      301 ikhgevtlvg ysnlaglvpa taselyatnl vnlirlllps tppvltfsre deivkqallc
      361 hegnylpfqt vken
//
LOCUS       WP_115177367             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_115177367
VERSION     WP_115177367.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53514
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq gkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_115178065             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_115178065
VERSION     WP_115178065.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53805
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vtmlafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_115185421             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_115185421
VERSION     WP_115185421.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53628
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc tdchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddiryaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_115200828             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_115200828
VERSION     WP_115200828.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53598
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfygkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_115204688             310 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_115204688
VERSION     WP_115204688.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..310
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35778
     Region          5..170
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifelfskr qkklrgevad vyqytnipnq frvqvvhivr dtigedsdye teasniykli
       61 hqtlckeygv fslkqyhdsn fqaifdyfls endhekcldi ielsfkling yiksnewkfr
      121 gttkqkpdda ieelnirfke aglgyqfesg elvkvdsqfi hsdvvkptlq ilgknsnysg
      181 andeflsahe hyrhqrykec lndclksfes lmkaihkkhs wqfndtdtak klinsclsnn
      241 lvpeylqnqf ssirillesg iptirnkegg hgqgavitkv peylasytlh ltatnllfla
      301 kceesytkkq
//
LOCUS       WP_115206656             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            parahaemolyticus].
ACCESSION   WP_115206656
VERSION     WP_115206656.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54649
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvviesqag vlasfddaay eaagakvvss
       61 devwasglil kvnapivdee kgidesallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaefltv dfqedsgsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgrpap klitkemvds mkagsvivdl aaanggncey
      301 tvkdqvimtd ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvikeg eitwpappiq vsaqpqakqa qpvkkepkve eptsptkkli glvaavgafa
      421 wiasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvsflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_115213086             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus lacunae].
ACCESSION   WP_115213086
VERSION     WP_115213086.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus lacunae
  ORGANISM  Cupriavidus lacunae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus lacunae"
                     /db_xref="taxon:2666307"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38935
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvvvqagag lsasqpdsay eavgatigsa
       61 aeafgaqlvl kvrapdpael aqmkpgtvlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaaralil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra iqadivitta lipgrkapvl lqeatvqqmk pgsvvvdlaa aqggncpltv
      301 adevvnhngv iiightnlas mvaadasaly arnvldflkl vvdkdaqftl nldddivaac
      361 lmtrreelal as
//
LOCUS       WP_115213483             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus lacunae].
ACCESSION   WP_115213483
VERSION     WP_115213483.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus lacunae
  ORGANISM  Cupriavidus lacunae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus lacunae"
                     /db_xref="taxon:2666307"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39127
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvpveth ayesrvaatp etvkkyvaqg hkvvvqagag vrasqpdsay eavgatigsa
       61 aeafgadlvl kvrapeagel aqmkqgavlv gmlnpfdaes karmaaagit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgami easdvrpavk eqieslggkf ldvpfitdee reiaqgvggy arpmppdwmr
      241 rqaelvhera kqadiiitta lipgrkapvl lqeatvqqmk pgsvvvdlaa aqggncpltv
      301 adevverhgv ifvgytnlas mvaadasaly arnvldflkl vidkdgqfvi nkdddivtac
      361 lmtrreelal ac
//
LOCUS       WP_115214555             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus lacunae].
ACCESSION   WP_115214555
VERSION     WP_115214555.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus lacunae
  ORGANISM  Cupriavidus lacunae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Cupriavidus lacunae"
                     /db_xref="taxon:2666307"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54087
     Region          3..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvrellk lgyqvavetg agqeasfsdd dyraagaaiv
       61 daaslwasvd vvikvrppqg hpglgveeaa llkkhatlig fvwpaqqmam lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyakems
      241 pafieaemrl faeqarevdi iittalipgk papklleagt vglmragsvv vdlaaeqggn
      301 celtvpgeav rqngvtiigy tdlpsrmaaq asqlygtnir hllteltpgk dgqlvvdmdd
      361 emirgatvlh qgvvtwpppp ltvaipqqqa paatppvhae aepprsrtga tlvalaivaa
      421 allglgavap pafmahftvf vlaifvgyqv vwnvtaalht plmsvtnais giivvgalvq
      481 lgkpslvtav iagcavlvat iniaggflvt qrmlkmfqrd
//
LOCUS       WP_115214630             372 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Cupriavidus].
ACCESSION   WP_115214630
VERSION     WP_115214630.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38888
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipqetr agetrvaatp etvkkyvaqg hevivqagag vrasqpdsay eaagarigta
       61 aqalgaalvl kvrapdeael gqmkpgatlv gmlnpfdgen narmaaagiv afaleaaprt
      121 traqsmdvls sqaniagyka vleaadhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfeteee reiaqgaggy arpmpadwmr
      241 rqaelvhqra sqadivitta lipgrpapvl lkeetvmamk pgsvvvdlaa aqggncpltv
      301 adqvverhgv vlvghtnlas mvaadasaly arnvldflkl iidkegkpsi nleddiveac
      361 lmtrrdkmal as
//
LOCUS       WP_115218088             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Suttonella
            indologenes].
ACCESSION   WP_115218088
VERSION     WP_115218088.1
KEYWORDS    RefSeq.
SOURCE      Suttonella indologenes
  ORGANISM  Suttonella indologenes
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Cardiobacteriaceae; Suttonella.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Suttonella indologenes"
                     /db_xref="taxon:13276"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54534
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipkesl agearvaatp ktvkelkklg favaveanag lasqfddaay reagaeivqg
       61 davynsdliy qinpptdael akikdgttlv sfvwprqdqa lvdklaqrki tvlamdmvpr
      121 israqsmdal ssmanisgyr avveaahefg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igaakslgai vrafdtreev aeqiesmgge flrvdfeekd ggsvntgyak vmskefieae
      241 mklfaeqakq vdiiittaai pgkpapklit nemvasmkrg svivdlaaat ggnceatvag
      301 krhvtengvi vlgytdlanr lagqssqlya tnlvnlskll spqkdgqihv nfedsilrnm
      361 tvirdgeltf pppeisvsav pqakaeaaka petaavekpa spkifrqvtl aclafmaflf
      421 iggapapfla nmmvfvlsiv igyyvvwnvs hslhtplmsv tnaisgiivv gamlqighgs
      481 amasflafva illvsinifg gfavtrrmla mfrkd
//
LOCUS       WP_115217341             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_115217341
VERSION     WP_115217341.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53587
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe ftkgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka lqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_115220945             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            donaldsonii].
ACCESSION   WP_115220945
VERSION     WP_115220945.1
KEYWORDS    RefSeq.
SOURCE      Legionella donaldsonii
  ORGANISM  Legionella donaldsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Legionella donaldsonii"
                     /db_xref="taxon:45060"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39952
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miiaalnesn sdtrvaitpn avkhylklgl evtceagagk asgfsdadye eagativadk
       61 kdllkktkil vtvnepspkd lqglpagslv igpldneqeg elltwcckek vsafsmnlip
      121 risraqsmds lssqanlagy ravlegvnhf nraipmmmta agmihpakil ilgagvaglq
      181 aiatakrlga vvyafdvrra akeqveslga efievseeds etsggyaget sedykrrqae
      241 lidqyarqsd ivvstalipg rkapilltkk tvegmkpgsi ivdlatargg ncelskrdki
      301 ikhgevtlvg ysnvaglvpa taselyatnl vnlirlllps tppvltfsre deiikqallc
      361 hegnylpfqt vken
//
LOCUS       WP_115226776             394 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Iodobacter
            fluviatilis].
ACCESSION   WP_115226776
VERSION     WP_115226776.1
KEYWORDS    RefSeq.
SOURCE      Iodobacter fluviatilis
  ORGANISM  Iodobacter fluviatilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chitinibacteraceae; Iodobacter.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Iodobacter fluviatilis"
                     /db_xref="taxon:537"
     Protein         1..394
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41598
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mliaipaevl pgefrvaatp etikklikag htvrveskag qhaaitdtay teagaeiaph
       61 paalyqgaql ilkvraplah elpllperaa lvalfdihry dhldalnakq isayalelip
      121 ritraqsmdv lssqaniagy ravllatqyy prfmpmlmta agtvkparvl ilgagvaglq
      181 aiatakrlga ivevfdvrpa treqveslgg kfievalndd ekaaaetagg yaremsedyk
      241 lrqallidqq arladiiist aqipgkaapv lipeetvsgm ktgsviidla vdsggncpls
      301 rsdevvrsen gviivghsnl asllaadasa lyarnlltfl sllqdadgay aphnddeiik
      361 atllsqhgeq lfgrapahtq gasaphtsqp tana
//
LOCUS       WP_115279407             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium tokaiense].
ACCESSION   WP_115279407
VERSION     WP_115279407.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium tokaiense (Mycobacterium tokaiense)
  ORGANISM  Mycolicibacterium tokaiense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Mycolicibacterium tokaiense"
                     /db_xref="taxon:39695"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51972
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl agetraaatp qtvgqliklg ysvvvesgag aaasfadaay veagaeigsp
       61 wnadiilkvn apddaeiaal rdgstlvsli spalkpelvd klasrpitvl amdavprisr
      121 aqsldvlssm aniagyravv eashrfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agsmgavvqa tdprpevadq vrslggeyvs vdpnagevsa tgyakemgdd ykareaqlya
      241 elardvdiii ttalipgrpa priitadmva amkpgsvivd maasnggnve gtvkdqavvt
      301 dngvtiigyt dlagrlpsta sqlygtnlvn llklltpgkd gqlvldfddv vqrsvtvvrd
      361 geitwppppv qvsaapaaaa tatsvekpap kppmsaqrrl gltfaaaaal fvlialspaa
      421 lqvhlvvfal aivigyyvis gvhhalhtpl msvtnaisgi ivvgallqig tgdlvitvla
      481 tvaillasin vfggfavtrr mlamfsrs
//
LOCUS       WP_115287354             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_115287354
VERSION     WP_115287354.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35960
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhkhsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechav frsvllrihe rkgivyheqd slntlmtnlm argvisaeya
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vsp
//
LOCUS       WP_115290429             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ectopseudomonas mendocina].
ACCESSION   WP_115290429
VERSION     WP_115290429.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas mendocina
  ORGANISM  Ectopseudomonas mendocina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Ectopseudomonas mendocina"
                     /db_xref="taxon:300"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38861
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikklvgqg hqvtvqagag isasipdsay eaagatigne
       61 tsafgadlvl kvvapteael vhmkagavlv gmlnpfcndt iarmnargit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee rkcaqgvggy arpmpaswme
      241 rqakavhera kqadiiitta lipgrkapil lheatvqemk pgsvvidlaa aqggncplte
      301 adqvvvkhgv tlvghtnlaa lvpadasaly arnlldflkl vidkegqfql nleddivsac
      361 lmcnagevvr kng
//
LOCUS       WP_115299844             492 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Pasteurella multocida].
ACCESSION   WP_115299844
VERSION     WP_115299844.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella multocida
  ORGANISM  Pasteurella multocida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Pasteurella multocida"
                     /db_xref="taxon:747"
     gene            1..492
                     /gene="nrfA"
     Protein         1..492
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=54899
     Region          14..491
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mngviivntl kkrlfvattm iwglsvtlpv laeykpieqp vepanpslki esrndlfkek
       61 ypkqyqtwad tskstdldsv nyedprvivl wagyafakdy kkprghfyav tdvreilrta
      121 apmtpdagpm pmacwscksp dvprliaerg eagyfgatwa sggsevvnpi gcadchdtts
      181 kdfaegkpal riarpyvlra lekidhkfdt sdrtdqraal canchveyyf agdlkqvtfp
      241 wdngitvdam ekyyddigfv dwthavskap mlkaqhpdye twmlgvhgkn gvtcidchmp
      301 kvqgadgkvy tdhqignpfn afehtcanch dqskeklqam vksrkteikd vmlrledqlv
      361 aahfeakaaw eagaskeemk ealqdirhaq wrwdyaaagh gghihapdvl lkvigtgldk
      421 ssdartklvr vlakhgitdp vqlpdistae nawkatgvdi ekerkakaef lktvvpqwdk
      481 earekgllpa ek
//
LOCUS       WP_115302166             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            beliardensis].
ACCESSION   WP_115302166
VERSION     WP_115302166.1
KEYWORDS    RefSeq.
SOURCE      Legionella beliardensis
  ORGANISM  Legionella beliardensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Legionella beliardensis"
                     /db_xref="taxon:91822"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39991
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miiaalnesp nesrvaitpa avkhyiqlgf kvyieenagi asgfankaye dveahvisnr
       61 qellkntnvv vlvnapnpdd ltclppealv vapvdndpds alikwccaen islismnlip
      121 risraqslds lssqanlagy ravlegihhf nraipmmmta agmiqpakil ilgagvaglq
      181 aiatakrlga vvyafdvrra akeqveslga efievedgad letaggyane msedykarqa
      241 alihkyakls divittalip grkapilitr qtveemkpgs vivdlatarg gncelsevdr
      301 vikhgevtlv gysnvaglvp ataselyann lvhlirlitv aptalvfnae deiiqqamlc
      361 hegnympfqa akea
//
LOCUS       WP_115309014             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Kingella
            potus].
ACCESSION   WP_115309014
VERSION     WP_115309014.1
KEYWORDS    RefSeq.
SOURCE      Kingella potus
  ORGANISM  Kingella potus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Kingella.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Kingella potus"
                     /db_xref="taxon:265175"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53784
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mmigipketl sgetrvsctp atvsqlkklg fevcveqgag eaaslddaay eaagaqtgta
       61 advwkcplvy kvnapngnem rrlkegqtlv sflwpaqnpe lvqkladkkv nvlamdmvpr
      121 israqsldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vkafdtrlev aeqiesmggk flkldfpqea ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaavp gkpapklitk emvasmkpgs vivdlaaatg gnceltkpgg
      301 lyvtdngvqi igytdmanrl agqssqlyat nlanltklls pnkdgeitld fedavirnmt
      361 vtrdgeitfp ppaiqvsaap qqaqrpsena aakpeakpvp awkklapavv gavlvlwvga
      421 vapaaflnhf ivfvlscvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllafvavl iasvnifggf fvtrrmlnmf rkg
//
LOCUS       WP_115318095             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium aichiense].
ACCESSION   WP_115318095
VERSION     WP_115318095.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium aichiense (Mycobacterium aichiense)
  ORGANISM  Mycolicibacterium aichiense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Mycolicibacterium aichiense"
                     /db_xref="taxon:1799"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52327
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipresl pgetrvaatp qtvgqliklg ydvlvesgag vaasfsdeaf veagagigtt
       61 aetlatdivl kvnaptsaei aalrdgatli slispalkpd lveelstrpi tvlamdavpr
      121 israqsldvl ssmaniagyr avieaahafg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaagslgai vratdprpev adqvkslgge ylsiespeie vsatgyakem gddykareaq
      241 lyadqsqdvd iiittalipg rpapriitad mvasmksgsv ivdmaaangg nvegtvkdqa
      301 iltdngvtii gytdlagrlp aqasqlygtn lvnllklltp ekdgalvldf ddvvqrsvtv
      361 vrdgettwpp ppvqvsaapa paataapavq qtkepmtmgr rlgitfgaaa vlfglialsp
      421 aalqvhltvf alaivigyyv ighvhhalht plmsvtnais giivvgallq ighgdvivtt
      481 laavaillas inifggfavt rrmlamfsrs
//
LOCUS       WP_115314856             499 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Phocoenobacter uteri].
ACCESSION   WP_115314856
VERSION     WP_115314856.1
KEYWORDS    RefSeq.
SOURCE      Phocoenobacter uteri
  ORGANISM  Phocoenobacter uteri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Phocoenobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Phocoenobacter uteri"
                     /db_xref="taxon:146806"
     gene            1..499
                     /gene="nrfA"
     Protein         1..499
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56224
     Region          1..494
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtklrrsllt ltiagftffs mqnafaadse yttksgkkpv paeelakand iqiqakneqf
       61 aekypkqyns wyktsestea tpaieedprm ivlwggylfs heynkprghf ytvtdvrnil
      121 rtgaprsdkd gpmpmscwtc kgpdvprlia kwgekeyfsg kwfkagseiv nsvgcadchd
      181 trskefaegk pslniarphv lralevigqd fdkldrdgkr tavcanchve yyfdpkavnn
      241 vvfpwfngtd vdsmekyydd ikfkdwthsi skapmlkaqh pdfeiwsmgm hgkngvtcid
      301 chmpkvkgad gkvytdhqig npfdafestc anchdqskek lqaivksrkh dvqesrikle
      361 dqlvkahfea kkawevgate eemkealqai rhaqwrwdys aashgghmha pdvllkviss
      421 gldrvadars alavvltkhg velpiqipni dtaeqawkam gidiekqrak kaaflkevip
      481 qwnkkaleng lidtlppak
//
LOCUS       WP_115324457             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Trueperella pyogenes].
ACCESSION   WP_115324457
VERSION     WP_115324457.1
KEYWORDS    RefSeq.
SOURCE      Trueperella pyogenes
  ORGANISM  Trueperella pyogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Trueperella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Trueperella pyogenes"
                     /db_xref="taxon:1661"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52962
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresg gqtlvaatpd tvgklsklgy evvvehdags aasfpdslye sagarivske
       61 eawdadivta ldapaladld lmrsgatlis rmapgrnpdi lqalssrsit glamdmvpri
      121 sraqsmdvls sqanvagyra vieaahhfgr lfsgqvtaag kvapanvyvi gagvaglaai
      181 gtansmgavv katdvrpeta eqvesmgagf vaipvaaees adgyakemdq eqaaaaekly
      241 teqaawadiv ittaaipgrr spvlltaeav agmkpgsviv dmgaanggnv vgsrpdevvv
      301 tdngvviigy selaarlpgq asqlygqnif nffklatpdk dgvlhldldd eivrsmlvtl
      361 dervmypppp vkvsaapapv passeevtsa eakekswiak hwwkiaagav ftwliltapa
      421 gstthflvfa lavvigfyvi tsvthalhtp lmsvtnaisg iivvgalmqv sassvvvqil
      481 sfiaiavasi nifggflvte rmlkmfhrs
//
LOCUS       WP_115330575             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            busanensis].
ACCESSION   WP_115330575
VERSION     WP_115330575.1
KEYWORDS    RefSeq.
SOURCE      Legionella busanensis
  ORGANISM  Legionella busanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Legionella busanensis"
                     /db_xref="taxon:190655"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40391
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miiaalnesp adsrvaitps vvkqytklgf kvyceknagl asgfsdkaye eveasisdnr
       61 kellnntnvv tfvntpdptl lttlpdkali iapvdnepes elikwcckhr islfsmnlip
      121 risraqamds lssqanlagy ravleginhf nraipmmmta agmikpakil ilgagvaglq
      181 aiatakrlga vvyafdvrra akeqveslga efieveddad leaaggyane msesykarqa
      241 alihkyakla divvstalip grpapvlikr dtveemkegs vivdlatarg gncelsekdq
      301 iikhsdttii gysnfaglip ataselyann vlnlirlitv aptslcfnve deilqqallc
      361 hegsympfqk tkev
//
LOCUS       WP_115333087             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_115333087
VERSION     WP_115333087.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36022
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvg yqfeseeiir vdsqlihadv vqptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel asymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_115333868             467 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella baltica].
ACCESSION   WP_115333868
VERSION     WP_115333868.1
KEYWORDS    RefSeq.
SOURCE      Shewanella baltica
  ORGANISM  Shewanella baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Shewanella baltica"
                     /db_xref="taxon:62322"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51769
     Region          1..467
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mmkkmtgksf alsalvaasf maagamasdk teprnevykd kfanqyaswh dtdkstentd
       61 vlasdpslvv lwagygfakd ynaprghmya itdvrntlrt gapanaedgp mpmacwscks
      121 pdvprlieeq gedgyfkgkw akggpevvnt igcgdchekg tpklrisrpf aergmealgt
      181 pfakaskkdk qsmvcgqchv eyyfekkegr kgfvkfpwdm gttveqmety ydgiefsdwt
      241 halsktpmlk aqhpgyetwk lgvhgkndvs cvdchmpkvt ndkgrkytdh kvgnpfdrfe
      301 etcatchsqs keflvgltne rkakvkelkg raeaqlvkah feaaaawkag ateaemkpil
      361 tdirhsqwrw dyaiashgaa ahapeevlri lgtavdkaad arvklaqlla kkgitdpiai
      421 pdistkakaq aalgmdmekm naekevfkkd mlpkwdeeak kreatyk
//
LOCUS       WP_115335396             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            baltica].
ACCESSION   WP_115335396
VERSION     WP_115335396.1
KEYWORDS    RefSeq.
SOURCE      Shewanella baltica
  ORGANISM  Shewanella baltica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Shewanella baltica"
                     /db_xref="taxon:62322"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53329
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevvieanag qlssfddaaf eaagakvttd
       61 vwqadlifkv napsdaeieq ikdgatvvsf iwpaqnpelv aklakrkinv mamdmvpris
      121 raqsldalss maniggyrav veaahqfgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggqfl kldfgneegg ssdgyaktms defiaaemal
      241 faeqakevdi iittalipgr papklitkam vdsmksgsvi vdlaaatggn ceytqsgelf
      301 vtpngvkvig ytdlpgrlpa qssqlygtnl vnlmklmcke kdgtasinfd dvvmrnmtvi
      361 kegevtfppp pisvsaapak paakiepknt tpkapsklky vlaalgvagf aavasvappe
      421 flshftvfll scvvgyyvvw nvshslhtpl msvtnaisgi ivvgallqig qgstlvtvla
      481 fiavliasin ifggftvtqr mlkmfrkd
//
LOCUS       WP_115382774             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Jannaschia
            formosa].
ACCESSION   WP_115382774
VERSION     WP_115382774.1
KEYWORDS    RefSeq.
SOURCE      Jannaschia formosa
  ORGANISM  Jannaschia formosa
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Jannaschia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Jannaschia formosa"
                     /db_xref="taxon:2259592"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55723
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkevh adearvaitp esaghlqklg yevaveagag ekagfldsay rdagvevvdd
       61 aaqlwkiadv iakvrpptee evarleqgkl lisffypssn eklmelakdk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aqfvflefed selpdgaatg gyappsspef
      241 qakqlekfre lapeidivic talipnrpap vlwtkdmvea mkpgsvivdl aaerggncel
      301 trkdekfvte ngvtivgytd fpsrmatqss tlygnnirhm mfdltpgkdg qvvhnmaddv
      361 irgatvahag eitfpppppk vaaiavqkke kpkeltpeek raaevaafrs etkfqvglla
      421 vggallllag lftpasfmqh fivftlacfv gfqviwnvah slhtplmavt naissiiilg
      481 alvqigsgsi lvsilaalav fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_115376922             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_115376922
VERSION     WP_115376922.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53626
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aiskpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_115393020             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodovulum
            sp. 12E13].
ACCESSION   WP_115393020
VERSION     WP_115393020.1
KEYWORDS    RefSeq.
SOURCE      Rhodovulum sp. 12E13
  ORGANISM  Rhodovulum sp. 12E13
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Rhodovulum.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Rhodovulum sp. 12E13"
                     /db_xref="taxon:2203891"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55986
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspkevm egerrvamtp dsakqlqklg hecyveagag vpagftdday aeagvtvvtg
       61 eqalfdavdv vakvrpptea evdmlregqt lisffypasn edlmkraadr gatvlamdmv
      121 prisraqkmd alssmaniag yravleagne fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaatslg aityafdvrp evaeqiesmg aefvyldfee etqdgaatgg yaapsspefr
      241 ekqlekfrel apdvdivitt alipnrpapv lwtkdmveam kpgsvivdla aerggncelt
      301 vkddrvvtdn dvtilgytdl nsrmatqsst lyatnvrhlm tdltpekdgv ivhdmeddvi
      361 rgatiahene vtfpppppkv qaiaaqpkkd kpkeltpeek raqevaafrk qtinqvallg
      421 vgaaavlavg avpgmpasfm qhfivfvlsv fvgfqviwnv ahslhtplma vtnaissiii
      481 lgalmqigss siivtilaaa avfmaginif ggflvtrrml amfqks
//
LOCUS       WP_115389138             467 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Shewanella].
ACCESSION   WP_115389138
VERSION     WP_115389138.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51854
     Region          1..466
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvkklnqksf alsalvaasl maagafasdk teprnevykd kfknqyaswh dtaksseivd
       61 vlaedpnlvi mwagygfakd ynaprghiya vtdvrntlrt gapksaedgp mpmacwscks
      121 pdvprlieeq gedgyftgkw akggpevvna igcgdchekg spklrlgrpf aerametlgt
      181 pfdkasrkdk qsmvcgqchv eyyfekvegr kgfvkfpwdq gttvesmeay ydaiefadwt
      241 halsktpmlk aqhpgyetwq lgvhgknnvt cvdchmpkvt ndkgrkftdh kvgnpfdrfe
      301 etcaqchtqs kefmenltae rkvkvnelkl kaedqivkah feaaaawkag atevemkpil
      361 tdirhaqwrw dyaiashgva ahapdealrv lgtavdkaan arvklaqlla kkgitepval
      421 pdistkakaq aalgmdmkkm vadkeefkkn vlpkwdaeak kreatyn
//
LOCUS       WP_115397669             304 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_115397669
VERSION     WP_115397669.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..304
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36187
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldeisnlll ktddkrkhid tielafkyid tylrtyevtl
      121 glepdkaise lnnifhdhsl kyryengriv rlrrikrlkn iryylyspge ygfveydlme
      181 aynrlmlndf acvvrechav frrvlirihe rkgiiyheqd slntlmanlm argvisaeya
      241 hkfhflsnvl eseiflpiap ekshhhyvmm lriseelacs iyyltersif fltqraeedd
      301 vaps
//
LOCUS       WP_115425114             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_115425114
VERSION     WP_115425114.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53540
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rcftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_115429482             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_115429482
VERSION     WP_115429482.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53632
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta tpakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dktalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_115432953             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Crenobacter cavernae].
ACCESSION   WP_115432953
VERSION     WP_115432953.1
KEYWORDS    RefSeq.
SOURCE      Crenobacter cavernae
  ORGANISM  Crenobacter cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Crenobacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Crenobacter cavernae"
                     /db_xref="taxon:2290923"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40191
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mliaipaecv anetrvaatp etvkklvamg hsvivqkgag lasavpdsaf aeagasvaet
       61 raatyanadi vlkvrpplde eiaeikdgta liaqlapyqn asfpalaakk vsafamellp
      121 rttraqsmdv lssqnniagy ksvllanqyy prfmpmlmta agtvkparvl ilgvgvaglq
      181 aiatakrlga vveafdvrps tkeqveslga kfvevpmtde ekaasdgvya kemsddykrr
      241 qgelvakhak aadivittal ipgkkapill sadvvagmkp gtvivdmaae aggnceatrp
      301 gevhvtdgrv tvvgtynlpg lmagdasaly aknlltflsl mlskegfsin leddlleatl
      361 vthagevrfg qpskepapqs aastqa
//
LOCUS       WP_115440387             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_115440387
VERSION     WP_115440387.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53556
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkata
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_115437113             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_115437113
VERSION     WP_115437113.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53807
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 tavwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakdv diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_115467739             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinomonas piezotolerans].
ACCESSION   WP_115467739
VERSION     WP_115467739.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas piezotolerans
  ORGANISM  Marinomonas piezotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Marinomonas piezotolerans"
                     /db_xref="taxon:2213058"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55292
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeie dgelrvamtp avaervkklg fdlviesgag aaasysdeay iaagvevtsd
       61 tkalwhdsdv likvrppieh pelgfygiel lgqnqtlist lypaqnsvkl nqlaergtna
      121 valdavpris raqkmdvlss maniagyrav veaaqhfgrf ftgqitaagk vppakvlvig
      181 agvaglaaig aaksmgaivr afdtrpevke qvesmdaefl eldfddedgs geggyakvms
      241 pefiaaemal faeqakdvdi iittalipgk papeliteem vrtmkpgsvi vdlaaetggn
      301 ckltqandvv nvhgvtligy tnlpsrmaaq ssqlfatniy hlltelcpnk dgqidlnmed
      361 evirgatvvk qgnitwpppa prlsaapktd vseplpeake sakkeekkps afgflvpvli
      421 vgallmgvgs vapaefmghl tvfvlscfvg ymvvwgvshs lhtplmsvtn aissiivvga
      481 ltqisndsvi vsilaalaif itsinivggf avthrmlkmf rk
//
LOCUS       WP_115475427             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cereibacter johrii].
ACCESSION   WP_115475427
VERSION     WP_115475427.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter johrii
  ORGANISM  Cereibacter johrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cereibacter johrii"
                     /db_xref="taxon:445629"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55544
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreif egearvamtp dsalqlqklg hhcvietgag mkagfsdeay aaagvevlps
       61 aealfeaadi vvkvrgperp eaerlrrgqt lisffwpaqn aellelckek gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvflefee aqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrpapkl wtedmvsamk rgsvivdlas erggncdltv
      301 pdqkivtpng vtvvgytdfp srmaaqastl ystnirhmlt dltpkkdgvi hhnmeddvir
      361 gatvthdgai tfpppppkva aiaaakprek vkeptpeekr aaeiaafrkq tvsqvamlav
      421 gtalllfvgm yappsfmahf ivfalacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 llqigsgnfl vvllaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_115488281             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_115488281
VERSION     WP_115488281.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38633
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag lkasivdsay eaagatigsa
       61 gdafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaeqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqtvvengv iicgptnlag avaadasaly arnlldflkl vfnkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_115515398             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Undibacter
            mobilis].
ACCESSION   WP_115515398
VERSION     WP_115515398.1
KEYWORDS    RefSeq.
SOURCE      Undibacter mobilis
  ORGANISM  Undibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Undibacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Undibacter mobilis"
                     /db_xref="taxon:2292256"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39288
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavarete aneprvaasp etvkkfkalg aevvvargag nasgypdaey eaagatiaea
       61 vggdadlilk vrrpstgeia sykkgaivia imdpygneaa lkamadaglt tfamelmpri
      121 traqsmdvls sqanlagyra vidgaetygr ampmmmtaag tvpaarvfim gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 alvaehikkq divittalip grpapklita amvasmkpgs viidlaverg gnvegavpgq
      301 vvqvgpakiv ghlnvpgrla asasalyakn lltfidtmid kkekklainw ddelikatml
      361 trdgavvhpn fmpktaa
//
LOCUS       WP_115520387             591 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Helicobacter sp. MIT 01-3238].
ACCESSION   WP_115520387
VERSION     WP_115520387.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter sp. MIT 01-3238
  ORGANISM  Helicobacter sp. MIT 01-3238
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Helicobacter sp. MIT 01-3238"
                     /db_xref="taxon:398627"
     Protein         1..591
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62678
     Region          18..563
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqqtlftats qsqigipqig ipkesqknea rvsaspasvs alqklgftvv vakgagakag
       61 fsdeeyqnng ativtqnqal ssdivlvvna psdeeikqlk kgailigllg iahdkplles
      121 lnaqginals mdcvprisra qsmdalssma niagyraiie ssfafgrffg gqitaagkip
      181 pakvlvigag vaglasigta nslgavvraf dtrpevkeqv qsmgaeflei nieeeagggd
      241 gyakvmsday ikaemelfat qakevdiiit talipgkpap klitkqmves mrqgsvivdl
      301 aaqnggncel tkanelivsk ngvkiigytd lpsrlptqss qlyatnvlnl lklmceksqa
      361 iqeskeskeg kegkleidfd deilrgacvc kdgqitfppp pikvsatknp adnlaksgkk
      421 dsakedlaqk dstqsstdss kscplrkiwh kyysyaplgf givailaffg icanapsefl
      481 shfmvfalac vvgyyvvwnv nhalhtplms vtnaisgiiv vgallqmgeg slisalafvg
      541 vfiasinifg gffvtqrmlk mfrldrddrq dskttkssna ksssakasnv k
//
LOCUS       WP_115523329             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. RT-1].
ACCESSION   WP_115523329
VERSION     WP_115523329.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. RT-1
  ORGANISM  Arthrobacter sp. RT-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Arthrobacter sp. RT-1"
                     /db_xref="taxon:2292263"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53324
     Region          3..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivael gretrvaatp vtvkqllglg yevvvekgag esasfrdeay aeagalvvga
       61 deawgsevvl rinpptedei trltegatli gslspglrpe lvealasrpi talaldavpr
      121 israqsmdvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksiggt ylkvevaeem kstdgyakat seaynaraae
      241 iyseqaadvd iiittalipg rpapklltae dvasmkagsv ivdmaagqgg nvegsvager
      301 ivtdngvvil gytdlparlp aqasqlygtn mvnllklltp dkdgqlridf ddvvqrsvtv
      361 vregektwpp ppvqvsaapa aktqadvaes tapkkkqgls nagkaglfaa giavlfgina
      421 vapaplpqhf tvlmlsivvg fyvigkvhha lhtplmsvtn aisgiivvga llqvtsenlv
      481 mqvlaavavl lasinifggf avtrrmlamf sagkvrs
//
LOCUS       WP_115526096             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. RT-1].
ACCESSION   WP_115526096
VERSION     WP_115526096.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. RT-1
  ORGANISM  Arthrobacter sp. RT-1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Arthrobacter sp. RT-1"
                     /db_xref="taxon:2292263"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40050
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiprerr dgewrvaatp etvkqltalg aevlleegag saaghpdhdy rqagaqvvpg
       61 ldlarldala hvrpldpdta rslkrgavtv glaspsselp tvealaeagv tafalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplymtaa gtvpparvlv lgagvaglqa
      181 igtakrlgar vfandirpas adevasmggt firldletae aaggyarqls sdagtrqrql
      241 laphvaqsdv littaavpgr rapllvtrem vqgmrpgsvv vdlaaesggn vegvvpgqdi
      301 avptadgagh vtlvglkdpa samasdasrl yaknvanlla lmihegvvtp dfddevvaga
      361 clthdgavrh lptaellgar tragqegvl
//
LOCUS       WP_115531644             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            dinghuensis].
ACCESSION   WP_115531644
VERSION     WP_115531644.1
KEYWORDS    RefSeq.
SOURCE      Trinickia dinghuensis
  ORGANISM  Trinickia dinghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Trinickia dinghuensis"
                     /db_xref="taxon:2291023"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39729
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaeir agetrvagtp etvkklvskg havlveqgag aqahfpdday aqagatlvdt
       61 vrawdadlil kvqsptdael ahlrrggllv gmldpfdadh varinargvq afalesiprt
      121 traqsmdvls sqaniagyka vlmaatlyqr ffpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpaak eqteslgakf ldvpyetdee reaaqgvggy arpmppswls
      241 rqsalvhara aqadivitta lipgrtaptl ldenavramk pgsvivdlaa grgamsgara
      301 ggnctltqad evvvrhgvhi agytnlpsmv atdasslyar nvldflklii dadgqpkidl
      361 rddivaatll drgtsmlkta
//
LOCUS       WP_115538764             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cylindrospermopsis raciborskii].
ACCESSION   WP_115538764
VERSION     WP_115538764.1
KEYWORDS    RefSeq.
SOURCE      Cylindrospermopsis raciborskii
  ORGANISM  Cylindrospermopsis raciborskii
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Aphanizomenonaceae; Cylindrospermopsis.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Cylindrospermopsis raciborskii"
                     /db_xref="taxon:77022"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40635
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeie vserrvslvp dmvaklvkqg leisvetgag ekayfsdgdy eaagakiitd
       61 aavlwgeadi llkvsppqer edgreeidll kpgavllsfl nplgnpevar klaqrqital
      121 smeliprttr aqsmdalssq asiagyktvl laaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgalvea fdirpavkee vqslgakfve iklteettaa ggyakeised
      241 skkrtqevva ehvkhsdivi ttaqvpgrka pilvtedmvk gmkpgsvivd laaeqggnca
      301 ctapgkdivy hgvtiigpin lpssmpvhas qlyaknvtal mqlvvkdkal ninfaddivd
      361 aacithngei rnqrikdalq avpv
//
LOCUS       WP_115565348             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pontibacter diazotrophicus].
ACCESSION   WP_115565348
VERSION     WP_115565348.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter diazotrophicus
  ORGANISM  Pontibacter diazotrophicus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pontibacter diazotrophicus"
                     /db_xref="taxon:1400979"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39814
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mniavlkesk aserrvaltp dvvkslskag fkcgieseag vasgfynkay eaagglifpd
       61 raallgdadv llkvnaptad elqllrdgsa lisflyaytv pelvdlclrk kisafamdav
      121 prisraqkmd alssqanlgg ykavllgana lgkifplmmt aagtitparv lifgagvagl
      181 qavatakrlg avvevtdvrp etkeqveslg grflevqaeg vkteggyase vsaeylqkqk
      241 elvsrhvada divittalvi gkkapllvta emvesmkpgs vivdmavesg gncalsefnk
      301 tvikhgvtii gesnlpamvp vnaselyakn istlllhlat negfkwemee evtkgslith
      361 qgelvhpftk eilaktv
//
LOCUS       WP_115578839             293 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Helicobacter anseris].
ACCESSION   WP_115578839
VERSION     WP_115578839.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter anseris
  ORGANISM  Helicobacter anseris
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Helicobacter anseris"
                     /db_xref="taxon:375926"
     Protein         1..293
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34255
     Region          20..156
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
     Region          <235..284
                     /region_name="Abi_C"
                     /note="Abortive infection C-terminus; pfam14355"
                     /db_xref="CDD:433897"
ORIGIN      
        1 mifdnlpsrr kkiengtlyp diyqydevsq klrniivrlf dqsyaknfsh qihtlicdeh
       61 glfqlyklee nacsfsmnyf gdianficlf kneqleifld lltiifhffr ihdqkilqel
      121 nqrmlengfg yqfendtlir idslpmhknv vkptlellqd srfenanvey rqafddcnhr
      181 ryeemfvnlc ksaestikii cdinkfelpk sstlssltet lknnnflpny steslnglak
      241 vlntignirn nngghgtgve krkidqsfit yamhstastl lfllqrqkew esk
//
LOCUS       WP_115581319             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas protegens].
ACCESSION   WP_115581319
VERSION     WP_115581319.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38671
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigna
       61 ndafgaelil kvaapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqsdivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_115589441             503 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Actinobacillus lignieresii].
ACCESSION   WP_115589441
VERSION     WP_115589441.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus lignieresii
  ORGANISM  Actinobacillus lignieresii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Actinobacillus lignieresii"
                     /db_xref="taxon:720"
     gene            1..503
                     /gene="nrfA"
     Protein         1..503
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56123
     Region          1..489
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkrltknlam atiamlgcls saawaeekpa qtpsltdkal kheklgvvve sanhkfaeky
       61 plqynswkat sestdrgsal aadpryvvlw agyafakdyn kprghyyait dvreilrtga
      121 pkdendgpqp macwtckgpd varlieekge rgyfdpkwak ygaeivnsig cadchdttsk
      181 efeegkpalr varphvlral etvgwkfedl dkhgkrtavc anchveyyfk gktdvtfpwd
      241 kgvdvdsiek yydeiqfadw thalskapml ktqhpdfeiw sqgvhgkngv tcidchmpkv
      301 kdkdgkvytd hkignpfdqf datcktcheq sketlekrvk ehkhqvkeam irledqlvka
      361 hfeakaawea gatqeemkdi ltairhaqwr wdysaaghgs hmhapdvmlh viasgidraa
      421 daraqlgvvl akhgvttpva ipdistkeka qkaigldipk dqaakdeflr tvvpqwdaea
      481 rkkgllpaee epkavvapka eak
//
LOCUS       WP_115597786             529 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Corynebacterium amycolatum].
ACCESSION   WP_115597786
VERSION     WP_115597786.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium amycolatum
  ORGANISM  Corynebacterium amycolatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Corynebacterium amycolatum"
                     /db_xref="taxon:43765"
     Protein         1..529
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54557
     Region          1..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigiplepd pqqtivaatp etvgklvklg yevavqadag laakftdady estgativde
       61 svwhsdivvt ldtppeqfra llndgamlis rlapgrneel veelaqrnit alamdavpri
      121 sraqsmdvls smaniggyra vveaaaaygr lftgqvtaag kmppatvyvi gagvgglaai
      181 gtansmgaiv katdlrpeag eqvesmgaef ipipaateks edgyakemtn dqaaaaakly
      241 seqsaqadiv ittanipgrr spllltaadv aamkpgsviv dmaaagggnc evtvpgktiv
      301 tdngvtiigy tdlagrlpaq asslygqnif nlfklitpek dgspvlnled eiirgitvtk
      361 arpqngagat gaeilwpppp ikvavtpaap lqeqqaqqaa leenapekvs fmgsglgski
      421 algltallai vvmlsaphsv sanfmvltla ivlgfyvisa vtprlhtplm setnaisgiv
      481 lvgailqvgs snllvsglaf aaivvssini fggfavtdrm lgmfvkeea
//
LOCUS       WP_115611999             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cardiobacterium valvarum].
ACCESSION   WP_115611999
VERSION     WP_115611999.1
KEYWORDS    RefSeq.
SOURCE      Cardiobacterium valvarum
  ORGANISM  Cardiobacterium valvarum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cardiobacteriales; Cardiobacteriaceae; Cardiobacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Cardiobacterium valvarum"
                     /db_xref="taxon:194702"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53222
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mnigipkesl agetrvactp atvtqlqklg favvvergag agasladeay aaagasladt
       61 aevwqcpliy kvnapsdaev srlsagqtlv sflwpaqnpd lvqkladkkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvli igagvaglaa
      181 igtanslgai vkafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvasmkpgs vivdlaaatg gncevtkpge
      301 lfitdngvkv igftdmanrl agqssqlyat nlvnlaklls pnkdgeitld fddviirnmt
      361 vckdgsitfp pppiqvsaap qqaksaapvq eeakptpfwk klapavigaa lilwvgavap
      421 aaflnhfivf vlacvigyyv vwnvshslht plmsvtnais giivvgallq igqgngfvst
      481 lafiavlias inifggfyvt rrmlnmfrkg
//
LOCUS       WP_115607737             501 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Actinobacillus ureae].
ACCESSION   WP_115607737
VERSION     WP_115607737.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus ureae
  ORGANISM  Actinobacillus ureae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Actinobacillus ureae"
                     /db_xref="taxon:723"
     gene            1..501
                     /gene="nrfA"
     Protein         1..501
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56009
     Region          1..486
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkrltkklam atiamlgcls ssvwaeeaks psltdkalkh eklgvvvesa nhkfaekypl
       61 qynswkatse stdrgsalev dpryvvlwag ylfsaeynkp rghyyavtdv reilrtgapk
      121 dendgpqpma cwtckgpdvp rlieekgerg yfdpkwakyg aeivnsigca dchdtkskef
      181 eegkpalrva rphvlralet vgwkfedldk hgkrvavcan chveyyfkgk tdvtfpwdkg
      241 vdvasiekyy deiefadwth alskapmlka qhpdfevwsq gvhgkngvtc idchmpkvkd
      301 kdgkvytdhk ignpfdqfdv tcktcheqsk etlekrvkeh khqvkeamir ledqlvkahf
      361 eakaawdaga tqeemkdilt airhaqwrwd ysaaghgshm hapdamlhvi atgidraada
      421 raklgvvlak hgvttpvaip distrekaqk aiglnmpkle tdkaeflrtv vpqwdaeark
      481 kgllpaveep naiaapkaea k
//
LOCUS       WP_115651780             425 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Brucella
            abortus].
ACCESSION   WP_115651780
VERSION     WP_115651780.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..425
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43993
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlyipke sdpsetrvag saetvkkfia lgfdvvvekg ageksripda efaaagarig
       61 tavdaktadv ilkvrrpgda elkayksgaa lfamldpygh edavaalara gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskdyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vskemvasmr pgsvlvdlav erggnvegav
      301 pgeiadvngv kivgylnvpg riaasasqly arnliafvet lvdkeskvlk idpeeglvka
      361 tllthqgril hpafakaeta paavtekaek pkaapkaaak pakkapakaa kkpsspkspv
      421 dggea
//
LOCUS       WP_115661211             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_115661211
VERSION     WP_115661211.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38929
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr ageirvaatp etvkkyvaqg hkvvvqagag lsasqpdsay eavgatigsa
       61 adalgaqlvl kvrapeaael aqmkpgavlv gmlnpfdten narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vidkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_115662015             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_115662015
VERSION     WP_115662015.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38799
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr ageirvaatp etvkkyvaqg hkvvvqagag lsasqpdsay eavgatigsa
       61 adalgaqlvl kvrapeaael aqmkpgavlv gmlnpfdten narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vidkdgqftl nleddivaac
      361 lmtrreeaal ag
//
LOCUS       WP_115660362             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Grimontia
            hollisae].
ACCESSION   WP_115660362
VERSION     WP_115660362.1
KEYWORDS    RefSeq.
SOURCE      Grimontia hollisae
  ORGANISM  Grimontia hollisae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Grimontia.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Grimontia hollisae"
                     /db_xref="taxon:673"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54794
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil ahetrvaatp ktveqllkmg fevvvekdag alasfdnaaf eqagakvvdv
       61 davwqsdiif kvnaphkdea tgineidrik egatlisfiw paqnealmqd lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvfvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaeflqv afeeqagsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgrpap klvtkemvds mkpgsvivdl aaanggncey
      301 teadkvvvtd ngvkvigytd mvgrlptqss qlygtnlvnl mkllckekdg ninidfddvv
      361 lrgvtvvkdg eitwpappiq vsaqpqakaq pkpvkeekve epvspvkkla alivgvgafg
      421 wvasvappaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvsflaf iavliasini fggftvtkrm lemfrkd
//
LOCUS       WP_115664035             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_115664035
VERSION     WP_115664035.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54076
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvkellk lgyqvvvetg agleasfsdd dyraagaaiv
       61 daaslwasvd vvakvrppqv hpslgveeaa llkkhatlig fvwpaqqmpm lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyarems
      241 pafieaemrl faeqarevdi iittalipgk paprlleagt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpgk dgqlvvnmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevpvaaea apprrrtgtt lialalaaaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_115667028             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_115667028
VERSION     WP_115667028.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38735
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetr agearvaatp etvkkyvaqg hqvvvqagag lrasqpdsay eaagatigta
       61 sdalsaplvl kvrapeaael aqmqpgavlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vidkdgqftl nleddivaac
      361 lmtrreeaal ag
//
LOCUS       WP_115669980             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paenirhizobium selenitireducens].
ACCESSION   WP_115669980
VERSION     WP_115669980.1
KEYWORDS    RefSeq.
SOURCE      Paenirhizobium selenitireducens
  ORGANISM  Paenirhizobium selenitireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Paenirhizobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Paenirhizobium selenitireducens"
                     /db_xref="taxon:448181"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55386
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigsprelf agearvamtp dsaiqlkklg ydcmiesgag kaagfsdday ravgvevveg
       61 aealyagadv iakvrppetv everlssgkt lvsffypaqn kellerardk ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aqfvylefea tqdgaatggy aapsspefre
      241 kqlakfrela peidivitta lipgrdapkl wladmvasmk pgsvvvdlaa erggncdltv
      301 pdqkivseng vtiigytdfp srmaaqastl ystnirhmmt dltpakdgmi vhnmeddvir
      361 gatvtkdgei typppppkiq aiaaakpkek vkelspeekr akevaafkaq trsqvgllvi
      421 ggllmalvga yapaefmshf ivfvlacfig fsviwnvshs lhtplmavtn aisgivilga
      481 llqigsgnwl vvilaslsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_115681102             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_115681102
VERSION     WP_115681102.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38961
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvvvqagag lnasqpdsay eavgatigsa
       61 adalgaqmvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra iqadivitta lipgrkapvl lqeatvqqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vvdkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_115678542             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus neocaledonicus].
ACCESSION   WP_115678542
VERSION     WP_115678542.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus neocaledonicus
  ORGANISM  Cupriavidus neocaledonicus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Cupriavidus neocaledonicus"
                     /db_xref="taxon:1040979"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38705
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetr agearvaatp etvkkyvaqg hkvvvqagag lnasqpdsay eavgatigsa
       61 adalgaqlvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgarf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilvghtnlas mvaadasaly arnvldffkl iidkdgqlvi nkeddivaac
      361 lmtrrdeqav a
//
LOCUS       WP_115682445             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_115682445
VERSION     WP_115682445.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38666
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetr agearvaatp etvkkyvaqg hkvvvqagag lnasqpdsay eavgatigsa
       61 adalgaqmvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lqeatvrqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vvdkdgqftl nleddivaac
      361 lmtgrkqaal ag
//
LOCUS       WP_115682705             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_115682705
VERSION     WP_115682705.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53976
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvkellk lgyqvvvetg agleasfsdd dyraagaaiv
       61 daaslwasvd vvvkvrppqv hpslgveeaa llkkhatlig fvwpaqqmpm lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyakems
      241 pafieaemrl faeqarevdi iittalipgk paprlleagt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpgk dgqlvvdmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paavpapaea apprsrtgtt lialalavaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_115687240             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_115687240
VERSION     WP_115687240.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38705
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetr agearvaatp etvkkyvaqg hqvvvqagag lrasqpdsay eaagatigta
       61 adalsaplvl kvrapeaael aqmqpgavlv gmlnpfdaen narmsaanit afaleaaprs
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vidkdgqftl nleddivaac
      361 lmtrreeaal ag
//
LOCUS       WP_115688002             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_115688002
VERSION     WP_115688002.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38917
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvvvqagag lsasqpdsay eavgatigsa
       61 adalgaqlvl kvrapeaael aqmkpgavlv gmlnpfdten narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vidkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_115693569             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudolabrys taiwanensis].
ACCESSION   WP_115693569
VERSION     WP_115693569.1
KEYWORDS    RefSeq.
SOURCE      Pseudolabrys taiwanensis
  ORGANISM  Pseudolabrys taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Xanthobacteraceae; Pseudolabrys.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Pseudolabrys taiwanensis"
                     /db_xref="taxon:331696"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39167
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavaresd lyegrvaatp etvkkfmalg atvavargag vasgvtdady eaagatisdt
       61 paadadivlk vrrptaeeva gykrgalvia imdpygndaa lktladagls afamelmpri
      121 traqsmdvls sqanlagyra vidaaaeygr alpmmmtaag tvpaakvfim gvgvaglqai
      181 atarrlgavv satdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpaprlvta emvasmrpgs vlvdlaverg gnvegaqagq
      301 vavvngvkiv gylnvpgrla asasalyakn lltfvetlid kkekklavnw ddelvkatll
      361 trdgavvhpn flpktaa
//
LOCUS       WP_115702153             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            sainthelensi].
ACCESSION   WP_115702153
VERSION     WP_115702153.1
KEYWORDS    RefSeq.
SOURCE      Legionella sainthelensi
  ORGANISM  Legionella sainthelensi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Legionella sainthelensi"
                     /db_xref="taxon:28087"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40644
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miiatlhaag netrvaitpn sakqfiksgf evkieknagl aagfrdqdye qvgvtisdsk
       61 kniltkanil lcinepnpee leglsqgaiv ighidndphs qliswckekq itllsmnlip
      121 risraqsmds lssqanlagy ravleastqf hraipmmmta agmiqpakvl vlgagvaglq
      181 aiatakrlga vvyafdvrra akeqveslga efievsqeqd setkggyase vseeykklqa
      241 elidqyakls divistalip grkapillyk htieqmkpga ivvdlatsrg gncevsvidk
      301 tikhgeitii gfsnlaglvp ataselyann lvhlihllas tppeitlnpn deiiqqavlc
      361 hqnqylpfqv iketqna
//
LOCUS       WP_115707880             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            sainthelensi].
ACCESSION   WP_115707880
VERSION     WP_115707880.1
KEYWORDS    RefSeq.
SOURCE      Legionella sainthelensi
  ORGANISM  Legionella sainthelensi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Legionella sainthelensi"
                     /db_xref="taxon:28087"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40630
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miiatlhaag netrvaitpn sakqfiksgf evkieknagl aagfrdqdye qvgvtisdsk
       61 kniltkanil lcinepnpee leglsqgaiv ighidndphs qliswckekq itlvsmnlip
      121 risraqsmds lssqanlagy ravleastqf hraipmmmta agmiqpakvl vlgagvaglq
      181 aiatakrlga vvyafdvrra akeqveslga efievsqeqd setkggyase vseeykklqa
      241 elidqyakls divistalip grkapillyk htieqmkpga ivvdlatsrg gncevsvidk
      301 tikhgeitii gfsnlaglvp ataselyann lvhlihllas tppeitlnpn deiiqqavlc
      361 hqnqylpfqv iketqna
//
LOCUS       WP_115713021             519 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Cupriavidus].
ACCESSION   WP_115713021
VERSION     WP_115713021.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54006
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvkellk lgyqvvvetg agleasfsdd dyraagaaiv
       61 daaslwasvd vvvkvrppqv hpslgveeaa llkkhatlig fvwpaqqmpm lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyakems
      241 pafieaemrl faeqarevdi iittalipgk paprlleagt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpgk dgqlvvdmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevpapaea apprsrtgtt lialalaaaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_115719001             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Gallaecimonas mangrovi].
ACCESSION   WP_115719001
VERSION     WP_115719001.1
KEYWORDS    RefSeq.
SOURCE      Gallaecimonas mangrovi
  ORGANISM  Gallaecimonas mangrovi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Gallaecimonadaceae; Gallaecimonas.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Gallaecimonas mangrovi"
                     /db_xref="taxon:2291597"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53459
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipaesl tgenrvaasp ksvaelqklg fsttiesgag kgasfddsay qeagaelgda
       61 wdsdlvfkvn apnddeiarl kpgatlvsfi qpaqnpelie klnkqqvnvl amdmvprisr
      121 aqsldalssm aniagyravv eaanafgrff tgqitaagkv ppakvlviga gvaglaaiga
      181 agslgaqvra fdtrpevkeq iqsmgadfle vqldedegss sdgyakemsq afidaemalf
      241 meqakevdii ittalipgkp apklitrdmv kamkpgsviv dlaapnggnc eltkpgkrsk
      301 sdngvvilgy tdlasrlagq sstlyatnlv nlakllckek dgninidfdd vvlrnmtvvk
      361 egevtfpppa isvsaapkpk pqaqakpnte teeaapkapg rkkyvlaalg llafawvada
      421 apaaflshft vfvlacvvgy yvvwnvthsl htplmsvtna isgiivvgal lqagsggltg
      481 ilaflailva tvnivggftv trrmlkmfqk g
//
LOCUS       WP_115728142             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces culturomici].
ACCESSION   WP_115728142
VERSION     WP_115728142.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces culturomici
  ORGANISM  Actinomyces culturomici
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Actinomyces culturomici"
                     /db_xref="taxon:1926276"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51874
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpsegp aqplvalapq tiglvaklgh evlvergaga sasfpdsaye eagalladad
       61 evwacdavva ldapddalia qmrpgallia rlapqrtpgl aerlaptgit alamdavpri
      121 sraqamdvls sqanvagyra vveaaarfgr vftgqvtaag kmppakvyvi gagvaglaai
      181 gtansmgaqv satdvrpevg eqvesmgasf vplptaqers adgyakamde daaaaanrly
      241 aaqaaksdiv ittanipgra apilldaaav damapgsvvv dmaaanggnc altvpgevvt
      301 tpggvtivgy edfaarlpaq ssqlygrnva nllalltpnk dgeivldfdd vivrgiavas
      361 qgeamwpppp iavsaapssp epspeevaaq arakeearar skrrmllgga iavlalaalv
      421 latpaaatgh yivlllavil gfyvisnvtp alhtplmsvt naisgiilig aisqigdphp
      481 aiagaafvai vlasinifgg favthrmlam frk
//
LOCUS       WP_115730838             453 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aminobacter aminovorans].
ACCESSION   WP_115730838
VERSION     WP_115730838.1
KEYWORDS    RefSeq.
SOURCE      Aminobacter aminovorans
  ORGANISM  Aminobacter aminovorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Aminobacter.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Aminobacter aminovorans"
                     /db_xref="taxon:83263"
     Protein         1..453
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46391
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtifipre ldeiesrvga spdtvkrlvg lgfavvvetg agtlsripda dyaavgavig
       61 kagdaskadv vlkvrrpsea evkgykpgaa vlatmdpygn eagvaamaka gvtafamefm
      121 pritraqvmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrmg aivtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegaq
      301 agkvvttang vkivghlnvp grvaasasll yaknlfafle tmvdkaakqi vinrddelvk
      361 atmltdggki vhpnfanaaa aaavekpkpi vagqnrgddp atdsaapaka epkkpaaana
      421 dkpaakkpaa kksvekkpve kaaakksskq gda
//
LOCUS       WP_115734584             453 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aminobacter aminovorans].
ACCESSION   WP_115734584
VERSION     WP_115734584.1
KEYWORDS    RefSeq.
SOURCE      Aminobacter aminovorans
  ORGANISM  Aminobacter aminovorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Aminobacter.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Aminobacter aminovorans"
                     /db_xref="taxon:83263"
     Protein         1..453
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46482
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msgtifipre ldeiesrvga spdtvkrlvg lgfevvvetg agtlsripda dyaavgavig
       61 kagdaskadv vlkvrrpsea evkgykpgaa vlatmdpygn eagvaamaka gvtafamefm
      121 pritraqvmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrmg aivtatdvrp avkeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegaq
      301 agkvvttang vkivghlnvp grvaasasll yaknlfafle tmvdktakqi vinrddelvk
      361 atmltdggki vhpnfanaaa aaavdkpkpv vagqnrgddp atdsaapaka epkkpaeaka
      421 dkpaakkpaa kksvekkpve kaaaqksskq gda
//
LOCUS       WP_115745922             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. CB09001].
ACCESSION   WP_115745922
VERSION     WP_115745922.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. CB09001
  ORGANISM  Streptomyces sp. CB09001
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces sp. CB09001"
                     /db_xref="taxon:2083284"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53436
     Region          13..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtghqpahhp prrvgvvaes lpgetrvaat pstvrlllgl gyevvvesga gaasgfgdea
       61 yaeagasvge awaadvvlkv daptadetaa lregttlval lapaqrpell dalsargvta
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvrslggeyl avdvaqeesa dgyakatsad
      241 ydraaarlyh eqardvdvvi ttalipgrpa prlltaadva amrpgsvvvd maaahggnve
      301 gtvagrtvvt angvtligyt dlaarlpaqa sqlfgtnlvn llrlltpgkd grividfddv
      361 vqrtvtvvra gtvtwppppv pvsaappata paaasadapv ggkprrptpa grfgpiglgm
      421 latfllvafa paqlaqnftv falavvigyy vigkvhhslh tplmsvtnai sgivvigalv
      481 qighestlvt vlsfvaillt svnifggfav trrmlsmfsr gesr
//
LOCUS       WP_115746040             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. CB09001].
ACCESSION   WP_115746040
VERSION     WP_115746040.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. CB09001
  ORGANISM  Streptomyces sp. CB09001
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Streptomyces sp. CB09001"
                     /db_xref="taxon:2083284"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52014
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvtsetr pgetrvaatp vtvrqltglg hdvvvesgag slsgfadqay veaganigtv
       61 veawgadvvl rvngptvget awlrpgtyia glmapaqspe llealakrdi talamdavpr
      121 israqsldvl ssmaniagyr avieaahrfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgav vratdprpev adqvaslggt ylpveaqteq stdgyakats eaydaaaarl
      241 ysdqaadvdi iittalipgr paprlltaad vaamkpgsvi vdmaasnggn vdgsvagevv
      301 ttangvtiig ytdlagrlpa qasqlygtnl vnllklltpn kdgkvvldle dvvqrgltvt
      361 nagevlwppp pvkvsaapaa qaaapptear aerepmsaar ktslvvaglv afyfvnayap
      421 apipdhfsvl slsvvigyyv igkvahalht plmsmtnais gvivagaliq vgldntviei
      481 lagvaillas inifggfavt rrmlsmfskg a
//
LOCUS       WP_115757425             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            thiocyanatus].
ACCESSION   WP_115757425
VERSION     WP_115757425.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus thiocyanatus
  ORGANISM  Paracoccus thiocyanatus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus thiocyanatus"
                     /db_xref="taxon:34006"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55152
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkeny egearvavtp ssaghlkklg hevfvesgag vgagfsdaay qaagvtvlpg
       61 aavligdvdv vvkvrppaea elrqmrrgqv lishfwpaqn adllelareq gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaavslg aqvhafdvrp evaeqiesmg aefvyldfae taqdgaatgg yaapsspefr
      241 ekqlekfrel apemdivitt alipgrdapk lwtadmveam ktgsvivdla aerggncelt
      301 vpderivten gvvvigytdf psrmgaqase lygnnirhml sdltpgkdgv lvqnmeddvi
      361 rgatvahdgd vtwpppppkv aaiaaqkpre kvkeptpeer rakeiadfra qtrsqvtllv
      421 ggavamllvg lfapasflsh fivfvlavfv gfqviwnvsh slhtplmait naissiiivg
      481 allqigsggg lvvvlaalsv lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_115769356             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_115769356
VERSION     WP_115769356.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53476
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqws wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_115769567             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_115769567
VERSION     WP_115769567.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53632
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta tpakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchnttspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_115781868             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia caffeinilytica].
ACCESSION   WP_115781868
VERSION     WP_115781868.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caffeinilytica
  ORGANISM  Paraburkholderia caffeinilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia caffeinilytica"
                     /db_xref="taxon:1761016"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39466
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvrkyvtqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatlv gmldpfnaen alklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswla
      241 rqsalvhera kqadvvista lipgraaptl isvetvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvtrhgvqi vgytnlasmv padasslyar nlldflklii skegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_115776405             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia caffeinilytica].
ACCESSION   WP_115776405
VERSION     WP_115776405.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caffeinilytica
  ORGANISM  Paraburkholderia caffeinilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia caffeinilytica"
                     /db_xref="taxon:1761016"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39736
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaesr agetrvagtp etvkkltaqg htvlvqstag erahfpdsay aqagatlves
       61 aeafaadlvl kvqtptetel qhmkrdamlv gmlnpfdvdq variraagls afalesiprt
      121 traqsmdvls sqaniagyka vllaaslypr flpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpcetdee rdaaqgvggy arpmpaswia
      241 rqsalvhera kladivitta lipgrtaptl lneetvremk pgsvivdlaa gkgasvgdrr
      301 ggncpltead avvlrhgvhi agytnlpamv atdasslyar nvfdflklii dtngnpkidt
      361 gddivaatll ghdasmlkta
//
LOCUS       WP_115788929             391 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter silvisoli].
ACCESSION   WP_115788929
VERSION     WP_115788929.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter silvisoli
  ORGANISM  Arthrobacter silvisoli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Arthrobacter silvisoli"
                     /db_xref="taxon:2291022"
     Protein         1..391
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40113
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiarerr egerrvaatp dtvkqlaglg vevlvesgag lhsghpdeay kdagawivke
       61 ldfgtvdlll hvrpldldsa kslkqgavtv glaspsselp tvralaetgv tsfalelvpr
      121 israqsmdal tsqalvagyr cvleaamrlp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandirpas adevasmggt firldvetae asggyarels adrgalqrel
      241 laphvaaadv littaavpgr rapllvtram vqamrpgsvv vdlaaesggn vegvvagedt
      301 aiptadgrgt vtlvgmkdpa salpadasrl yaknvanlve llvkegafap dwedevvags
      361 clthdggvrh aptaealaal ttadsatega n
//
LOCUS       WP_115834834             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylovirgula ligni].
ACCESSION   WP_115834834
VERSION     WP_115834834.1
KEYWORDS    RefSeq.
SOURCE      Methylovirgula ligni
  ORGANISM  Methylovirgula ligni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Beijerinckiaceae; Methylovirgula.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Methylovirgula ligni"
                     /db_xref="taxon:569860"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39154
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaetd paearvaatp etvkkfiglg asvtvesgag lkssfldady saagatiaqg
       61 paatladadi ilrvrrpags elagakkgal llaildpygh vdalqqlada gvdafamelt
      121 pritraqvmd vlssqanlag yravidaaae ygravpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrig aivtatdvrp atkeqveslg akfiavedee fkqaetaggy akemsaayqe
      241 kqkaltashi akqdivitta lipgrpapkl itedmiaamr pgsvivdlaa erggntaltr
      301 pgekfvtgng vtilgylnia grlaatassl yarnllafad afidktnktl avnwddeivk
      361 atlltkdgal vhpnfqkpa
//
LOCUS       WP_115838030             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Winogradskyella sediminis].
ACCESSION   WP_115838030
VERSION     WP_115838030.1
KEYWORDS    RefSeq.
SOURCE      Winogradskyella sediminis
  ORGANISM  Winogradskyella sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Winogradskyella.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Winogradskyella sediminis"
                     /db_xref="taxon:1382466"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35891
     Region          5..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifdlfskr qkrlrgefpe iytydnipqh lrvqiihiik daigirkhgh edkpeeaydf
       61 ihqtlcreyg ifslgdrysk ndedhvlnfl lstedtekai dvielsfkfi driikqsfde
      121 yewnteikik pdeaieelne rfkehgigys fdgseiirvd stythaeitk ptisllwnnk
      181 fdganeeylk ahehyrhgrn keclteclka festmkiics ekgwtykqtd taktliqicf
      241 knqlvptftq nqftslknll esgiptirnk lgghgqgqtp qivdnemtry glnltgtnii
      301 flieqsgik
//
LOCUS       WP_115850359             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thermasporomyces composti].
ACCESSION   WP_115850359
VERSION     WP_115850359.1
KEYWORDS    RefSeq.
SOURCE      Thermasporomyces composti
  ORGANISM  Thermasporomyces composti
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Thermasporomyces.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Thermasporomyces composti"
                     /db_xref="taxon:696763"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39904
     Region          1..358
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,71,90,284,310,312)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,274..275,317..318,322,
                     325..326)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,224,235,
                     252..254,261,263)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlrerr pgerrvamlp efvprllstg vevvvetdag aemgipdeay rdagarvldd
       61 vfdadvvvsv qpinlatara laegtvtisf lptrqelplv rrmrerklts fsmdlvprts
      121 raqpmdavts qsmvagyraa ivaaerlprf fpllmtaagt vepatvlvlg agvaglqaia
      181 tarrlganvq aydvrraaae evaslgarfl dlglpplege ggyaremtee rslrqrella
      241 pyvadadvli ttaavpgrpa pllvtsemve amrpgsvvvd lvadqggnva gsvpgqelsv
      301 ngvliwggqn vpsqlpmqas rlysqnilnm lmlllrdgel rldfddeila sacvthagev
      361 rhrptaelip evg
//
LOCUS       WP_115853852             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Kushneria
            indalinina].
ACCESSION   WP_115853852
VERSION     WP_115853852.1
KEYWORDS    RefSeq.
SOURCE      Kushneria indalinina
  ORGANISM  Kushneria indalinina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Kushneria.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Kushneria indalinina"
                     /db_xref="taxon:184067"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55719
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapresa rgearvaltp esakqlqklg heclvetgag aeagfnddty reagvtvvds
       61 aaalwrdaev vikvrepnde eaerlrngqt liaffwpaqn eamlekcrat gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfdn aqdgsesggy aspsspefre
      241 kqlecfreqa sdvdivitta lipgrpapkl wledmvalmk pgsvvidlaa ekggncdltr
      301 adervvsdng vvvvgytdyp srmatqasll yatnirhmlt dltpdkdgvi qhnmeddvir
      361 gatvthqsei tfpppppktr aigaakpkpk ekeatpeekr asetaafksq tkrqvtllav
      421 ggalmlllgq vapasfmqhf ivfvlacfig fqviwkvshs lhtplmavtn aisgiiilga
      481 vlqigsgsvi vsilaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_115871804             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cutibacterium acnes].
ACCESSION   WP_115871804
VERSION     WP_115871804.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53884
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgenrvaatp ttvpallklg yevvveagag ehaaqpdray eeagarivep
       61 geawkadlvl avneptddqi slmragavlv tflhprqdla lteklaaagv tglsmdmvpr
      121 israqsmdal ssmanisgyr avveaafayg rtfggqvtaa gkvppakvfv igtgvaglaa
      181 lgaansmgae vyatdvrpet aeqvqsigat flhvrtgdsd qgvssdgyak etsddynara
      241 aelymeqagk ddviittaai pgkpspklit aemvyamkpg svivdlaalg ggnceltrpg
      301 esyvtdngvt iigytdlpsr lpgqasqlyg tnlvnllkla tpekngelvl nfddevirtm
      361 tvchegqvaf ppppvqvaaa pkpvakaeia sapatpekkp rpwpqtfgiv avlsialial
      421 ltfspmefva lfgtfaiavv vgyyvvwnvt halhtplmsv tnaisgiiiv gaitqlgses
      481 wgirivaalt vliasinifg gftvtqrmlk mfrka
//
LOCUS       WP_115882381             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Lutibacter
            oceani].
ACCESSION   WP_115882381
VERSION     WP_115882381.1
KEYWORDS    RefSeq.
SOURCE      Lutibacter oceani
  ORGANISM  Lutibacter oceani
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lutibacter.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Lutibacter oceani"
                     /db_xref="taxon:1853311"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40459
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigilketq kgekrvaisp niakmliekg fevfveedag sscsfknsdy skvgapirsk
       61 sdifkncdvl ikinpfdnde ieqlkkgqii maqlfhkshp ndmkliaarg atafsmdamp
      121 risraqdmdv lssqsnlagy kavilgayem tkifplmmta agtitpsrvl vygvgvaglq
      181 aiatakrlga vveatdirpe tkeqteslga kfisvdntge ekaeggyaka asedyirrqk
      241 eavnkslfqa dlvittamvp grkspilite dqikqmknga viidlaaaqg gnveisklnk
      301 tvikhgvkii gttispesvs tnasdlygkn mfnfikhltk dnefkwelde eitdetlivy
      361 ngkirkngkt e
//
LOCUS       WP_115930393             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cutibacterium acnes].
ACCESSION   WP_115930393
VERSION     WP_115930393.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53931
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigiprell pgenrvaatp ttvpallklg yevvveagag ehaaqpdray eeagarivep
       61 geawkadlvl avneptddqi slmragavlv tflhprqdla lteklaaagv tglsmdmvpr
      121 israqsmdal ssmanisgyr avveaafayg rtfggqvtaa gkvppakvfv igtgvaglaa
      181 lgaansmgae vyatdvrpet aeqvqsmgat flhvrtgdsd qgvssdgyak etsddynara
      241 aelymeqagk ddviittaai pgkpspklit aemvyamkpg svivdlaalg ggnceltrpg
      301 esyvtdngvt iigytdlpsr lpgqasqlyg tnlvnllkla tpekngelvl nfddevirtm
      361 tvchegqvaf ppppvqvaaa pkpvakaeia sapatpekkp rpwpqtfgiv avlsialial
      421 ltfspmefva lfgtfaiavv vgyyvvwnvt halhtplmsv tnaisgiiiv gaitqlgses
      481 wgirivaalt vliasinifg gftvtqrmlm mfrka
//
LOCUS       WP_115933629             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_115933629
VERSION     WP_115933629.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53562
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gysfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_115938596             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cutibacterium namnetense].
ACCESSION   WP_115938596
VERSION     WP_115938596.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium namnetense
  ORGANISM  Cutibacterium namnetense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Cutibacterium namnetense"
                     /db_xref="taxon:1574624"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53675
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgenrvaatp ttvpallklg yevvvesgag ehaaqpdray eaagarivep
       61 geawkadlvl avnepsddqi almragavlv tflhprqdla lteklaaagv tglsmdmvpr
      121 israqsmdal ssmanisgyr avveaafayg rtfggqvtaa gkvppakvfv igtgvaglaa
      181 lgaansmgae vyatdvrpet aeqvqsmgat flhvrtgdsd qgvssdgyak etsddynara
      241 aelyleqagk ddviittaai pgkpspklit aemvaamkpg svivdlaalg ggncelthpg
      301 esyvtdngvt iigytdlpsr lpgqasqlyg tnlvnllkla tpekngelvl nfddevirtm
      361 tvchegqvaf ppppvqvaaa pkpvakaeta sapatpekkp rpwpqtfgiv avlsialial
      421 ltfspmefva lfgtfaiavv vgyyvvwnvt halhtplmsv tnaisgiiiv gaitqlgses
      481 wgirivaavt vliasinifg gftvtqrmlk mfrka
//
LOCUS       WP_115939830             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_115939830
VERSION     WP_115939830.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53690
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta tpakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnylsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdisikeka qkaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_115947155             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cutibacterium acnes].
ACCESSION   WP_115947155
VERSION     WP_115947155.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium acnes (Propionibacterium acnes)
  ORGANISM  Cutibacterium acnes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Cutibacterium acnes"
                     /db_xref="taxon:1747"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53833
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgenrvaatp ttvpallklg yevvveagag ehaaqpdray eeagarivep
       61 geawkadlvl avneptddqi slmcagavlv tflhprqdla lteklaaagv tglsmdmvpr
      121 israqsmdal ssmanisgyr avveaafayg rtfggqvtaa gkvppakvfv igtgvaglaa
      181 lgaansmgae vyatdvrpet aeqvqsmgat flhvrtgdsd qgvssdgyak etsddynara
      241 aelymeqagk ddviittaai pgkpspklit aemvhamkpg svivdlaalg ggnceltrpg
      301 esyvtdngvt iigytdlpsr lpgqasqlyg tnlvnllkla tpekngelvl nfddevirtm
      361 tvchegqvaf ppppvqvaaa pkpvakaeaa svpaipekqp rpwpqtfgiv avlsialiav
      421 ltfspmefva lfgtfaiavv vgyyvvwnvt halhtplmsv tnaisgiiiv gaitqlgsel
      481 wgirivaalt vliasinifg gftvtqrmlk mfrka
//
LOCUS       WP_115977082             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. 3212.3].
ACCESSION   WP_115977082
VERSION     WP_115977082.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 3212.3
  ORGANISM  Streptomyces sp. 3212.3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Streptomyces sp. 3212.3"
                     /db_xref="taxon:1938846"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53204
     Region          8..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mldsppqqvg vvteataget rvaatpdsvr rllslgyevv vepgagaasg fsddayneag
       61 arvgdawqad vvlkvnapsh eeiqklrdga vligliapah npglvdelae rsitvlsmda
      121 vprisraqsm dvlssmania gyravieaah vfgrfftgqv taagkvppak vlvagagvag
      181 laaigaagsl gavvratdpr aevaeqvrsm ggeflaveve qevssdgyak atseaydrra
      241 aeiyseqard vdiiittali pgrpaprlit aadvasmkpg svivdmaaaq ggnvegtvsg
      301 kaivtdndvt iigytdlagr lpaqasqlyg tnlvnllrll tpgkdgrltl dfddvvqrsv
      361 tvvregektw ppppvevsaa parripappa aspqikearl sppvryglig lgmlamflli
      421 afspaqlvgn ftvfalavvi gyyvigkvhh alhtplmsvt naisgivvvg allqighagl
      481 avsvlsfvai mlttvnifgg favtrrmlgm fskg
//
LOCUS       WP_116000720             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassotalea euphylliae].
ACCESSION   WP_116000720
VERSION     WP_116000720.1
KEYWORDS    RefSeq.
SOURCE      Thalassotalea euphylliae
  ORGANISM  Thalassotalea euphylliae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Thalassotalea.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Thalassotalea euphylliae"
                     /db_xref="taxon:1655234"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54500
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipkesl kgenrvaatp tsvkalkqrg fevaieklag kkasfhdsdy veqgatlvsq
       61 ddvwqsdiif kvnpptddei glmkegahlv sfiqpaqnse lveklkqkni ttiamdmvpr
      121 mtrsqsldal ssmaniagyr avveashqfg rfftgqitaa gnlppakvmi igagvaglaa
      181 igaagslgav vrafdtrpev keqiesmgae fleldfeeed tgsgdgyakv mskafieaem
      241 alfaeqakev diiittamip gkpapklite emvesmkpgs vivdlaaagg gnceltqpgk
      301 lttvkgvkii gytdlvsrlp nqssqlyann lvnltklicp ekdgelvidf edqvirnmlv
      361 vhdgevtfpp ppiqvsaapa akpepakpva aveeveeeks pakkyammav aglvfgwvas
      421 vapsdflahf tvfvlacvvg yhvvwnvtha lhtplmsvtn aisgiivvga llqvgsdnlv
      481 vqvlsgiail iatinivggf fvtkrmlkmf qk
//
LOCUS       WP_116005214             535 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Simplicispira].
ACCESSION   WP_116005214
VERSION     WP_116005214.1
KEYWORDS    RefSeq.
SOURCE      unclassified Simplicispira
  ORGANISM  unclassified Simplicispira
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Simplicispira.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="unclassified Simplicispira"
                     /db_xref="taxon:2630407"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55585
     Region          11..535
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtsptppvq rigvpretfh gekrvatvpd vveklvklgf kvavesgagd aahfsddtyr
       61 avgaevlpda salwaasdiv lkvrppssde vtlmreggtl igfvwpaqnp elmqqltakk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaaslg aivrandtra evadqvkslg gefvkvdyee dgaggggyak
      241 vmsegfqaaq rqmyatqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eaverhgvti igytdlasrl akqsstlyat nllrlveelc kakdgvavvn
      361 meddairglt vtkdgaitwp apalkpvavp aapakpaaav vvkakgghgq saepasvksa
      421 aalfvfgall fwliganapk eflghftvfv lgcfvgymvv wnvkpalhtp lmsvtnaiss
      481 iivigalvqi spvaaavnrp ndaitwlaaa givltainmf ggfavtqrml amfrk
//
LOCUS       WP_116008530             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassotalea euphylliae].
ACCESSION   WP_116008530
VERSION     WP_116008530.1
KEYWORDS    RefSeq.
SOURCE      Thalassotalea euphylliae
  ORGANISM  Thalassotalea euphylliae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Thalassotalea.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Thalassotalea euphylliae"
                     /db_xref="taxon:1655234"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54486
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipkesl kgenrvaatp tsvkalkqrg fevaieklag kkasfhdsdy veqgatlvsq
       61 ddvwqsdiif kvnpptddei dlmkegahlv sfiqpaqnse lveklkqkni ttiamdmvpr
      121 mtrsqsldal ssmaniagyr avveashqfg rfftgqitaa gnlppakvmi igagvaglaa
      181 igaagslgav vrafdtrpev keqiesmgae fleldfeeed tgsgdgyakv mskafieaem
      241 alfaeqakev diiittamip gkpapklite emvasmkpgs vivdlaaagg gnceltepgk
      301 ltnvkgvkii gytdlvsrlp nqssqlyann lvnltklicp ekdgelaidf edqvirnmlv
      361 vhdgevtfpp ppiqvsaapa akpepakpva aveeveeeks pakkyammav aglvfgwvas
      421 vapsdflahf tvfvlacvvg yhvvwnvtha lhtplmsvtn aisgiivvga llqvgsdnlv
      481 vqvlsgiail iatinivggf fvtkrmlkmf qk
//
LOCUS       WP_116018059             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thalassotalea euphylliae].
ACCESSION   WP_116018059
VERSION     WP_116018059.1
KEYWORDS    RefSeq.
SOURCE      Thalassotalea euphylliae
  ORGANISM  Thalassotalea euphylliae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Thalassotalea.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Thalassotalea euphylliae"
                     /db_xref="taxon:1655234"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54428
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipkesl kgenrvaatp tsvkalkqrg fevaieklag kkasfhdsdy veqgatlvsq
       61 ddvwqsdiif kvnpptddei glmkegahlv sfiqpaqnse lveklkqkni ttiamdmvpr
      121 mtrsqsldal ssmaniagyr avveashqfg rfftgqitaa gnlppakvmi igagvaglaa
      181 igaagslgav vrafdtrpev keqiesmgae fleldfeeed tgsgdgyakv mskafieaem
      241 alfaeqakev diiittamip gkpapklite emvasmkpgs vivdlaaagg gnceltepgk
      301 ltnvkgvkii gytdlvsrlp nqssqlyann lvnltklicp ekdgelaidf edqvirnmlv
      361 vhdgevtfpp ppiqvsaapa akpepakpva aveeveeeks pakkyammav aglvfgwvas
      421 vapsdflahf tvfvlacvvg yhvvwnvtha lhtplmsvtn aisgiivvga llqvgsdnlv
      481 vqvlsgiail iatinivggf fvtkrmlkmf qk
//
LOCUS       WP_116038688             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodohalobacter sp. SW132].
ACCESSION   WP_116038688
VERSION     WP_116038688.1
KEYWORDS    RefSeq.
SOURCE      Rhodohalobacter sp. SW132
  ORGANISM  Rhodohalobacter sp. SW132
            Bacteria; Pseudomonadati; Balneolota; Balneolia; Balneolales;
            Balneolaceae; Rhodohalobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rhodohalobacter sp. SW132"
                     /db_xref="taxon:2293433"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39980
     Region          2..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 migvcketeq nekrvtitpe gvkkltgegq eivvesgagv dssysdeayt eagatiepsr
       61 ekilsecdil lavqapaved lkkmkpgsvl isfiwplqns dyvdvlkeln isglamdtip
      121 risraqsmda lssmsniagy kaallganql dkylpmmmta agtippakvl vlgagvaglq
      181 aiatakrlga vveafdirsa vkeqieslga sfieaeedag edsetkggya keqtesdkek
      241 qqqlvhdhva ksdivittal vpgrpapkli pkamvddmka gsvivdiaae qggnceltka
      301 getvlhngvs imgplnipsm lafhasklys knqlslldll lengkpnfnf ddeiivnatv
      361 thngelispf vkenmq
//
LOCUS       WP_116082503             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tropicimonas sp. IMCC34011].
ACCESSION   WP_116082503
VERSION     WP_116082503.1
KEYWORDS    RefSeq.
SOURCE      Tropicimonas sp. IMCC34011
  ORGANISM  Tropicimonas sp. IMCC34011
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Tropicimonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Tropicimonas sp. IMCC34011"
                     /db_xref="taxon:2248759"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55530
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligtpvetf egekrvamtp ksvediaklg hsclieagag aaagfsdady eaagadvvpd
       61 akalyeeadi iakvqppsda evdmlrsgqt lisffwpvan edlleraser gatiiamdmv
      121 prisraqkmd alssmaniag yravieasan ferfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aivrafdvrp evseqiesmg aeflfldfed sqdssgsggy aapsspefre
      241 kqlelfrqqa pdvdivitta lipnreapel wtedmvkamk pgsvivdlaa ekggnckltq
      301 kdkkivtdng vtiigytdfp srmatqsstl yatnirhmlt dltpekdgtv nqnmeddvir
      361 gatvahagev tfpppppkvk aiaaapkkaa areltpeekk aaeaetfrqq trfqvgllva
      421 ggllmlliga fapasflqhf ivfalacfvg fqviwnvsha lhtplmavtn aisgivilga
      481 llqigssswl vvilafvsvl iatinvvggf lvtrrmlamf qks
//
LOCUS       WP_116100917             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis thermalba].
ACCESSION   WP_116100917
VERSION     WP_116100917.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis thermalba
  ORGANISM  Amycolatopsis thermalba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Amycolatopsis thermalba"
                     /db_xref="taxon:944492"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52199
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mlvgvlkeat pgetrvaatp ataaqllklg yevvvdpgag elasfsdeay aeagasigna
       61 vqaeivlgvn apakeqldal kpgatlisll apalnqelvd dlanrpitam amdavprisr
      121 aqsldvlssm aniagyravv eaahtfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agsldavlra tdprpevadq vkslggeyls ieapdvevsa tgyakemsdd ykarerqlye
      241 eqcrdvdiii ttalipgrpa priitadmva smrpgsvivd maaanggnve gtvagkavtt
      301 dngvtilgyt dlpgrlpaqs sqlygtnlvn lmklvtpgkd gtpvfdlddi virsmtvvrd
      361 gellwppppa pvsaapaqaa pkaaaqepep akkklspaar igltavagal lfllvaaspp
      421 alqghltvfa mavvigfyvi ghvhhalhtp lmsvtnaisg iivvgallqv ghgggvvtwl
      481 afaaillasi nifggfavtr rmlsmfsrs
//
LOCUS       WP_116110138             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis ruanii].
ACCESSION   WP_116110138
VERSION     WP_116110138.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis ruanii
  ORGANISM  Amycolatopsis ruanii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Amycolatopsis ruanii"
                     /db_xref="taxon:944491"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52098
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mlvgvlkeat pgetrvaatp atvaqllklg yevvvdpgag elasfsdeay aeagasigna
       61 vqaeivlgvn apakeqldal kpgatlisll apalnqelvd dlanrpitam amdavprisr
      121 aqsldvlssm aniagyravv eaahtfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgavvra tdprpevadq vkslggeyls ieapdvevsa tgyakemsdd ykarerqlye
      241 eqcrdvdiii ttalipgrpa priitadmva smrpgsvivd maaanggnve gtvagkavtt
      301 dngvtilgyt dlpgrlpaqs sqlygtnlvn lmklvtpgkd gtpvfdlddi vvrsmtvvrd
      361 gellwppppa pvsaapaqaa pkaaaqepep akkklspagr igvtavagal vfllvaaspp
      421 alqghltvfa mavvigfyvi ghvhhalhtp lmsvtnaisg iivvgallqv ghgggvvtwl
      481 afaaillasi nifggfavtr rmlsmfsrs
//
LOCUS       WP_116114513             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Austwickia
            chelonae].
ACCESSION   WP_116114513
VERSION     WP_116114513.1
KEYWORDS    RefSeq.
SOURCE      Austwickia chelonae
  ORGANISM  Austwickia chelonae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermatophilaceae; Austwickia.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Austwickia chelonae"
                     /db_xref="taxon:100225"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53791
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipketn agetrvaatp qtvaqllklg yevtveadag qrsalsdtaf tdsgatistv
       61 edvwsadivi kvnephddel arlcdgatli allaprlnqe lvdklttrki talsmdavpr
      121 israqaldvl ssmaniagyr aiveaahefg rfftgqvtaa gkvppakvfv agagvaglaa
      181 igaanalgai vrandvrpev aeqvesmgae fvhvddpgaq vssdgyakem geeyqrrqaa
      241 myaeqcrdvd iivttalipg rpaprlitae miatmkagsv ivdmaaatgg nvegsvagek
      301 vvtdngvtli gytdlagrlp tqasqlygqn mvnflklatp gkdgelcldm ddivmrgmtv
      361 vkdgelmwpp ppvqvsaapp ptapapevte pappkktspa akaaiftgig alslllfafs
      421 pepflghfmv fmlsvvigyy vignvhhalh tplmsvtnai sgiiivgvll qigrdsspvf
      481 vdvlafigvl lasinifggf tvtqrmlgmf rkd
//
LOCUS       WP_116118988             380 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Paraburkholderia].
ACCESSION   WP_116118988
VERSION     WP_116118988.1
KEYWORDS    RefSeq.
SOURCE      unclassified Paraburkholderia
  ORGANISM  unclassified Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="unclassified Paraburkholderia"
                     /db_xref="taxon:2615204"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39447
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatlv gmldpfnten ssklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvdtvqamk pgsvlvdlaa grgaeyegqr
      301 ggncpltetd kvvikhgvti vgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_116121080             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. BL6669N2].
ACCESSION   WP_116121080
VERSION     WP_116121080.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL6669N2
  ORGANISM  Paraburkholderia sp. BL6669N2
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Paraburkholderia sp. BL6669N2"
                     /db_xref="taxon:1938807"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54989
     Region          5..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlmigiple aaagerrvat vpevveklik lgfsvavqsg agaganfddd ayraagasia
       61 ataaelwsgs divfkvrpps teevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvr slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk liiaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl ygtnllrvve elckgkdgti nvdfdddair
      361 gltvikegkv twppppikqa vvapkpaaaa paaaapaksk ghghggepms akslaivfai
      421 galaflfvgq fapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapplge lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_116132073             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tropicimonas sp. IMCC34043].
ACCESSION   WP_116132073
VERSION     WP_116132073.1
KEYWORDS    RefSeq.
SOURCE      Tropicimonas sp. IMCC34043
  ORGANISM  Tropicimonas sp. IMCC34043
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Tropicimonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Tropicimonas sp. IMCC34043"
                     /db_xref="taxon:2248760"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55261
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspkevf pgearvamtp dsaralqklg ydcaiesgag lgagfsdaty adagvevidg
       61 aealfgavdv vakvrpptea evallrsgqt lisffypvsn ealmeaardk ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvflefee aqdgaatggy aapsspefre
      241 aqlakfrela pemdivitta lipnrpapvl wtkdmveamk pgsvivdlaa erggnceltv
      301 pdekivtdng vtivgytdfp srmaaqsstl ystnirhmmt dltpgkdgqv vhnmeddvir
      361 gatvtfdgdi tfpppppkik aiaaqkpkek pkeltpaerr aeevaafkaq trqqvtllav
      421 galvllaigl vapasfmqhf ivfvlsifig fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsif maginifggf lvtrrmlamf qks
//
LOCUS       WP_116136676             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            diaoshuihuensis].
ACCESSION   WP_116136676
VERSION     WP_116136676.1
KEYWORDS    RefSeq.
SOURCE      Trinickia diaoshuihuensis
  ORGANISM  Trinickia diaoshuihuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Trinickia diaoshuihuensis"
                     /db_xref="taxon:2292265"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39867
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahearvaatp etvkkyvqag hrvtiergag aaasftdday asvgaelvea
       61 daalsadlvl kvqspnetel almkrgavlv gmlepfnadn aarlaqagit afaleaaprt
      121 traqsldvls sqaniagyka vllaadlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetqee rdaaegvggy arpmppswla
      241 rqalqvhera kvadivitta lipgrdaptl lsaetvqamr pgsvivdlaa grgpelaglp
      301 gvrggncplt epdkvvtkhg viivghtnlp amvaadassl yarnlfdflk livtkeglln
      361 idlsddivaa tllardgavt rkaa
//
LOCUS       WP_116173325             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Kutzneria
            buriramensis].
ACCESSION   WP_116173325
VERSION     WP_116173325.1
KEYWORDS    RefSeq.
SOURCE      Kutzneria buriramensis
  ORGANISM  Kutzneria buriramensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Kutzneria.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Kutzneria buriramensis"
                     /db_xref="taxon:1045776"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52451
     Region          6..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mgrtlgvvte saagetrvaa tpatvrqlsa lgyevlvesg agaaasfpde ayaqagaria
       61 drgevwatdv vikvdpptes eigalhegat ligmigpalr pelvealser pitalamdav
      121 prisraqsld vlssmaniag yravieaanv fgrfftgqvt aagkvppakv lvagagvagl
      181 aaiatasslg avvratdpra evaeqvkslg geflavnveq eastdgyaka tseaydkraa
      241 eiyaeqarev diivttalip grpaprlvta aqvatmkpgs vivdmaaaqg gnvegtvage
      301 vvvtangvti igytdlagrl paqasqlygt nvvnllkllt pgkdgeivld fddvvlramt
      361 vvrdgettwp ppkisvsaap pqqqqetpap qqqptqprra rhalvaaaav alfllvgfsp
      421 nelighltvf alsvvigfyv ignvhhalht plmsvtnais givvvgallq lgrgsmvvtv
      481 laaaavllas invfggfavt rrmlrmfsrs
//
LOCUS       WP_116201394             506 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis circi].
ACCESSION   WP_116201394
VERSION     WP_116201394.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis circi
  ORGANISM  Amycolatopsis circi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Amycolatopsis circi"
                     /db_xref="taxon:871959"
     Protein         1..506
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51709
     Region          1..505
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvlkeaq pgetrvaatp etvgklrglg ydvavepgag lasgffdqay adagatsgpv
       61 aeadvvfgvn apssgqldav ksgatvvsll apalkpelve dlakrpital amdavprisr
      121 aqsldvlssm aniagyravv eaahafgrff tgqvtaagkv npakvlvvga gvaglaaiga
      181 agslgaivra tdprpevadq vkslggeyls iedpsaevsa tgyakemged ykarerelya
      241 sqcrevdiiv ttalipgrpa priitgemva smkagsvivd maaanggnve gsvagekivt
      301 dngvtilgyt dlagrlpaqa sqlygtnlvn lmklmtpekd grlvvdfddv vvrsitvvkn
      361 geltwppppv qvsaapqkpa aapvkepekq pmssgrrlgv vlgiaavvlv laalapaall
      421 phltvfalai vigyyvighv hhalhtplms vtnaisgiiv vgallnlvsg ntvvvvlagv
      481 atllatinif ggfavtrrml amfsrs
//
LOCUS       WP_116208283             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraperlucidibaca baekdonensis].
ACCESSION   WP_116208283
VERSION     WP_116208283.1
KEYWORDS    RefSeq.
SOURCE      Paraperlucidibaca baekdonensis
  ORGANISM  Paraperlucidibaca baekdonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Paraperlucidibaca.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Paraperlucidibaca baekdonensis"
                     /db_xref="taxon:748120"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38872
     Region          1..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetq agetrvaatp etvkkfvamg ckvvvqagag vasscidsay eaagasiaat
       61 aadalgnadm vlkvvaptad etalikqgat vlaafaphqn phfdayaakg ltcvamelip
      121 ritraqssdi lssqanvagy kavlmaaney aglfpmmmta agtikpartv vlgvgvaglq
      181 aiatakrlga vveasdlrpa areqveslgg rwldvpmsee eaakalstgg yawqpspeyi
      241 rdqaavvdka vsnanivitt aqipgrkapt lvkaetvakm kpgsiivdma vstggnvegs
      301 qldqtvvtdn gvrivgigni palvateasa lyarnmlnfl apmhnkdtse ivlnreddmv
      361 kptlivdagt vnyqkpn
//
LOCUS       WP_116220910             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            versutus].
ACCESSION   WP_116220910
VERSION     WP_116220910.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus versutus
  ORGANISM  Paracoccus versutus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus versutus"
                     /db_xref="taxon:34007"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55448
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigglkeif egearvaitp ssaghlrklg hdvhvetgag vragfsdaay eaagvtvhpd
       61 aaalvgavev vvkvrppsea elrqmrrgqt lishfypaqn pdllelareq gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigaavslg aqvhafdvrp evaeqiesmg aefvyldfqd qvqdgaatgg yaapsspefr
      241 ekqlekfrel apgmdivitt alipgrdapk lwtrdmvaam ktgsvivdla aerggncelt
      301 vpderivten gvviigytdf psrmgaqase lygnnirhml sdltpgkdgv ivqnmeddvi
      361 rgatvahdgd vtwppppprv aaiaaqkpre kpreptpeer raqeiaafra qtrsqvtllg
      421 agaaamllvg lfapasflsh fivfvlavfv gfqviwnvsh slhtplmait naissiiivg
      481 allqigsggw lvvllaalsv lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_116240525             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium bovistercoris].
ACCESSION   WP_116240525
VERSION     WP_116240525.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium bovistercoris
  ORGANISM  Microbacterium bovistercoris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Microbacterium bovistercoris"
                     /db_xref="taxon:2293570"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52303
     Region          3..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtqlgivrea ggearvaatp atvrtlqglg ytivveqdag aaasypdeay veagativdr
       61 eaawgsgvvl ginapgpeei alladgatvv allspalrpd lvealaqrgi tavaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvtsiggt ylpvdvevae stdgyakats adydrraaei
      241 yteqaadvdi iittalipgr aaprlitaad valmkpgsvi vdmaaaqggn vegsvageri
      301 vtangviilg ytdlasrlaa qasqlygtnv anlvalltpg kdgelaidfd dvvqrsvtvv
      361 rdgevtwppp avqvaaapak paaekdaapa apekkqmstg rkalligigi valflvnlfa
      421 ppplpqhftv lmlavvvgfy vigkvhhalh tplmsvtnai sgvivvgaml qvttanpvvq
      481 vlaavailla sinifggfav trrmlamftk gadk
//
LOCUS       WP_116258419             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium tuberculosis].
ACCESSION   WP_116258419
VERSION     WP_116258419.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37621
     Region          10..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdpqtqstr vgvvaesgpd errvalvpka vaslvnrgva vvveagager allpdelyta
       61 vgasigdawa advvvkvapp taaevgrlrg gqtligflap rnadnsigal tqagvqafal
      121 eaiprisraq vmdalssqan vsgykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwldlg isasgeggya reltdderaq
      241 qqkaleeais gfdvvittal vpgrpaptlv taaaveamkp gsvvvdlage tdgnceltep
      301 grtvvkhdvt iaaplnlpat mpehaselys knitalldll ikdgrlapdf ddeviaqscv
      361 trgkds
//
LOCUS       WP_116274763             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            leguminosarum].
ACCESSION   WP_116274763
VERSION     WP_116274763.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39114
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare itgeetrvaa saetvkkmks fgfdivveag agaasripdg efeaagarig
       61 sfadaasadv vlkvrrpseq eisgyksgav viaimdpygn deaiaalaga glsafamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqg
      241 kqaalvaehi akqdivitta lipgraaprl vsramlaamk pgavavdlav erggniegvv
      301 ageiadvdgv kvigfanmpg rvaasasaly aknlvtflet mvnkesrsvv vnlddelvka
      361 tmltyagdvv hpafggakkg dl
//
LOCUS       WP_116292391             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116292391
VERSION     WP_116292391.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38889
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvvvqagag lsasqpdsay eavgatigsa
       61 adalgaqlvl kvrapeaael aqmkpgavlv gmlnpfdten narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgaggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vidkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_116296069             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116296069
VERSION     WP_116296069.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38888
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvvvqagag lnasqpdgay eavgatigsa
       61 adalgaqmvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra iqadivitta lipgrkapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vvdkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_116296536             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116296536
VERSION     WP_116296536.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54068
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvkellk lgyqvvvetg agleasfsdd dyraagaaiv
       61 daaslwasvd vvvkvrppqv hpslgveeaa llkkhatlig fvwpaqqmsm lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyakems
      241 pafieaemrl faeqarevdi iittalipgk paprlleagt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpdk dgqlvadmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevplpaea apprsrtgtt lialalaaaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_116300426             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Alkalilimnicola ehrlichii].
ACCESSION   WP_116300426
VERSION     WP_116300426.1
KEYWORDS    RefSeq.
SOURCE      Alkalilimnicola ehrlichii
  ORGANISM  Alkalilimnicola ehrlichii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Alkalilimnicola.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Alkalilimnicola ehrlichii"
                     /db_xref="taxon:351052"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39936
     Region          3..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mairvgvpke tapgerrval vpgvlrqlgk lgvevlmekg agiesgfdda dyegvtivds
       61 adqlyaqadv tmkvqppsve eagklkegtv llgflapheg ddrikklcer kissfsmelv
      121 prisraqsid alssqasiag ykavllaatl tgrffpmltt aagtvrpakv lvigagvagl
      181 qaiatarrlg aiveaydvrs atkeqceslg akfvdtgvka egeggyarel tkeeqaqqak
      241 vladhiansd avittaaipg raapkiidka tvermkrgav iidlaaetgg ncevtkpgee
      301 vdhqgvivyg prnvpssvav hasemyarnl ynlltllvqe gelnlnwedq vikdsclthd
      361 gevkheptrs rleggks
//
LOCUS       WP_116304438             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_116304438
VERSION     WP_116304438.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53588
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhaleeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_116313047             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116313047
VERSION     WP_116313047.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38975
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvviqagag lnasqpdsay eavgatigsa
       61 adalgaqmvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra iqadivitta lipgrkapvl lqeatvqqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vvdkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_116318108             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus sp. P-10].
ACCESSION   WP_116318108
VERSION     WP_116318108.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus sp. P-10
  ORGANISM  Cupriavidus sp. P-10
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus sp. P-10"
                     /db_xref="taxon:2027911"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39089
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etikkyvaqg hkvvvqagag vrasqpdgay eavgatigta
       61 aealgaqmvl kvrapddael aqmkpgsvlv gmlnpfdaen narmaaanvt afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra iqadivitta lipgrkapvl lqeatvqqmk pgsvvvdlaa aqggncpltv
      301 adevverhgv ilightnlas mvaadasaly arnvldflkl vvdkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_116321765             520 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Cupriavidus].
ACCESSION   WP_116321765
VERSION     WP_116321765.1
KEYWORDS    RefSeq.
SOURCE      unclassified Cupriavidus
  ORGANISM  unclassified Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="unclassified Cupriavidus"
                     /db_xref="taxon:2640874"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54299
     Region          3..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvkellk lgyqvvvetg agqeasfsdd dyraagaaiv
       61 daaslwasvd vvvkvrppqv hpslgveeaa llkkhatlig fvwpaqqmal lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyakems
      241 pafieaemrl faeqarevdi iittalipgk papkllqpet vglmrsgsvv vdlaaeqggn
      301 cvltvpgesv rrngvtiigy tdlpsrmaaq ssqlyatnir hllteltpgk dgrlvvnmdd
      361 emirgatvqh qgtvtwpppp ltvaipqqqa paasppvqae aapppnrtgv klavlavaai
      421 allalgavap pafmahftvf vlaifvgyqv vwnvtaalht plmsvtnais giivvgalvq
      481 lgkpslltav iagcavlvat iniaggflvt qrmlkmfqrd
//
LOCUS       WP_116325519             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116325519
VERSION     WP_116325519.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54062
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvkellk lgyqvvvetg agleasfsdd dyraagaaiv
       61 daaslwasvd vvakvrppqv hpslgveeaa llkkhatlig fvwpaqqmpm lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyarems
      241 pafieaemrl faeqarevdi vittalipgk paprlleagt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpgk dgqlvvnmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevpvaaea apprrrtgtt lialalaaaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_116329764             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116329764
VERSION     WP_116329764.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40448
     Region          1..382
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,307,333,335)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,140..141,150..151,154..155,158..159,161..162,
                     164..169,171,173..175,178,201..202,297..298,340..341,345,
                     348..349)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(135..136,140,143,146,187..190,210..212,247,258,
                     275..277,284,286)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(137..138,140,150,193..194,201,217..218,220..223)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(170..174,177,180,203,205)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvvvqagag lsasqpdsay eavgatigsa
       61 adalgaqlvl kvrapeaael aqmkpgavlv gmlnpfdten xgavlvgmln pfdtennarm
      121 saanitafal eaaprttraq smdvlssqan iagykavlva ahhyqrfmpm lmtaagtvka
      181 arvlilgagv aglqaiatak rlgavieasd vrpavkeqie slggkfldvp fltdeereia
      241 qgaggyarpm ppdwmkrqae lvhqralqad ivittalipg rkapvllqea tvaqmkpgsv
      301 vvdlaaaqgg ncpltvadqv vnhngvilig htnlasmvaa dasalyarnv ldflklvidk
      361 dgqftlnled divaaclmcr dgqvvreaa
//
LOCUS       WP_116335552             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116335552
VERSION     WP_116335552.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38541
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetr agearvaatp etvkkyvaqg hkvviqagag lgasqpdsay eavgatigsa
       61 adalgaqlvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaaqhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra iqadivitta lipgrkapvl lqeatvqqmk pgsvvvdlaa aqggncpltv
      301 adqvanhngv ilightnlas mvaadasaly arnvldflkl vvdkdgeftl nleddivaac
      361 lmtgrkqaal ag
//
LOCUS       WP_116346373             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116346373
VERSION     WP_116346373.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38813
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvvvqagag lgasqpdgay eavgatigsa
       61 adalgaqlvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra iqadivitta lipgrkapvl lqeatvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vvdkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_116348427             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116348427
VERSION     WP_116348427.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54104
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvrellk lgyqvvvetg agqeasfsdd dyraagaaiv
       61 daaslwasvd vvvkvrppqv hpslgveeaa llkkhatlig fvwpaqqmpm lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gnggyakems
      241 pafieaemrl faeqarevdi iittalipgk paprlleagt valmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpgk dgqlvvdmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevpvpaea apprsrtgtt lvalalaaaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_116358866             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116358866
VERSION     WP_116358866.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53864
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpesvrellk lgyqvvvetg agqeasfsdd dyraagaaiv
       61 daaslwasvd vvakvrppqv hpslgveeaa llkkhatlig fvwpaqqmpm lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveidedgs gsggyarems
      241 pafieaemrl fagqarevdi iittalipgk papklleagt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlyatnic hllseltpgk dgqlvvdmad
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevpvpaea apprsrtgta lvalalaaaa
      421 llalgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_116367981             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Parahaliea
            mediterranea].
ACCESSION   WP_116367981
VERSION     WP_116367981.1
KEYWORDS    RefSeq.
SOURCE      Parahaliea mediterranea
  ORGANISM  Parahaliea mediterranea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Parahaliea.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Parahaliea mediterranea"
                     /db_xref="taxon:651086"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40543
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpketh pgenrvpvip etvkklallg aevviepgmg agsgfsdeqy ieagasvepd
       61 rnklfaeaqv llrlrkptld evalipsgci hisyldpfne helvralqmq gvtaismemi
      121 prttrsqkmd alssqanlag yvtvllaanh lpsilpmmmt pagtlkpakv filgagvagl
      181 qaiatakrlg akvtafdtrp vvaeqvqslg atfleidlgd tgetaggyak eltpeqidrq
      241 rqaqkeviaq sdvvittaqv fgrkppvlvt rdmvegmqpg svivdmaaet ggnvegsvpg
      301 etvevngvki igqanlpnnv crdaskmyss nlfnlvedvw dkeskqfvvd fehdilpgci
      361 ithggevtne tiknilegan
//
LOCUS       WP_116372805             363 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium sp. MFM001].
ACCESSION   WP_116372805
VERSION     WP_116372805.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium sp. MFM001
  ORGANISM  Mycobacterium sp. MFM001
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Mycobacterium sp. MFM001"
                     /db_xref="taxon:2049453"
     Protein         1..363
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37279
     Region          7..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtetqttvgv vaesgaderr valvpkavgp lvksgvgvvv esgagerall pddlyteaga
       61 sigdawaadv vvkvapptad evsrlrngqt ligflaprna dnqiealrqa gvqafaleai
      121 prisraqamd alssqanvag ykavllaase strffpmltt aagtvkpatv lvlgvgvagl
      181 qalatakrlg artsgydvrp evadqvrsvg aqwldvgida sgeggyarel tdeeraqqqk
      241 aleeaitgfd vvittalvpg kpaprlvtaa avqgmkpgsv vvdlageagg nceltepgqt
      301 vvkhdvtiaa plnlpatmpe haselyskni tallellikd gklapdfdde vvaaacvtrg
      361 eds
//
LOCUS       WP_116379178             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116379178
VERSION     WP_116379178.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38931
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigipqetr agetrvaatp etvkkyvaqg hkvvvqagag lnasqpdgay eavgatigsa
       61 adalgaqmvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra iqadivitta lipgrkapvl lqeatvqqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vvdkdgqftl nleddivaac
      361 lmcrdgqvvr eaa
//
LOCUS       WP_116379936             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116379936
VERSION     WP_116379936.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54063
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpnerrvaa tpdsvkellk lgyqvvvetg agleasfsdd dyraagaaiv
       61 daaslwasvd vvvkvrppqv hpslgveeaa llkkhatlig fvwpaqqmpm lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyakems
      241 pafieaemrl faeqarevdi iittalipgk paprlleagt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpgk dgqlvvdmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevpapaea apprsrtgtt lialalaaaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_116380195             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116380195
VERSION     WP_116380195.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38575
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetr agearvaatp etvkkyvaqg hkvviqagag lgasqpdgay eavgatigsa
       61 adalgaqlvl kvrapdaael aqmkpgavlv gmlnpfdaen narmsaanit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lqeatvrqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vvdkdgqftl nleddivaac
      361 lmtgrkqaal ag
//
LOCUS       WP_116384320             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116384320
VERSION     WP_116384320.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38932
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvpveth acesrvaatp etvkkyvaqg hkvvvqvgag vrasqpdsay eaagatigta
       61 adalsadlvl kvrapeitel ahmkpgavlv gmlnpfdaen karmaaagit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfvtdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadivitta lipgrkapvl lheatvqqmk pgsvvvdlaa aqggncpltv
      301 adevverhgv tfvghtklas mvaadasaly arnvldflkl vidkegqftl nleddivaac
      361 lmtrreeaal ag
//
LOCUS       WP_116384343             535 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116384343
VERSION     WP_116384343.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55631
     Region          11..535
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqpnpssapq rigvpretfp geervatvpd vvekliqlgf kvavesgaga aanfsddayr
       61 aagaevidga aqlwatsdiv lkvrppgsde valmrdggml agfiwpaqnp elmqqlatkn
      121 atvlaidclp rtlsraqkmd altsaagvsg yravieaaha fgsyfngqit aagkvpparv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvrslg aefvkvdyde dgsggggyar
      241 vmsegfqaaq rqmyarqaqd adviittalv pgkpapklit aemvrsmkpg svivdmaaeq
      301 ggnceltvpg eavvchgvti igytdlasrl arqsstlyat nllrlteelc ktrdgqaivn
      361 meddairsla vikdgaitwp applkaapap apkaaaapap ekkaghghgs rapmsaralt
      421 ltvaiaavlf wcigafapaa flghftvfvl acfigymvvw nvtpalhtpl msvtnaissi
      481 iaigalvqia apevgmdgrp dglirwlafa alvltavnmf ggfavtrrml amfrk
//
LOCUS       WP_116393334             398 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Parvularcula marina].
ACCESSION   WP_116393334
VERSION     WP_116393334.1
KEYWORDS    RefSeq.
SOURCE      Parvularcula marina
  ORGANISM  Parvularcula marina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Parvularculales; Parvularculaceae; Parvularcula.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Parvularcula marina"
                     /db_xref="taxon:2292771"
     Protein         1..398
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41221
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(13,72,91,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(42,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkakk dprvgatpet vkklaalgae vsietgagea agfsdaayqe mgastgeaes
       61 vlsgadivvv ssppgkskla smgrgaklig lldpweeqer ladyagagvd afamellpri
      121 traqsmdvls sqanlagyka vvdaaheygr afpmmmtaag tvapakvfvm gagvaglqai
      181 atakrlgavv satdvraaag eqveslggtf ifvkeameeg egkggyakel tpeqqqaqkd
      241 lvaehlkkmd ivittalipg rpapklltte mvtsmrpggv vvdlaaprgg nveggdgeea
      301 ftlgatkvla pknilaglpg easnlyarnl lnfitlitdk eekqvavdwe deivrgialt
      361 rdgqivheqf ggsppiqslp veevaedsep eiidegda
//
LOCUS       WP_116385262             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116385262
VERSION     WP_116385262.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54053
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvkellk lgyqvvvetg agleasfsdd dyraagaaiv
       61 daaslwasvd vvvkvrppqv hpslgveeaa llkkhatlig fvwpaqqmsm lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyakems
      241 pafieaemrl faeqarevdi iittalipgk papklleadt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpgk dgqlvvnmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevpvpaea apprsrtgtt lialalaaaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_116386640             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus taiwanensis].
ACCESSION   WP_116386640
VERSION     WP_116386640.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus taiwanensis
  ORGANISM  Cupriavidus taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Cupriavidus taiwanensis"
                     /db_xref="taxon:164546"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38610
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetr agearvaatp etvkkyvaqg hqvvvqagag lnasqpdsay eaagaaigta
       61 advlgaplvl kvrapdagel aqmkpgavlv gmlnpfdten narmaaagit afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfltdee reiaqgvggy arpmppdwmk
      241 rqaelvhqra lqadiiitta lipgrkapvl lheatvrqmk pgsvvvdlaa aqggncpltv
      301 adqvvnhngv ilightnlas mvaadasaly arnvldflkl vidkdgqftl nleddivaac
      361 lmtrreaaal ag
//
LOCUS       WP_116401342             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylovirgula sp. 4M-Z18].
ACCESSION   WP_116401342
VERSION     WP_116401342.1
KEYWORDS    RefSeq.
SOURCE      Methylovirgula sp. 4M-Z18
  ORGANISM  Methylovirgula sp. 4M-Z18
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Beijerinckiaceae; Methylovirgula.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Methylovirgula sp. 4M-Z18"
                     /db_xref="taxon:2293567"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39294
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaenp sletrvaatp dtvkrftalg anvvvqsgag lssgildady eaagasiapd
       61 raatvadadi vlkvrrpdge elgglkagal fvatmdpygh edalkamada gvcafamelm
      121 pritraqvmd vlssqanlag yravidgage ygralpmmmt pagtvpaaki fimgvgvagl
      181 qaiatarrlg aivtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsaayra
      241 kqaelvashi akqdivitta lipgrpapkl itaamvqsmk pgsvivdlav erggncelak
      301 agetvvsdng vkivghlnvp grlaatassl yaknlyafve tlidkkektl avnwddelvk
      361 atlltkdgai vhpnfqpka
//
LOCUS       WP_116408199             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            leguminosarum].
ACCESSION   WP_116408199
VERSION     WP_116408199.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55364
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligsprerm ggearvamtp dsatqlqklg yqcaietgag klagfsdeay raagvtvvds
       61 aetlfasadv iakvrppesn evarlssgkt lisffypaqn kellnqtkas ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsvslg aityafdvrp evaeqiesmg aqfvfldfee rqqdgaatgg yaapsspefr
      241 eaqlrkfrei apdmdivitt alipgrdapk lwladmvamm kpgsvvvdla aerggncdlt
      301 vpdqkivsdn gvtvigytdf psrmaaqsst lystnirhmm tdltpnkdgv ivhnmeddvi
      361 rgatvalkge vtypppppki qaiaaqkrqe kpkeltpeek raaeaaafkv atrnqvglli
      421 aggllmllig afappvfmgh fivfalacfv gfqviwgvsh slhtplmavt naisgiiiig
      481 allqitaggw lvtglaavsv aiatinivgg fmvtrrmlnm fqks
//
LOCUS       WP_116407253             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            leguminosarum].
ACCESSION   WP_116407253
VERSION     WP_116407253.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39172
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare iageetrvaa saetvkkmks fgfdivveag agaasripda efeaagarig
       61 sfadaasadv vlkvrrpteq eisgyksgav viaimdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaaav yerampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqg
      241 kqaalvaehi akqdivitta lipgraaprl vsrtmlaamk pgaiavdlav erggniegvv
      301 ageiadvdgv kvigfanmpg rvaasasaly aknlvtflet mvnkesrsvv vnlddelvka
      361 tmltyagdvv hpafggakkg dl
//
LOCUS       WP_116425931             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas citronellolis].
ACCESSION   WP_116425931
VERSION     WP_116425931.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas citronellolis
  ORGANISM  Pseudomonas citronellolis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas citronellolis"
                     /db_xref="taxon:53408"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38682
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvaata etikklvgqg hqvivqsgag inacqpdsaf eaagakigsa
       61 adalgaelvl kvvapraeel aqmkpgavli gmlnpfdndn iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqadivitta lipgrkaptl lheatvqemk pgsvvidlaa aqggncplte
      301 agqvvvkhgv tlvghtnlaa mvpadasaly arnlldflkl tlsaegfkvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_116434007             371 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Herbaspirillum].
ACCESSION   WP_116434007
VERSION     WP_116434007.1
KEYWORDS    RefSeq.
SOURCE      unclassified Herbaspirillum
  ORGANISM  unclassified Herbaspirillum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="unclassified Herbaspirillum"
                     /db_xref="taxon:2624150"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38686
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlgipvesr dgetrvaatp etvkklvaak hevlvesgag ikssitdeay vaagaviaat
       61 advygaeall kvrapsader arlksgtvvv gilnpfdadn laamaaaglt afaleaaprt
      121 traqsmdvls sqaniagyka vlmaantyqr fmpmlmtaag tvkaarmlim gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfiteee keiaqgvggy arpmpadwmr
      241 rqaelvhera kqadiiitta lipgrkapvl iseetvkamk pgsvildmav dqggncplse
      301 pgktvikhgv hiigegnlaa lvaadasaly srnvldflkl ivdaegklvi nreddivaat
      361 llcsggevlr k
//
LOCUS       WP_116450522             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastococcus litoris].
ACCESSION   WP_116450522
VERSION     WP_116450522.1
KEYWORDS    RefSeq.
SOURCE      Blastococcus litoris
  ORGANISM  Blastococcus litoris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Geodermatophilales; Geodermatophilaceae; Blastococcus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Blastococcus litoris"
                     /db_xref="taxon:2171622"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52300
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpretr aretrvaatp atvgklialg yevvvesgag aaasfpdegy agagaqvsta
       61 ddawqadvvl rvnapstdei prlrdgatlv sllspglnpd lvdalaarpi tvlavdavpr
      121 israqsmdvl ssmaniagyr avveaahtfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdvrpev aeqvrslgge yvavpageqe vssdgyarem gedfnrraaq
      241 myaeqapdvd iiittalipg rpaprlitee mvasmrsgsv ivdmaaaqgg nvagsvpdei
      301 vvtgngvsii gytdlpgrlp aqasqlygqn lvslmtlltp gkdgqlvldf ddvvqraitv
      361 vragektwpp ppvqvsaapa papapaaepa pppeppspsr rfavvglgaa vlflvtafsp
      421 neliqhvtvf alavvvgfyv ighvhhalht plmsvtnais giivvgallq ighddavvtv
      481 lafvailvas invfggfavt rrmlgmftr
//
LOCUS       WP_116475559             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Zobellella
            maritima].
ACCESSION   WP_116475559
VERSION     WP_116475559.1
KEYWORDS    RefSeq.
SOURCE      Zobellella maritima
  ORGANISM  Zobellella maritima
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Zobellella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Zobellella maritima"
                     /db_xref="taxon:2059725"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53395
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipretl ngetrvaatp ksveqlrklg fdvcveqgag lkasfddaay qavgatlass
       61 devwqagliy kvnapnaeev eklvagttlv sfiwpaqnpe lveklkakgv tvmamdmvpr
      121 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvlv igagvaglaa
      181 igaagslgai vrafdtrpev keqinsmgae fleldyeees dssdgyakem skafieaema
      241 lfmaqakevd iiittalipg kpapklitae mvanmapgsv vvdlaaqngg nceltkpgel
      301 fvsdngvkii gytdlngrlp tqsstlyann lvnlakllsk ekdgnikvdf ddvvlrnmtv
      361 vkdgevtfpp paisvsaapk aaakpqaaae phakqpsnlk yylggagvvl fgwlataapv
      421 aflshftvfv lacivgyyvi wnvshslhtp lmsvtnaisg iivvgalsqv ggggfvtfla
      481 fiavliasin vfggftvthr mlkmfrrg
//
LOCUS       WP_116494510             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            rhizogenes].
ACCESSION   WP_116494510
VERSION     WP_116494510.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium rhizogenes (Agrobacterium rhizogenes)
  ORGANISM  Rhizobium rhizogenes
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rhizobium rhizogenes"
                     /db_xref="taxon:359"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55548
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgapkeiy esearvamtp dsaqalqklg yeclietgag ksagfsdeay raagvtvves
       61 adalysgsdi iakvrppeap eidrlspdkt lisffypaqn qtllqqakdk gaaviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv liigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfae qqdgaatggy aapsspefre
      241 kqlakfrela pqidivitta lipgrdapkl wladmvaamk pgsvivdlaa erggncdltv
      301 pdqrivsdng vivigytdfp srmaaqastl yatnirhmma dltpgkdgqv vhnmeddvir
      361 gatvayegei typppppkik aiaaqkpkek tkeltpaekr aqeitlfktq trnqvallav
      421 gtallllvgv yapasfmshf ivfvlacfig fqviwnvshs lhtplmavtn avsgivilga
      481 llqvgssnwl vvilaalsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_116518025             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pusillimonas noertemannii].
ACCESSION   WP_116518025
VERSION     WP_116518025.1
KEYWORDS    RefSeq.
SOURCE      Pusillimonas noertemannii
  ORGANISM  Pusillimonas noertemannii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pusillimonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pusillimonas noertemannii"
                     /db_xref="taxon:305977"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38400
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligipresa agetrvaatp etikkyvaak hsvvvetgag aaasytdeay qaagatlgsn
       61 qdalgaslvl kvrspsaael ghmqpntvlv gmldpfnqeg lqaiaqaglt sfaleaapri
      121 traqsldvls sqanlagyka vmlaanqygr ifpmmmtaag tlkaarvvvl gagvaglqai
      181 atakrlgavv easdvrpaaq eqvaslgakf ievpfetdee reiaqgvggy arpmpaawma
      241 rqaalvserc kqadivitta lipgrpaptl vseetvqamk pgsvivdlav erggncplse
      301 kdqvvvkhgv aligysnlpa lvatdasaly arnvldflkl itdaegglai qredeivaac
      361 lmtldgnvlr sa
//
LOCUS       WP_116521299             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter insuavis].
ACCESSION   WP_116521299
VERSION     WP_116521299.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter insuavis
  ORGANISM  Achromobacter insuavis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter insuavis"
                     /db_xref="taxon:1287735"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38376
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipretr dgetrvaatp etvkkyvggk htvvvergag taaryldeay eaagatlgsa
       61 qealgaelvm kvrapstael pqmkagavvi gmldpfdaeg laqmaaaglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgvggy arpmppawma
      241 rqaalvserc kqadivvtta lipgrpaptl vsaetvaamk pgsvlvdlav erggncplse
      301 kgkvvekhgv tligltnlpg lvatdasaly arnildflkl iinadgalai qrddeivsac
      361 lvceggnvtr gs
//
LOCUS       WP_116525893             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_116525893
VERSION     WP_116525893.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53647
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp vsaktvtvea knetfapqhp dqyqswkats
       61 eqsvredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdhf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdfik tvvpqwedqa rkngllsq
//
LOCUS       WP_116526017             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_116526017
VERSION     WP_116526017.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35895
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlilndf acvvrechaa frsvilrihe rkgivyheqd slntlmanlm argvisaeyv
      241 hkfhflsnvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 vap
//
LOCUS       WP_116530141             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            sp. KLBC 81].
ACCESSION   WP_116530141
VERSION     WP_116530141.1
KEYWORDS    RefSeq.
SOURCE      Microvirga sp. KLBC 81
  ORGANISM  Microvirga sp. KLBC 81
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Microvirga sp. KLBC 81"
                     /db_xref="taxon:1862707"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55144
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egearvamtp esalqlqkng hecfvesgag laagfsdaay eaagvtlins
       61 aaelfdtvdv vtkvrppted evsrlcpgqt lisffwpaqn pellelcrdk gatviamdmv
      121 prisraqkmd alssmaniag yravieagna fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg avtyafdvrp evaeqiesmg aqfvflefdq tqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrpapkl wtddmvqamk pgsvivdlaa erggnceltv
      301 pdqtivteng vtiigttdfp srmaaqastl yannirhfla dltpnkdgvi hhnmeddvir
      361 gatvthqsai typppppkvq aiaaakpkek pkeltpeekr aqeaaafkaq trtqvgllva
      421 ggvlialvga sapasfmahf ivfalacfvg fqviwsvshs lhtplmavtn aisgivvlga
      481 llqvgsghrl mvalaslsfl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_116528496             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Microvirga
            sp. KLBC 81].
ACCESSION   WP_116528496
VERSION     WP_116528496.1
KEYWORDS    RefSeq.
SOURCE      Microvirga sp. KLBC 81
  ORGANISM  Microvirga sp. KLBC 81
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Microvirga.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Microvirga sp. KLBC 81"
                     /db_xref="taxon:1862707"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39319
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsete gaetrvaatp etvkkykglg advvvqagag tkagitdael dasgaviaps
       61 reetlrdadi ilkvrrpadg eltgakpgal lisimdpygq daalknlaaa qvaafamelm
      121 pritraqvmd vlssqanlag yravvdatae ygrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedee fkqaetaggy akemsaeyqa
      241 kqaalvashi akqdivitta lipgrpapkl vsramvesmk pgsvivdlav erggncelaq
      301 pgqvvehngv kivghlnmpg rlaatassly aknlyafvet lvdkeskals vkwddelvka
      361 tcltrdgavv hpafqpka
//
LOCUS       WP_116539778             364 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium uberis].
ACCESSION   WP_116539778
VERSION     WP_116539778.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium uberis
  ORGANISM  Mycobacterium uberis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Mycobacterium uberis"
                     /db_xref="taxon:2162698"
     Protein         1..364
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37530
     Region          7..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mteaqttvgv vaesgseerr valvpkaias lvnsglavvv esgagegall pdelyteaga
       61 higdawatdv vvkvapptaa evvrlhrgqt ligflasrna dnligtlkqa gvqafaleai
      121 prisraqvmd alssqanvag ykavllaase strffpmltt aagtvkpatv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwldvgida sgaggyarel tddertqqqk
      241 alekavsgfd vvittalvpg kpaprlvtaa avegmkpgsv vvdlagetgg nceltepgqt
      301 virhnvtiaa plnlpatipe haselyskni talldllikd gklvpdfdde vvaescvtrd
      361 reds
//
LOCUS       WP_116546297             471 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Plesiomonas shigelloides].
ACCESSION   WP_116546297
VERSION     WP_116546297.1
KEYWORDS    RefSeq.
SOURCE      Plesiomonas shigelloides
  ORGANISM  Plesiomonas shigelloides
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Plesiomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Plesiomonas shigelloides"
                     /db_xref="taxon:703"
     gene            1..471
                     /gene="nrfA"
     Protein         1..471
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52211
     Region          1..471
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivklnttsi ttglalfltg tllcssalaq vearndkfad ahqpqyqswt qtqqsserad
       61 alaedpkmvi lwagypfakd ynkprghyya ltdvrdtlrt gapktaedgp lpmacwscks
      121 pdvarmiese gedayfkgmw akggpeivns igcadchatd sqefkdgkpa lhlsrpyasr
      181 amdaihmpfa kqgrfdqqaq vcgqchveyy fsgdnkavkf pwdngtsada maeyydelgf
      241 kdwvhglskt pmlkaqhpey etwqagihgk nnvgcvdchm pkvqgqdgkl ytdhkvgnpf
      301 drfdqtcanc htqskemlqg vvkerkeain tlklkveqql vhahfeakaa wdagateeqm
      361 qpilqdirqa qwrwdyaias hgvhmhapdi alktlgdaln laadartkla rllatkgitg
      421 eiplpdistk ekaqaalgmd mkqfisdkqq flkttvpawe keakaagrls q
//
LOCUS       WP_116552692             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. SDI].
ACCESSION   WP_116552692
VERSION     WP_116552692.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. SDI
  ORGANISM  Pseudomonas sp. SDI
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. SDI"
                     /db_xref="taxon:2170734"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38911
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqrgag lnasvpdsay eaagatigsa
       61 tdafgaqlvl kvvapddsel aqihsgtvlv gmlnpfnndl iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgqytl nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_116556508             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pararhodobacter oceanensis].
ACCESSION   WP_116556508
VERSION     WP_116556508.1
KEYWORDS    RefSeq.
SOURCE      Pararhodobacter oceanensis
  ORGANISM  Pararhodobacter oceanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pararhodobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Pararhodobacter oceanensis"
                     /db_xref="taxon:2172121"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55282
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif pgenrvamtp esaqalqklg htclietgag aaagfedaay taagvevvas
       61 aqalfdaadv vvkvrepvae eiallkegqt visffwpgqn telleqakdr gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aitmafdvrp evaeqiesmg aefvflefde paqdgaatgg yaapsspefr
      241 ekqlekfrel apdvdivitt alipgrpapk lwtedmvkmm krgsvvvdla aerggncdlt
      301 vpdekitten gvtivgytdf psrmgtqsst lysnnirhml adltpakdgv inhnmeddvi
      361 rgatathage itfpppppkv qaiaavkrek pkeltaeekr aaetaafkaq trqqvtllgv
      421 ggvllllagi fapasfmahf ivfvlacyvg fqviwgvshs lhtplmaitn aissiiilga
      481 llqigsgswl vmilaalsvf maginifggf mvtrrmlamf qks
//
LOCUS       WP_116572628             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides gansuensis].
ACCESSION   WP_116572628
VERSION     WP_116572628.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides gansuensis
  ORGANISM  Nocardioides gansuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Nocardioides gansuensis"
                     /db_xref="taxon:2138300"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52883
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresk pgeklvaatv atagqlkqlg ydvvvesgag vaadqtdeaf aaarvgvada
       61 dtvwssdvvv kvnapndeei arlrrgatii slmaparspe lldklqaagv talamdavpr
      121 israqsmdvl ssmanvagyr avieaahefg rqftgqvtaa gkvpparvfv vgagvaglaa
      181 vgaagamgai vrafdvrpev aeqvesmgae fvtvdmetev sadgyakemt aeqeaataam
      241 ydeearaadi vittalipgr papklitaet iagmrsgsvi vdmaaanggn teltrtderf
      301 vtdnlvtilg ytdlasrlaa qtsqlygtnv vnllklltpe kdgqltldmd dvvqrgitvv
      361 ldgeamwppp pvqvsaapaa paaavapvek kekkpvdprk klfggalaav lfalvaaysp
      421 tsflghftvf alavfvgyyv isnvahalht plmsetnavs giilvggilq vgsdnlavta
      481 lalvavlvas inifggflvt lrmlqmfrkd
//
LOCUS       WP_116579887             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. B1(2018)].
ACCESSION   WP_116579887
VERSION     WP_116579887.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. B1(2018)
  ORGANISM  Pseudomonas sp. B1(2018)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. B1(2018)"
                     /db_xref="taxon:2233856"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38577
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag vnasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvvv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaaavhera kqadivitta lipgrkaptl lsvetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_116573790             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides gansuensis].
ACCESSION   WP_116573790
VERSION     WP_116573790.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides gansuensis
  ORGANISM  Nocardioides gansuensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Nocardioides gansuensis"
                     /db_xref="taxon:2138300"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52456
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgvlkeah agetrvaatp ttvaalqklg yevvvepgag eaasftdeay aaagarlgdp
       61 latdvvigvn aptlaqrdrl epgatliaml nprfdeeiva dlalrsital smdavprisr
      121 aqsmdvlssm anvagyravv eaahefgrmf tgqvtaagki pparvfvvga gvaglaaiga
      181 asamgavvra fdvrpevaeq vesmgaefvq vefeaevstd gyakemtaeq eavtaamyde
      241 earaadivit talipgrpap rlitsetiaa mrngsvivdm aaanggnaal teidervvtd
      301 ngvtilgytd lagrlaeqas qlygtnivnl fklltpaqdg dlvldfddvv qrgitvvrag
      361 estwppppvq vsaapaavaa evapgkhvkp rmavgakvgl vlgaigllwl vnalaptddl
      421 rrhftvlmls ivigyyvigk vahalhtplm svtnaisgvv vvgalvqvas ddrivvglsa
      481 aaillasini fggfavtrrm lsmfskga
//
LOCUS       WP_116597268             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Primorskyibacter marinus].
ACCESSION   WP_116597268
VERSION     WP_116597268.1
KEYWORDS    RefSeq.
SOURCE      Primorskyibacter marinus
  ORGANISM  Primorskyibacter marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Primorskyibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Primorskyibacter marinus"
                     /db_xref="taxon:1977320"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55400
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf dgenrvamtp dsalqlqklg ydcvietgag laagfsdaty eaagvkiaat
       61 aetlwqeani iakvrppsda eaerltadkt lisffypasn kelmdlcask gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yaavsspefa
      241 aaqlakfrel apdidivitt alipnreape lwtedmvkam kpgsvivdla aerggnckmt
      301 vpdekivtdn gvtiigytdf psrmatqsst lyatnirhmm tdltpekdgn pvhnmeddvi
      361 rgatiahase vtfpppppkv qaiaaqkkek pkeltaeekr anevaafrtq tkqqvtllav
      421 ggalvlgvgl iapasfmqhf ivfvlavfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_116601326             535 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus alkaliphilus].
ACCESSION   WP_116601326
VERSION     WP_116601326.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus alkaliphilus
  ORGANISM  Cupriavidus alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Cupriavidus alkaliphilus"
                     /db_xref="taxon:942866"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55618
     Region          11..535
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqpnpssapq rigvpretlp gekrvatvpa vvekliklgf kvavesgaga aadfsddayr
       61 aagaevidga aqlwaasdiv lkvrppsrde valmreggtl igfiwpaqnp elmqqlatkn
      121 atvlaidclp rtlsraqkmd altsaagvsg yravieaaha fgsyfngqit aagkvpparv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvrslg aefvkvdyde dgsggggyar
      241 vmsegfqaaq rqmyarqaqd adviittalv pgkpapklit aemvrsmkpg svivdmaaeq
      301 ggnceltvpg eavvchgvti igytdlasrl arqsstlyat nllrlteelc ktrdgqaivn
      361 meddairgla vikdgaitwp applkaapap apkaaaapap ekkaghghgs rapmsaralt
      421 ltvaiaavlf wcigafapaa flghftvfvl acfigymvvw nvtpalhtpl msvtnaissi
      481 iaigalvqia apevgmdgrp dglirwlafa alvltavnmf ggfavtrrml amfrk
//
LOCUS       WP_116602687             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus alkaliphilus].
ACCESSION   WP_116602687
VERSION     WP_116602687.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus alkaliphilus
  ORGANISM  Cupriavidus alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Cupriavidus alkaliphilus"
                     /db_xref="taxon:942866"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53978
     Region          3..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtigvpre vhpgerrvaa tpdsvkellk lgyqvvvetg agleasfsdd dyraagaaiv
       61 daaslwasvd vvvkvrppqv hpslgveeaa llkkhatlig fvwpaqqmam lerlaqrgat
      121 vlamdcvpri sraqkldals smanmagyra vieaahafgr pfagqitaag kipparvlvi
      181 gagvaglaai gaarslgavv rafdtrpvvr qqieslgaef ltveieedgs gsggyakems
      241 pafieaemrl faeqarqvdi iittalipgk papklleagt vglmragsvv vdlaaeqggn
      301 cvltvpgesv rrdgvtiigy tdlpsrmaaq asqlygtnir hllseltpgk dgqlvvnmdd
      361 emirgatvlh qgavtwpppp ltvavpqqqa paevpvpaea apprsrtgtt lialalaaaa
      421 llglgavapp afmahftvfv laifvgyqvv wnvtaalhtp lmsvtnaisg iivvgalvql
      481 gkpslltavi agcavlvati niaggflvtq rmlkmfqrd
//
LOCUS       WP_116603505             482 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Edwardsiella piscicida].
ACCESSION   WP_116603505
VERSION     WP_116603505.1
KEYWORDS    RefSeq.
SOURCE      Edwardsiella piscicida
  ORGANISM  Edwardsiella piscicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Hafniaceae; Edwardsiella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Edwardsiella piscicida"
                     /db_xref="taxon:1263550"
     gene            1..482
                     /gene="nrfA"
     Protein         1..482
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52828
     Region          40..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mikvsnalqr iligaalalf gggaqaatad aaaaaetapp kvearndrfa aphldqyasw
       61 katadqsers dalaedprlv ilwagyafak dynkprghay altdvretlr tgapmkpedg
      121 pqpmacwsck spdvarmiad qgeaayfhgt warggpeivn algcadchnt asddfaagkp
      181 alhlsrpyaa raleaigkpf dkanridqqs mvcgqchvey yfsgkektvk fpwdqgtsvd
      241 eieayydgia ftdwvnplsk apmlkaqhpe yetwragihg qnniscvdch mpkvqnaegk
      301 lytshkignp fdsfeqtcrt chtqdkatlq qtvakrkqdv neiklkvedq lvrahfeaka
      361 awaagaseae mqpiltdirh aqwrwdfsia shgvhmhapd valrmlgtal dkaanartql
      421 vrvlakhgvn davplpdist kaqaqqalgm nmqqftqekq tflntvvpew eaqarsagrl
      481 dh
//
LOCUS       WP_116609608             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia unamae].
ACCESSION   WP_116609608
VERSION     WP_116609608.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia unamae
  ORGANISM  Paraburkholderia unamae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia unamae"
                     /db_xref="taxon:219649"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39564
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anetrvaatp etvkkyvaqg htvtiqagag tgasypdeay tavgaqvada
       61 atafgaelvl kvqsptvsel pfmkrgavlv gmldpfnaen aaklaeagvt afaleaaprt
      121 traqsldvls sqaniagyka vlvaanlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaegvggy arpmppswlt
      241 rqsalvhera kqadivista lipgrdaptl lpsetvqamk pgsvvidlaa grgpvadqas
      301 grrggncplt eadkvvmqhg vqicgytnla smvaadasal yarnlldflk livtkegaln
      361 idladdivaa tllardgava rka
//
LOCUS       WP_116613832             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia unamae].
ACCESSION   WP_116613832
VERSION     WP_116613832.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia unamae
  ORGANISM  Paraburkholderia unamae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Paraburkholderia unamae"
                     /db_xref="taxon:219649"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54246
     Region          3..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpmtiavpre thegerrvaa tpesvaqlik lgyaveveag agvnasypdd ayraagariv
       61 ddaqallsga divakvrpps seevqrlkpg atligfiwpa qhaalleqla areatvlamd
      121 cvprisraqk ldalssmanm agyravveaa qhfgrvftgq itaagkmppa kvlvigagva
      181 glaaigaarg lgaivrafdt rpevgqqves mgaeflsidi eeegggsggy arqmsakfie
      241 aemalfeaqa revdiiitta lipgkpaprl idaktvacmr agsvivdmaa eqggnceltq
      301 pglvvnangv tvigytdlps rmanqssqly atnirhlltd ltpakdgelk ldmddvvqrg
      361 ttvmqrgqic wppppvqvsa apqaaaqtkp vvvangqakd esvqaarrng vgslaalvia
      421 allllalgav appafvahft vfvlavfvgy qvvwnvtpsl htplmsvtna isgiivigal
      481 lhpgnagtiv tvlagialvv atiniaggfl vtqrmlkmfq rt
//
LOCUS       WP_116624596             410 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Mesorhizobium].
ACCESSION   WP_116624596
VERSION     WP_116624596.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     Protein         1..410
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42442
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtifipre tdaneqrvaa spdtvkrlvg fgfdvvvetg agagsriide dftkagarig
       61 kaadaakadv vlkvrrpsea elkgyksgaa vlaimdpygn daalaamaka gvtgfamelm
      121 pritraqvmd vlssqanlag yqavidaaye ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvaslg akfiavedee fkqaetaggy akemskeyqa
      241 kqaaltadhi akqdivitta lipgrpapkl isaamvasmr pgsvivdlav erggnvdgav
      301 pgkvvttang vkivghlnvp grvaasasll yaknlfafle tmidkeakal kinrddelvk
      361 atmltdggav vhpqfakaae ptkvatkpat ptvapkatqk kapakkkgda
//
LOCUS       WP_116630852             514 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Alitibacter langaaensis].
ACCESSION   WP_116630852
VERSION     WP_116630852.1
KEYWORDS    RefSeq.
SOURCE      Alitibacter langaaensis (Pasteurella langaaensis)
  ORGANISM  Alitibacter langaaensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Alitibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Alitibacter langaaensis"
                     /db_xref="taxon:756"
     gene            1..514
                     /gene="nrfA"
     Protein         1..514
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=57345
     Region          50..507
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mlkktlssla miglgfamvn sasaedypqt thekaeqlqq plpdaaakra ptkaelakpn
       61 pelkvdtvne kfakdfprqy nswaktaeqt efhreveddp rmivlwggya fakefnsprg
      121 hfytvtdvrn ilrtgapkda nsgpqpmacw tckgpdvarl iselgeegyf sgkwaregaq
      181 vvnsigcadc hdtksqefkd gkpalriarp hvlraldavg knfatsdrtd qraaicanch
      241 veyyfdkteg vnnvvfpwyk grdvdsieky ydeinfsdwt hsiskapmlk aqhpdfeaws
      301 mgthgkngvt cvdchmaktq dkdgkvytdh qvvgnpakdn fentcarchd qsketmvktv
      361 eqhkadvrdv lvkledqlvk ahfeakaawd agatqdemkd alqairhaqw rwdyaaashg
      421 mhihapdval kviasgldra adaraklavi lakhgvqqpi kypdvstaek awkvmgidie
      481 kerkdkeefi ktvipewnke avekgliltp ppak
//
LOCUS       WP_116650730             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Wenzhouxiangella sediminis].
ACCESSION   WP_116650730
VERSION     WP_116650730.1
KEYWORDS    RefSeq.
SOURCE      Wenzhouxiangella sediminis
  ORGANISM  Wenzhouxiangella sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Wenzhouxiangellaceae; Wenzhouxiangella.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Wenzhouxiangella sediminis"
                     /db_xref="taxon:1792836"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55915
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkvgalketa pgearvaltp esagrlkklg yeclvekgag laasftdaay eqagvtvvds
       61 adalwkqadv ivkvrepsea eieaapegkt lisfvwpaan edllekmkak nlsvlamdmv
      121 prisraqkmd alssmaniag yravveagnn fgrffmgqmt aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqiesmg aefvyldfee eqtdgaetgg yaapsspefr
      241 ekqlekfrel apdvdivitt alipnrpape lwtedmveam kpgsvivdla aerggnctlt
      301 kkderivtdn dvtiigytdf psrmatqssn lyatnirhml ddltpekdgk pvidmeddvi
      361 rgslvchege itwpppepkt kaigsakpkk kepeetaeek aareekamka slnrtaimla
      421 vggllclglg tvappsfmqh fivfvlsvfv gyhviwgvah slhtplmait naissiiivg
      481 allqiasgns vvfvlaaasv lmasvnifgg flvtrrmlam fkrs
//
LOCUS       WP_116633915             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium sp. TPD7012].
ACCESSION   WP_116633915
VERSION     WP_116633915.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. TPD7012
  ORGANISM  Microbacterium sp. TPD7012
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Microbacterium sp. TPD7012"
                     /db_xref="taxon:2171975"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51749
     Region          4..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mavigivrep agearvsatp atiaslrklg htvsvergag aaasypdsey eaagatlvdr
       61 agawgseivl aitapdaaai alladgatli allspalrpd lveslaqrgi talaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvtsiggs ylpvdvavaa ssdgyakats edynrraaei
      241 yteqaadvdi iittalipgr aaprlitasd valmkpgsvi vdmaagqggn vegsvagert
      301 vtdngviilg ytdlasrlaa qasqlygtnl anlvalltpa kdgqlvidfd dvvqrsvtvv
      361 rdgavtwppp avqvaaapaa kaveapaeia tpatmstgrk valivlgiaa lfavnafapa
      421 plpqhftvlv lsvvigfyvi gkvhhalhtp lmsvtnaisg vivvgamlqv tspipvvqvl
      481 aaiavllasi nifggfavtr rmlamftkgg hk
//
LOCUS       WP_116654633             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pelagibacterium sediminicola].
ACCESSION   WP_116654633
VERSION     WP_116654633.1
KEYWORDS    RefSeq.
SOURCE      Pelagibacterium sediminicola
  ORGANISM  Pelagibacterium sediminicola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Pelagibacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pelagibacterium sediminicola"
                     /db_xref="taxon:2248761"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55705
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtlkesf agearvavtp ssaahlqklg hevfvesdag slagfsdddy rkagvtvegs
       61 aadlvaavdv vakvrqpseg eiaqmregqt lisffypgqn kdllekakdq gitaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aqvfafdvrp evaeqiesmg aefvfldfee kaqdgaatgg yaapsspefr
      241 ekqlekfrel apqmdvvitt alipgrdapk lwtkdmveam kpgsvivdla aekggncdlt
      301 vpeqrivtdn gvviigytdf psrmgtqase lygnnirhfm adltpkkdgv vnhnmeddvi
      361 rgatvardhd itwpppppkv aaiaaqkpke kkkeltpeer raaeiatfka etksqvtlla
      421 agavvlllvg lvapasfmsh fivfvlacfv gfrviwnvah slhtplmait naissiiilg
      481 almqigsgsa wvmilatlav lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_116657671             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. NDM].
ACCESSION   WP_116657671
VERSION     WP_116657671.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. NDM
  ORGANISM  Pseudomonas sp. NDM
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. NDM"
                     /db_xref="taxon:2170733"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38818
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag ikasvvdsay eaagasigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera rqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_116668110             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_116668110
VERSION     WP_116668110.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38659
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lvcrdgqvir kna
//
LOCUS       WP_116683488             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Fulvimarina endophytica].
ACCESSION   WP_116683488
VERSION     WP_116683488.1
KEYWORDS    RefSeq.
SOURCE      Fulvimarina endophytica
  ORGANISM  Fulvimarina endophytica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Fulvimarina.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Fulvimarina endophytica"
                     /db_xref="taxon:2293836"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55774
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreth kgesrvamtp ksaqelrklg heclietgag tkagftdeay reagvtived
       61 aaklyetadi vvkvrepkde eierlskgkt lisffypgqn ealleaakts gatviamdmv
      121 prisraqkmd alssmaniag yravieagsn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfae etkdgaesgg yasvsspefr
      241 eaqlakfrel apdmdivitt alipgreape lwtrdmvesm kpgsvivdla aekggncklt
      301 vmdekivtdn gvtivgytdf psrmatqsst lyatnirhmm adltpgkdgt vvhdmeddvi
      361 rgatvthdge itypppkpkv kaiaaqkpke kvkektpeek raeekaafaa qtksqvtlla
      421 vggglvlfag lfapasfmqh livfvlsvfv gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgsa fviilaalav flaainifgg flvtrrmlam fqks
//
LOCUS       WP_116688930             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pelagibaculum spongiae].
ACCESSION   WP_116688930
VERSION     WP_116688930.1
KEYWORDS    RefSeq.
SOURCE      Pelagibaculum spongiae
  ORGANISM  Pelagibaculum spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Pelagibaculum.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Pelagibaculum spongiae"
                     /db_xref="taxon:2080658"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53510
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipresl agetrvaatp atveqlqklg ftiavesgag eaasfqdaay ensgasisps
       61 advwqadmlf kvnapsdeei akiregatlv sfiwpaqnae lmeklaarni tvlamdsvpr
      121 lsrsqsmdal ssmaniggyr avieaahefg rfftgqitaa gkvppakvli igagvaglaa
      181 igaagslgai vrafdtrpev aeqinsmgae fleldyeeed tgsgdgyake msaafieaem
      241 alfaaqaaev diivttalip grpapklita emvasmkpgs vivdmaaqtg gnceltvpgq
      301 khvtengvvi lgytdlpgrl ptqssqlyss nlvnlmkllc kekdgtldid fedtvvrgvt
      361 viregevtwp appikvsaap qqpksepiap peppkpmaps kkyaimagvg ltfawladaa
      421 pteflshftv filacvvgyy vvwnvshslh tplmsvtnai sgiivvgall qvgsggfvvg
      481 llafiailia sinivggftv tqrmlkmfrk
//
LOCUS       WP_116695743             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_116695743
VERSION     WP_116695743.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35777
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlckeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnlfhehgl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechaa frsvllrihe rkgivyheqd slntlmanlm argvisaeyt
      241 hkfhflsdvl eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg
      301 aap
//
LOCUS       WP_116700400             527 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Labrenzia
            sp. 011].
ACCESSION   WP_116700400
VERSION     WP_116700400.1
KEYWORDS    RefSeq.
SOURCE      Labrenzia sp. 011
  ORGANISM  Labrenzia sp. 011
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Labrenzia.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Labrenzia sp. 011"
                     /db_xref="taxon:2171494"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55939
     Region          5..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpealkigtp ketfpgearv amtpdsakql qklgyvcliq sgagsaagfs dkayedagve
       61 viktaaslwk ksdivtkvrp pdeketrhln kgktlisffn pggneeglea arakganvia
      121 memvprisra qkmdalssma niagyravie agnnfgrfft gqitaagkvp pakvlvvgag
      181 vaglaaigta tslgavtyaf dvrpevaeqv esmgaefvyl dfqeeqqdga atggyasvss
      241 pefreaqlak frelapemdi vittalipnr papklwledm vaamkpgsvi vdlaaerggn
      301 vdgtvadekv vtdngvtivg ytdfpsrmas qastlyatni rhmlsdltpe kdgqivhdme
      361 ddvirgatvt yqgeitfppp ppkvqaiaak pkekpkeptp eekraqevaa fkaqtkqqvs
      421 llvaggllll lvgliapasf mqhfivfvla vfvgfqviwn vshalhtplm avtnaissii
      481 ilgaimqigs gsflvillag lsvfmagini fggflvtrrm lamfqks
//
LOCUS       WP_116708098             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomycetospora cinnamomea].
ACCESSION   WP_116708098
VERSION     WP_116708098.1
KEYWORDS    RefSeq.
SOURCE      Actinomycetospora cinnamomea
  ORGANISM  Actinomycetospora cinnamomea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Actinomycetospora.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Actinomycetospora cinnamomea"
                     /db_xref="taxon:663609"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52522
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresg ehetrvaatp atvvglvelg atvvvepgag krasfpdaay taagaelgdp
       61 wgadvvlalg tpdaahldrm tpgatlvamv gparnpella dlarrgltvl aadavprisr
      121 aqsldvlssm aniagyravv eaahrfgrff agqvtaagkv ppatvlvaga gvaglaaiga
      181 atslgavvra tdprpevaeq vrslggefla vgtgdagqes sdgyaratsa dydaraaely
      241 teqaadvdvv ittalipgrp aprlltaadv armkpgsviv dmaagqggnv egsvadevvv
      301 tgngvtivgd tnlaarlpvq asqlygtnll nllkllvpar dgqmvldldd vvirsmtvah
      361 rgdvlwpppp ipvsaapavp vepetstpvv apakpaspar rygliaaafa vlfagtafap
      421 aelatnltif vlavvigyyv igkvhhalht plmsvtnais gvvivgallq fgqhgtvvsv
      481 lagvavllas inivggfavt rrmlamftrg paqersaq
//
LOCUS       WP_116745747             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium sp. 78].
ACCESSION   WP_116745747
VERSION     WP_116745747.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. 78
  ORGANISM  Janthinobacterium sp. 78
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium sp. 78"
                     /db_xref="taxon:2135631"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38711
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklvakh qvivqagagl qasipdaaya aagaqigtaq
       61 eayacaivlk vrapdasera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpflteeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvikhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_116761330             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Acinetobacter].
ACCESSION   WP_116761330
VERSION     WP_116761330.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40102
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklinag hsvviqrgag vkaayidsay eqvgakited
       61 ayigsqmilk vrapkgeeiq klepnttvva mfdpyrntel dqfasqnvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparivim gvgvaglqai
      181 atakrlgaiv eatdlrptak dqveslggkw ldvpmsdeek qkaadaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr liraetvakm kpgsvildma vetggnvegs
      301 kegetvmten gvkilgvpni pstvsteasa lyarnvfnfv etlfdkdknf vlnqedeiqk
      361 allvthgsqv llkra
//
LOCUS       WP_116767797             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter sp. H-02-3].
ACCESSION   WP_116767797
VERSION     WP_116767797.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter sp. H-02-3
  ORGANISM  Arthrobacter sp. H-02-3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Arthrobacter sp. H-02-3"
                     /db_xref="taxon:2703675"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38290
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqvgvgreqr agerrvaatp etvqqltalg ltlvvesgag teagfadaaf keagatvise
       61 lplaaldvll hvrplapeta arlrpgaitv glaspaselp tvralaaagi tsfalellpr
      121 israqsmdal tsqslvtgyr avleaavryp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandiraas adevasmggt finldldaaa egtggyaral gedraqrqrs
      241 llaphvaatd ilittaaipg raapllvttd mvtgmragsv vvdlaaesgg nvegviagqd
      301 iqvpveggsv tlvglqdaas ampsdasrlf arnvsnflal mtdggtvapd fdddvvagtc
      361 lthggavrhs ataaalgeea
//
LOCUS       WP_116791075             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter dolens].
ACCESSION   WP_116791075
VERSION     WP_116791075.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter dolens
  ORGANISM  Achromobacter dolens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter dolens"
                     /db_xref="taxon:1287738"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38502
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipretr dgetrvaatp etvkkyvggk htvvvergag taaryldeay eaagatlgsa
       61 qealgaelvm kvrapsavel pqmkagavii gmldpfdaeg laqmataglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgvggy arpmppawma
      241 rqaalvserc kqadivitta lipgrpaptl vsaetvaamk pgsvlvdlav erggncplse
      301 kgkvvekhgv tlvgltnlpg lvatdasaly arnildflkl iinadgalai qrddeivaac
      361 lvceggnvtr rs
//
LOCUS       WP_116801890             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_116801890
VERSION     WP_116801890.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53656
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd ftqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_116827967             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_116827967
VERSION     WP_116827967.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38863
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lrasvpdsay eaagavigdt
       61 detyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaqtvaqmk pgsvvidlaa aqggncpltv
      301 adqvivehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_116830179             300 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas syringae].
ACCESSION   WP_116830179
VERSION     WP_116830179.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..300
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34655
     Region          5..162
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mavtdlfskr qkrlrgggpd vyvydklpmp lriqmlymln eligdehefy ktfstcnqiv
       61 ryvvktlrle ygkhhiatdp enddyhelil flrkeedier vmdaieliin qtdeypdyde
      121 qcrdfindln irfrehgvgy elingeiiri dsrfhhavvv kpaiqflkqp gfegaqqefi
      181 layehyrhgr hkealnealk tvestmraic sargwaykss dnakrlivil qnehlfpayy
      241 qshlsalvsl megvvslrnn esahgqgpev rhvrddvvay alhmtasvvv mlaglhvdkp
//
LOCUS       WP_116833879             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_116833879
VERSION     WP_116833879.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38774
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvidsay eaagatigsa
       61 sdafgaelil kvvapsdsel tliksgtvlv gmlnpfnnet isklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_116853597             181 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Chitinophaga silvisoli].
ACCESSION   WP_116853597
VERSION     WP_116853597.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga silvisoli
  ORGANISM  Chitinophaga silvisoli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Chitinophaga silvisoli"
                     /db_xref="taxon:2291814"
     Protein         1..181
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=21093
     Region          4..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mifdlfskrq krlrgevpei ftydhipdnl rvqivhiidd vigaerfasn ldpddiysti
       61 hgilcreygv frlwgkyeke keqlfnyilk aklveevlda vdltfkyfls vlkpsylnyk
      121 hnttskldpd aaiqelnvrf kengigysfe ggeilridst fmhkevtqpt lsllwnncll
      181 r
//
LOCUS       WP_116836152             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_116836152
VERSION     WP_116836152.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53558
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged syfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapdeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq iraekqgfik tvipqweeqa rkngllsq
//
LOCUS       WP_116856180             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga silvisoli].
ACCESSION   WP_116856180
VERSION     WP_116856180.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga silvisoli
  ORGANISM  Chitinophaga silvisoli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Chitinophaga silvisoli"
                     /db_xref="taxon:2291814"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39394
     Region          1..359
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,90,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,275..276,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,225,236,
                     253..255,262,264)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigvlkeql pekrvslvpd ivkqlgkqgv tvwvepdaga aafhsddtyi qagaalmprt
       61 dilqqsdlvc siqipedwhl lragtilagv yqplhhhdlm qqwaaksltt ysldniprtt
      121 raqsmdilss qaniagykav llaavsygry fpmfmtaagt iapakvlilg agvaglqaia
      181 tarrlgavve vfdtrpvvre evmslgakfi svegaadasq aggyaveqsa dykqqqevli
      241 aasitkadiv ittaqipgkr apllvtaqmi nsmrpgsviv dlaagtggnt altqnqqtvf
      301 hngitiigds nlaasmpada sklyaknvfn flqllikdgq lvnnlqddii kgacithega
      361 viserlqavl k
//
LOCUS       WP_116858010             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_116858010
VERSION     WP_116858010.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38568
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsats etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_116859173             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_116859173
VERSION     WP_116859173.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38564
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnadgfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_116872802             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Terrimonas
            sp.].
ACCESSION   WP_116872802
VERSION     WP_116872802.1
KEYWORDS    RefSeq.
SOURCE      Terrimonas sp.
  ORGANISM  Terrimonas sp.
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Terrimonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Terrimonas sp."
                     /db_xref="taxon:1914338"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40341
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miagilkeph genrvsllpe qaealmkkni evwiedgagi nafadneayt fknirvvsrk
       61 elllqadiil sihnlsseei vglrneallv gvyqplynie likdytaaiv tlcsidmlpr
      121 ttraqsmdvl ssqaniagyk avltaaniyg ryfpmfmtaa gsiaparvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgak fieiggaada staggyavdq teeyrqqqqm
      241 kiaesitkad ivittaqipg knapvlitek mlktmrngsv ivdiaagtgg ntpftknnea
      301 vkyngvtilg danlpstmpf dasklygknv lnflsllldk dgniqldfed elvkgacith
      361 rgevvhekik nlisn
//
LOCUS       WP_116887321             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_116887321
VERSION     WP_116887321.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38819
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvgqg hritvergag lkasipdtay eaagatlgea
       61 adalgaqlvl kvvapndqel gqinpgsvla gmlnpfnndl iakmadrgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadiiitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvmahgv tlvgptnlpa qlaadasaly arnlldfmkl lfdkdgalai nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_116898837             525 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Wenzhouxiangella].
ACCESSION   WP_116898837
VERSION     WP_116898837.1
KEYWORDS    RefSeq.
SOURCE      unclassified Wenzhouxiangella
  ORGANISM  unclassified Wenzhouxiangella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Wenzhouxiangellaceae; Wenzhouxiangella.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="unclassified Wenzhouxiangella"
                     /db_xref="taxon:2613841"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56440
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkvgapketa agearvaltp esagrlqklg ydclvekgag laasftdeay ekagvevvds
       61 aealwqqadi ivkvrepsne eieaapegkt lisfvwpaeh edllekmkak nmsvlamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrffmgqmt aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqiesmg aefvylefde eeqqdgaetg gyaapsspef
      241 rekqlekfre lapdvdivit talipnrpap elwtedmvea mkpgsvivdl aaerggnctl
      301 tkkderivtd ndvtiigytd fpsrmatqss nlyatnirhm lddltpekdg tpvidmeddv
      361 irgslvcydg eitwpppepk tkaiasakpk kkepeetkee kaereatelk aslnrtgwml
      421 giggllclgv gavappsfmq hfivfvlavf vgyhviwgva hslhtplmai tnaissiiiv
      481 gallqvassn atvmwlaaas ilmasvnifg gflvtrrmla mfkrs
//
LOCUS       WP_116912478             376 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Variovorax].
ACCESSION   WP_116912478
VERSION     WP_116912478.1
KEYWORDS    RefSeq.
SOURCE      unclassified Variovorax
  ORGANISM  unclassified Variovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="unclassified Variovorax"
                     /db_xref="taxon:663243"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38507
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etvkklvasg hairvqagag iaasvtdaay qaagaeitdq
       61 agafsadmvl kvrtpteaet allksgavvi gmlnpfdaag lqrlasagvv afaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmpaswla
      241 rqqvevakrv aladvvista lipgraaptl itedmvkamk pgsvivdiaa gkgadgiggn
      301 cpiseadktv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrmtqd gqvtrk
//
LOCUS       WP_116919156             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tamilnaduibacter salinus].
ACCESSION   WP_116919156
VERSION     WP_116919156.1
KEYWORDS    RefSeq.
SOURCE      Tamilnaduibacter salinus
  ORGANISM  Tamilnaduibacter salinus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Tamilnaduibacter.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Tamilnaduibacter salinus"
                     /db_xref="taxon:1484056"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41326
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligiprett pgenrvaiip sgipelleag feviiesgag taahfaddey rnngaiiadd
       61 aaslyrqasv vlkvrtpsed eaaqmrpdtt litimdpwfh qdrvrqlaer gvrtfaldfv
      121 prttraqsmd vlsamggitg yravlsgams lpryfpmlmt aagtihparv fvigagvagl
      181 maiatarrlg avveaydlrp evreqveslg adfveidvpd adngdggyag eqsdafydaq
      241 rqqlsdcvar adlvittaai pgrqaptlvt remihrmkrg svivdlaaer ggnvegtvln
      301 gktevdgvtl vghvdhpsrv pvhasqlltr nmvafiknmt edgqlapsde ddivcatrit
      361 dqgaithagl reaiaptttq qpeeata
//
LOCUS       WP_116926774             557 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Comamonas
            sp. JNW].
ACCESSION   WP_116926774
VERSION     WP_116926774.1
KEYWORDS    RefSeq.
SOURCE      Comamonas sp. JNW
  ORGANISM  Comamonas sp. JNW
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Comamonas sp. JNW"
                     /db_xref="taxon:2170731"
     Protein         1..557
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56735
     Region          22..557
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mssispptap apqaaasppq cigvpheifp gekrvatvpa vvdklvklgf rvsvaagage
       61 aasfgdeayr aagaqvlpsa aiwagadilf kvrpptpeev ewmhagqilv gfvwpaqnpa
      121 lmaqlaakgl tvlamdalpr tlsraqkmda ltsmagvsgy ravveaahaf grffngqita
      181 agkvppaqvf iagagvagls aigtavslga vvrandtrae aadqvlslgg tfvpvdyaee
      241 ggggggyakv msegfqaaqr qmyaqqaawa diiittalip gkpaprlita emvqamkpgs
      301 vivdmaaeqg gncaltvpge avvrhgvtiv gytdlasrla aqsstlyann llrlteelck
      361 akdghalvnm eddairgltv vyqgsiswpa palaaapvak paaatagaag taaaspaaak
      421 krghghghgh gagsplpart lailfavlal lfwligahap aaflghltvf vlacfigymv
      481 vwnvtpalht plmsvtnais siiaigalvq mappgvvgtd rpglligala fvalvltain
      541 mfggfavtrr mlamfrk
//
LOCUS       WP_116960030             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hydrogenophaga borbori].
ACCESSION   WP_116960030
VERSION     WP_116960030.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga borbori
  ORGANISM  Hydrogenophaga borbori
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hydrogenophaga.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Hydrogenophaga borbori"
                     /db_xref="taxon:2294117"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38845
     Region          1..376
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,300,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etakklvaqg hvvrvqagag lhasatdaay eaagaqitda
       61 agalgadlvl kvrspqasel plmkagatlv gmlnpfdaeg lralaaaglt gfaleaaprt
      121 traqsmdvls sqaniagyka vmlaanaypr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf idvpyetpee keaaegvggy akpmppswlq
      241 rqaaevakrv amadvvista lipgraaptl iteemvksmk pgsvivdiaa gkgpgnadgs
      301 vggncpltea drtvvkhgvt iigetnlpal vaadasalya rnvldflklv lpkdasavqv
      361 pmdddivvac lmtqagevkr k
//
LOCUS       WP_116974605             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_116974605
VERSION     WP_116974605.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53444
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdg tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheie ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_116977928             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga silvatica].
ACCESSION   WP_116977928
VERSION     WP_116977928.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga silvatica
  ORGANISM  Chitinophaga silvatica
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Chitinophaga silvatica"
                     /db_xref="taxon:2282649"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39928
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,91,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miagilkekn getrvsltpe vvkqlqqmsv tvlveqdaga kafynddayv eagavitsqs
       61 eilsradiif tlqppatdql salkgkilig vfqplyhine veqwatsklt tfsldavprt
      121 traqsmdvls sqasiagyka vllaaytysr yfpmlmtaag siapakilil gagvaglqai
      181 atarrlgavv evfdtrpavk eevmslgakf vevagaadas qaggyaveqs enykqlqqqr
      241 iaesiikadi vittaqipgk papilvptem iekmragsvi idlaagtggn tsltrnnetv
      301 sfkgvtiigd snlpasmpad asklyaknvf nflklilnke gnlhlnfedd ivkgacithd
      361 gqivneriks mlqpa
//
LOCUS       WP_117014136             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Duganella].
ACCESSION   WP_117014136
VERSION     WP_117014136.1
KEYWORDS    RefSeq.
SOURCE      unclassified Duganella
  ORGANISM  unclassified Duganella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Duganella.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="unclassified Duganella"
                     /db_xref="taxon:2636909"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38663
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvgipaetr pgetrvaatp etvkklaakh qvivqsgagl sasvtdeaya aagaqigsaa
       61 eafaaevvlk vrapnaeera lipagavvig mlnpfdadnn aamaaaglqa faleavprit
      121 raqsmdvlss qaniagykav mvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpfltdeek eiakgvggya rpmpadwmrr
      241 qaelvherak ladiiittal ipgrpapvli seetvkamkp gsvivdlavs qggncplsel
      301 nktvvkhgvh ivgepdlatl vaadasalya rnvldflkli idkedklvid redeiikatl
      361 lcsggellrk
//
LOCUS       WP_116982707             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Emticicia
            sp. C21].
ACCESSION   WP_116982707
VERSION     WP_116982707.1
KEYWORDS    RefSeq.
SOURCE      Emticicia sp. C21
  ORGANISM  Emticicia sp. C21
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae; Emticicia.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Emticicia sp. C21"
                     /db_xref="taxon:2302915"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39465
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiiketk afekrvalsp evckqliqag fecaieneag tssffedtay eaigakvekd
       61 kssllasadi vlkvnpltve evgqmkkgav sisfmyaatn pelieasakq gisafsvdai
      121 prisraqkmd alssqanlgg yksviigayh lgkifpllmt aagtikpakv vimgagvagl
      181 qaiatakrlg avvevsdirp etkeqvqslg gkfievkgdd sikieggyvk gvsedflkkq
      241 qeviarhise adlvittali pgkkapmlvp edvvksmklg svivdmaveq ggncacseyg
      301 ktvvkhgvti vgepnipsll plnaselyak niatfllhla tkdgfkwemd eeitkgsliv
      361 hegkavhpsv vr
//
LOCUS       WP_116991975             370 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Duganella].
ACCESSION   WP_116991975
VERSION     WP_116991975.1
KEYWORDS    RefSeq.
SOURCE      unclassified Duganella
  ORGANISM  unclassified Duganella
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Duganella.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="unclassified Duganella"
                     /db_xref="taxon:2636909"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38647
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvgipaetr pgetrvaatp etvkklaakh qvivqsgagv sasvtdeaya aagaqigsaa
       61 eafaadvvlk vrapnaeerg liaagtvvig mlnpfdadnn aamataglqa faleavprit
      121 raqsmdvlss qaniagykav mvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpfltdeer eiakgvggya rsmpadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlavs qggncplsel
      301 nktvvkhgvh ivgepdlatl vaadasalya rnvldflkli idkedklvid redeiikatl
      361 lcsggellrk
//
LOCUS       WP_117139634             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas amygdali].
ACCESSION   WP_117139634
VERSION     WP_117139634.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas amygdali
  ORGANISM  Pseudomonas amygdali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas amygdali"
                     /db_xref="taxon:47877"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39136
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipketl agetrvsatv dtikkyllqg hqlivesgag lcaaipdsay kecgasigtm
       61 sdaygcevil kvhpptdeeq sfisegsllv gmlnpfddlm igkmavrgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaqgvggy arpmpaswmq
      241 rqaqaihera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvqangv tivgptnlpa qlgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_117153683             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraliobacillus quinghaiensis].
ACCESSION   WP_117153683
VERSION     WP_117153683.1
KEYWORDS    RefSeq.
SOURCE      Paraliobacillus quinghaiensis
  ORGANISM  Paraliobacillus quinghaiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paraliobacillus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Paraliobacillus quinghaiensis"
                     /db_xref="taxon:470815"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55648
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkery agetrvaaip ktveqlkkfg fdilvevgag erasftdeqy qkagaintst
       61 aevwqsdiiy kinppneeei vkmkegatlv sfifprqnen linnlnekki nvlamdmvpr
      121 israqsvdvl ssmaniggyr avmeashafg rflngqitaa gkvppakvfv igagvaglaa
      181 igtgrslgai vrafdarsev aeqiesmgge flrveieedg ttasgyakem seafikaemd
      241 liaeqakevd iiittaliqg mpapklitke mvdsmkpgsv ivdmaaltgg nceytvpnel
      301 tvtesgvkii gytdlpgrmp gqasdmyatn lvnltkllck ekdgnitidf gdvilrnmav
      361 sregqitfpp peisvsaapv kkeeihpete tsvkepkksa gwkygfgiaa illfgwigqv
      421 sppeflthft vfflsivvgy yviwkvtsal htplmsvsna isgiivvgal lqitsdilav
      481 kilafigili asinifggfm vthrmlkmfk idrev
//
LOCUS       WP_117178041             550 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhodoferax
            lacus].
ACCESSION   WP_117178041
VERSION     WP_117178041.1
KEYWORDS    RefSeq.
SOURCE      Rhodoferax lacus
  ORGANISM  Rhodoferax lacus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Rhodoferax.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Rhodoferax lacus"
                     /db_xref="taxon:2184758"
     Protein         1..550
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56783
     Region          25..550
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtgvatgas sgntaapatt qtaqrigvpr eifpgekrva tvpdvvekli klgfsvavet
       61 gagdaadlsd dayraagasv vadaaqlwat sdivfkvrpp tpaevaampe gqtlvgfvwp
      121 aqnpdlmqql takkatvlai dalprtlsra qkmdaltsqa gvagyravie aanafgrffn
      181 gqitaagkva pakvfiagag vaglaaigta aslgaivran dtraevadqv vslggefvkv
      241 dfeeegsggg gyakvmsegf qqaqramyak qakevdiiit talipgkpap klitadmvrs
      301 mkpgsvivdm aaeqggncel tvpgqavvth gvtivgytdl vsrlsrqsst lystnlfrlt
      361 eelcktkdgv invnmeddai rgltvtkdgt itwpapapkv aaapavakpa aapaakkahg
      421 hgapsepmag nklavmfgvs aalfwfvgan apqaflahft vfvlacfvgy mvvwnvkpal
      481 htplmsvtna issiiaigal vqiapplvvg aagrpddwir wlatggivlt sinmfggfav
      541 tqrmlamfrk
//
LOCUS       WP_117184663             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas capsici].
ACCESSION   WP_117184663
VERSION     WP_117184663.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas capsici
  ORGANISM  Pseudomonas capsici
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas capsici"
                     /db_xref="taxon:2810614"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38964
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hritvqsgag ihasvpdsay eaagatigga
       61 seafagelil kvtapndsel aliksgtvvi gmlnpfnnet iarlaergit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera rlsdivitta lipgrkapvl lsaetvvqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgqlqi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_117315133             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chromatocurvus halotolerans].
ACCESSION   WP_117315133
VERSION     WP_117315133.1
KEYWORDS    RefSeq.
SOURCE      Chromatocurvus halotolerans
  ORGANISM  Chromatocurvus halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Chromatocurvus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Chromatocurvus halotolerans"
                     /db_xref="taxon:1132028"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40373
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mllgipketh pgenrtavtp etakklcrlg adlqieagag egagfqdaey sdagatvvsd
       61 realissadm llrirkpale eiasmkkgci hisyldpfne heliarfreq gvtaismemi
      121 prttrsqkmd alssqanlsg yvmvvlaamn lprifpmmmt pagtlkpaki fvigagvagl
      181 qaiatakrlg grvtafdtrp vvaeqvrslg gtfleidlge tgeaaggyak eltpeqidkq
      241 reaqkaviae sdvvittaqv fgrkppvivt rdmvegmqpg svvvdmaaet ggnvegsvpn
      301 eivqvngvtv igygnlpnfv crdashmyas nlfnlvddcw deeakafsid lehdiqsgcv
      361 ithagevvne tiaklqaggd
//
LOCUS       WP_117330304             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_117330304
VERSION     WP_117330304.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53641
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knetfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd falgkpaltl
      181 srpyaerame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhaleeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_117335917             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. DHOC27].
ACCESSION   WP_117335917
VERSION     WP_117335917.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. DHOC27
  ORGANISM  Paraburkholderia sp. DHOC27
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia sp. DHOC27"
                     /db_xref="taxon:2303330"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39485
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvsqg hrvtiqsgag tgasfpdeaf saagaeivea
       61 gaafgadlvl kvqspteael pllkrgavlv gmldpfnadn aaklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaadlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlm
      241 rqsalvhera rqadvvista lipgrpaptl isvetvqamk pgsvlvdlaa grgpeyegrr
      301 ggncpltead kivtrngvqi vgytnlasmv aadasslyar nlldflkliv skegtlnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_117339367             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            mayottensis].
ACCESSION   WP_117339367
VERSION     WP_117339367.1
KEYWORDS    RefSeq.
SOURCE      Leptospira mayottensis
  ORGANISM  Leptospira mayottensis
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira mayottensis"
                     /db_xref="taxon:1137606"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41207
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigilkeak eetrvsvtpd vvdalkkiga vvlvekgage qsyyhdedyk kvgaslvsrq
       61 diigksniii sihladpatl akikpgtiyl gmfqpainas aiqklaskkv evlsldaiar
      121 itraqsmdvl ssqatvagyk avllaashla rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvhslgak fvevegashs aaaggyaveq teeykkrqqe
      241 aidkyaqkad iiittalipg kkapllitkk ivdnmksgsv ivdlassmgg nceytkhgqn
      301 vttprgvtvi ghknlagsip adaskmfskn vlnflkllik dkkinhdlsd eilssttivy
      361 kgevrhkltl dalssksgaa kpkksvakk
//
LOCUS       WP_117370599             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shinella
            sp. WSJ-2].
ACCESSION   WP_117370599
VERSION     WP_117370599.1
KEYWORDS    RefSeq.
SOURCE      Shinella sp. WSJ-2
  ORGANISM  Shinella sp. WSJ-2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Shinella.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Shinella sp. WSJ-2"
                     /db_xref="taxon:2303749"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39844
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msqcvfiare sdaaegrvag svetvkkmks lgldvlvetg aglrsrilda dyeaagariv
       61 gageanaadv vlkvrrptsa eistykfgai viatmdpygn eaaiaeiaka glttfamelm
      121 pritraqsmd ilssqanlag yqavidaahe fdrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vtrqmlaamk tgsvvvdlav erggniegse
      301 pgkvvevegv rvigylnvpg riaasasaly aknlitflet mvdketksvs vnvedelvka
      361 tmltnggavv hpnfggsvqq gegk
//
LOCUS       WP_117387575             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium marinum].
ACCESSION   WP_117387575
VERSION     WP_117387575.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37079
     Region          7..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdpqttvgv vaestpderr valvpkavgs lvnsgvavvv esgagerall pddlyteaga
       61 tigdawaadv vvkvappsad evgklrggqt ligflaprna dnsigalkqa gvqafaleai
      121 prisraqvmd alssqanvag ykavllaase strffpmltt aagtvkpatv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwlnigida ageggyarel tdeeraqqqk
      241 aleaaisgfd vvittalvpg rpaprlvtaa aveamkpgsv vvdlagetgg nceltepgrv
      301 vvkhdvtias plnlpatmpe haselyskni talldllltd gklapdfdde viadscvtrg
      361 dd
//
LOCUS       WP_117401599             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomadura spongiicola].
ACCESSION   WP_117401599
VERSION     WP_117401599.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura spongiicola
  ORGANISM  Actinomadura spongiicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Actinomadura spongiicola"
                     /db_xref="taxon:2303421"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52413
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigvlkedp pgerrvavtp dtvpqlqklg yevvvesgag agagfpddqy eaagaaigda
       61 taadvvlgvn ppapgqldal rpgatligll nprlkpelve dlakrpital sldavprisr
      121 aqafdvlssm agiagyravi eaahefgrff tgqvtaagkv ppakvlvaga gvaglaaiga
      181 agslgaivra tdprpevadq vrslggdyla vaepepddtp dtgyakemsd dynvraaaly
      241 adqcrevdii vttalipgkp aprlitaemv atmrpgsviv dmaaanggnv egtvpgervv
      301 tdngviilgy tdlagrlpaq asqlygtnll nlmklmtpqr dgqlvldfdd vvqrsmtvvr
      361 egeltwpppp vsvsaapakt qpareveada peskpdpllr rlgvavaaaa tfglialspa
      421 alqvhltvfa laivigyyvi gnvhhalhtp lmsvtnaisg iivvgallqi gtgdaaitvl
      481 slaaillasi nvfggfavtr rmlamfvrs
//
LOCUS       WP_117409001             400 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Microbispora triticiradicis].
ACCESSION   WP_117409001
VERSION     WP_117409001.1
KEYWORDS    RefSeq.
SOURCE      Microbispora triticiradicis
  ORGANISM  Microbispora triticiradicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Microbispora.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Microbispora triticiradicis"
                     /db_xref="taxon:2200763"
     Protein         1..>400
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          7..>372
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mshaaqrlgv vaesapgetr vaatpatipq llslgyeviv esgagersgf tddayvraga
       61 riggreetwg agvvlkvnap aeeeiaalrd gatlvsligp aanpdlldal trrpvtvlam
      121 davprisraq sldvlssman iagyraviea ahafgrfftg qvtaagkipp akvlvagagv
      181 aglaatatav slgaivratd prpevaeqvr slgaefldvg vaqrsgadgy aretsrdydl
      241 raaemyaeqa advdivvtta lipgrpaptl ltaehvalmr pgsvivdmaa aqggnvagtr
      301 agevvvtang vtiigytdla grlpaqasql ygtnlvnlmk lltpdkdghv rldfddpvqr
      361 amtvvrdgek twppppiavs aapaapaata appppapvat
//
LOCUS       WP_117413832             393 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Breoghania
            sp. L-A4].
ACCESSION   WP_117413832
VERSION     WP_117413832.1
KEYWORDS    RefSeq.
SOURCE      Breoghania sp. L-A4
  ORGANISM  Breoghania sp. L-A4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Breoghania.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Breoghania sp. L-A4"
                     /db_xref="taxon:2304600"
     Protein         1..393
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40960
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvplerd avetrvaata etvkkfiglg fdvvvekgag kasrildady kdagakiaad
       61 asatlgdadv vlkvgrpgad elklmkkgal vfaimdpfgh ekdvkamata gvsgfamefm
      121 pritraqvmd vlssqanlag yqavidaaee ydralpmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg asvsatdvrp aakeqvesla akfvavedde fkqaetaggy akqmspeyqk
      241 kqaelvashi akqdivitta lipgrpaprl itkemvqsmr pgsvlvdlav erggnvegak
      301 pgkvikvgev kivghlnvpg riaatasaly aknlyafvet mvdkeaksln vdwddelvta
      361 tvltrdgavv hsaftgskpa pavpaaakke gge
//
LOCUS       WP_117433357             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium marinum].
ACCESSION   WP_117433357
VERSION     WP_117433357.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marinum
  ORGANISM  Mycobacterium marinum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            ulcerans group.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Mycobacterium marinum"
                     /db_xref="taxon:1781"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37109
     Region          7..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdpqttvgv vaestpderr valvpkavgs lvnsgvavvv esgagerall pddlyteaga
       61 tigdawaadv vvkvappsad evgklrsgqt ligflaprna dnsigalkqa gvqafaleai
      121 prisraqvmd alssqanvag ykavllaase strffpmltt aagtvkpatv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwlnigida ageggyarel tdeeraqqqk
      241 aleaaisgfd vvittalvpg rpaprlvtaa aveamkpgsv vvdlagetgg nceltepgrv
      301 vvkhdvtias plnlpatmpe haselyskni talldllltd gklapdfdde viadscvtrg
      361 dd
//
LOCUS       WP_117619010             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter sp. Arc7-DN-1].
ACCESSION   WP_117619010
VERSION     WP_117619010.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. Arc7-DN-1
  ORGANISM  Marinobacter sp. Arc7-DN-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter sp. Arc7-DN-1"
                     /db_xref="taxon:2304594"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55922
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipreif kderrvaatp psvhkliglg yevvveggag eaanysdeay ekvgaaiaad
       61 ttslwqdadf ilkvrapmkn pslnrhevdl mkegaflvsy iwpaqnpell eklaakkits
      121 faidslpris raqkmdalsa maniagyrav ieaanhfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig aansmgaivr afdtrlevke qvesmgaefl vldfddedgs gsggyakqms
      241 defikaemal faeqaeevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgtva hhhgvtligy tdlpsrmakv asdlyatnll hllteltpek dgkplvnmed
      361 dvirgltvvr dnsitwpppq peapvssapp pgteepsaad kaaakknadr rsligkstll
      421 vvtalalygv gayapesflq hftvfvlacf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gamlhlaqae nlavgimafv avliasinvg ggfrvthrml kmfrr
//
LOCUS       WP_117868369             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ruegeria
            sp. AD91A].
ACCESSION   WP_117868369
VERSION     WP_117868369.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria sp. AD91A
  ORGANISM  Ruegeria sp. AD91A
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Ruegeria sp. AD91A"
                     /db_xref="taxon:2293862"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55627
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeil dgenrvamtp dsavqlqklg yecliekgag vaagfsdaay eaagvevvkt
       61 aaslwktadi iakvriptet elkrltkgkt lisffnpagn eegmelaksk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee dqqdgaatgg yasvqseefr
      241 naqlakfrel apeidivitt alipnrpapk lwledmvkam kpgsvivdla aerggnvegt
      301 vpdekvvtpn gvtiigytdf psrmaaqsss lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgstvtyege itfpppppkv qaiaaqkkpe vkeltpeekk aqevaafkaq tkqqftllgv
      421 ggalmllvgl iapasfmqhf ivfvlaifvg fqviwgvahs lhtplmaitn aissiiivga
      481 lmqigsgsfl villaalslf maginivggf lvtrrmlamf qks
//
LOCUS       WP_117920020             308 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Agathobacter rectalis].
ACCESSION   WP_117920020
VERSION     WP_117920020.1
KEYWORDS    RefSeq.
SOURCE      Agathobacter rectalis (Eubacterium rectale)
  ORGANISM  Agathobacter rectalis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Agathobacter.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Agathobacter rectalis"
                     /db_xref="taxon:39491"
     Protein         1..308
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35611
     Region          3..165
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 myellskrik nadgepevft ynsfpqafrn qvfyiledvl dpystydenl wdifeenfcr
       61 ekglkgmgyg kmqngygkss ieeyftdcdd sdfldaidyf fyltdkklrt mkpeyqydyd
      121 adgaindaiv elnyrfkqhn lgyefansqi itidstflhk tavkpalkll feegfegaed
      181 eirnayerrr kgdnknaile agkafestmk iicdkqgyay dknkdtaqkl itilenngfy
      241 psymnahlts irktletglp vvrnkvaghg qgnqiitipd eytdyalhla atnilflvrl
      301 yrnkkqnp
//
LOCUS       WP_117984742             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_117984742
VERSION     WP_117984742.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35670
     Region          5..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiydlfskr qkrlrgdvpd vyqytnlpqn frvqvvhivk stigndsdyn tpaskiynyi
       61 nntlcreygv fklqeyasen feyiynfflk ekdpekcldv ieltfkcing yvrqnswefr
      121 dchqspddai eelnnrfres gigyqfesge vvrvdsqfih sdvvkptlqi lgnsqefaga
      181 ndeflsaheh yrhqrfkecl ndclksfesl mkaihkkrsw eygstdtakk lissclsngl
      241 ipdymqnqfs slrillesgv ptirnkeggh gqgdevtnvp ehlasytlhl tasnllflak
      301 cdenftkkk
//
LOCUS       WP_117952687             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Seongchinamella sediminis].
ACCESSION   WP_117952687
VERSION     WP_117952687.1
KEYWORDS    RefSeq.
SOURCE      Seongchinamella sediminis
  ORGANISM  Seongchinamella sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Seongchinamella.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Seongchinamella sediminis"
                     /db_xref="taxon:2283635"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40246
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaipreth pgenrvpitp dvarklvrmg adlvieagmg igsgfadsay adagatistd
       61 rkelfasadm llrlrkpald eialmkrgai hisyldpfne helvkafrda gitsismemi
      121 prttrsqkmd alssqanlag yqmvieaama lprifpmmmt pagtlkpanv fvigagvagl
      181 qaiatakrlg akvtafdtrp vvaeqvqslg akfleidlge tgetaggyak eltpeqvaiq
      241 rqaqkdviak sdvvittaqv fgrkppvlvt kdmiegmapg svivdmaaet ggnvegsvpn
      301 etvewsgvti igkgnlagev avdasqmyss nlfnlvedsw cddkklfvvd fegdilpgci
      361 ithggditne tiknivegga
//
LOCUS       WP_118110413             308 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Roseburia inulinivorans].
ACCESSION   WP_118110413
VERSION     WP_118110413.1
KEYWORDS    RefSeq.
SOURCE      Roseburia inulinivorans
  ORGANISM  Roseburia inulinivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Roseburia.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Roseburia inulinivorans"
                     /db_xref="taxon:360807"
     Protein         1..308
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35546
     Region          3..165
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 myellskrik nadgepevft ynsfpqafrn qvfyiledvl epystynenl wdifeekfcr
       61 ekglkgmgyg klqngygkss iekyfkdcdd idfldaidyf fylidkkirt ikpeyqydyd
      121 adgainaaia elnyrfkqnn lgyefansqi itidstflhk tavkpalkll feegfegaed
      181 eirnayerrr kgdnknaile agkafestmk iicdkqgyay dknkdtaqkl itilenngfy
      241 psymnahlts vrttletglp vvrnkvaghg qgnqiitipd eytdyalhla atnilflvrl
      301 yrnkkqnl
//
LOCUS       WP_118136011             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oceanicella sp. SM1341].
ACCESSION   WP_118136011
VERSION     WP_118136011.1
KEYWORDS    RefSeq.
SOURCE      Oceanicella sp. SM1341
  ORGANISM  Oceanicella sp. SM1341
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Oceanicella.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Oceanicella sp. SM1341"
                     /db_xref="taxon:1548889"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40056
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipketr dhetrvaavp etvkkfiklg aevvvqsgag ltasvpdaey eaagatiakt
       61 yaqtlkgadv ilkilaptea elkslakgqk lfcsmqpynq peimegcaer gvdafamefm
      121 pritraqsmd vlssqsnlag yravieaaaa ygrampqmmt aagtvapaka fimgvgvagl
      181 qaiatarrlg aivtatdvrp ateeqvqslg akfiavknee feqaqtsggy akemsddykk
      241 qqaelvaghi akqdivvtta lipgrkapil vtkamvasmr pgsiivdlav eqggnvegvv
      301 lgenvvteng vtilglpnip grmaadssal ysrnhynfls pffgeegfal dpedelvkgi
      361 qltkdgeiih pnfakketa
//
LOCUS       WP_118141080             955 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118141080
VERSION     WP_118141080.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..955
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106481
     Region          34..954
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnsrfksyny klfvaslval aplganakta qtsesdtasa dkemvqvayr kvakddilgg
       61 vsvvdvenlm kknyhtysld nmqgyvggwn gnslwgmdad nagylvlvdg vpreannvqp
      121 seiaqisflk gaqavvlygs kaakgavvit tkrghndglk vevqanagln vaksypeyls
      181 saeymtlyne arrndglsel ysaediynhg aglnpyrypn ldfyssdflr kmnsryeata
      241 eisgggkrah fysninyyrq gdyfkfgeak nnntqrfsvr gnvdiditdd ikawvnssat
      301 fydshsakgn yweaastwrp nfpqnaapli stdmiapnak aawdlmsvak lvdgkyflag
      361 tqanssnvfa diysagsskf tsrqfqfdtg vninlhkvlk glsfethfav dyatsyntsf
      421 dnsyavyipt wanvdgkdmi valkkegedk ksgnqnisgs tdnqtmffsg qfnynntfnk
      481 vhnlsamlia sgfqqsksgq yhknssanla fdasynyaqk yyadfglaai hsaqlapghr
      541 ealspslslg wrlknesflk nskvvddmmi svsgsiined idiangdnry ylyqsiwtsd
      601 ygygwydgss dkytyskrge nkdldfikrk elslnfktsl wqklvtldas ffinsmegyl
      661 issptfypsh lntgypaasf mpvlnynnnr rvgfdfaanf nkkvgdvdls lgvtgtyytt
      721 katkrdennv eqyqnrqgka ldgiwgyksa glfqseeeik tspdqsyfgg tvkpgdikyv
      781 dvngdnkidq ydqvflgkgg wygapftlgv nltakwknft ffalgtgnfg awgvknnsyw
      841 wvkgdskysa vvrnrwteet ketatyprlt sldgnnnfqt sdfwmyktda frlakvqity
      901 dlpstlfqkt wlkglsayvs ganlltisge revlemnvgs apqtryynig vkatf
//
LOCUS       WP_118141206             991 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118141206
VERSION     WP_118141206.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..991
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109285
     Region          28..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdknnlskkv glllagcfit fnalgqttik gqvvdatgep vigasilvkd tkngavsdld
       61 gnykldnvkd gsvlvfsylg yrtqeipvkg nhvinvslke ndevldevvv vgyavgskrt
      121 vsgavdrikk edmnkgvvts paealkgkva gviisqaggd ptsspsirvr gtsslsggnd
      181 plviidgvfa dmtmfnslap gdiesltilk dasetaqygs rgasgvivvt takgklgyss
      241 lsyngqfgvn tvyknldlms aseyretaks lgltytdmgg dtnfleeier nvgltqnhni
      301 sfssgtdtss lraslgfvlr qgalknsdmk nftakldgtq ylfdkhlkle lgifgsqrns
      361 niqydmhkmf ysataynpty pnvrndkgew dedllanevw nplglldidd fykdasvnvh
      421 gkatvniidg ltvsafgsyn ywnrdnkfyi pnniqmgkln gngwayiant nrkdymgnvm
      481 vnfskdfgkh hidalalmeg qkytydwnsq eahgfdtnyf kfnnmkaaan vswgnlqsny
      541 teytlssyma rvnymladky iatvnvrtdg ssklgngqkw gwfpsaslaw visnepwmkk
      601 ikqidnfkir agygvtgnqd aidpytslal mepngvttvn gatsttfavt snsnpdlkwe
      661 vkktfdagfd lsmfkqrlnv tfdwytsets dmlytytvpv ppftydrlla nmgtmtnmgf
      721 elavrgdiik tkdftfnsgl nfsyqknklk klsgtykgqp mttsehisva tvgaaglvhn
      781 ngvtyliegq pvgvfylphc tgidekgqyi iedlddngti dtgdsgdrkv cgqaipkyfl
      841 gwdmsfkykn wdltmqfnga fghkiynats mtlnnmsnfp tynilsgaqh lnngkgihdv
      901 qisdywlekg dymnfeyasl gytftkdmlk wkfinnihls lsvnnictlt gykgltpmin
      961 satisgdnlg iddkniypls rtytlslsvn f
//
LOCUS       WP_118145772            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraprevotella
            clara].
ACCESSION   WP_118145772
VERSION     WP_118145772.1
KEYWORDS    RefSeq.
SOURCE      Paraprevotella clara
  ORGANISM  Paraprevotella clara
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Paraprevotella.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Paraprevotella clara"
                     /db_xref="taxon:454154"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118928
     Region          34..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 magtlggyaq eeaatdtvta arpaspikkn vktrpvsgrv favtsgtplg galvsvsgyd
       61 gysalteedg tykldvpeya talkitapdy ntvrvginqs gklrdvtmys namrsaygad
      121 dnilntvvad kfdyspslni tseigdqlga nvrtisrggt pgignfmmmn ginslhsngq
      181 plividgviv dqqydrtmvh dgfyndilts fnvneiksvk vmangtaiyg akgangvili
      241 etkrntslat kidatvsagi tllpkslpmm sgsqfktyas dllkttgtnl sefqfltsdp
      301 nnyyynkynn ntdwndviyr eafsqnygit vqggdevasy flalgyngaq svledndvnr
      361 lnirfntdin mfkhlfirfd asysnvtrnl kdqgapenyd egtvtsvnyl glvkspmlsp
      421 yaysngkisd vafdnsdedy ldqalasign vnyrlanpas ineygtaqnk nyfensylni
      481 aitprwqfnk hlslsslfsy tltntndkyy vpingvpdyy vssigltven eirslyssqn
      541 sitsdtkiew gnqygahsid llggfrymnd rykvdtqlgy ntgsdktpfi ndtqnktttg
      601 stnewtsmsw ygqarydyrk ryfvegnlai esssrfgkea kdgfklagvr wgvfpgiqag
      661 wvlsneswfd vpgidyakft mgydvsgndg idfdatrtyf ksilfqnlan glvlgnlgnt
      721 evqwettrrf sfgtelnflk nrlnlkvnvf kswtdnllty helnfitgle nnwvnggsle
      781 nkgynitvng hiiatrnwnw elgasvghyk nkltalpdgq dyvdaevyga tirsqigqpv
      841 nlfygyktea tasgthvyat seeakadgly ilgengidkt yfgagdvkfa dngdkeinka
      901 dmqiigdpnp diygniftsl sykrirldvn fnyslgnday nylrsqlegg srfmnqsiam
      961 vnrwtyegqk tdmptvmwed pmgnarfsdr wiedasylrl ksitlsyelp lnstfihglt
     1021 fwgqannvft vskylgadpd fsmsnsvleq gidrgllans rnfmlgikin l
//
LOCUS       WP_118145778            1120 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraprevotella
            clara].
ACCESSION   WP_118145778
VERSION     WP_118145778.1
KEYWORDS    RefSeq.
SOURCE      Paraprevotella clara
  ORGANISM  Paraprevotella clara
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Paraprevotella.
REFERENCE   1  (residues 1 to 1120)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1120)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1120)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Paraprevotella clara"
                     /db_xref="taxon:454154"
     Protein         1..1120
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125928
     Region          31..1118
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miktmkqlky yflicclvva svvnaqgits vsgtisdsfg pvvgaaivem dasnrnisat
       61 vtdfngnftl kiknpknrlk isyvgmktqi lpinkkvyhv tledamvlkq vevkakkrve
      121 ssglaipere vsfasqtina kefeglglts vdealqgria gldivmnsgn lgagttmrlr
      181 gastistlts seplivvngd vwnvdqsnfd vqnandeqfa qllninpedi esisvlkdaa
      241 ataiwgsqga ngvieiktkr gkrgkprlty slrltgtyqp dgvdlltgdq ytmlmkeayf
      301 nprlsdaaad ipefnyitdk rvfsewqmfn nntdwvkevk qvglrqnhfv sitgggekat
      361 frisggydhe tgsiieqkld rfttrmmldy yvsdrikiis dfaltytdnq rnsddllaia
      421 ykkmpnlaif eedeqgnslg ryyemlkakd aledqrnlvn piasakyakn syttyaidpk
      481 lelqydflgi ddtkhrltyn gkvimnvfna yedtyyprel stdnwnasgv sratsfssks
      541 lafttthtlt fvphflnedh sfmtmgrfql vsgtssdqkt evaglpngve apsaggitpg
      601 mssnfnrwrs lyytfsahya fkeryifdvs arvdgttkfg pgkrwgvfpa vsgrwnvvde
      661 pwmegtrkwl smlsirpgwg mtgnqpnkdy lyvnqysaas nyfgatgmap nnlklntlqw
      721 emkytwnvgf dlgfwddrik adinlytqtt kdmlmgnvri ssisgftnyp yqnvgdmnnk
      781 gweinlntnk liqkgkfwmd lnftfannkn eitrmdprvl etlnsdwvae nrkllqrvqv
      841 dnpfgaiygy rykgvymyny dtylqkerla adgdadakaf ianfnnnggw taplvynang
      901 eivrdmkgdp lqmmfnyvsg gtgyefkggd aiyedvnhdg ninqldivyl gnslpkltgg
      961 fgfkfnygdw alnaqfnyrv dydivnlarl dmesmgsnnn qsqavnyrwr kegdftsipr
     1021 alstsgnfan yntmisdrfv edgtflrlny lqisynmpqk mvkkiglsgl rfylsgnnlf
     1081 cltkysgvdp elgyggysvt qdaaqtprak sytfgvtvdf
//
LOCUS       WP_118146471            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraprevotella
            clara].
ACCESSION   WP_118146471
VERSION     WP_118146471.1
KEYWORDS    RefSeq.
SOURCE      Paraprevotella clara
  ORGANISM  Paraprevotella clara
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Paraprevotella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Paraprevotella clara"
                     /db_xref="taxon:454154"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123354
     Region          24..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkikyliml lfcmgslaam gqnqvasgtv sddlgplmgv yvgeidaanr ivsatvtdmn
       61 ghftlkvqnp knklrftymg fktayyeigk rvvfdimmee nskvmkevvv earpkiatgg
      121 ldipereqsf sqqtikmtef eglsftsade alqgriagld iiatsgnlgs gttmrlrgvs
      181 tiygnaepli vvddnifetd andnidyssm tderfaells inpediesit vlkdaaatai
      241 wgskgangvi nivtkrgvrg kpkltyslrl kgtyqpegyk llngdeytml mkeelfnvnq
      301 npesqpelny dqtyseyeqf nnntdwrkev kqfglfqthy vslsgggeka nyrlsagydh
      361 qvgsiiaqkl drfttrmald yfvndritis sdfaltytdn kknsddllkv aymkmpnaai
      421 ydedaygnsl gtyytiprfv erykddkdel daqrkavnpv asawlaqnee rtyniqpqfd
      481 iqyrllglde estqltykgt vvlsiynayk dsyypwelks nvytqtegni ntasssfdks
      541 fgfttrhqlt fipfianhdh svrlffkgev tsgtssaqsl ssyllpsgti tsaaggghlk
      601 atttgaghwr saywlfqghy afqskyslda tlrhegntrf geshrwglfy alsgrwnisd
      661 eswmeptkkw lsmfavrfgw gvtgnqppka dthysvynvd gkyinsigmr pgnirltdlr
      721 weqvmdwnlg wniglfndll tadinlyskq tsdlftndpk ipstsgftsl ptenggdmkn
      781 qgyeinlsln rvkiagdlsa tfnltfannr ntitamdpir laaingtgvn vpdngeymtr
      841 vllnnpfgal yglrykgvya ysydhfdqaq aegatcpvar dangnviygp dgtpmqmyyn
      901 ytqtkyafkg gdaiyedinh dgsidhydvv ylgsslpklt ggfgfrlyyk gwslnaqfny
      961 rygnkianva rmnaekmhgs enqstavnyr wrkegdgadg shvlpralyg agynwlgsdr
     1021 fvedgsflrl nylqfsygfe sklirrigls rlslyvsgen lfcltrysgv dpevgyggmg
     1081 vttdnattpr aksytlglta tf
//
LOCUS       WP_118146672            1096 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Paraprevotella].
ACCESSION   WP_118146672
VERSION     WP_118146672.1
KEYWORDS    RefSeq.
SOURCE      Paraprevotella
  ORGANISM  Paraprevotella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Paraprevotella"
                     /db_xref="taxon:577309"
     Protein         1..1096
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123894
     Region          23..1095
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrylllmaf lcavwragaq vmvsgrvvda ndglelmgct vaekdatnrv vggmttdmng
       61 nfafkvknvn nklvftfmgy ktqefpigsq rkfnvkmedn tmkvsevvvk aqkrgpdgaf
      121 nipqrevsma mttfkmdame gvsvagadda lqgrvagldi vvggspgsgs qmrirgttsi
      181 tgnsqplvvv ngvpysgeid esfdfgtane eeyadllsvn vedieeitvl kdaastamwg
      241 skgangvlli ktkrgtrgkt rvsytyklsg stqpkgmkll sggdytmmmk qayfnrtlsg
      301 rdetyeqydy delryepdnq nynnntdwvd evtrhgwtnd hyltvsggge raafrisggy
      361 ydqkgtvmgq ryqrfstrsq ldyyvsdrmv fgsefqftys dndrnyenll diaykkmpnm
      421 avyeenadgs stgryynmda esgfnkeqre lknpvalgkl aknnlkgyri mpklslqydf
      481 fnpeehylry lgwvaidlnn ereekflpae cvynaadnyg sanvaetkts gkltvatehg
      541 ltwqsrflnd dhnlqaqalm qlttttshsq yvkmqglpss aindatatgy isgtengnsn
      601 dktlgwmgrv hysfkgryif danlrvdgst qfgpsnrygf fpgvggkwii sdepwlqkyt
      661 gkvltllafr pswgiagrqp gqnylqysvl ttnstgymdm savyptrirl dglkwekvts
      721 lnlgfdmelw ngkvsviydw ykkrtddllf kdidipsssg fatltyknvg rmdndgwelt
      781 vnfnkvvekg kfsldintnf asnknmirsl dpsvlnnfnn hsdfgngayy trlqegnsfg
      841 siygfrykgv ysysydrydq avaegktvpv ardengvpmt nfdgtvkpmy yyhsttkyqf
      901 qggdaiyedi nhdgsidqyd vvylgncnpk ltggfgftlr ydrfslnvfc nyrwgnkivn
      961 marmnaenmy haynqcttvn wrwrkegdvt dmpravynqg ynwlasdryv edgsflrvky
     1021 itlryrfpsn wvkrigmtnl sayltvnnlw cftkysgvdp eisictdtak dyygiavdns
     1081 mtprakewtf glsatf
//
LOCUS       WP_118153291            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118153291
VERSION     WP_118153291.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123606
     Region          24..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrllfllv nlflfvggvl aqtkvtgtvv sqedgepvig asvvvagaar tgtvtdiegh
       61 fslevpagkk lvvsyigmqs qtltpaakmt irlkadsksl gevvvtgmqk mdkrlftgat
      121 tkisgdktkl dgvadisral egkaagvsvq nvsgtfgtap kirvrgatsi ygsskplwvv
      181 dgvimedvte vdaddlssgn aetlissaia glnaddiesf qilkdgsats iygaramagv
      241 ivvttkkgka gtnrinytse ftmrlkpsyr nfnimnsqdq mgvyremynd gyfsfeksyr
      301 asnsgvfgkm yhlmntydsk tgtfglpnte eamnsylqka eyqntdwfdl lfsnsisqnh
      361 svsmstgtdk aqyytsfsvm ndpgwskqsk vqrytanvna lyniskklsf naianasyrk
      421 qrapgttsqs vnnvtgevsr dfdinpysya lntsrtmdpn elyvrnyapf nifreldnny
      481 lsldvvdmkf qgelkykpit kvelavlgay kystttnaat itdqsnqawa yramddatmr
      541 danpwlytdp dkanslpfsv lekggfyret kykmnswdfr atasyndvyn kdhivnlfgg
      601 leinsldrsr syfngvgmqy dmgylpafny nffkqlaeen gqyysldnsy qreasffgta
      661 tysykgryti ngtiryegsn klgksrsarw lptwnvsgaw naheeswfak lnpvlshltl
      721 kasysltadr gpasvsnslv viqsynpwrp fagdketgle iyrlgnddlt yekkhelnlg
      781 ldmgflnnri nvtfdwyrrn nydligpkrt mgvggeiyky anvasmrshg eeltistrni
      841 etkdfkwstd fifshskntv tdldsranim qmitgtgftm ngypvrslfs idfkglnkkg
      901 lpivvnqnge etsyggdlyf qstttdylky egptdpting sfgntfsykg fklnvfitya
      961 agnkvrldpa fsssysdmta mpkefinrwt qagdeaytdv pviadqrmkq ndnyigylyn
     1021 aynystarva kgdfirmkei slaydfpgkw iqalrlnsvn lklqatnlfl iysdkklhgq
     1081 dpeffntggv atpmprqftl tlrvgl
//
LOCUS       WP_118152662             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudotabrizicola alkalilacus].
ACCESSION   WP_118152662
VERSION     WP_118152662.1
KEYWORDS    RefSeq.
SOURCE      Pseudotabrizicola alkalilacus
  ORGANISM  Pseudotabrizicola alkalilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudotabrizicola.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Pseudotabrizicola alkalilacus"
                     /db_xref="taxon:2305252"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54830
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkelf egenrvamtp dsaiqliklg htcvietgag akagfsdasy ekagvevvps
       61 aaalydaadv vvkvrgpead earllksgqt lisffwpaqn adllaqiagq gatavamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aivnafdvrp evaeqiesmg anfvflefda selpdgaatg gyaapsspaf
      241 aakqlakfre lapemdivit talipgrpap klwtadmvqm mkpgsviidl aaerggncdl
      301 tvpdqkivtd ngvtvvgytd fpsrmaaqss tlysnnirhm ladltpkkdg viahnmeddv
      361 irgatvthag avtypppppk iaaiaaakpk pkaveltpae kraqevaafk tqtrnqvsll
      421 avgtvlllgl glvapasfmq hfivfvlavf igfqviwnvs hslhtplmai tnaissiiil
      481 galmqigsgs ylvillaals vfmaginifg gflvtrrmla mfqks
//
LOCUS       WP_118152214             941 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118152214
VERSION     WP_118152214.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 941)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..941
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104293
     Region          52..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnknavlm amallslpas aqvkidtiap hryaaqsidv ganvnfsreq stsavsvits
       61 estnkrsakn ignsilgqgs glislqnsgn yaginptfyi rgmqsldgnt plfvvdgier
      121 diqyisaeev esvsvlkdaa atalygykga ngvvlittkr gkfnskeikv nldhainfma
      181 hkpkfvdaqt yakamneaya ndgfenpryt qeevdafgsg kypylypnvn wvdetfrnhs
      241 vtnmlnasft gggekfkyya lldlqydngf vknpdthegy stnnkyvkgn lrmnmdmils
      301 knttmkvnll gvlaesnapg nsaklwdmvy glpsaafavk gedgkwggns twagtvnpva
      361 qsqdagysrn hnrgiytdlt irqelpavlk glavqgriay dhfsniyeny sktyvygspt
      421 vvdwldgepq lgkaftggse sdlgasistn sftrrfhada sadyqntfgv hsiysqlkyd
      481 yefsdefain stlyrqnisw ythygllnry fldlalvesg snrlapgskw alsptvsaaw
      541 vlskenfmkn lnwvdflklr asygiiqtdi lpesgwmyym qqyqttgety pfnsgfqsdf
      601 grtyldaiat sgltrekaak fnagvdatlf ggldfsfdgf yqrrsniwvs tagkysselg
      661 vdapyegdgi vdswgweasl dynkqigdvk fniganidyy rsqikeqdea pklypnlvst
      721 ghrvsqlfgy kaigffkdqa didaskpqll gstprpgdik yedvngdgqi dtndktaigy
      781 stvapeiyyn ihlgvewkgl gidamfqgtg rytgvlstks mykplvgntt isqyyydnrw
      841 tpetastakf palsstsnan nyntntlwmf drsffklrni evyynfpkal laktkllnaa
      901 klyvrgvdlf sfdhldesdp evfgatnpln rsivaglsvt f
//
LOCUS       WP_118154283            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118154283
VERSION     WP_118154283.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114927
     Region          32..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqrmkhcf faltlcctag smygqvaqds sktiekkssv ngkkiqkskf sddpielnnv
       61 vvtalgikre ekslgyatqt vsgseitatm panwsqalqg qvaglnvisa ggplsstqin
      121 lrgnvsmnmd gngalivvdg vplsspmnnp ggsygaggns egsidfgngf sdlnpddies
      181 iqvlkgasas alygsraang vimvttksgk kakkglgisy nfnnsweqaa hfpdyqyefg
      241 qgvaknigsk gtewagqpyy sygagddgla stsgtssafg akfdgqmfyq ydpekegrad
      301 vatpwraykd nhsglfqtgh tmtnslaltg nngtgnmris lthsksewil pnsgyqrlta
      361 afagsqqisk rvkinarmsy tyrdventpq ltynsnslsy flifmnpnfn ldwfkpmwyk
      421 gkenikqirp fssylpnpyv llyeatnpak khsfngnisa nftinrfldl qlrsglqata
      481 qqqeqhrpwd dkafptgffk kqnifdyevn sdvllsyhns fenglnvnas aggnmmqsyy
      541 dllsasvtgl ntpgvyslan gvsnplvgtt irkkrvnsly fmanlayqem lflditgrnd
      601 wsstlprknr sffypsvsls gvlnsmmkmp kwvnllkvra swaqvgndtq pyktspyytt
      661 sdfsgslvkp gtlynadfkp emstnweggl dfkafgsrlg ldvtyyynrt knqilnapfd
      721 pttgytkgti nsgcvsnrgv eivlrgtpir nrdwqwdmta twstnknkie slsefaderq
      781 ilgsyvsgnv siigtkggtt gdiwgyklkr nakgeviits aglparpsei eyvacalpdw
      841 egafntslrf knwsfsmqwd gkvggktysq shhkmceqgh laetlngrkp gtslyldiad
      901 pdvlklfekq kitpvagvyc iapgvvdngd gtyspnqklv tlesyykeyy rignvetntf
      961 sttylklrev rldyqlpksw lkntfinnas vgiygrnllc itsypmydpe ttsldgntfv
     1021 pgvevgtlpt srswgvnlkv df
//
LOCUS       WP_118154664            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118154664
VERSION     WP_118154664.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115544
     Region          41..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkktmflgl lgaglmwmpa sailaaqmnn aamsvqqnqg ikgtvvdatg etligasvkv
       61 agttngavtd idgnftlnck pgatlevsyi gyktmtvkaa ngmkiqmqed gkalnevvvt
      121 algikrdrka lgygleevkg eeltkaketn vinslsgkva glvvqntagg asgstrvllr
      181 gntemagnnq plyvvdgvpl dntnfgsage aggydlgdgi sainpddiet mtvlkgpaas
      241 alygsrashg vilittkkae kdrisveyng sytidtqlak wddiqevyga gyngelptss
      301 tsgtnaswgp kaddfmfkyf dgeerpfmmh pnnasgffrt gfttqnsail svnsgktgmr
      361 fsvtdmrnkd ilpntnmsrd nfnlrvntsa gpvdfdftan ytrekvknrp algdsqsnvg
      421 knlmtlagty dqawlkhyed adgnysnwng ndqynknpyw dlyknsntsd kdvfrftgka
      481 iwninkhfkl qgtigtdins mnfedfiakt tpgtpagklt dqifnnrtln aeilalynns
      541 wgdfdvnata ggnifkvnnk tttniglnqq mngiqnimny qeqntresmy kkqisslyas
      601 aslgykhtyy legtlrgdks stlptnnnty vypsvsgslv fsefiknkkf inygkirasw
      661 akvgsdtdpy llalnyttgk ysysgytigm ianstqpnkd lkptmtgsye vglemkflng
      721 rlgldatyyn qnsknqilsl astttsgyay rlinageiqn qgveialnar alqikdfawd
      781 lgvnfskntn kvksltdgmd yfelakatwc gvsvgaqvge nygairghdv vrneqgqvvi
      841 naatglpmvd qnvktignss wdwtggfytt fsyknfrlsa sfdvkvgadi ysmsmrsayq
      901 tgkakgtlag reewysseea rkasgmdlaa wreagkckgl vvdgvidngd gtyrkndiav
      961 npedywkhva egvqsafvyd nsyvkcreit fgytfpesil gkyvkgltvs fvarnpfivw
     1021 knipnidpds syntsglgle ygslpsrksy glnvnvkf
//
LOCUS       WP_118155073             875 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides stercoris].
ACCESSION   WP_118155073
VERSION     WP_118155073.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 875)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         <1..875
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <13..874
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 rrtlkslvad lriivttksg kegkvqvdfg asfgfkkvtk mtevmspydf vayqreigsl
       61 dygnyndmdi wksidgidyq deifgrtgnq qqynvnvagg skqltysvsy ahneeksiml
      121 gsgfkkdnin aklkselnkw ltldfnarls ystieglsgg adtnesnaan stvanavvfr
      181 pvnalshssd ddeesnaalq ktplerllat nkgrnsfrqn ynfglnwkpf knwtfrsefg
      241 ygwryedteq ywgtdavsns kygyngrpqa yllrettknw rnantltyen kkmfdgrdrl
      301 nvlvghevss smeesienvs vnfpttmgfe dmkanmgagt alpnqstisa eenmlsffgr
      361 vnytmmdkyl ltvtvradgs skfgdgnrwg vfpsaalawr isdeafmant kdwlsalklr
      421 lsfgtagnnr insgllytty slsgndsrnp ffngtstpml ehgtylynpk lkwettvtrn
      481 lgidygfwnn risgsvdvyw nttrdllmka eipgnsgysy qyqnfgqtsn kgiemsmdav
      541 lvdtknfsln ftanvaynrn ridklttdsp wqssnwagst iskyedfrve eggrlgevwg
      601 frtngyytvy dpvtnptgel vwgdkqwvlk dgmkdnspti tggsyypggl kiqtdengnp
      661 lkqrlgntva pwvggfglng rfgnsrtgel dvniffnyst gnviingtkl assfrsgsrt
      721 gynlnndfrl gnrytwidpe tglnlassst avlnhygdmq aaglrlnein ssanmynpaa
      781 astmqlidya vedasflrln nltigyslpk hlvkkaflqn vrvyltgynl fcwtsysgad
      841 pevdvsskrn amtpgvdyaa ypksrtfvgg initf
//
LOCUS       WP_118155031            1194 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            stercoris].
ACCESSION   WP_118155031
VERSION     WP_118155031.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1194)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1194)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1194)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1194
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         1..1194
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133961
     Region          35..100
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          113..1190
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrkryllfp lffflfclpf caeaqvgekk ltvefkneel ssvfkqlski sgykilftyd
       61 dvksytysga ikdknireil divlsgkkle ytidkefiti ttkgpskqak vytvngvvls
      121 addgepliga tvmvkgtstg vltdidgkft lpnvssrskl efsyvgmlpq slspsptmkv
      181 tlqsdvqtls evvvtgmqrm dkrmftgatd qlkaenikmd gmadisrgle grsagvsvqn
      241 vsgtfgtapk irvrgatsiy gsskplwvvd gvimedvaei gaddlssgda etlissaiag
      301 lnaddiesfq ilkdgsatsi ygaramagvi vvttkkgksg tnkisytgef tmrmkpsysn
      361 fnimnsqeqm dvyknmeqng slsfvdsyra sqsgvygkmy hlinqysatg gvfglantpe
      421 argaylkqae frntdwfdll fsnsisqnha vsmatgtdka syytsisvmn dpgwtkrskv
      481 qrytaninst ynifknltln lignasfrkq qapgtlgsqa dpvsgevkrd fdinpysfal
      541 ntsrtldpne yyvrnyapfn ifheldnnym dlkvtdmrfq gemkwkpiqk velsilgayk
      601 yssttqnhyv kdysnqaway ramddatmqq anpwlytdpd kintlpesvl pvggfyrdtk
      661 ytmssydlrs tvsyndvfne nhivnffggm elnatdrskv wfngagmqyg mgmlssydyl
      721 ffkqgneent pyntvdetka rqvaffatgt yswkgrytvn gtvryegsnk lgksrsarwl
      781 ptwnisgawn aheetwfskl nsilsnltlk asysltadrg pafvsnslam vssynpwrpn
      841 advmesglgi lqgknselty ekkhelnlgi dlgfldnrin fsmdwykrkn ydligwlstt
      901 gldgeigkya nvasmrshgi eltlstrnia kkdfkwntdf ifsktknkvt dleafssvmd
      961 mvsgygfamq gypvrslfsl dfrglneegl ptfinengel ttsninfqer nnkshliyeg
     1021 ttdptitgsl gnvfsykglk lnvfitysfg nvirldpvfs nqytdldamp kefknrwmrp
     1081 gdehrtnipv iadkymnvnd sylsraynay nyssdriakg dfirlkeisl sydlpkkwie
     1141 plkisnlglk lqatnlflly addklngqdp effniggvav pmakqftfti rlgi
//
LOCUS       WP_118158633             944 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118158633
VERSION     WP_118158633.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..944
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105499
     Region          41..943
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiyrrfil savlvfpvvi sagaqelagd nasslqndsl vqvafrkvsq nnllggasvv
       61 nveeltkkny ntwsltdmqg yvggyngnsl wgmdeklilv dgvprnidyi spteisqitf
      121 lkgaqavvly gsraakgvim ittkrgkstd lqvdvrantg fyvaksypey lgsaeymtly
      181 nearandglg alysaediyh ygsgenpyry anvnmyssdy ikkaynrsdv taeisggnhr
      241 ahfytninyl rsndvfkige akhngtngln irgnvdltln dfitayvnak vsfysrrsan
      301 gsyywsaast lrpnrispli plsyidanaa sawdlvansn nivdgkyfla gtqsdmtnvf
      361 gdyyasgysk atdrsfqfda gvnigldkvl kglsfhtrfs vdystayits ynnsyatyap
      421 twsnnggkdi ivgltkyned kksgvqnisg ssdnqtvlfs gqfdyentfn ddhhlaamli
      481 asgyqqsysg eyhktsnvnl gmqlgynfrn kyyadfggav ihsaklapgh rnafspsltl
      541 gwklsnesfl enspvvdelm lsvsgsilnt dlgidnyymy dgyynqsdga wwgwresvsl
      601 hstnskqgan edlsfikrke lsvnlktslw nrmitadasf fvnsiegkiv tsttqypeyf
      661 ftyyptasfr pyinydndrr mgfdfnvnyn krfgkvdfta gvtgtyyttk atkrdelyqd
      721 kyqyrkgyav dgiwglqcig ffkdeqdiid speqrlggti rpgdlkyvdq nndgiiddkd
      781 qvylarggwy gaplalginl takwkgltff vlgtgefggh amknnesyyw isgedkysav
      841 vrgrwtpeta atatyprltt esgtnnfyss dfwmyktdaf rlakvqvtyd lpskwfknsf
      901 vhgvsayisg sdlltisker ealelnvgss pqcrfynlgv tatf
//
LOCUS       WP_118160715            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            splanchnicus].
ACCESSION   WP_118160715
VERSION     WP_118160715.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter splanchnicus
  ORGANISM  Odoribacter splanchnicus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Odoribacter splanchnicus"
                     /db_xref="taxon:28118"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121011
     Region          47..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqknacsvsr slrkqrltai ifcllaaftl pvplqagvpq qqstypvngl vtdaegvplp
       61 gvtvrygitg gatdngghfa lrlpeergrl tfscvgyktv tvgyrageml rvrleesres
      121 leevtvvayg eqrrgqvsgs vatvdaarlq nkpasnvltl akgqmagvyi asqsgdpggn
      181 dvsiivrgan dlaiagnrnp lfvidgvias ddaslkvggn pltslnpddi etftvlkdaa
      241 aaaiygsraa ngvviittkk grynqhplls anvshtfilq pllperiggn aerlarleam
      301 knyagvyydr etdsyrypeg yalgkpydyf wnegngadmt vyqdslnpfy nnstdlmayy
      361 lrpahatnan iqvrggaegi aysvglgfyd eagtlrgtgn rrfsafsnla fkpahhlygn
      421 frfylaytdn nrsrkgvdaf npaptaystl pdflftstvl pgpgtpyfge ltrryestre
      481 kndsyklrts fdltyeiadg lalksgvavd ylqnnqnvfl pkevneygkt yssgtiarhl
      541 mvlnenllty rrtfgsshtv dlllgfsvqq demnnntgka lgaasntihy apwysqvyda
      601 earldlkdyy sdyekktmvg lfgrlnynyr eryyagftlr rdasstfged vrwgwfpsyf
      661 vgwtfteepf mqalkpwlny gklrfsqgrt grifeypyla qgeldqgapy lghptvvpew
      721 wagvsnsglt wektteydag ldlglldnri gltfdyylkr trgllynppt pgthtgflap
      781 wrnmygidne gvelevkgel vrgrtwqwnl sfnvsrnrnr larslngrdf qntaarfann
      841 isviglplyg iyafddrgiy dsqsdvpsyy edgvkkylrg egsayyragd riitdvdgng
      901 qiynygtlae driyigsplp qfqggistdl mwkgldvtvl fnfvcrkwvl daargaslgt
      961 ylalnpadma rpyltgsldg lfwehpgdga pypanrmeng lynfatnlas naqrisylkl
     1021 qavtvgytlp eavrkatgfg arifisgenl ftltdyrggd petvdpytgv dnynayplsr
     1081 rftigltlnf
//
LOCUS       WP_118160677            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Odoribacter].
ACCESSION   WP_118160677
VERSION     WP_118160677.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter
  ORGANISM  Odoribacter
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Odoribacter"
                     /db_xref="taxon:283168"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120511
     Region          50..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkqlygrg vpmlciacql tvaplffssr vqavpvapti lttaqtqemr tikgivrdvn
       61 nqplpgatir ikgtstgvvs dvdgnytitv pddpnttllv sfvgmkpqeq kigkstalnf
      121 ileedatvld qvvvngvfer kantftgsvr tigkddlkrv gnsnvlqslk nldpsimffd
      181 nmslgsdpna mpemvlrgks sinmedvdlk atyqndpnap lfvldgfets lqkimdldmd
      241 rvesltilkd asakaiygsk aangviviel kknpsgdlrv tyngsmeiea pdlssydlcn
      301 aaekleveqa fgmfndpgad fesqrmmikm ynqrqsavks gintdwiskp lrlgvgnkhs
      361 lsvelgdkal qaivdlsyqn ikgvmkgsdr tnisgaisll yrhqnflfrn qltitsneah
      421 dskygtfdey tklnpyytpy dqyghltdni vpsldpgnsv tvnawyedie feanplynaq
      481 lntllqdkyv ditnnfelqw fvmtglkata rfglteqrsr sdefypsdhl kfasystdrl
      541 tekgsydlen geqhslsgkf dvqynknfls vhdifvnagf dlsrkqsstn lqqaegfpsd
      601 kmtdiifarq ylkdakpkgt eetvkdfgyy lsanysydnr lnfdatfrqs assmygansr
      661 wgkfwsvggs wnihneswme gsnitqlrlr attgstgsqs saaynalasy eyfldktygd
      721 qlgaqllnmr nedlkwqekv eqnygfdfny knrysftfey yhsitnnavn plslapstgf
      781 ttvqenvgkv lnrgfdlrag atvwqqpadr sylsfslmis rnknilkeis eamrsyneqq
      841 eklategnvp vqkyydgvsm daiwampslg idpangreiy iakdengnpy rtytydaaqq
      901 vicgdelpkf qgnagvnfey kgfginavlt yqygakmynq tlvdkvenad mkynvdrriy
      961 tdrwrkpgdi alykaiseev yvsekqqfas ektyptsrfv qkrnelkiss lqlsydffrh
     1021 dfvkkigler illrfnandl ftfssidier gtsypfartf nfslnvtl
//
LOCUS       WP_118161179            1016 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118161179
VERSION     WP_118161179.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1016
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112501
     Region          30..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknkilila llvclsipvr aqntdnniig ivvdksgnpv ygasvnvegg avetrvetdk
       61 dgkfeiavek gqrlsvvsvd kgsttvvakt dgpmtivmgy aaqtidvgan rtfnrhesta
      121 avsttyneef nkrssrnisn slygyglglt tlqnavstgl madptfyvrg lqslssstpl
      181 vlvdglerdm slvspeeves vsilkdaaav alygykgvng ailittkrgk yktkeitfty
      241 dhiintqsrr pefvdaatya savneargye glgarytpee vdafrngvgs ggasrmypyl
      301 ypnvnwidet fkdrgvsnky tiefrgggak fryytmanll tdkgfiktpn andgystqnm
      361 ysranlrtnl didltattkl klnllgtlse sripgasvnl wdmiysipsa afpvrtedgs
      421 wggsttwagt snpvaqsqga ayskghsrsl fadltlsqdl sgllkglgan frlaydnysn
      481 iledhsktyt yagyatswtt ngpfytaisg gessemgsga gidnwarqfn fagsvdynrs
      541 frkwdvysqf kwdyeyrdsy glnttiyrqn vswynhvgfs nryyldlalv gsassllapg
      601 hkwafsptis aawvlseekw lkdvswvnfl klrasfgvin vdylpkdgst tvydywdqiy
      661 tttgtqykfn ssydsefgst iigrlatans thekaykynv gvdavlfngl dvtaegyyqr
      721 rkdiwvsseg kytdvlgvda pfenagivds ygvelglnyt krlgdvvfnl ggnfawnkne
      781 ikeqleeprl yknlvqtgnr lgqvygmvae gffkdkedia nslpqnfstv vpgdikykdv
      841 ngdgiidand ktaigystta peiyysfhlg aewkgigvdv mfqgtgnysa vlntksmfwp
      901 linnttlsth yyenrwtpen qnakyprlss qsnannyqan tvwladrsfl klrnaevyyr
      961 fpeewmkktk ilgsaklyvr gtdlfcsdhi dvtdpecygv atplnksvvv gvtigf
//
LOCUS       WP_118161188            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118161188
VERSION     WP_118161188.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112686
     Region          30..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mymknriitl lcivclftgn evcraqvqev isgvvrnesn epldgaiisv pdnpeyttss
       61 dkdgkfimei psgasmvick ipgyrnqtmk ftlnkpvefc lisdiagqdt slevamlqke
      121 rkggytgais tvqgeelvkt pnsgfsatlt grlagltsiq ststpaddat tmyirglnsi
      181 ngnsplvvld gipaplfdmn tldantvesv silkdaaaka lygprassgv ilittkrgei
      241 grtkvnvnmd fsiqqatqrp kivstgeyaq mrnqallndg gtplyslyei agftdgtmpg
      301 hdwydtfmnd aasmqrynvn isggnnrvky lvnagylhqn slidaekndn ynpalklhrf
      361 nilanvdvtl hrylncflnt nvtidrmnqg yngtgdimns iyqmaptvpg pitedgkvit
      421 aeyneyptyg linrsgyshq tginlnvayg mnldlgfltk glsvkgivgy eanydgtiyg
      481 stdyaryaan gsglfgthtt lplslsktan mryfinfqgf inynrifggk hevdafvsyf
      541 nenmmkngdl pydrlslmgh vkygydsryy iqgdftydgt eqfkpgnrfk ffptvsaawv
      601 vsnesflkdt dwlsflkira sagwlgndqi sdtrflyatd vrykdagyll snyygfhtve
      661 gmqgnpyihy eesfqqnygi dvtlfnslgi tfdywnvkqt qmaiqnnsvs saqgiasenl
      721 pfenlgkmnn kgfdlelsyi knlkcglrmt irgnmgynkn evtdikelnr tasgyyypyr
      781 ktgysagqqf gylidysngn gyynsqeeid ksglrfsgas prpgdfiykd lnndgnider
      841 dqapmdkaqt lptlsyggsi qleyknfdly vqlqgvsgta ayysgcgifd nayqgvytdl
      901 hrnawtadry aanekisypa lttgsssslq sneffysknn ymrlknvalg ytlpkrwssk
      961 lklekirfyi sganllttss lkfdnldpeq ysysvypiyr tfniglnlnf
//
LOCUS       WP_118161264            1121 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118161264
VERSION     WP_118161264.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1121)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1121)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1121)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1121
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1121
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124207
     Region          110..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnyrkkailm vvalfclnia ilaqavslkm nnvsvkeamt qlknksgysf vykvgdldtr
       61 kivsvkakql neaidqilyg qevvyevkgk niivqkgqar qntskdtkkr kvtgtvsdan
      121 gepiigatik ekgttngtas dldakfslev spgavlevsy igyqtqevkv gdrvslsvtl
      181 aenqqildev vvvgygttsc knlttsiatv ktekiskaat snisgmllgr aaglqatvas
      241 pqpggginis irgggtpiyv vdgvvmpsgs fevgtgstsl pssvnragla glnpndiesi
      301 eilkdasaai ygigaadgvi lvttkkgkeg kptivyegsy svqkhypyld vlsgpelmnm
      361 vnvfskenyl ydkgqypygn aayddkwtpi ftptqianap ttdwldkvlk tgavtnhnlt
      421 isggsekfky ylgvnyyked atvynsdmer yslrtnitsq ltnflkltti vnlnqnnytn
      481 stvggdvgnl rdqgagalfg aifypsylpv ydaegqynvf srtpnpvsmh dindkseqng
      541 yymnfsldvd iiknmlsakv lyglnkents rdsyipsdiy yalqrksrgn lgygkrqqst
      601 legtltfqhk fgelldmnlm agmgryldsg dgsdisyena ndhiqgssvg madgpfypts
      661 ykyknekrsq fvrgsfdlfg ryvvsaslrr dgtdkffpsk kyalfpsvsl awkmneesfi
      721 kniswinmlk lrasygetgs dnlgttlygi vttaredvqf nnnsvtyipy ilsganyedv
      781 twqktvmkni gldfsifrdr iwgsvdvfrn dvthllgtap tellgmhgtr pingghykrt
      841 gidvslnsln lqthdfkwts qitmshynav wiermpnydy qkyqkrknep mnafyyyktt
      901 giidmdksnm pesqrslgpa acmpgypive dkngdgiidv ndsymdnmlp klyfgfgntf
      961 twknfdldif mygqlgvkkw ndaysysada gnlsrgvdah nvgiysyniw ntqtntngyf
     1021 pgiaisksva lpenlgfdyt renasyirvr nitlgynlgp kelsvfkgyi rgirvfvdfq
     1081 npltftkykg ydpeintsss nltggqypqm rvysigaklt f
//
LOCUS       WP_118161546            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118161546
VERSION     WP_118161546.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117944
     Region          46..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqklnsgald rillfvyils lstnaiaqnk nnsketyllp phgnyvygrv ieklskepmv
       61 gvtirldghs tgvitdingc yvltlpekgg lviysyigfe trkikvtsrq kvdvqmveat
      121 esiqevivtg ynsiqkesft gnttkieked llkvnpnnli saiqtfdpsf riqenlaags
      181 dpnslpqfvl rgqtgigett lgqtstssis revlsgnsnl pifildgfev dvekiydldm
      241 nsihsinilk daaatamygs raangvivie rrapeagkfr vqysgvlsae lpdlssynlv
      301 narekleter laglydsntp eidpytngyy qrlnnvltgv dtywlsqglr talnhkhsvf
      361 idggendvrw gvelgfrgte gvmkhssrkn anaafyvdyr igglqiknkv tytynkstdv
      421 pfnsfsdysh llpymrlyde ngdyvrrlek fdgasgtqvn plyeinfyns fdhsgydevt
      481 ddlslnwrit dglrlrgqfs vlmrnstgdl ykdpasasys astgningek testqkrtvi
      541 dgslslmynn tfkghnlnic lssnmrqtqs tasetryrgf pggdlvssny aaevygkpss
      601 sdnttrlvga lltsnytynn iyladltgri dgssefgsdk rwsmfwstga ginihnydfm
      661 ksnelfsmlk frvsygltgk tnfslysakd myqlqtdswy ptgygvflyq mgnpnlkwer
      721 kytldygvei glwhdkiylk asaydertid litdytipss tgftsykenm gkvkntgvel
      781 elrarlysdr nwlfqlygsf arnkntiiei sqamrdynkr veelfsgynp esssdskyak
      841 tylkyyegas ltsiygmksl gisptngkei ylrrngdvtd vwsadewtii gdtapkgqgs
      901 fgytlsykql smfasflytf ggdaynntlv syvenadikn dnvdkrvlld rwqkpgditt
      961 mkdirdrnvt tgassrfvqk nntlqwsslt msynfrpeql kklhlsglrl sftmndlfyw
     1021 stirqergld ypysrsfnlt tniif
//
LOCUS       WP_118162867            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118162867
VERSION     WP_118162867.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112795
     Region          28..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkyknlmwa claslaipag aqdadnnirg mvvdkwghpv ygasvmvkgm petrvetdkd
       61 gkfsieasag qqlnivsvdk gmttvkaegk slvkvvlnya gqsidvgagr tftrsestaa
      121 vstiynedfd krsaknvsns ligqgmgmmv lqnsgnyadv eptfyvrglq slssssplil
      181 vdglerdmsl lspeevesvs vlkdaaaval ygykgingai littkrgkyn skeirftydh
      241 vnnymdrkpe fvdastyaqa yneargyegl spryadkeve yfrngdfpyl ypnvnwldet
      301 fkdsgisnky tiefrgggsk fryysmldlv tdrgfvkegd mndgystqnk ysranlrtnm
      361 didvsrttkl kvnilgtlse slrpgasanl wdmiytvpaa afpikdedgl wggnnttwlg
      421 tqnpvaqsqg aayskghtrs lfaditlnqd lsavteglgf nfrlaydnys siwedhsqay
      481 qyggyvvsyd eltgplytht tageptemgk sasinnwarq fnfsggfdyn rtfgdkhdvy
      541 sqlkweyeyr dsyglnttiy rqnvswfthy gydkryfldl alvgsgssll apghkwafsp
      601 tvsaawvlse edfmnnaawi dflklrasfg iinadylpas dvydywdqiy tttgtrymfn
      661 saydstfgtt elgrlastny thergykynv gidatlfkgl nlsvdayyqr rnniwvsseg
      721 kytavlgqtp pyenagvvds wggefsldyt krigdvvlna ggsfnwnrne ikeqleeprm
      781 ydnlvqtghs lnqiygleav gffkdaddia nslpqsfgav ypgdikyrdv ngdkvinsnd
      841 vtaigystva peiyytfhlg aewkglgfda qfqgtgrysa ilntksmfwp llstttlsth
      901 yyenrwtpdn qdakyprlst qsntnnyqtn tvwladrsfl klrnievyyn fpkswlqktk
      961 figdarlyvr gvdllcfdki dvldpesyga tnplnksliv glkvgf
//
LOCUS       WP_118164780            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118164780
VERSION     WP_118164780.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112182
     Region          44..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkieratqll flllisqggn aayanlprga saspvqvsaq ankitvsgtv vdvngeplvg
       61 vsvlekgtgn gtitdidgnf tmsagegatl eisyvgyqnl tvsaketlgv lvmkedteql
      121 devvvtalgi krsqkalsyn vqevkndvlt kvkdanfvns lngkvagvsi qrsasgvggg
      181 trvvmrgnks ikgdnnvlyv idgvpmgnqa drtgdgtgfg agrtssegia sfnpediesl
      241 svltgpsaaa lyganaangv ilittkkgaa gkvsvnvsss aefsnpfvlp rfqntygnvs
      301 geaaswgekl pvpssynpad ffntgttftn sfnlsvgndk nqtyvsgsav nakgivpnnk
      361 yhrynamvrn ttkffndklt mdlsasyvre yynnmlsygt yfnpllgayl yprgenfeke
      421 kyferydael gynvqswtpg dfgmavqnpy wvayrnlrpe vkdrymlyas lkyeitdyln
      481 vsargrldnt ytekedkrya sthgtfakpl gryaysnetf rqkyadiman lskpfagdfy
      541 anvnvgasfe eydtkgrgyg gqlllvpnlf aydnvdpstg vpsqtggdnr kmnlgvfgsa
      601 eiswksavyl tltgradkps qlinskspwi fypsvglsai vtdllpetmr qsispvlgfl
      661 kvrasytevg spipytgltp gtithsiegg vikpfkyypl pelkpertrs yevgidskwl
      721 nntvslgvtl yksntydqll eaklsetsgy dymfvqagnv enrgieltlg ydqtfgnfsy
      781 stsltatanr nkiialasnv knpvtgeald lsdikvgrfr lregeevgti yaeerlkrdq
      841 dgyivynegq tittestepy klgsvnakwn lgwrngftyk gfnlnflvta rlggiviskt
      901 qavldqfgvs qasadardag kvmvgnvavq pkdyyesvvn ldaynvysat nvrlqeaslg
      961 ytfpnswfkg tpfhsvnlsv ygtnlwmiyn kapfdpelaa stgtfgqgyd yfmlpsqrty
     1021 gvslkfgf
//
LOCUS       WP_118166671             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nostoc
            sphaeroides].
ACCESSION   WP_118166671
VERSION     WP_118166671.1
KEYWORDS    RefSeq.
SOURCE      Nostoc sphaeroides
  ORGANISM  Nostoc sphaeroides
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Nostoc.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Nostoc sphaeroides"
                     /db_xref="taxon:446679"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41491
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakeie vcerrvalip dtvtrlvkqg levwvetgag ersffgdsdy eaagatiisd
       61 taklwgetdi llkvsppqer edgrseidll kegavllsfl nplgnpvvaq qlanrkital
      121 smemiprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkleeetvaa ggyakeisea
      241 skqrtqevva ehvknsdvvi ttaqvpgrqa prlvteemva qmkpgsvivd laaeqggnca
      301 ctepgkdivw ngvtiigpin lpssmpihas qlyaknvtsl mqllikdkal qvdfgddivd
      361 aacvthagei rnqrvrdalq alntqqpavn
//
LOCUS       WP_118166182             948 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Phocaeicola].
ACCESSION   WP_118166182
VERSION     WP_118166182.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..948
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106810
     Region          43..947
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkniriksvl caalatssly vgaqnlpsel ldassdslsv aeeelvqvay rkvnkkdllg
       61 gvssvnveel mkkdyftysl dgmenmvsgw ngsslwgmds ylvlvdgvpr dannvmpsei
      121 kditflkgas avvlygsraa kgviyittkr gkegdtridv rgntgffvpk sypkylgsae
      181 ymtlynearv ndgmdplysd vdiynhgsgi npyrypdvnl ysddylkkay nqsdvtaeis
      241 ggsekarfyt ninlyntgsl ikvgnakddr ttrfsvrgni dvnlgqyvkt yvnanatfyd
      301 grsargnfwg aaaslrpnri splipvdyim qnntdawnlv nnsrylidgk yllggtqvdq
      361 tneianlyaa gvntytsrqy qfdmgvdvdl smllkglsfq trfaidyatt ynryygdtya
      421 tyepqwanvn gqdqivgltk ygddvhdgiq hiagswnrqt mafsaqlnyn nkfadshnis
      481 amliaagyqq gesavyhkts nvnlglqvdy dylskyymsf ggalihsarl pennrnafsp
      541 sltlgwrlsn esfledssvl ddlmlsvsgs vlntdlgidd yymyqssydq angawwgwad
      601 gnqshatear rgnnsdlsfi krkeisvglr gslwnkmltf dasffknsle gmlvqpsnsy
      661 pnyfvsywpe stllpyvnyn nstrtgfdla lnfnkkmgev dfnlgvnaty ytnentkvde
      721 lyedayryrk gkptdgmwgl qaegfynsee eiqnsgitss fgelkpgdlk yvdqngdkii
      781 dekdevylge rygwqgtplt vglnltlkwk nftlfalgtg ywgasafmsg dyywvygdkk
      841 ysevvrgrwt petaetatyp rlttqtdnhn yrnsdfwmyk tnrfnlsrlq ltydlpkqwl
      901 gnsfvrsfsv yayasnllti skerekleln tgaapqtrfy nigfkigf
//
LOCUS       WP_118170899             636 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118170899
VERSION     WP_118170899.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..>636
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          58..>622
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkdthsri tdkcrclfvv aysamsitgl ssvlavenha lsspvsdrve svqqkkhvsg
       61 nvqdangmpl igasviikgt ntgmitdieg nfaldakqgd iivisyigmk saevkvpang
      121 qirvmlkeds qlmdevvvtg ygdfkkatyt gsasvlntdk leslpvvsva qmmeanipgl
      181 ssvasssqpg skatvrvrgi asmnastepl yvldgvpvas rdmsglsana sagglgliet
      241 lnpadiesit vlkdaasasl ygakgsngvi littkkgkeg kmrvsmqaty gitdiaynyr
      301 pimggeerre liyegfvnyr lnqgdseaea kayadgqidn yaarpangya dwedallkkg
      361 hqqdyslsvs ggneksnfig tlgytnqtgi sinsgmerft gridanskwn kfeygmnatf
      421 swtrnkhtpe gqyyasalys skyqltpsip iynedgsyht gfqnngginp lyensvdsny
      481 arlartmasa kaayhildgl klstvftvdy slnkdfffys pdgkdgeatq gsgqmmmier
      541 msytsqtnla ynktfgkhni navlayevmk ydyedmygek qvygqtlnps ldngakpadl
      601 tntrqedamv syvgslnygy ndlsstykcn flgadn
//
LOCUS       WP_118170997            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118170997
VERSION     WP_118170997.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115795
     Region          25..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkqclviv mtllclcvka qnlrvtgvvr dksdviigas vmvknstvgt vtdmdgrysv
       61 evpangvlif syigytpvek qvdgqtvinv tmnddvqaid evvvtaigik qqkkklgytt
      121 qqvntealdq pgtvnvgnal sgqvagltvn nptgifqaps fslrgktplm vidgvpvesd
      181 lfdvspenie sinvlkgtaa aalygsrgkd gailittkla kedgltvtag lssmvsagft
      241 vfpetqtefg sgsngqyafw dgadggisdg dmtwgprfag qkiaqwnspi rnketgetip
      301 wwgdvsgtiy ddqskyervp iawephdnlr dflrtgiitk atfsvasksk kanynfngdf
      361 snqrgqvpnt svytgglnfn smynlsnsvt lsanlsynkv yspnyprygy gpknhmytil
      421 lwmgndvngk elaehyyrpd segtrqanyn yawynnpyfa aneltqkhdr ntmngqlkln
      481 wdvipglslq graagrlest fedmsvpksy mnygdsrngd yktwntdqld inadflatyt
      541 rafsrnftlt vnagtslyyr qirkqsqstd glivakvynl gnslnpvsat nsmnekaies
      601 vygsvnvdlf eslfltftgr ndwsstlakg nnsyfypsvs lstlvneyvk lpswmdylkv
      661 ngawaqvssd ldpyslyaty sngtlygsip svtypgtlln anilpqktts yevgvstsfl
      721 hnrigidlty yhmldensii elpissasaf tkryvngney ttngfelivs atpvknknft
      781 wnvatnwssn irkltgiygd qekfgdlkkg dradamyate wektpdgrli ldantglptq
      841 safktkvgnq spdvrfglqn tfkikdftvn idmdgaiggt listttqkmw wggkhpkstm
      901 yrqeeydngg kpvyvpegvn ivsgevtydv ngnivsdtrv ykknetavni qtwaqnypyr
      961 avvrteesel fantfsrsfl klrrvavtyd ltkfiqsqfi kgldvtvfgn nlavlkktpy
     1021 ldpdfgasdg dlqdpsaryv gvsvnikf
//
LOCUS       WP_118171195             702 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118171195
VERSION     WP_118171195.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..702
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=76938
     Region          44..>702
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklrylqias sicitcchlg mshpalasqt yskmltkeyv vtkknvngti vdkdgnplig
       61 vtifekgtdn gcitdfngqy qlslsnrdav ivisyvgykt qelkgdqlve kivleedava
      121 ldelvvvgya vqkkkeltgs tsslkasdkk lsvttsldqm mqgnlsgvni tnasgmpgga
      181 vrvsirgvgs ingsneplfv idgipvsnsd nsgvngrfgg svqnplsmln pndiesidvl
      241 kdaaataiyg sratngvvmv ttkrgkkgqr ttvnlsasyg lqslpkeiem adsdlyltvr
      301 neavnnyntq nnlkpgdnly ktlevnprpg qpdtdwidli thdqaavqny evsvssgsek
      361 trfysslgyf dqegiiltnr frryslrtnv dhdisnafqt gvsialskti nnrvpndnvg
      421 ngiftrsieq rpfdvpfked grymiggvdi prhngiqvln eqksknewyr vlanayltik
      481 llegleykls lsgdirysnd ylkltkdhpy gspkgeitdy rsmmqnylid ntltytkqik
      541 dfnftalggy smqeintdas sivgkdfpss qfdyinaagr insasttggk nrlistffrl
      601 nmgyadrylf tfsiradgss kfadgnqwgt fpsvsgawri snesffpkdg iisdlklras
      661 wgmtgnqegi gnydsrslan gghnyngqdg iaittlanpd lk
//
LOCUS       WP_118171220            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118171220
VERSION     WP_118171220.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121533
     Region          33..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhsdyhgkl lrlamvfval flcgtmayaq tdrmisgivv dengdplpaa hirqvsqtkg
       61 eelaavitdm nghfrltllr takeieisyl gyeskkvrlt sansyriile paselldevv
      121 vtgyqtisre ratgsfakvd skkletqrls svsslmegri agysdgkirg vtsmnglttp
      181 lyvidgfpve ktisdglgnw venvpdlnie dienitvlkd aaatsiygar aangvvvitt
      241 kkagknqlnv sfsatltvrp ynfytghlad tadmiemeke waamnpnlqg egasqyaqnl
      301 ldnasmyscl gvqailkhha gaiseaqmeq tlhelasqgf ryyddvkkyg krnpfsqqyn
      361 lnigrgtekn tfnaslsyrn nreedkytds etfglnlqnt srltswlsld lgtylnygdg
      421 ttqsynltsp gynyvpyssl lngdgsyytn taadrysksq qeiissygly smditpldel
      481 grnlsksknf snrtfarlnf kftdwlryta sfqyevgeyk tsqlqdkesy avrnkvntfa
      541 tdasgsgqat ynlpygniyt tgtnsirayn frqqldfnkt faekhdvtal fgmevrenkt
      601 eynnrkyyny dpalltydli dervlsntyt gvlgnyvsfn kndisniyel vnrfvsfygn
      661 aaytydgkym vtgsirwdrt nlfatgskyq kkpiwsvgag wnldkesffk vsfinmmklr
      721 fscgiggnia knsapymtay ynnnthvggi qgtisnrpnp dlrwekttta nigvdfsmfr
      781 nrlngsieyy nksgvdllan tngvptegfg fstytmnngk mrnrgfeltl sgdvimgkdw
      841 nwnvggvlgy nknkvtyvnv kapaiflqfd ypaayprvgv pynaiygylw agldskgqpq
      901 vydsegnihv ssspqkveda vylgtsvpvy sgaintnlry knwelaaqll fegghkmrnt
      961 niaypglgvt skdvskrwrq pgdeaytdvp ryvpseskdy nsyssdlysk asihvldadn
     1021 wrlknlsvty hvpasvcqkf yvknarimlg menvftlaks rdvkwmlggy skpnylcnvn
     1081 lnf
//
LOCUS       WP_118171226             949 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118171226
VERSION     WP_118171226.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..949
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106561
     Region          38..948
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknrliipa llaflsmqgy aqelndsits gkpakysdev veigyhkaqr leestssist
       61 vynedfnkrs aknianslfg ygtglttlqg sgryadaept ffirglqsls tnnplilvdg
      121 ierditdvtp eevetvtilk daaavaiygh kgingvvnit tkrgiyntre ikftydhgfg
      181 wqarkpkfvd sysyanamne alandgltar ytqdelnafr sgqypylyan vdwlgetyrd
      241 mdatniynis frggaskfry yamanlttnk gfianpymnd gystqdqysr anlrtnldid
      301 ltektklkln vlgilsetrt pgangqggan lwdmiytlps aafparleng twggsatwag
      361 tknplavsqa aaytkfhert lfadmtltqd lssitpglga sgmlsydnya qywenhsktf
      421 vygsnsvtaw engvpsstty ytdgkessms sdakciaftr vfnfaatlfy dkqinkdnki
      481 ysqlkwdyey rntkgtdqtw yrqnasfyth ygykdkyfad lsvvasasnk lapghqwsis
      541 ptvglawvms kenfmkdlsw infmklrasf gvintdrlpl dddsevtnyw eqtyggggyy
      601 pfdtnysvgt qswslgrlas lnsthekayk ynfgldasmf ngldvsfday yerrsdiwvs
      661 ssghyssvlg ftapyenggi vdswgveiga nyrkkiadit lniganlala kneiieqmee
      721 prmydnlitt gkplkqtygm evigyfkdqa dienspkqsf gdvkpgdiky kdvngdniid
      781 andkvaighs ttapeiyysf nlgaewkglg fdamfqgtgr ysavlntksl ywplinntti
      841 sqeyydnrwt penqdakypr lssqsnenny qtntlwladr sflklrsiel yykfpqiwvk
      901 kskilsnaki yvrgvdllcf dkiniadpev ygatypltrs vvagltigf
//
LOCUS       WP_118171483             898 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118171483
VERSION     WP_118171483.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98566
     Region          27..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgrvslclvi mfficsaqki daqvqnirek qdtisatksl ehirpenikk gplnnaldvl
       61 sgqsagvnvt tngtdrlaml nsirvrgtts imggndplvi idgvtsdiat lstiypadie
      121 sftilknate tamygsrgas gvieiktkkg tgrgfeisyd gnygfesmyk hlqmlngpey
      181 iataealgld ynnggyntnf hdvitrtgli hqhhlafsgg sensnyrasf gfmdhntivk
      241 vndyrnlvvk ldatqkafdg rlvgdfgvyg ysskihdifd trmlfysaaa qnptypagtd
      301 vngnwvknsa ashinhpgal lyekndseer nfnthlglkf nildnlilsa fgsysysstg
      361 naqfcptwvw aqgnvyrgef kgedyftnvs lsynnawgds hldavvgaey lkqvrtglwv
      421 qakgittndf synnigatss rpfggtsssy edpslasimg svtysykdry siaaalrgdg
      481 ssmvsdnntf gffpsvslgw dvkkedflsd tdfitmlklr tgygrsgnlg gitsyttlnt
      541 vkengivsin gaptvtmgsi rntnpdlkwe trstfnigfd lgiwdnrlml tselyysktt
      601 dmlyeydvpv ptfafdklma nigsmsnqgv elgisvvpiq rkdmemninf nmsyqknkll
      661 slsgeyngmh mtasditpig slygagqngg dnnvvyqivg qplgvfylph ckglkenelg
      721 gysydiedln ddgeidfsdg gdryiagqat pkvtigsnis fryksfdiam qingafghki
      781 fngtglaytn msifpdynvl kgapekniid qnvsdywlek gdyvniehit igynipmksk
      841 avkslrlsag isnlatitgy ngltpminsy vvsntlgidd krtyplyrty slglsiqf
//
LOCUS       WP_118172440            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118172440
VERSION     WP_118172440.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114721
     Region          43..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkrlksvsm llflmgastg aayaaanpgv advkitqqng actgvvvdat getvigasvv
       61 vkgttngtit gldgdfslsn vkkgdiiqis fvgyqtveip wdgqpmnvtl qddtqtlgev
      121 vvtalgikre kkalgyamqe vkgdallear etnlanaltg kvsgvqiirs sngpggsski
      181 qlrgansvtg lnqplivvdg vpmdnftgas nndidnptld mgnglsdina ediesmsvlk
      241 gasaaalygs ragngvilit tkkgtkregl gitisgsvsa ettfmlpkrq kafgqgengv
      301 fdstngyswg pevtgqsytk wdgttanmqi fdnvknffdt gvnlsesisf qqqydktsiy
      361 tslnrmddss mipganlsrt nltlrasstf gkddrwsida kvqyintlae nrpisgargn
      421 nafytifnmp ttidirdfss pvkdefgemi wwskgginpy wskdynpnkd srnrflmngs
      481 lkykftdwld aeikagsdmy ftegeeklya gsptnnknsr ystsekkffe nnfsflisgh
      541 kdelfgkfgg nfsfggnlme rkstgldnam gkltapdlfs langdkkdls itetyihkki
      601 nslygtlgin yngwafldat frndwssaln kenrsffyps vslswvisdm vgkvgkgmpe
      661 wftyakaras faqvgndmda yqlyntysig sdpngnttag qgktkydadv rselitswea
      721 gaelkffnnr lgvdfawykt nakrqlmnip lnnlsgydnm kvnagniqnt gieimlnarp
      781 ietaqfswdt qlnfsqnksk iiellpgkpg mqyalggsda lqvyavagga ygeiwgtkyq
      841 rveegefkgq lllnesglpq atsdkhkige qqpdfllgwt ntfnyknftl sflidgrfgg
      901 difsftnmnl qrsgiaecta pggkredivv agvikdgngy kvndqsvsle ryykalatgr
      961 agiseayiyd atnirlrnia lsyrfpssml kktpfqqvkl gftvnnvwmi sshldgidpe
     1021 svyatstnat glenssapts rsylfnvtlg f
//
LOCUS       WP_118181076             535 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia phosphatilytica].
ACCESSION   WP_118181076
VERSION     WP_118181076.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia phosphatilytica
  ORGANISM  Paraburkholderia phosphatilytica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Paraburkholderia phosphatilytica"
                     /db_xref="taxon:2282883"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55402
     Region          3..531
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtmmigvpre rypgerrval tpettahllk lgfavtvesr ageraafsdd ayraagaqia
       61 adtkalyata dlvvkvrapa adetldeiel lregttlvsf iwpaqnaall qrlaqrnvtv
      121 lamdcvpris raqkldalss manmagyrav ieaahqfgrg fmgqitaagk iapakvmvig
      181 agvaglaaig aarslgaivr afdtrpevrq qvesmgaefl aldfeedgsg aggyakemsp
      241 afieaemalf laqakevdvi vttalipgkp apklitaemv rsmrqgsviv dmaaeqggnc
      301 eltqpgvaan vegvtivgyt dlasrmatqs sqlygtnvrh lltdltpqkd geivvnlddq
      361 vingvtvirn gelrwppakp pvapsppvaa asaaakpsat hgagagvsae aaaaqkrkaa
      421 slgfvglaia avliaalgav appafvahft vfvlaifigy qvvwnvtpal htplmsvtna
      481 isgiivtgal lqlgapgtlv avlaglalli atvniaggfl vtqrmlnmfq rgqgd
//
LOCUS       WP_118190065            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118190065
VERSION     WP_118190065.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115668
     Region          41..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkktmflgl lgaglmwmpa sailaaqmnn aamsvqqnqg ikgtvvdatg etligasvkv
       61 agttngavtd idgnftlnck pgatlevsyi gyktmtvkaa ngmkitmqed gkalnevvvt
      121 algikrdrka lgygleevkg eeltkaketn vinslsgkva glvvqntagg asgstrvllr
      181 gntemagnnq plyvvdgvpl dntnfgsage aggydlgdgi sainpddiet mtvlkgpaas
      241 alygsrashg vilittkkae kdrisveyng sytidtqlak wddiqeiyga gyngelpnss
      301 tsgtnaswgp kaddfmfkyf dgeerpfmmh pnnasgffrt gfttqnsail svnsgktgmr
      361 fsvtdmrnkd ilpntnmsrd nfnlrvntsa gpvdfdftan ytrekvknrp algdsqsnvg
      421 knlmtlagty dqawlkhyed adgnysnwng ndqynknpyw dlyknsntsd kdvfrftgka
      481 iwninkhfkl qgtigtdins mnfedfiakt tpgtpagklt dqifnnrtln aeilalynns
      541 wgdfdvnata ggnifkvnnk tttniglnqq mngiknimny qeqntresmy kkqisslyas
      601 aslgykhtyy legtlrgdks stlptnnnty vypsvsgslv fsefiknkkf inygkirasw
      661 akvgsdtdpy llalnytmgk ysysgytigm ianstqpnkd lkptmtgsye vglemkflng
      721 rlgldatyyn qnsknqilsl astttsgyay rlinageiqn qgveialnar alqikdfawd
      781 lgvnfskntn kvkslvdgmd yfelakatwc gvsvgaqvge nygairghdf lyndkgqvvv
      841 daatglpkid qkvktignst wdwtggfyst fsyknfrlsa sfdvkvgadi ysmsmrsayq
      901 tgkakgtlag reewytseea rkasgmdlaa wretgnckgl vvegvidngd gtyrkndiav
      961 npedywkhva ngvqsafvyd nsyvkcreit fgytfpesil gkyvkgltvs fvarnpfivw
     1021 knipnidpds syntsglgle ygslpsrksy glnvnvkf
//
LOCUS       WP_118190163            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118190163
VERSION     WP_118190163.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116317
     Region          24..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmtfia clflslgmal aqtqvsgkvt saedgepvig asikvagtnt gtvtdvdgnf
       61 slnvpagakl evtylgmlpq tvkagqkmki vleadnktld evvvtamgis rdkkalgyas
      121 qklgsedlni agtsslasam qgkltgvdir qssgapgasa qiiirgarsf sgdntplyvv
      181 dgmpiassad ydtgasvtga dkanrsidin pddiesidvl kgqaasalyg irasngviii
      241 ttkrgkangg rpqitfstdl saqtvskkfe rqtvyaqgnm gqggstgayn pnasmswgpk
      301 iadlandaty ggntdnvytq qygkhegmyy npkyaaagld gwttpqtydn vgdffntgft
      361 qnsnfgisqk ngnlaysfgi gdtyqkgiip stgmmrttar gavdfeinkq wktgfsanys
      421 stkitsapga ndsfmsylyg apaefnlkgt pyhkpnspsd qvlyrsgvfq npywwaanse
      481 yrqatnrvfg nayvefrpnf nwdkerfnlv freqagldvy tttnddiney gtlvsgnktg
      541 gsienygvqr nvfnnlftan ftakldaaqk wdlgfllgse fnhenartwd yagdnflfyg
      601 qptisnvskm tynseyksee rtvgffgqls lsyanqlylt vtgrndivst mprgnrsffy
      661 psvslgwift elpalkgnhi lsygklrasf aqvgqaghyy anyyyvpsyg sgmygftpvs
      721 yplagqgsyt pyyvkydpnl kpqntmnwef gadlnffdnr irleytasyq dikdqifnvp
      781 tagstgyqyl ctnagemttw shefainasi iqtkdwdldl gvnftkltnk vksladgves
      841 imlggfvepq vraqagytyp niygiafkrd eqgrlllkdg lpqgtsdsqn lgectpdfnm
      901 gfnlkarwkr lslsatldwq kggkmyngti mtmnmfgatk eslpyhegtm vvdgideatg
      961 qpnkievskq sywyayhdvt esgiydrsyv klrdvtlsyq lpkfagidis vygfarnlll
     1021 wskmkdldpe ssqgngnmsg cferfsipnt ssfgggfkit f
//
LOCUS       WP_118190414             942 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118190414
VERSION     WP_118190414.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105324
     Region          37..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msniisryka ilpvslfals aqgvmaqdap eadtinvafr kadardvitp vstvnvknll
       61 eknyntysld nmqalaagyn gslwnqgdal vlidgvprda nnvlpteied itflkgasav
      121 vlygsraakg ailittkrgk ieplkitara nyqmsvaksy ptyldgaqym tlynqaland
      181 glsakysaed iyntaagtnp yrypnqqfyn sdylkkaksr ydvtaefegg gkfaqfytnv
      241 syyregdfln fgegknnytd rlnvrgnidl qladwasgwv nanatyynqh gsnsefwkaa
      301 stlrpnrvap fiplsyldpk danslalinn srniitnpvg lpagqyflga tqedqtnafa
      361 dmyaagyntw tsrqmqfdtg vkfdlssvlk glsfktmfav dystsyttsl ndsyatfgvn
      421 wtqfdgkqii gsvtqygedk htgtlnssns aerqtlawtg qfdyvnsfgn hnvnatllan
      481 gyqqtisgey hkvsnanlgl lvsynyahky yadlaanvvh saklpegnrn aispsatlgw
      541 rlseenflkd vnwlndlrlt agytvlnqdl dikeyfmyen iftatgtwwg wsdannaiqt
      601 sdsqrggndk lgfikrkefn vglngalfgn rlsfavnyyn tvtdgllaqp dyiypsymht
      661 ywpvstfvpy inygknrrtg vdfslgykdk vgdfeygiqa fgqtnssknl kvaenveydy
      721 mrtegkltda lwgyeclgyy nskeeiendk vkssfgtlkp gdlrykdqng dniidskdrv
      781 vigrwsakft ggmnltlkyk nftlfamltg qfggnalknd tynwvygerk ysdvvlgawt
      841 eskykngesi typrlttqsg dnnfnasdyw mystdridls rvqltydfnk slfgdnslvk
      901 glqvyvngss lltiagerkq mernvdsapq trsftigakv ef
//
LOCUS       WP_118190967            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118190967
VERSION     WP_118190967.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123708
     Region          51..103
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          116..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mirrnylksl mifiltclpl lgasaqqkvt vnvvnaslkq vfstienqts yrfsyksdii
       61 dhrkditirk sgvpvtavld aalkgrnlky svvsqksivv sekhaaaapq qsnkhkmqgv
      121 vkddngepvi gatvsvvgtd elavtdmdgr ftinaakgak vkvsylgfvd revkasenmn
      181 iamsedtqal sevvvvgygt mkrsdmtgal ssvntkemak rtttnpaeal qgkvagvnil
      241 rsggnagagv sikirgiktt gsneplyivd gfpgdinsvn pqdiesmeil kdgaaaaiyg
      301 svaangvvli ttkngkkget kvdfssylsf tqvskdldll daegykkvhk mmyenagepl
      361 payvthetgv nsdwvdairr kglaqsymis lrggaekgqy svsynhadek giflgnserh
      421 diarmkvhat kgiidldanv dfkftkghqp qyqlkeaymm splvpiydes rkygfglsdf
      481 dglpnnrnvv addhykknty kkyhttanaa ltfnffpwln fktsygyrge heidnshypd
      541 ytadykspnl ypnnyeyray wqeqvfenvl sfnkqiqkhs inamlgtsls mikynwesvs
      601 vegktnvnev ingqlntsdk pagfldpnfp tisggvggty ygtgsyweyn rasffgriny
      661 nfndrylfqf tfredgsskf gadsrwgffp svavgwrise epffpknsvi snlkfraswg
      721 qlgnenalgk ydflarissy ndmymgyvqg agsnpwtgsi aralenrslk wettdtknig
      781 fdfglfgnhl ngninyyine trdllitrri apsagldnpt lnvgkmrnqg felelnwndk
      841 isdfeynvgf nistiankvv alanedqtiy gvglkygseh fptqtkvgkp igafylyqad
      901 gifqsleevq ahknskgell qpnaqpgdvr fkdmngdgvi deddktysgt giakveanln
      961 lgasykgfdf savigsafgn klyngiryyy egmnsgsnfl kttlnawtpt ntktdiprai
     1021 ygdpnqntre strflengdf vrlrqvqlgy tlpkalskhi ycesirfyvs aenvftitgy
     1081 sganpefsqg vlnsgvdrft ypfsrsytvg aqvsf
//
LOCUS       WP_118192218            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118192218
VERSION     WP_118192218.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116493
     Region          24..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvkrltmlmg glvlstgmal aqttvtgkvv sqedgepvig asvrivgtkt gtatdvdgnf
       61 tlpnaskdav leisylgmqt ktmkasakmk iilasdarnl devvvtalgm krsektlgya
      121 astanaselt vaksgslmsg lqgkmagvqi sgggvtgtsq kvvirgissv ssnnplyivd
      181 gvpinndrlg dnsvdfgsga gdinpedies vtvlkgasat alygsraang vimittkkpq
      241 gnkkasityd gsltftdvlr vpmtqnlfgq gwgswsneen gswgprldgr ehwygstgls
      301 ngetltkpfs yvknnirdfy qvgkewnnnv slrygdekvg ivasygnvss ngitpndgdt
      361 yhrntfslrg yanidrfhld mslnyvrkdm rrsrdmymel lqgasdvrft dmkdynlern
      421 nvdnyytlya tnpyymvdnf ystyqddriy gklelsydit kdikvigrfg gdytnykter
      481 iepriiyteg syqatgngtt vgnqgyysky rsqrgqidas llltgnhtfg dfsvgatlgw
      541 nlnqrnydnv ggyneqldip gwnslsntss ysitdtdswn rrllgllgqv elgykdwafl
      601 nlsarndwss tlpmgdnsff ygganmsvll nqaipalknv kqidllkvra aigqtgndad
      661 vymtnsyyrp fqsyytylpi sgvsglteyn rlpnkslkpe itteyelgls gtffgnrlsf
      721 dvayydrttk nqiisatlap etgytsntrn vgklqnkgie amvnftpirt kdwewsvgat
      781 yaknwskvke lwdgldeyti pvgttstgly ssmrgvsyvl kvgepigifk lpatqkvtdk
      841 nspyygyriv ngngflqsst tdydylgssq pdfvmgftth lkwknlslaa tgdwhkgglm
      901 ysetsyithf ngnstetvfn erdafvyphs vkivggeyve nnipvasnym nyvqgnysyn
      961 pevrrdfvvs rsyfklrela ltydfpktit salkmqklsl slvghnllli tpkhqnyidp
     1021 essnfgndis sefgetmgsv strnyginlk vvf
//
LOCUS       WP_118192341             879 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Segatella copri].
ACCESSION   WP_118192341
VERSION     WP_118192341.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 879)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 879)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 879)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         <1..879
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..878
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 tssasdmlvg kiagvdvqtg ggqpgsgaqi rirggaslna sndplyvidg laidnntnkg
       61 msnvlaminp ndiesftvlk dasataiygs rasngviiit tkkgrsgqkp svtyngdvtl
      121 stvqkkykvm naseykqalt nlgidtsglg tadtdwqdei frtaistnhn vsiqgglknm
      181 pyrvslgfed nngivkttwm krfntsinva ptfldkhlnv nftakymfek dryakvgdai
      241 ggaltmdptq pvrvddaayd cvggyfqylq akddkvtdps wtsiakaqmp qnpvavldny
      301 kciaksndis gnlevdykih gfedlhlhaa igaqytdgkq detiskysys nnyfgyygyd
      361 haykysiegk afaeyahkfg vhdidimaga eqshyhrtgy nygtgtdeyl kannplyett
      421 egkwnyehdp vskddemwrt hnslvsyfgr lnynlldryl ftatfradgs srfrkgkkwg
      481 yfpaaafawk innepflkdv kwldelklrl gwgktgqqng iddfyystly rvsngyaqyp
      541 fgdkyyqtlr ptasnpdltw ektttynagl dftalngrfg vnvdgyyrkt tdllasvaia
      601 ggttfgdqll knigslenyg ielafnvkpi vtkdfiwdvt ynigwnhnei teleaglqdw
      661 vwtgdkvsrg nntkiqvnkv gqpinsyyvy qqvydengkp iegayvdrng ngtiddddry
      721 cykspapdvi mglttkfiyk nwdfsaafha signyvyydf lnskavlnei nasgafrntt
      781 teavnlgftg tatnptntsd yfvrnasylk csnmtlgysf palikvgaek icsgrifftv
      841 qnpfiitkyk gidpevssgi dsnpyprpis fqlglnlnf
//
LOCUS       WP_118192351             846 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Segatella copri].
ACCESSION   WP_118192351
VERSION     WP_118192351.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         <1..846
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..845
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 ggaslsasnd plyvidglai dnntnkgmsn vlaminpndi esftvlkdas ataiygsras
       61 ngviiittkk grsgqkpsvt yngnvtlsti qkkydvmnas eykqaltslg idtstlgsyd
      121 tdwqneifrt svstnhnisi qgglknmpyr vslgfednng ivkttwmkrf ntsinvapsf
      181 ldkhlnfnft akymfekdry akvgdaigna lsmdptqpvy gngedykyvg gyfqylqnks
      241 dqisdpdwkk maasqvtqnp vavldnykci aksndisgnl evdykihgfe dlhlhaaiga
      301 qytdgkqned iskysfsnny fgyygtdhqy kysiegkafa eyahkfgvhd idimagaeqs
      361 hyhrtgynyg sgideylrdn npqfveadgk mnyiysptyq kntmwkahns lvsyfgrfny
      421 nlldryllta tfradgssrf kkgkkwgyfp aaafawkinn epflkdakwl delklrlgwg
      481 mtgqqngipd fyytpvytvs dtyaqypfgd kyyitmrpsa ynpeltwekt ttynagldft
      541 alngrfgmnv dgyyrkttdl lstiaiaggt nfgdqllkni gslenygvel afdvkpivtk
      601 dfiwdvtynv gwnhneitql daglqdwvwt gdkvsrgnnt kiqvnkvgqp iksfyvfqqv
      661 ydengkpieg lyvdrdgngt iddddrycyk spapdvimgl ttkfiyknwd fsaafhasig
      721 nyvyydflne kavladlnkd nifrnttaea vdlgfwgkts katntsdyfv rnasylkctn
      781 mtlgysfpal ikagaekics grifftvqnp fiiskykgid pevssgidsn pyprpisfql
      841 glnlni
//
LOCUS       WP_118193427            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118193427
VERSION     WP_118193427.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118515
     Region          24..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkllsilm lctllvgvaf aqnktitgrv tssdngetlp gvsvvvpgtt vgtqtdvnga
       61 ftlqiptdat tlefsyigfl pqtvtigtnt tfdislvada tqlgevvvvg ystttqgaft
      121 gsatvvssed ldrkntsdis kalsgevagl qvvngsgqpg rsatirirgl gsvngnrdpl
      181 yvidgvpmdg gntstsplts fspltsinpa diesttvlkd aaataiygar gangvilitt
      241 rsgkgkpsfv evdaqigsnm sllprydiit speqyiglsw egmynyadgr vddptayana
      301 nlfgsggina kynmwnvang gelidpatrt vrsgvtrryd peswkdhafq ssnrtemnvk
      361 fggsndrtny ysslgylddk gysinsdyqr lsarlnlfhe vkpwldasmn fgysrsetnn
      421 ggqsqdsgsv fwfvdnipsi yplfekdadg ndipepifgg stydygtgrr fggltnsiad
      481 ahyntnrhnr ndlngnvaln fkilegltfe nrlgvqyynn kyvdltnkfy gsavsqngsl
      541 yqqrsemtsy nllnllryrk rfgehnfeal aaheatdwsr niltvsgynl vdpdleefsn
      601 tvvsnpigsy tnryklesyf aqvtydydnt yflsasarrd gssrfvkdkw gnfgsigaaw
      661 lisneefmqd qnvfnslklk asygligeqa gigyypgydl ysidnlndnp afsffskgne
      721 dltwetskmf qtgiefdlgq ylsgsidyyi knttdlifdr rvgpsigyal ikvnggslrn
      781 qglefnltsr vleqddyyln lsvngelfkn kltsmpiepa tglekdldiq glygwatghs
      841 vydfymrewa gvdpedgvgm wnayyidnng ngaadageyi aslaqylnen pdqasavqkt
      901 ttktyanatq tfvgksaipk irgafnlsag yknfdltvqm lysfggyayd gayarlmsnd
      961 liggnnwntd ilnrwqnpgd itdvprisnn rdanvgssst rfltkanylt lnnvrlgynl
     1021 psnllsnlgi agatiwvsgd nlwahserqg fytftseags sdmyryspls tisaglrvrf
//
LOCUS       WP_118193414            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118193414
VERSION     WP_118193414.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113200
     Region          27..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqrliatl lsvlflfcay qthaqtrtit gtvydnentr fsgvtvtvvg kstststdnn
       61 gnfsitandd dvlsfsavgf eqqtipvgsr snititmean vsdlsevvit gefgmernar
      121 avgssvqkid gatisesgre sfvsalagrv pglnvtstsg tpgasntvvl rnitsisgnn
      181 qplyvvdgvp mnnstfdplt gmagagvdty svrnmdyssr gndfnpedie sitvlkgaaa
      241 aalygsdasn gaiiittkkg ragagrvqys nsfkfdkayg ypelqtkyan gnygttnyyy
      301 takfgglype gmtlydnfas vlqtgftqrh nvsvdagtek stirasfsml gqegvikttd
      361 ydrtnlglag qsqvtdwlkf egsmqytrms nnkvmrgtdg plyramiwpm vdnmanyltd
      421 dgvfmkvpdy yldqdllnpl fglyknkffd ksdrflsnva inltpienaf lraqvgwdvg
      481 mqnfetsahp yyaarnaglg qynlvqsnfs dptiniltgy nntfmdgkls fsgqlgyhqm
      541 engvtrlssy gsdfivpdfq sinntepstq vasqrntkrr iqaisgqfef gydnlafitl
      601 rgrndwsstl pvennryfyp sveasfilsd ldfmksvepi nyvklrgsva qvgkdagple
      661 idpeleptel tgggfkygft gpnpnlrpem ttayefgadv qllnnrlnas ftyfgtrnad
      721 qivkgfrlsy atgfvlnnmn vgtfktwgwe ahvdgdivrk pegvtwnvgv nvshggskvl
      781 flpenvseyy naytwnsgni rngimvghpi ttltgraylr ndagdiliep ttgmpltdpe
      841 wsvigdrepl lrfgitsslr yknfsasalf agrfgatvvn gtkrvmmtqg tslesvelre
      901 sgpfvfegvl rdgnentdnp tkntivtdyr nygatiyggn dedwlekdvh ylrlqelrla
      961 yrlpastlnw tkiassfdvf vvgndlvtwt nysgidavgn tvsaaaggtg gegydvwsip
     1021 nprgisfgis ltln
//
LOCUS       WP_118193420            1155 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118193420
VERSION     WP_118193420.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 1155)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1155)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1155)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1155
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..1155
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127993
     Region          45..1154
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkvlllsva lglmvsadal attsvaatnr sataiysanr lkqntvqgtv sdeqgpvpgv
       61 tvsvvgtntv vvtdsngqyr idapvgatlr fssigyatkd ivvssatldv vlevsqssle
      121 qvvvvgygvq kkehltgavs svnveevlgs rpipdvgrgl qgtvpglsiv vpsgevgsdp
      181 vikirgqigs ivgssnplil vdnveipsiq mvnpddiesi svlkdaasts iygakaafgv
      241 vlittkkgak mdgnevayst nlsfqspfkd ieiagidgle ytleahenmk ssgpaggfwr
      301 vsresfekik ewqtlygdvv ayndpvvygr dwyfdgtdky gyriydpvet mvkdhgfsqk
      361 hnislngkke dtrynfsvgy lgqegmmkpa nhddykrfts nlnastavnd fltlrggarf
      421 tdgtkrypns atgfgadpwl ylyrwsrlfp tgvtelgeei rdpyfdtkna ndaieqkryv
      481 nlnlgttvdf tsnwnliady ayttefnkft nslpkmdgaf hwyapvawnd eegnrvyvde
      541 agnitedqen gipgfrfpmn eyigkdqtyf yqnsfnsakh tfnaystynl nledkhdfkf
      601 mlgtniiayk wdshwsertn linpdnpqfn ftvgtpdvgg sanwdsqvgf fgranyafmd
      661 kylfeanlry datskfpthl qwkwypsfsa gwvlsnetfm qsldpilsfa kirgswgsig
      721 dqsvpnslyl ptmaigqnsw lnsggeqffq lgtpppvsma iswqdiehln lgadlrffnn
      781 rfgitaewfq rdtrnmiipg eslpdtygan apqgnygnlr tkgwelaady shmfenglrl
      841 slnanisdat tvvtkgadwn tpwenrslgs tfatgrrygd iygfvtdrly qkedfvhdad
      901 gniqqvtivh rgtakvtnql vgdnpvyqty fedgnqvmli spgdvkfvdv ngdgyidngq
      961 ntfgdpgdqv vignstpryq ygfrvgadfk gfdlsvffqg vgkrqiwgng qlaipgyhvk
     1021 dgampqaiae dfwkedrtda fyprawnlgg gnsgfvmrpq trylldmsyl kiknitfgya
     1081 lpqnilrtih lsrariyvsl enmftfdnlr glpidpeais ghsmltdnng nynlgrtgts
     1141 npafksasfg iqigl
//
LOCUS       WP_118193432            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118193432
VERSION     WP_118193432.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120722
     Region          24..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqklliffm agfliissay aqnrrvsgkv tsqedglgip gvtvavsgtt tgtttdnegf
       61 ysldipasat alefsfigyt kqtleigdrs tinvalvtda tqlgevivta lgierqrnel
      121 pyaaqevkae eitrtrdnnf vnalsgkvag ldikqsgtmg gstnvvmrgv ksmtgnnqal
      181 fvvdgapisn antntvnqtt grggydygna aadinpddie sltvlkgaaa talygsraan
      241 gvimittkkg kknsmnitvn sgvtfgnidk ttfaeyqkey gagyineysk seyirlaeia
      301 nsdgdpdndm dptdfptygs edgsfwfrqt pfengnsliv pftedasygg afnpnlmvyq
      361 wdafdpsspt ygqktpwvaa qndpstfykt gvnstqsisl dgggdnatfk agytrndetg
      421 vlpnskiikn ifnlggsydi tenlkasgta nfskidglgr fgtgyagnnv nqqfrqwwqt
      481 nvdmkeqeaa yfrnkqnitw nwsnhnatnp iysnnpyftr yenyqndtrn ryfgnfalsw
      541 tpiewmniig rvtydgssek qeerwaqgga dvpgyrlynr sfsetnydll vnfnkdined
      601 isfsgllggn irrstlsgid aqtvgglafp glyslsnsfs pmdapveqye rvgvdgifas
      661 anfgfmdtyf ldatirrdqs stlpennnty wypsvaggfi fsnliddksf lnygklrlny
      721 aqvgadaapl slydtyiinf pfngihqtsi naskqninll pertrsveag ielaffnsrl
      781 gfdasyyntt sfdqimavsv statgygfqf vnagsienkg feiaaygvpv qtdnfswtin
      841 anfsrnrnkv velyeentnl qlatfqggvs lnatvgqpfg tfrgvdyvyq geqkvvgedg
      901 yylssapntv mgdinpdwsa giqnaftykn falnflidik qggdvwsldq yygmatglyp
      961 etaglndlgn psrlpiaqgg gvilpgvked gtpndirven ydsnvtpygy annptavglf
     1021 dasyvklrea aityslpsew lertraikgi dvslvgrnlw iihknlpyad peaglssgnf
     1081 qgyqsgaypt vrsvgfnlrf kf
//
LOCUS       WP_118193665            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118193665
VERSION     WP_118193665.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109986
     Region          30..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekklpiqvh vilffllayc nslfaqntnv agkvtdasgq glqaisvqvi gsttgtstda
       61 dgnfaisaga tdsllfssvg yvsqtiginn rttitiqmse dtkvlsdvvv talgiersak
      121 slsysttnis adeltevkgp tllnslagka agvvvsqgag gpgsnprivl rgnksivgdn
      181 qplyvvdgvp iggfadynpe diaslqvlqg asaaalygsq aangvilitt kkgqfgttsv
      241 dfssstmfdn plvlpelqts ygqglggeav egindswgpk inngsdrhik effetgqnfi
      301 nsisissgnq vsraflsysn tnsksvipny gfkrdnftvr gtseildgkv eleaglnyik
      361 sktenqnass wynspmfgly lfpmgddmsk yspngggvwd errhmyvqnw pyiknehssn
      421 qnpywitnrl qndqlrdrtv ftasakwnit dwvnvqartt lnrysgdvey ryaatsdpts
      481 igangaytke vsngedlysd llisanrsln ddltlnavlg asntvesyrs fyngtdgalt
      541 tlsypnyfsv yaltgnfvkt esqrkevsra vfatatfgik etlyidatar newsstvdea
      601 ffypsvgfsy ilsenlapse tvsfiklrat yaevgnslpf gaaerspnys lspdgnvigr
      661 pnlpffsgtd ttslkpertk slefgaemrf fndkvnfnit yydattrdqv ftitapsgag
      721 atsfwinggt iqnrgieaya syngkfgelq wtpslnftrn tnrikelsdl lttdrfvlas
      781 anrltnlylv rpgsdllgdr eyaayhdiyg kkylynedgs hqvnaaglpl lsaqdnqyig
      841 nanpdfllnf nnqfryknfn lsflidsrfg glvassteqw ldykglskrs geardnggvm
      901 vngnlidaet yygyisakad ygaaaseyty sstnirlref sigytfddlg dtfkninvsl
      961 vgrnlfflhk kapfdpelal gtangsqgfe sfqipslrsf gltlrvgl
//
LOCUS       WP_118193961             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Albibacterium indicum].
ACCESSION   WP_118193961
VERSION     WP_118193961.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40283
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgvlketk ekerrvalsp eivklllkke fqiqvesgag vasnfsdedy kvagaqivsk
       61 sdifnsdvil kvnaptleea sqfkngsvsi sllypytqpe lletfnsrqi ssfamdavpr
      121 israqkmdal ssqanlagyk avimganalg kifplmmtaa gtitpakvli fgagvaglqa
      181 iatakrlgav vevsdvrpet keqveslggr flvvesaeev kteggyakev sqeflakqqq
      241 liqekikdad lvittalvmg kkspilvtee mvksmkagsv ivdmavesgg nceisefnqi
      301 vekhgvtiig esnlpsllpv nasqlyavnl stlllhladk egfkweleee itkgalithq
      361 gqlvheftks ilsk
//
LOCUS       WP_118194733            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118194733
VERSION     WP_118194733.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111690
     Region          25..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnmymkcia lmimiglsap lfaqktisgt vsdnmgplpg asvlvkgtdr glqtdangky
       61 tiqasegevi tfsmigfttq eiavgsqtvi nvnlsqdnqa ldevvvtalg iqrekkslgy
      121 alqevkgddl vqarepnlan altgkvaglq vvrgsggpag sskivlrgfn sltgdnqpli
      181 vidgvpmdnf tgasnndfwn psldmgnglg dinpddiasm svlkgasaaa lygsragngv
      241 ilittksgrk teglgityst svgfesaftt pemqnsfgqg tegifdsqsg sswgpaitgq
      301 tvenwdgrqv plraydnvnn yfgkgfnqkh nlslsqsfnn tsvyssvsym gddsqipgae
      361 lerfsfltka ttsfgpeerw taetkvnyin tkafnrpvsg snsnnafttm yllprsldit
      421 qfensvdefg nmiwynagng inpywnslyn rnedarnrfl lngslkyrfn ewlngelrag
      481 adlyqtsfnt klnsgsplsa tgryslgknd fnetnlsalf saqkdniwgr wggaatlggn
      541 lmaqkstsis snagelvvpn lfsinngvnn ptvtegysek rinsvygtvq vnydgfffld
      601 gtfrndwsst lkdpffypsv stslvlsemi nksggnmpsw isyakvrgsy aevgndmnay
      661 qllntywigk dpdgnttagr nstlynenvv aeliksweag aeirflnnrf gldfswyksn
      721 atnqlitlpm nplsgytgri inagniqneg ieimtnalil dnpeglswnl nvnysknknk
      781 ilsladdvts yplggydnia inavvgedyg diwgtsfrrv tdesseyfgq lllnenglpv
      841 qsnekirlgn qqatgllgii nsfsyagvnl gfqidarfgg kvfagthqmm qrsgtaaita
      901 pggsredmiv agviqsgdny venttpvtvq qywgavagvg ntgiseaniy datnvrlrnv
      961 sidynlpkkf lqntpiqgak iglsmnnvwm ihsnlngldp estyatgtna vgfeygsgpt
     1021 trsflvnlsv sf
//
LOCUS       WP_118194906             943 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118194906
VERSION     WP_118194906.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 943)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 943)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 943)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..943
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..943
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104712
     Region          15..942
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mykmittsll cmaavvlkaq ntpidsvsak ssnlgatsti ytndltkyqs atiltglqgr
       61 lkglnvspfr gmmllrtdan tssdivgaip nvgggiygdn seflisargq spvaivdgve
      121 rdlysldpea iesvtirkda lsnmflgmrs srgtliittk npdpeggfhl sltgkfgiss
      181 alksgpnpls syqyayllne allndgkspl ysyddfeayr ngtspylhpd vnwrdaimkn
      241 sttsqaynln vtgggrvaqy fvslgyysen glfktsdans yntnfkynry lisskvninv
      301 tdefkvnmsl lgrveegtqp ggisgtgysd llsniwqtpn naypifnpdg syggnasytq
      361 nlyaqtvgsg yissntrdvv gtihlnydfn klvkglsvga ignisaqvrn aivrtkqaqv
      421 fqydvtesgt dvysmygnvs sqsndyrsvs tyqymygkly vdwerqfgmh gvkaslfgdt
      481 rsilnnfdlp mipsnvgqkv eynydnkyfa qaavtesyyn ryaegrrwgt fwavglgwdi
      541 skekfmeqae widqlklrat ygytgngidn agyygylkry avdggfwyln gtsgsnggsv
      601 seitplansl ltwekgkkfn vgvdvallkn rltfsadyyn dnyydmlqar gksieligis
      661 ypaenigkar ysglelelsw mhrigkvnyy asanwsmeqt krifmdeqyv pydymrmtgq
      721 pigaiyglva dgflsakdia dgypvmngfd niqagdvkyv dmnhdgeine fdrtviggdk
      781 ptcyfginlg lewkglevsa liqgaynrdl ynsdrtlleg fqvrgqsfgq aytnlldrwt
      841 petaetatyp rltaggnmyn ygnnwnsslf vqngnyirlk navvsyklpe sfcrnylggl
      901 rvkifvegqn lltwagtklq dpevaftsyp lqrtittgin lnf
//
LOCUS       WP_118195102             998 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118195102
VERSION     WP_118195102.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110716
     Region          36..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnihfktct cllgillmlf sgiqargasl evqqerkisg tvidekgepv igasvvvvet
       61 kqgtitnidg kfqvnapqng rlkisyigye tqevaikdrq slkivlkees talnevvvvg
      121 ygtmkrkemt saishvgakd lnqissldas mllqgkvssv svsntaladp nstgsiqirg
      181 issrnaglgp livvdgvpgg dmtninpadi esidvlkdga asaiygtrgs ngvilvnlkk
      241 gtrdgevhtt ysaavtfnka kkeldimnae eyrayrtvsn plsdmgastd wfdavtrlgv
      301 thmhtltfsg gnartnyrvt adyrkaqgid lrsdrreyga ratishttkd glftfaanmt
      361 prvidrnksa svygsviknn ptmpvydpes angyyrfpsg gdssniveql neeengteik
      421 llewnataav nllplfnpkn pnmvlksqvt vsqyqvdkfn gwfipstygp nvnsgvagka
      481 srdfdkntnn nlewvtnfst rikdhqiram vgysynygvs sgmgaenwdf ssdgltynnl
      541 gsgleaakeg ktmmssyknd hklisffgrv nydwkerylf tfslrhegss rfgenhkwgn
      601 fpavsvgwri sdekfmkgfs widdlkvryd ygvtgnqeig nyqslatyra ygwyqyggnn
      661 fhvwgpsknv nselrwekgh nqnigldfsl fkhkvtgsfn yfhrkqsdll gsysvsvppn
      721 lfstiyanvg tlrntgfeld itvnavrtkd ftysftlvga tnnnkfvsfs ndvykgqkyy
      781 stcnmanpnn pgylqrieeg erignyftyr yagvdkkgdw liydkkgnvi pvaqgteedk
      841 avtgnglpkf tgsmthnfty knfdltvalr gaagfdifnv hdfyfglqsm stnqlttays
      901 knahittgkn vitdyfiepg dylkidnitl gytmnlnkky iekirlfgta nnlytftkft
      961 gvdpstyevn gltpgtfggg ynyypsafqf ilglqvsf
//
LOCUS       WP_118195411            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118195411
VERSION     WP_118195411.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114353
     Region          38..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrynkfifi lfvtailsgi atsleaqdkp kkkktaliev kglvtdntgk plsgvtvlsg
       61 egsiinytda ngkfalktka ngtllieafg ykdvvinlak eqptviklqn edlyaserdi
      121 heradggkty qrdlvgtvsk lsmenvlkyp dlqlsnalqg qaagliaisg dgglgyntst
      181 lyvrgqhnng tntalviidg ierpiddilp eeiesievlk datakilyga aatngvvlvr
      241 tkrgeahkri vrvgveygvq pstrvpkyld synysklfne arindgmnpy ytdtqlegyr
      301 nssgvndvly pnvdyynefl lnqniyrkgt iefnggnegv kyalvggytg gsglekvger
      361 salhrmnarg nldikitdfl tvtadvaarv elknwgakdg agifstlssn rpneypfiip
      421 netlsgqftp nedgtpffga strivdnlya dmvyggdtse ryvnsqtnlg anfdfnkyvk
      481 gltfnayvtf dnysylrqel rntyptyaid tysdldgeti trytqmkkld lpktqkiasn
      541 ntyryfgmra digyertlgv hdfsaigafr ytknemtgmt qdfkdanisl rlnysydkry
      601 laeltlagmg snkfdkndrf ffspavgasw iisnesfmke vkavnflklk asfgvlgytg
      661 ntgfflyqtg wnnngnynff qdqtdhkvsl arwgnpdltw eysqefnigi eglffnnrls
      721 telnyfhecr kdiigvnnaq yaatagnytm yenigqvtnq gidiainwkg nigrdflytv
      781 ganmtysknk ldkwneiegv esyrkaigrp tstifglqal glfgkdiple dhslqsygiy
      841 qngdiayadl nnngivddnd rmslgqsfpv ttwginvdlk ykgfglymlg tlhtgitqlc
      901 tnayywnngl ngyselalnr yhevnnpsgt mprlttttes nnfrdssfwt engsffrlkn
      961 ielsytfenk agrffankck lfvrgtnllt fskikdldpe rlnagitnyp aymtvtggls
     1021 vsf
//
LOCUS       WP_118195250            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118195250
VERSION     WP_118195250.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126649
     Region          36..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          114..1115
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknqaqkfi vlflfflfay swrveaqtgk ekqitmefkn eglpsifkrf ekvsgykvlf
       61 iydeissyts tgkvekatvd ealkviigkn plkyhidgqf initkedskk ffsqvkgkvf
      121 seedglpvig atiivedann iraitdnngn fqlsnvskds rvrisyvgle tqflnpssym
      181 svvmksdtka ldevvvtgmf nrkkegftgs avtikgedlk kystnnvaka iaavapglri
      241 mdninmgsnp nnlpdmrmrg ganmdmatqs avdfnstsnd vlavqgeyet yanqpllimd
      301 gfeitiqtla dmdpdrvasi vvlkdaaata iygsraangv iviesktpkp griwvtygge
      361 lrieapdmtg ynlmnareki daelqsglyt yggetvekwq lyqsklrevl agvntywldk
      421 plqtafqqrh tvtleggdea lryrmyvgyn sspgvmkdsk rdvltgsldf qyrlkkvllk
      481 nsitldnsva nespwgsfse ytrlnpylrp ygengeiqkr ldnfegvgge ssylnpmynt
      541 tfnskdqskn ftvrelfrve ynptnelrfe gafnlsksvg hrdifrpaqh tlfdnvtdpt
      601 lrgdyrrsqs eavswgidlt gswnkqlkdh yltanarmsv lennsetygn yvtgfpndnm
      661 dnllfgkkyn ekvtgdertt rsigwvaagg ysykykysfd fnirldgssq fgknnrwapf
      721 wstglrwdlk kenfmkdvsf isdfilrgty gttgsqgfdp yqahgyytys nlllpyyssd
      781 atgseilamh neslkwqttk stnlalelgf fdqrltarve yyrkitdnmv tsislapslg
      841 fgsypenlgk ienkgweisl saipykntak qaywtitvng srntdkllei seamkyrndl
      901 nasnlkdtpl pryeegesls riwvvrslgi dpasgdeill krngemtsav nwsandvvpi
      961 gnteptwqgy inssftykgw gadvsfryqf ggqvynqtli dkvenanlky nvdqrvsqlr
     1021 wekpgdkaqf ralnpsgwet katsrfimde nifqgsslsv yyrmdrtntk fishwglssa
     1081 kvtfnmedff ywstvkrerg lyypysrqft falnvaf
//
LOCUS       WP_118195416             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118195416
VERSION     WP_118195416.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110287
     Region          45..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrttcyfrs ltkvllfsgt isvlpvaqly antvtdplsv tfnqqqlsgt vkdakgepvp
       61 gvtvsvkgst mgtstdvngq filqnipegs vlvvsmigyl nqevtvtgst vditlqedaq
      121 gldevvvvgy gsvdkkelts avttlrqddl iagapsplms mqgkvaglnv nssngtdpns
      181 nvtlqlrgvn svnasqgplv vidgvpggnv nsvakedies isvlrdasaa aiygtrasgg
      241 vilittkrpq igkavvslts effvesirkr pevlsgdrfv evglgedlgh rtdwydevtn
      301 dnpfshrqvl nisggsenan vyatvnkrda kgmaigskrd eiggrvnsnf kffdgfaels
      361 tnvsynqvns dfanndvfnm amvlnptetp ydasdvtgyn vltggydywn pvaevmlrtd
      421 qrqyryllan stlklnlneh lnttatvgvi nnsehgnfyr saqhrlsrqd gvdgyasqey
      481 trsldrifew tvnynrrwed hsinavggys yqdfngrgfn annsdfpvdg iaendmgsgs
      541 yltdgragma swkdpwvkla affgrvnysf kdryvltatg ryegsskfap gnrwgffpgl
      601 slgwrvsqep fmqdltfind lkiragyget gnegfgaevs trmysadtwf lqdgqwfrty
      661 gvrhnqnpgi kwevkkeynl gmdfsildnk lggrfdyykr viddliydis vsqppaihdk
      721 ttmnvgsmen tgyefelnfr avenedftyn tsivashnks klrslwgsqt ftdrksfpap
      781 gspgsavrly pgedigqffi wrfagftddg ywklydengn afdvrerskt vgdksfvgqa
      841 ipklqlswtn qfsyknwdas vymrswighd vfnminmyys lpnvegqnvl adafdkhrdi
      901 vgekelsdyw lekgtflkvd alsigytfnq esikpfrnlr vyatgrdlfv ftnytgldpe
      961 vningldpgf eernvypktr tfmlgfqfnf
//
LOCUS       WP_118195519            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118195519
VERSION     WP_118195519.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119718
     Region          29..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrksklisav lftawmtfhs igalgqqilr gevknligep ivganiflkk gevsfssgeg
       61 grfsipvkrl pdtllvshlg fvtyemglgh gelqyltifl qeegrelrav evstgyqqlp
      121 reratgafef vdkkllsrgv ssnimdrleg vasslnfdkr nasenglvap vplvrgvsti
      181 nanlsplivv dnfpyegdin ninpedvesv tvlkdaaaas iwgaragngv ivistkkalg
      241 sksrislssn fsatprpdlf ynggylaagd fievermlfd qgfyqedvrt plspivealf
      301 rddpsidnlv nyyskydirr eaeehlyrna gsfrnslsis ggsdsyayyi sagddrskyn
      361 ivsdessrtt ltsntsikpl enlslhlgvn fvhtnrqnng islrelrtqg lypyaqlade
      421 ernplpiptd yrmtyvqeae dngllnwgfy plseiglkek ydknmetrvn lgidyklpag
      481 ltfamkfqyr nsnrelrnlr teesyytrnl inrftqadgs havprgsilt enkdrvrayi
      541 graqidfdrr fddkhvvkal agaevrevkt tanaqgvygf deeiytfqnr idystrfytl
      601 ptgranipsq gnsfreltdr yisyfsnasy syddrylisa sarsdgsnlf gvktnqqrvp
      661 lwstgaawlv dnegfynnet itylklratf gysgnidrst tafptgyylt dhvtgldyvs
      721 istagnpqlr wekvrtfnlg adfatkngrl sgsleyyskh stdllgnipl dptsgyflgt
      781 gysyrinyad lkakgfeatl nsknqigrlq wditaifnyn tdkvtdykfe gtavasylst
      841 yvepvprlgy pafglysypw hgldpetgdp qvlvdgvisd dysayvrdlt vddlvyhgsq
      901 ipkytgsvmn sfrygafdls mnimwkagyf frknsinynn lfqnwdghrd fydrwqkpgd
      961 eqrtdvpslp qnivsnrdlv yersevlvek gdhvrfrdir lgytmlrngh kglpfknlnv
     1021 yahaqnlgii wkstksgidp eypymtvrpr atlslglrid f
//
LOCUS       WP_118195538            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118195538
VERSION     WP_118195538.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117031
     Region          43..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmekckyll fcgtlalwma ggfqqvyaat epssqaiqqq snkvtgkvsd atgpiigasv
       61 vekgtangti tdldgnfsln vkagatlvvs yvgykseevk agrgplnitl kedakaldev
      121 vvtalgikre rkalgygide vkgealtkak etnlinsmag rvpglvvsqt aggpsgstrv
      181 ilrgstemtg nnqplyvvdg vpldntnfgs agtnggfdlg dgissinadd venmsvlkgp
      241 aasalygsra shgvilittk rankdkisve yngtltfdtq lakwdevqqi ygmgsngtys
      301 ydaisntnks wgpkadgsnm lkyfdgverp flivpdntsn ffrtgitatn saiigvnsgk
      361 tgirftytdm rnkdivpqth msrdifnlra ntsagkvdld fsvnytredv knrpalgdsk
      421 snigknlmtl attydqewlq tyqtadgeys nwngmdpynv npywdiyknf nkskkdlfrm
      481 ngkavwnidp hlklqatlga elnwftfddy kapttpgfea grlqnsafrn rmynfevlal
      541 ynnhwgdfdf natlggnvyk vnnqttvtta qdmkirdvps ltsfneisvv pgsyrkqins
      601 vygavnvgwk hmlyldatlr gdqsstlptg nnmyvypsfs gsfvfseltk lgdllpygkl
      661 rmswaqvgsd tdpyqlglvy tkskyaypgy tigyidngti pnkdlkptkt nsvemglelk
      721 flknrigldf tyysqisknq imgmasswtt gynyrlinag kienkgieia lstrpiqtrd
      781 fswdinlnfs knsnkvkeld gesdmfelek aswldvqvaa kvgenfgsiv gpdfqrnekg
      841 dilidpqtgl pqydksnhvl gnaswdwtgg lltnftyknl slvavfdvkv gadlysmsar
      901 aayesgkspe tlagrdawyr seeerlaagi akgadnwkpt ggfvapgvid ngdgtyrpnd
      961 iyinpedywm svcrnapsmf iydnsyvkcr eltlsynvpk swlknvisgl tvsfvarnpf
     1021 ivwknipnid pdsnynnttg mgleygslps rrsygfnvnv kf
//
LOCUS       WP_118195910            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118195910
VERSION     WP_118195910.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120077
     Region          22..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkslltiifv lfywtvlaqt eitisgrvtd kergvpiaga tvtleatgms istssegeys
       61 lnlrprnlqd tlqvralgyt tvrlsvslan aanhnfelep svnvleeiei ntgyqklnkr
      121 sstgsvevid geelgystas nlinridglv sgayldrtey dfnlgaqqpe ltirgessir
      181 sssfplvvvd nfpyegdien inpndiesit vlkdaaassi wgvragngvl vittkkgrld
      241 qpltvdvssd lmvaskpdlf adrivssadf idmesylyeq gfydgeinnw rnpplspvvh
      301 llmdhdegsi sdqelrrqld llgtydvrdd flkyvyrnhv enntsislrg ggdktaysvs
      361 lgyskndytm ptngqerltv rfnqsympik kltlstdlsf trlnksiynt gnriaynqir
      421 ilnkklypya qlkdetgdnt vlridydesf iqenqefitk swdfipldel grdgnlsesq
      481 qvvmglnldy eivdgvrlsg hsqlfrtmse ssslfsedsy ytrdlfnsft tiegdefshg
      541 vpaggirddn naklwgyalr aqldireeis ndhmiqglig aeareinnss asrrvygvye
      601 grtyytqvdh vspirrmagi ggsgylpdgi yfsrtanrfv sffsninyaf kdryflsasa
      661 rndasnifgv etkdkwsplw svgggweisk epffgsdiln ylklrssfgy sgnvdnsvpa
      721 elviehsnyp dfysylsyns ivslqnptlr wekmeifnla ldmriiqnkl nisidyynkw
      781 skdllgsmli dptlgasavt anaselkgkg vdisigtnlr sgywlwsgll ragynktile
      841 kyretlstvt stiihsanfi grehnvlasl kwgglssedg apqgfdngel stnyrnlvre
      901 tpeedlifhg pgrprssilf rnrigyknfe lgfsiggqfs yyfrkgsiny sdffedwrgh
      961 adfydrwqvp gdethtdipa lyypldgnre gfyslsealv rrgdhlrlrd irlsyrtsap
     1021 diglknievf vlgtnlgliw tlnpegidpv ygasippplt itggfkigf
//
LOCUS       WP_118196136             939 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118196136
VERSION     WP_118196136.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 939)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 939)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 939)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..939
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..939
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104845
     Region          23..914
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrkfiyigc tvfamsllsm tgvqaqeesk dslvnvafgk vaqedlthai stvntseltk
       61 ktannnslvg lesfvggyng sslwgqgplv lvdgvprsas svkasevesi smlkdaaavv
      121 lygsraakgv ilittkrgkd spmhidvran vgvnvpkayp kyldadcymt myneacrndg
      181 iaerydagti yntamgtnpy rypdidfyss dylkkfytns dvtgevyggn ekthyylnfg
      241 mnyansllky geskkaydms fnvrgnvdmt lapwlkattn aaiifdnsyq grgdfwgaas
      301 tlrpnwfapl lpidmmdpnv ayiqeyitns nhlidgkyll ggtsadttnp fsellaagyt
      361 kekarrfmfd vavmadlggl lkglsfktay svdytsyyse ayaekyaiye pkwsnvngkd
      421 miigltkfnd dtkstneyvg kstydqtmtf saqfdynrtf ktfhnvsatl lgwgyqtqss
      481 adeghessdy hrtsnvnlgl rasynydhky yadfsgalvh saklpegnrn afspsvtlgw
      541 rlskekfmes vgfvddlkit asyaklhqdl disdyymykg yfsdkggwfq wydgtvggnt
      601 tgskrgdnpn ldfitreevr vgidatlfnr llrinanyft qktsglltqg astiypsffd
      661 lgtdlsflpw inynedkrtg fdfslsankk igdfdvtlgv ngmvfsskas irdevanesy
      721 llrqgralda tygyvcegff qdqadiekha kqtfgtvrpg dlkykdingd gvinsddqid
      781 lgaggwstsp ftfglnltlk yknftlfamg sgqtgavafk nnsyywnrgt skfseivmgr
      841 wteetketat yprlstsngd nnfrnstfwm yknnvfrlsn vqltydfptd tfngtfirgl
      901 slycggsnll tiakereyme mslgapqyrn fylgfkaaf
//
LOCUS       WP_118196344             920 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118196344
VERSION     WP_118196344.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..920
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102323
     Region          34..919
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkyhifft gmlsiaffmg atvdtkaqds iavvsrvnie hlkampdlql sntlqgqaag
       61 livipntggi gyanstfyvr gqhsngtnka iviidgierp iddilpeeie sievlkdasa
      121 kilygaqatn gvilvrtkrg qagkrvirfg aeygvqpvtr lpeyldsyny atlfneacvn
      181 dgllplysda dlqgyrnstg vndllhpnvd yykeflrsss tfrkatlels ggnarakyav
      241 tvgytgssgl ekvgdrsdln rvnargnldi ritdflsasa dvaarvekkd wgakdgggmf
      301 seistlrpne ypfmisaedi hghngiaade tsllfgassr kssnlysdml yggntseryv
      361 nsqtnlglnf dlnefvegla aeayitfdny sylrqqlrnd yptysidryl ntagdeeirf
      421 terkklnlpk kqsiasnsty ryfgwnarvk ynrsfglhdm ganaafryta eeatgssqdl
      481 kegnftfran yaynkrymle atlaamgsnr fqgdnkyffa hsvggawiis nesflkdmka
      541 vnllkmkvsy ghlgyagdtd fflhrtnwkk gdkeefkpst gasttdlirl gnpdlkweys
      601 nelnigiegr flnnrlsgev nyfrelrkni iginsakyat iggnfipsen igevlnqgid
      661 acvnwndkvg edftynlgfn itftknklrk tnelsniedy rksigqptsa ifgwqsqglf
      721 gkdvaiaghp fqsfgnyqvg diayadlnnd gmvdnndqtr igqsfpkttl gvdvtlnykg
      781 fglyilgtat tgvtqmltst yywnkgldgy svlaeeryhp vnnptgtqpr ltttsgvnny
      841 rnstfwtkng sffrlknvel sytlnnnskk gigknykffv rganlfvlsg ikeldpeqml
      901 agisnypvyr titggvsinf
//
LOCUS       WP_118196443            1197 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118196443
VERSION     WP_118196443.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1197
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134440
     Region          127..1194
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqqitlsr kkamrkvvwm kaaflllmfv ialhgraqnt dsklislelk eaplgealkq
       61 fsnvsgykvn fpsedvgayr vsvsihqlap laalqkileg kpfeyevkqh fitvrkvkpa
      121 lttrkvrnie grvvdekgdp lpganirgid spfgaisdik gnftckvmee thtlevsfvg
      181 mqtekvsikg rthvnvvmhe dkqqlgdvvv tgyqrisrer stasfgfids eqltrqmhsd
      241 lasslegqia glrmninpnn gdmspilrgv gtfspnvgtm plivvddmpt dltlseinpy
      301 nvesitvlkd aaaasiygal aangiivvvt kqakeegahv ninadwfits kpnfnslnla
      361 stsdiidyqt avfdanvaes gsasgflssy kagyynplfq lyldrengtl snseveatln
      421 qwrnndyyke yrdnvwrtav tqrynvsvsq kvgknnhfls fnyendkgrt indkrnkfsl
      481 yyksnyaits wlnvnagvda rlgssdtpnt lftsytmqqr yerimdadgn rynspyvnvs
      541 gysggayngs vvskaegvsp yktfgfnvld algeggtksr nvsirpfvsl qarflkmfky
      601 nfmyqyewnh sksevfdaed sylmrmtyns midtngnsam pkggrfyqne lssnrytvrn
      661 qidfdkswkn htvtaiagle frenkipkpt qqlmygydpq tltsdiidwq ayrdgvgtsa
      721 lsgntitlsg lsptlqesrh ryasfyanas ysylsrynvs gsirwdqadl fgldirnqrh
      781 plwsvgaswi mseesfmkdi vwldflkarm tygingnvdq ssttyfvvkq ktqsnpiktt
      841 yltyddddlp npklrwekta tynvgldfrl fnnlvngsle yynrhssdll vrrymdptlg
      901 aksrvvnnge mrnrgiefsl tanlirkmdw nfavdfnfah nknkmlkvdh sdsdtstsfi
      961 vspqnyfmeg tshntlwayr idriengypv avdkdgndlv tfnedgtvan ittgsslkgt
     1021 enlvnfgslt pkfngavslr lsykgialna ffvyaggnkl rnsvvsmsdq vgiqtlkdit
     1081 nrwsadapda nvrmyidmpt kvktyastfq dwwqygdinv kdagyvklrs lslgyslpsg
     1141 icrqirlnsl nlklqvnnlf twckagsdid pesyglnsgt rgmaspktys iglstsf
//
LOCUS       WP_118196505             937 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118196505
VERSION     WP_118196505.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..937
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104007
     Region          2..935
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklifsqait ltnaqplkvt lgedtqvlde vvvtalgikr sekaltynvq qvkgdelttv
       61 kstnfmgala gkaagvqins sasgpgggvk vvmrgaksit qnnnalyvid gipmynrass
      121 ggdgamatqp ssesiadinp ddiesmsllt gpsaaalygy egangvvlit tkkgradktt
      181 vtysnnttfs dpmmmpkfqn tygnmtgemm swgletdkry dpanffntgs nvsnalslst
      241 gndksqsyis vattnatgim pnndydrynf sfrnttnfln nkfildtsan yiiqndknmv
      301 sqgqyfnplt slylfprged fsdvavyery ddlsgvntqy wpygdlggvs sqnpywimnr
      361 mnrendrrry klaaslqyni ieglnvqgrv sidnteskyt ekfhagtvgn fagpkgryke
      421 enrldrqvya dvlanfnktf nefnvtanlg asikdlrmel tslhgdlnnv tnhftienlt
      481 rsgyykvnad glkrqtqsvf anaeigwrsf lylsltgrad wdsslalser gnkpffypsi
      541 glssilsevi dlpewfsflk arfsftsvgn aydpyltkvr yvyddqldqy kaeslypnsd
      601 lkpeitksye aglnmrffkn tlnfdityyn sdtrnqtfaa plpassgyta vniqagsvqn
      661 qgiemalgyk newrdfgwss nftftynknk ikrladgvtn ritgepiemp yvdkarlggs
      721 tspvvrlteg gsmgdlyinr dfkrdnngyi yldaktglps mveteykkig sllpkvnlgw
      781 rnsftykglr lnillsgrfg glvvsntqaf ldrcgvseys aqlrqaggvt innrnvsakd
      841 ylgivaagtg egdhyvyeat nirlqevsle ytlpkkwlyn iadvtlglig nnlgmiycka
      901 pfdpelvass tstfytgvdy fmqpslrnmg fsikvqf
//
LOCUS       WP_118196729            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118196729
VERSION     WP_118196729.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117379
     Region          36..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiyinrvs arlmftlilv lslfctslya qeklvtiqgv vysaddreal pgvsivanet
       61 svgvtdangs fslnvntgtt lrfafiglsp yemevtraes glviqlqnea rglsevvvta
      121 lgiereakgl gygvttvkge dfteamsnnw tdalkgkvpg lnltqassgp instrinlrg
      181 drsldpnrne alivvdgipm ingkassgvd qaygpgasgd dkdipidfgn glsdinpddi
      241 esvtvlkgaa atalygsrag ngaliittks grnkdgigvs fnsntsvndi lqwpdrqyey
      301 gqgnnnrnaa gelyysyqls pdgantgsts safgpkfegq syyqydptle gqsaspqpwv
      361 pyednvtgff rtgfnttnsv aidgagerfs grasithtkn ewimpntgfe rlvaslntnm
      421 rvsdkltlng kfsytdkssd nlpgtgynnq siayfmifqn pnvdlawyep rwkegkeqie
      481 qihpfssyie npyliahemt nslqsanvvg nlqgtytfdd rwslmlrsgl nmrqdqreqr
      541 rpwntsnfpq gfykqqdvyf fesntdallt fqdelnqdfs inasvgantm rgesklnnsi
      601 argltlpgiy klsnasdral aeneimkrqt nsvyglvnfs wkdrifldit grndwsstlp
      661 ednrsyfyps vsssfvlsdl ltlpeaisfa karlswaqvg tdtdpyrlsk yystsafpgs
      721 aeaptslhna elkpeisssw eaglnfalln nrvyadvnfy nnetvnqvlt ipldvttgfs
      781 safinggkir nrgievmlga tpvstrdfsw ntnitwsknd nevltlseni gseeqiiats
      841 gtasiiatvg gstgdiwgyg lvrnengdvv fdaetglavr paditkigna yadwrggffn
      901 efkyknfrls alidgqyggi vysqthhkms eqgklthtll gretgtvige gvvenadgsy
      961 spnttpvain twygdyyrra nietnsfdas ylklrevrle ytlpasfvsr lrvkgasvav
     1021 ygrdiamisd fpifdpetas lngstivpgv emgqlptprt wgfnlkfnf
//
LOCUS       WP_118196823            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118196823
VERSION     WP_118196823.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120888
     Region          24..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvkkvlflfc cmfahviyaq nmmikgtvid anndpllgvt imvkgtttgt itdvdgnfsi
       61 kgktgetliv syigmqtqev vfrgqplkim lkddaqalee vvvvgygtmr kkdltgsviq
      121 vrpdkianen pktvqdilrg tpglaigyna dakgggsmni rgqrsvytdg nhnspllild
      181 gmmfygelse inpddigqid vlkdasaaav ygakaangvi iittkkgkrg kpvvnvstni
      241 gltqrsayre rfspsaylqh yadwkaksty ganaegnwdd yqigvykgmd dyytnpdklt
      301 nidldiwrgy tsnesgesdl siwakrlgft gnvlenilsg ktvdwedkaf rlgfnqdyna
      361 svsgasekvd yyfslgylrn egaliddtyr avranmklna kvtnwfeiga nvnfqdrtdg
      421 sidmdegqfm rnspyadyad edgnpiqypn detysqrgyn ydfqkqyldl ekgytvlnsi
      481 fnakvklpfg ityqfnvapr yqffyeryfm sadlpgsnpn nrgadrehak rfdwslnnti
      541 twdkifdkkh hfivtlaqea eerqrwsdri earniqpsda lgfhntqngs kesssysttd
      601 shetadgllg rlfysyddry mlttsirrdg ysafgstnpy awfpsvavaw tfsnekffqk
      661 iknvmssgkl rasygsngnr sladpytala nlsagsgdym gyltstgeve lmrylmasrm
      721 anptlqwekt kswnfaldfg flndritgtm efytmntndm imsqplpvft gfnnittnlg
      781 qvnntgfefs lntvnikqkn fewnitfnfs ynknkikhlf yeyenvldan snvigqkesd
      841 ytangwfigk pinqiwdykv igiwqndewk eaakykqqpg dpkvwnnpen diynadgsvq
      901 tivyndddkq flgtttppin wslrnefvlw kdltvsiniy srmghkalst nylnndddgg
      961 rmsyaaaclq akeywtidnp tnkygridan gpdgakkpgm lynrsfirle niavgytlpr
     1021 kltqkwgier vkisgtvrnv atwakdweyg dpetgglgtr lyslglnlsf
//
LOCUS       WP_118196863            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Albibacterium
            indicum].
ACCESSION   WP_118196863
VERSION     WP_118196863.1
KEYWORDS    RefSeq.
SOURCE      Albibacterium indicum
  ORGANISM  Albibacterium indicum
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Albibacterium.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Albibacterium indicum"
                     /db_xref="taxon:2292082"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115121
     Region          36..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkqnrmprr waylflsclf ifspfslfsq evggftgtvt dqlsneplig vsikvkdrnl
       61 ststdaegnf vinasdgeil qlsyigykdt evtvtgtsln vsmaedraql devvvvgygt
      121 qkrsdltgsi qrvsgetfen qpvtqigeml sgtvagfygt qgasadgggs mevrgttslt
      181 ggttplvvld gviysgslad inpndiesid vlkdassaav fgakaasgvv mvttkkgksg
      241 kpminftakt gvsslsndkf gpldakgyen frrdffrtkg tglpdwywnd pndlpegvti
      301 eqwrnassnp hadntleylg rlnffeteve qylagqttdw qdqvfhsgin qdydvsiggg
      361 adnynyywsl gyvdnegiil gdefnairsr lnvdfkvnew lnvgtnaqls vrdestvpaa
      421 igdiksmgpy skvyeddgsi kwypndyyht nplinhllqd rlnkttsffa svygnltlpy
      481 gfnfrvsfqp rlsygknynf wgpgtivges dhidgygrrd dsslsawmid niltwkrefg
      541 ihdfdvtlly naeqtktyls radnetflpn qqliyhglqf gskpflnnnd teaggnamma
      601 rvnyslldry lftasvrrdg ysafgiannk atfpaaafaw vvseedffpe nsvlnrlklr
      661 lswgingnrd igiyaalaqi atnlyydgsn lqmglynntl anpglrwekt eaynvgfdig
      721 lldnkidlsi dlydmtttdl lmarqlpeit gfnqitanlg elanrgidia lnttnienen
      781 ltwrsnfvfs lnrnkieslf gefedvevng qlvrrelpdy tnqwfpgkai davweydvtg
      841 vwqlheaeea akfgmlpgdy kstdvdgnya ydalidksfi gytkprvrlg lrndvsfleh
      901 fsasvflrad lghianfaha lhesteydrr giwnvpywtp tngnneyart sevhgaydgg
      961 lrifkprsfv rvqdvslsyt mpskvvervg akgirifasa rnlftftdwp gydpesgdtp
     1021 mpmtytlgvn lal
//
LOCUS       WP_118200376            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118200376
VERSION     WP_118200376.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116369
     Region          24..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmtfia clflslgmal aqtqvsgkvt saedgepiig asikvvgtkt gavtdvdgnf
       61 slnvpagtkl evtylgmlpq tvkagqkmki vleadnktld evvvtamgis rdkkalgyas
      121 qklgsedlni agtsslasam qgkltgvdir qssgapgass qivirgarsf sgdntplyvv
      181 dgmpiassad ydtgasvtga dkanrsidin pddiesidvl kgqaasalyg irasngviii
      241 ttkrgkangg rpqitfstdl saqtvskkfe rqtvyaqgnm gqggstgayn pnssmswgpk
      301 iadlandaty ggntdnvytq qygkhegmyy npkyaaagld gwttpqtydn vgdffntgft
      361 qnsnfgisqk ngnlaysfgi gdtyqkgiip stgmmrttar gavdfeinkq wktgfsanys
      421 stkitsapga ndsfisylyg apaefnlkgt pyhkpnspsd qilyrsgvfq npywwaanse
      481 yrqatnrvfg nayvefrpnf nwdkerfnlv freqagldvy tttnddiney gtlvsgnktg
      541 gsienygvqr nvfnnlftan ftakldaaqk wdlgfllgse fnhenartwd yagdnflfyg
      601 qptisnvskm tynseyksee rtvgffgqls lsyanqlylt vtgrndivst mprgnrsffy
      661 psvslgwift elpalkgnhi lsygklrasf aqvgqaghyy anyyyvpsyg sgmygftpvs
      721 yplagqgsyt pyyvkydpnl kpqntmnwef gadlnffdnr irleytasyq dikdqifnvp
      781 tagstgyqyl ctnagemttw shefainasi iqtkdwdldl gvnftkltnk vksladgves
      841 imlggfvepq vraqagytyp niygiafkrd eqgrlllkdg lpqgtsdsqn lgectpdfnm
      901 gfnlkarwkr lslsatldwq kggkmyngti mtmnlfgatk eslpyhegtm vvdgideatg
      961 qpnkievskq sywyayhdvt esgiydrsyv klrdvtlsyq lpkfagidis vygfarnlll
     1021 wskmkdldpe ssqgngnmsg cferfsipnt ssfgggfkit f
//
LOCUS       WP_118201158            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118201158
VERSION     WP_118201158.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115008
     Region          32..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqrmkhcf faltlcctag smygqvaqds sktiekkssv ngkkiqkskf sddpielnnv
       61 vvtalgikre ekslgyatqt vsgseitatm panwsqalqg qvaglnvisa cgplsstqin
      121 lrgnvsmnmd gngalivvdg vplsspmnnp ggsygaggns egsidfgngf sdlnpddies
      181 iqvlkgasas alygsraang vimvttksgk kakrglgisy nfnnsweqaa hfpdyqyefg
      241 qgvaknigsk gtewagqpyy sygagddgla stsgtssafg akfdgqmfyq ydpekegrad
      301 vatpwraykd nhsglfqtgh tmtnslaltg nngtgnmris lthsksewil pnsgyqrlta
      361 afagsqqisk rvkinarmsy tyrdventpq ltynsnslsy flifmnpnfn ldwfkpmwyk
      421 gkenikqirp fssylpnpyv llyeatnpak khsfngnisa nftinrfldl qlrsglqata
      481 qqqeqhrpwd dkafptgffk kqnifdyevn sdvlfsyhns fenglnvnas aggnmmqsyy
      541 dllsasvtgl ntpgvyslan gvsnplvgtt irkkrvnsly fmanlayqem lflditgrnd
      601 wsstlprknr sffypsvsls gvlnsmmkmp kwvnllkvra swaqvgndtq pyktspyytt
      661 sdfsgslvkp gtlynagfkp emstnweggl dfkafgsrlg ldvtyyynrt knqilnapfd
      721 pttgytkgti nsgcvsnrgv eivlrgtpir nrdwqwdmta twstnknkie slsefaderq
      781 ilgsyvsgnv siigtkggtt gdiwgyklkr nakgeviits aglparpsei eyvacalpdw
      841 egafntslrf knwsfsmqwd gkvggmtysq shhkmceqgh laetlngrkp gtslyldiad
      901 pdvlklfekq kitpvagvyc ivpgvvdngd gtyspnqklv tlesyykeyy rignvetntf
      961 sttylklrev rldyqlpksw lkntfinnas vgiygrnllc itsypmydpe ttsldgntfv
     1021 pgvevgtlpt srswgvnlkv df
//
LOCUS       WP_118201476            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118201476
VERSION     WP_118201476.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116500
     Region          24..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvkrltmlmg glilstgial aqttvtgkvv sqedgepvig asvrivgtkt gtatdvdgnf
       61 tlpnaskdav leisylgmqt ktmkasakmk iilasdarnl devvvtalgm krsektlgya
      121 astanaselt vaksgslmsg lqgkmagvqi sgggvtgtsq kvvirgissv ssnnplyivd
      181 gvpinndrlg dnsvdfgsga gdinpedies vtvlkgasat alygsraang vimittkkpq
      241 gnkkasityd gsltftdvlr vpmtqnlfgq gwgswsneen gswgprldgr ehwygstgls
      301 ngetltkpfs yaknnirdfy qvgkewnnnv slrygdekvg ivasygnvss ngitpndgdt
      361 yhrntfslrg yanidrfhld mslnyvrkdm rrsrdmymel lqgasdvrft dmkdynlern
      421 nvdnyytlya tnpyymvdny ystyqddriy gklelsydit kdikvigrfg gdytnykter
      481 ieprilyteg syqangngtt vgnqgyysky rsqrgqidas llltgnhtfg dfsvgatlgw
      541 nlnqrnydtv ggyneqleip gwnsldntis nsltdatswk rrligllgqv elgykdwafl
      601 nlsarndwss tlpvgnnsff ygganvsvll nqaipalkni kqidllkvra aigqtgndad
      661 vymtnsyyrp fqsyytylpi sgvlglteyn rlpntnlkpe itteyelgls gtffgnrlsf
      721 dvayydrttk nqiisatlap etgyttntrn vgklqnkgie amvnftpirt kdwewsvgat
      781 ysknwskvke lwdgldeyti pvgttstgly ssmrgvsyvl kvgepigifk lpatekvtdk
      841 nsqyygykvv dnngflksss teydylgssq pdfvmgftth lkwknltlaa tgdwhkgglm
      901 ysetsyithf ngnstetvfn erdafiyphs vkvvggqyve nnipvssekm nyaqgnysyn
      961 pevrrdfvvs rsyfklrela ltydfpktit salkmqklsl slvghnllli tpkhqnyidp
     1021 essnfgndis sefgetmgsv strnyginlk vvf
//
LOCUS       WP_118201211            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118201211
VERSION     WP_118201211.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124014
     Region          51..103
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          116..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mirrnylksl mifiltclpl lgasaqqkvt vnvvnaflkq vfstienqts yrfsyksdii
       61 dhrkditirk sgvpvttvld aalkgrnlky svvsqksivv sekhaaaapq qsnkhkmqgv
      121 vkddngepvi gatvsvvgtd elavtdidgr ftinaakgak vkvsylgfvd revkasenmn
      181 iamsedtqal sevvvvgygt mkrsdmtgal ssvntkemak rtttnpaeal qgkvagvnil
      241 ksggnagagv sikirgiktf gdneplyivd gfpgdinsvn pqdiesmeil kdgaaaaiyg
      301 svaangvvli ttkngkkget kvdfssylsf tqvskdldll daegykkvhk mmyenagrkl
      361 payithetgv ntdwqdaiqr kglaqsymvs lrggaekgqy svsynhadek gifignserh
      421 diarmkvhat kgiidldanv dfkytkghqp qyslkeaymi splvpiynen ekygfgltnf
      481 dgipnnrnvv addhykknty kkyhttanaa ltfnffpwln fktsygyrge heidnshypd
      541 yiadpksqnk ypnsyeyray wqeqvfenvl sfnkqiqkhs inamlgtsln mikynwesvs
      601 vegktnvnev ingqlstsdk pagfldpnfp tisggvggty ygtgsyweyn rvsffgriny
      661 nfndrylfqf tfredgsskf ssdnrwgffp svavgwrise epffpknsvv snlkfraswg
      721 qlgnenalgk ydfltriasy ndmymgyvqg agsnpwtgsi artlenlplk wettdtknig
      781 fdfglfgnhl ngnvnyylne trdllitrri apsagldnpt lnvgkmrnqg felelnwndk
      841 indfeynvgf nistiankvv alanedqtiy gvglkygteh fptqtkvgkp igafylyqad
      901 gifqsleevq ahknskgell qpnaqpgdvr fkdmngdgvi deddktysgt giakveanln
      961 lgasykgfdf savigsafgn kiyngiryyy egmnsasnfl kttlnawtpt ntktdvprai
     1021 ygdpnqntre strflengdf vrlrqvqlgy tlpkalskhi ycdrirfyvs aenvftitgy
     1081 sganpefsqg vlnsgvdrft ypfsrsytvg aqvsf
//
LOCUS       WP_118201568             942 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118201568
VERSION     WP_118201568.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105042
     Region          24..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msniisryka ilpvslfals aqgvmaqdat eadtinvafr kadardvitp vstvkvknll
       61 eknyntysld nmqalaagyn gslwnqgdal vlidgvprda nnvlpteied itflkgasav
      121 vlygsraakg ailittkrgk ieplkitara nyqmsvaksy ptyldgaqym tlynqaland
      181 glsakysaed iyntaagtnp yrypnqqfyn sdylkktksr ydvtaefegg gkfaqfytnv
      241 syyregdfln fgegknnytd rlnvrgnidl qladwasgwv nanatyynqh gsnsefwkaa
      301 stlrpnrvap fiplsyldpk danslalinn srniitnpag lpagqyflga tqedqtnafa
      361 dmyaagyntw tsrqlqfdtg vkfdlasvlk glsfktmfav dystsyttsl ndsyatfgvn
      421 wtqfdgkqii gsvtqygedk htgtlnssns aerqtlawtg qfdyvnsfgn hnvnatllan
      481 gyqqtisgey hkvsnanlgl lvsynyahky yadlaanmvh saklpegnrn aispsatlgw
      541 rlseenflkd vnwlndlrlt agytvlnqdl dikeyfmyen iftatgtwwg wsdannsiqt
      601 sdsqrggndk lgfikrkefn vglngalfgn rlsfavnyyn tvtdgllaqp gyiypsymht
      661 ywpvstfvpy inygknrrtg vdfslgyndk vgdfeygiqa fgqtnssknl kvaenveydy
      721 mrtegklida lwgyeclgyy nsqeeidnae akssfgtvkp gdlkykdqng dgvidskdrv
      781 vigrwsakft ggmnltlkyk nftlfamltg qfggnaikdd tynwvygerk ysdvvlgawt
      841 eskykngesi typrlttqsg dnnfnasdyw mystdridls rvqltydfnk slfgdnslvk
      901 glqvyvngss lltiagerkq mernvgsapq trsftigakv ef
//
LOCUS       WP_118207056            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            stercoris].
ACCESSION   WP_118207056
VERSION     WP_118207056.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113164
     Region          15..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msdwkqssqs tqqaktitgk vvdvagepii gasvlvkgss tgsvtdidgk fsveapvgst
       61 lvvsfvgyat eevkvgtasd ytvtlkddtq slsevvvtam gikkekkalg ysvsdinske
      121 lmknkqtnvv nslagkipgv nitqaggaag agsnivirgg nsasesrdnq plfvvdgiiy
      181 dnstvntgns gtdgmtktat tfsnrvmdin pediesmsvl kgaaaaalyg sraangviii
      241 ttkkgeegav rvnvsskyty swanklpevq kqygrgeynt sgafidktmd swgdridgma
      301 ydniddffqg ssvwdnsvsv sggskngsfy lsgsnyhqsg iipttgydkt tfrfngeqky
      361 giltvganvs ysqastdktl tsaglygqgg ngamtavygw pvddqmsryl nddgskyril
      421 eglqdleddv enpywilnkn tltdetsrft gavnaslklt dwwdvsarag idkyttssnt
      481 lrrpggavkq iyqngymskg dvnyqyittn vmsnfhktfg dfdlnllvgt tteatkttnn
      541 trwgynfvte glysfnniik anqyfkestv rkrmvglyge frasyknlvy ltvtgrndws
      601 stlpvnnrsy fypsvsgsfv ftellpknnv lsfgkirgsw arvgkdaday slgyymwpva
      661 tlnggkygmg nswtggsvgl kpeiqdsyel glemrffngr lgfdytyyqs ktkdqicapr
      721 laqstgyifl tlnggsvenk gmelsitgkp ivtkdfqwet tlnlsgnrgr lgdfidgvdi
      781 fyvtdaqvga akagsipngg yflgltgnky etaqgpdgkm ynvidpstgl ykdtqvetni
      841 vgnrepklig gfnnsfsykn fnlsflfdir lggdiyngte yylvtkglst ktinresvsf
      901 tgvvntgtaa kpsyetktit ynanetyqvg nstrsgkymi qeyyknyakn aynfitdtnw
      961 lrlrsislsy dfkdllkkqn iikgltatit gtnlfvwtny kgmdpetcvs gsgtggsgsa
     1021 gidycgvpat agmsfginlt f
//
LOCUS       WP_118207240             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            stercoris].
ACCESSION   WP_118207240
VERSION     WP_118207240.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109634
     Region          5..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mssaktlqis fvgmqtqdva irpnvrvilk sdaeqldevv vtamgikrdr kalgyaaqdl
       61 nseqlnkagt tslasaiqgk ltgvdirqss gapgassqiv irgarsfdgn nqplyvidgm
      121 pvnttadfdt gksvtganya drsidinped iesvnilkgq aasalygira sngvivittk
      181 rgsknnmnkp svtistnlsa qrvsrkferq niysqgnsia agydpsssmt wgpkiselan
      241 dpkyggnmnn qytaadgmre gqyynpkraq agldgwttpq iydnvgdflg tgftentnvn
      301 lsqsinginy sfgvnnshqn giipstgmdr wgarglvdwk inpqwntgfs mnysstkits
      361 apgandgimn vvysapaeyd lkgipnhepg nptnqilfrs tsftnpywwa ehneylqhtn
      421 rafgntyley qpdlglgenf slkireqagl diwtsdyatv remgstsslk ggdienygsq
      481 hnvfnnlftv nfdgkfgksd ewrlnvilgn efnhesirnw dyygsnfnfp gftnignats
      541 ltsseykrqe rtvgffgsls mswqdqvylt vtgrndyvst mprgsrsffy psvslgweft
      601 klpflqnnki lnygklrasf aqvgqagnyy anyyytptyg ggmysyypvt yplpsgvstf
      661 tpyyrvydee lkpqnttnye vgadlhffgs rlkveytysl qnvedqifyv pvdgatgyqe
      721 mltnagkmrt hahelsinaa ilqakdfdln lginftkvnn kvielapgve simlggfvep
      781 qiraqagcty pniyglgfkr deagnlllln glpqssgnsq dlgncspdft tgftlggryk
      841 rlslsttwsw qqggkmyhgt nmtlnyfgat keslpyhegs mvaegideat gqpntvevnk
      901 adyyqayyni tesgvydtsf iklrdltlty qlpklgifdi siygfarnvl vwanlpnfdp
      961 essqgnnnms gyferfsvpn tssfggglti nf
//
LOCUS       WP_118207255             683 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides stercoris].
ACCESSION   WP_118207255
VERSION     WP_118207255.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         1..>683
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          57..>667
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnedrkkrgi knhkilmtva icalflgssn tfaarstshe nhgvteqmqs vavnvlvvda
       61 qgepiiganv vekgttnggi tdingkirmn vtagallqis fvgyttqeik atpnlrvvlk
      121 ddtelldevv vvgygsqkke nltgavasvn vnqtlegrpi adigrglqgt tpglsiqvps
      181 gevgsdpiik irgqigsieg eatplilldn veipsiqmvn pddiesisvl kdaasasiyg
      241 akaafgvvli ttkkgaksdr vnvsyqgnls fqnmakemkm gqfnaleysv eamkrsgkta
      301 tggisffmte sglerarewq nkyggklgpd dpyvygrdwy vdangrnigl rtfdpydymi
      361 rewapthshn vsingksgkt tyniglgylh qngmmkpakk ddftrynasv rlsteinkyl
      421 tiragsifss rdkrypysts sttadpwlyl yrwgpnmplg vnedgndlrs pwsetkqant
      481 asqvdnylni slgttvnvtk dwkfdfdyty anetgvikkp gtrysaanaw sagvprtdan
      541 gnqiyvnnlg qqvdaaaega mpayklpyee ytphgsnpdh iyrkssgarr htfnattdyn
      601 wqinddnnfk fllgmnlvty dyednwsqit dltditnpqf dlavgtqtas gnqkwegqmg
      661 yfgrinlksa tklfsvllas krp
//
LOCUS       WP_118207352             515 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides stercoris].
ACCESSION   WP_118207352
VERSION     WP_118207352.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         <1..515
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <17..514
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 llrylkkify nsvaelriny nykekyllea nlrydgtskf psgmkwrwfp sfsagwrlse
       61 eafmewakpa lnslklrgsw giigdqtvdn glyvsslgtg qvnwlgadgq klfyrgtpsa
      121 vassitwqdi atldlgfdar ffhgdfgvtf dwyqrdtrnm ivpgsgiayt fgaaapkgny
      181 gslrtrgwev sldynhrfnn glginamftl sdaqteitey sdtrlisdyy vgkkygeiwg
      241 yrterlyqkd dfvydnngel vtvwalngke vaagtpgake mnklkdpngv yqdflqsgdf
      301 kfgpgdvkya dlngdgklgn gagtvedpgd keiignetpr feygirlgad ykgfdfsifm
      361 qgvgkrqiwg ngflaipgyn tadgaipdai asdywteent gafyarpwnq sgsndaynyy
      421 kqsrylldms yfriknitlg yslpeniikk vrmqkariyl alenfftfdn lnglpidpea
      481 isgysmfnae nynsgrtgvg tptfksvsvg vqlnf
//
LOCUS       WP_118207436            1190 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides stercoris].
ACCESSION   WP_118207436
VERSION     WP_118207436.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1190)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1190)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1190)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..1190
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         1..>1190
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          35..100
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          113..1171
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrkryllfp lffflfclpf caeaqvgekk ltvefkneel ssvfkqlski sgykilftyd
       61 dvksytysga ikdknireil divlsgkkle ytidkefiti ttkgpskqak vytvngvvls
      121 addgepliga tvmvkgtstg vltdidgkft lpnvssrskl efsyvgmlpq slspsptmkv
      181 tlqsdvqtls evvvtgmqrm dkrmftgatd qlkaenikmd gmadisrgle grsagvsvqn
      241 vsgtfgtapk irvrgatsiy gsskplwvvd gvimedvaei gaddlssgda etlissaiag
      301 lnaddiesfq ilkdgsatsi ygaramagvi vvttkkgksg tnkisytgef tmrmkpsysn
      361 fnimnsqeqm dvyknmeqng slsfvdsyra sqsgvygkmy hlinqysatg gvfglantpe
      421 argaylkqae frntdwfdll fsnsisqnha vsmatgtdka syytsisvmn dpgwtkrskv
      481 qrytaninst ynifknltln lignasfrkq qapgtlgsqa dpvsgevkrd fdinpysfal
      541 ntsrtldpne yyvrnyapfn ifheldnnym dlkvtdmrfq gemkwkpiqk velsilgayk
      601 yssttqnhyv kdysnqaway ramddatmqq anpwlytdpd kintlpesvl pvggfyrdtk
      661 ytmssydlrs tvsyndvfne nhivnffggm elnatdrskv wfngagmqyg mgmlssydyl
      721 ffkqgneent pyntvdetka rqvaffatgt yswkgrytvn gtvryegsnk lgksrsarwl
      781 ptwnisgawn aheetwfskl nsilsnltlk asysltadrg pafvsnslam vssynpwrpn
      841 advmesglgi lqgknselty ekkhelnlgi dlgfldnrin fsmdwykrkn ydligwlstt
      901 gldgeigkya nvasmrshgi eltlstrnia kkdfkwntdf ifsktknkvt dleafssvmd
      961 mvsgygfamq gypvrslfsl dfrglneegl ptfinengel ttsninfqer nnkshliyeg
     1021 ttdptitgsl gnvfsykglk lnvfitysfg nvirldpvfs nqytdldamp kefknrwmrp
     1081 gdehrtnipv iadkymnvnd sylsraynay nyssdriakg dfirlkeisl sydlpkkwie
     1141 plkisnlglk lqatnlflly addklngqdp effnlksatk lfsvllaskr
//
LOCUS       WP_118207641            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118207641
VERSION     WP_118207641.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123603
     Region          24..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrllfllv nlflfvggvl aqtkvtgtvv sqedgepiig asvvvagaar tgtvtdidgh
       61 fslevpagkk lvvsyigmqs qtltpaakmt irlkadsksl gevvvtgmqk mdkrlftgat
      121 tkisgdktkl dgvadisral egkaagvsvq nvsgtfgtap kirvrgatsi ygsskplwvv
      181 dgvimedvte vdaddlssgn aetlissaia glnaddiesf qilkdgsats iygaramagv
      241 ivvttkkgka gtnrinytge ftmrlkpsyr nfnimnsqdq mgvyremynd gyfsfeksfr
      301 asnsgvfgkm yhlmntydsk tgtfglpnte eamnsylqka eyqntdwfdl lfsnsisqnh
      361 svsmstgtdk aqyytsfsvm ndpgwskqsk vqrytanvna lynistklsf naianasyrk
      421 qrapgttsqs vntvtgevsr dfdinpysya lntsrtmdpn elyvrnyapf nifrelenny
      481 lsldvvdmkf qgelkykpis kvelavlgay kystttnaat itdqsnqawa yramddatmr
      541 danpwlytdp dkanslpfsv lekggfyret kykmnswdfr atasyndvyn kdhivnlfgg
      601 leinsldrsr syfngvgmqy dmgylpafny nffkqleeen gqyysldnsy qreasffgta
      661 tysykgryti ngtiryegsn klgksrsarw lptwnvsgaw naheeswftk lnpvlshltl
      721 kasysltadr gpasvsnslv viqsynpwrp fagdketgle iyrlgnddlt yekkhelnlg
      781 ldmgflnnri nvtfdwyrrn nydligpkrt mgiggeiyky anvasmrshg eeltistrni
      841 etkdfkwstd fifshskntv tdldsranim qmitgtgftm ngypvrslfs idfrglnnkg
      901 lpivvnqdge etsyggdlyf qstttdylky egptdpting sfgntfsykg lklnvfitya
      961 agnkvrldpa fsssysdmta mpkefinrwt qagdeaytdv pviadqrmkq ndnyigylyn
     1021 aynystarva kgdfirmkei slaydfpgkw iqalrlnsvn lklqatnlfl iysdkklhgq
     1081 dpeffntggv atpmprqftl tlrvgl
//
LOCUS       WP_118210942            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118210942
VERSION     WP_118210942.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112241
     Region          44..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkieratqll flllisqggn aayanlprga saspvqvsaq ankitvsgtv vdvngeplvg
       61 vsvlekgtgn gtitdmdgnf tlsagegatl eisyvgyqnl tvsaketlgv lvmkedteql
      121 devvvtalgi krsqkalsyn vqevkndvlt kvkdanfvns lngkvagvsi qrsasgvggg
      181 trvvmrgnks ikgdnnvlyv idgvpmgnqa drtgdgtgfg agrtssegia sfnpediesl
      241 svltgpsaaa lyganaangv ilittkkgaa gkvnvnvsss aefsnpfvlp rfqntygnvs
      301 geaaswgekl pvpssynpad ffntgttftn sfnlsvgndk nqtyvsgsav nakgivpnnk
      361 yhrynamvrn ttkffndklt mdlsasyvre yynnmlsygt yfnpllgayl yprgenfeke
      421 tyferydael gynvqswtpg dfgmavqnpy wvayrnlrpe vkdrymlyas lkyeitdyln
      481 vsargrldnt ytekedkrya sthgtfakpl gryaysnetf rqkyadiman lskpfagdfy
      541 anvnvgasfe eydtkgrgyg gqllkvpnlf aydnidpstg vpsqtggdnr kmnlgvfgsa
      601 eiswksavyl tltgradkps qlvnskspwi fypsvglsai vtdllpetmr qsispvlgfl
      661 kvrasytevg spipytgltp gtithsiegg vikpfkyypl pelkpertrs yevgidskwl
      721 nntvslgvtl yksntydqll eaklsetsgy dymfvqagnv enrgieltlg ydqtfgkfsy
      781 stsltatanr nkiialasnv knpvtgeald lsdikvgrfr lregeevgti yaeerlkrdq
      841 dgyivynegq tittestepy klgsvnakwn lgwrngftyk gfnlnflvta rlggiviskt
      901 qavldqfgvs qasadardag kvmvgnvavq pkdyyesvvn ldaynvysat nvrlqeaslg
      961 ytfpnswfkg tpfhsvnlsv ygtnlwmiyn kapfdpelta stgtfgqgyd yfmlpsqrty
     1021 gvslkfgf
//
LOCUS       WP_118211609            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118211609
VERSION     WP_118211609.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116295
     Region          25..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrklmllmt clmigiglvn aqiskvtgnv tseedglpvv gasvlvkgtt vgtvtdidgn
       61 ftltnvpssa gtlvisfigm qsqevkikpn vnvvlksdae qleevvvtam gikrdrkalg
      121 yaaqdlkseq lsksgttsla naiqgkltgv evrqssgapg assqiiirga rsfdgnnqpl
      181 yvidgmpint sadfdtgssv tganyadrsi dinpedieti nvlkgqaasa lygirasngv
      241 ivittkrgsk nnlnkpsvti stnmsaqrvs rkferqtvya qgdkisaynp sssstwgpki
      301 tdlvndpvyg gntdnqytae fgkhegqyyn tqrakagldg wttpqiydnv gdflgtgfte
      361 ntnvnisqsl ngvnysfgln nsyqngiips tgmnrwgarg lvdwkineew ntgfsanyss
      421 tkitsapgan dgimnvvysa paeydlkgip thvpgditnq vlfrstsfvn pywwadhney
      481 lqhtnrvfgn ayleyqpkln wgdgftlkfr eqagldiwts nyadvkemgt tsallggeie
      541 nygsqhnvfn nlftinfdgr fgnedewgln iilgnefnde nirtwdyyas nfnfpgfpti
      601 gnatnlasan eytrrertvg ffgsvsaswk dqlyltvtgr ndyvstmprg srsffypsvs
      661 lgweftklpf legnsvinyg klrgsfaqvg qagtyynnfy ytpsygggfl aytpvsyplp
      721 sgvssyvpyy vvydenlkpq ntvnyeagid lhlfnsrikm eytyslqnvk dqifsvptdg
      781 aigyqymmtn agkmrthahe fsinaailqs kdydlnlgin ftrilnkvie lapgvesiml
      841 ggfvepqvra qagctypniy gaafkrdseg nmlllnglpq atgdsqnlgn cspdfttgit
      901 fggrykrlsl attwswqqgg kmyhgtnmtl nyfgatkesl pyhegtmvae gideatgekn
      961 tvevskqayy qeyynisesg iydtsfvklr dvtltyqlpk mgifdisvyg farniliwan
     1021 lpnfdpessq gnnnmsgyfe rfsvpntssf gggltikf
//
LOCUS       WP_118211459            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118211459
VERSION     WP_118211459.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116654
     Region          25..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkltlmla llfvwtgvaw sqgvtvkgvv tseedglpiv gasvlvkgtt qgtitdvdgn
       61 fmisgvkads ktlivsfvgm kskevaiknt pmhvvlksda evldevvvta lgmkrsektl
      121 gyaattmkse didagksgsv mgglsgkvag vqissagntg tsqkvlirgi sslnnnsply
      181 ivdgvpidns tfrgsptdds sttdfgnaan dinsedvesv tilkgasata lygsraangv
      241 vmittkkagv ekltvtydgs ftaskvlrvm qtqdlfgqgw gswnrsengs wgprldgtih
      301 ewgsdqletp mtkpfsyveh nlrnfyqtgf eknnnvsiry gndkvgvvas ygnlssngil
      361 pnngdqfsrn tfslrgymni dkfsldmtmn yvrkdisrsn dmymellqha vdvnysemkd
      421 ynderynldn yytfyatnpy ymidnyrsny qddrvygrie msyeimkglk atgrlggdfs
      481 nnrtnsqepk ttfsngsysq lggateslgy yseyrynrsq idatallnad ykvsdfsina
      541 vagwnlnqrs ygysggyvdg lavadwysly ntsssavsvt ykelrrliga faqaelgykd
      601 mmflnlsgrn dwsstlpagn nsffygganv sflitemlps lkehqvdflk vraalgqtgn
      661 danvykttsw yqianfkdin gyytsmpigg vmgmtsnntl pssslkpemt teyefglsgs
      721 ffgnrltvda syynrmtkdq iisaslapet aysyetknig kiqnqgvelm vnltpvrtkd
      781 wtwdlgftft knmsevkelw egtdeysytn wrgvyyvlkv gepvgmfrip aankvmdens
      841 pyygynivnn ngylsdsnte yeyvgsseak fnmgfnttlk wkgftlnasa dwrkggymls
      901 ntsyishfng nstqtvfner nsfiyphsvk vvngqyvenn ipvrademyn algnysyspe
      961 vrrhfiipkd yfrlrevsls ysfpksmlak tpfqqvslal vgrnlllftp kennyvdpev
     1021 snlgndllse fgettgtsst rnigvnvkvv f
//
LOCUS       WP_118214533            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118214533
VERSION     WP_118214533.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121044
     Region          62..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqtnkvfyt lvaiflscsi emagqvqkvi sgtvtelfgk taeplvgvnv nlvnnqnrsl
       61 gggitnlngq ynvkipegek dltivysyig mktkrikytg qtllnvtles esmavdevvv
      121 sarrlnrndl gisdkemvsa tqkvdmekli aaapvvsiee alqgqlggvd ivlggdpgsr
      181 sairirgtst lnassdpliv idgvpyptei sddfnfstat eedlgallni spndiasvev
      241 lkdasataiw gtqgangvlv iktkqgtvgk trfsfsskwt mkedpstipm lngkeytslm
      301 qesiwnsaky iglnnpgnky lnmlsdapai gdnpdwryyd eynqntnwld yvrqkalvsd
      361 nsfsmnggge katyrfslgy msdigttigt smnrlntsmv inyqfsnklk fgadfsysqt
      421 ntdanwtnti rsealskmpn kspftvndlt galtdeyfty hdpnfegsfn gksnynpvam
      481 aheainrtvq regkitfrad yeilpgfyyk gwasinmrai ktrrflpqvv tgveqvnkya
      541 nqsadaysdq lalqtenklm yiknwndkhn iianvlvrtg qyinsgynse vygnassdls
      601 dpvvgttisd mnssesetrn vsfvgvlnyt llnryvvhgs lnaegnsamg rnermgyfpa
      661 vglawnfqne pfmekardkw ldeakfrfsi gqsgrapsga svylgayvkg tdymnmsatk
      721 qarmqldnlk wetsteynyg ldasvlkgrl rftfdyyykt vkdllqknyk lpsttsfgsi
      781 syfnsgkmen kgwefrtdvv ifenkdwrin gyvnfsrnen kitelpanmv qenyspknga
      841 yaaraevgrp igsfygyryk gvyqntdaty ardaegnvmn dakgrpivmk nltatcqpgd
      901 amyedinhdg vinqydivyl gnanptltgg agltvkykqf sintffhgrf gqsvvntarm
      961 nnesmhgnan qstavlrrwk negditdipr alygegfnyl gsdrfvedts flrlkqltln
     1021 yafpksicnk lgitsltcfv tgynlftwss ytgqdpevnl psrptdlatd gattpvsrry
     1081 tfgfnlsf
//
LOCUS       WP_118216310            1195 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118216310
VERSION     WP_118216310.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1195)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1195)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1195)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1195
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1195
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134448
     Region          37..102
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          113..1191
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrkwylfit ciacicllsp qanaqttttk teitiefnne rlpsllkrle kasgykilft
       61 yddvkkytvs gsaknkgike ileiilndkp leyhiedqfi titsknskqp kifdvtgtvi
      121 sqddglplig atilikgskt gvltdidgrf hiekvasnsi lqfsyigmvp qevkaspkmd
      181 itlvsdvqtl sevvvtgmqk mdkrlftgaa tklsaenikl dgipeisral egraagvsvq
      241 nvsgtfgtap kirvrgatsi ygsskplwvv dgvimedvte vdadnlssgd avtlissaia
      301 glnaddiesf qilkdgsats iygaramagv ivvttkkgka gsskitytge ytmrlkpnyr
      361 hfnilnsqeq mgiykeldna gylnladmyr asnsgiygkm yhlindynak tdsyglmnte
      421 earnqylqea efrntnwfdl lfnnsisqnh aisfstgtek asyytslsim ndpgwtkkse
      481 vkrytanvna lyhiskalsl nlisnasyrk qkapgtlsss vdpvsgevkr dfdinpysya
      541 lntsrtldpd ayyvrnyapf nilheldnny idlnvtdlkf qgelkwkpih kielsalgay
      601 ktsmttqsht ikdysnqawa framddatmr qanpwlytdp enantlpvsv lpvggfyret
      661 kysmdsydfr gtasyndvyn enhifnffgg meinavnrqr twfngvgmqy emgmlpayey
      721 qyfkqgseen aqyytvertr qrevsffgta tysyqgkytl ngtlryegsn klgksrsarw
      781 lptwnlsaaw naheekfwqp lldyvsnmtl kasysltadr gpasasnsra iiqsynawrp
      841 ftsikesglr vvnienqelt yekkhelnig aeigflnnri nlavdwykrd nydligiint
      901 kgtggqltkl anvasmkshg ieftlstqni kkkdfswntd fifsntknev tdlqsnssvi
      961 emisgsgfal egypvrslfs mdfrrlnesg yptfinedgn ltvsninfqe rikkghliye
     1021 gptdptitgs fgnsfkyknf llnlfitysf gnvirldpvf hnqysdldam prefinrwtk
     1081 ggdekytdip viadkranqq dpylsyayna ynystariak gdfirmkeis ltynfpkkli
     1141 vkagvsdlsl klqatnafli ysdkklngqd peffntggva spvpqqftlt lrlgi
//
LOCUS       WP_118216705             925 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118216705
VERSION     WP_118216705.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..925
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102915
     Region          2..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkinifla gvlcslgvma qedtlivrqn devvemgrti tmdaremtga vsvttnlshk
       61 nsikpsnqlf gtlpglqvlq kagtvwenga tlyirgnssl nsnsplvlvd gfersidels
      121 seeiesvsvl kdavatslyg irgangvilv ktkrgsvgap kitfsyefnm aspkrlpkfa
      181 dgytyamaln eamendglap rysgteldaf knqtypgvyp nvdwldeslr dmsygdnvnf
      241 taqggsqfvr yytmlnfldn rgllkptsdn dgystqlkys rlnvrtnldi tvsptttvql
      301 nllgnftehn rpgestdkif nalfqvpsga fpvktdrgiw ggttnysnnp valisgrgya
      361 rsqtramyad vnmkqdlsai lpgwsagfkv gidntasywd nntkefgyes asvdfatgen
      421 iyttlrnegt lgfsksvgsv athfnlefyt nyikqwnkhs lnatllysmd kaktksqnsg
      481 rafmdivgsa hyaynnrylv dfslsgsass ildpddrwgi fpaigagwil seenfmkrdw
      541 lnllkvrasy gisgradygv nlfqniygsg nsyyfqnatn vpssssgmkf tqlgidglty
      601 ekshklnvgi dfrawnkltm tldafydhrt dilvssggsv sqifgmsvpq inngvvdnkg
      661 ieaslawddn ignfkyhlgg qftftrnkik nqneeyrpyd ylkrtgssmn qifgyevigi
      721 yksqdeidnr gveqllgdvr pgdlmfkdqn gdnkidaydq vplgynatcp eihysfdlgl
      781 eykgfgvyal fqgvgnyskv lntasvyrpi vnnntistyy wenrwsesnp ngtlprltys
      841 gsdnnyntns mwvsdasflk lrtlelyynf ptkllkktgf lagvkvfarg hdlfcldgid
      901 lrdpesigte hptmtqyafg fnlsf
//
LOCUS       WP_118216937            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118216937
VERSION     WP_118216937.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121641
     Region          27..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekhrflmwf allfigvvsg yaqqlaitgr vldskkepli gvtillkgsa ngtvtdidgn
       61 fsikalkget lvvsyigykt qeillssdkt tmtvelleds emldevvvig ygtmrkkdlt
      121 gsvtqvrpda laneapktvq dvlrgtagln vgfdksakgg gsmsirgqrs vysdgghndp
      181 liildgmmfy gelseinpnd iaqidvlkda ssaavygaka angvvivttk kgksekpvis
      241 fsanvgwatr adgrkvydad gylnyrrdfy ttdtygvnps tgkyeayqtg grpagyfdrp
      301 tdanlgkyrl tmdawrnqtt qdagmssdei warriglnas evtlanflsg ktfdwydhsf
      361 qtglnqdynv sisgmtervn yylslgylsn egivrgneyn airanmklda kvtdwfsvga
      421 nvnfqnrsdg diavdwyrqi tsnspftspy neagelvahp qgenaywkgy nfdfdrqyld
      481 lekgftvlnt iltakltlpf gitysfnaap rlqyfydryy rssehpdwqa etedrvnreq
      541 skrfdwslnn titwdytfak khhtiltlvq eaeerqswad riqarnilps ealgfhgtan
      601 gdknlsefrs tdnretacgy larlfysydd kymgtfsfrr dgysafgttn pyanflsgal
      661 awtftnedfw kwgdilesgk lrvsfgqngn rslansyial anlalgmysq gyinsttgtl
      721 ldmkylfvdr lpntglqwek ttswnvgldl sflrgrinas leyyimpttd mimnqslpdf
      781 tgfasittnl grvenrgfei slntrnietk nfewntsfsf srnkneikkl ygeyetivda
      841 agntitkekd dvdnkwfigh pisaiwdyev tgiwqvneve eaakygqkpg dpkvanhyta
      901 ddrknadgtt tavynnndkr flgettppih wsmrnsfily knwsfsfnly symghkslds
      961 nylnndnnys qitncqniyt kkywtvdnss ntyarlsaqg ptglaapsrv vdrsfirlen
     1021 vsvaynvpae llsrfkiqna kifatvrnva twskeweygd petgdiaprt yslginltf
//
LOCUS       WP_118216914             910 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118216914
VERSION     WP_118216914.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..910
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100843
     Region          38..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrirnlfcl slllvavglp avaqtklhvp lpdsittvgy atglrknlsg lveritenqm
       61 nkdqitnpld airgrvpglt ilkgsngpaa ldavrlrgtt slttgndpli ivdgvfgdls
      121 mltsiypadi esfvilkdas etaqygsrga sgvieittkk gvsgrtsvny ngsfgiassy
      181 ktvrmlngne frtlaqergi sildmgnntd fqkeieqtgl qhnhhiafsg gtntsnyrvs
      241 lalmnregvi vneklqnfts nmnmtqyvfd nflkcdlgmf gsvqkernlv nlhkvfysaa
      301 synptfpnhk npetgnwdgy ayasqlshpl awmdvkdkna tshistharl tfnlaeawkl
      361 tffgsytynv venaqylpva vwaqgqayrg dkkmesllgn lmlsykkewr khffdvlgla
      421 eiqkdkysgf yttvtnfsnd klgydnlqgg airpwdgtns yyedprlvsf mgrvnytydd
      481 ryiltvnarg dasskfgsnh kwgffpavsv awvvskekfm eklsfidnlk iragyglagn
      541 qngidsyttl nlmrpngiap vgstpvvtmd klrntnpdlk wevkqtfnag ievallgnrl
      601 lltanyynsk tkdmlylynv svppftyntl lanigsmrny gtelsigitp lktkdmelni
      661 nanltfqqnk llsldgnyqg ehisateyks lagldgagfh ggynhivyqi vgqplgafyl
      721 phctglvsdg nggytyqiad lngggvsled gedryvagqa vpktilgsni sfrykdfdis
      781 lqingafghk vyngtsltym nmnsfpdynv mkkapaqnik dqtatdywle dgdyinfdyv
      841 tlgwnvplkn trylqslrls ltvnnlatis gysgltpmin sssvnatlgi ddkrnyplyr
      901 iytiglsvnf
//
LOCUS       WP_118216952            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118216952
VERSION     WP_118216952.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120988
     Region          26..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkllfiml aylflwtsat laqvskvagv viseegnepv vgasilvkgf sqgvitnvng
       61 eftltnvpnd artliisfvg mktqevaikp qlriimsnds qmldevivtv aygtakkssl
      121 tgaissvnqd qiemrptssv tsalegttsg vqinstygap gsdpsirirg igtvngsstp
      181 lyvvdgvpfg gnisdinpad iesisvlkda asaalygnra sngvilistr kgtsnkisfd
      241 lkinqgvysr gikeykrtsp nqfmeaswqn lknarmsagd daataakyas enliseqlyl
      301 niynkadnal fdangnlvsd aqilpgyadd ldwysdairn gyrqeysfsg ntaneksnyy
      361 fsigyldekg yvtnsdfnri sartsmsftp kkwfkaginl sgthqnshat ngdsdagytn
      421 afmycrqiap iypvhlhnad gsyrldalnn kqydpgyykd degvtistrn qyvdrhviwe
      481 nelstdktir ntlqaiafad vkflndftft vkgdlnvrns eqtsydnati gdgkgnngrt
      541 krvtyrykny tfqqqlnwnh vygkhyidvl aahenysnny dyeyafktte tfagkpnlsn
      601 ftditsltgy etdyrtesyl grirynyaek ynlevsfrrd gssrfskqnr wgnfgsigan
      661 wiiseedfmq sltwinslkf ranygqvgnd agtgyygymg lyagsqnani gayylsqnea
      721 ldlkwetgea ygialegrlf nrwnisleyf dkrnkdllfd vylplsagat sttsaqatia
      781 knlgtisnkg feintdidiy kdkkwkvnfa tnatfvknki vklpeqnkdg iisgnykive
      841 gksryefflp tyvgvdqltg nslytlnled yfitlpdgsk lgnaestdis dnesltsing
      901 tyytnnttya lkefhgsalp kvygsftgtv syksltfsal ftyslggqty dgvyrslmtt
      961 gtspgnfhsd imnawkaapd gmsensadri widgipqins tmsannnsas srwlvssdyl
     1021 vvknltlsyr lpasfvkrld lqgisvsanc enlwtftarq gmnpqqsfgg sqynylvtpr
     1081 vfsvginikl
//
LOCUS       WP_118217141             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118217141
VERSION     WP_118217141.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110845
     Region          7..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvilaqktlt gcvvgedgvp lagatvleig tsngtvtdme gkfkltvadn amlrfsfmgy
       61 ktqeisvggk tflnitmved aveldkivvt algiekkehs lsyamsqikn eeltrvkmpn
      121 litsltgkat gvqinqvssg lgasakvsir girsvagenq plyvidgvpm lnssseqafs
      181 aiggtanagn rdggdgisnl nsediesisi lkgapaaaly gsqagngvil ittkkgksqg
      241 qrsisfstsl mfdkavslpe mqnrygvsei idswgerqnl pkndnlkdff stgmasitsv
      301 slshgneklq nyfsyanttg kgiidknrls khnltfrets tlfndrlrld gsvnlmrqvt
      361 knkptvggfy mnplvglyrf prgedltyyk dnfevydesr nlniqnwhts yddfeqnpyw
      421 ivnriqskev rlhaivslsa sfkvndwltv qtrgnvdcin dklrqkfyas tapalagtng
      481 ryiemdyqdi qfygdlmlmm kkqwgdfsvn galgtslndk ttnstrydsk taslyyanvf
      541 nlaniimngs aaldqkidar rqlqslfatv qvgykesayi dltarndwas tlshtkhekr
      601 gylypsigts lilsrlftlp ewvsyakvrg aysmvgndip pfmtyplshi taggeyland
      661 aapfkemepe mnysweagae arflnsrigf nltfyktntr nqffklptla gdkyayryvn
      721 agnilnrgwe ialdatpvlt kdfmwsttln fatnknkiva lheelkefvy gptsfsssya
      781 mklvkggsig diygkafvrd asgnivyete gsnaglpkie gdgntvkvgn snpkfqmgwn
      841 htlsykdisl yflvdcrygg kvlsqtqadm dlygvsevta qardegyvml eghridnvkg
      901 fykivggrag tteyymydat nirlrelsls yqlpaswmek skvlkkvqls fiarnlfffy
      961 kkapfdpdlv lstgndnqgi dvygmpttrs wgfslkcef
//
LOCUS       WP_118217159             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118217159
VERSION     WP_118217159.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109209
     Region          32..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvkrtklcl crslllmagl lfavasfaqd ltvkgkvtdt tgetviganv tvkgttngii
       61 tdidgnytls gvkpssvlvf sfigyktqei pcsgrkeinv vlsedaqald evvvvgygsl
      121 skkelsssiv qvdrskflqg smnnpmemlt gkvagltvnn taaanpnass slqirgatsi
      181 sasndplvvi dgvaggdirn laaqdiesmt vlkdaasaai ygtrgangvi littrkgvge
      241 agrvqvtyds wfgvnlaksg pdilsadefr rsrratdygy stdwydlllr dfsydnnqyl
      301 sidgstkngy ygasfnykka tgldlnssre efggrfvlnq rmmdgiveln gslnarrvne
      361 vwgndgmfdt alsmnptmpl ynedgtyfqp tsptgarnpv qelkeidnng qrvyllgtae
      421 vkvnlirsek qmlntslsys lhyndlkqhy ytpstagesy wngyngraev tyqkwytsrl
      481 ewlgnysldl gdhnfkamvg ynyeqttwer lqagnsdfnf ddilwnnlgs gsylakgkas
      541 mgtgkslakl igvfgrinyn wknlliasas iryegstkfg adqkwgafps lslawemanm
      601 gflkdhqniv qslkprvsyg vtgrsdfdcy qslatygshk naqlnvtdty lmdgawvtgy
      661 apsvnanskl gweksvsmni gvdfalwnrl rgsvewfdrq srdllynyta pqppyiysti
      721 lvnvgttvnr gievslegda fkgtpvewtt gvnysygttk ldklsnslyk asyvelyqkp
      781 gvgtseyffr veegskigqf ygyeyagven gdmmiytdeg ekvpvskadv kykrhigngt
      841 ptsylswsnt lryknfdlsl mfngafgfei fnmrrygmgl kgcgtdnvlr daygkdadit
      901 tgggvissff lekgdyfkld nltlgytitp kenkfirgmr vyltaknlft ltgysgndps
      961 avaingltpg vdtnsaypsa tqlsvglnir fk
//
LOCUS       WP_118218353            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118218353
VERSION     WP_118218353.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123510
     Region          25..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkhiillfi ilcigltkas aqhsitgkvl datnqepipf asvtiknvks gtttdnngnf
       61 tlkvnnndil ivsfmgyetk evnigtqkkv tillsessvl ldavvvtgfq nlkkttftgs
      121 svkikaddin lpgetdisrm legkaagvsi qnvsstfgsa pkirvrgats ingenkplwv
      181 vdgivledvv nvsndqlasg dpttllgssv agintndiet idvlkdaaat alygaramng
      241 vvvittkrgk egkprihysg nytvrtkpry sefnimnsad qmsvyaemer kglltsdivn
      301 nqssgiygim ynrintwdes kqqyllenty aarhnflmeh aaantdwfdl lftnsimneh
      361 tlsvssgsqk sksyislgfl ndpgwtvadk vnritmnfrn dyqlndkigf sfqtvgsvrm
      421 qnapgslsrs sdvvsgissr nfdinpfnya lntsralray dsngereyyt lnfapfnile
      481 eldnnyikln vidlkaqaef nwqifkglky nftgairyvr skqeheihen snmanayraa
      541 gnstirennp ylykdpsdps aepivvlpkg gfyntaenll lnydirnsvs fskiwnekhe
      601 fnallgqqik ysdrqtnsnt gygfqydmgg tvsmnylimk qmieqnfdyy sraltydrfa
      661 afyanvdyty drrysisgtv rydgsntman sssarwlptw nisgkwnign eafmkdfvwl
      721 dalalragvg ltasmpplsn atpifinsnt trpstdiesg ieiytlgnsd ltweksyqsn
      781 fgfdatflkg rldfsfdyfi rnsfdllsvi kvsgiggery kwansadlsa sgfditlsgk
      841 pivtkdfmws ssftmgyskn eiknsmqqpq vntlvgitgg nkngypvngl fsipfaglnp
      901 engvpmfyde ngtitsdinf qststdylky egptdpkytg gfnnsftwkg isldifftfq
      961 agnvirlnpv fnssyndsqa tpkeffnrwe frgdekhtni paiadkdlis dlsstypysa
     1021 ynysdirvak gdfirlksls vgytipqklf kswklfsdir lrvtgknlwl lysdkklngq
     1081 dpefvntggv aqpiqkqvif sldvsf
//
LOCUS       WP_118218375            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118218375
VERSION     WP_118218375.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117034
     Region          43..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmekckyll fcgtlalwma ggfqqvyaat epssqaiqqq snkvtgkvsd atgpiigasv
       61 vekgtangti tdldgnfsln vkagatlvvs yvgykseevk agrgplnitl kedakaldev
      121 vvtalgikre rkalgygide vkgealtkak etnlinsmag rvpglvvsqt aggpsgstrv
      181 ilrgstemtg nnqplyvvdg vpldntnfgs agtnggfdlg dgissinadd venmsvlkgp
      241 aasalygsra shgvilittk rankdkisve yngtltfdtq lakwdevqqi ygmgsngtys
      301 ydaisntnks wgpkadgsnm lkyfdgvkrp flivpdntsn ffrtgitatn saiigvnsgk
      361 tgirftytdm rnkdivpqth msrdifnlra ntsagkvdld fsvnytredv knrpalgdsk
      421 snigknlmtl attydqewlq tyqtadgeys nwngmdpynv npywdiyknf nkskkdlfrm
      481 ngkavwnidp hlklqatlga elnwftfddy kapttpgfea grlqnsafrn rmynfevlal
      541 ynnhwgdfdf natlggnvyk vnnqttvtta qdmkirdvps ltsfneisvv pgsyrkqins
      601 vygavnvgwk hmlyldatlr gdqsstlptg nnmymypsfs gsfvfseltk lgdllpygkv
      661 rmswaqvgsd tdpyqlglvy tkskyaypgy tigyidngti pnkdlkptkt nsvemglelk
      721 flknrigldf tyysqisknq imgmasswtt gynyrlinag kienkgieia lstrpiqtrd
      781 fswdinlnfs knsnkvkeld gesdmfelek aswldvqvaa kvgenfgsiv gpdfqrnekg
      841 dilidpqtgl pqydksnhvl gnaswdwtgg lltnftyknl slvavfdvkv gadlysmsar
      901 aayesgkspe tlagrdawyr seeerlaagi akgadnwkpt ggfvapgvid ngdgtyrpnd
      961 iyinpedywm svcrnapsmf iydnsyvkcr eltlsynvpk swlknvvsgl tvsfvarnpf
     1021 ivwknipnid pdsnynnttg mgleygslps rrsygfnvnv kf
//
LOCUS       WP_118218409            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118218409
VERSION     WP_118218409.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115251
     Region          45..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkiryirl iglifvlivg ssltfaqnks krksakkplv evisivtdek gsplknvsii
       61 cgegavvlyt dakgrfqtkv endatvmvea lgyedkvykl tgsnivpeki vlkkeplflt
      121 eeslvnradg gktykgnevg atsvlengqf gtfpdltltn mlqgkmlglq vrstvsglgn
      181 ntpdlfirgq hgmsentaiv iidgverpaa dlipeeieri ellkdataki lygaraangv
      241 lwvttrrgka nrriynatae agvvqmtrtp dflnsyqyan lynearandg ltpyynqkql
      301 egyknskgan dllypnvdly dqllnknany rkvsfdmtgg tdrvryalia gyvggsgfed
      361 vtytpqlhrl tlrgnldfnv tdfltisadv agrmemrkwg qldcgqvfta lsthrpneyp
      421 ltmspeetgl assdgiplfg asllrpmnay aetmyggytd erytrsqtni glkfdldmlt
      481 kglkagafls fdnydylqls lskvyptyai ktyrnfagee qimytqmkkt dvatsqsrks
      541 ttlqqtlgwn afaayentfn qkhdvsarlt ymyskttnqg vtqdiinany alrlnymydr
      601 ryaveadmal mgsnrfksgn kyffstaggl awilsnedfl kdneyvnflk lktsagilgy
      661 drstehllye rawsqdgsfr fgttnngata yystfvragn pnlkwekaae wnigveglfl
      721 nnrlytemny frekhtdiig svdasygdyt gnftyqdnmg svlnhgiegm ftwsdrindw
      781 aysvganfvw sknkvlkwnq vkhgeeyryt vgrstdammg lvaeglfgkd vvinghatqt
      841 fadyqegdia ykdlngdkii dgrdvkelgn sfprttlgid fnvsykgwgl ylqgyselgv
      901 htwatnayyw nngegkyskl aldryhpann ptgnyprltt tagennfrns sfwlkntsff
      961 rmknvelsyt fnqfspssvv kkmkvfarga nlfvlssvkd ldpellnagv tnypvtrtft
     1021 ggvsfvf
//
LOCUS       WP_118218437            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118218437
VERSION     WP_118218437.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116996
     Region          4..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrisssrtl rityvgmkpq dvpiksgtik vmmksdsevl qevvvtgmqk mdkrlftgat
       61 kqldadnvkl dglpdisrgl egraagvsvq nvsgtfgtap kirvrgatsi ygsskplwvv
      121 dgviledaid vgpddlssgd aetlissaia glnsddiesf qilkdgsats iygaramagv
      181 ivvttkkgra gvskisytge fttraipsyk efnimnsqeq mgiykemeqk gwlnsadlfr
      241 tkdtgvygrm yrlideynns ngqrgllntp esrnaylrea emrntdwfdv lftnaisqnh
      301 svsitagtek ssfyaslsam ldpgwykqsk vkrytanvnt tynlyknlsi nlisnasyrq
      361 qnapgtmsss ldiasgkmsr gfdinpysya lntsrtldps adyisnyapf nilheldnny
      421 ieinmvdvkf qgelkwkviq glelsalgav ryqtssqehn vlddanqava yrtgmddati
      481 reqngllykd pdnpyalpit llpeggiyqr qdrrmlgldf rgtlswnhlf aekhitnffa
      541 gmevnslkka yssfqgwgmq ysmgeipsyv yqffkngies gsryyslghs etrsiasfln
      601 atysydgryt lngtfryegt nrmgrsrssr wlptwnlsga wnvheeaffk vlqptlsnlt
      661 lkasysltad rgpaevtnsq aiirsfspyr pftdiqetgl yiediensel tyekkhelni
      721 gidlgllenr infsadwyqr nnydligvvp tqgvggsink yanvatmksh gveftlstrn
      781 irtkdfswnt dfifsyakne vtqlkgltsm melvsgngfa regypvrglf sipfagldad
      841 gipqylidgk ltttgvnfqe rekldylkye gptdptitgs fgnvftykgf klnvfmtysf
      901 gnvvrldpvf nykysdltam prefknrwtv sgdeaktnip viisdpqyqa ntslylayna
      961 ynysteriak gdfirmkeis lmyefpkswi apakisnlsl klqatnlfli yadkklngqd
     1021 pefvntggva spvprqftlt lrlgl
//
LOCUS       WP_118218975            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118218975
VERSION     WP_118218975.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117616
     Region          41..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mynivikrnd wfyfalltmc mflgiltpnv saqemskyad itgkvvdqyg npvsdvtvtm
       61 knsdfrvitg vdgvfkfqlk kgdilrlshp gflhkevrvn klkntervfk vtldeqfvkd
      121 rqtfngpyek kdkdsflgss stvytdklss mmgttilpal agrlaglnit qyrgarvhqt
      181 sanstsgiig nipvfgegfy sdntefnvgs rgiapvvvid giqrelysid pdaiesvsiq
      241 kdalssmflg mrssrgalvi ttkepikqgf qlsftgrfgv qstlktpnpl sahqyaylln
      301 ealqndgkep fytyddfnkf rtqsspythp nvnwfdeiln ktsttqsynl nvaggnrfaq
      361 yfvsvgymge kglfsnptes dahdtnlsfs rymisskvni nitddftakv tllgrvedgn
      421 qpgvnysnll ngiyttpnna ypvknpngtw ggnvtfdnnl msqainsgyi mdtardmagg
      481 inlkydfnkl vkglsarlvg nisiqnrsyt erskrapvys ysldkggnea ytqygtsdsq
      541 inkfysvtsy qqmygqfavd ynrhfgphgv katlmgdtrn tlinydlpql psniiadvay
      601 dyakkyfvqa alsesyynry apgkrwgtfy afglgwdisn enfmesadwl nqlkirgvfg
      661 ktgngidnsg yymyqqtfsh ignagyplgt qmsylgnvtt enaplanpfl twekaykwnl
      721 gidlamfnnr lkftadyynd kyfdllqnrg ksieligqsy pmenigkvrr fggdlsityq
      781 drindfnyyv sanwsceqsk llymdeqevp eeylrqtgrp agaiyglvad gffttreeie
      841 rspviegfen iqpgdikykd lnddkvinef drtviggdkp ysyfgidlgf ewrglefsmf
      901 wqgaynrdly lqdwtllegf qtngryygqa yenmlgrwtp etaqtatfpr ltaggngynr
      961 gngwnssfwl rsgnfirlkn islgyslpds fcnnylgglr lkifvngqnl ftksacelvd
     1021 pevgftsypl qrcistgini rf
//
LOCUS       WP_118219950             937 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118219950
VERSION     WP_118219950.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..937
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104035
     Region          2..935
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklifsqait ltnaqplkvt lgedtqvlde vvvtalgikr sekaltynvq qvkgdelttv
       61 kstnfmgala gkaagvqins sasgpgggvk vvmrgaksit qnnnalyvid gipmynrass
      121 ggdgamatqp ssesiadinp ddiesmsllt gpsaaalygy egangvvlit tkkgradktt
      181 vtysnnttfs dpmmmpkfqn tygnmtgemm swgletdkry dpanffntgs nvsnalslst
      241 gndksqsyis vattnatgim pnndydrynf sfrnttnfln nkfildtsan yiiqndknmv
      301 sqgqyfnplt slylfprged fsdvavyery ddlsgvntqy wpygdlggvs sqnpywimnr
      361 mnrendrrry klaaslqyni ieglnvqgrv sidnteskyt ekfhagtvgn fagpkgryke
      421 enrldrqvya dvlvnfnktf nefnvtanlg asikdlrmel tslhgdlnnv tnhftienlt
      481 rsgyykvnad glkrqtqsvf anaeigwrsf lylsltgrad wdsslalser gnkpffypsi
      541 glssilsevi dlpewfsflk arfsftsvgn aydpyltkvr yvyddqldqy kaeslypnsd
      601 lkpeitksye aglnmrffkn tlnfdityyn sdtrnqtfaa plpassgyta vniqagsvqn
      661 qgiemalgyk newrdfgwss nftftynknk ikrladgvtn ritgepiemp yvdkarlggs
      721 tspvvrlteg gsmgdlyinr dfkrdnngyi yldaktglps mveteykkig sllpkvnlgw
      781 rnsftykglr lnillsgrfg glvvsntqaf ldrcgvseys aqlrqaggvt innrnvsakd
      841 ylgivaagtg egdhyvyeat nirlqevsle ytlpkkwlyn iadvtlglig nnlgmiycka
      901 pfdpelvass tstfytgvdy fmqpslrnmg fsikvqf
//
LOCUS       WP_118220036             993 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118220036
VERSION     WP_118220036.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111392
     Region          26..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkllftigl lfissvslva qemmngivkd gsgkplsgvk vskvgeyrnn nvtdedglfs
       61 lllkkgdyie lnyadvatkr ikitgdtlnl vfdikkdavv dlgflkrted tqtqsvtaiy
      121 adlleknats pdrvnnalfg lisglhltqt vgwdanagmn irgrgglgsg aplvlvdgfe
      181 rgltnmtiee iesvqvlkdg aatalmgarg angvilvntk rgiynsfdvd vnyrhgfdfp
      241 vnrpemaday tyamaqneal yydglplqyt krdlerfkdg tnpnyypnvn wyeegtrnfs
      301 ennqfnvmmr gggkrvryma lldyknkfgl lnedythysd rynsqirtye lglrmnldvd
      361 itsstqmkfg lygiigedkr pntaintifq nfykvpaaaf pvktlndnwg sntlfkmnpi
      421 aaiadvgyvq enrrmletdm ritqdfsmfl kglsaevava ydntatfqdi gsktykyevg
      481 ylseeglpvs etygtdskvq itksvlsaql irasveakln ydytsgkhql sasavyrqdm
      541 keplennasy yrqnimgfvg ynygnrymvd vvgnyygtsv llkgdkfrfy pavsagwnla
      601 nedflkgasn ldllklrasw grsavdeldy glgnyfwtgg tgypfgdgmt vvnglkeqrl
      661 pvyglnleta dkynvgvdlr lwknftatae vyydhrtnil vannnvsgil gidppkacig
      721 evksrgvels lgwsgqhkdf nyfvnanwal ndseivengq ayqpydylyt rghkvgqlfg
      781 leavgyfrde ediakspeqt fsvvrpgdvk ykdqngdgri dsedriaigk sttvpemvfg
      841 lnlgfeykgf gidmvfngvs gltkqlnvan vhqplrngnt niatwylkdk irwteamkdv
      901 anvprlstls nennyqtstq wiedgsflkl rnlnvyynlp qkwvkkikld klqiyakaqn
      961 vfsidkidyf ncedltlgyp dlfsvclgln inf
//
LOCUS       WP_118220194            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118220194
VERSION     WP_118220194.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123813
     Region          25..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkylcili clfanalafa saanrtitgv visgednepl igasvyvnad dlkkagasqt
       61 slgtitdmdg kfsisipekv trlhcsyigf eeqdivlqag kdtyrivlqa sahtlgdvvv
      121 tgyqelerrk ltaaiakvdv tdgmvgaaks idqalagqia gvavtttsga pgaparirir
      181 gtaslngtqd plwvldgipl egtdiaklst etdndivnmk qssiaglspn diesitilkd
      241 aaataiygar aangvivits krgrtgkpvi nfntrltytp nldtsrlnll nseqkvnlel
      301 elmkepddvf sahpylhkgg vasilrqhnl fetyqqqgwn gltteaqnai nrlktintdw
      361 ndilfrdaft qeynfsisgg sekvtyynsl gysqengnvp gvsmsrfnlt nktsyqvnri
      421 lkigtslfan rrkskdfitd kygysnpiyy srtanpyqei ydaegnyvyd ydivsnsdne
      481 pdpergfnll edrantsket ittainaifn adlrfndhwk ltsqvglqwe qsgveqyiga
      541 ntfsmrdmrk dsksgntyri peggmhkvsn attsqitwkv qgewsqtfkn ihevqimggs
      601 eirknwyetl asnaygydpk tlttkplili enddakkypl htetyaenaf asfyangsyt
      661 lmqrytlgas vridgsdlfg vdkkyrflpi ysasglwrls nesflqpakq wmdnlalrls
      721 yglqgnidkn tspylvgsyg nqtilpnnpd etsisigsap ndklrwekta synigvdfsa
      781 lksainlsvd yyyrkgtdli gyknlpleng fltqtinwas lenkgleinl qtrnittknf
      841 swyttfnfay nnnkvlkdyv kensptpgle gypvgaifai kskvdpetgr iliypkgsne
      901 aitveelfkm edltggmggf ydynadadfq qslyeyvgtn dapytgglln tlsyrnweln
      961 fnfsfyfgah vrtnpsyniv dfdpghnvnq dilnrwtpen hsnqlpalls rnnypadyal
     1021 fggipaiyrn ldmwvkklny vrlqnirlay tlpqewlrki niggatvave grnllvfgss
     1081 yknymdpesm snlystpvak svtfnlslnf
//
LOCUS       WP_118220546            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118220546
VERSION     WP_118220546.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121792
     Region          24..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrlsvvfl lligtltyal aaerqvegvv issednlpli gasvyvtadd lkkngnnqst
       61 igvitdidgk fsisipdgit rfycsyvgyd vveiklipgk kqyditlqps ahmldavvvt
      121 gyqtverrkl taavskidis dqmmgatksi dqalagqiag lsvsnisgtp gapakirirg
      181 tsslngtqdp lwvldgiple gtnipnmevl kdidnigqta iaglnpadid nitvlkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs skltyspkln idrlnllnse ekvgleldll
      301 esgypyretk gevyriisgl gelknfkdgg wnalssnaqg ainrlkatnt dwsdilfrda
      361 ftqeynlsls ggsekatyyt sfgymkengn ipnvsaerln lvmktsykvn silkvgasmf
      421 anrrknstyl pddrgltnpi yysrlanpyf tpydangnyn ydvdveddtd mdfglnlfee
      481 rkntsnqtti nglssifdae lrfddrfkit tqlglqldkt siekiaeees yvmrtekknh
      541 rnngvtylpe ggfhkanens lsqltwkamg eyrdtyndih efevmvgtei rktweeklys
      601 agygfdrktl ttkpiifpee sqafklheka hvenayvsaf stlsysllnr ytlggsirfd
      661 gsdlfgvdkk yrylplysvs glwrisqepf manakwidnl vvrasyglqg nidkntspyl
      721 lgnyrienil pggsedmidv sgapnkklrw ekthsvnagf dfavlnqain lsvdyyyrkg
      781 vdligtqmlp letgfemltv nwasmqnqgv evalstrnih tknfmwttnf nfaynnnkil
      841 kealredale pgregypvga lfalktagld eegypmfegk dgkavsamef fklqewgfga
      901 tdltarerre lytyvgtadc pytggfnntf tykafelgvn fsfdfggkvr sqptysivdf
      961 dkgrntnrdi lnrwtpente tifpvllsqn erldeymwys nqneiyrnld iwirdlnyvr
     1021 lqnirlgytl ptnfsrklgm tsatiaiegr nllvfgssyk nyldpetmsn ayatpapksv
     1081 tlslnlnf
//
LOCUS       WP_118220594             925 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118220594
VERSION     WP_118220594.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..925
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102858
     Region          2..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkinifla gvlcslgvma qedtltvrqn nevvemgrti tmdaremtga vsvttnlshk
       61 nsikpsnqlf gtlpglqvlq kagtvwenga tlyirgngsl nsnsplvlvd gfersidels
      121 seeiesvsvl kdavstslyg irgangvilv ktkrgsvgap kitfsyefnm aspkrlpkfa
      181 dgytyamaln eamendglap rysgteldaf knqtypgvyp nvdwldeslr dmsygdnvnf
      241 taqggsqfvr yytmlnfldn rgllkptsdn dgystqlkys rlnvrtnldi tvsptttvql
      301 nllgnftehn rpgentgnif nalfqvpsga fpvktdrgiw ggttnysnnp valisgrgya
      361 rsqtramyad vnmkqdlsai lpgwsagfkv gidntasywd nntkefgyes asvdfatgen
      421 iyttlrnegt lgfsksvgsv athfnlefyt nyikqwnkhs lnatllysmd kaktksqnsg
      481 rafmdivgsa hytynnrylv dfslsgsass ildpddrwgi fpaigagwil seenfmkrdw
      541 lnllkvrasy gisgradygv nlfqniygsg nsyyfqnatn vpssssgmkf tqlgidglty
      601 ekshklnvgi dfrawnkltm tldafydhrt dilvssggsv sqifgmsvpq inngvvdnkg
      661 ieaslawddn ignfkyhlgg qftftrnkik nqneeyrpyd ylkrtggsmn qifgyevigi
      721 yksqdeidnr gveqllgdvr pgdlmfkdqn gdnkidgydq vslgynatcp eiyysfdlgl
      781 eykgfgvyal fqgvgnyskv lntasiyrpi vnnntistyy wenrwsesnp ngtlprltys
      841 gsdnnyntns mwvsdasflk lrtlelyynf ptkllkktgf lagvkvfarg hdlfcldgid
      901 lrdpesigte hptmtqyafg fnlsf
//
LOCUS       WP_118220827             919 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118220827
VERSION     WP_118220827.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..919
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103254
     Region          36..918
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrknayivg iallcsisai adgdtktksk inerqtsavs tvtseelekn stpnpyntly
       61 gllpglsvlq qtgwtdnakl ivrgrgslng aepliivdgf prpleylnva eiesvsvlkd
      121 gaatavwgpr gangvivitt krgkeakmsi dvnyrfgmgl pinqpkfvda ytyaqaknea
      181 llldglqpqy tnahleafrn gsnrdlyadt dwlneglrnq synnqadftf qgggkrlryf
      241 tmlsykndyg ilnsaytdys drynaqmkky slnfrmnldv eltsttmakl tmlgmlyerk
      301 rpntaedkif tglyktpsaa fpvrtsngyw gsntvyndnp iariadvgyy kenqrmlqad
      361 lriiqnlsvi tkglsaemav sydnsatyqe tgsknflyei nssvlnpetg eyqvnterfg
      421 ddkaltvdnk dladqyiran leakvaydrt fgkhtfiasg lyrqesltpt gkaqsryrqy
      481 itatagysyd nrylldvvvn hsgtsvlpkg drfrtypavs agwvlsnesf mesvsfidll
      541 klraswgrsg ydgfdyyldr qywvggagfv tndaggtlsg lkegrlaisd msceisdkyn
      601 vgldtrlfkn ltftadyfmd rrrnilvdga nmvssalgie vaktfmgavd tkgfelalnw
      661 ngekkdfsyh aganlsyvkt kivengegyk pysylsakgy pvgqifglea igyfrdaedi
      721 aksptqtfsd vrpgdikykd qnndqkiddn drvaighsst ipklyyginl gfeykgfgvd
      781 mlfqgvggys kmlnvanvyw plrnntnist wymddnirwt eetkdianlp rlttlntsnn
      841 fqnstqwlvn gsylklrnln vyynlpqqwi kkakmeacqv fvrannvfsl dhvkysnced
      901 lsvnypdmls vyfgfnvkf
//
LOCUS       WP_118221203             938 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118221203
VERSION     WP_118221203.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..938
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105112
     Region          51..937
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkyiivls lfaglclptt aqesneeqtd kfvgqtidvg aerlltreea tgsvsvisse
       61 ttdrrsakni gnsiigqgng lislqssgry advnptfyir glqtlngkns plvmidgiqr
      121 divsiapeev esvivlkdaa avalygykgi ngainivtkr gkyntrsvkv tydhlftsla
      181 nkpkfvdayt yglavneari ndgmtgrysn qelnalrdgt mpylypnvnw vdetfrdnam
      241 tnkyniefrg ggekfryytm ldlisnkgfv kepganegys tqdkyvkgnl rmnmdidltk
      301 ttdlqvnllg vlqetsrpga qadlwdlvyt vpsaafpird kngvwggsdt wagtqnpvaq
      361 svgaayyknh trslfadmkl tqdlsgltkg lnafvrisyd nianiyedhs keyvysvnap
      421 twadgasept vkseiygkds emgteaktne fdrllhfdvg fnyqrtfgdh siysqlkwdy
      481 edndpnginn tvnrqnitww shygylnryf vdlalvesgs srlapgtkwa fsptlsaawv
      541 iskekfmenv kwvnflklra sagiinvdnl pgdevwsyya qqygtsggvy pfdsgwnssf
      601 grsylervat tnpnhekayk ynvgvdaklf gcldvtldlw kehrtniwvt segkyseifg
      661 mdppyenagi vdskgievgl dyskklgqve fnvggnfsln knkikemlee prqyanlvqt
      721 gnpyeqlygl eaigffkdea diaasptqnf stvkpgdiky rdvngdniid andkvaigys
      781 ttcpeiyysl hlgaewkgig fyamfqgtgn ysavldtksm ywplinntni sqyaydnrwt
      841 pqnqnakfpr lssqsnanny qtstlwladr sflklrnlev yyklpaswlk ktrivnaakl
      901 yvrgidlfsf dhidendpea yginpmtksv alglsvtf
//
LOCUS       WP_118221573             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118221573
VERSION     WP_118221573.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109209
     Region          32..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvkrtklcl crslllmtgl lfavasfaqd ltvkgkvtdt tgetviganv tvkgttngii
       61 tdidgnytls gvkpssvlvf sfigyktqei pcsgrkeinv vlsedaqald evvvvgygsl
      121 skkelsssiv qvdrskflqg smnnpmemlt gkvagltvnn taaanpnass slqirgatsi
      181 sasndplvvi dgvaggdirn laaqdiesmt vlkdaasaai ygtrgangvi littrkgage
      241 agraqvtyds wfgvnlaksg peilsadefr rsrratdygy stdwydlllr dfsydnnqyl
      301 sidgstkngy ygasfnykka tgldlnssre efggrfvlnq rmmdgiveln gslnarrvne
      361 vwgndgmfdt alsmnptmpl ynedgtyfqp tsptgarnpv qelkeidnng qrvyllgtae
      421 vkvnlirsek qmlntslsys lhyndlkqhy ytpstagesy wngyngraev tyqkwytsrl
      481 ewlgnysldl gdhnfkamvg ynyeqttwer lqagnsdfnf ddilwnnlgs gsylakgkas
      541 mgtgkslakl igvfgrinyn wknlliasas iryegstkfg adqkwgafps lslawemanm
      601 gflkdhqniv qslkprvsyg vtgrsdfdcy qslatygshk naqlnvtdty lmdgawvtgy
      661 apsvnanskl gweksvsmni gvdfalwnrl rgsvewfdrq srdllynyta pqppyiysti
      721 lvnvgttvnr gievslegda fkgtpvewtt ginysygttk ldklsnslyk asyvelyqkp
      781 gvgtseyffr veegskigqf ygyeyagven gdmmiytdeg ekvpvskadv kykrylgngt
      841 ptsylswsnt iryknfdlsl mfngafgfei fnmrrygmgl kgcgtdnvlr daygkdadit
      901 tgggvissff lekgdyfkld nltlgytitp kenkfikgmr vyltaknlft ltgysgndps
      961 avaingltpg vdtnsaypsa tqlsvglnir fk
//
LOCUS       WP_118221358             925 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118221358
VERSION     WP_118221358.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..925
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102542
     Region          46..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mninrmlmla ttvvsltana qvklsdknan aydlgygvei snflstasat titgeelqqt
       61 sttnlaqaly grlpgltals qggfsgdenk gasfnirgyh tlndksilil vdgyerpidr
      121 lsveevesvt ilkdaaatal lghegingai lvktkrgveg kthvkvnysh kfqfdpefad
      181 mvdgygyana fnrarhndgl saayteqeln lfkdgsdpyf ypnvnwrdlt fknsaeedha
      241 yvsvyggtnk vkyythidyt dvrgafkdtk qpdyntqlrq skaniranld fnitnttlms
      301 vnlfgmfqet krpsdisadd ataaiynlpa safpyktstg iwggneaygd anpiakiqes
      361 gfykthqrql wvdaklsqkl dfllnglnvf vsagyanssi yaenshkahq ygyerytgti
      421 gdknnvalnt fgnketnltf nnwnagqwwk akasvginyk rsffdndhfn atvvydnsgv
      481 stdgrgntfy rqnimgvfhy dfqnryvadl vlagngasrt ypskwafspt lslgwiyadn
      541 nddllnygkl rasagiqhtd ymptygmwlp twdvshgyvi ignnygdkwg aslgsfpttd
      601 fsqetstsfn lgtdlrlana ldisvdafyq lrshimlsas senssvagiq ssyndvgevk
      661 sygfevnaky vkkiapdlnl nlganlswar nevskyigip typlsdpvgh rvneawglks
      721 agffkdqadi nssyrqeyst vspgdikyqd lngdqvinef dvtslngatd ipelnyafnv
      781 gveykgfgln awfqgtgnym kylpsaiwgg madngnlsvd yynncwdvag snalyprltt
      841 lnnsnnsqks nvwykpvhfl kmrnievyyk vpatvlskls ltaakvfiqg enllsfdnid
      901 amdaevllta ypmfkgvnig vtltf
//
LOCUS       WP_118221868            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118221868
VERSION     WP_118221868.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116111
     Region          47..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrfkeismc iaamlivpai sinaspnnia gkptspatev mqqqtqitvk grvtdsadep
       61 lagasvqiqg tgqgvitnad gnytiaakqg ailkfsyigc kpqsvkvtka qinvqmeeda
      121 nmlnevvvte fglkrvqrgi gssvqkvtad eiaesgrdnf italqgrvsg mnvvsssgap
      181 gastqvtlrs itslsgsnqp lyvvdgipmn nssfsassgm avddvydsrt ldfssrgndf
      241 npedienitv lkgaaaaaly gsnasngaii ittkkgtagk gkvsysnrfr wdtsyglpdp
      301 qtkysngnyg vtnyfntarf gglypegtkl ynnldqilqt gftqvhnvsv etgtekltmr
      361 aaasftdqtg tikntdyqrs nfslsgkadi tkwmrfessm qyastqnnkm pkgtsgplyy
      421 alrwplvddm snyldpdgvh mrypypyvdg dmynplflmn knkyydesdr iigniagiiq
      481 pnshiflraq ygwdigtqtf etsehplwak nnydiqpslg gvynlakenf sdlsmnilag
      541 wndkffdgkl avtaqvgyhq venkitrlss ygknyivwdm asinnvdqkt iiakkrstir
      601 riqaisaqae fgwdnmafit lrgrndwast lptdnrsyfy paleasfvlt elpifkgnev
      661 inylklrgav aqvgkdtspl sinpelepte lrgggykygf tgpnsklkpe mttsyeigae
      721 grflndriva dftyfrtrct dqivrgfrls yatgfvlntr nlgdfktwgw eghidgdiih
      781 nyngwrwnvg vnlshtgskt islpmaefyd tytngntagi rlgtmvgdpv tsihgldfer
      841 ndkgevlidp ttgaprvsse wthigdrepk lrfgfstevt fkrqwrlsam fsgkfkstvi
      901 ngtgrylaqn gidwdsvkkr eqgsviipgv lkdgnensen ptpnniaity gnyggtiyag
      961 sardwvqpni nylrmselrl sytftekflk katngllsya qiyvsgsdlf titnynglda
     1021 vgntmsasag gvggegydtw gipsprgvtc glsiqf
//
LOCUS       WP_118222249             910 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118222249
VERSION     WP_118222249.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..910
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100892
     Region          24..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrirnlfcl slllvavglp avaqtklhvt lpdsittvgy atglrknlsg lveritenqm
       61 nkdqitnpld airgrvpglt ilkgsngpaa ldavrlrgtt slttgndpli ivdgvfgdls
      121 mltsiypadi esfvilkdas etaqygsrga sgvieittkk gvsgrtsvny ngsfgiassy
      181 ktvrmlngne fralaqergi sildmgnntd fqkeieqtgl qhnhhiafsg gtntsnyrvs
      241 lalmnregvi vneklqnfts nmnmtqyvfd nflkcdlgmf gsvqkernlv nlhkifysaa
      301 synptfpnhk npetgnwdgy ayasqlshpl awmdvkdkna tshistharl tfnlaeawkl
      361 tffgsytynv venaqylpva vwaqgqayrg dkkmesllgn lmlsykkewr khffdvlgla
      421 eiqkdkysgf yttvtnfsnn klgynnlqgg airpwdgtns yyedprlvsf mgrvnytydd
      481 ryiltvnarg dasskfgsnh kwgffpavsv awvvskekfm eklsfidnlk iragyglagn
      541 qngidsyttl nlmrpngiap vgstpvvtmd klrntnpdlk wevkqtfnag ievallgnrl
      601 lltanyynsk tkdmlylynv svppftyntl lanigsmrny gtelsigitp lktkdmelni
      661 nanltfqqnk llsldgnyqg ehisateyks lagldgagfh ggynhivyqi vgqplgvfyl
      721 phctglvsdg nggytyqiad lngggvsled gedryvagqa vpktilgsni sfrykdfdis
      781 lqingafghk vyngtsltym nmnsfpdynv mkkapaqnik dqtatdywle dgdyinfdyv
      841 tlgwnvplkn trylqsfrls ltvnnlatis gysgltpmin sssvnatlgi ddkrnyplyr
      901 iytiglsvnf
//
LOCUS       WP_118222662             954 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118222662
VERSION     WP_118222662.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..954
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106035
     Region          42..951
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyiqakfil camlavspmf vsaqaidwne tdslvsekdp mvqvafrkva qkdllggvsv
       61 vnveeltkkn yntysldnmq gyvggwngns lwgmdgdnag ylvlvdgvpr dannvmpsei
      121 aqisflkgaq avvlygskaa kgavvittkr gnveglnvsv rantgfhvak afpeylgsae
      181 ymtlyneall nddpsanlry taeqiynhgs gvnpyrypnm nyyssdyvkk aynrsevtae
      241 itgggkrarf ysnvsyysng dfldfgeakn nrtdrfnvrg nvdvninsfi nayinanatf
      301 ydsksakgdy wnvastarpn fpenaaplip ldmidpnatd awellgttsn iiggkyflsg
      361 tranatnafa dsyaagsskw tsrqfqfdag vdvnlnkvlk glsfnamfav dyatsystsf
      421 dnkyavfvpt wsnyggkdvi valskegnde rpgtqnvggs tdkqtiaftg qfnyqntfnk
      481 nhnvsamlia ngyqqtvsaq yhrisnanla lqagynyqqr yyadfsaali hsaklakghr
      541 qalspsvtlg wrlsnenflk dspvvddlll svsgsilnqd idlvmgdnef ylyesvwtqn
      601 dgyawydgpa gkytistrgq nsdlsfikrk efsanlktsl wnrlitadas ffinsmegyl
      661 inqptfypsh lntgypaasf mavlnynnnk rvgfdfnina nkrfgdvdls lgvagtyydt
      721 kitkrdeiyd dtyryregrs vdgvwglqsa glfqskeeie sspeqklgst vqpgdikyvd
      781 qngdnviddk devflgkggw ygapftfgin ftakwksltf fvlgtgnfga yglknssyyw
      841 vdgddkysai vrnrwtpeta atatyprlsa rsssnnfras dywlyktdrf dlakvqityd
      901 lpkrilrntf inelsayvsg anlltisker khmemnvgsa pqsrfynigv kavf
//
LOCUS       WP_118223268            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118223268
VERSION     WP_118223268.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122363
     Region          23..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskkilflff cvfalaahsq nvvikgsvtd vnkepllgvn ikvkgtstgt itdidgnfsi
       61 ngpkgatlvi syigmvtqev eykgqplnvv lkddsqalee vvvvgygsmr kkdltgsvvq
      121 vrpdkiandn pktvqdvlrg tpgltvgyge sdagakgggs mkirgqrsvy tdgghndpll
      181 ildgmffyge lseinpddia qidvlkdasa aavygaraan gviiistkkg kqgkptinft
      241 asigltqkaa yrdrwqspea ylqhyvdwke kntygvnaet geyaaysrpg neytskpgyf
      301 rnpnnlddvs leawrgyttn degesdlsiw arrlgfrpnt almdnllsgk vmdwqdkafr
      361 lgfnqdynas isgagekidy ymslgylrne gafvddtyra irgnfklnak vtdwfeigan
      421 infqdrsdge igmnkggfme nspyavfkdd egnyvqdplm fqydrnnltn wyyekqflel
      481 qkgyttfnti fnaklklpfg itytfnaapr lqyfhdryfm saerpnskpt drgvnreqak
      541 rfdwslnnti twdkmfadkh hvivtlaqea eerqywsdri earnilpsdv lgfhntqngd
      601 ksassfksdd shqtadglmg rvfysyddry matftmrrdg ysafgssnpy ayfpsgglaw
      661 tfsnekffqp ythimstgkl rvsfgkngnr slanpyeala nlypgggkmq gyitssgdly
      721 lmrylmaqrm enpglqwekt qswnfaldfg flndritgtl eyyrmstkdm imgqrlpnft
      781 gfesittnlg qvdnngfeia lntlnidnkn fqwsttfsls ynknrikhly gdyedildas
      841 gnvigkkead yvgngwfidr pisaiwdykv tgiwqkdeve eakkygqvpg dpkvwnnpan
      901 deydadgnlk kviynnddkv fqgqtaapvt walrndftlw kdltlsiniy srmghksleg
      961 mylnndddgg gmtyrlvnke akeywtvdnp snkyarieaq gpegargarr lynrsfvrle
     1021 nisigytlpr qwtkrvdier akvyatvrna avwgskdwey ygdpetgnya sriwtlglnl
     1081 tf
//
LOCUS       WP_118223355             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118223355
VERSION     WP_118223355.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109985
     Region          38..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpkfnqkrii sgtmrlitmv cmlcmcqfit aqtknfqgvv kdskgntlpg vtiletgttn
       61 gvstdvdghf eikmnpgntl tvsyigyvtr tiqtnantts lniileedvf llddvvvvgy
      121 gsmkkgevts aitsvkkdnf lagmvkspeq llqgkvaglq lsnytgdpvl glemtirgvn
      181 slsgntspli vidgipggsm taissedies idvlkdgsaa aiygtrgtng vivittnrak
      241 atkmsleyna svsfetiskh admltandyr rlkddpdfpg iqdegtttdw vdaisrtavs
      301 qnhflslkgg naqsnyvasi dyrkregvin ktdresitak iglnhnmfnd klrfqlnind
      361 syvtqqrawy aaylnallen ptrpiydeng nyteykvnlk pynpvamine eydkegynql
      421 mmsgkmtisp ieglnlsvmg alqrfdrmen ksntfkhmst vvngdygnvw nwadntlqkt
      481 lelvgdytks fgvhnmgvma gysyqddddk giyqwakdfp tdmfgpwnig smndmkdnka
      541 amtsyrnthk lisffgrvty nydekymfma slrregssrf gdnhkwgwfp avsagwrlsk
      601 enflrdvkwl ddlkfrvgyg vtgnevnanl lsmyllgygg yayingkwtq gaapyqnpnp
      661 dlkwetksel nlgldfsflk nrlsgsidvy hrvtsdllst yevptppyiv ssmmanvgki
      721 rnrgiellls gtaiqtrdlr fditgtfsyn knkivslsng lyqkdywyag atgspiqtht
      781 hivkegdpvg nfhgfqthsl tsdglwmvyg adgepklltd andgdkrvig ngipttygsl
      841 nlalnykgfd vsvmfrgafn fqvlnrqrmh wettarigeg nlpssvlnkp fgsnsyvkga
      901 pamqsyyved gdyvkldnvn igytfnlknq nviqrlrlyv agnnlltmtg ykgldpevsi
      961 kglapgvegs gsgelypttr qftiglnllf
//
LOCUS       WP_118223649            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118223649
VERSION     WP_118223649.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121022
     Region          26..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkllfiml aylflwtsat laqvskvtgv viseegnepv vgasilvkgf sqgvitnvng
       61 eftltnvpnd aktliisfvg mktqevaikp qlriimsnds qmldevivtv aygtakkssl
      121 tgaissvnqd qiemrptssv tsalegttsg vqinstygap gsdpsirirg igtvngsstp
      181 lyvvdgvpfg gnisdinpad iesisvlkda asaalygnra sngvilistr kgtsnkisfd
      241 lkinqgvysr gikeykrtsp nqfmeaswqn lknarmsagd daataakyas enliseqlyl
      301 niynkadnal fdangnlvsd aqilpgyadd ldwysdairn gyrqeysfsg ntaneksnyy
      361 fsigyldekg yvtnsdfnri sartsmsftp kkwfkaginl sgthqnshat ngdsdagytn
      421 afmycrqiap iypvhlhnad gsyrldalnn kqydpgyykd degvtistrn qyvdrhviwe
      481 nelstdktir ntlqaiafad vkflndftft vkgdlnvrns eqtsydnati gdgkgnngrt
      541 krvtyrykny tfqqqlnwnh vygkhyidvl aahenysnny dyeyafktte tfagkpnlsn
      601 ftditsltgy etdyrtesyl grirynyaek ynlevsfrrd gssrfskqnr wgnfgsigan
      661 wiiseedfmq svtwinslkf ranygqvgnd agtgyygymg lyagsqnani gayylsqnea
      721 ldlkwetgea ygiafegrlf nrwnisleyf dkrnkdllfd vylplsagat sttsaqatia
      781 knlgtisnkg feintdidiy rdkkwkvnfa tnatfvknki vklpeqnkdg iisgnykive
      841 gksryefflp tyvgvdqltg nslytlnled yfitlpdgsk lgnaegtdis dnesltsing
      901 tyytnnttya lkefhgsalp kvygsftgtv syksltfsal ftyslggqty dgvyrslmtt
      961 gtspgnfhsd imnawkaape gmsensadri widgipqins tmsannnsas srwlvssdyl
     1021 vvknltlsyr lpasfvkrld lqgisvsanc enlwtftarq gmnpqqsfgg sqynylvtpr
     1081 vfsvginikl
//
LOCUS       WP_118223891            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118223891
VERSION     WP_118223891.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116492
     Region          6..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhssaktlqi syigmkteev gikshlkitm ktdseilqev vvtgmqrmdk rlftgaatkl
       61 sadnvkmdgm aeisralegr aagvsvqnvs gtfgtapkir vrgatsiygs skplwvvdgv
      121 imedvtevga ddlssgdavt lissaiagln addiesfqil kdgsatsiyg aramagvivv
      181 ttkkgkagsn kisytgeftm rmkpnyrnfn imdsqeqmdv yktmasngyl nfsdvyrasd
      241 sgvygkmyhl indysngkfg lantpeaing ylqqaeyrnt dwfdilfnns isqnhaisms
      301 sgtekasyyt slsamsdpgw tkqssvqryt aninalynis qqvslnligs tsyrkqkapg
      361 tlsssidvvs gevrrdfdin pysyalntsr aldpneyyvr nyapfnilhe ldnnnmdlnv
      421 vdlkfqgelk wkpfkkvels algaykhsst tqshsitdys nqawayramd datmrdanpw
      481 lytdpdvans lplsvlpvgg fyretkygmn sydfrgtisy ndvfaedhvi nlfggmqlta
      541 tdrsktwfng vgmqydmgml psyeylffkq gkeensqyyt veetrsreva ffatgtysyk
      601 grytvngtvr yegsnklgks rssrwlptwn vsgawnmhee affedltptl snltlrasys
      661 ltadrgpanv tnsrvviqsy npyrpfasvs esgleiydle nseltyekkh einlgadigf
      721 innrinlvfd wyrrnnydli giintmgvgg qiakyanvas mrshgveftl strniatkdf
      781 kwntdfiish akntvtelys nsrvidmisg sgfaqqgypv rslfsmdfkg lnedgvptfi
      841 nekgvlttsd infqernnkd hlvyegptdp titgsfgnvf sykgfklnaf itysfgnvvr
      901 ldpvfsnkys dldampkefk nrwtvtgden rtnvpviadr rmnqqdqyls raynaynyst
      961 ariakgdfir mkeislsydf pkswishlkl sdlslklqat nlfliysddk lngqdpeffn
     1021 tggvaapvpk qftltlrmgi
//
LOCUS       WP_118223895             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118223895
VERSION     WP_118223895.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108712
     Region          5..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mssaktlqit yigmqaqdva ikpnvkvimk sdtemldevm viaygttkke sftgsaevik
       61 seklkerpva nvtkaldgmv agvqttsgsg qpgsgssvvv rgygsinssq splyvvdgvp
      121 ydgnisainp ndietmtvlk dasagalygs rgangvimit tkkgnsgkvk vnlkanwgvs
      181 sraipryetm deagyletif qsyknnqiin ggvspelagv aaleamksgs tamlgqneqy
      241 npfnysitel idpvtgkvrs daklrysedw mdealksnpl rqeyvasfsg gsdktkymfs
      301 lgyldeegll kttkfnryng rlnidsevtn wlkagmsany srnesntave nssgssnvwy
      361 saqlmapifp vfekdangat iydnlgnavf dygknrpaga ssewntiatl yddmystqsd
      421 nlsgrvytel gdlkntflqg lkfsvnygfd linsagatyy npyngnsvsv kgtiqkatar
      481 tfsytfnqll tydrkfgdhh fealvghefy kyrydylsat ktgfpfggly eldaattitg
      541 assyqnnyav qsvlsrlnyd fadkyylsas frtdgssrfy kdnrwgkfws vggnwrishe
      601 sfmsditwin nlslkasygv qgndailngt kqnfyawqsf ydlgyanssm sgaavtslen
      661 kelkweknan lnigieaklf drvsatiewy qrkttdmlms fpmatslgfd gynknvgsmr
      721 ntgidltlgv difkdtpfiw nltllgstik nkvlqladkp eiisgsyiir egetlysfyt
      781 ataagvdpat geqlywawdt dengvkgkky itndmakata ckeiqgsrip dlygsinntf
      841 kykgfdlsil ctysiggkvl dgiyntllyg nyvgqakskm lerawrnpgd itdiprieig
      901 ksyivtdnsl idasyfaikn ialgyslpsk wmksigfdsa rltatadnvv lfnhlkgmdp
      961 qynftggtdf gyvpvrtisf giditf
//
LOCUS       WP_118226906             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            eggerthii].
ACCESSION   WP_118226906
VERSION     WP_118226906.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides eggerthii
  ORGANISM  Bacteroides eggerthii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Bacteroides eggerthii"
                     /db_xref="taxon:28111"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109167
     Region          3..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvsfvgmqt qevaikpnvr vilksdaeql devvvtamgi krdrkalgya aqdlnseqln
       61 kagttslasa iqgkltgvdi rqssgapgas sqiiirgars fdgnnqplyv idgmpintta
      121 dfdtgnsvtg anyadrsidi npediesvnv lkgqaasaly girasngviv ittkrgsknn
      181 mnkpnvtist nlsaqrvsrk ferqdiysqg nsitagydpt ssmtwgpkis elandpkygg
      241 nmnnqytatd gmhegqyynp kraqaglsgw ttpqiydnvg dflgtgften tnvnlsqsin
      301 ginysfgvnn shqngiipst gmdrwgargl vdwkinpqwn tgfsinysst kitsapgand
      361 gimnvvysap aeydlkgipn hepgnptnqi lfrstsftnp ywwaehneyl qhtnrafgnt
      421 yleyqpnlgl genfslkire qagldiwtsd yatiremgst sslkggdien ygsqhnvfnn
      481 lftvnfdgkf gksdewrlnv ilgnefnhes irnwdyygsn fnfpgftnig natsltssey
      541 krqertvgff gslsmswqdq vyltvtgrnd yvstmprgsr sffypsvslg weftklpflq
      601 nnkilnygkl rasfaqvgqa gnyyanyyyt ptygggmysy ypvtyplpsg vstfipyyrv
      661 ydeglkpqnt tnyeigadlh ffgsrlkvey tyslqnvedq ifyvpvdgat gyqemltnag
      721 kmrthahels intailqakd fdlnlginft kvnnkviela pgvesimlgg fvepqvraqa
      781 gctypniygl gfkrdeagnl lllnglpqss gnsqdlgncs pdfttgftlg grykrlslst
      841 twswqqggkm yhgtnmtlny fgttkeslpy hegsmiaegi devtgqpnti evnkadyyqa
      901 yynitesgiy dtsfvklrdl tltyqlpklg ifdisiygfa rnvliwanlp nfdpessqgn
      961 nnmsgyferf svpntssfgg gltinf
//
LOCUS       WP_118236336            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118236336
VERSION     WP_118236336.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121665
     Region          33..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhsdyhgkl lrlamvfval flcgtmayaq tdrmisgivv dengdplpta hirqvsqtkg
       61 eelaavitdm nghfrltllr takeieisyl gyeskkvrlt sansyrivle paselldevv
      121 vtgyqtisre ratgsfakvd skkletqrls svsslmegri agysdgkirg vtsmnglttp
      181 lyvidgfpve ktisdglgnw venvpdlnie dienitvlkd aaatsiygar aangvvvitt
      241 kkagknqlnv sfsatltvrp ynfytghlag tadmiemeke waamnpnlqg egasqyaqnl
      301 ldnasmyscl gvqailkhht gaiskaqmeq tlhelasqgf ryyddvkkyg krnpfsqqyn
      361 lnigrgtekn tfnaslsyrn nreedkytds esfglnlqnt trltswlsld lgtylnygdg
      421 ttqsynltsp gynyvpyssl lnddgsyytn tvadrysksq qkiissygly smditpldel
      481 grnlsksknf snrtfarlnf kftdwlryta sfqyevgeyk tsqlqdkesy avrnkvntfa
      541 tdasgsgqat ynlpygniyt tgtnsirayn frqqldfnkt faekhdvtal fgmevrenkt
      601 eynnrkyyny dpalltydli dervlsntyt gvlgnyvsfn kndisniyel vnrfvsfygn
      661 aaytydgkym vtgsirwdrt nlfatgskyq kkpiwsvgag wnldkesffk vsfinmmklr
      721 fsygiggnia knsapymtay ynnnthvggi qgtisnrpnp dlrwekttta nigvdfsmfr
      781 nrlngsieyy nksgvdllan tngvptegfg fstytmnngk mrnrgfeltl sgdvimgkdw
      841 nwnvggvlgy nknkvtyvnv kapaiflqfd ypaayprvgv pynaiygylw agldskgqpq
      901 vydsegnihv ssspqkveda vylgtsvpvy sgaintnlry knwelaaqll fegghkmrnt
      961 niaypglgvt skdvskrwrq pgdeaytdvp ryvpseskdy nsyssdlysk asihvldadn
     1021 wrlknlsvty hvpasvcqkf yvknarimlg menvftlaks rdvkwmlggy skpnylcnvn
     1081 lnf
//
LOCUS       WP_118233264             980 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118233264
VERSION     WP_118233264.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109322
     Region          2..979
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvisyigmkt qevvikpsvk vvmmpdteil devtvvaygt krkqdlvgsi ssvkneiisn
       61 sqatsvsnal egavaglqvv sssgqpgqda nivlrgigsi sasnnalivv dgvpfngkls
      121 dinptdiasv nvskdavsns lygsraaggv vmittktgrk dkvainfngs wgvaqraykd
      181 ydmatdpgef yrlswyglrn tywaagnsie esnlaasqdl lgelgnynay iipqgeylvt
      241 pdgklnpnar pryndsfada lfdnafrqey nvsasggndr tdyyvsmgfl dndsyvlgss
      301 yerftaranv nsqlkswlkv gtnvgyskat qngvqenaga asnpfevars wapifpvhay
      361 daegnmkyye dgspmydagn getdgtskrp tatnqnvian mkediretvy nnltsrsyle
      421 isflknfkft anysydftns sqtvfytpli gdgqsfggrg tkgsyntttt nfnqilaysn
      481 vfgdnhhlsa kigheyykye yqylagqktn ffnpnnpeld nggqmqyins ytanhniegy
      541 fgmadydysn kyylsaafrr dgtsrfldrw gnfwsvgaaw risneafmeg tnswlndlkl
      601 rasygtqgne silseydyay vytpyqdqyt vtwngselgy spefygnpdl twekqktfdv
      661 gvdfrlfdrv ygsfeyfyrr tddmlfkrpv aystagrpyn wenlgamknt giefevnvdi
      721 fnqpdlkwtv slvgshyknr ivtlpeenre ngitsgpfnl regksrfeyy tymyagmdek
      781 gnamwymdet nekgevtgrt ttttyadatr yfigksalpd fngglsttfs ykgidlsiat
      841 afqiggyayd ysylsgmsss fyvghnkdmw ktfnpetgqg slpiwnadna snsftqqsdl
      901 nlikasyfsi rnitlgytlp knlmqklgve klriyatadn lglwskrqgf dprvamagsd
      961 deyggyspmr visgginltf
//
LOCUS       WP_118240926            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118240926
VERSION     WP_118240926.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121695
     Region          33..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhsdyhgkl lrlamffval flcgtmayaq tdrmisgivv dengdplpaa hirqvsqtkg
       61 eelaavitdm nghfrltllr takeieisyl gyeskkvrlt sansyrivle paselldevv
      121 vtgyqtisre ratgsfakvd skkletqrls svssliegri agysdgkirg vtsmnglttp
      181 lyvidgfpve ktisdglgnw venvpdlnie dienitvlkd aaatsiygar aangvvvitt
      241 kkagknqlnv sfsatltvrp ynfytghlad tadmiemeke waamnpnlqg egasqyaqnl
      301 ldnasmyscl gvqailkhht gaiseaqmeq tlhelasqgf ryyddvkkyg krnpfsqqyn
      361 lnigrgtekn tfnaslsyrn nreedkytds esfglnlqnt trltswlsld lgtylnygdg
      421 ttqsynltsp gynyvpyssl lnddgsyytn tvadrysksq qeiissygly smditpldel
      481 grnlsksknf snrtfarlnf kftdwlryta sfqyevgeyk tsqlqdkesy avrnkvntfa
      541 tdasgsgqat ynlpygniyt tgtnsirayn frqqldfnkt faekhdvtal fgmevrenkt
      601 eynnrkyyny dpalltydli dervlsntyt gvlgnyvsfn kndisniyel vnrfvsfygn
      661 aaytydgkym vtgsirwdrt nlfatgskyq kkpiwsvgag wnldkesffk vsfinmmklr
      721 fscgiggnia knsapymtay ynnnthvggi qgtisnrpnp dlrwekttta nigvdfsmfr
      781 nrlngsieyy nksgvdllan tngvptegfg fstytmnngk mrnrgfeltl ssdvimgkdw
      841 nwnvggvlgy nknkvtyvnv kapaiflqfd ypaayprvgv pynaiygylw agldskgqpq
      901 vydsegnihv ssspqkveda vylgtsvpvy sgaintnlry knwelaaqll fegghkmrnt
      961 niaypglgvt skdvskrwrq pgdeaytdvp ryvpseskdy nsyssdlysk asihvldadn
     1021 wrlknlsvty hvpasvcqkf yvknarimlg menvftlaks rdvkwmlggy skpnylcnvn
     1081 lnf
//
LOCUS       WP_118240973             909 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118240973
VERSION     WP_118240973.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 909)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..909
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..908
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 yqtqeipvgn ggkkditmqd dselmdevvv igygtqrkgd vtsaissvks esfvkgavtd
       61 agqliqgkva glnislpsgd ptgntqimlr gisslkggts plvlvdgvpg slntvapedv
      121 esidvlkdgs ataiygtrgt ngviiittkq srkemaptid yngyvsvsni lnrpdfmdad
      181 dlrqkwnegy tfnganlkdf gantdwlgel trtavshshn lslrggsknt nytasinytn
      241 rqgtfiktdf eaingrmdit hsmydnklta nvstfvsqht mprswntyay rqalihnpte
      301 pvkdengdwf erdlyfydnp vsyiretige mkrknirfng sltfrpiesl tlkamyarrs
      361 ttstdgyyqt kkhvsttksg rngyayryds dfdnnlielt anfqkafgkh nvsvligyny
      421 edntnsnlsm snydfptday synkmeagma lkrgeasmts yknsdkligl ftrvsynfnd
      481 ryllmaslrh egsskfgkdh kwgnfpgisl gwrinrenfm knvnwmdnlk lrvgygvtgi
      541 nvadpytsls slnyngafly ngtwvkalet irnnnadlrw ekkhefnvgl dwdvlggrlg
      601 gtvdyyirrt kdalwdyevp vppymyptml anasemenkg leiliratpi qtekftwntn
      661 vsystnsnkv valssekfsm dqdyfytgyt gepiqttthi vqvgkpigtf yglksvditd
      721 dglwlvenkk gehvlaeetd atdwqvlgng ipkhylnwnn tfnffnfdls inmrgafgfq
      781 ilnyqrmyye nakpeiqynr lnsafdkvyg ktqlkddqry vsyyvedgdy wkidnvtlgy
      841 tfklskqhii knlriyasvl nlatitgykg mdpevplssn tyglldagtd nrdkyptnrt
      901 ytfgvnltf
//
LOCUS       WP_118241003             905 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118241003
VERSION     WP_118241003.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 905)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 905)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 905)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..905
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..905
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..904
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 yqtqeipvgn ggkkditlqd dselmdevvv igygtqrkgd vtsavasvka edftagkigd
       61 aaelikgkva gltiakgsgd pnaestirlr gvislqggst plvlvdgieg glgtvspeni
      121 asidvlkdas aaaiygtrga ngvilittkn gqresrtaan ysgymslskf gktldfygae
      181 eirqgltnya dkgydtdwld avsrtafthn hnfnisggsk nttysadfty rkeegvllet
      241 yneemrmrfd vshwmlndml kvnfnmvktf hkngpidaag lgiyrqaimr nptepiwned
      301 gtfyenfavn yyynpvgiir eqdgkynsen trmtgnitfe piknwqtnlm lsrrvtsdhn
      361 rgyytseyfs qksenhtgya yhsqneyttd nlevtskynh twnkhrfdal vgynyqynvn
      421 egfgannydy ptdfylwnnl glgtalkdgk agmssykndn tligffgrvs ygydnkynvl
      481 lsvrregssk fgennkwatf psvslgwtis nekfmegltw lnnlklragy gvtgvivgds
      541 ynsltryeyg spyfydngvw hqglsvksnp npdlkwetsk efnigldwav lderlsgsid
      601 vyqkktsdml ydftvptppn lynktlanag kmrnqgieia vnaipvrtkd fewkttvtas
      661 hnankllsls ndlyetsnqi dhaylgepin lstqrmevgr smgqfygmks vgvsenglwl
      721 ienaktgeie eftdnmlsnd dyrqylgnal pklylgwnns fryknfdlsf qmtgqfgfki
      781 lneprayyen nsiaynrlks vqkapyggqy tlstaqkqtf vsyyledgdf lkitnitlgy
      841 niplksskfv knirayvsad nlfcitgydg ldpemsngdi wslgidwrdk ypstrsftfg
      901 lnvsf
//
LOCUS       WP_118241013            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118241013
VERSION     WP_118241013.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112456
     Region          26..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkilalti laftsmnama qeevnvtgkv vdkvgnpvsg aavsvlgqpl tmvstdvmgn
       61 ftisvskdaq lwiqtpydak kvvkaemdkk mtvimdffsn kvnygfgleq tytestgaas
      121 tvysddiatr ssytvgnsly gnvlglttmq ktgtmweqip smfirgqksl ngnngillvv
      181 dglerdnayq vlryltpeev esvtvlrdaa avalygykga ngvvnivtkr glykkreisf
      241 aydhgftcqn rlpemsdsyt yaramneala ndgkaakysq nelnafksgk ypyyypnvnw
      301 wdevfrergs sdiatltfrg gasklryytm lnlqngrgfy knanendgys tqekyskanf
      361 rsnldidltp ktkmqvnimg mlnefsrpgy gsdnligkly mtpsaafpir tenglwggna
      421 twdgynnpva laqgrgyskg htlglwadms lrqdlssitk glgasfrmgy dnvasywedh
      481 ckdyaygstv vtewkngeps afseytggsd semkggskld wqyrsfnfma nvdwkrqfge
      541 hkvyttlmyt ykydnnanin snlyhcnwsw ythygyknry ffdfalvnsa snlletgnqw
      601 hisptvglaw vasnesllnn yswlnflklr asfgvintdn ipyngywyet mngsgggypi
      661 qdnfsnggsw qegqlpsing ttekaykynv gldatlfggl tltadafyek rqdiwvytgg
      721 knssilgata syanagvvds kglefganyi kslgkvrfnf ggtftltknk iveqleepka
      781 yeylratgka vgqifgyqav gffvdqsdid dspsqqfgvv kpgdikykdq nndnvinefd
      841 qiplgynssv peiyysfnig aewkgigvnf dfqgvgnyts wttlnglyrp lsngnaisny
      901 yyenrwtpet pnaryprltt etvqnntqss svwlvdgsfl klrncevyyk lphsvvnkwh
      961 lnsaklyvrg vdlfcwdhik eidpesigng ipttrsinig lsvgf
//
LOCUS       WP_118241025            1164 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118241025
VERSION     WP_118241025.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1164
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130304
     Region          129..1163
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mstkllseti crkglmvkcf valivfccsv geafaqtdtk vtinvnnvli rtaldqlqre
       61 akihfvydee nidsgkrvsl sytetplnav lddfckqtsl ryevkrnlil ilpskaektt
      121 gkhepfymtg vvtdetgesi igatimiggt sqgtvtdidg ryslqvtpgd lvsftfvgma
      181 dkvvkvqagk kvvnvkmetn ataladvvvt gyqtlskera tgsysvisek stkgkletdv
      241 lsrieglvag inktssnsnd vvirgittym gntkplyvvd gmpyegdlas inptdvqnit
      301 vlkdaaassi ygaraangvi vittkrgqeg ktkvsyngsi klspkpdfdy lnlmssselv
      361 dmqiegfdyy htayenlnkr qavnpvvdll yqhergqltd sqladallpy rtndnrkqie
      421 defarvgivh qhnlaisggs nknrymatvn ymgdygnqky qskdrigfsl kddvdffdwl
      481 sadfgvtgsf yrskgdngag sysslmssyp syymlrdlqg nplnfqrtks dyelqrlqsi
      541 glmdetyspi knraeesyhn nsnyyrlhag lkfkllegln idlkyqtegt ydknrtlysn
      601 msytvrnmin daaqydaatg sltlnvpkgg qldesryesy sytmraqvnf nrifgkhais
      661 alggaerrlv rrtgaqnyym gyddnslgvk pinplamspi ngteallgsf nwvygeynal
      721 thtedryvsf yangsytfde rysltgsiri dqsnlfgtdp kyqyrplwsv ggswqianep
      781 fmedcmwlnr lnlrmtygvg gnvpkdagpy mtvvdsgyne wvgdfgsyiq nppnsqlrwe
      841 ktastnvgid fsafnsrlsg sidyyykktt dllgnrnadp tlgwasllqn ygsmfnrgve
      901 lslqsvniqn knftwgtnlm fsynkneltn legtketvfy ysaynvaavg ypinsvfsyr
      961 yagldptngn vlvynkegek vskvssiddm vysgtrtpky taslknffsy rdfdfsfmfv
     1021 yygghvlrdv vagymggaps anltrkalnh wrkpgdenip gvapsfnrni yytdaqtwys
     1081 adihvkkady iklrdislsy nlpknwlrky fiesaavtcq isnvwwwaan gdidpeaytt
     1141 sgygwgaltl pnpttytigl slnf
//
LOCUS       WP_118241120             898 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118241120
VERSION     WP_118241120.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98580
     Region          27..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgrvslclvi mfficsaqki daqvqnirek qdtisatksl ehirpenikk gplnnaldvl
       61 sgqsagvnvt tngtdrlaml nsirvrgtts imggndplvi idgvtsdiat lstiypadie
      121 sftilknate tamygsrgas gvieiktkkg tgrgfeisyd gnygfesmyk hlqmlngpey
      181 iataealgld ynnggyntnf hdvitrtgli hqhhlafsgg sensnyrasf gfmdhntivk
      241 vndyrnlvvk ldatqkafdg rlvgdfgvyg ysskihdifd trmlfysaaa qnptypagtd
      301 vngnwvknsa ashinhpgal lyekndseer nfnthlglkf nildnlilsa fgsysysstg
      361 naqfcptwvw aqgnvyrgef kgedyftnvs lsynnawgds hldavvgaey lkqvrtglwv
      421 qakrittndf synnigatss rpfggtsssy edpslasimg svtysykdry siaaalrgdg
      481 ssmvsdnntf gffpsvslgw dvkkegflsd tdfitmlklr tgygrsgnlg gitsyttlnt
      541 vkengivsin gaptvtmgsi rntnpdlkwe trstfnigfd lgiwdnrlml tselyysktt
      601 dmlyeydvpv ptfafdklma nigsmsnqgv elgisvvpiq rkdmemninf nmsyqknkll
      661 slsgeyngmh mtasditpig slygagqngg dnnvvyqivg qplgvfylph ckglkenelg
      721 gysydiedln ddgeidfsdg gdryiagqat pkvtigsnis fryksfdiam qingafghki
      781 fngtglaytn msifpdynvl kgapekniid qnvsdywlek gdyvniehit igynipmksk
      841 avkslrlsag isnlatitgy sgltpminsy vvsntlgidd krtyplyrty slglsiqf
//
LOCUS       WP_118242792            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118242792
VERSION     WP_118242792.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112808
     Region          28..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkyknlmwa claslaipag aqdadnnirg mvvdkwghpv ygasvmvkgm petrvetdkd
       61 gkfsieasag qqlnivsvdk gmttvkaegk slvkvvlnya gqsidvgagr tftrsestaa
      121 vstiynedfd krsaknvsns ligqgmgmmv lqnsgnyadv eptfyvrglq slssssplil
      181 vdglerdmsl lspeevesvs vlkdaaaval ygykgingai littkrgkyn skeirftydh
      241 vnnymdrkpe fvdastyaqa yneargyegl spryadkeve yfrngdfpyl ypnvnwldet
      301 fkdsgisnky tiefrgggsk fryysmldlv tdrgfvkegd mndgystqnk ysranlrtnm
      361 didvsrttkl kvnilgtlse slrpgasanl wdmiytvpaa afpikdedgl wggnnttwlg
      421 tqnpvaqsqg aayskghtrs lfaditlnqd lsavteglgf nfrlaydnys siwedhsqay
      481 qyggyvvsyd eltgplytht tageptemgk sasinnwarq fnfsggfdyn rtfgdkhdvy
      541 sqlkweyeyr dsyglnttiy rqnvswfthy gydkryfldl alvgsgssll apghkwafsp
      601 tvsaawvlse edfmnnaawi dflklrasfg iinadylpas dvydywdqiy tttgtrymfn
      661 saydstfgtt elgrlastny thergykynv gidatlfkgl nlsvdayyqr rnniwvsseg
      721 kytavlgqtp pyenagvvds wggefsldyt krignvvlna ggsfnwnrne ikeqleeprm
      781 ydnlvqtghs lnqiygleav gffkdaddia nslpqsfgav ypgdikyrdv ngdkvinsnd
      841 vtaigystva peiyytfhlg aewkglgfda qfqgtgrysa ilntksmfwp llstttlsth
      901 yyenrwtpdn qdakyprlst qsntnnyqtn tvwladrsfl klrnievyyn fpkswlqktk
      961 figdarlyvr gvdllcfdki dvldpesyga tnplnksliv glkigf
//
LOCUS       WP_118242996             948 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118242996
VERSION     WP_118242996.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..948
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106783
     Region          43..947
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkniriksvl caalatssly vgaqnlpsel ldassdslsv aeeelvqvay rkvnkkdllg
       61 gvssvnveel mkkdyftysl dgmenmvsgw ngsslwgmds ylvlvdgvpr dannvmpsei
      121 kditflkgas avvlygsraa kgviyittkr gkegdtridv rgntgffvpk sypkylgsae
      181 ymtlynearv ndgmdplysd vdiynhgsgi npyrypdvnl ysddylkkay nqsdvtaeis
      241 ggsekarfyt ninlyntgsl ikvgnakddr ttrfsvrgni dvnlgqyvkt yvnanatfyd
      301 grsargnfwg aaaslrpnri splipvdyim qnntdawnlv nnsrylidgk yllggtqvdq
      361 tneianlyaa gvntytsrqy qfdmgvdvdl smllkglsfq trfaidyatt ynryygdtya
      421 tyepqwanvn gqdqivgltk ygddvhdgiq hiagswnrqt mafsaqlsyn nkfadshnis
      481 amliaagyqq gesavyhkts nvnlglqvdy dylskyymsf ggalihsarl pennrnafsp
      541 sltlgwrlsn esfledssvl ddlmlsvsgs vlntdlgidd yymyqssydq angawwgwad
      601 gnqshatear rgnnsdlsfi krkeisvglr gslwnkmltf dasffknsle gmlvqpsnsy
      661 pnyfvsywpe stllpyvnyn nstrtgfdla lnfnkkmgev dfnlgvnaty ytnentkvde
      721 lyedayryrk gkptdgmwgl qaegfynsee eiqnsgitss fgelkpgdlk yvdqngdkii
      781 dekdevylge rygwqgtplt vglnltlkwk nftlfalgtg ywgasafmsg dyywvygdkk
      841 ysevvrgrwt petaetatyp rlttqtdnhn yrnsdfwmyk tnrfnlsrlq ltydlpkqwl
      901 gnsfvrsfsv yayasnllti skerekleln tgaapqtrfy nigfkigf
//
LOCUS       WP_118242950            1131 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118242950
VERSION     WP_118242950.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1131)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1131)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1131)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1131
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1131
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125795
     Region          67..119
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          133..1130
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkkkvlsdl kanicrfcmi gtcflvsnsv sgtttvkwds dgnmftvqas sstirnvlny
       61 ieensdyifv ydedvqsylg kqvnislenk kidkvldelf aetslsyakn grqvmvsrkn
      121 sttsvkqqgs nlqikglvkd adgealigas vvvkgtsigt vtdmdgnfil evpqngtlvv
      181 syigfltqev kvngknnini tlkedsqtld evvvigygav kkkdltgaia aikgddlaak
      241 ktttlstalq gsvsglmvsr dnnapgasas smrirgittm dnsnpliivd gvqcddidyv
      301 nsndvesisv lkdaaaasiy gskaasgvil ittkrgkead lslnytgefg weiptkqpem
      361 vgvtrylemn nellyndnpn agfyqlytad qvknwmeynk tnpndypvtd wqglilkgsa
      421 qrqthtvsis ggnkavrtka slsydevgal ytgrkfqrym mrvnndfnis dklsakldin
      481 vrraknrrpv ydpfsdmrkm paiyaamwdd griaegksga npyaalingg tytawstqig
      541 gkaslefkpi kelslqaiva pfinytkake frnyayytlk ddpdviggti egggssfstn
      601 klsetrndny hvtsqviany mksfgkhdlt vmagyenyvm rsenlsaard qyeltqypyl
      661 nigpedfmtn sgtgseytsn sffgrvlydy adryllqanv rhdgssrfas kyrwgtfpsf
      721 sagwvvteen fmkklnldwf sfmkiraswg mlgnerigds yfpymalmtf gdayfytdgt
      781 vtsnktaaqr dlaveditwe tttstdigid lgffnnrlhv tadyywkttd dmllsieipy
      841 fmgyanpktn agkmstkgwd lelawndqvg efsygatfnl sdfkskidyl nnsdiisgnk
      901 vkragvlfne wygyvcegiy qtqedvdnsa klndqvsvgd lkykdisgpd gvpdgkisad
      961 ydrvplgnsl prfqfggtln aaykgldlsv afqgigkqls ylakemvqpl rdnygnipai
     1021 idgkywslfn teeqnlqaky prlskvsldn nyamsdfwlf ngsyfrlkni tlgytlptkw
     1081 tdkigikktr iymsasdlfc isnyptgwdp emgvssypit tsvifglsvn f
//
LOCUS       WP_118243759            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118243759
VERSION     WP_118243759.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112179
     Region          44..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkieratqll flllisqggn aayanlprga saspvqvsaq ankitvsgtv vdvngeplvg
       61 vsvlekgtgn gtitdidgnf tmsagegatl eisyvgyqnl tvsaketlgv lvmkedteql
      121 devvvtalgi krsqkalsyn vqevkndvlt kvkdanfvns lngkvagvsi qrsasgvggg
      181 trvvmrgnks ikgdnnvlyv idgvpmgnqa drtgdgtgfg agrtssegia sfnpediesl
      241 svltgpsaaa lyganaangv ilittkkgaa gkvnvnvsss aefsnpfvlp rfqntygnvs
      301 geaaswgekl pvpssynpad ffntgttftn sfnlsvgndk nqtyvsgsav nakgivpnnk
      361 yhrynamvrn ttkffndklt mdlsasyvre yynnmlsygt yfnpllgayl yprgenfeke
      421 kyferydael gynvqswtpg dfgmavqnpy wvayrnlrpe vkdrymlyas lkyeitdyln
      481 vsargrldnt ytekedkrya sthgtfakpl gryaysneaf rqkyadiman lskpfagdfy
      541 anvnvgasfe eydtkgrgyg gqlllvpnlf aydnvdpstg vpsqtggdnr kmnlgvfgsa
      601 eiswksavyl tltgradkps qlinskspwi fypsvglsai vtdllpetmr qsispvlgfl
      661 kvrasytevg spipytgltp gtithsiegg vikpfkyypl pelkpertrs yevgidskwl
      721 nntvslgvtl yksntydqll eaklsetsgy dymfvqagnv enrgieltlg ydqtfgnfsy
      781 stsltatanr nkiialasnv knpvtgeald lsdikvgrfr lregeevgti yaeerlkrdq
      841 dgyivynegq tittestepy klgsvnakwn lgwrngftyk gfnlnflvta rlggiviskt
      901 qavldqfgvs qasadardag kvmvgnvavq pkdyyesvvn ldaynvysat nvrlqeaslg
      961 ytfpnswfkg tpfhsvnlsv ygtnlwmiyn kapfdpelaa stgtfgqgyd yfmlpsqrty
     1021 gvslkfgf
//
LOCUS       WP_118244181             571 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118244181
VERSION     WP_118244181.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..571
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=61962
     Region          51..>563
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mntqlnrmlf srafvkvsac vvlsagclpm ttyaesieap vvenvlqqka isgkvvdskg
       61 esiiganvme kgttngtitd fdgnfslkvs anstivisyi gyqsievsaa qikaggqitl
      121 kedtelmdev vvvgygtqkk atltgsvssi ggddlkkist anltntlagk tagviantrs
      181 gepgaddaei lirgkgtlgs taplivvdgi adrsfgrlna ediesisvlk dasaaiygar
      241 aangvilvtt krgkegkikv nysgnvsisq ptripemlda yqyatyvnef daaqgnalty
      301 petalakild gsdqinypnt nwwnavaknw atntehslsi sggnerfsfy tsaqylyqdv
      361 iyrdspqnyn qyqfttnlda kitkaikfsm dilgrqtvnn rgvystedlf gyflttspms
      421 apyypngmlr ighdgitnna vlmvsdlpgt dkstnntlnl kprlridlda ltsglylegy
      481 aaldytfnng ktqntpydiy sydattdeyi nhrdatgavs asswssnsst itlnarigyn
      541 rtfndvhkid afvayeqcky nynylygyrt n
//
LOCUS       WP_118244517             485 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola plebeius].
ACCESSION   WP_118244517
VERSION     WP_118244517.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         <1..485
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <10..484
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 ainpvpksci ynlnssyiss alpdldygst nkddqsnags sdetarqnwf grinygykdk
       61 ylaevtlryd gsmnfapghr wglfpgfsag wvmseehffe plknvvsffk lkgswgmmgn
      121 dnisayqyls mygfsnagyt fgkdpvfaqg vyetvtanpl vtwetaktwn vgfssqflng
      181 kfgldfdyfq srrsdilitr nasiptysgl slpaenlgkv knhgfevigt yrdhagdfew
      241 gvtgnvtyak nevvymdeai dtpewqcqtg hpidggiyyq algiyqtqde idstphlagt
      301 kvgdliyqdt nkdgnitwdd avrrdksatp kwifgltlng awkgldvnaf fqgqadaeil
      361 vqptmnmatd fyegrwsdsn taeqnlaakw prafmkesqv dgrnsqsstw wlrdasfvrl
      421 ksleigytfp skwttklgie nlrvyangnn lftidgvdif dpemtssikg ypiqrtwtfg
      481 lnvtf
//
LOCUS       WP_118244680            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118244680
VERSION     WP_118244680.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112664
     Region          41..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvrktslll fllltgqgtl fasgakengl plplsqqadk isitgsvvds kgepligvsi
       61 leegttngti tdfdgnfsls vsagamidis yigyktqsla akpsmgkivm kedtkvldev
      121 vvtalgikrs ekalsynvqq vdgdkintvk danfisslng kvagvtinss staggasrvv
      181 mrgvksiats nqalyvidgv pmynmmnggt egsifsqqpg tdgaadinpe diesismltg
      241 psaaalygna aaagvvlitt kkgqedktsv tisnntmfsr vsmlpemqsk ygnlpndins
      301 wgpvvnsnyd pkdffrtgan iinnvslstg nkknqtyfsa sttnttnilp nsgynrynfl
      361 vrnttnflnd kltldanasy ilqndknmvs qgyynnplpa iyrfprgenf ddvrmferyn
      421 nvyglmeqyw pygetssgmg npywiqerql renkktrymi gaslkykifd wfditgrvki
      481 dnyenrytyk ayastgklas gdkgsytdif sqskntyadv igtinktisd wsinvnagas
      541 lndtryenig ydgglkipnf favhninfke awkakqegwh dqtralfasa eigwrsmlyf
      601 tvtgrndwds rlaysdyksf fypsvgasai lteafdmpew lsylkvrgsy tevgnaynrf
      661 mttvtypyde qgqswqslad ypntklkper tksweagida rffndlsfnl tyyrsntynq
      721 tfyadlsass gysriplqsg nimnegiema igydktwndf sfstsytltw nrnevkelad
      781 nvynyadgsl lsfdelpvas ygsmdarlll rvggsmgdvy sqrvlkrdmn gyilndpesg
      841 lsmtdqenyl gsilpkvnmg wnlgfgykgl nlgmtftarl ggivisetqs ilnaggvskv
      901 sadyrdaggv pinqtkvspk eyfttingas yyytysannl rlgelnlsyt lprkwfndkm
      961 gmtvgfvgkn lwmiyckapf dpelttsaas nfyqgfdaym lpstrnfgfn vkfqf
//
LOCUS       WP_118251788            1130 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118251788
VERSION     WP_118251788.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1130
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124259
     Region          41..1127
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkrlksvsm llflmgastg aayavanpgv tdvkitqqtg tctgivkdat gegvigasvv
       61 vkgttngtit gldgdfslsn vkegdiivis fvgyatqeik wtgkpldvll kddtqllgev
      121 vvtalglkre ekalgyavte vrgdelkaan tispvtalqg kvagveisss dggifgaaki
      181 qirgastmgn nnqpiyvvdg vildnnvsgn ddlnwgsnss dygnelknln pddfetvsvl
      241 kgaaatalyg srglngavvi ttksgkggsg lgisfsqtfg idhayktpdi qtvygdgpyv
      301 grydadgdgn iwqptqfqvn sagqhtligt wgtgfgpkyd gsqienydgt mttysphknn
      361 mldmyqigfn tntnlaihgg ndkttfyasm sykhaesttp nntferysfl vkathklndw
      421 vdvaasvnfs nstprnaarn igenfvngtw tpnydpqyfr nkylgehggv astdygdiyg
      481 nvpgktywfe idkydyrqke tvvrptfevn mkitdwlkfk adanmnyyyn rgdnkelgtg
      541 yandggyyki wqntkeqttf ggsftwnkti kdyyiggfar feyyntsrye ysvntdggmv
      601 vpgqwfvdns knpkksdggl ksekrmlsai falnlgwknq vyldvtgrnd wssalvyang
      661 tgnhsyfyps vsgswiiset freqlpewis fakvrgswaq vgndtdpyyv nqaygfgtie
      721 lpnggniytn tlntimkasn lkperknawe igldfrtfkn rlnldvtyyk entkdqimei
      781 atpwvsgist qlinagniqn qgielalnti pfqnedwewg ldftwtknts kivelhpdaa
      841 eyislagqvn aydyrigsva kvggsygmlm tdilparddq grvllnysdt rravyerrsg
      901 vvqelgdmqp dflgsmstsl rwknlslhvg ldmrigglva mysnrygsna gwtktslkyr
      961 daasggltwt sqyaggsngi tyedgvileg vfapgtsatg idgkshdisg mthqqaidag
     1021 iiepthasay hvfrnswgeg vvnddwvhel syialrditl syrmpksias kigakglnls
     1081 laarnvgyiy nslpnkvhpe svrgnrsaef rirgyepyir nytftinaef
//
LOCUS       WP_118254220            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118254220
VERSION     WP_118254220.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115701
     Region          41..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkktmflgl lgaglmwmpa sailaaqmnn aamsvqqdqg ikgtvvdatg etligasvkv
       61 agttngavtd idgnftlnck pgatlevsyi gyktmtvkaa ngmkitmqed gkalnevvvt
      121 algikrdrka lgygleevkg eeltkaketn vinslsgkva glvvqntagg asgstrvllr
      181 gntemagnnq plyvvdgvpl dntnfgsage sggydlgdgi sainpddiet mtvlkgpaas
      241 alygsrashg vilittkkae kdrisveyng sytidtqlak wddiqeiyga gyngelptss
      301 tsgtnsswgp kaddfmfkyf dgeerpfmmh pnnasdffrt gfttqnsail svnsgktgmr
      361 fsvtdmrnkd ilpntnmsrd nfnlrvntsa gpvdfdftan ytrekvknrp algdsqsnvg
      421 knlmtlagty dqawlkhyed adgnysnwng ndqynknpyw dlyknsntsd kdvfrftgka
      481 iwninkhlkl qgtigtdins mnfqefiakt tpgtpagklt dqifnnrtln aeilalynns
      541 wgdfdvnata ggnifkvnnk tttnvglnqq mngiqnimny qeqntresmy kkqisslyas
      601 aslgykhtyy legtirgdks stlptnnnty vypsvsgslv fsefiknkkf inygkirasw
      661 akvgsdtdpy llalnyttgk ysysgytigm ianstqpnkd lkptmtgsye vglemkflng
      721 rlgldatyyn qnsknqilsl astttsgyay rlinageiqn qgveialnar alqikdfawd
      781 lgvnfskntn kvkslidgmd yfelakatwc gvsvgakvge nygairghdf lyndkgqvvv
      841 daatglpkvd qeiktignst wdwtggfyst fsyknfrlsa sfdvkvgadi ysmsmrsaye
      901 tgkakgtlag reewysseea rkasgmelae wraagnckgf vvdgvidngd gtyrkndiav
      961 npedywkhva kgvqsafvyd nsyvkcreit fgytfpesil gkyvkgltvs fvarnpfivw
     1021 knipnidpds syntsglgle ygslpsrksy glnvnvkf
//
LOCUS       WP_118254680            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118254680
VERSION     WP_118254680.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123515
     Region          24..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrllfllv nlfllcggal aqtkvtgtvv sqedgepvig asvvvagaar tgtvtdidgh
       61 fslevpagkk lvvsyigmqs qtltpaakmt irlkadsksl gevvvtgmqk mdkrlftgat
      121 tkisgdktkl dgvadisral egkaagvsvq nvsgtfgtap kirvrgatsi ygsskplwvv
      181 dgvimedvte vdaddlssgn aetlissaia glnaddiesf qilkdgsats iygaramagv
      241 ivvttkkgka gtnrinytge ftmrlkpsyr nfnimnsqdq mgvyremynd gyfsfeksfr
      301 asnsgvfgkm yhlmntydsk tgtfglpnte eamnsylqka eyqntdwfdl lfnnsisqnh
      361 svsmstgtdk aqyytsfsvm ndpgwskqsk vqrytanvna lyniskklsf naianasyrk
      421 qrapgttsqs vnnvtgevsr dfdinpysya lntsrtmdpn elyvrnyapf nifrelenny
      481 lsldvvdmkf qgelkykpis kvelavlgay kystttnaat itdqsnqawa yramddatmr
      541 danpwlytdp dkanslpfsv lekggfyret kykmnswdfr atasyndvyn kdhivnlfgg
      601 leinsldrsr syfngvgmqy dmgylpafny nffkqlaeen gqyysldnsy qreasffgta
      661 tysykgryti ngtiryegsn klgksrsarw lptwnvsgaw naheeswfak lnpvlshltl
      721 kasysltadr gpasvsnslv viqsynpwrp fagdketgle iyrlgnddlt yekkhelnlg
      781 ldmgflnnri nvtfdwyrrn nydligpkrt mgvggeiyky anvasmrshg eeltistrni
      841 etkdfkwstd fifshskntv tdldsranim qmitgtgftm ngypvrslfs idfkglnkkg
      901 lpivvnqnge etsyggdlyf qstttdylky egptdpting sfgntfsykg fklnvfitya
      961 agnkvrldpa fsssysdmta mpkefinrwt qagdeaytdv pviadqrmkq ndnyigylyn
     1021 aynystarva kgdfirmkei slaydfpgkw iqalrlnsvn lklqatnlfl iysdkklhgq
     1081 dpeffntggv atpmprqftl tlrvgl
//
LOCUS       WP_118255007            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118255007
VERSION     WP_118255007.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123918
     Region          51..103
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          116..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mirrnylksl mifiltclpl lgasaqqkvt vnvvnaslkq vfstienqts yrfsyksdii
       61 dhrkditirk sgvpvttvld aalkgrnlky svvsqksivv sekhaaaapq qsnkhkmqgv
      121 vkddngepvi gatvsvvgtd elavtdidgr ftinaakgak vkvsylgfvd revkasenmn
      181 iamsedtqal sevvvvgygt mkrsdmtgal ssvntkemak rtttnpaeal qgkvagvnil
      241 ksggnagagv sikirgiktf gdneplyivd gfpgdinsvn pqdiesmeil kdgaaaaiyg
      301 svaangvvli ttkngkkget kvdfssylsf tqvskdldll daegykkvhk mmyenagrkl
      361 payithetgv ntdwqdaiqr kglaqsymvs lrggaekgqy svsynhadek gifignserh
      421 diarmkvhat kgiidldanv dfkytkghqp qyslkeaymi splvpiynen ekygfgltnf
      481 dgipnnrnvv addhykknty kkyhttanaa ltfnffpwln fktsygyrge heidnshypd
      541 yiadpksqnk ypnsyeyray wqeqvfenvl sfnkqiqkhs inamlgtsln mikynwesvs
      601 vegktnvnev ingqlstsdk pagfldpnfp tisggvggty ygtgsyweyn rvsffgriny
      661 nfndrylfqf tfredgsskf ssdnrwgffp svavgwrise epffpknsvv snlkfraswg
      721 qlgnenalgk ydfltriasy ndmymgyvqg agsnpwtgsi artlenlplk wettdtknig
      781 fdfglfgnhl ngnvnyylne trdllitrri apsagldnpt lnvgkmrnqg felelnwndk
      841 isdfeynvgf nistiankvv alanedqtiy gvglkygteh fptqtkvgkp igafylyqad
      901 gifqsleevq ahknskgell qpnaqpgdvr fkdmngdgvi deddktysgt giakveanln
      961 lgasykgfdf savigsafgn kiyngiryyy egmnsasnfl kttlnawtpt ntktdvprai
     1021 ygdpnqntre strflengdf vrlrqvqlgy tlpkalskqi ycdrirfyvs aenvftitgy
     1081 sganpefsqg vlnsgvdrft ypfsrsytvg aqvsf
//
LOCUS       WP_118255319            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118255319
VERSION     WP_118255319.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115402
     Region          24..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmtfia clflslgmal aqtqvsgkvt saedgepiig asikvvgtkt gavtdvdgnf
       61 slnvpagakl evtylgmlpq tvkagqkmki vleadnktld evvvtamgis rdkkalgyas
      121 qklgsedlni agtsslasam qgkltgvdir qssgapgass qivirgarsf sgdntplyvv
      181 dgmpiassad ydtgasvtga dkanrsidin pddiesidvl kgqaasalyg irasngviii
      241 ttkrgkangg rpqitfstdl saqtvskkfd rqniyaqgng inaynpsssm nwgpkiadla
      301 ndatyggntd naytqkygkh egmyynpkya dagldgwatp qiydnvgdff dtgftqnsnl
      361 sisqkngnma ysfgigdtyq kgiipstgmm rttargavdf einkqwktgf sanysstkit
      421 sapganggim nvvysapsey nlkgtpthap nnptsqilfr stsfnnpyww kdnnefkqht
      481 nrvfgnayle yrpnfgwdte rynlvireqa gldvyttnns dvyemgsaqn aggeienygv
      541 qhnifnnlft anftaklgad sawdfgallg sefnhdyqri wdydgtnflf ygqptmtntt
      601 vkplteeyka qertvgffgq lslsyanqvy ltvtgrndiv stmprnnrsf fypsvslgwi
      661 ftelpalknn hilsygklra sfaqvgqagh yyanyyyvpg ygsgmygitp isyaingvss
      721 yvpyyvkydp nlkpqntvnw efgadlnffd nrlrleytas yqdikdqifd vptagstgyq
      781 ylrtnagemt twshefaina siiqtkdwdl dlgvnftklt nkvksladgv esimlggfve
      841 pqvraqagyt ypniygvafq rdeqgrlllq dglpvgtags qnlgectpdf nmgfnlkarw
      901 krlslsatmd wqkggkmyng tlltlnyfga tkesipyheg tmvaegidia tgepnkvevs
      961 kqdywmaynn iteagiydrs flklrdvtls yqlpkfagid isvygfarnv llwskmkdld
     1021 pessqgngnm sgtferfsvp ntssfgggfk itf
//
LOCUS       WP_118255405            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Prevotellaceae].
ACCESSION   WP_118255405
VERSION     WP_118255405.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110962
     Region          24..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrhilfasv llastsafaq sgnvsgvvvd kmgnpvsgal veiqnnkfik aytdkngafe
       61 igasandelv idapdqskkt valngskeik vvmdyasrpv elgfgikqnv gestvsvasa
      121 sndefnkrss knignsllsg svlgltalqg tgdyasyeps fyvrglqsln gssplilvdg
      181 iernitylsp eevenvyvlk daaatalygy kgangvvniv tkrgkyktne ikftydhafn
      241 wearrpkfvn aydyavglne ayandgkspr ysdaelgyfk sgefpylypn vdwinetfkn
      301 ngssdiynlt frgggerlry ytnvnlisnl gfiahpkens gystqnkysk gsirtnldid
      361 ltsttklman isgtlmeasr pglssddlwg kiytvpaaaf pvkteaglwg gnttwtgyyn
      421 pvaltegray skahtrslfa dmtlsqdlsa vtdglsvwtr faydniaayw enhtreykyg
      481 mdtatewkdg kptafshytg gkdgtmseds kldwqnrnfn fgiganydht fgdhsissvl
      541 mwnyefrnwn gqnntqyrtt atlynhygyk eryladvsls latsnklapg hrtnfsptls
      601 aawvlskenf mqnvsfidfl klraswgiin ldyipaegyw nqtfgggnsy fvgkdnatss
      661 ggwsegrlas tnvmaeratk ynvgmdatvl vglnltvdgy yqrrdrqwvn aggkvssvlg
      721 asnryinggi vdswgvelga nyakeiakdl kltagvnytl akneikeeye epraydylkr
      781 tgnpvgqifg lqavgffkdq adidhspaqq faqckpgdik ykdqngdgii ngddvvkmgy
      841 nttcpeiyys fnlgleykgl gftatfqgaa nysayldtqs myrplvnntn igqyyfdnrw
      901 tsataetakf prlsaetndn nnrynsiwla drsflklrnv evyynfpksl lgatkfinna
      961 klyvrgvdll cfdhikeldp ecygatypvn rsvslglvlg f
//
LOCUS       WP_118255641             945 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118255641
VERSION     WP_118255641.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..945
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104888
     Region          35..944
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnkktiys altvvtalla qlpasaqesa dsamvnvafk kayqsdvlgg vstvnvrelt
       61 eknyntysld nmqgyvsgyn gsgmwgysna lvlidgvpre annvrpdeie disflkgaqa
      121 tvlygskaan gvvlittkrg kvndglsvkv nantgwnvak afpeylgsae ymtlyneafl
      181 ndggavnnlp ysaetiynya sgknpyryps vdfyssdyik kafnrsevsa eieggnqkar
      241 fyanvsyyrn gdnlnfgeak knytdrfnvr gnvdfvlsst inayvnanat fygaksantn
      301 nssyweqart frpnrvapli pvdmidpnak saltmigats niidgkyflg gssadltnvf
      361 gdiyasgtnv yhsrqfqfda glnfdlssvl kglsfhtmva idyataysts fnntyatfqp
      421 twanyngkdv ivglnnngtv dkksgaqnis gstdnqtiaf nahfdynrtf ndvhnvsaml
      481 vangyqqsks aeyhkvsnan lglqlsynyd hkyyadfala tpwsaklpsa krlgvspsat
      541 lgwrlskekf mensffddlt lsasytdmkt dlgiddyymy lgtyqsggww dwnggsghsa
      601 mqskrgsnde lsylhrkeis atvhaevlnk alsfdasyfl skwtngilea rnqvpsylfs
      661 yypessfvpy infnedkrsg fdfavnykkq fgdfgfgvga nvtyytteat krddsqyadt
      721 yqyrqgqpld aiwgyeclgf fqdendikns ptqiiggtir pgdlkykdqn gdnvidskdq
      781 vylgkggwyg tpttigmnlt lkykgftlfm lgtgnfgaha vknstyfwvg gsakytaemr
      841 grwtketaat atfprlttea gtnnyqtsdf wmystdridl qkvqlsydfp kamfmksfvr
      901 glqlfvngns lltiakerkl mdmnvnnsgs aplnrfysig akvsf
//
LOCUS       WP_118255674             941 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118255674
VERSION     WP_118255674.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 941)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..941
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104262
     Region          52..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnknavlm amallslpvs aqvkidsiap hryaaqsidv ganvnfsreq stsavsvits
       61 estnkrsakn ignsilgqgs glislqnsgn yaginptfyi rgmqsldgnt plfvvdgier
      121 diqyisaeev esvsvlkdaa atalygykga ngvvlittkr gkfnskeikv nldhainfma
      181 hkpkfvdaqt yakamneaya ndgfenpryt qeevdafgss kypylypnvn wvdetfrnhs
      241 vtnmlnasft gggekfkyya lldlqydngf vknpdthegy stnnkyvkgn lrmnmdmils
      301 knttmkvnll gvlaesnapg nsaklwdmvy glpsaafavk dedgkwggns twagtvnpva
      361 qsqdagysrn hnrgiytdlt irqelpavlk glavqgriay dhfsniyeny sktyvygspt
      421 vvdwldgkpq lgkaftggse sdlgasistn sftrrfhada sadyqntfga hsiysqlkyd
      481 yefsdefain stlyrqnisw ythyglldry fldlaliesg snrlapgskw alsptvsaaw
      541 vlskenfmkn lnwvdflklr asygiiqtdi lpesgwmyym qqyqttggty pfnsgfqsdf
      601 grtyldaiat sglthekaak fnagvdatlf ggldfsfdgf yqrrsniwvs tagkysselg
      661 vdapyegdgi vdswgweasl dynkqigdvk fniganidyy rsqikeqdea pklypnlvst
      721 ghrvsqlfgy kaigffkdqa didaskpqll gstprpgdik yedvngdgqi dtndktaigy
      781 stvapeiyyn ihlgvewkgl gidamfqgtg rysgvlstks mykplvgntt isqyyydnrw
      841 tpetastakf palsstsnan nyntntlwmf drsffklrni evyynfpkal laktnllnaa
      901 klyvrgvdlf sfdhldesdp evfgatnpln rsivaglsvt f
//
LOCUS       WP_118255717            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118255717
VERSION     WP_118255717.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116484
     Region          24..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvkrltmlmg glilstgial aqttvtgkvv sqedgepvig asvrivgtkt gtatdvdgnf
       61 tlpnaskdav leisylgmqt ktmkasakmk iilasdarnl devvvtalgm krsektlgya
      121 astanaselt vaksgslmsg lqgkmagvqi sgggvtgtsq kvvirgissv ssnnplyivd
      181 gvpinndrlg dnsvdfgsga gdinpedies vtvlkgasat alygsraang vimittkkpq
      241 gnkkasityd gsltftdvlr vpmtqnlfgq gwgswsneen gswgprldgr ehwygstgls
      301 ngetltkpfs yvknnirdfy qvgkewnnnv slrygdekvg ivasygnvss ngitpndgdt
      361 yhrntfslrg yanidrfhld mslnyvrkdm rrsrdmymel lqgasdvrft dmkdynlern
      421 nvdnyytlya tnpyymvdnf ystyqddriy gklelsydit kdikvigrfg gdytnykter
      481 iepriiyteg syqatgngtt vgnqgyysky rsqrgqidas llltgnhtfg dfsvgatlgw
      541 nlnqrnydnv ggyneqldip gwnslsntss ysitdtdswn rrllgllgqv elgykdwafl
      601 nlsarndwss tlpmgdnsff ygganvsvll nqaipalknv kqidllkvra aigqtgndad
      661 vymtnsyyrp fqsyytylpi sgvsglteyn rlpnkslkpe itteyelgln gtffgnrlsf
      721 dvayydrttk nqiisatlap etgytsntrn vgklqnkgie amvnftpirt kdwewsvgat
      781 yaknwskvke lwdgldeyti pvgttstgly ssmrgvsyvl kvgepigifk lpatqkvtdk
      841 nspyygyriv ngngflqsst tdydylgssq pdfvmgftth lkwknlslaa tgdwhkgglm
      901 ysetsyithf ngnstetvfn erdafvyphs vkivggeyve nnipvasnym nyvqgnysyn
      961 pevrrdfvvs rsyfklrela ltydfpktit salkmqklsl slvghnllli tpkhqnyidp
     1021 essnfgndis sefgetmgsv strnyginlk vvf
//
LOCUS       WP_118258356            1197 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118258356
VERSION     WP_118258356.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1197
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134716
     Region          131..1196
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknwdllln fwqyrkskff lrmkismill lvgvmhlsan tfsqtkvsln mkdatvqevf
       61 snlekmtnyt flykldlvnk cgkvnvdatd qdfsqlllel lnplglsfti ddqvvvitas
      121 kakddvkkel tikgrvfmkd stgvpgatvi lkgtstgvit nmageftiti pytespvlif
      181 sflgmktrev ryvgqkemmv lmeedvkamd evivtgyqri rksdmvgstn sikredmffn
      241 gtnsieqmlq gklpgmvvmn tsglvgkrqk vrvrgtstll gnqepvwvvd giiqedplpf
      301 ktreldalgn isqdnfdmvk dfvgnaiswl npndieditv lkdasatvmy gvkaangvil
      361 iktkqgqagr msvnysgdis itprltyekm nlmnskervd vsreiyergl tsdnrplesi
      421 gyegalgryl akeisydefn devkklestn tdwfkllfrn svsmnhslsi sggtdkisyy
      481 gsvnatinrg tsignestsy saaiginakf gekvnlglri ngstsetdgy yqvdpynyas
      541 ttsrvipcfe ngekffykdk sgylynilhe ismtgntntn rsmgvsasfr wdiltglqfe
      601 stfglntsni vgesyadeqs hyiteirkye fgtqrpaddl yqrsplphgg elnttedrnf
      661 nytwrntlsy nyvlaekhrf slmvgqecrs nkydgvasti ygyfpgrgks vslpptiikn
      721 qngedqrndl ldkyktvvtd rksnyigyfa sftygfdery iltasfrsda snrfgqdtrn
      781 rflpvwsigg rwnvhyepwm qnqqvisdln frvsygwqgn vaenygpdli arigsgteti
      841 dqnrtgeymm fikslpygnl rwektktinl gtdfglfqnk itwtieyynk ktedmiveke
      901 vpyaygvtsm pinggsmtnq gievsvgftp vrtnnftwsm sinssknfne vkstvnenen
      961 wraaasgsln kagyavssfw afdfsglnpk tgsaefnips veenpagqtd attfmkymgt
     1021 lepdftggvs msfrykslsl sssfnlqigg kkflyevfde sivtstpsay vnlpkeltkr
     1081 wrkpgdetft dipalsstea syyklpngas eyaprlynys dvrvvnasfl rcnalslnyt
     1141 lpekwvkkmy lknlsfsasv snpfiivske fkgmdpevat gsqpisrtys fginvsl
//
LOCUS       WP_118258333            1144 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118258333
VERSION     WP_118258333.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1144
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127301
     Region          33..1143
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkplyikfti twilifliys issslyaqnk tlkvtgtvyd esgitlpsvt itvkgqkgvg
       61 vlsdndgkft isvpegatlv fsfvgmksqe vivnakqipy kvilqedsks leevvvtgyq
      121 tlkkhevvgs tytvkgddvr iaginridaa lqgmipgvsi tipsgligsa pqvrvrgtst
      181 vignaspvwv idgiiqedpl pfagaqlndi lssgdlnsam asisgssisg lnpddiesit
      241 flkdasatai ygvkaangvi vittkrgsnt dgrinvnfrt dismtprrty aqtdqmnsad
      301 rialskeiie sgvpfskfpq hvgyegaylq linkeismne fnqkvtqmek qntnwlklls
      361 rnavsqnysl slsggndkln fygsvgfnks lssykgndqs nktinfsvda klrdnlrtkf
      421 qfsasqsetd ayytgvnped yalntsriia pnewyvines kayfqmddgs aiqreirynf
      481 lnelkhtgne nkntkfqitg nliwnitpei kyelttaftr nsseaniwad dhsyavskir
      541 ganygelvtg endswlslas vlpyggilny nntnqqsytv rnqlnygkil deegnhalni
      601 algheirgns yigqqgteyg ympdrgksvd ydysqqankd yildiypdin yretanvpsy
      661 rerhstkltd qtenylsyya tlgytystky tlsfsfrqda snkfgqntnn rfnpvlsagi
      721 rwnvseenfm rrfgwlsnlt lkasygtqgk apdispnlia nfniapdilt geqylsiknl
      781 pnkdlkwekt rsfnggiels ildnriygsi dyyykktida itymnipien gtpnmavnng
      841 tiinkgydis ltvipvntkd frwsinatsg fnrneikdne dnitlgkitd gsviidgfal
      901 nsfwsfpyig lsdkgtpnfa iidqtpgvkt kvetgtlldy mvysgvkdpi fsgglstsfr
      961 ykqltlsasf nfqlghhkrl npfmksqsng grigqlripd peknastqln krwrqagdek
     1021 ytdipailas dedlsqylpd nslslsssge iyryqmynls dlrvvkadhl rcnsiclaya
     1081 lpknqldkik ltnltfaltv tdpfiikskk lgkqdpetls tsatnvipvv drqrkfslsi
     1141 slgf
//
LOCUS       WP_118258491            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118258491
VERSION     WP_118258491.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114111
     Region          42..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvdlvlkfd snlcgvvkwi llfccvcfpe ipvagesrss livitgevkd adgeplpgvt
       61 vvlkgtslgc vtgtdgkfrl eipeqkeivl lfrfvgmknq evtvtgarhi rvtmvkdmke
      121 lddvivtgyy tqaknaftge itrikgedll rvsptnllqa lailtpglri venneagsdp
      181 nvvpeilirg assimtkgqe gvnaplimld gveisvedly dldiydieqi lvlkdasaav
      241 lygekaangv ilverargks dkprfsynft pmfsfpdlts lrlcdaeekl elerlaglyd
      301 rvdgsldpay dyklenirrg vntdwttkpl rnafthshsa tmtgrgggie ykvtgrlsnt
      361 ygvmkgdyrr nygvnislsy rfardvvaty qlaytmtegk nspygsfary trlnpynpvy
      421 dedgeyirny yfdpvnrtme rqvnplynat lasfsrsqnk avtnylslrw dmdetlfitg
      481 nvsvrqgdtw nkvyvspeda sftlqeipqn kkgtytayst ettnwagklv lnyrlllnda
      541 gttvlslsag tdigkdksss mqvkaegfmk dkmtdikfas qyattrpvgg ekesaevgff
      601 angsldlmgr yfvnasykta gsskfgskhr fapvwstgig wnlheegfmn fdwlnvlrlr
      661 fsvgstanvt ftpyqaltty lydsdlihyg gmgavpitmg npdmkwqvtr kynwgltatf
      721 wkervnveas yyvnktrdal mpltlpssvg vssvlvnmgk lhnsgyefsi saqvvkrnnl
      781 lwmvmvngah vfdkltsisd alkaenmaay ygvkpqpmfv eggsqfgiya mrsagidpas
      841 gqevyikkng nytftydkne rvevgntnpm legslftsls yrgftlnvta aykfggdiyn
      901 ttlankveyi dpygnvdrra fterwkkpgd lvrflgipes vsdenryser fverdntfai
      961 tsimlnyefk pgylrkigik rlnlgigvad iarfssvkqe rgteypfqrs fhimfrptf
//
LOCUS       WP_118260108            1129 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118260108
VERSION     WP_118260108.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1129
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128571
     Region          69..120
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          139..1127
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkrivhll pkrrllktwl imrfivlfmc vsamqltaav ysqevkvtls vkdasfesvi
       61 rlleanteyt flyedrhiae igglnlnfrd tdikvvldkc lqgtnlsyrl mnnhtiviqr
      121 gvavdttkqk apqkmsvfgv vkdvkgevlp gvtirikntq lgfvtdidgk fkfdfpkqdt
      181 vilifsfvgy ktqefqvknd kpitivlked vtemdevvvt giftkakesy tgavttitak
      241 dlqrvgnrnl vssirnidps fniadnidig sdpnklpdit vrgsssldvg vrdlqedsrs
      301 tqstnqplfi mdgfeitler mmdldenqve sitllkdasa tamygtrgan gvvvivtkkp
      361 eagrirvtyk gslnieapdl tsydllnare klqyewaagl yentnanqtq elwdlynqrk
      421 mdaergvnty wlkypvrtgv ghkhslrfeg gdevyrysvg lsyndiagam kgsnrrtfng
      481 nvflsykykn ltfqndlqis snrsynspyg tfndfakins ywtpydeegn lvkvlenyyy
      541 lsllrtnfvy nplynaklps kdesrytqiq nnfaiewhil pelfvrgrlg itsktdrtdv
      601 yksakhtdfd kyteddygrk gsysygtgea fnyeadftln ysknfmekhq lyvglgynfa
      661 qeknefftil aegisninmd flgmasmyek dghpqssegf srrmggianv nytydrryfv
      721 dasfkiegss kfgsdnryap fwsvgigwnl hheafmmdnn llnvarlkls ygtsgsqafn
      781 syqamttfkd yggssyqgwy gvylmamgns dlgwqktkql nvgaeleffn gririnadyy
      841 nkvtddllsd itlpsssgfg sykanvgqva ntgvelgvnv yvfrdtkrdl twliggtlah
      901 nkneikkisn sleflndqms sedggnpsfm yeegqsmnti favkskgidp sngkeiyikk
      961 dgtetytwda kdkvpcgine pkiwgnlntm frykgitlna ifgyryggqm ynytlvskve
     1021 niypfdnadk rvlydrwknp gdnaffkgvr dftttnatsr fvmdentlec rsislgydwe
     1081 akwldqvgis yltitgymed vfrissikqe rglsypfsrk fsvslsvrf
//
LOCUS       WP_118260185            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118260185
VERSION     WP_118260185.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116067
     Region          52..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktydrkvf trkllsdrrt vavtirlfmi lllgfplltr agtvdptrvg nrevrgkvvd
       61 ekklpipgvs vrlggtslgt atdvdgkfkl lvpadtatlv vsfigmktev vkiprlkage
      121 eqkeltivlr eedvkledvv vtgiftrkke sftgsassys aaelktmgtq nilqslktld
      181 pafailednq fgsdpnrlpn meirgkssml glrdeldadp nqplfildgf estlaaindl
      241 dinrvasiti lkdaastaiy gskaangviv vetvkpeagk lqvsytgnmn lsmpdlssyn
      301 lmnareklef erlagrfepa swsttsevel nrlyneklkv iesgvdtywl aeplrvgvnq
      361 khslyvqgge gnflfglgag yngvsgvmek sdrdvisgni dliyrmskfq fsnkfsltst
      421 dyrnpivafs eyaaanpyyk krnetgtiek wlennnffka anplwnasqn srdegknlal
      481 tnyfmaeyfp tvewrvrarl gltygnddte kfysrndtrf enmetikkge yrssntrtnq
      541 vegelsvtya kvlgkhrinl vvggnvssnk sltqgysavg fpdgdfsyps fsngypengt
      601 ptyyesvsrs vngyfntgys fddrylmdfs lrtsgssvfg tsrkynttws vglgwnlhke
      661 kfimdhvgwi dllklrasig npgnqsfdsa qslltysfqy gsmnyfglga mlaqignpdl
      721 kwqitvdkni gldvtlfnkr fsltadyyyk vtdpllikvs tplssgtety mtnageqvsq
      781 gltasvtyyi fqnfeerfsw mvranvrtqk tridkignkl stlnssgkgs ntvryydgad
      841 pddiwavksa gidpsngkel fyakdgsyty dfsyddevic gntrpdvegv igsslnwkgf
      901 svslnfryqm gadvfnealy skvenisrsd lnknqdkral yerwqeegdi vrfkniasae
      961 ttpmssrfvq eenvltlesv ylgyefydgw ikklglsslk fqvsmrdvfr astirsergi
     1021 sypfarsmea glsfnf
//
LOCUS       WP_118260510            1174 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118260510
VERSION     WP_118260510.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1174)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1174)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1174)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1174
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1174
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131662
     Region          128..1173
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkqsfyyf ygkknllkim rllfilmtmt smtisangfs qeqrvtldvk nvgamelfkq
       61 iqketnlffv yndadlisfn nlsvsakdea vdvllnrvft glkflfeenv iivkptvtkd
      121 ekkevkkfvi kgkvvdekkq plpgvtvrld sttvgcatda qgtftlalpv etgrlifsfv
      181 gfkqeikkfk agdellvvlk edvsdldevt viaygernkr eligsvssvk akdleevpsa
      241 slqnllqghm agvevsnisg apggggsrvi vrgynslmng ttsgeplyvv dgvpihsfts
      301 pvtgtntlae idpatiesve vlkdaasaai ygsrasngvi littkkgkvg rgdfqanvsy
      361 sysvlpktpe qiigngerrw wlnaarnyrl sgnfgnpmtg dnwqlpksyy eayannagty
      421 dyfwgnghsl endgygyips iqdslnpfyn natnwwkqvf rhgkiinanl qssggnervt
      481 ylvgggwyqe egimygsefk ranlisnvnm kprknlslda rlylsysdrs rgtssglgga
      541 siekltadpk gtssllpaeg evkerllqml nskvdkgysy nirtslnlgy efiaglklta
      601 sisanysear snsfrpsfld qqnnlsesvg qmegnmilqn eellsyrfsl kekhnfdllf
      661 gfsyirtsmn slygsgkgsp sdkihyvvdg fptketiage vvplqkyssd feekvqvsgf
      721 griaynfkqk ylteftlrrd gssvfgedvr watfpsvavg wafseeqfmd klwwlsygki
      781 raswgtsgqe fnqpylahgt yvlgdlflgg vgmdpatifn ksltweesdq ydlgldvdlf
      841 dyrlkfkldy yykysksvlw naplpgsvyy fnsawqnale vsneglelem vadilretkv
      901 swrarfnisr nwnrfeksys gldvpgntnp yvigrslfgf yvyknlgmiq naedvpsyfd
      961 qnmyqnalya nsygttyreg myqladlngd gridgdndry yaastlplas ggfaneliwk
     1021 gfdlnvlftf sfgrkminrl kkgglvfdtk fgpvfqdyrn ltfwqqpgde tdyprieaay
     1081 agytgqfdaf tdkdietvgf vrlkqltlgy nvpkeimkki glesgrvfft genlflitny
     1141 sgvdpetvdp isgfdnfdny plarkltlgl tikf
//
LOCUS       WP_118260203            1175 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118260203
VERSION     WP_118260203.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1175)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1175)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1175)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1175
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133181
     Region          49..116
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          128..1174
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maillskkrs idrnvsrriv kmfliqfvfc lcfftsiasg vtqnrvvnld fenvelskal
       61 kslseaanck fvfnyddlnn ykvsaklenk sveecldill arvpfkysqe gelivisyks
      121 ndekkiykvr gvvkdetgmp lpgvaviqkg ttlgaatdvd grfefqltek nvtlvfsfvg
      181 mktkellydg sdklldvtme eevemlgevv atgyqtisre rstgsvtilk aedlrkvqgt
      241 slvskieglt pglstygdkl emrgtssfav sstpllvvdg ivmnqglnsi npddvetitv
      301 lkdaaatsly gvrasngviv ittkkgksdk vnfdlsagfy inplpklsym dyastsdiid
      361 felefllnnd lykqnpgdyf ddknqttssk pytrieryyy elykgnmtqv qvdekinamr
      421 kndyrkeark lmsetaltqn ynlsiskgge ksnlyfslry edngkylksd vasqysiylk
      481 nelnltdwft ltygantyia kmkesmsgis yldvmpyekv ltdegnpvyq ygynfyrsie
      541 ideteglefm gfnlneernn nmqktnslyv rlfadadfkl wkgldlgvkf qyerkninik
      601 qfdeadsykm relvnrytsg svgnfvynlp qgghlsennq neeyfnfraq lnyqttmgek
      661 hdltvlagae irqdewngtm serygyddkk ltykqvdwat laqgvvgqls sasltfserl
      721 qvtstkhryv sayanagyty dskyslnasv rveqadlfgt dpkyryrplw svgagwlmtr
      781 esflndiawl dmlklrvtyg itgnvdqsss pyllgayits pytqnsltsi ltppnpmlrw
      841 ektstlnigt dfsllgrlkg slefyrryss dllanktldp slgfesarvn ngamrntgle
      901 islsydwlnn kewalnttlt aannknkimk vgftpsnald mlrypgsnyl kgdtynsiya
      961 yryaglteng dpsvydenge ikanepvrni nalvnvgqlt pkwngalavn lrwktwefft
     1021 kfvyytghsl rndvtplyst ygslqststy gsingamhkd mvnrwtennk dtdipamrsa
     1081 tsadsnrenl wryadshvls asfikcrnig vsysfpknll qkinlqnvvi raqvdnpfyw
     1141 aandegidpe sfnanegmrt qfmmptysvg lninf
//
LOCUS       WP_118260445            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118260445
VERSION     WP_118260445.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124389
     Region          109..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrltivflfc fmlggnatim aqyrlnmkmg ettfeelfqe irkqtgcivm ynndmlnkne
       61 kvdanfgkie leellekils dkgltfeinr efvilmkapq kreeqkkvti tgivkdkqge
      121 sligvtvlvk gtsigavtds lgrykitlpe qqdlvlifsf igmqskevki nnqkeinvtl
      181 eedietleev vvstgyynrk kesytgatts fagdklrmvs sgnvlstlsv ldpsfklldn
      241 iemgsdpnti peftirgggs lqseyenspn mptfildgfe vnaekifdld pnrvasitil
      301 kdaaataiyg srasngvvvv etvepqagkl rlnytfsgdf sfadlsvydl mnatekleye
      361 rlaklythsn iemgdrytdl ynqrlkwvqe gidtdwlskp ikdlgfghkh fllieggdss
      421 iryalsvnyn ktdgvmkksg rrtvgigstl qynyknlrfi ndltysnvkg tnspygsftt
      481 ytyqnpyfhp ydengnvkqy lyeptldgdv lvtnplynaa kktrnestys efnnnfsiew
      541 nimegmtlrg kfslnskqes tddfkpatht dfattqykgs yqkgeqktft ydanivfnya
      601 rsfikhninl aavwnvresn idsysvtavn ypneqmdhfg mgtafqdgak pvgdyevsrl
      661 mgfagnvnyg wdnrylldls irtdgssvyg anqrwgtfgs igiawnihre kwfensrivn
      721 nlklrgsigs tggqnfypfq sirmfsykdd lvdgityngs igallksygn tdlkwqknlk
      781 rnigldfalf tsrlsgyvnf ykedskalli dvllapstgf dsykdnlgev enqgietnir
      841 gsvirdtgke lqwdlfvslm snrnrllkln dalaaynrmq ddkvnnaddd qksnrpvvry
      901 qkgksinaiw aneslgidpn sgqeifldqq gnkvdkwstd nykplgctdp dvegsfgtmf
      961 mykgfqlnaf fkysiggdiy nqtlvdkven vnpknnadrr vlydrwkeag diarfkaidn
     1021 tettmptsrf iekenyvqls slsvsyrfpv eklrrlgmes lkvtaigndi frastvkmer
     1081 gtvypfarty tlslqvtf
//
LOCUS       WP_118260601            1186 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118260601
VERSION     WP_118260601.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1186)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1186)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1186)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1186
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1186
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=135273
     Region          127..1185
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksgeckgn lrsaqkifrv mkmmcflmfv llvqvrgdvv aqnqvvsvdm kncsveeflr
       61 eikeqtgirf mykseyvkai prfdvrvedr evmdlleevf agkgikclyd ngviiltkha
      121 gkeervtvkg vvkdsrgaal pgvtvvlkgt ttgvatgiag dfvitlpkrd slilvfsfvg
      181 mqtkevrwrg epelrvvled dvsemdevvv tgyqtitrek vtgaastisa rqleerytan
      241 ildnlegrva glvtygdktm irgtsslyve tapllvvdgl pmegkiedln pydiesvtvl
      301 kdaaaaaiyg arasngiivi ttkkakqmgs teiefsgnls ifekknldyh dnfymspaeh
      361 vdvesdywdy yffrnrdead pissfasayn kssyitpiqh ayyqyatkqi dkaelesvka
      421 dlrknnfake fekhvlrrqf lqqynlafrt rtekfnsnlv inyrrdnngi vhsydnqvni
      481 ayrafydmkk wlsvnfgatg iiskikesas eyatnpfevp pytrllnddg synyystgmf
      541 nhyytkdded palktmnfnh leelgydqki tdrrnmryqg elvfkiidgl tvntsfiyet
      601 erqnisnyse adsyvmrmlr nyytqgpgqy lipenggklt tedtrgdywt argqlnlqrt
      661 faekhaidfl ggfefretrs kgtknlllgy ddmlqshgam tvdfpylknl ysanpyfanv
      721 yygsayykyi gnaidivpee hhryasgymn vtytydnryn afasfrkdya dlfganakfr
      781 gkplwsvgas wnlnreafmq divwlnnlkl rvsyggtgni yqgttsymta stgttnrytk
      841 qpmakvespa npnlkwekts tinvgidfsl fdhrlrgsvd wynkkgsdif sqktleptkg
      901 fssmnmnmad mtnngvemiv ssdlfrakke ggftwtaslt asynknkitk melqtmrame
      961 ltssgfkegy ptsalfsyry aglnqegvge rqdelgqpmy wtedgrkvfs idiqmeptga
     1021 lvysgqsdpk vtlamnnsfh ykgfslnfmm vyygghkmrc rqyapvwrln piypmadyyl
     1081 dawsptntdt dvpgigewcy tatttsvyld tdifvqpadf lkirnltlgy dvprevvhai
     1141 glnnlqvrfq idnlpalwkk nkvgidpetm girkqmtyvl glnfnf
//
LOCUS       WP_118261225            1200 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118261225
VERSION     WP_118261225.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1200)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1200)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1200)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1200
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1200
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134114
     Region          113..1199
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkrtmmys lvcflflfvf vsgniygqng kvnlnykdas fvevindfhe qtgvkfmynl
       61 ekvkdkkckd limkdmpvkd airvvlkyfg ltysmiegvv vvkelgenlq tgktvtgtvc
      121 dengellpgv tvlvkgttlg vatdvngnfk vtfpgetent lifsfvgmrt kmvkctddkp
      181 lkitmqmdaa qleevvvfdd gynrlprkdm vgayttvkae dimmpayqsv dqmlqgkiag
      241 lqvintssrv gatpqikirg tstllgnksp lwvvdgviqe eplsidvssq ltgnmadlig
      301 neiswlnpld ienvtvlkda sataiygsra sngvivittk rgakerasvr ysthfsvrqr
      361 shyglydfmn skeriqfske aydagaryqq eplpqkytye glmamfndrq iteqefmvqm
      421 ekletvntdw fdlltrnsis qnhnlsvsgg sqkvtynasv gysknagiei gnendqftsr
      481 lnvfaelnkr lsislnlngs irnsdgygpg vnpysyalnt sravpayeed gslayyknyy
      541 tyqlnpvlgg yntysynifn emensysknk gvnfnvsatl dfkildwlsw qatgsltqsm
      601 ndsegyagek tstveclyrg ypynseksgs ekfnaallpw ggtlttsnse glslnmshrl
      661 afsktfnedh rinamlgmel rsskqrsngn tvwgyvperg eiivspslpt evvpvgggth
      721 ydvqwgalnn lfdggwrktt trtnymsffg tlayslknry vfnfnvrsda snrfgedqnk
      781 kfdptwsagf swkvaeepfm renvewlelm nlratygvqg yvitsispel iasyegilrs
      841 yneyylsiss lpnphlkweq tktwnfgldl slfgvsmsve yygrrtsaia rtdvaqeygv
      901 sslllnggil tnhgievtln ftpykkddfa wtvgltsarn wnrsklsdlt akadgvnhsd
      961 flsgnssrpl kkgkplaafw sfsfagldpe ngyplfnyid nnaseaygsq dvdplsflvy
     1021 sgssepvfdg glntrlrwkg lsfganfaia lgakkrlpnp yssftqgkip spfsnisktl
     1081 nkrwkkkgde tfthipaiyt svediynlyl pnglymsryd mwaqsdvmvv dasylrctql
     1141 slaynfphnl cskiglssis vnaninnlfv iaskkwngyd pelgdsitpk iyslglsvgf
//
LOCUS       WP_118261240            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118261240
VERSION     WP_118261240.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124216
     Region          33..99
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          118..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrvleitf clivfcfmfn kghaqakrit tkfeneslvs vlekleaisg rdffyqrdsv
       61 mqgvmindsf agatlegild kilngngfry eiegnvvlin hgreltdvpk rilgqegkki
      121 vgrvtdknge plpgvtvlvk ntrlgvvtdv dgkfeltlpg lggvlqfsfi gmkgcevqik
      181 dfkplqvvle edvtemeevv vtgifnrpre sftgavktvs akelknfrgq nllstlrnid
      241 psinmvidnt lgsnpnreve itirgnsslp tsleeaenda anrlnaplvi vdgfevtiqk
      301 lqdfndeeie sinilkdasa taiygargan gviviktkdp qpgklkvffq ggvnleipdl
      361 ssydlmnakd klslermvgl ydagtpyeda llkqlynerl tdalmgetew iripvrvgig
      421 rrlnlrlegg seefrwsasl snnltkgvmk gsernasnas itlsynyknl ifrnvvsfdt
      481 ykadngtygs fatyarlnty frakdeegrl ikswtnfpgy sdisnplvda rldgenysra
      541 stirnifsid wtiarglslk gqlgisksfs nkhkylpaeh ssfsypgidt fakgtydytt
      601 gegfaidgnl tlnystvlne khsiytgvya timqskdfay sfsvqgllnk nfkdfanals
      661 yktgtvpsgt dnraasvgft gninytydsr yyidasirvd gssqfgrdkr fapfwslglg
      721 wnihnekfmd khalfstfrl rlslgesgsq qfapyqarsm ysfstesryl vwtstelmgl
      781 gneklswqtt iqynagmdve lfngrllagv dcfykktrdl lstidlklvh gfngytenig
      841 stenvgyeam lggyilrnsg vgltwnvtgk laytrnkilt lsdelkrete krrqtseygt
      901 lfyegrsqns iyavrslgin padgkelfld aegnvtetwd payrvycgvg eptyrgslns
      961 lisyknlsfn lsfgfhwggk qynstlldkv evpvglegsg veqsiinnvd nrvfterwqk
     1021 pgdykffkgy sdkatrsssr fvmddqafql qslslqygwr tgfvqkvlha etvnvsvnms
     1081 dlfylssikr ergtdypfan niqfalsvif
//
LOCUS       WP_118261431            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118261431
VERSION     WP_118261431.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115438
     Region          52..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mcvrvfvlll cllsiqggrl fagkrkcfpe ilrvdslvre ekcvvvkgvv cdaqgeaivg
       61 vniiekgtmn gvttdrrgkf sleidlhgtl ivsfvgyrtr iipvegrtdf vitlehdyil
      121 lddvivtalg lqkkesalsy aaiqvdkdel vrvknpnmiv almgkvagmq vnrsssgmgg
      181 avkvvmrgnr svagnnqply vidgvpmlne sseqpytaig gtadagnrda gdgisnlnpe
      241 diesisilkg apaaalygtq aangvilitt kkglagkqev aftssvafdk ammlpklqnh
      301 ygmsdeiesw gerenittgn pipsffrtgv taihslsfmt gnervqtyfs yantmgkgil
      361 gkhelskhni nfretatfye grlkidgnvn llsqhvknrp vpggfymnpl vglyrfprgm
      421 diteykehfe vwseerhlnv qnwhaptedf eqnpywiqer itsrdqrtra ivslalnlki
      481 tncfsvqarg nvdyvndkfr qkyyastapa lagnngryid sgneqvqtyg dvigtykgkf
      541 sdfsldvslg vsisrkkane lrydsktasl kfanvfnian inmntsayis eqidairemq
      601 slfittqigf rdylfldvsa rndwsstlay tsresrgffy psigvsclmn rvlklpeqvt
      661 sgkvrvawsk vgndiplyit npvahvlagg giqasdaasf eemkpemsls mevgtewkff
      721 dsrlhidfty yqthtknqff klpakdgdey ayryvnagni qntgvelmie gtpveiknfs
      781 wktginyafn knkvvrlhve lpvfqygpyg fsssyamklk kggsfgdiyg kafkrdtdgk
      841 ilyetdgerq glpmiegdgn tvkvgnanpd ftlgwtnafs wkglelsllv dgryggkvls
      901 qtqadmdmyg vtkvtgdard rgyvilegek itnvkgfyks ivggragvte yymydatnfr
      961 lrelalgytf pkrwmeatkf frdvqlafta rnlffiykea pfdpdlilst gndnqaievy
     1021 gmpttrsmgf slrvmf
//
LOCUS       WP_118261658             949 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118261658
VERSION     WP_118261658.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..949
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106626
     Region          38..948
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknrliipa llaflslqgy aqelndsits gkpakysdev veigyhkaqr leestssist
       61 vynedfnkrs aknianslfg ygtglttlqg sgryadaept ffirglqsls tnnplilvdg
      121 ierditdvtp eevetvtilk daaavaiygh kgingvvnit tkrgiyntre ikftydhgfg
      181 wqarkpkfvd sysyanamne alandgltar ytqdelnafr sgqypylyan vdwlgetyrd
      241 mdatniynis frggaskfry yamanlttnk gfianpymnd gystqdqysr anlrtnldid
      301 ltektklkln vlgilsetrt pgangqggan lwdmiytlps aafparleng twggsatwag
      361 tknplavsqa aaytkfhert lfadmtltqd lssitpglga sgmlsydnya qywenhsktf
      421 vygsnsvtaw engvpsstty ytdgkessms sdakciaftr vfnfaatlfy dkqinkdnki
      481 ysqlkwdyey rntkgtdqtw yrqnasfyth ygykdkyfad lsvvasasnk lapghqwsis
      541 ptvglawvms kenfmkdlsw infmklrasf gvintdrlpl dddsevtnyw eqtyggggyy
      601 pfdtnysvgt qswslgrlas lnsthekayk ynfgldasmf ngldvsfday yerrsdiwvs
      661 ssghyssvlg ftapyenggi vdswgveiga nyrkkiadit lniganfala kneiieqmee
      721 prmydnlitt gkplkqtygm evigyfkdqa dienspkqsf gdvkpgdiky kdvngdniid
      781 andkvaighs ttapeiyysf nlgaewkglg fdamfqgtgr ysavlntksl ywplinntti
      841 sqeyydnrwt penqdakypr lssqsyenny qtntlwladr sflklrsiel yykfpqiwvk
      901 kskilsnaki yvrgvdllcf dkiniadpev ygatypltrs vvagltigf
//
LOCUS       WP_118261611            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118261611
VERSION     WP_118261611.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116219
     Region          52..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktydrkvf krkllsdrrt vtvitrlfmi lllgfplltr agtvdstrva sreargkvvd
       61 errqpipgvs vrlggtsmgt atdvdgkfkl lvpvdtatlv vsfigmktev vkiprlragv
      121 eqkeltivlr eedvkledvv vtgiftrkke sftgsastys aaelktmgtr nilqglktld
      181 pafailednq fgsdpnrlpn meirgkssml glrdeldadp nqplfildgf estlaaindl
      241 dinrvasiti lkdaastaiy gskaangviv vetvkpeagk lqvsytgnmn fsmpdlssyn
      301 lmnareklef erlagryepv nwsttnevvl nklyneklkv iesgvdtywl aeplrvgvnq
      361 khslyvqgge gnflfglgag yngisgvmek serdvisgni dliyrmpkfq fsnkfsltst
      421 hlknpivafs ayaaanpyyk kyneegtvdk wleyndyfka snplwnasqn srdegknlll
      481 snyfmaeyfp ttewrvrarl gltygnddte kfysrndtry envettkkge fysnnvrtnq
      541 veaevsvtya kmlgrhrinl vaggnissnk sltqgysavg fpdgdfsyps fsngypeygt
      601 payyesvsrs vngyfnagya fddrylmdfs lrtsgssvfg tsrkynttws vglgwnlhke
      661 kfimdhvawi nvlklrasig npgnqsfdsa qslltyafqf gsmnyfglga elsqvgnpdl
      721 ewqitvdkni gldvtlfnkr fsltadyyyk vtdpllikvs tplssgtaty mtnageqvsq
      781 gftasvsyyv fqnfekrfsw mvranvrtqk nridkignkl stlnangkge ntvryydgad
      841 pddiwavksa gidpsngkel fyakdgsyty dfsyddevvc gntrpdvegv igsslnwkgf
      901 svslnfryqm gadvfnealy nkvenisknd lnknqdrral yerwqevgdi vhfkdiasae
      961 ttpmssrfvq eenvltlesi yvgyefydgw ikklglsslk iqasmrdvfr astirsergi
     1021 aypfarsmea glsfnf
//
LOCUS       WP_118261682            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118261682
VERSION     WP_118261682.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          21..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 aayavanpgv tdvkitqqtg tctgvvvdat getvigasvv vkgttngtit gidgdfslsg
       61 vkqgdviqvs fvgyltqeik fkgeslkiil qedsqtlqev vvvgyggvqk aktmtasaat
      121 vkmselaklp vasmseglgg rvtgvvtqqa sgapgenari wirggenily viddvvmdsg
      181 qgneffnrlr pddiasmsil kdaaatavyg praangvvvi atkrgqegap titlnqkvsi
      241 mtpayrpkgl ssyeyalarn eaelasfqes ptfndtelsk yymgdlwqkg ygfeeirnlv
      301 nerynlgysl qdindlfdpl ktqgkniqdy yssydpwdmf dhtqpmyqtn vslrgggeri
      361 kyysslgymk qngvsdkysy eqvnmilntd amllsdkslk ftfnlngnts nnnkpadgeg
      421 vfnnamygdw mpkrpaawst glprkgsvea qlnngfnnte syrfqmnaal kwsvpwvegl
      481 saqaslnftt syyhqrhfnh dqegvydnpy atavssynpe nanlyekwnk yklltgifqi
      541 dytrsfgkhn lsamvnyqsq vrksnwtdak kkgypttlap qldlggtlvs aggsaeewgs
      601 asyigrftyd ydnkylfqys anyngslsys pdkrwgyfqa fslgwvmsde vwfknlvnpn
      661 ivnmiklrgg fglvgnevgs pfsfltqyaq ssnrilfgen masnvgwyes dvannlqwss
      721 skqygigldf gflkdrltgs fdtflylnkg dvmdmtddmi rvdilgmpnt pkinapytts
      781 rkggfevsln wqdkigkvgy rvgvnysywd ervtrhsssd sdwwtptfdn igkrpyvtng
      841 esitypyglk tnglhgswqn mynsllhann nmtlgtpalv dlngdgrvnd yyvfnaegst
      901 phtqfgvtlg adwngfdlel ffqgatgarg ampsplrsqq symwnygqya fqnaytpsnp
      961 dvdaalptpv pegngfgysy idiwsfdasy lklknislry dlkrsvlknl pviqgldlsf
     1021 vvtnaftwtk ksyplkdlqd pefittgasi ynnngtlgsy ptqrsytlgv tvtl
//
LOCUS       WP_118268561             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Chromobacterium].
ACCESSION   WP_118268561
VERSION     WP_118268561.1
KEYWORDS    RefSeq.
SOURCE      Chromobacterium
  ORGANISM  Chromobacterium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Chromobacterium"
                     /db_xref="taxon:535"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38679
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhiaipaerl agehrvaatp dtvkklvagg havtvesgag laaaqpdaay qeagaviaad
       61 raaalaqadi vltvrplded giaalkdgat ligqlnpyhn hnlpalaakr vsafalellp
      121 rstraqsmdv lssqnniagy ravllatqhy prfmpmlmta agtvkparll ilgvgvaglq
      181 aiatgkrlga vveafdvrpa tkeqveslga kfievpmsee ekiansgvya kemsesyrqr
      241 qgelvakhak aadivittal ipgkpapkll saevveamkp gsvivdlaae tggncaltrp
      301 getvrldngv tvvgqtnlpg llaadassly aknlltflgl lltpeglnln ledeilsatl
      361 vthagqvrfp aad
//
LOCUS       WP_118274060            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            uniformis].
ACCESSION   WP_118274060
VERSION     WP_118274060.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides uniformis
  ORGANISM  Bacteroides uniformis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Bacteroides uniformis"
                     /db_xref="taxon:820"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114841
     Region          43..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyttlytli lglfsigwtd cpedfmermq rpghseiqls kvtisgrvld esgfplagat
       61 iqeketanga iadsegkftl vvadnavlrv sfigymsqdi eveghstfhi tlredmield
      121 nvivtalgie kkenslsyat dlikneeltr vkmpnlitsl tgksagvrvn qvssglgasa
      181 kvsirgirsv asdnqplyvi dgvpilnsts eqaysaiggt anagnrdggd gisnlnpedi
      241 esisilkgap aaalygsqaa ngvilittkk gqshgqrsvs fstslmfdna falpkmqnry
      301 gvsdgvdswg eranlpeydn lrdffstgvt sitsislshg neklqnyfsy anttghgiig
      361 khnlskhnlt fretsvllns rlkldgsmnl mrqvvknkpt vggfymnplv glyrfprged
      421 iayykenfev ydegrnlniq nwhtsyedfe qnpywitnri lskenrmhvi vslsanlkin
      481 dwlslhargn vdyindkvrq qfyastapal agangryiem dyqetqyygd ailmmkkqwd
      541 afslnaalga sindktvnst rydsktaslk yanvfnlani imngsagldq kidarrqlqs
      601 lfataqlgyn efvyldlsar ndwsstlayt sheksgffyp svgfslifnk lmtlprwvsl
      661 akirgaysmv gndipmfitn psshitagge flasdaapfk dmepemthsf eagiearflk
      721 nriglnatfy ktntrnqffk lptlsgdkya yryvnagniq nvgwevslda vplltnhfkw
      781 ktevnfstnc nkiislheal keflygptsf sssyamklvk ggsigdiygk afvrddagni
      841 vygtegdntg mplvegdgnt vkvgnanpkl ilgwnhmlsy knfsfyflvd crlggdilsq
      901 tqadmdmygv sevtarardk gyvmlegnri dnvkgfyknv vggragvtey ymydatnirl
      961 relsvgyqlp aawmektkvl kraqlsfsgr nlfffykkap fdpdlvlstg ndnqgievyg
     1021 mpttrswgfs lkcef
//
LOCUS       WP_118275163            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118275163
VERSION     WP_118275163.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113639
     Region          2..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvisyigmqt qevtikphvr vvmqsdtell devvvvaygt atkrsftgsa teikgdrian
       61 knpselskal tgevagvqvi stsgqpgsna sirirglgsv nssraplyvv dgipfgsdls
      121 gidpsdiest tvlkdatata lygsraangv illttkrgkk gktqveanvk ygintriipl
      181 ydtmesperf ieltwegikn kyqyaggrde aaaaamaskl lwgyddpqkg yqntgiykgy
      241 nmwstgdvid pstgkfkagv vrkftpekwe dyifrtgekv eanvkisggs dklshytsfg
      301 ylkdegyyig sdferfnars nlsqditswl ksnvnmaysy melnkpgqgd nmnngfqfin
      361 fmpsifpvfq rdadgnkikd nvvggylydy gmaegygrpy asgvnpagai qldkneyqsh
      421 sfngnamfea tflkdfkgtv nfglqylgtk nneltnpyyg daeglgrifk nmstffsfts
      481 nqilswkksf gvhnldafva hestfykssd nygqkskivr pnntewsnav imdymdsqty
      541 gfdmesyfgq irydyndkyf fhgtlrrdgs srfakgqkwg tfgsigaawa itnenfmkdv
      601 swlknlkykl swgvlgnqdf itnptiagyy pyndlytign lndeisfsfk ykgnpdltwe
      661 rsetwntgie fniadilege veyynkttkd mlflkqvsps lgyaqypvnd gkmvnkglef
      721 slvahlvktn disldlrvng ghyknkmtqm pmddttgkek pleiqgaygw skghslydfy
      781 ireyagvdpe tgmalynsyy nvkadgskdl itdmvtyqqn nkierlevek tsdynnatkk
      841 yvgksgiptl qggfgfdlav kgfelnttfs yslggyaydg vyatlmsnnt pgsgnwhndi
      901 enrwqkpgdi tdvprltsgy deytnasstr fitsrsylnl snvrlsytfp kkwmnrmnig
      961 slsvyvsgdn lmfisarkgf vsmagntvst dpnedsggsd rsqyaplsti mggikiqf
//
LOCUS       WP_118275165             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            uniformis].
ACCESSION   WP_118275165
VERSION     WP_118275165.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides uniformis
  ORGANISM  Bacteroides uniformis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Bacteroides uniformis"
                     /db_xref="taxon:820"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109366
     Region          2..979
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvisyigmkt qevvikpsvk vvmmpdteil devtvvaygt krkqdlvgsi ssvkneiisn
       61 sqatsvsnal egavaglqvv sssgqpgqda nivlrgigsi sasnnalivv dgvpfngkls
      121 dinptdiasv nvskdavsns lygsraaggv vmittktgrk dkvainfngs wgvaqraykd
      181 ydmatdpgef yrlswyglrn tywaagksie dsnlaasqdl lgelgnynay iipqgeylvt
      241 pdgklnpnar lryndsfada lfdnafrqey nvsasggndr tdyyvsmgfl dndsyvlgss
      301 yerftaranv nsqlkswlkv gtnvgyskat qngvqenaga asnpfevars wapifpvhay
      361 daegnmkyye dgspmydagn getdgtskrp tatnqnvian mkediretvy nnltsrsyle
      421 isflknfkft anysydftns sqtvfytpli gdgqsfdgrg tkgsyntttt nfnqilaysn
      481 vfgdnhhlsa kigheyykye yqylagqktn ffnpnnpeld nggqmqyins ytanhniegy
      541 fgmadydysn kyylsaafrr dgtsrfldrw gnfwsvgaaw risneafmeg tnswlndlkl
      601 rasygtqgne silseydyay vytpyqdqyt vtwngselgy spefygnpdl twekqktfdv
      661 gvdfrlfdrv ygsfeyfyrr tddmlfkrpv aystagrpyn wenlgamknt giefevnvdi
      721 fnqpdlkwtv slvgshyknr ivtlpeenre ngitsgpfnl regksrfeyy tymyagmdek
      781 gnamwymdet nekgevtgrt ttttyadatr yfigksalpd fngglsttfs ykgidlsiat
      841 afqiggyayd ysylsgmsss fyvghnkdmw ktfnpetgqg slpiwnadna snsftqqsdl
      901 nlikasyfsi rnitlgytlp knltqklgve klriyatadn lglwskrqgf dprvamagsd
      961 deyggyspmr visgginltf
//
LOCUS       WP_118289722             930 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118289722
VERSION     WP_118289722.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 930)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..930
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..929
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 vgygvqkksd vtgamarvgs eelntrpvnn afealqgkaa gvditsserp gtvgsirirg
       61 nrsisassdp lyvvdgvpls aggietinpr diesidilkd asstaiygsr gangvilitt
      121 krgkagrlal nysgsvtlet lkdkspamsa sdyitwrrwa yynsdpvnnp rgdqpnydkd
      181 qiyfaasgdp aalanvnkgw nngtwdgsrv tdtdwadivt qtgithehti sgsggnetaq
      241 affsigylnn qgtqkgqeye rynfsmsvdl qvkpwfkmgg singswavqd ygysrtgqss
      301 gsgpvdiysa akaiprfgvp ydeegniitn pcgsttnvyt videwnkstd nrqtfralgs
      361 fygqfdfgki wapleglsyk isfgpdfrhy rqgifiskds avkmgsknya kyatdrylsw
      421 tldnqinynk tfgkhnlgvt llqsaskynk esgsesanai pnenfewynm gsvditdaat
      481 ygagmstgms enqlasymar inyayndryl ltvsgrydgs svladghkws ffpsaalgwr
      541 idqedfmkdi swinqlklrf glgttgnsav saystlgniq sfyvpfgstl tpayatnepy
      601 ytssqvkman kdlgwekttq ynygvdfsfl ngrisgsmdi yhsntndlll smtiptltgf
      661 nstyanvgkt knfgvdlsln lvpiqtkdfe wsstinaayq kdeivelang kqdeisnawf
      721 igesinvfyg tasdglwqes daaemakfna nghkfeagmv kpvdqdgnyi idsndriilg
      781 nknpkwvlgw sntfnykgle lgielngrfg ymvdtggegq ygmynqreis ywtpdntgad
      841 yqkpiystag gdayssllgf kdasfikirn islgynfnsk alknigissl klyaqaknig
      901 nlyssvdfmd ldlgttyynr gftfglqvgf
//
LOCUS       WP_118291148             949 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Phocaeicola].
ACCESSION   WP_118291148
VERSION     WP_118291148.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..949
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106595
     Region          38..948
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknrliipa llaflsmqgy aqelndsits gkpakysdev veigyhkaqr leestssist
       61 vynedfnkrs aknianslfg ygtglttlqg sgryadaept ffirglqsls tnnplilvdg
      121 ierditdvtp eevetvtilk daaavaiygh kgingvvnit tkrgiyntre ikftydhgfg
      181 wqarkpkfvd sysyanamne alandgltar ytqdelnafr sgqypylyan vdwlgetyrd
      241 mdatniynis frggaskfry yamanlttnk gfianpymnd gystqdqysr anlrtnldid
      301 ltektklkln vlgilsetrt pgangqggan lwdmiytlps aafparleng twggsatwag
      361 tknplavsqa aaytkfhert lfadmtltqd lssitpglga sgmlsydnya qywenhsktf
      421 vygsnsvtaw engvpsstty ytdgkessms sdakciaftr vfnfaatlfy dkqinkdnki
      481 ysqlkwdyey rntkgtdqtw yrqnasfyth ygykdkyfad lsvvasasnk lapghqwsis
      541 ptvglawvms kenfmkdlsw infmklrasf gvintdrlpl dddsevtnyw eqtyggggyy
      601 pfdtnysvgt qswslgrlas lnsthekayk ynfgldasmf ngldvsfday yerrsdiwvs
      661 ssghyssvlg ftapyenggi vdswgveiga nyrkkiadit lniganfala kneiieqmee
      721 prmydnlitt gkplkqtygm evigyfkdqa dienspkqsf gdvkpgdiky kdvngdniid
      781 andkvaighs ttapeiyysf nlgaewkglg fdamfqgtgr ysavlntksl ywplinntti
      841 sqeyydnrwt penqdakypr lssqsnenny qtntlwladr sflklrsiel yykfpqiwvk
      901 kskilsnaki yvrgvdllcf dkiniadpev ygatypltrs vvagltigf
//
LOCUS       WP_118291871            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118291871
VERSION     WP_118291871.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 tngtitgidg dfslsnvkeg diivisfvgy atqeikwtgk pldvllkddt qllgevvvta
       61 lgmkreekal gyavtevkgd alraantisp vaalqgkvag veikqsdggi fgatkiqirg
      121 astlggnnqp iyvvdgvils ndissvspse ysdeantkan dygnelknln pddfetvsvl
      181 kgaaatalyg srglngavvi ttksgkgakg fgisvsqtlg idhafktpdi qtefgpgifa
      241 gwndldgngt iwdpyqvkvs ngektyigns sygygprydg sqirnydgtw ttysphknnm
      301 ldmyqlgfnt ntnvtvrgsg ekasfyasas ykkansttpn ntferysfll kgtyqisdrv
      361 diagsmnfvn skprnaarni geyfvnpnig mlgshldtky frdkylgehg gvastsygdq
      421 ygslpssykn ywfaidnyds yrketvirpt levnveifnw lrfkadanmn yyynrseeke
      481 lgrgyandgg yygmaqktke eftvggtftg nkqfgdfslg gftrfeyynk sqsewsvgtn
      541 ggmvvpgqwf iknskqtpsy sgemkgtkrm msaifalnts wknqlyldvt grndwssalv
      601 ysnatgthsy fypsvsgswl vsetfkekmp swislaklra swaqvgndtd pyyinqtynf
      661 gtlenpqggs nvytnelldq iksanlkper knswevgldf rvlndrlald vtyykentkn
      721 qimsvgipsv sgassqlina gnienkgiei alntipfknk dwqwdlnfty tknkskivel
      781 sdmlsspyyt lmgsvnggdy hvgsvakvgg aygllmsdav pavndkgekl ltwddswraa
      841 setpsgivqe vgtltpdflg sisttltwkn lslhiatdmr fggmtasyan lygtqggwle
      901 sslkgreghg glswtsqyae sngityhdgv ipqgvfkegt iatfvdgtkn dvsgmsyaql
      961 ikegklepth agayninhsa wnspwgstid dvwfhevnyi slreislsyr fakeiahkvg
     1021 aqglsvmlsa rnlgylynsl pnninpesgr gndsrefrir gfepytanym mtinvdf
//
LOCUS       WP_118292308            1013 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118292308
VERSION     WP_118292308.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1013
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112067
     Region          26..1012
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrriftfflt fllgmfvtal yaqthtvsgt vidkdanepl iganvlikgt tigtvtdldg
       61 kytlqagdkd ilvfsylsmk tieepvngrt vinvkmasdt etlgevvvta mgikrqsetl
      121 tysaqtvggk dvndiksvnm inslqgksag mmitpnstga ggsskilfrg nksisgnnqp
      181 lvvvdgvpvm mnitnsqvds nyggqrdggd amstinpddi aqitllkgas aaalygavaa
      241 ngaimittks aqsgkvsvnv ssnttmespm vlpefqttyg msdngtfswg eklsskapny
      301 akkffrtgft tnnsislsgg neniqsyfsy anvysqgitp qndyrshnln skvgfnilkd
      361 ihidfmakft nqhitnqaaa gylwnpltgv ylfprgedwn gykenfevyd pargcyvqnw
      421 tntqqqqfgn pywmlnrqtp itdrnryefg gsikwnitpd lniqgrmrye rgeehwvhna
      481 yassvgnlyp mgrmkdnryf sdqlygdvlv synhtfndfs lsatagssft ktktshvdlw
      541 gegsqfsqpg sgnifypnif tpnnyygnms tvgkddnwmt qkrlnsvfat aqlgyregif
      601 ldisarndws salaftescs ffypsfggsv llnkfvdmgk nidlfkfras ysivgndvpv
      661 fmsnllyslg sqgaitppdk apfrtlkpek thsleigfdg tflqnrlnin ltyyktntkn
      721 qffsvaapye sglrnryvna gnvenkgfef nigwyeqftd nfswstnlnf syndnkikel
      781 vddlpngltl tdfggakvil kegghygdly vrhlmrdeng kplqnekgep ivsgdsmdel
      841 eyagnmnakv nmgwtntfry kdfslsflid akfggkvism teaaldgwgv skrsgearda
      901 ggitvdgvkf dadkyyrttg nnnfnspyav enyvydatni rlrevtfgyt frnllgagkn
      961 ltaaiigrnl fffhkdapmd pdvsagtgng iqgvdmfalp tsrsfglnlk lnf
//
LOCUS       WP_118292364            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118292364
VERSION     WP_118292364.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 etvigasvvv kgttngtitg idgdfslsgv kqgdviqvsf vgyltqeikf kgeslkiilq
       61 edsqtlqevv vvgyggvqka ktmtasaatv kmselaklpv asmseglggr vtgvvtqqas
      121 gapgenariw irggenilyv iddvvmdsgq gneffnrlrp ddiasmsilk daaatavygp
      181 raangvvvia tkrgqegapt itlnqkvsim tpayrpkgls syeyalarne aelasfqesp
      241 tfndtelsky ymgdlwqkgy gfeeirnlvn erynlgyslq dindlfdplk tqgkniqdyy
      301 ssydpwdmfd htqpmyqtnv slrgggerik yysslgymkq ngvndkysye qvnmilntda
      361 mllsdkslkf tfnlngntsn nnkpadgegv fnnamygdwm pkrpaawstg lprkgsveaq
      421 lnngfnntes yrfqmnaalk wsvpwvegls aqaslnftts yyhqrhfnhd qegvydnpya
      481 tavssynpen anlyekwnky klltgifqid ytrsfgkhnl samvnyqsqv rksnwtdakk
      541 kgypttlapq ldlggtlvsa ggsaeewgsa syigrftydy dnkylfqysa nyngslsysp
      601 dkrwgyfqaf slgwvmsdev wfknlvnpni vnmiklrggf glvgnevgsp fsfltqyaqs
      661 snrilfgenm asnvgwyesd vannlqwsss kqygigldfg flkdrltgsf dtflylnkgd
      721 vmdmtddmir vdilgmpntp kinapyttsr kggfevslnw qdkigkvgyr vgvnysywde
      781 rvtrhsssds dwwtptfdni gkrpyvtnge sitypyglkt nglhgswqkm ynsllhannn
      841 mtlgtpalvd lngdgrvndy yvfnaegstp htqfgvtlga dwngfdlelf fqgatgarga
      901 mpsplrsqqs ymwnygqyaf qnaytpsnpd vdaalptpvp egngfgysyi diwsfdasyl
      961 klknislryd lkrsvlknlp viqgldlsfv vtnaftwtkk syplkdlqdp efittgasiy
     1021 nnngtlgsyp tqrsytlgvt vtl
//
LOCUS       WP_118294484            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-24].
ACCESSION   WP_118294484
VERSION     WP_118294484.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-24
  ORGANISM  Bacteroides sp. AM16-24
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Bacteroides sp. AM16-24"
                     /db_xref="taxon:2292002"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121750
     Region          24..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrlsvvfl fligtltyal aaerqvegvv issedklpli gasvyvtaed lkkngnnqst
       61 igvitdidgk fsisipdgit rfycsyvgyd vveiklipgk kqyditlqps ahmldavvvt
      121 gyqtverrkl taavskidis dqmvgaaksi dqaltgqiag lsvsnisgap gapakirirg
      181 tsslngtqdp lwvldgiple gtnipsmevl kdidnvgqta iaglnpadid nitvlkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs skltyspkln idrlnllnse ekvgleldll
      301 esgypyretk gevyriisgl gelqnfkdgg wnalssnaqg ainrlkatnt dwsdilfrda
      361 ftqeynlsls ggsekatyyt sfgymkengn ipnvsaerln lvmktsykvn silkvgasmf
      421 anrrknstyl pddrgltnpi yysrlanpyf tpydangnyn ydvdveddtd mdfglnlfee
      481 rkntsnetsi nglssifdae lrfddrfkit tqlglqldkt siekiaeees yvmrtekknh
      541 rnngvtylpe ggfhkanens lsqltwkamg eyrdtyndih efevmvgtei rktweeklys
      601 agygfdrktl ttkpiifpee sqafklheka hvenayvsaf stlsysllnr ytlggsirfd
      661 gsdlfgvdkk yrylplysvs glwrisqepf manakwidnl vvrasyglqg nidkntspfl
      721 lgnyrienil pggsedmidv sgapnkklrw ekthsvnagf dfavlnqain lsvdyyyrkg
      781 vdligtqmlp letgfemltv nwasmqnqgv evalstrnih tknfmwttnf nfaynnnkil
      841 kealredale pgregypvga lfalktagld eegypmfedk dgkavsamef fklqewgfga
      901 tdltarerre lytyvgtadc pytggfnntf tykafelgvn fsfdfggkvr sqptysivdf
      961 dkgrntnrdi lnrwtpente tifpvllsqn erldeymwys nqneiyrnld iwirdlnyvr
     1021 lqnirlgytl panfsrklgm tsatiaiegr nllvfgssyk nyldpetmsn ayatpapksv
     1081 tlslnlnf
//
LOCUS       WP_118292503             902 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118292503
VERSION     WP_118292503.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..902
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..901
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 qeipvgnggk kditlqddse lmdevvvigy gtqrkgdvts avasvkaedf tagkigdaae
       61 likgkvaglt iakgsgdpna estirlrgvi slqggstplv lvdgiegglg tvspeniasi
      121 dvlkdasaaa iygtrgangv ilittkngqr esrtaanysg ymslskfgkt ldfygaeeir
      181 qgltnyadkg ydtdwldavs rtafthnhnf nisggskntt ysadftyrke egvlletyne
      241 emrmrfdvsh wmlndmlkvn fnmvktfhkn gpidaaglgi yrqaimrnpt epiwnedgtf
      301 yenfavnyyy npvgiireqd gkynsentrm tgnitfepik nwqtnlmlsr rvtsdhnrgy
      361 ytseyfsqks enhtgyayhs qneyttdnle vtskynhtwn khrfdalvgy nyqynvnegf
      421 gannydyptd fylwnnlglg talkdgkagm ssykndntli gffgrvsygy dnkynvllsv
      481 rregsskfge nnkwatfpsv slgwtisnek fmegltwlnn lklragygvt gvivgdsyns
      541 ltryeygspy fydngvwhqg lsvksnpnpd lkwetskefn igldwavlde rlsgsidvyq
      601 kktsdmlydf tvptppnlyn ktlanagkmr nqgieiavna ipvrtkdfew kttvtashna
      661 nkllslsndl yetsnqidha ylgepinlst qrmevgrsmg qfygmksvgv senglwlien
      721 aktgeieeft dnmlsnddyr qylgnalpkl ylgwnnsfry knfdlsfqmt gqfgfkilne
      781 prayyennsi aynrlksvqk apyggqytls taqkqtfvsy yledgdflkm tnitlgynip
      841 lksskfvkni rayvsadnlf citgydgldp emsngdiwsl gidwrdkyps trsftfglnv
      901 sf
//
LOCUS       WP_118294755             910 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-24].
ACCESSION   WP_118294755
VERSION     WP_118294755.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-24
  ORGANISM  Bacteroides sp. AM16-24
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Bacteroides sp. AM16-24"
                     /db_xref="taxon:2292002"
     Protein         1..910
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100877
     Region          24..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrirnlfcl slllvavglp avaqtklhva lpdsittvgy atglrknlsg lveritenqm
       61 nkdqitnpld airgrvpglt ilkgsngpaa ldavrlrgtt slttgndpli ivdgvfgdls
      121 mltsiypadi esfvilkdas etaqygsrga sgvieittkk gvsgrtsvny ngsfgiassy
      181 ktvrmlngne frtlaqergi sildmgnntd fqkeieqtgl qhnhhiafsg gtntsnyrvs
      241 lalmnregvi vneklqnfts nmnmtqyvfd nflkcdlgmf gsvqkernlv nlhkvfysaa
      301 synptfpnhk npetgswdgy ayasqlshpl awmdvkdkna tshistharl tfnlaeawkl
      361 tffgsytynv venaqylpva vwaqgqayrg dkkmesllgn lmlsykkewr khffdvlgla
      421 eiqkdkysgf yttvtnfsnd klgydnlqgg airpwdgtns yyedprlvsf mgrvnytydd
      481 ryiltvnarg dasskfgsnh kwgffpavsv awvvskekfm eklsfidnlk iragyglagn
      541 qngidsyttl nlmrpngiap vgstpvvtmd klrntnpdlk wevkqtfnag ievallgnrl
      601 lltanyynsk tkdmlylynv svppftyntl lanigsmrny gtelsigitp lktkdmelni
      661 nanltfqqnk llsldgnyqg ehisateyks lagldgagfh ggynhivyqi vgqplgvfyl
      721 phctglvsdg nggytyqiad lnsggvsled gedryvagqa vpktilgsni sfrykdfdis
      781 lqingafghk vyngtsltym nmnsfpdynv mkkapaqnik dqtvtdywle dgdyinfdyv
      841 tlgwnvplkn trylqslrls ltvnnlatis gysgltpmin sssvnatlgi ddkrnyplyr
      901 iytiglsvnf
//
LOCUS       WP_118294916            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-24].
ACCESSION   WP_118294916
VERSION     WP_118294916.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-24
  ORGANISM  Bacteroides sp. AM16-24
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Bacteroides sp. AM16-24"
                     /db_xref="taxon:2292002"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121488
     Region          27..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekhrflmwf allfigvvsg ysqqlaitgr vldskkepli gvtillkgsa ngtvtdidgn
       61 fsikalkget lvvsyigykt qeillssdkt tmtvelleds emldevvvig ygtmrkkdlt
      121 gsvtqvrpda laneapktvq dvlrgtagln vgfdksakgg gsmsirgqrs vysdgghndp
      181 liildgmmfy gelseinpnd iaqidvlkda ssaavygaka angvvivttk kgksekpvis
      241 fsanvgwatr adgrkvydad gylnyrrdfy ttdtygvnps tgkyeayqtg grpagyfdrp
      301 tdtnlgkygl tmdawrnqtt qdagmssdei warriglnas evtlanflsg ktfdwydhsf
      361 qtglnqdynv sisgmtervn yylslgylsn egivrgneyn airanmklda kvtdwfsvga
      421 nvnfqnrsdg diavdwyrqi tsnspfatpy neagelvahp qgenaywkgy nfdfdrqyld
      481 lekgftvlnt iltakltlpf gitysfnaap rlqyfydryy rssehpdwqa etedrvnreq
      541 skrfdwslnn titwdytfae khhtiltlvq eaeerqswad riqarnilps ealgfhgtan
      601 gdkslsdfrs tdnretacgy larlfysynd kymgtfsfrr dgysafgttn pyanflsgal
      661 awtftnedfw kwgevldsgk lrvsfgqngn rslansyial anlalgkysq gyinsttgal
      721 ldmkylfvdr lpntglqwek ttswnvgldl sflrgrinas leyyimpttd mimnqslpdf
      781 tgfasittnl grvenrgfei slntrnietk nfewntsfsf srnkneikkl ygeyetivda
      841 agntitkerd dvdnkwfigh pisaiwdyev tgiwqvneve eaakygqkpg dpkvanhyta
      901 ddrknadgtt tavynnndkq flgettppih wsmrnnftly knwsfsfnly symghkslds
      961 nylnndnnys qitncqniyv knywtvdnps ntyarlsaqg ptglaapsrv vdrsfirlen
     1021 isvaynvpea flskykiqsa kvfatvrnva twskeweygd petgdiaprt yslginltf
//
LOCUS       WP_118295547            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-24].
ACCESSION   WP_118295547
VERSION     WP_118295547.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-24
  ORGANISM  Bacteroides sp. AM16-24
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Bacteroides sp. AM16-24"
                     /db_xref="taxon:2292002"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114979
     Region          31..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtktvslfsi ffvvlmvcat tlfgqsgnev tvtgkviddk getiigatil vkgtttgvit
       61 didgnysikv pgassvllfs yvgltpvtev vgdrrvinvk mssasevlee ivvtalgikk
      121 ekkklgyavq dlvapgltkm paantasnlt gkiaglkvsn spnlfdtpal llrgvapvvv
      181 idgvpvesat fwevapedie smsvlkgpaa avlygqmgqn gviqittkka kegvrisvns
      241 stgfdtgmia npsyqkkygt gykgqyrvgn stdefwgawg peldgrllaq wnspydengk
      301 riaipwiprg kdnldnmlrt gvvtnnnvsv etksqkgdfr islsqmhqkg vfentsldsy
      361 tvnmsggiqf sdklrfdani nynkmdspnf psvgygrnsp iysmilwaga nvdvrdlkdy
      421 wapgleglqq rnfdvadgye ngsydynnpy filyenlhgy hkntsygsas lkydvtkeln
      481 itlrtgvnmn elmedyrtaq stayarngny sqtyytdfqi ltdlmakydk kigafdigam
      541 lgfnarqynd rghkaatdgl avpgiytlen tlkptkpssy krelaeyavy gyldlgwkny
      601 illnltarnq wsstiptfgk nsylypsaql stivseyvkl pefisylklr gsyarvgsaf
      661 spyyfasvyt qtqswnnnig ltspsslysk dikpsystgy evggelrlfn nrlafdatyf
      721 yfidgpqtys qpiseasgwk syilnglktl rkgwelsita spfknpkgfs wdailnlssy
      781 rqylkelpeg qtkfgelkvg drmdaiygta mmyapegney agqviigang qiqkddikqk
      841 lgysnndlmv gftntmsydk ltlnfsfdac iggkilsqyn rymwaggrsl diddqarkdw
      901 yagkdyqaqg vnvisgtler dgdgniisdt rqfapntktt nyfdyiqnsk gyygidecvl
      961 vdrsflkfre vsltydlssl lrntfikgan vslvaknlfl itksglvdpd qynegttwdn
     1021 lqtpsfrnvg fnvnltf
//
LOCUS       WP_118295736            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-24].
ACCESSION   WP_118295736
VERSION     WP_118295736.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-24
  ORGANISM  Bacteroides sp. AM16-24
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Bacteroides sp. AM16-24"
                     /db_xref="taxon:2292002"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122348
     Region          23..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskkilflff cvfalaahsq nvvikgsvtd vnkepllgvn ikvkgtstgt itdidgnfsi
       61 ngpkgatlvi syigmvtqev eykgqplnvv lkddsqalee vvvvgygsmr kkdltgsvvq
      121 vrpdkiandn pktvqdvlrg tpgltvgyge sdagakgggs mkirgqrsvy tdgghndpll
      181 ildgmffyge lseinpddia qidvlkdasa aavygaraan gviiistkkg kqgkptinft
      241 asigltqkaa yrdrwqspea ylqhyvdwke kntygvnaet geyaaysrpg neytskpgyf
      301 rnpnnlddvs leawrgyttn degesdlsiw arrlgfrpnt almdnllsgk vmdwqdkafr
      361 lgfnqdynas isgagekidy ymslgylrne gafvddtyra irgnfklnak vtdwfeigan
      421 infqdrsdge igmnkggfme nspyavfkdd egnyvqdplm fqydrnnltn wyyekqflel
      481 qkgyttfnti fnaklklpfg itytfnaapr lqyfhdryfm saerpnskpt drgvnreqak
      541 rfdwslnnti twdhtfadkh hviltlaqea eerqywsdri earnilpsdv lgfhntqngd
      601 ksassfrsdd shqtadglmg rvfysyddry matftmrrdg ysafgssnpy ayfpsgglaw
      661 tfsnekffqp ythimstgkl rvsfgkngnr slanpyeala nlypgggkmq gyitssgdly
      721 lmrylmaqrm enpglqwekt qswnfaldfg flndritgtl eyyrmstkdm imgqrlpnft
      781 gfesittnlg qvdnngleia lntlnidnkn fqwsttfsls ynknrikhly gdyedildas
      841 gnvigkkead yvgngwfidr pisaiwdykv tgiwqkdeve eakkygqvpg dpkvwnnpan
      901 deydadgnlk kviynnddkv fqgqtaapvt walrndftlw kdltlsiniy srmghksles
      961 mylnndddgg gmtyrlvnkp akeywtvdnp snkyarieaq gpegargarr lynrsfvrle
     1021 nisigytlpr qwtkrvdier akvyatvrna avwgskdwey ygdpetgnya sriwtlglnl
     1081 tf
//
LOCUS       WP_118296428            1009 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-24].
ACCESSION   WP_118296428
VERSION     WP_118296428.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-24
  ORGANISM  Bacteroides sp. AM16-24
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Bacteroides sp. AM16-24"
                     /db_xref="taxon:2292002"
     Protein         1..1009
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112656
     Region          28..1008
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknkilvls lllsfslngf aqnsdgnvsg rvtdrwgnpv sgalvtvvnn pnvfvstdtn
       61 gkfvisaekg aqleisapdq sektvdvlte kpmnivmgya dqaihagyer qqtiaestss
      121 vatafnqqfn nrssqnvnks mfgnilglta lqetgtyweg nptfylrglq sisgsapvim
      181 idgierdiqy ltaeevesit vlkdaaaial ygykgingvi nvvtkrgkyn sreinftydh
      241 iinwqprrpq fvdahtyasa mnealgyegs spmylanels afksgqypyy ypnvnwmdev
      301 fkntgatnny nmdfrgggqk fryytavnlq vnkgfinnan qnegystqek yskanlrtnl
      361 didlsdktkl vanifgslse tshpgakdpd dskkelnlwn liyklpaaai parledgtwg
      421 gssiwpgtyn pvaqsqgaay tkghsralfa dmtlrqdlss ilpglggsfq laydnvsnii
      481 edhsksyvyn sytvtmgedg vptanlntpq gedtpigegk tntfqrsfnf ygslyydrlf
      541 gshslysqlk wnyeyrnssg rntslyrqhl slyshygykg ryfadlniva sasnrlapaq
      601 rwavsptisa awvlskedfl kdnkyinflk lrasfgvint dnipgdgywl qtyksngtys
      661 faetytkldd ggwtmgqlas lnsvhekalk ynfgldaslf nsldvtfdty yqrrkdiwvd
      721 gdgqyssvlg ftppfinggv vdswgfelga nynkqvgevr ltaganftla kskiveqsee
      781 pvaysylakt grpmeqlrgl vavglfkdqa eidnsprqty stvypgdiky kdmngdnvid
      841 dndvvsighs ttlpeifysf nigaewrnlg fnalfqgtgr ysamldltsm yrpllssttl
      901 sqyyyenrwt pgnqnalfpr lasqssqnny rnstwwmrda sflklrniei yyklpkslla
      961 ktkivnnaki yvrgndllcf dhigqmdpet ynsttpttrn vvigltvgf
//
LOCUS       WP_118296798            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-24].
ACCESSION   WP_118296798
VERSION     WP_118296798.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-24
  ORGANISM  Bacteroides sp. AM16-24
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Bacteroides sp. AM16-24"
                     /db_xref="taxon:2292002"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118313
     Region          19..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mihtnrclsn tyhahssakt lqisyigmkt eevsikprlk vtmkidseml qevvvtgmqr
       61 mdkrlftgat sklsaddvkl dglpeisral egraagvsvq nvsgtfgtap kirvrgatsi
      121 ygsskplwvv dgvimedvte vsaddlssgd avtlissais glnaddiesf qilkdgsats
      181 iygaramagv ivvttkkgka gsnkisytge ftmrmkpsyt nfnimnsqeq mgvfkemana
      241 gylnfsnvyr asdsgvygkm yhlindytsn ggfglpnttk ainaylqqae yrntdwfdyl
      301 fnssvsqnha ismssgteka syytslsvmn dpgwtkqssv qrytanvnal yniysnlsln
      361 lignasyrkq kapgtlgstp nyvtgevsrd fdinpysyal ntsrtldane tyvrnyapfn
      421 ilhelknnym dlnvvdmkfq gelkwkilkn leasalgayk ystttqshyv kdysnqawaf
      481 ramddatmrd anpwlytdpd kvnslpvsvl pvggfyretk ygmnswdfrg tlnyndvfae
      541 dhiinlfggm evnsmdrtkt wfngvgmqye mgmlpsydyq yfkqgneent nyytveesrs
      601 revaffatgt ysyrgrytvn gtiryegsnk lgksrssrwl ptwnvsgawn vheeaffedl
      661 rptlsnltlk asysltadrg panvtnsrvv issfnpwrpf tsvkesglqi ddlenselty
      721 ekkhelniga eigfldnrin laadwykrdn ydligaintm giggqvmkya nvasmkshgi
      781 eftlstrniv tkdfkwntdf ifsqaknevt dletntrild mvigsgftmk gypvrslfsi
      841 dfqglneegl ptfinesgtl tvtdlnfqsr vkdylvyegp tdptitgsfg ntfsykgfkl
      901 nvfmtysfgn virldpvfkn wysdlaampk efknrwtqsg denttnipvi adrrlnqeyn
      961 hlsyaynayn rstarvakgd firmkeisls ydfpkswiap lkfnnlslkl qatnlfliya
     1021 dktlngqdpe ffntggvavp vprqftltlr lgi
//
LOCUS       WP_118299654            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118299654
VERSION     WP_118299654.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117903
     Region          25..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgkrihlfll alaigviqga aqvttvrgiv tteedgepvi gasvivkgts lgtvtdvngr
       61 felsgfppsa trllisyisl makevaiapq vsvtlksdth lldevvvtal gisrekkalg
      121 ytaqevkqda lvqgkdnnll nslsgkiagv riintqgdvg ssrivirget siagenqplf
      181 ivdgipvdns qlnarssgrd fknaiadlnp ediktltvlk gpnaaalyga raahgaivit
      241 tkggdkrqkg igitlhsstq vsfvatlpef qnlfgqgagg rfsyvdgkga gvndgvdesw
      301 gprldiglli pqfdspldad gnrvatpwvs hpnnvrdyfr mgistnngis vargddkyqf
      361 rvgynyekqv sivpdagtnk tnislntdyh lakwivvgat anyivytaps lpgsatpsgs
      421 nvrsnspmlq flwfgrqvdt nslkadytrn wnssyydnpf wsasyntqsq erhrligdlh
      481 aefrltdgln vrfrtstdwy ndrrkskvkw gsagagspyg syaedaytvk enntevlaty
      541 ikqlnknwgi dallgfnvrn kqyennyqaa prlavadlyt ltnsrdplts sndfyrlrqy
      601 glygsiqldy rrwaflnitg rndwsstlpv dnnsyfypsv tasvllseaf gwrskavnyl
      661 kirggwsqvg adanpyqlat vftsetafng nplqssstig mnpnlkpekt ssieagfeaa
      721 fwdnrlyldf tyyktdsrnq ilklattaas gytsqvrnag hirnrgyeiq lgavpiqtsk
      781 gfrwnldlny gansskvvkl ddeglitsyq lyssgiqila svgeaygtlf gtsyvrdang
      841 nvvvdanglp kisttnktlg kftpdwtggi sntfsyrsls lsflidasvg gsifsntnkt
      901 gkytgvlant lsgrdaehgg lwyytdamgn nvrlpespsy svssdglyya qvngqstrvy
      961 qdgimvegvt esgskneevv saekyyhriy siaeanvyda syvklreval syrlprlwtq
     1021 klhlqeasvt ltgrnlwtiy ksvpnidpes alttgnaqgv eayslpttrs fgvnlsvkf
//
LOCUS       WP_118299663             942 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118299663
VERSION     WP_118299663.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105160
     Region          39..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtiinsiykg kryailltti ltfyapvlfa qhiadsalve vaygqqpewr rtsaissirg
       61 edllkttsas lgnslqgqlp gltllqqsge pgydfsianl ylrgrtsyas gqkmlvyvdg
      121 feapieslst aeiesvtllk dasalalygm rgangvllvt tkkgcvsapq vsirlqtgiq
      181 qplgvpdpin aydyatlynq arvndglprl ytpeelnayq nntdpyfypn vnwkkailnn
      241 taplsmadls fkgggdvvqy yvmmnllqni gfykdtdkkr rensnayyas fnfrsnlniq
      301 iskhlstgln fsgsvgnrsi pggsssangl lgaiwrtapn afpvynpdgs yggnaaftnp
      361 vgnivsrgly kensrtfqli fmpkydlekl tkglsvsagi aynnymadss iknqnyarys
      421 lskgaggevl ytpygadspl esdegfrtdw srlnfkaqld ydrvfkqhql tasifflsdl
      481 yqkygsrddi kylnyagrvt ysynqkyige faasytgcdd yapgkrygff pafsagwils
      541 kenfmkninw veylklrasi glvgnnqnen grylfdqtys sngsyflgtg ssstggfrad
      601 mianpdiswe kervfnigld avllkglsve fdyfhkeryd ilsqpystip gfvgasygdi
      661 lpymnvgkvk nqgfegtiry esslknnfny yvetsawyak neivdmaeev klydyqyrkg
      721 rsvntpfvlv adglyqesdf dsngslkshl pvpqfgevtp gdikyidkng dgvvdsndsy
      781 pvgysnipew nyalkigfew kgidvealfh gvanrdiyls gplaysftdn gsasklalds
      841 wtpenpnasy prlstrtfen nyristywkr ngnyfrmkni rigytfpqsi araiklsrly
      901 vyanasnlft vshldgladp essslitypl trsynlgiki df
//
LOCUS       WP_118299709             920 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118299709
VERSION     WP_118299709.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..920
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102301
     Region          34..919
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkyhifft gmlsiaffmg atvdtkaqds iavvsrvnie hlkampdlql sntlqgqaag
       61 livipntggi gyanstfyvr gqhsngtnka iviidgierp iddilpeeie sievlkdasa
      121 kilygaqatn gvilvrtkrg qagkrvirfg aeygvqpvtr lpeyldsyny atlfneacan
      181 dgllplysda dlqgyrnstg vndllhpnvd yykeflrsss tfrkatlels ggnarakyav
      241 tvgytgssgl ekvgdrsdln rvnargnldi ritdflsasa dvaarvekkd wgakdgggmf
      301 seistlrpne ypfmisaedi hghngiaade tsllfgassr kssnlysdml yggntseryv
      361 nsqtnlglnf dlnefvegla aeayitfdny sylrqqlrnd yptysidryl naagdeeirf
      421 terkklnlpk kqsiasnsty ryfgwnarvk ynrsfglhdm ganaafryta eeatgssqdl
      481 kegnftfran yaynkrymle atlaamgsnr fqgdnkyffa hsvggawiis nesffkdmra
      541 vnllkmkvsy ghlgyagdtd fflhrtnwkk gdkeefkpst gasttdlirl gnpdlkweys
      601 nelnigiegr flnnrlsgev nyfrelrkni iginsakyat iggnfipsen igevlnqgid
      661 acvnwndkvg edftynlgfn itftknklrk tnelnniedy rksigqptsa ifgwqsqglf
      721 gkdvaiaghp fqsfgnyqvg diayadlnnd gmvdnndqtc igqsfpkttl gvdvtlnykg
      781 fglyilgtat tgvtqmltst yywnkgldgy svlaeeryhp vnnptgtqpr ltttsgvnny
      841 rnstfwtkng sffrlknvel sytlnnnskk gigknykffv rganlfvlsg ikeldpeqml
      901 agisnypvyr titggvsinf
//
LOCUS       WP_118300800            1164 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118300800
VERSION     WP_118300800.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1164
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130465
     Region          129..1163
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mstkllseti crkglmvkcf valivfccsv geafaqtdtk vtinvnnvli rtaldqlqke
       61 akihfvydee nidsekrvsl sytetplnav lddfckqtsl ryevkrnlil ilpskaektt
      121 gkhepfymtg vvtdetgesi igatimiggt sqgtvtdidg ryslqvtpgd lvsftfvgma
      181 dkvvkvqsgk kvvnvkmetn ataladvvvt gyqtlskera tgsysvisek stkgkletdv
      241 lsrieglvag inktssnsnd vvirgittym gntkplyvvd gmpyegdlas inptdvqnit
      301 vlkdaaassi ygaraangvi vittkrgqeg ktkvsyngsi klspkpdfdy lnlmssselv
      361 dmqiegfdyy htayenlnkr qavnpvvdll yqhergqltd sqltdallpy rtndnrkqie
      421 defarvgivh qhnlaisggs nknrymatvn ymgdygnqky qskdrigfsl kddvdffdwl
      481 sadfgvtgsf yrskgdngag sysslmssyp syymlrdlqg nplnfqrtks dyelqrlqsi
      541 glmdetyspi knraeenyhn nsnyyrlhag lkfkllegln idlkyqtegt ydknrtlysn
      601 msytvrnmin daaqydaatg sltlnvpkgg qldesryesy sytmraqvnf nrifgkhais
      661 alggaerrlv rrtgaqnyym gyddnslgvk pinplvmspi ngteslsgsf nwvygeynal
      721 thtedryvsf yangsytfde rysltgsiri dqsnlfgtdp kyqyrplwsv ggswqianep
      781 fmedcmwlnr lnlrmtygvg gnvpkdagpy mtvvdsgyne wvgdfgsyiq nppnsqlrwe
      841 ktastnvgid fsafnsrlsg sidyyykktt dllgnrnadp tlgwasllqn ygsmfnrgve
      901 lslqivniqn knftwgtnlm fsynkneltn legtketvfy ysaynvaavg ypinsvfsyr
      961 yagldptngn vlvynkegek vskvssiddm vysgtrtpky taslknffsy rdfdfsfmfv
     1021 yygghvlrdv vagymggaps anltrkalnh wrkpgdenip gvapsfnrni yytdaqtwys
     1081 adihvkkady iklrdislsy nlpknwlrky fiesaavtcq isnvwwwaan gdidpeaytt
     1141 sgygwgaltl pnpttytigl slnf
//
LOCUS       WP_118300993             538 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118300993
VERSION     WP_118300993.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..538
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <20..537
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 amfliiseiy lflfrthvky atdrylswtl dnqinynktf gkhnlgvtll qsaskynkes
       61 gsesanaipn enfewynmgs vditdaatyg agmstgmsen qlasymarin yayndryllt
      121 vsgrydgssv ladghkwsff psaalgwrid qedfmkdisw inqlklrfgl gttgnsavsa
      181 ystlgniqsf yvpfgstltp ayatnepyyt ssqvkmankd lgwekttqyn ygvdfsflng
      241 risgsmdiyh sntndlllsm tiptltgfns tyanvgktkn fgvdlslnlv piqtkdfews
      301 stinaayqkd eivelangkq ddisnawfig esinvfygta sdglwqesda aemakfnang
      361 hkfeagmvkp vdqdgnyiid sndriilgnk npkwvlgwsn tfnykglelg ielngrfgym
      421 vdtggegqyg mynqreisyw tpdntgadyq kpiystaggd ayssllgfkd asfikirnis
      481 lgynfnskal knigisslkl yaqaknignl yssvdfmdld lgttyynrgf tfglqvgf
//
LOCUS       WP_118301021            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118301021
VERSION     WP_118301021.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121699
     Region          33..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhsdyhgkl lrlamffval flcgtmayaq tdrmisgivv dengdplpaa hirqvsqtkg
       61 eelaavitdm nghfrltllr takeieisyl gyeskkvrlt sansyrivle paselldevv
      121 vtgyqtisre ratgsfakvd skkletqrls svsslmegri agysdgkirg vtsmnglttp
      181 lyvidgfpve ktisdglgnw venvpdlnie dienitvlkd aaatsiygar aangvvvitt
      241 kkagknqlnv sfsatltvrp ynfytghlad tadmiemeke waamnpnlqg egasqyaqnl
      301 ldnasmyscl gvqailkhht gaiseaqmeq tlhelasqgf ryyddvkkyg krnpfsqqyn
      361 lnigrgtekn tfnaslsyrn nreedkytds esfglnlqnt trltswlsld lgtylnygdg
      421 ttqsynltsp gynyvpyssl lngdgsyytn taadrysksq qeiissygly smditpldel
      481 grnlsksknf snrtfarlnf kftdwlryta sfqyevgeyk tsqlqdkesy avrnkvntfa
      541 tdasgsgqat ynlpygniyt tgtnsirayn frqqldfnkt faekhdvtal fgmevrenkt
      601 eynnrkyyny dpalltydli dervlsntyt gvlgnyvsfn kndisniyel vnrfvsfygn
      661 aaytydgkym vtgsirwdrt nlfatgskyq kkpiwsvgag wnldkesffk vsfinmmklr
      721 fsygiggnia knsapymtay ynnnthvggi qgtisnrpnp dlrwekttta nigvdfsmfr
      781 nrlngsieyy nksgvdllan tngvptegfg fstyimnngk mrnrgfeltl ssdvimgkdw
      841 nwnvggvlgy nknkvtyvnv kapaiflqfd ypaayprvgv pynaiygylw agldskgqpq
      901 vydsegnihv ssspqkveda vylgtsvpvy sgaintnlry knwelaaqll fegghkmrnt
      961 niaypglgvt skdvskrwrq pgdeaytdvp ryvpseskdy nsyssdlysk asihvldadn
     1021 wrlknlsvty hvpasvcqkf yvknarimlg menvftlaks rdvkwmlggy skpnylcnvn
     1081 lnf
//
LOCUS       WP_118305307            1189 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Butyricimonas].
ACCESSION   WP_118305307
VERSION     WP_118305307.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas
  ORGANISM  Butyricimonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae.
REFERENCE   1  (residues 1 to 1189)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1189)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1189)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1189
                     /organism="Butyricimonas"
                     /db_xref="taxon:574697"
     Protein         1..1189
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132548
     Region          129..1188
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksgeckgn lrsaqkifrv mkmmcflmfv llvqvrgdvv aqnqvvsvdm kncsveeflr
       61 eikeqtgirf mykseyveai prfdvhaker qvlalldevf agkgikclyd ngvivltkvq
      121 qqkgpeevvi kgvvkdereq plpgvtvlik gttigvatds kgefslttvk qdsltllfsf
      181 igmksrevkw tgqkmlhvvl qddshdmeev vvtgyqtisr resasaistv kakdimvqgv
      241 gsidqmlqgr ipgmmvlnts gepsatpkir irgnatingn kspvwvvdgv ileqdvpfta
      301 sdinsedaey lignaiagln pqdietitvl kdasataiyg vkaangvivi ttkkgvvgrp
      361 visyngnltl ntrpsykdyh rmnsqervlf srqliesnmn fgrvptgety eaayeqlmsk
      421 qisqaefeqk vetlqrrntd wfdllfrsdv ththalnvsg gteavkyyvs agysniegaa
      481 rgsdsekfst lakvdveyne ylgftakidy attsntgyss vvnpfdyays ttrtmpayne
      541 dgsyymsyra agstgrdyig ynilkelknt gksskmddfn allalrlklw kglkyegtfs
      601 whtgntntrd wataqsykvt eirgyeygay teydpefsds rlpyggmltq gstrksgytl
      661 rnmlsyshlf gvhdvsvsag tearrneykg vsttgygwvp efgemfspve tssyistygg
      721 nkptntnsft qvasffgias ycydnryvfn anirsdgsnk fgsdpkyrwl ptysfavkwi
      781 asnesflena kwinnlsfrg sygiqgnihe satpylivtv gdrdgvtglp iskisklpnp
      841 dlrwektksw naavdfalfd grvkggfdiy rkntsdlims kqvaastgqn vlyynagkmv
      901 nkgfegfvnl glvnnrdwdw rfgfnfgrnv neitlanrdd lseatvvdqm lagtlavegq
      961 pigsmyayrf aginqdngyp lfyakngqkv hralrqdlel vhcgsifpkl sggfdtqvtf
     1021 kkvlslslnf aystgsvsrl pkfydsytid pltnlsdewl kcwkqagdnt iypapynstd
     1081 mknylatetg svydisegis ghsdpynlyn dcdirvakad flklkmvals ysvpqnvldf
     1141 lhissmlvrf qvtnlftiad kkwkgldpet nganipalpt ysfginvsf
//
LOCUS       WP_118306977             932 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_118306977
VERSION     WP_118306977.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..932
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103648
     Region          2..931
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtlanaqplk vtmgedtqtl devvvtalgi kreqkalsyn vqqvkgdelt nikdanfina
       61 lsgkvagvti nassagagaa arvvmrgtks lekndnalyv idgipmfnvn sgdnaggtmn
      121 kqpgsnsvad inpediesmt iltgpsaaal ygsdasngvi littkkgtvg kvqisysnst
      181 sfsspmmmpk fqniygnreg elgswgslmd tpsnfdpsdf fntgmtemng ftlttgteqn
      241 qtyasvsttn stgilpnnay nrynfsirnt akfcdnklsl dlgaqyiiqn nknmvgsgqy
      301 fnplvslylf prgenfqevq myerysearn lmvqywpesi fgtdldmqnp ywimnrmqne
      361 lskrrymfna slkwditdwv nvtgrvrvdn sdsdsyekyy astrgtftes sskgyyghtk
      421 qndrsvyadv masinknffd dklslnatvg asindiqeda mylkggleqi pnffhygnin
      481 vntskrnesk whdqvqsvfa saelgwnhql yltvtgrndw asqlaftskg syfypsvgls
      541 wlvsesvklp kaisylkvrg swaevasspn ryltqmqyty neqtntyeyp ashyntnlkp
      601 entkswelgv nakflgnrin ldmtfyrsnt fnqtfyvdas assgyknniv qtgniqnqgi
      661 elalgysdtf dkvkvstnft ytlnqnkivs langainpet geaiemeyys kgtlgtsggp
      721 tlrlyengsm gdiyinqrlr qspngyiwkd psngslaien teyrkvgsil pkyylgwngs
      781 vawkgwnlgf aftgrfgglv vsdtqamidk ygvsessava rqaggvwvgd skvdaeeyys
      841 kvttavgtyy tysatnirls elslsyqlpk twfknhvnmt lgltgknlwm iyckapydpe
      901 stssvtsnfy qgvdyfqqps lrslgfnvkl tf
//
LOCUS       WP_118306978             930 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_118306978
VERSION     WP_118306978.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 930)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..930
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103740
     Region          4..929
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhysqaitlt naqplkitmg edtqkldevv vtalgikrse kalsynvqkv nndaltsvkd
       61 anfvnslngk vagvniqrsa sgvggstrvt mrgnksisgd nnvlyvvdgv pignqadrtg
      121 dgtgfgsgrt sgegianfnp ddiesvsvlt gpsaaalyga saangvilin tkkgeagkmr
      181 idvsssvefm tpltmpkfqn rygisgnyys wgdklenqss ydpkdffelg atfnnsfnls
      241 tgndknqtyf siaavnsdgi vpnnkyhryn vtlrntakfl ndkltldasa syireyynnm
      301 isygtyfnpi vgaylyprge dfekekyfer ynselgysqq qwgpgdfgmd iqnpywiayr
      361 nirpevkdry mlyaslkydi tnylnvagrv rldntyteke dkryastint yastngryty
      421 snetfrqkya dimvnfdkqf aeiyhatina gtsfeeydtk grgyggqlll vpnkfvysni
      481 dptqstasqt ggdsrrrnfa vfasaelswn salyltltgr adkpsqlvns ddpwifypsv
      541 glsaivtell pnnikeklep tlgflkvras ytevgspipy tgltpgtlth eleggtfkpf
      601 kyypisnlka ertrsyevgl dskwfnntit fgvtyyhsnt ynqllkatlg snfeymfvqa
      661 gnvqnrglel slgfdkkfgn fnysttftat tnknkiiqla rdvlnpvtnt lidltdiqvg
      721 rfrlreggei gtvyanewlk rdgnnyidyq pgqalttett spyklgsvnp kwnlgwqhgf
      781 sykgfnlnll ftariggivi sktqamldry gvseasadar daggvslgyf kvdpktyyda
      841 vsnldayyty satnvrlqea rltytfpnkw fkgtvnnlsl svygtnlwmi ynkapydpel
      901 tastgtfgqg ydyfmlpsqs tyglslkfgf
//
LOCUS       WP_118307338             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_118307338
VERSION     WP_118307338.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109413
     Region          74..976
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mviilpnffl qkpvcrllav mgflgfsgai asqssspvni dsvetymkkd sfeknvgsrf
       61 vtnrsidsfg vsdtvdirml qrsqflsiqq llkgnvagvy vqenngepgt iqsmlvrgls
      121 spvfsnkdvs gvqptiylng vplmlensyv ydikqfdinp igaaanmlag ldissiesie
      181 iikdplqlak lgplaangai wittkdgyyg genvsigvsa gmafapssvr mtngsygkaf
      241 rqrfydtysl tpgkqpdylm dtrdvryfgk pdwaddyyqs sllynvnasi gggskkanyv
      301 ftlattkdag aadntsytky nigfalnmvp ldglnvstii naakidrvrn rnfrdrfaem
      361 eymvdfstpl apagnlyndf lisndltkdd nynnllngll alsytkqrfn atasikldyt
      421 tnvrrafwpm allesvnfvs nysgynqrii getsasyllp ladihklniq wngsitsdly
      481 hynytraydg dddmkpttst gnfkqyryvd rlenrwvsts ialdykyknl lnvgllaryd
      541 gnsaiqsdhr wmftpaasae wnlknqfftg stalsglslr asyariaksf qsdryelgpq
      601 ylatsitwsg epllssangf atitrpyasg wvgydlklpy sdkmelalkg sffdnriiae
      661 islyknyekn lltylpvtqe mgyeyklasg mdisnqglel nlsasilknt plkwdlsfna
      721 synknklekl penqkttvig dhklqvgqsv dafwvyqnkg iytndsevpv mngktlnvng
      781 vpfkagdpvw tdvdgnnqin dndrvltgha ippytggltn qfaykrfdfs fnlffalghs
      841 alnlrdqqry dfatldniqs lqsvkeiffw qntnqrddyp iynpqssvhp yraeqdlfle
      901 klsylklrni tvgytlpikk vgsnipksly fyltgsnlls fsnfsagdpe lvnfngtydg
      961 yslpiprsvs lglrfkf
//
LOCUS       WP_118307392            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_118307392
VERSION     WP_118307392.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124840
     Region          25..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkhlciii cflvnalama saanrtitgv visgednepl igasvyvhtd elkkagasqt
       61 slgtitdidg kfslsvpdkv trihcsyigf eeqvivlqgd kksyrivlqt sahtlgdvvv
      121 tgyqtlerrk ltaaiskvev sdamvgaaks idqaltgqia gvsvtntsga pgspakirir
      181 gtasmngtqd plwvldgipl egtdipkmdn kssdndivni gqssiaglsp ndiesitilk
      241 daaataiyga raangvivvt tkrgrtgkpv vnfntkltyt pnletsrlnl lnseekvnle
      301 lqmmkeapfn kwgfypipvy sekggvaail kqynlmdiyr ekgwegltpe aqnainrlks
      361 intdwndilf rdaitqeyni sisggsekvt yynslgytle ngnipgvsls rfnltsktsy
      421 qinkllkvgv sifanrrknt tfltdtyglt npvyysrian pyfepfdnnn nylydydvvt
      481 gsipdllqgy nileerents nksvttains ifdielrfnd qwkvtsqvgv qwdqlsreey
      541 agtnsfnlrn qrensayykg ndriylipeg gmlkstnstt sqitwkvqge ykntfndihn
      601 iqimagseir knwyenqast gygydpktlt fknlefrdsk qanewklktk sfkenafasf
      661 yangsytlmd rytlggsvrm dgsdlfgvdk kyrylpiysv sglwrisnep linqfkwidn
      721 lalrlsyglq gnidkntspf ivgtygnisi lpgsneesit insapnsklr wektasyntg
      781 idfsvfnqai nlsvdyyyrk gtdlignkml plengftsma vnwasmknqg ieinlqtrni
      841 atkdfswyts fnfaynqnkv lkvmtekdqv tpslegypvg aiftlktkgi ksetgqiyie
      901 nkdgeavtie elfqmadkgn ldgeysigvd ketergfysy agtsdapytg gfmntfnyrn
      961 welnlnfsyn lgahvktdpt yyiadpdpgr nmnrdildrw tpenkngkfp altslntnpa
     1021 dyylfstrrd lyksldiwvk klsyirlqni rlayhfpsew lhklniggvt vglearnlfv
     1081 fgssyknymd pesmsnlyst pvpksvtfnl slnf
//
LOCUS       WP_118307441             898 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides thetaiotaomicron].
ACCESSION   WP_118307441
VERSION     WP_118307441.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         <1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          2..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 ikreqkalsy nvqqvkgeal tavkdanfin slagkvagvq issgatgagg atrvvmrgmk
       61 sltknnnaly vidgvpmfnt gssggdgqyg smggsdavad lnpddiesis mmtgpsaaal
      121 ygsaaangvv lvntkkgkke kisltvsnst tfskayimpe mqnrygtssg lfswgdltdk
      181 rydpkdffnt gsniinsitl stgsdknqty fsasttnsdg ilpnnsynry nftarnttnf
      241 lndkltldig aqyiiqnntn mvsqgqyynp lpalylfprg dnfdeirlye rydtnygfmk
      301 qywpygdggl slqnpywtqn rirrtsdkkr ymlnaslkwk vtdwlnitgr vnldnsdyrn
      361 ktekyastla tfcsvnggfe damrqersly tdlmatvdkt fgdfrlntni gmslyhtsmq
      421 tigfagdlii pnffalnnin yaanykplpd gyddevqsif anvelgwrsq lyltltgrnd
      481 wdsklafsnq ssyfypsvgl savltemfal pkiisyakvr gsytvvassf dryltnpgye
      541 ynsqthnwan ptvypmdnlk pektksweig lnlkfwenrf nldatyyrsn tlnqtfkvdi
      601 psssgynkai vqtgnvqnqg ielalgftde wagfrwasna tftlnrnkvk rlaggstnpv
      661 tgelidmpnm pvgwlgkenv aprviltegg tmtdiyvyne ltkdnngnik vdaqtgglsm
      721 htaetptkvg nlnanynlgw tnnftykgin lgvvlsarvg glaysatqgv ldyygvssit
      781 anardnkgvp mnngkvdtqk yyqtigtgeg gygryylysa tnvrlqelsl sytlpkkwln
      841 nvanvtfglv grnlwmiyck apfdpelsas tssnyymnvd yfmqpsmrni gfnvkvqf
//
LOCUS       WP_118307529            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_118307529
VERSION     WP_118307529.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122910
     Region          32..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meklylkrsw rigtclmvll tffalslsaq nrkvtgvvvd efgdplpgan itvvgnqnlv
       61 tatnmegqft lnnvpkdail nvrfigyavk tirlatlknn dllrivlsed vkelndvvvt
      121 algisresks lgyarqsidt eslldtrdpn llnslsgkvs gvnfisnggp lsstrveirg
      181 nnsltgnnqp lyvidgvpim npmgedgdld ygnpasaisp ddiesievlk ganaaalygs
      241 daangvilit trkatkksgl gvsygynmqf tflrefpayq nvygsaslpa vgvgdgfnyy
      301 gsnskngyay dpslpygifv fnwanpnqrs wglpmlgfdl vgrnnqirsy vpnkngitdm
      361 yemgvamths vsvnkvfnga girfnytgid ydgmlknfdn mkrhtfdlrv nmdlakwlss
      421 eisvnyqlet adnrdfkgds nrnpmraimn mprdvvmeel lpwkretgea ftrgngfynp
      481 ywllneisng dgrnnfrgnl tlnikpiqgm nirlrasvek ankngwkfdn yytmwdidgq
      541 yetfreasnn ynyegvisyn rnikkvslsa nlgtsmqknd wyklwnqvsq laapdvksls
      601 nnasilsgte svnakekqsv fgmlslgyhg lfvdgtfrnd wssslpkann syfyasgsas
      661 avlteifpkl ksktfsfakl rgsiarvgnd agfdrlinsy sygglfrndm awfqgdavrk
      721 npnlkpetti skeigaevrl ldgrltadvt yydkytrdqi veselsylsn yqrviinsgk
      781 isnkgweisv sgvpvkvknf ewktifnwsk nnsmveslpe gidkiqigsg vynvksyaev
      841 gkpygaiyak tfkrdaegyi lcqldgspke gqdyeylgcv qadwrggwnn vfrlgnfsfs
      901 vmfdfqkggk ffsqtsiqss vdgqsvksle grdadffsrk ilgesdeery gfmrpqnant
      961 ptangqiypd wgrpkgvvlp ncrydedveg lagqqvlgyc tperywmhyt srdisrfiyd
     1021 asyvklreit vsydlpkkwl rktpfqtfrv aavgrniatl fantphgldp qatsttgnaq
     1081 gfergfnlps atygfdikvs f
//
LOCUS       WP_118307946             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118307946
VERSION     WP_118307946.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110827
     Region          7..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvilaqktlt gcvvgedgvp lagatvleig tsngtvtdme gkfkltvadn amlrfsfmgy
       61 ktqeisvggk tflnitmved aveldkivvt algiekkehs lsyamsqikn eeltrvkmpn
      121 litsltgkaa gvqinqvssg lgasakvsir girsvagenq plyvidgvpm lnssseqafs
      181 aiggtanagn rdggdgisnl nsediesisi lkgapaaaly gsqagngvil ittkkgksqg
      241 qrsisfstsl mfdkavslpe mqnrygvsei idswgerqnl pkndnlkdff stgmasitsv
      301 slshgneklq nyfsyanttg kgiidknrls khnltfrets tlfndrlrld gsvnlmrqvt
      361 knkptvggfy mnplvglyrf prgedltyyk dnfevydesr nlniqnwhts yddfeqnpyw
      421 ivnriqskev rlhaivslsa sfkvndwltv qtrgnvdcin dklrqkfyas tapalagtng
      481 ryiemdyqdi qfygdlmlmm kkqwgdfsvn galgtslndk ttnstrydsk taslyyanvf
      541 nlaniimngs aaldqkidar rqlqslfatv qvgykesayi dltarndwas tlshtkhekr
      601 gylypsigts lilsrlftlp ewvsyakvrg aysmvgndip pfmtyplshi taggeyland
      661 aapfkemepe mnysweagae arflnsrigf nltfyktntr nqffklptla gdkyayryvn
      721 agnilnrgwe ialdatpvlt kdfmwsttln fatnknkiva lheelkefvy gpisfsssya
      781 mklvkggsig diygkafvrd asgnivyete gsnaglpkie gdgntvkvgn snpkfqmgwn
      841 htlsykdisl yflvdcrygg kvlsqtqadm dlygvsevta qardegyvml eghridnvkg
      901 fykivggrag tteyymydat nirlrelsls yqlpaswmek skvlkkvqls fiarnlfffy
      961 kkapfdpdlv lstgndnqgi dvygmpttrs wgfslkcef
//
LOCUS       WP_118307964            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118307964
VERSION     WP_118307964.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121688
     Region          24..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrlsvvfl lligtltyal aaerqvegvv issedklpli gasvyvtaed lkkngnnqst
       61 igvitdidgk fsisipdgit rfycsyvgyd vveiklipgk kqyditlqps ahmldavvvt
      121 gyqtverrkl taavskidis dqmvgaaksi dqaltgqiag lsvsnisgap gapakirirg
      181 tsslngtqdp lwvldgiple gtnipsmevl kdidnvgqta iaglnpadid nitvlkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs skltyspkln idrlnllnse ekvgleldll
      301 esgypyretk gevyriisgl gelqnfkdgg wnalssnaqg ainrlkatnt dwsdilfrda
      361 ftqeynlsls ggsekatyyt sfgymkengn ipnvsaerln lvmktsykvn silkvgasmf
      421 anrrknstyl pddrgltnpi yysrlanpyf tpydangnyn ydvdveddtd mdfglnlfee
      481 rkntsnetti nglssifdae lrfddrfkit tqlglqldkt siekiaeees yvmrtekknh
      541 rnngvtylpe ggfhkanens lsqltwkamg eyrdtyndih efevmvgtei rktweeklys
      601 agygfdrktl ttkpiifpee sqafklheka hvenayvsaf stlsysllnr ytlggsirfd
      661 gsdlfgvdkk yrylplysvs glwrisqepf manakwidnl vvrasyglqg nidkntspyl
      721 lgnyrienil pggsedmidv sgapnkklrw ekthsvnagf dfavlnqain lsvdyyyrkg
      781 vdligtqmlp letgfemltv nwasmqnqgv evalstrnih tknfmwttnf nfaynnnkil
      841 kealredale pgregypvga lfalktagld eegypmfegk dgkavsamef fklqewgfga
      901 tdltarerre lytyvgtadc pytggfnntf tykafelgvn fsfdfggkvr sqptysivdf
      961 dkgrntnrdi lnrwtpente tifpvllsqn erldeymwys nqneiyrnld iwirdlnyvr
     1021 lqnirlgytl ptnfsrklgm asatiaiegr nllvfgssyk nyldpetmsn ayatpapksv
     1081 tlslnlnf
//
LOCUS       WP_118308199             925 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118308199
VERSION     WP_118308199.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..925
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102465
     Region          46..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mninrmlmla tavvsltana qvklddknan aydlgygvei snflstasat titgeelqqt
       61 satnlaqaly grlpgltals qggfsgdenk gasfnirgyh tlsdksilil vdgyerpidr
      121 lsveevesvt ilkdaaatal lghegingai lvktkrgveg kthvkvnysh kfqfdpefad
      181 mvdgygyana fnrarhndgl stayteqeln lfkdgsdpyf ypnvnwrdlt fkntaeedha
      241 yvsvyggtnk vkyythidyt dvrgafkdtk lpdyntqlrq skanirtnld fnitnttlms
      301 vnlfgmfqet krpsdigadd ataaiyqlpa safpyktstg iwggneaygd anpiakiqes
      361 gfykthqrql wvdaklsqkl dfllnglnvf vsagyanssi yaenshkahq ygyerytgti
      421 gdknnvalnp fgnketnltf stwnagqwwk akasvginyk rsffdndhfn atvvydnsgv
      481 stdgrgntfy rqnimgvfhy dfqnryvadl vlagngscrt ypskwafspt lslgwiyadn
      541 ndallnygkl rasagiqhtd ymptygmwlp twdvshgyvi ignnygatwg aslgsfpttn
      601 fsqetstsfn lgtdlrlana ldisvdafyq lrshimlsas nenssvvgiq ssyndvgevk
      661 sygfevsaky vkkitsdlnl nlganlswar nevskyigtp typlsdpvgh rvneawglks
      721 agffkdqtdi nssyrqeyst vspgdikyqd lngdqvinef dvtslngatd ipelnyafnv
      781 gveykgfgln awfqgtgnym kylpsaiwgg madngnlsvd yynncwdvag nnalyprltt
      841 lnnsnnsqks nvwykpvhfl kmrnievyyk vpatvlskls ltaakvfiqg enllsfdnid
      901 amdaevlsta ypmfkgvnig vtltf
//
LOCUS       WP_118308827             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            eggerthii].
ACCESSION   WP_118308827
VERSION     WP_118308827.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides eggerthii
  ORGANISM  Bacteroides eggerthii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Bacteroides eggerthii"
                     /db_xref="taxon:28111"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109754
     Region          5..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mssaktlrvs fvgmqtqeva ikpnvrvilk sdaeqldevv vtamgikrdr kalgyaaqdl
       61 nseqlnkagt tslasaiqgk ltgvdirqss gapgassqii irgarsfdgn nqplyvidgm
      121 pinttadfdt gnsvtganya drsidinped iesvnvlkgq aasalygira sngvivittk
      181 rgsknnmnkp nvtistnlsa qrvsrkferq diysqgnsit agydptssmt wgpkiselan
      241 dpkyggnmnn qytatdgmhe gqyynpkraq aglsgwttpq iydnvgdflg tgftentnvn
      301 lsqsinginy sfgvnnshqn giipstgmdr wgarglvdwk inpqwntgfs inysstkits
      361 apgandgimn vvysapaeyd lkgipnhepg nptnqilfrs tsftnpywwa ehneylqhtn
      421 rafgntyley qpnlglgenf slkireqagl diwtsdyati remgstsslk ggdienygsq
      481 hnvfnnlftv nfdgkfgksd ewrlnvilgn efnhesirnw dyygsnfnfp gftnignats
      541 ltsseykrqe rtvgffgsls mswqdqvylt vtgrndyvst mprgsrsffy psvslgweft
      601 klpflqnnki lnygklrasf aqvgqagnyy anyyytptyg ggmysyypvt yplpsgvstf
      661 ipyyrvydeg lkpqnttnye igadlhffgs rlkveytysl qnvedqifyv pvdgatgyqe
      721 mltnagkmrt hahelsinta ilqakdfdln lginftkvnn kvielapgve simlggfvep
      781 qvraqagcty pniyglgfkr deagnlllln glpqssgnsq dlgncspdft tgftlggryk
      841 rlslsttwsw qqggkmyhgt nmtlnyfgtt keslpyhegs miaegidevt gqpntievnk
      901 adyyqayyni tesgiydtsf vklrdltlty qlpklgifdi siygfarnvl iwanlpnfdp
      961 essqgnnnms gyferfsvpn tssfggglti nf
//
LOCUS       WP_118310334            1214 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118310334
VERSION     WP_118310334.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1214)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1214)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1214)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1214
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1214
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=136840
     Region          49..117
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          133..1213
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkkrddgip vreacvkkwf lvmklicvft lflllkvsan gfsqkkisld fekasmleii
       61 qelrqqtgyk fffnhnelkk vkdvsvkfvd eeleqvldvl lgkvnlsyri eqgviiivpg
      121 evkneerevr iigkvtderk qplpgvtviv kgltlgtstd vngrfsltlp kmqnvsllfs
      181 figmetqevk ytgqdsihvv lkeaaeqlde vivrtgyqni dkrkltsavq tikmddikva
      241 gvntidqmle gripgmifmq nsgqvgaapk lrirgtstvl gnreplwvld gvvltdpvnv
      301 dpaqindldf vnllgnaisg lnpndieqid vlkdasatal ygakagngvi vittkkgkag
      361 ppsvtysgtg sftrrprysd raiylmnske rvdvsrelve rgvyynnvds wvgyeavvqd
      421 yyngaidyke ynrlvsyyet lntdwfdivc qdvfshshtl slsggsanir yyaslgmsde
      481 ngaikgennk rysttlnlta nyerftarfq lqgnvssrny npselgvldy aynmsravpa
      541 fnpdgsryfy qrtsgsmpvy nfnvlnemdn sgdktkgsai nmqahigysv iddlklegtl
      601 syavsntnqe iyftedtyyv hklradqter ndmcpvggel rksdvrntnw marvqanytk
      661 nvgnegkhnv sgsaglelns qrydgfnitr rgyhrdrgkl fssvpqtytg yynqfmasan
      721 algvitenlt nsvawyamag ydygnrymvn lhirgeasnl fgsrandrmm piwalsgrwn
      781 mkqdilksvd wvddmalrgs fgyqgnmlsn qtpnmiirqe tdytgkygef hskvahypnp
      841 dlrwektast nltldfsllk nkingsvswy ykktrdaflt ktiseingit qyvvnsgtlv
      901 nkgievslnf tpinrvgldg gkrgfvwrid pqlgqvlnel vnnainnrnn vlrdeieytd
      961 mltgdvdiag eplntfysyr fkglssvdgs pifygaedel qeelskkynn meredvflev
     1021 mersgrrepy lqggisnylg yrnfglsfnl ayslgnkirl lklcteygtt nphpssnlrr
     1081 efvnrwrkpg denytnipgl ntvagthsnp wwssgpnsth riasniyemy dnsdirvvsg
     1141 nylrlsslsf rynvddrfck klglksayin ltgtnlftia hkklrgqdpt qsgsspsvnl
     1201 svrptyscnl sitf
//
LOCUS       WP_118310404            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118310404
VERSION     WP_118310404.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116237
     Region          52..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktydrkvf krkllsrrma vivvirlfmv lllgfpvlvn agtrdstrle srqvegkvtd
       61 ekkvplpgvt vrwegtsvgt atdaegrfkv lmpvdsatlv vsfigmktvr vkipklkage
      121 vrkvlsivlw dedvkledvv vtgiftrkke sftgsastys aaelktmgtq nilqslktld
      181 pafailednq fgsdpnrlpn meirgkssml glrdeldadp nqplfildgf estlaaindl
      241 dinrvasiti lkdaastaiy gskaangviv vetvkpeagk lqvnytgnmn fsmpdlssyn
      301 lmnareklef erlagryepv nwsttnevvl nklyneklkv iesgvdtywl aeplrvgvnq
      361 khslyvqgge gnflfglgag yngisgvmek serdvisgni dliyrmpkfq fsnkfsltst
      421 hlknpivafs ayaaanpyyk kyneegtvdk wleyndyfka snplwnasqn srdegknlll
      481 snyfmaeyfp taewrvrarl gltygnddte kfysrndtry envettkkge fysnnvrtnq
      541 veaevsvtya kmlgkhrinl vaggnissne slsqgysavg fpdgdfsyps fsngypeygt
      601 payyesvsrs vngyfnagya fddrylmdfs lrtsgssvfg tsrkynttws vgvgwnlhke
      661 kfimdhvawi nvlklrasig npgnqsfdsa qslltyafqf gsmnyfglga elsqvgnpdl
      721 ewqitvdkni gldvtlfnkr fsltadyyyk vtdpllikvs tplssgtaty mtnageqvsq
      781 gftasvsyyv fqnfekrfsw mvranvrtqk nridkignkl stlnasgkge ntvryydgad
      841 pddiwavksa gidpsngkel fyakdgsyty efsyddevvc gntrpdvegv igsslnwkgf
      901 svslnfryqm gadvfnealy nkvenisknd lnknqdrral yerwqevgdi vhfkdiasae
      961 ttpmssrfvq eenvltlesi yvgyefydgw ikklglsslk iqasmrdvfr astirsergi
     1021 aypfarsmea glsfnf
//
LOCUS       WP_118311280            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            AM23-5].
ACCESSION   WP_118311280
VERSION     WP_118311280.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. AM23-5
  ORGANISM  Prevotella sp. AM23-5
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Prevotella sp. AM23-5"
                     /db_xref="taxon:2292054"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116494
     Region          24..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmtvva glalstsmaf aqsqisghvt ssedgspvig asikvagtnt gtvtdidgnf
       61 slnapagakl eityigmqsk takassnmki vldadnqsld dvvvvaygta krqsitgsvt
      121 avdskeienr istsvtgale gaapgvqvns sygepgkapt ihirgvgtlv kdadqplyvv
      181 dgaafdgnis elnpndiesm svlkdaasaa lygnraangv ilittkraky gikptinlqi
      241 nngvytrgig eyerlgadqw measwlamkn yamsgsmgld ataaaqyatt hlisdyvkrn
      301 iynakddalf dangkliasr lsgyddldwq dgvertghrq eynvsgavsg ekfnvyasag
      361 ylnekgytkn saferftgri nskftpskwf egginlsanv snrqfndgak gslfanpfhv
      421 trymapvypm ymhnadgsya ldengekqfd vtseylsnrn iayemtadkd ktrravidaq
      481 vygkinlpyn fsvmvkangn nstenrqtyn npnigdgaan ngrlisyayq yatytaqell
      541 twnqtygkht vdvlagheny swerkltsgm ntnmaaagnl tmgnflknsf fegsddvdkt
      601 esylgriryn ydekyfadfs yrrdgssrfa kdarwgdfys fglnwnakke sflqdvewln
      661 dlrvrasyge vgnnagvsly ayqslyeink nggngafisq slpapnikwe ttqtvdlgve
      721 grvfdrlnfs igyfdkrskd llfevrlpys agsfphnenm tnwsiyqnig tisnrgfeia
      781 lsgeiiknkd wnwtvsadat tlknkviklp ggkdilhgvq kyseghsaye fftyhfagvd
      841 qmtgnslydi adenveaaen agtlvtingk nyttetsyae rkwagtalps vygsfgtnlr
      901 wkdlslgvlf tyslggkvyd asyrslmsta sassasanhk dilkswngvp egmtetspnr
      961 ldpngtpiid fnlstynndt sdrwltsady lifkninlsy nlpkawiqsm giqglqvkag
     1021 aenlftltar kgmnpqysfn gdsedtyvsa rvfnfglsvt f
//
LOCUS       WP_118311665            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Prevotellaceae].
ACCESSION   WP_118311665
VERSION     WP_118311665.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117070
     Region          24..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkrltmlmg glvlstgmal aqttvtgkvv sqedgepvig asvkiagtkt gtvtdvdgnf
       61 tlpnaskdav levtylgmep kkvkasakmk imlvadsrnl devvvtamgi srsskalgys
      121 aavvggekis esrtndvmss lagkvagvqi sstssdpgss nsviirgvss lsgnnqplyv
      181 vdgvplnnst vsssnnlvss nsldngydfg nganavnpdd vasmtilkga aatalygsra
      241 angvvlittk sgkkqnkgig veyngglqfe svlrlpqlqn efgmgwygdk tdiengswgp
      301 afdgstlkyg nvydnsqklk sylpiknnvk dffdtglrys nsvsfngatd asnfflslsq
      361 ihddgiiptd adsynkytfs grashkiknv tlsmsanyay qknnfvttgq ktgsmynaim
      421 qtprdisive mkdlndpfnt pgyyytpygv tnpyyilnny kneyeserfy gklqldwdif
      481 tdlkfstrfg ldtttgdhnt gepnmsalya ntpnwadalk sltgsvteqt errremdfna
      541 mfnythkfid kldvnaalgf ngnerkytyl ygavtnltip tyfnltnsse kptldqyqsl
      601 rrlmgaygqv elgwddwayl tmtarndwss tlpkgnrsff ypgvtgsfvf skflspeaqk
      661 ivtfgkfraa wgktgndasv ymtnsvyaqa santsgwgss kfpftngnyn aytkgntlgs
      721 ntlspemtte fefglnmafl qnrisfdvsy ydrnsdkqif slnmdpasgy tyqnmnlgki
      781 rnrgiealvs vtpiktkdfk wdlswnftkn kskvislpee lggesviygf sggtslyaiv
      841 geelgvfkay tskrddqgrl ivdanglpqk tdkqeivgsm nskyqmgisn tlsykgvsls
      901 fdfdirkggv mfsrtknity ftgnaiqtay nhrnpwiipn svvqsgtdan gapiytentt
      961 altptniyny wnngadnyda eflvdksyvk lrsvvlswdl pkawlaktfl tgvkvsvfgn
     1021 nlflwtpssn tfidpesssf gndlsgnfge ysanpssrkm gfnvsvkf
//
LOCUS       WP_118311735            1128 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Prevotellaceae].
ACCESSION   WP_118311735
VERSION     WP_118311735.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1128)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1128)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1128)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..1128
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123388
     Region          40..1127
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maktnktmnl afalmvgsag aayagipavn svqnvqqdet ctgivkdatg etvigasvlv
       61 kgtttgtvtd ldgnfelkgv kkgtvlrisy vgyetqevvf ngkplnvtlk ddakslnevv
      121 vtalgmkret kalgyavtel kgenldknlv npvsalqgkv agvdisgsdg glfgsakili
      181 rgastlssnn qpiyvvdgvi ldngvkngda dwsqndtdwg nelknlnpdd fesvsvlkga
      241 aatalygsrg lngavvittk sgkgkkglgi nfsqtfgidh vyggpdfqnv rgdgymsgya
      301 nfkssgnmqd tdsfylnadg krsvafpdgg ggvswgpkfd gqpiefydys tvnyspyknn
      361 ftdayddafn tntniavsga ndktsfytsm sykyangttp nnsfsrlslm akashkitnk
      421 veleagitfa nsnpkqggmt nfgecfidgt fsrmydtryw rsrykgvhgg lastayndey
      481 gnapgrsvww siyeneysqk etsvrpnvkv tadltnwlkf saegnynyyy krseskelgs
      541 gyaneggayg lgqytkeqtn lnanfswnka vsdfnisgfi rgeyyhnfqq essmktkggl
      601 ivpgqyfign sketpeasat isgektimsi agqlalswkd qvyldvtgrn dwssslvytd
      661 khgnfsyfyp svsgswlihe tfrgklpswi sfakiraswa qvgndtdayr insaytiygi
      721 dktyglqvpe tlydsnlkpe rknswevgid wrflnnrigi datyyrentk nqimsisvps
      781 isglsnqvvn agniqnqgve lalnttpiqt kdwewdlnft ytknkskivs lhenvanyis
      841 lvgmpsygnf rigsvakvgg eygllmsdat pnydektglp iletasyngr havyysrsgv
      901 ekevgsiqpd flgsvnttlk yknwslsasl dmrfggmvai ygshygtayg ylksslngtd
      961 aahggityks iwdgkqyddg iipeaimpgg vtintptgny tiaeggelya dlvkrgivdp
     1021 qhasswnywn nswgrasvwk nndwfhelny ialrevslsy rmpqsianki gasnlsfvlt
     1081 grnlgyllns lpnnfnpesm rgtqsgqfmi rsvspytasy tftisatf
//
LOCUS       WP_118313720            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118313720
VERSION     WP_118313720.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118606
     Region          28..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknryilllf tlffvvtgsv aqdgavivsg tvydkagnne tfpgvniicr daktqkrirg
       61 tasdleggfs ikvpvgselv ftyvsykpti ykvkksvsgi sifleenine vqetvivgqr
      121 rvskanltas atvidakela dtpvpnimnl lqgrvagmdi qmnnglpgas gtynirgvsd
      181 islvgnndsg wdlassaplf vvdgipqtdv edynaeglis gsgvspisni pvedianiqi
      241 lkdaaatsly gsagaygvil ietkkgdspk prvtysgnft istppslrev aignternll
      301 kwqilnndts qlyhgyqdim fmpavsdsln pyfnnntdwq dqfyrvtynq shnisfsggd
      361 nlfnykvngn yytekgivkn tdfnryaltg nmnytspnsk ftigvdmkvg ftdnstgsgn
      421 avsqsgvasg asassllppp slysasvaal qvfgvgnstv ksnysatvnl gyalpfdikw
      481 rgtfnysyns tdqekftpai lsdskysaia ynynsneskv yidthvsrtf dlkyvmlglt
      541 tgirynsrts tgnsitytgl pndyiigpvg hgksegsatv sqnqstfsfm fapnfkiktk
      601 dsfkaggdky ifdptispel ssvygtrtkw ninpslgfrw nigyesfmdr ftwldnmsfr
      661 ltwgqvvkyk atrydvfgty didpgntyng esyipidykr lpninldpvt tttwnfgydm
      721 sifnnrlsan idayyrqvdn qlsdielpnh agfekvrste vslvnyglev slrgkplsvq
      781 skwnlligln falnrdvitk lpnearqiln sdawvanrlg gnttsmllyi nkgvyatded
      841 vpvdpatgkr lrlggkntde ayfkagdpiw vdvngdyvid dkdrvvaana rpkvtgglff
      901 nlsykefsmh vntsfvfkrd iinsvlaksf kayddpvrks ieslrkdasl spiekynfwt
      961 ennrynaiyp npynyhhnkv idpfreaqtl fleegsyfkl ntvslsyrfp krwldffrvr
     1021 gvtlkasvnn iwtfsnysgi spesvnglgr dtsggypnsr twtmgvvlsl
//
LOCUS       WP_118316934            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides bouchesdurhonensis].
ACCESSION   WP_118316934
VERSION     WP_118316934.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides bouchesdurhonensis
  ORGANISM  Parabacteroides bouchesdurhonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Parabacteroides bouchesdurhonensis"
                     /db_xref="taxon:1936995"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115004
     Region          42..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlknskpvsl illagalcfs gnvyadlapv kqgttisqqs gkvtgtvedd fgpvtgasvv
       61 vkgttngtit dfdgnftled vkkgdiiqis figyttleip yngqpfgsik laedtqklde
      121 vvvtalgikr ekkalgyatq elkgdailda resnvtnals gkvsglqvvr ssggpgsssk
      181 ivlrgnssit gtnqplivvd gvpmdnfqgg vadawgnkgp dmgnglsdin pediesmnvl
      241 kgasaaalyg sragngvili ttksgkkqtg lgitvnagvt aetmfmepdi qssfgqgstg
      301 iynvksrssw gpiadgsvni dswngqnvpm ytydnvgnyf dtgvsfnegi sfqqanegts
      361 vfasinrsdd kgivpgakls ktsinlrgtm efgpdkrwkl dgkinylnni ghnrplqgin
      421 qsnafstiyn lprsinildl kncvdsegqm iwwdtektpq enpywtkdyr tnedtrnrfl
      481 gtmslsykif dwwnvelkgg tdyytttttn klyaggnvtp kgnysegset fyennfsflt
      541 taqkdnllgk fggfvtfggn lmmqkrtkek istgdllipn lfsvnnaadk nnmgyeytlt
      601 qrkmnslygs lqinydgwmf ldltarndws stmssanrsy fypsvslsav vsdmiqkngg
      661 slpdwmtfak vrasfaevgn dldpyqlytv ysmekdpfgn pvakpgnvly npdvkselik
      721 sweagvdlkf lnnrlgidfa wyksnatrql ldlpldpfsg ysskkinagn iqnagveima
      781 yadifqnpkg fswnitanls fnrnkvidly eginemglsd gsfndevkvv artgglygdi
      841 ygrkfqrves gpdagkiivd aqglplltse lqylgnqqpk cmlgitntfn yknislsfli
      901 dariggkiys attaklyyng aaagtvvnga reefvvpnsv tasgdsytan ttpvtpqlyw
      961 eragngnlgv geaflydatn vrlrnltlgy sfdkkllakt pierlrlsft annvwmiash
     1021 megidpesvs ttntnatgie lgaaptsrsy tfnvtvgf
//
LOCUS       WP_118318965             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides bouchesdurhonensis].
ACCESSION   WP_118318965
VERSION     WP_118318965.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides bouchesdurhonensis
  ORGANISM  Parabacteroides bouchesdurhonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Parabacteroides bouchesdurhonensis"
                     /db_xref="taxon:1936995"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110805
     Region          24..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrksfilfvl fcigtctsvl waqkkvsgvv mekdasmpli gcnvvekgtt ngtvtdldgq
       61 yalevgdnav lqfsylgmet ieepvgdrtv invdmfsdsq kieevvvtam giqrkakslt
      121 yatqqlagqe ltrakdanmi nalqgkaagl vitpnatgag gsskiilrgn ksafgnnqpl
      181 ividgipmnn pkttqlegey egrdggdalg nlnpddiasm nvlkgasaaa lygsmaangv
      241 imittkkgrd gaarvdfssn itletpltap klqgrygaik ngdqlsaksw gekvnnndse
      301 akdrlndffr tgstyinsvt inggtekvqs flsyanttal gmmptndfqr hnmtaretfk
      361 lfkdrltvda slsyitqkat nrphggtyin altgaytfpv ngdwnyykkn yevydggrnl
      421 maqnwytsld dftanpywvl nriksqekrd rimasatakl kvtdylnvqg rlsvdntfdr
      481 ferkwyatty eawapvgngr yrqerfdakq fygdlmanfn ktwnekweln aslgtsflqt
      541 qvqntlldsd klglvlpnvf lpeningngn qkttnpkkrl nsvfgtvqfg ykgmvyldvt
      601 grndwassla ytnnysyfyp svgltvllne mipmtekinl lklrgsysiv gndveayity
      661 pmdhynlgql epntkepfte mkpekmhsme fgidlgmldn rlnfdityyk tnnknqyfsi
      721 daplgsgyes yyinagniqn qgfessisyr wdfakdwswk pefnisyndn kikelsdklk
      781 dgvslgsgag irfmlkeggs fgdiygkdlv rengvivtqn gspvlsdeey lgnvnadwhm
      841 gfgntftfkd fnlyflidgs iggnvvsmtq syldsfgvte etadardngg vnlgdgtmmd
      901 aqrfyeatgg kdkavgqyvy satnfrlrel slgytfrnll gasknlnlsf varnlfflyk
      961 dapcdpdmsv stnngwqgfd sfgmpatrsy ginlkvtf
//
LOCUS       WP_118319133            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides bouchesdurhonensis].
ACCESSION   WP_118319133
VERSION     WP_118319133.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides bouchesdurhonensis
  ORGANISM  Parabacteroides bouchesdurhonensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Parabacteroides bouchesdurhonensis"
                     /db_xref="taxon:1936995"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116154
     Region          43..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkkfrpvsl illmgialsf sgslyanpet enpvtdisqq ngkvsgtved algpvtgasv
       61 iikgttngti tdldgnftle gvkkgdiiqi sfigyitqdi pytgqstikv dlvedtqkld
      121 evvvtalgmk rdkkalgyam qelkgddlia srepnlansl sgkvsglqiv rssngvggss
      181 kivlrgnnsl tgsnqplivv dgtpmdnftg gvddvwgnsg admgnglsdi npediesmtv
      241 lkgasaaaly gsragngvil ittksgrkte gvgitvnagi taetiflkph mqdnfgqgsv
      301 nvydnqsrls wgpkadgqmv tdwlgrevpl htydnidaff rtgtsfnegv sfqqdingts
      361 vftsinrsdd asitpeskln ktnitvratt fldkdkkwka dakvnyinmn ahnrpiqgvn
      421 psnafntiyn lprslnikef ekcvdengnm iwydasknpq enpywvtkyr qnedtrnrll
      481 gnvslkyapt dwfdielrgg tdyytttkne kvyaggntsp rglysegset fyennfsfla
      541 tarkdnlinr lggfitfggn lmqqqrnkmn asagellvpd lfslnngvnk ptvtselirr
      601 kmnslygslq lnwdgylfld vtarndwsst msnanrsyfy psvslsavis dmlpklgsqm
      661 pdwfsfakvr asyaevgndl dpyqlynyfs vskdpngnnm akpgkvlfds nvrseliksw
      721 eagfdirffn nrlgldaawy ksnatrqlld lpmdpfsgys srkvnagniq negvelslng
      781 aifdnprgfn wnataqfsln rnkiidlypg vtlydiktfd aiqivavqgs lygdiygqtf
      841 qrvtdkdsph ygkivvgddg lplistdksk vgnqnpdwml gltnsfaykg fnlsflidfr
      901 iggdlysata sglytrgnae gtvvngdrqp fvvpnsvmqs gngyvennvq vtpqnyweri
      961 gstgnyglpe mytydatnvr lrnitfgyef drqmlkktpf qrvrlsatcn nvwmihynlp
     1021 gidpesvaat ntnatgfeng aaptsrsytf nvtigf
//
LOCUS       WP_118322991            1127 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM10-21B].
ACCESSION   WP_118322991
VERSION     WP_118322991.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM10-21B
  ORGANISM  Bacteroides sp. AM10-21B
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1127)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1127)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1127)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1127
                     /organism="Bacteroides sp. AM10-21B"
                     /db_xref="taxon:2292001"
     Protein         1..1127
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125336
     Region          43..1123
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfikrewgd ashwklhlhk glvimgmala flfagnayaq evktikgtvr dvtgepliga
       61 sviekgtnng vitdvdgnft lkvpadatls iaymgyatre irlakrkkqg dlrvtlreds
      121 qqlkevvvta mgikkdtkrl gyavstiesd eivkagatnf asamygkapg iritqtqggs
      181 agavsinvrg ltsitgnnqp liildgvpir nggtgkstdf aefgndgqir snglvdinpe
      241 diesvsvlkg asatalygse aangavvits kraksgkltv dftaqvtanl paylpkvqts
      301 ygpgryntey sdyekqtggf yqrtmngesy kslynttmsf gpkydgsdvl ywdgkvrpyl
      361 patdnpwkel frtgwnqtyn laisqgtets snrfsytfmd empnaltgsf tkhnfkltgs
      421 yklakpltle yslnyiiqdv kdrpqtslnl ygsfsnmfss fmdipylkqs yvtslgyrnt
      481 yaiggdatlt pdeawaynpg ylngvsnmlw nmyhhhsket enrligmirp twqitnwlsl
      541 raqiatditd tkqtleyete rpnslydpsg sfqninrryd ivygdvmlnf nynirrfdia
      601 atlgwtgrye nmnnmrvstn gglvtenwfd lnasrytass tlqrmellkt gymgtlslgw
      661 dnylfleltg rqersstlkd qsffypsanl sflfsnafrm pawwnhgklr lsygivgnap
      721 etyaanviye qgsdngftwn yvpsswgnan irpekkyeye igfeskflnn rvgfdvsyyn
      781 nrvkdqilst pqpstsgvky vlmnvgevan egwdisvsat piltkdfrwd ltanygiyrn
      841 kvvklaegvp yleisniggg gakiqavegr pmgdiyvqvp qvnengdylv sdkglylnqt
      901 dlqrvgninp dgvgglfssf syknifldfs idfriggdvi nemyqystas gltpeslqyr
      961 dtehgglsyy ypgnnnasgv pvqvdpslga gpngeviyhd gvilpgvvas tgekntriip
     1021 agyyynqtyn wgtqpeqyty hhsvfdntyv klreltvgyq fpeklvsklg mtrlsvsvfg
     1081 rnlfyfykal knydaessvg tswasqavvg gsttatrnfg vslrasf
//
LOCUS       WP_118323351            1009 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM10-21B].
ACCESSION   WP_118323351
VERSION     WP_118323351.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM10-21B
  ORGANISM  Bacteroides sp. AM10-21B
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Bacteroides sp. AM10-21B"
                     /db_xref="taxon:2292001"
     Protein         1..1009
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114659
     Region          34..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktlyiyiil mlllpffses niyaqkkskq yseitakvvd kegnpiqsvk itvdeglfes
       61 ftdkqgvfsl kvtnnstlvf dmlgydskyl evsaikqnpv vimeksipyg gvedkvelpf
      121 retvarevvg aistigedii sksnqmnvln ilsgkapgln vsqvpaepgr satilnirgl
      181 srsttdnapl iiidgierpl edltpeeies itvlkdatsk ilygpkavng vllvktkrgi
      241 kykrerqfni efgaqlpvrm peylnsaaya tmynqarfnd glspyytqad idgyrmktns
      301 ilypdvdfhk lclndhmsyr kaiaqfrggn eaaqyyvnat yagyggyeai gnsntsnkfn
      361 lrvnldykvn dwlkafvdia gqmefyttny mladelffrl sshrpnaypv rfsdpenset
      421 eiygamenan lassreniya emllggsken tvrkgqtnig ldlsldryvk glsakayvtf
      481 dvynylvvgk nenfssyrpl fsknsligke lltvekkvsd ksriedqmyr nygyfgqlsy
      541 drifrtkhql ksdlvifqsk renlgssqdd vnrtfalrtn yvynkkwiae ldmavmgssr
      601 fakgnrygyf ptvglawias eekflkdkew ldflkikast gllgtdnyfd fflfesrwnt
      661 nqsthfgpkl eedintstlv hvgnpdltwe ksfeinigae asflncltan fnyfnnyryd
      721 iltpitsfss inggelmyrn ygsvrnqgie laleysgnig kfhysiggnt iwskavyeka
      781 ddmeglpsnr kkegkpldty fglmaeglfk skdeiathpv qdfgpiqigd vkytninnds
      841 rinendmlpi gneyprfqfg lninlaykgf elslsgsgma qydiylnnsy ywmredqkys
      901 tfvkeyfnps tgegkfprls tqqnqnnyrs sslwmrsgnf fklrdamfsy slpqniankm
      961 tlkqvklfvr gsnlftissi kdldpeyida gvtgypffrs ftgginvvf
//
LOCUS       WP_118323217            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM10-21B].
ACCESSION   WP_118323217
VERSION     WP_118323217.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM10-21B
  ORGANISM  Bacteroides sp. AM10-21B
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Bacteroides sp. AM10-21B"
                     /db_xref="taxon:2292001"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115465
     Region          30..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myktirqfsi ffvvllmctt vsfaqtngsi tvtgtvidek gesiigatvq vegttngvit
       61 didgkysvrv endkstlrfs fvglvpvveq vkgrriinvv lksdtevlde vvvtalgikk
      121 ekkklgyavq dldaptltki psantasnlt gkiaglkvsn spnlfdtpal llrgvapvvv
      181 idgvpvesat fwevapedie smcvlkgpaa avlygqmgqn gviqittkka keavkisvns
      241 stgfdtgmia npsyqkkygt gyqgqyrvgn stdefwgawg peldgrllpq wnspydadgn
      301 riaipwiprg kdnlknmlrt gvvtnnnvsv etkfdkgdfr islsemhqkg vfentklnsy
      361 tvnmsggiqf skklrfdani nynkidspnf psvgygrnsp iysmilwaga nvdvrdlrny
      421 wapgleglqq rnfdigpgyd ngsfdynnpy filyenlhgy hknaaygsas lkydvtneln
      481 itlrtgvnmn qlmedyrtay staynrngny sqsykndfqi ltdliakydk klgifdvgam
      541 lgfnarqynd ashyaetdgl avpgiytlsn smkpttptss krelaeyavy gyldlgwkny
      601 lmlnltarnq wsstiptfgk nsylypsaql stvvseyipm pefisylklr gsyarvgsaf
      661 spyyfspvys etgtwnnnlg ltspeiiysk dikpsystgy evggelrlfn nrlgfdatyf
      721 yfidgpqtyn qpisetsgyg ayclnglktl rkgwelsita spfrndkgfn wdlilnlssy
      781 rnylhelpeg qtqygelkvg drmdaiygsa imyaptnsey agqviigdng niqkdnikqk
      841 lgyanndlmv gfsnnmsygp vslnfsfdac iggkmlsqyn rymwaggrsl diddqerqnw
      901 yagkeyiaeg vkvvsgelkr dgegnvisdt rkfapndipt nyfdyvqnsk gyygidecvl
      961 vdrsflklre vsltydltkh ltktpikgas vslvgrnlfl itksglvdpd qynentvwdn
     1021 lqtpsfrnig fnvnvtf
//
LOCUS       WP_118326081             926 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118326081
VERSION     WP_118326081.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 926)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 926)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 926)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..926
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..926
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102875
     Region          1..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvtlgedtq vldevvvtal gikratkals ynvqevkgde lttvksanfm nslagkvagv
       61 ninasssgvg gatrvvmrgt ksissdnnal yvidgvpifn tnkgdtngqy saqprgegis
      121 dinpediesm svlsgpaaaa lygsnaasgv ilittkkgke gkariiisnn stfsnpfimp
      181 efqnsyinra gsfaswgdka sslfgtyepk dffntgtniq nnvslsvgne knqtylsvgt
      241 tnatgiiqns kydrynftfr nttkflkdkm tldvgfsyii qedlnlmaqg eyfnplpavy
      301 lfprgenfea vrmyktydtt rkidvqnwgw gdpgysmknn pywvanemnh gmkkqryman
      361 aslkyeildw ldvtgrvrid natndysdkr nastdlyftn ssiygfykyy kaddrqayad
      421 vmaninkrfg dlslsanigg sftqtyyder gfqgglkdms nvfslynmtt tldkdtypie
      481 sgykqrtnsi fasaeigwks mlymtltgrn dwdsalinte qssffypsig lsgvisemvk
      541 lpkaitylkv rgsfasvgap ipknlssnkt yewdpatsqw klqtyrplpk lypertnswe
      601 aglnakffnn slslevtwyk antrkqtfqv plsgtavyat myaqsgnien kgmefslgyn
      661 kswgdfswns nltfsfnknk ivellddavd degnhyslse idkggigsak vilrkggsmg
      721 dmyvtnrlkr dnegnvyidk asqnvkkedi knsdefihig svlpksnlgf rndfsykgis
      781 lgfmlaarfg givisptqav mdqfgvskvt alardnegvp vnngkvdpqt yytevggisg
      841 lmsnyvysat nvrlqelsvg yslpakwfnn kcnlslsitg hnlwmiynka pfdpeatast
      901 gtyyqgvdyf mqpslrswgf nvkiqf
//
LOCUS       WP_118327757            1164 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118327757
VERSION     WP_118327757.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1164
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130320
     Region          129..1163
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mstkllseti crkglmvkcf valivfccsv geafaqtdtk vtinvnnvli rtaldqlqke
       61 akihfvydee nidsekrvsl sytetplnav lndfckqtsl ryevkrnlil ilpskaektt
      121 gkhepfymtg vvmdetgesi igatimiggt sqgtvtdidg ryslrvtpgd lvsftfvgma
      181 dkvvkvqagk kvvnvkmetn ataladvvvt gyqtlskera tgsysvisek stkgkletdv
      241 lsrieglvag inktssnsnd vvirgittym gntkplyvvd gmpyegdlas inptdvqnit
      301 vlkdaaassi ygaraangvi vittkrgqeg ktkvsyngsi klspkpdfdy lnlmssselv
      361 dmqiegfdyy htayenlnkr qavnpvvsll yqhergqltd gqladallpy rtndnrkqie
      421 defarvgivh qhnlaisggs nknrymatvn ymgdygnqky qskdrigfsl kddvdffdwl
      481 sadfgvtgsf yrskgdngag sysslmssyp syymlrdllg npldfqrtks dyelqrlqsi
      541 glmdetyspi knraeesyhn nsnyyrlhag lkfkilegln idlkyqaegt ydknrtlysn
      601 msytvrnmin daaqydaatg sltlnvpkgg qldesryesy sytmraqvnf nrifgkhais
      661 alggaerrlv rrtgaqnyym gyddnslgvk pinplvmspi ngteslsgsf nwvygeynal
      721 thtedryvsf yangsytfde rysltgsiri dqsnlfgtdp kyqyrplwsv ggswqianep
      781 fmedcmwlnr lnlrmtygvg gnvpkdagpy mtvvdsgyne wvgdfgsyiq nppnsqlrwe
      841 ktastnvgid fsafnsrlsg sidyyykktt dllgnrnadp tlgwasllqn ygsmfnrgve
      901 lslqsvniqn knftwgtnlm fsynkneltn legtketvfy ysaynvaavg ypinsvfsyr
      961 yaglnptngn vlvynkegek vskvssiddm vysgtrtpky taslknffsy rdfdfsfmfv
     1021 yygghvlrdv vagymggaps anltrkalnh wrkpgdenip gvapsfnrni yytdaqtwys
     1081 adihvkkady iklrdislsy nlpknwlrky fiesaavtcq isnvwwwaan gdidpeaytt
     1141 sgygwgaltl pnpttytigl slnf
//
LOCUS       WP_118337327            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_118337327
VERSION     WP_118337327.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124811
     Region          25..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkhlciii cflvnalama saanrtitgv visgednepl igasvyvhtd elkkagasqt
       61 slgtitdidg kfslsvpdkv trihcsyigf eeqvivlqgd kksyrivlqt sahtlgdvvv
      121 tgyqtlerrk ltaaiskvev sdamvgaaks idqaltgqia gvsvtntsga pgspakirir
      181 gtasmngtqd plwvldgipl egtdipkmdn kssdndivni gqssiaglsp ndiesitilk
      241 daaataiyga raangvivvt tkrgrtgkpv vnfntkltyt pnletsrlnl lnseekvnle
      301 lqmmkeapfn kwgfypipvy sekggvaail kqynlmdiyr ekgwegltpe aqnainrlks
      361 intdwndilf rdaitqeyni sisggsekvt yynslgytle ngnipgvsls rfnltsktsy
      421 qinkllkvgv sifanrrknt tfltdtyglt npvyysrian pyfepfdnnn nylydydvvt
      481 gsipdllqgy nileerents nksvttains ifdielrfnd qwkvtsqvgv qwdqlsreey
      541 agtnsfnlrn qrensayykg ndriylipeg gmlkstnstt sqitwkvqge ykntfndihn
      601 iqimagseir knwyenqast gygydpktlt fknlefrdsk qanewklktk sfkenafasf
      661 yangsytlmd rytlggsvrm dgsdlfgvdk kyrylpiysv sglwrisnep linqfkwidn
      721 lalrlsyglq gnidkntspf ivgtygnisi lpgsneesit insapnsklr wektasyntg
      781 idfsvfnqai nlsvdyyyrk gtdlignkml plengftsma vnwasmknqg ieinlqtrni
      841 atknfswyts fnfaynqnkv lkvmtekdqv tpslegypvg aiftlktkgi ksetgqiyie
      901 nkdgeavtie elfqmadkgn ldgeysigvd ketergfysy agtsdapytg gfmntfnyrn
      961 welnlnfsyn lgahvktdpt yyiadpdpgr nmnrdildrw tpenkngkfp altslntnpa
     1021 dyylfstrrd lyksldiwvk klsyirlqni rlayhfpsew lhklniggat vglearnlfv
     1081 fgssyknymd pesmsnlyst pvpksvtfnl slnf
//
LOCUS       WP_118337685             913 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Phocaeicola].
ACCESSION   WP_118337685
VERSION     WP_118337685.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..913
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102811
     Region          35..912
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkiifitc lalssgsvvk gqtavadscy lnegtaaist vtyerlekns slslqnslfg
       61 evlgltsmqg mngiwderas lsirglqsls nngililvdg ierpiadltv eevesvsvlk
      121 daaavalygy kgingallvk tkrgregkmd ikisydhgfn qplylpdmad sytyakamne
      181 ayandgkspr ynqfeleafk ngkypnyypn vdwtdevigd wgstniynls fsggsrkmry
      241 ytlfnlenns gffkntntne gysnqneysk anirmnldvq ispstslqtn vlgilteynh
      301 ssyntivdql ytvpsaaypi ktedgiwggd fvwgglnpva nlqakgysrs hartlmadmk
      361 ltqkldfitq glgayvklay dnsstfweir tktysyaadk vsymydipss vtrvtggkdt
      421 eltftknmng pmyyrfnfdg gfdynrtfgk hkvysllswr flhdvqkdrn ntinqqylts
      481 ytnygfmnry fvdlalvmsg snrlpdgykf afsptvsaaw nitredfmrn qsvfdllklr
      541 asagilhsdy vpswnfdvqn fggggsywfg nnkvsaggtq esrfpttyfr heramkynvg
      601 ldarlfnsls ltadayyqkr drimvvnnnv ssilgvnlpy spqgrvdskg velglsydkt
      661 igsltinaga rftlsknevi enlqapvayd ylsttgvpvg qqygleaigf fkdekdimds
      721 pkqlfsdvrp gdikykdqng ddfidendri aigyninvpe iyyafnlgme ykgfgfdaqf
      781 qgvgnysawm takglyrplv nnttisnyyy enrwtpetpd akfprltsve nanntqnstl
      841 wmtdasflkl rhcevyykfp lkliskarmk taklyvrgmd lfsidkievt dpevtgisyp
      901 vdrsihvgfa lnf
//
LOCUS       WP_118338011             898 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118338011
VERSION     WP_118338011.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98461
     Region          27..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgrvglclvi mfficsaqki daqvqnirek qdtisatksl ehirpenikk gplnnaldvl
       61 sgqsagvnvt tngtdrlaml nsirvrgtts imggndplvi idgvtsdiat lstiypadie
      121 sftilknate tamygsrgas gvieiktkkg tgrgfeisyd gnygfesmyk hlqmlngpey
      181 iataealgld ynnggyntnf hdvitrtgli hqhhlafsgg sensnyrasf gfmdhntivk
      241 vndyrnlvvk ldatqkafdg rlvgdfgvyg ysskihdifd trmlfysaaa qnptypagtd
      301 vngnwvknsa ashinhpgal lyekndseer nfnthlglkf nildnlilsa fgsysysstg
      361 naqfcptwvw aqgnvyrgef kgedyftnvs lsynnawgds hldavvgaey lkqvrtglwv
      421 qakgittndf synnigatss rpfggtsssy edpslasimg svtysykdry siaaalrgdg
      481 ssmvsdnntf gffpsvslgw dvkkegflsd tdfitilklr tgygrsgnlg gitsyttlnt
      541 vkengivsin gaptvtmgsi rntnpdlkwe trstfnigfd lgiwdnrlml tselyysktt
      601 dmlyeydvpv ptfafdklma nigsmsnqgv elgisvvpiq rkdmemninf nmsyqknkll
      661 slsgeyngmh mtasditpig slygvgqngg dnnvvyqivg qplgvfylph ckglkenelg
      721 gysydiedln ddgeidfsdg gdryiagqat pkvtigsnis fryksfdiam qingafghki
      781 fngtglaytn msifpdynvl kgapekniid qnvsdywlek gdyvniehit igynipmksk
      841 avkslrlsag isnlatitgy sgltpminsy vvsntlgidd krtyplyrty slglsiqf
//
LOCUS       WP_118338370            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118338370
VERSION     WP_118338370.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112230
     Region          44..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkieratqll flllisqggn aayanlprga sassvqvsaq ankitvsgtv vdvngeplvg
       61 vsvlekgtgn gtitdvdgnf tlsagegaal eisyvgyqnl tvsaketlgv lvmkedteql
      121 devvvtalgi krsqkalsyn vqevkndvlt kvkdanfvns lngkvagvsi qrsasgvggg
      181 trvvmrgnks ikgdnnvlyv idgvpmgnqa drtgdgtgfg agrtssegia sfnpediesl
      241 svltgpsaaa lyganaangv ilittkkgaa gkvsvnvsss aefsnpfvlp rfqntygnvs
      301 geaaswgekl pvpssynpad ffntgttftn sfnlsvgndk nqtyvsgsav nakgivpnnk
      361 yhrynamvrn ttkffndklt mdlsasyvre yynnmlsygt yfnpllgayl yprgenfeke
      421 tyferydael gynvqswtpg dfgmavqnpy wvayrnlrpe vkdrymlyas lkyeitdyln
      481 vsargrldnt yteredkrya sthgtfaksl gryiysnetf rqkyadiman lskpfagdfy
      541 anvnvgasfe eydtkgrgyg gqllkvpnlf aydnidpstg vpsqtggdnr kmnlgvfgsa
      601 eiswksavyl tltgradkps qlvnskspwi fypsvglsai vtdllpetmr qsispvlgfl
      661 kvrasytevg spipytgltp gtithtiegg vikpfkyypl pelkpertrs yevgidskwl
      721 nntvslgvtl yksntydqll eaklsetsgy dymfvqagnv enrgielalg ydqtfgnfsy
      781 stsltatanr nkiielasnv knpvtgeald lsdikvgrfr lregeevgti yaeerlkrdq
      841 dgyivynegq tittestepy klgsvnakwn lgwrngftyk gfnlnflvta rlggiviskt
      901 qavldqfgvs qasadardag kvmvgnvavq pkdyyesvvn ldaynvysat nvrlqeaslg
      961 ytfpnswfkg tpfhsvnlsv ygtnlwmiyn kapfdpelta stgtfgqgyd yfmlpsqrty
     1021 gvslkfgf
//
LOCUS       WP_118338284            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118338284
VERSION     WP_118338284.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121165
     Region          23..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meflllcaml vlsvspayaq rnrtihgivv denkeplpaa hvkqvnddpk gsiaavitdi
       61 qghftltlpy gtkeieasyl gytsqriklt atndyyialq pstelldevv vtgyqtiske
      121 ratgafskvd akkletqrls dmgsmlegrv agysdgkirg vtsmnglttp lyvidgfpve
      181 kttndgygnw iesvpdlnme diesitvlkd aaatsiygar aangvvvitt krakkdelnv
      241 sfsatltvqp ydtyadkyla gsstmveler ewarqnphls gdnvqsyaqt vldnmsyssl
      301 girnilnyya ghisrdqmes nltnlasqgy ryyrdiekyg krnpfsqqyn lnigkgtekn
      361 tfnasvsyrn nqledkysen rtiginlqns tkmtswltld vgtylnygkg ttqsfnlfsp
      421 gytympyngl vngdgtyytn teeeryslyn lnllhnngly nlditpldei kmnqtknrdf
      481 snrtfarltf kftdwlkyta sfqyeyaeyk teqlkskdsy evrnkvntfs tsnndgtstf
      541 alpygnifft ssntthaynf rqqldfnktf advhdvtmil gtetrenkle yndrtlynyd
      601 pqlltyslid agalsnfrgq wgyasfgqqn fayiselinr yvsvysnaay tydgkymvsg
      661 sirwdktnlf stgskyqkrp iwsvgagwnv drekffhvsw vnmlklrasy giggniakns
      721 apymiayysn nnqvggiqgt issrpnpnlr wektttlnvg vdfallgnrl ngsieyynkr
      781 gtdllantng vptegwgyst ysinngkmtn qgfeltlsgd virnndwnwn isgvlgynkn
      841 kvtyinveap vsylvidypt ayprvgnpyn aiygyqwagl setgtpqvyd akgnlytdmt
      901 ppeiedlvyl gttvpvyngs intnlrwknw elaaqflfeg ghkmrntnva fissgmgvvs
      961 kdienrwrep gdeaytdvpr yisseselyn ynyqsmyans sinvidatnw rlrnlsltyr
     1021 ipasvchkly lknarimlgm envfmvakss nakyllggyt kpnylcgvyl nf
//
LOCUS       WP_118356250            1136 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118356250
VERSION     WP_118356250.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1136
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124749
     Region          41..1135
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkrlksvsm llflmgastg aayavanpgv tdvkitqqsg tctgivkdat getvigasvv
       61 vkgttngtit gldgdfslsn vkkgdiivis fvgyqtqevk wtgqpidvtl kddtqqlgev
      121 vvtalglkre ekalgyavte vkgdelkaan tispvaalqg kvagveisgs dgglfggtki
      181 qirgastlss nnqpiyvvdg vildngvsgn ttadwdagan nasdygnelk nlnpddfetv
      241 svlkgaaata lygsrglnga vvittksgkg tqglgisvsq tfgidhafkt pdiqtlygpg
      301 ympgqsdadq ngsmwdehqf tvnqngehtl vgvpnfgfgp rydgsqirny dgtwttyspr
      361 knnmldlykl gfntntnvsi rggnektsfy tslsyknaks ttenntfery smllkashkl
      421 ndwvdvaasf sfanskprna qlnagelfvn antnvinplf dvdyfrnkyl gehggiasts
      481 ygdqygsvps saknyffkvd nydyvrketv irptfevnvk mtdwlkfkad anmnryytsi
      541 edkqlgsgya neggyygitq dikeqftvgg tftaskqikd fslggfarfe yyntssqhsk
      601 vstdggmvvp gewfvenskk tkksestisg skriisaifa lnlgwknqfy ldvtgrndws
      661 salvyanrtg nhsyfypsvs gswlinetfr esmpswinla klraswaqvg ndtdpyavnq
      721 tysfatmemy dgniytneld klmkiadlkp erknsweigl dfrtfnnrln ldftyykent
      781 tdqimkinvp aisgvtqqlv nagniqnsgi eialnttpik tkdwqwdldf tytrnrskiv
      841 slhpnvanyi elsgyvnayd yhigsvakvg esygvlmsdv tqarnengvp llewddswrg
      901 ayraqsktae vvgnmtpdfl gsvattltwk dlslnvgldm rfgglvasyc nlygtqagwt
      961 esslqyrdpe hggmtwtsqy adskgiqytd gmipegvfke gtiatlvdgt kmdvsglsya
     1021 qlvqegklep thagswygnn yawgaqtidd swvhklsyia lrnitinyrl pnsishklga
     1081 kglnlsfsar nlgylynslp nnlnpesvrs nsasefrirg fepytasyif tinanf
//
LOCUS       WP_118356258            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118356258
VERSION     WP_118356258.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          39..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 krlksvsmll flmgastgaa yavanpgvad vkitqqtgtc kgvvvdatge tvigasvvvk
       61 gttngtitgi dgdfslsgvk qgdviqvsfv gyltqeikfk geslkiilqe dsqtlqevvv
      121 vgyggvqkak tmtasaatvk mselaklpva smseglggrv tgvvtqqasg apgenariwi
      181 rggenilyvi ddvvmdsgqg neffnrlrpd diasmsilkd aaatavygpr aangvvviat
      241 krgqegapti tlnqkvsimt payrpkglss yeyalarnea elasfqespt fndtelskyy
      301 mgdlwqkgyg feeirnlvne rynlgyslqd indlfdplkt qgkniqdyys sydpwdmfdh
      361 tqpmyqtnvs lrgggeriky ysslgymkqn gvsdkysyeq vnmilntdam llsdkslkft
      421 fnlngntsnn nkpadgegvf nnamygdwmp krpaawstgl prkgsveaql nngfnntesy
      481 rfqmnaalkw svpwveglsa qaslnfttsy yhqrhfnhdq egvydnpyat avssynpena
      541 nlyekwnkyk lltgifqidy trsfgkhnls amvnyqsqvr ksnwtdakkk gypttlapql
      601 dlggtlvsag gsaeewgsas yigrftydyd nkylfqysan yngslsyspd krwgyfqafs
      661 lgwvmsdevw fknlvnpniv nmiklrggfg lvgnevgspf sfltqyaqss nrilfgenma
      721 snvgwyesdv annlqwsssk qygigldfgf lkdrltgsfd tflylnkgdv mdmtddmirv
      781 dilgmpntpk inapyttsrk ggfevslnwq dkigkvgyrv gvnysywder vtrhsssdsd
      841 wwtptfdnig krpyvtnges itypyglktn glhgswqkmy nsllhannnm tlgtpalvdl
      901 ngdgrvndyy vfnaegstph tqfgvtlgad wngfdlelff qgatgargam psplrsqqsy
      961 mwnygqyafq naytpsnpdv daalptpvpe gngfgysyid iwsfdasylk lknislrydl
     1021 krsvlknlpv iqgldlsfvv tnaftwtkks yplkdlqdpe fittgasiyn nngtlgsypt
     1081 qrsytlgvtv tl
//
LOCUS       WP_118364340             993 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            eggerthii].
ACCESSION   WP_118364340
VERSION     WP_118364340.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides eggerthii
  ORGANISM  Bacteroides eggerthii
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Bacteroides eggerthii"
                     /db_xref="taxon:28111"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111447
     Region          22..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilytvgl aftlslgama qqtlngvvkd asgkpfpgvk iskagefrin sitdesgvfs
       61 leleegdyid lnyadvvlkr vkvtgetmni vldshkdgms dlgfmkrtee nrtqsvstiy
      121 adqlmkgats tnrvnnalfg lipglqlsqn agwrtnagmk irgasgsplv lvdgfqrglt
      181 nmtleeiesv qvlkdgaata lygaraangv llintkrgvy nsfdidvnyr hgfnfpinqp
      241 emadaytyam aqnealhydg lplqytakql enfkqgtnpn fypntdwvke gmrdfsqnnq
      301 fnimvrgggq rvrymalldy knefgllned ythysdryns qirnyeldlr inldvdvtpa
      361 tkvkfslygi iaedkrpntg idaifqnlyk vpsaafpikt angnwgsnsv fkmnpiaaia
      421 dvgyvqenrr llegdmrltq dlsmfvkgln aevavaydns atyqdigskt ylyeifnqta
      481 aglpttkteg snstlqvsss klsdqfiras veaklnydrt fnkhqvaasv vyrqemeepl
      541 gvngayyrqn vmgfagynyd nrymldvvan yygtsvlleg dkfrfypavs agwnianeaf
      601 ledvsqldml klraswgrsa tdgldyglgn yfwisdktsg kyafgeslgt lvnglreqql
      661 pmyrleleta dkynigvdlr mwknftasae vfydrrtnil vdnnrtsgml gvtpaksnig
      721 enetrglels mgwnqqlkdf nyyvnanwgl ndskviengq ayqpydylyt kghkigqlfg
      781 leaigyfnde edianspeqt fsvvrpgdvk ykdqngdkri dsedrvaigk stsipdmvyg
      841 lnlgfeykgf gidmtfngvs gltkqlnvss vhqplrngnt niatwylkdk vrwtestkdi
      901 anvprlstls nennyqtstq wiadgsffkl rnlnvyytlp qawskkmkmd kcqvyakaln
      961 vfsidkidyf ncedialgyp dlfsvyvgln inf
//
LOCUS       WP_118385584            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            AD1].
ACCESSION   WP_118385584
VERSION     WP_118385584.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. AD1
  ORGANISM  Aquimarina sp. AD1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Aquimarina sp. AD1"
                     /db_xref="taxon:1714848"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116411
     Region          25..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myfkkiiavf livlshctll aqdsitlegt vtsredgipi pgvnvlilks ntgtttdfdg
       61 fyqlkvnkgd vvsfsftgkk titvaidnqt tldialeeea seleqvvvig ygvqkksslt
      121 asvsklentn ldelpysdvs nsikgkiagv qirnttgnvg depeiivrgi gsislssapl
      181 vvvdgfpfdd glqfinpsti esievlkdas staiygsrga ngvilittke gkaektsfef
      241 kslsgfkqaa rsidiidaia fsdldrsrdq lvenfnaqqe nrepnfvnyd nvqigkrtia
      301 qniggptnwq dealrnpari dnyqlnvygg gsrtnylisa nyiyneglrk dndlerlnls
      361 arlksklsdn lsfdlkinps ytltrrssin ftdtgryetw ipvrhnqyts dltgqpvgsf
      421 ahalhfrnln fdyvdpvtgl tentgnienl wsssnfnpis rqeasrrnrf eyrllangsv
      481 kwkiargltl rsslggyvry rtgeeyfgsd gdrdgetegi ladqltvkyi nentlnynrd
      541 fnghdiglll gityentter lsnlritnfd detittlngg tiidldntft lkdktvlssy
      601 lgrinyaykd rylvslagra dgfnkfgknn kygffpsvsv gwnvanenfw rnsigntinn
      661 lklrsswgis gsapalfdfl aptivdfgny signtggvtt gqgevdflqg npditwetnt
      721 efnngidlgl fngavnltvd yyyklsekll lrqqisnstg fdeqwnnigk vqnsgwefdl
      781 stnlgrgklk wqgsanisfn enklisfggs eriinngert dqyitrvgep yiqfygyqtd
      841 gifqnaedla nspsgiadav gglkrvdvng dgvineddrt vigdpfpdfi wgftntftyg
      901 nldlnfsfqg sqggevvwge afynevaryg atyaedqwfn enipasrpgi rigvpwletd
      961 yavqdasyis lrevvlgysi pthstkkmgl ekmriyisgq nlwyqaaddy lgnnpegntd
     1021 rnnvlirgyq rgvtpvqrql algldinf
//
LOCUS       WP_118387136            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            AD1].
ACCESSION   WP_118387136
VERSION     WP_118387136.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. AD1
  ORGANISM  Aquimarina sp. AD1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Aquimarina sp. AD1"
                     /db_xref="taxon:1714848"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115758
     Region          25..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfrgilt lllafvvqlt faqektisgn vtdnsglplp gvnivvkgts kgtqsdfdgn
       61 ytiqvnrgav lsfsylgftt kevvvgdgdt vnvqlaedaa tleevvvtaq girkakkalg
      121 yavatiased iasqpqtdvv rsltgkapgv nitqtsglsg tgtniiirgy ssingnnqpl
      181 fvvdgvpfns dtnssegftt ggasassrfl didpnnikei silkglsatt lygqagrngv
      241 vlvttksgaa qggankkfei tfnqsyfsne isdlpdfqds ygngfnqtas aafsnwgadf
      301 nqriagdgva adgtiahpyd rsdlnavfpe fvgarydyrp ydniepffrt gnvvtsslsv
      361 ssgndtssyn isvgrtddeg fvignkyqrl nfsaggstkl snkftisssf nyvltdlitp
      421 ptsagfgsna ndgaaslfan ilytprsidl fnlpfqnpvd gssvyyrtdn siqnprwtqq
      481 narniedtrr ffgnftalye fndwlnlsyr lsldsyvqde dryvnkggtq apggflstfv
      541 tsntvwdhtl slnfdkdlnd swglsgnlgf nprreerkrd ftssteqfvf glinhqnfee
      601 ttgfsdlref nivgaylsat vdyndylfln vagrndwyss lqkenrsify psaslsfvpt
      661 safeglrgsk ainylklrlg ygssagfpdp yatvigldsn antfidpngg aiinslsead
      721 rlgnanlkpe liteleagve aklfdnrvsf dvsvydkrsk dlilnnrfld pstgntvtsd
      781 nvaevsnqgl evgfgltpir gndpddfrwd isgqytinen iveslggese geviagfigf
      841 gnyaipgeay gvifgttyqr ddngnrvvga dgnyianpep tiigdpnadw ratlinnfsy
      901 kgftlgmqwe ythggdiyst tagallargl ttdtdfdrtq tfvldgvqtd gsvntvqina
      961 tdlyfnnigv asagginerg iydattlrlr eatlgynvps kfldktpfgr vsisfiaqnm
     1021 wykafnfpkg infdpevtsl gvgngqgfdy ltgptakryg fnlsltf
//
LOCUS       WP_118386714             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            AD1].
ACCESSION   WP_118386714
VERSION     WP_118386714.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. AD1
  ORGANISM  Aquimarina sp. AD1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Aquimarina sp. AD1"
                     /db_xref="taxon:1714848"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107224
     Region          25..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktftksalf llwlipmsff aqssvsgtvt dagngqpipg vniiikgttn gtssdfdgny
       61 vlngvnngdi iefsyvgfia qeftysgtsr idvalqedaa eleqvvvigy gaarkkdltg
      121 svstvtaddf nkgnivspen llngrvagvn itaggapgsg aairirgggs laasndpliv
      181 idglpvnnnv vggsqsilss inpnniksft vlkdasaaai ygnrasagvi iietikgskg
      241 lqvdynfqsg iytvpetvdv fsagefrdiv reqalinnsi dpsllgnant dwqkeiyrna
      301 vstdnnisir gslfdvlpvr lslghldqeg lrltsefers satlvlnptf lngnlkfnln
      361 anatfekrrf angvegaaia fdptqpvyda nspfggffey dsinpdgsln nilavsnpva
      421 sllqrnnrse vnryfgnfkv dyslwflpev tatvnvgfde qngdgfnels renssgqllt
      481 dgtldgarte ftsyrrntlf dsylnykkef ggfnldvtgg ysyqnfrved fntgelrgdn
      541 dsnqairafd pdlvlvaffg ranfsvndky lltlsyrrdg tsrfsednrw gnfpsaafaw
      601 nisdenfltn sqtlsnlkir lgygvtgqen igagqfnklp ylaqyqlgqn tsqyifgdas
      661 itvanpslrn eelqwevatq ynigldfglf ndringsvdv yrretedlfi sgslpdganf
      721 gnigqqnlge lltegielnl nadiikgknf vwninynaam inqeveklvg gedqlvgpsv
      781 ggtggniqlh regfapfsfl vfkqlydang apiegayadl ngdniinsed kyvyrnrdad
      841 vtmgfqsnmt ykgfdlsfnl raslgnyvfn gvangstyna innngtlanl ntsvldtnfn
      901 vfgdtfqsdi yvenasflkm dnvtlgytft kffgdtssir lwggvqnvft iteysgldpe
      961 ifsgvdqtif prartflmga nvkf
//
LOCUS       WP_118388895            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            AD1].
ACCESSION   WP_118388895
VERSION     WP_118388895.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. AD1
  ORGANISM  Aquimarina sp. AD1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Aquimarina sp. AD1"
                     /db_xref="taxon:1714848"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108086
     Region          27..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqtqtskg lllflfffpv mlfaqetitg kvviestgeg apfvniveng tnngtasdid
       61 gnfsitvgsl parlrvfalg fstkmvdvsq agnitiqise stesleevvv tglgssikra
      121 nlanavstvs seelvgntgq ttvdgalygk vtgvnitass gapgggtalr lrgissingn
      181 nqplfivdgv yinnveipsg lrfasganrg neenagnrla didpndieni eilkgasaaa
      241 iygtranagv viittkkgkg gktkirfsqd tgvnviqnrl glrpwtatsv fdafftpnpd
      301 dpeaearsra aaeaevaafn naiqngglid yedeiygnvg fisetklsas ggndktrfyi
      361 ggsyrdeegi iqktgfdrfs irsnidhkis difdvslssn yvrsnssrsf tgneneggls
      421 fgytlaftrp wnnlfpdadg nypnnpnypg npifvrdqak nedsnnrfiq gvkfttklln
      481 kekdkvrfvv nggidylane tyvyvpethq aqvgnqegfv aegrnnftqf nlltfavwdh
      541 talngdlglt tqggvsyleq qanlvnsrgs nlfggqtsvd qsvnqvidqt rsnqkdfgyf
      601 aqiegnykdq iiatlgyrld kstlngdqnk lygfpkasla inianfefwn veginqlkvr
      661 saygetgssa afgsiytrln psniggnggl svgtrgdtdi epetsaefev gmdlgildsr
      721 vsleasyynr kvsdlilsrn vpassgftte ttnladlvnq glelavrgdv wrgdnfywnt
      781 giqfyfnrse vtrldvpafa qpgagfgtgl gtffieegqp vtqivgnidp dgdgpiegsl
      841 qqvgnvepdf qmafnnqftl fkqldisfll qwkqggenln lsrfltdlgq tspdletpeg
      901 qarlgtaana erfiedagyv rlreaaiyyr fptniveglf gevvegvklg vsgrniftit
      961 dyssydpevs vnggaglssg ievtpfpssq qfyfhlnvnf
//
LOCUS       WP_118389012            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            AD1].
ACCESSION   WP_118389012
VERSION     WP_118389012.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. AD1
  ORGANISM  Aquimarina sp. AD1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Aquimarina sp. AD1"
                     /db_xref="taxon:1714848"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112922
     Region          23..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqkkltlis flflvigvla qekkisgiit davnntplpg vnvivkgtst geqtdfdgay
       61 tinastgdil vfsyigfktv eksigssnti nigleedaeq ledvvitafg irqeskklgy
      121 svqqlkseti tqtadpnigs airgklagvn insnsggigs svsinirgis slgannqpli
      181 vldgviiddn qggqgdfasg ldygntlsnl npndienisl lkggnataly gfrgingvlv
      241 ittkkgrsdk ptveinssit assilvspkf qneygqglfd tstnqlvydi tngssfgprl
      301 dgtqrerfdg vgtasysand ndfkdffrsg fsflnsvavs qgtekfdyrf sysrlddesi
      361 vpgsnlkrqn fsikagasit swlkilgkvd yihqdarnrp eltggqtnit ralslrprni
      421 sntllrdnfl esdgtpnnwa gafitnpyyt sntllnedev dryislleln idiapglkgl
      481 mrlsqdhits sqqifnpfga fdiagngrfs dtnstartnn ydliftyntd ignnfnlgat
      541 lgfshsdvsf kslqaigetf llpnffslnn fesisvvpgn aknssnsifg smtigfnnyl
      601 faeftarndw sstlpindas ffypsvglsf vatdafpslq dneilsnlkl rgsfaqtgna
      661 tgafslvnty nvssnlfngq rffffgnaee gagtgpelnn pdlvpeisna lefgldarfi
      721 nnriglsaty ytirtedqil rltlppssga anqiinaglv tnkglelsld adiiktdnfk
      781 wsttvnfttn enkveelaqg vdrnilirqf ndvvqvaaev gssaqglfgt tfskddsgnv
      841 iydtnglpvi nteisqigdv apdaflnwgn sfsykqfsls flfdarfggd vfslseiqrh
      901 tqgtaietle greffsggqg islpqnavid gtldpnvqqr gvnpqtywgr vgqisenwvy
      961 dgsfikfrel tfgytfpert ikglhlsnls isyvgrnlai lhsntdnfdp etgfntsfgg
     1021 veffgipsas shglrvnltf
//
LOCUS       WP_118391357            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118391357
VERSION     WP_118391357.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117074
     Region          43..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmekckyll fcgtlalwma gsfqqvyaat epssqaiqqq snkvtgkvsd atgpiigasv
       61 vekgtangti tdldgnfnln vkagatlvvs yvgykseeik agrgplnitl kedakaldev
      121 vvtalgikre rkalgygide vkgealtkak etnlinsmag rvpglvvsqt aggpsgstrv
      181 ilrgstemtg nnqplyvvdg vpldntnfgs agtnggfdlg dgissinadd venmsvlkgp
      241 aasalygsra shgvilittk rankdkisve yngtltfdtq lakwdevqqi ygmgsngtys
      301 ydaisntnks wgpkadgsnm lkyfdgverp flivpdntsn ffrtgitatn saiigvnsgk
      361 tgirftytdm rnkdivpqth msrdifnlra ntsagkvdld fsvnytredv knrpalgdsk
      421 snigknlmtl attydqewlq tyqtadgeys nwngmdpynv npywdiyknf nkskkdlfrm
      481 ngkavwnidp hlklqatlga elnwftfddy kapttpgfea grlqnsafrn rmynfevlal
      541 ynnhwgdfdf natlggnvyk vnnqttvtta qdmkirdvps ltsfneisvv pgsyrkqins
      601 vygavnvgwk hmlyldatlr gdqsstlptg nnmyvypsfs gsfvfseltk lgdllpygkv
      661 rmswaqvgsd tdpyqlglvy tkskyaypgy tigyidngti pnkdlkptkt nsvemglelk
      721 flknrigldf tyysqisknq imgmasswtt gynyrlinag kienkgieia lstrpiqtrd
      781 fswdinlnfs knsnkvkeld gesdmfelek aswldvqvaa kvgenfgsiv gpdfqrnekg
      841 dilidpqtgl pqydksnhvl gnaswdwtgg lltnftyknl slvavfdvkv gadlysmsar
      901 aayesgkspe tlagrdawyr seeerlaagi akgadnwkpt ggfvapgvid ngdgtyrpnd
      961 iyinpedywm svcrnapsmf iydnsyvkcr eltlsynvpk swlknvvsgl tvsfvarnpf
     1021 ivwknipnid pdsnynnttg mgleygslps rrsygfnvnv kf
//
LOCUS       WP_118391584             942 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118391584
VERSION     WP_118391584.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104572
     Region          2..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklifsqait ltsaqplkvt lgedtqvlde vvvtalgikr atkalsynvq evkgdelttv
       61 ksanfmnsla gkvagvnina sssgvggatr vvmrgtksis sdnnalyvid gvpifntnkg
      121 dtngqysaqp rgegisdinp ediesmsvls gpaaaalygs naasgvilit tkkgkegkar
      181 iiisnnstfs npfimpefqn syinragsfa swgdkasslf gtyepkdffn tgtniqnnvs
      241 lsvgneknqt ylsvgttnat giiqnskydr ynftfrnttk flkdkmtldv gfsyiiqedl
      301 nlmaqgeyfn plpavylfpr genfeavrmy ktydttrkid vqnwgwgdpg ysmknnpywv
      361 anemnhgmkk qrymanaslk yeildwldvt grvridnatn dysdkrnast dlyftnssiy
      421 gfykyykadd rqayadvman inkrfgdlsl saniggsftq tyydergfqg glkdmsnvfs
      481 lynmtttldk dtypiesgyk qrtnsifasa eigwksmlym tltgrndwds alinteqssf
      541 fypsiglsgv isemvklpka itylkvrgsf asvgapipkn lssnktyewd patsqwklqt
      601 yrplpklype rtnsweagln akffnnslsl evtwykantr kqtfqvplsg tavyatmyaq
      661 sgnienkgme fslgynkswg dfswnsnltf sfnknkivel lddavddegn hyslseidkg
      721 gigsakvilr kggsmgdmyv tnrlkrdneg nvfidkasqn vkkediknsd efihigsvlp
      781 ksnlgfrndf sykgislgfm laarfggivi sptqavmdqf gvskvtalar dnegvpvnng
      841 kvdpqtyyte vggisglmsn yvysatnvrl qelsvgyslp akwfnnkcnl slsitghnlw
      901 miynkapfdp eatastgtyy qgvdyfmqps lrswgfnvki qf
//
LOCUS       WP_118397330             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aeromicrobium sp. A1-2].
ACCESSION   WP_118397330
VERSION     WP_118397330.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium sp. A1-2
  ORGANISM  Aeromicrobium sp. A1-2
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Aeromicrobium sp. A1-2"
                     /db_xref="taxon:2107713"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53357
     Region          14..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mspaeqetpq asvvgvvaes qrgetrvaat petvgkligl gyavavesga geaasftdea
       61 yaeagatigs tpdvwrsdiv fkvnaptiae igqladgatl vsliapglnp elvealsqrp
      121 itvlamdavp risraqsldv lssmaniagy ravveaahvf grfftgqita agkvppakvl
      181 vagvgvagla aigtasslga vvratdprae vadqvssvgg eylpvdvete qstdgyakat
      241 seaydaraae iyseqaadvd iiittalipg raaprlitea dvasmrsgsv ivdmaagngg
      301 nvagsvagea ivtangvtii gytdlagrlp tqasqlygtn lvnlmklltp ekdgrivldf
      361 ddvvqrtitv vhngetlwpp ppvqvsaapv aapvaavepk pakvpmsaar klsligigvl
      421 alflvnayap eplpehftvl vlaivigyyv igkvhhalht plmsvtnais giivvgamlq
      481 iaqddttirv lsfiaillas invfggfavt rrmlsmfskg
//
LOCUS       WP_118400302            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            coprophilus].
ACCESSION   WP_118400302
VERSION     WP_118400302.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprophilus
  ORGANISM  Phocaeicola coprophilus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Phocaeicola coprophilus"
                     /db_xref="taxon:387090"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115760
     Region          23..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkatlgivfl cllsslnawa qnikvtgvvt dkegtligat vtvkgnsgtg tvtdldgrye
       61 invpadgtlv ysyigyntve kpvkgqkvin vqmtdeiqai devvvtaigi kqqkkkigyt
      121 tqqvnteald qpgtvnvgna lsgqvagltv nnptgifqap tftlrgktpl mvidgvpves
      181 dlfdvspeni qsinvlkgta aaalygsrgk dgailittkl adkegltvka glssmvtagf
      241 tvfpetqtef gsgsngqyaf wdgadggisd gdmtwgprfe gqkiaqwnsp irnketgevi
      301 pwwgdvsgti yddqskyerv pitweahdnl kdflqtgiit katfsvasks kkanynfngd
      361 fshqkgqvpn tavytgglnf nsmynlsdav tlsanlsynk vyspnypryg ygpknhmyti
      421 llwmgndvng kelaahhwrp daegerqany nyawynnpyf atyeltqvhd rnvtngqvkl
      481 nwdimpglsi qgraagrled tfedmkspks ymnygdsrng dyktwntdql dintdvlvty
      541 trafnknfal tvnagsslyy rqirseyqat dglivpgvyn mgnslnpvsa tnsmnekaie
      601 svygsvnldl fdgvyltltg rndwsstiik gnnsyfypsv slsamldqyi slpswmdylk
      661 ingawaqvss dldpyslyat yskgilygst psvtyqsdll nanilpqktt syeiglstsf
      721 lrnrlgldvt yyhmidknsi iqlpisvasg fnnryvngnt yttngaelii tatpiqskkf
      781 twnlstnwst nirklteiyg gqekygdlkl gdradamyat ewektpdgql ildsngmptq
      841 safksyignq dpdvrfglqn tfkfdhftvn vdmdgaiggt listttqkmw wggkhpkstm
      901 yrqeeyengg kpiyvpegvn ivsgevtydv ngniisdtrv ykknetavni qtwaqnypyr
      961 avvrtsesel fantfsrsfl klrrvavsyd fshlihsnsi kglevtlygn nlavlkktpy
     1021 ldpdfgasds dlqdpsaryi gvsanitf
//
LOCUS       WP_118401478            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118401478
VERSION     WP_118401478.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114869
     Region          30..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtktvslfri ffvalmmcat tllgqsvnei tvtgkviddk getvigasil vkgtgtgvit
       61 didgnysikv pgsqsvlifs yvgltpvsev vgdrsvinvt mastsevlee ivvtalgikk
      121 ekkklgyavq dliapgltkv paantasnlt gkiaglkvsn spnlfdtpal llrgvapvvv
      181 idgvpvesat fwevapedie smsvlkgpaa avlygqmgqn gviqittkka kegvrisvns
      241 stgfdtgmia npsyqkkygt gyqgqyrvgn stdefwgawg peldgrllaq wnspydengn
      301 riaipwiprg kdnldnmlrt givtnnnvsv etkwekgdfr islsqmhqkg vfentslnsy
      361 tvnmsggiql seklrfdani nynkmdspnf psvgygrnsp iysmilwaga nvdvrdlrdy
      421 wapgleglqq rnfdvadgye ngsydynnpy filyenlhgy hknttygsas lkydatkdln
      481 itlrtgvnmn ermedyrtaq stvysrngny sqtyytdfqv ltdlmakydk rigafdigam
      541 lgfnarqynd rghsastdgl avpgiytlen tlkptkptsy krelaeyavy gyldlgwkny
      601 illnltarnq wsstiptfgk nsylypsaql ativseyvkl pefisylklr gsfarvgsaf
      661 spyyfasvyt qtqswnnnig ltspssiysk dikpsystgy evggelrlfk nrlafdatyf
      721 yfidgpqtys qpiseasgwt syvlnglktl rkgwelaitg spfknpkgfs weavlnlssy
      781 rkylkelpeg qtkygelkvg drmdaiygta mmcapegsgy egqviigang qiqkddikqk
      841 lgyanndlmv gftntmsygk ltlnfsfdac iggkmlsqyn rymwaggrsl diddqarkdw
      901 yagkdylaqg vnvisgtler dgdgnvisdt rqfapntktt nyfdyiqnsk gyygidecvl
      961 vdrsflkfre islsydlsal lkntfikgan vslvaknlfl itksglvdpd qynedttwdn
     1021 lqtpsfrnvg fnvnltf
//
LOCUS       WP_118401602             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118401602
VERSION     WP_118401602.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111392
     Region          1..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlssaktlqi syigmqtqev aikstvkvfm ksdsemldev mvvaygtakk saftgsasvi
       61 ksetlekrqv snisnalsgt vsgvqtqstn gqpgekatvr irgigsmyas nnplyvvdgi
      121 pyegdisavn sqdiesmtvl kdaaaaalyg argangvilv ttkkgktget lvsldarwga
      181 nsrlvknydv lqnaatymet aysaiyngyv ynskytaera yqqanadlip glgyqiynvp
      241 ngqnligrdg klnpyatlgy sdgdyyytpd nwsdemfesn mrqeynlsvs ggtdklsyyf
      301 saayladdgi iensgferis srinvdyqak kwlkfgvnls yanvksrypg dqdtdaatss
      361 gnaffvgnfi apiypmyvrn aegqimhdan tgyriydygd gestnftrnf msmsnpmssf
      421 lydteeylmd ilngkwyakv dildglslta slglhvdntr lhivgnkyyg qsasqngsvq
      481 qyssrtysld qqylltykka fdvhhidila gyesmdynte shyilgynmy sdknwtasnv
      541 idrkngsgsy deyatigiit rasydfdeky yasasyrrda ssrfhpdnrw gnfwsvsaaw
      601 dmakenfish idwinmlklk asfgqqgndn llykeypnyy pyqdqftvsg segvfsdgvl
      661 fykgnkditw etsnsfnvgv dfallkgrvd gsieyfnrqt kdmlyykpva msngytqfpm
      721 nigsvrnsgv eielnytpiq tnnfkwvinw ngtmmknkil elhpdlkgem ingsyiyreg
      781 eslyqfyltk yagvdhesge aqywakdtdg aeyktsdwsa ayntnrqasg dllptiyggi
      841 gttldfygfd fsiqcayqlg gkiydsgyqa lmhgggshdl gynwhkdiln awtpenansd
      901 ipridaidky tnsssdrwlt ssdyfainni tlgytlpqrw lrnlgigslr vygaadnval
      961 fsarrgldpr msyttastdr ytpirtisgg lkvtf
//
LOCUS       WP_118401894            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118401894
VERSION     WP_118401894.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112128
     Region          27..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkykiivla mlacvslksw aqeegniagk vvdklgnpie gvlisvennp lvqattdrng
       61 kfeiiadhtk rlqvrtgrdd tkivpvadgk dltivmdfss ekvnygfgln qtnaestgav
      121 stvyadqidn rstfnvgnal ygnvtglytm qktgnvwdqi ssmairgqkt lndkngilll
      181 vdglerdngy qalnyispee vesvsilrda aavalygfrg vngvvnivtk rgkyksrein
      241 fsydhgfnsq tripkmadas tyanaineal andgksarys qnelnafksg kypylypnvn
      301 wmdevfrdqg ttdiatltfr ggstkmryft mlnlqnnrgf iknansndgy stqdkysran
      361 frsnldidlt sktrlqanis gvlnefsrps ssgdnligkl ytvpsaafpi ktekglwggn
      421 stwngdynpv ylaqghgytk ghtralyadm llrqdlssit kglggsvrig ydnlasywed
      481 hrrsekygmq svtqwtngep saftdfeggs vgtsesskld wqyrslnfqa nvdwnrnfgk
      541 hdlysmllyt ykyddrngvn vtlftqnagw ythygydnry fadftlmfsa snkldpnsrw
      601 lpaptvglsw visneafmkn qnvidfmklr asfgiintdn tpadgywlnk mggggsypvi
      661 ggsnfgdgdg gwsegrlpsl ngvlekayky nvgldmsllk gltftidgfy errsdiwvsa
      721 sgqnsavlgv dgayknagiv dswgtemgld ynkrigdfql rlggtfsfnr seiienleep
      781 kayeylsakg ksvgqiwglq aighfvdqad idnstpqqfg pvkpgdikyk dvnndgvins
      841 ndmipmgyns vwpeiyygfn vglewkglgf nayfqgvgny tawltssvyr plinntsisq
      901 yayenrwtpe npnarfprlt tenvenntqs ssvwlqdrsf lklrncevyy kipsawlnki
      961 kmktakvyvr gtdlfsidki dltdpeaigd vypatrsihi glslgl
//
LOCUS       WP_118401884            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118401884
VERSION     WP_118401884.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123833
     Region          25..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkivlsla clligiglai aqtpktvtgl vifeednqpi vgasvlikgt nqgavtdldg
       61 kftltnvpgt akilrityvg mqtievniks gtmkivmkpd aevleevvvt gmtkmdkrlf
      121 tgaatklsse dvkldgladi srslegraag vsvqnvsgtf gtapkirvrg atsiygsskp
      181 lwvvdgiime dvtevsadel ssgdavtlis saiaglnand iesfqilkdg satsiygara
      241 magvivvttk kgqagkshis ytgeftmrmt pryadfnimn sqeqmgvyke mkekgwlnfs
      301 dtyraaqsgv ygkmyqlmnt ynpvtgtfal ehtdtamndy lqeaeyrntd wfdalfsnsv
      361 mhnhsvslss gtekasfyas lsamadpgwy kdsevnryta nlnatynisk qlsinlissa
      421 ayrkqkapgt lsqsvdpvyg evkrdfdinp ysyalntsra ldsktmytrn yadfnilhel
      481 dnnymnldva dlkfqgelkw kpitglefsa lgavkysats qehlitddsn qamayrampd
      541 atvrdrnpfl ytdpdnpyal pisvlpqggi yqrtnykmlg ydfratgswn hvfvekhivn
      601 lfagmetnss drnktyfngw gmqytqgeip fytyqffkks ieegtdyysl tntrsrsaaf
      661 fanatysyqg kytvngtyry egtnrlgksr sarwlptwni saawnmheee ffeslkpala
      721 hfalkasysl tgdpgpntvt nstmvlksyk pyrpfaniqe sglkiidlan ddltyekkhe
      781 lnigadmgfl dnrinfaidw ykrdnydlig viqtpgvggq irklanvatm kshgveftls
      841 trniqtkdfg wttdfifsqa knevtdlesd aevidvvsgt gfalkgypvr glfsyqfkgl
      901 nedglptfid qdgnltsdgn didfqsqkld ylkyegptdp titgsfgnif rykgfklnvf
      961 itysfgnvir ldpvfsneyt dltsmpkefk nrwvlagees ittiptivtk rqsdtdnhlk
     1021 tlynaynyst eriakgdfir mkeisvsydf pkkwlekifi ndlslklqat nlfliysddk
     1081 lngqdpeffr sggvaapvpk qftltlrlgi
//
LOCUS       WP_118402283             910 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118402283
VERSION     WP_118402283.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..910
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100698
     Region          38..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrirnlfyl slfltvpglq avaqeklhvs lpdsittvgy atglrknlsg lveritenqm
       61 nkdqitnpld airgrvpglt ilkgsngpaa ldavrlrgtt slttgndpli ivdgvfgdls
      121 mlmsiypadi esfvilkdas etaqygsrga sgvieittkk gvsgrtsvny ngsfgiassy
      181 ktvrmlngde fravakergv sildlgnntd fqkeieqtgl qhnhhiafsg gtntsnyrvs
      241 lalmnregvi vneklqnfts nmnmtqyvfd nflkcdlgmf gsiqkernlv nlhkvfysaa
      301 afnptfpnhk npetgswdgs vlasqlshpl awmdvndkda tshistharl tfnlseawkl
      361 alfgsytynv iensqylpva vwaqgqaykg tkkmesllgn lmlsykkewr khffdvlgla
      421 evqkdqysgf yttvtnfsid glgynnlqgg alrpwegtns yyedprlasf mgrvnytydd
      481 ryiltvnarg dasskfgsnh kwgffpavsv awvvskekfm eklpfidnlk vragyglagn
      541 qngidsytsl nlirpngvap vgsspvvtmd qlknmnpdlk wevkqtfnag iemallgnrl
      601 lltanyynsk tkdmlylynv svppftyntl lanigsmrny gtelsigitp lktkdmelni
      661 nanltfqqnk llsldgnyqg ehisateyks lagldgagfh ggynhivyqi vgqplgvfyl
      721 phctglvsdg nggytyqiad lngggvsled gedryiagqa vpktilgsni sfrykdfdvs
      781 lqingafghk vyngtsltym nmnsfpdynv mkkaptrnik dqtatdywle dgdyvnfdyi
      841 tvgwnvplkn trylqslrls ltvnnlatis gysgltpmin sssvnstlgi ddkrnyplyr
      901 tytiglsvnf
//
LOCUS       WP_118402635             942 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118402635
VERSION     WP_118402635.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106102
     Region          42..939
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiykglaf caalafahth iaaqetladl veaaqadtlq kvqvafrsid rndllggvsv
       61 idmkemsekv yttyslslvd nvvggfngni wgnneylviv dgmvrdannv lpheidqitl
      121 lkgasavvly gpraakgvis ittkrgevgd lrinihansg fytpksypky lgsaeymtly
      181 nearlndglt anysqediyn hasglnpyry pdfdmyssdy lrkaynrsea iaeisggsek
      241 vkyytstgyy ressllkvgn tednyisrff vrgnvdmklh klitaqadan vtfydsysan
      301 vdwwgqaatl rphlvspfip lsyiedadkn slntvlnsny iqdgkyffgg tqqnptnpva
      361 dayaagdnkf vsrqfqfntr fdvnlspllk glyfrakygi dyastydqgy ssayatfspv
      421 wstynghdvi ssitqygkde ksaveninns ayrytynvsg qfdyqntfne dhnvfamvla
      481 nawqtqrsgh yhrttnanlg fqasynyqhk yyadfsaamp ystklpegnr tafsptvtlg
      541 wnlakedfmg nsifdnlmlt asvgiinqdl dittsdnedg yflyqpvvqp ggwyswgdng
      601 glsatefqrg dgsamtfvkr keftaglrgs mwnrlltfdf nfftskmegg lartsslypi
      661 yftqvgypss siipyvnfne dkrtgfdfsv yankkvgevd ltlgvsgmwy kstaekrden
      721 vefdylsvvg ralnghwglq segffndqae idaapkqtfg dvkpgdiryk dqnndgkidd
      781 ndrvflgrwd spfmsginlt akwrdftlyv mgnlyiggyg mkdnsyywvk gdgkysevvr
      841 nrwtpetaat atyprlttts gdnnfrtsdf wmykndrfnl tqvqltynmp kevlrgsfvk
      901 glsffvnann lltiakerka lelnvgstpq trfyqlglkg tf
//
LOCUS       WP_118403442            1166 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118403442
VERSION     WP_118403442.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1166)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1166)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1166)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1166
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1166
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128462
     Region          54..1165
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkeeifsgk tqgkylsaak iicfsflfsi pvaafaesvv evpavsvvqq qgivkgtvvd
       61 eqgetvigan ikvvgttvga itdlngmfsv napvgaklei sfigyvtqvv tvpvsrslkv
      121 ilkedselld evvivgygtq rvkdltgaas nvkmedipdi pgtsiidala gqviglsvtq
      181 sdgrpgstgs fkvrqpmsfd adgnsgsfnq plividdvvq vdengdpsmt afnmlnqsei
      241 esmtvlkdas aavygsrasa gvilvktkrg nvgapkisys gkldfadavs haktmnayel
      301 gvftnrlynq admvngngnn syfkyslael eamknlnynw ldeawhssvs hrhsltvngg
      361 sekvtffagi nyqkqetnlg nvqdydkwtf raggevkvas glklsatlsg ynsnkvgnna
      421 qvnvgagpwg nqtasrdyam lshmpkyipw etsiydevsg etktyfvspw ggpqlldnst
      481 dskvsgapvw nyfaeeaska rsynktngys anfsltydvp fikglnlkgt yaisynnsts
      541 eqvgdyykla ragntnkpdm hllgdytewn finygdpnge nidkkprvky akngskseqy
      601 sfaisynrtf gqhdvsatgv veraesegdd lsqlyqglgm syggtsatag tlssddtgty
      661 yrkyesgsls yigrasykya nrylaqfvfr sdastkfape nywgffptgs lgwvaseekf
      721 fnnstlgkif dflkvryslg ktgkdnveaw rwlqiynikp tggmgfgslg gqytsgasin
      781 gtanrnikwd ttikqnigld mnmlnnrlsv tadfyydktk dlimtisdpe epiyvgaklp
      841 sinygkkdaw gfelsvrwsd dikqsllpsw gpikysigld ygiswnktvl gveptfdypa
      901 eavnrtdytg yrgmgaeygf ktwkhtssgd gilrnqtdid nywdyltkla eaagvspnfl
      961 gitskekmyp gmlvyediag didtenktia gpngviskeh gedyakladn rrhgintklr
     1021 lqwgnfswsa qisttwggfl dfrgsqtkts sfmwsqfsyi ndmfdmddnp ngryptmaag
     1081 naygetsdfw qvsafrmyvr nmtfaysfpk silkkvnvda lsinltgnnl wdfhnpypdh
     1141 fvnvydgikt gyptlrtwsl glnltf
//
LOCUS       WP_118403493            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118403493
VERSION     WP_118403493.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121442
     Region          24..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrlsvafl lligtftyal aanrqvegvv issednlpli gasvyvtadd lkkvgnnqst
       61 igvitnidgq fsisipegva rfycsyvgyd vlevklipgk nkyditlqps ahmldavvvt
      121 gyqtverrkl taavskidis dqmmgatksi dqalagqiag lsvsnisgtp gapakirirg
      181 tsslngtqdp lwvldgiple gtnipnmevl kdidnigqta iaglnpadid nitvlkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs tkltyspkln idrlnllnse ekvgleldll
      301 asgypyretk gevyriisgl gelnnfkdgg wnalsssaqs ainklkatnt dwsdilfrda
      361 ftqeynlsls ggsekatyyt sfgymkengn vpnvsaerln lvmktsykvn silkvgasmf
      421 anrrknssyl pdsdgltnpi fysrlanpyf tpynehgnyn ydidvendvd mdfgfnpfee
      481 lknttnetti nglssifdae lrfddrfkft tqlglqldkt siekiadees famrkekknh
      541 rsngvtylpa ggfhkanens lsqltwkamg eyrdtyndih efeamvgtei rktweeklys
      601 agygfdrktl ttkpiifpee sqafklheka hvenayvsaf stlsysllnr ytlggsirfd
      661 gsdlfgvdkk yrylplysvs glwrisqepf masakwidnl vvrasyglqg nidkntspfl
      721 lgnyrienil pggsedmidv sgapnkklrw ekthsvnagf dfavlnqain lsvdyyyrkg
      781 vdligtqmlp letgfemltv nwasmrnqgv evalstrnvh tknfmwttnf nfaynnnkvl
      841 kealredale pgregypaga lfalktagld eegypmfqdk dgkavsamef fklqewgfga
      901 tdltarerre lytyvgtadc pytggfnntf tykafelgvn fsfdfggkvr sqptysivdf
      961 dkgrntnrdi lnrwtpente tifpvllsqn erldeymwys nqneiyrnld iwirdlnyvr
     1021 lqnirlgytl ptnfsrtlgm tsatvaiegr nllvfgssyk nyldpetmsn ayatpapksv
     1081 tlslnlif
//
LOCUS       WP_118403520            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118403520
VERSION     WP_118403520.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112182
     Region          36..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkktkiypw kmyfhvllgm ffllptllna qnatvkvsgi vtdtnnepli gvsvaekgtt
       61 ngaitdvdgk ysltvrptst lrfsfisykt qevkvdgrkt inirmeddvq alnevvvigy
      121 gtldkkelts avshisskdf lhissldpsm miqgkvagvs vtntaaadpn nqasiqirgi
      181 ssraaglgpl ividgipggn ltninpndia smdilkdgaa saiygtrgsn gvivittkkg
      241 srdgkfhaty ngmltasipl heldqltaee freyrvpnnp tsdlggatnw ideitrtgft
      301 hqhtvtlsgg tsqsnyrvsv dyrnatgidi rssreeygar asinhttkng lldfsvniap
      361 riayrenssw dafkiamdan pttplfdpen pnlysdftgq ealwnpveel kleqnggetk
      421 lldwdatvkl nllpllakdg hsihslstql tfadqqsdnf dywfrpstsr lamkndykge
      481 asrtyskyrq hslewlgnya melkghrara mvgysyqyfq nsglnaankd fssdgllynn
      541 lgsgewakee grnemgtnks dskliaffsr lsydyknryl mtaslryegs srfgddnkwg
      601 yfpavsagwr iseeafmkdi twiddlkirg dygvtgnqdf gnylslstms sfgsyyyngq
      661 yftvwgagkn pnpglkwekg knwnigvdfs mfkgilsgsv nyynrkqqdl lgdynvpvpp
      721 ylfsttfvnv gtmrntgiev dlniqavkmk dfsytvnlvg atnenkflkf snneftgqny
      781 ydlanmespn qpgklqriee gqrlgnyytw kyagidadgd wvvwnkdnte mikisdakee
      841 dkrvtgnglp kftasmtntl tyknwgltif lrgafgfdlf nvhdfywgip smqsnvlkka
      901 ytknaaikqg knvltdyfie rgdyvkldmv tlsytfqinn kwldsarlyv tgknlatitg
      961 fngvdpstyq tngltpgvnl ngtegtrryy psttqvmfgv qldf
//
LOCUS       WP_118404378            1178 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            splanchnicus].
ACCESSION   WP_118404378
VERSION     WP_118404378.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter splanchnicus
  ORGANISM  Odoribacter splanchnicus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1178)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1178)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1178)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1178
                     /organism="Odoribacter splanchnicus"
                     /db_xref="taxon:28118"
     Protein         1..1178
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132630
     Region          133..1177
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkksnqtra ggrilvpkwm mkmkvvfill vcslvqvqaa vsarqskvsv elknvtlekv
       61 fqelerqtgy sflynhrevv twknvsisae nqgleavlkd llprlgmsfs fddnlviika
      121 tsyqepekkf vrvrgfvyda akqplpgvtv rvvgttigta tnekgwfawd lpllkgtlef
      181 ssvgfkkrrv efsektardt lhitltedvs dldevvvray gtqnkremvs aistvtaeem
      241 kelpaasiad mlqgrlagvn ivqqsgapgs aaviavrgfn sllvdgasdg qplwvvdgvp
      301 mysfvspvtg tntladldps miesvqvlkd aaaasiygsr agngvilvtt kkgkvgeakf
      361 sanasysisq lmeypeqtgg rmerwlelkf rrniknnyyd watgkyhvpt syedvyrngn
      421 giydqfwgng ywgspslihs lqdsldpyyn nstnwwkyaf rrskvvnanv qavggterfr
      481 ymvglgyyde qgiminsgyk ranlisnlta qftpklrmdt rvylsyvdrt mnrssssgss
      541 khtryeglsv npsqqltvlp atkeleaewk ksvlgikdrt ddyramvtaf leyellkglt
      601 fsasgnidys qsnlnkytpg vfdeyhhesk segnigrqvm lsseellhyn tsvndvhnid
      661 vllgvntnke qafsmygygl rgvsddvyyy npqkvppvvn hgtpefpeya atryyssdft
      721 ekrmvsyfgr lgynykqryl leftfrrdgs stfgegnrwa nfpsvavgws fseepfikrl
      781 tgswlnwgki rgsygksgqt ftsaylahgl mnimdrnffg ktgvttdkpv spyltwektn
      841 qydlgldmdm fnyrlnmkld yyykytssli ydipipgsly tfgaqvenam eisneglele
      901 lqadilresa vswrmkfnma rnwnrfeksy sgkdvvdgdg tllvagrpln glyvwahrgy
      961 ynsdaevprl ykidgqeiyf ngvatdgisg avgnyrlldl dgdgnpdsyy agsplplahg
     1021 gwvnelmwkn fdlnvlvnft igrkminnrm glgfstqsen ghltklfdyr klrpwdgvnk
     1081 npnapawgns lsmntdsaie kvhhlalkqi tlgynlpdri skkagfsgvr ffltaenlfy
     1141 lsnysggnpe vvniytgrdn gdtyplprky tlgltlnf
//
LOCUS       WP_118404623            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            splanchnicus].
ACCESSION   WP_118404623
VERSION     WP_118404623.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter splanchnicus
  ORGANISM  Odoribacter splanchnicus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Odoribacter splanchnicus"
                     /db_xref="taxon:28118"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120442
     Region          50..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkqlygrg vpmlciacql tvaplffssh vqavpvaptf lttaqtqemr tikgivrdvn
       61 nqplpgatir ikgtstgvvs dvdgnytiav pddpnttllv sfvgmktqeq kigkstalnf
      121 ileedatvld qvvvngvfer kantftgsvr tigkddlkrv gnsnvlqslk nldpsimffd
      181 nmslgsdpna mpemvlrgks sinmedvdlk atyqndpnap lfvldgfets lqkimdldmd
      241 rvesltilkd asakaiygsk aangviviel kknpsgdlrv tyngsmeiea pdlssydlcn
      301 aaekleveqa fgmfndpgad fesqrmmikm ynqrqsavks gintdwiskp lrlgvgnkhs
      361 lsvelgdkal qaivdlsyqn ikgvmkgsdr tnisgaisll yrhqnflfrn qltitsneah
      421 dskygtfdey tklnpyytpy dqyghltdni vpsldpgnsv tvnawyedie feanplynaq
      481 lntllqdkyv ditnnfelqw fvmtglkata rfglteqrsr sdefypsdhl kfasystdrl
      541 tekgsydlen geqhslsgkf dvqynknfls vhdifvnagf dlsrkqsstn lqqaegfpsd
      601 kmtdiifarq ylkdakpkgt eetvkdfgyy lsanysydnr lnfdatfrqs assmygansr
      661 wgkfwsvggs wnihneswme gsnitqlrlr attgstgsqs saaynalasy eyfldktygg
      721 qlgaqllnmr nedlkwqekv eqnygfdfny knrysftfey yhsitnnavn plslapstgf
      781 ttvqenvgkv lnrgfdlrag atvwqqpadr sylsfslmis rnknilkeis eamrsyneqq
      841 eklategnvp vqkyydgvsm daiwampslg idpangreiy iakdengnpy rtytydaaqq
      901 vicgdelpkf qgnagvnfey kgfginavlt yqygakmynq tlvdkvenad mkynvdrriy
      961 tdrwrkpgdi alykaiseev yvsekqqfas ektyptsrfv qkrnelkiss lqlsydffrh
     1021 dfvkkigler illrfnandl ftfssidier gtsypfartf nfslnvtl
//
LOCUS       WP_118406677            1139 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Alistipes].
ACCESSION   WP_118406677
VERSION     WP_118406677.1
KEYWORDS    RefSeq.
SOURCE      Alistipes
  ORGANISM  Alistipes
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1139)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1139)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Alistipes"
                     /db_xref="taxon:239759"
     Protein         1..1139
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128508
     Region          65..112
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          133..1138
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpnftnaff qktrclrtvl rravvcmlll gttvvhaqer kitvdtrqev tlvqlfrqve
       61 assdylfnyk dqdvadirvs vkvadasiqe vmdlalarts ltytvkgrhv iigqsaarsa
      121 gtpprtdsrp valtgrvtde kgmpfvgvti iqegttngcv tdadgnyris vpvgasvsfs
      181 yigyktqrth vgvqtrvdir lepsdislet vvvtalgikk aekslgyslq qvnsdafdkv
      241 ktdnpinaln gkvagltvnt ragiledppi klrgetpiyv ingtpvtyyr gvssddiesi
      301 tvlkgpqaav lygsrganga ilittktgdd igekteitln sstmftagyl tlpeqqsiyg
      361 tgdfgqysyl dgkgggvydg lwtwgpkldq kdpttpsgyf etvqynspid pktgkriptp
      421 fvshkdnfrn flqqglttsn nvsishkfke gsfrislnql yrrgqtpntd lkrfgvnmaa
      481 nynitrklhi nasmiynyty sknrpwsgyg nshpyynilv ymganndird lrnyweegqe
      541 gyaqrnwnhv wfnnpwfvae eytrpysepe liasasldyd itddlnfmvk aatdskhqnq
      601 eeckpyawvg ndrglysvgs drrvdvnlda mlsykkrfge fdldamlgvs lfnyqrnylf
      661 sttegglqqp dlynlsnsqn tpsttskier rrmagaygsv tlgyrdafyl sftgrndwss
      721 tlnknnrsff ypsvafsali teavklpkav sfwkvraswa kvgfdqstvy mlqdtysfnt
      781 ywdgnaaftp pttiidpnik pyftssfevg tdlrffgsrl rfdfsyyrty degqiqkvdi
      841 nqssgyeeml tngndyrreg yelmvgatpi ktkdwkwdis fnwfqtrkyl dkiyngayny
      901 nnlkvgdrad alyesvwqrd pqgnfivfen ngrpiedpfk rvigyagadw efgisstlry
      961 rnwslsfdia grvggvirsd lnarmieagt hkltaapere ldwtktpsyi psnavvvvdg
     1021 dieyddhgnv lydtrgyaps ttpvyfkswi gymgklngpy tmgynlfkgd fiklrtmsvg
     1081 ydfsdllsgs rifkglelsv igtnlliwkk ldnedpdaay knfsypterm igfnltlkl
//
LOCUS       WP_118406730            1124 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Alistipes].
ACCESSION   WP_118406730
VERSION     WP_118406730.1
KEYWORDS    RefSeq.
SOURCE      Alistipes
  ORGANISM  Alistipes
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Alistipes"
                     /db_xref="taxon:239759"
     Protein         1..1124
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125841
     Region          22..1123
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkfltlfvl vcpllalaqq trqitgqvld radgaplvga tvfiapeetq akdynpqgti
       61 ayeqgrfafk lpasvrkvvv sylgyeartl disgksdfti ylsasdnkvd avvvtgyqri
      121 ekrkltssis svkmsdiard gvasvdemls gsiaglvstp tsggpgaask ikirstvtln
      181 gntdplwvld gmplegndip kdwsskesvd nlynmsiagl npwdieditv lkdaaataiy
      241 garaangvii ittkkglrnq amrvnvsasl fvtdrpdlsr lnlmnasqkv dlelglaana
      301 rlnylpgmgg varildkage rpalvnggsl aslspetqsa igalrrngtd wgreiyrtal
      361 nqqysvsisg gsgktgyyfs ggyyneqgtt vgtgferlnl tmktdydllq nlrfgasvfv
      421 gqnkndsyls dtdvftnpsr ytrtvnpyln aynpdgsyay dpdmtvntgn tdvldfnfle
      481 erarteytlk trsiktifdl dyrpvkglkl ytqfglqvdn satekmaqen tyftrkyqlk
      541 smvdqvvrlp kggviqnwng dlsqynwkaq aeyagtfggk heldlmagle mrgvtnttvh
      601 tkgfgydhkt mttkpinvpe dsdllddesf rqytksfyen rymsyfftgs ytydnrytvf
      661 gsmrydgtnl fgvdpkykfn pmwsisgaws inrerflrda rwldnlrlrv sygaqgnidr
      721 ttspyilgtw nstslggase dridvtsppn qnlrwettys wntaldfaaf ehrigftfel
      781 ygrrskdlit trtipsetgf istssnygei sskgieftln tvnvrtrdfr wetsiniahn
      841 tdkvekvrid dnswspslqg yssgavfaik tagldangip mfwrdgkkis lqefvgfrve
      901 asdpwglgip eyfeygpamn vsqkdvrgyl tyvgsrnpdv tggfnnrfyy knfdlaiscn
      961 fvfgqlmtrs pfynpaqtnp gqnyttemnk vwspsntsgt ypsltgnlqa dgsawgdwde
     1021 npdpyrvyyw imdnfptnvn lfnsldiwnr kinyfrvnsi rlgysfpqri trklhmaglr
     1081 vhfearnplv iatnydgyfd petygniyaq pmartysvgl nitf
//
LOCUS       WP_118406830            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroidales].
ACCESSION   WP_118406830
VERSION     WP_118406830.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122578
     Region          57..104
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          115..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkktirqsk rliislfvtf fcltasaaqa qtalvtidlq qvkmvqvmde ienqtkylfi
       61 ydknmdtgrl vnvhvnkrpv aealdqmvkg tdvvyeiqgs niiltvrsqq tdgpkvvsgk
      121 vtdnkgdavi gaailvkgtt vgtssgvdgv ytlripevna ntmitvnylg yepiellvgt
      181 reridivlqe qslgvdavvv talgikkqek altynvqevs gsivntvkda nfvnslsgki
      241 aglqinasas gaggstrvvm rgvksingdn nalyvvdgip lpslrskqte giyetpdggd
      301 yegianinpe diesmsvltg ataaalygsq gangvilitt kkgqegrvrv nyannttfss
      361 plvmpefqnt ygtssdapsm swgeklvspp hrydpedffq tgfdetnsig itagternqt
      421 yfsaasvntr giipnnvynr ynfslrnsav llpekltldl gatymkqysr nalvqgiyhn
      481 pligvylfpr gddirkyqly erynaglgys eqfwglefin gvenpywvtn relfennmqr
      541 ytfnatlkwn vtdwltlsgr vrtdntrmny trkiyassnt lfaseygnyl nhtmshnnly
      601 adallsidks ffdralslqf nlgasltddk hslvgyeghl agipnkftyn nivssdlntl
      661 pgqenyhdqn qavyatlqlg wkgmlyldvt arnewasqla ftdelnifyp svglsaviss
      721 madlsktgis flkirtsyae vgnppqryit grnysikggv vttetiapat hlrpertksf
      781 evgmnakfld nkiwadftyy ntatynqlfc ydappstgyk kaylnagkvn nwgieavagy
      841 kntwknfsws tsftfsmnrn tirelvpegt idpvtgaevn lpevnmdfgg yrvklkkggs
      901 igdfyvtglk tddkgniyvd pnsntvttdp dtwiyagntd ararlgwnnq fswkgislga
      961 lfdariggrg vsvtqalmdr fgvseasvda rengiqlseh qmlpgsgaqe ffnntgdgmg
     1021 mlaryvydmd nvrlrelslg ydlpskwfrn kmqatvslvg rnlwmlynka pfdpeqtast
     1081 styyqgidff mqpsvrtigf svrlqf
//
LOCUS       WP_118407015            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Alistipes].
ACCESSION   WP_118407015
VERSION     WP_118407015.1
KEYWORDS    RefSeq.
SOURCE      Alistipes
  ORGANISM  Alistipes
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Alistipes"
                     /db_xref="taxon:239759"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123257
     Region          23..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltilill amavvcrasa qnrvvtgtvs eedgtpltga vvqvvgtnna ataaidglyt
       61 lknvpsgavl rvsflgydpv ekkvdadrmd filkasaqei asvvvtgmqk mdkriftgat
      121 dqllasdvkl dgiseisrgl egrsagvsvq nvsgtfgaap kirirgatsi fgdskplwvv
      181 dgvimedvin vdanslssgd attlissaia glnaddiesf qilkdgsats iygaramagv
      241 ivittkkgtp gitkvsytge ftmrmvpsys nfnimnsqeq mavyqemydk gwlnyantvy
      301 rsesgvygkl sqlintydpa tgqfavlntp egrnaylrqa efrntdwfke lfrnsiqhsh
      361 sasissgsek gsyyasvgam vdpgwsiqsk vnrytllvnt tqhilkdklt lnlignasyr
      421 eqrapgslss evdpvfgtvk rdfdinpysy alrssrtldp defytrnytp fnikdelskn
      481 ymdlnvsdvk fqaelkwkit pkvevsalga ikyqassteh hiedssnqaq ayrsmatsii
      541 qsnnpylydn pdepnrdkys ilpqggiykr sdfraksrdf rasisyndtf ndkhilnlfg
      601 ivevnaidrr atsfqgwglq ydmgetpfyi ldlfkkqlee ntqyyslsnt rernaafagt
      661 fsysydyryt ingtlryegs nrlgrsrkar wlptwniagk wsidqesffe plrpafssla
      721 lrlsysltad rgptwvnnst atiyplnpwr gateirepal sisapensel tyekkhelnv
      781 gldmgflddr itlsmdayrr nnfdlignvv tmglggavdk qgnvaemksq gvelslftrn
      841 ierkdfkwqt nfifawmdne vtklktmtrm idyitgtgys megtprgslf slkfkglnem
      901 giptflaadg sitstniqfq etvnmsnlvy egpvdptitg slgnifkwkg ftlnvfmtys
      961 fgnvvrldpi fsngysdlta mprefanryl npgderrtnv pviastrqnn disnlyvays
     1021 aynysdvrva kgdfirmkei slsydfpqsv ssklrmsgls lkfqatnpfl iysdkklqgq
     1081 dpeffntggv avpmpkqftl tlrvsf
//
LOCUS       WP_118407073            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118407073
VERSION     WP_118407073.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117047
     Region          43..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmekckyll fcgtlalwma gsfqqvyaat epssqaiqqq snkvtgkvsd atgpiigasv
       61 vekgtangti tdldgnfsln vkagatlvvs yvgykseevk agrgplnitl kedakaldev
      121 vvtalgikre rkalgygide vkgealtkak etnlinsmag rvpglvvsqt aggpsgstrv
      181 ilrgstemtg nnqplyvvdg vpldntnfgs agtnggfdlg dgissinadd venmsvlkgp
      241 aasalygsra shgvilittk rankdkisve yngtltfdtq lakwdevqqi ygmgsngtys
      301 ydaisntnks wgpkadgsnm lkyfdgverp flivpdntsn ffrtgitatn saiigvnsgk
      361 tgirftytdm rnkdivpqth msrdifnlra ntsagkvdld fsvnytredv knrpalgdsk
      421 snigknlmtl attydqewlq tyqtadgeys nwngmdpynv npywdiyknf nkskkdlfrm
      481 ngkavwnidp hlklqatlga elnwftfddy kapttpgfea grlqnsafrn rmynfevlal
      541 ynnhwgdfdf natlggnvyk vnnqttvtta qdmkirdvps ltsfneisvv pgsyrkqins
      601 vygavnvgwk hmlyldatlr gdqsstlptg nnmyvypsfs gsfvfseltk lgdllpygkl
      661 rmswaqvgsd tdpyqlglvy tkskyaypgy tigyidngti pnkdlkptkt nsvemglelk
      721 flknrigldf tyysqisknq imgmasswtt gynyrlinag kienkgieia lstrpiqtrd
      781 fswdinlnfs knsnkvkeld gesdmfelek aswldvqvaa kvgenfgsiv gpdfqrnekg
      841 dilidpqtgl pqydksnhvl gnaswdwtgg lltnftyknl slvavfdvkv gadlysmsar
      901 aayesgkspe tlagrdawyr seeerlaagi akgadnwkpt ggfvapgvid ngdgtyrpnd
      961 iyinpedywm svcrnapsmf iydnsyvkcr eltlsynvpk swlknvvsgl tvsfvarnpf
     1021 ivwknipnid pdsnynnttg mgleygslps rrsygfnvnv kf
//
LOCUS       WP_118407346            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118407346
VERSION     WP_118407346.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125016
     Region          25..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkylcili clfanalafa saanrtitgv visgednepl igasvyvnad dlkkagasqt
       61 slgtitdmdg kfsisipekv trlhcsyigf eeqdivlqag kdtyrivlqa sahtlgdvvv
      121 tgyqelerrk ltaaiakvdv tdgmvgaaks idqalagqia gvavtttsga pgaparirir
      181 gtaslngtqd plwvldgipl egtdipeink dndndivnms qssiaglspn diesitilkd
      241 aaataiygar aangvivvtt krgktgkpvi nfntkltytp nlntsrlnll nseekvdlel
      301 qllkearfdi lwgltdpipv fpekgkvasi mkqynlidiy keqgwggltp eaqnainklk
      361 tintdwndil frdaftqeyn fsisggsekv tyynslgyvk engnvpgvsm srfnltskts
      421 yqinkilkig msifanrrkn ntfmtdtygl inpiyysria npyfapfdeq gnylydydvv
      481 rssetdekqg fnifeerant nkesvttain sifdvqlrfn dqwkvysqig vqwdqlsqee
      541 yaginsynir niretnkywk dgvhtylipe ggmlkttnst tsqltwkiqg eykntfgdih
      601 diqimagsei rknwvdnqas tgygydpkkl tfqnlifnde aqandwnlkt ksykenafas
      661 ffangsytlm nrytlggsvr mdgsdlfgvd kkyrflpiys vsglwrlsne sfirqykwid
      721 nlalrlsygl qgnidkgtsp flvgkydnvn ilpgyseeni iinsapnskl rwektasynl
      781 gmdfsvlnqa inlsvdyyyr kgtdligska lalengftnm sinwasmenk gvevnlqtrn
      841 ittknfswyt tfnfaynqnk vlkvltdksq vtpslegypv gaifalktkg inpdtgqiyl
      901 enkegkavtv eelfrmtsne dglgtyqigp nseeqrdfys yvgtsdapyt ggflntfnyr
      961 nwelnlnfsy nfgahvkttp synvsdldpg rnmnrdildr wtpenktgkf palatynynp
     1021 adyylfstrn diyrsldiwv kklsfvrlqn irlayrvpse wlhklsigga tvglearnlf
     1081 vissnydnym dpesmgnlys tpvpksitfn lslnf
//
LOCUS       WP_118407314            1197 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118407314
VERSION     WP_118407314.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1197
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134506
     Region          127..1194
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqqitlsr kkamrkvvwm kaaflllmfv ialhgraqnt dsklislelk eaplgealkq
       61 fsnvsgykvn fpsedvgayr vsvsihqlap laalqkileg kpfeyevkqh fitvrkvkpa
      121 sitrkvrnie grvvdekgdp lpganirgid spfgaisdik gnftckvmee thtlevsfvg
      181 mqtekvsikg rthvnvvmhe dkqqlgdvvv tgyqrisrer stasfgfids eqltrqmhsd
      241 lasslegqia glrmdinpnn gdmspilrgr gtfsdkvgtm plivvddmpt dltlseinpy
      301 nvesitvlkd aaaasiygal aangiivvvt kqakeegahv ninadwfits kpnfnslnla
      361 stsdiidyqt avfdanvaes gsasgflssy kagyynplfq lyldrengtl snseveatln
      421 qwrnndyyke yrdnawrtav tqrynvsvsq kvgknnhfls fnyendkgrt indkrnkfsl
      481 yyksnyaits wlnvnagvda rlgssdtpnt lftsytmqqr yerimdadgn rynspyvnvs
      541 gysggayngs vvskaegvsp yktfgfnvld algeggtksr nvsirpfvsl qarflkmfky
      601 nfmyqyewnh sksevfdaed sylmrmtyns midtngnsam pkggrfyqne lssnrytvrn
      661 qidfdkswkn htvtaiagle frenkipkpt rqlmygydpq tltsdildwq ayrdgvgtsa
      721 lsgntitlsg lsptlqesrh ryasfyanas ysylsrynvs gsirwdqadl fgldirnqrh
      781 plwsvgaswi mseesfmkdi vwldflkarm tygingnvdq ssttyfvvkq ktqsnpiktt
      841 yltyddddlp npklrwekta tynvgldfrl fnnlvngsle yynrhssdll vrrymdptlg
      901 aksrvvnnge mrnrgiefsl tanlirkkdw nfavdfnfah nknkmlkvdh sdsdtstsfi
      961 vspqnyfmeg tsyntlwayr idriengypv avdkdgndlv tfnedgtvan ittgsslkgt
     1021 enlvnlgslt pkfngavslr lnykgialna ffvyaggnkl rnsvvsmsdq vgsqtlkdit
     1081 nrwsadapda nvrmyidmpt kvktyastfq dwwqygdinv kdagyvklrs lslgyslpsg
     1141 icrqirlnsl nlklqvnnlf twckagsdid pesyglnsgt rgmaspktys iglstsf
//
LOCUS       WP_118407649            1139 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118407649
VERSION     WP_118407649.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1139)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1139)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1139
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125778
     Region          65..117
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          125..1138
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkttfekl pqanagrskn wktlraicll lflsvsftay sqitvnvkdi slraslkkie
       61 qvsnykffyn eslpelnrkv slnvkdatie qtmqqllggm dlaykkeqdn vivlirkaqd
      121 ksitkkvtgt vvdekgepvi gasivikges hgtitdfdgk ftladvpekg iltvsyigyk
      181 tvdlsatgqt fvkvvlqeds kmidevvvvg ygvqsqklvt tsiskvkmen idqgndynpi
      241 kmlqgrvagv nissasgtpg eapnvtvrgi gsvsggsspl yvvdgipsek ypnlnpndie
      301 smevlkdasa aaiygsrana gvvlittksg qqgktkievs grygfaylas diemansmey
      361 mntmqaaidn ynvqmganlq lyvpsqiqet nwvkeisrkn sktgtgsisv sggnekttff
      421 aslgantqeg ylnkssydqy nmrakfthki nnlfklnmnl agsasrsdll eetstslkvl
      481 rtareeqpwy spykeggtsy kvngtdilrh npvmlineed wvakkyqlsg vfsidvtpfk
      541 gfkytptvsv ygildntskk lsdkhdarkn ssgwgalaeq kdqsfryvid nifsynnewn
      601 kliysvmlgh sfekytyeqf gaksdnyang afpssnfdli nagpniyagn isytsyales
      661 yfgrialnwd nkyilnaslr sdgssrfakn krygyfpsas fawrasneef fpknkyvnda
      721 klrlswgmtg smagvsnyap lslisaggas yngsagfqis qdaraltwek asqfnigfdi
      781 emfqsrltln idmfyqkttd llfkkpvnat tgyttlqsni gslenkglel alngkiftgk
      841 fkwdlggnis fvknkllsli egndmyivps sgsnllggsm halingqpis tfymlkmegi
      901 yqrddevpak lyakgvragd vkyfdynedg disdadrmnv gkaipdfygg itsnfsykgf
      961 dlslfgqfsv ggkvmsawrg vnssegtdhl glalsnvkvn drgesveqyf nvskevangy
     1021 wrgegtsnti prpvrigvht gydydynvqt stryledasy fklktvtlgy tlpesvvkkl
     1081 rvnslrvyvs adnlltltky sgydpetsfs gspgdsnygv dfglqpvlrt fifglnlnf
//
LOCUS       WP_118407622             958 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118407622
VERSION     WP_118407622.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 958)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 958)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..958
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105935
     Region          1..957
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqtqevvikp nlkvvlksds qkldevvvta mgikrseksl gysvtsvkgd eitkaresnv
       61 lnslsgkiag vqigqssgta ggsssiqirg assigsvssp lfivdglpid ngafnpdrtn
      121 givdvgnrag dissddiesi nvlkgaaata lygarakdga ivittkkgsr nsqvsvtvns
      181 strfenvlkl pdfqndyaqg sygkynvkml ngwgpkissv qdqtfadfkg eqvtlqaypd
      241 nvkdfyetgm syinnvaiag gtersdfris vsttnqtgvv pgsdynkyaf avnggmnftk
      301 nftgrvsaqy irsdsegrpa qgsndnnlli plingmprtv nindvknnwi deygkqisld
      361 pegksnnpyw iinknkftnq ldrlignivl tykpieglti snnagtdfyt etrrkvyskg
      421 tignlegqfq twdlykriln ndlmisyekt faedygvkvm lghniyqedw rnnnvlaqnl
      481 vvdelyaytn akttspvnyt skkrlvglyg disfsyknmv fldvtgrndw sstlpvnnrs
      541 yfypsisgsf iftelmknkd vlsygklrms yanvgsdeqp yqlafqytpv nsyflqynlt
      601 nvfphnglvg ftgprvlpne nlkpqnqasf evgtdlrffq nrirldltyy ksvtknqivs
      661 idvplstgyf anninagkvs nkgievalgv tpvqtkdfkw dleatfaknt qkvdelaegl
      721 deysltsgls glqikaevgg sfglygtgwk rddsgnyvin ektglreivn nvrlgdvypd
      781 ftmginntfs ykgftlsfli dirqggslys etvgtlrttg laaetaahre dasfiepgvi
      841 lqsdgtyran dvpvksmqdy wghvakssnn egnifdasyv klrelnfsys fprkwfrsff
      901 vksldlgfea rnlwiikdhv phidpeanff gpaqigggve fnsipttrsf gfnirltl
//
LOCUS       WP_118407722            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118407722
VERSION     WP_118407722.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119032
     Region          25..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksnkwllsl avgflccgsa ysqttvkgki tsesgeplig atitvknstd gtvtdidgny
       61 slktkktlss kdlllfsyvg yktlqknytg ntmnvklaee sqqlndvvvt algikreekg
      121 lgyatetvkg dkitsalpsn wstalngkva glsvissggp lnssrislrg dvslnqngnd
      181 alvvvdgvpm sspmtnpgva ygagsnsels vdygngfsdi npddiesiqv lkgasataly
      241 gtraangvim vttksgagap kgigvsysgn fsiddvmrwp dyqyefgqgl psnigpagsi
      301 yegepyysyg kaedgsyast sgtssaygar fdanrkfyqy dpvtqgrase atpwvayknn
      361 rkdlfqtgyt itnsvaltgk sdrgsvrasi thtknewilp ntgfqritam isaqqqisra
      421 lrinfkssyt yrklnntpal gynsnsisyf lifqnpnvnl dwlrpmwrtg qenvkqlqpy
      481 ssfignpyvi lyesenpsek hsnvssvsan lrinskfdfm irsgiqlstd qreqhrpisd
      541 vvfgngffkk qnvfdyelns dalftyhdsf anglhvnasa ggnmmqqsyd mlaasvvgli
      601 tpgvyklang vsnpnvqtvi kkkalnslyf tanfaykdkl fldvtgrndw sstlpksnrs
      661 ffypsvsvsa vmnelflmpe pinllkvrgs faqvgndtdp yktspyygts dfpgsavvas
      721 tlynqdfkpe istnyeagfd lrmfqnrigl dftfyynrtk nqildapmdp ttgyskatin
      781 sgcvrnrgye iqldvtpvvs rdfrwnatft wsknenkiis laegadenql issignvsii
      841 grvggttgdl wgyklvrdpe gnvvindngl persgeieyv ataypkwkag lynefsyknf
      901 tlsvlldgqv ggkmyshshh kmteqgklah tlngrlpgte fymskddpri ataglspqdg
      961 mymiapgvvk nddgsfsknt kvvtvesyyk eyyrmanvet ntfstdflkl remrleyklp
     1021 gstlkktpfs kasiafyarn lfcitdyplf dpesaalngs smvtgvetgs lptartfgln
     1081 inlsf
//
LOCUS       WP_118407810            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118407810
VERSION     WP_118407810.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116913
     Region          40..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mynivtkisr rfyfvllams mlwgmmspkv faqevggani tgkvvdqygn pvpdvtitik
       61 nsdfkvitgi dgaftfqmkk gdvlrlshpe fihkevkvnk lkntervfkv tlneqfiknk
      121 etisgpyepk nkknylgsaa tvytdelssm mgttilpalq grmaglnvsq yagarahqia
      181 ansrndliga iplfgqgfys dntefsvgsr gnapvvvvdg iqrelysldp eaiesvsvqk
      241 dalssmflgm rssrgtllit tkepikegfq lsftgrfgvq salktpkpls ayqyayllne
      301 alqndgkdpl ysyddfnkfr thsnpythpd inwfdeilnk naitqaynln vtggnkvtqy
      361 fvsvgyqgek glfanptdnd ahdtnlsysr ymisskvnin itddftakvt llgrvedgnq
      421 pgvsygnlln siyntpnnay piknpngtwg gnktfdnnlm sqsinsgyik dsardmvggi
      481 nlkydfgklv eglsvrmvgn vsiqnrsyvq rskrapvyay gfdkegkefy tlhgatntqs
      541 nffnsvtsyq qmygqiavdy nrrfgkhgvk atlmsdtrqt lvnydlpqlp sniigdvayd
      601 yaekyfvqaa lsesyfnrya pgnrwgtfya fglgwdiske nfmedanwld qlkirgifgk
      661 tgngmdnsgy ygyrqtfssn vaagypmgtn lgmgnltten tplanpyltw ekayklnvgv
      721 dlslfnnrlk ltadyyndky fdllqsrgks iqligqyypa enigkvrrfg gelsltyqdr
      781 vsnfnyyisa nwscdqskll ymdeqyvpee ylrqtgrpvg vmyglvadgf ftskeeiens
      841 pviegfkniq pgdikykdln gdkvinefdr tviggdkpys yfginlgfew kglefsmlwq
      901 gaynrdyylg dvtltegfqq ngqfygqaye nmlgrwtpet aetatfprlt aggnnynrgn
      961 gwnssfwlrs gnyirlknis lgynlpdsfc rnnlgglrvk lfvngqnlft ksacdlvdpe
     1021 vsftsyplqr cistginirf
//
LOCUS       WP_118407899            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118407899
VERSION     WP_118407899.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114354
     Region          38..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrynkfifi lfvtailsgi atsleaqdkp kkkktaliev kglvtdntgk plsgvtvlsg
       61 egsiinytda ngkfalktka dgtllieafg ykdvvinlak eqptviklqn edlyaserdi
      121 heradggkty qrdlvgtvsk lsmenvlkyp dlqlsnalqg qaagliaisg dgglgyntst
      181 lyvrgqhnng tntalviidg ierpiddilp eeiesievlk datakilyga aatngvvlvr
      241 tkrgeahkri vrvgveygvq pstrvpkyld synysklfne arindgmnpy ytdtqlegyr
      301 nssgvndvly pnvdyynefl lnqniyrkgt iefnggnegv kyalvggytg gsglekvger
      361 salhrmnarg nldikitdfl tvtadvaarv elknwgakdg agifstlssn rpneypfiip
      421 netlsgqftp nedgtpffga strivdnlya dmvyggdtse ryvnsqtnlg anfdfnkyvk
      481 gltfnayvtf dnysylrqel rntyptyaid tysdldgeti trytqmkkld lpktqkiasn
      541 ntyryfgmra digyertlgv hdfsaigafr ytknemtgmt qdfkdanisl rlnysydkry
      601 laeltlagmg snkfdkndrf ffspavgasw iisnesfmke vkavnflklk asfgvlgytg
      661 ntgfflyqtg wnnngnynff qdqtdhkvsl arwgnpdltw eysqefnigi eglffnnrls
      721 telnyfhecr kdiigvnnaq yaatagnytm yenigqvtnq gidiainwkg nigrdflytv
      781 ganmtysknk ldkwneiegv esyrkaigrp tstifglqal glfgkdiple dhslqsygiy
      841 qngdiayadl nnngivddnd rmslgqsfpv ttwginvdlk ykgfglymlg tlhtgitqlc
      901 tnayywnngl ngyselalnr yhevnnpsgt mprlttttes nnfrdssfwt engsffrlkn
      961 ielsytfenk agrffankck lfvrgtnllt fskikdldpe rlnagitnyp aymtvtggls
     1021 vsf
//
LOCUS       WP_118408012            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118408012
VERSION     WP_118408012.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126594
     Region          36..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          114..1115
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknqaqkfi vlflfflfay swrveaqtgk ekqitmefkn eglpsifkrf ekvsgykvlf
       61 iydeissyts tgkvekatvd ealkviigkn plkyhidgqf initkedskk ffsqvkgkvf
      121 seedglpvig atiivedann iraitdnngn fqlsnvskds rvrisyvgle tqflnpssym
      181 svvmksdtka ldevvvtgmf nrkkegftgs avtikgeelk kystnnvaka iaavapglri
      241 mdninmgsnp nnlpdmrmrg ganmdlnaqa tvdlnsasnd vlavqgeyet yanqpllimd
      301 gfeisiqtla dmdpdrvasi vvlkdaaata iygsraangv iviesktpkp griwvtygge
      361 lrieapdmtg ynlmnareki daelqsglyt yggetvekwq lyqsklrevl agvntywldk
      421 plqtafqqrh tvtleggdea lryrmyvgyn sspgvmkdsk rdvltgsldf qyrlkkvllk
      481 nsitldnsva nespwgsfse ytrlnpylrp ygengeiqkr ldnfegvgge ssylnpmynt
      541 tfnskdqskn ftvrelfrve ynptnelrfe gafnlsksvg hrdifrpaqh tlfdnvtdpt
      601 lrgdyrrsqs eavswgidlt gswnkqlkdh yltanarmsv lennsetygn yvtgfpndnm
      661 dnllfgkkyn ekvtgdertt rsigwvaagg ysykykysfd fnirldgssq fgknnrwapf
      721 wstglrwdlk kenfmkdvsf isdfilrgty gttgsqgfdp yqahgyytys nlllpyyssd
      781 atgseilamh neslkwqttk stnlalelgf fdqrltarve yyrkitdnmv tsislapslg
      841 fgsypenlgk ienkgweisl saipykntak qaywtitvng srntdkllei seamkyrndl
      901 nasnlkdtpl pryeegesls riwvvrslgi dpasgdeill krngemtsav nwsandvvpi
      961 gnteptwqgy inssftykgw gadvsfryqf ggqvynqtli dkvenanlky nvdqrvsqlr
     1021 wekpgdkaqf ralnpsgwet katsrfimde nifqgsslsv yyrmdrtntk fishwglssa
     1081 kvtfnmedff ywstvkrerg lyypysrqft falnvaf
//
LOCUS       WP_118408730            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118408730
VERSION     WP_118408730.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115147
     Region          45..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkiryirl iglifvlivg ssltfaqnks krksakkplv evvsivtdek gsplknvsii
       61 cgegavvlyt dakgrfqtkv endatvmvea lgyedkvykl tgsnivpeki vlkkeplflt
      121 eeslvnradg gktykgnevg atsvlengqf gtfpdltltn mlqgkmlglq vrstvsglgn
      181 ntpdlfirgq hgmsentaiv iidgverpaa dlipeeieri ellkdataki lygaraangv
      241 lwvttrrgka nrriynatae agvvqmtrtp dflnsyqyan lynearandg ltpyynqkql
      301 egyknskgan dllypnvdly dqllnknany rkvsfdmtgg tdrvryalia gyvggsgfed
      361 vtytpqlhrl tlrgnldfnv tdfltisadv agrmemrkwg qldcgqvfta lsthrpneyp
      421 ltmspeetgl assdgiplfg asllrpmnay aetmyggytd erytrsqtni glkfdldmlt
      481 kglkagafls fdnydylqls lskvyptyai ktyrnfagee qimytqmkkt dvatsqsrks
      541 ttlqqtlgwn afaayentfn qkhdvsarlt ymyskttnqg vtqdiinany alrlnymydr
      601 ryaveadmal mgsnrfksgn kyffsaaggl awilsnedfl kdneyvnflk lktsagilgy
      661 drstehllye rawsqdgsfr fgttnngata yystfvragn pnlkwekaae wnigveglfl
      721 nnrlyteiny frekhtdiig svdasygdyt gnftyqdnmg svlnhgiegm ftwsdrindw
      781 sysvganfvw sknkvlkwnq vkhgeeyryt vgrstdammg lvaeglfgkd vainghapqt
      841 fadyqegdia ykdlngdkii dgrdvkelgn sfprttlgid fnvsykgwgl ylqgyselgv
      901 htwatnayyw nngegkyskl aldryhpann ptgsyprltt tagennfrns sfwlkntsff
      961 rmknvelsyt fnqfspssvv kkmkvfarga nlfvlssved ldpellnagv tnypvtrtft
     1021 ggvsfvf
//
LOCUS       WP_118408817             942 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118408817
VERSION     WP_118408817.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105200
     Region          39..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtiinsiykg kryailltti ltfyapvlfa qhiadsalve vaygqqpewr rtsaissirg
       61 edllkttsas lgnslqgqlp gltllqqsge pgydfsianl ylrgrtsyas gqkmlvyvdg
      121 feapieslst aeiesvtllk dasalalygm rgangvllvt tkkgcvsapq vsirlqtgiq
      181 qplgvpdpin aydyatlynq arvndglprl ytpeelnayq nntdpyfypn vnwkkailnn
      241 taplsmadls fkgggdvvqy yvmmnllqni gfykdtdkkr rensnayyas fnfrsnlniq
      301 iskhlstgln fsgsvgnrsi pggsssangl lgaiwrtapn afpvynpdgs yggnaaftnp
      361 vgnivnrgly kensrtfqli fmpkydlekl tkglsvsagi aynnymadss iknqnyarys
      421 lskgaggevl ytpygadspl esdegfrtdw srlnfkaqld ydrvfkqhql tasifflsdl
      481 yqkygsrddi kylnyagrvt ysynqkyige faasytgcdd yapgkrygff pafsagwils
      541 kenfmkninw veylklrasi glvgnnqnen grylfdqtys sngsyflgtg ssstggfrad
      601 mianpdiswe kervfnigld avllkglsve fdyfhkeryd ilsqpystip gfvgasygdi
      661 lpymnvgkvk nqgfegtiry esslknnfny yvetsawyak neivdmaeev klydyqyrkg
      721 rsvntpfvlv adglyqesdf dsngslkshl pvpqfgevnp gdikyidkng dgvvdsndsy
      781 pvgysnipew nyalkigfew kgidvealfh gvanrdiyls gplaysftdn gsasklalds
      841 wtpenpnasy prlstrtfen nyristywkr ngnyfrmkni rigytfpqsi araiklsrly
      901 vyanasnlft vshldgladp essslitypl trsynlgiki df
//
LOCUS       WP_118410303            1164 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118410303
VERSION     WP_118410303.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1164
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130386
     Region          129..1163
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mstkllseti crkglmvkcf valivfccsv geafaqtdtk vtinvnnvli rtaldqlqre
       61 akihfvydee nidsgkrvsl sytetplnav lddfckqtsl ryevkrnlil ilpskaektt
      121 gkhepfymtg vvtdetgesi igatimiggt sqgtvtdidg ryslqvtpgd lvsftfvgma
      181 dkvvkvqagk kvvnvkmetn ataladvvvt gyqtlskera tgsysvisek stkgkletdv
      241 lsrieglvag inktssnsnd vvirgittym gntkplyvvd gmpyegdlas inptdvqnit
      301 vlkdaaassi ygaraangvi vittkrgqeg ktkvsyngsi klfpkpdfdy lnlmssselv
      361 dmqiegfdyy htayenlnkr qavnpvvdfl yqhergqltd sqladallpy rtndnrkqie
      421 defarvgivh qhnlaisggs nknrymatvn ymgdygnqky qskdrigfsl kddvdffdwl
      481 sadfgvtgsf yrskgdngag sysslmssyp syymlrdlqg nplnfqrtks dyelqrlqsi
      541 glmdetyspi knraeesyhn nsnyyrlhag lnfkllegln idlkyqtegt ydknrtlysn
      601 msytvrnmin daaqydaatg sltlnvpkgg qldesryesy sytmraqvnf nrifgkhais
      661 alggaerrlv rrtgaqnyym gyddnslgvk pinplamspi ngteallgsf nwvygeynal
      721 thtedryvsf yangsytfde rysltgsiri dqsnlfgtdp kyqyrplwsv ggswqianep
      781 fmedcmwlnr lnlrmtygvg gnvpkdagpy mtmvdsgyne wvgdfgsyiq nppnsqlrwe
      841 ktastnvgid fsafnsrlsg sidyyykktt dllgnrnadp tlgwasllqn ygsmfnrgve
      901 lslqsvniqn knftwgtnlm fsynkneltn legtketvfy ysaynvaavg ypinsvfsyr
      961 yagldptngn vlvynkegek vskvssiddm vysgtrtpky taslknffsy rdfdfsfmfv
     1021 yygghvlrdv vagymggaps anltrkalnh wrkpgdenip gvapsfnrni yytdaqawys
     1081 adihvkkady iklrdislsy nlpknwlrky fiesaavtcq isnvwwwaan gdidpeaytt
     1141 sgygwgaltl pnpttytigl slnf
//
LOCUS       WP_118410182            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118410182
VERSION     WP_118410182.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121267
     Region          43..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkrlksvsm llflmgastg aayavanpgv advkitqqng actgvvvdat getvigasvv
       61 vkgttngtit gidgdfslsg vkqgdviqvs fvgyltqeik fkgeslkiil qedsqtlqev
      121 vvvgyggvqk aktmtasaat vkmselaklp vasmseglgg rvtgvvtqqa sgapgenari
      181 wirggenily viddvvmdsg qgneffnrlr pddiasmsil kdaaatavyg praangvvvi
      241 atkrgqegap titlnqkvsi mtpayrpkgl ssyeyalarn eaelasfqes ptfndtelsk
      301 yymgdlwqkg ygfeeirnlv nerynlgysl qdindlfdpl ktqgkniqdy yssydpwdmf
      361 dhtqpmyqtn vslrgggeri kyysslgymk qngvsdkysy eqvnmilntd amllsdkslk
      421 ftfnlngnts nnnkpadgeg vfnnamygdw mpkrpaawst glprkgsvea qlnngfnnte
      481 syrfqmnaal kwsvpwvegl saqaslnftt syyhqrhfnh dqegvydnpy atavssynpe
      541 nanlyekwnk yklltgifqi dytrsfgkhn lsamvnyqsq vrksnwtdak kkgypttlap
      601 qldlggtlvs aggsaeewgs asyigrftyd ydnkylfqys anyngslsys pdkrwgyfqa
      661 fslgwvmsde vwfknlvnpn ivnmiklrgg fglvgnevgs pfsfltqyaq ssnrilfgen
      721 masnvgwyes dvannlqwss skqygigldf gflkdrltgs fdtflylnkg dvmdmtddmi
      781 rvdilgmpnt pkinapytts rkggfevsln wqdkigkvgy rvgvnysywd ervtrhsssd
      841 sdwwtptfdn igkrpyvtng esitypyglk tnglhgswqk mynsllhann nmtlgtpalv
      901 dlngdgrvnd yyvfnaegst phtqfgvtlg adwngfdlel ffqgatgarg ampsplrsqq
      961 symwnygqya fqnaytpsnp dvdaalptpv pegngfgysy idiwsfdasy lklknislry
     1021 dlkrsvlknl pviqgldlsf vvtnaftwtk ksyplkdlqd pefittgasi ynnngtlgsy
     1081 ptqrsytlgv tvtl
//
LOCUS       WP_118410437            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118410437
VERSION     WP_118410437.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 getvigasvv vkgttngtit gldgdfslsn vkkgdiiqis fvgyqtveip wdgqpmnvtl
       61 qddtqtlgev vvtalgikre kkalgyamqe vkgdallear etnlanaltg kvsgvqiirs
      121 sngpggsski qlrgansvtg lnqplivvdg vpmdnftgas nndidnptld mgnglsdina
      181 ediesmsvlk gasaaalygs ragngvilit tkkgtkregl gitisgsvsa ettfmlpkrq
      241 kafgqgengv fdstnsyswg pevtgqsytk wdgttanmqi fdnvknffdt gvnlsesisf
      301 qqqydktsiy tslnrmddss mipganlsrt nltlrasstf gkddrwsida kvqyintlae
      361 nrpisgargn nafytifnmp ttidirdfss pvkdefgemi wwskgginpy wskdynpnkd
      421 srnrflmngs lkykftdwld aeikagsdmy ftegeeklya gsptnnknsr ystsekkffe
      481 nnfsflisgh kdelfgkfgg nfsfggnlme rkstgldnsm gkltapdlfs langdkkdls
      541 itetyihkki nslygtlgin yngwafldat frndwssaln kenrsffyps vslswvisdm
      601 vgkvgkgmpe wftyakaras faqvgndmda yqlyntysig sdpngnttag qgktkydadv
      661 rselitswea gaelkffnnr lgvdfawykt nakrqlmnip lnnlsgydnm kvnagniqnt
      721 gieimlnarp ietaqfswdt qlnfsqnksk iiellpgkpg mqyalggsda lqvyavagga
      781 ygeiwgtkyq rveegefkgq lllnesglpq atsdkhkige qqpdfllgwt ntfnyknftl
      841 sflidgrfgg difsftnmnl qrsgiaecta pggkredivv agvikdgngy kvndqsvsle
      901 ryykalatgr agiseayiyd atnirlrnia lsyrfpssml kktpfqqvkl gftvnnvwmi
      961 sshldgidpe svyatstnat glenssapts rsylfnvtlg f
//
LOCUS       WP_118413865            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroidaceae].
ACCESSION   WP_118413865
VERSION     WP_118413865.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidaceae
  ORGANISM  Bacteroidaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Bacteroidaceae"
                     /db_xref="taxon:815"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121657
     Region          33..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhsdyhgkl lrlamffval flcgtmayaq tdrmisgivv dengdplpaa hirqvsqtkg
       61 eelaavitdm nghfrltllr takeieisyl gyeskkvrlt sansyrivle paselldevv
      121 vtgyqtisre ratgsfakvd skkletqrls svsslmegri agysdgkirg vtsmnglttp
      181 lyvidgfpve ktisdglgnw venvpdlnie dienitvlkd aaatsiygar aangvvvitt
      241 kkagknqlnv sfsatltvrp ynfytghlag tadmiemeke waamnpnlqg egasqyaqnl
      301 ldnasmyscl gvqailkhht gaiseaqmeq tlhelasqef ryyddvkkyg krnpfsqqyn
      361 lnigrgtekn tfnaslsyrn nreedkytds esfglnlqnt srltswlsld lgtylnygdg
      421 ttqsynltsp gynyvpyssl lngdgsyytn taadrysksq qeiissygly smditpldel
      481 grnlsksknf snrtfarlnf kftdwlryta sfqyevgeyk tsqlqdkesy avrnkvntfa
      541 tdasgsgqat ynlpygniyt tgtnsirayn frqqldfnkt faekhdvtal fgmevrenkt
      601 eynnrkyyny dpalltydli dervlsntyt gvlgnyvsfn kndisniyel vnrfvsfygn
      661 aaytydgkym vtgsirwdrt nlfatgskyq kkpiwsvgag wnldkesffk vsfinmmklr
      721 fsygiggnia knsapymtay ynnnthvggi qgtisnrpnp dlrwekttta nigvdfsmfr
      781 nrlngsieyy nksgvdllan tngvptegfg fstytmnngk mrnrgfeltl sgdvimgkdw
      841 nwnvggvlgy nknkvtyvnv kapaiflqfd ypaayprvgv pynaiygylw agldskgqpq
      901 vydsegnihv ssspqkveda vylgtsvpvy sgaintnlry knwelaaqll fegghkmrnt
      961 niaypglgvt skdvskrwrq pgdeaytdvp ryvpseskdy nsyssdlysk asihvldadn
     1021 wrlknlsvty hvpasvcqkf yvknarimlg menvftlaks rdvkwmlggy skpnylcnvn
     1081 lnf
//
LOCUS       WP_118415696            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118415696
VERSION     WP_118415696.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123754
     Region          51..103
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          116..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mirrnylksl mifilmclpl lgasaqqkvt vnvvnaslkq vfstienqts yrfsyksdii
       61 dhrkditirk sgvpvtavld aalkgrnlky svvsqksivv sekhaaaapq qsnkhkmqgv
      121 vkddngepvi gatvsvvgtd elavtdmdgr ftinaakgak vkvsylgfed revkasenmn
      181 iamsedtqal sevvvvgygt mkrsdmtgal ssvntkemak rtttnpaeal qgkvagvnil
      241 rsggnagagv sikirgiktt gsneplyivd gfpgdinsvn pqdiesmeil kdgaaaaiyg
      301 svaangvvli ttkngkkget kvdfssylsf tqvskdldll daegykkvhk mmyenagepl
      361 payvthetgv nsdwvdairr kglaqsymvs lrggaekgqy svsynhadek giflgnserh
      421 diarmkvhat kgiidldanv dfkftkghqp qyqlkeaymm splvpiydes rkygfglsdf
      481 dglpnnrnvv addhykknty kkyhttanaa ltfnffpwln fktsygyrge heidnshypd
      541 ytadykspnl ypnnyeyray wqeqvfenvl sfnkqiqkhs inamlgtsls mtkynwesvs
      601 vegktnvnev ingqlntsdk pagfldpnfp tisggvggty ygtgsyweyn rasffgriny
      661 nfndrylfqf tfredgsskf gadsrwgffp svavgwrise epffpkntvi snlkfraswg
      721 qlgnenalgk ydflarissy ndmymgyvqg agsnpwtgsi aralenrslk wettdtknig
      781 fdfglfgnhl ngninyyine trdllitrri apsagldnpt lnvgkmrnqg felelnwndk
      841 isdfeynvgf nistiankvv alanedqtiy gvglkygseh fptqtkvgkp igafylyqad
      901 gifqsleevq ahknskgell qpnaqpgdvr fkdmngdgvi deddktysgt giakveanln
      961 lgasykgfdf savigsafgn klyngiryyy egmnsasnfl kttlnawtpt ntktdiprav
     1021 fgdpnqntre strflengdf vrlrqvqlgy tlpkalskhi ycesirfyvs aenvftitgy
     1081 sganpefsqg vlnsgidrft ypfsrsytvg aqvsf
//
LOCUS       WP_118415792             955 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118415792
VERSION     WP_118415792.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..955
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106117
     Region          43..954
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnskfksyns kfllaglvsl apmaadakta aenetdtvaa dkemvnvayr kvakgdilgg
       61 vsvvdveglm kknyhtysld nmqgyvggwn gnslwgmdad nagylvlvdg vpreatnvmp
      121 seidqitflk gaqavvlygs kaakgavlit tkrgkndglk vevqanagln vaksfpeylg
      181 saeymtlyne arandgltpl ysaediynhg lgtnpyrypn ldmyssdylr kmnsryeata
      241 eisgggkrah fysninyyrq gdflkfgeak nnntqrfsvr gnvdvnitdd ikawvnsnat
      301 fydshsaigd ywnaaatwrp nfpqnaspli stdmiapnak aawdlmsvak lvdgkyflag
      361 tqanssnifa dyyaagksky tsrqfqfdtg vninlhkllq glsfetrfav dyatsyttsf
      421 nnsyaiyipt wsnidgkdmi valkkegedk ksgvqnians vdnqtmlfsa qfnyantfnk
      481 vhnlsamlia sgyqqsksgv yhktssanla ldasydyakt yyadfglaai hsaqlapghr
      541 vgfspslslg wrlknenilk nskvvddmmi svsgsiined idlavngnry ylydtnwqta
      601 dgygwydgsa gkytfskrsa nkdldfikrk elsvnfktsl wqqmvtldas ffvnsmegyl
      661 istptfypsh fkpgypdasf mpvlnfnnnr rigfdfaanf nkkvgdvdlq lgvtgtyynt
      721 katkrdemna wsyqnregka ldgiwgykfa gffqseeeik nspdqsrlgs dvkpgdmkyv
      781 dvngdgkids ydqvflgkgg wygspftlgv nltakwknft ffalgtgnfg ayglknnsyw
      841 wvkgdgkysa vvrnrwtkat ketatyprlt tlsgsnnyqt sdfwmystda frlakvqity
      901 dlpstlfqkt wlkglsayvs ganlltiskn revlemnigs apqtryynig vkatf
//
LOCUS       WP_118416638            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118416638
VERSION     WP_118416638.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115362
     Region          7..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 malaqttvtg kvvsqedgep vigasikieg tkmgtvtdvd gnfslvapng naklvisylg
       61 mksqkvvaks kmkivleged ntlndvvvta lgvsrqkkal gyavtelkgd emlksrggls
      121 npvnalqgkv agltisssag smggsskvll rganslsgsn qplfvvdgvp ieggdnnste
      181 tqrggggydy gnliqdinpd dvenisvlkg asatalygsr asngvimitt krakksaglg
      241 vefsssvgfe tvtklpklqs qygggygyad dyaygddgdd mgtatingke ylipdygqde
      301 swgpkldgrq vlswydlltw knngsvgdpt tsawspassd yrdffktgvs ytnniavsqs
      361 ydnssfrisy tntsltgylp nssqyknaln vtgnimspdk klnvftsvny fnnrtkgrqd
      421 tgygdnnimv kftqwgqrql nmneleslyk npdgsqaswn iggiddttiq fhnnpywsry
      481 mnyendsrnr vygnvgfsyq iipqlkfqyk anldfwvdkq yernavysqe lskykeisrq
      541 qyelnhefll mynqtfgdys isanvganim rnhyeyvygl tqgglaipey ynlanslqaa
      601 kaynykrvkg inslfgditl gwknmlylea tlrgdksssl pssnntyvyp svtgswlfse
      661 llknkapwlt ygkvrlgfak vgndtdpyqv lstytqytni dsstpgyrlp ntlnnadlkp
      721 esttsyelgl emafldnrlg fdvtyyqtnt kdeilplsvs gttgyiykmi nsgeienkgi
      781 evaihatpik thdfewntsf tiasnknkvk sladgvdyyk iasapfmaev gakvgeeygi
      841 imgtnfvyde ngnkcvdpet glymatdgne vighiypdft ggwvnsfryk gfdasiqfdf
      901 skggqffstt tlwgnycgmm eetaangvre ngiisegvvy gtnepntmkv sardyyenyy
      961 ngpaaqsvlk sdyiklrein vgytfklnps wfvkslrlsa ygrnlgvwgp dckhfdpemi
     1021 vtssgnvqgi eggatpmvan ygfgvslkf
//
LOCUS       WP_118416465            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118416465
VERSION     WP_118416465.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115499
     Region          41..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkktmflgl lgaglmwmpa sailaaqmnn aamsvqqnqg ikgtvvdatg etligasvkv
       61 agttngavtd idgnftlnck pgatlevsyi gyktmtvkaa ngmkitmqed gkalnevvvt
      121 algikrdrka lgygleevkg eeltkaketn vinslsgkva glvvqntagg asgstrvllr
      181 gntemagnnq plyvvdgvpl dntnfgsage aggydlgdgi sainpddiet mtvlkgpaas
      241 alygsrashg vilittkkae kdkigveyng sftvdtqlak wddvqttygm gyngalptss
      301 tagtnsswgp kaddfvfkyf dgqehpfmmy pnnasdffrt gltaqnsail svnsgktgmr
      361 fsftdmrnkd ilpntnmsrd nfnlrvntsa gpvdfdftan ytrenvknrp algdsqsnvg
      421 knlmtlagty nqawlknyed adgnyqnwng ndqynknpyw dlykngntsk kdvfrltgka
      481 iwnidkhlkl qgtigtditn mnfedfiakt tpgtpagklt dqifnnrtln aellalynns
      541 wgdfdvnata ggnifkvnnk titntglnqq mngiknimny qeqntresmy kkqisslyas
      601 asigykhtyy legtirgdks stlptsnnty vypsvsgslv fsefiknkki inygkvrasw
      661 akvgsdtdpy qlalnystgk ysyagytigm isnstqpnkd lkptmtgsye lglemkffng
      721 rlgldatyyn qnskdqilsl astttsgysy rlvnageiqn kgielalngr llqikdfgwd
      781 mgvnfskntn kvkslvdgmd yfelakatwc gvsvgaqvge nygairghdv vrneqgqvii
      841 daatglpkvd qnvktignss wdwtggfytt fsyrnfrlsa sfdvkvgadi ysmsmrsayq
      901 tgkakgtlag reewyaseea rqaagmdisa wreagnckgl vvdgvidngd gtyrkndiav
      961 npedywkhma tsvqsefvyd nsyvkcreit fgytfpesll gkwvkglnvs fvarnpfivw
     1021 knipnidpds syntsglgle ygslpsrksy ginvnvkf
//
LOCUS       WP_118416839            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118416839
VERSION     WP_118416839.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116819
     Region          24..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmtfia clflslgmal aqtqvsgkvt saedgepiig asvkvvgtnt gtvtdidgnf
       61 slvlpngkns vkvsyigmqd ktvvlkagnn kivlasdsks ldevvvtamg itrqskalgy
      121 sasvvggekl sesrtgdims giagkvagvq isasssdpga snsvvirgvs slsgnnqply
      181 vvdgvplsns stssetsmva sanslnesyd fgnganavnp ddvesmtilk gaaatalygs
      241 raangvilit tksgkkqskg vgieyngglq lesvlrlpqm qnqfgmgwyg nktdlengsw
      301 gpefdgsslr ygniydnsqq yktyraikdn vkdffdtgir ynnsvsfnga tdvsnfflsl
      361 sqihddgiip tdadsynkyt fsgrashkik nvtlsmsany ayqknnfvst gqqagsmync
      421 imqtprdisi aelkdlnnpf ntpgyyytpy gvtnpyylln nnknqyeqer fygklqldwd
      481 iikdlkfsgr fgldtttghh degqpnmskl yqgtpnwada lsaltgkasq qtertreidl
      541 namlsyshnf mdkldvnava glngnerryn yfyaevtnlt iptfynlnns sekptvdqyk
      601 qlrrlmgayg qidlgwdnwa yltmtarndw sstlpkgnrs ffypgvtgsv ifsqfltpem
      661 qkiitfgkvr aawgktgnda nvymtssvfa qggantsgwg tsqfpftngn ynaysvgnvl
      721 gsptlspemt tefelglnma flqnrlsfdv syynrvsdkq ifslamdpas gytaqntnlg
      781 kirnrgveal isgtpiktkd fkwdislnwt lnrskvislp eelggesviy glsggtglya
      841 ivgeelgvfk aytsqrdaeg hiivdpktgl plktteqqiv gsmnskyqmg isntfsykgv
      901 slsfdfdirk ggvmysrtks vnyfvgnaiq taynsrhpfi vpnsvvqtgt dangapvyge
      961 nttalnatnl ynywnngadn ydadflvdks yvklrsvvls wdlpkawlak tfltgvkvsv
     1021 fgnnlflwtp ssntfidpes tsfgndlsgn ygeysanpss rkigfnvsvk f
//
LOCUS       WP_118417147            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_118417147
VERSION     WP_118417147.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121360
     Region          5..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maqtkvtgtv vsqedgepvi gasvvvagaa rtgtvtdidg hfslevpagk klvvsyigmq
       61 sqtltpaakm tirlkadsks lgevvvtgmq kmdkrlftga ttkisgdktk ldgvadisra
      121 legkaagvsv qnvsgtfgta pkirvrgats iygsskplwv vdgvimedvt evdaddlssg
      181 naetlissai aglnaddies fqilkdgsat siygaramag vivvttkkgk agtnrinytg
      241 eftmrlkpsy rnfnimnsqd qmgvyremyn dgyfsfeksf rasnsgvfgk myhlmntyds
      301 ktgtfglpnt eeamnsylqk aeyqntdwfd llfsnsisqn hsvsmstgtd kaqyytsfsv
      361 mndpgwskqs kvqrytanvn alyniskkls fnaianasyr kqrapgttsq svnnvtgevs
      421 rdfdinpysy alntsrtmdp nelyvrnyap fnifrelenn ylsldvvdmk fqgelkykpi
      481 skvelavlga ykystttnaa titdqsnqaw ayramddatm rdanpwlytd pdkanslpfs
      541 vlekggfyre tkykmnswdf ratasyndvy nkdhivnlfg gleinsldrs rsyfngvgmq
      601 ydmgylpafn ynffkqlaee ngqyysldns yqreasffgt atysykgryt ingtiryegs
      661 nklgksrsar wlptwnvsga wnaheeswfa klnpvlshlt lkasysltad rgpasvsnsl
      721 vviqsynpwr pfagdketgl eiyrlgnddl tyekkhelnl gldmgflnnr invtfdwyrr
      781 nnydligpkr tmgvggeiyk yanvasmrsh geeltistrn ietkdfkwst dfifshsknt
      841 vtdldsrani mqmitgtgft mngypvrslf sidfkglnnk glpivvnqng eetsyggdly
      901 fqstttdylk yegptdptin gsfgntfsyk gfklnvfity aagnkvrldp afsssysdmt
      961 ampkefinrw tqagdeaytd vpviadqrmk qndnyigyly naynystarv akgdfirmke
     1021 islaydfpgk wiqalrlnsv nlklqatnlf liysdkklhg qdpeffntgg vatpmprqft
     1081 ltlrvgl
//
LOCUS       WP_118417229            1196 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_118417229
VERSION     WP_118417229.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..1196
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134065
     Region          39..102
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          114..1192
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkiwklliv cflcalcslp dqvnaqtqpq kkitieisne rlpsvlkrle kisgykilft
       61 yddvkkytvs gvikdkaieq aldiiltdkp leyhienqfi titpkgpskq arifnvkgvv
      121 isgddgqpli gatvlikgtk tgvltdidgk flmekvpsna tlqfsyigmt pqdlsptpdm
      181 kvtlesdvqs lsevvvtgmq rmdkrmftga taqlsadnvk idgmpeisra legraagvsv
      241 qnvsgsfgta pkirvrgats iygsskplwv vdgvvmedvt evsadqlssg davtlissai
      301 aglnaddies fqilkdgsat siygaramag vivvttkkgk agisrinytg eysirlkpsy
      361 sefnimnsqe qmgvykemqk kgwlnfaety raadsgvygk myqlmntydp vtgqfalmni
      421 aktqreylks aemrntdwfd elfrtnimhn hsvslssgte kasfyaslsa lvdpgwtqqs
      481 svnrytanln atfnisktls inlissasyr kqrapgtlsq sidpvygevr rdfdinpysy
      541 alntsrtlsp defytrnysp fnimyeldnn ymnlhvvdmk fqselkwkpi qglelsalga
      601 vkyqttsqeh fitdnsnqaq ayramgdati rdknpflytn pddpyalpis ilpqggiyqk
      661 tdykmvgydf ratanynhsf geshitnlfl gtetnsidrn ktffngwgmq ytmgaipfyt
      721 yqffkksiee gtdyysvndt rarnvaffan gtysfqgkyt lngtiryegt nklgkarksr
      781 wlptwniaaa wniheesffk avepilshft lktsysltad rgpadvsnsm milksfkpyr
      841 pftnvqesgm ylvdlensel tyekkhelni gvdmgfldnr inlsadwysr nnfdligivn
      901 sqgvggkiak maniasmksh gieftlstkn ivtkdfdwns dfifsnskne vtdlksnasi
      961 idlvtgsgfa regypvhglf sipflglned gfpmfrnsdg svtvtdinfq erenvdfliy
     1021 egptdptitg sfgnifrykn frlnifltys fgnkirldpv fsnkytdlta mpkeyknrwv
     1081 ipgdeattni pvianrrqse kdrylktayn synysdarva dggfirmkev slsydfpqtw
     1141 ltslhlnsls lklqatnlcl lyadsklngq dpeffrsggv atpvpkqftl tlrlgl
//
LOCUS       WP_118417573            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_118417573
VERSION     WP_118417573.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124788
     Region          25..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkhlciii cflvnalama saanrtitgv visgednepl igasvyvhtd elkkagasqt
       61 slgtitdidg kfslsvpdkv trihcsyigf eeqvivlqgd kksyrivlqt sahtlgdvvv
      121 tgyqtlerrk ltaaiskvev sdamvgaaks idqaltgqia gvsvtntsga pgspakirir
      181 gtasmngtqd plwvldgipl egtdipkmdn kssdndivni gqssiaglsp ndiesitilk
      241 daaataiyga raangvivvt tkrgrtgkpv vnfntkltyt pnletsrlnl lnseekvnle
      301 lqmmkeapfn kwgfypipvy sekggvaail kqynlmdiyr ekgwegltpe aqnainrlks
      361 intdwndilf rdaitqeyni sisggsekvt yynslgytle ngnipgvsls rfnltsktsy
      421 qinkllkvgv sifanrrknt tfltdtyglt npvyysrian pyfepfdnnn nylydydvvt
      481 gsipdllqgy nileerents nksvttains ifdielrfnd qwkvtsqvgv qwdqlsreey
      541 agtnsfnlrn qrensayykg ndriylipeg gmlkstnstt sqitwkvqge ykntfndihn
      601 iqimagseir knwyenqast gygydpktlt fknlefrdsk qanewklktk sfkenafasf
      661 yangsytlmd rytlggsvrm dgsdlfgvdk kyrylpiysv sglwrisnep linqfkwidn
      721 lalrlsyglq gnidkntspf ivgtygnisi lpgsneesit insapnsklr wektasyntg
      781 idfsvfnqai nlsvdyyyrk gtdlignkml plengftsma vnwasmknqg ieinlqtrni
      841 atkdfswyts fnfaynqnkv lkvmtekdqv tpslegypvg aiftlktkgi ksetgqiyie
      901 nkdgeavtie elfqmadkgn ldgeysigvd ketergfysy agtsdapytg gfmntfnyrn
      961 welnlnfsyn lgahvktdpt yyiadpdpgr nmnrdildrw tpenksgkfp altslntnpa
     1021 dyylfstrrd lyksldiwvk klsyirlqni rlayhfpsew lhklsisgat vglearnlfv
     1081 fgssyknymd pesmsnlyst pvpksvtfnl slnf
//
LOCUS       WP_118417824             899 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides thetaiotaomicron].
ACCESSION   WP_118417824
VERSION     WP_118417824.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 899)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 899)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 899)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..899
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         <1..899
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..898
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 qkalsynvqq vkgdeltnik danfinalsg kvagvtinas sagagaaarv vmrgtkslek
       61 ndnalyvidg ipmfnvnsgd naggtmnkqp gsnsvadinp ediesmtilt gpsaaalygs
      121 dasngvilit tkkgtvgkvq isysnstsfs spmmmpkfqn iygnregelg swgslmdtps
      181 nfdpsdffnt gmtemngftl ttgteqnqty asvsttnstg ilpnnaynry nfsirntakf
      241 cdnklsldlg aqyiiqnnkn mvgsgqyfnp lvslylfprg enfqevqmye rysearnlmv
      301 qywpesifgt dldmqnpywi mnrmqnelsk rrymfnaslk wditdwvnvt grvrvdnsds
      361 dsyekyyast rgtftesssk gyyghtkqnd rsvyadvmas inknffddkl slnatvgasi
      421 ndiqedamyl kggleqipnf fhygninvnt skrneskwhd qvqsvfasae lgwnhqlylt
      481 vtgrndwasq laftskgfyf ypsvglswlv sesvklpkai sylkvrgswa evasspnryl
      541 tqmqytyneq tntyeypash yntnlkpent kswelgvnak flgnrinldm tfyrsntfnq
      601 tfyvdasass gyknnivqtg niqnqgiela lgysdtfdkv kvstnftytl nqnkivslan
      661 gainpetgea iemeyyskgt lgtsggptlr lyengsmgdi yinqrlrqsp ngyiwkdpsn
      721 gslaientey rkvgsilpky ylgwngsvaw kgwnlgfaft grfgglvvsd tqamidkygv
      781 sessavarqa ggvwvgdskv daeeyyskvt tavgtyytys atnirlsels lsyqlpktwf
      841 knhvnmtlgl tgknlwmiyc kapydpests svtsnfyqgv dyfqqpslrs lgfnvkltf
//
LOCUS       WP_118417832             926 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_118417832
VERSION     WP_118417832.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 926)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 926)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 926)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..926
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..926
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102000
     Region          38..925
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkinyilit lllggsvsln aqtskaasem qladtlsigy qmnvssrtss ysingvnasa
       61 fekspyidis kalygkvagl nvyqgtgssa dnvstlsihg naplvlidgf prdisditsm
      121 eiescyvlkd aaaaalygmr gangvvlitt krgisnglkv nvdynfgvnt qfrspdfada
      181 ytyanalnta lsgdglpary naqeldafrt giypydypnv dwwnetlnnt glthnlkmsf
      241 sggsdkfrfy tvvdyyrdrs mlkkntedtr fdttptdtrl tvrtnldvkv testllkagi
      301 vgrlkefrgt rygrsaifnk iygipsaafp iryengiygg ssvygtgnpv allkdyghir
      361 nvygtlladl sirqdlsalt kglaaeasvs fdniggmnet tnkeyrymns nasitsdgtl
      421 mttpaiygtd setlghtqpf erlmlrsdfq akvdynrtfg khqvggaliy dmqsvvkngr
      481 nnsqknqsvl vnatytydnr yslnavfnrs gsaylpdgdk ysnypavsaa wivsneafme
      541 kvtpinlfki rasyglsgwd gnlshelwrq sygsgdagyn fgvnaggqsg gsegdlpvig
      601 lvaeksqkat fgfdlaafdn rlnatvegfy ekrsdilvsg anstsgiigi tvgqvnegiy
      661 kykgvdasls wndkigdfhy gigasmsyln tevvnvnqay qeydylytkg nrigqmygle
      721 aigffnsqqe innspqqtfs dvapgdvkyk dqngdnride kdvvkmfgss vprfyfgfnl
      781 nfsykrlels adfqgmtgvt vsllnsplys plvsngnisn tflneeiswt penktnatmp
      841 rlttqenlnn yrasslwyrd ssflklrnll vaytfpksqt rfadlkvfvq gtnlfsldni
      901 hfadpeqlgi aypstrsywa giklnf
//
LOCUS       WP_118417841            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_118417841
VERSION     WP_118417841.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117963
     Region          41..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrsiyrllil gaflyhsqls aaipinassp epeaitqgkl titgvvidka tgeslpsvav
       61 mvkgtsvgsl tdadgkfsiq vpdrnttlvf tfvsyqkkei avgdknfikv tmeenvqmld
      121 eavvigyqsv arrnvhgavt sikaddlqgi tapsidimlq gavpgvniqt fsgepggrnt
      181 ftvrgntevs sadltsspli vldgvpvdps vvgysassan flsninpndi ltldflkdaa
      241 aaaiygskaa ngvliittkr gkegkprisf ngrfgivtkp vtpkiymgaa errakldqma
      301 iygnennlea tpqiltdsin pmfnnatnwf dlfykngvvh dynltvsggd ekanyriggg
      361 yykeegtiig tgferfsftg nfvnkvgsrl elntsvaynv nqrepvpggn svnnaigmdi
      421 snmpstllql tdidrnrmlg syeqaiydns ddmirlseqa sydilkgkvl sfntqfsyvk
      481 sssrldksep gtanvdrmss alsesrqmtt wnienyftfn kifgahsvma llgqsaegit
      541 skyssmegry lssdyihvvn gvskdnltay sgieeakaas ffarasyifk drysisssir
      601 tdgssrfgsn qrwgtfptas afwlvseepf mnnlkdvvsl lkfrgswgks gslpsgfygh
      661 hnrymaasst ydgggaiipn fadgiaqkel tweetkewdl gmdleflngr ftliadiynk
      721 ekhgifysfm lpktsgyeky ytnavavrna gvelalvarv lpatskwqwn inanisynkn
      781 qimqlpdgnk tvvednrylm vgqpinsfrl sqyngiylne dmipfdpytg lkyknesgqy
      841 vqvgwadyed vdkdnqyvsw kdkkpigdpn pkwvgglntn lsygpwslfv qtsftlgrdi
      901 lntqfaktma plsaqygade egvgfsggpg anyanpadgh wyyaedfvar rmmvdlsrys
      961 fwqkdgdntn ypsrsqymnn nnfiersslf lengsylkln timlsynldk lkkwginnar
     1021 lsltaenvai ikskntlaad psnvspdgyy tgngyglprk ftiglmfdf
//
LOCUS       WP_118417851            1124 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118417851
VERSION     WP_118417851.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1124
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123581
     Region          7..1122
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvvqqtrtvk glvsdelgpv agatvivkgt qngvitnvng eftlsgvkvg dvievsyigy
       61 atlsvkynge qrlslqlked sqqlgevvvt alglpkqaks vgyatsrvst aeieranaln
      121 pvnalqgkva gvqinaggas gitssssiti rgaksvdknn spifvvdgmi iqeamtgnla
      181 gtdwgsqlkn lnpadyesvt vlkgaaatal fgsrgangai mivskggkfg kkglgievnq
      241 tvettdvyks pvdmqnvfga gvvyngyqgd lgpdgtllkt snswgprmdg rminqylpng
      301 estpfvphed nwkefyqtgv nsttnvavng gnekssfrls ygytgnkgvf knndfsrhni
      361 afrgntelnk vfsielgvky afssakngas qggwdwgnnv gmmtsynlpr nydvgahyqq
      421 yrdpetkavv natfgalssy fhtrdtqlqq rnensllsdi ilrakitpwl tssikanyny
      481 yaissekrwc gtganygpsg sggygrggst egnynfmgml qfteqpfkvg nedftfsaia
      541 aaelygntek hswkketngg lvvpgvfafs nsknkiepef dytprnqqtf giygivnlsw
      601 rdqvflelta rndwlstlty pvymtsgrnn fsvfypsing swvftdtfrk kmpewfsfgk
      661 iraslarvgm gtkayatsdg ygifkqkniy lpdrsgsvla atpnlgttyn edlkpeiqqs
      721 ielgfdvrff nerlnidfay yktntfnqim kvgsvtesga nsklinagni qnqgielqve
      781 gtpirtkdwr wslggnltvn rgkvieldne vkewqlmggy daapeiwaye ggefgvltsy
      841 knssymspiv twqgekgdpr ngkmviqyer eyasphsvsm yspvtyyqrn ekgdrdrhil
      901 gkvepdftls lntslsyknf dlyiqgdgrf ggnyfsnmwk yasptgslks slegraqeyg
      961 gikrinykge taydglmlda vfaegakapv qnpdgtagel vdvggmtyke aiekknirpv
     1021 mtgawyawny gwgmaampgs iqdntwfclr eitlgyrlpe kickkfgany lrlgftarni
     1081 cyiinkltdg lnpasisnnn plqpmdiggv pfyrtyavnl tvrf
//
LOCUS       WP_118418053            1013 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides thetaiotaomicron].
ACCESSION   WP_118418053
VERSION     WP_118418053.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         <1..1013
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 kpdaevleev vvtgmqkmdk rlftgaatkl daegvklngm adisrglegr aagvsvqnvs
       61 gtfgtapkir vrgatsiygs skplwvvdgv imedavevsa dqlssgdaet lissaiagln
      121 addiesfqil kdgsatsiyg aramagvivv ttkkgkagvs risytgeftt rlvpsyndfn
      181 imnsqdqmgv ykemqqkgwl nfaetsrtae sgvygkmyql intydpttgq yallntdeak
      241 naylreaemr ntdwfdtlfs pslsqnhsvs lssgtekssf yaslsamhdp gwykqsgvdr
      301 ytanlnmnhn ilknlsinli ssasyrkqka pgtlgqdidl vngqvkrefd inpysyalnt
      361 srtldpntyy tsnyadfnil neldnnymel niadlkfqge lkwkpitgle lsalgavkyq
      421 stsqehnikd qsnqasayra glddktimdr npflyknpdn pyalpisilp eggiyqrrdy
      481 kmlgydfrat aswnhvfndi hitnffagte instdrskny yqgwgmqysm geipyyvyef
      541 fkkgiedgnn yyslsqtrsr saaffanaty sykgrytvng taryegtnrm gksrsarwlp
      601 twnvsgawna heekffsnlt svlshftlka sysltadrgp advtnsqaii tsyspyrpft
      661 siqesglyik elenseltye kkhelnigad mgflnnrinl avdwykrnny dligivntqg
      721 aggqilkyan iasmkshgie ftlstknikt kdfnwntdfi fsnaknevtd lkqnanvmel
      781 isgngfakqg ypvrglfsip fvgldkdgip viinekgeat stdinfqerq ntgflkyegp
      841 tdptitgslg nmfsykgfrl nlfitysfgn virlnpvfka yysdltamtr efknrwtlpg
      901 deaktnvpai lskrmydsne dlkyaynayn ysteriakgd firlkeisla ydfpkawinp
      961 lkltdlslkv qatnlfliya ddklngqdpe ffnaggvasp vprqftitlr lgl
//
LOCUS       WP_118418029            1124 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118418029
VERSION     WP_118418029.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1124
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125825
     Region          30..1123
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myrlinikka lttvlllftl ltavaqtagt vtgtvrneqg etligvhvqv lgtkakavsd
       61 vngnftikav pgqtlqvsyi gmltqrvkvg gqplnivlkd dsrqidevvv tgyqnirnrv
      121 ytgaatsvkm ddiklegvad vsrmlegrvp glsiqnisgt fgsaprinir ggasiignvq
      181 plwvidgavy edlvhlsldq lasgdavtli ssavsglnpa diqdiqvlkd asatsvygar
      241 alngvivitt ksgrresplr vtystentvr lkprysefdl lnsqetmsly qemndkgyfg
      301 isnslygrrs giyyqlykgv stvnpatgty ylpntpearm dflrkheyan tdwfdllftm
      361 kpitnhvitl sgggkntaty asigfyhdag wtvtdkvrrl ttnvkntfyi ndkltamlta
      421 qgnirsqkap gtmpqrknnt lgvferdfdi npftyalgts rtlrpynedg sleyyrnnwa
      481 pfnifneyan nkmnidvldf kiqgeatyrl nddiaiktll strqvytstt hevheasniv
      541 qafranenpf vaqqniylvh dkdnpqlqpk vglthggiln kteaslksvl arialdfdkr
      601 mgehdlkafa ftevrsavrt vnpfqgygiq ydrgnqvytn plifsklige gndyfnlhkr
      661 ndrgvtfsfn gtygyagkyv fnmvfnsegs ntsgkgaral wlptwnvgak wnidqeafmk
      721 dnktiprlal rvsygltakm neeainansi yksgivnrhn fndrenkfni lhlenrdltw
      781 ekmyelniga elglfnnris ttldvyqrnt fdlidlvrts gvggqyykya nfgdmrtrgv
      841 elglhtkniv tdgfswstsl tlsamdqkit rlqntpnafd mvagrgrgni vgyprgslfs
      901 fnfqglnnng lptfdfglyp ssqgeysnia gadfldtqya ksyllyhgpi epqvigglsn
      961 tfkykdwefs ffitmqagnk irlnptfdpe fgdlnvfsks yynrwlnpgd efktdvpalp
     1021 sqeliakvgk enieraynty nysqqmvadg sfvrmknisl gynmpdkflk kvrlhaanlr
     1081 lnitnpfliy sdkklkgqdp eyyksggvsl ptpkqytvtl nigf
//
LOCUS       WP_118418212            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118418212
VERSION     WP_118418212.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125046
     Region          25..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkylcili clfanalafa saanrtitgv visgednepl igasvyvnad dlkkagasqt
       61 slgtitdmdg kfsisipekv trlhcsyigf eeqdivlqag kdtyrivlqa sshtlgdvvv
      121 tgyqelerrk ltaaiakvdv tdgmvgaaks idqalagqia gvavtttsga pgaparirir
      181 gtaslngtqd plwvldgipl egtdipeink dndndivnms qssiaglspn diesitilkd
      241 aaataiygar aangvivvtt krgktgkpvi nfntkltytp nlntsrlnll nseekvdlel
      301 qllkearfei lwgltdpipv fpekgkvaai mkqynlidiy keqgwngltp eaqnainklk
      361 tintdwndil frdaftqeyn fsisggsekv tyynslgyvk engnvpgvsm srfnltskts
      421 yqinkilkig msifanrrkn ntfmtdtygl inpiyysria npyfapfdeq gnylydydvv
      481 rsnetdekqg fnifeerant nkesvttain sifdvqlrfn dqwkvysqig vqwdqlsqee
      541 yaginsynir nirennkywk dgvqtylipe ggmlkttnst tsqltwkiqg eykntfgdih
      601 diqimagsei rknwadnqas tgygydpkkl tfqnlifkde aqandwnlkt ksykenafas
      661 ffangsytlm nrytlggsvr mdgsdlfgvd kkyrflpiys vsglwrlsne sfirqykwvd
      721 nlalrlsygl qgnidkgtsp flvgkydnvn ilpgyseeni iinsapnskl rwektasynl
      781 gidfsvlnqa inlsvdyyyr kgtdligska lalengftnm sinwasmenk gveinlqtrn
      841 ittknfswyt tfnfaynqnk vlkvltdksq vtpslegypv gaifalktkg inpdtgqiyl
      901 enkegkavtv eelfrmtsne dglgtyqigp steeqrdfys yvgtsdapyt ggflntfnyr
      961 nwelnlnfsy nfgahvkttp synvsdldpg rnmnrdildr wtpenttgkf palatynynp
     1021 adyylfstrn diyrsldiwv kklsfvrlqn irlayrvpse wlhklsigga tvglearnlf
     1081 vissnydnym dpesmgnlys tpvpksitfn lslnf
//
LOCUS       WP_118418182            1198 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118418182
VERSION     WP_118418182.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1198)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1198
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=135114
     Region          130..1195
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqqitlle krtkkklvwm rtaflllvft atalqgwaqn aenrqislem kneplgsalk
       61 qfsnvsgykv nfpsedvapy rvtvsiyqma pfaalqkile gkpfeydvkq nfitvrkvka
      121 tsttasgkfr nvggqvvdes gdplpganvk vlnspfgait daegnftcrv pvdvhtlevs
      181 fvgmqsekvs vkdrnnvrvi mhedkqqlgd vivtgyqris rerstaafgf vdseqlnrqm
      241 hsdlassleg qvaglrmnin sntgdmspil rgvgtfshdv gteplivvdd mptnlrlsei
      301 npynvesitv lkdaaaasiy galaangviv vatmrakkeg ahvsinadwf ittkpnfksl
      361 nlastsdiid yqtavfdanv aekgsaanfl ssfeynyynp lfqlyldqan gditsgevna
      421 tlrqwcnndy ykeyrdnawr taitqrynvt vsqkagnsnh llsfnyekds qrvisgksnk
      481 islyyksnya vtnwlnlnag vdvrmgrsyt pnsgytsytl qqryerilda dgnhytspyv
      541 nvdtspsyng svvrkaegvs pyrtfgfnvl daleesitks hdvsirpfvs lqarflkmfk
      601 ynfmyqyewn kgkselfese ntyvmrmlyn smvdtngkaq lpqggrfnqt eveskrytvr
      661 nqidfdktwk dhavtaiagl efrenkiptp arqllygydp qtltsdfmnw qtyrdgvgts
      721 alsgrtitls glsatlhesr hryasfyana gysylsrynl sgsirwdqad lfgldirnqr
      781 hplwsigasw ilseesfike iswldylklr mtygingnvd qssttyfvvk kktqsnpikt
      841 tyltyedddl pnpklrwekt atynigldfr lfknlisgsl eyynrhssdl lvrrymdptl
      901 gagsrvvnng emrnrgvels lttniirkkd wnfavdfnfd ynknkmlkvd hsesdnarvf
      961 iaspqvyfme gtsyntlway rihriengyp vavdkdgndl vkfnedgtva sitsgsslkg
     1021 tddlvnlgsl tpkfsgsvgl rfnyknfdln affvyaggnk lrnsvlkmdd qlgtqtlkgi
     1081 anrwtaddsn aqvrmyldip aqvktyastf qdwwqygdin vkdagyvklr slsvgynlpf
     1141 tvcqhlrlss lkvkvqvnnl ftwckagsdi dpesygmndg trgiaspkty siglstsf
//
LOCUS       WP_118418165             993 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118418165
VERSION     WP_118418165.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111422
     Region          26..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkllftigm lfissvslva qemmngivkd gsgkplsgvk vskvgefknn nvtdedglfs
       61 lllkkgdyie lnyadvatkr ikitgdtlnl vfdikkdavv dlgflkrted tqtqsvtaiy
      121 adlleknats pdrvnnalfg lisglhlsqt vgwdanagmn irgrgglgsg aplvlvdgfe
      181 rgltnmtiee iesvqvlkdg aatalmgarg angvilvntk rgiynsfdvd vnyrhgfdfp
      241 vnrpemaday tyamaqneal yydglplqyt krdlerfkdg tnpnyypnvn wykegtrnfs
      301 ennqfnvmmr gggkrvryma lldyknkfgl lnedythysd rynsqirtye lglrmnldvd
      361 itsstrmkfg lygiigedkr pntdintifq nfykvpaaaf pvktlnnnwg sntlfkmnpi
      421 aaiadvgyvq enrrmletdm ritqdfsmfl kglsaevava ydntatfqdi gsktykyevg
      481 ylseeglpvs etygtdskvq itksvlsaql irasveakln ydytsgkhql sasavyrqdm
      541 keplennasy yrqnimgfvg ynygnrymvd vvgnyygtsv llkgdkfrfy pavsagwnla
      601 nedflkgasn ldllklrasw grsavdeldy glgnyfwtgg tgypfgdgmt vvnglkeqrl
      661 pvyglnleta dkynvgvdlr lwknftatae vyydhrtnil vannnvsgil gidppkacig
      721 evksrgvels lgwsgqhkdf nyfvnanwal ndseivengq ayqpydylyt rghkvgqlfg
      781 leavgyfrde ediakspeqt fsvvrpgdvk ykdqngdgri dsedriaigk sttvpemvfg
      841 lnlgfeykgf gidmvfngvs gltkqlnvan vhqplrngnt niatwylkdk irwteamkdv
      901 anvprlstls nennyqtstq wiedgsflkl rnlnvyynlp qkwvkkikld klqiyakaqn
      961 vfsidkidyf ncedltlgyp dlfsvclgln inf
//
LOCUS       WP_118418365            1173 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118418365
VERSION     WP_118418365.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1173
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131757
     Region          32..98
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          117..1172
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mndrrnsffr lfllillclg vqslraqtvt kvfkneplka vlkeverqtk ysiiyktdev
       61 nenkkitasf qqatvnnvla tvldkdveyk lqnrmiiitk kternttavp sqplhrvtgk
      121 vvdvngdpvi gasvqvmgqs mgtitnldge ftlssvpana lvvvsyigfe kkeikvsdlq
      181 kssrvilred tatleevvvv gygtqkkinl tgavavvdsk amedrpvpra sqmlqgtvpn
      241 mnvtfgsgyp gasatinirg vnsisgnasp lvlidgiegd idrlnpndia sisvlkdass
      301 aaiygarasy gvilvttkeg sarkttvsyd gryswsnqtt stdfetrgyy sagindlfyt
      361 nyngkpytny teedyrqlwl rrndktenpe rpwvvtdqrd grdtyvyygn fdwynylyrk
      421 nrpmwehnis vsggneklny ylsgntvdqt gifrqnpdky kvynfrskis akitprltis
      481 nntkyhynsy sypglsginn nfntavnhal asfvpinpdg savyltslsn savldgmgai
      541 laygkhkned qryefsttfe asfnvmknln vranysylhy nyqtmnrtvn vpyskypgei
      601 sylttgsgvn qlketqtnhw yqafnvygdy mldiadhqik imtgynyetk rlkdikvsrq
      661 gllsddlndl nlavgdamtm sggqneyall gafyrlnysy kggrylfets grydgssrfr
      721 sghrfgffps asvgwrisee pffgnlkkni dnvklrlsyg slgnqqvgyy dyiqtintng
      781 tmnyifgdqk kgsyasvsdp nsadltwetv stwnvgldlg flnnrlnlta dayvrdtkgm
      841 qtsgkklpga yganepkqna anlrtkgwel mltwndafkl ankpfrynls vgladntsei
      901 tkfdnpskil sdyyvgqklg diwgyvvdgl frtdeeaany nvdqtavnfv intaqvnpgl
      961 hagdmkfvdl dgdhtissgs ntaddpgdrk iignslpryt ysiqggfdwy gfdfsiylqg
     1021 vghqdwypgt nsvffwgpya rpyssfiprd flsqvwspen pdayfprpig ylalgnnrsl
     1081 gvvndrylqn laycrvknit vgytipavwt kkvkierlhi yfsgenlftf splksdyidp
     1141 eqasaensiq sangnaklyp wsktysfgvn vtf
//
LOCUS       WP_118418392            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118418392
VERSION     WP_118418392.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116912
     Region          6..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msssrtlqit yvgmksqdvp iksgtikvmm ksdsevlqev vvtgmqkmdk rlftgatkql
       61 nadnvkldgl pdisrglegr aagvsvqnvs gtfgtapkir vrgatsiygs skplwvvdgv
      121 iledaidvgp ddlssgdaet lissaiagln sddiesfqil kdgsatsiyg aramagvivv
      181 ttkkgragvs kisytgeftt raipsykefn imnsqeqmgi ykemeqkgwl nsadlfrtrd
      241 tgvygrmyrl ideynnsngq rgllntaear naylreaemr ntdwfdvlft navsqnhsvs
      301 itagtekssf yaslsamldp gwykqskvkr ytanvnttyn iyknlslnli snasyrqqna
      361 pgtmnstldi asgkmsrgfd inpysyalnt srtldpsvdy isnyapfnil heldnnyiei
      421 nmvdvkfqge mkwkviqgle lsalgavryq tssqehnvld danqaiayrt gmddatireq
      481 nkllytdpdn pyalpitllp eggiyqrqdr rmlgldfrgt lswnhlfaek hitnffagme
      541 vnslqktyss fqgwgmqysm geipsyiyqf fkngiesgsr yyslghsetr siasffnaty
      601 sydgrytlng tfryegtnrm grsrssrwlp twnlsgawnv heesffkalq ptlsnltlka
      661 sysltadrgp aevtnsqaii rsfspyrpft diqetglyid dienseltye kkhelnigid
      721 lgllenrinf sadwyqrnny dligvvptqg vggvinkyan vatmkshgve ftlstrnirt
      781 kdfswntdfi fsyaknevtr lkgltsmmel vsgngfareg ypvrglfsip fagldedgip
      841 qylidgkvts tsinfqerek ldylkyegpt dptvtgsfgn vftykgfkln vfmtysfgnv
      901 vrlnpvfnyk ysdltampre fknrwtvsgd eartnipvil sdpqyrants lylaynayny
      961 steriakgdf irmkeislmy efprswiapa kisnlslklq atnlfliyad kklngqdpef
     1021 vntggvaspv prqftltlrl gl
//
LOCUS       WP_118418387            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118418387
VERSION     WP_118418387.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119105
     Region          25..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnkwllsl sigllccgsa yaqttvkgki tseggeplig atvavinstd gtvtdidgny
       61 slktkktltq kdllvfsyvg yktlqknyag ntmnvklaee sqqlndvvvt algikreekg
      121 lgyatetvkg dmitsalptn wstalngkva glsvissggp lnssrislrg dvslnqngnd
      181 alvvvdgvpm sspmtnpgva ygagsnsels vdygngfsdi npddiesiqv lkgasataly
      241 gtraangvim vttksgagap kgigvsysgn fsiddvmrwp dyqyefgqgl psnigpagsi
      301 yegqpyysyg kaedgsyast sgtssaygar fdanrlfyqy dpvtqgrasv atpwvayknn
      361 rkdlfqtgyt ltnsvaltgk sdrgsvrasi thtknewilp ntgfqritam vsaqqqisra
      421 lrinfkssyt yrklnntpal gynsnsisyf lifqnpnvnl dwlrpmwrtg qenvkqlqpy
      481 ssfignpyvi lyesenpsek hsnvssisan lrinskfdfm irsgiqlsad qreqhrpisd
      541 vvfgngffkk qnvfdyelns dalftyhdsf anglrvnasa ggnmmqqsyd mlaasvvgli
      601 tpgvyklang vsnpnvqtvi kkkalnslyf tanfsykdkl fldvtgrndw sstlpksnrs
      661 ffypsvsvsa vmnewftlpe qisllkvrgs laqvgndtdp yktspyygts dfpgsaivss
      721 tlynqdfkpe istnyetgfd frmfhnrigl dftfyynrtk nqildapmdp ttgyskatin
      781 sgcvrnrgye iqldvtpvvs rdfrwnatft wsknenrils laegadenql issigsvsii
      841 grvggttgdl wgyklvrdpe gnvvindngl persgeieyv gtaypkwkag lynefsyknf
      901 tlsvlldgqv ggkmyshshh kmteqgklqh tlngrlpgte fymskddpri aaaglspqdg
      961 mymiapgtvk nddgtyspnt kvvtvesyyk eyyrmanvet ntfdtsflkl remrleyklp
     1021 nstlkktpfs kasvalyarn lfcitdyplf dpesaalngs smvtgvetgs lptartfgln
     1081 invsf
//
LOCUS       WP_118418429            1116 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118418429
VERSION     WP_118418429.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1116
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126470
     Region          36..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          114..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnqaqkfi vlfllflfay swrveaqtgk ekqitmefkn eglpsifkrf ekvsgykvlf
       61 iydeissyts tgkvekatvd ealkviigkn plkyhidgqf initqkdskk ffsqvkgkvl
      121 seedglpvvg atiivedpsn irtitdnngn fqlsdvpkds rvrisyvgle tqflhpssym
      181 svvmksdtra ldevvvtgmf nrkkegftgs avtikgedlk kystnnvaka iaavapglri
      241 vdninmgsnp nglpdmrmrg sanmdmgtqs vdfnstsndv lavqgeyety anqpllimdg
      301 feisiqtlad mdpdrvasiv llkdaaatai ygsraangvi viesktpkpg riwvtyggel
      361 rieapdmtgy nlmnarekid aelksglyty ggetvekwql yqsklrevla gvntywldkp
      421 lqtafqqrht vtleggdeal ryrmyvgyns spgvmkdskr dvltgsldfq yrlkkvllkn
      481 sitldnsvan espwgsfsey trlnpylrpy gengeiqkrl dnfegvgges sylnpmyntt
      541 fnskdqsknf tvrelfrvey nptndlrfeg afnlsksvgh rdifrpaqht lfdnvtdptl
      601 rgdyrrsqse avswgidltg swnkqlkdhy ltanarmsvl ennsetygny vtgfpndnmd
      661 nllfgkkyne kvtgderttr sigwvaaggy sykykysfdf nirldgssqf gknnrwapfw
      721 stglrwdlkk enfmkdvsfi sdfilrgtyg ttgsqgfdpy qahgyytysn lllpyyssda
      781 tgseilamhn eslkwqttks tnlalelgfl dqrltarvey yrkitdnmvt svslapslgf
      841 ssypenlgki enkgweisls aipykntakq aywtitvngs rntdklleis eamkhrndln
      901 asnlkdtplp ryeegeslsr iwvvrslgid pasgdeillk rngemtsavn wsandvvpig
      961 nteptwqgyi nssftykgwg advsfryqfg gqvynqtlld kvenanlkyn vdrrvsqlrw
     1021 akpgdkaqfr tltpsgwetk atsrfimden ifqgsslsvy yrmdrtntkf ishwglssak
     1081 vtfnmedffy wstvkrergl yypysrqftf alnvaf
//
LOCUS       WP_118418488            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118418488
VERSION     WP_118418488.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115173
     Region          45..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkiryirl iglifvlivg ssltfaqnks krksakkplv evvsivtdek gsplknvsii
       61 cgegavvlyt dakgrfqtkv endatvmvea lgyedkvykl tgsnivpeki vlkkeplflt
      121 eeslvnradg gktykgnevg atsvlengqf gtfpdltltn mlqgkmlglq vrstvsglgn
      181 ntpdlfirgq hgmsentaiv iidgverpaa dlipeeieri ellkdataki lygaraangv
      241 lwvttrrgka nrriynatae agvvqmtrtp dflnsyqyan lynearandg ltpyynqkql
      301 egyknskgan dllypnvdly dqllnknany rkvsfdmtgg tdrvryalia gyvggsgfed
      361 vtytpqlhrl tlrgnldfnv tdfltisadv agrmemrkwg qldcgqvfta lsthrpneyp
      421 ltmspeetgl assdgiplfg asllrpmnay aetmyggytd erytrsqtni glkfdldmlt
      481 kglkagafls fdnydylqls lskvyptyai ktyrdfagee qimytqmkkt dvatsqsrks
      541 ttlqqtlgwn afagyentfn qkhdvsarlt ymyskttnqg vtqdiinany alrlnymydr
      601 ryaveadmal mgsnrfkpgn kyffstaggl awilsnedfl kdneyvnflk lktsagilgy
      661 drstehllye rawsqdgsfr fgttnngata yystfvragn pnlkwekaae wnigveglfl
      721 nnrlyteiny frekhtdiig svdasygdyt gnftyqdnmg svlnhgiegm ftwsdrindw
      781 sysvganfvw sknkvlkwnq vkhgeeyryt vgrstdammg lvaeglfgkd vainghapqt
      841 fadyqegdia ykdlngdkii dgrdvkelgn sfprttlgid fnvsykgwgl ylqgyselgv
      901 htwatnayyw nngegkyskl aldryhpann ptgsyprltt tagennfrns sfwlkntsff
      961 rmknvelsyt fnqfspssvv kkmkvfarga nlfvlssvkd ldpellnagv tnypvtrtft
     1021 ggvsfvf
//
LOCUS       WP_118418518             944 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118418518
VERSION     WP_118418518.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..944
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105497
     Region          41..943
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiyrrfil savlvfpvvi sagaqklagd nasslqndsl vqvafrkvsq nnllggasvv
       61 nveeltkkny ntwsltdmqg yvggyngnsl wgmdeklilv dgvprnidyi spteisqitf
      121 lkgaqavvly gsraakgvim ittkrgkstd lqvdvrantg fyvaksypey lgsaeymtly
      181 nearandglg alysaediyh ygsgenpyry anvnmyssdy ikkaynrsdv taeisggnhr
      241 ahfytninyl rsndvfkige akhngtngln irgnvdltln dfitayvnak vsfysrrsan
      301 gsyywsaast lrpnrispli plsyidanaa sawdlvansn nivdgkyfla gtqsdmtnvf
      361 gdyyasgysk atdrsfqfda gvnigldkvl kglsfhtrfs vdystayits ynnsyatyap
      421 twsnnggkdi ivgltkyned kksgvqnisg ssdnqtvlfs gqfdyentfn ddhhlaamli
      481 asgyqqsysg eyhktsnvnl gmqlgynfrn kyyadfggav ihsaklapgh rnafspsltl
      541 gwklsnesfl enspvvdelm lsvsgsilnt dlgidnyymy dgyynqsdga wwgwresvsl
      601 hstnskqgan edlsfikrke lsvnlktslw nrmitadasf fvnsiegkiv tsttqypeyf
      661 ftyyptasfr pyinydndrr mgfdfnvnyn krfgkvdfta gvtgtyyttk atkrdelyqd
      721 kyqyrkgyav dgiwglqcig ffkdeqdiid speqrlggti rpgdlkyvdq nndgiiddkd
      781 qvylarggwy gaplalginl takwkgltff vlgtgefggh amknnesyyw isgedkysav
      841 vrgrwtpeta atatyprltt esgtnnfyss dfwmyktdaf rlakvqvtyd lpskwfknsf
      901 vhgvsayisg sdlltisker kalelnvgss pqcrfynlgv tatf
//
LOCUS       WP_118418666             914 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118418666
VERSION     WP_118418666.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..914
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101298
     Region          38..913
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvqharlify slllllipce stlaqkipvt pidslitvgy atgslktlsg svekitetqm
       61 nkdqitnple airgrvpglt iqrgsngpaa ldavrlrgtt sltsgndpli ivdgvfgdls
      121 mltsiyptdi esftilkdas etaqygsrga sgvievttkk gmsgrtqvay ngsfgistvy
      181 knlkmlsgde yrrvasergi sildkgnntd fqkeieqtgl qqnhhiafyg gssessyrvs
      241 lgfmdrqgvi lnedmknfts nmnmnqkmfd gflncelgmf gsiqknhnlv dyqktfysaa
      301 tfnptypnhk dpvtnswdgi ttasqitnpl awmevqddda tshistharl tfnlleglkl
      361 nlfgaytyni vensqylpts vwangqaykg tkkresllgn mmltykknwk khffdvlala
      421 elqketytgy yttvsnfstd kfgynnlqag alrlwegtns yydqprlasf mgrfnytyad
      481 ryvltlnart dasskfganh kwgffpsasa awviseeefm kqlpmvdnlk frigyglagn
      541 qsgidsyttl nlvkpngvvp vgnsavvslg dlrntnpdlk wevkhtfntg idvalfgnrl
      601 llsanyynsr ttdmlylynv svppftyntl lanigsmrnw gteiaigitp lktkdmelni
      661 nanitfqrnk llslsgmyng emlsapeyks lsgldgagfh ggynhivyqm vgqplgvfyl
      721 phstglesdg nggytygiad lngggvsled gedryvagqa vpktilgsni sfrykrfdls
      781 lqvngafghk iyngtsltym nmnifpdynv mkkapkqnik dqtatdywle kgdyvnfdyv
      841 tlgwnvpiek vqklkkyvrs lrlaftvnnl atisgysgls pminsstvns tlgvddkrgy
      901 plartytlgl sinf
//
LOCUS       WP_118419063            1016 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118419063
VERSION     WP_118419063.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1016
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112442
     Region          30..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknkilila llvclsipvr aqntdnniig ivvdksgnpv ygasvnvegg avetrvetdk
       61 dgkfeiavek gqrlsvvsvd kgsttvvakt dgpmtivmgy aaqtidvgan rtfsrhesta
      121 avsttyneef nkrssrnisn slygyglglt tlqnaastgl madptfyvrg lqslssstpl
      181 vlvdglerdm slvspeeves vsilkdaaav alygykgvng ailittkrgk yktkeitfty
      241 dhiintqsrr pefvdaatya savneargye glgarytpee vdafrngvgs ggasrmypyl
      301 ypnvnwidet fkdrgvsnky tiefrgggak fryytmanll tdkgfiktpn andgystqnm
      361 ysranlrtnl didltattkl klnllgtlse sripgasvnl wdmiysipsa afpvrtedds
      421 wggsttwagt snpvaqsqga ayskghsrsl fadltlsqdl sgllkglgan frlaydnysn
      481 iledhsktyt yagyatswtt ngpfytaisg gessemgsga gidnwarqfn fagsvdynrs
      541 fqkwdvysql kwdyeyrdsy glnttiyrqn vswynhvgfs nryyldlalv gsassllapg
      601 hkwafsptis aawvlseekw lkdvswvnfl klrasfgvin vdylpkdgst tvydywdqiy
      661 tttgtqykfn ssydsefgst iigrlatans thekaykynv gvdavlfngl dvtaegyyqr
      721 rkdiwvsseg kytdvlgvda pfenagivds ygvelglnyt krlgdvvfnl ggnfawnkne
      781 ikeqleeprl yknlvqtgnr lgqvygmvae gffkdkedia nslpqnfstv vpgdikykdv
      841 ngdgiidand ktaigystta peiyysfhlg aewkgigvdv mfqgtgnysa vlntksmfwp
      901 linnttlsth yyenrwtpen qnakyprlss qsnannyqan tvwladrsfl klrnaevyyr
      961 fpeewmkktk ilgsaklyvr gtdlfcsdhi dvtdpecygv atplnksvvv gvtigf
//
LOCUS       WP_118419388            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118419388
VERSION     WP_118419388.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117887
     Region          25..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgkrihlfll alaigviqga aqvttvrgiv tteedgepvi gasvivkgts lgtvtdvngr
       61 felsglppsa trllisyisl makevaiapq vsvtlksdth lldevvvtal gisrekkalg
      121 ytaqevkqda lvqgkdnnll nslsgkiagv ritntqgdvg ssrivirget siagenqplf
      181 ivdgipvdns qlnarssgrd fknaiadlnp ediktltvlk gpnaaalyga raahgaivit
      241 tkggdkrqkg igitlhsstq vsfvatlpef qnlfgqgagg rfsyvdgkga gvndgvdesw
      301 gprldiglli pqfdspldad gnrvatpwvs hpnnvrdyfr mgistnngis vargddkyqf
      361 rvgynyekqv sivpdagtnk tnislntdyh lakwivvgat anyivytaps lpgsatpsgs
      421 nvrsnspmlq flwfgrqvdt nslkadytrn wnssyydnpf wsasyntqsq erhrligdlh
      481 aefrltdgln vrfrtstdwy ndrrkskvkw gsagagspyg syaedaytvk enntevlaty
      541 ikqlnknwgi dallgfnvrn kqyennyqaa prlavadlyt ltnsrdplts sndfyrlrqy
      601 glygsiqldy rrwaflnitg rndwsstlpv dnnsyfypsv tasvllseaf gwrskavnyl
      661 kirggwsqvg adanpyqlat vftsetafng nplqssstig mnpnlkpekt ssieagfeaa
      721 fwdnrlyldf tyyktdsrnq ilklattaas gytsqvrnag hirnrgyeiq lgavpiqtsk
      781 gfrwnldlny gansskvvkl ddeglitsyq lyssgiqila svseaygtlf gtsyvrdang
      841 nvvvdanglp kisttnktlg kftpdwtggi sntfsyrsls lsflidasvg gsifsntnkt
      901 gkytgvlant lsgrdaehgg lwyytdamgn nvrlpespsy svssdglyya qvngqstrvy
      961 qdgimvegvt esgskneevv saekyyhriy siaeanvyda syvklreval syrlprlwtq
     1021 klhlqeasvt ltgrnlwtiy ksvpnidpes alttgnaqgv eayslpttrs fgvnlsvkf
//
LOCUS       WP_118419393             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118419393
VERSION     WP_118419393.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110782
     Region          37..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknihfktct cllgillilf sgiqvkgasl evqqeskvsg tvtdekgepv igasvvvves
       61 kqgtitdidg kflvnvpkng hlkvsyigye tqevavknrq llkvilkees talnevvvvg
      121 ygtmkrkemt saishigakd lnqissldas mllqgkvssv svsntaladp nnqgsiqirg
      181 vssrnaglgp livvdgvpgg dmtninpadi esidvlkdga asaiygtrgs ngvilinlkk
      241 gtkdgqvhtt ystsvtfnka kkeldimnae eyrayrtvsn plsdmgadsd wfdavtqlgv
      301 thmhtltfsg gnartnyrvt adyrnargid lrsdrreyga raninhttkd glftfsanit
      361 prvidrnksa nvysnaiknn ptmpiydses angyyrfpsg tegsniveql neeengteik
      421 llewnataav nllplfnpkn pdmvlksqvt isqyqvdkfn gwftpstygs nvndgvtgka
      481 srdfdksttn nlewvtnfst riknhqiram vgysynygvn sgmsaenwnf ssdgltynnl
      541 gsgleaakdg ktmmgsyknd hklisffgrv nydwkerylf tfslrhegss rfgenhkwgn
      601 fpavsvgwri sdekfmkgls widdlkvryd ygvtgnqeig nynslatyra fgwyqyngnr
      661 fhvwgpsknt nselrwekgh nqnvgldfsl fshkvtgsfn yfhrkqsdll gdysvpvppn
      721 lfstiytnvg tlrntgfeld vtvnavrtkd ftysftlvga tnnnkfvsfs ndvykgqkyy
      781 stcsmanpnn pgylqrieeg erignyftyr yagvdkkgdw liydkkgnvi pvaqgteedk
      841 svtgnglpkf tgsmthnfty knfdlsvalr gaagfdifnv hdfyfglqsm ttnqlttays
      901 knahittgkn vitdyfiepg dylkidnvtl gytmnlnkky vekirlfgta nnlytftkft
      961 gvdpstyevn gltpgtfggg ynyypsafqf ilglqvsf
//
LOCUS       WP_118419608             940 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118419608
VERSION     WP_118419608.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..940
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104336
     Region          60..939
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 melkyinkyr niflgisllm lagypgkssg gnyvvlqdti apiigyniks saaavssisg
       61 dvmnthatdn lsnalgglla gvqaqqkgge pgsdgstlli rgfrtlsngv ntplvlidna
      121 pgdytfldpn eietvqilkd aaataiygqr gangvilvtt krgkegpltl kvnaqfglqh
      181 ltglpeflns aeyaqlynea rynegdkypf ysqediykya dqtgdniyth psvdyldqfl
      241 kslapiqrys lnfyggsqfv kynillgvmn qggfyeyavr dskystnass trynmrtnld
      301 initrklnlm fnisgqmvrn kspyggtsqi wstlmhelpn aypiftpsgn lggtstnfnn
      361 pvglmsrsgy revndrniqa mmeatqqldf itdglsvtas aayhgfntyg yqkrqeyavf
      421 svndfleetq ygldkplqdg tdlsndmdyt vsawgalnyn rkwgkhslqa vamayldkny
      481 ppkyspysnl nfglavdynw mgryflsgsl sysgnddfap gerfgtfyai aaawaldket
      541 ffrndvvdrl klrlsygltg nnrnscgery lyqtqyatgg gypfgnsfsn vagtverrag
      601 npyytwekar qfnvgmdmef mkkfsltfdy ftdrrfdilt spggrladif ggnlslsnig
      661 kvnswgiesv lgyndqfggv klnvelnasf stnkvienge vyglspnqrg igkpgygewg
      721 lkaigffyde ddiknsvpqg fgdykpgdik yadlnddgiv dgqdvtrlgg tgipnlftsa
      781 nfkieykgvd lgfqlvglfn rmvyvpfefh ngipeggkla kgayerwayy tdasgnlvdt
      841 rntakyprll ttkstnntqn stmtwrkadf iriknielgy tlpahlskki gmqslriyan
      901 aynpgllydr lkigdpeypg aciwsygkta iysigttisf
//
LOCUS       WP_118419469            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118419469
VERSION     WP_118419469.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115351
     Region          45..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkiryirl iglifvlivg ssltfaqnks krksakkplv evisivtdek gsplknvsii
       61 cgegavvlyt dakgrfqtkv endatvmvea lgyedkvykl tgsnivpeki vlkkeplflt
      121 eeslvnradg gktykgnevg atsvlenrqf gtfpdltltn mlqgkmlglq vrstvsglgn
      181 ntpdlfirgq hgmsentaiv iidgverpaa dlipeeieri ellkdataki lygaraangv
      241 lwvttrrgka nrriynatae agvvqmtrtp dflnsyqyan lynearandg ltpyynqkql
      301 egyknskgan dllypnvdly dqllnknany rkvsfdmtgg tdrvryalia gyvggsgfed
      361 vtytpqlhrl tlrgnldfnv tdfltisadv agrmemrkwg qldcgqvfta lsthrpneyp
      421 ltmspeetgl assdgiplfg asllrpmnay aetmyggytd erytrsqtni glkfdldmlt
      481 kglkagafls fdnydylqls lskvyptyai ktyrnfagee qimytqmkkt dvatsqsrks
      541 ttlqqtlgwn afaayentfn qkhdvsarlt ymyskttnqg vtqdiinany alrlnymydr
      601 ryaveadmal mgsnrfksgn kyffstaggl awilsnedfl kdneyvnflk lktsagilgy
      661 drstehllye rawsqdgsfr fgttnngata yystfvragn pnlkwekaae wnigveglfl
      721 nnrlytemny frekhtdiig svdasygdyt gnftyqdnmg svlnhgiegm ftwsdrindw
      781 aysvganfvw sknkvlkwnq vkhgeeyryt vgrstdammg lvaeglfgkd vvinghatqt
      841 fadyqegdia ykdlngdkii dgrdvkelgn sfprttlgid fnvsykgwgl ylqgyselgv
      901 htwatnayyw nngegkyskl aldryhpann ptgnyprltt tagennfrns sfwlkntsff
      961 rmknvelsyt fnqfspssvv kkmkvfarga nlfvlssvkd ldpellnagv tnypvtrtft
     1021 ggvsfvf
//
LOCUS       WP_118419730             936 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            xylanisolvens].
ACCESSION   WP_118419730
VERSION     WP_118419730.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides xylanisolvens
  ORGANISM  Bacteroides xylanisolvens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 936)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Bacteroides xylanisolvens"
                     /db_xref="taxon:371601"
     Protein         1..936
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103825
     Region          1..934
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgyasqaitl tnaqplkvtl gedtqvldev vvtalgikrs ekaltynvqq vkgdelttvk
       61 stnfmgalag kaagvqinss asgpgggvkv vmrgaksitq nnnalyvidg ipmynrassg
      121 gdgamatqps sesiadinpd diesmslltg psaaalygye gangvvlitt kkgradkttv
      181 tysnnttfsd pmmmpkfqnt ygnmtgemms wgletdkryd panffntgsn vsnalslstg
      241 ndksqsyisv attnatgimp nndydrynfs frnttnflnn kfildtsany iiqndknmvs
      301 qgqyfnplts lylfprgedf sdvavyeryd dlsgvntqyw pygdlggvss qnpywimnrm
      361 nrendrrryk laaslqynii eglnvqgrvs idnteskyte kfhagtvgnf agpkgrykee
      421 nrldrqvyad vlvnfnktfn efnvtanlga sikdlrmelt slhgdlnnvt nhftienltr
      481 sgyykvnadg lkrqtqsvfa naeigwrsfl ylsltgradw dsslalserg nkpffypsig
      541 lssilsevid lpewfsflka rfsftsvgna ydpyltkvry vyddqldqyk aeslypnsdl
      601 kpeitksyea glnmrffknt lnfdityyns dtrnqtfaap lpassgytav niqagsvqnq
      661 giemalgykn ewrdfgwssn ftftynknki krladgvtnr itgepiempy vdkarlggst
      721 spvvrltegg smgdlyinrd fkrdnngyiy ldaktglpsm veteykkigs llpkvnlgwr
      781 nsftykglrl nillsgrfgg lvvsntqafl drcgvseysa qlrqaggvti nnrnvsakdy
      841 lgivaagtge gdhyvyeatn irlqevsley tlpkkwlyni advtlglign nlgmiyckap
      901 fdpelvasst stfytgvdyf mqpslrnmgf sikvqf
//
LOCUS       WP_118420192            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118420192
VERSION     WP_118420192.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116971
     Region          43..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmekckyll fcgtlalwma gsfqqvyaat epssqaiqqq snkvtgkvsd atgpiigasv
       61 vekgtangti tdldgnfsln vkagatlvvs yvgykseevk agrgplnitl kedakaldev
      121 vvtalgikre rkalgygide vkgealtkak etnlinsmag rvpglvvsqt aggpsgstrv
      181 ilrgstemtg nnqplyvvdg vpldntnfgs agtnggfdlg dgissinadd venmsvlkgp
      241 aasalygsra shgvilittk rankdkisve yngtltfdtq lakwdevqqi ygmgsngtys
      301 ydaisntnks wgpkadgsnm lkyfdgverp flivpdntsn ffrtgitatn saiigvnsgk
      361 tgirftytdm rnkdivpqth msrdifnlra ntsagkvdld fsvnytredv knrpalgdsk
      421 snigknlmtl attydqewlq tyqtadgeys nwngmdpynv npywdiyknf nkskkdllrm
      481 ngkavwnidp hlklqatlga elnwftfddy kapttpgfea grlqnsafrn rmynfealal
      541 ynnhwgdfdf natlggnvyk vnnqttvtta qdmkirdvps ltsfneisvv pgsyrkqins
      601 vygavnvgwk hmlyldatlr gdqsstlptg nnmyvypsfs gsfvfseltk lgdllpygkv
      661 rmswaqvgsd tdpyqlglvy tkskyaypgy tigyidngti pnkdlkptkt nsvemglelk
      721 flknrigldf tyysqisknq imgmasswtt gynyrlinag kienkgieia lstrpiqtrd
      781 fswdinlnfs knsnkvkeld gesdmfelek aswldvqvaa kvgenfgsiv gpdfqrnekg
      841 dilidpqtgl pqydksnhvl gnaswdwtgg lltnftyknl slvavfdvkv gadlysmsar
      901 aayesgkspe tlagrdawyr seeerlaagi akgadnwkpt ggfvapgvid ngdgtyrpnd
      961 iyinpedywm svcrnapsmf iydnsyvkcr eltlsynvpk swlknvvsgl tvsfvarnpf
     1021 ivwknipnid pdsnynnttg mgleygslps rrsygfnvnv kf
//
LOCUS       WP_118420423            1126 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118420423
VERSION     WP_118420423.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1126)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1126)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1126)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1126
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1126
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123596
     Region          41..1125
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkrlksvsm llflmgastg aayavanpgv tdvkitqqsg tctgivkdat getvigasvv
       61 vkgttngtit gidgdfslsn vkkgdiiqis fvgyqtveip wdgqpmnvtl qddtqtlqev
      121 vvtalgmkra tkalgyavte iksdelnsnv vnpvsalqgk vagveisagd gglfgsskil
      181 irgastlgsn nqpiyvvdgv ildnatkngd adwsasdtdw gnelknlnpd dfesvsvlkg
      241 aaatalygsr glngavvitt kngkgkkglg vsfsqtfgid hvyggpdfqn qrgdgymsgy
      301 anykssgnmq dtnsfylngn gdrsvawggg vswgpkfdgq piefydyttv nyspyknnfv
      361 daydngfnsn tnvsvqgand tssfytslsy kyadgntpnn sferisflgk ashkiskdve
      421 ieaaisfans tprqggetnf gekfidgtfs rmydtrywrt rykgahggla dnayndeygn
      481 apgkevwwsv yeneyiqket svrpslklta dlnswlkfta egnynyyykr neskelgsgy
      541 aneggyyklg qytkeqtnln asfswnkevk dfnisgfirg eyyhnfqqel qlntngglvi
      601 pgqffignsk npvgtsgnis gektilslag qvamswkdqv fldvtgrndw ssslvyadkh
      661 gnysyfypsv saswlihetf rgkmpewisf akirgswaqv gndtdaykin tayslygidn
      721 syglqvpdty yaanlkperk naweigldwr flrnrigvdf tyykentkdq imtikvpses
      781 glsnqlinag niqnqgiela inttpietkd wtwdlnftyt kntskivelh envanyitlv
      841 gdaaygnyri asvaevggey gllksdatpn ydpktglpil elasynsrhs vyytrsgkve
      901 tvgsiqpdfl gsvnsslryk nwtlrasmdm rfggmvaiyg shygtaygyl kssmngvdae
      961 nggitytsiw dgltyddgii peaimpggqt intpsgtyti aeggelyadl vnrgivdpqh
     1021 asswnywnns weraavwknn dwfhelnyia lrevslsyrm pgkiadkiga sginltltgr
     1081 nlgyllnslp nnfnpeslrg tqagqfmirs vspytasytf tinatf
//
LOCUS       WP_118420510             810 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118420510
VERSION     WP_118420510.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..>810
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          58..>796
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkdthsri tdkcrclfvv aysamsitgl ssvlavenha lsspvsdrve svqqkkhvsg
       61 nvqdangmpl igasviikgt ntgmitdieg nfaldakqgd iivisyigmk saevkvpang
      121 qirvmlkeds qlmdevvvtg ygdfkkatyt gsasvlntdk leslpvvsva qmmeanipgl
      181 ssvasssqpg skatvrvrgi asmnastepl yvldgvpvas rdmsglsana sagglgliet
      241 lnpadiesit vlkdaasasl ygakgsngvi littkkgkeg kmrvsmqaty gitdiaynyr
      301 pimggeerre liyegfvnyr lnqgdseaea kayadgqidn yaarpangya dwedallkkg
      361 hqqdyslsvs ggneksnfig tlgytnqtgi sinsgmerft gridanskwn kfeygmnatf
      421 swtrnkhtpe gqyyasalys skyqltpsip iynedgsyht gfqnngginp lyensvdsny
      481 arlartmasa kaayhildgl klstiftvdy slnkdfffys pdgkdgeatq gsgqmmmier
      541 msytsqtnla ynktfgkhni navlayevmk ydyedmygek qvygqtlnps ldngakpadl
      601 tntrqedamv syvgslnygy ndkyyagfsf rrdgssrlap dtrwgnfwav saswrlsqen
      661 fmkpwedvvs dmklrasygv ngnlptgyyg yhgtyttgaf yngkpapwed aianpdltwe
      721 knyalnlgvd lslfrrvnlt fdwytrttkd llmskqlnsi sgfgsiltnv gemkntgfei
      781 evrssniqtk dfswttlyla nlhtsflcnl
//
LOCUS       WP_118420422            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Phocaeicola].
ACCESSION   WP_118420422
VERSION     WP_118420422.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114763
     Region          43..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkrlksvsm llflmgastg aayavanpgv advkitqqng actgvvvdat getiigasvv
       61 vkgttngtit gldgdfslsn vkkgdiiqis fvgyqtveip wdgqpmnvtl qddtqtlgev
      121 vvtalgikre kkalgyamqe vkgdallear etnlanaltg kvsgvqiirs sngpggsski
      181 qlrgansvtg lnqplivvdg vpmdnftgas nndidnptld mgnglsdina ediesmsvlk
      241 gasaaalygs ragngvilit tkkgtkregl gitisgsvsa ettfmlpkrq kafgqgengv
      301 fdstngyswg pevtgqsytk wdgttanmqi fdnvknffdt gvnlsesisf qqqydktsiy
      361 tslnrmddss mipganlsrt nltlrasstf gkddrwsida kvqyintlae nrpisgargn
      421 nafytifnmp ttidirdfss pvkdefgemi wwskgginpy wskdynpnkd srnrflmngs
      481 lkykftdwld aeikagsdmy ftegeeklya gsptnnknsr ystsekkffe nnfsflisgh
      541 kdelfgkfgg nfsfggnlme rkstgldnam gkltapdlfs langdkkdls itetyihkki
      601 nslygtlgin yngwafldat frndwssaln kenrsffyps vslswvisdm vgkvgkgmpe
      661 wftyakaras faqvgndmda yqlyntysig sdpngnttag qgktkydadv rselitswea
      721 gaelkffnnr lgvdfawykt nakrqlmnip lnnlsgydnm kvnagniqnt gieimlnarp
      781 ietaqfswdt qlnfsqnksk iiellpgkpg mqyalggsda lqvyavagga ygeiwgtkyq
      841 rveegefkgq lllnesglpq atsdkhkige qqpdfllgwt ntfnyknftl sflidgrfgg
      901 difsftnmnl qrsgiaecta pggkredivv agvikdgngy kvndqsvsle ryykalatgr
      961 agiseayiyd atnirlrnia lsyrfpssml kktpfqqvkl gftvnnvwmi sshldgidpe
     1021 svyatstnat glenssapts rsylfnvtlg f
//
LOCUS       WP_118420515            1013 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118420515
VERSION     WP_118420515.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1013)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1013
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112020
     Region          26..1012
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrriftfflt fllgvfvtal yaqthtvsgt vidkdanepl iganvlikgt tigtvtdldg
       61 kytlqagdkd ilvfsylsmk tieepvngrt vinvkmasdt etlgevvvta mgikrqsetl
      121 tysaqtvggk dvndiksvnm inslqgksag mmitpnstga ggsskilfrg nksisgnnqp
      181 lvvvdgvpvm mnitnsqvds nyggqrdggd amstinpddi aqitllkgas aaalygavaa
      241 ngaimittks aqsgkvsvnv ssnttmespm vlpefqttyg msdngtfswg eklsskapny
      301 akkffrtgft tnnsislsgg neniqsyfsy anvysqgitp qndyrshnln skvgfnilkd
      361 ihidftakft nqhitnqaaa gylwnpltgv ylfprgedwn gykenfevyd pargcyvqnw
      421 tntqqqqfgn pywmlnrqtp itdrnryefg gsikwnitpd lniqgrmrye rgeehwvhna
      481 yassvgnlyp mgrmkdnryf sdqlygdvlv synhtfndfs lsatagssft ktktshvdlw
      541 gegsqfsqpg sgnifypnif tpnnyygnms tvgkddnwmt qkrqnsvfat aqlgyregif
      601 ldisarndws salaftescs ffypsfggsv llnkfvdmgk nidlfkfras ysivgndvpv
      661 fmsnllyslg sqgaitppdk apfrtlkpek thsleigfdg tflqnrlnin ltyyktntkn
      721 qffsvaapye sglrnryvna gnvenkgfef nigwyeqftd nfswstnlnf syndnkikel
      781 vddlpngltl tdfggakvil kegghygdly vrhlmrdeng kplqnekgep ivsgdsmdel
      841 eyagnmnakv nmgwtntfry kdfslsflid akfggkvism teaaldgwgv skrsgearda
      901 ggitvdgvkf dadkyyrttg nnnfnspyav enyvydatni rlrevtfgyt frnllgagkn
      961 ltaaiigrnl fffhkdapmd pdvsagtgng iqgvdmfalp tsrsfglnlk lnf
//
LOCUS       WP_118421294             925 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118421294
VERSION     WP_118421294.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..925
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102928
     Region          2..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkinifla gvlcslgvma qedtltvrqn nevvemgrti tmdaremtga vsvttnlshk
       61 nsikpsnqlf gtlpglqvlq nagtvwenga tlyirgnssl nsnsplvlvd gfersidels
      121 seeiesvsvl kdavatslyg irgangvilv ktkrgsvgap kitfsyefnm aspkrlpkfa
      181 dgytyamaln eamendglap rysnteldaf knqtypgvyp nvdwldeslr dmsygdnvnf
      241 taqggsqfvr yytmlnfldn rgllkptsdn dgystqlkys rlnvrtnldi tvsptttvql
      301 nllgnftehn rpgestgnif nalfqvpsga fpvktdrgiw ggttnysnnp valisgrgya
      361 rsqtramyad vnmkqdlsai lpgwsagfkv gidntasywd nntkefgyes asvdfatgen
      421 iyttlrnegt lgfsksvgsv athfnlefyt nyikqwnkhs lnatllysmd kaktksqnsg
      481 rafmdivgsa hytynnrylv dfslsgsass ildpddrwgi fpaigagwil seenfmkrdw
      541 lnllkvrasy gisgradygv nlfqniygsg nsyyfqnatn vpssssgmkf tqlgidglty
      601 ekshklnvgi dfrawnkltm tldafydhrt dilvssggsv sqifgmsvpq inngvvdnkg
      661 ieaslawddn ignfkyhlgg qftftrnkik nqneeyrpyd ylkrtgssmn qifgyevigi
      721 yksqdeidnr gveqllgdvr pgdlmfkdqn gdnkidaydq vplgynatcp eiyysfdlgl
      781 eykgfgvyal fqgvgnyskv lntasvyrpi vnnntistyy wenrwsesnp ngtlprltys
      841 gsdnnyntns mwvsdasflk lrtlelyynf ptkllkktgf lagvkvfarg hdlfcldgid
      901 lrdpesigte hptmtqyafg fnlsf
//
LOCUS       WP_118421263             925 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118421263
VERSION     WP_118421263.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..925
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102507
     Region          46..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mninrmlmla ttvvsltana qvklsdknan aydlgygvei snflstasat titgeelqqt
       61 satnlaqaly grlpgltals qggfsgdenk gasfnirgyh tlndksilil vdgyerpidr
      121 lsveevesvt ilkdaaatal lghegingai lvktkrgveg kthvkvnysh kfqfdpefad
      181 mvdgygyana fnrarhndgl saayteqeln lfkdgsdpyf ypnvnwrdlt fknsaeedha
      241 yvsvyggtnk vkyythidyt dvrgafkdtk qpdyntqlrq skaniranld fnitnttlms
      301 vnlfgmfqet krpsdigadd ataaiynlpa safpyktstg iwggneaygd anpiakiqes
      361 gfykthqrql wvdaklsqkl dfllnglnvf vsagyanssi yaenshkahq ygyerytgti
      421 gdknnvalnt fgnketnltf nnwnagqwwk akasvginyk rsffdndhfn atvvydnsgv
      481 stdgrgntfy rqnimgvfhy dfqnryvadl vlagngasrt ypskwafspt lslswiyadn
      541 nddllnygkl rasagiqhtd ymptygmwlp twdvshgyvi ignnydakwg aslgsfpttd
      601 fsqetstsfn lgtdlrlana ldisvdafyq lrshimlsas senssvagiq ssyndvgevk
      661 sygfevsaky vkkitsdlnl nlganlswar nevskyigip typlsdpvgh rvneawglks
      721 agffkdqadi nssyrqeyst vspgdikyqd lngdqiinef dvtslngatd ipelnyafnv
      781 gveykgfgln awfqgtgnym kylpsaiwgg madngnlsvd yynncwdvag snalyprltt
      841 lnnsnnsqks nvwykpvhfl kmrnievyyk vpatvlskls ltaakvfiqg enllsfdnid
      901 amdaevlsta ypmfkgvnig vtltf
//
LOCUS       WP_118421497            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118421497
VERSION     WP_118421497.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123238
     Region          53..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknsfrfkr nrkaiaalli cvgfvgihpl avfaeddvnv vqtvqqqkqt itgivkdatg
       61 epvigasvke kgdpsngvit didgnfrlsv panatieisf igyqtasvka isgkplnivl
      121 qentemldev vvvgygtmrk kdltgsviqi rpdnlaneap ktvqdvlrgt pglnvgmdas
      181 akgggslqir gqrslytdgg hndpliildg mmfygelsel npddiaqidv lkdasaaavy
      241 gakaangvii vstkkgkngk pminfstnws fstmganrdv ydgegylkyr rdwyvagtyg
      301 vnpetgayee yqadkkkypa gyydaptqen lnkygitldq wraytnagsd isdqevwgat
      361 rlglqgnsla nfllgqtfdw ydhsfrtgln qnynvsmsga tdrvnyyfsl gymdnegvav
      421 gndyttfrsn mkvnakvtnw fevganvnfq ertdgdttvd wgkqitensp fasyrnenge
      481 lerfpmgnvs gntgynydyr qqfkeresgy tvlntilnak ltlpfgitya fniapryqwy
      541 yyrsfqsskd pdvtagsasr nngkrfdwsl nntltwdktf lekhhftvtl vqeaeerrsw
      601 gdnlsannlq ptdalgfhyv kagdkessaf ssddghetad gmlarlfysy ddrymftgsi
      661 rrdgysafgt snpratfyst afgwtftnek ffnwepmsfg klrfswgqng nrslanpyia
      721 ladlgsgtgg tygyvdasgn tteyryftmn rlanthlqwe kttawnigld fgflnnrisg
      781 sfeyyhmptt qmimnqslpg fsgfgsvttn lgevqnrgve islsttnikn dvlewnttig
      841 fsfnkneikh lyyeyenvln aqgevigtke rddisnkwfi gqpigaiwdy kvtgiwqkde
      901 veeaakygqr pgdpkvwnnp dndkvnadgs vtivydnddk qflgqsspkv nwsmrneftf
      961 fkdltfsfni yskmghksle tdylnkdnag skvtngqnvy akkgywtvdn ptneygrlda
     1021 qgpsgvttpg klhnrsfirl dnislayklp kkfisrwsie kaiisgsikn vavwakdwky
     1081 wdpetgglap rtfnigltlt l
//
LOCUS       WP_118421675             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118421675
VERSION     WP_118421675.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110669
     Region          7..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvisaqktlt gcvvgedgvp lagatvleig tsngtvtdme gkfkltvadd vmlrfsfmgy
       61 ktqeisvggk tflnitmved aveldkivvt algiekkehs lsyamsqikn eeltrvkmpn
      121 litsltgkaa gvqinqvssg lgasakvsir girsvagenq plyvidgvpm lnssseqafs
      181 aiggtanagn rdggdgisnl nsediesisi lkgapaaaly gsqagngvil ittkkgksqg
      241 qrsisfstsl mfdkavslpe mqnrygvsev idswgerqnl pkndnlkdff stgmasitsv
      301 slshgneklq nyfsyanttg kgiidknrls khnltfrets tlfndrlkld gsvnlmrqvt
      361 knkptvggfy mnplvglyrf prgedltyyk dnfeiydesr nlniqnwhts yddfeqnpyw
      421 ivnriqskev rlhaivslsa sfkvndwltv qtrgnvdcin dklrqkfyas tapalagtng
      481 ryiemdyqdi qfygdlmlmm kkqwgdfsvn galgtsindk ttnstrydsk taslyyanvf
      541 nlaniimngs aaldqkidar rqlqslfata qvgykesayi dlsarndwas tlshtkhekr
      601 gylypsigts lilsrlftlp ewvsyakvrg aysmvgndip pfmtyplshi taggeyland
      661 aapfkemepe mnysweagae arflnsrigf nltfyktntr nqffklptla gdkyayryvn
      721 agnilncgwe ialdatpvlt kdfmwsttln fatnknkiva lheelkefvy gptsfsssya
      781 mklvkggsig diygkafvrd asgdivyete gsnaglpkie gdgntvkvgn sspkfqmgwn
      841 htlsykdisl yflvdcrygg kvlsqtqadm dlygvsevta qardegyvml eghridnvkg
      901 fykivggrag tteyymydat nirlrelsls yqlpaswmek skvlkkvqls fiarnlfffy
      961 kkapfdpdlv lstgndnqgi dvygmpttrs wgfslkcef
//
LOCUS       WP_118421310            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118421310
VERSION     WP_118421310.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116156
     Region          41..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnyhlslv llvlfgissp ylakaadren tpssqstqqa kkitgkvvda tgepiigasv
       61 lvkgtgtgtv tnvdggfsvd aqlgstlvis fvgytsaeik vgagnvytvt lkedaqtlne
      121 vvvtamgikk ekkalgyavs dinseellkn kntnvinsla gkvpgvnitq ssgaagagas
      181 iiirggnsts egrenqplfv vdgiiydnst qvvgnsgtdg mtrsnttysn rvmdinpedi
      241 etmsilkgaa aaalygsraa dgaiiittkk gaegsvkvdf ssklssswat klpevqtefg
      301 rgyysnngvl ddltylswge riasgtqlyd nigdffqnga vwdnnvsisg gtknssffls
      361 asnydqtgiv pktgynkttv rfngeqkygr ltvganvsys iadtdktlts aglydgggng
      421 tmtalyswpq tedmskylne dgskyrlfdg rldlasdken pywiinknkl sdntkrftga
      481 anasfkiadw wdvsarvgyd qytteaytyi apgsvakemy qngrlnksdy tynyistnvm
      541 snfhktfgdf dlnllvgttt esterhnqth wgydfitagt isfnnisken qffkdatskk
      601 rlvgvygefr asykniaylt vtgrndwsst lpidnrsyfy psvsgsfvft elfskndilt
      661 fgkvraswaq vgkdanayat ltyletpity gsftgvgnqy vlgnaylkpe iqtawevgte
      721 lrflggrlgl dytyyhsqtk nqiasprlsn angsimssin sgsvinngme iaitgkpivt
      781 kdfewnitln tsynrgklgd fldgvsmfyp tdaqfgtvka asvpnggkfl alvgsrfaye
      841 ttgednqeii ggryqvdttt glykihssts evvgnrepkf igglnntfhi kdltlsflld
      901 friggdvyng teyymvsngl skrtlengre yvtvtgvdsk tgadinqtyy adqsydingv
      961 tysgkamikk ywdnycsnsy nfitsvnwlk lrslsvsydf tklikrqnvi krlsvtatgt
     1021 nlftwtnykg mdpevstagg tggsgatgid ycsvpstssf sfgvnltf
//
LOCUS       WP_118421528            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118421528
VERSION     WP_118421528.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116479
     Region          6..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhssaktlqi syigmkteev gikshlkitm ktdseilqev vvtgmqrmdk rlftgaatkl
       61 sadnvkmdgm aeisralegr aagvsvqnvs gtfgtapkir vrgatsiygs skplwvvdgv
      121 imedvtevga ddlssgdavt lissaiagln addiesfqil kdgsatsiyg aramagvivv
      181 ttkkgkagsn kisytgeftm rmkpsyrnfn imdsqeqmdv yktmasngyl nfsdvyrasd
      241 sgvygkmyhl indysngkfg lantpeaing ylqqaeyrnt dwfdilfnns isqnhaisms
      301 sgtekasyyt slsamsdpgw tkqssvqryt aninalynis qqvslnligs tsyrkqkapg
      361 tlsssidvvs gevrrdfdin pysyalntsr aldpneyyvr nyapfnilhe ldnnnmdlnv
      421 vdlkfqgelk wkpfkkvels algaykhsst tqshsitdys nqawayramd datmrdanpw
      481 lytdpdvans lplsvlpvgg fyretkygmn sydfrgtisy ndvfaedhvi nlfggmqlta
      541 tdrsktwfng vgmqydmgml psyeylffkq gkeensqyyt veetrsreva ffatgtysyk
      601 grytvngtvr yegsnklgks rssrwlptwn vsgawnmhee affedltptl snltlrasys
      661 ltadrgpanv tnsrvviqsy npyrpfasvs esgleiydle nseltyekkh einlgadigf
      721 innrinlvfd wyrrnnydli giintmgvgg qiakyanvas mrshgveftl strniatkdf
      781 kwntdfiish akntvtelys nsrvidmisg sgfaqqgypv rslfsmdfkg lnedgvptfi
      841 nekgvlttsd infqernnkd hlvyegptdp titgsfgnvf sykgfklnaf itysfgnvvr
      901 ldpifsnkys dldampkefk nrwtvtgden rtnvpviadr rmnqqdqyls raynaynyst
      961 ariakgdfir mkeislsydf pkswishlkl sdlslklqat nlfliysddk lngqdpeffn
     1021 tggvaapvpk qftltlrmgi
//
LOCUS       WP_118421734            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118421734
VERSION     WP_118421734.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121058
     Region          26..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkllfiml aylflwtsat laqvskvtgv viseegnepv vgasilvkgf sqgvitnvng
       61 eftltnvpnd artliisfvg mktqevaikp qlriimsnds qmldevivtv aygtakkssl
      121 tgaissvnqd qiemrptssv tsalegttsg vqinstygap gsdpsirirg igtvngsstp
      181 lyvvdgvpfg gnisdinpad iesisvlkda asaalygnra sngvilistr kgtsnkisfd
      241 lkinqgvysr gikeykrtsp nqfmeaswqn lknarmsagd daataakyas enliseqlyl
      301 niynkadnal fdangnlvsd aqilpgyadd ldwysdairn gyrqeysfsg ntaneksnyy
      361 fsigyldekg yvtnsdfnri sartsmsftp kkwfkaginl sgthqnshat ngdsdagytn
      421 afmycrqiap iypvhlhnad gsyrldalnn kqydpgyykd degvtistrn qyvdrhviwe
      481 nelstdktir ntlqaiafad vkflndftft vkgdlnvrns eqtsydnati gdgkgnngrt
      541 krvtyrykny tfqqqlnwnh vygkhyidvl aahenysnny dyeyafktte tfagkpnlsn
      601 ftditsltgy etdyrtesyl grirynyaek ynlevsfrrd gssrfskqnr wgnfgsigan
      661 wiiseedfmq sltwinslkf ranygqvgnd agtgyygymg lyagsqnani gayylsqnea
      721 ldlkwetgea ygialegrlf nrwnisleyf dkrnkdllfd vylplsagat sttsaqatia
      781 knlgtisnkg feintdidiy rdkkwkvnfa tnatfvknki vklpeqnkdg iisgnykive
      841 gksryefflp tyvgvdqltg nslytlnled yfitlpdgsk lgnaegtdis dnesltsing
      901 tyytnnttya lkefhgsalp kvygsftgtv syksltfsal ftyslggqty dgvyrslmtt
      961 gtspgnfhsd imnawkavpe gmsensadri widgipqins tmsannnsas srwlvssdyl
     1021 vvknltlsyr lpasfvkrld lqgisvsanc enlwtftarq gmnpqqsfgg sqynylvtpr
     1081 vfsvginikl
//
LOCUS       WP_118422529            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118422529
VERSION     WP_118422529.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122382
     Region          23..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfrkilflff cvfalaahsq nvvikgsvtd vnkepllgvn ikvkgtttgt itdidgnfsi
       61 ngpkgatlvi syigmvtqev eykgqplnvv lkddaqalee vvvvgygsmr kkdltgsvvq
      121 vrpdkiandn pktvqdvlrg tpgltvgyge gdagakgggs mkirgqrsvy tdgghndpll
      181 ildgmffyge lseinpddia qidvlkdasa aavygaraan gviiistkkg kqgkptinft
      241 asvgltqkaa yrdrwqspea ylqhyvdwke kntygvnaet geyaaysrpg neytskpgyf
      301 rnpnnlgdvs leawrgyttn degesdlsiw arrlgfrpnt almdnllsgk vmdwqdkafr
      361 lgfnqdynas isgagekidy ymslgylrne gafvddtyra irgnfklnak vtdwfeigan
      421 infqdrsdge igmnkggfme nspyavfkdd egnyvqdplm fqydrnnltn wyyekqflel
      481 qkgyttfnti fnaklklpfg itytfnaapr lqyfhdryfm saerpnskpt drgvnreqak
      541 rfdwslnnti twdhtfadkh hviltlaqea eerqywsdri earnilpsdv lgfhntqngd
      601 ksassfrsdd shqtadglmg rvfysyddry matftmrrdg ysafgssnpy ayfpsgglaw
      661 tfsneeffqp ythimstgkl rvsfgkngnr slanpyeala nlypgggkmq gyitssgdly
      721 lmrylmaqrm enpglqwekt qswnfaldfg flndritgtl eyyrmstkdm imgqrlpnft
      781 gfesittnlg qvdnngfeia lntlnidnkn fqwnttfsls ynknrikhly gdyedildas
      841 gnvigqkead yvgngwfidr pisaiwdykv tgiwqkdevd eakkygqvpg dpkvwnnpan
      901 deydadgnlk kviynnddkv fqgqtaapvt walrndftlw kdltlsiniy srmghksleg
      961 mylnndddgg gmtyrlvnke akeywtvdnp snkyarieaq gpegargarr lynrsfvrle
     1021 nisigytlpr qwtkrvdier akvyatvrna avwgskdwey ygdpetgnya sriwtlglnl
     1081 tf
//
LOCUS       WP_118422835             938 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118422835
VERSION     WP_118422835.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..938
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106041
     Region          23..913
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrkfiyigc tvfamslfha gsiqaqeenk dslvnvafgt vaqkdlthai stvntseltk
       61 kvnsssslvg lesliggytg siwgqealil vdgvprsasn vrasevenis vmkdaaavvl
      121 ygsraakgvi littkrgkne pmhidvrgna ginvpksypk yldsdcymtl yneacrndgl
      181 sekyntsdiy ntamganpyr ypnidfyssd ylrkayynad mtgevyggne rthyylnfgm
      241 dysndllkyg esknaynmrf nvrgnvdmtl aswlkattna aivytnqyag rgnfwgvast
      301 lrpnwfapll pidmmdtnvs qiqeyiansn hlidgkyllg gtssdmtnpf adllaagyvk
      361 ekarmfmfdv slaadlgsll kgltfktsys vdytsyysea fketyavyep twaqvngkdm
      421 ivalkkhned kkdpneyigk stydqtmtfs aqfdyartfe kfhnvaatfm gwgyqtqksa
      481 denhessdyh rtsnvnlglr asynynhkyy idfngavihs aklpegkrna fspavtlgwr
      541 iskekfmenv dfindlkvta syaklhqdld isnyylykgt fskegyyvqw hdgtaggwtp
      601 vskrgdnpnl dfitrkefra gidatlfnrl lrlnanyfkq dtkglltqga sfihpayfal
      661 gsnssfmpwi nynedrrsgf dfslsankkf gdfnvtlgfn gmvyssealr rdelydedyq
      721 frkgraldas ygyvcegffq dqtdidnhar qtfgtvkpgd lkykdinedg vidnkdqiel
      781 gkngwaappf sfglnltvkw knfslfamgs gqtgaidyks ssyywnrgts kfseivwgrw
      841 teetkdvaty prltttngdn nyrnstfwty krnyfrlnqa qltydfpent fkgtfirgls
      901 vycggnnllt iskerkhlel stgspqcrnf yagfkaaf
//
LOCUS       WP_118422176            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118422176
VERSION     WP_118422176.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121806
     Region          24..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrlsvvfl lligtltyal aaerqvegvv issednlpli gasvyvtadd lkkngnnqst
       61 igvitdidgk fsisipdgit rfycsyvgyd vveiklipgk kqyditlqps ahmldavvvt
      121 gyqtverrkl taavskidis dqmmgatksi dqalagqiag lsvsnisgtp gapakirirg
      181 tsslngtqdp lwvldgiple gtnipnmevl kdidnigqta iaglnpadid nitvlkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs skltyspkln idrlnllnse ekvgleldll
      301 esgypyretk gevyriisgl gelknfkdgg wnalssnaqg ainrlkatnt dwsdilfrda
      361 ftqeynlsls ggsekatyyt sfgymkengn ipnvsaerln lvmktsykvn silkvgasmf
      421 anrrknstyl pddrgltnpi yysrlanpyf tpydangnyn ydvdveddtd mdfglnlfee
      481 rkntsnqtti nglssifdae lrfddrfkit tqlglqldkt siekiaeees yvmrtekknh
      541 rnngvtylpe ggfhkanens lsqltwkamg eyrdtyndih efevmvgtei rktweeklys
      601 agygfdrktl ttkpiifpee sqafklheka hvenayvsaf stlsysllnr ytlggsirfd
      661 gsdlfgvdkk yrylplysvs glwrisqepf manakwidnl vvrasyglqg nidkntspyl
      721 lgnyrienil pggsedmidv sgapnkklrw ekthsinagf dfavlnqain lsvdyyyrkg
      781 vdligtqmlp letgfemltv nwasmqnqgv evalstrnih tknfmwttnf nfaynnnkil
      841 kealredale pgregypvga lfalktagld eegypmfegk dgkavsamef fklqewgfga
      901 tdltarerre lytyvgtadc pytggfnntf tykafelgvn fsfdfggkvr sqptysivdf
      961 dkgrntnrdi lnrwtpente tifpvllsqn erldeymwys nqneiyrnld iwirdlnyvr
     1021 lqnirlgytl ptnfsrklgm tsatiaiegr nllvfgssyk nyldpetmsn ayatpapksv
     1081 tlslnlnf
//
LOCUS       WP_118423191             925 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118423191
VERSION     WP_118423191.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..925
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102465
     Region          46..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mninrmlmla tavvsltana qvklddknan aydlgygvei snflstasat titgeelqqt
       61 satnlaqaly grlpgltals qggfsgdenk gasfnirgyh tlsdksilil vdgyerpidr
      121 lsveevesvt ilkdaaatal lghegingai lvktkrgveg kthvkvnysh kfqfdpefad
      181 mvdgygyana fnrarhndgl saayteqeln lfkdgsdpyf ypnvnwrdlt fkntaeedha
      241 yvsvyggtnk vkyythidyt dvrgafkdtk lpdyntqlrq skanirtnld fnitnttlms
      301 vnlfgmfqet krpsdigadd ataaiyqlpa safpyktstg iwggneaygd anpiakiqes
      361 gfykthqrql wvdaklsqkl dfllnglnvf vsagyanssi yaenshkahq ygyerytgti
      421 gdknnvalnp fgnketnltf stwnagqwwk akasvginyk rsffdndhfn atvvydnsgv
      481 stdgrgntfy rqnimgvfhy dfqnryvadl vlagngscrt ypskwafspt lslswiyadn
      541 ndallnygkl rasagiqhtd ymptygmwlp twdvshgyvi ignnygatwg aslgsfpttn
      601 fsqetstsfn lgtdlrlana ldisvdafyq lrshimlsas nenssvvgiq ssyndvgevk
      661 sygfevsaky vkkitsdlnl nlganlswar nevskyigtp typlsdpvgh rvneawglks
      721 agffkdqtdi nssyrqeyst vspgdikyqd lngdqvinef dvtslngatd ipelnyafnv
      781 gveykgfgln awfqgtgnym kylpsaiwgg madngnlsvd yynncwdvag nnalyprltt
      841 lnnsnnsqks nvwykpvhfl kmrnievyyk vpatvlskls ltaakvfiqg enllsfdnid
      901 amdaevlsta ypmfkgvnig vtltf
//
LOCUS       WP_118423284            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118423284
VERSION     WP_118423284.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122496
     Region          29..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 migvtlllgn plfahaetne vqvamqqati kgtvvdtnge pvigatiqvk gttngiisdi
       61 dgnftlmgvs sqatlvisfv gyktqeiqln gkttvkvvlk edsemleevv vvgygsmrkk
      121 dltgsviqir pdklaaeapk tvqdvlrgtp glnvgmdtsa kgggslqirg qrsvytdggh
      181 ndpliildgm qfygelsein pedigqidvl kdasaaavyg akaangviii ttkkgktgkp
      241 vinvntnwsf ntmganrkvy daqgylnyrr dwyvaqnayg idpdtgnyie ygatwvpkkg
      301 gkpdegtwey ktpvgyydsp tqatfdkygi sledwfggtv pdgtdlnnvw gtrllmqgnn
      361 lanmvsgksf dwydhsfrtg inqnynvsls gatdranyyl sfgymnnegi vkgndyttfr
      421 snmkinanvt kwlevganvn fqertdgdtt vdwasqitrn spfaqyrdee gnlerfpmgn
      481 iageagfnhd wrqqwetkea gytvlntift tklhlpfgfq yafniapryq wyysrtahss
      541 edpsvetgsa trsngkrfdw slnntitwdk ifadvhhftv tlvqeaeerr kwsdkinank
      601 llptdalgfh yigiadkeas sfssddahet adgmlarlfy syddrymftg svrrdgysaf
      661 gtsnpratff stafgwtftn ekffnwkpms fgklrfswge ngnrqladan ialanlgfga
      721 gktygyinss gnlveykyma msrlansklk wekttawnig ldfgflddri tgsieyyhmp
      781 ttqmimnqri pqfsgfssit snlgevqnrg veislnttni knsvlewntt lgfsfnknri
      841 khlyyeyedv ldaegnvigt kesddisnkw figkpigviw dyevtgiwqk deieeaakyg
      901 qrpgdpkvwn npandeydad gnltkivydn ddkkflgqts pkvnwslrnd fkilkdfvvs
      961 fniyskmghk stsqnylngd nsaskitngq nvyvkeywtp nnptneygrl aaqgpsgvtt
     1021 pnkvydrsfi rlenvalsyn lpkklisrwg iekltlsgsi knvavwsihk weywdpetgs
     1081 iaprtfnlgl nltl
//
LOCUS       WP_118423402            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118423402
VERSION     WP_118423402.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121453
     Region          27..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekhrflmwf allfigvvsg yaqqlaitgr vldskkepli gvtillkgsa ngtvtdidgn
       61 fsikaskget lvvsyigykt qeillssdka tmtvelleds emldevvvig ygtmrkkdlt
      121 gsvtqvrpda laneapktvq dvlrgtagln vgfdksakgg gsmsirgqrs vysdgghndp
      181 liildgmmfy gelseinpnd iaqidvlkda ssaavygaka angvvivttk kgksekpvis
      241 fsanvgwatr adgrkvydad gylnyrrdfy ttdtygvnps tgkyeayqtg glpagyfdrp
      301 tdanlgkygl tmdawrnqtt qdagmssdei warriglnas evtlanflsg ktfdwydhsf
      361 qtglnqdynv sisgmtervn yylslgylsn egivrgneyn airanmklda kvtdwfsvga
      421 nvnfqnrsdg diavdwyrqi tsnspftspy neagelvahp qgenaywkgy nfdfdrqyld
      481 lekgftvlnt iltakltlpf gitysfnaap rlqyfydryy rssehpdwqa etedrvnreq
      541 skrfdwslnn titwdytfak khhtiltlvq eaeerqswad riqarnilps ealgfhgtan
      601 gdknlsefrs tdnretacgy larlfysydd kymgtfsfrr dgysafgttn pyanflsgal
      661 awtftnedfw kwgdilesgk lrvsfgqngn rslansyial anlalgmysq gyinsttgtl
      721 ldmkylfvdr lpntglqwek ttswnvgldl sflrgrinas leyyimpttd mimnqslpdf
      781 tgfasittnl grvenrgfei slntrnietk nfewntsfsf srnkneikkl ygeyetivda
      841 agntitkekd dvdnkwfigh pisaiwdyev tgiwqvneve eaakygqkpg dpkvanhyta
      901 ddrknadgtt tavynnndkr flgettppih wsmrnsfily knwsfsfnly symghkslds
      961 nylnndnnys qitncqniyt kkywtvdnps ntyarlsaqg ptglaapsrv vdrsfirlen
     1021 vsvaynvpae llsrfkiqna kifatvrnva twskeweygd petgdiaprt yslginltf
//
LOCUS       WP_118423617             925 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118423617
VERSION     WP_118423617.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..925
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102942
     Region          2..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkinifla gvlcslgvma qedtlivrqn devvemgrti tmdaremtga vsvttnlshk
       61 nsikpsnqlf gtlpglqvlq kagtvwenga tlyirgnssl nsnsplvlvd gfersidels
      121 seeiesvsvl kdavatslyg irgangvilv ktkrgsvgap kitfsyefnm aspkrlpkfa
      181 dgytyamaln eamendglap rysgteldaf knqtypgvyp nvdwldeslr dmsygdnvnf
      241 taqggsqfvr yytmlnfldn rgllkptsdn dgystqlkys rlnvrtnldi tvsptttvql
      301 nllgnftehn rpgestdkif nalfqvpsga fpvktdrgiw ggttnysnnp valisgrgya
      361 rsqtramyad vnmkqdlsai lpgwsagfkv gidntasywd nntkefgyes asvdfatgen
      421 iyttlrnegt lgfsksvgsv athfnlefyt nyikqwnkhs lnatllysmd kaktksqnsg
      481 rafmdivgsa hyaynnrylv dfslsgsass ildpddrwgi fpaigagwil seenfmkrdw
      541 lnllkvrasy gisgradygv nlfqniygsg nsyyfqnatn vpssssgmkf tqlgidglty
      601 ekshklnvgi dfrawnkltm tldafydhrt dilvssggsv sqifgmsvpq inngvvdnkg
      661 ieaslawddn ignfeyhlgg qftftrnkik nqneeyrpyd ylkrtgssmn qifgyevigi
      721 yksqdeidnr gveqllgdvr pgdlmfkdqn gdnkidaydq vplgynatcp eiyysfdlgl
      781 eykgfgvyal fqgvgnyskv lntasvyrpi vnnntistyy wenrwsesnp ngtlprltys
      841 gsdnnyntns mwvsdasflk lrtlelyynf ptkllkktgf lagvkvfarg hdlfcldgid
      901 lrdpesigte hptmtqyafg fnlsf
//
LOCUS       WP_118424716             955 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118424716
VERSION     WP_118424716.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..955
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106095
     Region          42..952
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyiqtkfil camlavspmf vsaqatdwne tdslanekdp mvqvafrkva qkdllggvsv
       61 vnveeltkkn yntysldnmq gyvggwngns lwgmdgdnag ylvlvdgvpr dannvmpsei
      121 aqisflkgaq avvlygskaa kgavvittkr gnveglnvsv rantgfhvak afpeylgsae
      181 ymtlyneall nddptaklry taediynhgs glnpyrytni nyyssdyvkk aynrsevtae
      241 itgggkrarf ysnvsyysng dfldfgeskn nrtdrfnvrg nvdvninsfi nayinanatf
      301 ydsksakgny wnvastarpn fpekgaplip ldmidpnata awellsttsn iidgkyflag
      361 tqanatnafa dcyaagsskw tsrqfqfdag vnvdlnqvlk glsfnamfav dyatsystsf
      421 dnkyavfvpt wanyggkdvi valskegnde kpgtqnvggs tdkqtiafsg qfnyqntfnk
      481 yhnvsamlia ngyqqtvsaq yhrisnanla lqagynyqqr yyadfgaali hsaklakghr
      541 qalspsvtlg wrlsgenflk dspvvddlll svsgsilnqd idlvmgdkef ylyesvwtqn
      601 dgyawydgpa gkytistrgq nndlsfikrk efsvnlkisl wnrlitadas ffinsmegyl
      661 ikeptfypsh lntgypaasf mavlnynnnk rvgfdfnina nkrfgdvdls lgvagtyydt
      721 kvtkrdeiyd dayryregka vdgiwglqsa glfqskeeie sspeqkklgs tvqpgdikyv
      781 dqngdnvidd kdevflgkgg wygapftlgi nftakwknlt lfvlgtgnfg ayglknssyy
      841 wvdgddkysa ivrnrwtpet aatatyprls arsasnnfra sdywlyktdr fdlakvqity
      901 dlpkrilrnt finelsayvs ganlltiske rkhmemnvgs apqsrfynig vkavf
//
LOCUS       WP_118424266             910 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118424266
VERSION     WP_118424266.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..910
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100845
     Region          38..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrirnlfcl slllvavglp avaqtklhvp lpdsittvgy atglrknlsg lveritenqm
       61 nkdqitnpld airgrvpglt ilkgsngpaa ldavrlrgtt slttgndpli ivdgvfgdls
      121 mltsiypadi esfvilkdas etaqygsrga sgvieittkk gvsgrtsvny ngsfgiassy
      181 ktvrmlngne frtlaqergi sildmgnntd fqkeieqtgl qhnhhiafsg gtntsnyrvs
      241 lalmnregvi vneklqnfts nmnmtqyvfd nflkcdlgmf gsvqkernlv nlhkvfysaa
      301 synptfpnhk npetgswdgy ayasqlshpl awmdvkdkna tshistharl tfnlaeawkl
      361 tffgsytynv venaqylpva vwaqgqayrg dkkmesllgn lmlsykkewr khffdvlgla
      421 eiqkdkysgf yttvtnfsnd klgydnlqgg airpwdgtns yyedprlvsf mgrvnytydd
      481 ryiltvnarg dasskfgsnh kwgffpavsv awvvskekfm eklsfidnlk iragyglagn
      541 qngidsyttl nlmrpngiap vgstpvvtmd klrntnpdlk wevkqtfnag ievallgnrl
      601 lltanyynsk tkdmlylynv svppftyntl lanigsmrny gtelsigitp lktkdmelni
      661 nanltfqqnk llsldgnyqg ehisateyks lagldgagfh ggynhivyqi vgqplgvfyl
      721 phctglvsdg nggytyqiad lngggvsled gedryvagqa vpktilgsni sfrykdfdis
      781 lqingafghk vyngtsltym nmnsfpdynv mkkapaqnik dqtatdywle dgdyinfdyv
      841 tlgwnvplkn trylqslrls ltvnnlatis gysgltpmin sssvnatlgi ddkrnyplyr
      901 iytiglsvnf
//
LOCUS       WP_118424021             938 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118424021
VERSION     WP_118424021.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..938
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105018
     Region          51..937
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkyiivls lfaglylptt aqesneeqtd kfvgqtidvg aerlltreea tgsvsvisse
       61 ttdrrsakni gnsiigqgng lislqsggry advnptfyir glqtlngkns plvmidgiqr
      121 divsiapeev esvivlkdaa avalygykgi ngainivtkr gkynsrsvkv tydhlftsla
      181 nkpkfvdayt yglavneari ndgltgrysn qelnalrdgt mpylypnvnw vdetfrdnam
      241 tnkyniefrg ggekfryytm ldlisnkgfv kepganegys tqdkyvkgnl rmnmdinltq
      301 ttdlqvnllg vlqetsrpga qadlwdlvyt vpsaafpird engiwggsdt wagtqnpvaq
      361 sigaayyknh trslfadmkl tqdlsgltkg lnafvrisyd nianiyedhs keyvysvnap
      421 twadgasept vkseiygkds emgtdaktne fdrllhfdvg fnyqrtfgdh siysqlkwdy
      481 enndpngvnn tvnrqnitww shygymnryf vdlalvesgs srlapgtkwa fsptlsaawv
      541 iskekfmenv ewvnflklrg sagiinvdnl pgdevwsyya qqygtsggty pfdsgwnssf
      601 grsylervat tnpshekayk ynvgmdaklf gcldvtldlw kehrtniwvt segkyseifg
      661 meppyenagi vdskgievgl dyskklgqve fnvggnfsln kneikemlee prqyanlvqt
      721 gnpygqlygl eaigffkdea diaasptqnf stvkpgdiky rdvngdniid tndevaigys
      781 ttcpeiyysl hlgaewkglg fyamfqgtgn ysavlntksm ywplinntni sqyaydnrwi
      841 pqnqnakfpr lssqsnanny qtstlwladr sfiklrnlev yyklpaswlk ktkivnaakl
      901 yvrgidllsf dhidendaea yginpmtksv alglsvtf
//
LOCUS       WP_118425297             621 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118425297
VERSION     WP_118425297.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..621
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=68702
     Region          32..>618
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvirlfcl ivcmtgfftn saqakifedd wvqglvvdqn geavigasif ekgtqngtvt
       61 dvdgkfrldv qsyehtleis yigyttqrik pkkgdnlhiv lvedsktmde vvvvgyqtmr
      121 ktdvvgavss ikskelnvtt ptvgqslvgk vsgvqiaqvs gapyqstkir vrgvasinas
      181 sdplyvidgy psnedlmlsp ediesievlk daasaaiygs raaggvvlit tkrgkegkak
      241 vnynfqfsvn qlakkvklln saqfadlvvd grnnayknfm vnagkawdda yfsdtndvra
      301 qrlgssnsaa mipeflydfe nqrvitpeyd tdwqdelyrn apsqrhhisv nggtdkirye
      361 vsaayqnqeg iilstgqrrl nlrgnldiqv sskfkvganf sntsnwnrev eegrfdhgpi
      421 lgaliyapif rcydengqlv kgemtsyssn ygfqqienpv alatetkirr ngvrntynlt
      481 asyeplkdlf lkanlgmyny sekyefyrpt slssganlpg tdqakaaans iartslqsdy
      541 laeftanynk swnqvhnfsg vagysiqknm ydilgvkatg yqddhitevt ghgadpsdit
      601 lnstsksnwt misyftrlvr p
//
LOCUS       WP_118430384            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118430384
VERSION     WP_118430384.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112255
     Region          44..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkieratqll flllisqggn aayanlprga saspvqvsaq ankitvsgtv vdvngeplvg
       61 vsvlekgtgn gtitdmdgnf tlsagegaal eisyvgyqnl tvsaketlgv lvmkedteql
      121 devvvtalgi krsqkalsyn vqevkndvlt kvkdanfvns lngkvagvsi qrsasgvggg
      181 trvvmrgnks ikgdnnvlyv idgvpmgnqa drtgdgtgfg agrtssegia sfnpediesl
      241 svltgpsaaa lyganaangv ilittkkgaa gkvsvnvsss aefsnpfvlp rfqntygnvs
      301 geaaswgekl pvpssynpad ffntgttftn sfnlsvgndk nqtyvsgsav nakgivpnnk
      361 yhrynamvrn ttkffndklt mdlsasyvre yynnmlsygt yfnpllgayl yprgenfeke
      421 kyferydael gynvqswtpg dfgmavqnpy wvayrnlrpe vkdrymlyas lkyeitdyln
      481 vsargrldnt ytekedkrya sthgtfakpl gryaysnetf rqkyadiman lskpfagdfy
      541 anvnvgasfe eydtkgrgyg gqllkvpnlf aydnidpstg vpsqtggdnr kmnlgvfgsa
      601 eiswksavyl tltgradkps qlvnskspwi fypsvglsai vtdllpetmr qsispvlgfl
      661 kvrasytevg spipytgltp gtithtiegg vikpfkyypl pelkpertrs yevgidskwl
      721 nntvslgvtl yksntydqll eaklsetsgy dymfvqagnv enrgieltlg ydqtfgnfsy
      781 stsltatanr nkiielasnv knpvtgeald lsdikvgrfr lregeevgti yaeerlkrdq
      841 dgyivynegq tittestepy klgsvnakwn lgwrngftyk gfnlnflvta rlggivvskt
      901 qavldqfgvs qasadardag kvmvgnvavq pkdyyesvvn ldaynvysat nvrlqeaslg
      961 ytfpnswfkg tpfhsvnlsv ygtnlwmiyn kapfdpelta stgtfgqgyd yfmlpsqrty
     1021 gvslkfgf
//
LOCUS       WP_118429050            1135 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            dorei].
ACCESSION   WP_118429050
VERSION     WP_118429050.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola dorei
  ORGANISM  Phocaeicola dorei
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1135)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1135)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1135)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Phocaeicola dorei"
                     /db_xref="taxon:357276"
     Protein         1..1135
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127254
     Region          54..104
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          117..1134
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkhaqlkl ftlfsllllf ctfesmaqek litinvknvs lkeifniien qtpyrfsyrs
       61 vvldadrnis isaenisvtt vlnqalkdrn leysivspkt ivisdkqtgn vkssetkkis
      121 giikdvngep iiganvkikg qsigtitdid grfvldastd atlqisyigy aslemntgnk
      181 kelnivlked tetleevvvv gygvqkkanl tgavssvkmd eilgdrpvts vsnvlmgamp
      241 glqvtgtsgq pgaemsfnir gvnsinegap lvlvdnvemd inmldpndie sisvlkdaas
      301 saiygaraaf gvilvttkkg mkdtrfsiny snnfsfskps nlphkatplq tvqaykdmgt
      361 vsyqtgqnvd twlellkeyd tnsgnypdgy avvdglrysl qetdllndmm etgfqqthni
      421 svgggnksis yrmsagmvdq ngilvtdkds ykrynissyi rsdihswitp eldikyansh
      481 selpytsasy giwgaavafp syfplgnmel dgeilpintp hnfinlsapk endrndlrif
      541 gkltitpfkd lkiigeytfn rktreittfd kkfnyahgan frkeqsvsns kyeienratn
      601 ynafnvyany nktlgkhdig imagfnqesn aykmmkasrt dminedlpsl sqatgdykns
      661 defeeyhvrg vfyrinysya gkylletngr ydgsskfpke nrfgffpsvs vgwrvseeqf
      721 mewskvflsn lklrgsygni gnqsiepyaf ipgmdsplan wvvngqattt lappalvsns
      781 ftwekvstld fgfdlglfnn rlnvvfdwyq rdtkgmlapg melpgvlgak aplqnsadlr
      841 akgweisldw ndrignvqyy lgfnlydsrt kitkydnevg llgkdsdgnl iyrkgmelge
      901 iwgyttdrly ttedfdsqgk lknnipkmeg ynpnpgdily vdfdgngiin ngkntsnepg
      961 dthiigndtr ryqygirgga awkgislsfi lqgvgkrdlw lmnelfyphy daystlfdsq
     1021 lnywtpehtn syfprlyeka egntkanqkt qtrflqngay lsirnislsy tfpiklikpl
     1081 gitnlsvffs genlftfdhl pkgidaervv tdnleqrgft ypymrqfsfg inlsl
//
LOCUS       WP_118430301             905 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118430301
VERSION     WP_118430301.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 905)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 905)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 905)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..905
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..905
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..904
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 yqtqeipvgn ggkkditlqd dselmdevvv igygtqrkgd vtsavasvka edftagkigd
       61 aaelikgkva gltiakgsgd pnaestirlr gvislqggst plvlvdgieg glgtvspeni
      121 asidvlkdas aaaiygtrga ngvilittkn gqresrtaan ysgymslskf gktldfygae
      181 eirqgltnya dkgydtdwld avsrtafthn hnfnisggsk nttysadfty rkeegvllet
      241 yneemrmrfd vshwmlndml kvnfnmvktf hkngpidaag lgiyrqaimr nptepiwned
      301 gtfyenfavn yyynpvgiir eqdgkynsen trmtgnitfe piknwqtnlm lsrrvtsdhn
      361 rgyytseyfs qksenhtgya yhsqneyttd nlevtskynh twnkhrfdal vgynyqynvn
      421 egfgannydy ptdfylwnnl glgtalkdgk agmssykndn tligffgrvs ygydnkynvl
      481 lsvrregssk fgennkwatf psvslgwtis nekfmegltw lnnlklragy gvtgvivgds
      541 ynsltryeyg spyfydngvw hqglsvksnp npdlkwetsk efnigldwav lderlsgsid
      601 vyqkktsdml ydftvptppn lynktlanag kmrnqgieia vnaipvrtkd fewkttvtas
      661 hnankllsls ndlyetsnqi dhaylgepin lstqrmevgr smgqfygmks vgvsenglwl
      721 ienaktgeie eftdnmlsnd dyrqylgnal pklylgwnns fryknfdlsf qmtgqfgfki
      781 lneprayyen nsiaynrlks vqkapyggqy tlstaqkqtf vsyyledgdf lkmtnitlgy
      841 niplksskfv knirayvsad nlfcitgydg ldpemsngdi wslgidwrdk ypstrsftfg
      901 lnvsf
//
LOCUS       WP_118430518            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118430518
VERSION     WP_118430518.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117084
     Region          41..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktvskkvlm cgafslsmlg gvpyvqadap dcllavqqga kisgvitdse gpiigasvve
       61 kgtsngtitd ldgrfsldvk pgailvvsyv gyasqevkat tgtmritlke dnqvldevvv
      121 talgikrerk algygvaevk gesltkaket nvinsmagrv pglvvsqtas gpsgstrvil
      181 rgstemtgnn qplyvidgvp ldntnygsag tyggydlgdg issinpddie nisvlkgpaa
      241 salygsrash gvilittkka dgkekfsvey ngtltidtql skwndiqqiy gmgskvhida
      301 isntntswgp kadgnnmlty fdgvsrpyli ipdntsgffr tgltatntav isashgktgv
      361 rfsytdmrnk divpkthmsr nnfslrants lskvdldfsv nytredvknr pamgdskani
      421 gknlmtlatt ydqawlktyq dengeysnwn gmdpynvnpy wgvyknqnis qkdqfrlngk
      481 aiwninphlk lqgtlgtemn wftfedyqap ttpgfeagrl qnstfenrmy nfellalynn
      541 twgdfdfngt lggnifkvdn lttittaqdm qirdvialls fneisveqnt yrkqinslyg
      601 avnlgwkhmv yfdatlradq sstlplnnns ylypsfsgsf ifseiinkkn alpygkirms
      661 waqvgsdtnp yqlglvytks kytypgytig yinnntvpnk nlkptrtnsf evgletkfln
      721 nrigldftyy sqiskdqimg masswssgyn yrlinageie nkgieialnt rliqtkdfsw
      781 dlnlnfsknq nkvkelvdgv dmfelekasw ldvqvaakvg enygsiigpd fqrnengdil
      841 idpstglpmy dksshilgna swdwtgglvt tlayknlsls avfdvkvgad lysmsarsay
      901 esgkaletlq greewyrsee qrkaagfpkg spdwkptggf iapgvidngd gtyrpndiyi
      961 npedywmsvc rnapsmfiyd nsyvkcrelt ltyqfpkkll knvvdnltis fvarnpfivy
     1021 knipnidpds nynnttgmgl eygslpsrks ygfnvnikf
//
LOCUS       WP_118430609            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118430609
VERSION     WP_118430609.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112847
     Region          28..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkyknlmwa clallavpag aqdtdnnvrg mvvdkwghpv ygasvmvkgm petrvetdkd
       61 gkfsieasag qqlnivsvdk gtttvkadgk slvkvvlnya gqsvdvgagr vftraestaa
      121 vstiynedfd krsaknmsns llgqgmgmmv lqnsgnyadv eptfyirglq slsssnplil
      181 vdglerdmsl lspeevesvs vlkdaaaval ygykgingai littkrgkyn skeikftydh
      241 vnnfmdrkpe fvdaatyaqa ynearryegl spryadkeve yfrngdfpyl ypnvnwldet
      301 fknsgisnky tiefrgggsk fryysmldlv tdrgfvkegn mnegystqnk ysranlrtnm
      361 didvssttkl kvnilgtlse slrpgasanl wdmiytlpaa afpvkdedgl wggnnttwlg
      421 tqnpvaqsqg aayskghtrs lfadltleqd lsavteglgf nfrlaydnys siwedhsqay
      481 tyggytvtyt dltgplytht tggeptemgk dgsinnwtrq fnfsggfsyn rnfadthdvy
      541 sqlkweyeyr dsydlnttiy rqnvswfthy gydkryfldl alvgsgssll apghkwafsp
      601 tvsaawvlse edfmnnaswi dflklrasfg iinadylpas dvydywdqiy tttgtrymfn
      661 saydssfgtt elsrlastny thekgykynv gvdatlfkgl nlsvdayyqr rnniwvsseg
      721 kytsvlgqtp pyenagvvds wggefsldyt khigdvvlna ggsfnwnrne ikeqleepri
      781 ydnlvqtghs lnqiygleav gffkdaddia nslpqsfgtv ypgdikyrdv ngdkvidsnd
      841 vtaigystva peiyyafhlg aewkglgfda qfqgtgrysa ilntksmfwp llstttlsth
      901 yyenrwtedn lnakyprlst qsntnnyqtn tiwladrsfl klrhievyyn fpkswlqktk
      961 figdaklyvr gvdllcfdki dvldpesyga tnplnkslii glkvgf
//
LOCUS       WP_118433825            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118433825
VERSION     WP_118433825.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121515
     Region          33..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhsdyhgkl lrlamffval flcgtmayaq tdrmisgivv dengdplpaa hirqvsqtkg
       61 eelaavitdm nghfrltllr takeieisyl gyeskkvrlt sansyrivle paselldevv
      121 vtgyqtisre ratgsfakvd skkletqrls svsslmegri agysdgkirg vtsmnglttp
      181 lyvidgfpve ktisdglgnw venvpdlnie dienitvlkd aaatsiygar aangvvvitt
      241 kkagknqlnv sfsatltvrp ynfytghlag tadmiemeke waamnpnlqg egasqyaqnl
      301 ldnasmyscl gvqailkhht gaiseaqmeq tlhelasqgf ryyddvkkyg krnpfsqqyn
      361 lnigrgtekn tfnaslsyrn nreedkytds esfglnlqnt trltswlsld lgtylnygdg
      421 ttqsynltsp gynyvpyssl lngdgsyytn taadrysksq qeiissygly smditpldel
      481 grnlsksknf snrtfarlnf kftdwlryta sfqyevgeyk tsqlqdkesy avrnkvntfa
      541 tdasgsgqat ynlpygniyt tgtnsirayn frqqldfnkt faekhdvtal fgmevrenkt
      601 eynnrkyyny dpalltydli dervlsntyt gvlgnyvsfn kndisniyel vnrfvsfygn
      661 aaytydgkym vtgsirwdrt nlfatgskyq kkpiwsvgag wnldkesffk vsfinmmklr
      721 fsygiggnia knsapymtay ynnthvggiq gtisnrpnpd lrwektttan igvdfsmfrn
      781 rlngsieyyn ksgvdllant ngvptegfgf stytmnngkm rnrgfeltls sdvimgkdwn
      841 wnvggvlgyn knkvtyvnvk apaiflqfdy paayprvgvp ynaiygylwa gldskgqpqv
      901 ydsegnihvs sspqkvedav ylgtsvpvys gaintnlryk nwelaaqllf egghkmrntn
      961 iaypglgvts kdvskrwrqp gdeaytdvpr yvpseskdyn syssdlyska sihvldadnw
     1021 rlknlsvtyh vpasvcqkfy vknarimlgm envftlaksr dvkwmlggys kpnylcnvnl
     1081 nf
//
LOCUS       WP_118433815             924 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118433815
VERSION     WP_118433815.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..924
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..923
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 kksdvtgama rvgseelntr pvnnafealq gkaagvdits serpgtvgsi rirgnrsisa
       61 ssdplyvvdg vplsaggiet inprdiesid ilkdasstai ygsrgangvi littkrgkag
      121 rlalnysgsv tletlkdksp amsasdyitw rrwayynsdp vnnprgdqpn ydkdqiyfaa
      181 sgdpaalanv nkgwnngtwd gsrvtdtdwa divtqtgith ehtisgsggn etaqaffsig
      241 ylnnqgtqkg qeyerynfsm svdlqvkpwf kmggsingsw avqdygysrt gqssgsgpvd
      301 iysaakaipr fgvpydeegn iitnpcgstt nvytvidewn kstdnrqtfr algsfygqfd
      361 fgkiwapleg lsykisfgpd frhyrqgifi skdsavkmgs knyakyatdr ylswtldnqi
      421 nynktfgkhn lgvtllqsas kynkesgses anaipnenfe wynmgsvdit daatygagms
      481 tgmsenqlas ymarinyayn drylltvsgr ydgssvladg hkwsffpsaa lgwridqedf
      541 mkdiswinql klrfglgttg nsavnaystl gniqsfyvpf gstltpayat nepyytssqv
      601 kmankdlgwe kttqynygvd fsflngrisg smdiyhsntn dlllsmtipt ltgfnstyan
      661 vgktknfgvd lslnlvpiqt kdfewsstin aayqkdeive langkqddis nawfigesin
      721 vfygtasdgl wqesdaaema kfnanghkfe agmvkpvdqd gnyiidsndr iilgnknpkw
      781 vlgwsntfny kglelgieln grfgymvdtg gegqygmynq reisywtpdn tgadyqkpiy
      841 staggdayss llgfkdasfi kirnislgyn fnskalknig isslklyaqa knignlyssv
      901 dfmdldlgtt yynrgftfgl qvgf
//
LOCUS       WP_118433958            1136 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_118433958
VERSION     WP_118433958.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1136
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124745
     Region          41..1135
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkrlksvsm llflmgastg aayavanpgv advkitqqsg tctgivkdat getvigasvv
       61 vkgttngtit gldgdfslsn vkkgdiivis fvgyqtqevk wtgqpidvtl kddtqqlgev
      121 vvtalglkre ekalgyavte vkgdelkaan tispvaalqg kvagveisgs dgglfggtki
      181 qirgastlss nnqpiyvvdg vildngvsgn ttadwdagan nasdygnelk nlnpddfetv
      241 svlkgaaata lygsrglnga vvittksgkg tqglgisvsq tfgidhafkt pdiqtlygpg
      301 ympgqsdadq ngsmwdehqf tvnqngehtl vgvpnfgfgp rydgsqirny dgtwttyspr
      361 knnmldlykl gfntntnvsi rggnektsfy tslsyknaks ttenntfery smllkashkl
      421 ndwvdvaasf sfanskprna qlnagelfvn antnvinplf dvdyfrnkyl gehggiasts
      481 ygdqygsvps saknyffkvd nydyvrketv irptfevnvk mtdwlkfkad anmnryytsi
      541 edkqlgsgya neggyygitq dikeqftvgg tftaskqikd fslggfarfe yyntssqhsk
      601 vstdggmvvp gewfvenskk tkksestisg skriisaifa lnlgwknqfy ldvtgrndws
      661 salvyanrtg nhsyfypsvs gswlinetfr esmpswinla klraswaqvg ndtdpyavnq
      721 tysfatmemy dgniytneld klmkiadlkp erknsweigl dfrtfnnrln ldftyykent
      781 tdqimkinvp aisgvtqqlv nagniqnsgi eialnttpik tkdwqwdldf tytrnrskiv
      841 slhpnvanyi elsgyvnayd yhigsvakvg esygvlmsdv tqarnengvp llewddswrg
      901 ayraqsktae vvgnmtpdfl gsvattltwk dlslnvgldm rfgglvasyc nlygtqagwt
      961 esslqyrdpe hggmtwtsqy adskgiqytd gmipegvfke gtiatlvdgt kmdvsglsya
     1021 qlvqegklep thagswygnn yawgaqtidd iwvhklsyia lrnitinyrl pnsishklga
     1081 kglnlsfsar nlgylynslp nnlnpesvrs nsasefrirg fepytasyif tinanf
//
LOCUS       WP_118433827            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Phocaeicola].
ACCESSION   WP_118433827
VERSION     WP_118433827.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115757
     Region          25..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkqclviv mtllclcvka qnlrvtgvvr dksdviigas vmvknstvgt vtdmdgrysv
       61 evpangvlif syigytpvek qvdgqtvinv tmnddvqaid evvvtaigik qqkkklgytt
      121 qqvntealdq pgtvnvgnal sgqvagltvn nptgifqaps fslrgktplm vidgvpvesd
      181 lfdvspenie sinvlkgtaa aalygsrgkd gailittkla kedgltvtag lssmvsagft
      241 vfpetqtefg sgsngqyafw dgadggisdg dmtwgprfag qkiaqwnspi rnketgetip
      301 wwgdvsgtiy ddqskyervp iawephdnlr dflrtgiitk atfsvasksk kanynfngdf
      361 snqrgqvpnt svytgglnfn smynlsnsvt lsanlsynkv yspnyprygy gpknhmytil
      421 lwmgndvngk elaehyyrpd segtrqanyn yawynnpyfa aneltqkhdr ntmngqlkln
      481 wdvipglslq graagrlest fedmsvpksy mnygdsrngd yktwntdqld inadflatyt
      541 rafsrnftlt vnagtslyyr qirkqsqstd glivakvynl gnslnpvsat nsmnekaies
      601 vygsvnvdlf eslfltftgr ndwsstlakg nnsyfypsvs lstlvneyvk lpswmdylkv
      661 ngawaqvssd ldpyslyaty sngtlygsip svtypgtlln anilpqktts yevgvstsfl
      721 hnrigidlty yhmldensii elpissasaf tkryvngney ttngfelivs atsvknknft
      781 wnvatnwssn irkltgiygd qekfgdlkkg dradamyate wektpdgrli ldantglptq
      841 safktkvgnq spdvrfglqn tfkikdftvn idmdgaiggt listttqkmw wggkhpkstm
      901 yrqeeydngg kpvyvpegvn ivsgevtydv ngnivsdtrv ykknetavni qtwaqnypyr
      961 avvrteesel fantfsrsfl klrrvavtyd ltkfiqsqfi kgldvtvfgn nlavlkktpy
     1021 ldpdfgasdg dlqdpsaryv gvsanikf
//
LOCUS       WP_118433077             954 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118433077
VERSION     WP_118433077.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..954
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          5..953
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 eipwdgqpmn vtlqddtqtl gevvvtalgi krekkalgya mqevkgdall earetnlana
       61 ltgkvsgvqi irssngpggs skiqlrgans vtglnqpliv vdgvpmdnft gasnndidnp
      121 tldmgnglsd inaediesms vlkgasaaal ygsragngvi littkkgtkr eglgitisgs
      181 vsaettfmlp krqkafgqge ngvfdstngy swgpevtgqs ytkwdgttan mqifdnvknf
      241 fdtgvnlses isfqqqydkt siytslnrmd dssmipganl srtnltlras stfgkddrws
      301 idakvqyint laenrpisga rgnnafytif nmpttidird fsspvkdefg emiwwskggi
      361 npywskdynp nkdsrnrflm ngslkykftd wldaeikags dmyftegeek lyagsptnnk
      421 nsrystsekk ffennfsfli sghkdelfgk fggnfsfggn lmerkstgld namgkltapd
      481 lfslangdkk dlsitetyih kkinslygtl ginyngwafl datfrndwss alnkenrsff
      541 ypsvslswvi sdmvgkvgkg mpewftyaka rasfaqvgnd mdayqlynty sigsdpngnt
      601 tagqgktkyd advrselits weagaelkff nnrlgvdfaw yktnakrqlm niplnnlsgy
      661 dnmkvnagni qntgieimln arpietaqfs wdtqlnfsqn kskiiellpg kpgmqyalgg
      721 sdalqvyava ggaygeiwgt kyqrveegef kgqlllnesg lpqatsdkhk igeqqpdfll
      781 gwtntfnykn ftlsflidgr fggdifsftn mnlqrsgiae ctapggkred ivvagvikdg
      841 ngykvndqsv sleryykala tgragiseay iydatnirlr nialsyrfps smlkktpfqq
      901 vklgftvnnv wmisshldgi dpesvyatst natglenssa ptsrsylfnv tlgf
//
LOCUS       WP_118434769             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118434769
VERSION     WP_118434769.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109174
     Region          32..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvkrtklcl crslllmagl lfavasfaqd ltvkgkvtdt tgetviganv tvkgttngii
       61 tdidgnytll gvkpssvlvf sfigyktqei pcsgrqeinv vlsedaqald evvvvgygsl
      121 skkelsssiv qvdrskflqg smnnpmemlt gkvagltvnn taaanpnass slqirgatsi
      181 sasndplvvi dgvaggdirn laaqdiesmt vlkdaasaai ygtrgangvi littrkgage
      241 agraqvtyds wfgvnlaksg pdilsadefr rsrratdygy stdwydlllr dfsydnnqyl
      301 sidgstkngy ygasfnykka tgldlnssre efggrfvlnq rmmdgiveln gslnarrvne
      361 vwgndgmfdt alsmnptmpl ynedgtyfqp tsptgarnpv qelkeidnng qrvyllgtae
      421 vkvnlirsek qmlntslsys lhyndlkqhy ytpstagesy wngyngraev tyqkwytsrl
      481 ewlgnysldl gdhnfkamvg ynyeqttwer lqagnsdfnf ddilwnnlgs gsylakgkas
      541 mgtgkslakl igvfgrinyn wknlliasas iryegstkfg adhkwgafps lslawemanm
      601 gflkdhqniv qslkprvsyg vtgrsdfdcy qslatygshk naqlnvtdty lmdgawvtgy
      661 apsvnanskl gweksvsmni gvdfalwnrl rgsvewfdrq srdllynyta pqppyiysti
      721 lvnvgttvnr gievslegda fkgtpvewtt ginysygttk ldklsnslyk asyvelyqkp
      781 gvgtseyffr veegskigqf ygyeyagven gdmmiytdeg ekvpvskadv kykrhigngt
      841 ptsylswsnt lryknfdlsl mfngafgfei fnmrrygmgl kgcgtdnvlr daygkdadit
      901 tgggvissff lekgdyfkld nltlgytitp kenkfikgmr vyltaknlft ltgysgndps
      961 avaingltpg vdtnsaypsa tqlsvglnir fk
//
LOCUS       WP_118434958            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            stercoris].
ACCESSION   WP_118434958
VERSION     WP_118434958.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113119
     Region          15..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msdwkqssqs tqqaktitgk vvdvagepii gasvlvkgss tgsvtdidgk fsveapvgst
       61 lvvsfvgyat eevkvgaasd ytvtlkddtq slsevvvtam gikkekkalg ysvsdinske
      121 lmknkqtnvv nslagkipgv nitqaggaag agsnivirgg nsasesrdnq plfvvdgiiy
      181 dnstvntgns gtdgmtktat tfsnrvmdin pediesmsvl kgaaaaalyg sraangviii
      241 ttkkgeegav rvnvsskyty swanklpevq klygrgeynt sgafidktmd swgdridgma
      301 ydniddffqg ssvwdnsvsv sggskngsfy lsgsnyhqsg iipttgydkt tfrfngeqky
      361 giltvganvs ysqastdktl tsaglygqgg ngamtavygw pvddqmsryl nddgskyril
      421 eglqdleddv enpywilnkn tltdetsrft gavnaslklt dwwdvsarag idkyttssnt
      481 lrrpggavkq iyqngymskg dvnyqyittn vmsnfhktfg dfdlnllvgt tteatkttnn
      541 trwgynfvte glysfnniik anqyfkestv rkrmvglyge frasyknlvy ltvtgrndws
      601 stlpvnnrsy fypsvsgsfv ftellpknnv lsfgkirgsw arvgkdaday slgyymwpva
      661 tlnggkygmg nswtggsvgl kpeiqdsyel glemrffngr lgfdytyyqs ktkdqicapr
      721 laqstgyifl tlnggsvenk gmelsitgkp ivtkdfqwet tlnlsgnrgr lgdfidgvdi
      781 fyvtdaqvga akagsipngg yflgltgnky etaqgpdgkm ynvidpstgl ykdtqvetni
      841 vgnrepklig gfnnsfsykn fnlsflfdir lggdiyngte yylvtkglst ktinresvsf
      901 tgvvntgtaa kpsyetktit ynanetyqvg nstrsgkymi qeyyknyakn aynfitdtnw
      961 lrlrsislsy dfkdllkkqn iikgltatit gtnlfvwtny kgmdpetcvs gsgtggsgsa
     1021 gidycgvpat agmsfginlt f
//
LOCUS       WP_118434739             924 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118434739
VERSION     WP_118434739.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..924
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102387
     Region          32..923
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkiniila svlcsfnlma qvdtltihkd kvvidygrni thdarevtga vstatsdkls
       61 hknsinatnq lfgmlpglqv lqnagavwed gatlyvrgmg tlnsksplil vdgferslke
      121 lsseeiesvs vlkdavatsl ygirgangvi lvktkrgslt spqisfsyef nmatpkrlpd
      181 fvdgytyasa lneamkndgl mprysvaeld afknqtnplf ypnvdwvdet lrgvsygdni
      241 tfsargggkf vsyytmlnfm dnrgilqptg dndgystqlk ysklnvrtnl diaasptttv
      301 qlnllgnfse hnrpgtgvsd iftalyqvpa aafpikterg iwggtttygn npvanisgkg
      361 yarsqtralf adihlkqdla allpgltggi kvaldntaay wdsntknfgy esavlnletg
      421 ekefnthane gtlsysksvg svtthfnfea yanlsrqwgk hdlnttfmys mdkikskgrn
      481 tgrafmdvig qahyaynnry lvdlslsgsa ssildpddrw gifpaigagw ilseesflkn
      541 dwlnflklra sygvsgrady avnlfqdiyg sggsyffkna ptsmsgmklt qlgvegltye
      601 kshklnvgvd fkawnklsla vdafydhrtd ilvaggnavs gilgmsvpnv ndgvvdnkgi
      661 eialnwddki snftyhlggq fsfvrnkiin qneeyrphdy qkrtggslnq ifgyevmgiy
      721 qsqeeidnre vkqylgdvrp gdlmfkdqng dnridaydqv algynstcpe iyysfdlgve
      781 ykgwgvyalf qgtgnyskll dtrsiyrpiv gnntistyyy enrwsetnpn gtlprltysg
      841 sdnnynnnsl wvadasflkl rtlemyyrfp ekllkktgfl ggakifarth dlfcidgidi
      901 rdpeaigash ptmtqyafgf nlsf
//
LOCUS       WP_118434976            1126 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            stercoris].
ACCESSION   WP_118434976
VERSION     WP_118434976.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1126)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1126)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1126)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1126
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         1..1126
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125024
     Region          43..1122
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksikkkrsm ashrklhfqk vlgsmivala llfagsagaq etktikgmvr dvtgepliga
       61 sviekgtnng vitdvdgnft ltvpadatls iaymgyatre ihlakrkkqg dlrvtlreds
      121 qqlkevvvta mgikkdtkrl gyavssiesd eivkagatnf asamygkapg iritqtqggs
      181 agavsinvrg ltsitgnnqp liildgvpir nggtgkstdf aefgndgqir snglvdinpe
      241 diesvsvlkg asatalygse aangavvits kraksgkltv dftaqvtanl paylpkvqtv
      301 ygpgryntey sdyekqtggf yqrtmngesy rslynttmsf gpkydgsdvl ywdgkmrpyl
      361 patdnpwkel frtgwnqtyn laisqgtets snrfsytfmg etpnsltgsf tkhnfkltgs
      421 ykpartlnie yslnyivqdv kdrpqtslnl ygsfsnmfss fmdipylkqs yvtslgyrnt
      481 yaggdatltp deawaydpgy lngvlnmlwn myhhhskete nrligmirpt wqitnwlslr
      541 aqlstditdt kqtleyeter pnslydpsgs fqninrrydi vygdvmlnfn ynirrfdiaa
      601 tlgwtgryen mnnmrvstng glvtenwfdl nasrytasst lqrmellktg ymgtlslgwd
      661 nylfleltgr qersstlkdq sffypsanls flfsnafrmp awwnhgklrl sygvvgnape
      721 tyaaniiyeq gsdngftwny vpsswgnani rpekkyeyei gfeskflnnr lgfdvsyynn
      781 rvkdqilstp qpstsgvkyv lmnvgevane gwdisvsatp vltknfrwdl tanygiyrnk
      841 vvkladgvpy leisnigggg akiqavegrp mgdiyvqvpq mnengeylvs dkglymnqte
      901 lqrvgninpd gvgglfssfs yknifldfsi dfriggdvin emyqystasg ltpeslqfrd
      961 tehgglsyyy pgnnnasgvp vqvdpslgag pngetvyhdg vilpgvvast gekntriipa
     1021 gyyynqtynw gtqpeqltyr hsvfdnsyvk lreltigyqf peklisklgm trlsvsvfgr
     1081 nlfyfykalk nydaessvgt swasqavvgg sttatrnfgv slrasf
//
LOCUS       WP_118433960            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118433960
VERSION     WP_118433960.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          5..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 eipwdgqpmn vtlqddtqtl qevvvtalgm kratkalgya vteiksdeln snvvnpvsal
       61 qgkvagveis agdgglfgss kilirgastl gsnnqpiyvv dgvildnatk ngdadwsasd
      121 tdwgnelknl npddfesvsv lkgaaataly gsrglngavv ittkngkgkk glgvsfsqtf
      181 gidhvyggpd fqnqrgdgym sgyanykssg nmqdtnsfyl ngngdrsvaw gggvswgpkf
      241 dgqpiefydy ttvnyspykn nfvdaydngf nsntnvsvqg andtssfyts lsykyadgnt
      301 pnnsferisf lgkashkisk dveieaaisf anstprqgge tnfgekfidg tfsrmydtry
      361 wrtrykgahg gladnaynde ygnapgkevw wsvyeneyiq ketsvrpslk ltadlnswlk
      421 ftaegnynyy ykrneskelg sgyaneggyy klgqytkeqt nlnasfswnk evkdfnisgf
      481 irgeyyhnfq qelqlntngg lvipgqffig nsknpvgtsg nisgektils lagqvamswk
      541 dqvfldvtgr ndwssslvya dkhgnysyfy psvsaswlih etfrgkmpew isfakirgsw
      601 aqvgndtday kintayslyg idnsyglqvp dtyyaanlkp erknaweigl dwrflrnrig
      661 vdftyykent kdqimtikvp sesglsnqli nagniqnqgi elainttpie tkdwtwdlnf
      721 tytkntskiv elhenvanyi tlvgdaaygn yriasvaevg geygllksda tpnydpktgl
      781 pilelasyns rhsvyytrsg kvetvgsiqp dflgsvnssl ryknwtlras mdmrfggmva
      841 iygshygtay gylkssmngv daenggityt siwdgltydd giipeaimpg gqtintpsgt
      901 ytiaeggely adlvnrgivd pqhasswnyw nnswgraavw knndwfheln yialrevsls
      961 yrmpgkiadk igasginltl tgrnlgylln slpnnfnpes lrgtqagqfm irsvspytas
     1021 ytftinatf
//
LOCUS       WP_118435370             976 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides stercoris].
ACCESSION   WP_118435370
VERSION     WP_118435370.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         <1..976
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..975
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 vvlkpdtevl devvvvaygt asrqsitgav asidskklem rpvtevtgtl egaapgiqvn
       61 nsygepgsdk seirirgfgs vngtnapliv vdgspyggsl ndinpqdies isvlkdassa
      121 alygnkaang vimittkkgk shklnfrigv kqgmytrgip eydklgvnqw meamrsgmqs
      181 ywekdggvtp qqafeasktv nddivfspif dkngaamfde ngkfvakvkp gyndldwlka
      241 lertgyrqey tasadamgek ydifssfgyl nekgyiigsd ydrftarlka nyqptswfkt
      301 gvslsgtmsg snyqanahda yfanpfytag qmapvypylm hnedgsvatd gngnsydisn
      361 ydylsgrnii yeiqndisrk ernavsgqiy gtisflkdfa atvrgdlynv nntekafnnp
      421 ycgdgaanng rlskvhdrtr eyrftqeltw ahdfdkhhid vllahesfkh synydfmmke
      481 qmkvsgntem snfakmtsid gynqeyttes ylsrarynfa eryfldasfr rdgssrfsdp
      541 wgnfwslgas wiisqekfmk dltwidnlkf rvsygevgnd agadyyayke lfysdvnagi
      601 gafykiqipn knlkwetsgs ldialegrlf nrfnfsldff nktskdllft vynplsagat
      661 dwfatsdetp sgmsqyfani gsvrntglev amdvdairtk dwkwniglnl ttihneitkl
      721 pggkdilhgt qnyseghsiy efytytyagv dqmngralyn ansqlgesti nalkaqdeyv
      781 tingknyvyn tsyaekewqg salpdvygsi ntsltwkdlt lsvlctyslg gkvydynyqg
      841 lmytttngpg alhkdvlngw qavpegmted spnrlnpngt pqfdlsslas tsygassrwl
      901 tdasyfvikn inlnysfpkk vvtkwglggl svygsienaa tftarkgmnp qysftgsqdn
      961 tfvaarvftl glnlnf
//
LOCUS       WP_118435328             973 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118435328
VERSION     WP_118435328.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 973)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 973)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..973
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107218
     Region          1..972
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqaqdvaikp nvkvimksdt emldevmvia ygttkkesft gsaeviksek lkerpvanvt
       61 kaldgmvagv qttsgsgqpg sgssvvvrgy gsinssqspl yvvdgvpydg nisainpndi
      121 etmtvlkdas agalygsrga ngvimittkk gnsgkvkvnl kanwgvssra ipryetmdea
      181 gyletifqsy knnqiinggv spelagvaal eamksgstam lgqneqynpf nysitelidp
      241 vtgkvrsdak lrysedwmde alksnplrqe yvasfsggsd ktkymfslgy ldeegllktt
      301 kfnryngrln idsevtnwlk agmsanysrn esntavenss gssnvwysaq lmapifpvfe
      361 kdangatvyd nlgnavfdyg knrpagasse wntiatlydd mystqsdnls grayaelgdl
      421 kntflqglkf svnygfdlin sagatyynpy ngnsvavkgt iqkatartfs ytfnqlltyd
      481 rkfgdhhfea lvghefykyr ydylsatktg fpfgglyeld aattitgass yqnnyavqsv
      541 lsrlnydfad kyylsasfrt dgssrfykdn rwgkfwsvgg nwrishesfm sditwinnls
      601 lkasygvqgn dailngtkqn fyawqsfydl gyanssmsga avtslenkel kweknanlni
      661 gieaklfdrv satiewyqrk ttdmlmsfpm atslgfdgyn knvgsmrntg idltlgvdif
      721 kdtpftwnlt llgstiknkv lqladkpeii sgsyiirege tlysfytata agvdpatgeq
      781 lywawdtden gvkgkkyitn dmakatacke iqgsripdly gsinntfkyk gfdlsilcty
      841 siggkvldgi yntllygnyv gqakskmler awrnpgditd iprieigksy ivtdnslida
      901 syfaiknial gyslpskwmk sigfdsarlt atadnvvlfn hlkgmdpqyn ftggtdfgyv
      961 pvrtisfgid itf
//
LOCUS       WP_118435491             991 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides stercoris].
ACCESSION   WP_118435491
VERSION     WP_118435491.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides stercoris
  ORGANISM  Bacteroides stercoris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Bacteroides stercoris"
                     /db_xref="taxon:46506"
     Protein         <1..991
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          4..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 ssaktlqisf vgmqtqdvai rpnvrvilks daeqldevvv tamgikrdrk algyaaqdln
       61 seqlnkagtt slasaiqgkl tgvdirqssg apgassqivi rgarsfdgnn qplyvidgmp
      121 vnttadfdtg ksvtganyad rsidinpedi esvnilkgqa asalygiras ngvivittkr
      181 gsknnmnkps vtistnlsaq rvsrkferqn iysqgnsiaa gydpsssmtw gpkiseland
      241 pkyggnmnnq ytaadgmreg qyynpkraqa gldgwttpqi ydnvgdflgt gftentnvnl
      301 sqsinginys fgvnnshqng iipstgmdrw garglvdwki npqwntgfsm nysstkitsa
      361 pgandgimnv vysapaeydl kgipnhepgn ptnqilfrst sftnpywwae hneylqhtnr
      421 afgntyleyq pdlglgenfs lkireqagld iwtsdyatvr emgstsslkg gdienygsqh
      481 nvfnnlftvn fdgkfgksde wrlnvilgne fnhesirnwd yygsnfnfpg ftnignatsl
      541 tsseykrqer tvgffgslsm swqdqvyltv tgrndyvstm prgsrsffyp svslgweftk
      601 lpflqnnkil nygklrasfa qvgqagnyya nyyytptygg gmysyypvty plpsgvstft
      661 pyyrvydeel kpqnttnyev gadlhffgsr lkveytyslq nvedqifyvp vdgatgyqem
      721 ltnagkmrth ahelsinaai lqakdfdlnl ginftkvnnk vielapgves imlggfvepq
      781 iraqagctyp niyglgfkrd eagnllllng lpqssgnsqd lgncspdftt gftlggrykr
      841 lslsttwswq qggkmyhgtn mtlnyfgatk eslpyhegsm vaegideatg qpntvevyka
      901 dyyqayynit esgvydtsfv klrdltltyq lpklgifdis iygfarnvlv wanlpnfdpe
      961 ssqgnnnmsg yferfsvpnt ssfgggltin f
//
LOCUS       WP_118435901            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118435901
VERSION     WP_118435901.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123805
     Region          25..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkivlsla clligiglai aqtpktvtgl vifeednqpi vgasvlikgt nqgavtdldg
       61 kftltnvpgt akilrityvg mqtievniks gtmkivmkpd aevleevvvt gmtkmdkrlf
      121 tgaatklsse dvkldgladi srslegraag vsvqnvsgtf gtapkirvrg atsiygsskp
      181 lwvvdgiime dvtevsadel ssgdavtlis saiaglnand iesfqilkdg satsiygara
      241 magvivvttk kgqagkshis ytgeftmrmt pryadfnimn sqeqmgvyke mkekgwlnfs
      301 dtyraaqsgv ygkmyqlmnt ynpvtgtfal ehtdtamndy lqeaeyrntd wfdalfsnsv
      361 mhnhsvslss gtekasfyas lsamadpgwy kdsevnryta nlnatynisk qlsinlissa
      421 ayrkqkapgt lsqsvdpvyg evkrdfdinp ysyalntsra ldsktmytrn yadfnilhel
      481 dnnymnldva dlkfqgelkw kpitglefsa lgavkysats qehlitddsn qamayrampd
      541 atvrdrnpfl ytdpdnpyal pisvlpqggi yqrtnykmlg ydfratgswn hvfaekhivn
      601 lfagmetnss drnktyfngw gmqytqgeip fytyqffkks ieegtdyysl tntrsrsaaf
      661 fanatysyqg kytvngtyry egtnrlgksr sarwlptwni saawnmheee ffeslkpala
      721 hfalkasysl tgdpgpntvt nstmvlksyk pyrpfaniqe sglkiidlan ddltyekkhe
      781 lnigadmgfl dnrinfaidw ykrdnydlig viqtpgvggq irklanvatm kshgveftls
      841 trniqtkdfg wttdfifsqa knevtdlesd aevidvvsgt gfalkgypvr glfsyqfqgl
      901 nedglptfid qdgnltsdgn didfqsqkld ylkyegptdp titgsfgnif rykgfklnvf
      961 itysfgnvir ldpvfsneyt dltsmpkefk nrwvlagees ittiptivtk rqsdtdnhlk
     1021 tlynaynyst eriakgdfir mkeisvsydf pkkwlekifi ndlslklqat nlfliysddk
     1081 lngqdpeffr sggvaapvpk qftltlrlgi
//
LOCUS       WP_118436619             942 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118436619
VERSION     WP_118436619.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105912
     Region          42..916
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiykglvl catlafayth taaqepladm leatqadtls kvqvafrsid qrdllggvsv
       61 idmkemseka ytsnslgfvd nvvggfngni wgnteylviv dgmvrdannv lpheidqitl
      121 lkgasavvly gpraakgvis ittkrgeigd lrinihantg fytpksypky lgsaeymtly
      181 nearandgla anysqedifn hasgsnpyry pnfdmyssey lkkaynrsea iaeisggsek
      241 vryytttgyy ressllkvgk tednyvsrff vrgnvdmqlh kfitaqadan vtfydsysan
      301 vdwwgqtatl rphlvtpfip lsyieatdqn slnavlnssy lqdgkfflgg tqqhptnpva
      361 dayaagdskf vsrqfqfntr fdvnlspllk glyfrakygi dyastynqgy snsyatfapt
      421 wsnyngedii ssitqygkde ksgtenisns ayrytynvsg qfdyqntfne dhnvfgmila
      481 nawqtqrsgh yhrttnanlg fqasynyqhk yyadfsvamp ystklptgnr vafsptvtlg
      541 wnlanekfle nsifdnlmlt asvgiinqdl ditasdnedg yylyktvvqk ggwyswgdng
      601 glaatefqrg nnpdmtyvkr keftaglrgs mwsnlinfdi nfftskmdgg lvrpgslypn
      661 yftqigypss siipyvnfnv dqrtgfdfsv yankkvgevd ltlgvsgmyy kstakkrden
      721 iefsylsavg ralngywgle segffrdeae itsaptqtfg dvkpgdiryk dqnndgkidd
      781 ndrvflgrwd splmsginlt vkwrdftffa mgnlylgghg mkdnsyywms gdskyseiar
      841 nrwtpetaat atyprltttn gannlrtsdf wiykndrfnl sqvqltyamp qnvlrgtfik
      901 glsffanann llmiakerkv lemnvgsapq trfyqlgfkg tf
//
LOCUS       WP_118437442            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118437442
VERSION     WP_118437442.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121516
     Region          24..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrlsvafl lligtftyal aanrqvegvv issednlpli gasvyvtadd lkkvgnnqst
       61 igvitnidgq fsisipegvt rfycsyvgyd vlevklipgk nkyditlqps ahmldavvvt
      121 gyqtverrkl taavskidis dqmmgatksi dqalagqiag lsvsnisgtp gapakirirg
      181 tsslngtqdp lwvldgiple gtnipnmevl kdidnigqta iaglnpadid nitvlkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs tkltyspkln idrlnllnse ekvgleldll
      301 asgypyretk gevyriisgl gelnnfkdgg wnalsssaqs tinklkatnt dwsdilfrda
      361 ftqeynlsls ggsekatyyt sfgymkengn vpnvsaerln lvmktsykvn silkvgasmf
      421 anrrknssyl pdsdgltnpi fysrlanpyf tpynehgnyn ydidvendvd mdfgfnpfee
      481 lknttnetti nglssifdae lrfddrfkft tqlglqldkt siekiadees famrkekknh
      541 rsngvtylpa ggfhkanens lsqltwkamg eyrdtyndih efeamvgtei rktweeklys
      601 agygfdrktl ttkpiifpee sqafklheka hvenayvsaf stlsysllnr ytlggsirfd
      661 gsdlfgvdkk yrylplysvs glwrisqepf masakwidnl vvrasyglqg nidkntspfl
      721 lgnyrienil pggsedmidv sgapnkklrw ekthsvnagf dfavlnqain lsvdyyyrkg
      781 vdligtqmlp letgfemltv nwasmrnqgv evalstrnvh tknfmwttnf nfaynnnkvl
      841 kealredale pgregypaga lfalktagld eegypmfqdk dgkavsamef fklqewgfga
      901 tdltarerre lytyvgtadc pytggfnntf tykafelgvn fsfdfggkvr sqptysivdf
      961 dkgrntnrdi lnrwtpente tifpvllsqn erldeymwys nqneiyrnld iwirdlnyvr
     1021 lknirlgytl ptnftrtlgm tsatvaiegr nllvfgssyk nyldpetmsn ayatpapksv
     1081 tlslnlif
//
LOCUS       WP_118437649             937 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118437649
VERSION     WP_118437649.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..937
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105574
     Region          40..936
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrkhktlkw gialvssmlt lnlsaqssli dyqsdkvdlg mgveqsqmlt tasvevvsgd
       61 elqktaaisl kealygkllg ltvlrpggtv sdyssgavfn irgqqttten gvlvlvdgie
      121 rsieyltvde vesvtvlkda aavallgyqg vngailvktk rgvegrqisv sydhkftfnp
      181 kvanfvdapt yanalnqarv ndglapmynd yelqafadgt hpyyypnvdw kkevfknygs
      241 edqfnlsmkg gnqklkyfsm ldytdsrgll dktdqeqyss qmrfskanir tnldvqftpt
      301 tkfvlnavgs fveikrpygv tengltdlly rtpasafpvm ndpegklagi wggnttygan
      361 nvvaqvrasg ftkshsrsfq gdfsliqnld fitkglsvsa rlgynnfsqi yetnalgfmy
      421 gyeryrfdea ghptelinys agdktnnltf dhwtnqhnrs sflevstdyh tsfrdddnfs
      481 asliwhqkns tyndqymtfn rmnvmaylhy dlqqkyvadl vlamngsnrs ypekwsfspt
      541 lslgyvfank ednrilnfgk lrfsagiqht dyvpiqglwl enyngsagsy ltglgdgswq
      601 wgtflgyqpt krfnletayk fnwgadlrlf kqvdvnfdvy yqlrddills gdglnsavfg
      661 rpsayvnwgr vasygvelgv nwvkqmnkdl sfnlgsnltw grnkqkrnie nvaydylsai
      721 ggrvsqawgl evvgffkdea ditaspqqnf dncrpgdfky kdqngdnvid endvvkmgyd
      781 tsvpelnfsl nlgfryknfg mnamfqgagm ytaylgtvgv wtpiidganl skeyynncwd
      841 rsetpvyprl tsrtnlnnyr gndvwyknvn ffklrncevy ymlpenwisk vkmsqckvfv
      901 kgenlmtlsn lkamdpenig tnfptlmgvn lgvsvkf
//
LOCUS       WP_118437499             910 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118437499
VERSION     WP_118437499.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..910
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100710
     Region          38..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrirnlfyl slfltvpglq avaqeklhvs lpdsittvgy atglrknlsg lveritenqm
       61 nkdqitnpld airgrvpglt ilkgsngpaa ldavrlrgtt slitgndpli ivdgvfgdls
      121 mlmsiypadi esfvilkdas etaqygsrga sgvieittkk gvsgrtsvny ngsfgiassy
      181 ktvrmlngde fravakergv sildlgnntd fqkeieqtgl qhnhhiafsg gtntsnyrvs
      241 lalmnregvi vneklqnfts nmnmtqyvfd nflkcdlgmf gsiqkernlv nlhkvfysaa
      301 afnptfpnhk npetgswdgs vlasqlshpl awmdvndkda tshistharl tfnlseawkl
      361 alfgsytynv iensqylpva vwaqgqaykg tkkmesllgn lmlsykkewr khffdvlgla
      421 evqkdqysgf yttvtnfsid glgynnlqgg alrpwegtns yyedprlasf mgrvnytydd
      481 ryiltvnarg dasskfgsnh kwgffpavsv awvvskekfm eklpfidnlk vragyglagn
      541 qngidsytsl nlirpngvap vgsspvvtmd qlknmnpdlk wevkqtfnag iemallgnrl
      601 lltanyynsk tkdmlylynv svppftyntl lanigsmrny gtelsigitp lktkdmelni
      661 nanltfqqnk llsldgnyqg ehisateyks lagldgagfh ggynhivyqi vgqplgvfyl
      721 phctglvsdg nggytyqiad lngggvsled gedryiagqa vpktilgsni sfrykdfdvs
      781 lqingafghk vyngtsltym nmnsfpdynv mkkaptrnik dqtatdywle dgdyvnfdyi
      841 tvgwnvplkn trylqslrls ltvnnlatis gysgltpmin sssvnstlgi ddkrnyplyr
      901 tytiglsvnf
//
LOCUS       WP_118440654             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola dorei].
ACCESSION   WP_118440654
VERSION     WP_118440654.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola dorei
  ORGANISM  Phocaeicola dorei
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Phocaeicola dorei"
                     /db_xref="taxon:357276"
     Protein         <1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 svvvkgttng titgidgdfs lsgvkkgdii qisfvgyqtv evpwngqpln vtlqddtqtl
       61 qevvvtalgi krekkalgya mqevkgdalv aaretnlana lsgkvsgvqi irssngpags
      121 skiqlrgsns vtglnqpliv vdgvpldnft gadnndmwnp stdmgnglsd insediesms
      181 vlkgasaaal ygsragngvi littkkgtks eglgvtfsgs vsvenvfmkp erqtifgqgs
      241 ngifnatsss nwgpaitgqs ytdwngrtqn mqyfdnvanf fktgvnlten iafsqqfdrt
      301 svylsatrmd dfskipgaey srtnlmsrit ssfgkdnrws vdakvqyils datnrpisga
      361 rsdnyfysmy mmpisldire fkqaknpedg kmywwekgsg qnpywakdyn tnqdkrnrfl
      421 lngslkyqit dwlnaeikag sdmyftetet klyagspsse ngrysfgeqk fyennfsflv
      481 taqkdrvlgd fggvftfggn lmerkstgvs nsvsaltvpd lfwltnstds nrsisqtyth
      541 rktnslygtl gvnydgwafl dltgrndwss tlsksnrsff ypsisaswvi sdminnrgkg
      601 mpewftyaka rvsfaqvgnd ldpyqlynvy gigsiyetgg tsasvsgstl fnedvrseli
      661 ssweagaevr ffnnrlgldv awyksnakrq llnlpmnsls gfssmkinag niqnsgveim
      721 lnatpvqtke ftwdtqvnfs tnknkiiela dgineytlgt ydnlkilava ggnygeiwgt
      781 tylrvtdens pyygkmllnd aglpqgdski qkigdqqatc lvgwtntfsy knftlsflvd
      841 ariggeifsg snrmlqangv aactvvngkr dkfvvdgvia dgnggyspst ievepqsywt
      901 avtgstgnmg igeanlydat nvrlrnvsln ytfprkmlak gpfqqvklgm scnnvwmihs
      961 nlhgidpesv fatstnatgf enassptsrt flfnvtlgf
//
LOCUS       WP_118441157            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118441157
VERSION     WP_118441157.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113066
     Region          8..1016
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdnfylfinq qfiilyssag tlvisfigmq sqevkikpnv nvvlhadsha leevvvvayg
       61 taskqsltga vasldakeme lrpvtqatna legaapgiqv nnsygepgsd ktsirirgfg
      121 singsnepli vvdgspysgn lndinpqdie smsvlkdass aalygnkaan gvvlittkkg
      181 ksnklnlrmn vkqgmytrai pqydklgakd wmeamlqgws sfyqkdagla padalvaaas
      241 tlnssvvrtk ifdkngadmf dangklvani lpgysdldwt dalqrtgyrq eygvsadaag
      301 ekydvfasfg ylnekgyiia sdfdrltarl nanfrptkwl ttgvtlsgts svsnfqgqas
      361 ssyyanpfyt gdmmapvypy yehnedgsiv tdengapvyd innydylsgr nilyelqnni
      421 nrknrntlng qvygtvkflk dfsatvrgnl ftynekskqf dnpncgdgaa nggrmavgnt
      481 rlfeyrfaqe lywahdfdrh hvdvllghes fknqinwdym mkeqmkvsgn temanfakmt
      541 sidgyedvyt tesylsriry nyaqkyffda sfrrdgssrf sspwgnfwsv gaswmisdek
      601 fmknidwvns lklrasygev gndagvnyya ykelyysdvn agigafykmq ipnanlkwet
      661 sgsfdialeg rlfdrfnfsv dffnktskdl lftvynplsa gatdwyasss ptgmsqyfan
      721 ignvrntgle vamdvdairt kdwkwnigln lttihneitk lpdgkdilng vqnyseghsv
      781 yefytytyag vdqmngraly nanpelgeat vnalksrgey itindknyvy ntsyaarewq
      841 gsalpdlygs intslswkdl tlsvlctysl ggkvydtnys slmyttsnga salhkdvmkg
      901 wtqvpegmte dspnrldpng tpqfdlssla stsygrssrw ltsasyftik ninlsynlpr
      961 nfvhklglgg isvygtiena aiftsrkgln pqysfngmqd ntfvgarvyt lglnlnf
//
LOCUS       WP_118441539            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118441539
VERSION     WP_118441539.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112838
     Region          28..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkyknlmwa claslaipag aqdadnnirg mvvdkwghpv ygasvmvkgm petrvetdkd
       61 gkfsieasag qqlnivsvdk gmttvkaegk slvkvvlnya gqsidvgagr tftrsestaa
      121 vstiynedfd krsaknvsns ligqgmgmmv lqnsgnyadv eptfyvrglq slssssplil
      181 vdglerdmsl lspeevesvs vlkdaaaval ygykgingai littkrgkyn skeirftydh
      241 vnnymdrkpe fvdastyaqa yneargyegl spryadkeve yfrngdfpyl ypnvnwldet
      301 fkdsgisnky tiefrgggsk fryysmldlv tdrgfvkegd mndgystqnk ysranlrtnm
      361 didvsrttkl kvnilgtlse slrpgasanl wdmiytvpaa afpikdedgl wggnnttwlg
      421 tqnpvaqsqg aayskghtrs lfaditlnqd lsavteglgf nfrlaydnys siwedhsqay
      481 qyggyvvsyd eltgplytht tageptemgk sasinnwarq fnfsggfdyn rtfgdkhdvy
      541 sqlkweyeyr dsyglnttiy rqnvswfthy gydkryfldl alvgsgssll apghkwafsp
      601 tvsaawvlse edfmnnaawi dflklrasfg iinadylpas dvydywdqiy tttgtrymfn
      661 saydstfgtt elgrlastny thergykynv gidatlfkgl nlsvdayyqr rnniwvsseg
      721 kytavlgqnp pyenagvvds wggefsldyt krigdvvlna ggsfnwnrne ikeqleeprm
      781 ydnlvqtghs lnqiygleav gffkdaddia nslpqsfgtv ypgdikyrdv ngdkvinsnd
      841 vtaigystva peiyytfhlg aewkglgfda qfqgtgrysa ilntksmfwp llstttlsth
      901 yyenrwtpdn qdakyprlst qsntnnyqtn tvwladrsfl klrnievyyn fpkswlqktk
      961 figdarlyvr gvdllcfdki dvldpesyga tnplnksliv glkvgf
//
LOCUS       WP_118441681            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118441681
VERSION     WP_118441681.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111781
     Region          26..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqilaltt lacmsmhama qeavdvtgfv idkagnpvsg aavsvvgvpa smvstdatgk
       61 ftisvlkddk lqiltstdav ktvnvelgkk mtivmdlste kvnygfnlnq tfaestgaaa
      121 tvysdkidnr ssytlgnsmy gnlaglttmq stgvmweqip smfirgqktl ngnngilivv
      181 dglerdnayn vlryltpeev esvtvlkdaa avalygnkgi ngvlnivtkr gkyksreinf
      241 sydhgftyqn rlpqmadayt yanamneala ndgksarytq nelnafksgk ypyyypnidw
      301 wdevyrergk sdiatltfrg gssklryftm lnlqngrgfi nnansndgfs tqekyskanl
      361 rsnldidlts ttklqvnimg tlnefsrpgl gsddligkly ttpaaafpir tesglwggna
      421 twtgwanpva ltqargyskg htlglwadmt lrqdlssitk glgasfrmgy dkvasywedh
      481 tmeykygsts vigwengeps nfsdyeagkd temaggskld wqyrsfnfma nvdwnrqfgd
      541 hkiystlmyt ykydnnvnin stlyhcnwsw ythyglkdry fldfalvasa snlletgkqw
      601 hlsptvglaw nltnedflkd sswlnflklr asfgiintdn ipyngywntt mngsgggypi
      661 qdnfgnggaw qegtlpslng ttekaykynv gvdatlfggl tlmvdgfyer rqdiwvstag
      721 knsaalgtss syanagivds kgveigadyt kkwgdfrfnl ggnfsftkni ikeqleepra
      781 ydylystgks vgqifgyqai gyfidqadid nspsqqfgev spgdikykdq ngdgvinefd
      841 qvalgynssv peiyygftlg aewkgigfsl afqgvghyts wttlaglyrp ltngntisqy
      901 yyenrwtsen pnaryprlst etvqnnqqss tvwlengsfl klrncevyyk fpheliskwh
      961 lntaklyvrg vdlfcwdhin qidpeslgng ipttrsinvg lsvgf
//
LOCUS       WP_118441808            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118441808
VERSION     WP_118441808.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116649
     Region          25..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkltlmla llfvwtgvaw sqgvtvkgvv tseedglpiv gasvlvkgtt qgtitdvdgn
       61 fmisgvkads ktlivsfvgm kskevaiknt pmhvvlksda evldevvvta lgmkrsektl
      121 gyaattmkse didagksgsv mgglsgkvag vqissagnkg tsqkvlirgi sslnnnsply
      181 ivdgvpidns tfrgsptdds sttdfgnaan dinsedvesv tilkgasata lygsraangv
      241 vmittkkagv ekltvtydgs ftaskvlrvm qtqdlfgqgw gswnrsengs wgprldgtih
      301 ewgsdqletp mtkpfsyveh nlrnfyqtgf eknnnvsiry gndkvgvvas ygnlssngil
      361 pnngdqfsrn tfslrgymni nkfsldmtmn yvrkdisrsn dmymellqha vdvdysqmkd
      421 ynderynldn yytfyatnpy ymidnyrsny qddrvygrve msyeimkglk atgrlggdfs
      481 nnrtnsqepk ttfsngsysq lggateslgy yseyrynrsq idatallnad yrvsdfsina
      541 vagwnlnqrs ygysggyvdg lavadwysly ntsssavsvt ykelrrliga faqaelgykd
      601 mmflnlsgrn dwsstlpagn nsffygganv sflitemlps lkehqvdflk vraalgqtgn
      661 danvykttsw yqianfkdin gyytsmpigg vmgmtsnntl pssslkpemt teyefglsgs
      721 ffgnrltvda syynrmtkdq iisaslapet aysyetknig kiqnqgvelm vnltpvrtkd
      781 wtwdlgftft knmsevkelw egtdeysytn wrgvyyvlkv gepvgmfrip aankvmdens
      841 pyygynivnn ngylsdsnte yeyvgsseak fnmgfnttlk wkgftlsasa dwrkggylls
      901 ntsyishfng nstqtvfner nsfiyphsvk vvngqyvenn ipvrademyn algnysyspe
      961 vrrhfiipkd yfrlrevsls ysfpksmlak tpfqqvslal vgrnlllftp kennyvdpev
     1021 snlgndllse fgettgtsst rnigvnvkvv f
//
LOCUS       WP_118441942            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118441942
VERSION     WP_118441942.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112125
     Region          44..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkieratqll flllisqggn aayanlprga saspvqvsaq ankitvsgtv vdvngeplvg
       61 vsvlekgtgn gtitdidgnf tmsagegatl eisyvgyqnl tvsaketlgv lvmkedteql
      121 devvvtalgi krsqkalsyn vqevkndvlt kvkdanfvns lngkvagvsi qrsasgvggg
      181 trvvmrgnks ikgdnnvlyv idgvpmgnqa drtgdgtgfg agrtssegia sfnpediesl
      241 svltgpsaaa lyganaangv ilittkkgaa gkvsvnvsss aefsnpfvlp rfqntygnvs
      301 geaaswgekl pvpssynpad ffntgttftn sfslsvgndk nqtyvsgsav nakgivpnnk
      361 yhrynamvrn ttkffndklt mdlsasyvre yynnmlsygt yfnpllgayl yprgenfeke
      421 kyferydael gynvqswtpg dfgmavqnpy wvayrnlrpe vkdrymlyas lkyeitdyln
      481 vsargrldnt ytekedkrya sthgtfakpl gryaysnetf rqkyadiman lskpfagdfy
      541 anvnvgasfe eydtkgrgyg gqlllvpnlf aydnvdpstg vpsqaggdnr kmnlgvfgsa
      601 eiswksavyl tltgradkps qlinskspwi fypsvglsai vtdllpetmr qsispvlgfl
      661 kvrasytevg spipytgltp gtithsiegg vikpfkyypl pelkpertrs yevgidskwl
      721 nntvslgvtl yksntydqll eaklsetsgy dymfvqagnv enrgieltlg ydqtfgnfsy
      781 stsltatanr nkiialasnv knpvtgeald lsdikvgrfr lregeevgti yaeerlkrdq
      841 dgyivynegq tittestepy klgsvnakwn lgwrngftyk gfnlnflvta rlggiviskt
      901 qavldqfgvs qasadardag kvmvgnvavq pkdyyesvvn ldaynvysat nvrlqeaslg
      961 ytfpnswfkg tpfhsvnlsv ygtnlwmiyn kapfdpelaa stgtfgqgyd yfmlpsqrty
     1021 gvslkfgf
//
LOCUS       WP_118443877            1198 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118443877
VERSION     WP_118443877.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1198)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1198
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=135212
     Region          130..1195
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqqitlle krtkkklvwm rtaflllvft atalqgwaqn aenrqislem kneplgsalk
       61 qfsnvsgykv nfpsedvapy rvtvsiyqma pfaalqkmle gkpfeydvkq nfitvrkvka
      121 tsttasgkfr nvggqvvdes gdplpganvk vlnspfgait daegnftcrv pvdvhtlevs
      181 fvgmqsekvs vkdrnnvrvi mhedkqqlgd vivtgyqris rerstaafgf vdseqlnrqm
      241 hsdlassleg qvaglrmnin sntgdmspil rgvgtfshdv gteplivvdd mptnlrlsei
      301 npynvesitv lkdaaaasiy galaangviv vatmrakkeg ahvsinadwf ittkpnfksl
      361 nlastsdiid yqtavfdanv aekgsaanfl ssfeynyynp lfqlyldqan gditsgevna
      421 tlrqwrnndy ykeyrdnawr taitqrynvt vsqkagnsnh llsfnyekds qrvisgksnk
      481 islyyksnya vtnwlnlnag vdvrmgrsyt pnsgytsytl qqryerilda dgnhytspyv
      541 nvdtspsyng svvrkaegvs pyrtfgfnvl daleesitks hdvsirpfvs lqarflkmfk
      601 ynfmyqyewn kgkselfese ntyvmrmlyn smvdtngkaq lpqggrfnqt eveskrytvr
      661 nqidfdktwk dhavtaiagl efrenkiptp arqllygydp qtltsdfmnw qtyrdgvgts
      721 alsgrtitls glsatlhesr hryasfyana gysylsrynl sgsirwdqad lfgldirnqr
      781 hplwsigasw ilseesfike iswldylklr mtygingnvd qssttyfvvk kktqsnpikt
      841 tyltyedddl pnpklrwekt atynigldfr lfknlisgsl eyynrhssdl lvrrymdptl
      901 gagsrvvnng emrnrgvels lttniirkkd wnfavdfnfd ynknkmlkvd hsesdnarvf
      961 iaspqvyfme gtsyntlway rihriengyp vavdkdgndl vkfnedgtva nitsgsslkg
     1021 tddlvnlgsl tpkfsgsvgl rfnyknfdln affvyaggnk lrnsvlkmdd qlgtqtlkgi
     1081 anrwtaddsn aqvrmyldip aqvktyastf qdwwqygdin vkdagyvklr slsvgynlpf
     1141 tvcqhlrlss lkvkvqvnnl ftwckagsdi dpesygmndg trgiaspkty siglstsf
//
LOCUS       WP_118443653            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_118443653
VERSION     WP_118443653.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119161
     Region          25..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnkwllsl sigllccgsa yaqttvkgki tseggeplig atvavknstd gtvtdidgny
       61 slktkktltq kdllvfsyvg yktlqknyag ntmnvklaee sqqlndvvvt algikreekg
      121 lgyatetvkg dmitsalptn wstalngkva glsvissggp lnssrislrg dvslnqngnd
      181 alvvvdgvpm sspmtnpgva ygagsnsels vdygngfsdi npddiesiqv lkgasataly
      241 gtraangvim vttksgagap kgigvsysgn fsiddvmrwp dyqyefgqgl psnigpagsi
      301 yegqpyysyg kaedgsyast sgtssaygar fdvnrlfyqy dpvtqgrasv atpwvayknn
      361 rkdlfqtgyt ltnsvaltgk sdrgsvrasi thtknewilp ntgfqritam vsaqqqisra
      421 lrinfkssyt yrklnntpal gynsnsisyf lifqnpnvnl dwlrpmwrtg qenvkqlqpy
      481 ssfignpyvi lyesenpsek hsnvssvsan lrinskfdfm irsgiqlsad qreqhrpisd
      541 vvfgngffkk qnvfdyelns dalftyhdsf anglrvnasa ggnmmqqsyd mlaasvvgli
      601 tpgvyklang vsnpnvqtvi kkkalnslyf tanfsykdkl fldvtgrndw sstlpksnrs
      661 ffypsvnvsa vmnewftlpe qisllkvrgs laqvgndtdp yktspyygts dfpgsaivss
      721 tlynqdfkpe istnyetgfd frmfhnrigl dftfyynrtk nqildapmdp ttgyskatin
      781 sgcvrnrgye iqldvtpvvs rdfrwnatft wsknenrils laegadenql issigsvsii
      841 grvggttgdl wgyklvrdpe gnvvindngl persgeieyv gtaypkwkag lynefsyknf
      901 tlsvlldgqv ggkmyshshh kmteqgklqh tlngrlpgte fymskddpri aaaglspqdg
      961 mymiapgtvk nddgtyspnt kvvtvesyyk eyyrmanvet ntfdtsflkl remrleyklp
     1021 nstlkktpfs kasvalyarn lfcitdyplf dpesaalngs smvtgvetgs lptartfgln
     1081 invsf
//
LOCUS       WP_118448145            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Butyricimonas].
ACCESSION   WP_118448145
VERSION     WP_118448145.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas
  ORGANISM  Butyricimonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Butyricimonas"
                     /db_xref="taxon:574697"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113961
     Region          42..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvdlvfgfr gklcdvvkws llfccvcfse ipvagesrss livitgevkd adgeplpgvt
       61 vvlkgtswgc atgmdgkfrl efpeqqemvl lfrfvgmknq evtvtgtryi rvtmvkdmke
      121 lddvivtgyy tqaknaftge itrikgedll rvsptnllqa lailtpglri venneagsdp
      181 nvvpeilirg assimtkgqe gvnaplimld gveisvedly dldiydieqi lvlkdasaav
      241 lygekaangv ilvervrgks nkprfsynft pmfsfpdlts lrlcnaeekl elerlaglyd
      301 rvdgsldpay dyklenirrg vntdwatkpl rnafthshsa tmtgrgggie ykvtgrlsdt
      361 ygvmkgdyrr nygvnvslsy rfardvvaty qlaytmtegk nspygsfaqy trlnpynpvy
      421 dedgkyirny yfdpvnqtme rqvnplynat lasfsksqnk avtnslslrw dvnealfitg
      481 nvsvrqgdaw nkvyvspeda sftlqeipqn kkgtymalst ektdwagklv lnyrlplnee
      541 gnsilslsag tdigkdksss mqvkaegfmk dkmtdikfas qyattrpvgg ekesaevgff
      601 vngsldllgr yfinasykta gsskfgskhr fapvwsagig wnlheerfmn fdwlnvlrlr
      661 fsvgstanvt ftpyqaltty lydpdlihyg gmgavpitmg npdmkwqvtr kynwgltatf
      721 wkervnveas yyvnktkdal mpltlpssvg vssvlvnmgk lqnsgyefsi saqvvkrnnl
      781 lgmvmvngsh vfdkltsisd alkaenmaay ygvkpqpmfv eggsqfgiya mrsagidpas
      841 gqevyikkng nytftydkne rvevgntnpm legslftsls yggftlnvta aykfggdiyn
      901 ttlankveyi dpygnvdrra fterwkkpgd lvrflgipen vsdenryser fverdntfai
      961 tsimlnyefk pgylrkigik rlnlgigvad iarfssvkqe rgteypfqrs fhitfrptf
//
LOCUS       WP_118448255             910 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118448255
VERSION     WP_118448255.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..910
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100958
     Region          24..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrirnlfcl slllvavglp avaqtklhva lpdsittvgy atglrknlsg lveritenqm
       61 nkdqitnpld airgrvpglt ilkgsngpaa ldavrlrgtt slttgndpli ivdgvfgdls
      121 mltsiypadi esfvilkdas etaqyglrga sgvieittkk gvsgrtsvny ngsfgialsy
      181 ktvrmlngne frtlaqergi sildmgnntd fqkeieqtgl qhnhhiafsg gtntsnyrvs
      241 lalmnregvi vneklqnfts nmnmtqyvfd nflkcdlgmf gsvqkernlv nlhkvfysaa
      301 synptfpnhk npetgnwdgy ayasqlshpl awmdvkdkna tshistharl tfnlaeawkl
      361 tffgsytynv venaqylpva vwaqgqayrg dkkmesllgn lmlsykkewr khffdvlgla
      421 eiqkdkysgf yttvtnfsnd klgydnlqgg airpwdgtns yyedprlvsf mgrvnytydd
      481 ryiltvnarg dasskfgsnh kwgffpavsv awvvskekfm eklsfidnlk iragyglagn
      541 qngidsyttl nlmrpngiap vgstpvvtmd klrntnpdlk wevkqtfnag ievallsnrl
      601 lltanyynsk tkdmlylynv svppftyntl lanigsmrny gtelsigitp lktkdmelni
      661 nanltfqqnk llsldgnyqg ehisateyks lagldgagfh ggynhivyqi vgqplgvfyl
      721 phctglvsdg nggytyqiad lnsggvsled gedryvagqa vpktilgsni sfrykdfdis
      781 lqingafghk vyngtsltym nmnsfpdynv mkkapaqnik dqtatdywle dgdyinfdyv
      841 tlgwnvplkn trylqslrls ltvnnlatis gysgltpmin sssvnatlgi ddkrnyplyr
      901 iytiglsvnf
//
LOCUS       WP_118448434            1175 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118448434
VERSION     WP_118448434.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1175)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1175)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1175)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1175
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133082
     Region          49..116
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          128..1174
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maillskkrs idrnvsrriv kmfliqfvfc lcfftsiasg vtqnrvvnld fenvelskal
       61 kslseaanck fvfnyddlnn ykvsaklenk sveecldill arvpfkysqe gelivisyks
      121 ndekkiykvr gvvkdetgmp lpgvaviqkg ttlgvatdvd grfefqltek nvtlvfsfvg
      181 mktkellydg sdklldvtme eevemlgevv atgyqtisre rstgsvtilk aedlrkvqgt
      241 slvskieglt pglstygdkl emrgtssfav sstpllvvdg ivmnqglnsi npddvetitv
      301 lkdaaatsly gvrasngviv ittkkgksdk vnfdlsagfy inplpklsym dyastsdiid
      361 felefllnnd lykqnpgdyf ddknqttssk pytrieryyy elykgnmtqa qvdekvnamr
      421 kndyrkeark lmsetaltqn ynlsiskgge ksnlyfslry edngkylksd aasqysiylk
      481 nelnltdwft ltygantyia kmkesmsgis yldvmpyekv ltdegnpvyq ygynfyrsie
      541 ideteglefm gfnlneernn nmqktnslyv rlfadadfkl wkgldlgvkf qyerkninik
      601 qfdeadsykm relvnrytsg svgnfvynlp qgghlsennq neeyfnfraq lnyqttmgek
      661 hdltvlagae irqdewngtm serygyddkk ltykqvdwat laqgvvgqls sasltfserl
      721 qvtstkhryv sayanagyty dskyslnasv rveqadlfgt dpkyryrplw svgagwlmtr
      781 esflndiawl dmlklrvtyg itgnvdqsss pyllgayits pytqnsltsi ltppnpmlrw
      841 ektstlnigt dfsllgrlkg slefyrryss dllanktldp slgfesarvn ngamrntgle
      901 islsydwlnn kewalnttlt aannknkimk vgftpsnald mlrypgsnyl kgdtynsiya
      961 yryaglteng dpsvydenge ikanepvrni nalvnvgqlt pkwngalavn lrwktwefft
     1021 kfvyytghsl rndvtplyst ygslqststy gsingamhkd mvnrwtesnk dtdipamrsa
     1081 tsadsdrenl wryadshvls asfikcrnig vsysfpknll qkinlqnvvi raqvdnpfyw
     1141 aandegidpe sfnanegtrt qfmmptysvg lninf
//
LOCUS       WP_118448442            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118448442
VERSION     WP_118448442.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116209
     Region          52..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktydrkvf krkllsdrrt vtvtirlfmi lllffplltr agtvdstrvg nrevrgkvvd
       61 enklpipgvs vrlggtsmgt atdvdgkfkl fvpadtatlv vsfigmktev vkiprlkagv
      121 eqkeltivlr eedvkledvv vtgiftrkke sftgsastys aaelktmgtq nilqslktld
      181 pafailednq fgsdpnrlpn meirgkssml glrdeldadp nqplfildgf estlaaindl
      241 dinrvasiti lkdaastaiy gskaangviv vetvkpeagk lqvsytgnmn lsmpdlssyn
      301 lmnareklef erlagrfepa swsttsevel nrlyneklkv iesgvdtywl aeplrvgvnq
      361 khslyvqgge gnflfglgag yngvsgvmek sdrdvisgni dliyrmskfq fsnkfsltst
      421 dyrnpivafs eyaaanpyyk krnetgtiek wlennnffka anplwnasqn srdegknlal
      481 tnyfmaeyfp tvewrvrarl gltygnddte kfysrndtrf enmetikkge yrssntrtnq
      541 vegelsvtya kvlgkhrinl vvggnvssnk sltqgysavg fpdgdfsyps fsngypengt
      601 ptyyesvsrs vngyfntgys fddrylmdfs lrtsgssvfg tsrkynttws vglgwnlhke
      661 kfimdhvgwi dllklrasig npgnqsfdsa qslltysfqy gsmnyfglga vlaqignpdl
      721 ewqitvdkni gldvtlfnkr fsltadyyyk vtdpllikvs tplssgtety mtnageqvsq
      781 gltasvtyyi fqnfeerfsw miranvrtqk tridkignkl stlnssgkgs ntvryydgad
      841 pddiwavksa gidpsngkel fyakdgsyty dfsyddevic gntrpdvegv igsslnwkgf
      901 svslnfryqm gadvfnealy skvenisrsd lnknqdkral yerwqeegdi vrfkniasae
      961 ttpmssrfvq eenvltlesv ylgyefydgw ikklglsslk fqvsmrdvfr astirsergi
     1021 sypfarsmea glsfnf
//
LOCUS       WP_118449408            1158 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118449408
VERSION     WP_118449408.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1158
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128108
     Region          69..120
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          133..1156
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknssipka gfrlfrpdpr mfgklfalfi fmtfctysyg vsqnkkmdvh fnnasidfvi
       61 eylesatdyt fvyndtdkeg ikisvslkda divtildavf kdtplayqik edrivvlrrk
      121 nntvkaeeek qlvvkgrvis ekekapiiga tvilegttlg vatdvegefs invpkdaktl
      181 iissigyvky rfslnsnvfd klniiqlkds vsfvdevviv gygttkvkda tgavsrlgek
      241 diamspagas vqsmlqgrap gvnvmiqsas ptspvnvmir gistltgntq plwvidgvpd
      301 ysqsstgdvt nalfnlnlsd iesidilkdv sataiygsra angviivttk rgklgmqptv
      361 dlslragiqt insnklnaln aaeykrfvet vgrqsieiag fdyntrlffn eskfnqlnts
      421 qwdgsmlell pdafmdgdtd wwdemtqnal ttqcdisvrg gtqnsnyfis fgyndqkgvv
      481 kggrsklltg rlnfetligk qvklgvnlsg ssrktnnkdn lidniirfrp dfpaynedgs
      541 inlvttstvi enphltlanr ndgrgltfsg saflewtild glkfkstgtv nytnsqtdvf
      601 skkgtrgyat aynsrnlgns enntyvwdnt ltwmktfgkh nlvamvghsi ekyksrmlsg
      661 gaeefpdeev linlgsgads wadsdeagnt lvsaiarvny kynnrylatf tfrtdgsskf
      721 gpdkrwgyfp sgalawvise eefmaplkly ipylklrasv gkigsqnlgn ydyislmgaa
      781 sydgqpgtkp tslgnpvlqw eettsidvgl dfgllnerlr gtigyynkqi nnliydgsvp
      841 anssyttvnq nvgtianvgw efdirgdvir tdkvnfeigf niatnsgkvk kldgivkelk
      901 mpyyyeyvrl vegghigdwy gykyagrlfr tqeeiialkp vsstgvqeny fgsynspgda
      961 ylidqdgdgk itakdkvklg nfnpkffggf nlslgwknly atavftysyg akrmwyyqye
     1021 ktsgvgtynv ynsifdsynf kggdalfprl ayagtvanal cdlyihdasf lrmnslnlny
     1081 rlptnwftgt fvnnvelsfs asnlftitky pgfdpqgnfg ststsatand vitvaqgvdy
     1141 stypsartys lgikftfk
//
LOCUS       WP_118448822            1197 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Butyricimonas].
ACCESSION   WP_118448822
VERSION     WP_118448822.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas
  ORGANISM  Butyricimonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Butyricimonas"
                     /db_xref="taxon:574697"
     Protein         1..1197
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134684
     Region          131..1196
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknwdllln fwqyrkskff lrmkismill lvgvmhlsan tfsqtkvsln mkdatvqevf
       61 snlekmtnyt flykldlvnk cgkvnvdatd qdfsqlllel lnplglsfti ddqvvvitas
      121 kakddvkkel tikgrvfmkd stgvpgatvi lkgtstgvit nmageftiti pytespvlif
      181 sflgmktrev ryvgqkemmv lmeedvkamd evivtgyqri rksdmvgstn svkredlffn
      241 gtnsieqmlq gklpgmvvmn tsglvgkrqk vrvrgtstll gnqepvwvvd giiqedplpf
      301 ktreldalgn isqdnfdmvk dfvgnaiswl npndieditv lkdasatvmy gvkaangvil
      361 iktkqgqagr msvnysgdis itprltyekm nlmnskervd vsreiyergl tsdnrplesi
      421 gyegalgryl akeisydefn devkklestn tdwfkllfrn svsmnhslsi sggtdkisyy
      481 gsvnatinrg tsignestsy saaiginakf gekvnlglri ngstsetdgy yqvdpynyas
      541 ttsrvipcfe ngekffykdk sgylynilhe ismtgntntn rsmgvsasfr wdiltglqfe
      601 stfglntsni vgesyadeqs hyiteirkye fgtqrpaddl yqrsplphgg elnttedrnf
      661 nytwrntlsy nyvlaekhrf slmvgqecrs nkydgvasti ygyfpgrgks vslpptiikn
      721 qngedqrndl ldkyktvvtd rksnyigyfa sftygfdery iltasfrsda snrfgqdtrn
      781 rflpvwsigg rwnvhyepwm qnqqvisdln frvsygwqgn vaenygpdli arigsgteti
      841 dqnrtgeymm fikslpygnl rwektktinl gtdfglfqnk itwtieyynk ktedmiveke
      901 vpyaygvtsm pinggsmtnq gievsvgftp vrtnnftwsm sinssknfne vkstvnenen
      961 wraaasgsln kagyavssfw afdfsglnpk tgsaefnips veenpagqtd attfmkymgt
     1021 lepdftggvs msfrykslsl sssfnlqigg kkflyevfde sivtstpsay vnlpkeltkr
     1081 wrkpgdetft dipalsstea syyklpngas eyaprlynys dvrvvnasfl rcnalslnyt
     1141 lpekwvkkmy lknlsfsasv snpfiivske fkgmdpevat gsqpisrtys fginvsl
//
LOCUS       WP_118449749            1224 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Butyricimonas].
ACCESSION   WP_118449749
VERSION     WP_118449749.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas
  ORGANISM  Butyricimonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae.
REFERENCE   1  (residues 1 to 1224)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1224)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1224)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1224
                     /organism="Butyricimonas"
                     /db_xref="taxon:574697"
     Protein         1..1224
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=139018
     Region          127..1223
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknrtirwp gtiwpqeigk mmklvvvifl tlgglsvsah tsaqqqhvtl dlkectvmel
       61 fqaiqqqtdl ffvynhrnfe higklnvqak nekvevllkr vfkdskldfv fneqtviikp
      121 qennkavvqg iirdkdkspl pgvtiiikgt ttgvtsdkdg rfklvlpsfr ettlvfsfvg
      181 mktreivwkg epelhitmee eatqmdevvi tgyqtvdrrk stssvtsvkm edlnipgvss
      241 idqmlqgqip dlifmsnsge vgvvpklrir gtstlignre plwvldgivm qdpvdvpasd
      301 lndpdyinri gnaiaginpq dieridvlkd aaatalygtr aangvivvtt kkgrigrpiv
      361 nynltttfrq rpsyndrain vmnsrermqf srelvaqhyp fpddinmvgy egllnqlynh
      421 eltdeqfeke verlsvintd wfdlltknsv shshtisisg gsseatyyas igytrdndvv
      481 wdsnneryta tmkmntnlts wfnaslnvng nvstrqyyqq elspmdyayk ttralpayde
      541 ngeyfyfqkr kwgtispeyy rynilnelen ssynqrgsal svtanlqfsl inwlkanvia
      601 syqtsntiqe swwgeqtnya aklrgteygv lpaprtegep dylgnptytg gtsllpygge
      661 lshnqsdnhs ytvrlqldgn ysfgksdqhn ingsigfems strnrgysrt ergyykdrgm
      721 sfvndidhek fpdyaqwvlq nparmtdgks ntissyasis ysyynyftvn tnarvdgsna
      781 fgdqsndkll piwsasanwn iselpglket kwldflrlka sfgyqgnmls dqspvmiisk
      841 eplnshfgen vasvsrypnp nlkwetttsy nlgmelglfq rkvmieaeyw wkhtedafmd
      901 ksiammngvp ndiyqvnqgd idnhgynvsl tfmpyqsqdw fwsvstsisk tfnkmkskvd
      961 vdqyelsnfl ngsalvkgkp igtfysykfi glspvnggpm fddyadnpei lrglnkydty
     1021 trvltpsgrr eptisgnlnt tlrwknirln gnfayslgnk irlfaiynaa sdavmdaqni
     1081 rpennvskff lnrwrkpgde rhtnipaiig kgddnyslye rhwsdkyqdi qplatsvwem
     1141 ydygdhrvvs gnylkcsnlg ltyqftetml kklrlsrldv sfsatnlfti sakelkgqtp
     1201 tqggfasiql sdrptytlgl tvsf
//
LOCUS       WP_118450743            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118450743
VERSION     WP_118450743.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116219
     Region          52..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktydrkvf krkllsrrma vivvirlfmv lllgfpvlvn agtrdstrle srqvegkvtd
       61 ekkvplpgvt vrwegtsvgt atdaegrfkv lmpvdsatlv vsfigmktvr vkipklkage
      121 vrkvlsivlw dedvkledvv vtgiftrkke sftgsastys aaelktmgtq nilqslktld
      181 pafailednq fgsdpnrlpn meirgkssml glrdeldadp nqplfildgf estlaaindl
      241 dinrvasiti lkdaastaiy gskaangviv vetvkpeagk lqvsytgnmn lsmpdlssyn
      301 lmnareklef erlagryepv nwsttnevvl nklyneklkv iesgvdtywl aeplrvgvnq
      361 khslyvqgge gnflfglgag yngisgvmek serdvisgni dliyrmpkfq fsnkfsltst
      421 hlknpivafs ayaaanpyyk kyneegtvdk wleyndyfka snplwnasqn srdegknlll
      481 snyfmaeyfp ttewrvrarl gltygnddte kfysrndtry envettkkge fysnnvrtnq
      541 veaevsvtya kmlgkhrinl vaggnissnk slsqgysavg fpdgdfsyps fsngypeygt
      601 payyesvsrs vngyfnagya fddrylmdfs lrtsgssvfg tsrkynttws vgvgwnlhke
      661 kfimdhvawi nvlklrasig npgnqsfdsa qslltyafqf gsmnyfglga elsqvgnpdl
      721 ewqitvdkni gldvtlfnkr fsltadyyyk vtdpllikvs tplssgtaty mtnageqvsq
      781 gftasvsyyv fqnfekrfsw mvranvrtqk nrideignkl stlnangkge ntvryydgad
      841 pddiwavksa gidpsngkel fyakdgsyty dfsyddevvc gntrpdvegv igsslnwkgf
      901 svslnfryqm gadvfnealy nkvenisknd lnknqdrral yerwqevgdi vhfkdiasae
      961 ttpmssrfvq eenvltlesi yvgyefydgw ikklglsslk iqasmrdvfr astirsergi
     1021 aypfarsmea glsfnf
//
LOCUS       WP_118450604            1146 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118450604
VERSION     WP_118450604.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1146)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1146)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1146)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1146
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1146
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128805
     Region          127..1142
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrsrikncml ggskrslvck lmmmmlllth lafssenafs qqsitvrfeq qtlsevlnvl
       61 kqktgyefly ndeeikdvtg itrsfsnasi qdilnscltg tkytfkmvdn livitpdnkk
      121 devkkvtvqg kvvddrgttl pgvtvllkgt avgvvtdidg kfkielpkrd tmilifsfvg
      181 mksheldvnk ikdlgkevsi kmfpdtedle evvvtgyanv kkesftgssi svkredllka
      241 satnvvqala sfdpsfriqk sniwgsdpna vpemyirgrs gigvkgldkd alsksslenn
      301 pnlptfimdg fevsvqkvyd ldpnrvetin ilkdaaatam ygsraangvi vittrapkpg
      361 evtisynltg slslpdlsdy nlanarekle iekaagiyep engyyanrad airaynerlv
      421 nvqkgvntdw lslplrnavn hkhslsiegg nvdlrynlel gytnengvmk gsyrdnvdvg
      481 ftvdwrlkdk lqvlnkisyn ftdapdspyg sfsdyahlqp ydrlydddgi lvqalkfsqe
      541 rgggkslnnp fyeaklnnyn wnkqdeiieq fmfqwfindy ltlkgqlalt ktmgrterfi
      601 dpkssnatar tansstsans sllgdlyrtd sdatkwdtqf slyysrslgl hnlnisaivn
      661 aqstksests ahyrgfpsga fhspnyaaei yqkpaksesl krlmgfllsa nytwndvyla
      721 dlsvrfdgss efgsdqkwap fwstgvglni hnygflkdnd minqlkvrvs ygqtgkvnfp
      781 sysaktvyat ndrwyatgfg tqlkalgnhn lkwettnkln igtdlqfwne rvslnfdyyy
      841 nktvdlitdv slpasagfts ykdnlgetln kgfdiqvrfd vykdkdwnvs lwgnlnhnrn
      901 eilkisdalr aynervneky aaaedaqgna nlskygteys epemkyeega sltsifavrs
      961 lgidpmtgne lflyrdgsvs slwkatesvr vgdeepkasg sfgvnlsykn ltlfasfayd
     1021 wgkqtynqtm vdgvenvdik nsnvdrrvlt qrwqkpgdva plrnikdmnt stmptsrfvq
     1081 ddnelslsal tlsydfntdw lkkirlkmlr lelstndlfr astvklergt sypfartfnf
     1141 slratf
//
LOCUS       WP_118450868            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Butyricimonas].
ACCESSION   WP_118450868
VERSION     WP_118450868.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas
  ORGANISM  Butyricimonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Butyricimonas"
                     /db_xref="taxon:574697"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125407
     Region          25..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslllial lcplwlfaqs esdyrtikgv vmdsvtnetl igatvmidpd aaeaknlgpk
       61 gtitdfdgkf elkvpkavky vvvsfvgykn akldvtktte fkvmlqpdqe qltevvvtgy
      121 qqiekrkvts aiqtvkmddi krigvasidq llegqvagmt siptngapga pnkmrirstv
      181 sltgstdplw vldgmilegn dipanfsdkd nidnlyntsi agvnpadied itilkdaaat
      241 aiygaraang vivvttkkgk agkmrvnasg svfyalkpdl dklnlmnase kvdfelglaa
      301 qknltyrsdy gsvarilnky gqletlqnng fdaisteaqn einklrksgv dwgdevyrna
      361 lnqqynlsis gggelanyyf sagyyneegt trgtgferyn mtmktdfnll enlnvgvslf
      421 ltdskrksyv tdteaftnps nytrmvnpyl evkdengdyi ydpdildndg rnlefnfiee
      481 mkntsyslkn rsikpmitld ykvtswlrlf tqfsmqlens ktekiankns yfvrkykeks
      541 kytyrpsdgs psetryflpd ggviqywdnd mtqyqwklqg efakyfgefh svnvmaglem
      601 rgnkttnvht kgfgydpnsl ttetlvipdn tnfqndanfe qysksftedr flsyymtasy
      661 tydnrytmfg slrydgsnmf gverkykylp iwsisaawna drenflqnad wltnlklris
      721 ygiqgnvdkn tsplvvgewg ntsvlpggse pnigvtnppn pylrwekttn wnvgldmgvl
      781 nnritfsida yhrvssdlig tralpgengf dyapmnwakv tnkgvefsls tvnvktkdfr
      841 wvmdfniahn kskinsietp dnsylpsgeg ysigalfalk tagldengip mfwkdgqkvs
      901 fsdfyglevn hdlfgdatls sklsnqeyrd lftyvgtsep kftgglinrf yyknfdltis
      961 gsfiidqtvq etpfydpsqt spgqnyskrm fdvwsssnpn gkypallgkt medgslnmaq
     1021 qwislkdpgn sfrnydiwfk qmsyfrvnsi rlgytlpsdi akklrlasmr vsletrnpfv
     1081 igtsykgyfd petygsiyaq plaktfscgl dltf
//
LOCUS       WP_118450914            1124 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            sp.].
ACCESSION   WP_118450914
VERSION     WP_118450914.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas sp.
  ORGANISM  Butyricimonas sp.
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Butyricimonas sp."
                     /db_xref="taxon:1969738"
     Protein         1..1124
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126456
     Region          128..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkfmkhqkl qfkpgsfrln glfrvvflic cllsagltqa qekkitaefk dtplsnvlkq
       61 leklstykil ftyddvqsyk vtvslkdati tealqkvldg kpfvfsdvan gkyisvvyqp
      121 kkksdttkei kgkvvdskge tvigatvrvv natigtatdi dgnftlrvpe nvttlevgfv
      181 gmktqlvsik dktevrvvme edntvledvv vtgifkkake sytgavssis seqlkmykgq
      241 nvlqtlknid aslnfmvnna mgsnpnnvpq inirgnsslp msvqeynesi kndvnsplii
      301 mdgfeitlek lmdynddeie sinilkdaaa taiygsrgsn gvivvvtrqp eagklrvnae
      361 igmdieapdl ssydllnaae klqlekmagl ydtdfpgndv kyserynkrl kavlsgvdtd
      421 wlskplhtgv gthynlrleg gseqfrwsga layknvvgam kgssrrnfng sivlmymmdk
      481 ltfknytsyg mnrgresryg efstyaqqqp ydapydengn lvryfdgfqy nnldkqnply
      541 daslnsfdks gyqsltnnfs iewdiieglk lrgqlgisst dnssdyflpa ehsyfttgdq
      601 kaeyatdegf frrglyrygt greysysgnv tvtynktfae khllsvgvdw slaetqsrsy
      661 sfelegfsse dmsflgnarq ymkdgipsgt ktstrrfglt gnvnyiydgr yyvdlayrvd
      721 gsstfgsdkk yapfwstgig wnlhneqflq ghpvlttlrl kasygetgsq qgsstgastt
      781 ykystdnkym nwngtilqgw gnpkltwqkt defnvgmefg lwtgrvkgei nvyakktanl
      841 lsnmdlplsm gfssyianvg evenkgweas fsgyairnpe rrmnlmfsgq lvynknkitr
      901 lsdaikaqne lylqedvdvs nlfyegrpqn aiyavrslgi dpstgneifl dkngkitdtw
      961 kpsdkvylgs kdqkyrgngs imfmwkgltv nvacsyywgg kvynetllnk vevtkntlst
     1021 qnvdarvlks rwfqagdvtf fkqlsntqtr atsrfvmddn vfeissigvq yrwdtpwiqk
     1081 ytratsitfg vnmsdilhls sikmergtsy pyarniqgyi kflf
//
LOCUS       WP_118450941            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Butyricimonas].
ACCESSION   WP_118450941
VERSION     WP_118450941.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas
  ORGANISM  Butyricimonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Butyricimonas"
                     /db_xref="taxon:574697"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115553
     Region          52..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mcvrvfvlll cllsiqggrl fagkrkcfpe ilrvdslvre ekcvvvkgvv cdaqgeaivg
       61 vniiekgtmn gvttdrrgkf slevdlhgtl ivsfvgyrtr iipvegrtdf vitlehdyil
      121 lddvivtalg lqkkesalsy aaiqvdkdel irvknpnmiv almgkvagmq vnrsfsgmgg
      181 avkvvmrgnr svagnnqply vidgvpmlne sseqpytaig gtadagnrda gdgisnlnpe
      241 diesisilkg apaaalygtq aangvilitt kkglagkqev aftssvafdk ammlpklqnh
      301 ygmsdeiesw gerenittgn pipsffrtgv taihslsfmt gnervqtyfs yantmgkgil
      361 gkhelskhni nfretatfye grlkidgnvn llsqhvknrp vpggfymnpl vglyrfprgm
      421 diteykehfe vwseerhlnv qnwhaptedf eqnpywiqer itsrdqrtra ivslalnlki
      481 tncfsvqarg nvdyvndkfr qkyyastapa lagnngryid sgneqeqtyg dvigtykgkf
      541 sdfsldvslg vsisrkkane lrydsktasl kfanvfnian inmntsayis eqidairemq
      601 slfvttqigf rdylfldvsa rndwsstlay tsresrgffy psigvsclmn rvlklpeqvt
      661 sgkvrvawsk vgndiplyit npvahvlagg giqasdaasf eemkpemsls vevgtewkff
      721 dsrlhidfty yqthtknqff klpakdgdey ayryvnagni qntgvelmie gtpveiknfs
      781 wktginyafn knkvvrlhae lpvfqygpyg fsssyamklk kggsfgdiyg kafkrdtdgk
      841 ilyetdgerq glpmiegdgn tvkvgnanpd ftlgwtnafs wkglelsllv dgryggkvls
      901 qtqadmdmyg vtkvtgdard rryvilegek itnvkgfyks ivggragvte yymydatnfr
      961 lrelalgytf pkrwmeatkf frdvqlafta rnlffiykea pfdpdlilst gndnqaievy
     1021 gmpttrsmgf slrvmf
//
LOCUS       WP_118451093            1144 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Butyricimonas].
ACCESSION   WP_118451093
VERSION     WP_118451093.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas
  ORGANISM  Butyricimonas
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Butyricimonas"
                     /db_xref="taxon:574697"
     Protein         1..1144
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127240
     Region          33..1143
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkplyiksti twilifliys issslyaqnk tlkvtgtvyd esgitlpsvt itvkgqkgvg
       61 vlsdndgkft isvpegatlv fsfvgmksqe vivnakqipy kvilqedsks leevvvtgyq
      121 tlkkhevvgs tytvkgddvr iaginridaa lqgmipgvsi tipsgligsa pqvrvrgtst
      181 vignaspvwv idgiiqedpl pfagaqlndi lssgdlnsam asisgssisg lnpddiesit
      241 flkdasatai ygvkaangvi vittkrgsnt dgrinvnfrt dismtprrty aqtdqmnsad
      301 rialskeiie sgvpfskfpq hvgyegaylq linkeismne fnqkvtqmek qntnwlklls
      361 rnavsqnysl slsggndkln fygsvgfnks lssykgndqs nktinfsvda klrdnlrtkf
      421 qfsasqsetn ayytgvnped yalntsriia pnewyvines kayfqmddgs aiqreirynf
      481 lnelkhtgne nkntkfqitg nliwnitpei kyelttaftr nsseaniwad dhsyavskir
      541 ganygelvtg endswlslas vlpyggilny nntnqqsytv rnqlnygkil deegnhalni
      601 algheirgns yigqqgteyg ympdrgksvd ydysqqankd yildiypdin yretanvpsy
      661 rerhstkltd qtenylsyya tlgytystky tlsfsfrqda snkfgqntnn rfnpvlsagi
      721 rwnvseenfm rrfgwlsnlt lkasygtqgk apdispnlia nfniapdilt geqylsiknl
      781 pnkdlkwekt rsfnggiels ildnriygsi dyyykktida itymnipien gtpnmavnng
      841 tiinkgydis ltvipvntkd frwsinatsg fnrneikdne dnitlgkitd gsviidgfal
      901 nsfwsfpyig lsdkgtpnfa iidqtpgvkt kvetgtlldy mvysgvkdpi fsgglstsfr
      961 ykqltlsasf nfqlghhkrl npfmksqsng grigqlripd peknastqln krwrqagdek
     1021 ytdipailas dedlsqylpd nslslsssge iyryqmynls dlrvvkadhl rcnsiclaya
     1081 lpknqldkik ltnltfaltv tdpfiikskk lgkqdpetls tsatnvipvv drqrkfslsi
     1141 slgf
//
LOCUS       WP_118451152            1119 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Butyricimonas
            virosa].
ACCESSION   WP_118451152
VERSION     WP_118451152.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas virosa
  ORGANISM  Butyricimonas virosa
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Butyricimonas virosa"
                     /db_xref="taxon:544645"
     Protein         1..1119
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127248
     Region          126..1115
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mifsrnkkhv ceafmrcsri fslillfaia rggtvntala qetvrtisvk fentsvlnal
       61 reinrlsgnq vvfrteevak etkrvtfesq ntpvitvvek clegttlnct lregriivvp
      121 qrlkdiqieg ivqdeskqpl pgvtvllkgt tlgtatdtdg kykltlpsnt pnpalvfsfi
      181 gmktqeityn gqetlnitmt qeanemnevv vtgifkkake sytgavttvt qkemkmfkgq
      241 nvlatlrnid painwvehne mgsdpntlpe inirgnsslp vgldelnaga saqlntplvi
      301 mdgfeisltk lmdfndeeie sinilkdaaa taiygsrgan gvivvttksp eagrmkiyas
      361 agfnmeipdl ssynlldske klalekeagf fdapedldnd ralkkkyndi wseilrgvdt
      421 ywlsqplrtg igqrynlrle ggsdefrwsi slgqnnikga mkgsdrnnfn gaitlsymyk
      481 nvifknqlmv dynksknsky gsfseyakmn pywrvkndeg eyvknytytk ggvvgnplyd
      541 aqlnirdesk ynqttnnfsi ewnmlkgltl raalgiskqn nssdkflpps hsdysktsyq
      601 endnffrkgk ydytsgeqsn lngnltlsyf kewkvkhqly agfdyfisqt kdvnysfyak
      661 gftndemdfw gnalqykegs kpqgsestsr qvgftgnvny tfnnryfvdl syrvdgssqf
      721 gskkrfapfw stgigwnvhn etfmkerwef mdklrlrlsy getgsvqfss ydalrmfeyf
      781 ttdrylifng adlkglgnen lewqitdewn ggievslwng lvtgqidlys kktsnllssm
      841 dvvpstgfds yranigevkn tgfeamlsty llrdtereli wmitgrivhn knqitklsda
      901 ikqqveeyka qnmentqlls egdsqttiya vpslgidpst grelfldkng kitdvwdlaa
      961 crnfgdtepk yrgnintmfs wqdltmnlsf ayqwggqqyn ktllnkveiv eseiknnvdn
     1021 rvfsdrwqkp gdvkpfkays dertkassrf vmddnvfqlq aisiqyrwrs kflqqhlrlq
     1081 sldfnlnlsd vfyissikre rgttypfsrk vnfsvalmf
//
LOCUS       WP_118451584            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118451584
VERSION     WP_118451584.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123204
     Region          53..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknsfrfkr nrkaitalli cvgfvgihpl avfaeddvnv vqtvqqqkqt itgivkdatg
       61 epvigasvke kgdpsngvit didgnfrlsv panatieisf igyqtasvka isgkplnivl
      121 qentemldev vvvgygtmrk kdltgsviqi rpdnlaneap ktvqdvlrgt pglnvgmdas
      181 akgggslqir gqrslytdgg hndpliildg mmfygelsel npddiaqidv lkdasaaavy
      241 gakaangvii vstkkgkngk pminfstnws fstmganrdv ydgegylkyr rdwyvagtyg
      301 vnpetgayee yqadkkkypa gyydaptqen lnkygitldq wraytnagsd isdqevwgat
      361 rlglqgnsla nfllgqtfdw ydhsfrtgln qnynvsmsga tdrvnyyfsl gymdnegvav
      421 gndyttfrsn mkvnakvtnw fevganvnfq ertdgdttvd wgkqitensp fasyrnenge
      481 lerfpmgnvs gntgynydyr qqfkeresgy tvlntilnak ltlpfgitya fniapryqwy
      541 yyrsfqsskd pdvtagaasr nngkrfdwsl nntltwdktf lekhhftvtl vqeaeerrsw
      601 gdnlsannlq ptdalgfhyv kagdkessaf ssddghetad gmlarlfysy ddrymftgsi
      661 rrdgysafgt snpratfyst afgwtftnek ffnwepmsfg klrfswgqng nrslanpyia
      721 ladlgsgtgg tygyvdasgn tteyryftmn rlanthlqwe kttawnigld fgflnnrisg
      781 sveyyhmptt qmimnqslpg fsgfgsvttn lgevqnrgve islsttnikn dvlewnttig
      841 fsfnkneikh lyyeyenvln aqgevigtke rddisnkwfi gqpigaiwdy kvtgiwqkde
      901 veeaakygqr pgdpkvwnnp dndkvnadgs vtivydnddk qflgqsspkv nwsmrneftf
      961 fkdltfsfni yskmghksle tdylnkdnag skvtngqnvy akkgywtvdn ptneygrlda
     1021 qgpsgvttpg klhnrsfirl dnislayklp kkfisrwsie kaiisgsikn vavwakdwky
     1081 wdpetgglap rtfnigltlt l
//
LOCUS       WP_118451512             942 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118451512
VERSION     WP_118451512.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106020
     Region          42..916
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiykglvl catlafayth taaqelladm leatqadtls kvqvafrsin qrdllggvsv
       61 idmkemseka ytsnslgfvd nvvggfngni wgnteylviv dgmvrdannv lpheidqitl
      121 lkgasavvly gpraakgvis ittkrgeigd lrinihantg fytpksypky lgsaeymtly
      181 nearandgla anysqedifn hasgsnpyry pnfdmyssey lkkaynrsea iaeisggsek
      241 vryytttgyy ressllkvgk tednyvsrff vrgnvdmqlh kfitaqadan vtfydsysan
      301 vdwwgqtatl rphlvtpfip lsyieatdqn slnavlnssy lqdgkfffgg tqqhptnpva
      361 dayaagdskf vsrqfqfntr fdvnlspllk glyfrakygi dyastynqgy snsyatfapt
      421 wsnyngedii ssitqygkde ksgtenisns ayrytynvsg qfdyqntfne dhnvfgmila
      481 nawqtqrsgh yhrttnanlg fqasynyqhk yyadfsvamp ystklptgnr vafsptvtlg
      541 wnlanekfle nsifdnlmlt asvgiinqdl ditasdnedg yylyktvvqk ggwyswgdng
      601 glavtefqrg nnpdmtyvkr keftaglrgs mwsnlinfdi nfftskmdgg lvrpgslypn
      661 yftqigypss siipyvnfnv dqrtgfdfsv yankkvgevd ltlgvsgmyy kstakkrden
      721 iefsylsavg ralngywgle segffrdeae itsaptqtfg dvkpgdiryk dqnndgkidd
      781 ndrvflgrwd splmsginlt vkwrdftffa mgnlylgghg mkdnsyywms gdskyseitr
      841 nrwtpetaat atyprltttn gannlrtsdf wiykndrfnl sqvqltyamp qnvlrgtfik
      901 glsffanann llmiakerkv lemnvgsapq trfyqlgfkg tf
//
LOCUS       WP_118451529             937 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            cellulosilyticus].
ACCESSION   WP_118451529
VERSION     WP_118451529.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides cellulosilyticus
  ORGANISM  Bacteroides cellulosilyticus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Bacteroides cellulosilyticus"
                     /db_xref="taxon:246787"
     Protein         1..937
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105600
     Region          40..936
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrkhktlkw gialvssmlt lnlsaqssli dyqsdkvdlg mgveqsqmlt tasvevvsgd
       61 elqktaaisl kealygkllg ltvlrpggtv sdyssgavfn irgqqttten gvlvlvdgie
      121 rsieyltvde vesvtvlkda aavallgyqg vngailvktk rgvegrqisv sydhkftfnp
      181 kvanfvdapt yanalnqarv ndglapmynd yelqafadgt hpyyypnvdw kkevfknygs
      241 edqfnlsmkg gnqklkyfsm ldytdsrgll dktdqeqyss qmrfskanir tnldvqftpt
      301 tkfvlnavgs fvetkrpygv tengltdlly rtpasafpvm ndpegklagi wggnttygan
      361 nvvaqvrasg ftkshsrsfq gdfsliqnld fitkglsvsa rlgynnfsqi yetnalgfmy
      421 gyeryrfdea ghptelinys agdktnnltf dhwtnqhnrs sflevstdyh tsfrdddnfs
      481 asliwhqkns tyndqymtfn rmnvmaylhy dlqqryvadl vlamngsnrs ypekwsfspt
      541 lslgyvfank ednrilnfgk lrfsagiqht dyvpiqglwl enyngsagsy ltglgdgswq
      601 wgtflgyqpt rrfnletayk fnwgadlrlf kqvdvnfdvy yqlrddills gdglnsavfg
      661 rpsayvnwgr vasygvelgv nwvkqinkdl sfnlgsnltw grnkqkrnie nvaydylsai
      721 ggrvsqawgl evvgffkdea ditaspqqnf dncrpgdfky kdqngdnvid endvvkmgyd
      781 tsvpelnfsl nlgfryknfg mnamfqgagm ytaylgtvgv wtpiidganl skeyynncwd
      841 rsetpvyprl tsrtnlnnyr gndvwyknvn ffklrncevy ymlpenwisk vkmsqckvfv
      901 kgenlmtlsn lkamdpenig tnfptlmgvn lgvsvkf
//
LOCUS       WP_118457106            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            BL5].
ACCESSION   WP_118457106
VERSION     WP_118457106.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. BL5
  ORGANISM  Aquimarina sp. BL5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Aquimarina sp. BL5"
                     /db_xref="taxon:1714860"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116420
     Region          25..1047
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mylkkiitiv mivlyhctvl aqdgitlegt vtsredgipi pgvnvlilgs nagtttdfdg
       61 fyqlkvkkgd vvsfsftgkk titisidnqt kidvaleeea seleqvvvig ygvqkksslt
      121 asvsklenkn ldelpysdvs nsikgkiagv qirnttgnvg depeiivrgi gsislssapl
      181 vvvdgfpfdd glqfinpsti qsievlkdas staiygsrga ngvilvttke gksektsyef
      241 kslsglkqaa rsidildaiq fsdldrnrdq lvenfnaqqe nrepnfvnyd nvqigkrtia
      301 qniggptnwq dealrnpari dnyqlniygg gtrtnylisa nyiydeglrk dndlerlnls
      361 arlksklsdn lsfdlkinps ytltrrssin ftdtgryetw ipvrhnqyts dltgqplgsf
      421 ahalhfrnln fdyidpvtgl tentgnienl wsssnfnpis rqeasrrnrf eyrllangsv
      481 kwkiakgltl rsslggyvry rtgeeffgsd gdrdgetegi ladqltvkyi nentltynrd
      541 fnghdlgllf gityentter lsnlritnfd detittlngg tiidldntft lkdetilssy
      601 larvnyaykd rylislagra dgfnkfgknn kygvfpsvsi gwnvanenfw rnsigntvnn
      661 lklrsswgis gsapalfdfl aptivdfsny slgntggvtt gqgevdflqg npditwetnt
      721 efnngidlgl fngavnltvd yyyklsekll lrqqisnstg fdeqwnnigk vqnsgwefdl
      781 stnlgkgklk wqgsanisfn enklisfggs erainngert dqyitrvgep yiqfygyrtd
      841 gifqtaeela nspsgitdav gglkrvdvng dgiineddrt vigdpfpdfi wgftntfiyg
      901 nldlnfsfqg sqggevvwge afynevaryg tiyaedqwfn enipasrpgi rigvpwletd
      961 yavqdasyis lrevvlgysi ptnaanrigl ekmrvylsgq nlwystaddy lgnnpegntd
     1021 rgnvlirgyq rgvtpvqrql algldinf
//
LOCUS       WP_118457236            1149 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            BL5].
ACCESSION   WP_118457236
VERSION     WP_118457236.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. BL5
  ORGANISM  Aquimarina sp. BL5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Aquimarina sp. BL5"
                     /db_xref="taxon:1714860"
     Protein         1..1149
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128109
     Region          72..1148
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkllkfhc ginlsikksr plfsavfill flnvakgesr vnetnnserf slayknssks
       61 tkvflfqaey evkgqitddr gipipgatis vvgtqrgvit dfdgnfvisv sngetiriqn
      121 lgfidqeili tgnkkeffiq lepaveslde viitdgyrks ykklfagvat rlntedikid
      181 gtsdasrlle grdagvvvdn lsgtfgaspr irirgntsln gnnnpiwvvd gviledniel
      241 sqnelgsgdi ssvigssvag lnpddiesfs ilkdasatal ygarakngvi vittkngkng
      301 plkinysgnf syrlrpryeq fdvlnsqqel svyaelvdkn lidlttaqfa esygvlgsyf
      361 nlrgtndvai gangqlsddf frryqtantd wfkvlftdvt tlqnhslsls ggsddasylf
      421 slgylkdegi tigdraerlt srlkntfkis dkftlgttla lsirdqvvpg tnnrtfnpit
      481 gefnrefdin pysysltnsr svtpydengn leffrknyap fniinelnnn qinidvadis
      541 aqldldyklk dnltfnsiin yrqaitrreh vigdnsnqae afradegvli ninpflfqdp
      601 dnptrpaysi lpegglniyn edilnyfyir nsitwnpein ydnqftflvg qeiksstrns
      661 reytgigisy engyivntnp daidqlasqn dqyfgisnlk drfvgffang gytlknkyil
      721 ngtirydgsn lqgtssksry ltsynvsgaw nihkenfits dwinqlrlka tyglsggrgp
      781 ltsatldlrs rvplrptdqe tvieinslan ddltfeklke fstglefslf enrlsgeigy
      841 ynrnsfdlig ivktsgvggq afqsgnyadl ktegyefgis tvnvktsnfq wntninvgyn
      901 teqitellfd ptlvqltqpa gapfsgreis alystrfagl nefgiptffd ennnivtnin
      961 lqerenleqi lkyegptqpr gaggfnntfk yknftlsanv tfkfdykirl nsnfgptytd
     1021 fnslpgdlvn rwrlpgdeni tnipailsdr tiqnqlgadn aydlynisda rvadgtyarm
     1081 rsmslgfdvp knylenlgiq saqfrvqgen lfliysdkal ngqdpeffns ggtalpvars
     1141 ftfslnvgf
//
LOCUS       WP_118457626            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            BL5].
ACCESSION   WP_118457626
VERSION     WP_118457626.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. BL5
  ORGANISM  Aquimarina sp. BL5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Aquimarina sp. BL5"
                     /db_xref="taxon:1714860"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114407
     Region          24..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvhhykllv laffmssisl aqqkrisgtv addlgvplpg vniviknttn gtqtdfdgny
       61 sipanrgail vfsyigfltq eivvadsnti nvalaqdaaq leevvvtafg itrnskklgy
      121 avstvqtddv lensepdlir slagkvpgvn vnlstgvaga snqinirgat tlggasqpli
      181 ivdgvaydns qvttsrqttg gggyesglss ldpnniasit vlkstaaaal ygsratggvi
      241 vvttktgatk gstnnklsvs vssgtyfeni anlpeyqnty gngvnfsyln angswgprfd
      301 sletiptwpn ilnafpeigp tvpyeaqpdn vknlfrtgtv fdnsinmsys gedgnfsvtv
      361 sdlnqdgyip fntydrtsva aggnfkllng irigstfsys eteqvggffg nnqfagsass
      421 fartlwlgra wdtslpfenp itgasltpnn gwdhplwswk hdqiitdtdr ivanvnlgyd
      481 fndnisvtyr vgfnkynlkr kqirdlgsra nnglgsvttd dfinedlest llvnfnydlt
      541 ddinltailg nnvlqnttsr vafqgtnfks pgiftianti nvtkniggfi ldndtrsrni
      601 gvfgdvslsy knylflnatg rndwsstlpk nnqsyfypsa svsliftdaf nldskvltfg
      661 klragyasvg ndapaeflnr tfasgnafng ipvinnnlfl gdqeitpeft deieigadle
      721 ffnqraiidf swykktttdl ispvsvpsss gfttfntnig emqntgveig ltlvpirten
      781 frwelfttft knenevtelv dgleriqldp nqvahaivgq pfgvfygsrf arddegnfli
      841 nqsgggivqd lengivgdpn pdfrmgfint isykglslra qvdwkeggdi qsisinsllg
      901 rgvtrdtedr ertfiipgfy gdnqgnpild angnkipntt qidtnelyfs paggntfgin
      961 tvaegsvydg tvyrlrelsl tydlpkeflk stpfgkisls vlgnnlwyfa pnvpkytnfd
     1021 pevtsfgssr iqgienssap tskrygfrln lsf
//
LOCUS       WP_118459278             976 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            BL5].
ACCESSION   WP_118459278
VERSION     WP_118459278.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. BL5
  ORGANISM  Aquimarina sp. BL5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Aquimarina sp. BL5"
                     /db_xref="taxon:1714860"
     Protein         1..976
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105744
     Region          27..975
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkksqiskg lllflfffpv vllaqetitg kvinegtgeg vpfinivedg tsngtasdid
       61 gnfsltvsnl pvtlrvfsig fttkkvnvdn agaitiqvee slealdeivv tglgssikrk
      121 nlanavstvs seelvgntsq ttvdgalygk vtgvnitass gapgggfalr lrgissingn
      181 nqpliivdgv yinnveipsg lrfasggnrg neensgnrla dldpndieni evlkgssaaa
      241 iygqrgnagv viittkrgkg grtkisfsqd tgitviqnrl glrpwtaqsv edtfdaterq
      301 rfedaiangg lidyedeiyg ntgfitdtrl nvtggnektq fyvggsfrde egiikntgfd
      361 rlslranidh kisdvfdfts ttnfvrsnss rsftgneneg glsygytlaf trpwvnlfpd
      421 angnypnnpn ypgnplfvrd qaknedtnnr iiqgfklntk lftnernrvr flinggidyl
      481 anetyvfvpk ehqaqvggqe gfisqgknnf tqinaqaiai wdhdmlgddl dlttqlgity
      541 ldqeanlvns rgsdlsvgqt nvdqsvnqvi dqflsseedf gyfgqieany knqfiatlgy
      601 rldkssrngd pnefygfpka slavnvssfd fwnieamnql klraaygetg npaafgatft
      661 slgssniggn ggssvaglng dpdvepetas efevgfdlgf lnsrvsleat yynknvkdli
      721 lsrslpassg fttettnlad lknegvelal radvldsdnf ywntgiqfyl nrsevtrldv
      781 pafaqpgagf gtglgtffie egqpvtqlvg nidgtltqvg nvepdfqmaf nnqltlfkqw
      841 dvsfllqwkk ggdnlnlsrf ltdlggtspd letpegqarl atpanaerfv epagyvrlre
      901 aaiyyrissd nikslfgdtv sdiklglsgr nlftitdyss ydpevsvngg aglssgievt
      961 pfpssqqfyl hlnvnf
//
LOCUS       WP_118460524             992 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118460524
VERSION     WP_118460524.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109207
     Region          32..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvkrtklcl crslllmtgl lfavasfaqd ltvkgkvtdt tgetviganv tvkgttngii
       61 tdidgnytls gvkpssvlvf sfigyktqei pcsgrkeinv vlsedaqald evvvvgygsl
      121 skkelsssiv qvdrskflqg smnnpmemlt gkvagltvnn tasanpnass slqirgatsi
      181 sasndplvvi dgvaggdirn laaqdiesmt vlkdaasaai ygtrgangvi littrkgage
      241 agraqvtyds wfgvnlaksg pdilnadefr rsrratdygy stdwydlllr dfsydnnqyl
      301 sidgstkngy ygasfnykka tgldlnssre efggrfvlnq rmmdgiveln gslnarrvne
      361 vwgndgmfdt alsmnptmpl ynedgtyfqp tsptgarnpv qelkeidnng qrvyllgtae
      421 vkvnlirsek qmlntslsys lhyndlkqhy ytpstagesy wngyngraev tyqkwytsrl
      481 ewlgnysldl gdhnfkamvg ynyeqttwer lqagnsdfnf ddilwnnlgs gsylakgkas
      541 mgtgkslakl igvfgrinyn wknlliasas iryegstkfg adhkwgafps lslawemanm
      601 gflkdhqniv qslkprvsyg vtgrsdfdcy qslatygshk naqlnvtdty lmdgawvtgy
      661 apsvnanskl gweksvsmni gvdfalwnrl rgsvewfdrq srdllynyta pqppyiysti
      721 lvnvgttvnr gievslegda fkgtpvewtt gvnysygttk ldklsnslyk asyvelyqkp
      781 gvgtseyffr veegskigqf ygyeyagven gdmmiytdeg ekvpvskadv kykrhigngt
      841 ptsylswsnt lryknfdlsl mfngafgfei fnmrrygmgl kgcgtdnvlr daygkdadit
      901 tgggvissff lekgdyfkld nltlgytitp kenkfikgmr vyltaknlft ltgysgndps
      961 avaingltpg vdtnsaypsa tqlsvglnir fk
//
LOCUS       WP_118460993             938 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118460993
VERSION     WP_118460993.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..938
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104643
     Region          40..937
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrhhkifkl slaavcatvt lnmnaqssli dykngkvdlg mgveqsqlfs taatqtisge
       61 elektaaisl kdalygrllg ltalkqggfs gsdgygatms irgnqttsen nililvdgie
      121 rsidymtiae vesvtvlrda aavalygyqg vngvilvktk rgitdghrls vsydhkftfn
      181 pkvadfvday tyaqainkar sndglsamyn nyelnafqtg lepyyypnvn wkdeafkdmg
      241 sedklnlsmk ggndklqyfa mldytdsrgi legtdqgnys sqlkfskanv ranldaqlts
      301 tttmqvnalg sffetnrpng adpngltwml yqtpasafpv kndpngelad vwggnttygm
      361 nnvvaqiqgs gflksharmf qgdvtlkqdl gfwveglsvs aragynnfse iyesnalgym
      421 ygyqrytfds ngvpsgltty sagnktnnld ynyyinkhnr ssylsvsady qtsfreddnf
      481 sasliwhqkn ttsngqymtf nrmnvmgylh ydlkqkymad lvlamngssr sypqkwsfap
      541 tlslgyiyan kddasflnfg kvrmsagiqh tdyvpiqglw lenynggggd yyfgagtgsq
      601 gwgtfigyqp trtfnletay kfnigtdlrl aksvdvnvdv yyqlrddill sgdglnssvm
      661 gipssyvnqg rvasygvevg anwvkrlnnd llfnvggsft wgrnkqlrti envaydylsa
      721 vggrvnqpwg levvgffkde ediansprqn fdvckpgdfk ykdqngdkvi neddevkmgy
      781 dtsipelnya lnlgfryknv gfnamfqgag mytaylgttg vwtplvdgan lskeyyensw
      841 dmsnnpiypr ltsrtnnnny rannvwyknv nflklrncev yyylpekwts kvrmsqckvf
      901 vkgenlmtlt nlkvmdpeni gtnyptlmgv nlgvslkf
//
LOCUS       WP_118461057            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            BL5].
ACCESSION   WP_118461057
VERSION     WP_118461057.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. BL5
  ORGANISM  Aquimarina sp. BL5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Aquimarina sp. BL5"
                     /db_xref="taxon:1714860"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116893
     Region          25..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfrgilt lllafvvqlt faqektisgn vtdnsglplp gvnivvkgts kgtqsdfdgn
       61 ytievsrgav lsfsylgftt kevvvgdgds invqlaedaa tleevvvtaq girrekkslg
      121 yavtvvqsde ieqkpesdin ralngkipgv qitgaggatg sstnvfirts vsitgnnqpl
      181 yivdgvpfes npnttggfta gttstsnrtl dlnpdniani svlkglsaan lygsrgrngv
      241 ilittkagst eksnkkfevs fsnttyitqi snlpefqnty gqgadqafnp gfvgnwgaaf
      301 sdidtvihpy angrnpgfdq lfpqffgiei pyqaaennvk dffrtglgrs tsvgvssase
      361 kgnfsinynn tdedgyiesn nlrknsfsvg gnlklsnnfn vggtlnyvnt tlrtppisas
      421 ngigaltifq rllfiprnid ltnlpfqnpv dgssvyyrpd ienpywlldn agtssdtrra
      481 ygsfnagytf ndhislqytf gldtftdlqr fsvnkgavar aeyqvgylrt ttstneilnh
      541 railnfdgyr aggfrfgalv gfesrrdefs rdgiastnqv vfgrqnhdny inhnsldpvt
      601 gvdlqfnder nvvgffgevk vdyndylyat vsgrndwvsn vqpqnrsify psaslsfipt
      661 safeglrgdv lnflklrggy atsagfptlf rtaqqlnsta nafgpstspt ttntfsgfla
      721 npdlkpelhr eielgieanf fnsritldas vysrvskdqi lqrnlapstg fsaqffnagq
      781 idgegieial gltpvktdsf swniqnnfta aetevveipe eriltsgfgg lgnyaieglp
      841 lgvivgtyyi rddngnilvd atntttqgry ltsndvpved nlavigdpnp dwrmttintf
      901 sykglslsaq leythggdil sntasnlltr gvtrdtedre sttilpgvvg npttglpvld
      961 angqpvqntv qigandiyfq nvfranegqv fdgstlrlrd vtlayklsee mlaktpfgsi
     1021 sfaisgqniw fkaynfpeyl nfdpevlstg vgngqgldfq taptskrysf sikatf
//
LOCUS       WP_118461063            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            BL5].
ACCESSION   WP_118461063
VERSION     WP_118461063.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. BL5
  ORGANISM  Aquimarina sp. BL5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Aquimarina sp. BL5"
                     /db_xref="taxon:1714860"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115354
     Region          26..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksqtnrilm lflalvtqis faqestvtgk vtddtgiplp gvniivkgtn sgtqsdfdgk
       61 ytinvnsgav ltfsylgfat kevtvgsnne invqlsedaa aleevvvtgv asgtskrklg
      121 vsvnsvkaed lqvqgaqsvd qalqgkiagt iiqsttgqpg qqqniilrsi nslnssqpmi
      181 lidgiqvsts qtsvggasnq ssrladidft nvervetisg aaagtiygaq gangviniit
      241 kkgkagapkv sirsnvsias aitnddanra tlhhystnsd gflidlngtp vtnlngnaqy
      301 lavdpnerdv ngtmlgaqgi ndtpfaepif lasdilftda fntttgitvs ggsenitylv
      361 sgnrseqesv lvegkyikyd arlnlgfdlg kkikintrfd vinstndtgt ntdnanasnl
      421 innvfqnlph vnffnrnsdg dltvspdatd pnsinpfffr etqtrqdnit rylanfdlty
      481 kplkvlslnm kygydtytqn ftffqenqss hlqsgsiptn itgiinqidt qeyfqnllls
      541 anltldfded lklnvpitst ttfnfdwrdq elrqtlvtgt nlpagpfgsf ninqavvktf
      601 ngflespfrt ygflinqkfd yqslfgfsgg frrdfsnrfg ngldftfpra dayfniaelf
      661 dssimnslkl raaygeagiq plfsqniftf alttvgseal ssipstvanp dlevetsqet
      721 evgidytftp ndgawfsrvd gsinyfdrkt egaifdlgip tstggsavfd nsydissdgi
      781 easidlglyn sqktkwdfgv rftkstatld rienglpvvv ndnfvlqege eigtfsvfpv
      841 itsldavdns gnriipaadv ddftiassgy vvnkntgnvv igpdkevrgs tqpdfvltfl
      901 ndislfndiv glsfqidwfq gldvynrarq wlynnglhad tavpvsiedp tgavqtgafv
      961 syytslyntn vptsefvedg sfirfrdisl rfkinkllkt dtfdqinltv sgrnlititd
     1021 ykgldpeaar gfgntfqrgf defthpnvks ynfglnltf
//
LOCUS       WP_118461261            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118461261
VERSION     WP_118461261.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112181
     Region          36..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkktkiypw kmyfhvllgm ffllpallna qnatvkvsgi vtdtnnepli gvsvaekgtt
       61 ngaitdvdgk ysltvrptst lrfsfisykt qevkvdgrkt inirmeddvq alnevvvigy
      121 gtldkkelts avshisskdf lhissldpsm miqgkvagvs vtntaaadpn nqasiqirgi
      181 ssraaglgpl ividgipggn ltninpndia smdilkdgaa saiygtrgsn gvivittkkg
      241 srdgkfhaty ngmltasipl heldpltaee freyrvpnnp tsdlggatnw ideitrtgft
      301 hqhtvtlsgg tsqsnyrvsv dyrnatgidi rssreeygar asinhttkng lldfsvniap
      361 riayrenssw dafkiamdan pttplfdpen pnlysdftgq ealwnpveel kleqnggetk
      421 lldwdatvkl nllpllakdg hsihslstql tfadqqsdnf dywfrpstsr lamkndykge
      481 asrtyskyrq hslewlgnya melkghrara mvgysyqyfq nsglnaankd fssdgllynn
      541 lgsgewakee grnemgtnks dskliaffgr lsydyknryl mtaslryegs srfgddnkwg
      601 yfpavsagwr iseeafmkdi twiddlkirg dygvtgnqdf snylslstms sfgsyyyngq
      661 yftvwgagkn pnpglkwekg knwnigmdfs mfkgilsgsv nyynrkqqdl lgdynvpvpp
      721 ylfsttfvnv gtmrntgiev dlniqavkmk dfsytinlvg atnenkflkf snneftgqny
      781 ydlanmespn qpgklqriee gqrlgnyytw kyagidadgd wvvwnkdnte mikisdakee
      841 dkrvtgnglp kftasmtntl tyknwgltif lrgafgfdlf nvhdfywgip smqsnvlkka
      901 ytknaaikkg knvltdyfie rgdyvkldmv tlsytfqinn kwldsarlyi tgknlatitg
      961 fngvdpstyq tngltpgvnl ngtegtrryy psttqvmfgv qldf
//
LOCUS       WP_118461535             954 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118461535
VERSION     WP_118461535.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..954
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106089
     Region          42..951
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyiqtkfil camlavspmf vsaqatdwne tdslanekdp mvqvafrkva qkdllggvsv
       61 vnveeltkkn yntysldnmq gyvggwngns lwgmdgdnag flvlvdgvpr dannvmpsei
      121 aqisflkgaq avvlygskaa kgavvittkr gnveglnvsv rantgfhvak afpeylgsae
      181 ymtlyneall nddptvklry taediynhgs glnpyrytni nyyssdyvkk aynrsevtae
      241 itgggkrarf ysnvsyyrng dfldfgeakn nmtdrfnvrg nvdvninsfi nayinanatf
      301 ynsktakgdy wniastarpn fpeyaaplip ldmidpnata awellsttsn iidgkyflag
      361 tqanstnafa dsyaagsskw tsrqfqfdag vnvdlnqvlk glsfnamfav dyatsystsf
      421 dnkyavfvpt wanyggkdvi valskegnde kpgtqnvggs adkqtiafsg qfnyqntfnk
      481 yhnvsamlia ngyqqtvsaq yhrisnanla lqagynyqqr yyadfgaali hsaklakghr
      541 qalspsvtlg wrlsgenflk dspvvddlll svsgsilnqd idlvmgdnef ylyesvwtqn
      601 dgyawydgpa gkytistrgq nddlsfikrk efsvnlktsl wnrlitadas ffinsmegyl
      661 inqptfypsh lntgypaasf mavmnynnnk rvgfdfnina nkrfgdvdls lgvagtyydt
      721 kvtkrdeiyd dayryregka vdgiwglqsa glfqnkeeie sspeqklgst vqpgdikyvd
      781 qngdnviddk devflgkggw ygapftlgin fttkwknltl fvlgtgnfga yglknssyyw
      841 vdgddkysai vrnrwtpeta atatyprlsa rsasnnfras dywlyktdrf dlakvqityd
      901 lpkrilrntf inelsayvsg anlltisker khmemnvgsa pqsrfynigv kavf
//
LOCUS       WP_118461280             919 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118461280
VERSION     WP_118461280.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..919
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103110
     Region          36..918
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrknvyivg iallyavsam adgdiktksn iderqtsavs tvtseelekn stpnpyntly
       61 gllpglsvlq qtgwtdnakl ivrgrgslng aepliivdgf prpleylnva eiesvsvlkd
      121 gaatavwgpr gangvvvitt krgkeakmsi dvnyrfgmgl pinqpkfvda ytyaqaknea
      181 llldglqpqy tdahleafrn gsnrdlyadt dwlseglrnq sfnnqadftf qgggkrlryf
      241 tmlsykndyg ilnsaytdys dryntqmkky nlnfrmnldv evtsttmvkl tmlgmlyerk
      301 rpntaedkif sglyktpsaa fpvrtsngyw gsntvyndnp iariadvgyy kenqrmlqad
      361 lriiqnlsai tkglsaeiav sydnsatyqe tgsknflyei nssvlnpetg eyqinterfg
      421 ddkaltvdnk gladqyiran letkvaydrt fgkhavtisg lyrqesltpt gkaqsryrqy
      481 itaaagysyd nrylldvvvn hsgtsvlpkg drfrtypavs agwllsnesf mesasfidll
      541 klraswgrsg ydgfdyyldr qywvggagfv tndaggtqsg lkegrlaisd mscevsdkyn
      601 vgldmrlfkn ltftadyfmd rrrnilvdga nmvssalgie iaktftgavd tkgfelalnw
      661 ngakkdfsyh aganlsyakt eivengegyk pysylsakgy pvgqifglea igyfrdaedi
      721 aksptqtfsd vrpgdikykd qnndqkiddn driaighsst ipklyyginl gfeykgfgvd
      781 mlfqgvggys kmlntanvyw plrnntnist wymddnirwt eetkdianlp rlttlntsnn
      841 fqnstqwlvn gsylklrnln vyynlpqqwi kkakmeacqi farannvfsl dhvkysnced
      901 lsvnypdmls vyfgfnvkf
//
LOCUS       WP_118462225            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118462225
VERSION     WP_118462225.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114697
     Region          21..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mssiflhdfl tpssqstqqa kkitgkvvda tgepiigasv lvkdtgtgav tnldgdfsvd
       61 vsvgntlvvs fvgyrtvevk vtnassyavt mqddsqtlne vvvtamgikr erkslgyaid
      121 dvnaeelmkn ksvnpinsla gkiagvnitq sggaagsgsq iilrggtsle rdnqpvfvvd
      181 gviydnsttv vgnsafdgst stsstqsnrv mdinpedien msvlkgpaaa alygsraaag
      241 vviittkkgk egavevnfst kyitqwakyl pkvqnrykrg faedqytdgk ytgttyndfs
      301 ynswgetitd gtpiydnigd ffqqggawdt nvsvaggskn ssfylsgsyy nqdgiipttg
      361 yekatfrfng eqkwkiftfg anvaysqant dktltsagly gsdgsgtmts vyrwsptddm
      421 thylnedgtr yrmfgdrldv vdertnpywi lnknkmkdnt erftgnfnvk aditdwwwis
      481 yrmgidsytt dnsntlgagg vyklqwqkgm ysensyryky lstnlmtnfa kqfgnfnfnl
      541 mlgtstddtr twsnyrmawn fevpnfyafd natsenrnfs sarsqkrlvg vfgefradwk
      601 stlfltvsgr ndwsstlpve nrsyfypsvs gsvvfteflp ksdwlsfgri raswarvgkd
      661 tspysldtal wpsqsflggf tgvsnywqag naalkpeite steiglelrf fnnrlkfdya
      721 fytnnsydqi msprlsnatg yilrsvnagd vynkgmelsi ggtpiltkdw swestlnvsg
      781 nrgtvknlme gveilyvtdv qvgnakaasf pdgnfmaiag sewkrddqgr vmldknglpd
      841 kntnknleig nrepkfaggw nntisykgls lnmlwdfrvg ghvyngtqya mtgagvsels
      901 anrekievsg vntagefvtn tfeagktyiy ngketsgkti ianyyqdiyp yeaanfmtkv
      961 nalrlrtisl sydfpkalla kikvlkrasi tatannlllf tnydgdpeva aagsgavgss
     1021 svgidycgvp stasfsfgvn ltf
//
LOCUS       WP_118464162             925 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118464162
VERSION     WP_118464162.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..925
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102560
     Region          46..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mninrmlmla tvvvsltana qvklsdknan aydmgygvei snflstasat titgeelqqt
       61 satnlaqaly grlpgltals qggfsgdenk gasfnirgyh tlndknilil vdgyerpidr
      121 lsveevesvt ilkdaaatal lghegingai lvktkrgveg kthvkvnysh kfqfdpefad
      181 mvdgygyana fnrarhndgl saayteqeln lfkdgsdpyf ypnvnwrnlt fknsaeedha
      241 yvsvyggtnk vkyythidyt dvrgafkdtk qpdyntqlrq skaniranld fnitnttlms
      301 vnlfgmfqet krpsdisadd ataaiyslpa safpyktstg iwggneaygd anpiakiqes
      361 gfykthqrql wvdaklsqkl dfllnglnvf vsagyanssi yaenshkahq ygyerytgti
      421 gdknnvalnt fgnketnltf nnwnagqwwk akasvginyk csffdndhfn atvvydnsgv
      481 stdgrgntfy rqnimgvfhy dfqnryvadl vlagngasrt ypskwafspt lslgwiyadn
      541 nddllnygkl rasagiqhtd ymptygmwlp twdvshgyvi ignnygatwg aslgsfpttd
      601 fsqetstsfn lgtdlrlana ldisvdafyq lrnhimlsas yenssvagiq ssyndvgevk
      661 sygfevsaky vkkitpdlnl nlganlswar nevskyigtp typlsdpvgh rvneawglks
      721 agffkdqadi nssyrqeyst vspgdikyqd lnddqvinef dvtsldgatd ipelnyafnv
      781 gveykgfgln awfqgtgnym kylpstiwgg madngnlsvd yynncwdvag snalyprltt
      841 lnnsnnsqks nvwykpvhfl kmrnievyyk vpatvlskls ltaakvfiqg enllsfdnid
      901 amdaevlsta ypmfkgvnig vtltf
//
LOCUS       WP_118462248             978 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            BL5].
ACCESSION   WP_118462248
VERSION     WP_118462248.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. BL5
  ORGANISM  Aquimarina sp. BL5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 978)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 978)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Aquimarina sp. BL5"
                     /db_xref="taxon:1714860"
     Protein         1..978
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106468
     Region          25..977
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktftksalf llwlipmsff aqssvsgtvt dagngqpipg vniiikgttn gtssdfdgny
       61 vlngvndgdi vefsyvgflp qeftysgner idvalqedaa eleqvvvigy gaarkkdltg
      121 svstvtaddf nsgnivtpen llngrvaglv intpgdpgan snirirgggs lnasndpliv
      181 vdglplsnen akgarsilst inpnniksft vlkdasatai ygnrasagvi iietikgskg
      241 lkvdynfqsg lftlpktidv fsadeyrali aerrpqdigl lgnantdwqe eiyksvvstd
      301 nnlsvrgslf dvlpvrlslg hlnqpglrlt seferssasl vlnptllngs lkinlnanas
      361 weknrfaagq etaairfnpt lpvydptspf ggfteyftdd gsgnitplng trnpvaallq
      421 renrsevqri ygnfkvsyal psfpeltgtv nvgfdetdse efnelstesi gsirlddgtf
      481 vgsrvdetqy rkntlfdgyl nykkdlgsfg ldltggysyq kfevdrfttn eqrddnesti
      541 pdfttdpnlv llaffgranf sinekylltl syrrdatsrf seenrwgnfp aaafawnisd
      601 enfmadsnlf snlklrlgyg vtgqqdiggs klsfassvvn gqptsqyiin gqlvtvtvpt
      661 ginpnltwet attynagldf gflngrings idvfkketnd llvdapvadg snftnaieqn
      721 vgdlqtegie fsvdaaiidr kdfswninyn vayldqeies lagadilvgg idggtggnaq
      781 vhregfapns ffafkqvyda ngapiegafv dlngdnvinn ldryiyrnpv advtmgfqsn
      841 lnykgfdfsf nlraslgnyl ynnvdsafgq lnlladgtqi gnlptsvldn nfnstsgnni
      901 vsdifienas flrmdnitig ytfnkflget ssfrlwtgvq nvfviteysg ldpevfdgid
      961 stiyprprtf lmganvkf
//
LOCUS       WP_118463678             949 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118463678
VERSION     WP_118463678.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..949
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106113
     Region          40..948
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknriiipa llaclclqgr aqevndslvn gkpaisshkv iqigyqkaqr leestssvst
       61 vynedfnkrs aknianslyg ygiglttlqg sgryadaqpt ffirglqsls tnnplvlvdg
      121 ierdisdltp eevesvailk daaavalygy kgingvvnit tkrgayntre ikftydhgfg
      181 wqarkpkfvd sptyasamne altndgmspr ytqdelnafr sgqypylypn vdwlgetfrn
      241 mdatniynis frggaskfry yamanlttnk gfiaspytne gystqdeysr anlrtnldid
      301 lsentklkln vlgilsesrt pgakdeagad iwnmiytlps aafparleng twggsatwvg
      361 tqnpvavsqa aaytkfhert lfadmtleqd lasitpglga sallsydnya qywedhsktf
      421 vygsnsvtsw engvpvntsy ytdgkesamg nvskciaftr vfnfaatlfy tkqinassni
      481 ysqlkwdyey rntkgtdqtw hrqnasfyth ygykdryyad vtvvgsasnk lapghkwsvs
      541 ptvglawvms kedfirdisw idflklrasf gvintdrlpl dddkdvtnyw eqtygggsyy
      601 pfdtnysvgt qswslgrlas lnsthekayk ynfgldaslf ngldlsfday yerrqdiwvs
      661 ssghyssvlg ftapyenggi vdskgfeiga synkkigevs lniganfala kneiieqmee
      721 prlydnlktt gnplkqtygl kaigyfknqa didnsptqaf gnvkpgdiky qdingdniid
      781 andkiaigys ttapeiyysf nlgaewkgfg fdamfqgtgr ysavlntksl ywplinntti
      841 sqeyydnrwt senqnakypr lssqsnenny qtnslwladr sflklrsvel yykfpttllk
      901 kskilsnaki yvrgidllcf dkikvadpes ygstypltrs vvagltigf
//
LOCUS       WP_118464633             910 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118464633
VERSION     WP_118464633.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..910
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100858
     Region          24..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrirnlfcl slllvavglp avaqtklhvt lpdsittvgy atglrknlsg lveritenqm
       61 nkdqitnpld airgrvpglt ilkgsngpaa ldavrlrgtt slttgndpli ivdgvfgdls
      121 mltsiypadi esfvilkdas etaqygsrga sgvieittkk gvsgrtsvny ngsfgiassy
      181 ktvrmlngne fralaqrrgi sildmgnntd fqkeieqtgl qhnhhiafsg gtntsnyrvs
      241 lalmnregvi vneklqnfts nmnmtqyvfd nflkcdlgmf gsvqkernlv nlhkifysaa
      301 synptfpnhk npetgnwdgy ayasqlshpl awmdvkdkna tshistharl tfnlaeawkl
      361 tffgsytynv venaqylpva vwaqgqayrg dkkmesllgn lmlsykkewr khffdvlgla
      421 eiqkdkysgf yttvtnfsnd klgynnlqgg airpwdgtns yyedprlvsf mgrvnytynd
      481 ryiltvnarg dasskfgsnh kwgffpavsv awvvskekfm eklsfidnlk iragyglagn
      541 qngidsyttl slmrpngiap vgstpvvtmd klrntnpdlk wevkqtfnag ievallgnrl
      601 lltanyynsk tkdmlylynv svppftyntl lanigsmrny gtelsigitp lktkdmelni
      661 nanltfqqnk llsldgnyqg ehisateyks lagldgagfh ggynhivyqi vgqplgvfyl
      721 phctglvsdg nggytyqiad lngggvsled gedryvagqa vpktilgsni sfrykdfdis
      781 lqingafghk vyngtsltym nmnsfpdynv mkkapaqnik dqtatdywle dgdyinfdyv
      841 tlgwnvplkn trylqslrls ltvnnlatis gysgltpmin sssvnatlgi ddkrnyplyr
      901 iytiglsvnf
//
LOCUS       WP_118465786            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118465786
VERSION     WP_118465786.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121809
     Region          24..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrlsvvfl lligtltyal aaerqvegvv issednlpli gasvyvtadd lkkngnnqst
       61 igvitdidgk fsisipdgit rfycsyvgyd vveiklipgk kqyditlqps ahmldavvvt
      121 gyqtverrkl taavskidis dqmmgatksi dqalagqiag lsvsnisgtp gapakirirg
      181 tsslngtqdp lwvldgiple gtnipnmevl kdidnigqta iaglnpadid nitvlkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs skltyspkln idrlnllnse ekvgleldll
      301 esgypyretk gevyriisgl gelknfkdgg wnalssnaqg ainrlkatnt dwsdilfrda
      361 ftqeynlsls ggsekatyyt sfgymkengn ipnvsaerln lvmktsykvn silkvgasmf
      421 anrrknstyl pdtdgltnpl fysrlanpyf tpfdangnyn ydidvendvd mdfgfnpfee
      481 rrnvtnetti nglssifdae lrfddrfkit tqlglqldkt siekiadges famrkekknh
      541 rqngvtylpe ggfhkanens lsqvtwkamg eyrdtykdih efemmvgtei rktwedklys
      601 agygfdrktm ttkpiifpee skafklheka hienayvsaf stlsysllnr ytvggsirfd
      661 gsdlfgvdkk yrylplysvs glwrisqepf manakwidnl vvrasyglqg nidkntspyl
      721 lgnyrienil pggsedmidv sgapnkklrw ekthsvnagf dfavlnqain lsvdyyyrkg
      781 vdligtqmlp letgfemltv nwasmqnqgv eiglstrnih tknfmwttnf nfaynnnkvl
      841 kealredaie pgregypvga lfalktagld eegypmfqnk egetvsamef fklqewgfga
      901 tdltarerre lytyvgtadc pytggfnntf tykafelgvn fsfdfggkvr sqptysivdf
      961 dkgrntnrdi lnrwtpente tifpvllsqn erldeymwys nqneiyrnld iwirdlnyvr
     1021 lqnirlgytl ptnfsrklgm tsatiaiegr nllvfgssyk nyldpetmsn ayatpapksv
     1081 tlslnlnf
//
LOCUS       WP_118466363            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118466363
VERSION     WP_118466363.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121113
     Region          26..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkrlfiml aylflwtsat laqvskvtgv viseegnepv vgasilvkgf sqgvitning
       61 eftltnvpnd artliisfvg mktqevaikp qlriimsnds qmldevivtv aygtakkssl
      121 tgaissvnqd qiemrptssv tsalegttsg vqinstygap gsdpsirirg igtvngsstp
      181 lyvvdgvpfg gnisdinpad iesisvlkda asaalygnra sngvilistr kgtsnkisfd
      241 lkinqgvysr gikeykrtsp nqfmeaswqn lknarmsagd daataaqyat anliseqlyl
      301 niynkpddql fdangnlvsd aqilpgyadd ldwysdairn gyrqeysfsg ntaneksnyy
      361 fsigyldekg yvtnsdfnri sartsmsftp kkwfkaginl sgthqnshat ngdsdagytn
      421 afmycrqiap iypvhlhnad gsyrldalnn kqydpgyykd degvtistrn qyvdrhviwe
      481 nelstdktir ntlqgiafad vkflndftft vkgdlnvrns eqtsydnati gdgkgnngrt
      541 krvtyrykny tfqqqlnwnh vygkhyidvl aahenysnny dyeyafktte tfagkpnlsn
      601 ftditsltgy etdyrtesyl grirynyaek ynlevsfrrd gssrfskqnr wgnfgsigan
      661 wiiseedfmq svtwinslkf ranygqvgnd agtgyygymg lyagsqnani gayylsqnea
      721 ldlkwetgea ygialegrlf nrwnisleyf dkrnkdllfd vylplsagat sttsaqatia
      781 knlgtisnkg feintdidiy rdkkwkvnfa tnatfvknki vklpeqnkdg iisgnykive
      841 gksryefflp tyvgvdqltg nslytlnled yfitlpdgsk lgnaegtdis dnesltsing
      901 tyytnnttya lkefhgsalp kvygsftgtv syksltfsal ftyslggkty dgvyrslmtt
      961 gtspgnfhsd imnawkavpe gmsensadri wvdgipqins tmsannnsas srwlvssdyl
     1021 vvknltlsyr lpasfvkrld lqgisvsanc enlwtftarq gmnpqqsfgg sqynylvtpr
     1081 vfsvginikl
//
LOCUS       WP_118466456             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AF39-11AC].
ACCESSION   WP_118466456
VERSION     WP_118466456.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AF39-11AC
  ORGANISM  Bacteroides sp. AF39-11AC
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Bacteroides sp. AF39-11AC"
                     /db_xref="taxon:2291999"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109989
     Region          38..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mpkfnqkrii sgtmrlitmv cmlcmcqfit aqiknfqgvv kdskgntlpg vtiletgttn
       61 gvstdvdghf eikmnpgntl tvsyigyvtr tiqtnantts lniileedvf llddvvvvgy
      121 gsmkkgevts aitsvkkdnf lagmvkspeq llqgkvaglq lsnytgdpvl glemtirgvn
      181 slsgntspli vidgipggsm taissedies idvlkdgsaa aiygtrgtng vivittnrak
      241 atkmsleyna svsfetiskh admltandyr rlkddpdfpg iqdegtttdw vdaisrtavs
      301 qnhflslkgg naqsnyvasi dyrkregvin ktdresitak iglnhnmfnd klrfqlnind
      361 syvtqqrawy aaylnallen ptrpiydeng nyteykvnlk pynpvamine eydkegynql
      421 mmsgkmtisp ieglnlsvmg alqrfdrmen ksntfkhmst vvngdygnvw nwadntlqkt
      481 lelvgdytks fgvhnmgvma gysyqddddk giyqwakdfp tdmfgpwnig smndmkdnka
      541 amtsyrnthk lisffgrvty nydekymfma slrregssrf gdnhkwgwfp avsagwrlsk
      601 enflrdvkwl ddlkfrvgyg vtgnevnanl lsmyllgygg yayingkwtq gaapyqnpnp
      661 dlkwetksel nlgldfsflk nrlsgsidvy hrvtsdllst yevptppyiv ssmmanvgki
      721 rnrgiellls gtaiqirdlr fditgtfsyn knkivslsng lyqkdywyag atgspiqtht
      781 hivkegdpvg nfhgfqthsl tsdglwmvyg adgepklltd andgdkrvig ngipttygsl
      841 nlalnykgfd vsvmfrgafn fqvlnrqrmh wettarigeg nlpssvlnkp fgsnsyvkga
      901 pamqsyyved gdyvkldnvn igytlnlknq niiqrlrlyv agnnlltmtg ykgldpevsi
      961 kglapgvegs gsgelypttr qftiglnllf
//
LOCUS       WP_118466565            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118466565
VERSION     WP_118466565.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120826
     Region          23..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskrilflff cvfalaahsq nvvikgsvtd vnkepllgvn ikvkgtstgs itdidgnfsi
       61 ngpkgatlvi syigmvtqev eykgqplnvv lkddsqalee vvvvgygtmr kkdltgsvvq
      121 vrpdklanen pktvqdilrg tpglavgyna dakgggslsi rgqrslytdg ghndpllild
      181 gmmfygelse inpddigqid vlkdasaaav ygakaangvi iittkkgkqg kpvinfsani
      241 gltqrsayre rfspsaylqh yadwrekgty gansngewda yqsgtykdmt dyfknpnklv
      301 gvdletwrsy tqnesgesdl siwakrlgft gnvldniiag ktvdwedkaf rlglnqdyna
      361 sisgasekvd yyfslgylrn egaliddtyr airanmklna kvtkwfevga nvnfqdrtdg
      421 sidmdedyfl rnspyadyad engnptqypq detysqrgyn ydfqkqylel ekgytvlnti
      481 lnakvklpfg ityqfnaapr fqffydryfm saelpgsnpn drganreqak rfdwslnnti
      541 twdktfaekh hfiltlaqea eerrywsdri earnilpsda lgfhntqngs kenssyktsd
      601 shetadgmla rlfysydery mlttsirrdg ysafgssnpy ayfpsvalaw tfsneqffqk
      661 fknvmstgkl rvsygsngnr slsnpyvala nlyegggaym gyitssgdlq lmrylmadrm
      721 anptlqwekt qawnfaldfg flndritgtl dvykmstkdm imsqplqnft gfsnittnlg
      781 qvdnngfels lntvniqqkn fqwnttlnfs ynknkirhlf yeyedvldas gnvigqkesd
      841 ytasswfigk pineiwnykv igiwqkdewe eaakykqvpg dpkvwnnpan dvynedgslk
      901 tvvyndddkq flgtttppin wslrneftlw kdltvsiniy srmghkglst nylnndddgg
      961 rmsyaaacke akeywtiynp tnkyarieaq gpdgakspgm lydrsfirle nisvgytlpk
     1021 qltkkwdier vkvfgtvrnv atwakdweyg dpetgglgtr iysfgvnltf
//
LOCUS       WP_118466944            1127 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            clarus].
ACCESSION   WP_118466944
VERSION     WP_118466944.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides clarus
  ORGANISM  Bacteroides clarus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1127)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1127)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1127)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1127
                     /organism="Bacteroides clarus"
                     /db_xref="taxon:626929"
     Protein         1..1127
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125516
     Region          43..1123
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfikkewge asyrklhlqk glgimgmvla flfaeniyaq dsqtikgmvr dvtgepliga
       61 sviekgtnng vitdvdgnft lkvpadatls iaymgyatre iklarrkkqg dlrvtlreds
      121 qqlkevvvta mgikkdtkrl gyavstiesd eivkagatnf asamygkapg iritqtqggs
      181 agavsinvrg ltsitgnnqp liildgvpir nggtgkstdf aefgndgqir snglvdinpe
      241 diesisvlkg asatalygse aangavvits kraksgkltv dftaqvtanl paylpkvqtl
      301 ygpgryntdy sdyekqtggf yqrtmngeny kslynttmsf gpkydgsdvl ywdgkvrpyl
      361 patdnpwkel frtgwnqtyn laisqgtets snrfsytfmd eipnsltgsf tkhnfkltgs
      421 yklakpltle yslnyiiqdv kdrpqtslnl ygsfgnmfss fmdipylkqs yvtslgyrnt
      481 yaiggdatlt pdeswaydpg ylsgvsnmlw nmyhhhseet enrligmirp twqitnwlsl
      541 raqlstditd tkqtleyete rpnslydpsg sfqninrryd ivygdvmlnf nynirrfdia
      601 atlgwtgrye nmnnmrvstn gglvtenwfd lnasrytass tlqrmellkt gymgtlslgw
      661 dnylfleltg rqersstlkd qsffypsanl sflfsnafrm pawwnhgklr lsygivgnap
      721 etyaaniiye qgsdngftwn yvpsswgnan irpekkyeye igleskffnn rlgfdvsyyn
      781 nrvkdqilst pqpsssgvky vlmnvgevan egwdisvsat piltkdfrwd ltanygiyrn
      841 kvvklaegvp yleisniggg gakiqavegr pmgdiyvqvp qvnengdylv sdkglylnqt
      901 dlqrvgninp dgvgglfssf syknifldfs idfriggdvi nemyqystas gltpeslqyr
      961 dtehgglsyy ypgnnnasgv pvqvdpslga gpngeviyhd gvilpgvvas tgekntriip
     1021 agyyynqtyn wgtqpeqyty rhsvfdntyv klreltigyq fpeklisklg mtrlsvsvfg
     1081 rnlfyfykal knydaessvg tswasqavvg gsttatrnfg islrasf
//
LOCUS       WP_118466696            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            clarus].
ACCESSION   WP_118466696
VERSION     WP_118466696.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides clarus
  ORGANISM  Bacteroides clarus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Bacteroides clarus"
                     /db_xref="taxon:626929"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123842
     Region          32..97
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          115..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msiflmipcs vfgetvvkwn aeenlftvqa tnstvkdiln yiethsdyvf vysenvqkvl
       61 nnkvsisvvn rkidtilkel stqtkleyki sgrqviismp qvdktqqein kknvkvtgnv
      121 adengealig asvmvkgstm gtitdidgnf sldafkgatl lisyigytsq etsidnrtsf
      181 kivlkedskt leevvvigyg tvkkkdltga vaavkgddlv akktttlsta lqgsvsgmmv
      241 rrdnnapgas assihvrgit tmdnseplii vdgvqcdnid yvnsndveni svlkdaaaas
      301 iygakaaagv ilittkrgsq sdlnltytge fgweiptkqp smvgvtryle mnnellyndn
      361 pggglfqlyt sdqvknwvky nktdpnnypi vnwrdlmlnn saprqthtvs lsggnksvrt
      421 qaslsydevd glydgrgfqr ymfrvnndft indklsatld vnirhaknrn siydpfgdmr
      481 kmpavypatw ddgrlasgks ganpygllly ggrtvahstq iggkaalnfk pfdglslqai
      541 vapfinyqkn kkfrnqvsyt lmdnpdaigg nlegggvtys tnelteerkd nwhvttqvia
      601 nymksfgkhd itlmagyeny vmkkeeltag rdqyeltqyp ylnigpedym ansgtgseyt
      661 snsvfgraiy syadrylfqa nirydgssrf asqyrwgtfp sfsagwvvse ekfmrnanid
      721 wlsflklrts wgmlgnerig dnyfpymalm tfnnalfykd gavvsektaa qrnlavedit
      781 wetttstdig vdlgflnnrl rvtadyywkk tkdmllsiei pysmgyanpk nnagkmsttg
      841 fdleiswndr indfsygisa nlsdfkskid ylrnsdiisd gkvkragvlf newygyvceg
      901 iyqtqeevdn satlnnqitv gdlkykdisg pdgvpdgkis adydrvplgn slprfqyggn
      961 ihagykgidl svafqgigkq nayltkemvq plrdnygnip sivdgnywsp fntaeenaka
     1021 kyprlsqvnr dsnyatssfw lfngayfrlk nvtlgytlps vwtqkagikk vrlyvsasdl
     1081 fcisnypegw dpemgvssyp ittsllfgls vnf
//
LOCUS       WP_118470852             476 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola dorei].
ACCESSION   WP_118470852
VERSION     WP_118470852.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola dorei
  ORGANISM  Phocaeicola dorei
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Phocaeicola dorei"
                     /db_xref="taxon:357276"
     Protein         <1..476
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <18..475
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 cnsilslyls afhffvvtlq ynyaerymls gslrydggsv fgannkwgif pavsggwlvs
       61 nekffknwrm swwntlklra sygvtgnnsi sntaayptls agnyagapgy kanslgnadl
      121 gwekthstdv aldlgffnnr iqlsldwytk nttdllyqvp vegasgfttv wdnlgdihne
      181 gfeielnthn ltgkfswsts fnmsynknev kalgkdntpv ysgfdknnps niltvgkpvn
      241 tfymydaigv wknqaeiday saahggkpvt fegkqivpgd irykdvnndg vfdkdndrdy
      301 lgsptpklvf gmtntftyrn fdlsilmtaq tggkifgvlg raidrpgmga kgnalghwre
      361 awwsedepgn gkvpyilsst tgatldsrwl yssnylrikn ltlgyklpin pkfisyarvy
      421 vsienlakwd syyggyspea antaassspg gssalgldyg gypspriytl ginvnf
//
LOCUS       WP_118476790             910 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118476790
VERSION     WP_118476790.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..910
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100849
     Region          24..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrirnlfcl slllvavglp avaqtklhva lpdsittvgy atglrknlsg lveritenqm
       61 nkdqitnpld airgrvpglt ilkgsngpaa ldavrlrgtt slttgndpli ivdgvfgdls
      121 mltsiypadi esfvilkdas etaqygsrga sgvieittkk gvsgrtsvny ngsfgiassy
      181 ktvrmlngne frtlaqergi sildmgnntd fqkeieqtgl qhnhhiafsg gtntsnyrvs
      241 lalmnregvi vneklqnfts nmnmtqyvfd nflkcdlgmf gsvqkernlv nlhkvfysaa
      301 synptfpnhk npetgswdgy ayasqlshpl awmdvkdkna tshistharl tfnlaeawkl
      361 tffgsytynv venaqylpva vwaqgqayrg dkkmesllgn lmlsykkewr khffdvlgla
      421 eiqkdkysgf yttvtnfsnd klgydnlqgg airpwdgtns yyedprlvsf mgrvnytydd
      481 ryiltvnarg dasskfgsnh kwgffpavsv awvvskekfm eklsfidnlk iragyglagn
      541 qngidsyttl nlmrpngiap vgstpvvtmd klrntnpdlk wevkqtfnag ievallgnrl
      601 lltanyynsk tkdmlylynv svppftyntl lanigsmrny gtelsigitp lktkdmelni
      661 nanltfqqnk llsldgnyqg ehisateyks lagldgagfh ggynhivyqi vgqplgvfyl
      721 phctglvsdg nggytyqiad lnsggvsled gedryvagqa vpktilgsni sfrykdfdis
      781 lqingafghk vyngtsltym nmnsfpdynv mkkapaqnik dqtatdywle dgdyinfdyv
      841 tlgwnvplkn trylqslrls ltvnnlatis gysgltpmin sssvnatlgi ddkrnyplyr
      901 iytiglsvnf
//
LOCUS       WP_118470942            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola dorei].
ACCESSION   WP_118470942
VERSION     WP_118470942.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola dorei
  ORGANISM  Phocaeicola dorei
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Phocaeicola dorei"
                     /db_xref="taxon:357276"
     Protein         <1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 dgdfslsnvk kgdiiqisfv gyqtqevkwt gqpidvtlkd dtqqlgevvv talglkreek
       61 algyavtevk gdelkaanti spvaalqgkv agveisgsdg glfggtkiqi rgastlssnn
      121 qpiyvvdgvi ldngvsgntt adwdaganna sdygnelknl npddfetvsv lkgaaataly
      181 gsrglngavv ittksgkgtq glgisvsqtf gidhafktpd iqtlygpgym pgqsdadqng
      241 siwdahqftv nqngehtlvg vpnfgfgpky dgsqirnydg twttysprkn nmldlyklgf
      301 ntntnvsirg gnektsfyts lsyknakstt enntferysm llkashklnd wvdvaasfsf
      361 anskprnaql nagelfvnan tnvinplfdv dyfrnkylge hggiastsyg dqygsvpssa
      421 knyffkvdny dyvrketvir ptfevnvkmt dwlkfkadan mnryytsied kqlgsgyane
      481 ggyygitqdi keqftvggtf taskqikdfs lggfarfeyy ntsskhskvs tdggmvvpge
      541 wfvenskktk kseatisgsk riistifaln lgwknqvyld vtgrndwssa lvyanrtgnh
      601 syfypsvsgs wlinetfres mpswinlakl raswaqvgnd tdpytvnqty sfatmemydg
      661 niytneldkl mkiadlkper knsweigldf rtfnnrlnld ftyykenttd qimkinvpai
      721 sgvtqqlvna gniqnsgiei alnttpiktk dwqwdldfty trnrskivsl hpnvanyiel
      781 sgyvnaydyh igsvakvges ygvlmsdvtq arnengvpll ewddswrgay raqsktaevv
      841 gnmtpdflgs vattltwkdl slnigldmrf gglvasycnl ygtqagwtes slqyrdpehg
      901 gmtwtsqyad skgiqytdgm ipegvfkegt iatlvdgtkm dvsglsyaql vqegklepth
      961 agswygnnya wgaqtiddiw vhklsyialr nitvnyrlpn sishklgakg lnlsfsarnl
     1021 gylynslpnn lnpesvrsns asefrirgfe pytasyifti nanf
//
LOCUS       WP_118468541             910 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            clarus].
ACCESSION   WP_118468541
VERSION     WP_118468541.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides clarus
  ORGANISM  Bacteroides clarus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Bacteroides clarus"
                     /db_xref="taxon:626929"
     Protein         1..910
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100359
     Region          46..909
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqyrklffl gficaawpvs yaqaqdvsag vpdslltigy tvghtrniss lvesftgkql
       61 kadqitnple aiygkvpglt iqraangtaa ldavrlrgtt sltsgndpli iidgvfgdis
      121 mltsvyptdi esftilkdas etaqygsrga sgvieittkk gvkgktrvsy ngsfgvasvy
      181 kslkmlsade frkvaeqtgv siidkgnntd frkeiqqtgf qqdhhiafyg grdessyrvs
      241 lgymsregvi vnenmrnfts nmnmtqslfd gfircdvgmf gsvqnnrnlv deqktfysaa
      301 afnptfpnhk ngdgswdgvt nasqitnpla wmevkdkesv sristhakll lnftpdlkmr
      361 lfgsysynmv ensqylptgv wahgqayrgv rkseslvgna mltyrkrlkr hfidalalae
      421 vqeekfsgfy ttvtnfssdl fgfdnlqaga lrpwegtnsy yertrllsfm granytyadr
      481 yvltvnarad asskfgdnhk wgffpsvsaa wnvteedfmk rfplvnnlkv rvgyglagnq
      541 sginsyttlr laqpngvvpv gsapvvslse lrntnpdlkw evkhnfnagf dlalfanrll
      601 fsvnyylskt tdmlymynvs vppftyntlv anigsmrnsg veiavgvtpl ktkdmelnin
      661 anvsfqqnkl lslsgvynge riaaaeyksi ssldgagfhg gynhiayqiv gqplgvfylp
      721 hstglvsdgn ggykygvadl ngngisledg edryiagqav pkatvgsnis frykdfdlsv
      781 qingafghki yngtsltymn mgifpdynvm kgapqvnikd qtatdywler gdyvnfdyvt
      841 agwnvplrgt kryvqnlrlt ftvnnlatit gysglspmin satvngtlgl ddkrnyplar
      901 tytlglsinf
//
LOCUS       WP_118476827            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118476827
VERSION     WP_118476827.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121556
     Region          27..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekhrflmwf allfigvvsg yaqqlaitgr vldskkepli gvtillkgsa ngtvtdidgn
       61 fsikaskget lvvsyigykt qeillssdkt tmtvelleds emldevvvig ygtmrkkdlt
      121 gsvtqvrpda laneapktvq dvlrgtagln vgfdksakgg gsmsirgqrs vysdgghndp
      181 liildgmmfy gelseinpnd iaqidvlkda ssaavygaka angvvivttk kgksekpvis
      241 fsanigwtar adgrkvydad gylnyrrdfy ttdtygvnps tgkyeayqtg grpagyfdrp
      301 tdtnlgkygl smdawrnqtt qdagmssdei warriglnas evtlanflsg ktfdwydhsf
      361 qtglnqdynv sisgmtervn yylslgylsn egivrgneyn airanmklda kvtdwfsvga
      421 nvnfqnrsdg diavdwyrqi tsnspftspy neagelvahp qgenaywkgy nfdfdrqyld
      481 lekgftvlnt iltakltlpf gitysfnaap rlqyfydryy rssehpdwqa etedrvnreq
      541 skrfdwslnn titwdytfak khhtiltlvq eaeerqswad riqarnilps ealgfhgtan
      601 gdknlsefrs tdnretacgy larlfysydd kymgtfsfrr dgysafgttn pyanflsgal
      661 awtftnedfw kwgdilesgk lrvsfgqngn rslansyial anlalgmysq gyinsttgtl
      721 ldmkylfvdr lpntglqwek ttswnvgldl sflrgrinas leyyimpttd mimnqslpdf
      781 tgfasittnl grvenrgfei slntrnietk nfewntsfsf srnkneikkl ygeyetivda
      841 agntitkekd dvdnkwfigh pisaiwdyev tgiwqvneve eaakygqkpg dpkvanhyta
      901 ddrknadgtt tavynnndkr flgettppih wsmrnsfily knwsfsfnly symghkslds
      961 nylnndnnys qitncqniyt kkywtvdnps ntyarlsaqg ptglaapsrv vdrsfirlen
     1021 vsvaynvpae llsrfkiqna kifatvrnva twskeweygd petgdiaprt yslginltf
//
LOCUS       WP_118477311             938 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            intestinalis].
ACCESSION   WP_118477311
VERSION     WP_118477311.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides intestinalis
  ORGANISM  Bacteroides intestinalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Bacteroides intestinalis"
                     /db_xref="taxon:329854"
     Protein         1..938
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106145
     Region          23..913
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrkfiyigc tvfamslfha gsiqaqeenk dslvnvafgt vaqkdlthai stvntseltk
       61 kvnsssslvg lesliggytg siwgqealil vdgvprsasn vrasevenis vmkdaaavvl
      121 ygsraakgvi littkrgkne pmhidvrgna ginipksypk yldsdcymtl yneacrndgl
      181 sekyntsdiy ntamganpyr ypnidfyssd ylrkayynad mtgevyggne rthyylnfgm
      241 dysndllkyg esknaynmrf nvrgnvdmtl aswlkattna aivytnqyag rgnfwgvast
      301 lrpnwfapll pidmmdtnvs qiqeyiansn hlldgkyllg gtssdmtnpf adllaagyvk
      361 ekarmfmfdv slaadlgsll kgltfktfys vdytsyysea fketyavyep twaqvngkdm
      421 ivalkkhned kkdpneyigk stydqtmtfs aqfdyartfe kfhnvaatfm gwgyqtqksa
      481 denhessdyh rtsnvnlglr asynynhkyy idfngavihs aklpegkrna fspavtlgwr
      541 iskekfmenv dfindlkvta syaklhqdld isnyylykgt fskegyyvqw hdgtaggwtp
      601 vskrgdnpnl dfitrkefra gidatlfnrl lrlnanyfkq dtkglltqga sfihpayfal
      661 gsnssfmpwi nynedrrsgf dfslsankkf gdfnvtlgfn gmvyssealr rdelydedyq
      721 frkgraldas ygyvcegffq dqtdidnhar qtfgtvkpgd lkykdinedg vidnkdqiel
      781 gkngwaappf sfglnltvkw knfslfamgs gqtgaidyks ssyywnrgts kfseivwgrw
      841 teetkdvaty prltttngdn nyrnstfwmy krnyfrlnqa qltydfpent fkgtfirgls
      901 vycggnnllt iskerkhlel stgspqcrnf yagfkaaf
//
LOCUS       WP_118481683            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118481683
VERSION     WP_118481683.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118529
     Region          24..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrklmllla clfvgiglvt aqtqkvtgvv iseedgqpvi gasvlvkgtq igaitnvdgd
       61 ftllnvpssa ktllvsfvgm qtqeveikph vkvtlksdse mldevvvvay gtasrqsitg
      121 avasidskkl emrpvtevtg tlegaapgiq vnnsygepgs dkseirirgf gsvngtnapl
      181 ivvdgspygg slndinpqdi esisvlkdas saalygnkaa ngvimittkk gkshklnfri
      241 gvkqgmytrg ipeyeklgvn qwmeamrsgm qsyyqknggm pveqafeask nvntivkspi
      301 fdksgaemfd engkfianvk pgyndldwld alertgyrqe ytasadamgd kydifssfgy
      361 lnergyiigs dydrftarlk anyqptkwfk tgvslsgtms gsnyqanayd qyyanpfyta
      421 gqmapvypym lhnedgsiat dengnsydin nykylsgrni iyeikndinr kernavsgqv
      481 ygtvsflkdf tatvrgdlyn vnntekafnn pycgdgaann grlskmhart reyrftqelt
      541 wghdfkqhhi dvllahesfk hsynydfmmk eqmkvsgnte msnfakmtsi dgytqeytte
      601 sylsrarynf aeryfvdasf rrdgssrfye pwgnfwslga swiisqekfm knltwidnlk
      661 frvsygevgn dagadyyayk elfysdvnag igafykiqip nknlkwetsg sldialegrl
      721 fnrfnfsldf fnktskdllf tvynplsaga tdwyatsdet psgmsqyfan igsvrntgle
      781 vamdvdairt kdwkwnigln lttihneitk lpggkdilhg tqnyseghsi yefytytyag
      841 vdqmngraly tansnlsent isalkasgny vtindknyvy ntsyaekawq gsalpdvygs
      901 intslswkdl tlsvlctysl ggkvydynyq glmytttngp salhkdvlng wqavpegmta
      961 dapnrldpng tpqfdlsgla stsygassrw ltdasyfvik ninlnyafpk rvvtkwglsg
     1021 lnvygsiena atftarkgmn pqysfsgsqd ntfvaarvft lglnlnf
//
LOCUS       WP_118482763            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Phocaeicola].
ACCESSION   WP_118482763
VERSION     WP_118482763.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola
  ORGANISM  Phocaeicola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Phocaeicola"
                     /db_xref="taxon:909656"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111764
     Region          26..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkrsflvvt mfligmfltg iyaqtitvsg svtskemsdp ligvnvlvkg ttngtvtdln
       61 ghysitvgpd dvlvfsyism qtveeavkgr kvidvsmvsd teslgevvvt amgiqrqset
      121 ltysaqtvgg sdvndiksvn minslqgksa glmitpnstg aggsskilfr gnksisgsnq
      181 plivvdgvpv mnsvsgaqvs snyggerdgg dvmstinpdd iasitllkga saaalygava
      241 angaimittk saqsgkvsin vssnttmetp mvlpefqnty gvsdngtysw geklaseapn
      301 yakefyrtgf ttnnsislag gneniqayfs ygnvysegmt psntyrshnl nskvgfnvlk
      361 nihidfsaky tnqyvknqaa agflfnpltg vylfprgedw nyyknnfevy desrgcniqn
      421 wtntglqqys npywtlnrqt pitdrhryef ggsikwditq dlniqgrmry ergeerwqhn
      481 lyassianly pmgrmkdnry fsdqlygdvl lsyshtfndf lvsatagssf tksktahvdl
      541 waegtqftsp gngniyypni ftpnnyygnm svvgkndnwn tekrlnavfa taqfgykdgl
      601 fvdvsvrndw ssalaytesc sffypsiggs flldrfvdmg knvnllkvra sysivgndvp
      661 vfmsnllysl qsqgaitppe napfrtlkpe kthsievgfd gtffqnrltm gltyyktntk
      721 nqffsvaapy esglrnryvn agnvqnqgfe fsagwyqqfn ddfswstdln lsyndnkive
      781 lvddlpnglt ltdfggakii lkkdgsygdl yvrhimrden grpmkdettg npivsgdtte
      841 dmiyagnmna kfnagwsntf hykdftlsfl idgkfggkvl smteatldgw gvskrtgdar
      901 nagkvvvdgv efdpkawytt tgasnfnspy anefyvydat nvrlrelslg ytfrnlfgvg
      961 knltaaiigr nlfffykdap mdpdvsagtg ngvqgvdmfa lptsrsfgln lklnf
//
LOCUS       WP_118482673            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            coprocola].
ACCESSION   WP_118482673
VERSION     WP_118482673.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprocola
  ORGANISM  Phocaeicola coprocola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Phocaeicola coprocola"
                     /db_xref="taxon:310298"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125904
     Region          60..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkfmtrkht eehlssrker fsdlmgkglf llafssalst niwaqttttt naqttsqnft
       61 gkvcdskdgs sligctvrvk gkkaatitda ngnysitakp gdiliisyig yetvevpags
      121 kkasnifmvd dsvimddvvv tgyqtlkkfn vtgsvntinn ekislrsstg lngllegtvp
      181 glnvyndnfr irggasmnsg ndplfivddf eveelpenmd mvesitvlkd asataiwgsr
      241 aangvivitt kkgkandfki sysnnfkvsa kpnfddlhra sseqiidydr eahlygynsm
      301 mggfgyqgag yslsqeilnd ywedvvidwe tgsvlpmdpt klaemdarln klktysnrkq
      361 lednllrnaf rqqhlvsisg gnerinyyls gsfigghsey vgdknrsyni nsrmsykllh
      421 nltlrsdlsa tfdnndngyt nlssdiynmf pfqmlldeqg nriadytqfs rmdadkytse
      481 ygylsfgknl ldevdlannt tkntdykarf gldyrilegl nlsadyqyer yqsinkdiqs
      541 vnsysvreli nqhtvineng lsyripkgdi ldhsqndiea wtmkigatln rnfgidkqhy
      601 vnatagfevr skhsttetyr klgyddqvls wspidavdla tngttppwyd ypmryyassy
      661 dgfndilnre vsyylsgvyt ydnrytvsgs lridksnlfg vsdkyrrnpi wsfganwnik
      721 nekffhcdai talmlrasvg ltgnfdrsgr tspimigqfi ssdlvdgggy mrittppnpl
      781 lrwertrsin lsvdlglfdr vnttftyyhn kgydllgeaq ldptvgyseq linsadmnnt
      841 gmeiqldadl irtrdftwnl gwvfgynkne itrnsahdss pvlnrvhgit rfvegysres
      901 iwsyrwagln emglpqayka dgtkvtsyed ldvedleysg tyqpkysgsl stgfrykslq
      961 anflftynfg hvfrveypdm npfgsspaln eriadrwrqp gdenktdipa icsdmmnylm
     1021 tyqtgasela qyssnsirkg dmirlreill nyelpkkwlh nspvkrlsit aqlnnvwlwt
     1081 ankegydpea vfpvsgtfsl tdpiaftcgv kldf
//
LOCUS       WP_118483049             993 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            coprocola].
ACCESSION   WP_118483049
VERSION     WP_118483049.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprocola
  ORGANISM  Phocaeicola coprocola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Phocaeicola coprocola"
                     /db_xref="taxon:310298"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108970
     Region          2..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvvsfiglet qevtikptvn vvlrsdaeql devvvtamgi krsekalgys atsvngekis
       61 asrtsdvmss lagkvagvqi satssdpgas nsviirgvss lsgsnqplyv vdgvpldnss
      121 vsssdglnsg fdfgnganav npddvenmti lkgaaataly gsraangvvm ittksgkkgk
      181 glgieynggv qwssvlrmpe mqnefgmgws gshttlengs wgprfdgsmq lygnvynnsq
      241 kikpyvaved nmknffdtgf rynnslsfng atdkstyfvs fsqisddgii ptdadsynky
      301 tfsgrgshki gnltfstsln yayqdnkfat tgqglsmans lwqtprdinv esladlndpf
      361 ntpgyyytpy gvmnpyyile hnlntynser fygkfqldyd flkyfkftyr mgldsttgqt
      421 eygaenlyal yyegtpngeg mgasspfagq ygeysimttr rreinqdfll sfdmpindfh
      481 vnalvgfngn erkysyqksa vnnltiptwf nlsnssqtpt vtqyselrrl mgvfgqfegs
      541 wknmlyltvt arndwsstlp kgnrdffypg vtgsfifsel lndeikdiit fgkvraswgk
      601 tgndadvyml spvygsaqys ipfgylkfpl sgvnsytlgn ilgsntlspe mtteyefgln
      661 maffnnrlsf daayynrnsd kqimslsmdp atgygsqnin lgkisnkgve llvsgtpiqt
      721 rdfswdvtvn ftknwskvvs lpeelggetv iyglngstsm yaivgqplgv fkaeaverdp
      781 qgrivadant glpvaaaefa tygdmnnryq mgvsttltyk gvslsadfdi rqggimyskt
      841 kntlyftgna iqtayndrnt fiipnsvnkv tnadgsisyv enttpvssad icnyyydpmg
      901 giggeidlid ksyvklrtvv lswdlpkkwl aktplqgvri saygnnlfiw tpssntfidp
      961 ettsfgndls gnygeyssnp tsrnfginln vkf
//
LOCUS       WP_118483606            1132 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            coprocola].
ACCESSION   WP_118483606
VERSION     WP_118483606.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprocola
  ORGANISM  Phocaeicola coprocola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Phocaeicola coprocola"
                     /db_xref="taxon:310298"
     Protein         1..1132
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124751
     Region          56..103
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          125..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrsknsckcs kkllrallls tlfavpsqfa saqlnialsn aqlgtmikqi qsqsqyqffy
       61 dddladtpis svnvkdasve evlntalagk gisyrvdenv vylskastsp sasstllkaa
      121 qqqtktvtgr iidakgepli gvtviekgtt ngaitdfdgn yslsvpdaav lqysyvgyqt
      181 vemsvagknv iditmkedte vleevvvtal gikrsekals ynvqqvnaee ltrnkdanfi
      241 nslsgkvagv tinasssgvg gvskvvmrgt ksimqssnal yvidgvpmya gtneggtefs
      301 skgatepiad inpediesms vltgaaaaal ygsdaangai vittkkgkeg rlsitvnsnt
      361 eftntfvtps fqnrygtgss ltegdqihsw gkrlnesnsy gfdpvsdyfq tgitgtesis
      421 lstgtdknqt yasaaavnsr givpnnkysr ynfsfrntts flddkmtldv gatyvlqkdq
      481 nmvnqgtynn pivgaylfpr gndwedikmy erydpvrkin tqywpvgdag ivmqnpywvn
      541 yrqlrnndkd rymlnaslsy kildwlsvsg rvrldnsint ytekyyagtn tqmtemstrg
      601 lytnatskdk qlyadflvni nktfgedwsl qanigtsftd mrsdvleirg piadgtsafe
      661 getpglanef niqnlsakkt srlqsgwreq tqsifasaev gykstyyltl tgrndwpsql
      721 agpnstsksf fypsvgasvv lselmpnlnq dylsymklra sfasvgtafe ryianpryew
      781 dsstgqwsnt tqyplynlkp erteswevgl tmrflkdfnl dltyyntvtk nqtfnpelgv
      841 sgysalyiqt gavrnqgiel slgyekewnk frwssnytfs tnqnkilela dnainpatge
      901 sfsistlnmg glgsarfllk eggsmgdiys nrdlkrdang niyvdatgqi atetisnvdd
      961 yiklgsvlpk anmawrndfs wnnfrfgfmi sarlggvvfs rtqamlddfg vseataeard
     1021 lgyvlvngnd qinpeawyrg igsgdavaqy ytysatnvrl qeasigytfp rkmlgdvcdl
     1081 tislvgrnlw mlyckapfdp envastnnfy qgidyfmmps trnigcsvtl kf
//
LOCUS       WP_118483983            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            coprocola].
ACCESSION   WP_118483983
VERSION     WP_118483983.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprocola
  ORGANISM  Phocaeicola coprocola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Phocaeicola coprocola"
                     /db_xref="taxon:310298"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121633
     Region          23..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksllltll llvhvcaawa adkvitgnvi adddkqplig vsvyvsaddl kkagsslmsl
       61 gvvtdidgnf sitvpsgvkk lqlsyigytt qqielksgqt hynialqpss tmlndvvvtg
      121 yqtverrklt aavakidise grigtvksid qalsgqiagl savstsgapg spvkirirgt
      181 sslngtqdpl wvldgipleg tdipsleslk niddvqqssi aglnpadiad itvlkdaaat
      241 aiygaraang vivittkngk agktkinfst rltwspqqni drlnllnase kvdlelqlmk
      301 sdyamnaekg eiyrilnryn aidafkkdgw dalskeaqne inalrlintd wndillqdaf
      361 sqeynlslsg gnekatyyts lgyskeqgni pnvssdrlnl vmkanykvnr mlkfgtsvfv
      421 nrrkngsyls tdgftnpmfy arianpyltp ydkdgnyvyd sdiqngnsdl lfntfeerqn
      481 tsnettinsl ssifdvelrf ddrfkitsqv glqldktsre qiadqesfam rlehknhryn
      541 gtsflpqkgg fhkayensds qvtwktmgty rdtyadihef eimvgselrr twattlysag
      601 ygydrrtmtn qpvvfpsdsq afplhtktnv enayvsafst msysllnryt lggsirfdgs
      661 dlfgvdkkyr ylplysvsal wriseepfte nakwldnlvi rasyglqgni dkntspyllg
      721 kyqsnatpil pgntedmivv tsapndklrw ekthsvnvgl dfavlnqain lsvdyyyrkg
      781 vdligmqmlp letgfsstni nwasmtnkgi eiglstrnih tksfmwtttf nfaynqnkvl
      841 keairedaiy psregypaga ifafpyagid engqmtfynk etgkvesmke ffkvqefgfg
      901 tynlshaelr nkyeyigttd spytggfnnt ftykawelgi ncifnaggyv rvqpsyslts
      961 fdrgqntnrd ilnrwtpenp ngtmpalvds ntdmdayffl dgavnpyays slwvkkqnym
     1021 riqsirlgye lpfsliqklg isqatvaleg rnlfvfgssy rnyldpetmg npyaqpipks
     1081 ftfslnlnf
//
LOCUS       WP_118484529             913 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            coprocola].
ACCESSION   WP_118484529
VERSION     WP_118484529.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprocola
  ORGANISM  Phocaeicola coprocola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Phocaeicola coprocola"
                     /db_xref="taxon:310298"
     Protein         1..913
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101818
     Region          23..912
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkyrkaksk yiavcsltlw lyqpvnaqie itilpdsvit vgyargtlkn isgsveqite
       61 qqmnkeqitn pleaiqgrvp gltimkssng taalesvrmr gttsltsgnd pliivdgvlg
      121 dlsmltsiyp tdiesftilk dasetaqygs rgasgvinit tkkgisgktr inyngsfgia
      181 hayrhldmls gdeyrkvtse ngisildkgc ntdfqkeieq lglqqnhnia fygggdasny
      241 rvslgylnre gviqnesmkl ftsnmnmsqd ifdkfiqcel glfgsvkknr nlfdyqktfy
      301 saaafnptfp nhkdyttdaw dqittasqit nplawmevnd rddvsyfsah arlnfnlspd
      361 lkfilfgsyt yndtensqyl ptivwangqa yrgnrrlesv lgnamltyrk qlkkhfidvl
      421 glaeleknty tgfyttvtnf ssdlmgfdnl qagalrpweg tgsyyeephl asflgrvnyt
      481 yddryvltvn artdasskfg anhkwgffps vsaawnvsse qfmkqitwid nlklrlgygl
      541 agnqggidsy ttmnlvrpng vapvgnspvv tyetlrninp dlkwevkhtf nagfdvgfyg
      601 krlllsvnyy nskttdmlyn yrvsvppfty ntllanigsm rnsgteisvg itplktkdme
      661 lninanitfq knkllslngm yngeyisase ytviagldga gfhggynniv yqivgqplgv
      721 fylphctglv pdgnggykye iadlngggin ledgedryva gqampktllg snisfrykrf
      781 dvslqingaf ghkiyngtsl tymnmnilpd ynvmeeaprq mikdqtatdy wledgdyinf
      841 dyltvgydvp lkntkflhnm rlaftinnlg tisgysgltp linsmtvdst lgvddkrtyp
      901 lsrtytlsls lnf
//
LOCUS       WP_118484624            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            coprocola].
ACCESSION   WP_118484624
VERSION     WP_118484624.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprocola
  ORGANISM  Phocaeicola coprocola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Phocaeicola coprocola"
                     /db_xref="taxon:310298"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115838
     Region          32..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mflllmvsgw gaawatpekv idastlqqsa kittqgtivd aqgepligvs ilevgttngt
       61 itdidgkftl qvasgatlei syigyktqkl aakpnlgtlq maddtevlde vvvtalgikr
      121 sekslgyamq evkgeslvaa retnlanals gkfagvqitr ssngaggssk iqlrgansvt
      181 gfnqplivvd gvpmdnftga ndfsgkshnd ywnpgtdmgn glsdlnsedi esmsvlkgas
      241 aaalygsrag ngvilittkk gkenpglgit isasvsaeti fmkpnrqttf gqgddgvysg
      301 tssnswgpri egqeytdwag vkrnmtyydn idsyfntgvn ttesfslsqm ynktsiyasv
      361 trmddankip ssklhrtnmt lraattfgkd drwsfdakiq yinsiaknrp ssgadgssfl
      421 smyttpvsld itdfkkclde ngdmrwwqrd sglnpywgqe ynlnqdsrnr flmnaslkyr
      481 ftdwlsaeik agsdmyftet etklydgspi vdngrysfge qkfyennysf lilaqkdnll
      541 gnwggnltlg gnmmerrstg lknglgklti pnqfwitngd kgdlsqdqsf trkkinslyg
      601 tlginydgwa fldatfrndw ssslskknrs ffypsvslsw visdmmnkle knmpswltya
      661 kvrasfaqvg ndldpyqlyn lykistngst ggilaetsgt vlynenvrse lissweagae
      721 irffnnrlgl dvawyksnak rqlldipmnr lsgyesmkvn agniqntgwe imlnatpvqt
      781 kdftwdmnin lstnknkiie llpgeeyknm tytlggydnl yvyavaggny geiwgtkfqr
      841 vtdenspyyg klllneaglp qgtstpekig dqqanclmgw tntfsyknft lsflidgrfg
      901 gdifsgtnri lqaygvaevt apggnredfv vdgvisdgkg gyvpstiavs qedywravst
      961 ssgnlgigea nlydatnirl rnvslnysip ksalkntpfq qvklgvscnn vwmikshlng
     1021 idpesvyats tnatgfenla aptsrtylfn vtlgf
//
LOCUS       WP_118485156            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            coprocola].
ACCESSION   WP_118485156
VERSION     WP_118485156.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola coprocola
  ORGANISM  Phocaeicola coprocola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Phocaeicola coprocola"
                     /db_xref="taxon:310298"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117511
     Region          43..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkncrytl lcgtlslcfi ggispmkait qpvhsaveqq thtvtgtvtd atgpvigasv
       61 iekgnttngt itdldgkftl nvapgatlvi syigyktiei easkkplniv maedskvlne
      121 vvvtalgikr erkalgygvd evkgesltka ketnvinsma grvpglvvsq taggpsgstr
      181 vilrgstemt gnnqplyvid gvpldntnyg sagtsggfdl gdgissinpd dienmsvlkg
      241 paasalygsr ashgvilitt kkangkekfs veyngtltfd tqlakwndiq qvygmgsngt
      301 ysidaisntn kswgpkadgs nmltyfdgva rpyliipdnt sgffqtglta tntaiisans
      361 ghtgvrftyt dmrnkdivpq snmsrdifnl rtntslgkvd vdfsanytre avknrpalgd
      421 sksnigknlm tlattydqew lknyqdenge ysnwngmdpy nvnpywdvyk nsnnskkdqf
      481 rfngkaiwni nkhlklqgti gaelnyfife dfkapttpgy eagylqnsnf rnrmynfell
      541 alynntwgdf dfnatlggnv ykinnqttvt taqdmqirdv valmsfnets leqnsyrkqi
      601 nsvygavnvg wkhlvyldat lrgdqsstlp ignnvyvyps fsgsfvfsel lkqsdlmpyg
      661 kfrlswaqvg sdtdpyqlgl vyskskftyp gytigyinns tmpnknlkpt ktnsfelgle
      721 mkflknrigl dftyytqnsk nqimgmassw tsgynyrlin ageienkgie ialntrpiel
      781 kdfswdlnln fsknsnkvkk lvdgmdmfel ekaawldvqv aakvgenfga ivgpdfkrne
      841 ngdilidpqt glpqydksnh vlgnaswdwt gglgttltyk nlslsalfdi kvgadlysms
      901 arasyesgks ketlagreew yrseeqrqaa giakgspdwt ptggfiapgv idngdgtyrp
      961 ndiyinpedy wmsvcrnaps mfiydnsyik creitlsyrv pqswlknvvk gltvsfvarn
     1021 pfivwknipn idpdsnynnt tgmgleygsl psrrsygfnv nlkf
//
LOCUS       WP_118493758             948 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118493758
VERSION     WP_118493758.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..948
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106853
     Region          43..947
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkniriksvl caalatssly vgaqnlpsel ldassdslsv aeeelvqvay rkvnkkdllg
       61 gvssvnveel mkkdyftysl dgmenmvsgw ngsslwgmds ylvlvdgvpr dannvmpsei
      121 kditflkgas avvlygsraa kgviyittkr gkegdtridv rgntgffvpk sypkylgsae
      181 ymtlynearv ndgmdplysd vdiynhgsgi npyrypdvnl ysddylkkay nqsdvtaeis
      241 ggsekarfyt ninlyntgsl ikvgnakddr ttrfsvrgni dvnlgqyvkt yvnanatfyd
      301 grsargnfwg aaaslrpnri splipvdyim qnntdawnlv nnsrylidgk yllggtqvdq
      361 tneianlyaa gvntytsrqy qfdmgvdvdl smllkglsfq trfaidyatt ynryygdtya
      421 tyepqwanvn gqdlivgltk ygddvhdgiq hiadswnrqt mafsaqlnyn nkfadshnis
      481 amliaagyqq gesavyhkts nvnlglqvdy dylskyymsf ggalihsarl pennrnafsp
      541 sltlgwrlsn esfledssvl ddlmlsvsgs vlntdlgidd yymyqssydq angawwgwad
      601 gnqshatear rgnnsdlsfi krkeisvglr gslwnkmltf dasffknsle gmlvqpsnsy
      661 pnyfvsywpe stllpyvnyn nstrtgfdla lnfnkkmgev dfnlgvnaty ytnentkvde
      721 lyedayryrk gkptdgmwgl qaegfynsee eiqnsgitss fgelkpgdlk yvdqngdkii
      781 dekdevylge rygwqgtplt vglnltlkwk nftlfalgtg ywgasafmsg dyywvygdkk
      841 ysevvrgrwt petaetatyp rlttqtdnhn yrnsdfwmyk tnrfnlsrlq ltydlpkqwl
      901 gnsfvrsfsv yayasnllti skerekleln tgaapqtrfy nigfkigf
//
LOCUS       WP_118494837            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            plebeius].
ACCESSION   WP_118494837
VERSION     WP_118494837.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola plebeius
  ORGANISM  Phocaeicola plebeius
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Phocaeicola plebeius"
                     /db_xref="taxon:310297"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116273
     Region          25..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrklmllmt clmigiglvn aqiskvtgnv tseedglpvv gasvlvkgtt vgtvtdidgn
       61 ftltnvpssa gtlvisfigm qsqevkikpn vnvvlksdae qleevvvtam gikrdrkalg
      121 yaaqdlkseq lsksgttsla naiqgkltgv evrqssgapg assqiiirga rsfdgnnqpl
      181 yvidgmpint sadfdtgssv tganyadrsi dinpedieti nvlkgqaasa lygirasngv
      241 ivittkrgsk nnlnkpsvti stnmsaqrvs rkferqtvya qgdkisaynp sssstwgpki
      301 tdlandpvyg gntdnqytae fgkhegqyyn tqrakagldg wttpqiydnv gdflgtgfte
      361 ntnvnisqsl ngvnysfgln nsyqngiips tgmnrwgarg lvdwkineew ntgfsanyss
      421 tkitsapgan dgimnvvysa paeydlkgip thapgditnq vlfrstsfvn pywwadhney
      481 lqhtnrvfgn ayleyqpkln wgdgftlkfr eqagldiwts nyadvkemgt tsallggeie
      541 nygsqhnvfn nlftinfdgr fgnedewgln iilgnefnde nirtwdyyas nfnfpgfpti
      601 gnatnlasan eytrrertvg ffgsvsaswk dqlyltvtgr ndyvstmprg srsffypsvs
      661 lgweftklpf legnsvinyg klrgsfaqvg qagtyynnfy ytpsygggfl aytpvsyplp
      721 sgvssyvpyy vvydenfkpq ntvnyeagid lhlfnsrikm eytyslqnvk dqifsvptdg
      781 aigyqymmtn agkmrthahe fsinaailqs kdydlnlgin ftrilnkvie lapgvesiml
      841 ggfvepqvra qagctypniy gaafkrdseg nmlllnglpq atgdsqnlgn cspdfttgit
      901 fggrykrlsl attwswqqgg kmyhgtnmtl nyfgatkesl pyhegtmvae gideatgekn
      961 tvevskqayy qeyynisesg iydtsfvklr dvtltyqlpk mgifdisvyg farniliwan
     1021 lpnfdpessq gnnnmsgyfe rfsvpntssf gggltikf
//
LOCUS       WP_118501857            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            AD10].
ACCESSION   WP_118501857
VERSION     WP_118501857.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. AD10
  ORGANISM  Aquimarina sp. AD10
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Aquimarina sp. AD10"
                     /db_xref="taxon:1714849"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112939
     Region          26..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mcnkllvflv fvsfvgfqti kaqdstvsgt itdekvgrpi pgvnvivkgt svgvlsdfeg
       61 nysvnlpkpd ailvfsslgf atkeipvngq tridvslses eeqldevivt alnirkeqkt
      121 lgysvtqleg esisevkstn ainalqgkia gvnitqpstg aagtsrviir gasslagrnq
      181 plyvvdgvti dntqlgaase wggsdlgdgi ssinpddvas vsvlkggaag alygsrasng
      241 viiittkngk nqkglgveys nqinfdqidt sfrdfqkeyg qgtqgvaptt qdaaldaaft
      301 swgarlgsip ssvqfdgvsr pyvnvgdnlk rfyrtgssli ntvalsksge gynyrfgisn
      361 ldnldvvpns einrktfsln ssstvanklt ldvsaryiie kvtnrprvsd apgnanfgta
      421 llpanvnvtd lgadtggare sdgferrisr spfltnpywa ssrfrtfdrr nriisaatvn
      481 yeifdwldis aragidhntt rttiitgygt afqiqadgtg ggdilerevn ltqvdadlll
      541 ninkditdkf kidatfgank ntqrsdrldl rgsnfivpfl eiignvrnpg aserrleeia
      601 lsgiygsigl syndylfltv tgrndwfstl savgkdspnn efypsingsf vfsdafemps
      661 wftfgkvrag ysevaggapn pyslnlpfqi fgqghqgqpl gqiatgavpn saitpfskee
      721 ievgfdmrff nsrlgidfay ytnttkrdiv nvnisntsgf snvlsnigel enkgiellis
      781 atpfqndnfk wntsvnigyn eseviatded ngnltignvr tfaanvsqvv gqpfgvilgt
      841 aylrnntgql vydadglpvi dperrvlgeg vppltlgfsn tvsyknftln flidgkfggk
      901 vyagtnatai stglhkktlv gregnftvtg vtnvtdanps gdpftfthdp ttiqgyygri
      961 sgiaeevved adfiklrqfs lgytfpsdil grtfinsasv sligrnlffi skkadnidpe
     1021 agfnagnaqg leyfglppir syglsvnvkf
//
LOCUS       WP_118505422            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            AD10].
ACCESSION   WP_118505422
VERSION     WP_118505422.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. AD10
  ORGANISM  Aquimarina sp. AD10
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Aquimarina sp. AD10"
                     /db_xref="taxon:1714849"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111853
     Region          23..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkinyyyffm flflntisfa qeievsgtvs sedglplpga tivvkdtstg tqtdfdgnft
       61 intkrgailv isylgfkdqe asasssplti tlvedentld evivtaqgis kskkslgyai
      121 skvaseeieq rpeadvsrtl qgkiagvqit assgstgnap lirirsslsl tqsngplivi
      181 nnvpsnasli didpndiksv nilkglnasv lygsegrngv ilietisgsg klgkksfkas
      241 vsqttytnev anlpeyqnty gvgnnqqisi gntgsfgapf adfdevphpl sgnpsfpefa
      301 natvpykaap nnvkdffrtg rgsitslrir stnkttavnl svgytseegi ignndlkrfn
      361 iglggklrvt dklkvstsln yssrqrnsqi gsniferlhy iprsldihnl pfqdpvtgan
      421 vyyrsddqnp lwvlnntgrf ddiirfsgtl nttykftdnl klsyrvgldh esefefdfsn
      481 kggtlssslq ngflnlsadk efevdqslil nanyklskki gfegqvgins nyntfkvqes
      541 dsdsqivfgf lrpdnfrttv adfdeikenl agvfgqfefn ydqflyvtls grndwgstve
      601 penrsifypg asisfiptsa fdfnsrsiny lklraayats sgfpsalrtr tilnldplef
      661 vsdtngnvav igvdnelanp dlrpelhkei evgmegsffn nnvsfevsaf rrisedqile
      721 adldpstgfd qtlinagrid tegieidlgi nlfrnknfrw nlrnvftafe ttvvdipsnr
      781 irindnsfai egqplgvive nyalrdaegn llvnpndgel ivsdevgled riiadptpdw
      841 rmstintfry kdfalsaqle yshggenyse fvkdllergv trdtenregs fvipgvlgdp
      901 gtglplldan grtipntiqq nafatvpnya dardllvfdn svfrireiaf sytlnkgksk
      961 lpfqsmrltl sgrnlfyfap nypkytnidp eldtsggnvt vpttkryafg vaisf
//
LOCUS       WP_118505763            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Aquimarina sp.
            AD10].
ACCESSION   WP_118505763
VERSION     WP_118505763.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. AD10
  ORGANISM  Aquimarina sp. AD10
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Aquimarina sp. AD10"
                     /db_xref="taxon:1714849"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117511
     Region          25..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktnckaila llmalivhfs yaqektvtgk vtddsglplp gvnivirgtn ngaqsdfdgl
       61 ysiqasegni lvfsylgfas qevtvgasnt idmqlqasta eldevvvtal gisrekkslg
      121 yavqevdgna iaqtrstnal galtgqvagv qinnaagnig gstrilirga gsitqenrpl
      181 ivvdgtpldn snyndedtqd ggggrdfgdt gfdinpddie nisvlkggaa aalygnrann
      241 gviiittkta kdgkaeivvn sgvsfesini fpkvqklygg gagdpgtigq snfatqning
      301 ttfnlvdyat deswgprydp nisvlgwdaf dpefpnefln prpwvypnad aesfydvgvs
      361 lnnsisfsks fedsklrlsf snvrttgiip nselekttis fsgstklskk frvdaginyv
      421 itdgfnrpes gygdnsliqk fyqfgqtsld ydrlrnyllp ngnqrtwnrr afddptprfs
      481 dnpywtifen tsadrrnrwf gntkfkydft dkisalgsif ldsydskist rvasgsqaqs
      541 rydedirtfq elnyelrlqy neslfedkvs lnaivganrr nsifsslegn trgglavpgi
      601 ynlnnsnedp riidtdeerr tnsifasvsl gyknflyldv tgrndwsstl ppennsyfyp
      661 avtgsflfsq lvdagwlsyg kvrgswasvg ndtdpyslrn vfnnrtaffg nirytqpden
      721 rnpdlrpeek ttwevgleia lfknrvrldv tyydeltedl itpvqidpst gysstfvnag
      781 klsnkgveal vtvtpvqnen fswdvtwnfs knvneleeli pgvetleiar fpfngvtlna
      841 vvgepygvir gtnfvfddqg nrvvdadgrf lesrnvenlg svlpdynmgi rntltyknin
      901 fgflidiqeg gvyrsltniw gnysgileet aannireqgi ildgvtgdvt fnadgtytva
      961 ntapnttvls aqqygqdhff radaqnvfda syvklrevtl gyslpakwrg plntiklslf
     1021 arnlfvwgla ndnfdpevat sgsgniqgse ggslpstrny gfnlqlkf
//
LOCUS       WP_118525715            1127 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF04-15BH].
ACCESSION   WP_118525715
VERSION     WP_118525715.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF04-15BH
  ORGANISM  Bacteroides sp. OF04-15BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1127)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1127)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1127)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1127
                     /organism="Bacteroides sp. OF04-15BH"
                     /db_xref="taxon:2292281"
     Protein         1..1127
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125951
     Region          24..1126
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkikilllm facfatgaam aqqrrisgtv sddfggimma nvtevdannr ivsatttdmn
       61 gnftmtiknp knklkitymg fqnhvevign ksvfkvkmkd asrqidevtv thkkktvsng
      121 lsipereisv arqkfnmdem qglsfesvde alqgkiagld ivansgnlga gttmrlrgtt
      181 tingnaepli vvdghifelp dnaqeidfen ldneeqfstl lqvnpediae ievlkdasat
      241 aiwgskgang vlsiktrrgk rgktrvnfsy rfsgnwqgqg mnlldgdgyt mmlkeayfnp
      301 kqntsssnml eldynpaypy iynnynkntd wvdavtqfgq ahnyyvtltg ggekatfrvg
      361 vgydkesgti ikqnldrftt rlaldyyvsd rikfssnfsl sftdnhknyd dilaraykam
      421 pnmsiyeyns sienpqmtgn yfnmlpltdq ggfqpnytsa nlgdmysngn pvaianqawk
      481 reqqfnitpq fsveykflgk dddetqlnyt gdvqmqiynt sensyypasl tnnkwydgin
      541 sasnreyksm qfttrhdlaf ypkfnnedha lsallrfemt sgtsndqslt srgipggltd
      601 ptldayltac stspgewrnl sytgsvhysy kskysltatf rtdgrtdfga gkkfgtfpgv
      661 sgrwniided fmkplkswms mlafrpgwgi vgnvvgggyn qynkyadfgs ygnnhgaikp
      721 enlrlaslqw ektsswnigf dlglwndlvt faleiynkkt tdlalqnvsi pshtgfssla
      781 wqnvgtmrnr gwelyantsk farvgkfsmk lsaniaqnin rieemdasvl eslnadfnya
      841 nesylgrvqi gnalgsiygf rykgvyaydy dhngytdvsr ktygdntaaa aqergdnytc
      901 piaydangnm itdakgnplp myfnyggvny qfqggdviye dinhdgqina ldivylgnsn
      961 ptcnggfgvd fyygnwslsa sfnyrignqi inmarmqaed mlnnnnqsqa tkwrwrkngd
     1021 vteipramns kaadgktyna lasdryveng dylrfqylrl gynfdakkik kiglsslsls
     1081 asannlwvws kytgtdpdvt tsgwgvatds nktprsksft vslnvgf
//
LOCUS       WP_118525003            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF04-15BH].
ACCESSION   WP_118525003
VERSION     WP_118525003.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF04-15BH
  ORGANISM  Bacteroides sp. OF04-15BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Bacteroides sp. OF04-15BH"
                     /db_xref="taxon:2292281"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121810
     Region          22..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiiqcilfi llsvtglqaq trtikgtild gefnneplpg atisvpasgg kamngttsdl
       61 egnftlkvda gtaylevrfi gyqtqkvalk pnvnqykvvl ksaskemdel vvtgyqkidr
      121 rkltaavttl nisdekigav ksidqalagq isglssvsts gapgaptkir irgtasingt
      181 qeplwvldgi plegtdipdm edlkdidniy qtsiaginps diesitvlkd aaataiygar
      241 aangvivitt kkgkagkpqi nfstkltysp ninmdrlnll nsdekvdlel dllrsdytfr
      301 enkgdvaril nsmgltnayk qggwdaltpe aqtainqlrq intdwndilf rdvfnqeynf
      361 sisggnekan yytsvgyyde qgnvtgvdnn rfnvtlktny qvnkrlklga svfanqrqqk
      421 symtdyngfv npvyysrlan pymrpfdeng nyiydvnvqg gkedseldfn ifeerantsn
      481 ertdrsvmai fdgelklndy fkltsqfglq vdastldkya gensfamrkd heraqysysd
      541 gkrsflpegg mhkvtethnn qwtwkamaey qqrfknkhdv qlmagteirh seysstfsaa
      601 ygydnrtlts qpvifpnedv akyfplhqes ftenafvswf atgsytykar ytlggsirfd
      661 gsdvfgvskk yrylplysvs glwrvkeenf lkdvdaindl girasyglqg nidkttspyl
      721 igsylqgtil pgysedmies etapnpslrw ektqnanvgm dlailnnair lgvdyyyrys
      781 sdligmkmlp letgfsstti nwasmenkgv evslatrnir tkdftwytni nlgfnenkvl
      841 ketvaenaty pgregypvga ifayktagld edgyplfltk dgkkvtatef lklnqhgast
      901 lsaqeqrdlf tymgttdpkv sggfintfey knwqlgvnff fnlgmkvrvt psysptnfdr
      961 gmntnhdiln rwtpenqnti ypklmtsser paeyiqysey qlynyldiwv rdcnymrlqs
     1021 vrlgyklpge wlkkfgissa svslegrnla viasdytnyl dpetmgnlya qpiqrsvifg
     1081 lninf
//
LOCUS       WP_118525140            1167 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF04-15BH].
ACCESSION   WP_118525140
VERSION     WP_118525140.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF04-15BH
  ORGANISM  Bacteroides sp. OF04-15BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1167)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1167)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1167)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1167
                     /organism="Bacteroides sp. OF04-15BH"
                     /db_xref="taxon:2292281"
     Protein         1..1167
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130775
     Region          95..1163
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfnkrlkklq egflvlflls nsgtlwanal kagpsshkns ehaiqrnnav qtagensqtt
       61 vedkntlpes gmsyantnas ntiqknasqk dndkknvtgv vlddfgeplp gvsirckefp
      121 dvmtitding kfnlqitkka ktlifsfigm etqekaitne amkitmsdkk eqmqevvvtg
      181 yqkidrklft gsasrvsged akidgvgdvs qmlqgkaagv avqsvsgtfg aapkirvrga
      241 ssiygnqspl wvvdgvvled vvevsaddls sgnaatliss avaglnpddi dnfqilkdas
      301 atalygaram ngvivvntkk grkghsslsy tgeftvrtrp synqfnimns kdqmsvllel
      361 edkgwfnhsk martsnggvf ylmndliykg elantqaakm aylqqaemrn tnwfkvlfrp
      421 tiqsnnslsl ssgtdkgnyy aslsflddpg wtvsdrvrrf tanmnasyqi skwltlnvnt
      481 sgsvrnqtap gtldrtvdpv ngeysrdfdi npfsyalnts rtmspdetyi mnyapfnild
      541 esannyidld mtdmkyqmel nykpvkglel saigafryvk stqehkimge snlamayraa
      601 gdatirennk flyrdpnnpd avpevvmpkg gfynttnnil ksyyarfsgn ynrllfeehp
      661 fnlmagseik yadrqsgfnn gygyqwdrgg tpfvdyriiq qlllggnqyy glseyydrfv
      721 affatgsfsf kgrytlnltg rmdgsnrlgr srdarwlptw nisgswnile eeflryqntl
      781 ttlsvratyg ltatmgpadn alavfrnnts frgddgyqes qiyieslqns eltwekqyet
      841 nvgfdigflr nrislssdiy srkgfdligl iktsgmggqk wkyanyanmk swgieftlnt
      901 knierkdfsw ttnvtfafnr nevtnltstn sifylmaaeg aplqgypvrs lfslqfqgln
      961 eegiptfine kgqltstein fqstdhtylk yegsvdptvt ggidnqfkyk rwafsfflty
     1021 qggnkvrldp dfsatygdyt tmpkelknrw mkpgdeqytn vpvipssyqy atidnldiay
     1081 naynysdirv anggflklke vslsydfagn wmkkiginnl qlkmvasnlw liyadkklng
     1141 qdpeffqsgg valpiprqvt fsirtsf
//
LOCUS       WP_118526644            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF04-15BH].
ACCESSION   WP_118526644
VERSION     WP_118526644.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF04-15BH
  ORGANISM  Bacteroides sp. OF04-15BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Bacteroides sp. OF04-15BH"
                     /db_xref="taxon:2292281"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124336
     Region          23..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkvllflf sllafsyssw aqkkasgvvi dgdfneplmg atikvkgtsl gvvtdingrf
       61 tlnnipnesk fleitymgfn pqsvpiqeni kvilqsekkn lgevvvtgmq kmdkrlfsga
      121 tvkidaekmk idgmadisrs legraagvsv qnvsgtfgsa pkirvrgats iygssrplwv
      181 vdgviqedvi nigadelatg dvetllssai aglnaddies fqilkdgsat siygaramag
      241 vivittkkgk agvsrinytg efttrmkpsy nnynimnskd qmdvyremaa kgwlnfsgdn
      301 tnglynapns gvygkmwqli ntydpttgqf alanttearn gylqmaeqrn tdwfdelfsn
      361 simqnhsisv ssgsdkatyy aslsvmndpg wylksgvqry tanlntsykl gkkvtlnlls
      421 naayrkqnap gtssqavnlv dgeisrdfdi npysyalnss rtldpketyr rnyadfnifk
      481 eldnnfieln tvdlkfqtel kwapvkelel svlgalkynt idnehfimde snqanayram
      541 dnsiiidsnd klypdpdhpy dlpitvlpeg giyrrtdykt kgfdfrtsfs wnrlwkddhl
      601 tnvyggmetn atdydystfn gigmqyemge tpfyiyqyfk qaieqgtsyy glshshsrsa
      661 afflnanyay qqrysvngtv ryegtnqlgr srsarwlptw nisgrwnldq ekffaplkkv
      721 vstaslklsy sltgdrgpnl tnstaifssy npfrpmtgtq esglelvmla nddltyekkt
      781 efnvgleigl fdnrintsmd fytrdnhdli gttrtqgvgg eiskyanvaa mkshgfelsi
      841 sstniqnknf rwttdfiysv yknevtqlna iastmdyvsg tgftmvgyph rglfsipfag
      901 ldengiptfy nekgeitstd lsfqysddfs wlkyegptdp tfsgslgntf syknfrlnvy
      961 itysggnvvr ldpvfsakyt dltatsrefk nrwmkpgdee httiptilsy rqyynntqla
     1021 taynaynyst ervadggfir lkeislnydf pkkicstlkl sslsaklqat nlcllyadkk
     1081 lngqdpefin sggvaspvpr qftftlrlgi
//
LOCUS       WP_118576787            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            splanchnicus].
ACCESSION   WP_118576787
VERSION     WP_118576787.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter splanchnicus
  ORGANISM  Odoribacter splanchnicus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Odoribacter splanchnicus"
                     /db_xref="taxon:28118"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120239
     Region          57..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkekqcygrg vpkgsllrlc ltcnlfiapl lissavcant dvkittstal pqtqnmrtlk
       61 gtvkdeqggs fpgatiqvkg ttlgvvtdid gnfsitipsd pntvlvisfv gmktqeikvg
      121 taptlnvilk edsqtleqvv vngvferkan tftgsvktis ndelkrvgns nvlqslknld
      181 psilfidnma lgsdpnavpe mvlrgkssin meetdlkaty gndpnaplfv ldgfevsiqk
      241 imdldmdrve smtilkdasa kaiygskaan gvivielkkn psgdlrvtyq gsveieapdl
      301 ssydlcnaae kleiekefgm yddedanydn qrmaqkiynq klsavvsgin tdwlskpvrl
      361 gvgtkhgvsv elgdrelrai idlsynnikg vmkgsdrtti sggislsyrr ekflfrnqtt
      421 vtsnvaqdsp ygsfeeyakl npyytpydqy gqisenivph letgnsvmvn nwykeiefqa
      481 nplynaqlnt llqkkyidlt nnfeiqwfaf tgmkitgrlg lsetrnredt fypanhlkfr
      541 dfkdddqyrk gsyqlinges snldgkvdvq ynkeflpght iyanagfnlg ekkmitnehn
      601 aegfpsdkmn diifarqyak dskpkgtest treigyylsl nysfnnrlnf dgtfrqsass
      661 qygadsrwge fwsvgaswnl hnetwlkdte inqlrlrata gstgsqstaa ynaiasyeyf
      721 ldshynnllg aqlksmrnet lkwqqkmeyn fgldfnfknr ysmsleyylq ttnntvnpid
      781 llpstgfttv qenigkvenk gidfslsaia wqrpadrsyl rfsvmmshnk nklkeiseam
      841 ksyneqqtal atssnkplnk yydgvsmdai wavpslgidp atgqeiylvt dengnyyrtf
      901 tydgnkqvvc gdalpkingn agisfeykgf ginavctykw gakmynatlv skvenadleg
      961 nvdrriftgr wrkpgdlapy kalgkvyvas sdelasptty atsrfvqknn eltisslqls
     1021 ydffrhafvk kiglerivlr ctvndlhkfs sikvergtsy pfarkfnfsl avtl
//
LOCUS       WP_118577368            1142 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            splanchnicus].
ACCESSION   WP_118577368
VERSION     WP_118577368.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter splanchnicus
  ORGANISM  Odoribacter splanchnicus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1142)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1142)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1142)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1142
                     /organism="Odoribacter splanchnicus"
                     /db_xref="taxon:28118"
     Protein         1..1142
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128446
     Region          45..112
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          130..1141
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkkqernnl rpgrgisgrt mfstvlllfg ivinlnaqer tkvsfkfqkt tfeqviqeiq
       61 nqtdydfiyn skafpqksfa ieaqnrevks ildelsrdlg leytimnkvi tlrmkntpss
      121 sapqsdqglr iikgkvvdek geplpgvsvv vkntvqgtas dvngnftikp egqekiilqf
      181 smigmqrqev eykgeqelki vmrennetln evmvigygst trkdmtgsis sldtkiiess
      241 aapnlaqmiq gqipglniml gdgspgspsr leirgastls snsgplivvd dvpmspdydi
      301 nminsadiks lnvlkgasat aiygsraagg vimittknns rnkkpviqys fdftnqrlvs
      361 dirtltadef ktllleaarn earasgyedi tqsadyqrfs tpgffgesnt pwmstlmqda
      421 itmqhrvsiq ggtaetsyna sfsylneegm lkslynkryt ynagfntdis kklkatvnvn
      481 gsftrrnrnp rgmetaiaar pdvkvynedg sfyhqqyqyg grlvttknpl aeitgtrdqe
      541 drnninlsts ldwkpislln fsmrysfqry htdydyyass etyegsdnfs gkfngygkrt
      601 nyltteqeve arasftktfk qkhylnlmva gtynennaen ywfamdnfgd dnvqngiwqg
      661 tepyekrpkd gyslgsvmls figraeykfm nryilnasir rdgsskfspk nrwgnfpava
      721 aawlvseedf fknnlpwfsy fklkggwgkv gngwvteygw rtmfdnsayl grpaiipsqv
      781 gnddlkwedt eawdigfefg lfdnqrikgs fgyysknteg llydltlsps mgagstkvnf
      841 asiinkgvef dlvanlistk dwqwsvsani sknknrvtni daefvsvpgs smltstvike
      901 gsslgliygf qtdgvfrsqk eidyyeslnk dhayqtgttg rktipgdlky vdqnndgyvn
      961 iattakddrv vlgcsrpdfe gglstrlgwk gftlsiqssy ayghqkmwka gaqqfqfnsy
     1021 epgnlldial krwtpenpds nypsmrlnky qnevvgfavy dasywkiqni nldyrvpvsw
     1081 lkhinvfssm tlsfsmnnvy tftsypgpsp esfsanmieg gsidystypq trnfnfsikv
     1141 tl
//
LOCUS       WP_118585065             146 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Roseburia inulinivorans].
ACCESSION   WP_118585065
VERSION     WP_118585065.1
KEYWORDS    RefSeq.
SOURCE      Roseburia inulinivorans
  ORGANISM  Roseburia inulinivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Roseburia.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Roseburia inulinivorans"
                     /db_xref="taxon:360807"
     Protein         1..146
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=16468
ORIGIN      
        1 mkpalkllfe egfegaedei rnayerrrkg dnknaileag kafestmkii cdkqgyaydk
       61 nkdtaqklit ilenngfyps ymnahltsvr ttletglpvv rnkvaghgqg nqiitipdey
      121 tdyalhlaat nilflvrlyr nkkqnl
//
LOCUS       WP_118655515            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Alistipes
            hominis].
ACCESSION   WP_118655515
VERSION     WP_118655515.1
KEYWORDS    RefSeq.
SOURCE      Alistipes hominis
  ORGANISM  Alistipes hominis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Rikenellaceae; Alistipes.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Alistipes hominis"
                     /db_xref="taxon:2763015"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118781
     Region          38..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 minnmrhkvn ikiallltcm flsafgakis aqsstvytik gvvtdefgkp lsgvvvnset
       61 gkngtstdie gsymltvddg skdivfsylg ykdkkvaiae ketidaklep dalksdeiid
      121 mgfvqqrrga isgavssvkg tpieaapvss fgaamngfvt nlmvrqnnyv lgnetvsmli
      181 rgasnpqngw qtplimidgv mssynsndvl ryltakeves itllkdastq alygvkgnag
      241 vlvittkrgk kgpvridvsy dqsvqqptis prfyhsweya tfkneatynd npslgktpvy
      301 spvdianyis genrelypdn nwrdmfykkl ttmsraninv tggsdkftyf tqvnfmhqgg
      361 qfkttneryk sgfntnwfny rtnvdikvnk ylssylrlsg nvrrdrapgs dafynaqqgl
      421 yedmywrgan iygpltpavy dqatgemldp ggklvveekn tysiygvlnr mgynkatsvn
      481 insqfgldld lsfvtkglkl ggyiayqtyg ynsltaiqsn elvkrkttdd psvlafetig
      541 ttkdselsyg kgyssyyhld yrayldyqrt fgkhnvqata fiyyqnlska dmgssnnvlp
      601 fntvlsgvea aygydnryfv kvdlgysate qfapdrrwia tpaisgawnl anehfmknvk
      661 wlnefkiras ygrtaeddlq ngrhgylden qfgtggsvpv laystwenkk gyallqaqtm
      721 lkqnygidvg lfngftfsfd yfkermdnml ihatstipsy qgipinnypa tqvgvyenkg
      781 ydlsanyykr inadwsfnvg gwvsyarnkv iykdetelge sysyrrkeeg fplgtsfglm
      841 vdysngngyf nsqeeidrye ctygwnmpsp rvgdlifkdi ngdyiidekd qvpfgyggip
      901 qvfyafnggf kyknlefsfl fqgvartggf esstwhlnye giytrlhega wtperyaagk
      961 eitapalsns qtssdmrnns ynwndraflr lknveiaytl plnvskkisa dkirfslsgq
     1021 nlvtwgrmkn kdiepeyggl ytipayrvyn vgvsvlf
//
LOCUS       WP_118696419            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_118696419
VERSION     WP_118696419.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114899
     Region          43..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyttlymli lglfsigwtd cpegfwermq rpghseiqls kvtvsgcvld eggfplagat
       61 iqeketanga iadsegkftl vvadnavlrv sfigyisqdi evegrstfhi tlrenmield
      121 nvivtalgie kkenslsyat dlikneeltr vkmpnlitsl tgksagvrvn qvssglgasa
      181 kvsirgvrsv asdnqplyvi dgvpilnsts eqaysaiggt anasnrdggd gisnlnpedi
      241 esisilkgap aaalygsqaa ngvilittkk gqshgqrsvs fstslmfdna falpkmqnry
      301 gvsdgvdswg eranlpeydn lrdffstgvt sitsislshg neklqnyfsy anttghgiig
      361 khnlskhnlt fretsvllns rlkldgsmnl mrqvvknkpt vggfymnplv glyrfprged
      421 isyykenfev ydegrnlniq nwhtsyedfe qnpywitnri lskenrmhvi vslsanlkin
      481 dwlslqargn vdyindkvrq qfyastapal agangryiem dyqetqyygd ailmmkkqwd
      541 afslnaalga sindktvnst rydsktaslk yanvfnlani imngsagldq kidarrqlqs
      601 lfataqlgyn efvyldlsar ndwsstlayt sheksgffyp svgfslifnk lmtlprwvsl
      661 akirgaysmv gndipmfitn psshitagge flasdaapfk dmepemthsf eagiearflk
      721 nriglnatfy ktntrnqffk lptlsgdkya yryvnagniq nvgwevslda vplltnhfkw
      781 ktevnfstnr nkiislheal keflygptsf sssyamklvk ggsigdiygk afvrddagni
      841 vygtegdntg mplvegdgnt vkvgnanpkl mlgwnhmlsy knfsfyflvd crfggdilsq
      901 tqadmdmygv sevtarardk gyvmlegnri dnvkgfyknv vggragvtey ymydatnirl
      961 relsvgyqlp aawmektkvl kraqlsfsgr nlfffykkap fdpdlvlstg ndnqgievyg
     1021 mpttrswgfs lkcef
//
LOCUS       WP_118706093             303 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Lachnospiraceae].
ACCESSION   WP_118706093
VERSION     WP_118706093.1
KEYWORDS    RefSeq.
SOURCE      Lachnospiraceae
  ORGANISM  Lachnospiraceae
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Lachnospiraceae"
                     /db_xref="taxon:186803"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35196
     Region          4..163
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mfklysertt npnelpdvye yenipdrfrn qlffiledil dyrtvtlddl wssisatfsr
       61 eigtkslvps kgyfnnkkke ieffisscet tifldfidfi snvfyhlkne ppysydtdyv
      121 dcienafiei nnrfkqnnlg yeiindelir idnkhlhsev ikpalhlihs edfkgaeeef
      181 lkafeyrrnn dnknaileal ksfestmkti cdkkgyiydp akdtaqklin ilennnfyps
      241 ymnshltnir ttletglpvl rnknaghgqg atvvnvsdef teyalnlaat nivllvkiyq
      301 sqk
//
LOCUS       WP_118713566            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118713566
VERSION     WP_118713566.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125773
     Region          127..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkinlffre qhgylqvlfr gtllvcflft isfvhaqvqk nitvefknel laevlkklek
       61 mssykilfty dhvqnyrvta slkevtilda ldkvlegkpf frtgitdgky isvkynsnkt
      121 stenklrtik gsvldknkep lpgvtvlikg tttgvvtdtd gsyvisipes ststlvfsci
      181 gmksvevvvk dnktinitme edvtevgevv vtgyfnqtke sftgtvtsfs geelrqvnpv
      241 naltalsvld psfkmlenis dgsnpnvvpk fevrgsssmp nvkneyegdp nmptfimdgf
      301 evsaekvfdl dpnriesmtl lkdaaataiy gsrasngvvv ivtkmpelgs irlsynmdls
      361 fnipdlrdyd llnaeeklel eraagyysst vanlleerea qynykkrlve qgnntywlnk
      421 plhvaighkh slfveggena mrysldlsye salgvmkesg rerisagmll qyqmkkivfk
      481 nqmmydvvna dnspygsfse yakanpyyay kdenghylyl leddtrgafd kvpnplyntq
      541 lnvedrssys nftnnfsidw yitealrlkg niaihhqkse gvvfkpakht dfsnmmgdny
      601 yrrgsyqate gkefgydasl vlsffkpmhd hvlnvnaaln mqdlskeeyk vkvegfpden
      661 ldyivfgasy pksstptgkd eisrliglvg nmnysfkery lldlsvrtda sskfgadtrw
      721 apfgsvgigw nlhnekfikd cakfinrlki raslgwvgsq sfspfqaipk yeydvnnryr
      781 ygigaimkgm anrslkwqkt tqrnvgidfd ilnrrfsvsa nyyvntsksl lsditlppsl
      841 gfstytenig qlenkgfdlk vrgtvfrnkn gfmnlsvgiv knnnklkkis nslrawnevq
      901 ddsvmntprv rfiegqslnt iwgvpskgin pangkeifvg rngiltstwn asdqqpigct
      961 dpkiegnisl nggykgfsls myftyslggd tynqtlvdrv enadkryncd rrvledrwqk
     1021 pgditffkdv annemtqats rfvekynwlk lstlnvsydf nanwlkyiqv enlrlsfnmt
     1081 dvfrwssvke ergldypfah afraslritf
//
LOCUS       WP_118713761            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118713761
VERSION     WP_118713761.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124084
     Region          131..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkrmlgyw sekipyervl rvmrlmfllt vcivcqlsae slaqtvklke qtlklksife
       61 qveaqtgkft lfsnneldmn ravkldrref tleelyrlll rdtklefeit rdyvvirpgr
      121 evardsvrkl iqvsgvvrde rhnplpgvtv lvkelkvgsa tnvkgryave vpleqftlvf
      181 sfigmetkei ayvgrdtinv vlkeeaaaid evvvnglftq nrnsytgsvt tikseeimrv
      241 sqtnllqala vltpgmrile nneqgsnpny vpeivirgts sisakeqqgl nrplimldgv
      301 eitleqlydl dmfdidrvdv lkdasataiy gdkasngviv vtrkrvtdsk lrvrynfvpn
      361 vqfpdvssfn fcnaaqklel ermyklydsp ygqydqdyya klervnagvn tdwvskplrn
      421 swsfnnslnl sgrgggldys vtlrfndtrg vmkgdyrqny gaafyfsyrl edrltlsfrs
      481 dwgktdskts pygnfadfav lnpydapkde dgnwnkklsw dkrnplydat tnsfeeqmsk
      541 tfsnsltfrl dvikglymtg tfnlawsdah sekfdspess twlgvsdpeq kgsydvsgsn
      601 gvswnmqtta synlglnedk sslltlnvgg slekrktnsf sfsgvgflkp dlndisfasr
      661 yptdggpgga esittaaglf gnmnlivknr yfvdasfrts gnssygtkdl yssywsagig
      721 wnihqenflk dswvnllrlr gsmgyvgngn fsdikpytiy kysvnnsyag vvgarpltmg
      781 ndelkaerql qlnlgvsaaf lnerlevsfe tyrqttkdll ldismppsag isstksnlge
      841 klntgyewkv sgvlirtndm ywraslnshq aknkvqkisn alkrdsdanr dstqyvapki
      901 qleegesdda ifavrslgid patgreifik kdgsrtfkyd pqdkvalgsk tpkfegsfst
      961 sftykrvsln lalsftfggy iynstraski enidpkanvd krafterwkk pgdivdyiti
     1021 drtygfaqse rfvekknevs ftsigvmydv npdwvkrigl rrlvlgvtis digristvky
     1081 ergtnypymr gfnftvsptf
//
LOCUS       WP_118713788            1149 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118713788
VERSION     WP_118713788.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1149
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128127
     Region          36..1148
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknniqhikh tiingvllvl lfiipdnlla qknqvtvsgc vtdvtgmtlp sasvtlksdn
       61 kigvltnakg eftitipens tlvfsfvgmk tqevtiekkk ifykivleek nqdleevvvt
      121 gyqrlkrhev vgstytvkgd diriagvnrl dmalqglipg vsitipsgmi gtaaqvrvrg
      181 tstivgnasp iwvvdgmire eplpfegqql ndilssgdms samtsisgss isgvnpddie
      241 sitflkdasa aaiygvraan gvivittkrg tntqgrisvn frsdisitpk rtyaqtdrmn
      301 sserielske iiesglpfsq fpenigyegl yqqlitkkis neefnhqvts mekrntdwfd
      361 ilarnaisqn ytlslsggne klnfygsvgy nnslnsykgn dqkrktvtln vdtklrenlr
      421 tylkfsanqs itnayytgvn pedyalstsr ilasdewylt nettpefkyt ennstkiikr
      481 dirynflnel khtgnenknt nfdvqgniiw nilpelkwem tgafsktttt anlwaddhsy
      541 avskirgany gelvtsekda wlalasalpy ggilnynfte qqsytfrnql nygktfgkdg
      601 vhainivlgn eirsntytgq kgleygympd rgksidynys tqgiieyvrk iypnsniidl
      661 ttpdfserhs tsiidrvenn msfyailgyt fstkysfsfn lrndasnrfg entnnrfnpt
      721 wsagirweig qenffrqfgw lnaltfrgsy gyqgtaasnv gpdiiaqfni apdvltgeqf
      781 laikqfankd lkwektgnln lgidislfgn rlfgtveyyy kkttdvispv aiptengtts
      841 msinngtvin kgydlavtvv plqhkdlrws isattsfnrn kikdnvdipn lekitngsvi
      901 vdgyalgsfw sfpyiglsne grpkfaiide tpgtltpvsg slleymvysg vkdpifsggl
      961 stsfrykqft lgatfniqlg hhkrlnpfmr sstssngaga ltipnpekna snilakrwrn
     1021 pgdekytnip allakdedlk nylpdnslsi dnynatyryt mynlsdyrvv kanhlrcnni
     1081 nvayafsrkq lektglsslv fgltvtdpfi ikskglgkqd petlssnank iipvvdrqrk
     1141 fslsislgf
//
LOCUS       WP_118713981            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118713981
VERSION     WP_118713981.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113919
     Region          43..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mridlvlmfg srcrevvryf llvcfvcltg gsvsgqahsp lvtitgevrd adgellpgva
       61 ivlkgtslgc atdgsgkfkl gipeqkemil lfsfvgmktr eimvtksqhl rvtleedtke
      121 lddvivtgyy tqaknaftge ftvikgedli rvsptnllqa lsiltpglki lenneagsnp
      181 nvvpeilirg assimtkdqa gvntplimld gveisvedly dldiydiekv lvlkdasaav
      241 lygekaangv ilvervrvks drmkfnynfa ptfsfpdlts lrlcnaeekl elerlaglcd
      301 rvdgsldpay dyklenirrg vntdwatkpl rnaftqshsa tmtgrgggie ykltgrfsda
      361 ygvmkgdyrr nygvnvslsy hfarnllany llsytmtdsk nspygsfaqy tklnpynpvy
      421 dengdyikny yfdpvnrtid rhvnplynat lasfsksqnk avtnylslrw dvaenlfvsg
      481 evsvrqsdsw nkvyvspeda sfalqelpqn kkgtytalsn ertnwrgklv lnyrlllndm
      541 gttvfalsag sdigkdksst mqvkaegflk dkmtdikfas qyattrplgg ekesaevgff
      601 vngsfdllgr yfingsykta gsskfgskhr fapvwsagig wnlheenfmn lnwldvlrlr
      661 fsvgstanvt ftpyqaltty lydpdlihyg gmgavpitmg npdmkwqvtl kynwgltasl
      721 wkdrvnveas yyvnktkdal mpltlpasvg vssvlvnmgk lqnsgyefsv sakllkkndm
      781 fwmvmvngsh vfdkltsisd alkaenmaay ygvkpqpmfv eggsqfgiya mrsagidpas
      841 glevyikkng nytftydkne rvevgntnpl legslftsfs yrgfslnvsa tykfggdiyn
      901 ttlankveyi dpyrnvdrra fterwkkpgd lvrflgipes vsdenrfser fverdntfai
      961 tsvvlnyefn pgylrkigik klnlgigvad iarfssvkqe rgteypfqrt fyitfrptf
//
LOCUS       WP_118714014            1126 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118714014
VERSION     WP_118714014.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1126)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1126)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1126)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1126
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1126
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126289
     Region          65..117
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          127..1125
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknkyslsl slkfltrvvl ltimgtsflc fsvkgdpvep qrvslnlkdv slsvlfqemk
       61 kqtsykffyn dvqvkdvgni tvvannetve svlervfqgk eytyrisgeq iivvkrqetk
      121 ksvqevvieg ivlerdsmpi vgatvvlqgt ttgvatdvsg kfrlvvpldd eiyievsflg
      181 mkkqvhkvlg lpnpkpmrlv mqpeamgmde vivtgyanir kesftgaatt vtkedilkis
      241 prnvidvlqv fdpslrmvkn nemgsnpntl pefyirgrtg mdgvtqldrl eaqqggnisq
      301 fslttnpnlp ifildgyeve vqkiydmdpn riasitilkd aaatamygsr asngviviet
      361 vtpelgklqv sytfnaslta pdlsdynlmn aeeklraevl sglydlslpn dveqyaikkn
      421 yitsgvntdw maqplqnqfn hshslyvsgg tegfrfgsdl syaheggvmk ksyrdrmsvg
      481 vyvdyrvgkl qirdnvsydi srssdspygs fsdytsqqpy yaiydedgkl kkqlnigvpn
      541 plyeaslgnf srsesynltn nlslywyind hlqlqsqfai trteseskkf tdplsttygs
      601 tdsdpfsrgd lyvnttdnfn wnlnaflayn nsigknylnl sfginaqesq sgnlsshyrg
      661 fpsaalhtig hakeivekps gednktrlmg iffsgnyswd nifladasir fdgssefgse
      721 sqwgsfwsfg aginvhnfef mrslpwinqf kvrgtygatg kvnyppyaar dmysilfddw
      781 ystgigatlq gvgnenlvwe ktnstnigfd lsffqskyni tfswynrqtv dmitdvtips
      841 sagftsykdn mgetrnrgye isfnasiinr kdfgvnafvn fahnegklmk isealkayne
      901 rvddyltlry tsyanaadks lpflkyeegg sltaiygmks lginpadgee lfvdrsgnvt
      961 svwsssqqqi igntepkgqg afginirwkr ltlytscmyt fgaqeynstl lshvecvdls
     1021 ksnadkrvls qrwqkpgdit plknianrnq ttqstsrfvq dnnefsinsi slsydfnpew
     1081 vrrigldvlr lqastndlat fssikqergl sypfartfnl glsvsf
//
LOCUS       WP_118714554            1178 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118714554
VERSION     WP_118714554.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1178)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1178)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1178)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1178
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1178
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133038
     Region          49..116
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          130..1177
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mamilncngs ackgrsgiml rvllvqfmls lcfftsiasg msqnrdinlt fekatlsqal
       61 kqlgevadck fvfnyddlnr yqvsvklenk sieeslgill qdkpfkfere geffvisykd
      121 dtkkedgflv kgtvkdefgl plpgvtvivk gtttgaatnp dgtfelrvke rntllvfsfv
      181 gmktkevmte gdkvlnvvle eeaemlgevv atgyqtisre rstgsaviln srkldqvqai
      241 dltsklegit pglmnyggtm airgrssfav gstpllvidg qvtnaslsvl npndiesvtv
      301 lkdaaatsly gvrasngviv vvtkkanknk tnvnvsagfy inplpdmgyl dyastsdiid
      361 fekefiqnnp tyqqnpadyf alkndrsnps nltsverlyy emslgnltqd eldqkldamr
      421 kndyrkeark alehtavtqd ynlsiargge hsnlflsfry edqgsyakss snkrfsvylk
      481 nemnvtdwfk ltygansyfs rseasngqag fmntmpyerl rdddgnlvyq yyrnyymaqd
      541 ineteglkfm gynsleaskq nmittkdlyl kffahtdfkl megldlglkf qyersntdkd
      601 qydevesykm relinqfasv dsygnfvynv pdgghllknh nrnefynfra qinyqkaisd
      661 dhevsvllgg eirqdqwnss anevygydkd kltyaqvdwl tltqkgvigq lntsrafnls
      721 enisngetkh ryvsayanag ytyagrytln gsirvdqadl fgtdpkyryr plwslgaswn
      781 itsesfmrdi kaldllklrv tygitgnvdq ssspyligay issmwtnsdv tdivsppnkm
      841 lrwektssln vgvdfslfar lngsfdvyrr ystdllankt ldpslgftsa rvnngemkni
      901 gvefsiaydw lkkykdwsln tmftaaynkn kiekigftps nasdmllypy snylegdtyg
      961 siyayryagl tetgdpsvyd engevqsgts vrdikalvvk gqlapkwnga ltvnlkwktl
     1021 elftkfvyya ghslrndvtp lysmyapdmf npgygeisgn mhkdmakrwt pentdtdipa
     1081 mglygsqqdr nlqwryadvh vlsasfvkcr niglsyvlpq dwvkylklsn islraqvnnp
     1141 fywaknkegi dpeafnaneg trtqeqvtty vfglninf
//
LOCUS       WP_118715002            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Odoribacteraceae].
ACCESSION   WP_118715002
VERSION     WP_118715002.1
KEYWORDS    RefSeq.
SOURCE      Odoribacteraceae
  ORGANISM  Odoribacteraceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Odoribacteraceae"
                     /db_xref="taxon:1853231"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124795
     Region          25..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslllial lcplwlfaqs egdyrtvkgv vmdsvtnetl igatvmidpn aveaknlgpk
       61 gtitdldgkf elkipkavky vvvsfvgykn ttldvtknte fkvllqpdqe qlgevvvtgy
      121 qqiekrkats aiqtvkmddi ksigvasidq llegqiagmt siptngapga pnkmrirstv
      181 slsgstdplw vldgmilegn dipsnfsdkd nidnlyntsi aginpadied itvlkdaaat
      241 aiygaraang vivittkkgk agkmrvnasa amfvttkpdl gklnfmnsse kvdfelsmtk
      301 ldyadnneka nkgevarila kydqleiyre ggfnaisqea qneintlrnr nvnwgdqiyq
      361 savnqqynls viggsekary fasvgyyneq gttkktgfer fngtlktdfd lrdnlqlgls
      421 mflahstrks yitdlggftn panytrtvnp ylevkdengm yiydqdiegv tglageryvp
      481 fniveerent dyslknlavk pmisldykpf twlklstlfg mqiensetek fadkdtyyvr
      541 kyrenaytyk dgywlpeggi iqnwtenmsq yqwrlqgefn nvfaekhavn vmvgyemrgn
      601 kstqvhtkgf gydpkalttk pldfpdgfnd issslyqqyk rtenenryls yymtasysyd
      661 nrytvfgsmr fdgsnlfgvs dkykylplwa lsaawnvdre dflknadwls nlklrlsygl
      721 qgnvdkntsp yivgtwgets glgsssepti svtsppnqkl rwektsnwnv gidmgvlnnr
      781 itfsvdgyyr kskdligvrs lplengfdft smnwaeltnk gfeftmstvn irtkdfrwvm
      841 dfniahnksn vdritvrene ktpslqgysv galfklntag ldengiqmfw kngervslqd
      901 ffalevgsdg apvskltnke fselytyagt tepkftggfi nkfyyknfdl tistsfvidq
      961 tmqetpfysp semspgsnys krvadiwsps npdgiypkim nhsywmdsdn dflftwmgds
     1021 qggfknydyw fkdmsylrvn sirlgytlpe niikklrlgs arisvearnp fviassykgy
     1081 fdpetwgnvy tqplpktfsc gldltf
//
LOCUS       WP_118715056            1124 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Odoribacteraceae].
ACCESSION   WP_118715056
VERSION     WP_118715056.1
KEYWORDS    RefSeq.
SOURCE      Odoribacteraceae
  ORGANISM  Odoribacteraceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Odoribacteraceae"
                     /db_xref="taxon:1853231"
     Protein         1..1124
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126444
     Region          130..1122
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknrfdrqg ipvnlrkmfs gmksrvflml fltfavsdvv laqsktvtln vkseplsdvl
       61 iyikdatgvq iifnenqleq vtcgpvsvkd vpvkeaidav lkgkgffcev ldgvyvikre
      121 akkeevkklt itgkvvdvkn nplpgvtvri kstmlgvatd vdgnysitlt ageekpvlvf
      181 sfvgmtsrev tyagkevinv tledeaseid evvvtgifkk akesytgavs sinaeqlkmy
      241 kgqnvlqtlk nidaslnftv nnavgsnpna vpqinirgns slpisvqeyn esasnavntp
      301 liirdgfeis leqlmdyndd eiesinilkd aaataiygsr gsngvivvit kqpeagklrv
      361 nvevgmdlei pdlssydlln aaqklelers lglydntvap sndvwykeay ykrlrdvlsg
      421 tdtdwlskpl htgvgthynl rmeggseqfr wgvsaaykdi qgamkessrr nfngsvtlmy
      481 qmkklifrny ssyttnegke skygnfsdyv kqqpynaayd qngklvryfd gfhkatgksq
      541 nplydatlns fdksgyqalt nnfsvewkpt eeltlrgqvg isgknttnda flpaehstft
      601 edeyystdeg flrrgtytys pgrtssydgn ltlaynkvfh dkhqvyvgld yslsesrsys
      661 yrivaegftn edinflgsar qyakdegpgg skmktrrmgl tgnanyifdn ryyvdlsyrm
      721 dgsstfgskk kyaqfwssgi gwnihnekff sndvvntlrl kasygetgtq qgsssgasti
      781 ykyitdnrym hwtgavlqgw gnpyltwqkt nefnigteig llqgrvkgef nfytkrtgnl
      841 lsnmdlphsm gfssyvsnvg evknrgweas atgylirdte reinwmiggq lvynknyisk
      901 lseavkaqne aylkedvdva nlfyegrpqn aiyavrsfgi dpstgkevfl dkngketdiw
      961 nasdkvylgs kdpkyrgnfn tmfmwkgftl nmsfgfywgg kvynqtlidr vevtrttlms
     1021 qnvdarvykd rwqkpgdvvs fkkfdntatr atsrfvmddn vfelqsvalq ykwdegwlhk
     1081 htpissvifs vnmsdlfhfs tvkmergtsy pyarnilgsv kflf
//
LOCUS       WP_118715089            1159 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118715089
VERSION     WP_118715089.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1159)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1159)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1159)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1159
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1159
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128664
     Region          69..120
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          133..1157
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknslipkp gfrlfcphpk vfvklfaliv fmtfyihsyg lgqnkkmdvh fnnvsidyvi
       61 eyleaatdyt fvyndtdkeg vkvsvslkda diitildavf kdtplayqik eerivvlrrk
      121 niptkteqek qlvvkgrvis ekekepiiga tvvlegttlg vatdmdgnfs lnvpkeaktl
      181 vissigyarf qliltpevfe kmnviqlkds vsfvdevviv gygttkvkda tgavsrlgek
      241 eiamspagas iqsmlqgrap gvnvmiqsas ptspvnvvir gvstltgntq plwvidgvpd
      301 ysqsstgdvt nalfnlnlsd vesidilkdv sataiygsra angviivttk rgkqgmqptv
      361 elslrsgiqt insnkldaln aseykrfvet vgrqsieiag fdyntrfffd etkfnqlnts
      421 qwdgsmlqlr sdafmdgdtd wwdemtqnat ttqcdisvrg gtantnyfis fgyndqkgvv
      481 kggrsklytg rlnletligk qlklgvnlsg ssrktnnkdn lidniirfrp dfpaynedgs
      541 lnlvttstvi enphltlanr ndgrgltfss saflewtild glkfkstgtv nytnsktdvf
      601 skkgtrgysi ayntrslgns eyntyvwdnt ltwmkdfgkh nlvavvgqsi ekyksnylsg
      661 gaddfpdeev linlgsgads wsdsdeagnt lvsaiariny kynnrylatf tfrtdgsskf
      721 gpdkrwgyfp sgalawvise eefmaplkty ipylklrasi gkigsqnlgn ydyislmgsa
      781 tydgepgtkp tslgnpvlqw eettsidvgl dfglfserlr gtigyynkqi nnliyngsvp
      841 anssyttvnq nvgtiantgw evdmrgdvir tdklnfeigf niatntgkvk kldgvvkelk
      901 mpyyyeyvrl vegghigdwy gykyagrlfr tqeeiialrp tsattgaqen yfgsydspgd
      961 mylidqdgdg kitakdkvkl gnfnpkffgg fnlslswknl yatavftysy gakrmwyyqy
     1021 ektsgvgtyn mynsifdsyn fkgsdalfpr layagtvana lsdlyihdas flrmnslnln
     1081 yrlpqnwftg tfvnniefsf sasnlftitq ypgfdpqgnf gsnptsatan dvitvaqgvd
     1141 ystypsarty sigikftfk
//
LOCUS       WP_118715257            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118715257
VERSION     WP_118715257.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123617
     Region          52..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkmdcqrqf ilnsrvacim ffaflvhapq gvksealqsn qvkqdsivqh lvtgkikdkk
       61 giplpgvtvr ldstlagtss dnsghyrmyl pvnrgrlifs figyktrais ftqvdtlldv
      121 tleenvseld evqviaygeq trrnsvgams lvkadeikdi pspsinnllq graagvdvtn
      181 mtgapggggs pivirgynsl aaengrvtsd plwvidgvpm fsytsgltgl ntiaeidtkd
      241 iesiqilkda asaaiygsra angviivttk kghrnqpptl gvnisqtwvt rptlpdlttg
      301 ngerrhrmqa menyreavhd eetnryrpvl syedsykngk dynlfwnkgv gldipivqds
      361 lnkfynnstn lfdyyfqtgk vtdaniqisg gssnityhvg lgyytetgvl rntgfnrikl
      421 itnlfikpfd rvesnirfyl artgrnragk ghdahtfinv rndletipde llststlmpg
      481 pgtaafdesv rrfneikekn esyrlrasfd laytitdglk lksslavdfs mqdqnifmpp
      541 alnvdnksys sgndeinmmw lnenllscnk tladghtldv llglsfqgdi akskggygkg
      601 apsdliryvt wsgsaydtek kqqlkeytss lerstmvgmf grvsynykqk yfasvtlrrd
      661 asskfgentr wgtfpsyaia ytfseepymd wardfmdhgk irlsygksgk qfehpylafg
      721 vlapgtipfh gnqtispfwn dgllnpklsw eetrqfdagl dldffnnrlg vvldyyyryt
      781 dklltlvslp gdynayvaqw qnayaisnqg lelqikadli qseklhwdin fniarnwnrl
      841 eksnngmdfv nrvsahnlni igkplngiyv yndqgyynsr deipsyyidg kqrylsppgn
      901 qiytpgdrri qdvdgngria tsvplledrv yggsplplaf ggiatslewk nldlnllfsy
      961 klgrhvlnag rgasvgttlk antsemmtpi ladldkisfw qkpgddtdfp vneldngknn
     1021 fatnlksnie kinylklksi sigytlpvfp kqskhharvf msvenvftit nssspdpesi
     1081 divtgidsnn nyplatrftl gltlnl
//
LOCUS       WP_118715445            1126 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118715445
VERSION     WP_118715445.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1126)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1126)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1126)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1126
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1126
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126989
     Region          126..1122
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkncktkvf crlsvmrgvl cglfllslit lldyspvygq qnvkrislkl easgllealr
       61 einrlsdnlv vfkkeevere rkrvtvdlrn vttkaaveac vegtgltcme yegkvvvtpr
      121 qqptsititg tvrdvggepl pgttvvvkgd slllgtsagi dgtyrftipt nvttlvfsfv
      181 gykskdvvig grtkidvvle edvksvdevv vtgiftrkas sytgavvtmt akdimragnq
      241 nlfqslknld pslfimdnle mgsnpnaipe mkmrgvssfp leetgvrlkg nyqnnpnqpl
      301 fmldgfevta ervmdmdmnr vesvtllkda sakaiygska angvvvittr rlsgneqrvt
      361 ytgsvdiqmp dlssynlcna eekleaerid giyddanfll htekqmlyqr rkqliaagld
      421 tywlskplrt gvghkhnlsv elgdaetlra vldlsynqvi gvmkgsdrrn isgtldlsyr
      481 rnnlifnntm tvnsnksyds pygnfsdyak mnpywrakdt etgqvvrwae nkvanpmyda
      541 eigtlkrety vdflnnfqve wrlmnslilr arvmlsfkrn dgdeflpath snfagitkds
      601 pvedqlrkgs yrldngrssd vsgdihgnya itlgkhaiva mggfgiseys yqayvhraeg
      661 fpnsqsadit farqyaldkr pegssslrre infvlggvys yddryfldfn vqtsasslyg
      721 ndnrwatgws vgvgwnlhne pffpwkdlvs qfkvrgsigl tgnqnfdtne avatyqyytd
      781 anylgmtgsy lgrlanpslk weqkkdynvg fdatihravl rfdlyradte nmltdvsvpt
      841 stgfstvkdn lglvrnsgie aylsygvlqk drtfltvfgs lvttkneiir lsesmrafne
      901 lrdkmasdrg nnrpvlkyvd gesmetiwav rsagidpmtg qevyirrdgs ltytyyesdl
      961 spvgnelpky rgnfgftleh kgfgisttfr yqagfqyynk tlidrvenvd mnynvdkral
     1021 ygrwkepgqv tpfkrlgtfq ydgdpqsrqe mtratsrfvq dcreltwgsl nvyydfqpev
     1081 lnylrmkrlr vsfymeeiak mssvkaergf dypfartmsf sligtf
//
LOCUS       WP_118715712            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118715712
VERSION     WP_118715712.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124656
     Region          63..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknlerqac rrksrakvki rlpreftvgi ylkmlflpll ccvsllanav evrdstgvkd
       61 niikgrvmde kgqpmpgvtv lldstrlgvt tdtegnftlk ltrekgvlvf sfigfktvka
      121 rfeagkllti rmkeemssld evtviaygtq rrrevvgams tvsgedikdv pspsianllq
      181 grvsgmnvtn mtgapggggt sinvrgynsf diageqrfsn plwvidgvpm qsftspvtgt
      241 ntlaeidpnd iesiqvlkda asaaiygsra angvmlvttk sgrlnqraki svnfsrtwsf
      301 dpslpeltgg naernlrlea lrnfqqayfd pstntykyvs syresynenm hynyfwnkgd
      361 gagiaayqds lnsfynnstn ffkyyfrtak vtnanlqlsg gntnmsynig lgyydesgvl
      421 rntgfsrvnl lanffikplp kvesnvrfyl artgrkrasr ltaytgftsg eeleqipeel
      481 ltmstilpge gtpafdemik rfntikedne syrvrtsldl syeiikglkl kssvaldftq
      541 qnqnlflpsd ldeynesyss gqiernltli nenlltyrht fvekhtldfl lglsvqeder
      601 nsigtwgkds psdlihyisw fgnvynvden ralkdgttgr evstsvgvfg rlnynylery
      661 flsvtlrrda sskfgenvrw gtfpsyavaw tfseepfmdw srgvldhgkl rvsygksgkq
      721 fdqpyiaqgs fspgdpylgn ptihpdlsrg lsnkyltwee tgqydfgldl dfrdhrfgvv
      781 ldyyyrytdk llypvmlpgn ysafnrqwrn ayaisnegie levkwnairn eklnwnisfn
      841 iarnwnrlek senkrdflte dnttnlniig kplnglyvlk tggiynddke vprmfingkd
      901 tplagngntq hyragdrvvy dvngdgvvns ddrvyagapa pvaqggivtt lewkgfdlnv
      961 lfnfvisrhi lnaargasvg tiigltpdds vtpvyvdlnn vsfwqkpgdk tdfpmnrleg
     1021 glgsfnsytt anvedvsylk lktfsigytl pdrwkkkvgf gvrvfvsgen lftitnysga
     1081 dpesvnimtg vdnlgnypln rkltlgitgt f
//
LOCUS       WP_118715909            1196 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118715909
VERSION     WP_118715909.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1196
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134188
     Region          115..1195
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkkrtahi fvsflflsvs llcnstihaq nstvnlnykd asfvevinef rkqtgvkfmy
       61 nlekvkdkrc kdlivknipt kqaidivlkh fnlaysmveg vvvvkeqpee pqtkrtikgt
      121 vfdenggtlp gvtvlirgts mgvstdakgn fsitlpsqne nslifsfvgm qtqvikctdd
      181 kplkitmktd asqleevtvv stgysslprk dmvgayttvk aedimmpayn sidqmlqgki
      241 pgmvvinsss rigstpkiti rgtstilgnt dplwvvdgii qpdplpidas savtedmrnl
      301 ignqiswlnp sdietitvlk dasataiygs kasngvivit tkkgsaerts irystnfsfr
      361 trpnygmfny mnskeriqfs keaydagvry qsdplpqiyt yeglmamynn rlinendfmk
      421 qmerletcnt dwfdilcrns fshnhnlsis ggtqkvtyna sfgyssnhgt qkgddmtqft
      481 srlnvstqft ksllitfnls gsfndrkgyg pgvtpesyat qtsraipayd engeyvfykq
      541 yynyqlnrtg qleygyniln emensysknn sknfnvsvna dwsitdwlky qfvgsiaysi
      601 nnsesfagek tsyieqnyrg yaygsetsgs akfkaallpf ggelatnats ntsynmqhkv
      661 vfsktineih rinamagmei rsednknntn tvwgyvperg eilvsptrpt evtpvggtvp
      721 iswgaldkly qggwknttit nnyvsffatf ayslkdryvf nanirsdasn rfgqdankqf
      781 dptyslgvsw rmaeeefvka hlswlnqlni ratygvqgnv vtsvspdlit qyqgilsgyn
      841 eyyltisslp npllkwertk twnlgldlql fngitmsley ygrrsnaiin qdiaqeygmn
      901 tmrlnggrih nhgleysmni tpyqrkdfaw tigfnasknw nktqnddirt kadkitksdf
      961 isgssdrflk kgyplsafws ysfagldpet gyptfnlidf eeadpdidpt tflvysgqkd
     1021 pyftggintr irykslslgv nfsvllgakk rlpnpyqnfn ygklptpfyn lskdllkrwq
     1081 kpgdekhtiy palytsvedv yniklpdgts snsiyamwgn sdamvvnasf lrctqislsw
     1141 nipaqicskf gatncsisan vnnpfvigss rfngfdpelg dsvmpkifsf glsvgf
//
LOCUS       WP_118715828            1170 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118715828
VERSION     WP_118715828.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1170)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1170)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1170)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1170
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1170
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131484
     Region          136..1169
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknqsfyyf ygkksllkim rllfilmtmt smtisansfs qqqrvtldvk nvgamelfke
       61 iqketnlyfv yndadlisyn kisvsakdes vdvllkrvfp rlefmfegnv iivkpsvard
      121 dekevkkyvv kgkvvdeknl plpgvtirld sttvgcatda sglfsltlpv asgklifsfv
      181 gfkmetkvfk agdelivkmk eessdldevt viaygernkk elissvstvk akdleevpsa
      241 slenllqghm agvevnnvsg apggggtria irgyntlmqn gisdntplyv vdgvpiqsft
      301 spltgtntla eidpmtiesv evlkdaasaa iygsrasngv ilittkhgke gkatfqanas
      361 yswtwlpetp vqiqgngerq wwlyaakyai tgysdrqtnl ikwptsmdet igtngmydff
      421 wkngvsstwe esgkvpllpq lqdslnpfyn nstnwwkyvf qtgktlnanv qasggtervk
      481 ymvgagwyne eginvgsefs rvnlisnlnf vprknltmdt rlslsysdms msggglgstk
      541 iaymtvnpkg tptllpssga aydqmfkyin dvsekkynfn iranvrlayq iisglelsat
      601 vgadysqaqv nrfepsimda nyglsksegr mngsmyfqte ellhynfslk erhnfdwlfg
      661 fsytrqssnd lagsgkgsps dyihyvvegm ptikdlngtm tamqsfnsgf keqkmvsyfg
      721 rvaynfdrky lieltlrrdg ssvfgkdvrw atfpsialgw nfsdeafmkn fwwlshgkir
      781 gswgtsgqtf ldpylaqgii dvgssflgvt glmptqmenr nltweksnqy dlgldmdlfd
      841 yrfkfkfdyy ykytksllwe vqlpgtvyfh ktmwdnavei snegveleaq ldilrntevk
      901 wrarfnisrn wnrlektytg vdidgkyvig rsanelqvyk dlgyvqnane vpitwdsqgn
      961 prylgvggma nptrpgmhml adlngdgvia dedlyfagst lpkayggias eitwkgfdln
     1021 llfsyslgrk minafrkgal nfnpmglgav fedyrnvsfw ekegdqsdyp vmssvyyynk
     1081 gqfdglvdsn ietvnfirlk qltvgynlpa ewarkcylqg irvfftgenl fllsnysgld
     1141 penvdvmtgi dnmttyptsr kltlgltvkf
//
LOCUS       WP_118715952            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118715952
VERSION     WP_118715952.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124932
     Region          107..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkltlflvff flasanaftq kvtllvksat lnevlrqikd qsgvrilyda gktkqiqceg
       61 ikivdmniae algqvlkdtr feffeeggvy ivremtaqqa kilrivgkvv dekkqplpgv
      121 tvqlkgvsig tattgdgsyv lsipnapkkf tlvfsfvgmi sqeivyagkd tinvmmkedv
      181 atledvvvtg ysnirnssft gnavtikkdd llkvsktnvi kaiqsfdpsf rikennrwgs
      241 dpnalpevyi rgesgigvkq mdkealaksn lkdnpnlptf imdgfevsvs klydmdpnri
      301 esitilkdat atalygsraa ngvvvittvp pkagklnidy nfvgdvtfpd ltdynllnak
      361 ekleterlag cfeadpsdqw anpyalkkey neklanvtkg vdtywlskpl qtvfnhkhsl
      421 yvdgggesvr fgiellyanq dgvmkgslrd rigaglslqy tyksfmiknq isyqkvrvke
      481 spygnfadfa kqlpydvykd eegkysttmr nwgtgspanr vnpmyepslh nfdksksdef
      541 innlslnwni ldglllkgql sltktmgesr rfydplskqs anlnplslkn lssgtlylgh
      601 tddlsldmsa tlsynralgn hmvnalvgis mkedqsdsdn styigfpsga lsapeyakem
      661 ynktnfsest krlvgflfsl nysfkdiyll dasmridgss afgtdkrfap fwsfglgvnl
      721 hkyefmksme fvdqlkirgs ygqtgkanfp ayaarttylv stdkwyktgi stklqalgnn
      781 kltwettnsf digaeitlfh dflyvkgsyy nkrtidlind vtvptstgft syrdnigevs
      841 nkgcefdlri sayrskdwlv ifnanlahnk nriekisesl kaynqrvrdq fekqyvygdp
      901 eqalqtqpfl qyeeggslss iwgvrslgin padgqevlln rqgmmtkaws asdqvvlgtt
      961 eptvqgtfgf nvvykqfslf tdfmyeaggq rynqtlvdkv envnvytdnv dkrvltgrwq
     1021 kpgdiakyks lvtgrdpvkn tkptsrfvqd ynmlswnsle lgydlspdit nklnvsmvrf
     1081 tfgmsdilhl ssvkqergis ypfartvtfs lkvsl
//
LOCUS       WP_118716069            1129 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118716069
VERSION     WP_118716069.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1129
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128608
     Region          69..120
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          137..1127
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkrivhll pkrrllktwl imrfivlflc msamqltaav ysqevkvtlq vkdasfesvi
       61 rlleknteyt flyedrhiae vgglnlnfrd tdikvvldkc lqgtnlsyrl mnnhtiviqr
      121 giavdttkqk apqkmsvtgi vkdvkgealp gvtirikntq lgfvtdidgk fkfdfprqdt
      181 vvlifsfvgy ktqefqvknd kpitivlked vtevdevvvt giftkakesy tgavttitak
      241 dlqrvgnrnl vssirnidps fniadnidig sdpnklpdit irgssslgvg vkdlqedsrs
      301 tqkanqplfi mdgfeitler mmdldenqve sitllkdasa tamygtrgan gvvvivtkkp
      361 eagrirvtyk gslnieapdl tsydllnare kleyewaagl yentnanqtq emmdlynrrk
      421 idaergvnty wlkypvrtgv ghkhslrfeg gdeiyrysvg lsyndiagam kgsnrrtfng
      481 nvflsykykn ltfqndlqvs snrsynspyg tfndfakins ywtpydeegn ivkvledyyy
      541 lsilttnfvy nplynaqlps knesrytqiq nnfavewhil pelfvrgrlg itskndredv
      601 yksakhtdfd kyseddydrk gtysygtget fnyeadftln ysknfadkhq lyvglgynfa
      661 qeknefftil aegisninmd flgmaskyek dghpkskegf srrmggiana nytydrryfi
      721 dasfkiegss kfgsdnryap fwsvgigwnl hqeafmagsq llnvarlkls ygtsgsqafd
      781 syqamttfkd yggssyqgwy gvylramgnn dlgwqktkql nigteleffn gririnadyy
      841 nkvtddllsd itlpsssgfd sykanvgqva ntgvelglnv yvlrdtkrdm mwliggtlah
      901 nkneikkisn sleflndqms sedggnpsfm yeegqsmnti favkskgidp sngkeiyikk
      961 dgtetytwdp kdkvpcgvde pkiwgnlntm frykgitlna ifgyryggqm ynytmvskve
     1021 nikpfdnadk rvlydrwknp gdnaffkgvr dftktnatsr fvmdentlec rsislgydwe
     1081 akwldqvgis yltitgymed vfrissikqe rglsypfsrk fslslsvrf
//
LOCUS       WP_118716217            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            sp. AF15-53].
ACCESSION   WP_118716217
VERSION     WP_118716217.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter sp. AF15-53
  ORGANISM  Odoribacter sp. AF15-53
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Odoribacter sp. AF15-53"
                     /db_xref="taxon:2292236"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115305
     Region          45..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrslgvcgli vcvillfgkt lyssekyagk avylidsvdg qperivvegv vydtegetmv
       61 gvnilergtt ngvitdrdgr fsirvnpkgt llvsfvgykt kfvsydgrdk lqiileqeyv
      121 llddvivtal girkqetsla yatarvnkde lvrvkdpnmi valmgkiagm qvnksasgig
      181 gsakvimrgn rsvagnnqpl yvidgvpmln esseqpntai ggtadagnrd agdgisnlnp
      241 ediesisilk gapaaalygt qaangvilit tkrglagkqe vvfssnltfd kamclpelqn
      301 hygesdvves wgeredirgs npitsffktg vmaintlalt tgnervqtyf sygnttgkgi
      361 lethrltrhn inlretasff egrlnvdgnv nllsqvtkns pvpggfymnp lvglyrfprg
      421 kdiseykehf evrdetrhld vqnwhapted feqnpywiln ritsrakrvr aivsvglnlr
      481 itedlavqar gsmdyvtdkf rqkfyastap alagsngryi esdyeqelty gdvigtykkk
      541 wndfslnvsl gasinnnkvn elrydsktas lkyanvfnia ninmttsayi tqridatrqi
      601 qsvfgtaqfg frkflfldvs arndwsstla ftshestgff ypsfgvslli dqlfklpgwv
      661 nfgklrgaws kvgndiplyi tnpvahvlag ggiqasdaap feemqpevnr slefgtewkc
      721 lnnrlhldft yyrtctrnqf fklaaedgde yayryvnagn irnegvellv egepvvasgf
      781 twktgvnyaf nknkvirlhk elpvfqygpy gfsssyamkl keggafgdiy gkafkrdekg
      841 nilyetegdr eglpvvegdg ntikvgnanp kftlswlntf sykgfvlnfl idgrvggkvl
      901 sqtqadmdmf gvtrvtgkar drgyvmlegr kitnvkgfyk sivggragvt eyymydatnf
      961 rlrelslayt lpkrwmektr vfkevqlafv arnlffiykn apfdpdlils tgndnqaids
     1021 ygmpttrttg fnlrvtf
//
LOCUS       WP_118766916             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cellulomonas rhizosphaerae].
ACCESSION   WP_118766916
VERSION     WP_118766916.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas rhizosphaerae
  ORGANISM  Cellulomonas rhizosphaerae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Cellulomonas rhizosphaerae"
                     /db_xref="taxon:2293719"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51835
     Region          4..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mttigipret rpgerlvaat ptsvgrlvgl gydvvveaga gsaaayadea yaeagative
       61 dawgadvvta vnapsderva alrpgavlva mlapaahpel aerlraqgvt alaldavpri
      121 sraqsldvls tlsnvagyra vieaaeqygg mfggqvtaag ktaparvfvi gagvaglaai
      181 gaadslgaqv rafdvrpeva eqiesmgaaf vraataqqqv stdgyasalt deqeaataav
      241 yahesaeadv vittalvrgt apttitadmv aamrsgsviv dlaasgggnc eltvpgqrvv
      301 tpngvtivgw tdlagrlprh tsqlfatnvv hllqlltpgk dgvlvldled pvqrgmtvth
      361 egdllwpppp vavsaapapv pppappapvd prpaarrrlv gfalaavlvt latsfappvf
      421 lghatvfvla vfvgyyvisn vshslhtplm aqtnaisgii lvgallqigs ddwlvttlac
      481 vaaalasinv fggflvanrm irmfrrda
//
LOCUS       WP_118778702             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_118778702
VERSION     WP_118778702.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53799
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118779372             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_118779372
VERSION     WP_118779372.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53843
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nllnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgnsf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118781720             508 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus haemolyticus].
ACCESSION   WP_118781720
VERSION     WP_118781720.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     gene            1..508
                     /gene="nrfA"
     Protein         1..508
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56675
     Region          1..501
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnalkksliv aasfaslslf nsavadmvyk pleqpvepvk pdlkiesvne kfaekypnqy
       61 nswrstangn gekiiyadee nprlivlwgg yafakeynap rghfyavtdv rnilrtgapk
      121 tandgpqpma cwtckgpdvp rliaewgekd yfnakwakgg peivnsigca dchdttskdf
      181 aegkpalria rphvlraldh lnnavqakak aegkttpnls fntaertekr aeicanchve
      241 yyfagdikqv tfpwdngqtv ddiekyyddi gfsdwthsls kapmlkaqhp dfeiwslgmh
      301 gkngvtcvdc hmpkvqgkdg kvytdhqiqn pfdafdrtca nchdqskekl rnivtsrkke
      361 vkdvmgrlee qvvkahfeak aawdagatke emeaalmdir haqwrwdyaa ashgghmhap
      421 evmlrvlgsg ldkaadartk laailtkhgv ktpvqipdis tadkawkvmg idiekerkak
      481 eeflktvvpq weqqakekgl lvdppaqk
//
LOCUS       WP_118784529             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_118784529
VERSION     WP_118784529.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53746
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealcakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118786540             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_118786540
VERSION     WP_118786540.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53817
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtmlafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118787474             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_118787474
VERSION     WP_118787474.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53737
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqppsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118788733             508 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus haemolyticus].
ACCESSION   WP_118788733
VERSION     WP_118788733.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     gene            1..508
                     /gene="nrfA"
     Protein         1..508
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56738
     Region          1..501
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnafkksliv aasfaslslf nsavadmvyk pleqpvepvk pdlkiesvne kfaekypnqy
       61 nswrstangn gekiiyadee nprlivlwgg yafakeynap rghfyavtdv rnilrtgapk
      121 tandgpqpma cwtckgpdvp rliaewgekd yfnakwakgg peivnsigca dchdttskdf
      181 aegkpalria rphvlraldh lnnavqvkak aegkttpnls fntaertekr aeicanchve
      241 yyfagdikqv tfpwdngqtv ddiekyyddi gfsdwthsls kapmlkaqhp dfeiwslgmh
      301 gkngvtcvdc hmpkvqgkdg kvytdhqiqn pfdafdrtca nchdqskekl rdivtsrkke
      361 vkdvmgrlee qvvkahfeak aawdagatke emeaalmdir haqwrwdyaa ashgghmhap
      421 evmlrvlgsg ldkaadartk laailtkhgv ktpvqipdis tadkawkvmg idiekerkak
      481 eeflktvvpq weqqakekgl lvdppaqk
//
LOCUS       WP_118792812             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            bergeri].
ACCESSION   WP_118792812
VERSION     WP_118792812.1
KEYWORDS    RefSeq.
SOURCE      Neisseria bergeri
  ORGANISM  Neisseria bergeri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria bergeri"
                     /db_xref="taxon:1906581"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53777
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallsklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsegel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlanltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vaptaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_118794727             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118794727
VERSION     WP_118794727.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53777
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwvcpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpspklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaas aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_118796707             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_118796707
VERSION     WP_118796707.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53857
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsedel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118800193             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118800193
VERSION     WP_118800193.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53683
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwvcpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_118802779             508 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus haemolyticus].
ACCESSION   WP_118802779
VERSION     WP_118802779.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     gene            1..508
                     /gene="nrfA"
     Protein         1..508
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56724
     Region          1..501
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnafkksliv aasfaslslf nsavadmvyk pleqpvepvk pdlkiesvne kfaekypnqy
       61 nswrstangn gekiiyadee nprlivlwgg yafakeynap rghfyavtdv rnilrtgapk
      121 tanegpqpma cwtckgpdvp rliaewgekd yfnakwakgg peivnsigca dchdttskdf
      181 aegkpalria rphvlraldh lnnavqakak aegkttpnls fntaertekr aeicanchve
      241 yyfagdikqv tfpwdngqtv ddiekyyddi gfsdwthsls kapmlkaqhp dfeiwslgmh
      301 gkngvtcvdc hmpkvqgkdg kvytdhqiqn pfdafdrtca nchdqskekl rdivtsrkke
      361 vkdvmgrlee qvvkahfeak aawdagatke emeaalmdir haqwrwdyaa ashgghmhap
      421 evmlrvlgsg ldkaadartk laailtkhgv ktpvqipdis tadkawkvmg idiekerkak
      481 eeflktvvpq weqqakekgl lvdppaqk
//
LOCUS       WP_118805629             508 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus haemolyticus].
ACCESSION   WP_118805629
VERSION     WP_118805629.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     gene            1..508
                     /gene="nrfA"
     Protein         1..508
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56807
     Region          1..501
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnafkksliv aasfaslslf nsavadmvyk pleqpvepvk pdlkiesvne kfaekypnqy
       61 nswrstangn gekiiyadee nprlivlwgg ysfakeynap rghfyavtdv rnilrtgapk
      121 tendgpqpma cwtckgpdvp rliaewgekd yfnakwaqgg peivnsigca dchdttskdf
      181 aegkpalria rphvlraldh lnnavqakak aegkttpnln fntaertekr aeicanchve
      241 yyfagdikqv tfpwdkgqtv ddiekyydei gfsdwthsls kapmlkaqhp dfeiwslgmh
      301 gkngvtcvdc hmpkvqgkdg kvytdhqiqn pfdafdrtca nchdqskekl rdivtsrkke
      361 vkdvmgrlee qvvkahfeak aawdagatke emeaalmdir haqwrwdyaa ashgghmhap
      421 evvlrvlgsg ldkaadartk laailtkhgv ktpvqipdis tadkawkvmg idiekerkak
      481 eeflktvvpq weqqakekgl lvdppaqk
//
LOCUS       WP_118809845             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118809845
VERSION     WP_118809845.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53860
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 aavwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakdv diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflkhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqdngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_118808106             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118808106
VERSION     WP_118808106.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53934
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsddgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatv gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_118810729             513 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Neisseria].
ACCESSION   WP_118810729
VERSION     WP_118810729.1
KEYWORDS    RefSeq.
SOURCE      Neisseria
  ORGANISM  Neisseria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria"
                     /db_xref="taxon:482"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53874
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsedel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitln fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118812338             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_118812338
VERSION     WP_118812338.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53787
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vtmlafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118815037             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118815037
VERSION     WP_118815037.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53741
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekvvp aakpepkpvp lwqklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_118818014             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_118818014
VERSION     WP_118818014.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53789
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgnsf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118821786             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118821786
VERSION     WP_118821786.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53863
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtvgatvadk
       61 aavwacpliy kvnapsegel pllkegqtii sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtmlafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118818353             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118818353
VERSION     WP_118818353.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53826
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvacts atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_118822656             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118822656
VERSION     WP_118822656.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53796
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl ssetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaas aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_118823907             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118823907
VERSION     WP_118823907.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53765
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_118824293             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118824293
VERSION     WP_118824293.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53919
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag waaslddaay qtagatvadk
       61 aavwacpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittasip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118824580             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118824580
VERSION     WP_118824580.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53757
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 aavwaypliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lfvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_118825748             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118825748
VERSION     WP_118825748.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53774
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 aavwaypliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkqge
      301 lfvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgivvvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_118827133             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Salinibacter ruber].
ACCESSION   WP_118827133
VERSION     WP_118827133.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40281
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maltigvpre tepgetrval vpdvadrlla tvddldirve egagqgayht dadydaagcs
       61 vvgrdatfda diiakvapps ddevdrlgeg qvlvgflspl erpetaqala drgvtalame
      121 lvprisraqk ldalsamssi ggyraaigaa erlpaffpll ttaagtvrpa rvlvlgagva
      181 glqaiatakr lgakvfgydi reptreeves lgasfvelev dieadqdesg yaeqvekekq
      241 erqpellqph laeadvvist alipgqpapl lineeavaam dpgsvivdla apnggncalt
      301 etgeeivahn vqilgptnlp aempvhasel yaktvaamie egleadafap dfddeifaes
      361 cltrdgtvqn drvqgllgta eeaka
//
LOCUS       WP_118827110            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118827110
VERSION     WP_118827110.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109985
     Region          27..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlipsvvf glallllpgl awaqqgtvtg tvteaetgsp lpgatvqivd egsgaasdae
       61 gqyriagvpa geqtlrvsfv gyqaqertvn vpeggtvrvn fqlqtgeaql eevtvsayrp
      121 etdrvatgad atvsgesiet adltsaegal qgrasgvrvt slggqpgsgf siqvrgalsv
      181 nagsdplyiv dgvqinkenn ldladgnpls tinpgniesi qvlkdaaaas iygaqaangv
      241 vvietkegrs gdtqinfstk lgsvsniepy gvmdseqyln fraealdnas renfgipasv
      301 afgsdpqtvv ngafgpdsin tdwtdqvfre gftqsynlsl rggsddtqfy isgnftrdeg
      361 qvidsnfrrg glrlnlnhqp adflnlsakt nlsttryqgt isdgafinsp fwaaynippt
      421 spvyttpgdp stafnltpns tfsynpvaqe kfntressan titsnvtanw dlpaefaart
      481 fvgvqyvdtk efdygdprlp pnagfggdgf nstqrditfn vsqtlsyent fasvntisal
      541 agaeikrnre qftsgsgegf pnelfrtlas aanptdvssf stqyrqisyf gnatytfdnt
      601 yqiggtlrrd ansrfgvdnq sgifgtvsgf wrisnesfle dtdvisnlkl rasygvtgns
      661 didnfqsrqq fsgsgeyngt pgirptalgn psltweekvs tnvgldygff ggritgsvdv
      721 frddreelll frdlsldsgf gsyldnvgei rvegldfsvs tinlndwngl twetnfnisf
      781 qrtevrsllp gddevtsggd vyrvgepaaq lrytryagan pangrpmyld angdltyvgn
      841 dtnneklign lqpdfyggfg ntisykglqv saffqydygr ktlnndrffa dvgyfpynka
      901 erlvdnrwke pgdvtespaa fgsllasgld tyadgtdpgi fttrfvenas yirlkevkvs
      961 ytlpksltet vgslrnvtvf vqgsnlatwt nytgpdpelv gtglgnypqa rtltagldlg
     1021 l
//
LOCUS       WP_118827418             967 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118827418
VERSION     WP_118827418.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 967)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 967)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 967)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..967
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104446
     Region          28..936
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mllrryllfv glllfaplvg haqstgsvag tvtdandrpl pgvnvaiqav qrgaatgpdg
       61 sytisalepg qytiqaslvg yetqratvtv eagenvvqdf vmtaaslnld evvvtgqgse
      121 vsrralgtnv stisaediqe tpttsidkll qgrvpgstir sqsaqpgqga linfrgitsv
      181 fanqtpviyv dgirvdnsss tsfsfggett salseiltnd ierieitkgg aastlygsda
      241 angviqvfta dgeagetevt frtrqgvdfp vsrffkdtgf sfpetreded spdfgrtnyi
      301 eneflrrgys qdyyvgvsgg seaitynlsg rlqdgsgvqp nnsntlyalr gnvsadvaee
      361 lsvqfngsyt rsnftrlsng taiadpltml evgdakfftg tnnlrdaldm atlpqikegv
      421 dryrlsaraa yrpnelfnss ltvgidgrtn eqralfprea dpltgntngi ltrfnrdfks
      481 itleyrgtis ypregpvtst ftfgaqgfrd eesqvwaeae tfalpgtedv geagsvvade
      541 lreqvfnggv ffkeqlgyen rlflstglrl dgnsafgedv gvqvypsael syiltdepfw
      601 qgslesvlsq lklraawgqt gkfpdpftrd vtfqatsfrg asaprfdnpg nanlgpekts
      661 tleggfessf fdgrfgldft vyqsrttnal fevpeqpatg rglqfrnvge irnvgtelsa
      721 dvrvlqlenl fwqvggswsw nqnemeslgg aapfniggsa efaqqrvkeg qpigawratt
      781 pydsngdgql dasefrftge tpfpvhtgaf ttsltvqnfr lfaladwatg sevldwgshw
      841 asfnglerap rpqkfdengd pitdadgnpv dfstaeagsa llqdgdylkl revtlsynvp
      901 gslldvagid qgsiyvtgrn lwaftrqelv dpelagltdt dnvalggsqs itlspprqiq
      961 vgveitl
//
LOCUS       WP_118827483             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118827483
VERSION     WP_118827483.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53590
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealcakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_118827533            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118827533
VERSION     WP_118827533.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114185
     Region          29..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrysvlllg vllgalcfsp tssaqdpatv rgvvtdstga plpganvrvq gtqtgvsada
       61 dgayelaavr pgrrtivfsf vgfekvsrtl elsagdtrtl ditlgtgtvg lenvvvtalg
      121 vdreerslgy svervsgsdv aeapepnvmn nlsgkvagln vtggsgglas tprvtirges
      181 slagsnrpli vvdgipidnt pntqgsdaqt tqvdfgngls qinaqnisem svlkgpsaaa
      241 lygsraadgv ilietkdgse tdgigatvrt svtasrplrl pdyqneysyg nggefayvdg
      301 tnapgwnwgv rmdegverpq wqgprneage liptevtsap nkvrnffntg tnvstdvavr
      361 gggenssfra slsrsdrtgi vpntnldrts tslsasydvt daltvdanan yanttsdnlp
      421 ssgygsesim yyftwgarhv endllkdywq eegtqqahyd rnwtnnpyfq vnentngler
      481 drlyggvsar yeftdnlnlr artgldysnq gtkqrkafss itapngwlqe adrtftewns
      541 nlllnytrev gdftfepsvg anfmrqtrrn vqltaqalsv pdvynignar snvqaderde
      601 aqeilgvfas gtvsyqdmlf ldltgrndws stlpldnnsy fypsaslsvi vsdlvdvpef
      661 lplsfakvra swaqvgndtd pfrltntytf gdawgstqtv vseadlanan lqpeitssye
      721 vgtnlrfydg raqldvtyyr sttrdqilsv plaqstgyns rlvnageirn tgvetrlqls
      781 piqdwsgfgw dvslnwtrnr stvveladgi dtfvlgegpf ggsaqaregg rmgdiygrvf
      841 drvedpssph tgeiiyedgl pqltddvekv gnynhdwrgg igstfsyenl qlnvlfdvrk
      901 ggllysntha tgieggsleg ttrarnetvv gdgvvqnddg tysenteeaa yvtwlrtyyd
      961 rpnvesnsfd atyvklrels lrynftpdwl tragvqnvgv svtgrnlflw tdvphvdpet
     1021 tisggdgqip gfevqqipst rsfgmnvqln f
//
LOCUS       WP_118829177            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118829177
VERSION     WP_118829177.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116228
     Region          27..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlipsvvf glallllpgl awaqqgtvtg titeaetenp lpgatvqvqd egtgaasgsd
       61 gqyriegvpa geqtirvsfv gyqpqertin vpaggtiran fqlqtsqael devvvtgvat
      121 gtdteklgfd vaqvsgdals evpatdpana lrgkvagaqi aegsgapgvs psiqlrgats
      181 itgdrsplvi vdgvitsggl sdismqdvts ievtkgaaas slygslagng viqiqtqdga
      241 qtgnldvtvr sevgasqvag dypsatrhpw tmegmevqlp ngdtrtvsga nvqeqvenfp
      301 dgtkilswpg rsnetfdvee dgtrlfdnpf pstfnnvena vtsklnttnf vsiagsqeef
      361 nykvsyenfq qdgilepvgs ynrntfrfng dyspegrlsv sanasyvtss gpvieeqgqd
      421 dnyfygllta dpyidmtekn dqgefafqpt gydvqqsnfq spyyvaqnrt wetdqnrlfg
      481 gvelnfdild nwvltgrqsi drtnqrtelf ypkgyqtpdd dallasgldn reddqsqdli
      541 tevsttynde frdlaytatv kylyeqretd dlslegagfp asgirsvgat dsenysigsf
      601 taeertenff lnldldyqdt yilsglvrrd gsslfgeder wqtyfrgsla yrltedfdip
      661 nvsklklrga ygtsgnrppf saqyetysat esglqvqnlg nselrsstif etsigidatf
      721 lqrfnltvny adsrtkddyl qvplaggvgf snqfqnigev esttweasld sqiltgddgp
      781 swsvgatfsr vrqeitdlgg apaftrdpan ldsdntdapa lslfrveegv pfgamygnkl
      841 ltsldqltvv dgevlnsggs srddftinnq gyvipagteg tpdeqpvymv nedggtavtq
      901 igntrpdfqv glrsnftwkg fgvyglldws qggdvynysk qllyfnyrhe dqqdfaeqgk
      961 diaysdgssn iynqggpssy fvedatfvkl relsvsytld qdllqdafgt gaveriklsv
     1021 igrnlftitd ysgwdpevgl rsdannfkld eyaypnfrtf tgsvsvqf
//
LOCUS       WP_118829180            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118829180
VERSION     WP_118829180.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111587
     Region          27..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlipsvvf glallllpgl awaqqgtvtg tvteaetgnp lpgatvqivd egsgaasdae
       61 gqyriagvpa geqtlrvsfv gyqeqertvn vpeggtvrvn fqlqsgtaql eavtvsayrp
      121 eadrtvegga aasissedve saqvqsaega iqgkasgvrv lstsgqpgag fsvnvrgavs
      181 vnagtdplyi vdgvqvnked nlafaqgnpl sslnsndies irvlkdaasa aiygaqaang
      241 vvlietksgr agdtrinvss qvgfrdaitp fdpmtteqff nfqdealnna vaaktpfrsl
      301 edagipantf ipgaegalta rqynrvalgp dtintdwkda ilrtgntqsy nasisggses
      361 tqfrvsgsfe rteaqaissg frqgqlraki eneaadylsl tananlstnk yegvteaavs
      421 vgspffasfq lrpnlpiynt vgdpssgfnf pgrtfpnpva sqelntresg vnsvsanveg
      481 dwdlprgfaa rsfagvqyed vqeefygdpr ipansgsggt gsfdtqrdis vnvsqsfsyr
      541 nrfsdvhdvs alagselrrv ketfsdaege qfpnelfrtl ssaadpvdas afstqfrqls
      601 ffgngsytyd dtyqiqgtlr fdgnsrfgqq nrygtfwtaa gfwrisnesf ledadflsnl
      661 klrasygvtg nsdgignfqs lqqygsggay dgsplirann ignaaltwee kvstnigldy
      721 gffggriqgs vdvfrddres lllnrdlpss sgfgsildnv geirvegidl slsttniddw
      781 ngitwttdfn isfqeaevtk llpdddliqg gayevgeapg qlnltpyaga npangvpmyy
      841 dkngnltydg gdpvddrqvg nanpdffggl tntvslggls vsaffqydyg rrtyandlff
      901 tninvpfttn ksqqlldrwk epgdlssvpk aygtafgqfl pfgtdlttya nglpeqqtfn
      961 strfvtnasy irlkrvqvry sfpgsilesl pqvrslsafv rgsnlitwte ydgvevesvg
     1021 nvsstvfpqa rsitfgidlg l
//
LOCUS       WP_118829197             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Salinibacter ruber].
ACCESSION   WP_118829197
VERSION     WP_118829197.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40323
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maltigvpre tepgetrval vpdvadrlla tvddldirve egagqgayht dadydaagcs
       61 vvgrdatfda diiakvapps ddevdrlgeg qvlvgflspl erpetaqala drgvtalame
      121 lvprisraqk ldalsamssi ggyraaigaa erlpaffpll ttaagtvrpa rvlvlgagva
      181 glqaiatakr lgakvfgydi reptreeves lgasfvelev eieadqdesg yaeqvekekq
      241 erqpellqph laeadvvist alipgqpapl lineeavaam dpgsvivdla apnggncalt
      301 etgeeivahn vqilgptnlp aempvhasel yaktvaamie egleadafap dfddeifaes
      361 cltrdgtvqn drvrgllgta eeaka
//
LOCUS       WP_118829455            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118829455
VERSION     WP_118829455.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114320
     Region          29..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrysvlllg vllgalcfsp tssaqdpatv rgvvtdstga plpganvrvq gtqtgvsada
       61 dgayelaavr pgrrtivfsf vgfekvsrtl elsagdtrtl ditlgtgtvg lenvvvtalg
      121 vdreerslgy svervsgsdv aeapepnvmn nlsgkvagln vtggsgglas tprvtirges
      181 slagsnrpli vvngipidnt pntqgsdaqt tqvdfgngls qinaqnisem svlkgpsaaa
      241 lygsraadgv ilietkdgse tdgigatvrt svtasrplrl pdyqneysyg sggefayvdg
      301 tdapgwnwgv rmdegverpq wqgprneagd lvptevtsap nkvrnffntg tnvstdvavq
      361 gggenssfrv sfsrsdrtgi vpntnldrts tslsasydvt daltvdanan yanttsdnlp
      421 ssgygsesim yyftwgarhv endllkdywq eegtqqahyd rnwtnnpyfq vnentnsldr
      481 drlyggvsar yeftdnlnlr artgldysdq gtkqrkafss itapngwlqe adrtftewns
      541 nlllnytrev gdftfepsvg anfmrqtrrn vqmtaqalsv pdvynignvr ssaqaderde
      601 aqeilgvfas gtvsyqdmlf ldlagrndws stlpldnnsy fypsaslsvi vsdlvevpel
      661 lplsfakvra swaqvgndtd pfrltntytf getwdntptv vseadlanan lqpeitssye
      721 vgtnlrfydg raqldityyr sttrdqilnl pfaqstgyds rlvnageirn tgvetrlqlt
      781 piqdwggfgw dvslnwtrnr stvveladgi dtfvlgegpf ggsaqaregg rmgdiygrvf
      841 drvedpnsph tgeiiyedgl pqltndvekv gnynhdwrgg igstfsyenl qlnvlfdvrk
      901 ggllysntha tgieggsleg ttrarnetvv gdgvvqnddg tysenteeaa yvtwlrtyyd
      961 rpnvesnsfd atyvklrels lrynftpdwl tragvqnvgv svtgrnlflw tdvphvdpet
     1021 tisggngqip gfevqqipst rsfgmnvqld f
//
LOCUS       WP_118830114            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118830114
VERSION     WP_118830114.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113857
     Region          39..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mppfvssyss fkivltavfg vllacglpgg vqavhaqdfe vtgtvvsadn qsplpgvnir
       61 eagtsrgtvt gpdggfslvv dspqdtltfs figyqtktvp vdgrseirvv letesqeleg
      121 vvvtalgier qqrsvgyats sieaqdlvdv tesnpanllq gnvpglvlss nasgpnssss
      181 inirgvssia gnndplfivd gvpidntvig gagkfggrdg gsalsvvspe nisdisvlkg
      241 agaaalygtr ardgvvlitt ktgrtsapge vsvqysstvt akdvisgfsd fqsrygqgtq
      301 grapsnqdaa lsaglsswga plgevdeapq fdgtvrpydd vadrqgfyrt glsqrhslsi
      361 nagfentslr lsashqnteg vvpnsgyeqt ninlrgqtrl ggltadasvt yqneltdnrt
      421 flndaarnpn ylisflpnni pksalqpgat eegvekqfts dglptnpywa vneleadddk
      481 drilgnvnln ysindwlslq gqtgldwysl rrtnvdafgs afepggsmte dtyrvwesns
      541 kllatatpsl tdelslrldv ggslrhrqfe qvgvfgrnfs ipdletisnt anptrnydfs
      601 eqqirsffgs asftyrnylf ltlttrsdws stlpednnpf vypsvsgsfv ftdafdlpda
      661 lsygkvrasw aeiggdtdpy rtsltygiig qhqgqaleti tqlsvplldl kptstreiel
      721 gfetqffndr fgvdftwyrr stvdqildvt vssasgytar tansgeirnt gvellltsip
      781 ystadwtwds rvnfaanrsq veslapgldv rvgpenrlat aniaqvvgqp anaiygntyv
      841 rddqgrivhg edglplsgek evlgtgapdw tlgfsntisy qnvsldflid akwggkvfsg
      901 tnanaygngl hkatldaraa cdeqagsngr ypedcfvgeg vigsvngege vtvdrendvg
      961 vrpseyygri sgeiaeefvy danfiklrql rlsydlpssv msrvpvrsas vsvvgrnlfy
     1021 lydsvpnisp essynseatp gfeqagvpqs rsigasvnlr f
//
LOCUS       WP_118831615            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118831615
VERSION     WP_118831615.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114312
     Region          29..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrysalllg vllgalcfsp tssaqdpatv rgvvtdstga plpganvrvq gtqtgvsada
       61 dgayelaavr pgrrtivfsf vgfekvsrtl elsagdtrtl ditlgtgtvg lenvvvtalg
      121 vdreerslgy svervsgsdv aeapepnvmn nlsgkvagln vtggsgglas tprvtirges
      181 slagsnrpli vvngipidnt pntqgsdaqt tqvdfgngls qinaqnisem svlkgpsaaa
      241 lygsraadgv ilietkdgse tdgigatvrt svtasrplrl pdyqneysyg sggefayvdg
      301 tdapgwnwgv rmdegverpq wqgprneagd lvptevtsap nkvrnffntg tnvstdvavq
      361 gggenssfrv sfsrsdrtgi vpntnldrts tslsasydvt daltvdanan yanttsdnlp
      421 ssgygsesim yyftwgarhv endllkdywq eegtqqahyd rnwtnnpyfq vnentnsldr
      481 drlyggvsar yeftdnlnlr artgldysdq gtkqrkafss itapngwlqe adrtftewns
      541 nlllnytrev gdftfepsvg anfmrqtrrn vqmtaqalsv pdvynignvr ssaqaderde
      601 aqeilgvfas gtvsyqdmlf ldlagrndws stlpldnnsy fypsaslsvi vsdlvevpef
      661 lplsfakvra swaqvgndtd pfrlantytf getwdntptv vseadlanan lqpeitssye
      721 vgtnlrfydg raqldvtyyr sttrdqilnl pfaqstgyds rlvnageirn tgvetrlqlt
      781 piqdwggfgw dvslnwtrnr stvveladgi dtfvlgegpf ggsaqaregg rmgdiygrvf
      841 drvedpnsph tgeiiyedgl pqltndvekv gnynhdwrgg igstfsyenl qlnvlfdvrk
      901 ggllysntha tgieggsles ttrarnetvv gdgvvqnddg tysenteeaa yvtwlrtyyd
      961 rpnvesnsfd atyvklrels lrynftpdwl tragvqnvgv svtgrnlflw tdvphvdpet
     1021 tisggngqip gfevqqipst rsfgmnvqld f
//
LOCUS       WP_118832032             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118832032
VERSION     WP_118832032.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53686
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvessag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_118838109            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118838109
VERSION     WP_118838109.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115144
     Region          40..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mppfvssyss fkivltavfg vlligiaavg sstgaraqdi evsgtvvaag dqaplpgvnv
       61 reegtnrgta tdvngeftis vsgenavlvf sfvgfqeksv pldgrseltv alneqvqdme
      121 evvvtafgme kkrqnlgysv edvegadiae sgannlgdal qgrvsgvsvq spatgpggss
      181 ritirgnanl agndplyvvd gvpirnvqeg sagrfggtdg gdalsklnpe diesmsvlkg
      241 gaaaalygtr aqngviviet kggdlaqeey fsaeysgsvr aqmmkstfge fqyeygqgtn
      301 gqppqnetqa lnqalsswga pidevdeavq fdgevrpyea rdenleefyd tgirsehsia
      361 lsrgsqaydv rmslsrmddg hiipatqlnr ttlnlrgage ignlfmdgkl nytiekasfr
      421 pelsdnpanp mlslsfmptt lgvntldphk dedgnhraws ssvfrpnpyw gmreferddq
      481 qrrvqgfala rynftedisl qarvgtdwyt lddtfsepgg tpwiqngrif etttrrredn
      541 fnvlfqmdqp ltsdvgvdlt lggnlryenn eevgaegskf vvpgltdfnn tqgdrqtgvy
      601 dfsekqvnsa fgsaefdyre ylyleitgrn dwsstlpenn nsffypsvss sflftqvldl
      661 pdvlssgtvr asyaevggdt dpyqlaltyg lvgshpsrtg gtvsrgaiqg gqipplglqp
      721 kqketyefgt nlqffqdrlg ldvtwyrens snqilgvpvs ntsgfnsrli nagniqnqgl
      781 eiqlrgtilq ksdyswnasv nftrndnevk elaegvetei lgqsrsghtt iqarpgepyg
      841 qivgpsfert degevifged glpivgeqkp lgnqeedwsl gltntfqwkg vtlqalfdvs
      901 wggdmysftn aqayqtgkhk etlpgreqgy vigdgvqrvt dgdgnvvelv endvpvdped
      961 yygyigsnfa epfvydasyv rlrqlrlsys lpqsavealp gvsstrlslt grnlwliydd
     1021 vpnvdpsasy ttgaahgleh aslpqtrnfg fdvqirf
//
LOCUS       WP_118839626            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118839626
VERSION     WP_118839626.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117696
     Region          27..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfrkllsvla glllllpatv laqdtgtvsg tvvdsttsqt lpgvnvtvqg lnigaatgpn
       61 gqfeisgvpa geqvlqasfv gytqknipvd veagetttvn vrlapqavgl edvvvtalgv
      121 ereeravsss vqqvdgadld atdnanfvns lrgkvsgani rssstmggss nivlrgyssi
      181 sgdnqplivv dgivvsnrsr qsgggtvegn ggfdfgnaas slnpsniksv svlkgpsaaa
      241 lygsrgangv iqittkdgsn lddeigvsfs ssvsmsqaye fmdyqnkygg gapsstfstl
      301 dgdfkkpdgd qyvvqyavde swgprldgrp vrqwyswddv nglkgeatpw eahpdaienf
      361 mdtgavftnn valsqqtesl nyrlgltsrn qgsvmpngsm dryqvnfngs idlsddlrat
      421 tfakysyqdv karsgmgygf eenpfaafnt ftqrqlnygp dsymrdyqra ngqqrgwnya
      481 gvsgaqgpvt qfqytdnpyv nryanfqqdd eqrllgkaev aydivpnltg tatvttdfrt
      541 hrfsdrrsdi stgapgsfse dvieeqetss slrfdysrsl tdqvdltsfv agkvryetye
      601 qnlgstqngl aapnvftlqn svgrpdveet fqesmvysty glvslgyqdi vflegtlrnd
      661 wsstlpadnn sylypsisgn liftgldalq dqdilsfgkv raswarvgqd tdpyrlgvty
      721 pgstpfqgqa lqnvqrsann pdlkperttg iefgadlrff nervnlstty yrdvtkdqil
      781 avdvsgasgi esslinagev snrgleaslt vtpvlqedlq wdvtanfnkn vnkvvdlaeg
      841 ldtynltagg vifgptiqar egkaygamvq pslrrdangd vvfkrngvpr ttsspqvvgn
      901 fqpdwtggls ttvsykgvtl savvdgqvgg dvyslsnkfg tysglvestv adnqretgvi
      961 pegvvvddat pnengnydve gtdfgeavgr ipaasywknw fsagggdqfi ydathaklqe
     1021 laityslpqr wfndfalrra svsltgsnlm flykeapnid psvtlgagnv qgvesaqipp
     1081 qrqytfrvnl sf
//
LOCUS       WP_118839629            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118839629
VERSION     WP_118839629.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113683
     Region          27..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlipsvvf glallllpgl awaqqgtvtg tvteaetgnp lpgatvqive egtgaasdae
       61 gqyriagvpa geqtvrvsfv gyqeqertvn vpaggtvrvn fqlqpqtarl eevvkigyge
      121 rerqeltgsv ssvsaaeied vgsvgspeel lsgtagvnvt stsglagqav svsvrgvssl
      181 ngnsqplyvl dgtpitsast gggfgqgtna lstissqniq sievlkgasa taiygsraan
      241 gvvlietkkg ssrerrtvta syqlggvtst sdfddvllda qqwsdahqea trnffetcdi
      301 aslggalcgp ttpfssyeql eqsiadnnfa qqlglppgin ifpesntyee avlgtpsayp
      361 espetqpwle eaqqtgitqq anlsvsggdd dtqyfisgvf skdesfvvtn qfnrftgrvn
      421 vsqeatdwle igtntsvtrt enfqassdnn vsgvltsagl ippfipirnd dgsfnfsnpw
      481 niaansigea nvndktirnw rvlstsfvea qpletltlra eggidalivd dftrndrrtt
      541 dgapngfgsq ifeeerrysi rgtatydrtf agrhdisava gasfedsrrn rvfseannfp
      601 saqfrnvasg sspattigdv vrkdglasff tratytldgk ytlegsfrrd gssrfsedne
      661 wgnfgsasfa yrigqenfmq qvetisnlkl rgsigwignr niggffpqfg lasagnnyne
      721 vpgvvpaqls npdlkwestr sieagldlgl vndrifltst yfrsrtndli tdrqlpynsg
      781 fasvtqnrge llnegieaql etqnlvgedf qwsttftvsw qrnevqdlpg gepilsgpqr
      841 aiegeelswf mleyagvnpd ngkplwigtd geptsspsgd aesvqggilp nwtggfstta
      901 nykgfdlras ltfedghsiy ndtrsflmgy nnfglhenal drwqepgdqt dvpravfgda
      961 adnstqestr fledggylrl qnvtvgytlp eqftsqfgvr slrvyfqgsn lftlddtsig
     1021 dpegstggat splnrgelff tppqarsftg gvelql
//
LOCUS       WP_118839645             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Salinibacter ruber].
ACCESSION   WP_118839645
VERSION     WP_118839645.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40309
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maltigvpre tepgetrval vpdvadrlla tvddldirve egagqgayht dadydaagcs
       61 vvgrdatfda diiakvapps ddevdrlgeg qvlvgflspl erpetaqala drgvtalame
      121 lvprisraqk ldalsamssi ggyraaigaa erlpaffpll ttaagtvrpa rvlvlgagva
      181 glqaiatakr lgakvfgydi reptreeves lgasfvelev dieadqdesg yaeqvekekq
      241 erqpellqph laeadvvist alipgqpapl lineeavaam dpgsvivdla apnggncalt
      301 etgeeivahn vqilgptnlp aempvhasel yaktvaamie egleadafap dfddeifaes
      361 cltrdgtvqn drvrgllgta eeaka
//
LOCUS       WP_118840048            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118840048
VERSION     WP_118840048.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114414
     Region          29..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrysvlllg vllgalcfsp tssaqdpatv rgvvtdstga plpganvrvq gtqtgvsada
       61 dgayelaavr pgrrtivfsf vgfekvsrtl elsagdtrtl ditlgtgtvg lenvvvtalg
      121 vdreerslgy svervsgsdv aeapepnvmn nlsgkvagln vtggsgglas tprvtirges
      181 slagsnrpli vvngipidnt pntqgsdaqt tqvdfgngls qinaqnisem svlkgpsaaa
      241 lygsraadgv ilietkdgse tdgigatvrt svtasrplrl pdyqneysyg sggefdyvdg
      301 tdapgwnwgv rmdegverpq wqgprneagd lvptevtsap nkvrnffntg tnvstdvavq
      361 gggenssfrv sfsrsdrtgi vpntnldrts tslsasydvt daltvdanan yanttsdnlp
      421 ssgygsesim yyftwgarhv endllkdywq eegtqqahyd rnwtnnpyfq vnentnsldr
      481 drlyggvsar yeftdnlnlr artgldysdq gtkqrkafss itapngwlqe adrtftewns
      541 nlllnytrev gdftfepsvg anfmrqtrrn vqmtaqalsv pdvynignvr ssaqaderde
      601 aqeilgvfas gtvsyqdmlf ldlagrndws stlpldnnsy fypsaslsvi vsdlvevpef
      661 lplsfakvra swaqvgndtd pfrltntytf getwdntptv vseadlanan lqpeitssye
      721 vgtnlrfydg raqldvtyyr sttrdqilnl pfaqstgyds rlvnageirn tgvetrlqlt
      781 piqdwggfgw dvslnwtrnr stvveladgi dtfvlgegpf ggsaqaregg rmgdiygrvf
      841 drvedpnsph tgeiiyedgl pqltndvekv gnynhdwrgg igstfsyenl qlnvlfdvrk
      901 ggllysntha tgieggsles ttrarnetvv gdgvvqnddg tysenteeaa yvtwlrtyyd
      961 rpnvesnsfd atyvklrels lrynftpdwl tragvqnvgv svtgrnlflw tdvphvdpet
     1021 tisggngqip gfevqqipst rsfgmnvqld f
//
LOCUS       WP_118841768             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118841768
VERSION     WP_118841768.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53720
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes gdsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaas aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_118841532            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_118841532
VERSION     WP_118841532.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114252
     Region          29..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrysvlllg vllgalcfsp tssaqdpatv rgvvtdstga plpganvrvq gtqtgvsada
       61 dgayelaavr pgrrtivfsf vgfekvsrtl elsagdtrtl ditlgtgtvg lenvvvtalg
      121 vdreerslgy svervsggdv aeapepnvmn nlsgkvagln vtggsgglas tprvtirges
      181 slagsnrpli vvdgipidnt pntqgsdaqt trvdfgngls qinaqnisem svlkgpsaaa
      241 lygsraadgv ilietkdgse tdgigatvrt svtasrplrl pdyqneysyg nggefayvdg
      301 tnapgwnwgv rmdegverpq wqgprneagd lvptevtsap dkvrnffntg tnvstdvavr
      361 gggenssfra slsrsdrtgi vpntnldrts tslsasydvt daltvdanan yanttsdnlp
      421 ssgygsesim yyftwgarhv endllkdywq eegtqqahyd rnwtnnpyfq vnentnsldr
      481 drlyggvsar yeftdnlnlr artgldysnq gtkqrkafss itapngwlqe adrtftewns
      541 nlllnytrev gdftfepsvg anfmrqtrrn vqltaqalsv pdvynignar snvqaderde
      601 aqeilgvfas gtvsyqdmlf ldltgrndws stlpldnnsy fypsaslsvi vsdlvempef
      661 lplsfakvra swaqvgndtd pfrltntytf gdawgstqtv vseadlanan lqpeitssye
      721 fgtnlrfydg raqldvtyyr sttrdqilsv plaqstgyns rlvnageirn tgvetrlqfs
      781 piqdwggfgw dvslnwtrnr stvveladgi difvlgegpf ggsaqaregg rmgdiygrvf
      841 drvedpnsph tgeiiyadgl pqltddvekv gnynhdwrgg igstfsyenl qlnvlfdvrk
      901 ggllysntha tgieggsleg ttrarnetvv gdgvvqnddg tysenteeaa yvtwlrtyyd
      961 rpnvesnsfd atyvklrels lrynftpdwl tragvqnvgv svtgrnlflw tdvphvdpet
     1021 tisggdgqip gfevqqipst rsfgmnvqld f
//
LOCUS       WP_118850461             408 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neorhizobium sp. SOG26].
ACCESSION   WP_118850461
VERSION     WP_118850461.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium sp. SOG26
  ORGANISM  Neorhizobium sp. SOG26
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Neorhizobium sp. SOG26"
                     /db_xref="taxon:2060726"
     Protein         1..408
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42061
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 makvifvcre gadeprvsas petvkrfigl gfsvvveaga gdasglpdrd yqaagatigt
       61 aadadgadii lrvnrpdpae fssyrsgaiv favmdpygse aalaamakag lttfamelmp
      121 ritraqsmdv lssqanlagy ravidashey grafpmmmta agtvpaakvf vmgagvaglq
      181 aiatarrlga vvsatdvrpa akeqvaslga kfiaveddef kaaetaagya kpmseayqak
      241 qaalvaehia kqdivittal ipgrpaprlv tramlasmrp gsvavdlave rggniegsek
      301 gkittiegvc vigyanvagr iaasasalya rnlyafletm vdkstkdfal nledelvkat
      361 mlthggsvvh ptfaaaaasg dtiekpvvte ttavdpiagd aavdreel
//
LOCUS       WP_118846942             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            lactamica].
ACCESSION   WP_118846942
VERSION     WP_118846942.1
KEYWORDS    RefSeq.
SOURCE      Neisseria lactamica
  ORGANISM  Neisseria lactamica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria lactamica"
                     /db_xref="taxon:486"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53762
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 atvwacpliy kvnapsegel pllkegqtiv sflwprqnea lvealsakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkddeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118855435             507 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus haemolyticus].
ACCESSION   WP_118855435
VERSION     WP_118855435.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     gene            1..507
                     /gene="nrfA"
     Protein         1..507
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56599
     Region          1..502
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnafkksliv aasfaslslf nsavadmvyk pleqpveapn pnlkieavne kfaekypsqf
       61 nswkatekgd kiiyadeqdp rlivlwggys fakeynaprg hvyavtdvrn ilrtgapkta
      121 ndgpqpmacw tckgpdvprl iaewgekdyf ntkwakggpe ivnsigcadc hdttskdfae
      181 gkpalriarp hvlraldale kataekdkae grphnnlsfn taartekrae icanchveyy
      241 fagdikqvtf pwnkgqtvdd iekyydeigf sdwthslska pmlkaqhpdf eiwslgmhgk
      301 ngvtcvdchm pkvqgkdgkv ytdhqiqnpf dafdrtcanc hdqskeklrd ivtsrkkevk
      361 dvmgrledql vrahfeakaa wdagatkeem epvlmdirha qwrwdytaas hgghmhapdv
      421 mlrvlgsgid kaadartkla ailtkhgvkt pvevpdista dkawkvmgid iekerkakke
      481 fletvvpqwv keakgngkla edtatkq
//
LOCUS       WP_118861667             508 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus haemolyticus].
ACCESSION   WP_118861667
VERSION     WP_118861667.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     gene            1..508
                     /gene="nrfA"
     Protein         1..508
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56710
     Region          1..501
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnafkksliv aasfaslslf nsavadmvyk pleqpvepvk pdlkiesvne kfaekypnqy
       61 nswrstangn gekiiyadee nprlivlwgg yafakeynap rghfyavtdv rnilrtgapk
      121 tandgpqpma cwtckgpdvp rliaewgekd yfnakwakgg peivnsigca dchdttskdf
      181 aegkpalria rphvlraldh lnnavqakak aegkttpnls fntaertekr aeicanchve
      241 yyfagdikqv tfpwdngqtv ddiekyyddi gfsdwthsls kapmlkaqhp dfeiwslgmh
      301 gkngvtcvdc hmpkvqgkdg kvytdhqiqn pfdafdrtca nchdqskekl rdivtsrkke
      361 vkdvmgrlee qvvkahfeak aawdagatke emeaalmdir haqwrwdyaa ashgghmhap
      421 evmlrvlgsg ldkaadartk laailtkhgv ktpvqipdis tadkawkvmg idiekerkak
      481 eeflktvvpq weqqakekgl lvdppaqk
//
LOCUS       WP_118859522             508 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus haemolyticus].
ACCESSION   WP_118859522
VERSION     WP_118859522.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     gene            1..508
                     /gene="nrfA"
     Protein         1..508
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56674
     Region          1..501
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnafkksliv aasfaslslf nsavadmvyk pleqpvepvk pdlkiesvne kfaekypnqy
       61 nswrstangn gekiiyadee nprlivlwgg yafakeynap rghvyavtdv rnilrtgapk
      121 tandgpqpma cwtckgpdvp rliaewgekd yfnakwakgg peivnsigca dchdtiskdf
      181 aegkpalria rphvlraldh lnnavqakak aegkttpnls fntaertekr aeicanchve
      241 yyfagdikqv tfpwdngqtv ddiekyyddi gfsdwthsls kapmlkaqhp dfeiwslgmh
      301 gkngvtcvdc hmpkvqgkdg kvytdhqiqn pfdafdrtca nchdqskekl rdivtsrkke
      361 vkdvmgrlee qvvkahfeak aawdagatke emeaalmdir haqwrwdyaa ashgghmhap
      421 evmlrvlgsg ldkaadartk laailtkhgv ktpvqipdis tadkawkvmg idiekerkak
      481 eeflktvvpq weqqakekgl lvdppaqk
//
LOCUS       WP_118866057            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            denticola].
ACCESSION   WP_118866057
VERSION     WP_118866057.1
KEYWORDS    RefSeq.
SOURCE      Prevotella denticola
  ORGANISM  Prevotella denticola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Prevotella denticola"
                     /db_xref="taxon:28129"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117112
     Region          78..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnkknglyl tafllclnls teahgvasdk tdamressmt alrqrdgnav sipstqvpqk
       61 pqnagekkkv vgvvkeenge pvigatvrlk gtqggavtdi dgrftlmaee gseleisyig
      121 yttktvrvgk adnydislsm gsakelnevv vtalgikreq kalsynvqqv nsdalgtnkd
      181 anfinslsgk vagvninass sgaggaskvv mrgtrsieqs snvlyvidgv pmfnlggsgd
      241 aifgsngtte aiadinpedi esmsvltgaa aaalygnras ngaivittkk gkvghteftv
      301 sqstefstaf rlpefqnryg tgsslrdagg nsyswgclln danymgydpk kdylktgimt
      361 teaftvstgs eknqsyfsas alnsggiipn nrynrynftf rntssmlgdr llldvgasyi
      421 iqndrnmtnq gvyanplvsa ylyprgndyn dmamfehfdt trniytqnwd nllsefvgqn
      481 pywinyrnlr tnkkyrymmn agltykvtdw lnvvgririd natntfekky yastnttiag
      541 angqyakvkt ddkqvygdvm lnvnkhflqn klslvanvga slsdikqdqt gldgpiadnl
      601 ipnvfneyqv daarekrlpa gyheqtksll gslelgwksq lyltvtgrnd wpsmlagphs
      661 nkhsffypsv ggswivsesv klpqaidylk vrgsfasvgi pflrnianpk yewdnttkqw
      721 ksqmvypiyd lkpettnswe iglqarflkh fnldatlywt ktfnqtfnpd isvssgysal
      781 yiqtgnvsnn gielalsysn nwagfgwssn ytlssnrnri nelvrnyvhp etgavinkdr
      841 ldvgglgnah filkeggtlg dlysltdvkr ddkgriyvdk ngkvyrnnnv gdvklgsvfp
      901 kanmawrndf sykgfnlsvm vsarfggivy satqaaldly gvseasakar drgyvevngn
      961 drlnpeswys tiggsdgipq fytysatnvr lqeaslsytf kknhffglgd ltlsvtgrnl
     1021 lmfyckapfd pettattgny yqgidkfmtp strnigfnik lkf
//
LOCUS       WP_118866545            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            denticola].
ACCESSION   WP_118866545
VERSION     WP_118866545.1
KEYWORDS    RefSeq.
SOURCE      Prevotella denticola
  ORGANISM  Prevotella denticola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Prevotella denticola"
                     /db_xref="taxon:28129"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112702
     Region          59..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkgkilpvs vflsccclna fasshaglsg nfgknviaaa vkanaskiqg tqqsdgdvkv
       61 tgtivdntge pvigatvrvk dtqngtttdl dgkfaltahk gatlvisyig mnteevkvtg
      121 napltvtlka eahqieevvv talgikrsek alsynvqkvg geslttvknp nfmnslsgkv
      181 agvninassa gmggaarvvm rgpksitrsn qalyvidgvp vnntsqgeis ggafssqpgs
      241 egiadinped iesisvlsgp aaaalygsaa aqgvimittk kgkegkvsvt vsnstqfanp
      301 fvmpefqnsy inragevksw gaktpsaygn ydpkdffntg tnvqnnvslt agtdknqtyi
      361 slgttnargi ipnnkydryn fafrntttfl ndrmtldfsf nyikehdtnl taqgqyfnpl
      421 tavylfprge sfdairtfei ydesrginvq nwnfgdalsm qnpywvakrm vrsnnrsrym
      481 vsaslkykif dwmdvvgrlr wddantkqed kryasttnlf ahskygfygy dkvndrslyg
      541 dlmfninktl ddfsvsanlg gsfsrikynv tgfqgglkap snlftpnaid ygtatadnrp
      601 iytdnahkin slfanvelgw rsmlfmtltg rndwdsaldg tdnvsffyps vgmsavisqm
      661 aklpswisym kvrgswasvg saispnitsp wryvynpasg tystvtykfp knfrpertns
      721 weaglttrff nnaltldvtl yqsntknqtf lrpitggqgf tseyvqtgnv rnrgielslg
      781 ynhtwgdfaw sssftysanr nkivellndp nevinqggln ganiilkkgg tmgdvymtsd
      841 fkrdaegnia vkdgnvsqvn lpnpsyrgsv lpkgnigfsn dfswkgfnlg fvvtarfggi
      901 vmsqtqalmd aygvskasae ardkggvavn kglvsaekyy svvggdnpiw seyiysatna
      961 rlqeahlsyt fprrmlsgme ltlgltannl fiiynkapfd peatastgty yqgfdylmqp
     1021 slrtlgfnvk lkf
//
LOCUS       WP_118866489             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            denticola].
ACCESSION   WP_118866489
VERSION     WP_118866489.1
KEYWORDS    RefSeq.
SOURCE      Prevotella denticola
  ORGANISM  Prevotella denticola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Prevotella denticola"
                     /db_xref="taxon:28129"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110913
     Region          24..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklriwmltl flfiglsplw aqtisvkgnv vdengealpg vsiipksapk sgtvsdidgr
       61 ftvsvrsgek ltfsfvgyks ieqvaasqmd irmepsdqmm ndvvvvgyme rkvantsasv
      121 vkvsakdlam kpvanpldav qgkvsglqvf sssgepsarl smalhgqgsl gagtgllvim
      181 dgmqvsmavl qamnpndies vqflkdaaat siygaraang vmyvttkhgk tetrpsinir
      241 aqyavsslan sdyfdqlmsg pellryyqet giytadeiat fkdkyfketd fkwykyvyqp
      301 apmytadvsv aggtsavryy lsggglsqdg lrmgssykkv fgrinldakl ndwiranvnt
      361 qvsyddtrvs pfgnnnavgg glaamnapfa spydpdtgke lervplldia tpshvistnp
      421 aktnafilsa ngnltitpvr nltlrslvgl eldygnsrsr tlpsyyrayg ngssergytm
      481 asnvtvtnta aynmafgdhh lttllgqeyt nykddgfsag gsgilddrly llnnvtknks
      541 vgeetngyaf lsfftqlsyd fseryfvdlv lrndassrfg knkrnglfws lgllwkakke
      601 nflknvewid eldlkasygt qgnssippys taayagkvgq kkgdmslgfv slgnpdlgwe
      661 hqskftvgvk trlfnrldvn ieyynrvtsd mlfevpqpys sglpvgsagy ptryenagry
      721 lnhgidfqmn vdllrgrdwg isanmnfnyn rdkvlelfeg rqtwqepggq layivgkpvt
      781 fvvplykgvn pdtgvpewyr pgkdkyqthr ddkdvvsews ssldqntgvn aytpftggwg
      841 isaywkgfyl tadfflalgk hmlsvdkqyy endyfvrdkk dnsngsrrlf dywkkpgdrt
      901 efpslewvrd pahqstyvdt kmlenasfmr lknftlgyel prkmlghqnv vrsakvfftg
      961 rnlltftkfr gidpevnrnv sygvnpntkq msigveigl
//
LOCUS       WP_118867100            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            denticola].
ACCESSION   WP_118867100
VERSION     WP_118867100.1
KEYWORDS    RefSeq.
SOURCE      Prevotella denticola
  ORGANISM  Prevotella denticola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Prevotella denticola"
                     /db_xref="taxon:28129"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122400
     Region          24..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrftlfll glvlsigtaf gqakingtvv sqedgeavvg asvmvqgttt gtvtdidgkf
       61 slnvpagkkl vvsyigmttq tltardgmkv vlandnhqlt evvvtgmtqq dkrlfsgaat
      121 kidaskakid gmadvsrsle graagvsvqn vsgtfgtapk irvrgatsif gsskplwvvd
      181 gvimedianv dasslssgda ktlissaiag lnaddiesfq ilkdgsatsi ygaramagvi
      241 vvttkkgkag qshlsytgey tlrlkpsyrn fnimnsqdqm evyrelekkg ylnyaeiana
      301 stsgvyghmy qllseydatk gqfglentqd ardaylraae yrntdwfdql fsssimhnhs
      361 vsasggtdkg qyyaslsamy dpgwykasrv qrytgnlntt yniskqvgln lianasyrkq
      421 rapgsltrtv dpasgtvsra fdinpysysl ntsrtldpnv fytrnyapfn ifnelennym
      481 dlnvhdfriq asvdykpisk vkltalvavk saastmehiv rensnqalay ramgtttird
      541 anpylytdpd npfalpesvl peggildrtg nhffgwdsrf sasyndvfnd thivnlyagm
      601 etnsvdrkqt fdrewgmmfd ageiaklnyr afkmfqeegt dyyslanthi rslayfgtgt
      661 ysykgryqvt gtfryegtny lgkatsarwl ptynvsgawn aheegwfadv fkkalthatl
      721 rlsysltgdr ppvtnslpif tavvpwrpft tvqetgydeq fgnknltyek khefnlgfdf
      781 gfldnrinlt adfywrrnkd ligyvnhpnl gsynlanvaa mksngvevsl ntqnirskdf
      841 swetnfifsw thneitslft harvidlvqg tgyslvgypv nsifsipfag lnsdglptfw
      901 dadgnrttsg iylqerdqdk igflkyegpa dptttgsfgn vfryknwdln vfitysfgnk
      961 vrlnpvfsnr yddmdalpke frnrwaysgn eattdipaia trrqnrndsq lnvaynsyny
     1021 sdariakgdf irmkeislgy tfpaslispi ginslalklq atnlflfyad kklngqdpef
     1081 fntggvaapv pkqftltlrl gl
//
LOCUS       WP_118867240            1108 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            denticola].
ACCESSION   WP_118867240
VERSION     WP_118867240.1
KEYWORDS    RefSeq.
SOURCE      Prevotella denticola
  ORGANISM  Prevotella denticola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Prevotella denticola"
                     /db_xref="taxon:28129"
     Protein         1..1108
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122662
     Region          50..1107
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkifketkqk hlyfsaafaf slalapagay agsnaraaav qavqqngnhk vtgrvvdstg
       61 epligatvlv egttngtvtd idgnftintp snaklvfsyi gyvgqsvavn gkntidvtlk
      121 eessllkevv vtamgiqrke esltyatqkv ksedlmkvqd pnvanslegk vsgltitpsa
      181 ggaggstkiv lrgaksilgs ssplivvdgv pmtndargkr dmagegftya gmsegsdpls
      241 linpddiesi nvlkganaaa lygsvaangv vmittkrgre gkldinvtsn itfdsplltp
      301 kiqntygatm ngntiqadgw gpkigsladn qltmssplns tnfqsgamhd ihlrnhaqdd
      361 vkdffrtgvt tnnslslsgg tekmttyfsm anshstgllr nnnynrntfs lrqsyrffnr
      421 lkvdlslnya qtitrnrpgg gtvgnplyhl yltprnvdmd yyrnnyvtqd gkwlsgpqny
      481 yelsggnysy ttdqaklqgp rqnwafmnaa nnnpywlinm nqskqkedri wgtisgnvdi
      541 ydglsfqari nydhtrykst skryattflp asmedygrfw dsdsktteiy idyllnynkt
      601 fgdfdlsata gwvghtikge ykgtdviaty ydrtlqklpt kvnyfdtsag gmgatsssks
      661 snwdrawlat aqmgwkdmvf vdasyrrdwy rpfryfklsg isntdnygyf giganailsk
      721 llklpepvny lkyrasysev gnsipniayn avstnlqtga ingsnyaqfv dprpektrsf
      781 etgveslwfn nrlsfdltyy natmshlymt aatgtgltkn mnsakvrnqg iemtlgydfk
      841 pvswlrwrts fnlsynknki lktaydeqgk erlieqkvgg vhvkymeggs igdmyvpdfd
      901 rdenghikln slgqpqfdks gklkyignmn anwqmgwsnt ftwkdlslsf lingriggkv
      961 islteqqldy ygysqrsada rleaeknniv akdygnvpgm mlpdgsgriv pvqsyyqaig
     1021 sadspadyvy natnfrmrel slgytfrnlf gmnrnlalsf iarnlffiyk daptdpdvsl
     1081 sttnglgafe lfntpstrsy gfslkmnf
//
LOCUS       WP_118867261            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            denticola].
ACCESSION   WP_118867261
VERSION     WP_118867261.1
KEYWORDS    RefSeq.
SOURCE      Prevotella denticola
  ORGANISM  Prevotella denticola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Prevotella denticola"
                     /db_xref="taxon:28129"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123366
     Region          24..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrfalflf glvlsigtaf gqtkingtvf sqddgepiig asvmvqgtta gtvtdidgkf
       61 tldvpagkki vvsyigmvtq tlaakdgmrv glandnhqlt evvvtgmtqq dkrlfsgaat
      121 kidaskakld gmadvsrsle graagvsvqn vsgtfgtapk irvrgatsiy gsskplwvvd
      181 gvimedvtev dadnlssgda atlissaiag lnaddiesfq ilkdgsatsi ygaramggvi
      241 vvttkkgkag snrisytgey tmrlrpsysq fnimnsqeqm giykemaadg lfsfsrtlra
      301 stsgvygkmy nllntydttn grfgiahndd ainaylreae mrntnwfkel fsnsismnhs
      361 ismssgtdka qyytsfsfmd dpgwaeqskv rrltysinan yniskkvtln ligntayrkq
      421 rapgsvnqdv dvvsgavnrn fdinpysyai nssraldpnt fyvrnyapfn ihhelannfi
      481 dfdvldlkvq aelkykpvsk vqlsvlgayk ysitsqatqi regsnmamay ramddatirn
      541 anpwlyldpd qpnslkfsvl pkggfydetk yrmnswdfra tasyndvfne rhivnfyggm
      601 einntvrtqs yfegvgmqyg mgylpnydyh yfkhaiednn lyydlynsyn rdvsffgtan
      661 yswkgryaan fttryegsnr lgkartarwl ptwnisgvwn aheepwfqkt fknamthatl
      721 rasysltgdk pavtnsqvii rssniwrpfa vdketglyis rfanpdltye kkhefnigmd
      781 lgflnnrlnv vfdwytrnny dligprttng tkgtiteyan vasmkshgee lsissknilt
      841 kdfqwttdfi fshvktrvtd ldsrsrimsm vsgsgftmvg ypyralfswe fkglnkhgip
      901 qvinqdgelt tsgvdfqsyd ldhlkyegpt dptvtgsfgn tfsykgwhls ifttyafgnk
      961 vrldpffsts ysdmsampke frnrwtktgd eahttipaia dlrsiqqdgy lhraynayny
     1021 steriakgdf irmkeislay dfpaqlirhi alssmslklq atnlfliysd kklngqdpef
     1081 fnsggvalpv prqftltlrl gi
//
LOCUS       WP_118867419            1161 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            denticola].
ACCESSION   WP_118867419
VERSION     WP_118867419.1
KEYWORDS    RefSeq.
SOURCE      Prevotella denticola
  ORGANISM  Prevotella denticola
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Prevotella denticola"
                     /db_xref="taxon:28129"
     Protein         1..1161
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129309
     Region          124..1160
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrhhqqvfst arrlpsfvfl avfillvswa spasaqvagk kfsisfkdkg vaqildfist
       61 kgdyqirysd dvkndslllt isfedvdelg avesllshts ftynvdgkvi dvfkmknatq
      121 gkytvhgtvk dkdglgvpfa ivqikgtsrg vtadvdgnfs mpvdqeegti sissvgyeak
      181 tlkyhagkpl nvtlpssaya mgevtvvayg krntreqvga vasvkvedlq kaptasienl
      241 lqgrmagvdv tnlsgspggg gsritirgfs slnqqgvndg tplyvidgip vsgsateatg
      301 ginplagldp ssiesvqvlk daasaslygs ragngvilit tkkgksgrte vsfnvsqsls
      361 wlpstpmqtm gkgerdiall laksqrgahy dyltdklvyp hsykdsygwd adndgaydyl
      421 wrngkvldpd rrlpgiaqds lntfynnrtn wwkyafrvgk ltkadmqlag gtdnirymvn
      481 agiydetgim issnfrrysl lsnldfnlst klsaftrinl tyatqkagsd ggrvqgltfd
      541 pkrtstllpg kgstaeqial rqlrdidktn snynvrlsvg lnynilkglk fsstysldhy
      601 ftrvytftpd ylkydlksev qasnitmtni qteniltynl alphehklel magmtynydl
      661 lqnlngtakg gptnsikyag egwpsllndg gtpraaqsfr tdqqeqalvs flgraaysyk
      721 krymaelsir sdgssvfgkd vrwgtfpsvg lgwafseepf mkrlwwlsfg klraswgksg
      781 qkfqepylal gvmeesnvyn gslglipqsm ankkltwees dqydlgldlq lldyrlkfkl
      841 dyyykysskl lmqsylpgnv flannmwdna saisnegief eaqydiirkk nwnwsvglnl
      901 shnknmlrkt yngedlndkv lgrpvygiyt fkdegivqke edipmyrnas gklmplyfqs
      961 innplrvggr kikdqnydgv iddkdlyyag stlpavyggl nshlewkgls ldvlfsytig
     1021 rkvmnmykns aftftkdfgv imnyfhasdf wtpenrdaky pslefadkdy vgqfdgnvds
     1081 nienisflrl kqlvigyqlp knwlkgsfik daniyfsgen lflitnysgv dpevinpytg
     1141 kddgtqypln rkvtlglnlk f
//
LOCUS       WP_118868051             508 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus haemolyticus].
ACCESSION   WP_118868051
VERSION     WP_118868051.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     gene            1..508
                     /gene="nrfA"
     Protein         1..508
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56825
     Region          37..501
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnvfkksliv aasfsslslf nsavadmvyk pleqpvepvk pdlkiesvne kfaekypnqy
       61 nswrstangk gekiiyadee nprlivlwgg yafakeynap rghfyavtdv rsilrtgapk
      121 tandgpqpma cwtckgpdvp rliaewgekd yfnakwakgg peivnsigca dchdttskdf
      181 aegkpalria rphvlralda lekataekdk aegrphnnls fntaartekr aeicanchve
      241 yyfagdikqv tfpwnkgqtv ddiekyydei gfsdwthsls kapmlkaqhp dfeiwslgmh
      301 gkngvtcvdc hmpkvqgkdg kvytdhqiqn pfdafdrtcv nchdqskekl rdivtsrkke
      361 vkdvmgrlee qvvkahfeak aawdagatke emeaalmdir haqwrwdyaa ashgghmhap
      421 evmlrvlgsg ldkaadartk laailtkhgv ktpvqipdis tadkawkvmg idiekerkak
      481 eeflktvvpq weqqakekgl lvdppaqk
//
LOCUS       WP_118868342             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118868342
VERSION     WP_118868342.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53692
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl ssetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaas aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_118878504             508 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Haemophilus haemolyticus].
ACCESSION   WP_118878504
VERSION     WP_118878504.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus haemolyticus
  ORGANISM  Haemophilus haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Haemophilus haemolyticus"
                     /db_xref="taxon:726"
     gene            1..508
                     /gene="nrfA"
     Protein         1..508
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56796
     Region          1..501
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnafkksliv aasfaslslf nsavadmvyk pleqpvepvk pdlkiesvne kfaekypnqy
       61 nswrstangk gekiiyadee nprlivlwgg yafakeynap rghfyavtdv rnilrtgapk
      121 tsndgpqpma cwtckgpdvp rliaewgekd yfnakwakgg peivnsigca dchdttskdf
      181 aegkpalria rphvlralda lekataekdk aegrphnnls fntaartekr aeicanchve
      241 yyfagdikqv tfpwnkgqtv ddiekyydei gfsdwthsls kapmlkaqhp dfeiwslgmh
      301 gkngvtcvdc hmpkvqgkdg kvytdhqiqn pfdafdrtca nchdqskekl rdivtsrkke
      361 vkdvmgrlee qvvkahfeak aawdagatke emeaalmdir haqwrwdyaa ashgghmhap
      421 evmlrvlgsg ldkaadartk laailtkhgv ktpvqipdis tadkawkvmg idiekerkak
      481 eeflktvvpq weqqakekgl lvdppaqk
//
LOCUS       WP_118911558             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118911558
VERSION     WP_118911558.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53701
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 tavwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakdv diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_118913941             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium shigaense].
ACCESSION   WP_118913941
VERSION     WP_118913941.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium shigaense
  ORGANISM  Mycobacterium shigaense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            simiae complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Mycobacterium shigaense"
                     /db_xref="taxon:722731"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37521
     Region          9..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtepqanair vgvvaesgtd errvalvpka vaslvnsgva vvvesgager allpdelytq
       61 agatigdaws advvvkvapp tadevgklhs gqtligflap rnaenaigal tqagvqafal
      121 eaiprisraq amdalssqgn vsgykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwldig idaageggya relteseraq
      241 qqqalekais gfdvvittal vpgrpaprlv taaavqamkp gsvvvdlage tggnceltep
      301 grtvvkhdvt iasplnlpat mpehaselys knitalldll itdgklapdf ddevvaescv
      361 trgkds
//
LOCUS       WP_118890979             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118890979
VERSION     WP_118890979.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53835
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvksgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_118924812             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides immobilis].
ACCESSION   WP_118924812
VERSION     WP_118924812.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides immobilis
  ORGANISM  Nocardioides immobilis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nocardioides immobilis"
                     /db_xref="taxon:2049295"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52849
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipresk tgetlvaata ktanqlqglg ydvvvesgag ahadqadeaf aeagvtvgsa
       61 ddvwaadvvv kvnaptadei grlragatii smmaparspe lveqlvaqgv talamdavpr
      121 israqsmdvl ssmanvagyr avveaahefg rmftgqvtaa gkmpparvfv vgagvaglaa
      181 vgaasamgai vrvfdvrpev aeqveslggq fvevdfesev stdgyaremt aeqeaatagm
      241 ydeearnadi vittalipgr papklihedt vagmkpgavi vdmaaanggn cagteadqrv
      301 vtehgvtilg ytdlagrlpa qtsqlygtni vnlmklltpe kdgmltldmd dvvqrgitvv
      361 rdgesmwppp avqvsatpkv vdthpagmke ekakltargr mtivgiaalv lfglisispp
      421 plqerltvfa laivigyyvi gnvhhalhtp lmsvtnaisg iivvgallql geestpimli
      481 afvatllasi nvfggfavtr rmlglftrs
//
LOCUS       WP_118928391             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides immobilis].
ACCESSION   WP_118928391
VERSION     WP_118928391.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides immobilis
  ORGANISM  Nocardioides immobilis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Nocardioides immobilis"
                     /db_xref="taxon:2049295"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52082
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvlkear pgesrvsatp atvaqllklg ydvvvepgag aassfpdevy aeagarvgsi
       61 aeadivfgvn apapaqldal kpgttlvail narldeelva dlgkrpital amdavprisr
      121 aqsldvlssm aniagyravv eaanvfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agamgaivra tdprpevadq vkslageyls iespevevsa tgyakemged yqaleaklya
      241 eqaadvdiii ttalipgrpa priitaemva smkpgsvivd maaanggnve gtvkdqavvt
      301 angvtiigyt dlagrlaaqa sqlygtnlvn lmklmtpekd gelvldfddv vqrsitvvrd
      361 gestwppppv qvsaapvapa vpveqeeska kahmssgrrm givfsaaaal faliaispaa
      421 lqvhltvfal aivigyyvig hvhhalhtpl msvtnaisgi ivvgallqig qndtavtava
      481 gaaillasin vfggfavtrr mlsmfsrs
//
LOCUS       WP_118932201             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter xylosoxidans].
ACCESSION   WP_118932201
VERSION     WP_118932201.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter xylosoxidans
  ORGANISM  Achromobacter xylosoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter xylosoxidans"
                     /db_xref="taxon:85698"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38455
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkyvggk htvivergag taaryldeay eaagatlgta
       61 qdalgaelvm kvrapsaael pqmksgavvv gmldpfdaeg iqqiaaaglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgtggy arpmppawma
      241 rqaalvserc kqadivvtta lipgrpaptl vsaetvaamk pgsvlvdlav erggncplse
      301 kglvvekhgv tiigltnlpg lvatdasaly arniqdflkl iinadgalai qrddeivaac
      361 lvceggnvar rn
//
LOCUS       WP_118928853             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides immobilis].
ACCESSION   WP_118928853
VERSION     WP_118928853.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides immobilis
  ORGANISM  Nocardioides immobilis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nocardioides immobilis"
                     /db_xref="taxon:2049295"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52834
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresk pgetlvaata ktvsqlvglg yevvvetgag eaadqaddaf kgagarigtc
       61 edaweadvvv kvnaptddei erlhkgatvi ammaparspe lveklqaqgv talamdavpr
      121 israqsldvl ssmanvagyr avvesahefg rmftgqvtaa gkipparvfv vgagvaglaa
      181 igaasamgai vrafdvrpev aeqvesmgaa faqvefeaev sadgyakemt aeqeaataam
      241 ydeearqadi vittalipgk papkliraet ianmrpgsvi vdmaaanggn cegtvtgert
      301 vtdngvtilg ytdlpgrlpa qtsqlygtnv vnllrlltpe kdgqltldmd dvvqrgltav
      361 kdgesmwppp pvqvsaqpqv aqkaapepea pkpppdprrk yaaaglaagl falaaaysps
      421 eflnhftvfv lavfvgyyvi snvahalhtp lmsetnaisg iilvggilqv gsanavttal
      481 aavavliasi nifggflvtl rmlemfrkd
//
LOCUS       WP_118935575             689 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118935575
VERSION     WP_118935575.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 689)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..689
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <11..687
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 adfvifnecp yisfgytdnk gviekseqek ytgrinadqq ikswlkvgtn ttftrtentl
       61 vddgvmnrar canpmleisd eietlnwqgi fdqnnfnplr slkvdndlvy nrllssnyin
      121 inpieglnlr stfsidyaqk qqnkytpndi yeserygtqg eakddrdtrt vwqwdnslsy
      181 evsfgkhkln amvgtsatrt tynyinatat gfgtnlfgyh slgsgykkdq rglstawseq
      241 tllsyiarvn ynyagkyllt atarydgssk fakgnqwgif psvsaawnit eekfmknqti
      301 fdqlklragf givgnqnidd faylslynvs ytgtsdtgyt nsfvsngrrg tpdiswekqk
      361 qwnlgvdmaf lqnrvrlsvd afliknkdll mshslptttg fsstieniga ienkglefal
      421 nanlvrakdf ewnfaatlsm dknkvtrlyg dndvvynvds drniqkegnl flgesrntiy
      481 iwktggiaqe idmdrlnkin wngynvnpgd lypldydnng qidqndrvvi gstdpkfygg
      541 fstdfswkgl slnavfsysy gakklspwye tligstgsgv astdlldrwt pentdaefpr
      601 vlagfdynhy gassmdfsvq kasflrlsal tlaytfptkv inalkltnlr vyatgsnlfc
      661 ltnyngydpe tgdwypptrm ytfglnlaf
//
LOCUS       WP_118939449             612 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides uniformis].
ACCESSION   WP_118939449
VERSION     WP_118939449.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides uniformis
  ORGANISM  Bacteroides uniformis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Bacteroides uniformis"
                     /db_xref="taxon:820"
     Protein         <1..612
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <17..611
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 ertfrrkkda eelscgfevd lqlwdnlkyh fnysadmgfw gnegatksky ylsannkath
       61 tsassfkaqn vtwqientlt ydktigkhtf gvvlgqsalk ykgdqlggnr wnlvnpnkps
      121 idyatgnvey tkdengnitg atvqygvygg pytehrmssm farlsynyne rymiqatirr
      181 dgssrfginn kygtfpsvsv gwnvtneefm adtrewlsnl kvraswgkng ndniaefgyt
      241 sltamgnnvl lgkdaikwng skaqrlanpd lkweeseqtd lgidlgffnn altfsadyyi
      301 kktngmiitm pipsyvgetk plgnvgdmen sgfefelgyk wniadakfav kgnatylkne
      361 lknlgndtgy mdldgiqgfs gggtrgsngq pfpyfygykt dgvfqnmdev rayvnkdgkm
      421 impdavpgdt rfvdvngdgs isaddrtnig ngtpdwtygl nlnadwkgfd fniffqgvag
      481 advfdgtyrt dvasgnypsw mlgrwtgegt snkyprlavg natnwmvsdl yvcdgsylrl
      541 knitlgytlp ktltrkltie rlrvyvqaen lvtwtkywgf dpeissgats lgvdrgiypq
      601 artytvgvnv sf
//
LOCUS       WP_118935695             924 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118935695
VERSION     WP_118935695.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..924
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          1..923
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 kksdvtgama rvdseelntr pvnnafealq gkaagvdits serpgtvgsi rirgnrsisa
       61 ssdplyvvdg vplsaggiet inprdiesid ilkdasstai ygsrgangvi littkrgkag
      121 rlalnysgsv tletlkdksp amsasdyitw rrwayynsdp vnnprgdqpn ydkdqiyfaa
      181 sgdpaalanv nkgwnngtwd gsrvtdtdwa divtqtgith ehtisgsggn etaqaffsig
      241 ylnnqgtqkg qeyerynfsm svdlqvkpwf kmggsingsw avqdygysrt gqssgsgpvd
      301 iysaakaipr fgvpydeegn iitnpcgstt nvytvidewn kstdnrqtfl algsfygqfd
      361 fgkiwapleg lsykisfgpd frhyrqgifi skdsavkmgs knyakyatdr ylswtldnqi
      421 nynktfgkhn lgvtllqsas kynkesgses anaipnenfe wynmgsvdit daatygagms
      481 tgmsenqlas ymarinyayn drylltvsgr ydgssvladg hkwsffpsaa lgwridqedf
      541 mkdiswinql klrfglgttg nsavsaystl gniqsfyvpf gstltpayat nepyytssqv
      601 kmankdlgwe kttqynygvd fsflngrisg smdiyhsntn dlllsmtipt ltgfnstyan
      661 vgktknfgvd lslnlvpiqt kdfewsstin aayqkdeive langkqddis nawfigesin
      721 vfygtasdgl wqesdaaema kfnanghkfe agmvkpvdqd gnyiidsndr iilgnknpkw
      781 vlgwsntfny kglelgieln grfgymvdtg gegqygmynq reisywtpdn tgadyqkpiy
      841 staggdayss llgfkdasfi kirnislgyn fnskalknig isslklyaqa knignlyssv
      901 dfmdldlgtt yynrgftfgl qvgf
//
LOCUS       WP_118935765            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_118935765
VERSION     WP_118935765.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         <1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          2..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 dfslsnvkkg diivisfvgy qtqevkwtgq pidvtlkddt qqlgevvvta lglkreekal
       61 gyavtevkgd elkaantisp vaalqgkvag veisgsdggl fggtkiqirg astlssnnqp
      121 iyvvdgvild ngvsgnttad wdagannasd ygnelknlnp ddfetvsvlk gaaatalygs
      181 rglngavvit tksgkgtqgl gisvsqtfgi dhafktpdiq tlygpgympg qsdadqngsm
      241 wdehqftvnq ngehtlvgvp nfgfgprydg sqirnydgtw ttysprknnm ldlyklgfnt
      301 ntnvsirggn ektsfytsls yknakstten ntferysmll kashklndwv dvaasfsfan
      361 skprnaqlna gelfvnantn vinplfdvdy frnkylgehg giastsygdq ygsvpssakn
      421 yffkvdnydy vrketvirpt fevnvkmtdw lkfkadanmn ryytsiedkq lgsgyanegg
      481 yygitqdike qftvggtfta skqikdfslg gfarfeyynt ssqhskvstd ggmvvpgewf
      541 venskktkks estisgskri isaifalnlg wknqfyldvt grndwssalv yanrtgnhsy
      601 fypsvsgswl inetfresmp swinlaklra swaqvgndtd pyavnqtysf atmemydgni
      661 ytneldklmk iadlkperkn sweigldfrt fnnrlnldft yykenttdqi mkinvpaisg
      721 vtqqlvnagn iqnsgieial nttpiktkdw qwdldftytr nrskivslhp nvanyielsg
      781 yvnaydyhig svakvgesyg vlmsdvtqar nengvpllew ddswrgayra qsktaevvgn
      841 mtpdflgsva ttltwkdlsl nvgldmrfgg lvasycnlyg tqagwtessl qyrdpehggm
      901 twtsqyadsk giqytdgmip egvfkegtia tlvdgtkmdv sglsyaqlvq egklepthag
      961 swygnnyswg aqtiddiwvh klsyialrni tinyrlpnsi shklgakgln lsfsarnlgy
     1021 lynslpnnln pesvrsnsas efrirgfepy tasyiftina nf
//
LOCUS       WP_118942126             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Profundibacter amoris].
ACCESSION   WP_118942126
VERSION     WP_118942126.1
KEYWORDS    RefSeq.
SOURCE      Profundibacter amoris
  ORGANISM  Profundibacter amoris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Profundibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Profundibacter amoris"
                     /db_xref="taxon:2171755"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56109
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egearvamtp esalqlqklg ydclieagag kaagftdaay keagvtvvrg
       61 avnlwkesdv itkvrpptkt eerrltkgkt lisfyfpgqn eelmelaaek gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtavslg aivyafdvrp evaeqiesmg aefvyldfed evqdgaatgg yaapsspefr
      241 ekqlekfrel apdmdivitt alipgrdapk lwtrdmvemm kpgsvivdla aerggncdlt
      301 vmdekvvskn gvtiigytdf psrmatqsst lyannirhmm ddltpekdgk ivhdmeddvi
      361 rgatavfkgk vtfpppppkv qaiaaqpkke apkeltveek raqelaefka atrqqvgmla
      421 aggllmllig ayapasfmah fivfalscfi gfqviwnvsh alhtplmavt naisgivilg
      481 allqvgssnw lvvilatvsi liasinivgg flvtrrmlam fqks
//
LOCUS       WP_118944804            1127 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            splanchnicus].
ACCESSION   WP_118944804
VERSION     WP_118944804.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter splanchnicus
  ORGANISM  Odoribacter splanchnicus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1127)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1127)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1127)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1127
                     /organism="Odoribacter splanchnicus"
                     /db_xref="taxon:28118"
     Protein         1..1127
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127185
     Region          124..1124
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkenkilfks frfiqaglli fvigvfgnvq qlhaqtqhys fdfrnktvqe aiamiekqsn
       61 yaflfsekss silnrklntq vkdtaingvl drvfkdlpls ykivgqqill tlktapvipq
      121 apirkiqgtv kdnrgetlpg vsivlkafps lgtttdidgn fvlqvpedne sllvsfvgme
      181 tlevklqegv gqydvilqps ntelsevvav gyfnrkkdsf tgsavtvsge qlrqvnpnnv
      241 fqslqtfdps frilennllg sdpnslpnin vrgtssvptg gngevlrrdn insnvnmptf
      301 ildgyevgve riydldvnri asitllkdaa ataiygsras ngvmvittva pkegqlevty
      361 nlelntsitd lssyhvlnar dkleyerlag lydyngalnq deldelyyqk mynivsgvdt
      421 ywlsqpirst lghkhslyis ggsqamrygi dlhyqgmpgv mkksernryg igvelsynkd
      481 qkllfkntls fdkvkaaesp ygsfseyvrm npyypktdgn gqliqeidsw tdrsgaggsm
      541 ntatvlnplf datlnsfqdk sywevndvfs iewnitealr lralasigqk styqdefvsp
      601 ldneyyfyat qdlkkrgkyt ynreqqsyyd gnatltysns fgrhfvnlal ganlrenkss
      661 gesmvatgft ndrftsigfa nsykensspy stsskerlfg tflsanysfd nrylldlsvr
      721 adgsskfgsd nkvapfwalg igwnlhheka lqavgvlsql rlkantgltg avsftpyman
      781 tlyeyykdnw ystgvgaivd qygnenlkwq rtrnydigld lgflddrffv sgryyykltq
      841 dmltdvtlpp stgfsyyken lgdirnqgye lnlklqavkq tdftvavfgn fthnrnklvk
      901 isnslkklne kadesqlede ykgtpllryn eglsmntiya vrslgidpen gkelfitkeg
      961 qlthdwnvad ivpicdaspd legffggniy ykgfllnfsf ytrfggyeyn qtlvdrvena
     1021 dprynvdrra fkyrwanpgd varfkdiadl gstqvtqrfi ekdnvlelks vylsydfspa
     1081 iakklfmksl rasvtlndlw rtssiaierg idypfarnfi fslqttf
//
LOCUS       WP_118944959            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Odoribacteraceae].
ACCESSION   WP_118944959
VERSION     WP_118944959.1
KEYWORDS    RefSeq.
SOURCE      Odoribacteraceae
  ORGANISM  Odoribacteraceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Odoribacteraceae"
                     /db_xref="taxon:1853231"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121296
     Region          47..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqknacsvgl slrkqrltai ifcllsaftl pvplqagvpq qqstypvkgl vtdakgvplp
       61 gvtvrygitg gvtdnggrfs lrlpeergrl tfscvgyktv tvgyragetl rvrleesres
      121 leevtvvayg eqrrgqvsgs vatvdaarlq nkptsnvltl akgqmagvyi asqsgdpggn
      181 dvsiivrgan dlaiagnrnp lfvidgvias ddaslkvggn pltslnpedi etfsvlkdaa
      241 aaaiygsraa ngvviittkk grynqhplls anvshtfilq pllperiggn aerrarleam
      301 rryagvyydr ktdsyrypeg yalgkpydyf wnegngadmt vyqdslnpfy nnstdlmayy
      361 lrpahatnan iqvrggaegi aysvglgfyd eagtlrgtgn rrfsafsnla fkpahhlygn
      421 frfylaytdn nrsrkgvdaf npaptaystl pdflftstvl pgpgtpyfge ltrryestre
      481 kndsyklrts fdltyeiadg lalksgvavd ylqnnqnvfl pkevneygkt yssgtiarhl
      541 mvlnenllty rrtfgsshtv dlllgfsvqq demnnntgka lgaasntihy apwysqvyda
      601 earldlkdyy sdyekktmvg lfgrlnynyr eryyagftlr rdasstfged vrwgwfpsyf
      661 vgwtfteepf mlalkpwlny gklrfsqgrt grifeypyla qgeldqgapy lghptvvpew
      721 wagvsnsglt wektteydag ldlglldnri gltfdyylkr trgllynppt pgthtgflap
      781 wrnmygidne gvelevkgel vrgrtwqwnl sfnvsrnrnr lakslngrdf qntaarfann
      841 lsviglplyg iyafddrgiy grrsdvpsyy edgvkkylrg egsayyragd riitdvdgng
      901 qiynygtlae driyigsplp qfqggissdl rwkgldvtvl fnfvcrkwvl daargaslgt
      961 ylelnpadma rpyltgsldg lfwehpgdda pypanrmeng lynfatnlas naqrisylkl
     1021 qavtvgytlp eavrkamgfg arifisgenl ftltdyrggd petvdpytgv dnynayplsr
     1081 rftigltlnf
//
LOCUS       WP_118945023            1136 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            splanchnicus].
ACCESSION   WP_118945023
VERSION     WP_118945023.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter splanchnicus
  ORGANISM  Odoribacter splanchnicus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Odoribacter splanchnicus"
                     /db_xref="taxon:28118"
     Protein         1..1136
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127622
     Region          125..1133
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mykdhlphgv sacrflltal cillfagnlr aagdeeymrk kisvqatnes ieqvldkisk
       61 ladirffyny svldfsrkit vnikdtelhd alskvlqgek veigyqpnrt vvlrpqrvpd
      121 gisainisgk iidadtkepl igasvvlkeq kgvgvvtdid gkfhitipeg gasallisyv
      181 gyeneelait gqgdmkdlti kmtaafveme gvvvtgmapr ksesftgsyv svkgeelkkl
      241 spnnllqalq ffdpsfrive nnkkgsdpna mpefqmrgnv qldnnfsnsd mnmlvgnysn
      301 qpnmplfvld gfettlqkiv dldpervasi tilkdasata iygsraangv vvfetkkpls
      361 galnvtysms mgitmpdlss ydmmnaaekl qfeydaglfs ndangnplsg silaeqrnyy
      421 nhykreierg vntywlsepv rtaiihrhtl tvdggdealr ynlnlnygne pgvikesgre
      481 tfgfslnlqy rrkkwnisnq lsidntkgtn spygsfseyv qmnpyytkrd eygnyqkiie
      541 rkslgpgngs ktitnplynt qfehkdytkn fnvtdnfsle fairenlrln aqfsltkgts
      601 ngeifksmnh sefeandvpl lergtynksi gntlnwntna sinynltkdk hllsmfarwe
      661 igqnqsdgif ltakgfpndn msdfqfaqev ekrdvnntes tsrsmgltat vsymydfrys
      721 vdfnvrgdms sqfgadsklk pfwsvgarwn asrekwlegt aisnlvlrts ygitgsqnyd
      781 pyqaiegytf eemmfqylss gvigsklkgf gnpdldwstt edfsaaielg ffndrltasv
      841 nyynhytdql llenniapss gfltmtnnig aisnkgvdvt lgftpiqdfe rqiqwnvsin
      901 gnhnknvvkk lsneikkqne nnlnernspa piyeegksts qlfvvrslgi dpatgneifl
      961 krngertffw dandkvavgd tepkfrggit ssltwkewsl nlgftyqlga yiynqtlvdr
     1021 venvnlaynv drraakdrwr kpgdiakyks isytgratel ssrfvqkvne iqfssisvgy
     1081 hfdpkkftfl kqckiaginl tgsmqdlgrl ssvkqergtd ypfsrtvnls lsvlfn
//
LOCUS       WP_118945050            1142 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Odoribacter
            splanchnicus].
ACCESSION   WP_118945050
VERSION     WP_118945050.1
KEYWORDS    RefSeq.
SOURCE      Odoribacter splanchnicus
  ORGANISM  Odoribacter splanchnicus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Odoribacter.
REFERENCE   1  (residues 1 to 1142)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1142)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1142)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1142
                     /organism="Odoribacter splanchnicus"
                     /db_xref="taxon:28118"
     Protein         1..1142
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128475
     Region          45..112
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          130..1141
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkkqernnl rpgrgisgrt mfstvlllfg ivinlnaqer tkvsfkfqkt tfeqviqeiq
       61 kqtdydfiyn skafpqksfa ieaqnrevks ildelsrdlg leytimnkvi tlrmkntpss
      121 sapqsdqglr iikgkvvdek geplpgvsvv vkntvqgtas dvngnftikp egqekiilqf
      181 smigmqrqev eykgeqelki vmrennetln evmvigygst trkdmtgsis sldtkiiess
      241 aapnlaqmiq gqipglniml gdgspgspsr leirgastls snsgplivvd dvpmspdydi
      301 nminsadiks lnvlkgasat aiygsraagg vimittknns rnkkpviqys fdftnqrlvs
      361 dirtltadef ktllleaarn earasgyedi tqsaeyqrfs tpgffgesnt pwmstlmqda
      421 itmqhrvsiq ggtaetsyna sfsylneegm lkslynkryt ynagfntdis kklkatvnvn
      481 gsftrrnrnp rgmetaiaar pdvkvynedg sfyhqqyqyg grlvttknpl aeitgtrdqe
      541 drnninlsts ldwkpislln fsmrysfqry htdydyyass etyegsdnfs gkfngygkrt
      601 nyltteqeve arasftktfk qkhylnlmva gtynennaen ywfamdnfgd dnvqngiwqg
      661 tepyekrpkd gyslgsvmls figraeykfm nryilnasir rdgsskfspk nrwgnfpava
      721 aawlvseedf fknnlpwfsy fklkggwgkv gngwvteygw rtmfdnsayl grpaiipsqv
      781 gnddlkwedt eawdigfefg lfdnqrikgs fgyysknteg llydltlsps mgagstkvnf
      841 asiinkgvef dlvanlistk dwqwsvsani sknknrvtni daefvsvpgs smltstvike
      901 gsslgliygf qtdgvfrsqk eidyyeslnk dhayqtgttg rktipgdlky vdqnndgyvn
      961 iattakddrv vlgcsrpdfe gglstrlgwk gftlsiqssy ayghqkmwka gaqqfqfnsy
     1021 epgnlldial krwtpenpds nypsmrlnky qnevvgfavy dasywkiqni nldyrvpvsw
     1081 lkhinvfssm tlsfsmnnvy tftsypgpsp esfsanmieg gsidystypq trnfnfsikv
     1141 tl
//
LOCUS       WP_118948808             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_118948808
VERSION     WP_118948808.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53737
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vsllsfvail iaginifggf fvtrrmlnmf rkg
//
LOCUS       WP_118949749            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Taibaiella
            helva].
ACCESSION   WP_118949749
VERSION     WP_118949749.1
KEYWORDS    RefSeq.
SOURCE      Taibaiella helva
  ORGANISM  Taibaiella helva
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Taibaiella.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Taibaiella helva"
                     /db_xref="taxon:2301235"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114454
     Region          24..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlllfil aftvsiqasf aqsqkikgrv tdskgegvpg asvkvkgtev gtvtdidgny
       61 elelpegkkv lvidgiagka qtevkdasap vnvvveqssq dlegveiygk kidkresvss
      121 istvtaeqia srpitnivsa ldgnaagvnv ssgggqpgas pdilvrgfgs lsassspliv
      181 ldgavydgtl ssinpydvat msvlkdasat siygargang vimittkkgk kgdkpiinid
      241 aqvgmftrmi peydrvsard yyklawegly niyseqtdpe taagaadant iplilggynt
      301 fnvpadqvyk ngqinpnasi lyeddwqkav srtglrqkyn vsvnngddks tyyfsvgynn
      361 ekgifkqsdy drittrlnit skitpwlnsg lslgvtydnm rsfaadgsay anpfmttrlm
      421 pslypiylhd pntgalvlda ngqpqydfgd npqygqvrqf atnqnviasi yndntttkaf
      481 sgfgsgylea kflkdftart nisvntyngn qsiyqnkffg dgepfngilt qqnnnnisyt
      541 wtqllmwkpt fgifnpddan hsldvtvghe nyllraessy lqragfggss iesgaaaayg
      601 igssqsvdyh aiesyfafag ytfkqrytln atfrrdgtsr fakdgrwgnf ysvggnwmls
      661 eesflkgktt widelklras ygitgnenlg ssnyyayltt ysyypnntys gyafggygnp
      721 alkwesqysf dvavdfslfn krltgtadfy qrgskdllfv qtlapstgvn aiqanvgavr
      781 ntgielelhg kpvvtknfsw tidvtawhyr nkmtqiqstt pgqdtiygsg silanglprd
      841 nyflpdyagv npdngkeqwr ladgttttdy niaqqpqncv yagtpyrdie gslrntlnyk
      901 gidfsfmftf glggkfydgv yqqlaaggwg taystdllnr wqkpgdqtdv pkmdyselsg
      961 rtstrfltsn sflniknvnl gytlpdkwlk tagfrsarvy vqaenifvft prkgqdlqqn
     1021 fvggsdyvyp pyrtimfgln igl
//
LOCUS       WP_118951388            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Taibaiella
            helva].
ACCESSION   WP_118951388
VERSION     WP_118951388.1
KEYWORDS    RefSeq.
SOURCE      Taibaiella helva
  ORGANISM  Taibaiella helva
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Taibaiella.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Taibaiella helva"
                     /db_xref="taxon:2301235"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117242
     Region          24..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllmlav flwsglqlam aqgrpvkgqv lddkgegipg asvqvkgtst gtitdidgnf
       61 alevpdesnt lvinavgfap qevkagdgdq titikmsasn ttldetvvtg nairrekral
      121 gystttigad elgkggstsp inslagkvag vnitttsnsp gsssrivlrg gssilgnnqa
      181 livvdgipis ngnfgtggni gnlsnqvdfg nrgndinpdd iesvtvlkgp aatviygsaa
      241 sngalmittk kgrrrpdgak ktevevntgv sfssilkypd fqntygqgnl hdiaddrren
      301 fswglpfdnq prpwgqiidg kqkvkpysal pnnvrdffdl gkiytnsvsv nsgnedmafr
      361 lgfntlnsns ifpgkgydky nvtfngnanl tnkfyasisl nytksiadlv gggqgaaslm
      421 dnlyqmprdi plrdlrnldd rfnsmdyide dgvhrygyyg ayainpyytl ekfknenrvd
      481 rvlgsftigy kpfswlkien rlgtdvysdr ryqsaplyns qpadqatgrg dgydlagpqa
      541 gvgryaediy nlaniyndlm vtfskevakd inlnvllghs miqqrlnnsf sstnedggli
      601 vpdyynltns ngkvlatntl tlvrrvglyg nadisyknml fagitarndw sstvpksyfy
      661 yggnasfvft elfdeslkri wnygklrisy gkvgndapay ssttvygatt vagdfgstvf
      721 plnnvpgfty gniignpnlt pefssefeig teqsfldsri tvdfsyynkr stnqivnvsl
      781 passgflagt intglltnng ieiaakftpv ltrtgfrwdl fgtftknnsm vkeiypgtdq
      841 intgngingm tvvaavgkpy gtfytnayqr dpngnivvna rtglpvidpt gskffgsyqp
      901 kfqaswgttv sykgislyvm fdmkhggqff srtrdilaft gtsaetekrd pyiwpnsviq
      961 nadgsyspnt tpfdpyrfyt sqtgrpnefl lvdasyvklr earisytlps kwvnktpfgs
     1021 atvsvfgnnl fiwtpkenqf adpelssnga anaqgfefsa apslrnygfn lrftf
//
LOCUS       WP_118952845            1164 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Taibaiella
            helva].
ACCESSION   WP_118952845
VERSION     WP_118952845.1
KEYWORDS    RefSeq.
SOURCE      Taibaiella helva
  ORGANISM  Taibaiella helva
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Taibaiella.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Taibaiella helva"
                     /db_xref="taxon:2301235"
     Protein         1..1164
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128795
     Region          132..1161
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnpkstlnlp krawlrpllf gaslglglsa rpeglraqdl gekislrter tqslatllsr
       61 idqqtgysfs flredfeain vaprefkaer leailktlqk eyhleytinn gvillrlsan
      121 kaqsrskgyl ygrvsderng ealigaivsi aqqavqtdvd gkfvvalspg eytaklsymg
      181 yndlsvqqir igsgdttata fklkpasndl nevvvtalgi kreekalgys vtrldnedvt
      241 damsnnwtnt megkvaglnm lksnggpagt naiilrgens lsgnsqaliv vdgvvisgss
      301 gqitgngsga yldgdspvdf gtslndinpd diesvsvlkg pgasalygar gangaiivtt
      361 ksgkkqkglg ltfnsnttfe silqwpdfqy eygqgvdgsd twysygqtid gastrstssa
      421 wgpkfdgqsy fqynpvtrta dsvrtpwvpy knnrknffqt artftntltl eggsdkttar
      481 lsytnldnkw ivpntgysrn tvalaldqyv tprlkisthi nytnkssdnl pttgynnqsi
      541 myfirglvpn anldwfrdyw apgqenimqt rpfsslldnp ylianemlnk vnrnnvigni
      601 tanyqftrel slmarttldw asearsqqrp fssqkfasgm yrtqniftqe lnydfllnyn
      661 kvfkknfvln aslggsrmhn kfisdemrae qllypgvynf ansknlilal pyrseyavns
      721 lygtfglsfr dylfldvtgr ndwtstlatp esyghssffy psvnlsgvlt emahlpkwvs
      781 fwklrgswaq vgsggttpyl taytysptsf psglanptdi ansdlrplit tsyeagtdlr
      841 lfrnrvgvdv alylnntrnq iisvpidraa gynatilnag lvqnkgieie ayikpfvskk
      901 kdgfnwrsfg tyaanrnkiv dlaegvtnyi msagpagrgt iearpggtmg dlygigyqrs
      961 pdgkivydas gyplwtdtai yignttpkwr aswgneftyk nfrfsflfdg qfggvgyslt
     1021 hsvlaeegkl tktlpgryng ivgdgvirnd dgsyrpndvi aadiqtyyks hfdrtniesn
     1081 tfstdyiklr evrldykiss nklkgagirs lvvglygrdl lmfsdwpayd pqfgtlgdgq
     1141 iykgfeigqf pstrsygfni kaef
//
LOCUS       WP_118954466             391 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            yasudae].
ACCESSION   WP_118954466
VERSION     WP_118954466.1
KEYWORDS    RefSeq.
SOURCE      Leptospira yasudae
  ORGANISM  Leptospira yasudae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Leptospira yasudae"
                     /db_xref="taxon:2202201"
     Protein         1..391
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41280
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigilkeak eetrvsvtpd ivdalkkiga tvlvekgage qsfyhdedyk kagaslvsrq
       61 dvlsksniiv sihladpatl akiksgtiyl gmfqpamnaq tiqklaakkv evlsldaiar
      121 itraqsmdvl ssqatvagyk avllaashla rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvhslgak fvevegashs aaaggyaveq teeykkrqqe
      241 aidkyaqkad viittalipg rkapllitkk ivdnmksgsv vvdlassmgg nceytkhgqn
      301 vvtpkgvtvi ghknlagsip sdaskmfskn vlnflkllik dkkinldlnd eilssttith
      361 egevrhkltl dalgskagsg aakpkksaak k
//
LOCUS       WP_118964658             391 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            yasudae].
ACCESSION   WP_118964658
VERSION     WP_118964658.1
KEYWORDS    RefSeq.
SOURCE      Leptospira yasudae
  ORGANISM  Leptospira yasudae
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Leptospira yasudae"
                     /db_xref="taxon:2202201"
     Protein         1..391
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41296
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigilkeak eetrvsvtpd ivdalkkiga tvlvekgage qsfyhdedyk kagaslvsrq
       61 dvlsksniiv sihladpatl akiksgtiyl gmfqpamnaq tiqklaakkv evlsldaiar
      121 itraqsmdvl ssqatvagyk avllaashla rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvhslgak fvevegashs aaaggyaveq teeykkrqqe
      241 aidkyaqkad viittalipg rkapllitkk ivdnmksgsv vvdlassmgg nceytkhgqn
      301 vvtpkgvtvi ghknlagsip sdaskmfskn vlnflkllik dkkinldlnd eilssttith
      361 egevrhkltl dalgskagsg aakpkksask k
//
LOCUS       WP_118966986             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Leptospira
            stimsonii].
ACCESSION   WP_118966986
VERSION     WP_118966986.1
KEYWORDS    RefSeq.
SOURCE      Leptospira stimsonii
  ORGANISM  Leptospira stimsonii
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Leptospira stimsonii"
                     /db_xref="taxon:2202203"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41318
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigilkeak eetrvsvtpd iidalkkiga tvlvekgage qsyyhdedyk kagaslvsrq
       61 diisksniiv slhladpatl akikpgtiyl gmfqpamnap tiqklaskkv dvlsldaiar
      121 itraqsmdvl ssqatvagyk avllaathla rffpmlttaa gtitpasvli igagvaglqa
      181 iassrrlgav vdvfdtrpev keqvqslgak fvevegaqhs aaaggyaveq teeykkrqqe
      241 aidkfaqrad viittalipg rkapllitkk ivdnmksgsv vvdlassmgg nceytkhgqn
      301 vitpkgvtvi ghknlagsip ndaskmfskn vlnflkllik ekkinldlnd eilssttith
      361 ggeirhkltl dalgskssta kpkksapkk
//
LOCUS       WP_118972383            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Taibaiella
            koreensis].
ACCESSION   WP_118972383
VERSION     WP_118972383.1
KEYWORDS    RefSeq.
SOURCE      Taibaiella koreensis
  ORGANISM  Taibaiella koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Taibaiella.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Taibaiella koreensis"
                     /db_xref="taxon:1268548"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112119
     Region          24..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllmlai flwsglqlam aqgrpvrgqv lddkgegipg asvqvkgtst gtitdvdgnf
       61 nlevpdesdi lvisaigfgq qevkagdgsg avsvrmstts kvmgetvvta lgikkekkal
      121 gysvsevnsd mieksgerna iqslsakapg vqvtssagtp gastkillrg nstftgnnap
      181 lvvidgipvd ngssnvsnqs fagdnpfnin ltgvnesnra ldlnpddies vsvlkgpaaa
      241 alyganggng aivittkkgr ygkgqalgit ftssvevnkv srlpktqdqy aqgnngvfqt
      301 gntpnswgpr idttnlsryd nfgnffqtgm gfnntlalng gsdnaifrvs lgnyttkgii
      361 pnsklkrtnl tmngeaklas wltvggtany thtetrmvqn gsnvsgpmls lfrmpvsydv
      421 tkdfydptth tgknyitayd nplfsvnrnp ydsyidrvfg ntyftanimk elvltykigv
      481 daygkqdrqi ydlgskgnda sdgtgqvnks stnflqvysd lilrynkrfg dfdfgamagy
      541 nywytetrts firgtqlsvp dfynlnnaat lyasntdgyq rsqaiygels lgyrsflylt
      601 ltgrnewnts fgkggksffy ptanmswifs ehipsnnfls ygklraaisk agippqiyad
      661 rnyylqpflt dgstngngfp ylgqsgympg nvnqpgglva esvtgkeigt elrfwdnris
      721 featyyhqvs nnlllqrpva pssgyvaeyv nagklrnqgv elslnfdvyk nkdwnvsvgg
      781 nwsknvskvl glaqgvtels iesgftaigs faivgepygv fygttwerna sgqllvdedg
      841 ypildvakni gnpnpdwlmg lncnvsykgl tfsmlwdirh ggsiwngtwa rlnnvgrtde
      901 saerdhdyvi pgvyapgtak egqtnttamp aqdyfryylg dlgaaenavq dggwvrlrsi
      961 glsyrytfrn tgsgnpfkyv evgftgrnlf lstkykgvdp etsltgsgsn iggwdyfnnp
     1021 gsksyifnlk lgl
//
LOCUS       WP_118973620            1165 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Taibaiella
            koreensis].
ACCESSION   WP_118973620
VERSION     WP_118973620.1
KEYWORDS    RefSeq.
SOURCE      Taibaiella koreensis
  ORGANISM  Taibaiella koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Taibaiella.
REFERENCE   1  (residues 1 to 1165)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1165)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1165)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1165
                     /organism="Taibaiella koreensis"
                     /db_xref="taxon:1268548"
     Protein         1..1165
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126635
     Region          104..1164
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkmrilftli tgfslqalsl naqqqdtlna ntpvsqdtsi tpqnapppvd lsqvgaadsg
       61 kaqapdstak lvvdsavkit dtsvvidtag kvevgteqaa vnqqqlngvv yekdgtttlp
      121 gatvqwlgnp vstqtdvdgk faieyrkegg tlsvssvgfs tqkikvepgq ndlkitmgln
      181 agtkidevvi talgaqrntr slgyavqqld greiqeakev nyinalqgkl agvqingnag
      241 smggsakvvv rgiksisgdn namfivdgvp manmnlnaag qgtggggfdy gnpaqlinpn
      301 dveniavlkg aaatalygsr gqngviyitt ksgkgagklt vnydfnlqld kvsllpsyqn
      361 qygggsgdft klyanehpeg fgpgggtynd ndgkgsydll pqyatdeswg prldgrlvrh
      421 ywswdpgkgn pnfgqsapws pqpdnvrdff ktgvtvannv sissgnekgt irfslgqthq
      481 dfiypgskld rvffglntty nftdrlsfsg gvnyimdksk drpgtgfngf npmlqfvmyg
      541 qrqldnnylk nykyadgseq twnrsawnnp mpvsaenpyw nqyesyntdr ndryfgnvgl
      601 syritdwlta darvfsdfld hidetrsard yfvggygrrt inynennyqa tlninknflg
      661 drlsleaivg gnilnvrsqt etgttngglm spgvyvlqns vlpatlnnay gnyqtnslfa
      721 tatlgwekml yltltgrndw asplkqtgny sffypsvgga fvfselipkn kwmtfgkarl
      781 syaqvgnitt pyqvarnfdf gtpfasgsts ypllttpdql ynaqlkpert seveagldlr
      841 flndrlslsv tyydrqtrnq iwvvalppei gygskivngg nvqnrgiels lnatplvlgd
      901 frwetgvnfs rnknkvldln tndgsiggie tfiigterrt qkvsivamkg mslgtiigtd
      961 yvldangnrk vlpdgsydvt skpvvigdan pdfiggfsnt fsykgiylsg lidfqkggdf
     1021 fsytnlygnk sglleetaad girengvinp gvkadgspnd kvisardhfn vdggnriska
     1081 nlydgsfiyl relrlgwnlp qkwlgktkmq sarlslvgrn lwlihsnapn vdpsfinnsi
     1141 gntpglegga lppvrsygvn lnitf
//
LOCUS       WP_118996497             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium tuberculosis].
ACCESSION   WP_118996497
VERSION     WP_118996497.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37505
     Region          10..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdpqtqstr vgvvaesgpd errvalvpka vaslvnrgva vvveagager allpdelyta
       61 vgasigdawa advvvkvapp taaevgrlrg gqtligflap rnadnsigal tqagvqafal
      121 eaiprisraq vmdalssqan vsgykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwldlg isasgeggya reltdderaq
      241 qqkaleeais gfdvvittal vpgrpaptlv taaaveamkp gsvvvdlage tggnceltep
      301 grtvvkhdvt iaaplnlpat mpehaselys knitalldll ikggrlapdf ddeviaqscv
      361 trgkds
//
LOCUS       WP_118992540             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pusillimonas caeni].
ACCESSION   WP_118992540
VERSION     WP_118992540.1
KEYWORDS    RefSeq.
SOURCE      Pusillimonas caeni
  ORGANISM  Pusillimonas caeni
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pusillimonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pusillimonas caeni"
                     /db_xref="taxon:1348472"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38403
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligipresa agetrvaatp etikkyiagk hsvlveagag aaasytdeay qaagatlgss
       61 qdalgadlvl kvrspsaael ahmkantvlv gmldpfnqeg lqalaqagla sfaleaapri
      121 traqsldvls sqanlagyka vmlaanqygr ifpmmmtaag tlkaarvvvl gagvaglqai
      181 atakrlgavv easdvrpaaq eqveslgakf ievpfetdee reiaqgvggy arpmpaawma
      241 rqaalvserc kqadivista lipgrpaptl iseetvqgmk pgsvivdlav erggncplse
      301 kdqvvvkhgv sligysnlpa lvatdasaly arnvldflkl itdaegglai qredeivaac
      361 lmtldgnvlr sa
//
LOCUS       WP_118996310             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pusillimonas caeni].
ACCESSION   WP_118996310
VERSION     WP_118996310.1
KEYWORDS    RefSeq.
SOURCE      Pusillimonas caeni
  ORGANISM  Pusillimonas caeni
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pusillimonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pusillimonas caeni"
                     /db_xref="taxon:1348472"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38747
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpvetf pgesrvaatp etvkkyvkag hqvvvqkgag laasctdeay aeagatlgta
       61 qeafaselil kvrapseaem ssispgqvvl gmldphdger lqslarsgav gfaleaapri
      121 traqsldvls sqanlagyka vllaaqyygr ifpmmmtaag tlkaaqvvvl gagvaglqai
      181 atarrlgavv wasdvrpsak eqveslggkf idvpfesdee reiaegvggy arpmpqswmd
      241 rqaaltaqrc aqadivitta lipgrpapal iseetvrsmk pgsvivdlav erggncplsv
      301 agevvqkhgv tlvgltnlps miaadasaly arnlqdflkl iidgegklai qkedeivkac
      361 lvceggqilw gk
//
LOCUS       WP_118997644             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            polysaccharea].
ACCESSION   WP_118997644
VERSION     WP_118997644.1
KEYWORDS    RefSeq.
SOURCE      Neisseria polysaccharea
  ORGANISM  Neisseria polysaccharea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria polysaccharea"
                     /db_xref="taxon:489"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53860
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiksmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi vavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_118998811             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_118998811
VERSION     WP_118998811.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53704
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvimwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_118999899             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cereibacter sphaeroides].
ACCESSION   WP_118999899
VERSION     WP_118999899.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter sphaeroides
  ORGANISM  Cereibacter sphaeroides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cereibacter sphaeroides"
                     /db_xref="taxon:1063"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55502
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreif egearvamtp dsalqlqklg hhcvietgag mkagfsdeay aaagvevlps
       61 aaalfeaadi vvkvrgpera eaerlrrgqt lisffwpaqn aellelckek gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvylefee aqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrpapkl wtedmvsamk rgsvivdlas erggncdltv
      301 pdqkivtpng vtivgytdfp srmaaqastl ystnirhmlt dltpkkdgvi hhnmeddvir
      361 gatvthdgai tfpppppkva aiaaakprek vkeltpeekr aaeiatfrkq tvsqvamlal
      421 gtalllfvgm yappsfmahf ivfalacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 llqigsgnvl vvllaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_119013977             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Simplicispira metamorpha].
ACCESSION   WP_119013977
VERSION     WP_119013977.1
KEYWORDS    RefSeq.
SOURCE      Simplicispira metamorpha
  ORGANISM  Simplicispira metamorpha
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Simplicispira.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Simplicispira metamorpha"
                     /db_xref="taxon:80881"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38479
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligipaetm agetrvaatp etvkklkaqg htvriqahag vaasmpdaay eavgaditda
       61 aaawgcdmvl kvrapqesem allrpgtvvv gmlnpfdgag lqrmaqaglt afaleaaprt
      121 sraqsmdvls sqaniagyka vmiaadkyqr ifpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetqee keaaegvggy arpmpqswld
      241 rqkaevakrv aaadivitta lipgraapvl vtedmvkamk pgsvivdlaa aqggncplte
      301 anavvvkhgv tlvgetnlpa lvaadasaly arnvldflkl vltkeatlqi dlqddivaac
      361 lvahegvvrr s
//
LOCUS       WP_119004627             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cereibacter sphaeroides].
ACCESSION   WP_119004627
VERSION     WP_119004627.1
KEYWORDS    RefSeq.
SOURCE      Cereibacter sphaeroides
  ORGANISM  Cereibacter sphaeroides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Cereibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cereibacter sphaeroides"
                     /db_xref="taxon:1063"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55526
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreif egearvamtp dsalqlqklg hhcvietgag mkagfsdeay aaagvevlps
       61 aealfeaadi vvkvrgperp eaerlrrgqt lisffwpaqn aellelckek gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvflefee aqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrpapkl wtedmvsamk rgsvivdlas erggncdltv
      301 pdqkivtpng vtvvgytdfp srmaaqastl ystnirhmlt dltpkkdgvi hhnmeddvir
      361 gatvthdgai tfpppppkva aiaaakprek vkeptpeekr aaeiaafrkq tvsqvamlav
      421 gtalllfvgm yappsfmahf ivfalacfvg fqviwnvshs lhtplmavtn aisgivilga
      481 llqigssnvl vvllaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_119021621             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            sp. JS92-SW72].
ACCESSION   WP_119021621
VERSION     WP_119021621.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. JS92-SW72
  ORGANISM  Halomonas sp. JS92-SW72
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas sp. JS92-SW72"
                     /db_xref="taxon:2306583"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55539
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaprera rgearvaltp esaaqirklg heclieagag eaagfsdaay reagvtlveg
       61 aealwreaev vikvrepdee eagwlregqt lisffwpaqn ealleacrgr gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnq fgrfftgqvt aagkvpparv lvigagvagl
      181 aaigtavslg avvrafdvrp evaeqiesmg aeflfldfee sqdgaatggy aapsspefre
      241 kqlalfreqa pdidivitta lipgrpapkl wleemvaamk pgsvivdlaa ekggncdltr
      301 pdervvtdng vvvvgytdfp srmatqasll fstnirhmlt dltpgkegai vhdmeddvir
      361 gatvthagei tfpppppkvk aiaaakpkpr ekaptpeekr aaelatfreq trrqvtllgv
      421 ggalmlllgq iapasfmqhf ivfvlacfvg fqviwnvshs lhtplmavtn aisgiiilga
      481 ilqigsgsgi vmllaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_119026010             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter soli].
ACCESSION   WP_119026010
VERSION     WP_119026010.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter soli
  ORGANISM  Acinetobacter soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter soli"
                     /db_xref="taxon:487316"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39858
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipteti agenrvaatp etvkklisag hrvliergag vraayidsay eqvgatited
       61 vysgsqlilk vrapqgdeiq klaahttvva mfdpyrnpdl dtfasqnvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak eqveslggkw ldvpmsseeq aradeaakng ygwtpgeqyi
      241 kdqaaivdka vsnadivitt allpgrnapr likaetvakm kpgsvildma vetggnvegs
      301 kvgetvften gvkilgvpni pstlsteasa lyarnvfnfv etlfdqdknf ainpeeeiqk
      361 allvthgghv llkrg
//
LOCUS       WP_119037150             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Hephaestia
            caeni].
ACCESSION   WP_119037150
VERSION     WP_119037150.1
KEYWORDS    RefSeq.
SOURCE      Hephaestia caeni
  ORGANISM  Hephaestia caeni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Hephaestia.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Hephaestia caeni"
                     /db_xref="taxon:645617"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38582
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlketa agerrvaatp etakkfvglg aevaiergag asasyadaay eaagaalgsr
       61 dealrgadii lgvqgpdpas iaaakqgawl vaglnpfger srvdayakag iealamefmp
      121 ritraqsmdi lssqsnlagy kavldaaaay drvfpmmmta agtvsaarvf vmgvgvaglq
      181 aiatarrlga qvsatdvrsa tkeqiqslga kpifvedvkg iegegsggya gemsdeykka
      241 qadlvsshia kqdivittal ipgrpaprli sdaqlatmkp gsvivdlave qggnvegava
      301 geivekhgvr ivghknvpsr laadasalfa rnlynflaaf wdkgagkpvl peddeiaaai
      361 rltqggkvvn erlla
//
LOCUS       WP_119048338             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119048338
VERSION     WP_119048338.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107888
     Region          24..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkryglsiv lsllcfhltf aqtqkisgkv tdartgapla gatvateknd kaaradaega
       61 ftievpaatk nlivtivgyk rmlvpvkgnl lniamevegv midevvvtgy ttvrrkkfag
      121 atamvssaev rkqpmasfdq alqgqaagvs viansgqpga agmvrirgng singnnqply
      181 imdgieitaa dfatinqadf drieilkdav atasygsrga ngvivintrr gkasqlqlny
      241 dgqvgfsklp kdrlivmnsk qkidyelqrg nlygwtpaqa dslravnfdw kdalfqtgvt
      301 qqhqisasgg sqtsrffgsl syldqegilk ttglkrytvr vnvdnnvknw rfgisvqggy
      361 sklnntgeav tttntplnai rwgnpyerdi dprtgdyqet ggantgllts gqpnaamelf
      421 lnhnnnlqlk gigiayleyh fpfvkglfar tiwgidygqt egelftsprv avgrprngal
      481 qrtfarnlry tgtsslnykk efgkheiegg lffevvknna rnfgftafgf tngfenetgi
      541 tpgstsnpny iantvggggq sglqsffama sygydskyyv nvvgrrdgss rfgfnnrygn
      601 fgsvgltwav teeafmknis vldelklras vgtngnnasa nyalplfarg ayagasawgi
      661 sspgnldlrw etnrtinigv dfslfkrrls gtvelydrqt qnlfygipid palnsfatid
      721 gnfgklrnrg ieislrgdii dtkdfrwtle gnitynqnrv lelkrdstvs gltilsvgrp
      781 vnslylveya gvnpdngnal yykrdksttp tfntndkvil gtsdapwfgg ltttfsykgl
      841 dlsaqlsffl erqmynndrs nvtnptyftd nmdvevltew kqpgditnvp rptssggnay
      901 qsqttrfled asfwrlrnvt lgytfpttwt naakvrsari fiqgqnwwtk tdfrsfdpem
      961 tgvsltgaqy paliqttvgl sigl
//
LOCUS       WP_119048439            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119048439
VERSION     WP_119048439.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112280
     Region          35..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkitstrll llclafhlaa vfagygqaag epapvtgtvk sgndpvpgat vmlatnkrvm
       61 tttdnagffs lqlpaaarqg tvqltitsig fatrtvavsa gqttidiqlq kdsgavltdv
      121 vvtalgirks rkavtyamse vngseftqar ennvanaltg riagvnatgl stgpggssrv
      181 iirgngsltg nsqplyving mpidnsvpgg gstpngstir tstdrgdgig ainpddiesm
      241 tvlkggaaaa lygsrgangv ilittkkgra qkgigveyng tftlenvsvf pdyqyeygqg
      301 dngvkpttla qaqatgrrsf gakidgstdy maadgknhpy taqkdnlknf yhtgttftnt
      361 ialsggnesv vyrfslsdln aksilpnnky nrktanlnis aklseklrle sviqynfekg
      421 nnrpiagdal gnpnwtpyev antvdarwls pgydasgnei vwndagivtn syfvvnkfkq
      481 tdnknrfigq aaisydilkn ltvkgtitrd fynynftsiv ptgtqywpng qydgiksdvs
      541 etnsmitgty kssiantvgf tvlagantrr fksdeltlag rdfttpyfys fsnlstssav
      601 pvasdiktns lfgsvdldyk nvlfltasgr qdwfstlspa nnkifypsvg tsfilsdvlq
      661 lpamfdlvkl raswaevggg gpdpyainla yssvpsastv plqnvssvai tnaslkpfts
      721 ttfevgfntq lfggrlgvdl alydrkssdd ivsvpistss gytsailnsg elsnkgiell
      781 iegtpikqkd fswntsfnfa ynksevlkla dgistfslgn svngnafinn qvgntygaiy
      841 gfrmlrdaag nivydpnsnl pvqtdvnqql gkgvppltmg fsntfrykhf sldilvdgkf
      901 gnsifsvmev yatrlglmks tlagrenglk ldgvtqtgak ysytvpvanl raayynslnr
      961 ytelfvhdas fvklrqviis yrlpegflkg lgvqsanlsl vgrnllilyk ktdnfdpeqs
     1021 ltngaaqgie siglprtrsy gvnlmlkf
//
LOCUS       WP_119048455            1116 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119048455
VERSION     WP_119048455.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1116
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121869
     Region          28..1115
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkliscltl gcwlmlslva taqdtelvvt gtvtragsse klsnvtvslk gtsratatda
       61 ngqyslkvnd prgilvftyv gfgekessin grsridmvld aanttltdiv vvgyaqqsrt
      121 kitaavskln peelkntsnp npvqamqgki agvsipigtg qpgagapnii irggtklnay
      181 gsglgnangn plgatdgtsp lviidgvfrs lndinpdnie slqvmkdaas tapygaqgan
      241 gvivvktkgg kfnskmglti nhrttwetpa rdykylnadq ylplarttvk ntfdgldknn
      301 llnnggfsag trvytakgqy gnsinltaly dnivaiegqa yvdnllahgy ktmddpinpg
      361 tkllyadnhy qdmiwvtglt nntnvsidgg sekasynmsa gytnqegsfv gtrykrydvl
      421 gnfsfkaten fridaminyq nvlpnfvday qnelvrgtri tpliriykdd gnptpgelyt
      481 vrnrfhtlky ddfrvnterl isrvagdlti mkglhwkpaf syaiqdyrel fmrkatpsne
      541 iqpstqrqkn eytdnmrdlm tdqilqydfn vggdhqfmvl ggfnfrkvtn siisigsqra
      601 nndyiytive pattviggvv tsnvtnfatt lkeqrsvsff gqfaydynnk yllggslryd
      661 gfsnfapgnr yatfpslsag wnihkenfwk vkpvsslklr aswgtsglsg lelvdtyggy
      721 gatqyavgsg vlrtnlsnpn lvwestettd laldagflqd rltfsidfyn kltkdrlask
      781 plpseapfps itynngvlqn kgveielggt virsrsftwr anisfaynkt lvkelpgngr
      841 aknrqggdvv ydpvskqnie aggfaegerp yglwaykvlg vfateaeaaa wnattkdnla
      901 spsgiavkkh agdfnfadin adgvidsrdq vfmgyrtpdk iggmqntfty kgislriavd
      961 yalghlisng alarslgtgr afnegapaea lggdiwqkeg dagkkyarfs fadfdfgqrn
     1021 ylrgatlgvn qsyssdvsvm iekgdflafr eialsydvpk ailkkiratn lnvfasvfnl
     1081 gyitkykgln pesyagfdpg gyprprqfsl gatlkf
//
LOCUS       WP_119048785            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119048785
VERSION     WP_119048785.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114924
     Region          22..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkvlllpvv llwcimvlaq nkvltgrvtd ekgdpipfas vkingtttgv aaddngffri
       61 sapdnavlev sasgyttrvf nsagqgatlt itltksneel aavivttglg ikrqakelgy
      121 aatsltnrti vqgkavnvaq alngkvsgvs vattnsgvfe nakinirgir sltgnnqpml
      181 vidgaptplg ylssippddi qdltvlksaa saaiygpdav ngvilvttkk gaskkisvti
      241 nstvqaarva yfpklqdqfg agagevvdqf gnfgyvpyen qqygprfdgt mqdigvaied
      301 gsiqrgpysn lyakdkkkfw ntgityqnsv slagedffvs iqdakikglm pqdenrrtsi
      361 rfnggkkygn lsvnyginyv lqnyevvnea gmanlfpayn gsifftvlqt pgnvpltsyk
      421 nwrddkfaqy snyyneyavn pywvignlrq kgreddlign ldvsyqfwpw lkgtarvstn
      481 laftnfkntt apvvvsdwav ahrnatqftn rpgsvfddqa qtstinldyf lngdkdinkd
      541 fnirylaggm vrnnrskdvs lggnnlvvpy lynvavrsgd anvplypsna ntesrllsay
      601 gsiginfrdw aflevtgrnd wdsrllqtnr sffypginga vvlsdaipgi knseiinfak
      661 vraaysksgn vnipvyslqa tysqpggfpy gnvagftanq tipnpnlkpe fvktfevgae
      721 lgflknrinv eatyfnqksd nqilqvsqss ttgytiglan aasfknygve ldlglnpvvn
      781 igkgridlkv natyndnevl stlnnipvvi ggnsgflqns vssptannia vvgkpafsfq
      841 ltdyvrdslg rvivdaktgy psqaselvvk grslplwvvg ispsytlgnf svsmtweykg
      901 ghnfysglgs dedfagisar sadygrerfv fpnssvwdgs kyvpntniqv qdgnysfwtg
      961 aalntaiatn yfasaaawrl revnisyvlp lkwfgnqtil kkvtvsaigr nlllfvpksn
     1021 qwgdpefnys stgntfglss sfqspasrlf ggsiavqf
//
LOCUS       WP_119049046            1132 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119049046
VERSION     WP_119049046.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1132
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124221
     Region          108..1129
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvnfalltt lllllrldsf aqkitivqkg iplgkvfnlv qeqsglslfy dsrlikkdkk
       61 ididvreasv etvmdyclkd lpftyvitdn iivikereas lsddkilfti kgmitgkdsl
      121 plagatvmlk eikraaqtdt ggnflvehvp pgtytllisf vgyvnsskvi svsdrtppve
      181 vklqktddrl deititalgl trrtrsltys tqkvegeefs tvkqtnilnn lqgkvagvqv
      241 nrtsggaggs vrvvlrgdks trnsqplyvl dglpivnptg gpvaglynes pdggdiisti
      301 npddiesvsi lkgaaasaly gsqgsngvvl ittrggsaga tkinlsssit fekpsilpqv
      361 qyhygqsasg dvsnpgseds wgsklateqd pnamrnffqt gttlinsisi tggtarssqy
      421 lsysntanqg ilpsssfkqh tlcfrqtgkf lndklvvdgs flgsiqnaqn rltpgiyynp
      481 ltglyllprn fdlnsyrdfe yfspsrylya qnwwninydk dlangggwgg qdyqqnpwwv
      541 marntahnrn qhallsaslk yyfnngftlq argyfnhftn dyerdiyatt qatlsrfngm
      601 mhtiksantt aygdlllsgs kklsedweln ftagaslqyl dgkmvsvsgs ptvanvfles
      661 alekntidir nfdeksnnpa rkevqsllgt vqvnfrnrlf idlsnrndws stlaytasan
      721 kgynyfsaga avvvnevwql pqfidylrfr asyavvgndi aafssyplyt ftrgngtppg
      781 sapvvsvqgl glkpeknksl eiglqwrafd nrlqldatwy rsnivnqyfk gvalppglgs
      841 ggyadinsgn irnlgieatl rykviqrsgf ewattvnmsr ntnkvvelfd paiipsttpn
      901 qlyrlqggtg gydgilkqgg aygdiygsgf lrnaaghivv saatglpytv ddiflgnpnp
      961 dviigwqnsl sirnctfswl idgkfggrvl svtesymdql gvsrrtgear dnggqvffkd
     1021 avdemgqpwk ggvdaeryyk yiggktplae afmysatsir lremaiayri pfrnkkigdm
     1081 rvgiignnlf flkrdapfdp elvagvnpgg vgvdvfglpa yrsvgfsfqy sf
//
LOCUS       WP_119048800            1164 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119048800
VERSION     WP_119048800.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1164
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126292
     Region          75..125
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          155..1162
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvvhikpkl lgcllglqlf avpaanaqdv yayatgkqra ahqqgdtnkk pedssqkqpl
       61 fkvlkdlnkt kgvyflfade slgdrlvnpa rkdhadieki lnqvlentgl kykkvndktf
      121 vilaaketar tdvnaapass assdaqtinn rlgdvvtgki tdatgagvvg vsitvkgtqr
      181 gttsnsdgnf sievnsgetl vftavgytpq evtpggrtsv nvllassgsq mtevvvtalg
      241 inrrsrsity atqkitgeel tavkdpnlvn slngkiaglt vnrsasgagg svkvvmrgnk
      301 stqnnsplyv idgipmfnss vaqpenlfgq ssgtasagrd ggdaisninp ediesmqvlk
      361 gasaaalygs qaangailvt tkkgragtar vnlassltld rvmlkpeaqf sygqdgpnne
      421 ngwgpkngkg dysddlfqtg atwinsislm agsdraqsyf sysntdnkgv iptarfnrht
      481 ltfrenakff ndkltvdglv tltrqkstnr psaglynnpq vgtyffprnl dfgayknnye
      541 vysparalmv qnwwnvkyda gtfgneysqn pfwilnrnvr edsrdrafss lslryeitrg
      601 lavqargsyd msvddydakl nastnpiiad lngrytwern knniaygdvl ffyntklstn
      661 lslaatlgas itdsrtadrt fidsygavna dgvkqglsia nifsvqnils gnaakqqsvl
      721 rsqtqsvlgs aslgykdmly lditgrndwa saltftddls flyysvgata vlnemahlpe
      781 vvdlakvrvs yaqvgnsvra fatnpplyri npvtgglikn vraafpnrtl kpednrsfei
      841 gtewrflnnr lgvdltwykn dnynqyfetp apsssgfnty flnlgqirnt gfeimvngap
      901 vktkdfewnt slnfatnknt vvnlsedgvt dgvngmfflt tfdntyasiv keggsfgdii
      961 sfgaarddkg nlalsndgap irntadrklv gnpnpdftag wnnnlrykhf dlsflidgrf
     1021 ggevmsitqa eldlrgfsea sasarenggv qvkgtkngvp fegkidakty ytaiggragi
     1081 gefymydata vrlrevslgy tvplkwkgvr slnvsfigrn lffikrdapf dpeislstdn
     1141 glqgvdvfgl patrsygvnv kvaf
//
LOCUS       WP_119049047            1038 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119049047
VERSION     WP_119049047.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1038
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112920
     Region          22..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqsllgfll lfiasqafsq grtvtgtvtd slgksiasas ikgnksglgt ttsdngkfsl
       61 vvmdkddale isstgysrqt vklgdnlssl tivlkadaqn letvvvtalg itrkarsvty
      121 stqtigadel stvkstnvln slngkiagvq vnrtssgagg svrivlrgdk strnsqplyv
      181 idglpivnqt ggpdaglyng apdggdilst mnpddiesln vlkgasasal ygsqgsngvi
      241 littkkgkag tarldfsssi tadrvsvlpk lqydykqsta pdatspgsed swgakgaant
      301 sgdyvkdffq tgltfinsig lttgnekssn ylsysntdnk gilptstlkq htitfrqttr
      361 llqdklvldg tftgsiqnah nrstpgiyyn pltglylfpr gldfnsfkny eyfsptryln
      421 aqnwwninyd kdqangggwg gqdyqqnpyw vmnrntvdnk nqnvyaslsa kyllnswltv
      481 qlrgninnfi nqyerhiyat tqgtlsrfng nllttrtntt nlygdvllsg drqlnqdfgl
      541 nftlgtaiqd qkgtmltvng tptvpnvfle saleratidv rnyntdngtp vrrrinsvfg
      601 svqlnyqnkl fldfsdrndw ssalaytpse tkgynyfslg vsgvlsdllt lpaavnyakl
      661 rvsyaqvgnd vnpfatyply tfnqggianp pnsypitdvp glelkpeksk afeigtqwnf
      721 lqnrlsldlt wyksntynqy fsginlqryn tktdfnagni qntgieasvs ykvfnskkft
      781 wnttinfshn knkivelfdp nivtnvtkda iytlgasgsy talrldgsfg dmygrtfktd
      841 aqgrtivnat thlpifvdsi fanpnpkaiv gwnnnfsigr fnvnllidgk fggkvlsitq
      901 gyldqmgvse rtadarnngn tvtinnavde aghawsgtvd aqtyykyvgg ktpagaayty
      961 satavrlrei aityqipvng kvikdlrvaa ignnlfffkk dapfdpeqva gvnaggtgid
     1021 afglpayrsy gvslkctf
//
LOCUS       WP_119049197             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119049197
VERSION     WP_119049197.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110125
     Region          38..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikliagagi vsclcfspvs vrafapdlpf ykkapvaitv tgvvkdakgn plpgisvqvk
       61 naqqgtatda kgafsievps gesilafsgt gfapqevkvg nqttlnitlq tssanldevv
      121 vvgygkqkkg evtsavasvk sedftkgfar dagqliqgkv agvsvvtasg dpnattqisl
      181 rgsstimsst qplvlidgip galntvaped iesidvlkdg saaaiygtrg tngvvlittr
      241 kkgnrpstvt yegqvnvqti arkmdfldad gyrrgikegi fpantdmgts tdwldvisrk
      301 pvsqthnisf qggnaqtnyv atlnlrqwqg ffkrseneql lgradinhsm fdgklklnln
      361 vigrnrkyfd apnyayiyrq aiirnptdsv ynsagfyred pnaynydnpl rpiqevdges
      421 vqnemrynvn vlftpirnln lklllssvkr tnlngyaenk nhrasetlrr tgyasrgtdy
      481 lrdnlleftt dythimdlhk vtimggysyq dvtsegfsan nsnfptdlys ynrlqsgdal
      541 qlangavgms sfknnnklig ffgrlnyvfd ekylisaivr hegsskfgan ykwgtfpaas
      601 lgwrisresf msnvdfindl klragfgitg tvpndpymsl islnysnnrf lynggwiqpi
      661 epvrnrnpdl rwekkteinf gldfaiwsnr isgsidvyqr rtkdmlynfp vpvppnfqss
      721 tlanagemkn qgieillnad ivrtkdfqfr gnvtwsynkn tlvsissddr fklandffda
      781 ghtgepiqii thrvkvgqpi gnffgyksid vddsgkwiie dkdgkpklls aasgddrkil
      841 gngvpkhtag vnlsfsykri dlavnmrgqf gyqilnyqrm yyenptvkay nmlesafdkv
      901 ygkarlsspl ayvshyieng dhwkidnvtl gynfnvggnk yiknlrvfas glnlivitgy
      961 kgidpevsrl gldpgsdsrd kyptmrtfta gvnmtf
//
LOCUS       WP_119049534             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119049534
VERSION     WP_119049534.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108299
     Region          22..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknaillacl cvcclfafaq kksvkgkvsd ntgapiagat itiegtdrat vsekdgsfei
       61 qvspgerlvi savgytaqnv apgngslnvv lalastqlde vvvtalgvrk ekrnltfssq
      121 evkgdellka kepnivnama gkvsgvqits ssgtpgsssr ivirgassvf gdnqalivld
      181 gvpinndetg nlssgpgtnr ladidpaiie ninvlkgaaa ttlygssgar gvimittkng
      241 kegrkpaltf sqdlsferpl lpeiqtkygq geagvffdge tqktsavwgp lmdtlringk
      301 papkysptdd ffrtgvtsns tvsvegggas sgyflsysyl tqdgtvpgtd ykrhslftky
      361 ttriyknlts tfqfnyinsk ndrspegyvl esplwtvlta pvsynlqpat npdgsqrlyr
      421 fsrnnpywvv dniynraavn rfvpvmtfny tplpwlsive rigadiyseq dkykenigsa
      481 alptgriier nlnfrqfnhd livnahkefg dfnvevllgn nlysryvqty qqnglglsvn
      541 gfdnisaast itatedhsev rkvgfyaqan vdykrllnls ltgrydgssv lakdnsfypy
      601 gsaalgfvfs ellspevrrv lsfakvrvsy avvgndgvga yslntpfepa avgnirfpls
      661 gqsgfllsrt lgnlslkneq igefetgvea rlfnnrlsle vsyfrkkttn glipgvaiap
      721 stgytgttvn saemenkgie alvnatvvka gkfswdlgln ftkinnkvla iyddlqqlgn
      781 gftqvivgqp ygvkyggryk rnpdgqilmd ntglpiraat dsiignitpd wmggmnntfr
      841 ygnfslsiff dmkkggdien nvdgygyfyg tpkatedrap rivpgikest grtndvmvtg
      901 qdyfrrlngi tesviqdgty lklrnvslsy nvspsllgrt pfkalsltvt grnlwihsph
      961 ftgadpevss fgssngsqgi ysfstptsrs fnitvragf
//
LOCUS       WP_119049373            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119049373
VERSION     WP_119049373.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112730
     Region          22..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkriltlvfc lsvllhvqaq qktvsgvvrd tkgesvpfat vleastkrav qtdqngrfsi
       61 rvsdgaqlti sstgyasqti sasesmsval vsnsnnlnev vvtalgirrq pkelgysvtk
      121 vsgddgtrak piniqngltg kvsglniqtt nngvfadtri tlrgirsltg nnqallvidg
      181 spmplslint inpndvqdvt vlkgntgaal ygqeggngvi iittrggsrn ksvisigtti
      241 qreslaflpk lqrefgngeg enpdgtprld pwtnnsygpr ydgsevdlgd pledgsqkrv
      301 ryaaqsktpv eqffrpaitf qndvslsggd eksryylsfq dvkvnglipk denrrttirl
      361 nasrefgklt tsfrmsytqg nynvvnqdrg ganniytsll ktaahipise fedwrnnpya
      421 tadgyynrfg wnpymlidid rnkgrsddlv atleaaykim dglnftyrlg snvayvsnks
      481 vlgainvsry ttdlkgiqna rasvadamgf ayrlnseafl tykkqinrfs vdglvgysli
      541 qrktkelrsr gnnliiptly nvsnrsgeat itqtnteirt talfgklsfg wdnwaflelt
      601 grnewdsrln lnknsffypg gslslllhev ipqikttpis ylklrgawal sgtvnlspys
      661 lestfssgtg fpygglagys anntinnpdi kpefvngkev gielgfnnnk imleatafhq
      721 dntdqiieva tssstgyqsa lvnaasfink glefdlrltp lieagkdfrm dlkanytysd
      781 nevtsiyegl telgttnlny aivgmpafvl klndfsrtpn gkvivdrvtg lpstdpvnka
      841 ygrtlpkhli ginpsfkykd fslsivadyr gghyvynsig trlvfegsga lttkydrkpf
      901 ifpnsayddg tgkfvdntdv ltsggsatfw tadvfqntqt pyytsaaswk lrevslsyel
      961 ptsilqhtrf vksavitvsg rnllmwvpss niytdpefsn ttgnaqgvnn sfntpptrif
     1021 gasinltf
//
LOCUS       WP_119049998             957 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119049998
VERSION     WP_119049998.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 957)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 957)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 957)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..957
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105669
     Region          17..954
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhikillit cglvaselav raqdttinag pdnnavqvaf gtvakkdllg gvstvnvsel
       61 lkknygvysl dnlqslvggy tgsvwgqtpl ilvdgiprqa sevrlveves itvlkgasav
      121 vlygsnaakg avlittkrgs akaltidvra ntgifvpkgy paylnaanym tlynealtnd
      181 glstvgagys qgtidstrag tygykypdid lfssnylkka fsrsdlttei sggnertryy
      241 tnigltynng ivnygdqkkn ndfafkirgn vdmdlnswlt astdvvanvs dnytgrgdlw
      301 gasstvtpnf nrylplipid rldpnnsalq tmvknsnhvi dgkyllggqa gnltnaltdm
      361 laagyiktrn rtfmfnvgan anldavlkgl sfkagysmdy tsiyseayqv ayavyrpews
      421 qvngqdvitn lqkfnndlnt tsesigrtty tqtmsfrsqf nydrtfsqkh nvtasllgww
      481 ymtqfssdad neggsdyhpi rntnlgfqag ynylhkyyld lsgalvhsak lqpgkqqais
      541 ptvsvgwris deaffkdhvs fvddlklsas yasvkqdldi tgvrpdgtpt dyylyanyyg
      601 nsgalagwyp wrdgvaggft tlsgrggnpd ltfikrnefr vgldasllnr litvdanyfl
      661 qktngllsrg ntvfpsyftg sgdfrpwlny nndqrsgvdf avnlnssigk vqyslgvtgm
      721 vysnkaerrd elqpegymnr agkdldaawg yisegffqsq aeinahatqt fgevrpgdir
      781 ykdvnndgli dyrdqvdlgr ygwganpfsf ginltlkykq ftlfalgsgq tggigfksss
      841 yywlrgngkf seeawgrwte atkttatypr ltsgagnnny qnssfwlfkn nrfnlsrvql
      901 tydfsqdffk hsiihglsly vladnllvvs kerelmetni gtapqyrfyn lgvkasf
//
LOCUS       WP_119050021             948 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119050021
VERSION     WP_119050021.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..948
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105082
     Region          69..947
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklclqgv crllscllin iigissgaaq tvsdtaagvf kegrdtiisp qqpvellfgk
       61 lpshrvlqsi stvttpqlvt tpspnilqal pgrmaglnig fssggpgldg ngmffnirga
      121 raqiilidgv ergylsinpe qvesisvlkd alstvmfgqr ssygiiairt kkgdvgkpri
      181 sftaqtgfet pialpkplsa wqyatlynea rqndagntpv tpqytqaqid ayknqtdpya
      241 wpnvdwyntv lnkragvery nlniqgsgkg fryfvdldnm rekgiiktsd inkyntnaql
      301 nryslrsnvg vdvtpvtfvq lnlfgrfqry nqpgggvggi fssllttpql aypvfnpngt
      361 lagsdkyqgn aniwgqavar gyqfqdvrdi avdlevtqkl dvltkglvlk akasnnntty
      421 ftttrgknfe vfqyqngayt kygatteqtt ggganeryri vylegslgyd rtfnkhafsv
      481 ltnasqqsrl afnttnlpen ytawsgrlny cfderyvaeg avsyagynwl apakrwatyw
      541 aggigwnlhk eafisrnlpf isnlklrany gltgqvnagy fsyiqtyfga ngywfgsgss
      601 ldkssgenai antgltpeka kkfdagidlg lwnnkltita dyffnkfydl vaaptlttav
      661 fgagyplqny qrfnywgtdi sltwqqrlka fnyfvsgnfs lvqskvvyna elpknydyqi
      721 ttgkpvglqy gytaiglfrs yeeindpata vmpsspkssl rpgdiryldr ngdgqitvdd
      781 qapignakpt vyyglntgfs fkgldlsili qgtfnrqsyv sgdfmngygn sgqnnayeyn
      841 lgrftaatae takqprlwlg nntnntqtss fwlkdndfvr lknveigytf pekwsrkigi
      901 psarlfangl nlltwaeihd lrkdmdpevw gasypimkif nfginikf
//
LOCUS       WP_119050210            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119050210
VERSION     WP_119050210.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115126
     Region          41..1046
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mietctiksk rgrpyaills lllpllsgla taqeqkpgnv iklsgsvksd vgialynvsi
       61 svkntklgtf tdaagkftln vsdssailvi ssvgytaqei rvgqrrqfdi tlaatnnnme
      121 dvvvigygta kkrditgait sisakqieer qattladalq gfaagmlvin dagkpgasgt
      181 iqirggstfe agnaplfvvd gmlrdnaddi npsdiqsvev lkdaasaaiy gsrsangvii
      241 ittkrgqesk pridiaylrn ygqiankirq anaaevrlyr qiqsgslglq gmngdslnpt
      301 yngdvnyide ltqlavkdqa dvslsgggqn fsyysslrfv ndigliinsn aklmqgrlni
      361 dwfaskrikf tnqiafgwrn vneidegtsi gqgyqrdpry rlytadgali pnlggrrnpv
      421 aeallltrdg erynvnifnq myvdfskylk ltsninvdfn nstnirfspt ilsttndnnn
      481 gseawskqfn wqfqsflnys rsfkehsvta llgtsvenns srsisvsgvn yatedvltmn
      541 sagqivvsgs pgtrsggten amaaafgrls ysykgkysin gtvrydgssr vgadnrwgaf
      601 laggaawrfs eekfmdwsrg ildegklrvs lgqngnergg dysarqkyrf gsnsyngvng
      661 lildktfgns tlgwektvqk nvglelqfwk rrinvtldyy vksttdllya qempkesgys
      721 qvyvnvgdie nrgvelqiga nlvrnknvew svngnisfer gnikrlangd firgnvegtg
      781 sasylitegg aigdfygwvt ggifqydesn afnekweqlt pvlgsngvla gytfndrpyt
      841 gkvnslyyqd rklrggdrwf kkfnfsdsas ddrdrvvign arpkfyyavt ndfrykqfrl
      901 tftvnasvgg kiynsfaqsm nvysssngia lpaliygawr kpgdiaqypt gkefsstggg
      961 rtgdyaledg sfvrlayvrf tynlnpqslk rifakrlsay iygsnlitwt dyswfdpefs
     1021 sgtltpgnds gryprrrelg iglnigf
//
LOCUS       WP_119050299            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119050299
VERSION     WP_119050299.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115264
     Region          25..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkkfflscv llclslcmlg qevmitgvis dakgaplpgv sikikgterg vttndkgffs
       61 iptkvndvle isyvgyapqt vkvvnerpls iklaesnsnl tetvvigyqk vtrkkntaai
      121 ssisgkelan lpaasfdqll qgrlsgvnvq nfsgapgatp svsvrgssli tsaydentvl
      181 ntplyvvdgv pqptetyvgp gtgtgmnylg gvnpndiesi dvlkdasaaa iygsraangv
      241 ilittkkgrs gapkvivsgy agivqrpelr dvtlgvaerr akmdillkql epsqkrglpy
      301 lltdslnpaf ngntdwqdmf yqsgsiksad lslsggsdgg tnyrfstnyy dekgiikatg
      361 fkrytmrlnl gartlggkle inpiinysrt dksrgngdgn spislgagnm ptslfnldpn
      421 kkafllgqye dnldknisnq fnftlnlgyn fnshlrltsl tsyiyrnarr dynrtselmn
      481 dngnysytfs dngvtimssn ylsyvnsfgk hnlsvvggqe ftydqyqytt asgsggasdq
      541 iqvvqgfqql kigaysdyqa ygllsyygrm aydfdgkyll sgsvrtdgss rfgednkwgf
      601 fpsasaawim teeswmkgit ntfsmiklra slgtsgampn enylqynlyn vndvpfngnd
      661 ragtynsita vtpnfyngaa qkglswersk qwnigtdvei qngkysasld fynkensfgl
      721 fsvllpvtsg ydvaktnsig vrnygveltl aanllpskse lkwfsrlnig fnknkimnlp
      781 nggrdlvlng drfdknhils vgspinafyl yktlgvyatd kdvpvnpftg glfrnpngey
      841 ragdfqfadl dgdylidvfn eglnpdkmpv gdpnpkvtgg itnnftwknl slsvfctftf
      901 grdvlnlfks drfansqdgs anynfarfsi adlnkyniwr epgdkaeyak ydlgsyryyy
      961 tsaqtfflek gdyfrvksii lgydlsrnll skfkidrfkv fgsidnvamf qrskdlpdae
     1021 avnsygeysg agypiprkft lglevqf
//
LOCUS       WP_119050462            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119050462
VERSION     WP_119050462.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114488
     Region          26..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrktlrllla vflllpgvtv syaqertvig tiysedntpl vsvtvtnktt kksvvtnpsg
       61 rfiiqaakgq vlaisyigya skevtvgdna eitiklsssq nqmdavevta lgiprskksl
      121 gystqqvkge dlaqaqrenl ltalagrvag vtvttttglp gasvgimlrg avsmdgsnqp
      181 lfvidgmpvd nstfhqsalv sdgpnrnndy tnrlgdinpn diesinilkg peatalygna
      241 gasgaiiitt rkakagrslt sydnafrvek vtrfpeiqqi ygrgtagnrd lltrtflgpk
      301 fadtatlynn iegffkngft qkhnlsvesg seknsyrlst nyvdqdgivp qtgyrrfsar
      361 ltgsailspk fdiqsslnyv tvktrkatkg qfgfllsllt wpsddnikny lnpdgsrrei
      421 segstseidn pywdveknrs edetnhfign vnlnfkpfkw lllkttlgvd qqtttgftfi
      481 npqsrsgist ggnietftet nllytgqfta iatkqfrdvs tqfvtgfafd qkeyevnamr
      541 gerfylpeyi sinntdpttm rskstlnrvr nvgwfgqaqa gykdiifatl sarydgastl
      601 vrpvrpettl aertdpafff ypaaslafnf selepfksms wldygklrfs agktgktaks
      661 ayvtdnryvp vqttgggfal svyagneqlt peftynyevg temkflknrl gidvayyhve
      721 sksqilaprv syasgailkw lnggtirnrg ievmltgtpv ktkdfnwdvt vnfdknvnri
      781 tampvglpmf yiadydmvpf ggvkamyreg nsisalgvea sgatafqrnn agqilinpss
      841 glpyrdtvgs mlgdrnpdfk igfintiryk nwslnfnfdi rkggdifnan dlvlnniglg
      901 krtadretpr viqgvlkdgl entanptant isvtpyyqng yynniynved yferdinwir
      961 lrdatlsynf tswltkknsf fksgsifvtg tdlfiltnyt gvdpnvsglt asaggyggqg
     1021 ydygalalpv ginfglrvsf
//
LOCUS       WP_119050480             938 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119050480
VERSION     WP_119050480.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..938
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104052
     Region          38..935
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyikimcmc gglavampva qaqdstatva pkagdngvqv afrkvnkndl lggvsvvdvp
       61 aqmkqnymty slenmeawan gfngnsmwgm gsyllvidgv preagnvlpt eiaqisflkg
      121 vnavalygsr avkgvvyitt krgeagdqqi hvranagmqv pkvypkylgs aeymslynea
      181 rrndgltely spetiynyas gknpfrypnv dyysdeylsk afgrydvtae isggnekary
      241 ytnvgyqtsg sllnfgeaik ndradrlnlr gnvdinlndy itayvdatai fytgkgvntn
      301 ywgsaatlrp hrfaplipls miepedeasq vlvknsnhii dgkyllggtq ldqtnpfaai
      361 yaggnnkyts rqfqfntgvk adlrhvlkgl sfqstfavdy nasynlaynn nytvyaptwn
      421 tysgvdlisn ltqygqdats giqnvsnswy rqtvsatgqf nyvnairnth nlsavllvng
      481 wqqsesavyh atsnanlglq lgynfkqtyy adfsgavvhs aklpegkrqa fsptvslgwr
      541 isnesflrgs svvdnlrlta sagilhtdld iasyylyqrt ytplgswfgw kdgtgvqate
      601 srreenlemt fpkreeisig vdgsffkglv kldanffvnk itgniiqpdv lypsyfttgw
      661 pvssfapfvn ynddkrigfd fnvslnkklg einwtlgvva ayykttatkr aeiyensyqn
      721 rqgkpldaiw glqnlgffkd addvknspaq sfgkvkpgdi kykdqngdgt idardevflg
      781 rggwygaplt lginlgaqwk nfsflalgvg rygaygmkns syfwvdgedk ysivvrdrwt
      841 pataetaryp rltttnsdnn frasdfwlyk tnrfdlakvq vsydlsgvlg akkfvkelgv
      901 yvsgfnllti stereilemn igsapqtrly nlgvkalf
//
LOCUS       WP_119050495             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119050495
VERSION     WP_119050495.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110326
     Region          94..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlqslmpak siafcvllgi tcgntaysfs gnqvsptiai pgrdtipgkk dttlahaaap
       61 kqvaaqttls kdgkinirpl sftpfitaqq yvkgnlagvy vqepsgepgt dqnlfvrgia
      121 mpllskrelf dnqaavylng iplatenpfa yeiqqydfnr igpatnllat lnidnvesie
      181 vikdpaklal lgpvaangai wittkaassg frqinvnayf gfapqervta ingvyennfr
      241 lpfydkygtl adrfnypayl kdssnadyyg rsnwtdlyyk nqalynldls ltggsdranf
      301 rffgaatrna nsadetslqr ynasfsinvl plswvtvssm ingthmirnr nrnfvdrlae
      361 arylpdvsnp lppnksvysn ylsefdenvk ddnkttavqg yfnilakmkg vrynggisfd
      421 ynegtrdvfy ptqllegnnf vsnyfgfnqr fifnntlgyt frinddnkid velgqnyqtt
      481 lnkfeyayay ngpnnfikln ivegdinktn ylqsqgfdvf yhpsnqkaav asffgkaawn
      541 ykelldvtav arrdgssvmq qdnrwytgfg lsasfdlyka llkdsralsa lrvsasygrn
      601 gkllsddrfa ggpnyrsdls wtgapsigsy aglpgisrpy tagwvgygip wayveqatag
      661 veasllkdkl qvrldvyskt dkdmllpvpv paeygyksay asgmdvnnsg vdltvqaavl
      721 aggkhkpals lqanlnynkn elkalpkgln qvvindhllq vgqridafwl yknegiynsd
      781 aevpvkpgts qpltyqgval kagdarwkdv ngdftinedd kvlsgqslpk vtggfggnla
      841 ygsfnldfhf yfalghklln kyaaqrldfi ntdassgidg vkeitywekk mdlsgypmyn
      901 pwsnaipyrl dqdlflddas fvklrsvtls ynlitgwkgm gksqvfreat myvtganlft
      961 itpfkgddpe lvqynglytg aglpiqrsii lgfkial
//
LOCUS       WP_119050642            1140 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119050642
VERSION     WP_119050642.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1140)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1140)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1140)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1140
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1140
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125526
     Region          142..1139
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqrsaygkgl hcharnvamh fqrsvsigll lllsiqflaf rpagesqvvs lnfknaplqk
       61 vfneirkqtg ytftysetdl skakpvnisi snirildalt lifqeqplty tvieriiiik
      121 ekaekkinqe qrslqslvpm dvhgrvlneh ndpvagvtvr vkgsekigty tdgegefvlr
      181 niesnvtlvl tavnitsiea kvdgrkyldl kvmgktapld evqviaygkt sqrfnvgnsa
      241 tvkaediekq pvknpllalq grvpglevtp anglrgsgvt iriqgtnsly sgndplilid
      301 gvpyasqtlr ttsvgtillg nsgsptgaav ggagsplnyi npsdiesidv lkdadataiy
      361 gsraangail ittkkgkagn tqldlnlsqg wgkvgkfmnv lntkqylemr reafnndgvp
      421 ipsiitnpsn tnydvnghwd ttrdanwqke liggtaqysn viltvsggtv ntqfrlsgty
      481 nrmttvflgn sgnpsknlsf slnnvslnkr ftlqfsgsym ddlntlpgvd ftksaitlpp
      541 napalytsdg slnwapnaag rssfsnpltq ldvkykaqtt nlvanlamgy klmdglelrt
      601 slgytnqqln eymgyplsiy apenrlvpdp sllraadysn sninswiiep qlnyqcsfgy
      661 hkfnaliggt aqqrnsngys lsgsgyttda sledpkaavs irvgstvpvt ykyvgvfgrl
      721 sysfkdrflf sltarrdgss rfgpanrfhn fgaigggwif seeglirkkl rflsfgkirg
      781 sygttgndqi gdyvyipqfa pysvavpyqg tagyslgglf nphleweetr klqigvdlgf
      841 fkdrvlitan yalnrcsnql mdynlpyitg adrinynfpa tlqnrsiela frsvnyrnan
      901 vewtsnvnit fpenkllsfp nietssyaqf liigksfnvl qlrsvigvdp ltgifllqgk
      961 ngptsnpsev lprvaiiepq qkysggfqnn iryrqlqfgf sfqfvkklgl kyfagqvpgh
     1021 fnrgngnqpt svldrwqkpg diaeyqkfsq nsslasiyss vfysdysitn asfirlnnvs
     1081 lscqlpsewm hkisfrsanl ylhaqnlfti tpykgwdpek pgtvalpqlr litvgiqatl
//
LOCUS       WP_119050662            1125 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119050662
VERSION     WP_119050662.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1125
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125039
     Region          98..1124
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskllvltv gtlllavkgh aqktitrtfi napletvird isdsagltca tnaarfrkcs
       61 pvtinftkve vyqaledack kqpvscrieq eaiiveprdv kgritderge planitvvss
      121 gsnkhfvtrk dgrftlyqaa ldsffdvsav nyesqhiild gsvwfnlilk ekvtiygdst
      181 gvtvcdgynr kpreratgsf gniglqqlia rpsptlgprl dglvpgmvvf ntdigltspl
      241 paitirgvst llanaqplfv vdrfpydgnl nqlnpndiec itilkdaaas siwgaragng
      301 vivittrqgk hnqgprlsfs tqltlldkyn srylpllgaa stlsledsff hrgyydvall
      361 sgfgsvppga eileqlrlgm idstkaasll qalaghdvrd dldkyyyrrt taqqyhlsle
      421 ggdtqsryyl sagydkinng ltqgtqyrys itsnysykpr ktveinlgaa lnqtgarndi
      481 pfpgiaytya mlanpdgtaa vvnrdrpqvw kdtqvlngmp dwsyrpldel slrddslhrl
      541 qtrlfinlay tvvkglklqi aaqnlventt httrypiasy ayrdlynnfs ylhgfgiasl
      601 vpqgpmediq qthyratnir gqidynhnwp dnkweltava gaeiarttad tsrgrhyskt
      661 vnfdtlynmy eallppmalp gkpytreafd yfrsyfaiag lalhgrymmt gsfridqsnf
      721 fgartnaltq plwsagmkwr ftnepfinis wlseaslrtn fglsgnidks lsalltttpp
      781 vinqygaetr tilnaanpnl qwetsrlfni gldfqfskkr fsgtveyyrr fskdllnnei
      841 trttagatpy rnnsaalrgh gvelqlnvrl plgkcqyngs lllayttnkv ihtdtskqka
      901 idyldpsagn llvgrpsdal yalhkapldp angdpraylq gepsndypai lngprdslqy
      961 mghstppwta aisqsisyyg itlsflligr fgyhyrqssm dyhgfisgtk lphpdydnrw
     1021 qqpgdetrtt vpsfpaiidp frdqvygysn vlvkkadnir mrevklsyml nekigkkagl
     1081 sgatiflyga nlgilwkash nsldpdspsa mplpksysig lsinl
//
LOCUS       WP_119050977            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119050977
VERSION     WP_119050977.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110638
     Region          34..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqrlrmwlm ailllplhif sqnatstins vlhgrvtdlk tgtplagasi sikntthsvv
       61 tdgqgkftfr tgqklpyili vtyigykpqt itvaaedvei kleelanqle dvvvtgvaeg
      121 tsrkklsfal tkvsteqlnt vpatdasqsl rgkvaglqid qaagnqgatv ylrgaksing
      181 niapllvvdg fvtglglsdl npqdiesiev vkgaaasaly gtrgeggviq vitkkgrgln
      241 kvnitidney gisnvqrtpp tsqyhfykvn adgsfvlssg nnrtldlkdn gfslnqhpyt
      301 kyndnvnnml snnpyftnfi svstagekyn lyasfqnqsk ggiagpispd trrtallnvg
      361 fkpnknieae vtvqyfnrnt pssslsssga gsvlysally epfidlterq adgkyafkpf
      421 gfdiqkfnvg npfyqlsyre ysnisnnfli ggrlkykfsk klsaevsgaf qneyaetedy
      481 ypvgyqtltp evtrnngyyg lsndriaskn gqlqlnyndh fgdfdfgvnl ksvyeesrvt
      541 gisasgynls apvkslnvve aatrsnsssw sqlvnygyfl niksawknkv fldvlgrldl
      601 ssrfgsdvat affprasvay ritedvdlgv vtdlkiraay gqagslpsfg akesrvslss
      661 sggvsytrrd ntdltravts evevgidavl fnriniqany aratskndfi svppfppttg
      721 tasiwdnlge vrsssyelei ngnvinkgkw qwnagatfsr vrskitslgd vpeftsgdfr
      781 kaagispysy ygysiltnls qlqvddkgfv snaaggtlrp deftvnklgf vvlksqigta
      841 aetpvfyqna atgnnkvigd aqadfqvgfs ntvswgpfsl yavldwkqgg qkynetvnyl
      901 tyqyrstftd ravaaglplp fttavfnaqq ttdywiensg yvslrevslg yqlpvqklgv
      961 grvlkgarls ligrnlytwt dftgvtpegw didfyaypif rtfsgrltln f
//
LOCUS       WP_119051256            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119051256
VERSION     WP_119051256.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123747
     Region          32..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqtlvkprpg mialvlaalf lapltmlaqt drqvsgtvtd astnlplqgv svtlagkttg
       61 tstndkghft leaavnskls fsftgyvtqt vtvpatgdls lrlevtnqsl nevvvigygq
      121 arkkdltgai tqirpdkiad qnpntvqdiv rgtpglsvgl dpngkgggsi qirgqrsvyt
      181 daghndpllv ldgmifygel seinpddiaq idvlkdasaa avygaksang vliittkrgq
      241 kgkprinfts nlgistkagn rdvfgpegyi qyredwykaa tfgvnaatgq yeayqvplsg
      301 wgtnkrpgyf enptpenlak ygitidqwra ystnlptdnd vsiygkrlam sdvtlnnyva
      361 gktynwqdhs frtginqdyn lsasgasdnm nyymslgyls nqgpirgddy kairanmkve
      421 gkiakwlevg gninfqnrtd gnlavdwqkq slrnspfany ylpdgrlawh pqgdgstnnl
      481 gynydfdrqy mdldkgytvf nailnakvkl pfnitysfna spryqtfrdr yfesarhpdw
      541 tannglvnre qtqrfdwsln ntinwehtfa kkhrvavtlv qeaenrqswk driearnilp
      601 sdalglhetq ngdkarstfd sedtketadg mlarlfysfd drymltasfr rdgysafgns
      661 npranffsia gawtfsnesf fkwepmstgk lraswgqngn rsladpytav anltvggggt
      721 mgyldnggnl keflylfmnr lannnltwek tesfnvgldf gflndritgs idyyitptva
      781 mimnrtlpdf tgfssittnl gkvdnrgfel sintvniknr dfswnttfgf skykntikhl
      841 yyeyqdildg qgnvistrer dvipnnwfig qpistiwnyr vtgiwqknev aeaaiynqrp
      901 gdpkvannyt addkvnatnp alssyyndnd keflgqtapp imwsmrndft yknfnfsfnm
      961 ysywghkslv giylnqdngt slvtnqanqw kkeywtldnp tnsyarldar gpvgtgsnap
     1021 gklydrsfir lenvtvgytl dkkllskvgv ekikvfasvr nvalwtkekd whygdmetfn
     1081 tsgdagqifr sgmapriftf glnatf
//
LOCUS       WP_119051262            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119051262
VERSION     WP_119051262.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115666
     Region          31..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkyssggps rssglwllsf lllfisaaha qtvtgtvsde kgtklsrisv lvkgtsqgtv
       61 tdndgkysig ippaagsnpt lifssvgyki qevgiggrtv vnvslaslne emgevvvtal
      121 gikrqarslg ysatsvkpee lsvnrtsnvm nslqgkvagv nisslgtgpg gtskirirgq
      181 sslsgqnnpl ivingvpidn tnfndntisv kgggvfadgg dglssinpdd iesmtilkga
      241 pasalygsra kdgvimittk tkgkvkgigv tynlnytnet pldfteyqse ygqgengvrp
      301 ttpnptsgqw sfgekftpga tqvlfnnltv pyqwqgsrik efyrhgqnls nsvafetsnd
      361 kgglrlslnn tdnkgimpnn sfnrktvnlg fsydlteqft vagnvnysre fnknppnitn
      421 qdnsitttlm gistsmplsv lndnkynaag neypwsrftn rtnpywvlae qfhnikrdrv
      481 fgnvtlryel lkwlsvqgri gqdywsrded vnnfptgqas raaappgfvn giytqesrrf
      541 retnldflvn ankefgdlgi nvnaggnqmr krsdinnvvv tdfiirglyt vqngrakdpv
      601 ytlieqgvns lygsaelnwq ktfyltgtvr ndwfstlspa nrsilypsvs gsyvfsehlk
      661 tatwlnfgkv rvgyaevgsd gdvapysdql fytvnanfin npagipvpvg tsnifngasg
      721 ttlpnpnlkp arvaeteigl elrmfnnrvn idlaayrkit sdqivsvqis dasgylntpi
      781 nsgksrnygf egmlnlvpik nryfnwefta ntsynitkvl siitdkpger ittgthvfng
      841 etrqvvgeei gqiagfgyar ndkgqrifqs nglplrtpdl vlfgsalpkw vggflntfny
      901 kgihltvfid yklggkilsg tnfnavregl hqmtlegrvg gvkgvgvdas gnpnnavaav
      961 qtywehlrtq qivepvvyng gywklrqlsi gydftkhvpa kwpikglkld fvannvlvlk
     1021 kwvdnidpet fgfgsdnqvg lespglpttr slglnlnikf
//
LOCUS       WP_119051277            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119051277
VERSION     WP_119051277.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113605
     Region          33..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mttplskngr plrvlglfli snlvaimama qvtisgkvtg pgeqalngis vsvknttfgt
       61 atdaagnfsl taplkpgtyt lafsgvgfka vertlqigsa ttytqqvtlv edalgldevi
      121 vtgtsagttr kqvgsyistl kaddlnkgat snvlaalqgk tagaqiiqns gdpaggisvr
      181 lrgissvnss seplyivdgv ivnnatnrvt ntqntydapn aatnntggnl fvgtvgqsrm
      241 adinpadier vevlngaaaa aiygsranag vvqiftkrgs tgapvvsfst glmvsslrkk
      301 ldvnqapikf ggptdgpgal tqdlitavgg vlptnttpvt rydyqdyifr talgtdnnvs
      361 vsggkdktky yasasyffnq giikntdykr fsfrmnldqe ltkwasmsvg lnyinsnane
      421 kpdgnsffsp mnavtilgnf hdiwkrdalg nlqavgergr inpvsviedf kqkqetnrli
      481 asaaiklrpm kgltidytlg idnyaqrgtt lmppftynas taffgggpdl saslngyasa
      541 annnffqinh elngtyqfdi sdnitsttqa gysvqyekng ytlshgrgla pfvetvnaaa
      601 tilpgsdert efsvsgvylq qnfkfnnqlf ltgavrmdgs svfgedqrnq vylkasgsyv
      661 lsesefwnkl slskwwnlak irvaygesgn ltgitpyarf ngynavaflg rsaifsntqy
      721 vdpdikperq kelefgtdls ffnnrlglqf nyyikkvndl lisrviapsn gyasylsnlg
      781 slrnkgfevv ltgtpvknkd wrwditaiyn hnrnealkig qaltllstna gapvailege
      841 pigvfygaff ardangnqik natglplqer gtqngplnyt tqrdanglpt gtplrkvvgd
      901 pnpdytasii nevsykkfgl rvqfdavqgv dvwnadfrtr qgvgngkvae qeylgqvprg
      961 yinsvyqide wrvddgsfvk lreislsyrf gkvkvfsdlt vsasgrnlis wddykgydpe
     1021 vtsggqstvl rgidfgtvpi prtfsisvaa kf
//
LOCUS       WP_119051300             989 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119051300
VERSION     WP_119051300.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..989
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108901
     Region          31..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrrsnfvr rgllcllall slsvtafsqt rtvtgkvtna adnqplqgvt vtvkgsttst
       61 qtdaegnysi avpnnvrilv fsfvghneqd vligatgatn valtpsgrsl dnvvvvgygt
      121 qkkrqltsav dhvgaedfrq ggarnaldli qgkvaglqir rsssnpntgv giqlrgvvsl
      181 tgdqgplvvi dgipggnldl lqqediesid vlkdgsaaai ygtqgnggvi littkkgkag
      241 pakydyatyf rkeyltkrpa fltpeefkak lasgeldaas ykdyggltdf fdaminhdnl
      301 sqyhtlalsg gtatssyras lfyrdfqgfa kensrreygg rlninqkgln nrltmqlnla
      361 tnfnnanllg gggwedqltk nptlshknpd gtwyfegtst nqyarlfqet nkrqqqttsi
      421 dgrasleiik dlkasifgsl vrnsyidgay relasessve syqgtgyasr stylqidyav
      481 eptieytkti hndhsvgvig gysyrysvae nfnannygfv ndrfrennig tgnqlglgka
      541 gmgsgkadnt liaffgrvny syldkymaqf ilrregssrf gennkwgnfp avsagwnisr
      601 edfmrdisfi nnlklrvgyg vtgnqgiany sslvtlgggg iyrfpdgqyr qtfgpernpn
      661 pnlrwekkke lnigldfsll dnrlsgsiev ynrqtedlle nytspqppfi rsniylnvgt
      721 isargvelti navpvktknf twntdvtast trnkldvlsn adfklpyrey ggiggfgalg
      781 nairtyeggv lgefwgkrfa eldangkwlf ynrkgekvan aainnsfdrs ttdlavigna
      841 ipklyaawsn sfsyknfdfr ayfrgkfghd ilntmalsyg nkvtktnllk dafgkyagik
      901 dtymysdyyi ekgdyvkide ltlgytfklk tqyirnmrvy vtaqnvatit gysgndpdfi
      961 qdlglgagid ergpypstrs flvglnvgf
//
LOCUS       WP_119051827            1096 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119051827
VERSION     WP_119051827.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1096
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121811
     Region          36..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkyfekacc alilsatcwl agtaqtpaat dnkhiirgki tdrknkepit gasvsemdad
       61 griikgaatd iegnyvlrit npknklsvsy vgykttsqai nerttinfql eagagadlee
      121 aivvaarrvd ngmgqkaern mttaasrvna kdmeemssas idqalqgrma gvditatsgd
      181 pgaamnirir gissinstgt plivvdgmpy eteipgdfnf gtadeqgyaq llnispadik
      241 eitalkdaaa tavwgsraan gvliittkrg srgkpsityt fkgaasilpk aipmlngdqy
      301 stlipeafmn rmgttmnpsv refnydpndp ywyhnysnnv nwvdaisqqg flqdhtismt
      361 gggekakyfa svgyfnqtgn tigtaltrin trinldytis dkikiftsia ythtdqarny
      421 fntdnksega irnvaylkmp nmsvfeydeq gnltpnyfsp asnvqgqyar iynpvamasl
      481 aklnvlgeri vprfqidysi vknllratfd vqfdinntkn nsflpqlatg rpntetvvnr
      541 tydgdidlfg vttrsslfft prfrnedhvf sgsfnlftgd nkavnqelmt sntassllvd
      601 psapsrtqnq elaavsrisq trtvgavlia nysfkdkylf eatlrgdgns rfgpdykygl
      661 fpggslrwri seewffkkik qlddlsfrls yalsgnaprs dysffntynt yawsylgqsg
      721 vypsrpelkn lrwetvhgan igmnislfka rvradidvyr nrttdlfsda laiptqngyn
      781 slsmnigtmd nrgwelaiwt tpfknktwti gfnfnisqnq niireiseya anskgnvgan
      841 geylrllqid npfgsfygyk ykgvykdkea tlatsaggkp iigpngqqvy mrfnypnvdy
      901 tfqpgdamye dinhdgniny mdvvylgnsn ptlvggfgpt fsyknkisls ayfnfrygye
      961 vingtkmntt nmnsfdnqst avlrrwrkeg dvtdiprgii aggynwlgsd ryvedasflr
     1021 frtvtaryvf dgkllsrlkm ktlsafitae nlitwtkytg qdpevnarga difrlaidys
     1081 mtppsktfti glvagf
//
LOCUS       WP_119051842            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119051842
VERSION     WP_119051842.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111675
     Region          29..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqllglsll lcfaalcsln vsaqekkwvs gilrdprgnp vasatvvekg ttnqtlsdge
       61 gafrlqvasg atlvissigf kaleapasts salnliiqpt aadlnevvvt algikrqkks
      121 lgyavqevkg ttlldarepn ltnaltgvva glqvirsstg pagsskinlr gntsltglnq
      181 plivvdgvpi dnfvgavnnd yfnpgldmgn gladinagdi esisvlkgas aaalygsrag
      241 ngvilittkt grkqnglgiq vsstlgvesi fthpdrqttf gmgsdgafap tasgswgpki
      301 tgqtvtnwkg qseqmqaydn vkaffgdglt qnhnvsfqqq instsiytsl nylndksmip
      361 gtkltrvnlt aravskfgkd nrwttdtkiq ysnanaknrp vaglntsnyp allynlpvsl
      421 dvtqfdppvn qfgamiwydg snrvnpywnt kynlnndard rfimtgslky nftswlnaev
      481 kggadmyttn ynskvyagsp ltttgrfsvg kqtysefnys tlitaqkdnl fgklggtatv
      541 ggnlmqqkss nvgvnagelk vpnlfsatng tgtpvitdty serrinsvyg tvgvnwdgyl
      601 fldatfrndw ssalhpdnas yfypsvslsy vftesfktlp switygklra syatvgndma
      661 pyqlyntyti sndpnqntva arkatrfdkn vrseliksse lgaelrfldn rigldfsyyk
      721 snatrqlidl pmdpmsgyta rkinagdiqn sgfevmldar ilnnpggltw nlsanfsrnr
      781 nvvkeisdrd svskyqlggf davsvqavkg elygeiygst flrvtdtkse yygqliltgt
      841 glpqaglqnq rlgnqqatgl lgvtntfgyk gftlgvlvda rfggkifsat qvgmqragta
      901 aatvvngera nftvdgvvvd gtgykkntta vspqlywsqv tnlgnagite lnmydasnvr
      961 irniqlnydl plkilsktpi qrarigvscn nvwlisshmn gldpesvfat gtnavgfenv
     1021 sppttrtvlf nlsltf
//
LOCUS       WP_119052477            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119052477
VERSION     WP_119052477.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110976
     Region          23..1004
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtlilflll fsfaanslla qskqikgtvt dkqgmpvyga tikikgnskg tsagtdgtfv
       61 vtvepgailv isavghetqe vktgtsstit vslgddiktl tdivvtgvaq atskeklafs
      121 ltkvstekin tapaldlsqt lrgkvagiqi tqtqgddgas vflrgaksif gnisplivid
      181 gfvtnfslsd lnpqdveaie vvkgaaasal ygtraeggvi qviskkgkgt kgvaitvdne
      241 vginniqrtp alanmhhyvt sdtdpygfay asgsttsriv nyksngfsvn lspyknnynn
      301 tdallgdnky fsnyvsiats gdkynaflsf rnqytggvae pidpnkkksl qlrlqfrptp
      361 kleaevyvny fnevkpsaav tangqgtffa aslqwepfin laaknaagny nvrpdgwniq
      421 ganlsnpmye wskreytnnt dnylaggklr ykvlrnlsve vlgsmrkqny tasdtyprgf
      481 ettttsesln ngnvslgyny yqmmngqaqv nyntrfgddi tlgvtgkmvy eewyekefgv
      541 sgydfsrssd iyvigntrtd trtgygsdmf tnqtvnygyy lnfqtswrdk vfvdalarvd
      601 qssrygideq taffprvsla yritqdfnlg naiselkarv nygaagsvpa ynlknsrvtv
      661 sasgftlnql astdlqrsit hewefgidav lyrkinvqfn yalarssgdv vrppaftpye
      721 aagvyknfgv tksnslelev ngnaiqtknf swdfgltfgr vrseikslgn glppftdglf
      781 wkdagvspfa mygnkvltsl sqlevdktsg kvinaaggay tlsdftvnnr gfvvlasqvg
      841 tkdekplllq kggasvstvi gdaqpdfqvg ftntftffkn ltlygtvdwq qggqkydqtt
      901 qylsfdgrtq iwqdyaasgl plpflqtlyn gnsytdfwia nssyvalrel slsyrfpgpk
      961 knkifkdisl sligrnlytw tdfkgtnpeg sheyfpypvy rtfstrlivn f
//
LOCUS       WP_119052850            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119052850
VERSION     WP_119052850.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107748
     Region          28..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtsnrlftas alllltlcfs aatlaqdkii tgkisdskdg tpvvgasvvp kgsakgtstg
       61 tdgsfrvnva eavttlvvss vgyitlevdi tgktvanisl easnsalnei vvvgygtark
      121 kdltgavasv kakdfnqgiq tspdqliqgk vagvqimnns gqpgggttvk irgnssirag
      181 snplyvvdgi pldgrsarpg gsgagigtsp aanplnfmnp ndiasievlk dasataiygs
      241 rgaygviiin tkrgqtgapk mdvnfyvgms klikqlkvld ageykkalad yglttgdygg
      301 svdamdailr tawtqnydvg fsggtengry risagyldqe giirksnfkk ystnisgffk
      361 fleskrlgvd yniiasqtve qiapvsndag ftgsiigqal qwnptrplir kkangqdsld
      421 idknsstvnp lamseayddh skvtsilgsi spyfkitkdl eyrmlfsiny stgirnaqia
      481 kyinlqdigp stdypdgrgv aytgtneltt kqfthtlnyn kkispsfnin allgfeymkf
      541 dtkgsgmnar dfgsynipft nyfqfssqst rgtfsfadpt telqsyfgra ivnykdryll
      601 tatfradgst kfgknnrygy fpsfavawnv qnesffdvdf intlkvragw gktgsqdapp
      661 gsaqerygfn gpnstfkvna enkdlkwqad eqidigldft iwenrisgti dyfhkkttgl
      721 lyptitaqpa ppgapptwkn ldaeivnkgv evtvqaniik trefswdlgv nasflkndvs
      781 glpapiatgg lhgqgisgat veqitnnqpi nvfytkrflg idkgtglany sddgyvlyyl
      841 gnpnpstvlg istsvnykkf favvnmngam gqkiynntan tvlpignlig grniaralig
      901 tevkenlanp ispssryien gsylklanat isynvgnigk alknlnvyia gqnlfvitkf
      961 tgfdpevntd kqvngipsvg ieytpypsar sfqiglnfsl q
//
LOCUS       WP_119053050            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053050
VERSION     WP_119053050.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109254
     Region          23..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkailvllc valnigqlla qtrtitgkvt dpaglplsgv tiiakgaagt ttasdgtfkl
       61 svpgsvkvis lsavgyegqe lsvvgknevi vsmkvdnqrl eevvvtgygs rrkaeftgav
      121 srvsskkieq vpmasfeqil qgrapglyia sgsgqpgsya rvnirgvgtl gngtdplyil
      181 dgmpieagvf rtmnpndfet vdvlkdaaga slygsrgang vivitskkgk sgkaqlqfrt
      241 qhgvntqpti kydmmntdqr lqfeetilgp gnilpvngag ltgypgwdys knnprygtlt
      301 paqqqleahl ldsikgintd wadhffrdgk fhsyelnasg gnqgmnyyts lsaynqegiv
      361 lrsnldrytf rgnldfktdr ltvairssag wskqsgiese agvalanpia aaylslpyvr
      421 lfnnaglpdv kgsniganay drlftttsli nqfkgtlgit atyavwggig lrttagvdyr
      481 nnntsryidp rsfagtsist gnrgsynegn nenlqlmtss gltfnrtfns vhtvnaqall
      541 efisnryraf natgyglntk lgitpaaita gsttnnmipt iggsktrnal yslvgvadys
      601 ydkkytlsas lrrdapsqvp egnrnnifws vgaswnimae dfmasqnfln dlrlrasygs
      661 sgnangfssd ygyitsygsg gyagvtgivp sspgnpsykl esqaianigv dlsawnnrlr
      721 atvewynkks knlfasqpis rstgfltlst naaevkntgv ealvavdvis nkdwtvtigg
      781 nvaylkneit slgslsefta gtgiyrvglp igthytvgwi gvdpqtgdai yqdingnpts
      841 vysasnnraa fgtyipkytg ganldarykn fdfsvlfsfa egvkrynner ffyelgnngv
      901 synmtadmln awtkpgqvtn fqrvgagstr qfsskdinda sfirlrnmqa gytfnfknps
      961 kairgfriya qaqnlltwtk wqgfdpeesn niatyefpnp rsytfgvdvn f
//
LOCUS       WP_119053047            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053047
VERSION     WP_119053047.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111723
     Region          25..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilctlls tllilsqfvv qaqertisgk isdpaglpvv gasvtikgsa lgtttaadgs
       61 fslrvpasak aiiisavgya sqdltignkn vftvslaqed kgleevivtg ygnqkrsqya
      121 gaaskveaka inqvpmgsld qilqgrapgl yatagsgqpg saanviirgv gtingtstpl
      181 yvmdgipvqa aafaalspgd iasvdvlkda vatalygsrg sngvivittk rgksgkvtfg
      241 vksqygfsdr trpkfdmmts sehlqfeeev glengfdigp gwylsrknpd naglpetrla
      301 rydqildslr nnttdwgdif frrgktqeye vnasgggert gfysslnyfk qegianrsql
      361 erisfrtnvd fktdrltigl sttlnyasss fiegengtsi vnpfsavyya lpyelpyrng
      421 vllhggntsg pgadpllpat agralvydqr egsaalerqn attskrneik ailganiryk
      481 lfdglsiist lgvdfrelmt erfidprtyt gtqvaigaqg sfsegtnrfm qlfgnaglny
      541 nktfagkhqv dasalvenmk atsrafsyvg yginpillnt paavtqgsta gfiptvaggr
      601 dgipgsgviq sligilryty dgkysfngsy rldassavpe knrsisyfgv ggswnimken
      661 fmstvdfvsd lqlrasygss aspfnspfgy lslygnsttp yngqpgyvvs qlgnddydwe
      721 ynnttnfgld fsvlnsrirg tiewynkatr nlfisqqlsa wsgatsqnvn agemrnrgve
      781 valsgdviak ndfrvtiggn vgfnkneits lgqvnefplg tsiirvglpy gthfipkwgg
      841 vdaatgnply ynkdgtlttq ynsstqsvad fgswlpkvng gfngslnykg iyieaffsfa
      901 agnkrynned ffnenysfat snqstewfkr wrkpgdvakv qrfgsarsfs skdiqdasyv
      961 rfrnlnvgyn iprkylqqia ifsaatvfaq aqnlytwttw rgfdpednnn istfeypnar
     1021 tftfginltf
//
LOCUS       WP_119053158            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053158
VERSION     WP_119053158.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117739
     Region          50..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskcnlftrv vtaclllalp llslaqkpvs gkvtsikdqa pvpsvsvvvk gttvgtstna
       61 dggfsinaka gdvlvfsgvg vlpkevavsg dnmqvaleld aralnevvvt algikkekkk
      121 lgyavqevkg edlvkarepn pinslvgkva gltvgasaem lagpqlvlrg rgislfvvdg
      181 vpinsdtwni spddiesytv lkgatasaly gsrglngaim ittkrgtrdk rgfsiefnst
      241 tmmekgynai pkvqdeygpg dhgkyafkdg kgggsndgdy dvwgpkfegq lipqydspvd
      301 pvtgvrqgtp wtargknnlq rflqtgllst nnisvssrsd kydlrfsisn tyqkamvpnm
      361 kinitnfnis agynfsdkvr legylnynrq ytpnfpdvny gpnsmiynit iwagadwdvd
      421 qmrnywqpgk egvqsiyaey qryhnpwfmv kewlrghykt dvngyaklsy qpvknielma
      481 rtqvttydlf rnekmpfsah pygreegrgd yredkrtlfe nntdflgtyt nrfrgnidvk
      541 gslggnirsf kynssfvttd ylnvpgwynf nntrnplras sfaadmltls gygyldvsln
      601 kyanislagr fdklsalpss knvyfypsaa vssvvsdyvv lpeaisflkv rgsyanvkgg
      661 ltqatigatp qasyplgygt eyyaaydgps yensaayttp pvynnqpgay ytstldnpei
      721 kpfsstvyea gadirflnnk igvdvtyftt kdgpriftap lsqttgytga lqngittkkt
      781 gwevslnatp vstssgfswt tmvnwstyke vytkfygdlt qldiytkigd rvdkfigsaf
      841 vktpdgkiin daggrpirnp vsqvqgntnp dwvwsfintl sfknfrfgfq fdgrvggkmv
      901 nyiqqqtyrg grhintvqgk mgearlqdyk gvkswvgegv visngtaiey dnlgnvtnyg
      961 klqyamnttp tylqdyisfy yntneanlid ktfaklrevt ltytvpqnil gksfmkqasi
     1021 slvgrnllyf skykdvdidq yagsqgsssl qtptakrygv ninivf
//
LOCUS       WP_119053316             976 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053316
VERSION     WP_119053316.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..976
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104612
     Region          27..952
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqflkqall vfmtaalpvl lwaqvavtgt vtdasgktip gasirlknsn lgtssdangk
       61 fsftipgtgg tleisaisfk sqtlqvsaan sslsiqladd vgkldevivt glatsvkrrn
      121 lanavatiss kelsgtapaq tfdaalngki tgayinansg apgggisvkl rgvtsvfgnt
      181 qplyvvdgvf idntatsagl tfvtgavrna atsnqdnpss rvadlraddi enieilkgas
      241 aaaiygskaa agvvlittkr gkqgktkisf aqdigfvkvr kllgtrslts kivadqgwdv
      301 aeynaavaag kiydyekdiy getgltrnts vsvtggtdkt sfyfsasqkn edgivkntgf
      361 rsnslrlnvd hrisdnikig istnyinssa drgitnndnn svsygvalss tpsftelhpd
      421 angnfprnky gasnpletia lasnnegvnr fitginidai fqksassttr figrggvdfy
      481 nlktfalfpn tlqfqeineg tvaqgfaksl ssnlilsvvn nftpstnlsl ttsagitqen
      541 gnfdnilnia thlvggqsnv nmagaltaiq lrnknqdngi fvqeeasiad avmltagirf
      601 drstnngdpd kyfiypkagl swnltrmgfw ngnlfdnlki raaygqagnf pvfgskfnsm
      661 vvantggllg tlvstirgnt gikpertael eagldfsvln srlnfeltfy nktitgfllq
      721 rpvagssgfs tqwinagdlr nrgieisvna qpiatrdvrw tttvnfwmnr skvtkldvdp
      781 vevgafstgl gifriekgat atqivgkdga ngthklgdte pkfqmnffne vtflknfslr
      841 fllhwkykgd nlnlsefltd lggtspdfdk dddgngvvng vqrvndylag sarnfvqeag
      901 ylrlrevgly ytfinmpasf ikglrlgisa nnyftktnyr nydpevsnfg tgfssnvdvm
      961 pfpaskratf hlavdf
//
LOCUS       WP_119053715            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053715
VERSION     WP_119053715.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115428
     Region          23..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilsllta lvmcavmahg qtrtvtgqvk dskgdpipfa sikikgsnsg saadangnfs
       61 itaqqgailv isasgytdge skvtatgain vslrnaeamq evvvtamgvs rskrsvgvav
      121 qeiqadkltq tkqvdlntal agriagvqvl ggsgakfgts tvrirgvntl gtgnplyvvn
      181 gvptdgrdin mddvesvsvl kgpaatslyg qrgsegvivi ttkkgkrnag iglefnqstt
      241 ferlatlpky qneygggysq dwytfkynpa tdapalqamd gakyydyfad eswgprmdgs
      301 lyapwyawds edpdyakqkp fvaqpdnird fyntgvaynt nvafskatdn sntrvsftnl
      361 artgitpnsr qsknwlsinn sidltkqfti ntninyvyey lfnvpaegyg tqtsgsfnqw
      421 fqrnleiakl krykrsdgsy tswningprd tspkywdnpy tevyenltnn krqrvygnig
      481 gtykfnshlr asilaradvy nqnynsrvas ntlnldayrt ytnntrelnf vgsveydnef
      541 gdfslragay aekrtnysny vneatagglt ipgyyniaas knrpttnnte nrkevrsvyg
      601 ytslgwrnmv fldlnlrndw ssalpqgnns ylyggvatsf vftellpend ilsfgkvras
      661 farvgsdida yniyqtytvg tpydtyptlt vpnsipnsvl kptlstsyev gtelrflknr
      721 vrfdfnyysr eakdqiinlt ipsttgysaa lvnagnianh gveislggtp vrtkeftwdi
      781 dfnigfnrne vkklymdskn lvvnpagqgs sfgfvgspsi svnarvgesy gvlvgdgykr
      841 neagkilvdd dgyplieqnk elgsilpdyt ggvyneftyk gftlgfsidf qkggklmslt
      901 smqnagsgls nitvgnndkg ipkrndvadg ggvrvdgvre sdgkpndvyl dtkeyyesvl
      961 snlweqwvyd atfvklrevr igynlpkrwy qklaiqnanf siiaqnpwli yskvkgidps
     1021 qlqtpwfdsg qlpgtrtlgf nlklqf
//
LOCUS       WP_119053717            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053717
VERSION     WP_119053717.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118669
     Region          23..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkfltllav lvlytvlaya qtktvtgkit delgdpipfa tvvikgtkva fvsdasgsfs
       61 akvkqgdilv vsaqslttke vtvgasnvva itlaknnnal aevvvtgayn tkktqrstsy
      121 naqvvsneql nvirqtnlng alagkvsglq frgqstaklg nvgnvrlrga sglggdegvi
      181 yvvdgtilps andiniddie dvtvlqgpaa aaqfgsqgan gaivislkka kknakgigvd
      241 lntgaqfeqv yilpnyqnty agggnadltq yvwkpgqpda wkaldgkyyh nysddaswgp
      301 rmvgqeyipw yawyegtpys fktaklnpqp dngkdyfqta siynnsisfs katdnmnlrv
      361 sygnidvkgi lpsswlkkht lnvnaamdln qhftlsanvn yisqkrqgdf ddgysnqstg
      421 sfnqwfhrdl dmgimkelrg lrtpegiyas wnhndptsyk sddpsafyag nywynfytwa
      481 dlvrnndgld rlygdvslty kinndlrirg tyrkqqnttw geskyssnll tsgtqttgnc
      541 peckgfygts esysnrenle vmasyskkln dfqfginagt dffrwisksn sastvdglnv
      601 pdlfnvsnsk grptigngrt eekykailvk gdigwrnmlf gdftlrndwf stlppdnndv
      661 lsksfgvsfv fsdllkvpal sygkiraswg eipqalgats ttfgayrypg fefgvganpw
      721 gsnflmstpn elvdsairga vkaqkeigld lkflnnrigi gvtywdgtek niprsvpvng
      781 asgftsilin tgeitkkgid vqfnarpfwl pnfkwevnat wgrllenkvv kiadqvkris
      841 veglwgttgp ilvheegkew gqifgsgikr ingqpvlddd gfyvaqaetf ygnvlpkytg
      901 giqnnfeiyk nftvnvnidy qkggkffsls dmwgsysglt artaavndkg npirdavadg
      961 ggmhifgvdk dgkpvdhyve aqdyyhnmyn nrtfdefvyd ltyvklrels igyniplkkl
     1021 gidkwinran fsivarnlll iyaetkdfdp seisslsgea gnlpgtrgig fnlrvgf
//
LOCUS       WP_119053720            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053720
VERSION     WP_119053720.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117166
     Region          23..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkilsllav lvvialpals qsrkvtgkvt dakgipipfa tirikgkttg ssadqngtfi
       61 ieaspsdvlv itaagydaqe lavgnnltlt aglqsnksld evivtaqgir rrpkelgysv
      121 arvtneditv grspqiaqsl sgkvsglaif nvnnsvdpav kivlrgyrsm tgnndalvvi
      181 dglpmppgsa tmlnllnpnd iesisilkgg qaatlygsdg vngalvittk kgskgkmkvt
      241 ysnatnieqi sflpeyqdky gsgshyaagf gtgawkpnyl drmkdnwrsy enqqfgdqyd
      301 gsmrpvgrvl edgsfyelpy saiagerrri wntglttnnq vsfsggndnt tfymslennl
      361 aqgvvpedks rrtgvrlsaa hesgrlkagf nlayvqanyd rttfdfynet inqaahipls
      421 klrdwrnnkf aspnayyndy ftnpyfrldn drtkygdani tgnvelnyki fswmnlynkl
      481 gilnntrsqk ntvakysysa waktkayvpd pwdqddgegi trtgtdiags vydmnaveni
      541 vnnefqvqmn kdfgdwsfks vlgfslydrk tktvevssgs ivvpgvnnva nrqgelggge
      601 gnteyrkygy yadlltgwkd lvfihgtfrl dgtskfyken rstslyqypy ygvdistnlt
      661 dlipglqtgv ldyaklragy sknvadnipl ygldltypna ggfpygntvg ltvgdvlpdn
      721 nlkpekvnsf evggefqlfn nrvnldftyy tqtttdqvit vkipnstgyn nlrlnvgksr
      781 nwgyetdlkv qiirnqnfnw dfsvrysqnd nkvielypgv ndfllsgysy agsyvinkea
      841 fpsikaisyv rdeasgrviv nkttgypsqg plknlgralp khilgwgtka gykdftlavn
      901 feyrggnviy sdlgrqmtft gsggwtadra phvfpnsayd dgtgkfvpnn nvnvaeaeys
      961 lwvdyyrlia enftvpgwfi klrdinlsyn fpaafiaktk vfagasisly grnlitivds
     1021 kndftdpeys fttgnglgin ntsqtppvrq yginvnltfk
//
LOCUS       WP_119053762            1147 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053762
VERSION     WP_119053762.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1147)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1147)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1147)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1147
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1147
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125918
     Region          113..1143
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 menvklktpf sflvllltag llqaqssqlr frhgagnlak vvedfgkqfk aqlayaneel
       61 aafrvtagsy eaptvgdlln kvlapanfka tasgsswiir ksetprqqta nmvlqgiite
      121 gdnpvpsatv iikqagqgtt iavadekgaf skklplaegt vdisavgylp skkkfaaseq
      181 qllkidlikd etqmqnvvvt algikraera lgyatttvdg kqltdamsgn wtdalsgkva
      241 glnlvrsnag ptgtnkiilr gennltgdne alivvdgvvi nngsgrrsai ageetygtgs
      301 dnmpadygsg lndinpedie svtvlkgpga aalygqraan gavvittksg snkrkglgit
      361 fssnvaweqv nrwpdlqwey gigldgqady dygrsansss ssaygprfdg qkffqynngl
      421 qgrdtiatpw vpyknklref fdvgntitnt isvdggtdkt tarfsvtnvt nkwiipntgy
      481 krntvslsvn skvndrlqvs skinytnkws dnlpgagygn qsimywyifw qpnadidwlk
      541 nywvkgqegr kifypyssfp enpyaivnef instnrhgvt gnvqatynft kelsmmlrts
      601 mdfgydqraq erpfdagsky rygsyrtqni fsmessadfl lkytkriqkd fefsitgggs
      661 tlkntytrde tradslidpg nytfanaagp litlpykskv vinsfygilt tsykdflyld
      721 itgrqdwnsa latpqrtent gffypsanls fvaseafklp kdisflklrf sasnvgsaqm
      781 ipyrtafyys sagslygggl enpgalnnpn lkplrtitye agvamkmfrd rlsvdlavys
      841 gytkdqilnr qldrasgnqy avinigkvan kgielalngt pitskegfkw ttgivfsant
      901 nivkelpdss ivlqngpvgg gqivakvggs mgdmygrgyv rspdgqvvyd aqsgvalisq
      961 dvtylgntip kwkigftnef sykqfrlnll fdaqygavgh slmnyklaeq gkttktlpgr
     1021 ysgiigngvv mgpdskyrkn dvvamdidey yrshfgtdna egntfrtdyi kfrearldyn
     1081 fkpnlvrklg lqratlgvyg rnlfiwsdwp mfdpefgtll gsdivqgfei aqfpstrsfg
     1141 fnlvvgf
//
LOCUS       WP_119053779            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053779
VERSION     WP_119053779.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114742
     Region          23..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnriialwai iivlpaslaa qtrivqgtvl drsnnlplpg vtiqagsaag ssttdakgsf
       61 tigitgkail tfsyvgyatl qiaadsiqdg egvlvkltps dnaldavvvt algvskqkks
      121 lgyatqelka kdiseakean ivnalagkva gvritntqgd mgssrivirg etsiagnnqp
      181 lfivdgipvd nsqlgaggsr dyrnaiadln sedietisvl kgpnaaalyg sraahgvili
      241 ktktgksrng igvtlnsntt fssvnilpdy qnvfgqgaeg kfsyvdgkgg gindgvdesw
      301 gpkldgrlip qfyskgvpvp fvahpnnvkd yfktgvllsn sialdgagdk ysyrisynne
      361 kqwgivpnse agknnlsfng sfdvtpklkv gvganyivnd apnlpgaggr ratstmlqft
      421 wfgrqvdinq lrdykdaagn tfnwnnsyys npfwvayent vsqrrnrfig nlnlsyqiid
      481 glsfnfrtgs dyyndkrksk iaygtngtpf gsyqetnyiv tennteatlr ynknissdfs
      541 ldiiaggnvr tktyeendqq aprlavanvy tltnsrdpli ssnyysklrt wssfasaqlg
      601 yknyafvnvt arndwsstlp qqnlsyfyps vnasvvlsda ldiksnvlsf lkvrggwskv
      661 gadadpyqli ntynfnapfn gnpqlntsgv dlnpnlrses tnstevgvea aflnsrirld
      721 lslyntnsid qilkvdvspt tgytqkllna gkinnkgiev qlgltpvkvk dfrwdidlny
      781 aanksklerl dnegnlqnyv lgsyrniqvl asvgkaygtl fgnayqrddk gnivvnnsgi
      841 plaspskkvl gkytpdwigg innsfsykqf nlsflidasi ggslfagtns tgsytgvlem
      901 tlpgrdadhg glyyyypgnd kskgtvglak gatppsgevv yedgmifkgv ntagnanavi
      961 ipasqyykaa rnieeefvys asyvkfrelk fgytlplgwi rklgltgatv slvgrnlwii
     1021 hkdvpnidpe taftngnaqg ledltlpttr sygfninvkf
//
LOCUS       WP_119053808            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053808
VERSION     WP_119053808.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117922
     Region          25..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlclplvma llaictqtys qslsirgivt deakkpmqgv sivqkgtstg tstkadgsfs
       61 lnvtgdnpil vishsgfark eipvsastpl lqitllpiae nmdevvvvsa lgltrkaksv
      121 tyssqsvdad rlteardvni vnglmgkvag lqvtttgqpg sssrvvirge gsitgnnqpl
      181 wvvdgvpian nisernnldy gntaadlnpd diesievlkg pnaaalygsm aangailvtt
      241 kkgkpgdksl gisvnqnmmw ytitefpayq nvygegsggr lvgganqlfp gtggintgty
      301 drswgapmlg qpyndfsgkp lpggyspqpn nvtdfykssl tntsnialsk sdavssfrls
      361 ytytksddvl qnqnkrdkhn lnlyatrklg nkvtidarll ytmddmknrt yrnlnpsspm
      421 sayvylprst nlaaltpwkd angnapglga fgtvenpywm lyenenrdtr nryiggvtat
      481 velakglrfr gqatgdigtf lgyeyrelgs lrqkdgffsn rmqdernwnf eamlqynrkf
      541 gpdftvtana atniatynsv ireafmdrll vhdkpsihna nttprasesl vrrqvgsvyg
      601 natvgyknfl yldvtaradk sstlpaggnt yfypsaglsf ifsdfiknkd lisygkvras
      661 warvgnsapp nslttnwsng glflgnptfn ystrlnnyel kpeqtvsrei gielglfkqr
      721 vnltatvyqs nstnqiitan tptesgfqqr vvnagemrnk gieltasvnv irkknfswdi
      781 ranwskndnl vmslvdgvpt lnlgsnlgat inavvgkpyg vimgtipyyv gdtmlvqasg
      841 rlypdvnkyv gvyrpdwlgs igstlrykaf dlsflvnvkw ggslysasyg rgnfngntie
      901 slegreewff snyilgengd ermgigqqvg tirvpyaddr kkgrkyavsy fplldannva
      961 ildkngrmqv gkpnnvwsep allsgdytln nteyltydas airltelvfg ytvpnkvfkn
     1021 gfikgvraal vgrnlwliyr ntprgidpes antsgnaqgi esggsfpyaq ygfdvkvnf
//
LOCUS       WP_119053819            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053819
VERSION     WP_119053819.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113230
     Region          42..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqncntrrha yarlrmtrll rimrmttill ltgalhataq ningtvlddk napvegasiv
       61 ltpgdkgtmt nkdgkftysq lapgtyslea sfvgfesqtk vvtvngtgta tvtfnlkvsd
      121 tkteaavvvt afgvtaqkrs lgyslqevka qaiteshqpn lvnalqgkva gvqitnsgga
      181 pgassimlir ggtslssnnq plyvidgipm dnstaisqgt nlqgqsapps nraidinped
      241 iasvtvlkgp aaaalyglra asgaviittk rgvsgksvis ysgtasfdhv nrlpdlqsty
      301 kqgeqgvynp aaigswgptf spgetiydnl gnffksgftq rhdvsfsggn drttfyasgs
      361 yfdqdgivkn tdftrksfri sadtklsdkf kvggnasyah tdrryvlqgk gagdgttgtt
      421 tsgggtmlgv ifwprnddmr nylnadgtqr tiigtdnpyw giqnnpisdk vdrfifvgsa
      481 iydpfkflnv tyrlgtdyyt dnfssiraag ttipgeekga isqssrnsqi ttstllvtgk
      541 hsikdinlsl tlgnnievfk sttgfsygrn finptfpsin ntntndrnvs qsiqqrrivg
      601 lfgdlsadwk givylnvrgr ndwsstlpvd arsffypafs tsvvvtdlld elgakvtgkv
      661 lsygkirasw arvgkdapph vlattlsnvt ntftinprgf ilnsndyfgn pslrpeftns
      721 lelggevrff dnrlgvdfty yrtlsddqil atrtppssgs flaylnggsi rnkgvelmin
      781 gtpikqkdft wqvdlnvakn tatveslpga ldrvelsdaw aagnvaqgaa flygslfgin
      841 gnvwkrnasg qllltnagyp qvqstyqnig drnpdwvggi tntftyknfs lafmwdvrvg
      901 gdiynateny lvrsglsmkt lnrgstmvfd giiessgakn tqpvlldqny yqtlypfngy
      961 dfvedgswyr mryatltysl pkkllgktpf tnafisvtgr nlivitnysg vdpevsgsga
     1021 gvggsgsfgf dnlgipatrg vdislkitl
//
LOCUS       WP_119053897             949 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119053897
VERSION     WP_119053897.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..949
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104074
     Region          57..948
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyknislac vvllcgftas qaqstnaslp dtialfakpa griidqglra eqswrttgai
       61 ftitgeelar tnagnllntl qgripgltvt tgagepgydn ptlymrgqss wniagnaiai
      121 yldgfqvdln alsalspfei esisllkdaa alaiygfdgg agvlsvrtke gttagktkie
      181 vnarygnlrp ismpkvmday gyttaynkal qndglpikyy npelykakdd pfhpnvnwyd
      241 kilnnssatq dynisfrggn skarffvlgg ytdfsgaykd adaidqdfgt nakyrrlnlr
      301 anvnvqatkn lsikatvsgv sedrstpagf tasslfsnll ripaaafpvk nlngtwgnna
      361 vynfnpvqll rqngiynsht rsiqtnvsft qkldalvkgl slnggisysn lyigiyekrf
      421 tvpsfeatkd aydnpvidgt gnvvykvlga vsqgitdegn dhwnrnsiql gfnydrsfgk
      481 htftgmlqvn rsnythdgqf ypvvkegvrg avtydydqky iadlsfsyag sgdfkagdry
      541 gvfpalglgw iaskeaflan nkvinflkvr asygltantn eayrflferw gitapgitlg
      601 ttnsgfggrt egdypnadft weekstanig vdltilekln atidvfrekr tgileapvgv
      661 paytgfnlrn tnsgeavnsg vevslqyrdk tkssleyyag vtfayahnei tkraqdaqpf
      721 dylyqkgyri nqfralqnag fyqvsdfean gnlkagvaks tygqvrpgdl kyvdinsdgi
      781 indydktplk ftklpeitlg fnigvkyagf didafvqgvm nrtvslldda feythplann
      841 nnitafsnnp wtpetassat aprlstlvna nnnqqaefwl rngnfvklrs velgytlpak
      901 gflkkfevlr lyvsgnnlls tkiegleper lsmgyplmkt vtlgakvkf
//
LOCUS       WP_119054535            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Paraflavitalea
            soli].
ACCESSION   WP_119054535
VERSION     WP_119054535.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113355
     Region          23..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkaaslail ffvlcatgla qnitvrghvr sgtdstvitm asvvvkgask gtttnaeglf
       61 tisaapnavl vfsslgfvqq eialngrsti dlylqqsegt qlnevvvtta lgikkrqqal
      121 gysvqevsge tmakvksata vgaltgkvag lnvlnttdlf qnpgislrgr tplividgip
      181 dpnadpykln addiesisvl kgtaagalyg algvngaily ttkkgkkgkl nvevnsstmf
      241 qtgytkvpkv qtqygngdag kyayvngsgn gtegggwiwg pkldqrdptt psgfyettqy
      301 nspvdpntgk lvplpwvsrg rdniknyfrt gilstnsvsa sigtdkgsfr vsashinqkg
      361 vvpntgvnns sfsiggnyml tsklsvdakl tfnkeysnny ptvgygppni lynlllwigp
      421 didirdlkky wlpgkeglqq rnynlswynn pyfvanelln gykrdnnfgq vsfdyqfnkd
      481 fsaklrtgfn qfatfkdvke pysyiaydyi skgnyattqa nyfdlttdli lnykhefsdk
      541 fnlsvtagga ntyrneksvy astdgltipg fynltnsinp avtsnylrer rtasaygmvd
      601 ietlgflyln ftgrydktst lpvknngyfy psagvsavls dvlkmpsavs flklraswak
      661 vntgfigdgg dpyahittys ignkwnnvps lawpttaisp dlvpatvqsg eygivasflk
      721 nrisvdatff rnrdynnfvn vpqsqssgit svlknaneyi rrgwefvvsg vpvknkrfrw
      781 etainfssvh rwlkdatdsp dgyignikeg drtdrifisa artpdgqaiy nsngmqatsp
      841 yaqyfgnddp dwiygwqntf syknlsltfs vdgrlggliy sttnqkmwwg gtapgtvtqy
      901 rddanagknt yvgpgvvves gtvqydshgn itsdtrkfap nttpvnyisf mqttsgqmln
      961 nyfyysgtyl kmrevvltyn lpakitrgif saasvsfign nlfllaklpn vdpdaesdnl
     1021 qtpsmrsmgv ninlkf
//
LOCUS       WP_119054712             369 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraflavitalea soli].
ACCESSION   WP_119054712
VERSION     WP_119054712.1
KEYWORDS    RefSeq.
SOURCE      Paraflavitalea soli
  ORGANISM  Paraflavitalea soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Paraflavitalea.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Paraflavitalea soli"
                     /db_xref="taxon:2315862"
     Protein         1..369
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39342
     Region          1..359
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,89,284,310,312)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,122..123,132..133,136..137,140..141,143..144,
                     146..151,153,155..157,160,183..184,274..275,317..318,322,
                     325..326)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(117..118,122,125,128,169..172,192..194,224,235,
                     252..254,261,263)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,122,132,175..176,183,199..200,202..205)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(152..156,159,162,185,187)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtigilkess aetrvsllpe avatltkkgi tvlveqgage taysndqeyt kagaqirnrq
       61 ellqssdmil aihqfpeags lsskiiigvy qplfhtalmq dwakqgvtaf sldmlprttr
      121 aqsmdvlssq aniagykavl laansygryf pmfmtaagsi apakililga gvaglqaiat
      181 arrlgavvev fdtrpavkee vmslgakfve vegaadaska ggyaveqsee ykqrqqqkit
      241 esiakadiiv ttaqipgkka pilitepmla nmrngsvivd laaatggntp ftknnetvay
      301 ngvriignsn lpatmpsdss klygknilnf lqliinkega ihlnwdddlv kgacithnge
      361 vvnervknt
//
LOCUS       WP_119057174             992 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Candidatus
            Ornithobacterium hominis].
ACCESSION   WP_119057174
VERSION     WP_119057174.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Ornithobacterium hominis
  ORGANISM  Candidatus Ornithobacterium hominis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Ornithobacterium.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Candidatus Ornithobacterium hominis"
                     /db_xref="taxon:2497989"
     Protein         1..992
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111282
     Region          25..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknvkklls vaafvfavhs ygqekvvtgq vldadgfpvq dayvyvegki dgvytdqdgn
       61 ysimaekgdk vmieyigket ktisitdkne yvvrltgqga valkevvvmg ygsardvasv
      121 asnvsvvsgd vvdkrpsana ldalqgqvsg lqiytstgep saassirlhg igsiggsnsp
      181 lfildgvqvd sgimnklnps dienisvlkd aaatsiygsr aangvvyitt krgktgegsl
      241 tvgvqqgfst ladtsffdgl fdakglaefw vdtkyrtqaq vdelrkkyph ntnwrkvyyk
      301 eytpmlqvnt sfaggadkar yyisgsyvdq egpsyrsglk rynlrsnidg klnnwlslgl
      361 nvsmayskyn qngwrsnnsn gslswfaqpf yspvdengke yaripgwnry hphylanknp
      421 sdhrqvqint sgyvelnpfk nltlrsqggv qlyvkkhdyk rlpsylgsln dgeamtnvtn
      481 yvmktitnta eykfklgdrh nfialagqey ndynfeeveg eggglnndrl tllgqttknk
      541 kvdqnrseya yssffgrley dfdkkyylna slrrdgssrf gkenrfanfw saglmwkvkk
      601 eqflddvnwl sdltvklstg tsgnslmgly dyqgnyesla lvkssqyngn pgyrlseagn
      661 palswekqtl stltldmefy krvglelsfy nrvtkdlifn vptafttgfs synqnvgklq
      721 nrgidvtfna sviktkdyhi rpyvnfnynq dkilgifqdr khwiipntgv gyvvgqsiny
      781 lypifkginn qtglaewylp yggekkvsqi rkdenavttt fsestleqnt gkkrytpmtg
      841 gfglsagykn fslqsdfsfa lgknlinndk ffaenpsift gynqsstvkd ywkkpgdvtr
      901 fpkygeqftr fdsrliedas fmrlknitla ydlpnsltdr vkflnggriy itgrnlwtlt
      961 kysgldpevd snialgrnpn tkqyvfgfel kf
//
LOCUS       WP_119057234            1017 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Candidatus
            Ornithobacterium hominis].
ACCESSION   WP_119057234
VERSION     WP_119057234.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Ornithobacterium hominis
  ORGANISM  Candidatus Ornithobacterium hominis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Ornithobacterium.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Candidatus Ornithobacterium hominis"
                     /db_xref="taxon:2497989"
     Protein         1..1017
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112471
     Region          120..1012
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktcmtlml aflvcqtpgy gqvnerniny eisapvslae flsslqvqtg vkinfnaadl
       61 kdfqieqvsf snssiediad ylmenytlnv elangemyvs dlfgesiygt gnqvdlstlv
      121 vtalgikree ralsynvqei kseeltrvkd anfmntltgk vagvqinqss agiggatkvv
      181 mrgakslvgd nnvlyvvdgm pminpsraas grfasqggge sisdfnpedi esisvltgps
      241 aaalygasaa ngvilittkk gkdgrmklnl ssttefyrpf ilpefqntyg napgsdrswg
      301 dklatpstfd pkdffqtgmn qtysaslsvg teknqtyfsv atttaegiip nngyyrrnft
      361 arntanfldd klhldvsgsy imqgdqnmis eggyfnplts lylfprgddf ntikayeryn
      421 parginevyw pynvkrklft aenpywivnr eltqshknry mfnsslkydf adwinitgrv
      481 rvdniynkie rkyyastdkl ftnsdkgyys aseekniqty adlmlnvnkk indfnlvani
      541 gtsyddrvge sigiggslnl ipnlfsaanl dpkksgvggq shrqtrnial fgsaelgykn
      601 mlyltltgrn dwasqlvnsk epsifypsvg lssivskmld lpkvisflkv rgsytevgsp
      661 itqlgvtpgt itydlspsag ltprstypfp dfkaertksy egglelkmfk nklnfdltly
      721 rsntynqtfl sslppssgys gfyvqagnvq negielalgl dqswndfswf tnftytrnvn
      781 likelvrgyt npvdgskfdl telyingali keggsmgdiy tegilrrdas gkliegnsgl
      841 feidrkqrik igkstpdftm gwnnqfgykg fnlsfvvtgn fggivnsgtq avldaygvsk
      901 ataeardkgg vtidghtyda ekyystigge elmgyytyda tnvrlqeasl gyafkgdlfn
      961 nvinkltisl vgrnlwmiyn kapfdpqsta stgtyrstef fmtpslrsfg inakidf
//
LOCUS       WP_119057532            1121 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Candidatus
            Ornithobacterium hominis].
ACCESSION   WP_119057532
VERSION     WP_119057532.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Ornithobacterium hominis
  ORGANISM  Candidatus Ornithobacterium hominis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Ornithobacterium.
REFERENCE   1  (residues 1 to 1121)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1121)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1121)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1121
                     /organism="Candidatus Ornithobacterium hominis"
                     /db_xref="taxon:2497989"
     Protein         1..1121
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125430
     Region          42..1119
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknrlklys lslilssgfs waalpvlsen qsfkihqqgl vkditgrvld edgnpiagve
       61 iqnktskitv vsdkqgyfll avgiddkiqf skagyftdfk vvddfnslei tlvrmsdgli
      121 ddevllsdvv vtgyqklnvn kaagsfdkid menferrgss niidalegls pglvlstnps
      181 apssskelti rgistlsgsa rplivvdgfq yegdlsginp yevksinllk daaassiyga
      241 kaangvivie tkkgrksgtq irytsnltfk ekvdigyvmn rvnsselvei qsqiakqeva
      301 ngsiinyrna fetnkpnatn rvgannnvyq lysdlhygyi tatefdsklq alknldntkd
      361 ledvylqnpl tnqqnisvlg gnefityrts lnytdeflni knyknnrilf dfvsdvnftq
      421 klnfnfqsnl slnryssnpl nfantnsftd ifnissydrl ldehrnplsv tkpayrnidn
      481 gifggkdaye iqrlinagll detyypaldf kryayhnddw svriqgllny dltrdvtlrl
      541 ggkiqkkalk tanlahadsw ymrhlvnnft plsytgdkad liipiggrlq etrgeetsyl
      601 lrgqldfdkt lgnhyvnilv gseiqtnqae ststdrlgyd ansnlflpvn yynfynnqfe
      661 kiympggnay rnglvfdnsf gssenrffsl yanaqyvygn kyiltastri dqsnlfgtdp
      721 ayrykpfwsv gakwrageea flkenavnld lrvsygfngn iannvgpfdi ahkayvqrvg
      781 nlmglslash stpnlrweqt gtfnfgldtd fwknrlnlsl dyyrkhskdi lsnvqidptl
      841 gtgnamrnda siinngyeig lrtknvltnk fswetqlnfr ynkgkvkevy fneahayrya
      901 gsimnlkgga pnalyvtnfa glnsegiaql rqasgklvni dtktdvnvfn iedlveagss
      961 lpihvaglnn nlrwnnfals flfiyqgghk llkdtyngei lsrnvnlvha dvakawqkpg
     1021 delvtdipar ssvvysnlla gssknvidgd firlrdvvls ytlpqnysss iglqeltlnv
     1081 rgsdlwlwak nnegidpetq glgvrtspvq ksftlglnli f
//
LOCUS       WP_119057898            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Candidatus
            Ornithobacterium hominis].
ACCESSION   WP_119057898
VERSION     WP_119057898.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Ornithobacterium hominis
  ORGANISM  Candidatus Ornithobacterium hominis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Ornithobacterium.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Candidatus Ornithobacterium hominis"
                     /db_xref="taxon:2497989"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119529
     Region          100..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvfaqveemp vsvrvnhtks lsqflddlqd efaliilynp eeiseirveq lnvkdrslkd
       61 lfdllannyg ikysfqndli nvfgpnetvk eslinsgsin lnevvatgys nqrrntlats
      121 vskldtkvle naprgnaata lqgaiaglkv tqntgqpgst psitlrggtd fngggsplil
      181 idnvpgsfya lnaddiesie vlkdaaasai ygaraangvi lvttkkgkag kssisvksry
      241 tinkraeskm kymnaadfik fnrmaisayr dqidpngfts yiegqypagt gnnpydsrft
      301 tmvltdknky llnfdgwqti qdplnpsqql ifqenkmsel fyqpsygqdy nisfsggner
      361 gtyylslghl dekglvfgsk fkrisanfng syklsdkfkv sssilyghsn ntpnylgndy
      421 fvfqraagqp ptariynnnp dgslssdlqp gisydfgnpl yygdkfirkn leqrltanlq
      481 fdyqflphfn lmlrgghftv nnrnerfnka ylnggrfida rnasashgqn frnqitsvls
      541 yqnkfgkhnl nlllgleyfr dnswemkaat knspidliyt mnvaseadgv pststteyai
      601 nskfgqlnyd fdnryllglt frhdgtsrla pgnkyeffpg islgwnlqne tffkesllnn
      661 vintikprls ygvngnievl gnfsvfgayt nsgiynsksg flntslpnyg lkweksatln
      721 fgldlglmnn risliadyfi rdvqdklsdl nlpvwtgfns ikvnngilqn rgleielsad
      781 lirnkdfkwn lsgtyyqvrn yakklpengl drnrqggvqi ynpltgkvey vaglqegkrv
      841 gldvvtayvf dgvyktqadi dahagrvvkf arnpntrflg dtkyldlngd niidyrdrki
      901 lgrttptfsg glssnlnykn lnlfvktdfa mghlvtnlnr vrgitqvqga qngpqeivns
      961 wtpsnsdsni prfvftdpqg nhkggngeny ydsnsiywek gdylaireit lsydldvski
     1021 nnaigglrlf ltgsnlhyft kysgnspeng gldygrfplp raytvglslt f
//
LOCUS       WP_119057902            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Candidatus
            Ornithobacterium hominis].
ACCESSION   WP_119057902
VERSION     WP_119057902.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Ornithobacterium hominis
  ORGANISM  Candidatus Ornithobacterium hominis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Ornithobacterium.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Candidatus Ornithobacterium hominis"
                     /db_xref="taxon:2497989"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125498
     Region          21..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklslplfa iaavsafaqe rtitgqvmde ngfpiagasv fihssviske vaepnirnna
       61 vgtitdvdgn yrlnipknls qisisydgfe tetisispqk nnynviltsy fakgqlnlkd
      121 lvvtgyqkid pnkvtsavat vqmesiqqkg vavvdqmleg qiagvnlqns tgragelgni
      181 qirgistlrg vsdplwvvdd iplegnntpd lsdknnlddl rsysiaginp ediekitvlk
      241 dasatsiyga raangvivvt tkkgkkgkln inlssntfvn frpdaerinl mnsqqkvdfe
      301 lelakrkdln yrsnngiiar llqkegflea yqngealpss ivsqldvlrs nnldwwkely
      361 qtsinhqhta sasgggdlhn fyislayyde qgalkgtdyd rlnitlknnf klneklsigi
      421 nlfgasisqs syltdqgsft npnnylrnvn pyqliyddng nyaydeniny iaknnadfvk
      481 fniieerqnt rnqlnslqlk gnfdlnyeif kglnyrslfg iqlerngnek wasedsyfsr
      541 iyragtryfa ngkqnywlps ggilqnfdtn nfhylwrnnl ewqkslgahd vnllagmeir
      601 kenttftntk afgyndktnq ptpivfrnqt datnslyeay kkielenaya sffgtasyty
      661 drrytvfgsl rydgsnlfgv dpkyrylpiw svsgawnihn erfmeylksi stlklrasyg
      721 fqgnidktts piviaqhqra avlpgasedv lrvtsppnak lrwektenig agaelglfhn
      781 rinliidyye rnstnlitps rlpletgfaq tmvnfgaikn qgweftlnta nidtknfhws
      841 ssfnisknkn ivkkvefntk nlnfpsgeay pvdaiwlird agldsngapq fynengeivs
      901 avdfyqlsdp waafypsfmv esglsvdqrr aqyqyggsrs pkwfgglanh fryknwdlni
      961 nssfvlgrka lanpaynfta vdpgvnytrd ilnawkpnnk ttknpriigq ktipdglvyn
     1021 wfnsgddfnt ylafqsrvke lnyfrinsir lgysipseyl knmgirnfkl svegrnlfvf
     1081 sngysgyfdp etygniyasp iqksitfgls lnf
//
LOCUS       WP_119059074            1121 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Candidatus
            Ornithobacterium hominis].
ACCESSION   WP_119059074
VERSION     WP_119059074.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Ornithobacterium hominis
  ORGANISM  Candidatus Ornithobacterium hominis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Ornithobacterium.
REFERENCE   1  (residues 1 to 1121)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1121)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1121)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1121
                     /organism="Candidatus Ornithobacterium hominis"
                     /db_xref="taxon:2497989"
     Protein         1..1121
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125564
     Region          42..1119
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknrlklys lslilssgfs waalpvlsen qsfkihqqgl vkditgrvld edgnpiagve
       61 iqnktskitv vsdkqgyfll avgiddkiqf skagyftdfk viddfnslei tlvrmsdgli
      121 ddevllsdvv vtgyqklnvn kaagsfdkid menferrgss niidalegls pglvlstnps
      181 apssskelti rgistlsgsa rplivvdgfq yegdlsginp yevksinllk daaassiyga
      241 kaangvivie tkkgrksgtq irytsnltfk ekvdigyvmn rvnsselvei qsqiakqeaa
      301 ngsiinyrna fetnkpnatn rvgtnnnvyq lysdlhygyi tatefdsklq alknldntkd
      361 ledvylqnpl tnqqnisvlg gnefityrts lnytdeflni knyknnrilf dfvsdvnftq
      421 klnfnfqsnl slnryssnpl nfantnsftd ifnissydrl ldehrnplsv tkpayrnidn
      481 gifggkdaye iqrlinagll detyypaldf kryayhnddw svrvqgllny dltrdvtlrl
      541 ggkiqkkalk tanlahadsw ymrhlvnnft plsytgdkad liipiggrlq etrgeetsyl
      601 lrgqldfdkt wgnhyvnilv gseiqtnqae ststdrlgyd ansnlflpvn yynfynnqfe
      661 kiympggnay rnglvfdnsf gssenrffsl yanaqyvygn kyiltastri dqsnlfgtdp
      721 ayrykpfwsv gakwrageea flkenavnld lrvsygfngn iannvgpfdi ahkayvqrvg
      781 nlmglslish stpnlrweqt gtfnfgldtd fwknrlnlsl dyyrkhskdi lsnvqidptl
      841 gtgnamrnda siinngyeig lrtknvltnk fswetqlnfr ynkgkvkevy fnethayrya
      901 gsimnlkgga pnalyvtnfa glnsegiaql rqasgklvni dtktdvnvfn iedlveagss
      961 lpihvaglnn nlrwnnfals flfiyqgghk llkdtyngei lsrnvslvha dvakawqkpg
     1021 delvtdipar ssviysnlla gssknvidgd firlrdvvls ytlpqnysss iglqeltlnv
     1081 rgsdlwlwak nnegidpetq glgvrtspvq ksftlglnli f
//
LOCUS       WP_119058182            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Candidatus
            Ornithobacterium hominis].
ACCESSION   WP_119058182
VERSION     WP_119058182.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Ornithobacterium hominis
  ORGANISM  Candidatus Ornithobacterium hominis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Ornithobacterium.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Candidatus Ornithobacterium hominis"
                     /db_xref="taxon:2497989"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124346
     Region          24..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrflfnlf lllcslsfvf aqertikgqv vdsngfplqe vfisvqgten svlsdengny
       61 siqakegdvi vfdyigfakk tekvgkstka mnvtlvnsni qelsevvttg itstdkrlft
      121 gasdrldass vkidglpdvs rglegrsagv tvqnvsgsfg sapkirvrga tsiygsskpl
      181 wvvdgvimed vvemnaddla sgdaltliss aiaglnpddi qsfeilkdgs atsiygaram
      241 agvivvttkr gsaglsnisy tgeftyrqip sysnfnimns qqqisvyeem rnagwlnysd
      301 lvnaresgiy gkmyellnkl dsngnfllan tpeskaaflr eaqyrntdwf kqlfnsnisq
      361 shsvslssgt ekstyyasls alvdpgwtls snvnrytanf nsnfkirdnl nlmvlssgsy
      421 rkqkapgtla qdvdivsgkv krdfdinpys falnssrtld pdkfytrnya pfnikhelne
      481 nyidinvadl kfqtelkwkp iksvetsllg aikyqstsqe hhvtefsnqa kayrampntt
      541 vrdnnpylyt npdnpyalpi svlpaggiys ktdhtmygyd mratasykne fnnihtvnfy
      601 lgaemnaadr krnnftgwgm qyslgenpfy iyelfkkgve ennlyyglyn skyrnlaffs
      661 natyswkkky tlnatlryeg tnklgksrsa rwlptwnisg awdvsrenff ddlyptvsdl
      721 ivkasyslta drgpasvtns lvdirssnyw kplseyregs lyinqlense ltyekkheln
      781 lglqtgfldn rimfnadwyk rnnydligvv ttqglggqiq kfgniadmks sglelslqtt
      841 niktddfrwd tsfiyskikn kvtnlktrar tidlvtsngf akeglpvrsi fsipfqglne
      901 eglptflnqn gettvtdiyf qerekldylv ysgnadptdv gsfgntfqyk gfklniftty
      961 sfgnvvrlnp vfsnsysdla alprdfenrw tvsgdekrtn ipvladkrmi naygsndlai
     1021 aynaynysts riasgdfirl kevslsydfs hnliknigfr nlslklqatn lfllyadkkl
     1081 kgqdpefins ggvalpvpkq ftltlragl
//
LOCUS       WP_119059273            1113 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Candidatus
            Ornithobacterium hominis].
ACCESSION   WP_119059273
VERSION     WP_119059273.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Ornithobacterium hominis
  ORGANISM  Candidatus Ornithobacterium hominis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Ornithobacterium.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Candidatus Ornithobacterium hominis"
                     /db_xref="taxon:2497989"
     Protein         1..1113
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125491
     Region          21..1112
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklslplfa iaavsafaqe rtitgqvmde ngfpiagasv fihssiiske vaepnirnna
       61 vgtitdvdgn yrlnipknls qisisydgfe tetisispqk nnynviltsy fakgqlnlkd
      121 lvvtgyqkid pnkvtsavat vqmesiqqkg vavvdqmleg qiagvnlqns tgragelgni
      181 qirgistlrg vsdplwvvdd iplegnntpd lsdknnlddl rsysiaginp ediekitvlk
      241 dasatsiyga raangvivvt tkkgkkgkln inlssntfvn frpdaerinl mnsqqkvdfe
      301 lelakrkdln yrsnngsiar llqkegflea yqngealpss ivsqldvlrs nnldwwkely
      361 qtsinhqhta sasgggdlhn fyislayyde qgalkgtdyd rlnitlknsf klneklsigi
      421 nlfgasisqs syltdqgsft npnnylrnvn pyqliyddng nyaydeniny iaknnadfvk
      481 fniieerqnt rnqlnslqlk gnfdlnyeif kglnyrslfg iqlerngnek wasedsyfsr
      541 iyragtryfa ngkqnywlps ggilqnfdtn nfhylwrnnl ewqkslgahd vnllagmeir
      601 kenttftntk afgyndktnq ptpivfrnqt datnslyeay kkielenaya sffgtasyty
      661 drrytvfgsl rydgsnlfgv dpkyrylpiw svsgawnihn erfmeylksi stlklrasyg
      721 fqgnidktts piviaqhqra avlpgasedv lrvtsppnak lrwektenig agvelglfhn
      781 rinliidyye rnstdlitps rlpletgfaq tmvnfgaikn qgweftlnta nidtknfhws
      841 ssfnisknkn ivkkvefntk nlnfpsgeay pvdaiwlird agldsngapq fynengeivs
      901 avdfyqlsdp waafypsfmv esglsvdqrr aqyqyggsrs pkwfgglanh fryknwdlsi
      961 nssfvlgrka lanpaynfta vdpgvnytrd ilntwkpnnk ttknpriigq ktipdglvyn
     1021 wfnsgddfnt ylafqsrvke lnyfrinsir lgysipseyl knmgirnfkl svegrnlfvf
     1081 sngysgyfdp etygniyasp iqksitfgls lnf
//
LOCUS       WP_119061384             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Dichotomicrobium thermohalophilum].
ACCESSION   WP_119061384
VERSION     WP_119061384.1
KEYWORDS    RefSeq.
SOURCE      Dichotomicrobium thermohalophilum
  ORGANISM  Dichotomicrobium thermohalophilum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Hyphomicrobiaceae; Dichotomicrobium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Dichotomicrobium thermohalophilum"
                     /db_xref="taxon:933063"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39977
     Region          2..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvriavpaee emeprvalsp etakkyvklg cqvviekgag arsyfpdhey enagaelads
       61 aeaalegadl vlkvgpptda qikamkngav vaamlepygp rgtidalaqq gvlafamelm
      121 prvtraqsmd vlssqsnlag ykavvdaaaa fgrampmmmt aagtvppakv fvmgagvagl
      181 qaiatarrlg gvvsatdvrp avkeqvkslg akfiavedee freaetaggy akemsdeykr
      241 kqneliaehi ksqdivitta lipgrpaprl isadmvktmk pgaiildmaa erggnceltr
      301 agedivhegi rimgpvnipg kvpgdassly arnlyaftel midsesgaik vdwddeiiqg
      361 taltrdgavi hpvltgeke
//
LOCUS       WP_119064270            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Phocaeicola
            vulgatus].
ACCESSION   WP_119064270
VERSION     WP_119064270.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121384
     Region          41..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkrlksvsm llflmgastg sayavanpgv tdvkitqqtg tckgvvvdat getvigasvv
       61 vkgttngtit gidgdfslsg vkqgdviqvs fvgyltqeik fkgeslkiil qedsqtlqev
      121 vvvgyggvqk aktmtasaat vkmselaklp vasmseglgg rvtgvvtqqa sgapgenari
      181 wirggenily viddvvmdsg qgneffnrlr pddiasmsil kdaaatavyg praangvvvi
      241 atkrgqegap titlnqkvsi mtpayrpkgl ssyeyalarn eaelasfqes ptfndtelsk
      301 yymgdlwqkg ygfeeirnlv nerynlgysl qdindlfdpl ktqgkniqdy yssydpwdmf
      361 dhtqpmyqtn vslrgggeri kyysslgymk qngvndkysy eqvnmilntd amllsdkslk
      421 ftfnlngnts nnnkpadgeg vfnnamygdw mpkrpaawst glprkgsvea qlnngfnnte
      481 syrfqmnaal kwsvpwvegl saqaslnftt syyhqrhfnh dqegvydnpy atavssynpe
      541 nanlyekwnk yklltgifqi dytrsfgkhn lsamvnyqsq vrksnwtdak kkgypttlap
      601 qldlggtlvs aggsaeewgs asyigrftyd ydnkylfqys anyngslsys pdkrwgyfqa
      661 fslgwvmsde vwfknlvnpn ivnmiklrgg fglvgnevgs pfsfltqyaq ssnrilfgen
      721 masnvgwyes dvannlqwss skqygigldf gflkdrltgs fdtflylnkg dvmdmtddmi
      781 rvdilgmpnt pkinapytts rkggfevsln wqdkigkvgy rvgvnysywd ervtrhsssd
      841 sdwwtptfdn igkrpyvtng esitypyglk tnglhgswqk mynsllhann nmtlgtpalv
      901 dlngdgrvnd yyvfnaegst phtqfgvtlg adwngfdlel ffqgatgarg ampsplrsqq
      961 symwnygqya fqnaytpsnp dvdaalptpv pegngfgysy idiwsfdasy lklknislry
     1021 dlkrsvlknl pviqgldlsf vvtnaftwtk ksyplkdlqd pefittgasi ynnngtlgsy
     1081 ptqrsytlgv tvtl
//
LOCUS       WP_119059492            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Candidatus
            Ornithobacterium hominis].
ACCESSION   WP_119059492
VERSION     WP_119059492.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Ornithobacterium hominis
  ORGANISM  Candidatus Ornithobacterium hominis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Ornithobacterium.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Candidatus Ornithobacterium hominis"
                     /db_xref="taxon:2497989"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124441
     Region          24..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrrflfnlf lllcslsfvf aqertikgqv vdsngfplqe vfisvqgten svlsdengny
       61 siqakegdvi vfdyigfakk tekvgkstka mnvtlvnsni qelsevvttg itstdkrlft
      121 gasdrldass vkidglpdvs rglegrsagv tvqnvsgsfg sapkirvrga tsiygsskpl
      181 wvvdgvimed vvemnaddla sgdaltliss aiaglnpddi qsfeilkdgs atsiygaram
      241 agvivvttkr gsaglsniny tgeftyrqip sysnfnimns qqqisvyeem rnagwlnysd
      301 lvnaresgiy gkmyellnkl dsngnfllan tpeskaaflr eaqyrntdwf kqlfnsnisq
      361 shsvslssgt ekstyyasls alvdpgwtls snvnrytanf nsnfkirdnl nlmvlssgsy
      421 rkqkapgtla qdvdivsgkv krdfdinpys falnssrtld pdkfytrnya pfnikhelne
      481 nyidinvadl kfqtelkwkp iksvetsllg aikyqstsqe hhvtefsnqa kayrampntt
      541 vrdnnpylyt npdnpyalpi svlpaggiys ktdhtmygyd mratasykne fnnihtvnfy
      601 lgaemnaadr krnnftgwgm qyslgenpfy iyelfkkgve ennlyyglyn skyrnlaffs
      661 natyswkkky tlnatlryeg tnklgksrsa rwlptwnisg awdvsrenff ddlyptvsdl
      721 ivkasyslta drgpasvtns lvdirssnyw kplseyregs lyinqlense ltyekkheln
      781 lglqtgfldn rimfnadwyk rnnydligvv ttqglggqiq kfgniadmks sglelslqtt
      841 niktddfrwd tsfiyskikn kvtnlktrar tidlvtrngf akeglpvrsi fsipfqglne
      901 eglptflnqn gettvtdiyf qerekldylv ysgnadptdv gsfgntfqyk gfklniftty
      961 sfgnvvrlnp vfsnsysdla alprdfenrw tvsgdekrtn ipvladkrmi naygsnnlai
     1021 aynaynysts riasgdfirl kevslsydfs hnliknigfr nlslklqatn lfllyadkkl
     1081 kgqdpefins ggvalpvpkq ftltlragl
//
LOCUS       WP_119064867             396 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Phocaeicola vulgatus].
ACCESSION   WP_119064867
VERSION     WP_119064867.1
KEYWORDS    RefSeq.
SOURCE      Phocaeicola vulgatus
  ORGANISM  Phocaeicola vulgatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Phocaeicola.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Phocaeicola vulgatus"
                     /db_xref="taxon:821"
     Protein         1..>396
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          43..>395
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkrlqsvsm vlflgtlfsg tistatasga nsfattqqag ickglvkdat gesvigasvv
       61 vkgttngtit dfdgnfsldg ikkgdvivis yvgyqtqeik wngsplnvil kedsktlsev
      121 vvvgygtqkk anlsgsvamv dskelenrpi qnvssglqgl mpgvaitgtn gapgqdagki
      181 rvrgigtlne agpyilvdgi etgtlsavdp ndiesisvlk daasaaiygs kaangvvlit
      241 tkrgktgqtk isysgylsfq natnmiermg syeyasllnq aleaegmskr fndtelqkfk
      301 dgndplypdt dwydlayktg vqhrhnvnin ggsenvkyma slgylnqtgi lpnagreqfn
      361 artnldmkin krlsarmnls fikndysdas sayygg
//
LOCUS       WP_119075537             988 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119075537
VERSION     WP_119075537.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106419
     Region          24..954
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myliknwall llligstlta aaqqkvtgrv tdaagngvpg vtvriqqsnr gtitdvngry
       61 sleaapgntl ifsftgyksh qaavsgntmd vqlaedyanl devvitglat svkrsnlana
      121 vatisakely gvapaqtfda alsgkipgal itansgapgg gisvkmrgvt sifgnsqply
      181 vvdgvfisnv svpaglniit aaasagnpqn qdnpssrvad inpddienie ilkgasaaai
      241 ygskaaagvi iittkkgssl gkttvrlvqd igftkvrkll gkrhfteeta fdlggdamrn
      301 qfiaardagk lydyekefyg etglisntgv svsggdertg myfsanrrse egiikntgyl
      361 nnsvrlnvdh kfndrisvgl ratymntssd rgltnndnns vtygvslati peflemhpda
      421 qgnypinpka anpfetrdkm rnnetvnrvi tggevkatlh qneqtntkli vrggidffnl
      481 kteaifprtl qfmagalnga siqgntnnln tnlmgilvny leagptltft tsvgatlets
      541 ymdnliatat nllpqqtnvd qasasqlqqf rqkyrdngif iqedvlimda itasagvrfd
      601 rstnngnykk yfvlpkasls wnlakmdfwn vpsinslklr aaygaagnva pygakflalt
      661 asniggqpgs lvdtqlgned ieqerqtele agldvsffng rlsleatyyq kkiydlllrr
      721 svppssgfaq qwvnggdlqn kgielslnat pvdtrkvrwq stvnfwknts evtrltipaf
      781 plgafgntlg nffieegksa tqiigtlgtg kgtgvlgnse pdfqmsfynd ltlfsnlslr
      841 vmmhwkkggd ninlteylsd vfgtshdydd dangngvkdg idrmnaagdn dasirvqdas
      901 yfrireigly ynipipknki isavnvgvsa snwftftdyk sydpessnfg sntmstatsr
      961 gstgistgve vtpypaskra mfhlgitf
//
LOCUS       WP_119075324            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119075324
VERSION     WP_119075324.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112312
     Region          29..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrtlrllav yalvmlmlpa allaqqkavt gtvlsdeggp mpgvtvrvks ttrntqtdir
       61 ghfsiqvgpg eallfsfvgy etqevtpgdg pvnitmrtst salgevvvta mgikkekkgl
      121 gysvqdikse ellknkdanl vnslngkiag vnvtnsggap gssasiiirg gtslerdnqp
      181 lfvidgmpmd nstgqgdnsa fdgsvnlstt nsnramdlnp ediesisvlk gpaaaalygl
      241 raaagaivit tkkgavgsvt gtvtsrymnn wvnklpkqqg iykqgsyyng syianttrsw
      301 gdkfaagepv ydnmgdffer ahafdnsftv sggsqtgnff lsgsnliqtg ivpttdftrs
      361 tvrfngeqkl giftfgvtas yarnesqktl tgsglwgssg sgymesiiaw prnddmsnyl
      421 npdgtkrrli lnpeliddid npnwlvyrnp qsdrntrfig tvyttakitd wfdvtyrlgv
      481 dnyttqytsl tapgsgvkva wqngmlsetd rtynyvnsnl mlnfhktvkd wdfglllgns
      541 tedtwlksns iraenfvipn fvsinnaake nqylsenltr rrlagfygdl rvsyknflyl
      601 nvtgrndiss tlppqnqsff ypsvsgsfvf telmpkssil sfgkvraswa qvgkdapayq
      661 tntylfgpel tigggfrnyw argnnklkpe tttstefgte lrflngrlgl dftyyinnsr
      721 dqilqprvsn atgyilsfvn tgeienkgie vsinanpvrr kdfnwdvtln vshnkgrvks
      781 lpgalpilyv tdvqvgnaka asfddgyfmg lsglkwqthe ngdllldwns gyplttnnat
      841 slvgnrepdm igglnnsfny knfnlsflfd frlggdvyng teyllvaygl skrtenrdqd
      901 itftgmslnp dtknyepvtr tvkasekyyr diylanapff iekvnwlrlr slslayslpk
      961 salggvnwlk gatltatgtn lllltnytgm dpetsaagag vigsgsvgid ycgvpatagl
     1021 aiglnlkf
//
LOCUS       WP_119076254            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119076254
VERSION     WP_119076254.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116300
     Region          23..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrhlykltll llltnltiya qnrkitgrvt agsgqplpgv svfikgtgtg tattpdgnya
       61 lnvpdtatql tfafigmetq tivingqtsi nvvlqsadkq lqevvvtalg israkkalgy
      121 avqevkstel qtrptnalsa lsgkvaglqv vssggnmggs srvllrgins isgnnqplfv
      181 idgitidnad lntkstvngs agkdvgnmiq dlnpddiesv nvlkgpaaaa lygtraangv
      241 ivittkkgra gkgldvtvns gvelervvrl perqqlyggg ksntfqeati ngqtykivdy
      301 gmdeswgpkl dgtpvlhwyn ldpeyadtyl kpepwaypeh dvrsffrtgi aatnnvsvsg
      361 ggenqtfrls ytnrsvrgtv pnsslsrntv nfsgssrfsr llatanfnyv knqstgrpwt
      421 gasnrnimle afqwgqtqvd yeklreykrp dgtprswnrn swentaagra tkyidnpyws
      481 ayesyleenr drfygnvgla ydvnnwlqls skvnadlyny qqqdriavys rsqsnyseya
      541 nnfsefnyef lanankrwnt isltayaggn imnqkrrvns avtqggliip dyynlknass
      601 vlnesnfyhk siyslfgsvs lgyknfwfid gtlrndwsst lpldrnsfay psvssslils
      661 elapfkennw ldllklrlsw aqvgndtdpy qlqqaydatq afngnpgykl psvlankdlk
      721 peitssteag vsvrafsnrl gldvtvynnn srnqiinipv stalgyesky inagkinnrg
      781 ievtltgvpv qtahftwdaa lnwsanrnkv vqlsegvttf pltdpsgsla tlvaregepy
      841 gqllgydfvy apdgskvidd kgqylrtqql vpigsvlpdw qfgiqqqfty krfdagflvd
      901 grvggkffsq tykvgtqtga lkhtadngir englildgvn gtvafnadgs ytvsntkpnt
      961 trvsaydway gystgpttqs ildatfvklr eitagytipf gktsavrqvr vaaygrnlwn
     1021 iytaskyidp eltnsggniq gveggnlpvp atfglnvqvk f
//
LOCUS       WP_119076424            1197 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119076424
VERSION     WP_119076424.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1197
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134330
     Region          134..1196
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgyiadlkmi rhrslprlyr llalivlfsv siqiyshaqq pqeertltls gtrtieeifs
       61 aiqtqmgltv tyeysvinrl qklrvnfkka tltqvmervl rgqkvgwaqv rgqvllfenk
      121 apvavkkeee paqitvsgvi tnpegqpipg atvmikgtlk gtqtnaqgrf riegspregm
      181 leissmgyla rqfrlegeqd lkfvltpavt qiepvtvvst gyqdlpkers tgsfvfidsa
      241 llhrrvgvni ldrlegvtsg llnyktlnmn tiskmptgvp lgislrglst lspnrvntnp
      301 lvildnfpye gdigninpnd iesvtvlkda asagiwgars gngvivlttk rgkyrqkmtv
      361 dfntnltivs kpnlykdrny msagdyidve ttlfnkgyfd gdinnsttrp pvspaveila
      421 klrsgtitde eaqgqldllk shdlrkdmlk yvyqrgvrqq yqvnvrggid klayflslgy
      481 dhgtdnlvrn gssrvtatsa ikyrpvkkle iegyvnyghn tilqhnelgy gnilvggsky
      541 rllypyasla dgngnplptv rdyranyvds vhglgfldwr yrpldeirna rrymnlsdlv
      601 lrgslkyria pfldvdiqfq netqaifskn yrseetyfsr nlinrfsvyd vsnsqftynf
      661 prggileren ydwrsysira slnyrqqigs hlltgiigse lrelsatgte fstaghageh
      721 gaaasgldlt tlfpvnpagq stlnsalsmt gtvlgllnrf isyytvagys ykkrydisas
      781 arrdganifg artnqklvpl wsvgggwsis kepfynlgwl pnlrlrmsyg fngnvyngaa
      841 yltgtritdp ltglpsivnl tpaneelrwe rvkiintgld fslwnsrisg tveyyhkegl
      901 dlveqvsnml qtglgavnrn sgsiltkgfd vnlnsrildk klawdaafmv shlkdritny
      961 srkptaasvv fpdplnllyv vgkplrgvls ykwagldpkn gdpqgylggv iskdylgirq
     1021 nfnpdslvyh gsatptffga irndftfkgv qlsfnitykl gyyfrrpsln lnyqsilnes
     1081 mnidysrrwq rpgdeahtdv palsypsssd rnlfyrfsev mvekgdhirl qdirlgynip
     1141 vrnntfiknm eaycylnnvg iiwrankfdl dpevystqfa nnvpnpfsis igfqanf
//
LOCUS       WP_119076443             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119076443
VERSION     WP_119076443.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107383
     Region          30..976
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktstffmr vswlgallll taslaysqsr tirgtvkdak dqsplpgvtv rvvgtstgtq
       61 tggdgtysln ittgaqlefs yigyetltia igsgntvnas lalssrtled vvvvgygtlk
      121 kkevtsavts ikaenfnpgv arspmdlvqg kvpglsitrv sgnnpnagas vqmrgittls
      181 gsigplivid gvpggnldll qqediasidv lrdgsaaaiy gtranggvil vttkkgrsge
      241 pqfnfssylq rdaiakkprf lnaeefkana pagndlggst diydllinkk nlsqyytlsa
      301 tggtdksnyr vagyynegeg iakrnsrkqy ggrlnvnqtg lqgkmtlqan laanfnkadl
      361 lggsngdfeq avqrnptapv kkpdgtylet tgfnnfnpva rqeqelserd qqtiqgdgkv
      421 tvevykglrv safgavvrnt wndrqyrlra srssqqdyqg ggyaykgnrv eldktfesvi
      481 dynnnfgehg italagysyq ystietysan nagfltdafq dwnlgnglyr tlgragmasn
      541 kvdntlvaff grvnytfrqr yfaqailrhe gssrfganhk wadfpafsag wtiseedflk
      601 ghrvinqlkl ragygvtgnq gfanyqslil lstggaylqn gswfetygps rnpnpdlrwe
      661 kkkewnigvd fslwgnrlag sfdvyqrkte dllanydtql ppfvtsqift nvgtisnkgf
      721 eivlnavpvq tknfsynidv tfnrqqnemt sitndqyrle klefgglpsp galgnairvv
      781 eggalgnffg krfagfddng kwlfykkdgs kvpagqitqd dltvigngvp kmmfswnnvf
      841 ryknwdlslf frgklgydil nlqelyfgnk awfpnnvlqs aitkhkalnd vpqysdyyle
      901 kggfmkldni algynfklks syvrslriya agrnvltftk ysgldpeled nglttgidgr
      961 gfyprtqsyt iglnlgf
//
LOCUS       WP_119076539            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119076539
VERSION     WP_119076539.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116662
     Region          23..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqallfitm lmvsvslaya qqrkvtgkvv gddgapipfa tiqikgttsg ttadqqgnfs
       61 lqvsgdnvvi iirsvgftqq eiplgsqtsv nvtlasdsqs lqevvvtalg vsrakkslgy
      121 avqeikadki tqtkqadlnt aiagkvagvq lrggsgakfg tttirlrgvn nltggnpiyv
      181 vdgvitpssa inpddvaslt vlkgpaatal ygqrasegav vistkkssgs gigvtlnhtt
      241 tfervyvlpe yqneygggss qswrtfvfnp aqhdpalqvl dgakyynyev deswgprmdg
      301 tmhapwyawd ktvnaedfgk qkpfvahpnn vrdffetgva nnttasfaks gegysnrfsf
      361 tnltrtgvip nskqqknwlt ytgslnltdq lvistgvnyv yeylynvpre gystqttgsf
      421 nqwfhrnlet dklkqyykra dgsfrswnit gptnpavkyw dnpyteayen vrnsweqtif
      481 ghvtlgysfl ngfkaqvisr gtfinqngdn rvasftlnpa ffgtsqdkrt etaflgsley
      541 eknvndfsfr aglwgeinkr krnqvssqta ggfivpnvyn vsnslnekvt snfvqnrqin
      601 slfgyasigy rdmvfldgsv rndvsstlpq dnnsyvygsl sgsfvftell enknflsfgk
      661 vrasvarlgt dtdpyglfet fplgtnyskp ivspsgatst vvysrqnvpd trpndelrpa
      721 mstsyeigte lqfannrarl dvnyfyrnnk dqivnvtvps ssgysgrlin agemenkgwe
      781 ftigasplkn kdwnwdvdin fafmknkiis iapgvdnlqv aldgsalsfg fvgsprvsln
      841 atkgksygqi lgggferdea tgkilvdddg yplmqnqvel gyvtpdwtgg lasgltyknf
      901 ylnfsldfqk ggrfvsiskm fnagsglgie tvgnndkgnp krdpvedggg ikldainant
      961 gkaneayadt kdlyesylfs mwenwtydas yvklrelsfg yslpakifnr tpikginvav
     1021 iaqnlwliys kakgldpsel esswieggql pgtrsigfnv kvnf
//
LOCUS       WP_119076672            1125 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119076672
VERSION     WP_119076672.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1125
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123592
     Region          26..1124
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfvrlhgll llvcllvsgp awsqerkisg kvvsdddnqp ligvnvvvka tkkgvqtnan
       61 gqfsidaspg evlvfsyigf eqqeitigsg itinarlkvn askmdevvit gygtakrskl
      121 tssiskldkk ilesgmranp aqalagtipg lrvsttsgrp galpnivlrg gtnfdgsgsp
      181 limvdgqmrg slsdinpedi esmevlkdas ataiygaras ngvilittkr gkdgsssisl
      241 kaqrgfsyln vpykfldaed yitwqrravv eaikngtlaa salgavgprg tgnlykdgag
      301 nvldgnydsr avwstmrltd anrellgmnd gwkvmkdpvp tnaagaydpn gtqaeliykd
      361 fnygdyafns paasqdynig mtggnnrgry yanigyfder glplktyyrr inftlngdyk
      421 ikdwltsess vqytvanwrd qaltngegny wgrmlsappt mrgtnaagel ilgrdasdgn
      481 pvinidkyir knqtdkftfs qsfrfdaghg lnfkvggilf ydegfnesfn rdfrtgllsy
      541 tnpntgwnrt rassaafdrt inqtynaias ykkqfagrhn idamagfeff dayqkgmgas
      601 gslaptddfm dlgltlnnat tqtrgtdsyh srerimsgfg qllydwdgky lasftirhdg
      661 ysrligdnqy gtfpaasvgw lahnerfmsp lknwlsylkl rgswgingni gigtnnaigv
      721 yelqgaygaq tayngtigfl qtalanptlk weksntvevg admgffnnrl tasaayynrl
      781 tsdkitfvnl ptsagvasir tnngslrnkg veleaaykvv qkkdftwqva anaaynrntv
      841 vklpyngnen nrqggqqvyd pasgkviwvg glqegqewga iygfvsdgii rnekdlaeyn
      901 kidmaagevq fgaaagkrva sqklitergl anfistkpgd mmwrdidrnd tidyrdmvri
      961 gqalprwtgg fnttltykgl rlfarfdfat ghsqqdfmqm walgsfqgef nateivkdtw
     1021 tpenpnakyp rytwadqlnt knfdrpsnmf yvksnylair eislsygipa rllkparisa
     1081 ltlsvsgqnl gyitnsmikl pertgaqnsa ytvptqlifa anltf
//
LOCUS       WP_119076766            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119076766
VERSION     WP_119076766.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110775
     Region          24..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfkafpltll lmllgatvvq aqtrivkgrv ldasgplyra svgvagsang tftdeagnfs
       61 lsvpagsvtl vissvgyttl qrtveageke vtitleqqnv klgevvvtal gigrktrslv
      121 yatqtvkpae ltevrdpnnv lnsfqgkipn afitqgsggv gspakivlrg nrsiqgtnsa
      181 livldgvpiy nsgfdnmasn inpddiesvs vlrgasaaal ygsqagngvi vittkkgveg
      241 klavtynagv tvespfslpr vqnrygqgnm gqmntnvges wgaemngqsy tdhfgnpavy
      301 saqpknirdf frtglnlnna igisagnekm qgylsltnnt vqgiipnndl rrnavnlrls
      361 nqlskrlstd akityftqqt dnkprngegn tpvldiyqis rnvttaqaer ymeinelgvp
      421 vpapwpstlg siygnpywvv nmdnlnetrd qvmgfisaky qivpwlsvtg ranldrsytn
      481 aeqktyqgtl lwatkpggyy sklsavstqq wydvmfsgdn alsekfrlny nagaiyqkse
      541 fdqtlsiadg lnvtnkfspn fatapqivss gtavitqsvf gqanfsyada lyldasvrnd
      601 wdsrlpaphs ftyysaglaa iisdlaklpe pisflkasin yaevgnggqf gllaasydyv
      661 pgagngylfr ksilpfpqlk peivknleag iearflqnrl glavtyykan slnqlltiti
      721 pvatgyssqy inagnirnqg vefvltatpl kkqsfnwdvt ynlafnrnkv ialsdelklv
      781 nlgsyidfgg lpqvkeggsy gdmvahrwar nengqylvta agkplttdvl geepgyignf
      841 npkatmgltn nfsykgislr vlvdgrvggi vvsgteqnla fsgitegtea hreggwnlgg
      901 vdehgqavta eidaqgfwqt asgkrfgvge ffaydatsfr vrevslgyni plrssagiik
      961 svkisavgrn lawlyrgksl ldipglpkrk mwmdpdmglg igntlqgvey gafpstrsvg
     1021 lnlnvtf
//
LOCUS       WP_119076812            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119076812
VERSION     WP_119076812.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123596
     Region          129..1117
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mritllggll llgsyhyays qtyatvrnfp ariqsghaem tslstllsdl eealnvkfsy
       61 naalighkkv rnasittlvk ngwdrelkir laqlgltltp nglqhyiirp vapqadlaae
      121 gqtvaverie vrgtvtdstt gtplpgvavv vkgtsngtit ntagaytlkn vpdnatlvln
      181 mlgyrvtevp vdgrasihvt matenrvldq fvvtalgikr eekslgyavq kisgeaiqtv
      241 kgtnigttlt gkisglvikn steffqapti elrgatpllv idgvpygnlt lrdispddie
      301 smdilkgata aalygqrgga gaiiivtkkg nnskglsvtl nsntmftagf lalpkgqtsy
      361 saglggeydp tdyvwgarld ngemaqqwnp etkqmenmel tsrgrnnfrn fleagyvtnn
      421 nisvaqtgey gsfrvsmthi hdkgqypnak ldmvnftvgg eiklgdrfsl eshmgynkrl
      481 spqiagkgyg dqgyiynilm wtgpeydlsk yrdywvvpdq qqnwhykawy dnpylmayek
      541 lkgidqnttn asltatykvf dgarvilrsg wdfyghvetr rnpiginstr gwnalgmyaf
      601 drstgystnn dliftyekki gdfavdalag gtiyyykdey tkastrngis ipgfyslaas
      661 verpdvtatq sakqvnslya kaslgwknri fldvtgrndw ssslpkttgs yfypsygasv
      721 vlsefmqlps wvsfwklrgs waqskndlav yatnrtysit aaawdgynaa typdnllgad
      781 vlprtdrtwe igtaayflkk rlrldatyyn kytynipasa svsstsgfss klvnidetyv
      841 rrgveitada tvlkrgrfqw etilnwstsr ryyksldsvy sadnlwtkvg arvdavtind
      901 werdlsgnvi hqangmplks dyktrigyld pswvwgwgnt fsygdfslsf nfdgrvggll
      961 dnytdakmwd tgshpdsdnn wrydetvngk inyvgqgvkv tsgsvvrdky gqitkddrqf
     1021 aandkavsye syarsyqtgi pggwvdpsfl klrdvsfayr vpgaiagkig arsasvavtg
     1081 qnvflwtkkf rfvdpdggsd dvsspslryi gmnlkvtf
//
LOCUS       WP_119077595             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119077595
VERSION     WP_119077595.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106160
     Region          28..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkmrllkal lfcsllflla ptvlaqtkpv tgkitdekge pipgatisvk gtntgtvsda
       61 gglfkmnvpv sattlvisfi gyaqqevdvt assnvtvslq penttltdvv vvgygiarkk
      121 dltgavaslk akdfnrgitn apdqliqgkv aglmvvnnng apgaaatvri rgnssvrsgn
      181 qplyvidgvp ldgrvarpni nannlgqmpd anplnfvnaa diasmevlkd asataiygsr
      241 gsngviiist kkaqtgpakl dfgysvgvsn imkqlevlna agyrealkqy nssggddggn
      301 sdgmkeilrn gvtqnyslai sggndnakyr asfglmdqqg ivrksglkky tgnlsgqfkf
      361 leskrlgidf nvmaaqtveq lapitnnagf tgsliaqalq wnpttpilna dgsfhllakn
      421 spvnplamse awddkssisy ilgnvspyfk itddleyrfl fsinrqtgir raqiqsfinl
      481 egvqdlgqay ygnaelttkl fthtlsynkq isaafnlnav lgyeyqdfnf qgvdlgalgf
      541 stdalpytsi lqnasqantf msayvnpnse lqsmfgrvta nlqdkyllta tlradgsskf
      601 gsnnkygyfp sfaakwnihn esflkggslf qqlalrlgwg itgnqefpag aaqeqyvlga
      661 sgsanlsnva npdlkweksn qlnagvdfym lnnrlsgnvd yfhkktsdll fnfpsilpap
      721 asfywinlpg evinkgvela vkgeiirgrk fswmlgvnat fiknelqhyt gpnvltgsis
      781 gqgvsdasvq rfanghplnv fyvrkfqgfd kdgqgiyenn gntmyyagdp npkqllgltt
      841 elgfkkwwlt inmngafghy vynntantvl pinnlgsrni akallgngen psnpittsdr
      901 ylekanflkm snvslnynvg niggvfknvn lsltgqnlfv itkysgfdpe vntdksingv
      961 tsfgieyspy ptarniilgi tlsl
//
LOCUS       WP_119077947            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119077947
VERSION     WP_119077947.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117109
     Region          24..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkgltalfl lliclsgqvm aqsrtvkgkv tasedgtpii gatiiakgtn vgtvtnaegd
       61 ytlnvpegve vlvvkfigmk dteakingat vnvvltadvt tltetvvtan airrdkrslg
      121 yaaptvknde ltrgqspspi nglvgkvagv nisttasapg sssrivlrgg ssitgnnqal
      181 lvvdgvpidn snimgggdsr ssvdfgnrgn dinpediesv simkgpnaaa iygsrasnga
      241 liittksgkk gkkgmemtln ssttfssilk lptyqnefgq gypantpsgf ytdpkenwsw
      301 gapftgemqe wgqeidgkrl skpysavknn vrdffetgva annnlslaga gdkttyflsl
      361 nslnsngifp gdydkynkyg irfngtaels nkfttsinin ynkikadmiq ggqgdgsvyn
      421 nvlqtprdip lqdlgdlnnp yyamggytna agqpvygyyg aytvnpywql reyrnqndvd
      481 rvtgnfaity kptswldvve rvgadiysdr rnfkypkysf vpadntsgey tvadnthtsn
      541 gkyeedqynl sevvhdlmit grkefskdfn aslmvgnnir qrtfttsevq tnpsgglvvp
      601 gwynmgnsng avqavnnysi rrlvgiyadl nlayknmlff gatarndwss tlpkannsff
      661 ypslnasfvf tellkdskvs nvlsygklrg swaqvgndad pyllntyfdr tdilgafgqt
      721 lfplngvpgl sqsnrignpd lkpeittafe igtelgffdn rftidfsyyq nkskdqilni
      781 piptvtgfss kvinagsiqn kgielalrgt pvrtsygltv elfgtyarnr sevlsllpgv
      841 eqvviggfgg mavvaavgkp ygtfystaiq rtpegnpivr atnglplltp spvylgsynp
      901 dyqaslgtni sykgwsfsal fdtkqgskfw srnkdnmdft gistesaang rqphpfpnsv
      961 vadpnnpgky ipntrnynmi sywtdlipsg ehvidgsfvk lretslsyrl pksvlsrtpf
     1021 gevqiglygn nlflwtpken qysdpevnsg gatneqgldf taqpslrnyg fnlrvsf
//
LOCUS       WP_119078314            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119078314
VERSION     WP_119078314.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112110
     Region          32..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrcmfharh fycllvlafi lpvslpaqnq pikgtvkdav sqapipgvsv svkgasqgta
       61 tgidggfsiq aaadavlvfs figyekkevp vgaqtvlnit lqqsasqlge vvvtalgier
      121 ktrslgyatq qlnntdlttv rqpganimns lsgkvagavi tpaatgpgga vrvvlrgnrs
      181 isgnnnaliv vdgvpidntm ttepggsgsa ntvatqqksi asgysgsdga asinpddves
      241 itvlkgpaaa alygsraang alvittkkgk sgkvtmnyng gvaidrpyll mdlqntygrg
      301 nggvygaqag eswgapttty knnvrdfynt gvtlnssvni sggtdklrgy asythnanng
      361 ivpknrlern tlnlrltgel lprlttdvkv tymnqiiknk prlgdngvtn ealimprdmh
      421 pdslrnferl dktgqpvpvy wttssafqnp ywdvhrtaln eernritlmg lakyqltdwl
      481 svqgrysldr yddkitgsyy fgtipvptlt ggryqeayin rwernmdvli sgnnklgndf
      541 ginynagaav lrnrgynsqs fanglsipnq fnlnfaatpa fsnltvekei qsvygnaqld
      601 frqqlfldvs arndwsstlp aphsyfypsv glsailsdml nlpdwisfsk vraaytqvgn
      661 dadpylliqt ytyslgagng fvardqikyi sdlkpektes weagtewrfl dgrlgldatv
      721 yksntynqli figlpqpsgy nqqyinagni qnqgvevmlt gtpvrrqnft wnsslnfaln
      781 rnkaislspg vtqaalttat gfgsllvkpg gmygdiydyv wsqdsktgqy lvttaglpav
      841 talqkignyn pdytlgwsnq lqykrfnlsm lidgrvggmv isgtdamtay fgiadyttky
      901 rdgglvlpgl kpdgttntta itaeqlwtqv sqggrngygq ffaysatnfr lrelslgydf
      961 dwqnklvksa rlsltgrnlf ffyrgkslld ipgigkrtip vdpevaigss nyqgiesgil
     1021 pitrsiglnl slsf
//
LOCUS       WP_119078150             947 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119078150
VERSION     WP_119078150.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 947)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 947)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 947)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..947
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..947
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104660
     Region          32..946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikklhgicl llltvetaqa qqgpsintdt lpavrnlnev vvtgalgikr sarevgaaaq
       61 lvgneelnqg kvvnpifglt skvaglrinm ydskvdpqvk ivmrgsrsln rgknepiyvv
      121 dgvpvpdinr lnpndiesit vlkganaaal ygsegvngal mittrsgqkg rtvvkfsntt
      181 tfsqvyllpp aqtrygqgte gvyaptmyes wgplfdgstr dlggvlpdgt qptqtyaats
      241 kdnrlnlfqt gitqqndlsf sggdnkstyf lslqhaaikg iipedasrrt garfngsrrf
      301 gklntsynin yiyfnrnttp dgpwitayql panfdypamk dwenpnsaan plyfftdqmk
      361 npyfqidntr drlaqqtlng kveldyqvtd wfkaiyrlgl ysvseetrst agkfeapgrr
      421 nvvgtvsdgs nnfrrvngdl ilsfnkdfgk fstrlvlgqn fradytkvsa vgagnltlpg
      481 lfnpgsrvge lngsagitey rsvagygelt agynnflflt ltgrndvvsv lspenrsyfy
      541 pgvsasfvfh dvitalkhsr alsfgkvfas wnktgnvtld pynlnnaysq vngfpfgnmv
      601 gftpsaeypn pniqpefvts yeaglqlsfl nnrlhfegsy aysdskgqif kantsraigy
      661 stavvnagrl tnnvielsls advirdrgrd irwniggaft hinnrvqely egleqfpifr
      721 qsyavkgsay pallvsdykr dpqgrvvvna ttgdpvqata qshlgtmvpp yqmglhtmfs
      781 ykgislraqf dsrlggwlys eiaprmftag thpwtddydr qpfvfpnsvi evsegkyepn
      841 tskltssggk sfwqqqgsvq yntaaksdff klrelainys lpasllrrqq lvkdvniglv
      901 gtnlfiirhk dniygdpeyl ynntdgylsf rqvppyrtyg fninvtf
//
LOCUS       WP_119078814             940 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119078814
VERSION     WP_119078814.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..940
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103716
     Region          50..939
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnyikiifs lfflapsavp aaahayaagv lfqdtarqaa rqdsiyplff ttkqkdqlvs
       61 avgfadgaal ravpltgign altgriagla tiqdagepgn dqplfllrgr tplvlvdgip
      121 rniytilpeq vasvtvlkda lsaaalglrg adgvilittr keakqrghnm dfsintgiaq
      181 plkqrellsa aayaelynea lqndgrpaly taddivkyrn gsapythpdn nwyarvmekq
      241 apyqryvlsa ngktdamgyf lsidyleqdg llnqsslnsy stnvdykrfg frgnvsidls
      301 prtklslnih gssrrrnapg gaaslsfapn tgrldistgs isglfnsiln tpanaypvyn
      361 pdgsfggnql fsnniwgqat gagysqinmn dgladlvler dmsdvwkgww vkgtasytme
      421 iihniirnks fatyemkvtg andtiyrqfg sigeqantsg vsvrngslfm dfstgvsrsw
      481 nehhldvalq yqrssarygn qlpfvikngi fraeyrmgnr yildvvtsys gnnwykpghq
      541 ynfypaaglg wnvhnenffp qnsffdqlkl rtnyglvgri danyfsylyt ysnygsayyi
      601 gtgaggvqgt eesqlpyvrt tekalkwnig adlgmlnnra tlsvdyyrnr fydllqqrgr
      661 ntallgapyp aenigksqys gleatagwsd kvnafeyeia anlaiqrgri iyndqppqah
      721 pwmetagdri gqqygyiadg fvttagegpv vegyrsvpgd lkyrdlngdg vinfydvtki
      781 gpdkpeiyyg isagfrfkgf dvslqlagla nrmmnltglg ewefqnegrg pafphhynrw
      841 tpetaataty prltagfnpn nhvnssfwls sadflrlktv algytfrggv ldrlkikgcr
      901 vfasgynllt fsgqdrfdpe ngslgyplqr ilnggisikf
//
LOCUS       WP_119078966            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119078966
VERSION     WP_119078966.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120375
     Region          27..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtlllavv lltlcvqvsl aqekkaitgs vsnasgtplp gvtisekgts ngtitgadgs
       61 frlstapnat lvfnfigytr revpvsgqsv ynitlsedvt glnevvvtal ninrakkslg
      121 ysqgtintek lenigspina fgalygqvag lkitstalgp aggmsinirn avslyegstn
      181 rplfvidgip mldwqtdinr stgnglndln mddiasfevl kgakaavlyg sqgangvili
      241 ttksgskkkg fgvdvnlshs rdnvwimqef qnefgsgfpa awvvpgtvda egfyqrfgkq
      301 ayyptnynfg prmdgrqilw ydsvmrpyva qpnniksfyr ngftnsanva lqggseiggf
      361 risytrrdyk gifegfklhd dnfnfngnik itnrvnfklv styattfnhn apptnqdvfv
      421 tygvprqldv dllrtqivdk endnyfwwym ndrntrypvg givrdglagn ylwnqtqndy
      481 dntrnhfins atvsvdighg frlellggfd witnkneqke kvrrplsvan ggryylsnst
      541 dvfyngqavl syekqvtsnf dinafvggvi qrrtsestnr ttpgdgfitr dwfsfrnakt
      601 tpvlsddtrr ysrlyglfgs vqfgwkgwly ldlqgrndws silppqnnsy fypgasvswi
      661 fsealekpaw lnfgkfrvsw advgrpgpey fantvydign yggvvtyapr adlpptdlkp
      721 erkrelelgi etkmfhnrfg levnyyngnt ydqimglsva qasgvnttri nagqighsgl
      781 evmltgtpvq gknfswetvl nfhndkpkvk klaqgitsqg lwgmsgasvv akegqpwgqi
      841 ivrpyrtndq gvriteggyy stdptkeeiv gkvlpdilgg fnntlrykgl elnfnidfqf
      901 gstlvsqtnm ymvgngsakq tvtyrdeahg glpyyinnag afvqlpshta pvpadskypf
      961 imhdgvilpg veadgkpnet iitaadkhsy ywqtfmdiqp divykndyik lrnivltynf
     1021 pkrltdkmhf erlaisafan nlwyiyktmp nvdaealngt nvffennafp strsygvgir
     1081 asf
//
LOCUS       WP_119078967            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119078967
VERSION     WP_119078967.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119322
     Region          27..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrilllatl lsfcfaplsr aqekkavtgs vrdangtllp gvtvkekgts ngamtaadgs
       61 fkisvqpaat lvfsfmgyvt qetpagtgpl nivlkedskn lnevvvtalg ikrearklgy
      121 amtelkgsei aktnsinpva alqgkvagvd isgaaggpqs anrivlrgak slngkdqpif
      181 iidgvifend kaddavnfgn vlknfnpdef esvsvlkgaa atalygsrai ngailittkk
      241 gltrkglgve vsqtvqfeqv yrtpialqnv ygggtngtfs kdaqgnnvvv pggnsfgprm
      301 egqmaklpng divpfspmpd namdgyqlgk yyntnvaveg gndkanfrfs ysrlsnnsvm
      361 pnndfnrnsf slkssavlsk flsaeggity afsntlnptr qggdytnqnv grkwiyvfpr
      421 nydpaywaar ylgpnpglsn mddylgqypg adywfslnhd twerkenlfm gnlnltatat
      481 dwlkfllrgt fsneqnkddr relgwgpnfs garglyavsg vnrtqytftg mamfspkmkd
      541 dftlnvnlga etwnsgigne ysarttngll vpgkftisns vgtvdargnk ilprkqinsl
      601 faaaslsykn affldvtgrn dwssslaypl gggnfsyfyp svsaawefte tyknalpswi
      661 tygklrasya vvggdtdpyq lnsgyvmeel wngginngyl yypynkdtyp ndnlkpsmah
      721 syevgadirf fnsrlgldva lyqsdikdqi lkldvpvesg vknkfinagh frnkgielai
      781 ngrpvqgkhf qwdvtfngsr ntnkiialdp gidtyemgsd qdvrvvaqvg rpygvlvtny
      841 gytpyvsadp akngkpvier sasfpvqfkr staevgnitp dfnlglnnsf syknwslnvl
      901 lqarmggdmf sashqygtgr gtiestlpgr daasggiawt dkdgvqrndg mipdgvfgeg
      961 mkgttatgls qdvsgmtyre aydkgyvtpl tpyqyysmig ewgigireas vfdasyvalr
     1021 evslgytfpa klverwklnk arvlltgrnl gylfnnlpdh inpeglrnns tfafseygga
     1081 pfvrnmalti qlgf
//
LOCUS       WP_119079042             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119079042
VERSION     WP_119079042.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110966
     Region          46..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknliyhqvq qhlcllnrfs khfgkkaall aslsmlvctl afgqgrpvtg svtdstgtvl
       61 pnvslrikgt tsgtfsgtdg kfklnvtgnd avlvvtyvgy hdkevpvgda sdlkivlqqs
      121 vsqltdvvvv gygtvqkknl tnavttvnnk dflqggfnsp lqqiegkvag vtisnpasad
      181 pnrgtdvqir gassldagng plividgmpg gdlrniaqqd iesisvlkda aaaaiygsrg
      241 angvvlvqtk tgkkgavavt ydsyiehdav aakpdilsad eflshqrdad lgartnwyde
      301 llrkdnfghn qyltvsggne ntifrlsgny rsktaidiat erkeygyran ftqkalngll
      361 efsgnlsqri akeeytnyda fkqaiklnpt lpvmdpnnpr eyntlqgydt wnpvqdllar
      421 engadqtysi idittklnil pnlsselkla rqghemlrre yytsksaesi qnnrtgrarl
      481 qnekwhdytl ewinnyntri nkhdiavmgg ysyqefntqg nwaenmdfls dafwynnlda
      541 gawnkedgrl gmdswkskek liaflgrvny nfdntyflta sfryegntkf grnnkwgmfp
      601 avsaawrisn lpafsgsrvi ndlklrasyg vtgrsgfdry tslakyapyg mylddnnewi
      661 rvygpgnnfn pnlqwerava ynigldfsll dnklsgsldv fdrrskdmla nyevpvgayl
      721 htemfvnvgt tsskgielta nwkvangkdf syntnltasy ikaklvtwsn nefqgnyrdl
      781 qdlpspgnpg kayrlepgte lgsffgykya gvndggeili wkdgvvgkek iiassqgsek
      841 drtyighgap ryelawgnsl ayknfdltlf frgrfdydil nlyqmyyglq aesginllkd
      901 ayarnghiks gkvitdyfle kgdyfkldnv tlgwsprfnn nfiknlrlyg svrnvftftg
      961 fsgldpttvg itgltpgygs lsvypvtrtf tfgaqltl
//
LOCUS       WP_119079050             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga alhagiae].
ACCESSION   WP_119079050
VERSION     WP_119079050.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40311
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milavlkeka genrvslvpe vvkqivqqqv tvwveagaga qafypdeayr eagaeiktra
       61 ellqqadmll sirppateew knvpagkiwl giyqplynpa lmqqwaekqf svfsldtipr
      121 ttraqsmdvl ssqaniagyk avllaaytys ryfpmfmtaa gsippakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgak fvevegaada skaggyaveq sadyklkqeq
      241 kiaesaarad ivittaqipg kpapilitke mvsnmkngsv iidlaaatgg ntevtkneet
      301 ivhggvtvig nsdlagtapa dasklyarnv lnflkliisk egqvhlnfed dlvkgtcith
      361 qgeivndrvk qlqaaav
//
LOCUS       WP_119079157            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119079157
VERSION     WP_119079157.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118478
     Region          46..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhffllitg lhlcafgmas gkpaerhpai lqpdiektar fdssvvvrgk vtdekgepli
       61 gvtirqkggn rgtasdkngs flitlpapgn vltfsflgyv sqeftirntq mlnvkllpds
      121 rmlnevqitt algikrdeka lgysapvvsg eqltealpsn wtdalsgkva gvnlvrsgsg
      181 ptasnkiilr gennltddne alivvdgvvi nqgsgrrsai egetaygtgs dnmpadygsg
      241 lndinpedie sltilkgpga aalygqrgan gaiiittksg sskkkglgvs insnasmeqv
      301 nrwpdlqfey gqgldgadyy sygasvdggs tsgtssaygp rfegqqffqy dpvaqkvgae
      361 rtpwvpyknk vnnffgkget ytntisvdgg tdkttarfsl tnannswiip ntgyqrntvs
      421 msvnskvndk ltisskinyt nkksdnlpga gygnqsimyw yifwqpsadl dwlrnywing
      481 qedrkisfpy stfpenpyav ayefinrtnr hgvtgnvqat yaftkelslq vrtsmdfgye
      541 qraqerpyda gakfqkgsyr tqnifsqeas sdfllryakk vnadfdfsvt aggsmlrnty
      601 nrdevradsl iypgiysmsn aagplvtmpw rskyainsfy glisgaykgy lfmdltarqd
      661 wnsvlatper tansgffyps vsasfipsda frlpqsinfa klrfsvagvg sggtvpyrta
      721 hnfatagsly sgglrlpssl anpdlrplrt ityeagaavk mfknrfgvdv tvytantkdq
      781 ilqrivdras gytrafinag kvnnkgievt lngsplknke gftwntnvvf sankntitql
      841 adsfvvlqtg pvgggqivat vggsmgdlyg rgyvrspdgq vvydertgwa kisedvkylg
      901 ntipkwrlgf snefiykqwr lnvlfdgqyg avghslthyk laeqgktknt lpgrysgiig
      961 ngvvmdadgk yrkndvvard ideyyrshfg idnaegstfr tdfikfrear ldytldpkvs
     1021 krlgmqrltv gvygrnlfiw sdwpafdpef gtlsgtdivq gfeigqfpst rtlgvnlvvg
     1081 f
//
LOCUS       WP_119079173            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119079173
VERSION     WP_119079173.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113766
     Region          59..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnyiekganv lfrantyrlr lpvlsgmval ctamispgar gataaipash qttapllsvg
       61 gtvtdstgap mpgvvvrvag tsqamvtddk grfqfsnvqe gavlvfrmig yvtqevkvtg
      121 sqvnitlqrd vhtlgevvvs dgyrtttvaa ntssissvga evmenkpftt faqtlqghia
      181 gltapltsgq pgaavdirir glgslslssn plividgmiv nadklgynmt tanalaglnq
      241 ndiesidvlk daaatalygs rgstgviiit tkrgkagktq irvdaeagvs gqmdppdagm
      301 plnaaqyaem frealvnggy tpaqvntlae syglnsgksn dwyslvtrtg kqqqynvsln
      361 ggtektkffg sagyfdqdat tigsdfkris gllnvdhhin qrmqlsvgvn asnvgqntpy
      421 saqfsgnptw aarvlrpfql aynedgaint sktgdtnfpg iynplwiaky dnkymsqtrm
      481 lgnvklkwni wdkltytayf sadyntieet tflnatmgdg vslkgrsrny ytryfnwltr
      541 nqldyrydfk gvdnfyataa vgyeaqkske yllaadgggf psahtsltal snaatplgay
      601 gqysnyafvs lyatagvnyr nkyaingsfr rdgssrfasn nryasfyaig gtwnvhqedf
      661 frhqhvlssl klrssygttg naslgnyawv pqagystays yagyngqqyy signidlrwe
      721 tarkfdagad igfagdrfml tvdyyhnnid glirsvptsl ttgftavsqn vgamvnkgwe
      781 ftlkgdvlri kdftwnsnfn lamnrnrmts lpegtgvqng nfylkeghsf ytfymkefag
      841 vdpqngaply ytdgthaaat dkiadakyvv ldresvpryt ggfnnvfsyk glslgvdfay
      901 nldywvlana dlyltsgtyy thnkyryiye nrwttpgqvt dvpkfstqtd nsvstyrlyk
      961 gdhirmknvt lgynfrnigl lkkwgvsrln vygratnllt ftfdkrlpfd pevtysgadn
     1021 qdmlqyktft vginval
//
LOCUS       WP_119080048            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119080048
VERSION     WP_119080048.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120294
     Region          56..108
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          116..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkhqhgwkr lfttvlllaa clhvsangfs qvkitlqvkd vdiqtaferi ekqsgyrily
       61 nqallkgigr vsvnarnepv revlnklled tplayevmen elivlkrkna spqdvkvtgk
      121 vtdatgasvp gatvhvkgts tgtvtdaegn ysitvpdngv lvftyigyvt qevpitdqtv
      181 vnivlqtasq dleqvvvvgy gtqrkrdltg titsvkgedi armpntnpis slqgkvaglt
      241 vvnsgvpgas ptvrirgvns tnnsnplyvv dgvfqqnidy lnpaeiesie ilrdpssmai
      301 fglsggngvi vvttkraakg etrvtlqsai gmqkvnnlid vtdatgfrkl fdeqlknina
      361 tpfdytnyta ntnwqelvlr tamlnnnsls isnsgekttt llnlgynthe gvlrngkyqr
      421 ivarlneeir innnlkvggd itgthwilns agadlnnakf aapivpvqyn entyysmpsf
      481 qrtqvgnpva rlnnmdgnsv nkgyrfvgsv fgelkflqnf twrsafytdl gfnnnrgysp
      541 lpfafinlge gnvptdttvn tnvrtgvnqr qeefrkfqqd htltfdktfn evhkvtavag
      601 fttyyegntn lnanrtdttl niprqpdywy vgivdpsmpg gfggggdeyt sigmlarvny
      661 ayankyllnl syrrdglski spanrwgnfg gvgagwvvse eeffkpvggi nflklrgswg
      721 tigsaqgirn nifragvkts stgvfgdniy tsvepdyipd pnlkwevvhg ldvgldvraf
      781 anrlsaeitl ynrktkdiit tvtlpgtlgn qsyitnlgti snkgvevtlg wndhvgedfs
      841 ysispnfsyn rnrvesigdn fnfllignsg anrtitgesi ghfygykqtg iyqssadmdk
      901 mprmsnslpg diafadtdgd gaitpndrin lgspfpdysf gvsvnlryrq fdlvlegqgv
      961 agnyvytqrr tgnfatlnye snrlnawsgp gtsnvepild ntrannylfs nyflepgdyf
     1021 rfrtvqlgys fsrdlltktg lqavrlylsg qnlhtfsrtt gytpeapist ilgagadngv
     1081 yplpatytfg lnvtf
//
LOCUS       WP_119080094            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119080094
VERSION     WP_119080094.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112812
     Region          36..1008
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnykhaiilt clsamllcvq adsyaqegkp vktqyvlvde egkpirnadv ysgtayaktn
       61 aegkfsiave agsdlvvvak gydkmslssg dalqqpritm kksallyaee drtnlafrka
      121 fqgdivgsvt kldiaeiqky dhtirlvdvi agrslgmmgy drirglgrgi tveditgsgt
      181 gramfvvdgl prdaenmrln evesitilkd vnsailygtg avngvvlvtt krgeafkkrs
      241 dfsvnygiat pralpkylns adymtyfnqa rendgltpqf sdetienfrt gnkyrypdvd
      301 yysdaylrsf knyydltgef sggnnvaqyy tnlgwynags llnfgeeakg rsnrfnvrgn
      361 vdlkindwin tavdaygvfl iskgargnyw sdaatvrphe yapllpinli nphdplllgr
      421 kndingqyll ggvsnrtttp fgygysggte eiisrnfafn nrvnvnldrv tpglsfhtnv
      481 sfdyfvaysq tvaneysvye pvwsatadsi vslkqygkds rpgtqsvggs sfrrrfggyg
      541 llgydrtfns khhftgsllg flgnykvegd fqgvklahag lrvgyafdrr ylvdfssayv
      601 gsvklakgnr gklspslavg wvlseedfms ssrnvnylkl hasagmmnsd flinnfflyd
      661 nryagsgsyn wfeggrsrsg iasswgtnpn ldytrrkeit lgvegrffnn vlgvtanvfh
      721 dvydrlvtrp ttrypsfytd fipyenfgan kyqgaelgve vnktfgdwki aagvnvlyst
      781 tevlkmdevy nnayqyragh padarfglea lglfqddaei aasprqvfga vrpgdikykd
      841 qngdgivden deiylgryqq pisgglqirv syrnftlyal geasygadef vnnnyywvdg
      901 ndkyselvlg awtpetkata typrlssqtn snnhrqstyw eydndyfnir riqlsydmpa
      961 fvskalrmrl lnvfvdgfnv frfgpsrriq dlsiggepsy rvfsvglnas f
//
LOCUS       WP_119080396             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119080396
VERSION     WP_119080396.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111181
     Region          74..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miyfypnsgk raalllglfm lgagamaqqk lykkadstgt agsaeaaerl knvpmlardt
       61 vgylpnsell lrttgavsrl pldevrklpy tsvnqlllgr vngvdvripg aepgkrssaf
      121 vrgasglllk ngdlfgaqpv yvvdgmplit ehafafdvqr fdfnrmgtei dplaflnvnd
      181 iqnievlkda gaaakfgpla angvinittw gprsgelkve vngfagisvk psvdvingrw
      241 erdfrlqfyd ryaskeqfrs fpayladstn styygnadwd eayyrngwvt glqaavsggn
      301 rlanfrfsvg qaaeqgvaek tamrrynvnf ginvmpvknl mwstfisaav inrdrpqllr
      361 drmgdedyil sldkppsssk eqveqyfsyl ekgvdknrna nvrvlntlqy sfgryvklns
      421 rfgidhgqny rdlfipstvn dgnnfvsnyd glhrrlvfdn sleitplqkk gqrlsvtlgq
      481 ynqwdmwkyn ygrafkgksd yiqiyqpgnd dnktgashnl rltanykdrv kanlasfyad
      541 idyalqdkyf fnlylrqdgs snvseaerwq lfptasaswk isgedfmkds rlfsnlrlra
      601 sagrigkvfh ddyykggpvy nveagwegtp nmatynafpv lnaayelgyi spgiawaytd
      661 qlnggldvgv lngrlnfsvd vytrqdknll lkvpamtesg ytgvlmngmd ianyggelgv
      721 navivngknf gwstalnasa nktkllklpg grtdvrmgnr rflvgkpvdk ywllindgiy
      781 atdadvppgm tyqglpmkgg dpkwrdvsgd nniddadrvv tgthnpavqg gwannlryrn
      841 felnmlfrya fggkllnkal adrfdfvnhe gvdaiegvke faywtkpegd lngmyrynpw
      901 spvrayqaeq tlflekasyv klrslsltyn fagawmekkg vrqlrvfvtg nnlftitnys
      961 ggdpeafdyf gydqgvynwp apksytlgfn lqfk
//
LOCUS       WP_119080432            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119080432
VERSION     WP_119080432.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119479
     Region          24..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkllgffl ltllqvtvvf gqdkritgrv tnsldgtpip gvsviiqgtt tgtqtdadgr
       61 yiikapggsv llfrsigfgt ktitvgdatl vdigleattd elsevvvvay gkvkkesitg
      121 svtsvaakdi ekrpitnvlg alegsaagiq vnnttgqpgs epairirgms singdnsply
      181 vidgvffggn isdlnpndia sisvlkdaaa salygnrasn gviiittkra skagdagitv
      241 vanqgiysrg vkeynvmnqq efmetmwkgy rnslmtnnpa typnkevaga kateslidny
      301 ltlniydkpn dqlfdangkl vadarirpgy lndlnwfndi etqghrqdys isgrsnsnks
      361 slyysvgyld ekgylkgsny krftgrinad lqakdwlkyg fnlagshqqs drlpggtgsa
      421 gsivspfnfa rsaapiypvh lhdpatgeyv ldeegqkryd dgsntrswlp grnaiwenel
      481 nkdkvyrnti ngqvyfdikf lkdftfsvkg dlnlrnsdnh tysnavigdg qgnkgraern
      541 nyrymnytaq qllswakain rhnvdvmigh enfydnynyl ngyktnetfa nqlelinfta
      601 itrltdyqhn yrtegyfara rynydekyyi dgsirrdgts rfskdarwgt ffslggswli
      661 skedffqpis nvvnyaklra sygevgndag vgasvlypym alytlgqnan vaalyksqls
      721 alalhwetss svtaaletrl fnranltvey fdkrsqnlll dvnlplsaga tstaeaaaim
      781 rqnvgsvsnr glevsldvdv vktkdwtwnv ganatwmkne ivrlseqnkn giiegnykyt
      841 vghgiydwwt yqfagvdqmt gnslyvldsd tykpdattge hlkylvning tyyttyhtya
      901 krdfvgspmp kmfggistal tyknfslsal mtyatdfkiy ddsyldlrtm sgtpesmhkd
      961 llrawdgvpa gmtetspnri dpkgipvvdf arsqynnvms sqylqngsyl viknisltyn
     1021 lpssllnkid issvrlnagv enlatftklq gmnpqqqfng rsvnawvtpr visfgvtvgl
//
LOCUS       WP_119080475             938 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119080475
VERSION     WP_119080475.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..938
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103875
     Region          50..936
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkkyampff fgvtaaalca rpaaaqedtl arkmpaypnv pahagrvlpl kdtvpvlfgq
       61 qqgasllqsy givygeelrn tpvttlentl ygklaglyle qfslnpgdda asanlrstlp
      121 lividgvprs glsidpeqva svtilkdalg tamygmrgqn gvilvttrhg yngkkrisft
      181 aqtavqqmvk tpkflhahdy aslynealan dgrqpaysaa dleawrtgad plghpdvdwy
      241 ntvlkdqagm qrynlniagg nrisryfvdl dylnqqgyfk tdsrntyptn nfykryifrs
      301 nvdveltrst lmnlsvygri rngnepgart dsifrnilst pnnaypvhnf dgslagnnqy
      361 tnniygqatr sgyrptynrn lsvdlslrqr ldvllqglfv kglasfnsyy dealnrsksf
      421 avynvalnpg adtvinqigs dgqqsngssi tsqtrqayte lqlgydstfg khgvsvtgly
      481 yrdsytdgnv lplvnsafsa raaynydlky llevtmaysy nnmyskgnrw gyfpavglgw
      541 niarenwfrd aapaistlkl rgsyglvgns lrsgyysylq ffnfngtynl gnpatgvsti
      601 geaalanpfl twekarktni gldvathndk lqftaeyyvn klsdlvmyrg tnasgvigat
      661 lpvenigrst qrglelsaay reqagvlgyy vkgnvtfart rvddmdevnr ryswnqrtgq
      721 pvgqifglva dgfyqskedv ensatldgys pvpgdikykd lngdgtinvf deraigsdkp
      781 lifygltagi swkgidlnmv wqgvgnrnin lngsntwefl nnangapgqa mehhlgrwtp
      841 ataasatypr lsvngnvnnh rtstfwvkda sylrlktlel gytlpqhwvr ylhlqsvraf
      901 asgynlltft plsrvdpesy lggypnqrii nfgvniql
//
LOCUS       WP_119080641            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119080641
VERSION     WP_119080641.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110432
     Region          34..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrsplrlrqr rwqalpliil fqllacvaia qvrisgkvts psgdalpgit vqlrgtstga
       61 ttdaegrynf ttnakpgnyt ldfsgigfks apqgitigss pvtadavmqd dvlnmdevvv
      121 igstlrqsrk qlgntvnsvs akqltntgsg nlgaalqgkv pgaqitqtsg dpsggisirm
      181 rgtstikgss eplyvvdgvv vsntttnvtn lnvnagesaa lgtnrmadin pndiekidii
      241 pgasasaiyg srasngvvli ttksgkagqm kidfgtsiim nelrkkvyis tygkqfgstt
      301 lrlgnisdgp apnvmytrpd gqvrrlatgl vdvtrydyqd qifdtglgtd nyvsisggse
      361 ktkyyfsggy yknegiirnt dfrrfnfktr veqvinehlt laggityans fsnekpngnv
      421 fwspintini tnniynieer daagnlkgve ptrvnplsvi edmhltqavs rtisdiqvki
      481 rpveglnidy ilgvdnfsqe gnnlierypy iaaqeglgyv stamvnsffi nndlnisynt
      541 kfgdfssltt agfnhqyqki tglfnegrdl lngitsinga atrldprytl dqrqifggfl
      601 qetfgyknia fitaaaridg stsfpkdtrt yfypklsasw slsdmgfwag mgnwfnsarl
      661 raswglagnl tgigsydqfs tylplslngl atynvntrlg nsdveperss eievgtdlsf
      721 lnnrlgvift vydkkivgns llvdrvlaps sggservenv gnltnkgwel ginatpvsnk
      781 dftwtvggsl arnknlvtss sqvtpimlan aagslsviva gepigvfygn yferdgkggm
      841 aldaegrpia aidpttkvll rrvigsphpd wlvsfnssls ykklslsfll dgalgqevfn
      901 adrrtrqgvg igdysereik gelprgyifa iynteewrve sgsfvklrev alsyelpsfa
      961 kfiksasvsl vgrnliswdd ydgydpetna ggnsatlrgi dfgnvpiprt fqlslrasf
//
LOCUS       WP_119080494            1152 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119080494
VERSION     WP_119080494.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1152)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1152)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1152)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1152
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1152
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125706
     Region          124..1151
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqksftkfia pflvmlvlcg slpsraqetl vrgaaksagk vallkvltgl earfkvhfsy
       61 nyeqvadkyv aassagnleq qlermlppvg ltavklgega yairpraaaa epkiaaprav
      121 dlavrgqvtd eqgqavpgvs vqekgtsngt atdgngrfsi rvasagsilv fssvgyqtre
      181 vaagngnvnv qlsqdvrsle gvvvtalgik rqekalgysi atldaekiat vkdvnvvnsl
      241 sgkvtgvnvr atssdpgatv lvnirgqsrf gdasanqply vvdgvpiasa vrtprqpvgq
      301 svvdygstvs dinpddiasv tvlkgasasa lygsraingv ilittksgsg akkglgvsvn
      361 sssmfdrawl fpnfqnefga gdragsdeti spatwgprid igtkhvqwds pldangdpip
      421 tdwvsypdrh kdfyqtgvtl tnniaitgnn kdgnfrlsyt nlmnegvipn tdlkrntlnv
      481 aagynlsskv rvstnigytk nksdnrptfn rgsvgnivyt ttpnvdikkl rnywvpgkeg
      541 leqfthlpgd mdnpyfvayq finafdrdrl tgnvtvnidi tkdlslmart gldmfsenre
      601 skrpfgsirn ptgayaiete tfreqntdfl ltykknlnpd wfisvsggan rmdqsgtstv
      661 qsseslvmpg lynisnakag tvfnnswrqr krinsvlgtg hvayknyafl dltarndwss
      721 tlpksnnsyf ypsatlslil tdmfrissgp lsfaklranw aqvgddtgpy qlyntysfgq
      781 dwgdvkranm qfalknnalk pliatsvelg tdlrffngrl gldftyyntm irnqivnips
      841 tmasgysskl inagkvqnkg feiglsgtpv kgaftwdvnv nftrnrnkii eltegltgfl
      901 qggaegvqye vregqqlgdf yarkwatvpd gpykgeplld sdgsnqrlnq yekignynpd
      961 fmvginnsfr yknftlnalv dwrqggqfys yvaknllsdg rttttlggrd pqsggiawnd
     1021 gtndrtdgmi lhgyiedgag gyklntkvtd penyygeyyw dynsrstfda syvklrelsl
     1081 tymfsqktlg rlpvsnvsla liarnlftwt aaeqgydpet smtisngsfs pgvtswgmpy
     1141 trsfgfklgf nf
//
LOCUS       WP_119091992             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            paracholerae].
ACCESSION   WP_119091992
VERSION     WP_119091992.1
KEYWORDS    RefSeq.
SOURCE      Vibrio paracholerae
  ORGANISM  Vibrio paracholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio paracholerae"
                     /db_xref="taxon:650003"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53945
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag vlasfddaay taagatigsr
       61 deiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqdsgiv
      481 tflafiavli asinifggft vtkrmlemfr rn
//
LOCUS       WP_119081218            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            alhagiae].
ACCESSION   WP_119081218
VERSION     WP_119081218.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga alhagiae
  ORGANISM  Chitinophaga alhagiae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Chitinophaga alhagiae"
                     /db_xref="taxon:2203219"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113748
     Region          23..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkvllfls lllqvaafaq nvtvtgtvrs asdntpligv siavsgttrg tttnqdgryt
       61 ltvpgdavli fsflghatqq vpvngrtsvn iqlqaggsdl aevvvttalg ikkqqktlgy
      121 avqevsgetm aktktttvlg altgkvagln innttdlfrn pgvslrgrsp lividgipdp
      181 dadpyklnad diesvsvlkg taagalygam gvngailytt kkgnkgklqv efnsstmfqp
      241 gytvipevqt vygggdqgky ayvngsgggt egggwiwgpk ldqrdpstps gfyettqydg
      301 pidpntnqri ktpwvsrgrn niknffrtgl lstnsvsasi gtdkgsfrvs ashifqkgvv
      361 pntelnnssf siggnyqlsp rltmdsklty nreysdnypt vgygppnyly nlilwigpdi
      421 dirdlqnywm pgreglqqrn ynlswynnph fvanellngy krnnsfgqvt fdykitddft
      481 vkfrngfnqy stnselrepn syiaydyisr gnystdvasy fdinsdliln yshrfskdfk
      541 invtaggann yrrfesaytt tdgltipgfy aitntinplk gsnqlrerrt asaygmldve
      601 tfgflylslt grydktstlp vknnayfyps agvsavlsdi ltlpnaisfl klrgswakvn
      661 tgfidgnnpy ahiptyniga kwnnvpslgv psqfispdli petvlsgeyg iaagffqnrl
      721 nvdvtyfrnk dynnfqlvtl sqgsgygsir knanvylrkg wefmvsgtpv rsrdfrweas
      781 vnfsrihrwl kdatdnpdgy lglikegqrt driyitesra pdgqaiynsn gmqaytpvgq
      841 yfglsdpdwi ygvqnnfkyk nfslslsfdg rlggliystt nqkmwwggta kgtvtsyrdd
      901 anagqntyvg pgvvvtggsv tydaygnits dtrkfapntt avnyisfmqt tsggmlnnyh
      961 yysgtylkmr elvltynfpd rwikgtfnga svslignnlf ilskipnvdp daesdnlqtp
     1021 smrsigfnin lkf
//
LOCUS       WP_119109852             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Simplicispira hankyongi].
ACCESSION   WP_119109852
VERSION     WP_119109852.1
KEYWORDS    RefSeq.
SOURCE      Simplicispira hankyongi
  ORGANISM  Simplicispira hankyongi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Simplicispira.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Simplicispira hankyongi"
                     /db_xref="taxon:2315688"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55194
     Region          12..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtsptpavq cigvpretfh gekrvatvpd aveklvklgf kvavesgagd aahcsddtyr
       61 aagaevlpsa aalwaasdiv lkvrppssde valmreggtl igfiwpaqnp elvqqltark
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaaslg aivrandtra evadqvkslg gefikvdyee dgaggggyak
      241 vmsegfqaaq rqmyatqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eaverhgvti igytdlpsrl akqsstlyan nllrlveelc kakdgvavvn
      361 meddairglt vtkdgaitwp applkaapap apkpaavpva ekkgghghgg pvpaknlaii
      421 favaalafwf igayapaafl ghltvfvlac figymvvwnv tpalhtplms vtnaissiia
      481 igalvqiapp eaavngrpgg lilwlafaal vltsvnmfgg favtrrmlam frk
//
LOCUS       WP_119136967             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas reidholzensis].
ACCESSION   WP_119136967
VERSION     WP_119136967.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas reidholzensis
  ORGANISM  Pseudomonas reidholzensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas reidholzensis"
                     /db_xref="taxon:1785162"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38717
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpletq tgetrvaatp etlkkliaqg hqvtvqrgag lnasipdsay eavgaslgsa
       61 adafgaqlvl kvvaptdqel alinsasllv gmlnpfnnet iakmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee recaqgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlpa qvaadasaly arnlldftkl lfdkdgalvi nleddivaac
      361 lmcrdghvir tng
//
LOCUS       WP_119130498             216 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Escherichia coli].
ACCESSION   WP_119130498
VERSION     WP_119130498.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..>216
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..>216
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigiprerl tnetrvaatp ktveqllklg ftvavesgag qlasfddkaf vqagaeiveg
       61 nsvwqseiil kvnaplddei allnpgttlv sfiwpaqnpe lmqklaernv tvmamdsvpr
      121 israqsldal ssmaniagyr aiveaahefg rfftgqitaa gkvppakvmv igagvaglaa
      181 igaanslgai vrafdtrpev keqvqsmgae fleldf
//
LOCUS       WP_119122321             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit, partial
            [Escherichia coli].
ACCESSION   WP_119122321
VERSION     WP_119122321.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..>475
                     /gene="nrfA"
     Protein         1..>475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
     Region          4..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngl
//
LOCUS       WP_119133064             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Gemmobacter lutimaris].
ACCESSION   WP_119133064
VERSION     WP_119133064.1
KEYWORDS    RefSeq.
SOURCE      Gemmobacter lutimaris
  ORGANISM  Gemmobacter lutimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Gemmobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Gemmobacter lutimaris"
                     /db_xref="taxon:2306023"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55636
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreif egenrvaltp dsavqlqklg htcvleagag akagfsdety rkagveivtt
       61 aaelyaaadv vvkvrgpeps evamlrqgqt lisffwpaqn pelleaaker gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aitlafdvrp evaeqiesmg aefvyldfse aqtdgaatgg yaapsspefr
      241 eaqlkkfrel apdidivitt alipgrpapk lwtedmvqmm kpgsvivdla aerggncdlt
      301 vpdekivten gvtivgytdf psrmaaqast lyannirhmm sdltpkkdgv vdhnmeddvi
      361 rgatvtkdga itypppppkv qaiaaqkpke kakeltpeek raqevaafkk qtrdqvlmla
      421 iggglillag lfapasfmah fivfvlsvyv gvqviwnvsh slhtplmavt naissiiilg
      481 almqigsgnw lvvilaaasv fmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_119155216             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Caldimonas
            tepidiphila].
ACCESSION   WP_119155216
VERSION     WP_119155216.1
KEYWORDS    RefSeq.
SOURCE      Caldimonas tepidiphila
  ORGANISM  Caldimonas tepidiphila
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Caldimonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Caldimonas tepidiphila"
                     /db_xref="taxon:2315841"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38562
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipletl agetrvavtp etvkklkaqg hvlrvqsgag vaasvtdeay aaagaeitda
       61 agalacelvl kvrapqpqel almkpgsvlv gmlnpfdaeg lqrmaaaglt afaleaaprt
      121 traqsmdvls sqanvagyka vmlaanayqr fmpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee reaaegvggy arpmppswle
      241 rqkvevakrv aqadivitta lipgrpapvl vseemvrsmk pgsvivdlaa pqggncplte
      301 pgrtavkygv tlvgetnlpa lvaadasaly arnvldflkl ilnkegglhi dlqddivaac
      361 rvtqqgqvtr k
//
LOCUS       WP_119166201             444 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algihabitans albus].
ACCESSION   WP_119166201
VERSION     WP_119166201.1
KEYWORDS    RefSeq.
SOURCE      Algihabitans albus
  ORGANISM  Algihabitans albus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodovibrionaceae; Algihabitans.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Algihabitans albus"
                     /db_xref="taxon:2164067"
     Protein         1..444
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46407
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiailkerr tqetrvaasp esvkkliglg iqvavekgag ngaafvdaay keagaeiagd
       61 aaaalkdakl vlkvrgpeak daadlpkgsl laaildpyrs leemkalaea gvtafamdfm
      121 pritraqsmd vlssqanlag ykavvdaaae fgrafplmmt aagkvapaqv lvmgagvagl
      181 qaiatakrlg alvsatdvrp aakeqveslg gkfvavedee fkqaesaggy akemsdaykk
      241 kqaeliaeti kkmdvvitta lipgraaprl vttemvksmk pgsvvvdlai dnggnvease
      301 agkvavkhgv kiiayhnlpg rlasdtsmly annlfnfval lydkekkdla idwddeivkg
      361 tliakdgkvv hpalenlepa rkpaakkaaa pkaaakktaa kktdpdktep ektsaktapd
      421 sdkqpdtdkt aetgktgeeq kngd
//
LOCUS       WP_119162090             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Propionibacterium australiense].
ACCESSION   WP_119162090
VERSION     WP_119162090.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium australiense
  ORGANISM  Propionibacterium australiense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Propionibacterium australiense"
                     /db_xref="taxon:119981"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54279
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresl pgeqrvaatp ktvpqliklg ysvvveqgag erasylddey eaagaglvdt
       61 etvwasdvvm avnepsveel gmmrpgatli tflhpranpd lvealqkagv tglsmdmvpr
      121 israqamdal sstasiagyr avvesayayg ktfagqvtaa gktapakvlv vgtgvaglaa
      181 vgaaksmgae vfatdvrpet aeqvesmggt flhvraaadd qgvsadgyak etsedynkra
      241 aelyaeqcek vdiiiltaai pgkpspklit admvasmksg svivdmaalg ggncvltrpg
      301 eeyttdngih iigytdmasr lpaqasqmya mnmvnlarla tpgkdgllvi dfddevlrnm
      361 tvtrdgeitf ppppiqvsaa paasagqagp epepekpkke rpwwflllvv gllsvvlial
      421 ltfapgsfvs lfgtfalacv vgyyvvwnvs halhtplmsv tnaisgiiiv galmqlpkdn
      481 maitiiaalg vlvasinifg gfsvtrrmln mfrkgdr
//
LOCUS       WP_119170254             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Shigella
            dysenteriae].
ACCESSION   WP_119170254
VERSION     WP_119170254.1
KEYWORDS    RefSeq.
SOURCE      Shigella dysenteriae
  ORGANISM  Shigella dysenteriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Shigella dysenteriae"
                     /db_xref="taxon:622"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53531
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg enkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpsdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarml
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_119171641             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Shigella
            boydii].
ACCESSION   WP_119171641
VERSION     WP_119171641.1
KEYWORDS    RefSeq.
SOURCE      Shigella boydii
  ORGANISM  Shigella boydii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Shigella boydii"
                     /db_xref="taxon:621"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53644
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkdts
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtsmdkaa dartklarll
      421 atkgiiheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_119182090             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Shigella
            flexneri].
ACCESSION   WP_119182090
VERSION     WP_119182090.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53698
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhh dqylswkats
       61 eqservdale edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakavlda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_119182337             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Shigella
            dysenteriae].
ACCESSION   WP_119182337
VERSION     WP_119182337.1
KEYWORDS    RefSeq.
SOURCE      Shigella dysenteriae
  ORGANISM  Shigella dysenteriae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Shigella dysenteriae"
                     /db_xref="taxon:622"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53574
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwv gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktaml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_119200102             940 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_119200102
VERSION     WP_119200102.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..940
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104185
     Region          11..938
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mffshttphi sqsitlanaq plkvtmgedt qtldevvvta lgikreqkal synvqqvkge
       61 altavkdanf inslagkvag vqissgatga ggatrvvmrg mksltknnna lyvidgvpmf
      121 ntgssggdgq ygsmggsdav adlnpddies ismmtgpsaa alygsaaang vvlvntkkgk
      181 kekisltvsn sttfskayim pemqnrygts sglfswgdlt dkrydpkdff ntgsniinsi
      241 tlstgsdknq tyfsasttns dgilpnnsyn rynftarntt nflndkltld igaqyiiqnn
      301 tnmvsqgqyy nplpalylfp rgdnfdeirl yerydtnygf mkqywpygdg glslqnpywt
      361 qnrirrtsdk krymlnaslk wkvtdwlnit grvnldnsdy rnktekyast latfcsvngg
      421 fedamrqers lytdlmatvd ktfgdfrlnt nigmslyhts mqtigfagdl iipnffalnn
      481 inyaanykpl pdgyddevqs ifanvelgwr sqlyltltgr ndwdsklafs nqssyfypsv
      541 glsavltemf alpkiisyak vrgsytvvas sfdryltnpg yeynsqthnw anptvypmdn
      601 lkpektkswe iglnlkfwen rfnldatyyr sntlnqtfkv dipsssgynk aivqtgnvqn
      661 qgielalgft dewagfrwas natftlnrnk vkrlaggstn pvtgelidmp nmpvgwlgke
      721 nvaprvilte ggtmtdiyvy neltkdnngn ikvdaqtggl smhtaetptk vgnlnanynl
      781 gwtnnftykg inlgvvlsar vgglaysatq gvldyygvss itanardnkg vptnngkvdt
      841 qkyyqtigtg eggygryyly satnvrlqel slsytlpkkw lnnvanvtfg lvgrnlwmiy
      901 ckapfdpels astssnyymn vdyfmqpsmr nigfnvkvqf
//
LOCUS       WP_119200262            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            thetaiotaomicron].
ACCESSION   WP_119200262
VERSION     WP_119200262.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides thetaiotaomicron
  ORGANISM  Bacteroides thetaiotaomicron
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Bacteroides thetaiotaomicron"
                     /db_xref="taxon:818"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120890
     Region          24..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikkvlflfc cmfahviyaq nmmikgtvid anndpllgvt imvkgtttgt itdvdgnfsi
       61 kgktgetliv syigmqtqev vfrgqplkim lkddaqalee vvvvgygtmr kkdltgsviq
      121 vrpdkianen pktvqdilrg tpglaigyna dakgggsmni rgqrsvytdg nhnspllild
      181 gmmfygelse inpddigqid vlkdasaaav ygakaangvi iittkkgkrg kpvvnvstni
      241 gltqrsayre rfspsaylqh yadwkaksty ganaegnwdd yqigvykgmd dyytnpdklt
      301 nidldiwrgy tsnesgesdl siwakrlgft gnvlenilsg ktvdwedkaf rlgfnqdyna
      361 svsgasekvd yyfslgylrn egaliddtyr avranmklna kvtnwfeiga nvnfqdrtdg
      421 sidmdegqfm rnspyadyad edgnpiqypn detysqrgyn ydfqkqyldl ekgytvlnsi
      481 fnakvklpfg ityqfnvapr yqffyeryfm sadlpgsnpn nrgadrehak rfdwslnnti
      541 twdkifdkkh hfivtlaqea eerqrwsdri earniqpsda lgfhntqngs kesssysttd
      601 shetadgllg rlfysyddry mlttsirrdg ysafgstnpy awfpsvavaw tfsnekffqk
      661 iknvmssgkl rasygsngnr sladpytala nlsagsgdym gyltstgeve lmrylmasrm
      721 anptlqwekt kswnfaldfg flndritgtm efytmntndm imsqplpvft gfnnittnlg
      781 qvnntgfefs lntvnikqkn fewnttfnfs ynknkikhlf yeyenvldan snvigqkesd
      841 ytangwfigk pinqiwdykv igiwqndewk eaakykqqpg dpkvwnnpen diynadgsvq
      901 tivyndddkq flgtttppin wslrnefvlw kdltvsiniy srmghkalst nylnndddgg
      961 rmsyaaaclq akeywtidnp tnkygridan gpdgakkpgm lynrsfirle niavgytlpr
     1021 kltqkwgier vkisgtvrnv atwakdweyg dpetgglgtr lyslglnlsf
//
LOCUS       WP_119215401             920 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides merdae].
ACCESSION   WP_119215401
VERSION     WP_119215401.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides merdae
  ORGANISM  Parabacteroides merdae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Parabacteroides merdae"
                     /db_xref="taxon:46503"
     Protein         1..920
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102776
     Region          39..918
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnklitiis lpvlciasvw aqekttgsdm lqfdettisa stvsgkelmk rsninpanal
       61 ygklnglfir qngeygdgeg ypsmnirgig slnnnsilvf vdglerdins lvleeieeit
      121 ilkdaaalap ygirgangvi lvktkrgkkg ktdihvsyqh svttpvrlpq madaatyaea
      181 vneglanegl aprytqqeie ayrsgkyptl fpnvdwfnet lrdhgqrdqv nftasggsnr
      241 iryysminfi sdrgllkntd qgsystqlan silnvrtnld iditsstrvk vnlsgklkek
      301 yspgsisdgv lmetlyalpa naypvrshng iwggsnmypk npvaessstg yttshartll
      361 adltltqdle alapglsaef rigfdayset wdarskqyly esniahldns giptdtvntq
      421 ygkeekqlgf nswlnnqnrh sniqfalnyq kdfsqsnlfa sirykqdknv ylgqyntymh
      481 qdiiasghyg llnkyyldfs iaasgtsrlp kanrwgvfpa isgawllnke sflnnidwld
      541 llklrlsygl tgsddvwknm dkypfggggg fvfgddfian ggiaegqlps lnatfekssk
      601 anigvdiril dlidfnvesy ydhrydimva dgnitsgffg atasnspsgi vnnygvevgm
      661 nvgkqmkdff fnvnaqlafa rnkivnmnea fkpydylkst grrlgqfygl eaigffkdqa
      721 dinnspiqtf stvypgdlky kdqngdnrid eldvvpmgyn ticpelfysm gfdfeykglg
      781 inaqfqgash ytiqrslscf yaplmnnqti sehylencwr sgkdntdaiy prltttesan
      841 nyrgnsvfmk nisflklrsa eiyyklpesc ikslrlrefk lfakgmdlfs idnvnetdpe
      901 viwstypaqr svhfgfdlaf
//
LOCUS       WP_119215499            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides].
ACCESSION   WP_119215499
VERSION     WP_119215499.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113342
     Region          60..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqkqncghp lrrkgsisrv skvtcgllfc lttgvfaage nvelltsdri envvpdqvgk
       61 tvtimvqdem gpvaganvvv kgttngnisd mdgkvvlqnv pnnstlvisf igyttqevkv
      121 snqatihvkl vedakaleev vvigygsldk kqvtsaitsl kaddlmvgvs gadisaslqg
      181 kigglvmnnl gsansgttfq lrgmtsinsg kaplividgf pggdirsltq ddiksidvlk
      241 dasagaiygt raaagvilit tksgsdtngk vrltysneft kkqnynapem lsgreyaehn
      301 igtdygsdtn wwdelinkgn fsqkhhlale mgtekaqvyt sffyeknqgi alqderqdyg
      361 grvnasfklf ddwlevrpav dyrqaarnnh ypnfqqamrn nptrspydpd setgynvwin
      421 esldynvvad amledyygld kwfkpevnlk lnikpipgln yqqvvgyenr qwelhqywps
      481 thrseidnsr kghahlafsk tenltsegyf syvkdfkggh nlnatagysy fevngenfgm
      541 dnynfsvdgi kywdigqgsy ltdgkagmss gksvterlfs ffaranysyq dkymlsasir
      601 hegsskfaad nrwanfwsat agwrisneef mkdfdwlddl kirfgygvtg nndfsatyma
      661 nmlgsdtnwm mpngtwaysy gksqnvnpnl gweekkewnl gvdysffegr lygkfdyyrr
      721 evdnllfsvk vpqppytqgs qmqnigsmes kgwefevggd iirtkdftws ssmnlshntg
      781 kiltlegdns yhngngfvap gtpgdaarme agstigsfym wkfagfddeg sfllynkdge
      841 vipaaqkten dkqyignytp kliigwshtl tyknfdlgin lrswidfdvy ntinmyygiq
      901 gqgnlnvlkd aygkfnhikg ekqicdyfle dgtflkidai tlgytlpmkk ytnnlidrir
      961 iygtvgnvct itgysgmnpe vditgwdkgt ekfwsdfypv vrtwtlgmqf nf
//
LOCUS       WP_119216420            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides merdae].
ACCESSION   WP_119216420
VERSION     WP_119216420.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides merdae
  ORGANISM  Parabacteroides merdae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Parabacteroides merdae"
                     /db_xref="taxon:46503"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122153
     Region          20..>135
                     /region_name="EssA"
                     /note="WXG100 protein secretion system (Wss), protein
                     EssA; cl11266"
                     /db_xref="CDD:299614"
     Region          71..120
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     pfam07660"
                     /db_xref="CDD:429580"
     Region          134..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnknirfpqk ekqpkklira mkffllfall ttgscfaset ysqeasfsmn yenktikeii
       61 neiennsefi ffyldksidl nrkvsinvke qkietildql fsntennysi sdrqiiiskk
      121 etpvntktnq kdtrtisgiv rdnmgpvtga nivikgttng tisdldgkft lenvpanail
      181 qisyigylpq eitvnnqssy nimlkednqs ldevvvvgyg tvrkadlags vavldnkafk
      241 dqpitqisda lqgrvsgvqv qssgvpggtv kirvrgsgsi nrsndplyvi dgivresglt
      301 glnpediqsm qilkdassta iygsrgangv vlittktgka nvrqimfdaq igvgtvakry
      361 etlnpyefat lyntyrketf speqlsafqn gtagtdwlde ifqngitqdy kltlsggsdk
      421 iqyiisgnyv gqegvvkent nkryqarani tsqltdwlhl tadvnashnv krsadfsaak
      481 gnivniamny apvlgimned gtytrdpysa itqlnpvgll neqigesmrd ivnahidlkf
      541 nilpgltftt sngidyndvk nysfattkvs ssssmsnnda yrmtlqttnn ltyngkwgdh
      601 altatavyea tqseyrymni sgnnlmtesv gwwnvemagt rnakndyskw almsgvgrvm
      661 ynykdrymlt gtiradgssk ffnnkwswfp siaaawsmgn enfmqhqnfi qdlkirasyg
      721 ligsqaidpy etlglmtqam yafggnayyt gywigqtvat pdlswetthq fdvgldfsil
      781 nsrlnisfdy fdkrtkdgll krtipnydgg gsywvnaaei snrgidfsin anifessdfs
      841 wntnfngtyl knevkdlagl dfiqganias gmfstdgvtr iavgqpigaf ygyewtglda
      901 agndsfvdrn kdgiidskdr tfigkatpdf tlgwnnslhw knwdlnifft gsfgaerfnm
      961 vrytgtsmtg dfafitlkey lndnfdtkgq sarypsvnvk gnnyqaaats tkylesanyf
     1021 rldnislsyn lpkavskfad lrftfscqnl ftitnykgmd pagisfvdtg tgsvdvndgi
     1081 dlgaypltrs ytfgvrmnf
//
LOCUS       WP_119238243            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Segatella
            copri].
ACCESSION   WP_119238243
VERSION     WP_119238243.1
KEYWORDS    RefSeq.
SOURCE      Segatella copri
  ORGANISM  Segatella copri
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Segatella.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Segatella copri"
                     /db_xref="taxon:165179"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115454
     Region          41..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkktmflgl lgaglmwmpa sailaaqmnn aamsvqqnqg ikgtvvdatg etligasvkv
       61 agttngavtd idgnftlnck pgatlevsyi gyktmtvkaa ngmkitmqed gkalnevvvt
      121 algikrdrka lgygleevkg eeltkaketn vinslsgkva glvvqntagg asgstrvllr
      181 gntemagnnq plyvvdgvpl dntnfgsage aggydlgdgi sainpddiet mtvlkgpaas
      241 alygsrashg vilittkkae kdkigveyng sftidtqlak wddvqttygm gyngalptss
      301 tagtnsswgp kaddfvfkyf dgeerpfmmy pnnasdffrt gftaqnsail svnsgktgmr
      361 fsvtdmrnkd ilpntnmsrd nfnlrvntsa gpvdfdftan ytrenvknrp algdsqsnvg
      421 knlmtlagty nqawlkhyed adgnysnwna ndqynknpyw dlykngntsk kdvfrltgka
      481 iwninkhlkl qgtigtdins mnfedfiakt tpgtpagklt dqifnnrtln aellalynns
      541 wgdfdvnata ggnifkvnnk titntglnqq mngiqnimny qeqntresmy kkqisslyas
      601 aslgykhtyy legtlrgdks stlptnnnty vypsvsgslv fsefiknkkf inygkirasw
      661 akvgsdtdpy qlalnystgk ysysgytigm ianstqpnkd lkptmtgsye vglemkflng
      721 rlgldatyyn qnsknqilsl astttsgyay rlinageiqn qgieialnar alqikdfawd
      781 lgvnfskntn kvkslvdgmd yfelakatwc gvsvgaqvge nygairghdv vrneqgqvvi
      841 daatglpkvd qnvktignss wdwtggfytt fsyknfrlsa sfdvkvgadi ysmsmrsayq
      901 tgkakgtlag reewyaseea rqaagkdisa wresgnckgl vvdgvidngd gtyrkndiav
      961 spedywkhma qnvqsefvyd nsyvkcreit fgytfpesil gkyvkgltvs fvarnpfivw
     1021 knipnidpds syntsglgle ygslpsrksy glnvnvkf
//
LOCUS       WP_119248681             898 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            AM34-19LB].
ACCESSION   WP_119248681
VERSION     WP_119248681.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. AM34-19LB
  ORGANISM  Prevotella sp. AM34-19LB
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Prevotella sp. AM34-19LB"
                     /db_xref="taxon:2292364"
     Protein         1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98983
     Region          39..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meqnlkvily avgamilaph tlhaqsenik gldslrlygs vsvvepellk kgvlnnalda
       61 lngqtagvnv ttngldriam lnsvrvrgtt simggndplv iidgvtsdva tlatiypadi
      121 esftvlknas etalygsrga sgviqvktkk gtgkgfqisy egnygieamf ksmemlnaae
      181 yiaaaqkfgl eynnkgfdtn fskaitrtgn vqnhylafsg gtpqsnyras fgyidhntii
      241 rskgyrnlva kidvtqkafg drltgdfgvf gssyknndif dsqmlfysad amnptypfdr
      301 lngswvknga asqvnppgal leerrdtknm nfnahlklny dilsnlsisa fgaysytsne
      361 nnqfcptwvw aqgnlyrgef kseewlanvs lnyqrvwgih slkamagaey qkdirtgfwt
      421 sakgfsnnsm yyhnigaaas rpfggtdsny edqalasvmg nidytlynky slsvsmrgdg
      481 sslvgddhtw gffpsvslsw dmkqeewlrq lkaitmlklr tgygrsgnlg gisayttmnt
      541 vrqngivsvn sspvvtmgmi rnnnpdlkwe tratwnlgad lglwnnrlvl taeyyysktt
      601 dmlyaydvpv ppfaydklla nigsmsnqgl evgfsitpiq kkdmelninm nlawqknkll
      661 slsgeydgmq msaaditamg alsgagqhgg ynnvvyqivg qplgvfylph ckglvedgng
      721 hyrydiedld kngtvdlsdg gdryiagqat pkvtlgsnis fryrdwylsl qmngafghki
      781 fngtglaytn mssfpdynvl kgapeknivd qnvsdywlek gdylnfeylt lgydipirkg
      841 vvqslrvsas vnnlvtissy sgltpminsy vvnstmgidd krtyplyrtf slglsvqf
//
LOCUS       WP_119249044             945 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Prevotellaceae].
ACCESSION   WP_119249044
VERSION     WP_119249044.1
KEYWORDS    RefSeq.
SOURCE      Prevotellaceae
  ORGANISM  Prevotellaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Prevotellaceae"
                     /db_xref="taxon:171552"
     Protein         1..945
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104901
     Region          35..944
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknnkktiys altvvtalla qlpasaqesa dsamvnvafk kayqsdvlgg vstvnvrelt
       61 eknyntysld nmqgyvsgyn gsgmwgysna lvlidgvpre asnvrpdeie disflkgaqa
      121 tvlygskaan gvimittkrg svndglsvkv nantgwnvak afpeylgsae ymtlyneafl
      181 ndggaennlp ysaetiynya sgknpyryps vdfyssdyik kafnrsevsa eieggnqkar
      241 fyanvsyyrn gdnlnfgeak knytdrfnvr gnvdfalsst inayvnanat fygaksantn
      301 nssyweqart frpnrvapli pvemidpnak saltmigats niidgkyflg gssadltnvf
      361 gdiyasgtnv yhsrqfqfda glnfdlssvl kglsfhtmva idyataysts fnnsyatfqp
      421 twanfngkdv ivglnnngtv dkksgaqnis gstdnqtiaf nahfdynrtf ndvhnvsaml
      481 vangyqqsks aeyhkvsnan mglqvsynyd hkyyadfala tpwsaklpsa krlgvspsvt
      541 lgwrlskekf mensffddlt lsasytdmkt dlgiddyymy lgtyqsggww dwnggsghsa
      601 mqskrgsnne lsylhrkeis atvhaemlnk alsfdasyfl skwtngilea rnqvpsylfs
      661 yypessfvpy infnedkrsg fdfavnykkq fgdfgfgvga nvtyytteat krddsqyadt
      721 yqyrqgqpld aiwgyeclgf fqdendikns ptqiiggtir pgdlkykdqn gdnvidskdq
      781 vylgkggwyg tpttigmnlt lkykgftlfm lgtgnfgaha vknstyfwvg gsakytaemr
      841 grwtketaat atfprlttea gtnnyqtsdf wmystdridl qkvqlsydfp kamfmksfvr
      901 glqlfvngns lltiakerkl mdmnvnnsgs aplnrfysig akvsf
//
LOCUS       WP_119249716            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella sp.
            AM34-19LB].
ACCESSION   WP_119249716
VERSION     WP_119249716.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. AM34-19LB
  ORGANISM  Prevotella sp. AM34-19LB
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Prevotella sp. AM34-19LB"
                     /db_xref="taxon:2292364"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116446
     Region          24..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkrltmlmg glvlstgmal aqttvtgkvv sqedgepvig asvkiagtkt gtvtdvdgnf
       61 tlpnaskdav levtylgmep kkvkasakmk imlvadsrnl devvvtamgi srsskalgys
      121 aavvggekis esrtndvmss lagkvagvqi sstssdpgss nsviirgvss lsgnnqplyv
      181 vdgvplnnss vsssngldng ydfgnganav npddvasmti lkgaaataly gsraangvvl
      241 ittksgkkqn kgigveyngg lqfesvlrlp qlqnefgmgw ygdktdieng swgpafdgst
      301 lkygnvydns qklksylpik nnvkdffdtg lrysnsvsfn gatdasnffl slsqihddgi
      361 iptdadsynk ytfsgrashk iknvtlsmsa nyayqknnfv ttgqktgsmy naimqtprdi
      421 sivemkdlnd pfntpgyyyt pygvtnpyyi lnnykneyes erfygklqfd wdiftdlkfs
      481 trfgldtttg dhntgepnms alyantpnwa dalksltgsv teqterrrem dfnamfnyth
      541 kfidkldvna algfngnerk ytylygavtn ltiptyfnlt nssekptldq yqslrrlmga
      601 ygqvelgwdd wayltmtarn dwsstlpkgn rsffypgvtg sfvfskflsp eaqkivtfgk
      661 fraawgktgn dasvymtnsv yaqasantsg wgsskfpftn gnynaytkgn tlgsntlspe
      721 mttefefgln maflqnrisf dvsyydrnsd kqifslnmdp asgytyqnmn lgkirnrgie
      781 alvsvtpikt kdfkwdlswn ftknkskvis lpeelggesv iygfsggtsl yaivgeelgv
      841 fkaytskrdd qgrlivdang lpqktdkqei vgsmnskyqm gisntlsykg vslsfdfdir
      901 kggvmfsrtk nityftgnai qtaynhrnpw iipnsvvqsg tdangapiyt enttaltptn
      961 iynywnngad nydaeflvdk syvklrsvvl swdlpkawla ktfltgvkvs vfgnnlflwt
     1021 pssntfidpe sssfgndlsg nfgeysanps srkmgfnvsv kf
//
LOCUS       WP_119260906             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [cyanobacterium endosymbiont of Rhopalodia gibberula].
ACCESSION   WP_119260906
VERSION     WP_119260906.1
KEYWORDS    RefSeq.
SOURCE      cyanobacterium endosymbiont of Rhopalodia gibberula
  ORGANISM  cyanobacterium endosymbiont of Rhopalodia gibberula
            Bacteria; Bacillati; Cyanobacteriota.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="cyanobacterium endosymbiont of Rhopalodia
                     gibberula"
                     /db_xref="taxon:1763363"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41033
     Region          2..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mikiavpkes eigelrvalv pdtvarfirl gfevlvqsga glgghftdae ytaagaqvis
       61 speqlwgead illkvappge qhgkmemdwl ksgakiisfl dplgnpekiq elaqrqitaf
      121 smeliprtsr aqsmdalssq aniagyksvl iasaslprlf pmmttaagti ppakvlviga
      181 gvaglqaiat arrlgavvea fdirptvkee vqsvgakfve ipiqentttt ggyakevtqn
      241 tqelirqvlt ehvkksdvvi ttaqvqgkra pvivseemva emkvgsvivd iaadrggnca
      301 ctepgknicy ngvhvigpln lpsslpvnas qvyaknlltl vkylvkdgvm qlnfdddiid
      361 gacvthegql rhpkvkeall rlvka
//
LOCUS       WP_119256637             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shinella
            zoogloeoides].
ACCESSION   WP_119256637
VERSION     WP_119256637.1
KEYWORDS    RefSeq.
SOURCE      Shinella zoogloeoides
  ORGANISM  Shinella zoogloeoides
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Shinella.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Shinella zoogloeoides"
                     /db_xref="taxon:352475"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39884
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msqcvfvare sdpaegrvag svdtvkkmka lgldvmvead aglasrilna dyeaagariv
       61 gkeeaktadv vlkvrrptas eiagykpgai viatmdpygn eaaiaemara gltafsmelm
      121 pritraqsmd ilssqanlag yqavidaahe fdrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vtrqmlaamk tgsvavdlav erggniegse
      301 agkvvevegv rvigylnvpg ripasasaly arnlltflet mvdketktvs vnaedelvka
      361 tmlthggavv hpnfggavhe gegk
//
LOCUS       WP_119272731             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Taklimakanibacter deserti].
ACCESSION   WP_119272731
VERSION     WP_119272731.1
KEYWORDS    RefSeq.
SOURCE      Taklimakanibacter deserti
  ORGANISM  Taklimakanibacter deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aestuariivirgaceae; Taklimakanibacter.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Taklimakanibacter deserti"
                     /db_xref="taxon:2267839"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38227
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavsaeth pgesrvavtp dtikafvkkg levaveagag agafisddaf agagakigkg
       61 daalhdadil lsvrrpeaka tqalkkgavv aaildpygdr pgletlakqg ltlfamelmp
      121 ritraqsmdv lssqanlagy kavidaagqf grafpmmmta agtvppakvf imgvgvaglq
      181 aiatarrlga ivsatdvrka teeqvkslga kfvfadvada ataggyarel saedkakqaa
      241 liaehiktqd ivittalipg rpapvlvtke mvetmkpgsv ivdlavergg ncplskpgei
      301 vthdgvtimg nlnlagrlag nasplyarnl qnfldplikd galkidwade iitgtlvakd
      361 gelvhkmfka
//
LOCUS       WP_119290879             376 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Azohydromonas].
ACCESSION   WP_119290879
VERSION     WP_119290879.1
KEYWORDS    RefSeq.
SOURCE      Azohydromonas
  ORGANISM  Azohydromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Azohydromonas"
                     /db_xref="taxon:312063"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38687
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpleta agetrvsvta etakklkaqg htvrvqsgag vaasvtdaay vaagaeivdr
       61 agafgcelvl kvrgpdadel slmkpgtvlv gmlnpfdrdg larlaaaglt sfaleaaprt
      121 traqsmdvls sqaniagyka vmiaanayqr lfpmlmtaag tikaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee reaaegvggy arpmpqswld
      241 rqkvevakrv aqadvvista lipgrpapvl itedmvksmk pgsvivdmaa gkgpagtdgn
      301 cplteagktv vkhgvtivge tnlpalvaad asalyarnvl dflklvlskd gtfqipaddd
      361 ivaaclmtqg gqvkrs
//
LOCUS       WP_119301168             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Dongia
            deserti].
ACCESSION   WP_119301168
VERSION     WP_119301168.1
KEYWORDS    RefSeq.
SOURCE      Dongia deserti
  ORGANISM  Dongia deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Dongiaceae; Dongia.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Dongia deserti"
                     /db_xref="taxon:2268030"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40156
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,323,325)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,330..331,335,
                     338..339)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvakerr pdekrcavsp dtikkyvgmg vevlveagag egcsipdsvl eaagakivpd
       61 araalseadv vlkvqrplta aeggpdelsf mkrgamlvas lnpyvakdqi ggyaqagiia
      121 camelmpris raqnmdvlss qsnlagykav idaaaefgra fpmmmtaagt vaparvfvmg
      181 vgvaglqaia tarrlgaivs atdvrpatke qveslgatfi avedeefkqa etaggyakem
      241 sdtykakqaa lvaehikkqd viittalipg rkapvlvtee mvksmkpgsi ivdlaveqgg
      301 ncplsevgkv vekqgvkivg hanvpsrlaa dasslyarnl lnfltllidk etkglkinwe
      361 deivkgvalt rdgqiihpnf ka
//
LOCUS       WP_119309288             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cohaesibacter haloalkalitolerans].
ACCESSION   WP_119309288
VERSION     WP_119309288.1
KEYWORDS    RefSeq.
SOURCE      Cohaesibacter haloalkalitolerans
  ORGANISM  Cohaesibacter haloalkalitolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Cohaesibacteraceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Cohaesibacter haloalkalitolerans"
                     /db_xref="taxon:1162980"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55422
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkelf egearvamtp ssakqlqklg fdcvlesgag alagfsdaty aeagveivpd
       61 aaalweaadi vakvrqpese elkylakgkt lisffnpagn eegmaaakta ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv livgagvagl
      181 aaigtsvalg aityafdvrp evaeqvesmg aefvyldfae eqqdgastgg yasvqseefr
      241 naqlakfrei agdmdivitt alipnrpapk lwladmvaam ktgsvivdla aerggnvegt
      301 vkdekvvten gvtiigytdf psrmatqase lystnirhmm tdltpekdgq ivhnmeddvi
      361 rgatvtyege itfpppppki kaiaakpksd vkektpeekk aeeeaalrka grqqisllvi
      421 gavvmgligl yapaafmghf ivfvlavfig fqviwgvshs lhtplmavtn aisgiiilgs
      481 llqlgsgswi vlllafisil iatinivggf mvtrrmlqmf qks
//
LOCUS       WP_119314366             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Calidithermus terrae].
ACCESSION   WP_119314366
VERSION     WP_119314366.1
KEYWORDS    RefSeq.
SOURCE      Calidithermus terrae
  ORGANISM  Calidithermus terrae
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Calidithermus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Calidithermus terrae"
                     /db_xref="taxon:1408545"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39177
     Region          2..359
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvqiavpket apgerrvalt pevvarlvke gcavrleaga gasafftdea yrqagaevvp
       61 aeavlegaqv vltvgpleas alprvsheai ligfqyphrd pkrvealadw gistlameli
      121 pritraqsmd alssqatvag yraaliaaql ssrffpmltt aagtirparv lvmgvgvagl
      181 qaiatakrlg anvwaydvrk aaaeqalslg akvielpisa egeggyarel taeeqamqle
      241 alarqvgqmd vvittaqipg rrapvlvtae mvgrmapgsv ivdlaaesgg nceltrpget
      301 veaggvrvag plnlpselpv hasemyaknl ynlcklllkn gelapdwsde ilagallthr
      361 heithgptrl lvga
//
LOCUS       WP_119338116             530 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_119338116
VERSION     WP_119338116.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54830
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ataadlwgrs divlkvrpps seevallreg stlvgfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgmi nvdfnddair
      361 gltvikegsv twppppiqqp aaapkppaap vaataskghg hgsgepmsak slaivfavga
      421 lafllvgqfa patflahftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa agdrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_119341262             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Meiothermus hypogaeus].
ACCESSION   WP_119341262
VERSION     WP_119341262.1
KEYWORDS    RefSeq.
SOURCE      Meiothermus hypogaeus
  ORGANISM  Meiothermus hypogaeus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Meiothermus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Meiothermus hypogaeus"
                     /db_xref="taxon:884155"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39598
     Region          2..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvqiavpket apgerrvalt pevtgrlike gwgvrleaga gaeayysdea yrnvgaeivs
       61 reelfkgaqv vftvqplerl dlvqlepgti vaglmyphrs parvqamatg klsalamelv
      121 pritraqsmd vlssqatvag yvaaliaare ssrffpmltt aagtirpakv mvmgvgvagl
      181 qaiatarrlg anvwaydvrk aaaeqalslg akvielpisa egeggyarel teeekkiqhe
      241 alakevgnmd avittaqipg rnapilitkd mvermhpgav ivdlaaesgg nceqtqpgkt
      301 vevngvkivg plnlpsalsv hasemyaknl ynlskllikd gqlapdwsde ilagallthq
      361 geithaptka ligga
//
LOCUS       WP_119350687            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Mariniphaga
            sediminis].
ACCESSION   WP_119350687
VERSION     WP_119350687.1
KEYWORDS    RefSeq.
SOURCE      Mariniphaga sediminis
  ORGANISM  Mariniphaga sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mariniphaga.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Mariniphaga sediminis"
                     /db_xref="taxon:1628158"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120900
     Region          26..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknknlktff sglfvlftfy sfaqvqvrgt vkdntgellp gvsiqikgtt qgvvtdmdgn
       61 ysinvpddqs vlvfsflgme tqeinvdgkt mldvemvsss igvdevvvta lgisrerksl
      121 gysvgevsge elasvsqdnv mnslagkvpg vqinqtgaag ssvsvvirga tslttdnqpl
      181 fvidgvpmsn tlnnvsemgn gnqvdygnai sdlnandiee mtvlkgpsaa alygtragng
      241 vilittksgk kskelgvqfs sntlfevptk lldfhykyan gernhvlteg saywagpeld
      301 agiiseqwgl depaelksyp nnmkdfmqtg itstnnialt ggndkgsfri synnmtmrgm
      361 ipnndrfnns lktsinynlv enltfssnvn iartysndip stgdrnnnpl qavysvship
      421 vermkeywlp gqegiqqnel pdsdnpyfia yamsnafsrd riygnaalty tffkdfsvta
      481 rysldrfnek retkvpfsal rmakgnyslq nltfqeynad ilasytkkva dwdvsvsagg
      541 nimnrksads fvgsggdrrn glvipglytv gniplsniqv ssstaekaiy slyglasigf
      601 kntlylditg rndwsstlpe vnrsyfypsa siswlanntf nlpeavsllk irggwakvgn
      661 dtnpyrleps lstgtwnslt tesvsstlln enlkpeeats ieggidfnly nnrlrfsgty
      721 ytmdnvnqif svplprssgy ssqlvnagli rsqgwelsig gtpisnpggv twdinlnfsn
      781 nsttveelid nlefiqiwse nagaysfigd kigdiysygi aqvedpnsey ykwpiidgte
      841 wirlrntedw ekvgnfnpdf ilgiqsgltv grwgisasid wrqggefvsy tyrygesdwk
      901 sqrqldnlip ggmyseqeli allksdpeky iiprrgnypr vgghtqgtgg mlledghydg
      961 afipgvvqva gqdtpddfsd dkyvehlggd gtaiipitdt ypwsynknit fdasfvklre
     1021 lsvsyrlpdi rgvknatiav ytrnlmlwta adigidpera fqanggtqgn tvsqfkqgfe
     1081 rqnvmpwsas cgiklnfnf
//
LOCUS       WP_119350943            1144 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Mariniphaga
            sediminis].
ACCESSION   WP_119350943
VERSION     WP_119350943.1
KEYWORDS    RefSeq.
SOURCE      Mariniphaga sediminis
  ORGANISM  Mariniphaga sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mariniphaga.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Mariniphaga sediminis"
                     /db_xref="taxon:1628158"
     Protein         1..1144
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124592
     Region          37..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikkvihin grifacilsl gilinlfavd aiaqetinvt gtvtsaedgl tlpgvsvavk
       61 gaaagtvtnm dgnynlkvan datlvfsfig fktqevavqg rstinivmev siealeevvv
      121 talgikreek slgfsvgkvs geeltrvaqe nvlnsmagkv sgvtisstgg agssvnmvir
      181 gatsisndnq plfvvdgvpm sntvnnvggf gsdnrvdygn aiadldpesi esvsvlkgpn
      241 atalygsrag ngvvlittkk aqegglkvsv tsntvmdfpv rflgvhtqfa sgffsyrpen
      301 vgggvlpein piegtgagpe ndkgywavqw dspldangvr vptevvsypn nfrnfindya
      361 ftttngasis ssssavnyrl gvtnmvhngl ipnsdlnkns lslsasstpr knltissdin
      421 ftnswadnrp asnrgtnplq wvyshpsnid itklkdygsg ndikrvsggh enpyflandv
      481 nnsfdryrvy gnimatweis sklslmgrmv lnktddvret kiapgytkep nngaygivss
      541 vslernmdfl ftyedswngf alttsaggnv ryaksqsvsn ssksgsglsv pnlftvgnis
      601 sgslvyssyk sqrqmnslya lanlawkeia yidltarndw astlvaskrs ffypsaslsl
      661 madqilnlgd rvdmlkirgg waqagndtnp yrleatygda gqwgdavrla kasgllspnl
      721 kpeiatswei gtdirlfsnr lrfegtyyti dnrnqifyvp lagstgfssi ninagllqsk
      781 glefmigltp vrtrdwkwdl nlnftkndtr ilelseelef vefwdqarvr nigyvkgnsa
      841 gpdglmntsd diyhdgrvgn lysrkvmrvt dpdseyygfp ilgsgldaew qgedeyskvg
      901 nynpdfimgl qssltyknft lnmtfdwrsg gqyvsqsfry lsedsmskvw ldglvhpgdl
      961 ggaasgalrd wvlankeqll lgddlrpvgg ptpefggfpe sfsgvtvydg tfapgvigyh
     1021 dengkfileq enlggegtvf lpyvvsypwd igeanlfdad yvklrevslt ymvpqkfsqk
     1081 lgmqdinlsl ysrniilwtk dsemgvdper ayqaegngrf nqgverynae pwvvpigfkl
     1141 gfsf
//
LOCUS       WP_119350853             940 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Mariniphaga
            sediminis].
ACCESSION   WP_119350853
VERSION     WP_119350853.1
KEYWORDS    RefSeq.
SOURCE      Mariniphaga sediminis
  ORGANISM  Mariniphaga sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mariniphaga.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Mariniphaga sediminis"
                     /db_xref="taxon:1628158"
     Protein         1..940
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104586
     Region          65..938
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqqyiyaky privlytlli fiatnaysfg gkkttiqeis dpdsvtvkde vilpdsnhei
       61 isyntvrndd iiksstytvg nalfglipgl ivrqgsgepg vdspnitirg ygtfgnsnap
      121 lvlvdgfehd lnsisiedie sitvlkdasa ailyggraan gviavttkrg kidrsnievn
      181 vlqgvqtply lpefvgsady atiynqalin dglpalytne eiqnyktgdp iyypstnwld
      241 kmvknvtpat klnvnatggn dkiqyyasig ylsntgiynh tekhegystn ikyeslsfrs
      301 nldiklndew nvkidmqgkl dnknapvdst ssiwnalyky ptyipvyakd gllggtsyyp
      361 enpmglinek ghmnihkrhl ltnitteynl erlvkglkig grfgydnyyt vtdgwqksfd
      421 sysvlgkdei tgepilssay gaktvltyfe pederqslrl nvqgyidyst elgssnqlna
      481 kvlyhqdelt lgsespyytq siggiidysi kdtyfakagm tysgseafkk gnrfalfpsi
      541 sagwilsnes flkdskvidy lklrasagtv grsdlglrfa yrdyykyfgs ysfgtsgiyg
      601 ggliqsdasn pdltfekadk feisfesvil knvnfsatyf ldnrrnilvs rnniapsiig
      661 iefrdvnage aksyglelsl ginkstnngg yfaqlnytlm gsevlynael pvpegseyyy
      721 rtgnqigqaf glefagffds hedianspvq qfgevnpgdm kykdknndgy vneydkgpig
      781 dtglksefgl ilgsnykgfd iqaviqgrlg ssmymggysq iywplineng vstyildqtp
      841 wtesdkahan ypklttvass nnyrsssfwy kdadfarlrs aelgynfses lasrckaeki
      901 rvflrgtnlf tltnleygdp ermtsypamk tynvgvnvqf
//
LOCUS       WP_119351218            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Mariniphaga
            sediminis].
ACCESSION   WP_119351218
VERSION     WP_119351218.1
KEYWORDS    RefSeq.
SOURCE      Mariniphaga sediminis
  ORGANISM  Mariniphaga sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mariniphaga.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Mariniphaga sediminis"
                     /db_xref="taxon:1628158"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116919
     Region          24..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkhlivtft llltlisgvy aqqrsikgtv tsasdglplp gvtvvvqgvs slgtvtdvdg
       61 kyslsvpsea kvlvfsfigm erkvaeigss gvldvelvms tealdevvvt algisrqtks
      121 lgysvqeveg keltearetn ianslagkva gvqvtniatg aggssrvvir gnssisgnda
      181 plyvvdgipi dnqnldsphy asggvdygdg ivnlnpddik smsvlkgpna aalygaraan
      241 gvivittksg karkglgisv nsnytfedva tlptyqnkfg pgyfsadgfe pigttiidgk
      301 eyevldprmf ayfgprlegq lvadwqdptk vmamnpqpeg nvrnffqtgy tatntisftg
      361 gneqstfyls lsdlrnegii pgskynrqsi nfrgttnitd kfsidakvny vhhegnnrpg
      421 lsanssnima qliqwpnhid mdrlknykde ngnpvnwttr yenpywtine iqnedardrv
      481 igfvslkyef tdwlslqart gtdfytdqrf erravgttsa rtglvsnytf hvmennsdil
      541 lmaekdlssn fsgsltlgas hlysknevtg mkgialrtpg lyhidnaaqi tprhrkvqre
      601 mnsvfaagql gyknylfldl tarndwssvl gmnnysffyp satasfvltd alqmdsnvln
      661 fgkiragyae vgndsspylt sfgyqslset vqgqgqaeiq rripnpdlkn eltqsyefgt
      721 dlrlldnrvr vdftyynsst knqilpvnis satgfeqmvi nageitnegv ellldvtpvq
      781 lsnsfrwdvt fnyaknkskv vsladgieth emsrdrwgti earpgydfgn ivgyafkrne
      841 kgekllndng myqrdpdevk vlgniqpdwi ggitnrfsyk gfslkalidi kmggnllsgt
      901 kyiqtargta kfteegvyen aeghwvgvad gvmendyyve dengnmvlhl qageksdiel
      961 erlflhgwyt radiieefvl dasyvslrev slgysfpasl lrntpvsnik msvvgrnlly
     1021 ihenmeglgi spegafssas gaqgsesytl pstrsfgfnl tvef
//
LOCUS       WP_119351933             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mariniphaga sediminis].
ACCESSION   WP_119351933
VERSION     WP_119351933.1
KEYWORDS    RefSeq.
SOURCE      Mariniphaga sediminis
  ORGANISM  Mariniphaga sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mariniphaga.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Mariniphaga sediminis"
                     /db_xref="taxon:1628158"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40755
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgllkehg tetrvallpd ivqnltdlkv evlveqeage kafvtdaaye eagakivtrn
       61 eifeksevvl qiqlpltnev dklkgsqvwi safnplwetd lvktfqekgl ttfsldsipr
      121 ttraqamdil ssmatvsgyk atleaalklp tffpmfmtaa gtirpanvli lgagvaglqa
      181 vatarklgaq vfvfdvrsav keevkslggk fvevegated kdaggyaveq teeyknkqqe
      241 ainaqaiksd viictaqipg rkapllvpke tvekmkpgsv ivdlaastgg nceltkndet
      301 vhfqgktiig qsnytslmpi dasrmfgknv lnflkliige egalnlnfed divkgtcith
      361 qgelynervk stienk
//
LOCUS       WP_119351885            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Mariniphaga
            sediminis].
ACCESSION   WP_119351885
VERSION     WP_119351885.1
KEYWORDS    RefSeq.
SOURCE      Mariniphaga sediminis
  ORGANISM  Mariniphaga sediminis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mariniphaga.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Mariniphaga sediminis"
                     /db_xref="taxon:1628158"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123887
     Region          135..1115
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkifcltgfl qketkkkwgr imrltfllmv gfilstsans ysqntrmdik lkngtiidli
       61 ayvednsefv flyknedldl ekklsveled atiykvldva fkgqnvawdv ydrqiiirkg
      121 antvpwvqrd mqqqktvtgv vtdqegqplp gvtvvvkgtt tgtvtdndgg fslripndae
      181 ilqfsfigmk tqdvsvagkt tftvsmeeet igleevvavg ygsmkrsdit gsissvnmes
      241 lknqpvrgls dmlsgrvagm nlsrtsgdig aptkirirga nsiegdnspl tvvdgvigap
      301 igpiqdvesi evlkdasata iygerasngv ilvttkkats aepvirlsln tgfsyrnidy
      361 pdkmnaaeya eyindynqaq tfsaaeitef rntggtnwld aitqtglknd hqisysqkld
      421 klsvymsary ddekgtmint esggnyslrs kvgfqpskrl tmdlditask sktkngglst
      481 gtskhhpffq alnwsptepv wldeengiyn ntdhhgalld spymyameqn nfredhsvas
      541 ilnanykitd ylsysvtgfa sksgtasgsy ynawlepndp ygrrsqserf dwrlinkidf
      601 nktfaeahnv mvtgvyeaea legwslngtg kkmplpdlas yytigisneq stssgydkas
      661 riaymgrlny nyksryyvta syrvdgksgp anrveenkfg gfpsfaaswr lseepfmkan
      721 gifdnfkira gwgqtgnpsd fvytimksnn ydygidanvl gyipgkpanp llkwetttqi
      781 dfgldittfn gklsvsfdyf dkltedlltl lelpvyygya tdgaylqnlg evsnkgfeft
      841 vdfkpvqtrd ffwdvnfnvs tvknkvldlg eqaafmtgtn gngmlsenty rvqedlplgt
      901 iwgykwlgiw qeseaaqaet ygnvpgdyky edvnndgayn lnddgqaigd anpdfvwaln
      961 nsisyknfdf slliqgmqgq dvfnlaraam stvhadarti mlkapatdyw tptntdaeyk
     1021 sihstsdakr lnssqwiedg swvkvkhvgl tynvprnwvk fgtlaltvsa qelltftnyk
     1081 gldpevsasg ssdlwggcdf gtqplpttvt fgvslef
//
LOCUS       WP_119354483             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azohydromonas sediminis].
ACCESSION   WP_119354483
VERSION     WP_119354483.1
KEYWORDS    RefSeq.
SOURCE      Azohydromonas sediminis
  ORGANISM  Azohydromonas sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Azohydromonas.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Azohydromonas sediminis"
                     /db_xref="taxon:2259674"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38687
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpleta agetrvsvta etakklkaqg htvrvqsgag vaasvtdaay aaagaeivdr
       61 agafgcelvl kvrgpdadel slmkpgtvlv gmlnpfdrdg larlaaaglt sfaleaaprt
      121 traqsmdvls sqaniagyka vmiaanayqr lfpmlmtaag tikaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee reaaegvggy arpmpqswld
      241 rqkvevakrv aqadvvista lipgrpapvl itedmvksmk pgsvivdmaa grgpagtdgn
      301 cplteagktv vkhgvtivge tnlpalvaad asalyarnvl dflklvlskd gtfqipaddd
      361 ivaaclmtqg gqvkrs
//
LOCUS       WP_119360147             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Meiothermus luteus].
ACCESSION   WP_119360147
VERSION     WP_119360147.1
KEYWORDS    RefSeq.
SOURCE      Meiothermus luteus
  ORGANISM  Meiothermus luteus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Meiothermus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Meiothermus luteus"
                     /db_xref="taxon:2026184"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39529
     Region          2..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvqiavpket apgerrvalt pevvgrlvke gvgvrletga gaaahfsdea ywkagaevvh
       61 reqlfsgaqv vftvqplptp elarletgti lvglmyphrd pervrtmatg nltalameli
      121 pritraqsmd vlssqatvag yvaaliaare ssrffpmltt aagtirpakv mvmgvgvagl
      181 qaiatarrlg anvwaydvrk aaaeqalslg akvielpisa egeggyarel teeekkiqhe
      241 alakevggmd avittaqvpg rrapvlitad mvermspgsv vvdlaaesgg nceltrpget
      301 veingvkvvg plnlpsalsv hasemyaknl ynlskllike grlepdwsde ilagallthq
      361 gqiahaptra llggs
//
LOCUS       WP_119364497            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Emticicia].
ACCESSION   WP_119364497
VERSION     WP_119364497.1
KEYWORDS    RefSeq.
SOURCE      Emticicia
  ORGANISM  Emticicia
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Leadbetterellaceae.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Emticicia"
                     /db_xref="taxon:312278"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114372
     Region          33..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meqnyqskdm kswlrlmall lclsplsifa qtkqingqvt sstnkdpmpg vgitvkgttr
       61 gtttdasgkf kieaastetl vfsfigfisq evkvgnisnl dvnlvedtqn leevivtalg
      121 ikkeskklgy saesvkvnei qqnrtvnimt slegkiagld itppssgags stkirlrgqs
      181 afagannspl ivinglpmdq gargangnas idlgdnmqqf npddvesmtv lkgataaaiy
      241 gsraangaii ittkngnknt gigveysany ssdevldftd fqyeygqgqa gvrpttqgqa
      301 ittgqfgwga kydgqptiqf dgvsrpylpa knrikdfyrn gsaftntial sggnatgsfr
      361 asfsnqdalg ispnnnyhkk ifnaginqsi sknlsmtfni nytneinnnp pqvgvqgvgt
      421 pnflyrlsns igldvlqeka vadngterqt sgfqttlinp yyimdrqfik nkrdrflsta
      481 tvkydilkwl yiqgrvnmdy gvtfleqnlp tgvgtstlln qagtgyngty gvnsstgrqm
      541 nmdfllagnk elgnfsidas fggniftnrn rtfdqsvtdf tvkdlysien gitksqtygv
      601 yneqvnslyg laelgykdlv ylnltgrkdw fsvlnpqnns sfypsvsgsf ifsellrdvs
      661 wldygklrgs yadvgssngi nafsglltyg ilqnpfngyp lgninntnsp npllrpfsvs
      721 ekeigielkm fksrvnldva yydkqtrdqi ltvvvsnasg yngtplnlgs lqnrgfefml
      781 dvvpvktsnf mwkasfntai nntkvlslap ntnrlvvtsf ggneflgslv yevgqplnql
      841 aaktyrrnan gdilvgtngr llasegadvl fgsalpkfig gwnntfsykn lsllvhidyk
      901 aggkvlssta lnglrqghtk aslvgreggv lfpgvyange kntvkvdpql fytdyrnlqi
      961 adpflfksdf iklrnitlny datrflsskv kfikgltlsa scrnvliikk yiddldpesf
     1021 assgdsrvgy eqtslpttrt yginlnvkf
//
LOCUS       WP_119377203             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Henriciella mobilis].
ACCESSION   WP_119377203
VERSION     WP_119377203.1
KEYWORDS    RefSeq.
SOURCE      Henriciella mobilis
  ORGANISM  Henriciella mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomonadales; Hyphomonadaceae; Henriciella.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Henriciella mobilis"
                     /db_xref="taxon:2305467"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38947
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkltilkets pgetrvaatp esvkkliglg hsvtiesgag taagfpdkaf seegatiakt
       61 aatalkgadl llkvrapsae eagkypeglt vialmnpfnm gdltdaynak klntlameft
      121 pritraqsmd alssqsnlag yramiegaqi ygrampmmmt aagtvapakv fvmgagvagl
      181 qaiatarrlg gvvtatdvrp aakeqvaslg akfiavenee fkeaetaggy akemsddykk
      241 qqaeltanhi akqdivitta lipgrpapel vseamvksmk pgsvivdmav asggncplsk
      301 pdevvdvdgv kvagfsnlpa rlpadsssly aknllaflpl itaedgalnl dtddeivtam
      361 lltrggetvn erlks
//
LOCUS       WP_119368418             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_119368418
VERSION     WP_119368418.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38817
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqrgag lnaaipdsay eavgaslgna
       61 adaygaqlvl kvvapndqel alinsgsllv gmlnpfnsel igkmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvqengv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_119370438             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas monteilii].
ACCESSION   WP_119370438
VERSION     WP_119370438.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas monteilii
  ORGANISM  Pseudomonas monteilii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas monteilii"
                     /db_xref="taxon:76759"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38760
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipleid pgetrvaatp etvkklvaqg hsvvvergag vhasipddaf iaagaavdar
       61 stvftsdvvl vvnpplgvdl avmkrgavlm gmlnpfdsdl iammaesgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr flpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslggkf ldvpyetdee recaegvggy arpmpaswmk
      241 rqaqavhera kqadivitta lipgrraptl isaetvaqmk pgsviidlaa aqggncpltv
      301 agqvvikngv tivgqtnlpa lvpadasaly arnlldfmkl linqdgelti nldddivaac
      361 lmccdgqvmr ans
//
LOCUS       WP_119378437             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Henriciella barbarensis].
ACCESSION   WP_119378437
VERSION     WP_119378437.1
KEYWORDS    RefSeq.
SOURCE      Henriciella barbarensis
  ORGANISM  Henriciella barbarensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomonadales; Hyphomonadaceae; Henriciella.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Henriciella barbarensis"
                     /db_xref="taxon:86342"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38937
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkltilkets pgetrvaatp esvkklvgld htvtietgag vaagfpdkaf sdegatiass
       61 agdalkgadv llkvrapsaq eatsypeglt vialmnpfgm gdlltafngk klntlameft
      121 pritraqsmd alssqsnlag yramiegatl ygralpmmmt aagtvapakv fvmgagvagl
      181 qaiatarrlg gvvtatdvrp aakeqvaslg akfiavende fkeaetaggy akemsddykr
      241 qqseltathi akqdivitta lipgrpapel vtedmvksmk pgavvidmav atggncklsk
      301 pdevvdingv kvagysnlpa rlpadtssly aknlvaflpl itaedgslnl etddeivtam
      361 iltkggetvn erlks
//
LOCUS       WP_119392018             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Taklimakanibacter lacteus].
ACCESSION   WP_119392018
VERSION     WP_119392018.1
KEYWORDS    RefSeq.
SOURCE      Taklimakanibacter lacteus
  ORGANISM  Taklimakanibacter lacteus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aestuariivirgaceae; Taklimakanibacter.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Taklimakanibacter lacteus"
                     /db_xref="taxon:2268456"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38245
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavsaett pgesrvaatp dtikafikkg fevaveagag sgafisddaf agagakigkg
       61 eaalkdadil lsvrrpeaqt trslkpgalv aaildpygdr pglealarqg ltlfamelmp
      121 ritraqsmdv lssqanlagy kavidaaaqf grafpmmmta agtvppakvf imgvgvaglq
      181 aiatarrlga ivsatdvrka teeqvkslga kfvfadvada ataggyarel saedkakqaa
      241 lvaehikaqd ivittalipg rpapvlvtke mvetmkpgsv ivdlavergg ncplskagev
      301 vthqgvtimg nlnlagrlag nasplyarnl qnfldplikd galkidwade iitgtlvakd
      361 gelvhkmfks
//
LOCUS       WP_119393215             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salinibius
            halmophilus].
ACCESSION   WP_119393215
VERSION     WP_119393215.1
KEYWORDS    RefSeq.
SOURCE      Salinibius halmophilus
  ORGANISM  Salinibius halmophilus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Salinibius.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Salinibius halmophilus"
                     /db_xref="taxon:1853216"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54554
     Region          7..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpfqvvipre tvagetrvaa tpdsvkklik lgytvavqsn agqhanfade dytsagaevi
       61 adtaellaka givlkvatpt daeidlipsg ailisyiwpa qneallkkla ergintlgme
      121 siprlsraqk mdalssmsni sgyravieaa nhfgrfftgq itaagkvppa kvmivgagva
      181 glaaigtakg lgaivrafdt rlaakeqves mgaeflelef eedgsgeggy akvmsdefik
      241 aemelfrqqa eevdiiitta lipgrpapkl ileevvktlk pgsvivdlaa eqggncectv
      301 pgevvtkhgv tivgltnlat hapaqasqly sqnlvhlltd ltpekdgepf inmddevlrg
      361 atvvkdgeit fpppplksqq dasakksapa peapvkpekk pmsgkaiagf waiafaamlg
      421 lgqvsspefv qhfvvfvlsi figwqviwnv shalhtplma vtnaisgivi lgtllqlggv
      481 ggsglilala figtlvamin vvggfyvthr mlamfrkd
//
LOCUS       WP_119398562             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudooceanicola sediminis].
ACCESSION   WP_119398562
VERSION     WP_119398562.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola sediminis
  ORGANISM  Pseudooceanicola sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudooceanicola sediminis"
                     /db_xref="taxon:2211117"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55323
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspkevf agearvamtp dsalqlqklg hecfvetgag tvagfadaay eaagvtvvad
       61 eaalfaavdv vakvrapsde eaklltsdqt lisffnpagn tdllelckaq gatvmamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigaatslg aityafdvrp evaeqvesmg aefvyldfee kqtdgaetgg yasvsspefr
      241 eaqlakfrei apdidivitt alipnreapk lwladmvasm krgsviidla aerggnvegt
      301 vpdekvmten gvtiigytdf psrmaaqass lyatnirhll mdltpakdgv inhnmdddvi
      361 rsatvtrgge itfpppplkv kaiaaqkpke kakeltpeer raaevaafkk qtrnqvglla
      421 igavlllgvg lvapasfmqh fivfvlsvfi gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsw iviilgalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_119405019             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Henriciella mobilis].
ACCESSION   WP_119405019
VERSION     WP_119405019.1
KEYWORDS    RefSeq.
SOURCE      Henriciella mobilis
  ORGANISM  Henriciella mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomonadales; Hyphomonadaceae; Henriciella.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Henriciella mobilis"
                     /db_xref="taxon:2305467"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38933
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkltilkets pgetrvaatp esvkkliglg hsvtiesgag taagfpdkaf seegatiakt
       61 aatalkgadl llkvrapsae eagkypeglt vialmnpfnm gdltdaynak klntlameft
      121 pritraqsmd alssqsnlag yramiegaqi ygrampmmmt aagtvapakv fvmgagvagl
      181 qaiatarrlg gvvtatdvrp aakeqvaslg akfiavenee fkeaetaggy akemsddykk
      241 qqaeltanhi akqdivitta lipgrpapel vseamvksmk pgsvivdmav asggncplsn
      301 pdevvdvdgv kvagfsnlpa rlpadsssly aknllaflpl itaedgalnl dtddeivtam
      361 lltrggetvn erlks
//
LOCUS       WP_119406682            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119406682
VERSION     WP_119406682.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115159
     Region          24..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllvslc llvlsitqvf aqnrtvtgtv takddglpip gvtvkvkgst igtqtnaagk
       61 fslsipanat lvfsfisyet qeiasgqrlt fnvvlvsask qlgevvvqga lgvkkqarav
      121 gyastnvdnk llteakvtna angltgkiag lqvntvnngv npdtrivlrg nrsingnnqa
      181 livvdgtpvs naflnqinpn didnitvlkg agasavygse gsngvvlvtt krgggvptvt
      241 ysnttqvenf syfpklqrqf gggageiidp ltgaygyvpy enqsfgplfd gstvplgapr
      301 sdgstpmvky sstgkdprla vfntglteqn disyqygddk gtfffsaqdv ytkgvvpndr
      361 nrrdgitvag srnygifktd yrvqytqtnt svsgpdffqg rgfywnvlnq qanapltdyk
      421 dlnsrygsvd gfynayypnp ywqtvnsrqv trkdaligna tisinpvkwf easykvsasy
      481 gwqqyratna qvdfspyaia dtytdadgnt yrtgniasqv kfkpgsvada dvfgdgtgng
      541 ysrlqgdlfl nfkhkigdft gslllgnsiy tkklkfvqng annlllkdfy nlayrtgdvt
      601 astgyleqnl vgflgdfnls ykdwaflevt grrdktslls kqnrsffyps aklslvltda
      661 ipslkkidfl sylkvrgsys kvgqvdvspy alqnvfasag gypygsiasv alssnlnnpn
      721 lkpelsyeqe yglelglfdn riyinssyyn thtknqtfgv aispatgyst avqnagelqn
      781 kgwefevkas pvvksggfsw dlganfsiyn skvlsllpgv qsfnipfasg akstsyaivg
      841 kpypmimgtd vnrdpqghvi vdaisglpsl nqtnqelgna apkyilgfnt afrykfvtls
      901 avaeyrggys iynavgraln ftgtsaisas agrqpfvypn sviqtganty vpntnvsvnd
      961 gnagfwtnsa yytstatyvs saafwklrev alnfdlyqfi kgqkyikglt fglvgrnllm
     1021 frpksnpwtd peysvdnsna vgittedqtp ptriyganlt vkf
//
LOCUS       WP_119406754            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119406754
VERSION     WP_119406754.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112692
     Region          25..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqmylrcta vllfslmtma ayaqkvvtgt vtektgqaap gvnvtekgtt ngtatnvngk
       61 ftltvkpgai ltfsfvgykt qevavgqntt invvmesges slnevvvtal gikrekkslg
      121 yavqevkgqt iadrkeaniv nalsgqvagl qitrssngpg gssritlrgn nsltgtnqpl
      181 ivvdgtpldn fignennnnd yynpgrdmgn gladinsddi esmsvlkgpa aaalygsrag
      241 ngailittkt gksqnglgit ftssfgfesi farpkmqtvf gqgtgggfvn tsdqswgekn
      301 ggqsqtaldg tkfaqnyndn ianyfqtglq smqgiswqqq ykstsvytsy nrlddksyip
      361 gaklirnnlt artvskfgsn drwtvdtkvq yinataknrp qsgynpnnyf yyletlpnsi
      421 dvtsyknpln sagnmrwwhd gpdlnpywas kyslnedird rfllnasiky qfnkwlnveg
      481 ragadkyttn aenrlyagap gvtggsygvr rtsftetnys mlftakkdnl fgkwggvatl
      541 ggnlmdrnrs flsasagtln vpnlfsinnv vgnpvlgqgl yrhninsvyg slginydqfl
      601 ffdgtfrndw ssalsaanrs yfypsatgsl vfsellnrng nlpswitygk lrgsyaavgn
      661 dmdeyqlvnt ytiskdplgn ttasrndvlf dpnvkselik syeaglemrf fgsrlgfdfs
      721 vyktnatrql inlpmdnlsg ytsrkinagn iqnkglelmv dgkiftgrgf nwntlvnfsm
      781 nrnlvkslta dvsqyalggy dniavvaqtg qiygtiygtt fkrvtdansp ykgqlilsna
      841 glpqtddgvk snlgnqqass llgvtnsfsy ksfsfsflvd arfggkifsg tlqkmqalgt
      901 asntvvggdr kdfvvdgvvl ntstnqyqkn tvavspqnyw aavagrgnlg iteaniydas
      961 nirvrnvqfs ydlpkslmts lgmqrakigv sannvwliks hlngmdpesv fatgsnatgf
     1021 esgsapttrt illnltvgf
//
LOCUS       WP_119407307            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119407307
VERSION     WP_119407307.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114177
     Region          27..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkiykvlla vllpfiliqt vaaqsvkisg vvtakadglp lpgvsvsvkg kntggqtdvn
       61 gkfsvtanvn dvlrvayigy ttqeipvtsg taslnvvlie qpnalnevvv talniskdkk
      121 slgysvqglk skdiseaket nfvnalagki agvqvtnsqg dmgssrivir getsiskdnq
      181 plfvvdgviv dnsqilgtng srdfanalsd lnsediesvs vlkgpnaaal ygsraaagvv
      241 lirtktgkga kglgvtvnsn tsfanvnilp dyqnqygqgs ngkfsyvdgk gggvndgvde
      301 swgpaldgsl ipqfnsngqa vpfvahpnnv rdffktgvtl nngvaiasst eksdfrvsyn
      361 nlhqtgivpn tsqgrnsfaf nssyrinnkl tvntivnyik ddadnlpgty gkratstmlq
      421 ftwfgrqvdi sqlknykdan gntfnwnnsy ysnpywlaye ntvgqhknhl igsielnyki
      481 idglsanfrt gtdyyndrrk ikvafgtngt pfgsyeeday avnenntear lqytkklnnd
      541 fsldvfgggn iavktieqnd qiapklavag lytltnsrdp lvssnnydkv ktysyfasaq
      601 vgfrnyafln fttrndwsst lpkdalsyfy psvngslvlt ealdiksdil syakvrggws
      661 kvgkpalayq lknlfttlal fggypqqsis tvdlnpnlkp etttsgeagf elgffndrih
      721 ldvsayntns vnqivtvdvs pstgfsqkli nggsinnkgi evqlgltpik skgftwdint
      781 nyslnrskvv kldaegrlqs ivlgsdrtvq vlaalgqpyg tlygnayqrn pqgqiiigan
      841 gtpvinptkq ylgkftpkwl gsinnsftyk ginlsflvda rfggsiysnt nrtgtytgvl
      901 astlpgrgaa ngglsyyypg nntsaaavqv tgaapagvtv yndgmifkgv kadgspntti
      961 lpaqsyykgf tnvdeafvyd asyiklrevk lgyslpakwi kkigfqgatf svvgrnlwii
     1021 hknvpnidpe tafnagnaqg ledltlptvr nigfnvnlkf
//
LOCUS       WP_119407598            1144 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119407598
VERSION     WP_119407598.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1144
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126764
     Region          135..1140
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkltflynav cairgvkyki llvlklttil llvgalhlsa asysqtvtls gknksvqsvf
       61 tdikrqtgyl ffysdkvnlk gktidadfhn tqlvdaltac lknfdlsfti vgktiviqnk
      121 ipepepapvi aankipvsgr vvdsvskttm pgvniaikgs kgvigqtnek gefnvqadag
      181 qtlvfsfigy ksaevkvvpg qsivvkllpd innikdivvt gyqvikkdny tgnaisvsga
      241 dlkrnnpqnv ikaiasfdps fkvldnnfag sdpnklpkin vrgataipsi nddildrnnl
      301 ssnynlpafi ldgfevslqk vvdldinrie svtllkdgaa tavygsraan gvmvittkap
      361 vagklqlsyn yeltfngpdl sdyhvlnakq kvdyerlvgl ystqtptsgd tkqdeldaql
      421 ftrlknvasg vntywlsqpl rnayqqkhsv yvqggdqsfr ygldmryqtq pgvmkgsdnt
      481 rysggvnfty npsskliirn dltitqvnqv nspygnfaty vnanpyfpir dstgrlvqel
      541 anwrintfrk gsdqyiteni fnplyeasls nfdksaytei leslsadykl skglrlralm
      601 svnknnstsd hyvsplssaf yntaadklnn rgsydygnng slrldgnvti nynkmlgdhy
      661 fnlvlganil asktdvksfs aqgfandrft nigfariyke nsgpfgditk srtagaffsg
      721 nyafqnkyll dasvrvdgss afgadrryap fgslgigwni hkenflqgsk visqlrlkgs
      781 iatlgsigfp ayqsrsiyly dtqhwystgi gatilgygns nlewqktrtt dvgmdiglfk
      841 drivispryy ykltkglitd inlapstgft tykdnlgdms nrgyelylva qvfhttdwni
      901 nvtgnlahnd nkiisisnsl kafnnnidnf qtntdnnafs tpltryvegk slttiyavks
      961 lgidpqngke llvkkdgtlt ydwnvkdvqd vgntapkaeg ffgtsvsykr flmsvsfhyr
     1021 fggqafnqtl idrvenadpr fnvdsrvleq rwkkpgdhtf fknitdltdt yvssrfvqkd
     1081 nlielqslyl sydfklaair rlglqnlrla atandifras tiqaerginy pfarsltfsl
     1141 lgsf
//
LOCUS       WP_119408781            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119408781
VERSION     WP_119408781.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116233
     Region          29..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkhilfyiv lavcitlfct eayaqaqnit vtgtvlekat nkilpgvniy lgnkgliqtd
       61 ykgkftvsvp anstltftfv gfvtekvkle pgqknitimm tedkkglnev iivayqnrnk
      121 esspgasvti takdiqdvpt snvenllqgk vaglnvqnnt gapgfrgsvq vrglsalsvs
      181 gsgsesflqp tsplyiidgv pldadkaaef gfqtqgpgvs plslipvedi qsiqvmkdaq
      241 atsmygsrga ygviiittkr gnskvprvry tgnffvnatp qlratiggna errakiqqil
      301 snatiidelr rlgqtgflad slnaywnnst nwqsifygtt hnqshnvald ggndrfnyka
      361 nmgvysekgv ikntgfdryn lnmnmefkpn dkfrffgslf gslgsqakgn gvgllqqgva
      421 angqastllp ppsfylspdg vtsalqtqns nstrnirtnv dgryefikgl alsssisydy
      481 tsdaestftp aaanaqfaqi ydyagrnytl ynrnaityah tfgadhtifv ntfneiykqg
      541 gqsgiirqtr ipndqlqgpv gsdsynsrgg gvlsnyrnat iasfagsfny dykkkyvlel
      601 syrldgtssn glenpysknp aagfrwnyyk enwfknwdwl tsgglrlswg qnivptgtlq
      661 siyglynlng nfnnnptigi nyefipnpal kpttttqynl gfdmtilqgk vdltfdtyyk
      721 kvdnllfdrf lsnstgfqkk ssndvsiadf gyelmltvrp ltakdfnwtv sfngainrdy
      781 llrlpaeyng qyikfdynnr qhivfrvgkn tlsnylltnq gvystdgdvp vdpvtgkkyq
      841 tgglafkggd prfkdvngdy ilddrdyeit gnsqplitgg mstninyknf glniyatyta
      901 krtilnnals drlsimrdpy allaavpldd ldiwrkpgdq skypnpyafs rfnqiqplrs
      961 dqslwqeegs ylkintvtls ymfdrkfvrq fgfnnvrvyf stnnlitfsg yngpnpenvt
     1021 slgrdissgy pvprtynlgl nielntsk
//
LOCUS       WP_119408636            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119408636
VERSION     WP_119408636.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110582
     Region          31..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfkhllnkl ilpllcvfmc fnntyaqtvs lkgkvtdekg eavagasvkl kgtnkgsvtn
       61 vsgafeisyt gngtlvvsai gyttaevkls gqttinitin sdskalnevv vtalgikrdk
      121 riltystqei ksesitqske pnianaiagk vsgvqvtsss gtpgssariq irgntsfygt
      181 neplmvidgv pvdnsetgnl nsgpgtnria didpsiiasi nvlkgaasta lygskgangv
      241 vmittkngal nkkplitfts dfsfenpllp qiqnkysqgt ngiyyngetq ktstswgarm
      301 dtlkingqpa kvynqsdlff ktghtynntv nigggnnsst ylvsysnfnq qgtvpttkfl
      361 rntffakyst hildnlnttf qlnysnsqnd rlpegyales pvwtiftapv synlqpstna
      421 dgtqrlyrfs rnnpywvldn iknhsgvnrf lptftadykp lpwltiterf gadiytemdr
      481 yhestqsvsn pngrlvdqnt nyrqlnndli vsankqfgdf nvdlvlgnni lssysentya
      541 ngvgltvpgl ynmssastvt ykensylsrk vgfylqsnie ykrflilslt grydgnsvls
      601 tehnfypygs aatsfifsef fspefskimn lgkvrvsygt vgndggigpy glltsyniat
      661 irnltfpyag qagflisdiy gnpklkneri nefetgfeag ffnnrislea sfyskktidg
      721 iipsvaiaps tgyaytsvns aimrnrgiei llnvnpvktr dfnwdltfnf trnrnkvlyi
      781 yqdqqqlgng fnfitvgqpy gviygtryar naagkiltgd dglpfaddnq giigninpkw
      841 lgginngfry kqfnfsfffd ikhggdiqnn vdgygyfygt pkvtenrgpr vvdginattg
      901 qpntvsvngq qyyqringvl esviqdgsyv klrnvslgyt lkpswlaksp fksatfsvtg
      961 rnlwihaphf tggdpevssf gasngsqgiy sfstptsksv dfslkvtl
//
LOCUS       WP_119408818            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119408818
VERSION     WP_119408818.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114334
     Region          45..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekkikasgm mlssaisvlf tlmcaadvra enavgarisv einvqtvtgk vldekgnpla
       61 gvsvsekgtk ngvvtdvngn yriqvatdna vllfsyvgyn lktepvngrs tlnvslepks
      121 taiseiivta lgikreskkl gyaaenvrvg eittnrstnf vnslegkvag ldisppasgp
      181 ggstkirlrg qsafqgdnap livlnglpls qspsstngyt qsvdlgdnmq qinpddietm
      241 tvlkgataaa lygsrasnga liittksgnk nsgigiefts nftqnqaldf tdfqyeygqg
      301 ennvrpktqg qaqssgawsf gekfdnapty qfdgvqrpya pernriskff rlanawtnti
      361 afsggndkgs frfsysnqda qgiipnndyh kkifnlglny nftpklsaqi yvnydhennn
      421 nppvigiqgs svtnyiyrys nsvsldvlka aavdangnet ptsrfttltn pywimnkqft
      481 kqtkdhllgt atlryqffdw lylqgrvnme ystsyyeqns ptgtlanaaa pvglyngsyn
      541 sndntyraln adfllggghk wgpfsfdatv ggntfpsssq gytvtatnfy vrdfytlgng
      601 vtntsafavs kstvnslygt aefgyksylf lnvtgrndwf svlspehnhy fypsvsgsfv
      661 fseflknpps wlnfgkirat yanvgsangi spysnsltfa lsqnsfngip lgsinnvttp
      721 nqaikpysvk ekeiglelrm fnsrvnldva vydkhttnqi lsvaisnasg ytgtivnlge
      781 lrnrgaefll elvpirkpnf swrsafntai ntskvlalan gqkqltlgtg effgsivdqv
      841 glplnqiqgs tyrrdangki ivsggkpvas tlpalfgsal pkatggwvnt ftykrftlma
      901 hidyktggki lsssnlnflr eglskeslvg reggvtfdav nadgtpntta vnaedfyany
      961 rsqgildpfi yksdfiklrn vsvsydfskm mkakfikglv lsavchnvlv ikkytpnidp
     1021 eaisssgdil tgyeqsslpt trtyglnlnv kf
//
LOCUS       WP_119409002            1059 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119409002
VERSION     WP_119409002.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1059
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118569
     Region          29..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmikknfyif cifqlyaaac fsqgrgsmsg rvinsadkap iskafisike wqrstlsdkd
       61 gaflfakpgk dqrlnvhvsc agfhnidtiv iinekpvilv mkpllinine vvvntgyqki
      121 sperltgavs tvsrsmierv vstdvlrplq dvvpglifnh dltagqnsis irgtstiygn
      181 aqplivvdnf pydgdisnin pndvesvsvl kdaasasiwg aragngvivi ttkkgrlgsp
      241 tqisfnsnlt igakpglfyq pkmssadfid vekllfsqgy ydglektsdq spvspvvdll
      301 fktrnglvtq qsadqsiavm ktkdirndla kyfyrnsvkq qyslnisggg dnnlyylsag
      361 ldrnresevr ndfsrvtvna sntfdflnhk lslntafnfv ynkaavnsni ndltwnngta
      421 lypyaslada rgnalpvvrd yalsfindpa qqklldwnyr plddlrqqqn ysysrdlrlq
      481 gglkykilsw lnanlqylye rsennnenlh neqsyftrnl vnsftqvaad gslsyvvprg
      541 sildtynsvl esnnvrllvn adknwdnvhh iefmggaelk svnvksgnnr kygydeehdl
      601 nsnvdyvnly plyynpgskt nvpnyitngd ltdhyisyfa natytfndky iatasgrvdk
      661 snlfgvktnq kgvplysagl awriskekfy nvsflpdlkf rlsfgyngni dktlsaytta
      721 qyfgssvsqi rqpyaqiinp pnpelswerv kiinagidfa skgrrlsgsv dvyqknginl
      781 igdmpfapst gilsfrgnta dtkttgidin lvtqnltgqf kwntatlfsf vhdavsryqt
      841 fysgqqyiqt qgipvqgrpl yaiysykwgg ldhdsgnpqg yldgklsqgy gsivnattkd
      901 nmiyngsarp vffgavrnnf syrnfslsvs inyklhyyfr kpsvdyttvl sgiggngdys
      961 krwrkpgdel itnvpsapdq idyyrehfyt yssalvekgd hirlqdiqlg yqwgkifiyg
     1021 yadnvamiwk atksgydpdy vvsgylpprt vslglrsrf
//
LOCUS       WP_119409296             945 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119409296
VERSION     WP_119409296.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..945
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107301
     Region          13..943
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnniirrtly nkladsvtkk pydlskfpav slqqllkgqf aglyvqepsg epgtvqnmfm
       61 rgapmpllsq rdvyqsqplv vldgiplvte hpfaydiqly dynrlgtatn pfahidmnni
      121 asievlkdls atavygprav ngvivltskt pvaaksitfd syiglaqrph vntingkyen
      181 afrqrfydly ttngrysdde nypiylsdsl nnvysgksdw sdlyyrnavv yginfgisgg
      241 tdranfrfsl gdlknngiad gtvlnrysam fninmkpikw llfsamvnan rldrqrnkyl
      301 rdrfaqinyf pdlsaplppn keyyadylaq ykkgfdnnki nivdgyakig idlgrfkftt
      361 tfnvdynegy rdvfyartll qgnsyasnyf gysqrimadn kasydltlnk vndfhfevgq
      421 stqwdtykys nayaykgvnd yikidlldsn pknpdgsdnp nylnptafpr eltfrfldki
      481 rhnlvsfyak tdysfkekyf isatvradgs snaqptsrwf yspvlsaawn ikkelldnst
      541 iindlilras agrlgrlnaf dnyaqgpqyt asvgytgnlt vpgynafgvl trpyatgwvg
      601 ygipwsysnq lnigadagfl nnrlhlsvdw ylkqeknlli gipafaeygy kqsiesgmav
      661 nnsgidvsis adiirntnfg wtsslnlnrn snklkalprg lnqiivnnrl lkvgspvdqy
      721 wllindgiyk sesevpvvng qplkyngial hagdprwrdi ngdnaidnnd kvlkghslpk
      781 lsggydnnfr ygnwnlninl yfnlgrdlih qemasrfdfi nregnsdvns vkeitfwekr
      841 gdynkyplyn pwstvipyrv dqdlflenas flklrtvsig ydltkamrlk kirltrfyvy
      901 atannvftit pytgqdpelv sydgydtgyg lpiprtytlg vkmel
//
LOCUS       WP_119409805            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119409805
VERSION     WP_119409805.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118403
     Region          24..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllaswc lfmlfisvah aqnktvtgrv tskddglplp gvsirvtgtt lgtqtnangq
       61 fvlnvpssak slsfsfigyt srtveigngp ldvklesaan klsevvisga ygtkqtsrsa
      121 syaaqvvksd elntirqpni nnalagkvag iqvrsqsaaa lgrgtnirlr gavgfgsgnn
      181 plyvvdgtil pnsddlnpdd mesvsilegp aasaqfgsqg afgaivmtsk kgkkgrgtgi
      241 elnvganfdr ayilpnyqnt ygggasadfi qyhwkqgdpe gwkaldgkyy pdytddsswg
      301 prmvgqeyip wyawaagtky sfktakwnpe pdnakdffqt gialnngiaf skagddynvr
      361 msynnqntrg ivpetklnkn ifnlnvnldl nkhfsagani nfvgtqlngq isdayasats
      421 gsfnswfhrd ldmgimkelq dlkspdgtyv swnhqnpnsy dpahpdqfya gnywynpylw
      481 qkqwrnlnqr drfygsvyfq yninkdlnfk vtyrrnqtnt wnegkissei qasgtqtgqk
      541 aaygtsnsys nrenyetlls ynkqikdfhv nanagtdiyn wsykdnsast vnglsvpnly
      601 sisnsvdpvs vgngrtqeqy ravfgkasig yksivyvdgt lrndwystlp kangansvls
      661 ksfggsfifs ellpgyrdwl sfgkvraswg qipralstgt etfgayvnnv vygvaankfn
      721 gyllqggpnn fvdpnlhgst tetvevgfnl gflndratfg atyyaakdkd fpqslnvnra
      781 sgvsfiqtnv gaikrkglel maggtpiklp nfswtinanf aqlidntvte isdkygvdrv
      841 qvagvwgtdm pylinqkgkw wgqiygngik rnangvpilt asgmyqndpn vyfgsalpky
      901 tgglqnsftv fkdfilnvnv dyqfggkfvs lsnrwgqfsg ltantaalnd kglsvrdpve
      961 dgggvkvtgv dannnpvtyy vdakayyqgl tnnktydpyi ydltfiklre valgynlpik
     1021 kwglgktlqs arfeltgrnl lliyakskdf dpseitateg etaqypgtrg igfnlrvtf
//
LOCUS       WP_119409762            1138 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119409762
VERSION     WP_119409762.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1138)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1138)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1138)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1138
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1138
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124163
     Region          31..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqnllkisr llllfvvclf tysnlqaqsl tirgiildda nqplpgvsvr ikgtntgtvt
       61 giegrftiaa tkgdvltfnf vgyasqevti gtetylsiqm ksdsksltev vvtalgvkke
      121 vrrigyssqd vkgeeltkar epnainslvg kvaglnvgvs aellgrpqlv lrgstdllfv
      181 vdgvpinsdt fnisaddvet ytvlkgpnaa alygfrgqng ailittkrgt kdkrgfsidl
      241 nsstmlekgl vavpknqtdy gygtayaydy gsglystaat agsgsfrani wgpkfdgqpv
      301 rqydspidpv tgirgtspwl argknnyenf ietgllsntn laigasgely dlrasyahny
      361 qkgtgpntgl nadnlnlslg ykisnklrvd gnlnfntqys knipdagygp nsypymfkvy
      421 gsaswdvrdm edyykapagn plgkpgvtqy yaeygrennp yfvanewlrg hyktdvygyl
      481 kltysfnkdl nlavrsqvtt wdqlrtekvp sstvlnsyla psgspfktwd atytgdfrqd
      541 hrnlienntd vllsynktik dfnisalaga nsrsykyvsd wsstnwlqsn gsqldnaays
      601 lnnsknsaar vyaynanmqv ysayysvdig yknyftlstt grvdktstlp sgnntffyps
      661 valssvisdy vkfpevisfl kvraswadvk galtsstips ayaastnftk tvnsgllgyg
      721 telyssydgp syanqlglss gtyyngtssi aisntlanpk vnpfdvgsye ggldvkffnn
      781 rlsfagtyfr tvngpsifpl gipsstlyya htenavtslk kgfelsldga virnpngfsw
      841 nilvnystfk etlkdiygde ksipinnhvy kigdrldgyy gikflrspdg qiinnsagip
      901 lpsqsgidnl qylghlnpdf sfginnkfsy kafslsfqfd grvggkiyde vysrmmnagt
      961 aietvqgayg aarladwnsl vstgkvgnng lgsyvgpgvv iasgtpkyan gvisnlnelt
     1021 fapntvpttv qnyasnglfn qnideaflis rtyaklrevt igytipqkfl gksfirrasi
     1081 tlvgrnllyf aarkdidldq yasgfnlstl gtqgvkglss dlqsstsrry gvnlnfgf
//
LOCUS       WP_119410198            1155 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119410198
VERSION     WP_119410198.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1155)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1155)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1155)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1155
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1155
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125919
     Region          113..1151
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklwlltml fflqlpfsal nakaqtvink ritfgadgim lkeafqqvek lsdisisynn
       61 tllddtrkvk vakaertvee tlnillkgtt ctfrqagekn iliiaktqdk gsikgkvvde
      121 kaqplpgatv ripgtgasai sagdgsyvln ivpgeytvev sfisfetkri qnvsvtsnaa
      181 ttlnvtltpa dnklnevvvt algikreeks lgyaatvvkg dqltgalagn wtdalsgkva
      241 glnlirsnsg pagsnkiilr gennltgdne alivvdgvvi nngsgrrtgv sgetpygvas
      301 dnmpadygsn lndlnpedie nvtvlkgpga aalygqrgan gaiiittksg akhnglgitf
      361 nsnaslesvn rwpdlqyeyg qgtagsryys fgagpdgast satssaygpk fdgqmfyqld
      421 pvtqkqstvr tpwvpyknqi rdffdvgqtf tnsisidggt dktsarfsat nvnnhwitpn
      481 tgytrnsial svtskindkl tisakvnynn knsdnlpgag ygnqslmywf ifwqpnanln
      541 wlknywkngq enkaifypfs sfpenpyavs yefinksnrn avtgniealy nitkelslql
      601 ratldmgyeq raqqrpydag tkyplgsyrt qniyseekgg dfllkynkki trdftvtata
      661 ggsmlrnnyn rdevradslv ypgvysmann agplvtlpyk akyainsfyg llstsfkdyl
      721 ymdltarqdw vstlatanrt dkvgffypsa slsflpseaf klpaainyak lrasiagvgs
      781 gttrpyqtsf nyvtagstya gglqnprtls npdlsplrtt tievgaearf fnsrlgfdla
      841 lytgstrnqi lsrtvdqssg fsqavfnvgk vnnkgielal ngtpirkanv fswnisatfs
      901 ankntieqla dssvvlrngp tgggqivakv ggsmgdmygr gyqrapdgqi vydpatgfak
      961 lasdlvylgn tnpkwkasmg hdfrykqfnl hllfdaqvgg vaysltnykl aeqgkttitl
     1021 pgryngmigk gviqnadgsy rpndviatdi dgyyrshygi dnaegntfst nflkfrearf
     1081 dytlnprfvk rlglqratig vygrdlyiwt kwpifdpefg tlntnadggs divqgfeiaq
     1141 fpstrtfgfn lvigl
//
LOCUS       WP_119410205            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119410205
VERSION     WP_119410205.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116572
     Region          25..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkftlifv llltlltqaf aqdvtvkgav sdnlgqplpg vtvknkatna vtvtdvkgny
       61 sitansdatl vftfvgfttq eqkingrttv nvtladankq leevvvigyg travkdvtga
      121 issvraekle nehpasttdi irgnipgisv glntsakggn tgdlqirgka slsgnvqpli
      181 vldgviypgq ladinpndie rvdvlrdpsa lavygsqsag gvvaittkkg kktstqitln
      241 anvgvaqllq nqkyytgegf lnwradgars sntsnpyyyy snpnklpdgv tlqqflngat
      301 gdpttiwlqr lglfpneian yqagkvtdws klifrngfrq dytaslsgss etvkyyisgn
      361 yvknqnliqg gqysdgrirv nlegkaakfl tigvnaqfgs rdegatiqtn tynnipmsnq
      421 aidateadwg qiinsspygd vynadgslrr idtddsglnq rnpflgqryn qnvavqntlf
      481 svifarldlp fgikytvnya pdlewyrnff yrpvanpnel sggtasrsqe sryrynldni
      541 lswnktfgih nfdatfllnk erfqswttta snsqltptdi lgyhniaagn lpvlgssdvv
      601 yagdaimgri nytllnryiv tatirrdgfs afglahprev ypsaavawif sdepfmkgda
      661 fkwldygklr fsygangnrt stfnpdpsis lavlggvkyp tannsgtitn tngiyvatlq
      721 naqlkwertv gpnigldftv lhnrlsgsid vydrkttdll vkrsildlqg ynssgdlvgg
      781 snnsnpftni gqvknrgfei sldgkiiqsq nfkwsasgtf flnrnkivhl ygafpvtdan
      841 gvttnvekdd igngwfighd inavwdykil gtwkteeatd aakygakpgd fklqdvdgdf
      901 kftnadkqfl gstnpkfsws lrndfnflgh fdvsfllvsn igqlkqynqa lnnpgsvgfa
      961 rmnsyvlpyw tpdnqindya rlnsgssgtt invwrknsfv rlqtasigyt fskellkrvg
     1021 itsakffvna snaavfsswp lwdpqnngpt prylsagfnv vf
//
LOCUS       WP_119410352             947 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119410352
VERSION     WP_119410352.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 947)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 947)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 947)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..947
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..947
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104939
     Region          48..946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkdyknfla wmlafcsysa vnaqtakttp adtiktanss ykdivdgglr iqkswrntga
       61 vftlsgedlt rmtsgnllnt lqgripgltv vtgsgepgyd nptfymrgqs swniqgnqvl
      121 iyldgfqvdm gaitglsaye iesvtllkda aalavygleg gagvlsirtk kgavldktqv
      181 fingkygils pielpkvmda fgyttnynna ltndglpiky anpelykasn dpfhpnvnwy
      241 dqllkktsai qdynfgfrgg nntakyfvlm nytnfegmyk nadiidkdfg tnakytklnl
      301 ranielqlnk nlvvtanisg itedrntpsg ftasqvfnni maipaaafpv knpngswgns
      361 svykfnpvql lqqngvyqsh trnlqtnfsf vqkldkltpg ldlkgevsfa nqyigiyqkq
      421 fsvnsfeivg qdpntgnaiy gstpvtpisq sssdgggahw nrtsvrlgfd ydrtfgkstf
      481 tgmiqarrqg ythdgivyqv rtqglagnit ydydkkyiid lsgsysgsad fapgnrygff
      541 pavglgwils kedflrdnat fnyvklrasy gtvgnineay rflyqqfavg angwitgtgn
      601 tyhggltegp fanldfawek kttlnvgvdf tvfknlsgtl dvftekrkgi leipsagvpd
      661 ytgfnlqyan tgevqnkgle aslryeqndn kfkyyiggsv ayarnkitkr senpqpynyl
      721 ytqgyeigqm kglvyqgfyq qsdfdangal kqgvvassyi nvkpgdlkfk dqdgngiind
      781 ydkvplnynk lpeitlgfnl gfkyagfdfd aylqgvlhrt vsllddayty thpfvynnni
      841 safsanpwtp etantatspr lstlsnpnnd qqsdfwmrng nflklrsvel gytipqlgfl
      901 kkidavrvfv ngtnlftwdk ikgleaerls mgyplvkavt fgmkvkl
//
LOCUS       WP_119411375            1018 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter celer].
ACCESSION   WP_119411375
VERSION     WP_119411375.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter celer
  ORGANISM  Mucilaginibacter celer
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Mucilaginibacter celer"
                     /db_xref="taxon:2305508"
     Protein         1..1018
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110406
     Region          23..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklymlvvf laccimyasa qeitvkgtvt dsqnsplpgv nvritgttkg tstdvngkfs
       61 lqapgngtlt fsyigyvsqt vsisgktvvn vtlandskml emvtvtalgi eqktktltya
      121 tqnvggaele kvkdanfvns lagkaagvvi tkgtggpgsa srielrgaks iggnsapiyv
      181 idgipigqga ggvnsglgdg agidplsnln pddiesiqvl kgasaaalyg saaangalli
      241 ttkkgkagat ridfnssssf etavglpvtq trygrtapga ndmwggkssg atnafikgfy
      301 ntgqnflnsv slssgsekaq vyvsyantka ngivpnnsll khnftlrgtg kflddkltld
      361 gsvnyiyqkq enppkagryy spmfglylfp tddnfskydk dhfevydpsr klsvqnwpym
      421 knefssnqnp ywianrdlse nfssryissf kakydiakwl fiqarttlda ynyrnefkay
      481 attdaiilgd lgsrngaynv nqgygthlys dflasantsi tknvsleatv gvsddrsfdy
      541 stytgssysf gmpyanyfsl nnydldhpfd inenegkgin qavfgtatig yketvflnat
      601 grnewsyttp ksyfypsvgl syvltktigt sdilsfaklr atyanvgkap grgannynpp
      661 ysinhttggt nainnlpyfd qeknyypsvk pertktyefg aqlklfdkld idlayydaht
      721 ndqiitiaap tasgaqnfil nggqirnfgf egtigynarf gdlqwtpaln fsrninqvrq
      781 lsplftadry tiassddsrl vgtyltkpkd gkygafgdyy graiiknpdg sikvddqglp
      841 vltdaastyv gnpnpkflag fnnnfrfkni nlsflvdsrf ggqvfsytet wldykgasqr
      901 sadardaggv lvngkkvnah dyysrvsgga dngavpeyty satnirlrel tlgytfklgd
      961 ksfknlnvaf igrnlfffhk nspfdpeqsi stttntmgid afgvpatrsf gfsvkasl
//
LOCUS       WP_119429953             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. 91RF].
ACCESSION   WP_119429953
VERSION     WP_119429953.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. 91RF
  ORGANISM  Pseudomonas sp. 91RF
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. 91RF"
                     /db_xref="taxon:2292261"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38785
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnndt iakiaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_119421422             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Desertibaculum subflavum].
ACCESSION   WP_119421422
VERSION     WP_119421422.1
KEYWORDS    RefSeq.
SOURCE      Desertibaculum subflavum
  ORGANISM  Desertibaculum subflavum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sneathiellales; Sneathiellaceae; Desertibaculum.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Desertibaculum subflavum"
                     /db_xref="taxon:2268458"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40345
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miiaipkerr agekrvaatp dsvkkliglg qqvvveagag agcsipddhy taagatiapd
       61 easalkdadl vlkvarplta aegtdevalm kkgasligml aplqnreqak tyaaqgvqaf
      121 amelvpritr aqsmdvlssq anlagykavl dstlhfgraf pmmmtaagtv apakvfimgv
      181 gvaglqaiat akrlgavvma tdvriatkeq aeslgakfvm vddeesreaq tsggyakems
      241 daykakqaql iadtvpkmdi iittalipgr kapvlvseam vktmkpgsvi vdlavemggn
      301 cplsrpdevv evggvkivgy tnvpsrlavd asslyarnll nfitplidkq skafkidyed
      361 eiikgtlltr dgqivhpqlq qsqa
//
LOCUS       WP_119430226            1034 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            oryzae].
ACCESSION   WP_119430226
VERSION     WP_119430226.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter oryzae
  ORGANISM  Pontibacter oryzae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Pontibacter oryzae"
                     /db_xref="taxon:2304593"
     Protein         1..1034
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113011
     Region          28..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknsirfilw glcmlllhve gfaqgkavsg tvtsaadkiq lpgvsvtvkg kqrgavtdak
       61 gfytipnvea sdelvfsfig mkpvtrtvgn astidvvlqn dsealdevvv talgikqekk
      121 algyavtevk gatiaqtqre nfinglagrv agveinttsg lpgastsimi rgvsslsgsn
      181 qplfvvdglp isnstfntns fassggaaln nrasdftnra adinpedies itilkgpeas
      241 alygidaasg avvittkrgk sgapridysn sfrlerinkf peiqqvyglg vngvednsgn
      301 vttyfgaryp egtqfydnid nffrngftqk qnislsggsd katyrisggy tgqegfvpgt
      361 dlskfnlssa vtaqmnkyis tdltfaytyt dnnsafkgag gpllglltwp ttddasiymt
      421 engtrrfyst gdseienpyf nvnknkinnv nnryitnarl mieplewlrf vgnagfdfss
      481 gnitmvrhpe saygyssggi fdqsldntrn fnlqyyaeln rsflndkfnt nlkvgsavns
      541 qesfiqavtg erflapglys iententthr grnrlsqrrl igvfgnltmd ydnilfltlt
      601 grndwsstlp ienrsffyps vgasfiftel eplrginhil sygklrgswa qvgkdanpys
      661 iraflepkst tgggfgyaft gpspdlrpem ttsyefgtel kffnnrlgid atyfnklsed
      721 qivqnmrlsy atgfilqafn agkmktegve lqlnaspvvn snftwdvlan fthlwselis
      781 lptgvnefyv sdtwlyrdvr agsvvggplt tftghdyfrn dageilidps tgyplrdlnn
      841 ftvvgdrqpd ftvgltnsfa yknlslsfll dfrkggdiyn gtehfltekg lsmrtldrea
      901 pvvfkgvvkd glentanpti ntkvidpsrd mnywstaygl pdinyiekdi nwvrlrdvtl
      961 nynlnsslls kvnfiksgsv fvtatdlfii tnysgldpvv ngnsaavggs ggvgfdygnf
     1021 pmpigvnfgl kvgf
//
LOCUS       WP_119430210            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            oryzae].
ACCESSION   WP_119430210
VERSION     WP_119430210.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter oryzae
  ORGANISM  Pontibacter oryzae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Pontibacter oryzae"
                     /db_xref="taxon:2304593"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117172
     Region          26..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknylslll llvacccgta faqqltisgk vtgaednfal pgvsvivkgt ttgvttgadg
       61 myqinvpnae atllfrflgy apkevqvgnq nvinvqlnad nkqlqevvvt algiersers
      121 lgyatqqveg enltltkeqn vigslagkva gvqitgssga smggtqkiki rgvnslnged
      181 eplivvdgtp isnanfaesa gvdygnlaqd inpedvesin vlkgpaasal ygirgqygvi
      241 mittkkgsrg qknitvqlns avsvervgnl mpyqnmyggg ssqtwrtlan gekyvdmqvd
      301 eswgpkmdgt mvrqifsfyp qdpeygkltp fvphpdnikd yyetgyninn gvtisggneg
      361 tnfrlslndt riegvepntw ldrnnlglsl gtdiaknlta tanltyaytn aqrpgqgsed
      421 gsrylgqwfq rsldlkrlen yqypdgtylh wnlrrsyass gtlsnftply wnnpyfeaye
      481 ntsndrrdrl fgnvglsytv leglkvsgfi rsdmytqsie srtafggkdl pryyvgkfqn
      541 refnyeflgq ynktfgdfsl nanvganlfd rrytylsqnt eggltaegfy nidasidrpt
      601 tnsyllrkel rsmyamasvg ykdtyfidas irndrssalp knnnsywyps vsasmvfsel
      661 igwtplsfgk vrvsyaqags dldvystsat yqvgtvysgp qtvntlyvpd vlnnpdikps
      721 fahsyeagld lrflngrlgl dltyykqrnk nqiieldvsg tsgyssaiin aglienkgie
      781 avlsatpvqt enfswnsvfn lsrnrnkive lypgvdvlth gtayysstys ylnsysgkay
      841 gsligqayqr deatgkilld snnlplytsa thdfgtvlpd mtggmqntfn yknfslsami
      901 dyqvggqffs rskmlavrtg ldpltvemnd ngknvrdpls egggvkvegi saetgaevta
      961 yvdpqryygv aarriyedwl ydasyvklre arlgytfsks emswlpvksa nlaiiarnpl
     1021 miwqdapkgl dpselstgsq aigwyesgql ptvrsyginl nvtf
//
LOCUS       WP_119430231            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            oryzae].
ACCESSION   WP_119430231
VERSION     WP_119430231.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter oryzae
  ORGANISM  Pontibacter oryzae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Pontibacter oryzae"
                     /db_xref="taxon:2304593"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110776
     Region          28..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksirsmlw glcllllhah tfaqsasitg vvtsaddgip lpgvtvrvkg gtdgtftgpd
       61 gqytinaekg qvlvysfigf lpqertigne gvinislktd aktldevvvt algierdkrt
      121 ltysvqtigg edlqdsnqpn ivnalqgqva gaqitssggs pglpseiilr gvssltgdnq
      181 pliivdgvrv snasingtsn rlsdfnpndi envsilkgas asalygidaa sgaviittkk
      241 gkagdmrina ayntvvetvg rlpeqqklyt vgfggtfdns ttsswgrkyr vdepiydnpq
      301 rffqtgvthd anvninggte kytyylsgny rngtstipnt evdrlsllmk gnsqlsekls
      361 fsasanyian tikeglvgss sggwgnsiyr yplrydiegy qypngdpnyv fynnngtpdi
      421 inddtgiisp lwgvhrnprs tevkrivlng llsydvldwl nlsyrlgqdf ynqqygyvnv
      481 pgtpgslegr lyqttgnytn itstfnatid kditpdihat aifgtnseyy egeslsvsge
      541 kfqnpdihsv nvieapnigl gegyarrrry gvygdvkvey kslfslsytg rndwsstlpa
      601 dnrsfyyssl gasfafselm dsqhwfgklr asyakvgkda piystdanli kyqgigggfv
      661 kdatagnpnl kpetttekef gvefrlfdnr ltfdatyyda ksedqiirar vplptgyviq
      721 tfnagsihnk gievsmggtp vksgdfswnv tlnawgnrsk mlelpdqvrv fpytfgqpyt
      781 aaiagsklde pvlgligtdy krnedgymii gedgypvids enkqqyignr epkvnfglin
      841 kfnyknfsls flwdfrvggd vynatrlgmt sagisedvge wrdrefvfng vvdrgdgnyv
      901 kntqpvvldy nyfttnytav gtnfvekvnw armryatvsy slpeniskrl nvsrmniefs
      961 aqnpilitny sggdpevnsa gpnaggaegg stmgvdygai plpksysvgi svgf
//
LOCUS       WP_119431096             988 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            oryzae].
ACCESSION   WP_119431096
VERSION     WP_119431096.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter oryzae
  ORGANISM  Pontibacter oryzae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Pontibacter oryzae"
                     /db_xref="taxon:2304593"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106266
     Region          57..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmklyplkll llllcfipis lyaqttvrgk vtdfgsgkal pgvsvvvvgt ttgtntdang
       61 dysitlpgas gkltfsflgy tsqtfdvtpa vntldvrlre sttslsevvv tglattvkra
      121 naanavatis treitgittp qtmdaaisgk lvganvvsns gapgggiamk lrgitsifgn
      181 aqplyvvdgv iidnssissg lnavtnaggg gssstqdnas nriadlnpnd iesievlkga
      241 saaaiygsla sagvviittk rgaagktivd fsqdigiarv skllgmrtlt edrvrasfga
      301 aavpqfvaar dagrlidyee elygntgmly ntrlnvsggs ertqffvggl iqdeegivek
      361 tgynkkslrf nldhmlsdrf dfslstnyin stadrgltnn dnkgvsfgva lsstpsfvdl
      421 fpdenglypn npfgasnflq trdlitnqen tdrflggltl ntklqdsems stklviragl
      481 dfynlrtral fprllqfqsn gngtggasiq gnnynlntny aaflvnnlnl sdnsvflttt
      541 vgvtrenfnq dqtlnvatql igtqsnldqa gavtvdqtrl kvrnkglfaq eefnwrdrvi
      601 atagirldks snnamvndfn sfpkfslavn ltnfdfwsid rfnlvklraa ygesggfppf
      661 gakytslvss nvggsggllp ntqlgneeie qerqkefetg idiglmenkl lleatyynkk
      721 vsnlivfrsv passgfttev lnagelrnrg velalsatpv etpglkwdsr vsywrntsei
      781 tqldipafpl gafgstlgtf fieegesatq ivgirgdegv vklgdaapdf qmnfhnffti
      841 qqnlsfsfll hwkkggdnin ltqlltdlgg tsfdyddddd gdgipnaeer vdalgvsaet
      901 fvqnasylrl reigvyynvp iaflsgmfgd vvrsvrigas annlftitdy dgydpevsnf
      961 gsnglstgvd vmpfpmskry ffhfsigf
//
LOCUS       WP_119430877            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            oryzae].
ACCESSION   WP_119430877
VERSION     WP_119430877.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter oryzae
  ORGANISM  Pontibacter oryzae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Pontibacter oryzae"
                     /db_xref="taxon:2304593"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114137
     Region          25..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvlllsli laflipvlsy aqgartitgk vtdqasgqal pgvavlakgt svgtatdvqg
       61 nysinvpdgs ntlvfryvgy sdveraigna ttinvsmgvd tkqlsevvvt aigieretka
      121 lgysvqevga eslerstqps lanalngkva gvnitsasgs pgagsriiir gatsvsgdnq
      181 plfvvdgvpi dnsttsagnp ndgtntvlsg vansnravdi npediesvtv lkgpaataly
      241 giragsgaiv ittkkgtkga avvnystsft ldyvnklpel qqrysqgsgg eflgtfggfn
      301 stlswgapld qlrfdgqpyr ydpngflvpv gsptatdqra iaydnldnff etgttwtnsl
      361 sisggtektd yyvslgrtdq egvvpnsdft rtsvringst qlseklntfg sanyiksggs
      421 riqqgsntsg vmlgllrapi tfdlsggfge dgednpgayv fpdgtqrtyr egagydnpfw
      481 tvnrnpynde vnrligyvga kydftdwina tfrlgtdwys drrtngfdiq srtapagrva
      541 edqvfnrdln tdflvninre lttdfsarli lghnyyssny qrlytqgdgl avptffdlgn
      601 aasittvest tkieraavfg dlslsykdyl flgftgrnew sstlpsndqs ffypsvnlgf
      661 vftqaldigg dvldfgkvra syavvgkdap ayslttpftf stwgdgwttg isfpftgvag
      721 fnqltqlgna gikpeknksi eagidlrffn nrlgldatwy knnsedqiip vsvssasgfl
      781 sailnageie nrgieailrg tpvqtndfsw dvivnftrnq sevislypgv etitlngfts
      841 pssravvgep ygvlfggrfa rndqgqmlig ddgfpfpade dgiigdpnpd wtagitntlt
      901 wkglslsall dirkggdiwn gtvgvmtffg takrtenrge tkvfegvrld gtpntqevvl
      961 deewyqangg gfgaieeqfv edgswvrlre ltlsyrlpss lledtpvksa siafnarnlw
     1021 lntdysgidp ennltgqgna lgldyfsmpn tegygltlrv sf
//
LOCUS       WP_119432650            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            oryzae].
ACCESSION   WP_119432650
VERSION     WP_119432650.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter oryzae
  ORGANISM  Pontibacter oryzae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Pontibacter oryzae"
                     /db_xref="taxon:2304593"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117193
     Region          24..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllllsft lffaflqdve aqsktvsgrv tavasgdalp gvtvlakgtt vgtatsadga
       61 ytinvpdgan tlvfrfigye tveraigntn tinvslaidd kkleevvivg ystttqqsft
      121 gtakvvsgek lesksvsnvs qalagevagv rvintsgqpg teatirirgi gsvngnrapl
      181 yvvdgvpfsg slnsinpadi esttvlkdaa ataiygsrga ngvvvittks grgkksyiea
      241 danfgtnmal lprystiksp eqyiglswea lynyadanpk ittnpvdyan anlfsnagir
      301 pgynlwnvad ggelidpetr tvrpgvtrky dpenwedygf qnsarqevnv kfggssdkts
      361 yyssfgylnd kgyiinsdye risarlnvrq evnswltggi nfnyarsetn nngqssnsgs
      421 ifwfvdnips iyplfmrdae ggfitdpifg gnqydygtvt argfggltna iadatydtnr
      481 nnrnelngsa sldfniakgl tfenrigaqy yhnkyvdrgn kyyggsasqn gslflrrtel
      541 fnynllnlvr yskdfgqhnv ealaaheatn wkrnildasg yslvdplled lnnaivknps
      601 asytdeysle syfgqinydf dkkyflsttl rrdgssrfrk dkwgtfgsvg aawlvtnedf
      661 mdnlpifnsl klkasyglig dqagvgfypg ydlfnvdnln dapafsfdvk gnpdltwets
      721 kmfqtgiefg ignhitgsvd yyqkntedli ferrvgpslg yallqvndgn lknqgvefdl
      781 tgdvfkakdy rlslnvngei fsneitkmpi dpatgqpkti dvqapyawse ghsiydfyvr
      841 ewagvdpqdg lgmwtvhydd angngsfdsg eqvtnladye sknpgatllt sttknyaqat
      901 qkyigksalp dvrgafnlsa gykgfdlsaq llysfggyay dytyaglmsn dvvggnnwht
      961 difnrwqkeg ditdvprlsn eydanvasts srfitkanyl vlnnvrlsyt vptsfvskyg
     1021 igglsvwvtg dnlwintard gfnpstaeag ssstyryspl stvtaglrik i
//
LOCUS       WP_119432939            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pontibacter
            oryzae].
ACCESSION   WP_119432939
VERSION     WP_119432939.1
KEYWORDS    RefSeq.
SOURCE      Pontibacter oryzae
  ORGANISM  Pontibacter oryzae
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Pontibacter.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Pontibacter oryzae"
                     /db_xref="taxon:2304593"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113562
     Region          24..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklllmsfv mvltllqqay aqnktvsgtv tdqstgqrlp gvtvlvkgtn vgtatgvdgt
       61 ytinvpaggt tlefrfvgya alerpignsa tinvalgtdv rqlnevvvta lgvarqeksl
      121 gyavgqvkae elsqakavna aqslsgkvag lqistiangv spttrislrg nrsllgnnqa
      181 lvvidgvqsp qsaldylnpn diasvsvlkg anaaalygsd asngalivtt kkgtkgsaki
      241 tysntssieq vsflpefqer fgagtehysr iyipfenqqy gpefdgsmre vgrtledgsi
      301 qmlpykaldn erykvwntgk tiqndislss ggdfstfyis lqdvktegvv pkdeyrrtgg
      361 rfngtgeygk fkasyninya qtrtqrttad fynltlqtaa nipltdyknw qgiynadgsi
      421 nyanpnnfyn eyyqspwfal dnnredigkt nlnanaqlgl qatnwlnlty rvgvnneets
      481 rkayvgkyty sdysknvikk yiakdvagsv rdytisnrri vtdlfatlnh kfgdfeatai
      541 fgnniredky kylnmqssal vqpdvynvsn rtgeatvvqt drlqrligwy gditigfrdy
      601 lflhasgrnd qtsllnadnr sffypgvdia fnasdvipal qnsvvdflkf tgavtkvgnv
      661 nvdpyaldlt fdtsggfpyg ntagftigst tpdqnlqpef ttsyevgaqt sflrgrigle
      721 aavykqnstn qtvtisissa tgfssalina getensgyel slnttpirta sgfrmdvnvn
      781 ysntdtkvve lfqgldevnl ssyaglttst gsgiyarvge qypvikvsny ardpqgrviv
      841 dattgypknn pdglivagqt nprhklgist nmsykglals alaeyrggnv iyhdlgntmv
      901 ftgtakitem ygrerfvfpn svidngdgty tpntsvtvad ggvgfwdsnf kqygenfvts
      961 gafwklreva ltyqipqnil aptkyvknvs vgfvgrnllt llpkenmytd pefsqttgna
     1021 fginttgntp ptrtygvnlt atf
//
LOCUS       WP_119435874            1016 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119435874
VERSION     WP_119435874.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1016
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112244
     Region          28..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekslkkgvl ilflflfagm nmiyaqqksv tgsvkdesni plpgvtvmvk gttngtitnt
       61 dgtysinvpg eeailvftfi gmkteevqvg tqtsinvtla sdvigleevv aigygtskrk
      121 dvtgsiavad lgelrtvpvn niletvkgsv pglnvgstnr agqvaslsvr gqnsvsagnn
      181 plivvdnaiy ngsigdiane diesftvlkd asaaavygar sangviiitt kkgkgingkp
      241 qfnanlsygi inemkplevy daegyikrml diralrgdea dpskvadyfa nqverdnyla
      301 tpdhkptvad pyslirqngf nkkanfsvan rtenssyyis tsltdqqgvi indkyknftg
      361 rinmsndltd wlnlsintmy sfrdfsgssp aqsstvgisp yasvynedgs ytqfpqqtts
      421 yispfwmiat sdvdhshnln avvkatvkvp wvkgltysst ysksmrwqer nefwdkntrt
      481 gllakstgsr yfgrdvdmlf dnmlsynrlf adrhsvsatl lysweeynne fvrgsasqfd
      541 ndvlrdyklg ngvvqtidtg ggergsigqm arvnysfdek ygitgtvrrd gfsafsknkk
      601 wgvfpsvavn wniskesfme nisfldnlgi rasygsngnq sitpystlak vgtgkylyeg
      661 ddtysitqgi tsfalndlsw etttgfnlgl nfgvlnnrlt gaidmyksnt tdqlfslslp
      721 yitggssiid nlgdienkgi eielhsvnvq kgdfqwnsdf afslnrnkvi tiygedddgd
      781 gieddlissn ifigkslgqi ytyrvigmwq qedvdngtir tgmnpgtykl edlpnedgey
      841 ddkitsendr qhignskanf rwslnnnfty knfslmvyly siwggndwfl sgantpqrdp
      901 fpyredvnkv vydywaldnt daefprpden skatvrgtky ydrsfiklqk vavsydasdw
      961 issksfikgl tlsvsgdnla tyaphwvgld petgqglnds avpslqsfif ttaikf
//
LOCUS       WP_119435995            1125 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119435995
VERSION     WP_119435995.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1125
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125042
     Region          72..120
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          124..1124
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknihlqer glffslfkka wlimkltvif tlfcvfhala gisqdvvesv einnapleef
       61 lsavekqtsv kflyryenie gkrvsinikn asvdeiltnv lpeqgltysh lrnnlivisa
      121 dqeriiigkv vdkdnqplvg vnviikgtlq gsvtnvdgey qisvpndqai lqfsyigfev
      181 kevligeqnt invtlyedsk sieevvvtal giekkkktlt ystqevdmeg mttikdlslg
      241 nalagkvagv sitsssgasg vsgdpriiir gdrsiqnnnq plividgipq afaesiapnm
      301 qgqprppldn lssinaddiq smnvlkgpaa salygssann gvivittkrg vkgkpritvn
      361 svtnfdlpyl ypefqneyaq gaggiyqata antswgpkmt gqsvqnwkge tvaltpqpdn
      421 vkdlfsvgyn ltnsfsysag seksssyfsy snttargvle dnkmvrhnln lrltaellen
      481 lnldfkithf rqtvkdqpts gdnlfspmwq lvkmprsmrt adiengsyln dkgeltqntw
      541 apestdninp ywamegfelp stlnrvnsfl slrynfsenl flqvrggmni snsdneerty
      601 wgtpyiysgf gnyktsfdki qnlnsdilla fdkelnkdfr vgfnlgaevk dmqrrgqwae
      661 arglsmmnkf alnfaknvit edletriqkq svygmgqfsf rnylfldvta rkdwsstlpe
      721 phdyfypsvg lsgiisdmvk lpdaitfvkl rgsyaevgnd agfasifqay nsdssgplgm
      781 itpqstkvae qlipektksw eagadlkffd nrlgvdltwy ksntynqlvr itnpptsgys
      841 sawlncgniq ntgveimlyv tpvkthnfnw dvslnfarnk nevveltefm dryevespnl
      901 smgetwiieg rpfgeiftyg ferngdgkvi vgsngiplid hgkadvylgn fnydwrsgli
      961 nsfnyknwhm sflidlnygg vrqsateamm lsagtskasl vgredgiivd gvkedgsvnd
     1021 irisaedyyk svggrinsgt gelfshdatn srlrefslgy nfpirnsvvk slkvsavgrn
     1081 lfyiyngcdw fdpdvsydvg tngqgsesaf lpgtrtlgfn vkftl
//
LOCUS       WP_119437087            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119437087
VERSION     WP_119437087.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116833
     Region          22..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllllfvv fttimssama qktitgkvid nsgaplpgvt vvvkeivsgt itntdgvysi
       61 sipenakvlm fsfigmktke veisnqtivn vtmepdvigl eevvaigygt vkkkdltgav
      121 tqvdaeklea eatsnmtdll ranvpglnvn fstsakglss assmevrget nlrgsganap
      181 livvdgmiyy gdladinpnd idafdilkda ssaaiygsra sngviiittk kgkkgkptin
      241 vsasvglatr ssanldlmng eefiqwriag feanqrgqvg kpgyyyspdn lpdgvtadaw
      301 kaydgsseat dltqiwlqri gfspvevdny kngneinwyd hylqtglrqd ynislsgstd
      361 nlsyywslgy vnnegvvyne kfetyrsrln legtvtdflk vgintafsvr desnytantd
      421 riwyntpyse fyegdtnvis yapsgnasms shpyieivfa drlrdynsln nkiygtltlp
      481 ygfsftseyi trfnwnrdfy sysseytgwa paggyanrsr snvfewqvnn ilkwnksyge
      541 hdfdftavqn aekyqywser myrseflpnd vlgwhnmgag tkdeeissdd qystadalma
      601 rlnytykdry lftgsyrrdg ysafgqkhpr anfgsvalgw tvsdedffdv swmdllklra
      661 sfgtngnrav gryealsdly sgrtvlttdg tanyasymyv nrmanpdlqw ertsaynfgl
      721 dfstfngrlr gnfelylmqt rdllvsrklp ditgyssvft nlgqvdnrgf elglnsinid
      781 qndfqwssnf tlshnrneiv slygdldeng kelddptnkw fighaldqiw dyetdgiwqe
      841 deaeeaakys lspgdykiid qltedtdgdg iadatdgvft nddkifqgys kpkfratfrn
      901 dfswknwtas ikmysylgyw kannylkgqn vfydrgvsmk vpywtpenps nkwasiesgt
      961 vvgfnvyekn sfvridnval tynipqnvln kikvqrctls liaqnpfvwa pnwswmdpen
     1021 ngyttpsyyt lklnltl
//
LOCUS       WP_119437659             991 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119437659
VERSION     WP_119437659.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..991
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110260
     Region          27..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktryfkfii glflvfavqk ytnadeltgr vldakgkpvs galiylvqyp dvkattdrng
       61 eytiaatens eavinsadnf sksvilsdsl vivmgletsp vnrgydlina tkntaasaqt
      121 vfaedleknd skvnasnalf gellglsvlq ksgtvaenqa rlnyrglgrp lvlvdgferd
      181 ldgltveeie svtllkdaas qaiygmrgan gvllvntkkg kyntmeidlk ydhgvkfaks
      241 sipmvdafty asamnealgn dglapefnqy qlnayrdgsq pgiysnvnwa neifkdvahs
      301 nsynvqvrgg ngitrfygav aydtdesfik lgapdpsipn qfkysnlnvr tnvdvniskn
      361 tlltinmlgk lqensrgmls esdlmksiyn tpagafpikt engnwgastt wktnpvaels
      421 tagftrfhtr tlyaninikq nldaitkgln asarfgmdsy svirekkyrt yqtetitpvf
      481 dndgnptdle ynligermtn fqewnagtid qwrkltgqgq ldykrtfnks tvgggyifei
      541 ssysgygqhk mfnrvnnvly asygydnkyl ldatfsvgss nvlnprrkwg yfpaisagwv
      601 vsqedfakns eaidylkvna swgitgsdnm nfdlykvyyq tgksylfgnf qgvgtiepgs
      661 lpvvnltypk trsvnvgaeg tffggmnvsv dvfdikkydq liesknivss vigidpgmtn
      721 saeyaykgve lglgytgtkg dlkysamghf tftrseiinn neqvwkndfn ratghpvgqi
      781 fgyesigffk dqadidnspv qtfsevqpgd ikykdqddng iidqydriai gnnsivpemy
      841 fsldlnveyr klginllfqg tanhsaimqa dgiyrplvnn knisqhyydn rwtetnqdal
      901 yprltnalne nnnvastiwl qdlsylklrt aeiyytlpkq wvervklgna tvfargynlf
      961 sidkmrvgda eafglnfpmy ssvnlgvkin f
//
LOCUS       WP_119438110            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119438110
VERSION     WP_119438110.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122980
     Region          40..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msnlrekklk lsglvlrckg illaiiclvl fqaegfaqak svsgkvtaen gellpgvsiv
       61 ikgktagtit nidgeyqlnv dendilvfsf igmvaqewgv vgkqtldvvl ktatealdev
      121 vvtgyggkqs rakltnsias vkeetltggv hanpaqaltg avsglkvttv sgnpgatpsi
      181 ylrggtnfdg tgsplvlidg qvgafndinp ndiesievlk dagatalyga ranngvilit
      241 tkkggqpeik vsakfglnyl theydflgae dylywvrkgy qnaaqmyqns qggwvgygsm
      301 sslsgaapyg ignryyddng naldgnktsl avyspmvyns dlafllnegw qtmidpvtgq
      361 eiifsefnke ddafnnpalt qdynvsfsga ndrgkyyagi gyydaegqpa ktwykrlnft
      421 fngeykirsw ltsnsnfqft dakwynvstt netnyfgriq stpptqrqyn pdgelilgnn
      481 vgdgnplvni dklkrdnntn kfimgqgfri dflsnlslkv nahwlldqgy yesfnkdyls
      541 rpgiwstsrs ssasydkels qtynavlnyd ltkgkhtgsa lagyeyynkk wnglsasgsg
      601 aptddfsdlg ltsteegkrs idtyhteeri rsyfgrvnyd yaekylvsgt frydgysrll
      661 gdnrwgffpg vsagwivnke dfmkdyssli sflkvrasyg lngnvsgiga yelqgsygtr
      721 nynnqvgyvv gsianpglkw ertktaeagi disflenmin tnftyynrlt ldkyaniplp
      781 issgissirs nngeyrnkgl evdmsvkalr kgdwkwdvsa nisynksive klpdnglern
      841 rqgafqvydg asgnliwvgg yqegqqpgdl yafkalgvfs dwdevnavaa drkdittgwf
      901 gsnarpvygp tawdalgesk gnglalkpgd mnwldvnedg vidnfdmvki gntrpkwfgg
      961 itstlaykgf kfyarmdysl gfvqvdaqra wflamaqgty nttvdtkntw tvdnpnaefa
     1021 eyrwadqlgs rnyarqstqw vykgdylafr elslsyslpg tllegigmka vtlsvtgqkl
     1081 gyltasklnn penfssgaqy aaysvpktvi fgvdvkf
//
LOCUS       WP_119437873            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119437873
VERSION     WP_119437873.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121907
     Region          27..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkristmlf talfammcft afaqtnvsgt vsgedgellp gvsilikgtg tgittdidgk
       61 yllngvpkda tlvfsfvgmk tqeipvngrt einvvlqlsa igvdevvvta lgitrekksl
      121 gysvgevsgs dlnetpmgsv lnavagkaag vqvsqmygla gssvnmvirg asslntknqp
      181 lfvidgvpvg ngidnnykda dmgnaisdln tediesmsil kgpsaaalyg sragngvvli
      241 ttksgkgvkk gigvsfntsy vldnpyhfvp fqsmfasgka gshnlgeqen eswgaildgt
      301 fpdsyqwdks lldndgtslq plvaypnrqq dfyrngfsqs nnvsfegkyd kanfrvsfgn
      361 minegilpnt dyarktigin gaynltdnlk vsaavnisea gsdnrqnigt grrdpsrsvl
      421 emgvqvnild lkdywlegqe niqqrkskpk qnnpyfnvye nltgfkrnqt maklqvdwei
      481 fkdfnfmgry ltnvinqrne arvawsdydn srgaysiekt likeenweam fsysknimdg
      541 lsltanlggn lrydyndais neasqlvlpg lftisngvpg tvsynsywge kavnsvygsv
      601 slgyqnlvyl dltarndwss tlpkdnrsyf ypsaslslli nemielpswi dlmklrsgya
      661 qvgndvgaya laqyyatasd wgdakrmymp gtlrnpelkp eiatskeigl dlalfdsrin
      721 ldatyyvvdn knqvlsistp tesgatakqi naglvrgrgw dislnsslvr krdfavdlgl
      781 tltrnrtkiv elaegisfyq fgsvgqvrlr syvgddigni yaypyltved ksseyygypi
      841 iaangraqld nreesiekvg nfnhkflmgi qpvikyknfs vyanfdfryg gefysrsmef
      901 frnngwleet fsgvgydgnk divqqikdnp ekyfnlwvgg rtgdyggfpw adpatqasrs
      961 yidkntgetv yvedasfipg vredgqggyi enlggegtvw mtpfdankya tryyggnnvy
     1021 satylklrel svtyrlpqql vskanlsnvs lslmaqnvft wtkakipvdp elafassgss
     1081 wtqgaeyynv tpwtrsfgik lnvef
//
LOCUS       WP_119439231            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119439231
VERSION     WP_119439231.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119005
     Region          23..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiaillsi lffmgnlvna qtksltgtvt saednmpipg vsvsvkgttl gtvtnldglf
       61 eltvpndary llfsfigmkn leveigsqtn favkmenaii gvdevvvtal gisrerkslg
      121 ysvqqvggee istikgadft salsgkvagl diktntnfgg stnvivrgsa sltgnnqalf
      181 vvdgvpidnt imndsyqkrg grgydygsta sdinpndies isvlkgaaat alygsraang
      241 vilittkkga kgknlgvsyt gnvtlgfvdk stfpeyqkey gagygldwys dsdypgleyw
      301 dwnddgtdey ivptyedasm gepfdaglnv yqwnafwpgl dtygkatpwv aakndpieff
      361 etattksnsi qvtggsdnlt yrfsyqnlqq ggimpnseld knnfsfsgsy ditsklkvss
      421 fanfiktetk grnitgysgn lisgfrqwwq tnvdileqkr ayeqlgvnvt wnmnepgdts
      481 paywnnpywq ryrnyqtdsr srfigytkfd wqvadfltft grvsvdyysf leeerlavgs
      541 iaeafgvgyn dtssgysvkr gdfseynfdl manfnkdite klnlaglvgt nirkqnssdf
      601 wastngglav egiyslanta splelpieha pkiqvngyfa naslgyndil flegsvrvdq
      661 astlpkdnqt yvypsatgsf iftkfidkdw fsfgkvrlny aevgndapfa slfntydqyy
      721 pfsgngvasn sntinnkelk sertksleag ltlnfvknrl gldlaiydnr tvdqimpaai
      781 syatgssfkf vnagevsnkg veimlnatpv kqrgftwdva lnwsknknkv idlaeglekl
      841 qladlqggvt vnavkgqamg tihgtdfvyy ndikdeahri vtdgyydvsa sdqiigdvnp
      901 dwigglrntf syknlrlsfl idwkhggdvf sldhwygsst glykesagln dlgnpvrnyv
      961 adgggvilkg vtadgapntv rsedmgtyyt pvgsyyapna lfiydasyvk lrelsvtynl
     1021 pkslfdnifi qdasialvgs nlwiihknlp yadpetsqga gniqgwqsgv mpstrnigft
     1081 lnvnf
//
LOCUS       WP_119439184            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119439184
VERSION     WP_119439184.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115854
     Region          24..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiaillsi llfmgnlvvn aqtrtitgtv tssedskpip gvsvavkgtt lgtitnidge
       61 ytlkapleaq tlvfsfigma tqefaigert vinvvlqpqa igvdevvvta lgiqkdkkal
      121 gysvqavgee elvrtgnasl lgamqgkiag vdikpssgmp gassqmvirg arsftgnntp
      181 lyvvdgmpia stspystgns vtgtdianra idinpadies idilkgqaaa alygirasng
      241 vilittksgr gmavgkpvvt ithnssfdvv srtpdyqtty aqgsygqysp tmsfswgpki
      301 kdlpndpkyg gntdntytqr dgmqqgkfyv pqreqaglnp watpqvynsw edyfqtgytt
      361 snnvnvsqat qegnfslgls vtdqsgiala tgmtrynaka agernlnknf kvgysanysk
      421 sdidklsgan dgsltgilaa prsydlkgtp yhypgdpyrq iyfrggsfdn sywipdnnkf
      481 nerterffgn gyinfvtpla dgmnlsiryq agadtytthl qdifgygsaa rsktgeinny
      541 gttytlfnst atanfdwtin selelsamig nelnnsmskg ysetgtafnf ggwnhignas
      601 ivtadesqsk srdvgifgsl alswrsmlfl natgrndivs gmprnnrtff ypsvslgfvl
      661 teipaiqnas wlsfaklras yaevgqagry yenyfvtpgy gggfwgtepi qypigginsy
      721 vpnttqydpk lkpqntesye lgvdlkffnn rfgvdytysr qevtdqifav plagstgass
      781 lvmnggavrt nshevmlyvt pikardfqwd msfnfaaven nvlelaegve siflggfvtp
      841 qvragignty pviygvsfvk ddagnivved spgawnhgmp ktgdpdvige vspdfilgat
      901 nsftyknlsl tavfewkngg emysgsngll dlygvskvte drestfvfkg vkpdgtpndi
      961 vrggpndpda lqdlytnvls nideyyihen sfiklrelsl rykfakpiyk tlnvgvslyt
     1021 rniliwtalr nldpetsqgn nnmggsferf slpqttsygf gfeitf
//
LOCUS       WP_119439354             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Maribellus
            luteus].
ACCESSION   WP_119439354
VERSION     WP_119439354.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40144
     Region          1..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgllkeyg tetrvallpe tvksftdlkv evlvekgage hacatdadye avgakavsra
       61 dvfgkadvll qiqppaegdv dkikdsqvwi safnplwetg lvktfqnkgv ttfsldmipr
      121 ttraqamdil ssmatvsgyq avleaaanlp tffpmfmtaa gtirpanvli lgagvaglqa
      181 iatsrklgaq vqvfdvrsav keevmslggk fvevegated kaaggyaveq teefkkkqqq
      241 aindhaakan vvictaqipg rkapllvpke avdnmkagsv iidlaastgg nceltkdnet
      301 vvykgvsiig qsnypakkpi dasrmfgknv lnfmkliiae egalnlnfed divkgtcith
      361 akelynervk svietk
//
LOCUS       WP_119439615             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119439615
VERSION     WP_119439615.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110567
     Region          49..996
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyiqqirlf lgisqynils tlkhgmgavs llmfvmllsf nanaqslevs gtvvddntqe
       61 plpgvtivvk gtttgttsdi dgnfaitvns adatlmfsfi gyetqeiavq gqatlairlk
      121 setrdidevm viaygttkks nltgsavalk neelkdvfts nissmlqgkv agvytasesg
      181 rpgagstiti rgkgslsgtt aplwvvdgii ygnsdpglsp advesitvlk dasatslygs
      241 laangvilvq trradkgvsk invnasrgyt vfntgnfelm nsqelydyqk twnpkvtedv
      301 lstdtdwlki gtqtgeaqey nvnytggndk isaylsgtyy getgalkgye yerysglanv
      361 dinaseklli kanlsgdyrt tydqqhstya mftympwdnp yfpdgsvldp rteagkayll
      421 dngkvwygrd nsnylydlqy nygtsrgnnf rinvgvdyqi ndwltfssmn nialaysqqe
      481 yytdqrsisg ladkgtlyey ygfsqtrftn qmlrfkkdfd lhslnafvaw eysdyhtdna
      541 daegkgvaag ltvlnataea vsvggykges akqsylvnlq yaydnkylat asfnrqgsss
      601 fgpnnqygnf wsasmgwnvy neeflknvkw lnvlkwsasm gqvgnapsgf qylgyfafvd
      661 qyngnsaatp yqkgnadisw ekvtsyntav narifnrvsf nldlyyknsd glltyvplpa
      721 mtgyngiwmn vgrvtnrgye ltispeiikt prfnwdmtin laynknqvee lyedqaytsg
      781 skrievghdm daffqriwyg anpnngdplw ekvvenedgt etvsltsdya datlqftgtk
      841 gtpsytggil nrisfdnftl sanisfvedv ykynsnrelf dsdgsyvafn nmklidgwnr
      901 wekpgdvath pkpfnggvna nknssryled asyirlrnvt laynvpknis sllklnnasv
      961 yvsadnlvti sdwsgmdpet galyplskkv lfgvkvdf
//
LOCUS       WP_119439625            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119439625
VERSION     WP_119439625.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112858
     Region          27..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvitltcl vflmiltips gvlaqnrtit gtvveaetqt plpgvsvvvq gttkgtmtna
       61 egkfsldate gqilqfsfig yaskeftvgk sntinvemqt dvqaidevmv taefgmkrva
      121 rsvgssiqni kaadisdsgr esfisalqgr vaglnvsssg gtpgssttvv lrsitsisgn
      181 nqplyvvdgi pmnnstfdpl sladgganfs vrnldfssrg ndfnpedies mtvlkgaaaa
      241 alygsdasng aiiittkkgt agtarvsysn afkwdkaygy pdmqtkyang aygttnyyyt
      301 srygglypeg mqlydnidav lrtgfsakhn vsieggseka svrasasfld qqgivkttdy
      361 srmnvslagk gkiskwlsfe gsmqlvsten tkvprgtsgp lyqamlwplv ddmsnylspd
      421 gshmrnpdyy tdtdllnplf gmyknklydd sdrfissfaf sitpvkdafv raqvgwdvgt
      481 styetsihpy yydnnggvgq ynlaksnfsy ptlnflagyn ktfldkfyvs tqfgyhqien
      541 gvtrlatygs nyavidfhsi nnvdpstvas tkttttrriq alsgqielay nnmafvtlra
      601 rndwsstlpk dnnsyfypai egafivselp fikefnpisy lklrgsiaqv gkdagpleid
      661 pqlqateltg ggyrygftgp nkdlrpemtt sheigfegrf lgdrinadft yfwthcedqi
      721 vkgfrlsyat gfvlnnmnvg tfetqgweah vdadiirtks gltwnvgvna shtssevvyl
      781 penvteyynp ytwnsgnirn gimvgqpvtt ltgraysrnd agqilidptt glpvidptws
      841 vigdrepklr fgfttrvnyk gfsltallag rykatvvngt krlmmqrgts wesvnlreqg
      901 pvvfdgvlqd gnenttnpts nnisvtydvy gssiysgyde dwleknvnyf rlqelrlsyr
      961 iptrilqktf isravvyvag ndlatwtnys gidavgntvs aaaggtggeg ydvwsipnpr
     1021 gysigvnitf k
//
LOCUS       WP_119439630            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119439630
VERSION     WP_119439630.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115512
     Region          23..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrksvlfifi lcllsslama qkktvsgivs ekssgtplpg vsvyekgttn gtitdvngsf
       61 qltveeksil vfsfigmktq eftvgakndf tvsmeadsee mdevvvtamg irkekkalgy
      121 avqeissdei lknkspnlin smsgkiagvn vtqssgsaga gaqiivrggt slerdnqplf
      181 vvdgviydns tpiggntgfd gmgklatsss nrimdinped iesmsilkgp aatalygsra
      241 aagvilittk tggkgavqvn mssklsvnwv nrypeqqnmy krgyyneagv fsdyttqswg
      301 dpfssgdqiy nnienffqng svwdnsvsis ggndkgsfff sasrydqqgi vpetgydkst
      361 frfngdqkyg kltvganvaf snantdktlt tsglwsaggn gamtaiyswa psddmtryln
      421 edgskyrmfe glqdlsddve npywiinkns lsdetdrftg tvytvldatd wfninyrlgy
      481 dtytkndhtf iapggaiket yqngfmsesd vvykylssnl mlnfnkkvdd fdfnlmlgqs
      541 teetkvttqr rrgydfvsdg vysfenineg nksfqsghst krligaygel rtsyksiayl
      601 tftgrndwts tlpeennsyf yssvsgsfvf tellpendll sfgkvraswa kvgkdtdpya
      661 tstslwapre flagvgvans wtrgnpylkp erttstevgl elhffkgrlt adysyytnds
      721 ydqivtprls qttgyillst nvgnvlnkgm elsitgtpvq kkdlrwdvsl nlagnrgsve
      781 nlltgqdvly vtdvqvgnak aasfnggkfm gisgsewsrd engniildwd tgmplsdnst
      841 thyvgnrepk ftgginnnin wknwnfsflf dlrvggdifn gtdyymtnag msqrsldret
      901 ltlsgvaknp etkeyeakef tynanqmyti ttssgatqns ygadiirkyw qnyypletsn
      961 yltktnwlrl rtvtlsynvp dsflnkqqli krmsftltgt nlllftnykg mdpetsvags
     1021 gvvgsssvgf dycgvpstag fsfgvnitl
//
LOCUS       WP_119440350            1022 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119440350
VERSION     WP_119440350.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1022)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1022)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1022)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1022
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1022
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113452
     Region          44..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiyfvlsh shlkwltikk svvifglial lltgltsvss aqgvmrgtit ddsnlplpgv
       61 svmvqnttng titdidgnyv lsnlntgdvv ifsfigmitq qitysgqsev niqmltdtks
      121 ldevvvtalg iqrdkkslty ssqqvtgeel mktkdvnfmn slagktagld vkksssgagg
      181 strtvlrgsk sisglseply vidgipminr kggqpgmwgg tdqgdglsqi npediesisi
      241 lkgsnaavly gsegangvvi intkkgrtgq tvvsassstv fesillmpel qftygadggq
      301 lswsdtkgsy ddtfvddffe tghnlintis isggnartta yfsygntsnk givpkntysk
      361 hnvtfkqatk lfndkvtvrs nvmissestk nrnpagyyln plvglytfpr erdfdsyken
      421 yevfnvdrnm nlqnwfiqgd hfqsnpywvi nkepredltk rliaqaaiew aidkhwniev
      481 rgnvdyadki feqkhyagsn fvncsqngrw qyqnyndfql ytdallkynn efgdfridgv
      541 lgavyskttl gkgvsvdngt dalfypnefy fqnlptnvqv sstladrrik qgllgtltlg
      601 ykemlfldla grnewastli gtgnesyfyp svgisaiise mltmptwvsy gkvrashttv
      661 anevpwnrih pqntitasgg vsrntqkpft dlkpemlksl elgtewsffd nrlsfdftyy
      721 ditsndqfie lpapsgsgft tyfinageiv nkgyevtlka epvrtenltw ttvfnfdsnk
      781 neivefvaey pdrtfsygss egyetyikag gsfgdlygyk fkrneagqim lnettgaplr
      841 tadreylgnl npdwslgwnn tvtyknfavs vlinsriggk tvsqtesild gygvskrtay
      901 ardlgyvpid aiqgttrvnk ldpklyytti gdrngtlepy vydrtnikla qlaisydfdv
      961 nalnipvkqa sisligqnll flykkapfdp eltmnttnss qsldnfnlps trtygfnvkf
     1021 tf
//
LOCUS       WP_119439958            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribellus
            luteus].
ACCESSION   WP_119439958
VERSION     WP_119439958.1
KEYWORDS    RefSeq.
SOURCE      Maribellus luteus
  ORGANISM  Maribellus luteus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Maribellus.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Maribellus luteus"
                     /db_xref="taxon:2305463"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119941
     Region          22..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkiillval cfaligsvya qqtvtgivtd eeglgipgvs vmekgtvngt itdadgnyti
       61 tvkadalivf sfvgmktiee slngrsvinv tlvtdaigvd evvvtalgir reakalgyav
      121 skvdnerila tgtpvnalqs lygsaagvqv astatgptgg mkinirnavs fdsnsttrpl
      181 ivvdgipihd qntglgadna ngrdygtgin dinpddiasf eilkgakasv lygsagangv
      241 vlittksgak gkdlgvsasf tttwdnvafl peiqnqygtg rspsttvtdd qgfylvdgvr
      301 tidnrgqafg pkfdpsvtld wwdgtqrpwv aqsesvydkm yrtghqyitn vaissggekg
      361 smrfsytntd lspttlagsy dkntfslnas ykmndyinis ysgnlffskn mnavtsttmg
      421 aqgitsslga ysydidvdll newmvtpdgy nyfanpafte sfssgrravv nylwdqtqne
      481 deftrlhniq slniditlnk ifsatimgga dvttersqyr gkltdpslig pasgnvyqdv
      541 vrdirktygq allnfnsdiv derfnlsgfv ggvvshsyld rkgarqiggf vipnffsyan
      601 mpsgaqptyq fqngedimys mmgsvqfaya dqifievqgr ndwssilppa nnsyfypgvs
      661 atwiaseslr lpewidfgkl rvswadvgrp gpryfgnvny gvtasgagfv ltppndlppm
      721 dengipnlkp ekkrefevgl etylfdsrlg idfsyynsnt ydqimqvaap agmgvssvrm
      781 nagnvsnkgw elmlktkpvk ardfswdvnl tfsgsktkiv kldgeltrmt lwnnaglnai
      841 aevggeygli yqqkgwnyyi npsdendpnn gkrivdasgn nyaydtksnk mvgkvlpdli
      901 ggvfssfnyk slrfianidy sfgstfisht etymlaagvl keslpyrdqa sggvqyymaq
      961 dgsgnlykap ggnpnggasy wdgvlldgvy tngtannkvv aaedyyyqsy fangffpedr
     1021 ifkndyvalr niaieytvpk klsslvrlse lslmgfvnnv aylykaapnt ipestvgtsw
     1081 ssasvastal paqrsmglav kvkf
//
LOCUS       WP_119441794             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neopusillimonas maritima].
ACCESSION   WP_119441794
VERSION     WP_119441794.1
KEYWORDS    RefSeq.
SOURCE      Neopusillimonas maritima
  ORGANISM  Neopusillimonas maritima
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Neopusillimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Neopusillimonas maritima"
                     /db_xref="taxon:2026239"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39405
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpletv vgerrvaatp etvkkyvkag hsvivqqgag reasytdeay teagatlgsa
       61 qdafaaelil kvrapqseel ksmgagkvvl gmldpfnaeh lqtmaqagit gfaleaapri
      121 traqsldvls sqanlagyks vllatqfydr ifpmmmtaag tlkatqvvim gagvaglqai
      181 atarrlgavv wasdvrpsak eqveslggkf idvpfetdee reiaegvggy arpmpqawme
      241 rqaaltaqrc aqanivitta lipgrpaptl itedtvrama pgsvivdlai erggncpltv
      301 agevvekhgv kivgltnlps mlatdasaly arnlldfmkl ivdengklai qkdddivkac
      361 licengqilw gke
//
LOCUS       WP_119443190            1103 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            oligotrophus].
ACCESSION   WP_119443190
VERSION     WP_119443190.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter oligotrophus
  ORGANISM  Hymenobacter oligotrophus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Hymenobacter oligotrophus"
                     /db_xref="taxon:2319843"
     Protein         1..1103
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119144
     Region          24..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllavpll gavgivqpav aqtrevsgrv tdaasgqglp gvtvivkgtt tgastnange
       61 ftlaapagat tltfssigyl pvertigtss tidvalstdt kqlsevvvta lgvertrnsl
      121 pyaatqiene titkaratnv vnglsgkvag vqirqsnslg gssnilirgt ksvsgnnqpl
      181 fvvdgvpisn sntntadqrt grggydygna aadiapddva svtvlkgaaa talygdraan
      241 gvimittkkg rkglgvtint gltagkvdks tfikyqdryg agygnyyedp sgkflyrdid
      301 gdgkddlvap lsedasygaa fdpnlnvfqw dafdpaspnf gkarpwvnak ngpisffeta
      361 vstnnsvsid ggndlgtfkl gyndirdkgi mpnsqvnkni vnfagslnvt prlttsasvn
      421 ftrikglgry gtgyssrnlm tnfrqwwqtn vdikeqkaay drnnqnvtwn whdpddltai
      481 ywdnpyftry qnfqndqrnr vfgnvvatyk fadwfnlmgr vtldsydemq eerqaigatt
      541 ndqpafysry drtfreanyd lignfnknit enfsfrglig anmrrertqs irsstngglv
      601 vpglyslsnt aqpltppgev dyrravdgvf asttfgfrem vfldltlrrd vsstlpkknn
      661 sfyypsaavg fvfsellkda twlsyakara nyaevgsgae aynvvdvydk ptafgnvplf
      721 svpgtknnpd lrsertkaae agvemaffqs rlgfdatvyq snsvdqiipv aissatgynf
      781 ryvnsgnvrn rgieltayvt pfrsddlnwt vnvnwtrnrn qvmslyegvd nvqiasyqgg
      841 vssnatvgqp ygvlrgsnyv ydsngnrqvt vtknaagipt aayfkqsata nevigdpnpd
      901 wtggigntls ykgislyalv dfrkggdvfs ldryyglatg ltpetagnne lgnpsrnpiv
      961 rnadgsyapn sggvilegty apgttingvd vsgqpnavrt sntnyglygy vrnpaagfvy
     1021 dasfvklrev slsyslpktl lakfgpvrgi dlslvgrnlw iihknlpdad pedalssgna
     1081 gqgyqvgayp ntrtiggnir fsf
//
LOCUS       WP_119443326            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            oligotrophus].
ACCESSION   WP_119443326
VERSION     WP_119443326.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter oligotrophus
  ORGANISM  Hymenobacter oligotrophus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Hymenobacter oligotrophus"
                     /db_xref="taxon:2319843"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111886
     Region          25..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslwsivl pgvllaqqvq aqqartvtgv vtaasdrspl pgvnvvvkgg tigaqtsadg
       61 sytlqvapga tlvfsfigyn tlertvgadg nidvaletss ttlqevqitt aygiqqerre
      121 inyaaqqvts kdiietrqtn ivnalqgkva gvqitssggs agegasivir ggnsldgdnq
      181 plfvidgvim dnssfvesta pgggsafngi lgrsvsstnr aadinpedie smtvlkgpaa
      241 aalyglraan gaviittkrg ksgatsityr tqfsvdevnr lpklqnqykq gaggvfdptt
      301 rnswgprfap geevydnlgn ffekgtsfqn yltmsggndk anflasashq dtkgvtpqne
      361 ydkttvrlsg rvqlspklga sgsaqylnsg grrplqgpgl fagtggffvs llnwprndda
      421 rnylnadgtr rrllplsvgt ndadnpywtt efnpqtdrtn rviantqlty dpakwvrlsy
      481 nigtdvytek frsvravgts qpnnqnggia ettnfvrlln snflatfnrn fgenlgtslv
      541 lgntveqavy ettdiiglif qnpsfvsinn tvnrnaltsn rtrrlvgnfg rlsfdffkqa
      601 tlelngrydl sstlprpnln knygkgffyg svaggwefsr tlgldtnpil nygkirasva
      661 evgkdtgpyr vdsplaqsty igggfrpgff gsnrllkper trayeagldl qflngrlgld
      721 asvyhqetrd qliaprvsqa sgyilqying gtvinrgvel alsgtpvkla ngfewtalan
      781 ftanrnkakq lpgfltevnq sdasiidvar gsafpgrpit siaaydfqrv qsgpdagkii
      841 igangyptin tavyqyagnr apdfttqvtn tftynglsfs fmwdfrkggk vvngndwltt
      901 rnglsertld rykevvfdgv vakgdgtyap ntrpveltqa yytsilgavg tpfiedaswt
      961 rlryatltys lpktwlgnsg tvksielgvt grnlllftky sgvdpetsaa gagvrgggst
     1021 gfdygsvpat rgvdmslrat f
//
LOCUS       WP_119453667             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Henriciella algicola].
ACCESSION   WP_119453667
VERSION     WP_119453667.1
KEYWORDS    RefSeq.
SOURCE      Henriciella algicola
  ORGANISM  Henriciella algicola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomonadales; Hyphomonadaceae; Henriciella.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Henriciella algicola"
                     /db_xref="taxon:1608422"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38846
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkltilkets pgetrvaatp esvkklvgld htvtiesgag vaagfpdkaf sdegatiass
       61 agealqgadl llkvrapsae eagsypeglt vialmnpfgm gdlltafngk klntlameft
      121 pritraqsmd alssqsnlag yramiegatl ygralpmmmt aagtvapakv fvmgagvagl
      181 qaiatarrlg gvvtatdvrp aakeqvaslg akfiavende fkeaetaggy akemsddykk
      241 qqaeltathi akqdivitta lipgrpapel vteemvkamk pgavivdmav atggncklsk
      301 pdevvdvngv kvagfsnlpa rlpadtssly aknlvaflpl itaedgslnl etddeivtam
      361 iltkagetvn erlks
//
LOCUS       WP_119463282             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacteroides abscessus].
ACCESSION   WP_119463282
VERSION     WP_119463282.1
KEYWORDS    RefSeq.
SOURCE      Mycobacteroides abscessus (Mycobacterium abscessus)
  ORGANISM  Mycobacteroides abscessus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacteroides.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Mycobacteroides abscessus"
                     /db_xref="taxon:36809"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37346
     Region          6..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(20,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(49,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdqpvtigv vresgederr valvpkaiag ligkgvnivi esgagerall pdelyteaga
       61 tvgdawsadv vvkvapptaa evarlrqgqt ligflaprna ensigalrsa gvqafaveai
      121 prisraqvmd alssqanvag yksvlvaase strffpmltt aagtvkpalv lvlgvgvagl
      181 qalatakrlg arttgydvrp evadqvrsvg aqwldlgida ageggyarel tdeerqkqqq
      241 aledaikgfd vvittalvpg rpaprlvtat avqgmkpgsv vvdlagetgg nceltepgqt
      301 vvkhgvtias plnlpatmpe haselyakni tsvlellikd galapdfdde ivagscvtre
      361 vs
//
LOCUS       WP_119444343            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            oligotrophus].
ACCESSION   WP_119444343
VERSION     WP_119444343.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter oligotrophus
  ORGANISM  Hymenobacter oligotrophus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Hymenobacter oligotrophus"
                     /db_xref="taxon:2319843"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110017
     Region          30..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhsylpklw fllfflvscc lnaaaqtgav sgrildenqq glpgvtvlie gtqlgsstna
       61 egqyliqnvp vgprvvvasf vgfstqripv tvtagqtatv antvlgentt llneavvigy
      121 gtqrrqdlsg sveqiserqf vkgqvtnpeq lvqgkvaglq vttnsgapga gsvirirggs
      181 slnagndplf vidgvpvdnr dlpgasnpls linpndiesi svlkdasaaa iygsrasngv
      241 iivttkkglq geklrvnvss qnsvatpvry vdvlsadefr alvnergnaq qkaslgtant
      301 dwqkeifrta qttdnnvslt gavgklpfra sagyldqegl lkrndlkryt galsltpvll
      361 dgnlrvdmnv kgswidnnfs nqdavgaavf ydptqpifss egrfapyggy fqfldngsin
      421 tlatrnpvgl ieqnrrrstv krsignlqld yklpflrdls anlnlgydiq rsrgtsvtdp
      481 nsgqltgarl grgifeqyar dnnnrlleay lrynkqiggs riellgghsy qsfdykeyvf
      541 ddrdvfgqvf qqpadrping kdyfdpgyrl lsfygranyt lkdkyiltgt fradgssrfs
      601 ednrwgyfps aafawrlkee gflknssavs dlklrlsvgq tgqqdignry ydyislytps
      661 rntaqyqlgn qfsntlragl yneelkwets ttynagldfg ffdgrisgal dayqrkttdl
      721 lsfiqvaalt nlsnegffnv gdletrgvea nvnlgivrgd kfdwsinana nvlrteitrl
      781 tnvdnpnfvg nptggiaggv gnniqinsvg yqpqtffvfq qvydsngkpv eglyvdrngd
      841 gvingsdryh yqsarprail gfgtnltygk aslaatlrsh lgnyvynnvr sqsffvqnsn
      901 gfvnntteev ndsrfgsaqy fsdyfmenas flrmenitlg ynfgniykdr anlnvsfavq
      961 nlftitnytg ldpepqrdgn sgidntiypr prtftvglnf gf
//
LOCUS       WP_119460306             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Virgifigura deserti].
ACCESSION   WP_119460306
VERSION     WP_119460306.1
KEYWORDS    RefSeq.
SOURCE      Virgifigura deserti
  ORGANISM  Virgifigura deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Rhodospirillaceae; Virgifigura.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Virgifigura deserti"
                     /db_xref="taxon:2268457"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40047
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,323,325)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,330..331,335,
                     338..339)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigiakerr qnerrvaasp dtvkklvglg aevtietgag ysasftdeaf taagaqiaes
       61 aqaalgeani vlkvqrplta aeggtdelal lkrgavlvgi lspyaakdqv aayaehgvda
      121 famelmprit raqsmdvlss qanlagykav ldaaaefgra fpmmmtaagt vaparvlvmg
      181 agvaglqaia tarrlgaivs atdvrpaake qvqslgatfv avedeefkaa etaggyakem
      241 sdaykqkqaa liadtvkkqd viittalipg rpapvlltee mvrtmkpgsv ivdlaveqgg
      301 ncplsepgqv veahgvkivg hlnvpsrlav dasalyarnl lafltsqidk eakalkidwe
      361 deiikgtalt rdgkvihptf tgega
//
LOCUS       WP_119463869             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio sp.
            PID23_8].
ACCESSION   WP_119463869
VERSION     WP_119463869.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sp. PID23_8
  ORGANISM  Vibrio sp. PID23_8
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio sp. PID23_8"
                     /db_xref="taxon:1583767"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54590
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvviesrag vlasfddaay eaagakvvss
       61 eevwksglil kvnapivdee kgideiallp dgatlvsfiw paqnselmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgrpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqvitte ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvvkeg eitwpappiq vsaqpqakpq npvkpqpkve eptspvkklg alavgvgafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsv iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_119468437             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_119468437
VERSION     WP_119468437.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53904
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvspakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg npapklitke mvdsmkagsv ivdlaaangg nweytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_119476266             997 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            lacus].
ACCESSION   WP_119476266
VERSION     WP_119476266.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus lacus
  ORGANISM  Algoriphagus lacus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Algoriphagus lacus"
                     /db_xref="taxon:2056311"
     Protein         1..997
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108509
     Region          30..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msnylpklks lmlafalvls vmatvnaqnr tisgtildaa lgdpvpgatv lvkgttrgta
       61 tdldgkftlq lqagdqtlvv sfvgyltqei eignqttitv nleediqslq eavvigygsq
      121 dkkeitsavv gvkpedfnrg nitnpaqllq gkvaglsitr pggnpnngft vrlrglstfg
      181 anssplivld gvigasienv dpndiqsidv lkdgsaaaiy gargssgvil itttkqgkke
      241 gttnvnintf gtmdqatnli pvlspeefva rggtdfgskt dwrdelidna fsyttnasvs
      301 gsfgnsnyma avnyrdnngi vngvgnerln trlnlsqgal nnrlrlninl sftnvdsesi
      361 ndaafryati ynptapites tetainrfgg yfqrdlfdfy npvalakqqk fvgetktalt
      421 syraefdils nltltaqysq drrntlsggf wslqdfqvgi gatgsaernt fdrkqrifes
      481 tlryetdlsd klnmtllggv gvqyttnqgf narvrqylfd lgwnnlgaga irvgnntnvs
      541 sfanedqlns vfgranfnwd nivfvsasvr setysgfgen nqtgifpafs vgsdftqvfd
      601 mglfsqfkpr vsygvtgnlp psptlalgvy gngnridldg dpltqndifv ginqfsnpnk
      661 dlkwetkkef nvgidfgiwd nkvtgsvdyy trnisdllfn vpvatgapnp fdpgrfntas
      721 stwvnladlr aagfefavgv tqigkgalkw tpnlnftiyd kttieslsng dlgfeelrfa
      781 tpgspgqnnn piiynrvgqt lgdiygpkln gltedgqyil sttdpnqfek lgnglpkgef
      841 gfannlmwgq wnlsfflrga wghdlynsyr gfyenadpas ntwnsvitdk tptnplvvst
      901 ptfnssvved asfirldnme lgynvktksa nlsslrfyaa aqnlftitny tgidpevrtn
      961 dsengdafts alspgierrn tyfqtrsftl gvtvnfk
//
LOCUS       WP_119476668            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            lacus].
ACCESSION   WP_119476668
VERSION     WP_119476668.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus lacus
  ORGANISM  Algoriphagus lacus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Algoriphagus lacus"
                     /db_xref="taxon:2056311"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117302
     Region          36..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksiltrltn kkivallvtv flcglsisng yaqsrisgtv edesglflpg vtvlvtgttl
       61 gavtdidgkf sltlpqgsnr ltfsyigyit qqievesqsv irvimqedsk nldefvvtal
      121 gvqrerkelg ytvqalkpad lvttqdnniv nalsgkiagv qvtssgsqig assriiirgn
      181 asfagnqplf vvdgvpidns ttnldgnggl dygnaaadid peniesltvl kganaaalyg
      241 nraangvili etkkgkkare gfgvefnssm vfdvpsyymn fqneygigtr ggeydwqqyl
      301 knnpnsnlsy neyakrfsyn yvngigggvq enatswgprl dagllldqwv kgpnspwesd
      361 pdnikdhyfq tgtnfinqva vtakgkeayg rvsfsnrkmt giffntdqtv ntlnanltln
      421 phekltvgtn fnyvnrrsdn lpvvsygsmt klawgafrhi pldevkkvyd efgnekgsgy
      481 nlnqnnfyye llqtngmnre rfygnvslty qindwltans lvgldyydel rksitlsrtr
      541 aninnrmggq fsqndqtrqe fntdvrldfn ktfendfsli glvggnyrqn kfssmtlsap
      601 dlnvpdlfni gnvkgtpgtg mfdsvkenys iyssatvgyk gylfagvtar ndwsstlpee
      661 nrsyfypsgn lsvtlseald iksknfshlq lrasmakvgs dtdpyqlmgt ytttlfnnia
      721 lfnspatlpp anlkpemtts teigadfrff ndrlsldaty ynrvtedmil nvptarttgy
      781 asqlinaaki rntgielvvr glvmnkggfr wdatinwakn nstvvelygg lenitispgf
      841 ggarlvgtpg qpwgdisglp yvrdesgnik iapngtpmtt nqqkilgnvt pkwigglqnt
      901 ftykkislga lldwrkggdf fsgtywhsyp tgaftntvqn nvreegiivp gvkgdgspnd
      961 vrisaqdyyn gawvwnnhey siidgsylkl reltlgytfs igklqnvavs afgrnlliih
     1021 rsekakelgl dpeaasqmgg gergvgfenf mppttrsygf nlrlnf
//
LOCUS       WP_119476886            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            lacus].
ACCESSION   WP_119476886
VERSION     WP_119476886.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus lacus
  ORGANISM  Algoriphagus lacus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Algoriphagus lacus"
                     /db_xref="taxon:2056311"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117246
     Region          28..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miaqksiwqg mmtaclifil nfsfaqqirv tgkvsdvnne plpgatvlvk gttrgtvtdv
       61 dgsysieags tetlvfsfvg fetkeqvvgn ssminiilse gvaltevvvt algveretka
      121 lgysvqavdg arftearetn vinslsgrva gvqvtnsstg lggssrviir gesslninan
      181 qplfvvdgvp isnnivgssg sgnqevdygn aageinpddi asmtvlkgpa aaalygsraa
      241 ngailittkt gkgkkglgvt insnttfdnv lrlpdwqdky gqgnngqfaf vngagagtad
      301 gvdeswgpel dkgfstpqfd sprnvegfrg gdlnapdgst itptpwvsqp dnvneffetg
      361 ltlsnnisle gsneksnirl swtnlnqtgt vpntdlkrnt iamngginvt dkltvnsain
      421 fqrtdsgnrp sisygteslm ylfiwygrql nnnslkdywm rgregvqqfn ynynyhdnpy
      481 fnvyentngq ekdrifgnis atykftpkls lmlrtgldty nelrdrrraf stqrfprgny
      541 reddvsfseq nsdflltyse ttkstwsysv alggnamrqe nryvqtvapq llipgiynft
      601 ntavnlqvnq ftsekrinsl ygfgqigykn vlfldvtgrn dwsstlpadn nsyfypsatl
      661 savisdiftl pgaisflkvr gayaevgndt dpyaltnvyn svtawgtiqa ksesnrlsna
      721 dlkpertgsf etgfdirfme grlgldftyf dnrtrnqiip ieldiatgya sriinageiq
      781 nkgievvlng rpvqsasgft wdfianftrt rgyvlelteg ldtytltgrn ganiqarvge
      841 rmgniygagf arvedpaspy fgqiihntsg tpitsptlkn qgnynpdwml giqnnlsykg
      901 islgflfdyr hggivvsrtk tigstsgqle etlfgrengy dlsvegngii segvirnadg
      961 sftpntikit srnwhnryye rnnveaakyd atflklrevt igytipkrvl gkmpiqdvki
     1021 slvgrnlalw tenphfdpet mamgggtlip gvedmsfpst rsigfnlnvk f
//
LOCUS       WP_119477187            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            lacus].
ACCESSION   WP_119477187
VERSION     WP_119477187.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus lacus
  ORGANISM  Algoriphagus lacus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Algoriphagus lacus"
                     /db_xref="taxon:2056311"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116803
     Region          25..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkallfvva lftmalsyev saqqrvitgk viseedglgl pgatvlvkgt tvgtttdldg
       61 nysinvpags dvlifsfvgl ktmeeaignr svvnvtlatd aaqlsevvvt aigierekka
      121 lgyavtsvdn sqlenrpead varvlqgkvp gvnitstngm sgsgtnmvir gyksatgnnq
      181 plfvvdgvpf ntstnaqngf ttggattssr fldidpnnie smsvlkglsa tvlygdqgrn
      241 gvilittksg askrkaaevt inqsvftnea aslptygqvy gngfqqapgf ffsnfgprmd
      301 tgltinhpya tssvaairne fpqfwvdgkv ggtpvqyeyk aykdpseiff rtglvsntsv
      361 qiaggsdrtg fnasfgytde egyvpgnele kynfglgmns aitdklsvns sftfaitdlk
      421 tppvnasygs gsdipsvfgh vlftprsvdl enlpfelpsd kssvyfrggn ditnpnwlvk
      481 yysntskvnr ffnstslnyd inddfsvtyr igldtytelq eirynkggat anlatrngyy
      541 rsininntiw nqdlilnwkk disdkiglsa llggnsrfds ynqngiasqg qlafglfrhs
      601 nfrtsantda ysggslnftq eerrygvyan vtfdysdylf lnmsarndwt stvekqnrsi
      661 lypgasisfi pttafdwsss tlndlkvrlg ygtsagypsp yntrnvlaqs arafdvngav
      721 ttthsvsntl gnpnlkpelh gelelgvegv mfnnklrfdi svyekntrdl itnapidpst
      781 gftftainig kirtrgaevq atvtpvstas gfvwnstlnw skyrteviel gggleevvia
      841 gftdlgnfai pgkpfniirg igfdrapdgq piilsngvhk ptsenvdlgd pnpawngswi
      901 nnftfkgftf nfmleyrhkg avfsntvtat largvtkdpv adreltfimp gvrqdgtnad
      961 gtpkyipndy qisaadyffs gyqgatdepn ifdgsmirlr evslayqlpn nlmsktpfkr
     1021 asialsgtnl wfealnfppn mnfdvdvlgt gvgnglgfdf vtgpssrrvg gtltltf
//
LOCUS       WP_119477968            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            lacus].
ACCESSION   WP_119477968
VERSION     WP_119477968.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus lacus
  ORGANISM  Algoriphagus lacus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Algoriphagus lacus"
                     /db_xref="taxon:2056311"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113451
     Region          26..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkflsmafa lvlvlgissl aqsqqrvlrg kvtastdglp mpgvtildks nqtgtttnvd
       61 geysisvtdq svlvfsfigf sskeitvgnq selnvvldee anelnevvvt sfgmqrdqks
      121 lgysvtqlgg drftesrain vgnaltgkva gvnvtppstg aagstrvvir ggssltgadq
      181 plyvvngvpi esgnlgsagm wggndagdgl aainaddies isvlkgntaa alygaraang
      241 vilittksgt aregigvsfn snftvenvvd rtnfqrqyga grdgnksatq qealddatng
      301 wgakwdgsnv iqfdgqqrpy sylgeglndf yrqgftwnns valfggndkt nyrfsysnlk
      361 nedvlpnsgy drnvaninvn sqqgkftlav vgqysnqqal nrprlsdspg nanfsmivkp
      421 ghypldvikg dpnkfgalad gtelryqgnv fqtnpywaay qfrredvtdr imgnmslkyd
      481 itdwlyvqgr ygidfqiidn ysyeaygtay kprgdyntga rtirennadl lvgfdkkfgd
      541 fdvdgfvggn mmrrtlenkt gggndlvvpf fhsvtnvaap tfgygfseyg insyfgaanv
      601 gyknmiflnl tgrqdqfstl spensklfyp svglsavvsd mlslpefitf akvrgsyatv
      661 gggapdpyal nltyglvgag hlgaslgqin ngsipnsnlg pytsneyeig adlrffenrv
      721 gldvayynrr tsddilntgi satsgfnttt inigelenkg ielllnvtpi qkgdfkwdls
      781 fnyahnisqv lslgtnaage piqfinldes rvrrerirhi vgqplgmiag fkhqtvngqk
      841 vytadgypva tagyetiaeg rhpisggltn nlsyknfrlm flidfrsggs imsgtdyfay
      901 qlglheqtlv grngdltvsg vtkqgdnyvp gtwtiptnaa npaqykldqy yqnysnitey
      961 vvydasfgkl refsfgytfp rtmiektpfq nlslslvgrn lallwsdtpn idpeaaytvs
     1021 gnsqgleyfs vpanrsfgfn lsatf
//
LOCUS       WP_119478898            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            lacus].
ACCESSION   WP_119478898
VERSION     WP_119478898.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus lacus
  ORGANISM  Algoriphagus lacus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Algoriphagus lacus"
                     /db_xref="taxon:2056311"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117500
     Region          21..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkllftwimv lvtgvvfaqg itltgkvvds qglpipgatl tesgtrtlsi tdaegkftfs
       61 sdivpftlrv sfigfqtyqv evtstsslse ivltestsel nevlvtalgi ernrqsltsa
      121 vsvvdnrals dvpqpnlina lsglvagvqv tngssgvgss srivirgens lsgnnealiv
      181 vdgvpiqnnl iasvlfndga niqevdygng aadlspddia sisilkgpgs aalygtrgan
      241 gvvlittkkg gktqglgvst ssivtfedll tlpayqneyg ggtngqyafq ngigagindg
      301 gissfgprln egqfiaqfds psvdirgnpv ragdvlsrtf pngtytpitp tpwisrpnnv
      361 kdffrtgvts qqaialnggd ekggfragyi nfrnqgilpn tdlkrdglsl sldrqltdrl
      421 rfdlfsnyvn srsnnrpglg ygyenvmygf nwtgrnfnia slrdywqagq egiqhfdfny
      481 lwttnpyltl fentngfdkn rflgnasgty dftdklslrv rlgadifddi rtfrrafstn
      541 rrvfggyred qisfqeintd fllsyadrlg sqwtysisig anrmnqeisn ayteanqlal
      601 pgiynlensr vplrgasqef skrinsiysf gnlafkdhlf veltvrndws stlpasnnsf
      661 ayysggvnyv mseavqlpkk wsyaairfna asvgndtdpy qlnntfqfnq nygsfirvtn
      721 rtvlnnpqlk perlnaleag lnlgwfrnrv mldvsayqnt sinqiigrpi statgfsnri
      781 enggevrtrg leaalsgsvi skkdlewtmg infstyrsvv tqlpdgvtqy vtgeasvfag
      841 aggsntvfyi arengrigdm ygtgfrmveg qvlygsnglp iqdatlrllg nynpdfilgf
      901 tnrlsfkriq ismvwdwrqg gtivsrtral gstsgvlket legreigivg qgvvnvgtae
      961 npqyvpnttv vsassfynnf fdrgneasal ynasylkirq lsiyyslpea wisrigfeqv
     1021 kvgfvgsnll lftenphfdp elnamqgqrl tygvedmsyp strsfgfsik tef
//
LOCUS       WP_119478750             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Algoriphagus lacus].
ACCESSION   WP_119478750
VERSION     WP_119478750.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus lacus
  ORGANISM  Algoriphagus lacus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Algoriphagus lacus"
                     /db_xref="taxon:2056311"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40003
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtvgviketk eferrvalsp dvvkllkkke feviiessag egsyfsdqdy lvagakvgsa
       61 tevfaadill kvnlftleei aqmktgsaci symyayqhpe viealnkksi ssfsmdavpr
      121 israqkmdal ssqanlagyk svilganhlg kifplmmtas gtitpakvli fgagvaglqa
      181 iatakrlgai vevsdvrpet keqveslggr fltvegaesv kveggyakev saeflekqqq
      241 lirdkikdad lvittalvmg kkspilvtee mvksmktgsv ivdmavesgg ncavseknkt
      301 vvkygvtiig esnlpsllpv nasqlyatni stlllhlagk dgikldleee itkgvlithq
      361 gelvhaftks iltk
//
LOCUS       WP_119479581            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            lacus].
ACCESSION   WP_119479581
VERSION     WP_119479581.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus lacus
  ORGANISM  Algoriphagus lacus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Algoriphagus lacus"
                     /db_xref="taxon:2056311"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119306
     Region          27..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkylltvli ayfltgslsa fqapglking tvssedglal pgaliylldt elrtitdeag
       61 rfelaapsgs ftlmvsyigm etsrteitlp laeplrilmk psaleltqvd ivstgyqslp
      121 keratgsfay ldsqlvqrkv stnildrled vtsgllfnra pnatndpisi rgrgtifant
      181 apliivdnfp ydgpleninp ndvasmtvlk daaaasiwga ragngvivit thkgnkdmpl
      241 qislntnvtv teardlhyvp qmsipefigi eqrlfasnfy rsqetnankp klspavetli
      301 slrdgkitqq eadarmelfg rsdirndird yylqsglsqq yaltlrgggk qssyyvslgf
      361 dpvrtdvign esgrwtlalg nnwhlledrl eagfqlnlan lqtqtstvlp qgfaydrlad
      421 gsgnplsian tystryiesv knkglldwty vplneigkqd yrsqaydlri spsvqyaltk
      481 dlkigvfyqy wrnlrtsrnr npmelfftrd qinrytqqgt dgslsypipv geilstsqse
      541 syshtfrpql tytrdwngth flngiggmei rdlqgldwad ryygyrddmg sslpvdqvtr
      601 fplyynpgql aavpsgdshg gntdrfvsyy anfgydyrhk yfltasvrkd qanifgvean
      661 mrgvplwsvg gawllseelf adkpnmpflk lratygysgn vdkrlsadvt aqytnflfyd
      721 vlpqmraatl vnppnpelrw ekvkttnlav dvetqngfls atveyyskhs qdllgdysip
      781 astgltsfkg nfaetqvrgv dltlslrpvr kafswtstll ysglkekvle fernptvanl
      841 ldsyylatpy pilgrplygi ysyewagldp qngnplgiln gepsadylgi sraatienlq
      901 yhgsarptsf gafrndfsfk gfslsvnvsy rmgyyykrrs idyfallrgs ighgdydqrw
      961 qnpgdeawtq ipslpatadt rrnsfytnsa vliekgdhir lndirlsytw dklhylnlpf
     1021 rsvqlytyas nlgiiwkasd dkldpdyqtt rplktfsagl kldf
//
LOCUS       WP_119479607            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            lacus].
ACCESSION   WP_119479607
VERSION     WP_119479607.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus lacus
  ORGANISM  Algoriphagus lacus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Algoriphagus lacus"
                     /db_xref="taxon:2056311"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119165
     Region          34..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrilipkav llfavlllqf vgtswsqesp nlvtltgvvl esetenplpg avvlvsslsk
       61 stvtdasgkf slslpegehe vivsfvgfks lrqvvstsdk tprvfklete efnlgavdvv
      121 stgyqqipke ratgsfvqid qelvdrrvst sildriedvs sgvifnrtvg gadpisirgr
      181 stlfgntqpl ividnlpyeg pleninpndv asitilkdaa aasiwgaqag ngvivittks
      241 gsykqpmrvs vqsnvtvvea pdlfyapqme igdfveqerr lfnsgfynsm instartpls
      301 pvvetllkvr ngqltaaegd rlllqysnqd sradlsryyy qkavlqqyaf qisgggdsyn
      361 fnfsggydrn asevvgnlnd ritlnarqnw klmkdkleis tglylsrgkn tvttsvptlr
      421 pyelladseg nalqvvgals nryvestaqs glldwrflpl qeigkrnldv vgmdfrgnlg
      481 lsyqivpglk aetryqywtn htesrsietp elyeirhqin sftqvgpdgs ltfaiprger
      541 fttsndisfs hnlrtnlkyq lkkgkgewna lagfemrdls srsdrmqyfg ykdelglstp
      601 vdyqtrfpqy fnpglrlnip yggthsgind hylsyfgnas yffqekylls asarkdmsnl
      661 fgvetnqkgv plwsvgggwi lsnesfykwe alpyvklrmt ygfngnvdks tsafttiryd
      721 nfheyipgfr yafisnppnp nlrwekigif nlavdfesks grlggslefy tknsqdlige
      781 tevpdsngly qyrgnfssti trgfdltlns vildkalrws tqtlisgwkd evtefegsrt
      841 vaqyfgsnss nvvplegkpl fsiyslpwgg lnpdngnplg fldgelseny saiistatpe
      901 sirfhgsarp tvfgslrntl dykgfslsfn itfragyyfr rssvdyaals rgqishadyg
      961 irwqnpgdel ttqvpsqpta lntvrqsfyq rssvlvergd hirfqdvrfg ytfskasnpr
     1021 fpflnmevft ylnnlgliwk atdqpidpdf piavpqrtaa iglridf
//
LOCUS       WP_119479058            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Algoriphagus
            lacus].
ACCESSION   WP_119479058
VERSION     WP_119479058.1
KEYWORDS    RefSeq.
SOURCE      Algoriphagus lacus
  ORGANISM  Algoriphagus lacus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Cyclobacteriaceae; Algoriphagus.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Algoriphagus lacus"
                     /db_xref="taxon:2056311"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119001
     Region          26..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktllllvl wslsgslysr qnplevlsgs vyssegfplp gafvsleste yravtdeegn
       61 fqlsapagdy vlivtyigme tfreaislpt stkpriilkp eefslesvdv vstgyqtlpk
      121 eratgsfvll dsqlvqrrvg pgilerledv tpglifnkgp qaandpisir grgtifsnta
      181 pliivdnfpy dgpieninpn dvvsisvlkd aaaasiwgar agngvivist qrarmkqpls
      241 vsfnsnftft eprdlfytpq msipefieie kllfgrnfyr sletnankpk lspavetfia
      301 lrdrkitqee adariqlygd sdnrrdiqsy ylqpgfnqqy aisvsgggeh saqnfsigyd
      361 kiqsdiigns garwtiatgs qwnflkdrvk agvqlnfsnq nngsttslpf gyaydrlade
      421 kgnpltiant ystryiesiq gkglldwtyt plkeirqldy rteaydlrvs psmqfqvtkg
      481 lelglyyqyw rnlsqsenrd pmslfttrdl inrytqvaqd gtlsypvpvg evlsvgnsea
      541 yshtfrpqls yqrewleshf vnvlagaevr dlqaenwstr yygyrddmgt sipvdlvtry
      601 pfyynkgqqg silsgntlgg ridrfvsyya nlgydfrhry fltasirkdq anifgvdanl
      661 rgvplwsagg gwivsetfse aiskmpfvkl ratygssgnv dkslsadvta qyisfqffdi
      721 lpqlraasiv nppnpdlrwe kistsnlald letqngflag tvevyskkgt dllgnysvpa
      781 slgltgftgn faetqvkgid ldlslrwfrn efswtstfly sglkeevldf erlptvsnll
      841 gtafsptpqp ivgrplygiy tyawggldpq ngnprgildg epssdylais rgatidnlqy
      901 hgparptsfg afrndfayrg fslslnisyr lgyyykrrsi dyftllrgei ghgdydnrwq
      961 qpgdeeftqi pslpatadtr rnafysnsav lvergdhirl ndirlsytwd klsipnlpfk
     1021 tlqlygyagn lgliwkased aldpdfqtak plrsfsaglk mdf
//
LOCUS       WP_119496920             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psittacicella melopsittaci].
ACCESSION   WP_119496920
VERSION     WP_119496920.1
KEYWORDS    RefSeq.
SOURCE      Psittacicella melopsittaci
  ORGANISM  Psittacicella melopsittaci
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Psittacicellaceae; Psittacicella.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Psittacicella melopsittaci"
                     /db_xref="taxon:2028576"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56266
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvrkeiq anekrvaltp tsvsklkklg yqvvieseag qastypdqmy ieagatvvpr
       61 eqvyqadill avnplerdev allkegatvi sflypaqnte lvtalqekni tslamdmvpr
      121 israqamdal sslaniagyr avveaaaqfg rflngqitaa gkiapakvlv igagvaglaa
      181 igtaknlgai vrafdarpev keqvesmgaq fltighieqq ktndgytrst seefdrksae
      241 lyaaqakevd iiittaaipg rkapllitke mvdsmkpgsv iidiaaatgg ncaytqagqv
      301 vttdngvkvv gytnyqsllg nqaselyann lvnllslitp ekngqyqleq sdvivrnmlv
      361 tltdgekgqa sllyppppis vsaapketak aapakpqvda ktlarkliwq tvglalaflv
      421 ylyltsflpa sfvadlnifm lasvlgyfli wnvhsalhtp lmsltnalsg ivvigaiyqv
      481 ssvefgvlak llaligvflg glnifggfav thrmlsmfik kdkdqggk
//
LOCUS       WP_119506038             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter baumannii].
ACCESSION   WP_119506038
VERSION     WP_119506038.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39768
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklisag hsvviergag vkaayidsay eqvgatitdd
       61 aytgsqiilk vrapqggeiq klaanttvva mfdpyrntel dqfsnqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgaiv eatdlrptak dqveslggkw ldvpmseeeq qraadaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 kvgetvvten gvkilgipni patvateasa lyarnvfnfv etlfdkeknf ainqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_119515826             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neopusillimonas maritima].
ACCESSION   WP_119515826
VERSION     WP_119515826.1
KEYWORDS    RefSeq.
SOURCE      Neopusillimonas maritima
  ORGANISM  Neopusillimonas maritima
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Neopusillimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Neopusillimonas maritima"
                     /db_xref="taxon:2026239"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39377
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpletv agerrvaatp etvkkyvkag hsvivqqgag reasytdeay teagatlgsa
       61 qdafaaelil kvrapqseel ksmgagkvvl gmldpfnaeh lqtmaqagit gfaleaapri
      121 traqsldvls sqanlagyks vllatqfydr ifpmmmtaag tlkatqvvim gagvaglqai
      181 atarrlgavv wasdvrpsak eqveslggkf idvpfetdee reiaegvggy arpmpqawme
      241 rqaaltaqrc aqanivitta lipgrpaptl itedtvrama pgsvivdlai erggncpltv
      301 agevvekhgv kivgltnlps mlatdasaly arnlldfmkl ivdengklai qkdddivkac
      361 licengqilw gke
//
LOCUS       WP_119530033             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psittacicella hinzii].
ACCESSION   WP_119530033
VERSION     WP_119530033.1
KEYWORDS    RefSeq.
SOURCE      Psittacicella hinzii
  ORGANISM  Psittacicella hinzii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Psittacicellaceae; Psittacicella.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Psittacicella hinzii"
                     /db_xref="taxon:2028575"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56447
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mhigirketq ahetrvaitp sgvarllklg yqvqvetnag lasdytdamy kaagativnt
       61 eqvyasdlll svnpltleqi alckaqativ sfvqpatnea lvnaclskni tllamdmvpr
      121 israqamdal sslaniagyr avieasaqyg rflngqitaa gkiapakvlv igagvaglaa
      181 igtaknlgal vrafdarpev keqvesmgak fltidhveqq ktndgytrst seefnrksae
      241 lyaaqakdvd iiittaaipg kkapvlltkq mvdsmkpgsv ivdiaaatgg nceytqadqv
      301 vttangvkvv gytnyqamlg nqaselysnn llnllalltp ekngelvldq tdvivrnmlv
      361 slaisdaeqa qflyppppis vsattqskpk eqattkpaen pkvvvkrrli ktaalavaff
      421 vylyitrylp aqftdslnvf vlasilgyfl iwnvhsalht plmsltnals givvigviyq
      481 vcspdttvia kllglvgvfm agcnifggfa vtqrmlkmfi kkdvpakggk
//
LOCUS       WP_119525466             529 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psittacicella hinzii].
ACCESSION   WP_119525466
VERSION     WP_119525466.1
KEYWORDS    RefSeq.
SOURCE      Psittacicella hinzii
  ORGANISM  Psittacicella hinzii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Psittacicellaceae; Psittacicella.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Psittacicella hinzii"
                     /db_xref="taxon:2028575"
     Protein         1..529
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56396
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvrkenl tnekrvalsp tgvarllklg yqvvvengag eastytdqmy ldagaqvaer
       61 nevyqadmif svnppsldev ehfkegstlv sfiypaqnta lvesfqqrnv tllamdmvpr
      121 israqamdal sslaniagyr avieassqfg rflngqitaa gkiapakvlv igagvaglaa
      181 igtaknlgai vkafdarpev keqvesmgaq fltighieqq ktndgytrst seefnkksae
      241 lyaaqakevd iiittaaipg rkapvlltke mvdsmkpgsv iidlaaatgg nceytqadev
      301 vttengvkvi gytnyqsmlg nqaselysnn lvnlaslitp ekngefvldq edvivrnmlv
      361 tlsdpsgqas llyppppisv saasptpkse pkavkpkvda ktmakrlviq tsvlalgflv
      421 yiyltaslpq afvadlnvfm lasvlgyfvi wnvhsalhtp lmsltnalsg ivvigaiyql
      481 ngadfgafak vlaligvflg glnifggfav thrmlsmfik kdqggkddk
//
LOCUS       WP_119534139             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Psittacicella gerlachiana].
ACCESSION   WP_119534139
VERSION     WP_119534139.1
KEYWORDS    RefSeq.
SOURCE      Psittacicella gerlachiana
  ORGANISM  Psittacicella gerlachiana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Psittacicellaceae; Psittacicella.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Psittacicella gerlachiana"
                     /db_xref="taxon:2028574"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56053
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigirkeah tnenrvaltp tgtakliklg yqvvietgag lastypdhmy tqagatvvsr
       61 eqvynsdiil avtppeleev pllkenstli sfiypgqnpa lvealqakni tslamdmvpr
      121 israqamdal sslaniagyr avveasaqfg rflngqitaa gkiapakvlv igagvaglaa
      181 igtaknlgai vrafdarpev keqvesmgaq fltighveqq ktndgytrtt seefnkksae
      241 lyanqakevd iiittaaipg rkapvlltke mvdsmkpgsv ivdiaaatgg nceytqadqv
      301 vttsngvkvv gytnyqsmlg nqaselysnn lvnllalitp ekngeikldq edvivrnmlv
      361 tlsnpaeana silypppais vsasskpttp kvtakpqvdt ktlarrlvwq tlglsvgflv
      421 ylyltanlpt afvadlnifm lasvlgyfli wnvhsalhtp lmsltnalsg ivmigaiyqi
      481 ndfdlgifak ilaligvflg glnifggfav tnrmlsmfik kdqggk
//
LOCUS       WP_119539130             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aureimonas
            flava].
ACCESSION   WP_119539130
VERSION     WP_119539130.1
KEYWORDS    RefSeq.
SOURCE      Aureimonas flava
  ORGANISM  Aureimonas flava
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Aureimonas.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Aureimonas flava"
                     /db_xref="taxon:2320271"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55466
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgvprerf agerrvaltp esvgrlqklg yeclveagag daarfsdaay kaagarvvpd
       61 aaalwaeadi vakvrppepd evehvrqgqi lisflypaqn adllerirdr gatvlamdmv
      121 prisraqkmd alssmaniag yravieagnq fgrfftgqit aagkvpparv lvigagvagl
      181 aaigtaqslg aqvrafdvrp evaeqiqsmg aeflfldfae aadgaatggy aapsspefra
      241 kqlelfraqa pevdivvtta lipgrdapkl wledmvalmk pgsvvvdlaa erggncdltv
      301 pdeivetang vrivgytdyp srmatqastl yatnvrhmmd dltpnkdgvp vvnmeddvir
      361 gatvthagei typppppkiq aiarqapkka veetsaqkaa reaaearksg qrqiallaag
      421 avllmliglt appsflqhfv vfalscfvgy hviwnvshal htplmavtna vssiiilgal
      481 lqvgttgwlv silaglailm asvnifggfm vtrrmlkmfq ks
//
LOCUS       WP_119554081             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            cavernicola].
ACCESSION   WP_119554081
VERSION     WP_119554081.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax cavernicola
  ORGANISM  Acidovorax cavernicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Acidovorax cavernicola"
                     /db_xref="taxon:1675792"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38339
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeta agetrvavtp etvkklvasg htvrvqagag iaasvtdagy qaagaeitda
       61 agalsadmvl kvrtpsdaea aqlkagavvi gmlnpfdaag lqrlaaagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf idvpyetqee kdaaegvggy arpmpaswlt
      241 rqqaevakrv aladvvista lipgraaptl itedmvksmk pgsvivdiaa gkgpegvggn
      301 cplseadktv vkhgvtivge tnlaalvaad asalyarnvl dflklvvtke gglkidledd
      361 ivaacrvtqd gqvtrk
//
LOCUS       WP_119558649             361 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Acidovorax cavernicola].
ACCESSION   WP_119558649
VERSION     WP_119558649.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax cavernicola
  ORGANISM  Acidovorax cavernicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Acidovorax cavernicola"
                     /db_xref="taxon:1675792"
     Protein         1..>361
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpsetv agearvavtp etvkklkalg hqlrvesgag laasvtdeay vaagaeisda
       61 agawqadlll kvrgpteaea pwlragttvv gmlnpfdspg lqrlatagvt ayaleaaprt
      121 traqsmdvls sqaniagyka vmiaanayqr ffpmlmtaag tvkaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf ievpyktaee reaaegvggy arpmpaswle
      241 rqkvevakrv aqadvvitta lipgraapvl vteemvqsmk pgsvivdlaa aqggncplte
      301 adqtvlrhgv lligetnlpa lvaadassly arnvldflkl iltpegglhv dleddivaac
      361 l
//
LOCUS       WP_119580400             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces europaeiscabiei].
ACCESSION   WP_119580400
VERSION     WP_119580400.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces europaeiscabiei
  ORGANISM  Streptomyces europaeiscabiei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Streptomyces europaeiscabiei"
                     /db_xref="taxon:146819"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53259
     Region          11..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mvqaepepqs igvpaestag etrvaatpvt vkrlvalgyg vvvepgagas srfsdaayee
       61 agarlgdpwa aeivlkvngp steevgrlrd gatlvalisp alnpdlvedl arrpitvlam
      121 davprisraq sldvlssman iagyravvea ahafgrfftg qvtaagkvpp akvlvagagv
      181 aglaaigaar slgavvratd prpevaeqvr slggefltvs aaqevstdgy aratsddydr
      241 laerlyaeqa advdiiitta lipgrpaprl itaedvarmk pgsvivdmaa aqggnvegtv
      301 agkavvtdnd vtiigytdlp grlpaqasql ygtnlvnlmk lltpgedgrl vldfddavqr
      361 smtvvrdgak twppppvkvt aapapdgape patptsseta akparparpa yvlvgagala
      421 lflvtafspg elighftvfv laivigfyvi gqvhhalhtp lmsvtnaisg ivvvgallqi
      481 ghgnaavtvl sfaaillasi nifggfavtr rmlgmfskg
//
LOCUS       WP_119606610            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            lutimaris].
ACCESSION   WP_119606610
VERSION     WP_119606610.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas lutimaris
  ORGANISM  Flagellimonas lutimaris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Flagellimonas lutimaris"
                     /db_xref="taxon:475082"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116457
     Region          25..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkklfgal lamclsiafa haqektvtgt vtdqegvplp gvniivkgtv kgtqsdfdgn
       61 yaleasvgdv lvfsylgqrt qersigagst idvqmeedas qleevvvtaq givrekrslg
      121 ysvttvdsek vesrpeadva rvlngkvagv nitsnngmsg sgtniiirgy ssatqsnqpl
      181 fivdgipfds gtntqsnfld gntessrfld ldpnniesvs vlkglsatvl ygnrgrngvi
      241 littkgaatg dapsktevsv tqsvfmsnav lpkfqdnygg gfhqgfgyff snwgprfdrt
      301 dddgvasagq firtgpngva ilqhpfnyia dptliagyed flddeypykp yngveeffrt
      361 gyvystsvnv rggsekvnfn anygrtedig vtpgnkllrn nfslggnaal snnftvsgvf
      421 nfartgyksp pnavstgsga afngsaifgd vlytprsvdl tnipfqaadg rslyyrsgnd
      481 iqnpywtvan sktsqetdrf tgnvsmsyai ndwmnltyrv gldtytelns ygqnrggvdg
      541 ptlgilrtts vrnsiwnhdl llsaekslse dlnltatfga nsrrdtyaqd giesqgqlvf
      601 gvlehynftt pssvnsfsgs nlnqnfeenl vgvyldatls ykdllylnvv grndwsstle
      661 rennslfypg aslsfiptta fpalqgnvln yaklrlgygs sagfptpfnt rdvlslgart
      721 fvdangnvvs gntvsdvlgn rdlspervqe leigldtrlf nrlnfnvsly qksttdlitn
      781 rtldsstgfr stfvnigeve tkglevdydl nllreseagi gfnlagnfta settvtdlae
      841 gtnnilltfa vsgeaanyav egrpfgvllg stiqrdengn kvvgsngryl vdnniteigd
      901 pnpdwttali ptitfknftl sanlqyrhgg dvysvttagl igrgvvdadd pihresnyvl
      961 pgvfadgspn nvaitatefg fntffaggin evnifdgtti rlqeaslgys ipkkmldktp
     1021 fgslsltlsg snlwykavnf pddvrydtns sstgvgngqg idfftgpstr rygltvrasf
//
LOCUS       WP_119606776            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            lutimaris].
ACCESSION   WP_119606776
VERSION     WP_119606776.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas lutimaris
  ORGANISM  Flagellimonas lutimaris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Flagellimonas lutimaris"
                     /db_xref="taxon:475082"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117065
     Region          25..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngllt lllafvvhis yaqdktitgt vsdadglplp gvnivvegtt sgtqtdfdgn
       61 yaisasegqt llftyigqkp atrvvgagsv invqmtedaq aleevvvtaq gikrekkalg
      121 yavtsvgsea ledraegdva rvlsgkaagv nitsaggasg satnvvirgl nsfsgnnqal
      181 fivdgvpfsn dtnqqgdfia gntgssrfld ldpnnianie vlkglsaatl ygtqgrngvi
      241 littksgsss tgpkkteitv sqsffandia smpnyqqqyg ngfdqsfgwf fsnwgpsfdr
      301 ggtagwgaqs aiddngtlah pystassatg ipqafpefqg arydwkpyds vedffrtgrt
      361 lntnvnisgs sedgktafna nvgyyndigf tpgnkfdrvn islggvtels nkftirgtmn
      421 yarsnvftpp iassrgngtd glsvygnvff tplsvdlmgl pfenpidgss vyyrqnnsii
      481 nprwtaknvv ynqftnrffw nlsanyalte nldlnwrtgl dfynernnns snkggvefns
      541 aifgflqtyd nnntiwdhfv singnydise klglsftaga tarsdsydrs gvsstgqivf
      601 gvkrhfnyqn qlplqfsrkr nivgllgqat ldyddflfln vsarkdwvsn fqsannsity
      661 pgaslsflpt nafpelksen alnflkiras ygtsanfdtd sayptvgfte qntqvfndgl
      721 sgesittnqv anfkanpdlk pelleelelg feskfwknrv sldftyflkt tndliveepl
      781 apatgftltq snigaienkg ieadlgidii ssenfswnsr vnfftndviv teqeqdqify
      841 sgsipagggl frggnvaqkg kslgsiygta iqrdengdfi vnsagsyqva eqdenglapi
      901 vgdaiadysm nfintfryks lslnfqinht kggdilssti atllgrglie etkdrlgtyi
      961 lpgvkadgsp nntqinnsty yftnllfgpt etriydasvl rlqevslays lpskflektp
     1021 fgqltftvqg fnlwydaynt pdganfdpnv qgvgvgngqg fdflngpsar rygfsvkasf
//
LOCUS       WP_119606897            1022 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            lutimaris].
ACCESSION   WP_119606897
VERSION     WP_119606897.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas lutimaris
  ORGANISM  Flagellimonas lutimaris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1022)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1022)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1022)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1022
                     /organism="Flagellimonas lutimaris"
                     /db_xref="taxon:475082"
     Protein         1..1022
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109749
     Region          24..1019
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllksfl llgaflcfgl akaqtvsgtv sdangplpga svlvkgttng tqtdfdgnft
       61 lndvedsatl vfsyigykta eiavngqtsi nvtleedaqa ldevviigyg qttvkdatgs
      121 vaavtsedfn ggviaspeql iqgktagvqi tqasgepgag mnlrirgsns irsnnnplfv
      181 vdgvplsges ttpsggdvin gsnatrnpln finpndiesm silkdasata iygsrgangv
      241 viittksgkt gqggvwefss nlsistpand ydlfdrdefl sttasvrsqa iadasdygyn
      301 tnwqdyitrt vasqnqnlsy srnygsgnvr atfsygkqfg vieksaqeri tgrinasqrf
      361 lddklrftlq asisrvndda ppisgtsgas gnligaaysa nptwpasstf flegnqlnpa
      421 nylqnfqsvt htdralinfs aeydltpelt akvsvgydds datavssisg nannfnrvtg
      481 ngqtayntln akskllegtl nykkdfdnss ldvivgysfq dfqrvgfnsq gwqapttdln
      541 emgelliedv nnirssidgp yqqagyapng tfinsinpfe dtatlgtssg gytsvwvdtf
      601 dntdelqsff aranyslndk flftatvrad gssrfsednr ygyfpsgala wkineedfig
      661 dnistlklri gagvtgnqeg lgyanflrrv rfaqpgisds geilrpgaqt vavqnpnlkw
      721 estldlnvgl dfgfnldrfs gsvdfyrket ndllfrqgaa apaadpfvfk nleegtiinq
      781 gievalnydf vqtedvtfss sfniaynknt veglngvtan fgalngpglt dafaqrlgeg
      841 rslfsyymae ysednfnpde kdfvgedglp dvnaglslnl rvknwdasay ftgqfgfsvy
      901 nntanaflnr ptfettrnvt qraldtnvsq evstlylesg dfvrlqnasv gynvpvsgdg
      961 aikslrlslt gqnlflitdy sgldpevsss tgdlgtgips asidytafpr prtvtlgina
     1021 kf
//
LOCUS       WP_119607416            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            lutimaris].
ACCESSION   WP_119607416
VERSION     WP_119607416.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas lutimaris
  ORGANISM  Flagellimonas lutimaris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Flagellimonas lutimaris"
                     /db_xref="taxon:475082"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120046
     Region          23..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksivafll aftvsiisys qvtfsgkvvd ensvplpgas vvvkggstgv atdfdgnfei
       61 elpqggeilv vsyigyvpqd ldtsgkstat imlqpdsqql eevvvtalni trdeeslgys
      121 vqkvggeeis qststntvst lsgrtagvqv vtngtgpgqs ssvvirgyss mqgdnqplfi
      181 vdgipinnnt dtrtntlgga snmnldygng aaeinpddve sisvlkgana talygsraan
      241 gaviittksg kgrkggisfs skttfesvlk apeyqgvygq gknfdfqfvd gygsgtydgv
      301 deswgplldg tlraqhdspt snglrggdvh gldyilgssg vdldrrgtit pipfvyggnp
      361 aeefmetgrt lintvsffgs ndngnyrvsy tnldnkgivp ntdikrntis asgdyqitdr
      421 lkvsskinyi rsdsdnrhvn gygtesvmyl fiwwgqqvnv nslrnywqdg legfqqynyn
      481 ynyhdnpyft myentnglak driignlsat ydisddfkfm vrggrdffse yrtikrayst
      541 qrfpngqfre dkinfqetnl dflltydkdv tdkfkvnanv ggnrmvqknh fnslmankll
      601 ipgiysfsnv dgalvqrtsr pekqinslya faqlgwnssi yldltarndw sstlpeqnns
      661 yfypsaslsv vlsdlfdfsg qdvlsfaklr ggwaqvgsdt dayrlsdyya lgtpvgdnpt
      721 aspsntlpnf dlkpeiqtsy efgtdlrffn nklsldatyy nsvsknqild idlpitsgkt
      781 artinagkir nqgleimlsa npvsnqsfnw ntsfnfglnr nkvleladgv eryqyggngi
      841 slvaeeggsl gdmwgtglvk vedenspyyg dvifneglvq qdntlrkvgn fnpdftlgwn
      901 ntityknlsl nflldwrqgg ellsrtrlia atsgnvvetl wgrspeyggp hpgiadsgls
      961 ytddngtawt dgvigdgvkl qdgqyvtndv ivpanayhnn ryrrgndteg iydatfiklr
     1021 earltydfpt klfkgddikn lsfsvigtnl wlwakdfnhg dpellsfggg syvpgvenat
     1081 vpttrslgfa invef
//
LOCUS       WP_119608807            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            lutimaris].
ACCESSION   WP_119608807
VERSION     WP_119608807.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas lutimaris
  ORGANISM  Flagellimonas lutimaris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Flagellimonas lutimaris"
                     /db_xref="taxon:475082"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116616
     Region          26..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklikkrnll fllfalvmas gwsqektitg lvtdeegipl pgvnilvqgt ttgtqsdfdg
       61 nysisasegq tliftyvgqr tvrinvgpgn tlnvqmeeda qaleevvvva qnikreagsl
      121 gyavsdvgse qiedraqgdi grilqgkaag vnitatngvs gsgtnfiirg ytsisgsnqp
      181 lfivdgvpfd gganeqndff dsagessrfl dldpnaienv kvlkglsatv lygergrngv
      241 vlittkggss kntakklevs vntsyfvsna ilpnfqkqyg ggfhqafgff fsnwgpdfad
      301 qrefpyganf rgiapdgtvl vrhpfdaind nsltaefqdl aasnyryqny nsvqeffrtg
      361 gvstnsinlr gstenvtynv nlghledkgf tpgnkvirnn fgiggsakls nnitvsgtln
      421 yantdyrtpp isasagsgtv gdgssvfgdv mytprgvdlf glpfqtstgr siyyrsgndi
      481 qnprwtlana kttqntervy gnlsfnyqia eslglsyqlg ldtytelssy gqnrggvdgd
      541 pngifrtttv knkiwnhtvn ltynkdlted fslqailgaq srndsfdrdg vestqqlafg
      601 vlrhfnfvnh atvnsftgee ialqarenqv giysditlgy kdglflnlaa rndwsstler
      661 dnysifypaa slsfiptkfi dgmvsdnfls slkmrigygt sagfpdpygt rnqlsltsra
      721 vvnqtgnvls gnsvanrlgn pdlkaetvse ieagidaqff rnrlslnvsv ykktaddlit
      781 dqnldpasgf tvtrinsgsl etkgieidfd ftpvrtdnfr wnlagnffad eslvtslpeg
      841 tdqivltssi dgrpanyaie gqpfgvlqgr atikddagnr vvggdglylv gndieiigdp
      901 npdwnagfts tfsykgltls anmlyrhggd ifsqtaatll grgtvavsgi dreatyilpg
      961 vlengepnni qvtatnvgfd tigfssgndl qiydgstlrl nelsigyamp qkwldktpfg
     1021 klsftlsgnn lwykafnfpe dvrfdtntls tgvgngqgid fitgpssrry glsvnatf
//
LOCUS       WP_119608810            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            lutimaris].
ACCESSION   WP_119608810
VERSION     WP_119608810.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas lutimaris
  ORGANISM  Flagellimonas lutimaris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Flagellimonas lutimaris"
                     /db_xref="taxon:475082"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114263
     Region          27..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mglikkgnll fllfillvny swsqsntitg kvtdefdspl pgvsvvvvgt nkgtqtdfdg
       61 nytievnpgq slrfsylgqk tvtriigeqs mlnvkleedt qsldevvvta lgiakdarti
      121 gygtdivkgd elvkaretni tnalqgkitg vqitnsggnl ggsskiiirg vsslsgrnep
      181 lwvvdgilin nsqtpgngsr itgtrdfang asvinpddve sinvlkgaaa talygsraag
      241 gaiivttkkg ksnpnggatv tinstvrfdn lfrkpdyqqe yamgtqgqyd agavgfdwgp
      301 rivgqtvqnl pvtgepgilk pvdnngvddf fktgftrinn fsvsdadekm dyrisvtsln
      361 qtgvlpgael drltiglnag vrhseklesr fgvqytktns igtgasgand pniiglssfs
      421 stldqnlfkp widasgnqin litsnngves nnplwirnen sndrnadrif gnfqltykpf
      481 tgfgvtsrig ldvqddrrli enskgtiara qgdfisdeir rnettidifa nydpdlnsdf
      541 svslltgvqy nqriferqqi qgvnllipel fspanaaqti girdftesrl fgiygsaeig
      601 yknwttltlt arndysstlp lennsyfyps aslafiftda fdissdfltf gklraswaqv
      661 gndtdpylln fnfnpvtsaf gqyslnlnfp fngalayaat ttipsvnlqp eeqtsyefgl
      721 dlklfngrln ldvayfnsrn enqilnipip estgfrfrte nvgrvdqegf eialdatpvr
      781 agdfywntgi nfsrvestvv slteglervt iasafnsvqv vavpgkefql fgipylrdev
      841 tgrpiidpnt grrqageatt lgsvlpdwtg gfvnsfnykg fnlsatmdvr wggviksstv
      901 eglqtgglvn etlrnregtf idtqgiliae npdgtvtrtd nnvplynaqd lwtslndnsv
      961 aepyvydasy iklrevgfsy tfpsrflest fikgltigve grnlallysk vphidpeasl
     1021 fgsgadgfgi erasipstrs mgfnlkltf
//
LOCUS       WP_119608750            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            lutimaris].
ACCESSION   WP_119608750
VERSION     WP_119608750.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas lutimaris
  ORGANISM  Flagellimonas lutimaris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Flagellimonas lutimaris"
                     /db_xref="taxon:475082"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111222
     Region          42..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlsfyvsr tvllllfylv lapwhssnvl agtkimrfqt mvsgtvtdmd gnplpgvniv
       61 veatgtgtis dmdggfriaa sdgdvlvfsm vgfksqsvpl sgrddirifm vedvtalgev
      121 vlnagyykvs ekartgniat vtsdvlekqp vanplagmqg hmsgvnivqn tgvpgggfsv
      181 evrgrnflng asdplfivdg vpfgsqslga arvsnqivgg displnainp sdiesievlk
      241 dadataiygs rgangvvlit tkkgragktr fdahlsttlg evsnylelld tpqylelrre
      301 giandgfqdl fegpifdffw pdlktwdqdr ytdwqeelig gtayrnnaql svsggndltq
      361 flvsgayqke ttvfpgdfky erasvhsnln hrsengrfml nlstsysqen nqlpsgdfta
      421 qaytlppnap alfdeegnln wenntwdnpl aileesyvvg sktlisnavl syairpnlel
      481 kssfgytnyr ldtyrtmpss arnpgfgltp qnysslmtng sqreswiiep qlnwrkewdg
      541 vsmdvllgtt fqqetseqsv lrgrgfpnne lirnmaaaet levlsnsdse yrynavfgrv
      601 nlnvlnryll nltgrrdgss rfgpgrqfgn fgavglawif seesifgads plsfgklras
      661 ygttgsdnig dyrfldtysv tgnnyngvtv veptgifnpq fgweenkkle aalelgffkd
      721 rvmvnaswyr nrssnqlvgi plaattgfss ltgnfdaive ntgveidlnt vnirsgkfgw
      781 tttfnltipk nklvafdgle tstfanryvl gepltivnly qslgvdpetg lyqfedyngd
      841 gnisssedre wiedlapdfy gglgntfkwg dltldvffqf kkqkaynalr ynaspgwqtn
      901 slvqlydrwq epgditdiqr assgldlsnn qgalqqesna avsdasfvrl rnislnykvp
      961 gldngldinv ylqgqnlwtl tdylgpdpeq psnirlpplr qltlglqfsf
//
LOCUS       WP_119618112            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacteriaceae].
ACCESSION   WP_119618112
VERSION     WP_119618112.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113860
     Region          20..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksiyltfva vfsciaafgq titgtvsdts gtplpgvtiv vsgtnngttt dfdgnysisa
       61 ssgqvlrfsy lgmttkdvtv gsattlnvvl eedstqldev vvtafgveqk qkslgysvtk
      121 vntedlnlag qanpieslqg rvagvqinrs sgtsgggvdi lirgvtsinp nrsnqpliiv
      181 dglaldndtf sgevrpsags nspnsseqfa fsnragdlnp ediesfnvlk gaaatalygv
      241 raangaiiit tkkgkqgrak initasttfr nvkttpplqt kyregfggap rtlydptset
      301 gfnrvqnsts fyswgpeyal dsydlgggni vdlsddrfys pydifrtgfn sqlnlnlsga
      361 ndrlnyyfsv gnnseqgvlp ntdykktnfr lkagykvtdn fnidgsiaft nsggkrangg
      421 dksvmsalyy yagtfpindy qnadgserdy sfgiidnpry lletsnledd vnrwignttl
      481 twspkdwvti tyaaqidnys darnryvgpd ldggaqiggf ileqninftg lesnflvaln
      541 kawsedfttd ltlghqlsds krsylearge glnvpgvnei gnttnffink eivqlrnvgv
      601 fgelkfgykd klflsltgrn dwvstlpken rsffypsvsl aydvsglfge ndiftfgklr
      661 aswaevgkgp gfgdvgqyfv vdsdfpfggv ggyrrstllg dldivpernq stefgadlrf
      721 lndrirldya yyntrvkdqi ftvgtayssg lsgitrnagd yeifghefll sadiirnqdi
      781 kwevilnwst segkvleipe diesvvfads gftgitsevr agdkmgnlyg ykwryenger
      841 yidangfpvi nteekvvvgn afpdfisslg snfkykgigl nfllewkkgg dlydagirna
      901 irngtptstl eryvnvvleg vmdngsggfv pntteafide nyyrnsnvyn raaeilvqda
      961 swvklrnisl sydfqsrfik dlnldrvsis asannillwt pfdgydpegn qysagsnvyg
     1021 ftglniplae sysfglniaf
//
LOCUS       WP_119618623            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacteriaceae].
ACCESSION   WP_119618623
VERSION     WP_119618623.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122557
     Region          24..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksyvylll ccllslsaws qdnvirgvvt dqagvplpga sivekgtsng vvsdfdgqfn
       61 ltpsknqiil eisyvgykhm eisarsgsfq eitmeedase ldevvvtaln itreekslgy
      121 avakvegdev tksvsgnwmn gmsgkvpglf faqagsgpsg sirvtlrgdq slnyggneal
      181 ivvdgvpiss gmtatravsn yaqadapvdf gdglsdinpe diesvsvlkg paaaalygsr
      241 aangaimitt ksgkkgkglg itinttvsfe qagffpdfqt eygngsdmge qpyslwelta
      301 dmapdgvatn rnysrytfge rfdpnkmryl yasknwetgt fsklpwvyqd dwytglfrtg
      361 vttintvsin gnngegtssr lsitdfkndw impntgfnrq saslafntpi ndwislnskv
      421 nyyrkrsdnm pgggydesnp myaliwgfnv nsiddwkney fdgrynfvnw saqgengqgl
      481 vfpsansynp yrtlyealsa hdknrvfgni glnfdlgngf sldlrsgldw stefrtqrrp
      541 fyttdypngf yreqtvryle nnndfmfrye nndmadgrft lsafvggnnr vneyynsrit
      601 leqlgeegiy httnlptgvn pdnynyrskk vvnsfygmls lgwddtyfld vtarndwsst
      661 lspgnwsffy psvaasvlvd kvldfqtnap widftklrfs wanvgndtga ysltqpygnt
      721 sfpggyvlpg tirnplikpe nieswevgle akffknrlsf ditkyysstt dqivsvnvdq
      781 itgatgriin ageitnegie iaagfvpirt kdfewsfdan wsknnntlvs lqegwdpeep
      841 lqtdmgttig grvyvysylg gemhniygrg fqrapegaty idengetvda sgmhivnsqg
      901 ypvldespdr eiakvnpdwr ggmtqrfryk nlslsasfsa qmggsafsvt nfalsyqgkl
      961 knslegrydg lvhegvnvve ntdgtvtytk nttvteniqt yynayiwnrn ntemntfstd
     1021 flklrelrld yqmprkimes tgifqdmsfg ifatnvfcwt dfpqydpetg mlngsnimmg
     1081 iesvtfpmtr tyglnvklsf
//
LOCUS       WP_119618836             991 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacteriaceae].
ACCESSION   WP_119618836
VERSION     WP_119618836.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..991
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107862
     Region          34..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklhdylgq mrsrlvlivf lasalsafaq sqytfsgtvt esgtgvplag asvfientsy
       61 gsvtdfdgny sfsatlesds ytlaisslgf stqriavtag gsssittdan laedllslde
      121 vvvtgtgaga nkrtlgnais svkaeelvdn gatqidqaia gkvtgalvqq nsgdpaggis
      181 irlrgpstia gssdplyivd giiisnssne lvdlggnaqn rladinpndi ekieiikgaa
      241 aaaiygsras ngvvqiftkq grsgepkftf mtntrinelr kkidynqvpl awavpsnrsd
      301 lttvevdryd lqdemfesgf gienyfsmtg gtektsyyls ashldndgii kntnfkrygf
      361 kanltqkafd wlditggfny irsvsddmpn gginsaygai tgfvfsdnsi dpspdesgvy
      421 pvtspavprt npaeavarfd faqktnrfit svaldanfte klsakytlgl dyynqsatay
      481 ipinntspnp dgyarrsdln sfqynsdlnf tyktditssi sststlggsw qyeerenigi
      541 natglppvve tatggsileq genrsqisyw gaffqqsfgf ndkiyvngav rmdgastfge
      601 dernqlyfka sasyvmsded fwkntfgdtf nlfklraswg qagnltalsa yarfsnynps
      661 altgsvslip stqlgneslk perqdetelg fdagllnnri giefsyykqk vtdlllqrvl
      721 apssgfssrf envgnlentg vevllrgapi ktkdfnwdlt atfsknknev tnvagggria
      781 lpgsfstnyv iegqplgvfy hgfyarnedg sialddagyp yrgqteeger skvigdpnpd
      841 wfgslineft ykdfglrvqf davqgydvfn wnrrlldnvv fgggynvgqe llgnrpkgyg
      901 saqasifeef vedgsfvklr evalsytfkp kwehidnvrf slvgrnlisw ddysgwdpev
      961 saagqsngvr gfdfatvpip rtyqlgvnvs f
//
LOCUS       WP_119619062            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacteriaceae].
ACCESSION   WP_119619062
VERSION     WP_119619062.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113137
     Region          23..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miqklkfvfv favllsiqga maqtitgtvs desgvplpgv nivekgtsng vssdfdgnys
       61 ivvsdgnail vfsslgmetv emsingrsti nvtmkedaqq lgevvvtalg isrekkslgy
      121 avtevqgdev slvkepnvvn slagkvagvv vsrttsgpgg gtrvvirgnn sisgnnqply
      181 vvdgvpidns alsaptgage fsipdlgtgi sdinpddies lsvlkgpnaa alygsrasng
      241 viiittkkga lkkgmgisft ssatfenpfv lpkyqneygr gtdgnfptin psdplsaqva
      301 avrgtsswgp rfdgserlay ngemrayeaq pnnvedffet gtsfintlsl ssgnetssvr
      361 fsytnsdlqs ilpnsnvdrd nfnlraftnl sdkltldarv tyflqkaknr ptqgtegvma
      421 ylwplarnvr indlkqyqnf enpldptnpy gvvaptasgg npywilqhds nmdrrsritg
      481 faklqyefnd wlsafvrvgt ddisqdteai trtghhffps grvnygknkr tetnydfllm
      541 fnkdlsekfn lnanvganal rfstissstr genikipgrp fldntenlfa tqsalikknv
      601 nsvygaisla yddmiyldlt grndwssala aenrsyfyss aslsvllnea fdlgsdinll
      661 kvrgsvasvg ndtdpqqlvn lfriaangfl dnvtvtrett lfseslrped vqstefglel
      721 rafnnrfytd lsyysisskd lifdvpldpg sgysnfrtnv geisnkgfei lvggtpvqte
      781 nfswetsinv srnrnklesl vegqdffefs ssntgrvstv arvgqgfgdi etttwlrnde
      841 gqliltaegr pqatserqkf gnyqpdavgg ftntfryknf slntlidfri ggevysgtda
      901 gldaagvser tlqyreggvl vegvvdngdg tfspntttis aqdywgavst igseyvydqt
      961 nvrlrevslt ynfpkkildn tfitnasisa vgrnllflyk dvdnfdpess ystsnfsqgv
     1021 lfyalpstrs fglslnvnf
//
LOCUS       WP_119619521            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacteriaceae].
ACCESSION   WP_119619521
VERSION     WP_119619521.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116555
     Region          81..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlkklskr itnllllvct ymicfivgtt etyamhlpll eweneeglfk iselglntng
       61 kdvpnakste ndmdnlqfsa sgnvsdgtgv plpgasvvek gtsngtqtdf dgnftiqvsg
      121 pnailvvsym gydsqevain gqssisvale esaqalsevv vtalgiksdk ralgyataqv
      181 dgddisgvka tnnfvnslsg kvagvqisst ssqpgsgtri virggssitg nnqplivvng
      241 vpfdaansst ssglgdidpn aieslsvlkg asaaalygsr aangvllitt ksgefeskpv
      301 itfsnsvsfd riyevplqkt wsqgfwdgtd wsyvdgetsf tstswgpris dvpgaqyydr
      361 wdvfktgitn estinasggs skasyfvsys nlmndgildp mkfrrnsina ntsfkftpkl
      421 tvsssilytt qknsrldeds snsafmntvl aapntwnpyp lyneegnlrs yrggsrdpyl
      481 wllnnvgdnn irdrfngtit ieyqilpkls frsvtgists slhedahynk ggyasvqgsy
      541 stserfdrni estetltydn dfgdfsvtal vghniseerr rqvyfngtgl vlpgiyntan
      601 vsgysageyn rmfraysyfg qavigyknfl yytvtgrndw assladsffy pshslgfvfs
      661 ellpksdvfn ygklrasyak vgapadpytr nvvlgsplsd gvlwpfngqq sylsttqian
      721 fgltnefkse velgaelkff qnrlgvdfay yhnwsdnqil geqflastgy tygnvniggi
      781 thkgvelgiy atpiqtedfe wdvnvnfskd npmvdnlgnt depigvgsyg tavvgqpypv
      841 iygpgflrdd qgrlvlsdap gtgygrplad nsqnqilgqt vpdwmgsfrt gfryknlsfs
      901 alldvsvggy lyslndhylt yygmakhqen rpednmitfd gvmghydagt gqvvvtsetp
      961 eptrydlywq tvaqnvwedn imprdyiklr evnlsyripk dmlsnvglta ldislsgrnl
     1021 wrkfkdgfeg adpevntdgi tngnaylgys mpatktytlt ltakf
//
LOCUS       WP_119619585            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacteriaceae].
ACCESSION   WP_119619585
VERSION     WP_119619585.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121614
     Region          23..1101
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklililm lalssgyvfg qsitvtgsiv daetnqpvpg vtvlqmgaan gassdfdgny
       61 sievpsnatl rftaigyesq eivvngrtvi nvvmsinteq lnevvvtglg itrekkalgy
      121 atatveaeal tevatpniaa alygrapgvq isatpggats avnitirgaq sitgtstpli
      181 ikdgipirng dvnngnywdd qrirgnglnd inpediesis ilkgasaaal ygseatngvv
      241 littkkgkgr gwsadfntay nfdrvaylpe fqnergpgyp lsisdagqde nlflyydldg
      301 dnvnetrgli gttlnfgprf dgqptlawdg kirpylpqds ysglfntaht tryntsvsnv
      361 tensntrfsf trsdngsivp nsssyknifn lnttinwteg frstlvvdyi ngrvnnrpyk
      421 idrlmnnfgg mmsrfdsaew ykdryqtslg yrwvtganqs ltpdeniiyg gykepvleyl
      481 yranrfqsee rsdrvignlt lewdladnlt lrgrvsndft teyienrnpn evpiafgnsg
      541 yfsmstrtns ikygelllsy taqinddfsl larlgynate qkmrytsaft dgglsvenwf
      601 dvaasvnqar qdndrenlik damigllnld ykgifyvegt irrdrtstms pqnnsfiyps
      661 vnssfilsda fampeainll kirgswgivg nypsiysani aynqnnlgvq gggssilytt
      721 lptdfgndni kpeekheyef gveanlfdnr fifettyyna qiqdqilglt ipitaggssv
      781 lsnvgtlrns gievgltyfp irgqnvnwel gitgsrqwnk veklapglde iihadydgna
      841 aqlvsrvgqp mgdllahpva tdsqgrkivd pngmykvdpd tlvtvgnaqp kviggirsgl
      901 tiknfslnvl adyrigghvm ptalnwmtsr glteeslnys tsergglsyy etndgtrvqi
      961 aanatsgpng eqvfhdgill egvqadgsen dvivsnpeyy ftvynwggpq yspntryely
     1021 iqennylklr eislgyslar kvvdkiglks ldlslfgrnl fyiyrsiknm daeqttagsn
     1081 wfqnvnnvgn gfstrsfglq vrarl
//
LOCUS       WP_119619854            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacteriaceae].
ACCESSION   WP_119619854
VERSION     WP_119619854.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111775
     Region          24..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllksfl llgaflcfgm ikaqtvsgtv sdangplpga svlvkgttng tqtdfdgnyt
       61 lnnidgsatl vfsyigyktv eravngqsti nvtleedaqa ldevviigyg qttvkdatga
      121 vaavtsedfn kgvisspeql iqgktagvqi sqgsgepgsg vairirgtss vrsnnnplfv
      181 vdgvplpsgd tssegtnigv gsssarnpls flnpndiesm silkdasata iygsrgangv
      241 viittksgkg gakggtweys sdlsystpak efdllnasef ldavdafggs ainygndtnw
      301 qdfvlrstas tnnnlaysqn ygsgnvratf nygkqfgiie kssqeritgr lnashrfled
      361 klrlnlqgtl srvndeappl sgsagstgdl lgaayasnpt wpasptfnpg drinplnllq
      421 nwqsmtytdr vlvnfsaeyd ildeltakvt vgydksdskr easlssksfn vgsgaagngr
      481 galndlinen rlleltlnyn teftnsklda lvgfsyqdfn vrgrnvqgwg ysspdlnqma
      541 tdlsnsastl eamisgryqq ygysfdvpnn paglfvnrlf ptpeteflge ttglgvralf
      601 tdifdntdel qsffaranyt iadkylftat vradgssrfg ennkygifps aafawkinee
      661 dfigdavstl klrlsygitg nqdgigygry irrerysggg igdggavnvp gtstvdfanp
      721 dlkweettqy gvgldfgfsn drlngsvdvy rketrdllls veaaqpspqp fffqnldatv
      781 lnqgiefsln ydilqgedys wtagfnmayn kneiqdfega ipagtirgag ltnafaqrlq
      841 ngqplysfyl refigfdeng npvheggtdn qkfvgksalp dftggfstsa ryrnwdasly
      901 fngqfgnyiy nntanafftg gaigsgnnvi kdvvalagee srfaeasvst rflekgdfvr
      961 lqtasigynv plsgegmfks mrlsltgqnl fvitdysgld pevsvtpatg dllnglpiag
     1021 idysafprpr tytfgfsvtf
//
LOCUS       WP_119619938            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacteriaceae].
ACCESSION   WP_119619938
VERSION     WP_119619938.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116129
     Region          25..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmtklkfifl lqflllawlg taqertitgt vrdderislp gvnvivkgtt rgtqtdfdgn
       61 ysigasrget lvfsylglqt qevvignass vdvtmledaq aleevvvtgv lgtksqpraq
      121 gfastnlsna dltdvtntnp feslsgkvag vdittpaqpg asskvivrgf ssitgsnspl
      181 yvvdgtpins ssngslesaf nrsfdggsgi ndldpnsies mtvlkgaaat avygsrgang
      241 ailittkkgr kesrisvdft tsidflevsr vphlqnqfgq gwnglsyssl pmgglgasne
      301 ngswgpafng qvrpwgqiid nsqqikpyva lpdnikdfyd vgqvytnsvr iggggtnsdf
      361 slgftntdsd gvipteaday drkvfnlnag vnnekfsvra slnyakrdqn vvntgqgdqa
      421 gegntfsqei iqiprdislv dlkdyqnnpf nnnsnfytpf asnpywvlne natkinsnrv
      481 fgninltynf sptlsaswqi gadienvnrk sygaivdylp gspqdllaal pivggvteyr
      541 lerkqydtyf tlnheydite dlnlttsagv afnqrstdal qvsvtdldip nyyeisnsas
      601 tpstgqsntl rrtiglfats tlgyanryfl tltarndwss tlpigqnsyf ypsatasiil
      661 ldnnatflkl rggvsqvgnd ttpyntesal vqglagayfg qinmplggvn sfelssqlgn
      721 sllkpeitne yeigteasff nrritldaaf ykkdtkdlll drllprstgy lnitgnyasv
      781 tnkgielvlg ltpfrsnnft wdinytftkn enevtdlqgl erfeinssya tyfyaeegqp
      841 lgvfrfrgpa vndqgqyivd gntgfytqds eeqylgtsqr dfimglknsf ryknfrlsfs
      901 mdwkeggkmy sytnrllgft gnsiattyne rkpfiipnsv vensdgtfse nttpisfedv
      961 tnfwgtasnp aieythvidk tfvrlrdlsf tysvssdfak tmglsaasit fygknlalwt
     1021 pdanpymdpe vstfgndlas efgefaanpa qrtygaalkf sf
//
LOCUS       WP_119620072            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacteriaceae].
ACCESSION   WP_119620072
VERSION     WP_119620072.1
KEYWORDS    RefSeq.
SOURCE      Flavobacteriaceae
  ORGANISM  Flavobacteriaceae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Flavobacteriaceae"
                     /db_xref="taxon:49546"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117154
     Region          23..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksivafll aftvsiigys qgtfsgkvvd ennvplpgas vvvkggsvgv atdfdgnfqi
       61 elsqggeile vsyigyvsqd fdttgkttat imlqpdsqql devvvtalgi qretkklaya
      121 vqkvsgeeis eaketnvvns lagkmagvqv tggnsgvgst sqiiirgens lnpspnansp
      181 lfvvdgipin nnvnntgseg nmgvdygnga mdinpddvet mtvlkgpnat alygsrgang
      241 vilittksgk gskgigvsyt nnttfedllt lpkyqnrygq gsngqfafnd ggqnrsltgg
      301 indhvdeswg palngqlipq hdspttsglr agdvhvrprn sdgtfadeii atpfspqpsn
      361 iddffrtgft lsnnialtgg nedgnfrvsf tdlqsesvip nsnfkrrayq vngsynltdw
      421 lkvtgsmnyi nsnsrnrpnn sygtenvmyl wiwfgrhinm nnlrdywqpg legvqqfnyn
      481 ynyhdnpfft vfentnafnk drlitnlrad iqlakglsfm frsgfdysne ldkrkrayst
      541 qrfpngqyre dfiyayeqnt dfllayntei nqdfdfgvsf ggnhrsaknr yqrisansls
      601 ipgiynfgna aepltqsdyd gkftvnslya fsnvsykdya fldvtarndw sstlpdgnns
      661 yfypsvglsf ilsdmftmpq aisfaklrgg wasvgndtdp ynlaatygfg ntfngfsrvy
      721 spselklsdl kpertnsfev gadvrffgsr lgldvaayks vtnnqilslp vsntsgystr
      781 vinagevenk glevtltatp vqtdsfswnt ninftanrge vkeltdglds ylvksnylqv
      841 vaevggrmgd lygtgfeqvt dksspyygqw iidpnsglpi rsnelrnlgn ynpdfmvgfq
      901 nsfsyknfrf gflfdwrqgg vyhsrtvaig gttgmldftv pgresgivaq gvidngsgsy
      961 tpnttsvnas nyyshvynrg neqssmfdat yvklrevklg ytfprkllek tplksasval
     1021 vgrnlalwte ndhvdpetis lsggsivpgv edmalpstrs fglnlnvef
//
LOCUS       WP_119628470             172 aa            linear   BCT 07-JUL-2024
DEFINITION  aromatic/alkene monooxygenase hydroxylase subunit gamma
            [Methylocaldum marinum].
ACCESSION   WP_119628470
VERSION     WP_119628470.1
KEYWORDS    RefSeq.
SOURCE      Methylocaldum marinum
  ORGANISM  Methylocaldum marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylocaldum.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Rosenzweig,A.C., Frederick,C.A., Lippard,S.J. and Nordlund,P.
  TITLE     Crystal structure of a bacterial non-haem iron hydroxylase that
            catalyses the biological oxidation of methane
  JOURNAL   Nature 366 (6455), 537-543 (1993)
   PUBMED   8255292
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Cardy,D.L., Laidler,V., Salmond,G.P. and Murrell,J.C.
  TITLE     Molecular analysis of the methane monooxygenase (MMO) gene cluster
            of Methylosinus trichosporium OB3b
  JOURNAL   Mol Microbiol 5 (2), 335-342 (1991)
   PUBMED   1904125
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Fox,B.G., Liu,Y., Dege,J.E. and Lipscomb,J.D.
  TITLE     Complex formation between the protein components of methane
            monooxygenase from Methylosinus trichosporium OB3b. Identification
            of sites of component interaction
  JOURNAL   J Biol Chem 266 (1), 540-550 (1991)
   PUBMED   1845980
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Stainthorpe,A.C., Murrell,J.C., Salmond,G.P., Dalton,H. and Lees,V.
  TITLE     Molecular analysis of methane monooxygenase from Methylococcus
            capsulatus (Bath)
  JOURNAL   Arch Microbiol 152 (2), 154-159 (1989)
   PUBMED   2505721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF045805.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Methylocaldum marinum"
                     /db_xref="taxon:1432792"
     gene            1..172
                     /gene="mmoZ"
     Protein         1..172
                     /product="aromatic/alkene monooxygenase hydroxylase
                     subunit gamma"
                     /EC_number="1.14.13.25"
                     /GO_function="GO:0015049 - methane monooxygenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=20022
     Region          6..166
                     /region_name="MeMO_Hyd_G"
                     /note="Methane monooxygenase, hydrolase gamma chain;
                     pfam02964"
                     /db_xref="CDD:427082"
ORIGIN      
        1 manypvhdnp vrdawmdkig klnkldkave flkdfrlkht tplrttyele ldylwienri
       61 eekvaqlkah aftdqqfled catgesarav aeswlakina ctdkwaaekv hiqfrqlykp
      121 pvmpvnyfmd adrqlgsrlm elrdidyydt pletlrkqrg vkvvhlqpas vq
//
LOCUS       WP_119628284             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylocaldum marinum].
ACCESSION   WP_119628284
VERSION     WP_119628284.1
KEYWORDS    RefSeq.
SOURCE      Methylocaldum marinum
  ORGANISM  Methylocaldum marinum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylocaldum.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Methylocaldum marinum"
                     /db_xref="taxon:1432792"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54902
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkeih agekrvatvp evaeklvklg fsvtvetgag dnanfsdday rqvgcdiaad
       61 aksiwadsdi vlkvrgpqvh pelavdevdc lreggnlisf iwpaqnpdlm erlaakkatv
      121 lamdsvpris raqkldalss maniagyrav ieaaqhfgrf ftgqvtaagk vppakvfvig
      181 cgvaglaalg aanglgaivr atdtrpevkd qvkslgaefv evnyqeegtg vggyakvmse
      241 gyqkaqkemi arqcmdvdiv ittalipgkp aptlitagmv esmkpgsviv dlaaeqggnc
      301 eltvpgevvv rhgvtiigyt dlpsrlarqs stlyatnllr lleelcptkd giinvnmede
      361 virgttvike geitwppppp kisaapagat pappveikkv ekkpllpawa qtgimlgvag
      421 llfyglgsva paafmshftv fvlacfvgym viwnvtpalh tplmsvtnai ssiiaigali
      481 qisspgvlit ilaglaivlt svnmaggfwv tqrmlrmfrk
//
LOCUS       WP_119638690            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119638690
VERSION     WP_119638690.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115419
     Region          25..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklkgila flmllvvhlt saqektitgt vtdhtgiplp gvnilvegta tgtqtdfdgi
       61 ytisaapgqt llftyigqkp tsvivggsst idvqmeedaq aldevvvtal gikrekkslg
      121 yaqqsieges vvlakdtdis dglagkisgv qlvgspssty essnirlrgn vgvlyvvdgi
      181 kinspgdinm qdvedisvlk glaatalygt earngaviit tktakdgetk vtvdiassls
      241 slyllpkyqn eygggysqtf aqvdgqnipn fsadeswgpr ldgtlvrqwd swivgdpgyg
      301 elrpwvptph giedfyetga tsnitvgflq ggekyniktt vnhvgttlin pnsdrkqtti
      361 sfkgsynvte klkfngvfny qyrytfnnpq drgyagnfne wwqrqldmtr lrnykrngqi
      421 vswnmraydn ptplywdspy fevyenlnhe tknaiygslg leyeilpelv atvdlrrtfd
      481 lynfddrnaw gglatpryle kttqneftea ytqlsynkki gdfdlvasag aqfnqrkykl
      541 ieaqtvgglq ipnyysidts vdkpnyvrds rhqklnstfa tasvgyknfl yldgsyridw
      601 gstaasdnns vdtygvsasf ifsefindgs flsfgkirag faqapsfpdv yrlqstydiq
      661 npygsnvals vpdilnnpgl iggvreeiei gtelsflnnr lgldftyfdr tdkelptels
      721 ltgatgyest ygngsiidtk gwevaltatp frnenfswdm nfnisgynkk vvkindlvty
      781 devetgrtas lahtagydwg niygydvvrn ddgvpvinsn glrvytnnyv kvanvqpdfn
      841 ggfintfryk nfdlgfsvdf qgggnffsvt rsllaysglg dftvgdnelg npkrdpvlds
      901 sgnevntvla qnvgtnsggv lvegvseetg episyytsay syyksmnrkv gewiydasyv
      961 klrqlkigyh iprsilgnlp vddvsislya nnlwliyssi dgidpseiea ysnsssndpd
     1021 dirwteaaqd pnqrtfglnl kfsf
//
LOCUS       WP_119638930            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119638930
VERSION     WP_119638930.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116489
     Region          23..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksiltfll aftasiigys qvtfsgtvvd enniplpgas vvvkggttgv atdfdgnfqi
       61 qlpsanetll vsyigyvake fatsgqtsat imlepdsqql devvvtalgi krekkslgya
      121 sqeldseevt sarepnllng isgkvaglqi tnspsglggs arvsirgdas lningnsplf
      181 ivdgtpisne ivgssgsgtq dvdygngaae inpqdiesin vlkgpaaaal ygaraangai
      241 iittkkgkse sgklgitint gvtvenilll pdwqneygqg nnqqfafvdg sgsgiadgvd
      301 eswgprldtg llipqfdspr edgtrggdyl vsdspiiptp wvsqpnntkd ffetgftktn
      361 siaisksgdm gnirfsyqnl dqegvvpntd lkrnsfnlnt alnltdkvtl naninyiktd
      421 sgnrpslsyg tesimylfiw ygrqintnnl rdywmrgreg lqqfnynyny hdnpffnvye
      481 ntnsqdkdrv ygnvsanyki ndhwnvmvrt grdfyrdlra kkrafstqrf plgyyrednv
      541 ffeesntdfl isydntfngk wninvsaggn qlrqkqdytq tvapqlinpg vysfnntrkp
      601 levstsdrek rinslygfar faydekvyld ltgrndwsst lptdnnsyfy psatlsaias
      661 difelpefvs fakiraayae vgndtdpykl esfytnespf gdypaltess lipnaelkpe
      721 itssyefgld lrffqsrvni datyydgrtk nqiipistdi asgytsklin agevrnygfe
      781 aiasfipiks dnftwrstfn fstnksevtd lggvnytlte rngayiqare ggsisaiygr
      841 gfqrvedkns pyygqkifnd qgipmrtddl vyqgdyapdy tlgmmnsfky kafdlsflld
      901 trqggivvsr tktigstsgq lketlegret givgegvvet spgvytpnav nvdartwnnr
      961 yyerdnveaa kydasytklr evtlgytlpk rfvdklpitg arlsvtgrnl llwtdnphfd
     1021 petvsvaggt lqpgienmsy pstktytinl ridf
//
LOCUS       WP_119639403            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119639403
VERSION     WP_119639403.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117035
     Region          25..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngllt lllafvvhis faqdktitgt vtdadglplp gvnivvegts ngtqtdfdgn
       61 ysisasqgqt llftyigqkp atrvvgagsv vnvqmvedtq aleevvvtaq gikrekkalg
      121 yavssvgadq leqktegdvg rilsgkasgv nitqqsglsg satnivirgy qsfsqnnqpl
      181 fivdgvpfss dtnaqgdfed gnngssrfld ldpnsiaevn vlkglsaatl ygeagkngvi
      241 littkngaag gkpkkseitv tsslffnqia smpeytmkyg ngfdqafgwf fsnwgpsfek
      301 egragwgnaa nfpgtydlqs dgtilhpyst agsatgipaa fpeyqgrrya wkpydsvgef
      361 fktgtvanls inaggssddg kvsynatfgh ledqgftrgn slnrntigig gramlsnkft
      421 vsgtmnysrt dfksppvalg dgnqvvgngs svfsnifftp rsvdlmglpy enpitggsvy
      481 yrqnnsiqhp lwtvahaktr qltnrafgnm slqyditenl nilyrfgydi ynernteaqd
      541 kggvgvstqy isgiygtwdn nntiwdhsli ltgnydltek ldmtfnvggt trstnydrqg
      601 vfssgqnvfg vlrhfnfdlq neiqytsykn ivglygqvdf gynnflyltl ngrndwvsnq
      661 svdnrslfyk gasfsfvpts aidglqsqgg vnflklrggy gesagfaegf ptsvnlsint
      721 qdfinddggy vvtnsvsntv anpnikpeky seievgvegr ffnfvnldls ayqritkdli
      781 inrpldpstg gtliqtnvge ikgkgleidl gfdlirgdnl nwsvntnfnt gysevtdlga
      841 dtdlivysgy snlgnaaieg erlgvivgsr vardengnfl tdssgnyise evdendrlpv
      901 igdpnpdfil nvnntfsykg fnfnflfnyv hggdiysqtv atllgrglia dtddretsfv
      961 lpgyntsgep nnvqinnsay yfsnvlfgpa emniydattl rlqevslgys vpkkfldktp
     1021 fgslsftvsg fnlwyeafnt pksanfdpnv aglgvgngrg fdwlngpssk rygvsvkatf
//
LOCUS       WP_119639615            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119639615
VERSION     WP_119639615.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112894
     Region          23..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlktrflcls mvlflmgmvh gqrqvtgtvg dvngplpgat vllkgtavgv ttdfdgnfai
       61 tlqeghdtlv fsyigyqake iivgqqsvlq vileestqsl qevvvtaqgi kkskkalgya
      121 ianvqseeve krpeadlart lqgkvagvsi tpadgqtgss stirirgtvs ltgsnapliv
      181 vnnipfngll rdidpndies isilkgfnas vlygsegrng viliqtksgs aktgdasttv
      241 tysstvytnt vsqlpefqnt yangtegief nqtiisnfgp afstlgevph pyatmadifp
      301 eyadktikia akpnnvrnif rlgigtthsl tlattreklg fnlsagytde qgiianndlk
      361 rfnlsvggkv qlmkklnlsa nlgystrkvn lvndedifsv vyhlprwidl telpyqnplt
      421 ggavyyrndt nplwilhnsg nyddkvrvfg nftadyqlat plnviyrvgf dsetysgfdy
      481 snkggydgdy lygylnigds kevvvnqtlm fnfnqdvikn lnleaqlgin sqltryagns
      541 snsdgqivyg flrptnyttt eadygtsqen lagafgqlqf ayknyfyatf sgrndwgstv
      601 evanrtlfyp gasfsfipts afnfggetvn ylkfryayat ssgypppyrt rstlvidplr
      661 faaqdgvypv tnrystryan lnlkpelhke vevgmeaklf hnrvtleasa ymrvskdqiv
      721 esrlapssgy ddqyinlgri dnegvevdlg vdifrghnfr wnlrniftad eslvvqttpt
      781 gadifitedr yavegqpfgv ikgdyalrde dgnllisgng sstrvgevit sddvgldtkv
      841 igdpnpdwkl ttintfgykd ftlsaqmeyt hggeiysssv vnmlqrgsak etenregtfi
      901 ipgyladddt geplldangd qipntiqlna srvgysnyyn andlgmwdts ifrlrevslg
      961 ytlkpmkgqk lpfkkmditl sgrnlwyrap nfpkyvnydp esdgwegdst vpstkriafg
     1021 vsvtf
//
LOCUS       WP_119639718            1038 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119639718
VERSION     WP_119639718.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1038
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113320
     Region          23..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfrnmiicvg lllcafqsya qqktvsgqvt dgsgqplpgv svlvvgtttg tqtdfdgnyt
       61 igvaqggvlr fsyigqktve rtvgtsntid vqmeedaqal devivtaygt stkeaftgsa
      121 sivgaedlai rnvtspvaal egkatgvqfi ssrgpgsspg ivirgvgtln gdtnplfivd
      181 gvqyegslnt inqediasft ilkdaastsl ygsraangvv iittksgrke gvqvnasmqy
      241 glvstaipfy pevtpgqyye tmwealknss agggdpafas aninnalgyn pfdvpndqiv
      301 gtdgrlnsna nviyqsldwy dvmsrtgvrq nynvnvsggg ddhkvffsas yldeesfvik
      361 skfdrittrl naefdvndnl tlggsaniai teatapssag tnsivnpfgf aknigsiypv
      421 yvndlqgniv tdisgnpvfd ngegfpdyni gsrpvnqgrh alqelllnde rnrnntygfr
      481 ffaeldifdg lsarvnygrd ineglnkeye natigdaqpt gryretrsrr qvenfnqilt
      541 yvksfgnhnf ditaghesfd rtfssnngma tvqaangiye fdnfsnivnl ggsstrksie
      601 gyfsrlnynf dnkyyisgsv rrdgssvfnk dtrwgtfysi gaswridqek flenssvinr
      661 lklrasygev gnddlgdyfi sqarfsitan aaapaiiytd ignsdlqwet ienfdlalef
      721 slfdnflegs veyykknssd llyllpiaps nglnevptnv gdmynsgwel altthlinkn
      781 dfkwdlalqa stfkneitsl pdpfiegqqr weegrslfdf yilrtagvdp dtgdqlflqy
      841 eldeegnsvp vldangeiat tndwqatera ytgdssipdl lgsisnsisy kgfsldvlvn
      901 yglggkfldl gyaammhsgt fgrslhpdil kawsqpgdit dvprmeagnp nivraaserf
      961 ltdasfwaik ninlgytfdr kiaqqlgldq lrvsvtgenl ylrsnrkgln pqfnlsgtps
     1021 gndfnpakii svglnvtf
//
LOCUS       WP_119639945            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119639945
VERSION     WP_119639945.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112328
     Region          23..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miqklkyvfv failfsvqaa maqtvtgtvs dgtgtplpgv nivekgtsng vtsdfdgnys
       61 itvsdsnail vfsylgfkpf easisgrsti svsleedtql ldevvvtalg isrekkslgy
      121 avteveseqi ntvkdynvan slvgkvaglv vnqsggvgsg srivlrgnns itgnnqaliv
      181 vdgipidmsg tesggsvyss svtgggitdl npediesvsv lkgpnaaaly gsraasgvll
      241 ittkkgtkgk glgisfnsnv tlenpmflpe yqnqygqgsn gtpyadlagm gtaswgsrmd
      301 gsqqlyytgn tkaysaqpnn vedyfetgek linsisldkg gddysmrfsy tnnyttsiip
      361 nsklqshnfn lrtlvdisdk lsfdgkatyf tqdltnrvnl gsegvlgyvy ymprsvdvnd
      421 lktyqidtps lydpanglsd ydvisysgsg ksignpywiq yedrnnqrrd rfigfgklny
      481 eftdwlsafi rmggdvtnvr tevvnpvghh fnrygylsft ddkftelnsd flitanknit
      541 eklnitanvg gnlskrtves mnvtgsqfki ptrallantn iqssthtpmq ikkvnslygs
      601 vslgydnfmy ldltarndws stladnnrsy fypsvsyail vdrfidpdkd vldmfklrts
      661 waevgndtgv yqlyqtfdvp qqgylglttl sapdirynen lkpesvksle fgaeaklfsn
      721 rlyfdfslyn ittndmiydl pvpaatgyny yksnigevqn kgvefliggv pirtkdfswd
      781 vsfnfsknkn tvnsliegld gtvlnttnsg nvaitanvgg gigdiygtvw akddagnrlv
      841 naegipyass erellgnsqp dwiggltntv syknlslrfl idgrvggeiy satsasldgs
      901 gvsertlqyr dggvvvdain sdtgvantes iraqeywgam ssiaenyvye qtnvrlrefa
      961 ftynfnrdlv rkiglnsasl gvigrnmfff ykkakdidpd atlgtgltgq gisinnvptv
     1021 rslglnlnlk l
//
LOCUS       WP_119639958            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119639958
VERSION     WP_119639958.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118793
     Region          24..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkirlkhafl llavlsiqfa isqktvsgtv tdengmplvg vsiiekgttn gistdfdgky
       61 sitvkdgsse lmfsyigftp vtklvgtast lditmvesae aldevvitsl gfkerkddlg
      121 yasstvggnk iseagetnvl nslsgkssgv risrnssdpg agsyiqirgl ssitrnsqpl
      181 iivdgvpisn dvrgnsdsgg vnqesrlndi npndiesiti lkgasaaalw gtqalggvin
      241 ittksgkfns klsvslksty sydeinrkyp lqdkfgqgdn gvydqrards wgdkladrsg
      301 gldeldtsge fyidqagnvy ypiltknsre tfhdsnfdki fsnghffenn lslsggnqks
      361 smffslgdln qqgiirnnsd yrrttvrfna rqnftdaisl kisssysrtk snriekgans
      421 sglylgllrn pvdfditgyr gdyfanndat pvsnrhrsyr eplgadgtat ynnplwtine
      481 qenlakvdrf itnveltatp sswltliarv gldhysekrn efftpgsasg afstgyisqe
      541 latnsifnmd yiaktafnft ddlngdfllg fnfndksrav ngytgtnfiq fldvdsgird
      601 vdnilpenii ttstqghert vgvyssasfs lydmlflnat vraetastfg dennkafifp
      661 stsiawqfsq lepfkdnntf sfgklrvsyg evgvqparyn tsnvyvsptf gdayggglnl
      721 glfgngafvp sssrgntnlk perkkeielg adlrffrdrl slsgtyfsnv tedvllefpq
      781 anstgytsvy tngaeienkg yeldlgyrii qtkdftwsld anftqvrnkv tdlagiesln
      841 lgglsavssr avegqplgvl wgsrtlrned gsivydeygf peqdqlegvi gdpnpdwqgs
      901 isstfsykkl rlsvlfetyq gadiyagtks vmrdlgtwsd taneitatrn yftwdgniin
      961 igdtfrgnva dfgagpvalt eawyngdggf fsngndelyi edgswtrlre lslsylldnp
     1021 wlknsiglqs aefsltgrnl flwtkfegnd pdtnlsgisa argieyfnnp stksylfslt
     1081 lnf
//
LOCUS       WP_119640042            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119640042
VERSION     WP_119640042.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116682
     Region          25..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkklfgal laiclsmafa yaqektvtgt vtdqdgvplp gvniivkgtt ngtqsdfdgn
       61 yligvttgdv lvfsylgqkt mernvgtenv invqmqedas qleevvvtaq givkekrslg
      121 yavttvesek vearpeadia rvlngkvagv nitsnnglsg sgtniiirgy ssatqsnqpl
      181 fivdgipfds gtntqtnfld gntessrfld ldpnniasvs vlkglsatvl ygnrgrngvi
      241 littkgaatg daptktevnv tqsvfmsnav lpkfqqnygg gfhqgfgyff snwgprfdrt
      301 dddgiasagq yigtgsngea ilrhpfnyma dptliagfed llddeypyvp yngveeffrt
      361 gyvystsvnv rggsekvsfn anygrtedig vtrgnrllrn nfslggnarl snnftvsgvf
      421 nfartgyksp pnavstgsga afngsaifgd vlytpisvdl tnipyqaadg rsvyyrsgnd
      481 iqnpywtvan sktsqetdrf tgnmsmsyal ndwmnltyrv gldtytelns ygqnrggvdg
      541 ptlgilrtts vrnsiwnhdl iltgeknlsd dlnlaatfga nsrrdtyaqd giesqgqlvf
      601 gvlehynftt pssvnsfsga nlnqnfeenl vgiyldatls ykdmlylnvv grndwsstle
      661 rennslfypg aslsfiptta fpsiqgnvln yakvrlgygs sagfptpfnt rdvltlgart
      721 fvdangnvvs gnsvsdvlgn rdlspekvqe leigldtklf nrlnlnvslf kksttdlitn
      781 rtldsstgfr stfvnigeve tkgvevdydl nifresesgf gfnlagnfta netivtdlae
      841 gtnnilltfa vsgeaanyav egrpfgvflg stilrddngn kvvgnngqyl vdnniteigd
      901 pnpdwttgli ptftykgfsl sanlqyrhgg diysvttagl igrgvvdpdk pidresnyil
      961 pgvfangspn nvaisstefg fntffaggin evniydgtti rlqeaslgys lpkkllektp
     1021 fgsmsftlsg snlwykavnf pddvrydtns sstgvgngqg idfftgpstr rygltvrasf
//
LOCUS       WP_119640287            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119640287
VERSION     WP_119640287.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110047
     Region          24..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllksfl llgaflcfgm ikaqtvsgtv sdangplpga svlvkgttng tqtdfdgnyt
       61 lngidgtatl vfsyigfktv eiavngqsti nvtleedaqa ldevviigyg qttvkdatga
      121 vavvtsedfn qgviaspeql iqgktagvqi tqssgepgag invrirgtss vrsnnnplfv
      181 vdgmplsges tsadgadvgt gsssaknpln flnpndiesi silkdasata iygsrgangv
      241 viittksgkt gkgqfeftsn lsystpakrf nllnrneflt alpnyggdpn aldygydtdw
      301 qelilrstas qnqnlsyskn ygsgnvrasf gygkqfgvve gyaqerltgr inasqrfled
      361 klkldatltv srinddggai snnsgstgdl igaayfanpt wparttfttg gseinplqll
      421 nyyddvthtd rflgnvsaey sitpelkgkv avgydkstse kyqvqsglst gigdapgqgq
      481 gafgqvdvtg klldvtltyn kefensklta lvgysfqsyq ragknitalg fgsndlnqmi
      541 sdlgtatsti esqlsgsyqq fgynssgtfv nrlfptvsqn esvtspggvp isavagnyfd
      601 ytdelqsffg raeytiadky iltgtlrvdg ssrfgpnnqy gyfpsgafaw klneedfigd
      661 afstlklrlg ygitgnqegl gygnftvrqr fagisidqnq ninapgleil sftnddlkwe
      721 etnqanigid fgfandrftg svdvyhkvtn dlllqqeaaq pspqafyfgn ldakvinkgv
      781 evsmnydiiq tedatwnlgv ngayndnmvk dfdgliqtge ingngltgay aqllaggqpl
      841 fsyylrefgg fdengislyp ngdvqefvgk salpkvtlgi ntsvsyknwd fnafltgqyg
      901 fyvynntqna yftagiigvg knitkdvltn gesnanaadv strflekgdf lrlqnaslsy
      961 nvplsgqgal kslrlsmigq nlfiitdysg ldpevnvpks lnnipslgid ytafprartv
     1021 tlgisatf
//
LOCUS       WP_119640142            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119640142
VERSION     WP_119640142.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113321
     Region          25..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkkywmvl glflfvfgsv laqeknvsgt vtdqdglplp gvsilvvgts vgtqtdfdgn
       61 ysimastgst lrfsyigqkt verkvgipsv invsmeedaq aleevvvtal gikrkprels
      121 ysvasvdnsa ltktravntv talagkvsgm qintisngvn pstrivlrgn rsllgnnqal
      181 ividgfpadr naldrlnsdd ikeisilkgg nasalygsda angvviittk sgtgkasitf
      241 tstaqldnis flpelqdefg vggfpdgtir plenvawgpr fdgslvdase qyedgrvwkv
      301 pyspipgnhk sffqtgslir ngfefsggne nsnflfsidh sniegtipqd kfnrtnarak
      361 gmydfgnlqv ssnisfyrsh sntvgvgghq arplywylln splhipinqm knwrtgeftr
      421 nevsyyafye npwfiidtqr nksnnsemif isdvnykftd wlsalarvgy tkytndlkey
      481 hgglsysfel pvtysridef spstrdyiyn ssrfnsdfii tankdisdll nvkanlghni
      541 rmtdykvidi tgnnliipgf ynvstrtgel qgsetsqnyr kvgvygditl sigdylflng
      601 qgrndwsssl skenrsffyp gggvsfvptd afkglkgtlq ylkasfsisk tgndpgpysn
      661 sttfsapagf pfestagltl sgtdrdpnlk peftksmeag iefgifkddr lsgsfsvyqt
      721 nttdqivpid vsttsgasrl ytnlgelqnq gvevdlkgti lksedfswnl gvnyslmkse
      781 vvsltegvde vvvggpysdn iaygavivaq kgqpyplikt tdyerddlgr vivdedgdpt
      841 pssnlvvqgk ttpdyivgln ntinykgftl yavadyrtgh vfynnlvdal eftgltkhsv
      901 tsgrqpfvfp nsvysdgndg yientnrlts gggnafwsty nniksnyvtd atvlklrevs
      961 lsyafddkla nklgiqdlnv gvygrnlymw rpadnvytdp efnynsgnav gfgtqnqmap
     1021 vrqfgmtlta kf
//
LOCUS       WP_119642135            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119642135
VERSION     WP_119642135.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119139
     Region          49..114
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          130..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnsltikqfi kltfrtfcfm iilallnpvl aanvrgqkle nyrvdvsvnd atvvevlkqi
       61 eeqtdfkfvy drkverlhkt ydiaynkvsl rsilelmakd adltfrrinn tisidvkpka
      121 pkrvveiafi tvtgtvtden gvplagasvq ekgtgngsit dfdgnytidv esnavlqfsy
      181 lgytpkevav dgrttidvql lqdatqledv vvvgygtqrk tdvtgsiasv esedfnkgiv
      241 mnpgqllqgk vagvnisnvs gepgaaqdvi irgvgslrsg ttplyvidgf aldntstgvp
      301 tnplnfinpq diesidvlkd asaaaiygar aangvivitt kkgksgrtqm dlsvstgfss
      361 lankvdvfsa nefrqqvvaa ggnlddggan tdwqdalsrt gfsknvnlsm gggadkftyh
      421 aslgvndqeg ilrandlkry sgrlnltqka lndrfkvefn mtasrtenlr adarsivgdm
      481 lqlnptlply tdgqptlldn alnpltreki fsdeavnhri lanvapsiei idgltyklnl
      541 gvdysttdrd vqyipyslle gyangsltst yttnkntlve ntltynfekd khnftvlagh
      601 tyqktfvhqk sfelegfadn giepkyqdqi sgestqtymy tyatenelqs ffgrvnyafd
      661 nkylltatmr adgsskfggn nkygyfpsva lgwnimnedf mstnatinnl klraswgktg
      721 nqeipskitk lsytdskdgn dsypingdes sledypygti ftrlanpdiq wevsqqtdig
      781 ldfglfnnrl sgtldyfqkv sknillevtp adpiqptdkf wtnipdmeik nngiefaldy
      841 hsdyskdfsy niggnlaytk nevanspykv lttgaaqgag qtdatingni ngepigsfym
      901 qeflgigddg lsilsedrkv vgsalpdlvy afylnfkykd fdlglnfngv sgnkvynhta
      961 mslfkkglla snfnttsias eypneditns navstrylek gdflrlnnat lgyslrpali
     1021 gldglvntir lsvtgqnlfv itdytgfdpe insnltidgi qtfgidyfny pkartvvfgl
     1081 nvsf
//
LOCUS       WP_119646103            1025 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pelagia].
ACCESSION   WP_119646103
VERSION     WP_119646103.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pelagia
  ORGANISM  Flagellimonas pelagia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Flagellimonas pelagia"
                     /db_xref="taxon:2306998"
     Protein         1..1025
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112990
     Region          23..1024
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlktrflcss mlflfigmvy gqrqitgtvg dvngplpgat vllkgtavgv ttdfdgnfai
       61 tlqeghdtlv fsyigyqake iivgqqsvlq vileestqsl qevvvtaqgi kkskkalgya
      121 ianvqseeve krpeadlart lqgkvagvsi tpadgqtgss stirirgtvs ltgsnapliv
      181 vnnipfngll rdidpndies isilkgfnas vlygsegrng viliqtksgs aktgdastsv
      241 tysstvytnt vsqlpefqnt yangtegief nqtiisnfgp afstlgevph pyatmadifp
      301 eyadktikia akpnnvrnif rlgigtthsl tmattreklg fnlstgytde qgiianndlk
      361 rfnlsvggkv qlmeklnlsa nlgystrkvn lvndedifsv vyhlprwidl telpyqnplt
      421 ggsvyyrndt nplwilhnsg nyddkvrvfg nftadyqlat plnvtyrvgf dsetysgfdy
      481 snkggydgdy lygylnigds kevvvnqtlm fnfnqdvikn lnleaqlgin sqltryagns
      541 snsdgqivyg flrptnyttt eadygtsqen lagafgqlqf ayknyfyatf sgrndwgstv
      601 evanrtlfyp gasfsfipts afnfggetvn ylkfryayat ssgypppyrt rstlvidplr
      661 faaedgvypv tnrystryan lnlkpelhke vevgmeaklf hnrvtleasa ymrvskdqiv
      721 esrlapssgy ddqyinlgri dnegvevdlg vdifrghnfr wnlrniftad eslvvqttpt
      781 gadifitedr yavegqpfgv ikgdyalrde ngnllisgng sstrvgevit sddvgldtkv
      841 igdpnpdwkl ttintfgykd ftlsaqmeyt hggeiysssv vnmlqrgsak etenregtfi
      901 ipgyladddt geilldangd qipntiqlna srvgysnyyn andlgmwdts ifrlrevslg
      961 ytlkpkkgqk lpfkkmditl sgrnlwyrap nfpkyvnydp esdgwegdst vpstkriafg
     1021 vsvtf
//
LOCUS       WP_119641152            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            aequoris].
ACCESSION   WP_119641152
VERSION     WP_119641152.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas aequoris
  ORGANISM  Flagellimonas aequoris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Flagellimonas aequoris"
                     /db_xref="taxon:2306997"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113887
     Region          20..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrniyltfva vfsciaafgq titgtvsdts gtplpgvtiv vsgtnngttt dfdgnytina
       61 ssgqvlrfsy lgmkpkditv gsettinval eedstqldev vvtafgveqk qkslgysvtk
      121 vntedlnlag qsnpieslqg rvagvqinrs sgtsgggvdi lirgvtsinp nrsnqpliiv
      181 dglalnndtf agevrpssgs nspssseqfa fsnramdlnp ediesfnvlk gaaatalygv
      241 rasngaivit tkkgkqgkak inltasttfr nvtttpplqt tyregfngap rtlydpnset
      301 gfdrvqnats fyswgpeyal dsydlgegni vdlsndrfys pydifrtgfn sqlnlslsga
      361 ndrlsyyfsl gnnneqgilp ntdykktnfr lkagykvtdn fsvdgsvaft nsggrrangg
      421 dksvmsalsy ysgtfpindy mnpdgserdy sfgiidnpry lmetsnledd vnrwignttl
      481 twspkdwvtv tyaaqidnys dvrnryvgpd ldggsqvggf ileqninftg lesnflvafn
      541 kswsedfttd ltlghqlsdt krnylearge glnipgvnei gnttnffink sivqnrtvgv
      601 fgelkfgykd klflsltgrn dwistlpken rsffypsasl aydvsdlfgd ndiftfgklr
      661 aswaevgkgp gfgdvgqyfv vdgdfpfggv ggyrrstllg dtnikpernq stefgadlrf
      721 fdnrirvdya yyntrvkdqi ftvgtayssg lsgitrnagd ykvfghelll sadvirnqdl
      781 rwelilnwst segevleipd dieaiifads gfagvtsevr agdkmgnlyg ykwvyengqr
      841 yigpdgypvi ntdervvvgn afpdfissig snlkykgigl nfllewkkgg dlydaglrns
      901 irngnplstl qrdvnvvldg vmddgnggfv pnttealidq nyyrnsnvyn rasevlvqda
      961 swvkirnisl sydfpaklik nfnlekvsvs asannlllwt pfdgydpegn qysagsnvyg
     1021 ftglniplse syslglniaf
//
LOCUS       WP_119645967            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pelagia].
ACCESSION   WP_119645967
VERSION     WP_119645967.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pelagia
  ORGANISM  Flagellimonas pelagia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Flagellimonas pelagia"
                     /db_xref="taxon:2306998"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115840
     Region          25..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngllt lllafvvhis faqdktitgt vtdadglplp gvnivvegtt tgtqtdfdgn
       61 yaisasegqt llftyigqkp strvvgaatv invqmvedtq aleevvvtaq gikrekkalg
      121 yavssvgeed leqradgdva rvlsgkasgv nitaaggmag sgtnvvirgl ssfsgsnqal
      181 fvvdgvpfss dtnaagnfld gntgssrfld ldpnnianve vlkglaaatl ygtqgkngvi
      241 littkagags ggakkteitv nqsyfvnama slpdyqdeyg ggfdqsfgwf ysnwgpkfak
      301 dgvagwgnqa aidengtlah pysttavakt reafpelqna ryawkpydsv edffrpggvs
      361 stsininggs adgntsfnvn tgylsdesfv pgnqldrfni svggrskltn kftisaamnf
      421 srtdytsppi aasrgngslg lslfghvfft prnvdlmglp yenpidhssv yyrngndiin
      481 prwvlnnisn nqltnrffwn asatyaisdn ldvtyrggmd fynerntqys nkggvgfdsa
      541 iygylktydn nntiwdhyla lngnydlsek lgmtftagat trsttfdqqg vsstgqlvyg
      601 vvrhfnysnq tpiqyserrn iagllgqvtl dydnmlfltg strtdwvsnl itennsrtyp
      661 sgsisflpta afpelqsqgg lnflklragv gssatfptgy ptvgiveqtt qvygeggett
      721 tnqvasfkan pdlkpellte yelgfeskff snrvsldfty fnrvtkdliv replspstgf
      781 tftqsnvgki egdgfeidas vdwfrsdspg gfnwntranf stykpvvteq eqdiiiyags
      841 stlfvggnaa ikgkplgsiv gtavgrdadg nflvndagdy vvveqdldgn vpiignpnpd
      901 fitnfinsis yknwnfgfqv nwtkggdmms ntiatllgrg livetlnren tyilpgvsqs
      961 tgevnmkqtn nssfyfdnil fgpaelkiyd asvvrlqevs lgytfpskfl dktpfgslsi
     1021 taqgfnlwyd ayntpkgahf dpnvqgagig naqgfdfing psakkygisv kvtf
//
LOCUS       WP_119646173            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pelagia].
ACCESSION   WP_119646173
VERSION     WP_119646173.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pelagia
  ORGANISM  Flagellimonas pelagia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Flagellimonas pelagia"
                     /db_xref="taxon:2306998"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120264
     Region          23..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksiltfll afvvsmigys qstfsgkvvd ennvplpgas vvvkgsttgv atdfdgnfei
       61 qlpsaneill vsyigyvake fatsgqtsat ivlqpdsqql devvvtalni trdekslgya
      121 vqkvggdevs qststntvst lagrtagvqv vtngtgpgqs ssvvirgyss mqgdnqplfi
      181 vdgipinntt dtrtntlgga snmnldygng aaeinpddva sisvlkgana talygsraan
      241 gaviittksg kgkksgisfs skttfesvlk apeyqgvygq gknfdfafvd gygngtydgv
      301 deswgplldg tlrpqhdspt tnglrggdvh gldyvlgssg vdlqrrgdii atpfvyggnp
      361 akefmetgrt lintvslygs nengnyrvsy tnldnkgivp ntdlrrntis lsgdyqisdr
      421 lsvsskinyi rsdsdnrhvn gygtesvmyl fiwwgqqinv hglrdywqdg legfqqfnyn
      481 ynyhdnpyft myentnglak driignlsat ykisddfkfm vrggrdffse yrfikrayst
      541 qrfpngqyre dkinfqetnl dflltydkni ndkfhvnanf ggnrmvqknh fnslmankll
      601 ipgiysfsnv dgslvqrtsr pekqinslya faqlgwdnsv yldltarndw sstlpeqnns
      661 yfypsaslsv vltdlfdins ndvlnfaklr ggwaqvgsdt dayrlseyya lgtpvgdnpt
      721 aspsstlpnf dlkpeiqtsy efgtdlrmfn nkltldatyy ntvsknqild idlpvtsgks
      781 artinagkir nqgveimlgv tpfenknfsw nssfnfglnr nkileladgv drysyggngi
      841 tlvaekggsl gdmwgtglvk vedkdspyyg evifnnglvq qdntlrkvgn fnpdftlgwn
      901 ntikyknisl nflldwrqgg ellsrtrlia atsgnvvetl wgrspeyggp hpgiadsglt
      961 ytdtngttwn dgiigdgvml qggeyvpnnv ivaanayhnn ryrrdndteg iydatfiklr
     1021 earltydfpk gflktddiks lsfsligtnl wlwakdfnhg dpellsfggg nfvpgvenat
     1081 vpttrsvgfs invef
//
LOCUS       WP_119647937            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pelagia].
ACCESSION   WP_119647937
VERSION     WP_119647937.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pelagia
  ORGANISM  Flagellimonas pelagia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Flagellimonas pelagia"
                     /db_xref="taxon:2306998"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116846
     Region          25..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkklfgal lamclsmafa yaqektvtgt vtdqdgvplp gvniivkgtt ngtqsdfdgn
       61 yligvtasdv lvfsylgqkt iernvgaesv invqmqedas qleevvvtaq givrekrslg
      121 yavttvesek vearpeadia rvlngkvagv nitsnnglsg sgtniiirgy ssatqsnqpl
      181 fivdgipfds gtntqtnfld gntessrfld ldpnniasvs vlkglsatvl ygnrgrngvi
      241 littkgaatg dapsktevnv tqsvfmsnav lpkyqqnygg gfhqgfgyff snwgprfdrt
      301 dddgiasagq yigtgpngea ilrhpfnyma dptliagfed llddeypykp yngveeffrt
      361 gyvystsvnv rggsekvsfn anygrtedig vtrgnrllrn nfslggnarl snnftvsgvf
      421 nfartgyksp pnavstgsga afngsaifgd vlytpisvdl tnipyqavdg rsvyyrsgnd
      481 iqnpywtvan sktsqetdrf tgnmsmsyal ndwmnltyrv gldtytelns ygqnrggvdg
      541 ptlgilrtts vrnsiwnhdl ilsgeknlsd dlnltatfga nsrrdtyaqd giesqgqlvf
      601 gvlehynftt psstnsfsga nlnqnfeenl vgiyldatls ykdmlylnvv grndwsstle
      661 rennslfypg aslsfiptta fpsiqgnaln yakirlgygs sagfptpfnt rdvltlgart
      721 fvdangnvvs gnsvsdvlgn rdlspekvqe leigldtklf nrlnfnvslf kksttdlitn
      781 rtldsstgfr stfvnigeve tkgvevdydl nifresesgf gfnlagnfta netivtdlae
      841 gtnnilltfa vsgeaanyav egrpfgvflg stilrddngn kvvgnngqyl vdnniteigd
      901 pnpdwttgli ptftykgfsl sanlqyrhgg diysvttagl igrgvvdpdk pidresnyil
      961 pgvfadgtpn nvaitstefg fntffagnin evniydgtti rlqeaslgys lpkkllektp
     1021 fgsmsftlsg snlwykavnf pddvrydtns sstgvgngqg idfftgpstr rygltvrasf
//
LOCUS       WP_119648184            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pelagia].
ACCESSION   WP_119648184
VERSION     WP_119648184.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pelagia
  ORGANISM  Flagellimonas pelagia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Flagellimonas pelagia"
                     /db_xref="taxon:2306998"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118846
     Region          24..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkirlkhafl llavlsiqfa isqktvsgtv tdengmplvg vsiiekettn gvstdfdgky
       61 sitvkdgsse lmfsyigftp vtklvgmast lditmvesae aldeviitsl gfkerkddlg
      121 yasstvggnk iseagetnvl nslsgkssgv risrnssdpg agsyiqirgl ssitrnsqpl
      181 iivdgvpisn dvrgnsdsgg vnqesrlndi npndiesiti lkgasaaalw gtqalggvin
      241 ittksgkfns klsvslksty sydeinrkyp lqdefgqgdn gvynqrards wgdkladrsg
      301 gldeldtsge fyidqagnvy ypiltknsre tfhdsnfdki fsnghffenn lslsggnqks
      361 smffslgdln qqgiirnnsd yrrttvrfna rqnftdaisl kisssysrtk snriekgans
      421 sglylgllrn pvdfditgyr gdyfanndat pvsnrhrsyr eplgadgtpt ynnplwtine
      481 qenlakvdrf itnveltatp sswltliarv gldhysekrn efftpgsasg tfstgyisqe
      541 latnsifnmd yiaktafnfs ddigadfllg fnfndksrav ngytgtnfiq fldvdsgird
      601 vdnilpeniv ttstqghert vgvyssasls lydmlflnat vraetastfg dennkafifp
      661 stsiawqfsq lepfkdnntf sfgklrvsyg evgvqparyn tsnvyvsptf gdayggglnl
      721 glfgngafvp sssrgntnlk perkkeielg adlrffrdrl slsgtyfsnv tedvllefpq
      781 anstgytsvy tngaeienkg yeldlgyrii qtkdftwsld anftqvrnkv tdlagiesln
      841 lgglsavssr avegqplgvl wgsrtlrned gsivydeygf peqdqlegvi gdpnpdwqgs
      901 isstfsykkl rlsvlfetyq gadiyagtks vmrdlgtwsd taneitatrn yftwdgniin
      961 igdtfrgnva dfgagpvalt eawyngdggf fsngndelyi edgswtrlre lslsylldnp
     1021 wlknsiglqs aeftltgrnl flwtkfegnd pdtnlsgisa argidyfnnp stksylfslt
     1081 lnf
//
LOCUS       WP_119647838            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pelagia].
ACCESSION   WP_119647838
VERSION     WP_119647838.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pelagia
  ORGANISM  Flagellimonas pelagia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Flagellimonas pelagia"
                     /db_xref="taxon:2306998"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109906
     Region          24..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllksfl llgaflcfgm ikaqtvsgtv sdangplpga svlvkgttng tqtdfdgnyt
       61 lngidgtatl vfsyigfktv eiavngqsti nvtleedaqa ldevviigyg qttvkdatga
      121 vavvtaddfn qgviaspeql iqgktagvqi tqssgepgag invrirgtss vrsnnnplfv
      181 vdgmplsged tsaggadvgt gtssaknpln flnpndiesi silkdasata iygsrgangv
      241 viittksgks gkgqfeftsn lsystpakrf dllnrdefls alpnyggdpn aldygydtdw
      301 qelilrstas qnqnlsyskn ygsgnvrasf gygkqfgvve gyaqerltgr inasqrfldd
      361 klkldatltv srvnddggai snnsgstgdl igaayfanpt wpartgfttg gseinplqll
      421 nyyddvthtd rflgnvsaey sitpelkgkv avgydkstse kyqvqsglst gignapgqgq
      481 galsakdvtg kllditftyd kefenshlta lvgysfqsyq regknitalg fgsndlnqmi
      541 sdlgtaasti esqltgsyqq fgynssgtfv nrlfptvsqn esvtspggvp isavagdyyd
      601 ntdelqsffg raeytiadky iltgtlrvdg ssrfgpnnqy gyfpsgafaw klneedfigd
      661 afstlklrlg ygitgnqegl gygnftlrqr fasigidqnq ninppglsiq sftnddlkwe
      721 etsqanigid fgfandrftg svdvyhkvtn dlllqqeaaq pspqdfyfgn ldakvinkgv
      781 evsmnydiiq tedatwnlgv ngayndnmve dfdgliqtge ingngltgay aqllagghpl
      841 fsyylrefgg fdangislyp ngdvqefvgk salpkvtlgi ntsvsyknwd fnaflsgqyg
      901 fyvynntqna yftagiigvg knitkdvltn gesnanaadv strflekgdf lrlqnaslsy
      961 nvplsgqgal kslrlsmigq nlfiitdysg ldpevnvpks lnnipslgid ytafprartv
     1021 tlgisatf
//
LOCUS       WP_119647897            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pelagia].
ACCESSION   WP_119647897
VERSION     WP_119647897.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pelagia
  ORGANISM  Flagellimonas pelagia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Flagellimonas pelagia"
                     /db_xref="taxon:2306998"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113456
     Region          25..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtknywmvl alflfvfeta laqeknvsgt vtdqdglplp gvsilvvgts vgtqtdfdgn
       61 ysimasvgnt lrfsyigqkt verkvgasav invsmeedaq aleevvvtal gikrkprels
      121 ysvasvdnsa ltktravntv talagkvsgm qintisngvn pstrivlrgn rsllgnnqal
      181 ividgfpadr naldrlnsdd ikeisilkgg nasalygsda angvviittk sgtgkasitf
      241 tstaqldnis flpelqdefg vggfpdgtir plenvawgpr ydgslvdase qyedgrvwkv
      301 pyspipgnhk sffqtgslir ngfefsggne ksnflfsidh sniegtvpqd kfnrtnarak
      361 gmydfgnlqv ssnisfyrsh sntvgvgghq arplywylln tplhipinqm knwrtgeftr
      421 nevsyyafye npwfiidtqr nkynntemif isdanykftd wlsalvrvgy tkytydlkey
      481 hgglsysfel pvtysridef spstrdyiyn ssrfnsdfiv tankdlsdll nvkanlghni
      541 rmtdykvidi tgnnliipgf ynvstrtgel qgsetsqnyr kvgvygditl sigdflflng
      601 qgrndwsssl skenrsffyp gggisfvptd afkglkgtlq ylkasfsisk tgndpgpysn
      661 sttfsapagf pfgstagltl sgtdrdpnlk peftksmeag iefgifkddr lsgsfsvyqt
      721 nttdqivpid vsttsgasrl ytnlgelqnq gveidlkgti lksedfswnl gvnyslmkse
      781 vlsltegvde vvvggpysdn iaygavivaq kgqpyplikt tdyerddlgr vivdedgdpt
      841 pssnlvvqgk ttpdyivgln ntinykgftl yavadyrtgh vfynnlvdal eftgltkhsv
      901 tsgrqpfvfp nsvysdgndg yientnrlts gggnafwsty nniksnyvtd atvlklrevs
      961 lsyafdnkla nklgiqdlnv giygrnlymw rpadnvytdp efnynsgnav gfgtqnqtap
     1021 vrqfgmtlta kf
//
LOCUS       WP_119648391            1041 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pelagia].
ACCESSION   WP_119648391
VERSION     WP_119648391.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pelagia
  ORGANISM  Flagellimonas pelagia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Flagellimonas pelagia"
                     /db_xref="taxon:2306998"
     Protein         1..1041
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115004
     Region          25..1040
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklkgila flmllvvhlt saqektitgt vtdhtgiplp gvnilvegta tgtqtdfdgi
       61 ytisaapgqt llftyigqkp tsvivggsst idvqmeedaq aldevvvtal gikrekkslg
      121 yaqqsieges vvlakdtdis dglagkisgv qlvgspssty essnirlrgn vgvlyvvdgi
      181 kinspgdinm qdvedisvlk glaatalygt earngaviit tktakdgetk vtvdiassis
      241 slyllpkyqn eygggysqtf aqvdgqnipn fsadeswgpr ldgtlvrqwd swivgdpgyg
      301 elrpwvptph giedfyetga tsnitvgflq ggekyniktt vnhvgttlin pnsdrkqtti
      361 sfkgtynvse klkfngvfny qyrytfnnpq drgyagnfne wwqrqldmtr lrnykrngqi
      421 vswnmraydn ptplywdspy fevyenlnhe tknaiygslg leyeilpelv atvdlrrtfd
      481 lynfddrnaw gglatpryle kttqneftea ytqlsynkki gdfdlvasag aqfnqrkykl
      541 iqaqtvgglq ipnyysidts vdkpnyvrds rhqklnstfa tasvgyknfl yldgsyridw
      601 gstaasdnns vdtygvsasf ifsefindgs flsfgkirag faqapsfpdv yrlqstydiq
      661 npygsnvals vpdilnnpgl iggvreeiei gtelsflnnr lgldftyfdr tdkelptels
      721 ltgatgyest ygngsiidtk gwevaltatp frnenfswdv nfnisgynkk vvkindlvty
      781 devetgrtas lahtagddwg niygydvvrn ddgvpvinsn glrvytnnyv kvanvqpdfn
      841 ggfintfryk nfdlgfsvdf qgggnffsvt rsllaysglg dftvgdnelg npkrdpvlds
      901 sgnevntvla qnvgansggv lvegvseetg epiayytsay syyksmnrkv gewiydasyv
      961 klrqlkigyh iprsilgnlp vddvsvslya nnlwliyssi dgidpseiea ynstdpddir
     1021 wteaaqdpnq rtfglnlkfs f
//
LOCUS       WP_119649260            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flagellimonas
            pelagia].
ACCESSION   WP_119649260
VERSION     WP_119649260.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas pelagia
  ORGANISM  Flagellimonas pelagia
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Flagellimonas pelagia"
                     /db_xref="taxon:2306998"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113957
     Region          20..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrniyltfva vfsciaafgq titgtvsdis gtplpgvtiv vsgtnngttt dfdgnytina
       61 ssgqvlrfsy lgmkpkdinv gsettinvvl eedstqldev vvtafgveqk qkslgysvtk
      121 vntedlnlag qsnpieslqg rvagvqinrs sgtsgggvdi lirgvtsinp nrsnqpliiv
      181 dglalnndtf agevrpsags nspssseqfa fsnramdlnp ediesfnvlk gaaatalygv
      241 rasngaivit tkkgkqgkak inltasttfr nvtttpplqt tyregyngap rtlydpeset
      301 gfnrvqnats fyswgpeysl dsydlgegni vdlsndrfys pydifrtgfn sqlnlslsga
      361 ndrlsyyfsl gnnneqgilp ntdykktnfr lkagykvtdn fsvdgsvaft nsggrrangg
      421 dksvmsalsy ysgtfpindy mnpdgserdy sfgiidnpry lmetsnledd vnrwignttl
      481 twspkdwvtv tyaaqidnys dvrnryvgpd ldggsqvggf ileqninftg lesnflvafn
      541 kswsedfttd ltlghqlsdt krnylearge glnipgvnei gnttnffink sivqnrtvgv
      601 fgelkfgykd klflsltgrn dwistlpken rsffypsasl aydvsdlfgd ndifsfgklr
      661 aswaevgkgp gfgdvgqyfv vdgdfpfggv ggyrrstllg dtnikpernq stefgadlrf
      721 fdnrirvdya yyntrvkdqi ftvgtayssg lsgitrnagd ykvfghelll sadvirnqdl
      781 rwelilnwst segevleipd dieaiifads gfagvtsevr agdkmgnlyg ykwvyengqr
      841 yigpdgypvi ntdervvvgn afpdfissig snlkykgigl nfllewkkgg dlydaglrns
      901 irngnplstl qrdvnvvldg vmddgnggfv pnttealidq nyyrnsnvyn rasevlvqda
      961 swvkirnisl sydfpaklik nfnlekvsvs asannlllwt pfdgydpegn qysagsnvyg
     1021 ftglniplse syslglniaf
//
LOCUS       WP_119652244             947 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canis].
ACCESSION   WP_119652244
VERSION     WP_119652244.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canis
  ORGANISM  Capnocytophaga canis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 947)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 947)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 947)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..947
                     /organism="Capnocytophaga canis"
                     /db_xref="taxon:1848903"
     Protein         1..947
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104053
     Region          2..946
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miinvllkee aeqleevvvt algikrqeks lsyatqtvsg keltdvpssn vlntlagkta
       61 gmsvsgsgsg vgssvkivlr gnrsiqgnnq plyvvdgtpi ssgafsgsai gdgygggida
      121 gdgmaginpe diesinvlkg ataaalygsq aangvilitt krgnsekiav svtssvqadv
      181 pyltykfqdr ytmgvdgvsq ssmdawgapr tnqdlsndfv knffntgfms qngvsvsggn
      241 kvtknflsyq nttatgimpn ntfdkhnlsl rsttslfddf ievdgsvalt hqdtgnapaa
      301 pgqyfnpilg lylfpagtta fnsyrdvyev pdpsrnglmt mnwanqtdvy knpywlinrh
      361 nysynvekai vklntkfnft swlnlqlrgs ydktatlger kvhagmttlt gkggrydhkt
      421 qnyalmyada lltanksyek fsisatlgts isdtkettne iqihnlaian lfdlrnyigi
      481 eggsdnkrth rqlqsvfgtv slgynemlyl dvtgrndwss tlpannrsyf ypsvgtsfvf
      541 temldqneak pewldfgklr fswtqvgndm pwgltepydk lqkggviean tvkpfddlkp
      601 ersnsleagv nlrflggrft fdaavyktit enqyfkvdnt sgsgysqyyi nagevenkgf
      661 eltlgftpik tndfqwngyl nystnkntvl slpsqyldkg feissvgykf rlkegeewgr
      721 myekrlkrdn qgnilltqti engvdkgiql qqsddfeyig nvnpkfligf knefsyknfs
      781 lgllidgrfg gnvisstqni ldrfgrsqrs aeardnggip ltgtlvtttk vtgspdvvtq
      841 tafnqkidaq tyykvapage tsvysatnvr lrelslsytl pkslvervky vesvrlslig
      901 rnlgffynea pydpeitlst ssnglsnadl ftmpasrsvg fsininf
//
LOCUS       WP_119652288            1033 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canis].
ACCESSION   WP_119652288
VERSION     WP_119652288.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canis
  ORGANISM  Capnocytophaga canis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Capnocytophaga canis"
                     /db_xref="taxon:1848903"
     Protein         1..1033
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113965
     Region          25..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrkflvtfv ltmvfcfhwl yaqnrtvsgv vtdesgipls gvsvlvkgtt rgvstdfdgk
       61 yniqaqaeei lifssmgfvt qekkanvtkl nvmlkedaee leevvvtalg ikrsekalgy
      121 alqeidgtkl leardanvtn alsgkvsglq ivkgaggmvg sskivlrgqn sltgdnqpli
      181 vvdgvpidnk asgaadiwgn sgmdmgngls dinpediesl tvlkgasaaa lygsragngv
      241 ilittksgke kkglgitfst tlatedifvk palqntyaqg vdnlydpkta rnwgpriegq
      301 tvtnwnnkqv kleaydnmnn ffrtgitatq alsfqqqink tsvygsvnym dntsmvpetd
      361 mnrtsmalrt ttnlgasdrw kvdfkinyvn tqahnrpiqg lnqsnvfktl tifprtldir
      421 efnppivngq qvwydtqtlp ddnpwwtlky ntnndvrnry isfgavtyef tnwlrgevkg
      481 gldyyntkmy qrkhsgslsv pkngqyaeas kefseknlsf lliaeksdll kdlngtltfg
      541 gnlmsqhise mnaksgdlli pnifslnngk ekptvtslit qrkmnslygs aqigwknsly
      601 ldatfrndws stmsevnrsy fypslsfsgv iselielpew vtfakvrasy aevgndlepy
      661 mlynsysvak dywgvptist neilydhsvr selvksyeag ldlrlfnnrv rldaavyktn
      721 amrqllrlpm detsgykfki inagnienkg velslgvgil qnpeglnwdt tvnfsknenq
      781 iidlypgvas yelltvdeim vlaevgkeyg aiygsairrv ndansphngk miltaeglpq
      841 rdavalhylg nqqpdyllgf snsfswkgin ldflvdarvg gkmfsmtrnl ltgygmaaet
      901 avdgkrdsfv vegvianssg gydvntkqvt pqrywgalaq nnigiteanm ydatsvrlrt
      961 lslgytfgkk hlesigiqnl kcsftannlw lihtnipgid pesvsgtgtn vtalefgapp
     1021 tsrtftfnit igl
//
LOCUS       WP_119652719            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canis].
ACCESSION   WP_119652719
VERSION     WP_119652719.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canis
  ORGANISM  Capnocytophaga canis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Capnocytophaga canis"
                     /db_xref="taxon:1848903"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114912
     Region          24..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkliwtms lfffalqftf aqektitgtv kdesghpllg vtvtvkgttk gvatdfdgny
       61 sikakvgdil hfiglglrsv dksvqasttk mdvvmeeeve qleevvvtam gvsrdekslg
      121 yatqkvegdr lskagqqnai salsgnvagv qvtasssmgg stritirgvg svtgdnrpli
      181 vvdgipmnns nynssslggr dygdasadin pddiesvtvl kggpatalyg srggngvivy
      241 ttksgkrgkt svdvksgitf estyiapilq nrygggsanq fekiningre yniaeystde
      301 swgpkfenql ylpwyafdke afpndylkev pwkasendvd sffrtgvtts nsvsvtrsiq
      361 atnlrlsast sktdgivpns hlkkstlsfn fnsklsekfk vdgglnyvlt ngfnrqdqgy
      421 tdnsvsqkfy qwgqrqldmk klrdyknpkt geqrswnrts wddptplysd npywiayent
      481 sedkrhrffg nvgvtytiad nlyavgnvyg dvysfrvkeh vaigsqaqpy fkdivrnasd
      541 fnyearlhfd pkigndfsln sfvgvsrrea rynyvngetv gglikpnfyn lsnsvetpka
      601 snyeswrrtn slygmvslgf kemlfveatg rndwfstvsk pvfypsvtgs fvfssvvkpd
      661 wlsfgkvrlg waqvgndtgp yrletyptvs npflgdprys npstannpnl lpevkttqev
      721 glevklfrnr vgldvtyydt rtkdlilplt tdpstgyayk yinagsmqnq gievslnvtp
      781 vktddfswdv twnfaknnnk llelhpqmkv yqlssffsst ilnavegqpy gqlyttnykf
      841 hegtgqpivg ddglyvkgkv eslgsvipdy nmglnnslry knfdlsvlfd fqkggkyfst
      901 nhmfgmysgm lketaegdir ekgivlsgvt adgqpnavpa gaaawgashy tgvraqsvfd
      961 atylklrnis lsytvdlpkn khikelvlsa ygrnlwttgl dykgidpeqt sygsgnvqgi
     1021 etgslpstrt ygmsvqikl
//
LOCUS       WP_119652724            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canis].
ACCESSION   WP_119652724
VERSION     WP_119652724.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canis
  ORGANISM  Capnocytophaga canis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Capnocytophaga canis"
                     /db_xref="taxon:1848903"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120665
     Region          24..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrgkliwtls lfffalqfvf aqektitgmv kdesgqpllg vtvtikgttr gvatdfdgny
       61 sikakagevl hfvalgmkpi drpvsasttk idvimeeeah eleevvivay gtakkqslvg
      121 sqamvsakql etrpitnltt alsgiapgvq stlssgqpgs satirirgfg sinagndpiy
      181 vldgsiyngr isdivmqdie nisvlkdaas tslygssagn gvvlittkrg skgkkekpsf
      241 tysnnlgfst rgqedyekvg amdylplrfq qwyndykynr gatdeqaaaw anynmiqqyk
      301 leympyagvn tyyqyaggtw nyhqtqptgg nvfpavmmmd gtlnpnitgl lwgedldwer
      361 alfrtgirne htisvnhstd kmksyfslny lkedgyrias dyerlagrgn vsydvnnwlt
      421 vgtnigystm vnhsptttgs nssntfrfvr siapifpihq hnadgsyvyd ahgkkvydyr
      481 ksrifipnyn pvylsevdll ttdnnsantr tfaeisllpe lkiklnynyd vlrytskqry
      541 nnifgaqpdg lleinnykga tttfnqlldy nktfgkhnvg vllghesyky dyiessmgkk
      601 kmaflgidem snftqlesat sktdqytkeg yfgrvnygfd nkydlslsfr rdgssrfhkd
      661 nrwgnfwsvg agwhlkkeaf lanvswidhl klrasygttg ndstsgyypy qttysfvnnd
      721 vqaglrigry gyrnllwekq vsadialefd vfkhlkgtve lfskesddli falplptstg
      781 itsvnknigk vqnrgieiel tidlikrpdf kwnftangti lknkvvrlpe hirelgqang
      841 nyrymegysi ydyhipqwag vnpntghamy vidaktypny advnhahfrg vdkdqyaayt
      901 ydyniakrdf sgsaipdlqg gfgtnatwkg fefgvqfsym lggkaydsvy qglmgrdtns
      961 gtaahvdlwn awkkpgdvtd vprldestag qyvsstsnrf lisrtslmlr nlsigytlpk
     1021 eilapygitn lrvgiagenl flwskrkgmn pmanfsgtts nlgydyakvf scgvsvsf
//
LOCUS       WP_119652998            1135 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canis].
ACCESSION   WP_119652998
VERSION     WP_119652998.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canis
  ORGANISM  Capnocytophaga canis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1135)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1135)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1135)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Capnocytophaga canis"
                     /db_xref="taxon:1848903"
     Protein         1..1135
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124572
     Region          26..1132
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfltlfa fvfswcltls aqmvsvkgtv tdegkvplpg vsvliknttr gvatdfdgky
       61 eikanrgdvl vfsylgfvtq ektvgagssq tinvllveea eqlgevvvta lgvnkqarsv
      121 gyattkvata eierlnvinp vnalqgkvag vainttgasg vtssagitir gaksldknns
      181 pifvidgmii qerltsptdg tdwgsqlknl npadyesitv lkgaaataly gsrgangaiv
      241 ivskggkfgk qglgvefsqs ietaniyrsp mklqnvygag hplngyeggf lgdgslqnts
      301 nsfgpkmegq lvnqympggq qtpfvahpdn wqtlyqnpfn qtynvaingg genssfrlsy
      361 symdnngvfk rnnfnrntva frglmklndi fsmeagvnya fskaqnganq ggwdwdnnls
      421 mlstlwtprn fdmdafveny rdketqavet etpwgrlrgy lhrrdlnlnq rnenslltnl
      481 tlraniapwl tasvkgnyny ygiskmekwy gagafygptk tggysrggev ygsynflgml
      541 qsndnkinia geeitldaiv atelygnles hswhkatkgg lvvpalfafs nsaetiiptf
      601 gytpannkvf gvsgilnlgw rdqlflevtg rndwlsslty pnymiggknn ysvfypsvns
      661 swvftetfqm pdwfsfgkir aswaevgmgt gayatskgyg ifrqesqfda qrnsvlvarp
      721 nlgtawnndl kpeiqssiel gtdlrffner lnvdfayykt ntrnqilsvg asiesgastq
      781 linagniqnq gielqiegtp iktdnfrwti gtnitknkgk iidlhpnvke wqlmwqydgg
      841 peiwayeggd ygvlatsyns pygssiyrfn npdnandprn gkpviyyrga ggspnkayvy
      901 syvtnnqkgi kdrvvlgkve adfylnints iayknfdlya lidgrfggnf hsnasvyatg
      961 agalestlqg rdaehgglpr vnykgetvyd ainldavfde dvkaplasdp nqridvgglt
     1021 yrealdkgia pmmatthyay nmgwgspnel hlqentwlml reisvgyrfd devckklgan
     1081 ylrvgltarn lgvlmsklrd glnpesissn npltpmvlgg vpysrtfsfn ltarf
//
LOCUS       WP_119653125            1119 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Capnocytophaga
            canis].
ACCESSION   WP_119653125
VERSION     WP_119653125.1
KEYWORDS    RefSeq.
SOURCE      Capnocytophaga canis
  ORGANISM  Capnocytophaga canis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Capnocytophaga.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Capnocytophaga canis"
                     /db_xref="taxon:1848903"
     Protein         1..1119
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124208
     Region          26..1118
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgkflkhil imslcfflqg vfaqekevsg vvtssddgmp ipavsvivkg tnrgvatdfd
       61 gkytikaneg eilqfislgf ttvekkvtgg sntliinalm keeanqleev vimgyggtre
      121 kakltnsiat vktevlekgs fsnpaqalsg avaglrvaqt sgkpgsvptl ilrggtnlng
      181 sgsplvivdg qvrgglndln pndiesmevl kdagataiyg aranngvilv ttkrgkvgss
      241 smnlrmkhgf dymnnkyefl nardylywqr navyntsriy qladgtwkgy ananslnnag
      301 aygtgnlhfh prtgelidpn iysqavwspm lfeglsdsqk qallnqgwet midpvtgkei
      361 ifsnfdrsst afrsfaltrd ytfsmtggne kgkyyaslgy fnqeglpvnn wykrlngtln
      421 aeyqlkpwlk sissfaiaha twndnmngmg dgtyfgrmls apptqkeyvn gklvlgrdrq
      481 dgnpwiydgk firknntdkf nlgqsfkvdl fkglsftlng yvmfdegvye sfdkdylerp
      541 nsinktrsss asfgrtlrqt yngifnykvs lgshnldama gyeyydnyyr dfsargegap
      601 tddfmdlglt lnqegkrhid sghsniriks yfgrlnydyd gkyllsftlr tdgysslidn
      661 rwgtfpgvsg gwvvtkedfv sdsfkdilsf aklrasfgln gnasgigayd lqgsygtgky
      721 kgqtgfhlgs lpntglrwek sktfevgadl mflenrlstn itfydrlted kyadiglphs
      781 sgitgirtnn gafrnrgief eanfkainke kmrwdiglnm thnrnivvkl pnnglkknrq
      841 gafqvydgtt gnkiwvggyq egqtpgdlyv yealgiykne eevrqlannl ideslggygs
      901 dnkklygpaa wealsnaeka nnrnlpiqpg dviwkdvngd gkidqfdkvk vgnifpkltg
      961 ginttfsyen lsisarmdya igfkqfingi gtlpwymana qgsfnsvvev kdswtpenpn
     1021 akyprymwad qlgkrnftrd tsmfvyegsy lsfrevtlay sfdsdlcksl sltnlevslt
     1081 gqnlgywtks kayspenlgt sandyslprt viiglnltf
//
LOCUS       WP_119656261            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            rubripertinctus].
ACCESSION   WP_119656261
VERSION     WP_119656261.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter rubripertinctus
  ORGANISM  Hymenobacter rubripertinctus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Hymenobacter rubripertinctus"
                     /db_xref="taxon:2029981"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118485
     Region          24..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkdlliaip lvalsvtqvi aqtrevsgri tdratgqglp gvtvlvkgtt tgvstnsdgs
       61 ytiavpasat tlafssigfv nveraigtdn viniglasds kqlgevvvsa lgvrqardeq
      121 gvavsqvqgs avarsgetsa itglsgkssg lqvtrtggdp gagayiqirg qnsvtgsnqp
      181 liivdgvpis nstlgsdigg vvqqsrlndi npndiesiqi lkgaaasaqw gsraangviy
      241 ittkrggsds gklsitygtt ysadrvsykh dlqdtygrgs qgvaaltsnt tgnswgdkis
      301 trsgapdvvn stgsggfyta qngqvyypit kknsqetfld knfdgvfqtg hflennlsls
      361 agnkdgnifl svsdlnqkgi vrnnsdyrrt tgrvnafrnf ndivkiagnm tysrvesnri
      421 qqgsntsgly lgllrqspdf dqggyigsyt apngdvflnr qrsyrrqign spspaynnpl
      481 wtineqsnpn evdrflgnve lnvtprpwlt ftvrpgvdty tdsrrtifpi nsaenggggs
      541 ateeiitetq fnadafvrat htfnnflsgn llvgtnfnqr qarnigasyl nfildvrdqs
      601 ffanatkanv tafdleskqr tsagyatagl vigeqvflna tgrlenastf gpqtksrffy
      661 psvdvawqfs klgaladnki lsfgklraay gqvglqpgsa ssfaiyltrd vyrnadntes
      721 ygpfldpaay sgsfarnflr gnpllkperk seievgtdlr flqdrislsa tyyqneitda
      781 ilpvpvaass gytseyanaa klenkgield lnamilkked ftwsvggnwt rnrnkvtdla
      841 gaesvflngf tgvssravkg eplgtlwggr wdrddagkfv ldadgfpqqa ategvignpn
      901 pkwrsgintn ltykgvrlfa lwetsfggdi wagtegvlrn fgtstytdve ttlsaadaqr
      961 vktydgitva qkysanadgs ytfrgrlqdf gagnvaldqt wfttqgggfg avgeqfiqda
     1021 swtrlreltm gytlqseafr nltrlqnvel tltgrnlllf tkefkgvdpe tnltgasngr
     1081 gleyfnnpgt rsflvglrit y
//
LOCUS       WP_119656601            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            rubripertinctus].
ACCESSION   WP_119656601
VERSION     WP_119656601.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter rubripertinctus
  ORGANISM  Hymenobacter rubripertinctus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Hymenobacter rubripertinctus"
                     /db_xref="taxon:2029981"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113851
     Region          34..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlhhyftpgr llllgglavl plaaaraqts qpytlqgrit dergqglpgv tvllagttlg
       61 tatdaegnyq ltlnqapgpy rltlsaigfk tetraitlgt stavvtnvtl nsasqaldnv
      121 vvigstvsvn rrelgnaitv vdgaqlqktg tgqllnalqg kvagaqitqn sgdpsgsmsi
      181 klrgitslsg ssdplyvidg vivsnqstnv sqrvlsndig vanpgqnrla dinpndiesl
      241 nvlngaaaaa iygsrasngv viittkrgks gaprvsayts fqlnelrksv pvntygkqfg
      301 fqglrlytig gispaqiaan pgttttpvtr anattqlasn lvdvprydyf keifrtasgt
      361 dngvsisggs ertqyfvsag ylknqgiikd tdftrynlra rvdqrltswa kvsagvsyin
      421 ssasekangn vfyspinain itnniyditr rdsngnllav eptrvnplst iedmkftqat
      481 nrtisdlqvn ltpfkgfsfd yilgvdaysq vgqgyirpyp yqataglpaa rypdgfasda
      541 nnteinlnsd vnlgyeynfs edfklnlrag ynyqylrnsl atqqgqfltp fittvrgass
      601 asvqadysla qsdlngfygq atvgyrnlaf ltgalrrdgs srfsssetnq yypkvsgslv
      661 lsdlgawqna afaqtfntlk lrasygdagn lngigpydrl yqfnavpfpr nalvpgaqla
      721 nnrvrperln eleggvdlgf fgdrlglsvt vyrqkitdlv varnlapttg gssiidnvgt
      781 menkglevll ngtairttdf swdmtavfsr nrnkvlslpg sngnvqaiai snsagapvyl
      841 lqgqpagvfy gstyarnpdg sllltsqgfp qdertsgqap gsvsyvpsrg adgqpsyapg
      901 ttvaqaiign pnpdwtgsfs tnftykklgl rvlldavqgv dvfnadkrtr qgvglgdlae
      961 kelrgelprg yifaiyntqq frvddgsyvk lrevalsygl ptfskyisal dlsligrnly
     1021 swdnyngfdp etsaggssdl lraidfgnvp iprsyqirla atf
//
LOCUS       WP_119657284             860 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Hymenobacter
            rubripertinctus].
ACCESSION   WP_119657284
VERSION     WP_119657284.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter rubripertinctus
  ORGANISM  Hymenobacter rubripertinctus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Hymenobacter rubripertinctus"
                     /db_xref="taxon:2029981"
     Protein         1..860
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=92430
     Region          30..853
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhpylakla lpllcagasv ssahaqgigt vsgrvldekg egmpgvtvli egsslggstn
       61 sdgsysiqnv psgphtlils fvgyttqrqt vsvtagqntt vsalsmsent tllneavvig
      121 ygtvkkadvt gsvvtvdeks fvkgqitdpv qlvqgkvagv qivssggapg agsvirirsg
      181 sslsasndpl ividgvpvdn sptdgasnal alinpndiat ftvlkdasat aiygsrasng
      241 viiittkkgv qgekmrvnfs sqvsraknyr qadvlsgdqf rqlvqdavan knplasaddl
      301 krlgtantdw qdaifrtawt tdnnvsltgn agpvpfrasv gylnqdgtll tnnikrntas
      361 lglsprlfdd hlridvnvkg swtdnrfada ggvvgtaasf dptqpiysgq payggyfeft
      421 daagnplgla prnpvaqlel rrdrstvkrs igniqldysl pflsalhanl nlgydvlrsn
      481 gtnaipaiss tnyiidpitk gignggvnnq ysqrkdnkll efylkynhdl pslssrvevl
      541 ggysyqdfir snpfnaprra sgdlanpdaa ngnpfktqyt llsfygrlny tildryllta
      601 tlrndqssrf sknersglfp avavawrikd edflkdvgal tdlkvrlgyg itgqqditst
      661 dypylgtyql gretvsyqfg ntyyttlrpd aydpnikwee tttynagldy gladnrvvgt
      721 vdvysrttkd lintipaaag tnfsdlyvtn vgslrnegie lgltvapirn ekidwtvian
      781 atfqrseitk ltvvddptyi gaktggisgn lastvqinsv gfqpysyyvy kqkyengkpv
      841 edqyedlngd gvirvypnrs
//
LOCUS       WP_119666022            1168 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119666022
VERSION     WP_119666022.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1168)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1168)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1168)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1168
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1168
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=128988
     Region          44..109
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          162..1166
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnryvyrqfq liglsallct sdlavmaqtn nlakyeknap apavslkdal nslkehykvd
       61 ivfgdqvieq ytvspgiiny rqsveknlea vlstsglkfr klkngtyaiv grmsgrrgas
      121 lgvseaktpi altslsehlp mlpqtistet grepekvadn pvrgkvtdek geglpgvnvt
      181 ikgttrgttt dasgnfslpn iekntilvfs figytpkeii adgkpilnvs lteeskslne
      241 vvvvgfgtqk katvtgaian vttkdlvqsp vanisnslvg rmpglfavqa sgepgndast
      301 lrirgvstfs gaadplilvn gievsnynni dpneienlti lkdasataiy girgangvii
      361 ittkrgkvgk pqlsytanla vtsftnlrkg mdsynyarly nealrndayv tgavytprft
      421 eadlakyrsg edpvfypntd wyalvlkpqa lqtqhnlnln ggtekvryfv sagffsqggq
      481 fnntdlikef danrkykryn frsnfdfdvt sklkvsldva sqtenlsgan wptvrviegi
      541 gkanpltspg figdklvnlp glgtvvnpla dmfgqgynrq frnflqgsvr vdylldflvp
      601 glsatgilny qnnntetltn lrplitynav rlpdgtvnli pqnieqpfsf gqnigknrrt
      661 yaqfgfdykr nfgdhsvtst vnynqtkyfd pnlaflvpng yqgvvgraty gyknrylaef
      721 tfgyngtenf apgkrfgffp ayslgwavse epffpkndvl tymkirgsyg evgndriggd
      781 rflyrpsayt qsnnpagyff getgstitay traiegrlgn pdvtweravk qnlglelslw
      841 kskisvtadv fsedrnnila nlgtvpatvg atlpaynlgr mrnrgfdgdi tyndrigqfn
      901 ftvrgnftfa rnkvlfqdev qrpftyqyrt gqrfgqyfgl iadglyntwe evndasrpvs
      961 awnnnrlqpg dirykdvngd giineddavp igysnfpeki fgvslsggyk gfdfsvlfqg
     1021 asnvslayar rqvrgwfens gavdylinsw saeryeqgqt iwfprvttga denhnnkmst
     1081 ywvrdgsyvr lknaeigynl pkemlsrlgl sstrifvsan nlltwssvfp gvdpeqsgtp
     1141 pgstiggttn eepypltrti nfglnlrf
//
LOCUS       WP_119666668            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119666668
VERSION     WP_119666668.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117801
     Region          35..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmystllkrp tiravwmlcl allihaegma qsqrftlrgr vtdangqsvp gvtvqlqgts
       61 lgtttdadgn yqftpsvapg nytlsfssig fgattqpvsl gsqetvttnv tlredvanld
      121 evvvtgstit ttrrelgnai stirgndlvq sgsggllnsl qgkvpgaqit qnsgdpsggi
      181 tvrlrgiksl sgasdplyvi dgviasnnsl nvsqlavsdq vgianpgtnr ladinpadia
      241 sinvingaaa aaiygsrain gvvlittkrg qtgaprvtft asaninelrk svplgtynkq
      301 fgfaglrlhp iagisptqit anpgvttvgi lrdgvttqla tnlvdvtryn yfdqifrtgy
      361 gtdntlsvsg grenttyyvs fgylknqgii rntdftrynl raridqrltn waklsvglsy
      421 vnslanekan gnvfyspins vnitnniydi tqrdaagnlq avestrvnpl stiedmnftq
      481 avsrtindvq lnltplkgls vdailgidty gqvgrsyirp ypyqaqaqlp lerypfgyaa
      541 tanntvlqln advnatyqrd ltealnlkli agfsyqysqq dlstsngqnl apfietvsga
      601 asttvralyn lsrfnlsgqf iqatvgyrnl afltgairqd rstvfspset nqlypkvsgs
      661 fvvsdlgfwk nasfngvfns lklrgsygda ggltaltpnd rfyqflpiay lgrntitpsq
      721 tlanpavrpe rmteleggvd lsffqdkinl gvslyrqriq dltvnrvlap ttggtgivnn
      781 vgemenrgve illgitpvkt kdftwdltfi ynrnrnkvls lasprielan vagapvfqlv
      841 gqpasqffgt fyarnyetga lllssnqnlp qqergdtyia tatkpieqvl sdaglninsl
      901 pagsyevagt yyvprrnaqg qpdlskpvlr kvignpnpkw tgsisselty kratlrflfd
      961 avygnqvfna dkrtrenvgi gtlteqemrg tltrgyifai gpieefridd gsfvklreva
     1021 lsyqlpsfvk glsglnlsli grnliswdny ngfdpetnag gnsdllrgid fgnvpiprty
     1081 rlqltatf
//
LOCUS       WP_119666863            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119666863
VERSION     WP_119666863.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116158
     Region          21..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkihlcafll llpflafsqq rtiqgkvrdn gdkaglpgts vtvkgttvgt vtdaqgsyqi
       61 nvpngasvlv fssvgfqske vtvgsqqvid vtltvdtkql sevvvtaagi krdknalgys
      121 vttldankla qksepdplra ltgkvagvnv qgsggaagga tnitirgnss lgnnnqplfv
      181 vdgvpfdnss fgstdgtvgg stvtnrafdl dpnniltmtv lkgaaaaaly gsraangaii
      241 ittkagksqs rkgleitynt gystetvagl peyqtrygqg tnfdyrsgvf gswgppypgv
      301 tsliptrqti phplttnnry pstvfpdifq adgttpvqvp yqsfaqynak nffrtgsvfe
      361 nalsistgge kgnftaglsr tgnqgvvpen eitrtavnig gnaqldnkfy vsgalnyvnt
      421 dqtspqltaa ngtgasildi lmfvptsfdl tnypytnpln gnnvydrvgt dnpywsvkns
      481 pttskvdryy gnivlgfdpl pwlniqntag fnvytdrrtv vngkggdyfp ngnisndnif
      541 rqeldntlll tatkpiseni gmkvilggnv nqrtterqvv fgdgiifrgi nslnntsvti
      601 prvlpnnrnv lqqrfyafft disldyrnyl flnlvarndv sstlppdsrs ylyggasasl
      661 vfteafrlpk silsfgklra gytrvgneat pyqtqtvyia npvlgagasg tgtistpfig
      721 qsaltqsdll anatlkpefi nelelgaelq ffnnrvgldv tyynkistsq iftvnavpss
      781 gytqkvinlg kssnegieig lnatpikapn glswdissaf tlnrnivrdi gslrelpygg
      841 fadlgsvhia grpygmirgs tyarddegni lvnpntgkpi lsgrteaign pnpdfilgvt
      901 ntltyrgltl salfdwkkgg dmysftayel lsrgvtrdte ereaiiigpg vlgdvntlkp
      961 ildgegrkip nnvgiavady yfsggfgpgg aaevnvfdat vfrlrevslg yqipkrwlek
     1021 tpfgsaflsv sgrnlwylap nfpkylnfdp evsslgagns qgfdfigipt trrlgvnlrf
     1081 sf
//
LOCUS       WP_119666873            1146 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119666873
VERSION     WP_119666873.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1146)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1146)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1146)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1146
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1146
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125614
     Region          64..115
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          153..1143
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknqsttipl ligislcawp nlvdaqllsr aepsltqqtt sasravrtrp lkkalsdler
       61 rfgvsfaydd qlvasrqtsv vpegasleea llqllrpqgl rytkikeklf viqpaetpaa
      121 eaprdakndm agtipsagvl tesalaavap qvkrisgqit detgqglpga nviekgtnng
      181 tntdangnfv lnvsdqattl tissvgyvsq dvaignqtti nvqlvpdnrt leevvvigyq
      241 avrkrdvtga navinptean rvtaqslpes iqglspgvtv rntgvpgqqa siqirgvasf
      301 lnteplyvid gmiadanpti ntddiesiqi lkdasaaaiy gsraangvvi ittkqgkegp
      361 arvsftgkyg iqqaykrwdv mnasefaalq rtqyqnsgqt ppvsvaegtf npaidtdwqd
      421 qvlrtgslqd ynltlsggtk tgryllsgsy fnntgyvigs nfnraslrin trnefgrftf
      481 genvvltnsn vqnqpigtnp iydmaynlpv ipvqdpsyis ptnpegygig sinsisyayn
      541 pvaarnlssn rsnfarlvgn aflefkfadw lsyrfnagld asfdytqnlr rvgvyqynaa
      601 pvpssinedr srftsllfeh tlnfnrtfgl hningvvgis qqntrrdvtt ggrtnlafag
      661 gqylptigaa sgiatsaggt peyyrilgyl grinytyndr ylltltgrvd qdsrfgpnyr
      721 tgffpsiaga wriseekffn vdwisdlkls asygklgivv ptlgsfpyta finnnpraif
      781 gdgqtanvga yqaqlanpnl rweeriqqny gltasflnnr itaefnvyns lssdailnlt
      841 vpgylgnlrg npyvntasir nrgvefsaty rnnenafkwd vsgnfttirn rvenvgnqgq
      901 dinyivsgnt rsqvgnpvgq wfvlktnglf qtqeeinnyr gpdgsliqpn akpgdiryed
      961 anndgridvn drqfvtspwp slqtgaqfng syknfnlnvq ligifgytvy ndirrildsy
     1021 qntnfrrdis pwtpnntdts dprlgleand qgiisnnlay sdrwlenasy vrvrnielgy
     1081 nlpktltnrl nvrgarvyvs gqnlftitky sgldpdvtga niqergvdng hwptprvisl
     1141 gincdf
//
LOCUS       WP_119666893            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119666893
VERSION     WP_119666893.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115760
     Region          29..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkglriwll fwcsallvgt svtvqaqnrv itgivssaee gplpgvnvvl kgttvgsttd
       61 algkyslsvp gdaavitfss igflteeltv gnrstfnltl kadtrqlqev vitalgvake
      121 kkalgygvqe lkgsaltear ssnvanalsg kiaglrissn ggpgsgssiq irgassvsgn
      181 nqplivvdgv piqqtsekqw ggglsevnpd nikeisvlkg pnaaalygsr aangvilvtt
      241 kngsgtkgig vevnsnvtfd epwikpqfqn iygggngyrt wytdgwsgai tdpleitqyr
      301 aaypngplsg tegtdeswgg pmdgrlvrhw wsgrevaplt pmpnnwndyw qtgrtitntv
      361 alsggndkgs frlavgrlsq dgimyfndfk rsnfklntay nftpklnvav saeyvksggn
      421 rgfqegqqfi wahrqtdwnr irnwrdysav hiqralpgrp adtdppnwqh tfftnpyylt
      481 ellpytndkd rlvgnialny qimpylslml rsgtdlwsdt rinivnferv rngnrtpgry
      541 seevlrqqet nhdfiltfnk sltsdittnv qvggvqrtny ykrnytyvge lvvdgvynls
      601 nsnvsqnave saiqksqmns lfgsfevgwr nalflnatar ndwsstlpad arsyfypsvs
      661 asavitdllg iqsnllsfgk vraswaqvgn ttdpyqlaqt frsggswngs vpefyentki
      721 snstlkpeit tgielgmdlr flkgrvgldv tyydqtsrnq ilavdiskas gynqrvlnag
      781 altnkgieiv ltgtpvklpn gfswettvnf arnrnkvvel aeglttyvln srqgltsear
      841 vgqpygtlfg igfehapdgq iiykdglpvv stnprvlgni qpkwtggwln sfsykgivls
      901 vlidtkmggq fydegtanar wtgqyaetai greegiigkg vvnvgsaenp qyvpntvimp
      961 attlygynnp rryheaaifd gsyvklreas lgyqipasll srvkirtakv slvgrnllml
     1021 fsnhphldpe vdrfggnaqg faygelpssr slglnlslgf
//
LOCUS       WP_119666894            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119666894
VERSION     WP_119666894.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112096
     Region          26..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqsfvrlflf llistmagva amaqdrtitg kvtsaddgtp ipgasvvvqg tsrgtttdat
       61 gtfriqaqsg qtlrisfign asrdvvvgns dvvnvtlrqe snalnevvvt algikrekrq
      121 lgyavtevag qdlansqrdn flnaiqgrva gvqvgassgm pgssssviir ginslsgnnq
      181 plyvidgmpi snntiasnsf vssrtsgqst enrtvdfsnr aqdinpndie titilkgpea
      241 aalygveaan gaivittkkg ragqgrisyq nsftwqepga lpetqrvysq gnngvpqann
      301 ynafgpryae gvqfynnaen flqtgfgqrh nvsfdggtdr ytyrlsagyt nsqgvipttn
      361 ykrlnislgg takitdklsl estiqyintd nqkvskgtns fllgmlvwpa nddmsnylnp
      421 dgsrrratta naeienpyfd vnknqlrdrg nravtnigan yaatdwltlt arvgldvfst
      481 qylikyhpes nraggvigga ldqatdnnrt ltaqyfatak rdfgkfstsv rvgqaiydyr
      541 yevlatrgek fldpnftsin ntdpltqksl ttlrqrrlig vfgdatfgyd nllfltvtgr
      601 ndwsstfppa nrsffypsas lgfvftdlvp qgafrnalsy gkfrvslaqv gkeapeysts
      661 qayesqtttg ggfaygftap npflkpekvn sfeigtelkf fngrlgvdaa yyrttstsqi
      721 irdlrisygt gfilktingg klwnngveis ltgepirsan ftwnstvnft ktnsqlvela
      781 pglpefyssd twlygnirng srlggslttl tgnsyvrnnk gdilispvsg lpftetawnv
      841 vadrnpdfvm gflnsfsykn fslnflldir kggdvynate sflyrqglsm ktldretpri
      901 ftgvlkdgle ntdnptrnti qvvpyynnay ysaladenfi erdinwlrlk evtlrynlps
      961 slltrsrvfk tagvfftgtd lllltnytgg dpgvngvnta tggsggygid fgnlplprvf
     1021 nvginvgf
//
LOCUS       WP_119667255            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119667255
VERSION     WP_119667255.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117147
     Region          25..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkflltqll lclfaiprla saqdrsitgk vvsaedntpl pgvsvlikgt tqgtttdadg
       61 tyritaaqgs elqasfigfa tqgikvngqs tinfslkpda anlqeivvta qgirknqrel
      121 gyatskvetg dvtvgrspql aqalsgkvtg lavynvnnsv dpsvkvvlrg yrsltgnnea
      181 lvvldgmqtt stilatinpn diesvtilkg gqaatlygsa gingailitt krgtkgklrv
      241 sysnstnieq isflpqfqek fgsgshyypa fgsagysndp lvrmqgnwrs yenqqfgdpf
      301 dgslrilgrt aedgsqlivp ysaikngrrk afdtgvsmnn qvsfqggdet ssfylslenq
      361 kiagtvpndk sertgarlsg tkeygkltag fnaayvqaay drttsdfyfn vinqpanlpl
      421 sdlrdwqtnp lanpngfynd yynnpyfead nnrakykdan lngninlnlr atpwltfter
      481 lgvmnnsrtg knttgkftys dwaktksfip epffregdgt giyraisdvl gavsdysste
      541 nvinnefliq vdktigpfqn klilgnsvyq rttkaisvgs ssivvpdvyn vanrqgeltg
      601 gesntqerrv gyyadltany rnwlilngtf rydqtsrfyk ptrptntwsy pyygaavsfi
      661 atdafpaiks sflnyakira nynknandni plygldlvyg ngggfpygnt vgltvgnrlp
      721 danlrpevvy steiggefql lndrinldvs aysqrsegqv itvrvpnttg fstllinvge
      781 tknwgyeael kyliarggkf swdaslrysy ndnkvvdlyp ginefqyggy syantnvikg
      841 erfpilktdg yqyapdgsgy vlvspttgyp lrqttlsprg gtlprhiagl gskveygsfg
      901 ftfnfeyrgg nvmysdlgrq mtftgagkwt enryphvfpn sailgsdgkt vtpnttvqvr
      961 eaeyglwvds yrliaenfvt pawfiklrdi nlsysfpqsl lsktrlftgg sialygrnvf
     1021 tfvdkknyyt dpefsyttdn gqginntlqt ppvrqygvnl nltf
//
LOCUS       WP_119667605            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119667605
VERSION     WP_119667605.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116786
     Region          49..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlsvyrtpsg tasscpirsg rwsalgrgfv lcisflllst tlfaalverp irgrvlneqg
       61 egmpgvnvvv egtrigtlts atgdfslnvp dsastllfsy igyqrqtiri rnqnvleirm
      121 vadagqleev vvtalgvtre kralgyavqe vkgdnltqar etnlinslag kvagvnvtgg
      181 snsiggssri virgetslag dnqplfvvdg ipinngvsas sqrqnidygn gaaeinpddi
      241 etisvlkgpn aaalygsraa ngvilittks gknkkgvgvs vnsttsfesv lrlpdyqney
      301 gqgrgdqyni gdggrswgpr ldgrmiavpv ntewpprnge mvpwvpypdn vkefyevgrt
      361 ltnnialtag ndngnfrlsy tnlnqtgivp ntdqqrhtas itgkyaltnk lnistgvnyf
      421 ytvsnnrpvl sygnesivyt wiwegrqvrt dkmrdywvkg legtqpftyn yqfndnpyyt
      481 myenlngllr nrltgnitat yqftpelsll vrtgmdmsne radrrrtfgs nafplgmysq
      541 drdyfeerns dflltydktl ssdwqfkvsv ggnqmrqrrd elstranals vpgvynlgns
      601 qvplvniqsd sryrinslys fgqvsyknal fldltarndw sstlpvgnns yfypsvatsa
      661 vltdlieglr tqtlsfaklr vgwarvgndt dpyrlrnvyn yntpwqsnqa vsessvinna
      721 nlkpesvdty eigtdirffn nrlgldvtyy ntvsrnqiin ipldqtsgyt srflnageir
      781 srglevvlna tpvklsngfr wdvalnwatn rarvvelidg ldtyslpsry vsvqarvggr
      841 mgdmygrgfl rdpqgniiha dglplftnel ikvgnynpdw tgglyntfty kgftlgglld
      901 mrkggsiysy myvrgneagq lveslpgren gyvgpgvirn pdgtfrpndv nvtaerywgs
      961 gyfnpeqatf datflklrel kfgyqvpnrw ltrlpfrdvn illvgrnlfl wtkvphidpd
     1021 ttgisgdtll pgiedmsmps arsigfninf rl
//
LOCUS       WP_119667515            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119667515
VERSION     WP_119667515.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116541
     Region          23..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrllvvqfl lcllsvplla qdisvsgkvt svsdgsslpg vniavkgtsr gtttnsdgty
       61 rlnvpanstl vfsfigfatq evavgnrttv dvrltddaaq lqevvvtalg isrekkalny
      121 avqdikqekl niareqnvan alagkiagvq vlgqsgakfg spsirirgvn sltgsdplyv
      181 vdgtptdisq vnmddvdnlt vlkgpsatal ygnrasagvi vittkrakag etrldinhst
      241 tldmvallpk yqneygggys qafetfefnp aihpaswqaf ngqnlidysa deswgprldg
      301 tlyrsaaswl pgpqfgqltp fvaqpnnvrd ffekpfshnt niafsrgtea fqsrisythi
      361 anngiipnsw qnrdyisakn silfgknlta nlninytath tfnqpadryg stggtgtsnn
      421 lfgvsnailn gynqtigsfn qwfqrqvsie dlrnyknpdg tfrswniggp ldprpkywds
      481 pytqvyentn esrnnrlfgd fgltyqilpn lkasgtvrrd qsnffqegri aagtlneagr
      541 ggysnvaant rennyellvs ynqdfgdnls vvanaggnir ynrtegvfqt tvgglsvpgf
      601 yniaasrdrp tarnylyerq vnslfanvsl gfrdfvfveg svrndwsstl pagnnsylyp
      661 sisaglifte lipknsilsy gkirggyaqv gtdvdpyqta laysvgnpyl nnptqflpva
      721 lpnanllpgr sasveagvdl rflnnrfgle ftayqnknrd qiiplpvapt sgysnayvna
      781 glietsglel hiyanpvrss sgfnwefdin adrnrsrvve llpgltnyql dgpqwrtltl
      841 naregkewgt lvgqgirkdp atgkpvvygs gpnaglyike dnvelgsvlp kfkggmintl
      901 sykdlvlris tdfvaggkff sttkmfnays glgaetagln elgnpkrdpv adgggillda
      961 vteegqpntt rvdaqtlyen wlfalnerwi ydktyvklre vslgynlpkr llgnrvksan
     1021 vsfiarnpll iysaigggid isesetlwye ggqlppvrsf gvnvrlgf
//
LOCUS       WP_119668745            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119668745
VERSION     WP_119668745.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114372
     Region          26..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktiyvlil llvclsnysr aqsnrvtgrv tgadnqglpg vnvvvvgttq gtttdasgny
       61 ainagpetsl ifsyisyvsq tipvnnrsvi nvqlvedaka idevivtalg ikkeaktlgy
      121 atasvnaeqi svnrttnfvs glqgklagvn isslgtgpag sakirirgqs sfagqnnpli
      181 vvngvpidns nyalggdfgn rasnssdggd glssinpddi etidvlkgat aaalygsrak
      241 dgvvmittks rgtgkgfgvt ynanfttdtp ldftdfqyey gqgeggkrpt tsnptsgvws
      301 fgekfqpgmt qtlfdnetwp yepvfnrvrk fyrvgtnftn tvtvanngqn ggfslsfgnt
      361 dnkgimennk fnrkvinlgf tqnitsrlta sgninysken ninppqlntq dlsvstvift
      421 lansmpfeal rqnqtlpngd efvfsrflvr nnpyysmnyk fenvrrdrlf gnvalkyqft
      481 dwlylqgrla qdsyirnqdy nipngyapia rapvgyvngs ytqdvrqnve rnldfilgfn
      541 ktfgnigvda tfggnhrfar ndynsvtvqd fvqpglytvm ngrikdplys lsekeinslf
      601 gaatisykef lylnatarnd wfstlapsnr silypslsgs fvfsqafdnm pawlsfgklr
      661 aayaqvgsdn vdpysnalyf avdnnsfpnp sgqlvpvggi natvvpnknl rplriqeaev
      721 glelrllqnk vgldltyyrk ltddqilaaq vsdassytsk linvgrsmnk giemlltfsp
      781 isnptfrwdv sanvsyntsr vmrlgltekd tiitvssggg rtlnqvvgkp lgqlytftyl
      841 rdaqgrqvfd ansgmplrnn tlknvgsalp myfggitntf syrgivlsal idfklghkmi
      901 agrninymrh glskrtlpgr dvgyvigngv npngevnqtr aavqpfyesi nplginedfv
      961 fnagfwklrq vtlgydftkf lpaslfikgl kinavannvl vlkkwtenmd peealvssdn
     1021 avgldfwpgl pptrsvgfnl nvrf
//
LOCUS       WP_119669653            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119669653
VERSION     WP_119669653.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121049
     Region          35..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtiflrlltp svpvnrrllv vflfcllsgl savaqtitgr vasaddnqpl pgvsivikgt
       61 ttgtttgadg kysinapsta vltfsyigye tqdvtvgnrt tidvtlrgda qtlgevvvta
      121 lgiqrekkal gyatqeiqgs altiaretnv tnqlagkiag vtvvgspsgi ggssrvtirg
      181 ersvdlnknq plyvidgvpi sngftggsgr nnlevdfgng asfinpddie sinvlkggaa
      241 salygaraan gviviktksg rgnkgigvei ntnqtvetpl vlpeyqtvyg qgngnggdfa
      301 fvngggaglt dgtdeawgpa fslnksypqy dsprtlngqp tnfrggdlna ptgsvitptp
      361 wvaetdnlrk flqtgrtntt sialtgsnda gnfrlahtml nqtgivpntd lkryttslsg
      421 gfnftpkfsa nafvsyikge sgnrpsisyg tesimylfnc wlppsvqlep medywmrgqe
      481 gvrqyswnyn yhdnpyltvy entngqlydr vignaslkyd ltpwlsvqgr taidyssekr
      541 eykrafstqr fpfgqyrdnr iiteerntdf lftankefne twtvsgtfgg nqlrqksdfl
      601 etnagqlnip giynltnsri plqtsqslve krvnslygsa qvafrnylfl evtarndwss
      661 altlpeyart fgtqdnsyfy psvavsavls dmftlpqsvs flkarlnyas vgndtdaftf
      721 tqsynpsdpf gssqvygetd rlanfnlkpe isdsfeggve lklfkrrvgl dvsyyqtntr
      781 nqilniplsi tsgynsrain aglirnngve valnlvpvel pnslrwgvdf nfsanrskvi
      841 rladniqnfv masrrvsiea rvgermgdmy gigfarvqnt dptkpyydat gqyvgqmvfs
      901 qgrpiattdr iklgnynpdf llginnslty rnlrlsflfd mrqggklyse tqtvgreggi
      961 iietlegran gynlnlpgng vigqgvkvvs tntdgtttfa pndvkvnsrq whtawtggrn
     1021 iaegvmydas fvklrevqlg faipdriwgr vplrgvtftl vgrnlavwsk vphvdpetls
     1081 yaggtalpgi eymaipttrs fgfnlgvkl
//
LOCUS       WP_119669655            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119669655
VERSION     WP_119669655.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119111
     Region          16..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvflfcllsg fsalaqtisg rvvsgddqqp lpgvsivlkg tttgtttrad gtysinvpss
       61 natltfsfig ydsqeitvgn rstidvtlas spkalnevvi talgikkdvr ntgvaiqtvd
      121 gaslvkarep npinnlvgkv agltigasae llrrptialr gytdvlfvvd gvpinsdtwn
      181 isnddietyt vlkgasasal ygfrgkngai littkrgskd krgfsvevnt sqqfdngfia
      241 ipkvqdeygp gdhgvyafgd gkgnglndgd ydiwgppldg rllpqydspv vpgqtftttf
      301 pngakftsnr qptpwtprgk dnlrrflqtg ilstnnvavs sstekydlrf slshnyqrgl
      361 vpntrlnitn fntslglnfs pklrfesnln fsrqttpnfp dvnygpnsli ynmniwggad
      421 wnvddmkqiw qpgkegtqqi yaeyqrynnp wfmakywqrg hykndlygyt slryqladgl
      481 qltgkaqltt wnllrnekfp ysmtvygree grgdyredrr nlldninqvl lqynksitpd
      541 ltvsalagge lrvlnynsdf astnylnvpg vynfansanp viatnytanm rvlsayysad
      601 ftfrdlvtls ttgrvdklst lpaqnntyfy psvalstvvs dyiklpdavs flklrasyan
      661 vkdaltqsti gttpglsypl gygdnysssy ggptyqnsav ysvplvynnr paayftntls
      721 npdlkpnsts qfeagldvrf lnnriavdgv yfnsndgpri fslptsettg ynarlvngir
      781 tqkqgievsv tgkalrmang lswdvtanys tyteklrevy peggintlas syfvgsssgn
      841 rfltagdrvd gfysgafyrt pdgqlindag grpivnpvaq flgyvnpkfv wginnrfayk
      901 nwnfsfqfdg rvggvigdyi kqktyqggrn letaqgaigd arkqdvlgvk ayvgegvqvs
      961 ngavikydpq tgaitnygel qftpnttktf aqdyiarvyg qteaflisrs yaklrevvig
     1021 ytlpstllnr vgvrqatvsl vgrnllyfae rndldldqfv nggisdlqtp ttrryginln
     1081 ltf
//
LOCUS       WP_119669888            1100 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119669888
VERSION     WP_119669888.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1100
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119441
     Region          24..1099
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrllplflf lfisslvsaq nrltvsgtvk ddkgvgvpgi sllvkgtttg tstdadgafr
       61 lnvpngnavl vvsgvgylrq evpvgnaatl sitikedpks ldevivtgfg ikqearklsy
      121 aaqeiqgqnl lrantpnlvn alqgkvagvq idqgsggpms ssririrgna slssntqplf
      181 vvdgvlirpt ttgadswgaa qdfgnimknl nadnvetvtv lkgsaasaly gsealngvvv
      241 ittkkgrdqk glgvsynhts sfetayrfvd vqnqygagls ptfpkaadgv evvqsqnsaw
      301 aysfgpkidg rmvrdldgrm vewkannpld ffqtgrytnh nvavegandr gsfrasysnl
      361 fnntimpgga elkrnnfnir atqrvgkifn ldvaadytin dnlnpirqgg tynpvfrfvy
      421 arprtldidy wadnyqsplg grktgtadpy gisqflwetf qyntyrneki frgnidvtan
      481 vtpwltalvr aniqnelyat enkflgpgvg fgggeysqys qannqsriqa lltasrdfgs
      541 lfhlnltvgg etnriiggrd frlrtdgglr ipgqfnlpns inpvvadigq grlaaskrtd
      601 avyaygdlsy kdalflnftn ridyssalty adgsgqysyy ypsvglawdf tqsvkelpka
      661 ltfgklrasy gftggdtdaw itnqtgfysa gsifnsingq iqqygfrdnv lpnynlrnrl
      721 arewevgtdl rlfnnrvgid vavynkltrn eifnlpvaqe agltnrlvna gkilnrgvei
      781 lltgtpvktn kfqwntsfnf srnrnkilel vdgvdtyels lafgndvrsi arvgsdygti
      841 vstyafarda qgrkligaas gtnggyltyl rsgaagqgsk dlgtllekfl lsnvnnfqfg
      901 nfsatfqvds kiggvmasat hqygsafgtf knslfgrdte sggitftdaq gnvrndgiip
      961 dgvlntgvta tvdgkqvdlg gmtykeavdk gylkpipafa yydnlsnwgs gireysvfen
     1021 swvavreasv sydvpatvln kvkvqslrls vvgrnlgyly rtakdginpq gllsnragef
     1081 aeygglpfsr nigvtvnvgl
//
LOCUS       WP_119670397            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119670397
VERSION     WP_119670397.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113236
     Region          25..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkylmlgwl ltllfclpal aqevtvsgrv tssddgsalp gvsiqikgts rgtttdsegr
       61 yrlsvpanar lvfsyigfgn qeiavgnqtt idvaltsgaq nlseivvtaq gierdkrslg
      121 ystqevnsal isqksepnll nslqgklagv nistqsgspg astninirgi tsfngsnqpl
      181 ivvdgiifsn dvnvtgntlf qsqsanrlad inpesiesin vlkgpaaavl ygsrasagai
      241 iittktgrnq qnktevtits synvqevygl prfqndygqg tnnlfvnntt nswgpafvgg
      301 ptsvtnlqgq vrpyqaypnn vrdfyrqghi lqntaniagg dvnrnfnisv sntaqqgitl
      361 nskfsrtnvq lggetrlnng lritgtgtya qtvqrgatlg nggsafgqlt riprsydlpn
      421 epyqdangqs iyfvaannpy wslynstlds qvdrffgnft lgydvtkwln ityratgdty
      481 tdrrkavenf gaaraaqgsi tqdnffrsel ngdllitakt drlfleglga nlllgnninq
      541 rrtqnvaavg aslvipgfln tsngsvltgs gesstlrrlv gyyaqlslny qnylfleltg
      601 radqsstlpk anstyfypsa slsfvptdff kvqsdilsya kvrasiarvg rdadpyllns
      661 vyvpstygnn lasvtfplti ggssvpgftp ssrigsnalt pefvtssevg lnlgffqnrl
      721 sldaayfftr stdqifnvai snstgfdtrt tnvgelqnqg ielvlsatpv rvsgfkwdit
      781 anftrirnkv isiapgvrqs giagngfigi tasivegqpy gvivstantr vqntnpndpa
      841 tydptgqyvg qyiinptsgq fapglagqvi anpnpnytlg innsfsykgf tlqalvdirq
      901 ggqlfsfpav dyrsggqlyv tgidrdqpri lpgvipitgs dgrvtgfrpn niqlssqayw
      961 qglgglasea avfdatnyrl revslnytlp kgllnktpfg tisvgvsgrn lffyapnyyt
     1021 dpevntqgag niqgldlngp pnarnygvnl rltl
//
LOCUS       WP_119670454            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119670454
VERSION     WP_119670454.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118225
     Region          24..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msrfllmsll fvcsswataw aqerkitgki vsaddgapip gvsvvlkgtt kgtnsdaegm
       61 ysivvpdkgg klvfsfvgsa tqevevgnrs sidvrlends kqltevvvta vgiqrdkkal
      121 ayavsnvkgd llqqrsepdp lralagkvpg vnitagngap gagtritirg nnsftgnnqp
      181 lfvvdgipfd nsvnstqgyn qntvttnray didpnnienm tvlkgaaasa lygsraangv
      241 ivittksgsk sarkglevnf nssysvenvs sipdyqntyt qgsnqtyngg fignwgtvfp
      301 aevdrvnaal gfdryskiid pdfpagtiph plvdatvpyg aaryqtafpe llqpngrgia
      361 vplvphdiig gffrtgkvle ngiqinstgd ktslnasvsr trndgiipns fterttlsfg
      421 gnatltnkln vagsvaytnt nqqspqsgag yyadygglas agsiygrlfy lprnydlnny
      481 pfenpvdgsn vfyraldnpl wtakynlyns avnriygnmt lsydvtpwln ltargglnty
      541 setrknvvrp ggtfvplgsv srqdltktev dftflataqh dfsekfnakl llgfnpnert
      601 ytessvagsp vidpnvltig gtlnqnaady rytrrlygvf geltlgynnf afltasvrnd
      661 hsstlpagnn syyypavags fvftevlnlp knilnfgklr anyamvgkda dpyqvftayn
      721 lgrtfyngta istaslpsql nnvnlkpeft sevelgaelq ffnnrigvdv ahfdristdl
      781 ivtrelprts gfateitnag kisnkgwevg ltlvpiraan gltwssfvay trirsrveda
      841 gpggeifigg tglsslgtif rnglpygqii gsrnardeng nllinpstgl piraassgvi
      901 gdpntkytvg wtntvsfknf tltvltdyka ggslfsstaa slllrgqlkn sedregmrvi
      961 pgvlgdpaty kplvgedgkp ikntiamtaf qyhftdgyga ygadevniyd atvvrlrevs
     1021 lgysvpkafl qryakvfgsl rlsvsgrnlw fyapnmlegl nfdpevlsnf adsniqgfdl
     1081 gaapstrrfg vnlnasf
//
LOCUS       WP_119670456            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119670456
VERSION     WP_119670456.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120280
     Region          24..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkillvsll lvcslwataw aqerkvsgkv tsaddgkpmp gvsvvlkgtt kgantdadgs
       61 ysiavpeqgg klvvsfvgtt tqeveignqs vidiklatdt rqlneivvtg vgvatdkrkl
      121 giavesvsak nlpqtpsasi dqalvgkiag aqissgngtp gapvnivlrg intinrgtap
      181 illidgvqvd atnydsngnl nnnptsllss idpntierve vvqgaaaatl ygaqgangvi
      241 qvftkkgksg klnidfsssi trneylnvgg vsksqfngfq tdaqnnvvyq sgrdannnpv
      301 yaplqfnpnt ltyngnvlyn pldvnnkadk pytanlkyyd hyafffrpsn tynnsialtg
      361 gsdkvdfals asnnqqesnv inngayqrsn ltsnigiqla kgltfrtttq lvytkstikt
      421 ndrlilyain narpfadfsa ldpdgnpgvy ygdavgvnhg npsfwqrytn nkdnkvdviq
      481 sfnlnykink fldldakygi nyskqeivtt ygnqsrnrnv iannnnqyrs yfgtdptgei
      541 dnnsmtttyq nflasafint dfqedfklni pirtttqlaf dyrnrnfrqf ytytlglpty
      601 epftaaqsst frvpgvvaps tgrpglpggg dytepfityg yvvnqridyg dlagvsggfr
      661 tdyssafgra skpftfprgd ayfrvsalkf wenstigtff pefklraayg qagiqprpfd
      721 ryqvlntrtl gtsnsfyipa sqpnpdlsve vsselevgtd laltpfknsi wlssvrlsgt
      781 ywkrstdnai fdvsaapssg insikdnafs lssnglqfsl natvlrtstl swnlttnfgn
      841 qtskitavkg nqevvvlssa gssnyvlkag ekigqlyghv aihqvdakdp ngnfyipadq
      901 qanytvasng wvvnkatkqp ffsadkysfg dpnpkfnmsf indftfknfl tfgfqfdwvy
      961 rshiynqtke wmyrdgihad ysipltiegq tgawtafyrg vyaqraangt knyfyedasf
     1021 vrlrnvaigv dfsklvnlpv lrraqlvlsg rnlltftkyt gfdpevssgt gssawdrgtd
     1081 hntmpnlrsy qatlnigl
//
LOCUS       WP_119670925            1005 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119670925
VERSION     WP_119670925.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1005
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109214
     Region          30..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtttyrlla rfvlwsgmcl lhavafaqtt vsgtikseng tpipganivv kgtstgttst
       61 adgtytlnvt qrnatlvfss igfqskevav gsgntlnvtl tedvanleev vvtglatsik
      121 rsnlanaist vsakeligtt qiqtvdnaly gkltgvnint nggapgggvs vqlrgisslv
      181 gasqplyiid gvyannavnr tgrgnltgas avetqddaan risdinpndi etvevlkgps
      241 aaaiygtran agviiittkr gtagktrltf aqdygfavaq rllgvdswse akintffaaa
      301 rrpieldrfr aangqtydye kyfygntapl sntrlglsgg ndktrfyisg aftnekgiir
      361 rtgfkrysir anidhkltqd itlsvgsnyi nsntdrgftg nqnnsgasig yniayvpnyf
      421 slfpdasgry pdnpyfsenp vavtdrginn snvnrfiqsf nltanlykse ravlkligqg
      481 gldfaqnttq vylpedlqfq raqgnpgdvi wgktenvntn lqaalvlnwn vsrvnltsqv
      541 gvvrlnfred rllnrsrgla ggqnnlrqgt vqeifdqrfq svtdvgvfaq qeanwedkii
      601 atagirfdks tligdanrfw afpkaslavn lanfnfiqss glakifsqik prvaygetag
      661 vpafgttftp lnsaniggll gsvvttaagn nvieperage lefgldlglf nnrisleaty
      721 ydkqtrsnlq nlqlspavgv stiptnlaql qnrgielals vvpaqlanfr wntrlmwwrn
      781 nllltrlgip pynlgafgvt lgtflyqegf spttivgtrp ardatdtpla envrtgafvl
      841 gnsqpdfqms wlneftlfgk vdinmlwhwk qggdninltq flmdsggttp dwndddngdg
      901 tpngrqrgla phngadrwvq dasyvrlrev avyynlpvqs fgkwfsnrvs ririgassqn
      961 pltftkyfgy dpetstfgvq avgsgvdiap yptqrrffgh lvvef
//
LOCUS       WP_119670998            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119670998
VERSION     WP_119670998.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117158
     Region          33..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmqhyfiskq grvltlllwa vlalsatsya qdrrvtgrvv ssadqqaipg vnillkntqt
       61 gtttdasgnf tlnvpanatl ifsaigfvgq evevgnratl tvtlqqseqa lsevvvtalg
      121 ikkeaktlgy atatvnpeqi ttnrtvnfvn alqgkiagvn isslgtgaag tskirirgqs
      181 sfsgqnnpli vvngvpidnt nfgqnngntg gdnsignrdr nysdggdgls sinpddieqm
      241 tvlkggtaaa lygsrakdga ilittrtraa gqgigviynt nfttdqpldf tdfqyeygqg
      301 eygvrptapn ptsgvwsfge rfagqtqvlf ggvtvpyqpv ydrirkfyrt gstwtnsvsv
      361 ssggekggfn lsvsntdnkg itrnntynrk tinlgfsynl spklsvtgsm nysneynknp
      421 pqiaqqdnst ptviytlans mpldlleanq inpatgnefv ysrfmnrtnp yfvlnnkfen
      481 irrdrlfgnl tarynftdwl ylqgrvgqdf wsrdqdynfp tgqaslaaap agfvngayvq
      541 earrfreina dfliganrqf gkfgvninag gnqlyrrsdl nsvqvtdfiv rdlyvpqngr
      601 vkdptfglse rkvnslyaaa efsyndylyi natarndwfs tlapgnrsil ypsvtgsfvf
      661 sqafntlpaw vnfgklraay aevgsdgdva pysnnlfyav aanlfpnpag qgqpvgfits
      721 ntvpsatlkp srtaeaevgl elklfnnrfg vdltyynkit sdqivaaqss dasgytntli
      781 nsgqsrnrgv elllsfapvr tkdfswdvtf ngsynetkll klltdddgsp ekdynkdgqp
      841 eqiivgngif igdlrqvvgq plgqlysfgy ardaqgriih gndglpnrta tpisfgsalp
      901 kyvggitnsf nyrgislsfl idfklggkml sgtnlnlfrh glqketlvgr gdpdnrmvgv
      961 gvnergepna vratvqdyys vgrskslgeq vvydagfwkl rqvtlgydft kflpkslfik
     1021 gvrlnavann vailkkwvpn idpesfgfss dnlvglestg lpttrsigfn lnvrf
//
LOCUS       WP_119671876            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Fibrisoma
            montanum].
ACCESSION   WP_119671876
VERSION     WP_119671876.1
KEYWORDS    RefSeq.
SOURCE      Fibrisoma montanum
  ORGANISM  Fibrisoma montanum
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Fibrisoma.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Fibrisoma montanum"
                     /db_xref="taxon:2305895"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114259
     Region          25..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknllrvcma iafslcflev maqpidvsgi vtaegdnapl pgvnvsvkgt stgtqtnasg
       61 qyrlrvnstd avlvfsyigf qtqeitvgnr tsinlvlkqd nqqlnevvvt algisrqkkd
      121 lgyatqsvda aeisqnrqtn vvsalqgkva gvtitntgga pgqgarilir ginsldasrd
      181 nqplfvvdgi lldnttstfg sgaelrgatn raadinpddi etinilkgga atalyglrga
      241 ngvvvittks gkagafranl nstfgienvn kypevqdqyt igyagvynpq dffpswgptv
      301 eeairidpth pqrlynhfrd ayqtgkqyqn nlsftggtdk itflssighl rhegvipftn
      361 fnklsvrlnt nvklsekfgv ntslnyinsg gdrynadrfn eslsywspry dvrdyikpdg
      421 tqnsygngnp iygaytnklr dnvnrlvggl nflyspfkwl slnyrvgldt ysedrlrtap
      481 gptglagerv fednglgfvy qyntnfrait stftasastk lgqyvnttfr lghdlydrri
      541 rsfgaegnel tvydyfdlrn aktvrtvqnd edyrlmgvfg eltldyrdyl fltltgrndi
      601 tssllapnns ffypsaslsy lfsqqfkmpe fislgklras yaqigkdaap ystvtgyaay
      661 ttlpsgltgf trgsllgdpn lrpeftdtfe aglemgffnn rlgldltyyn slsrdqiirv
      721 dvssgtgyvq aainsgsmrn rgielilrat pvqtgklswd vnlnfsanrn kilslreglt
      781 einyanqfgy lsssvtmrlv pgypygnlyg rsyqryypna aeanaspeld rgrpivigan
      841 gfpvinttqk ilgnsqpdwi gglnntlryg nftltalfda rvgqdrynql gnffsafgia
      901 eytedrnttk vfegvladgt pntkavwlgq grgpdgvdyt ngfyrnihrg vsenfiedas
      961 wvrlrsagit yalptslfrn sfvknvtlsv tgnnlalwtk ysgydpetss fnsgsnvdgf
     1021 tgftypavrs vlftlnagf
//
LOCUS       WP_119680161             445 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Indioceanicola profundi].
ACCESSION   WP_119680161
VERSION     WP_119680161.1
KEYWORDS    RefSeq.
SOURCE      Indioceanicola profundi
  ORGANISM  Indioceanicola profundi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Indioceanicola.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Indioceanicola profundi"
                     /db_xref="taxon:2220096"
     Protein         1..445
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46254
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,323,325)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,330..331,335,
                     338..339)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklaipkerr anelrvaatp dtvkkfkalg ldvvvetgag lgaaitdqay eaagasiapd
       61 vkatvsdadi vlkvqrplgp gegdvdemal lkpgstlvav lsphadkari aaygaanida
      121 famefmprit raqsadvlss qsnlagyrav leaayvfgra fpmmmtaagt vpparalimg
      181 agvaglqaia tarrlgavvs atdvrpatke qveslggtfv avmdeefqqa qtaggyakem
      241 saeyqakqka liaetikkqd ivittalipg rkapilvtdd mlrsmkqgav lvdmaveqgg
      301 niegavpgev vekygvkivg hvnlpsripv dssalyaknl ltfltpfikd gklefnwddd
      361 lvkgtaltrs grvvhpsfvt daapaapaps aaqpetdqsv qatppsteag eekpevikvk
      421 pakpdgtpeg qseksqdggt pstgt
//
LOCUS       WP_119688879             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. Marseille-Q5299].
ACCESSION   WP_119688879
VERSION     WP_119688879.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. Marseille-Q5299
  ORGANISM  Pseudomonas sp. Marseille-Q5299
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. Marseille-Q5299"
                     /db_xref="taxon:2942201"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38984
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigvpseta ygetrvavtp dtvkrlvasg hqvvvqrgcg llccvtdraf eavgakvgea
       61 sdafgaeivl kvvapsdqel elisagsvii gmlnpfnsel igkmadrgit afaleaaprt
      121 sraqsldvls sqaniagyka vllatqyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqveslgakf idvpyetdee racaegvggy arpmpeswml
      241 rqaqavhdra kqadivitta lipgrkaptl lntgtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlpa qvgadasaly srnlldfmkl lfdkdgaldi nleddivaac
      361 lmcrdgqvvr kns
//
LOCUS       WP_119694853             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ectopseudomonas oleovorans].
ACCESSION   WP_119694853
VERSION     WP_119694853.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas oleovorans
  ORGANISM  Ectopseudomonas oleovorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Ectopseudomonas oleovorans"
                     /db_xref="taxon:301"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38752
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etvkklvgqg hqvtvqagag isasipdsaf eaagatignd
       61 saafgaelvl kvvaptdael ahmksgavll gmlnpfcndt iarmnargvt afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpqswme
      241 rqakavheka kqadivitta lipgrkaptl lhestvtemk pgsvvidlaa aqggncplte
      301 adqvvvkhgv tlvghtnlaa lvpadasaly arnlldflkl vidkegqfql nleddivaac
      361 lmcnagevvr kng
//
LOCUS       WP_119703041             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aeromicrobium endophyticum].
ACCESSION   WP_119703041
VERSION     WP_119703041.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium endophyticum
  ORGANISM  Aeromicrobium endophyticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Aeromicrobium endophyticum"
                     /db_xref="taxon:2292704"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52798
     Region          13..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msvvgvvses vqgetrvaat petvgkligl gyevvvesga gekasftdaa yteagatirg
       61 taetwgsdvv lkvnapstde iglladgatl vslispalnp dlveqlasrp itvlamdavp
      121 risraqsmdv lssmaniagy ravveaanvf grfftgqita agkvppakvl vagvgvagla
      181 aigtanslga ivratdprae vadqvkslgg eylkvevete qstdgyakat tdayneraae
      241 iyseqaadvd iiittalipg raapvlitea dvasmkagsv ivdmaaangg nvvgsrpgea
      301 vvtpngvtil gytdlagrlp tqasqlygtn lvnllklltp akdgqlvldf ddvvqrtitv
      361 vrdgettwpp ppvqvsaapa aapaaapaep kppkavmtqr aklglvglgi lalflvnaya
      421 peplpehftv ltlaivigyy vigkvhhalh tplmsvtnai sgiivvgaml qigtegtend
      481 tvirvlafva illasinvfg gfavtrrmls mfsk
//
LOCUS       WP_119725936             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_119725936
VERSION     WP_119725936.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35995
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nesfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel vsymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_119716280             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Propionibacterium ruminifibrarum].
ACCESSION   WP_119716280
VERSION     WP_119716280.1
KEYWORDS    RefSeq.
SOURCE      Propionibacterium ruminifibrarum
  ORGANISM  Propionibacterium ruminifibrarum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Propionibacterium.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Propionibacterium ruminifibrarum"
                     /db_xref="taxon:1962131"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54137
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresl pgeqrvaatp rtvpqliklg ysvvveqgag erasypdddy aaagadladt
       61 stvwgsdivm avnepsveel gmmrpgsili tflhpranpg lvealqkagv tgmsmdmvpr
      121 israqamdal sstasiggyr avveaayayg ktfagqvtaa gktapakvlv vgtgvaglaa
      181 vgaaksmgae vfatdvrpet aeqvesmggt flhvrsaagd qgvsadgyak etsddynkra
      241 aelyaeqcqk vdiiiltaai pgkpspklit admvasmkpg svivdmaalg ggncvlthpg
      301 eeyttddgih iigytdmasr lptqssqmya mnmvnlakla tpgkdgqfvi dfddevlrnm
      361 tvtrdgeitf ppppiqvsaa ptapaakaaa apepekpkke rpwwflllvv gllsvalial
      421 ltfapgsfvs lfgtfalacv vgyyvvwnvs halhtplmsv tnaisgiiiv galmqlpkdn
      481 maitiiaalg vliasinifg gfsvtrrmln mfrkgdr
//
LOCUS       WP_119740258             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Noviherbaspirillum cavernae].
ACCESSION   WP_119740258
VERSION     WP_119740258.1
KEYWORDS    RefSeq.
SOURCE      Noviherbaspirillum cavernae
  ORGANISM  Noviherbaspirillum cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Noviherbaspirillum.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Noviherbaspirillum cavernae"
                     /db_xref="taxon:2320862"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38943
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr qgetrvaatp etvkklvaar hdvivqsgag isssitdday aaagaqlgta
       61 adafaadmvl kvrapsaeer aqlksgtvvi gmlnpfdadn taamastglt afaleaapri
      121 traqsmdvls sqaniagyka vmlaantyqr fmpmlmtaag tvkaarvlim gvgvaglqai
      181 atakrlgavi easdvrppvk eqveslgakf idvpfltdee reiaqgtggy arpmpadwmr
      241 rqaelvhera rqadiiitta lipgrkapil igedtvkamk pgsvivdmai eqggncplte
      301 lgktvtrhgv hligepnlaa lvaadasaly srnvldflkl vfdqegnfil nrddeivaat
      361 llcsggevlr k
//
LOCUS       WP_119741360             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_119741360
VERSION     WP_119741360.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38688
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvvdsay etagatigsa
       61 edalgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvivengv ticgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_119750457             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            onubensis].
ACCESSION   WP_119750457
VERSION     WP_119750457.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus onubensis
  ORGANISM  Paracoccus onubensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus onubensis"
                     /db_xref="taxon:1675788"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55662
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkeny egearvavtp asaahlqklg hevfvesgag aragfsnedy ekagvtvart
       61 aaevigavdi vakvrqpsdg eigqmregqt lisffypaqs pellekakeq gitaiamdmv
      121 prisraqkmd alssmaniag yrsvieaann fgrfftgqvt aagkvppaki lvvgagvagl
      181 aaigtatslg aqvhafdvrp evaeqiesmg aefvyldfee qaqdgsatgg yaapsspefr
      241 ekqlekfrel apqmdvvitt alipgrdapv lwtkdmveam kpgsvivdla aekggncelt
      301 ipderivten gviivgytdf asrmgaqase lygnnirhfm tdltpskdgv vvhdmeddvi
      361 rgatvthdhd itfpppppki aaiaaqkpke kpkqltpeek raqeiaafka etrsqvglla
      421 gggillllig flapasfmah fivfvlacfv gfkviwnvah slhtplmait naissiiilg
      481 almqigsgsa wvlilatlav lmaginifgg flvtrrmlam fqks
//
LOCUS       WP_119753013            1122 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119753013
VERSION     WP_119753013.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1122
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122158
     Region          38..1121
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrtlqrtkn slaypafraa laavllllvs vaamaqvtvs gkvtsgedas pipgvnivvk
       61 gstlgtisda dgaytinvps adatliftfv gylpqeasla grttvdivla tdskqlsevv
      121 vtalgiqkek kslgyavqsv sgenlttare tnvsnqlagk iagvtvvgsn sgiggsarvt
      181 irgersidln knqplyvvdg vpisngftga sgrnnlevdf gngagfvnsd diesmtvlkg
      241 gaatalygsr aangvivikt ksgkgtkgig vevnsnttfe svlrlpkyqn vygqgngngg
      301 dfafvnggga gltdgtdesw gpafngqqyp qfnsprtlng qtipyrggdm napagsvitp
      361 tawlndkdgv knffqtgrtl tnnvalvgsn ahgdfrlsyt glnetgtvpn tdlkrntvsf
      421 gggynltpkf sarafvsyik sesgnrpsis ygtenimylf ncwlprsvdv galkdywmdg
      481 qqgrrqfnwn ynyhdnpyft myentngqfv driignlslk ydftpwlslq lrtatdyand
      541 rrqfrrafst qrfpfgqyre nnivteerns dflltfnkei vpsvftltas vggnqlrqks
      601 dflevnapql nipgiynltn sraplqttqt dtkkrvnsly asvqlgyknm lfldlsarnd
      661 wssaltlpqe lktlgigted nsyfyssaal savvtdmvql peaisfakvr asiaqvgndt
      721 dpftftqsyn psdpygssqv ygendrlanf slkpeistay eggldlrffg nrlgvdvtmy
      781 esrtrnqiln iplsittgyn srsinageik nhgieimltt vpiqttwglr wnfdvnfskn
      841 rsevlslsdg lnnfvmasrr vsiearvger mgdmygigfa rvqntdptkp yydasgqsvg
      901 qmvydsqgrp iattdriklg nynpdwlagi nntltykgvk lgflfdvrqg gkvysetqtv
      961 greggiiqet lqgrengyyp qasvqndpql lnapagtyvv gegvnqnadg sfrvndhrvl
     1021 prqwhsawtg grsiaegvmy dasfvklrev qlgytfpdkf fgkvpfrsvs ialvgrnlal
     1081 wtdvphidpe vmsysggtal pgieymsips srsygfnvsl kf
//
LOCUS       WP_119753064            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119753064
VERSION     WP_119753064.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119901
     Region          25..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkfllvclt avfalasgel raqerivtgr llsqedgkpl pgvnvllkgt ttgsvtdadg
       61 qysisvpasg gtlvfsfigl ksqevevgsr ttvdvnmesd vtqlsevvvs algieqnkde
      121 lgtatsqisg saatksgest liaglagkas gvnivknsgd pgagayiqir gqstitgnlq
      181 plivldgmpi ynsstgisat dgmvggtvqq srlndlnpdd iqsveilkga saaalwgtra
      241 angvmvittk kgssqkgkin vslkytrsed kvyithdlth nwgsgslmrf qntptsgwsw
      301 gdyipgrtgg adayitdpaa agyqgyfeda kgnkiynian gtaaaphggk nsqniydykd
      361 qifktgsynd fgvslnggdk ddnfyisidn mkqdgviltn snydrtsfrv ntnkrfnsvv
      421 rigsnfgytk tksnrtqmgs ntsglylggl rtspdfdnsi fegtytdang vkfpdrqrsy
      481 rnplgirtns tydnpiwsqn hnisttdvdr fmgsfelgla plkwldvtar agvdsytdrr
      541 ydfldplsas lpggrldlqt iretqyngdl fgrgkfnisk dfnliamvgm nlnqrtferi
      601 ggyaqnfils shvpldltna gpatqnpyns fqvqrtaaiy stidlafkdq lflnltgrae
      661 sastfgravs stffypaatl awqftqlmds rvlnfgklra gfgqvgvqpt pyntatyyaa
      721 ggfadgwgsq llssaygngg yvesttlgna ylkperktef efgtdlrffq drvslsatyf
      781 tnetkdailp vatapstgfn qktanaatlq thglefdlsa tilkvggftw qingtwsmyr
      841 nkvtslagts slflngfagt ssravegqpi gvlwgvdwmk daqgnlilde rgypqaaane
      901 svignpnpdw kagigntfsf kglslyvlvd rtqggdiwag thgimnnfgr stdtdvqttv
      961 saadaatipv ygtltsgktv aqrytpnadg tytfrgslan ygagnvaleq gwytstgggf
     1021 gpvasqfikk atntrirevt layslnspgf raatkltsid fsltgrnlwi tgpdvkyign
     1081 dpetnltgvs ngrgleyfnn pstrsylfti kiny
//
LOCUS       WP_119753553            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119753553
VERSION     WP_119753553.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116311
     Region          22..1019
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkylltwca lafalfslaq ertitgrvss sedgsalpgv nvvvkgttng tvtdtdgnyk
       61 ltipsgdasl vfsfiglltq evpigdrttl dvqltldvkq lsevvvtaqg iererkalgy
      121 asttissadl ankpetdvgr alqgrtpglq ilnssgmags gskinirgis svngntqplw
      181 vvdgipints tndsntdfrd gniapsrfid idpnniasin ilrglsattl ygslgrngvi
      241 lvttksgass kqqqkfeasv sqsyfviqai lpeyqnkwan gfdgdygeff snwgslfsnn
      301 vavgkhpyye hralfpdhpe fadatgyvpk papnnvkdff kkgsssntsl nlgfkgenss
      361 lnlnyshlde sgyiqnnnmk rdnlalggta nltkklsits tfnfvrteik spptgagtgs
      421 nstggpsvfa nlfyvprnid lmnwpyenpi thasvyyrng ndvtnprwll snaqqtsktn
      481 rffanvslny elaswlkasy rlgldtysek qtywlnkgsv gypteaqlls nglyrsvnfl
      541 ntivdhtfml slnkeiatdl dltgvvgfna rtdtndqsgl essgqvvygl iehrnfsntt
      601 srdfrgnnln rtmrrtwaga yfdmglgykd flyvnltgrn dwsttlekan rslfypgasl
      661 sfipttafpd fasgvleflk lraaygtsan fpepyntrpy lainaqasqd vqgvvstqgi
      721 ptvlanknlk pellteiefg leaqlldnla kvdlsyynrq akdqilnrsl dpstgyqttl
      781 inagsirnkg velgltispf rkgdfhwdvr vnytkniskv eslpegskei liggftnlgn
      841 faiegqpfnv iqgnytvrnd kgeylvdeng nwvisndikv ianpnpkwlg slisdmnykg
      901 infgfqwdyv nggqvysyta atmvgrgvak dleafnpglp lilpgvkqsd gtpndlpvtt
      961 sgmffgnsii ggsandrgvf datrirlrev klgyslpssv ttklgvrgin isflgsnlwf
     1021 rainapkysr adfdrtafgv gngagfdflg gpsarrygvn lritl
//
LOCUS       WP_119753555            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119753555
VERSION     WP_119753555.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117264
     Region          22..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkilltcya lvfalsamaq ertvsgkvts aedgstlpgv nvivkgtvng svtnaegmyt
       61 vtvsgnnavl vfsfigltta evpvgeqntv diqlssdvtq lsevvvtgvg vatdkrklai
      121 avesvgskdf paaptasidq alvgkiagaq isstngtpga etnivlrgin tinrgtspiy
      181 lvdgvqvgat alntidlnai dhvevvqgaa satiygaqga ngviqmftkk gkdgkvhvdf
      241 sssvanntyl nignlhkahy hafvtdgenn vigtsgkplt ldpttlvyse nvqynplstt
      301 svlnkpydkn lqyydhfaff fkpantynns vtvsggkekt dfhftvsnnk qesniiengg
      361 vsrtnfsanf gteiakgltf rsitmlaytk ntiktqdrsi iysinnarpf anfeqldtdg
      421 dvgayfgdav gvnhfnplyy qrntnvkdnk edffqnfnln yklpkfveld lkyglnyqhq
      481 eqrtvyanqt annnatatqs wvsnfapdak geiddyffnk tfqnflgtai isfdfkedfn
      541 snlpiktvtq vaydvrktnn kqylsyglgl ptyspftasq attfvvpaad ivtrsktdpv
      601 yyggdytepf ftygylvnqr vefgevagvs ggfrsdysss fgrgskpftf prgdayfrls
      661 slnfwkdgal agaipdfkir aaygeagiqp kpfdryptlg tkslgtsnsf yipsaqpnpd
      721 lnvevskele igtdfgvtvl qgtnwfndig vsmsywkrst nnaiydvnva psaglgtlrd
      781 nafsieskgf qaalnfaifq nssltwnltt nfskqtseit atngqeivvl ssagstnyvl
      841 kpgekigqly grvalhhvdd kapdgsyfip eaqqanytva sngfvvntat kqpvfsskly
      901 sfgdpnpkfn isfinnmtyk nfltfvfqfd wvqgshlynq tkewmyrdgi hsdyekpiti
      961 ngetgaytaf yrgvyaqgqa ngtkdyfyed asfvrlrnvs vgidlnkvlh insmrklqlm
     1021 ltgrnlltft nytgmdpevs sgtansafdr gvdhntmpny ksyqvglnfg f
//
LOCUS       WP_119754700            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119754700
VERSION     WP_119754700.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112435
     Region          22..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrllqllf lltlasasay aqtvtgtvta agdgtpvpgv svllkgstsg tttdsegkfs
       61 lsvpdpqnsv lvfsfigfst qeiavgnqsn iavvmqedtk elsevvvtal giqreaktlv
      121 yatqtvptgq ltevrdannv insfqgkian aqitqgsggp gsgarivlrg nrsiqgsnna
      181 livvdgvpin nntntaatsd fgsvqssdga sninpddies vtilrgasaa alygssagng
      241 vivittkkgt kdkvtvnins gitsekafvl pkvqnsygqg nagllnsgvg dswgpkmdgq
      301 symndfghtl syspqpdnik dffrngvsln nsigvqggse kmqtylsytn kqvqgiipkn
      361 nlqshninlr isnqiskkfs tdakityisq tiknrprtge enapvidiyq iprsmplsea
      421 snfyettdnt gpipaawpst lssiyqnpyw minrtainqt rnrimgfvsl kyqvlpsvsi
      481 tgranvdrti dadeqqysnk tllwanqegg ydqlaktgit qqwydltlag ehkfgddfkl
      541 dyriggiyqd ylynqdlata nglliynkfs qgfaatntas statetqtqs vfgqaslafk
      601 eylfleatlr ndwdsripsp ytitypsfgl sgiisdmmtl pqpisflkvn anyaivgngg
      661 qpqirtntyt fsqgagkgfl artlteaipg lkfekvknle fgldarfmen rlgltvtyyk
      721 snsinqllki nqpvatgyln kyinagdiqn qgveivlnat pvkgnltwdi aanfglnrnk
      781 ikslsegldi aylgdnagya rtatpviqvg rgygdmvsrm wqrdsngnfv vdaktglpis
      841 tpdqtylgsf mpratlgltn tinykgfslr llvdgrfggv ildgtemnla fsgisevtek
      901 yreggwnlgg vdkdgnkvek tisaqdfwaa gsestsgkry gigeffayda tnfrirelsl
      961 gynipvpagf fiksarfsiv arnlawlyrg sslldipglg krklqidpdm slgngnwqgv
     1021 qygtlpstrs lgcnlnltf
//
LOCUS       WP_119755284            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119755284
VERSION     WP_119755284.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123040
     Region          139..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkifcteklf wlmrmcmfqw liiltfsgvs maidnhaqil etkitlnven inivealdei
       61 samtglkfay ssnviipiek vsinvqdqpl rtifndlfgt rridykireq dnmvflkkqs
      121 pvkkgpltap ltmtsaetii itgqvtdfnn vpmagvnivi kgttngtttd kdgnfsieae
      181 ndhvlvfsfi gystqeiqva nhttinvilq edikslgevv inagywevkn tertgnisrv
      241 tseeisrqpi snplqalqgr mpgvviqqqs gmpgggfvvr irgqnslrad gneplyivdg
      301 vpyngvsfag aassevipng npftalnpdd ienievlkda dataiygarg sngvilittk
      361 kakdgkpkvd vgiysgfskv ghfldllstp qylemrkeal rndktepgfl dpdlklwdst
      421 rytdwqreli ggtayatnak vsisggtkdt qfligggyfr qstvfpgnfn dqkisghvnl
      481 nhnptngkfs fnfsgsylfd nnnllrndit ryitlppntp vpfnedgsln wensswenpy
      541 aflqkpyegk tnnlisslsl kyqiipglfv ksnlgftdtq vkefsafpig ttnpaygint
      601 aisvfstgsi rtwnvepqie ysrpfakavl nvligttflq nrqlgndvea ygytsnavlk
      661 dlmsaaslsv vetrdityry naifgrinln wdkkyllnlt arrdgssrfg pesrfanfga
      721 igvgwifsne nfllensvit fgklrasygi tgsdqigdyq yldtyqatyn tyqgktgivp
      781 arlanaiysw ennkkleval dlglcnnrlq vstsyfnnrs snqlvglalp sitgfnsiqs
      841 nfpatvqnsg leielqsinv khldflwtas anltfprnkl leypnlqgss yantyevgks
      901 lyikkryhft gidtqtglit fedknsngvg tnypadlqai kqitqdyygg iqntlsykgf
      961 qlsiflqfvk qtgysymasp afvvpgrkgn qmtdvlsrwq kpgdvsefqm ftssysskgs
     1021 slyststyag dnsitdasfi rlqnlyfawe fpqtmarrlh mkggklytqg qniftwtkyk
     1081 glspetqsqt mlpplrtiti gfqisi
//
LOCUS       WP_119755939            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119755939
VERSION     WP_119755939.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117070
     Region          23..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkillvcsm claiawsvva qdrtvtgkvt eqdgsplpgv nvivqgtsvg tvtdvdgkys
       61 lsvpsgfnvl vfsfiglttq eidvasrtsv dvsmstdvkq lgevvvtaag iereakslgy
      121 avnsvsgdkv sqksepdllr smqgkvagvn ilsssgapgs atritirgnk smfgnnqplf
      181 vvdgipydng ynvtsnevtd gasyssriad idpnniesms ilpggaaaal ygvraangvv
      241 vittksgssr asrkgleiay ssgfaieqva nlpeyqnkyg tgskgdyaea ngswgpafnr
      301 pgpgvnygld gsttpngsev dsipywssya avfpngpkmv pyqaypnnvk dffkngkvfe
      361 nsitisggne ksvltlvasn lkqdgyiphs sfnktnvslg gqtqlvnglh vggnlsytns
      421 aqrgplsgyg sanqvsasaf srilfpgrsw ditgqpkfdp vtqgnvfflg saadnpywsa
      481 qnngirsnvd riaasvnagy ditdwlnvty kigvntyndr rkeitrkgsv gaaglgqiil
      541 dniyyqeies nllvtinkni tddlslkaii gqninqrtge sqavkgvnsi afdiddidnf
      601 nsvtpfggty yrrrlaglmg dvalgwkdyl flnltgrndw sstlpkskns ffypsvstsf
      661 iftealamdk silsmgkira awskvgndal pyslkatynl nqgnssnlvg alpgndlpfr
      721 ghpgattgtt vydpnltpef sttielgtdl sffqdrinvk atvykinttd qiapialpde
      781 tgfnqiitnf gelsnkgiel gldatpvkla ngftwniygt ythnenivek lspgvdeivl
      841 rnvfggsvtp mlavgkqygm lkgtydvtdd qgrflidpat gatiiskdfh yignpnpkfl
      901 aslgnafsfk gftlsclfnl ryggdlfsat nqfyvgrgvt ryteerdgtf iipgvygdtn
      961 tnkpilvdnk evhnttqvik ndlyfqtagg gfginasdkq sifdatvlrl sevtfgysvp
     1021 kvflkktpfg slsltftgrn lwykapnfpk ysnydpetts fggqnytgie yntapsvkry
     1081 gvnlrvtf
//
LOCUS       WP_119757549             259 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_119757549
VERSION     WP_119757549.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..259
                     /product="STM4504/CBY_0614 family protein"
     Region          <3..123
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 tlycyhnshs devyrrickt lrkeyglftl yahstsylde msnlllktdd krkhidtiel
       61 afnyidtylr tyevtlglep dkaiselnnl fhehglkyry engrivrlrr ikrlknicyy
      121 lyspgeygfv eydlmeaynr lmlndfacvv kechaafrsv llriherkgi vyheqdslnt
      181 lmanlmargv isaeythkfh flsdvlesei flpmapeksh hhyammlris eelacsiyyl
      241 tersiffltq raeedgaap
//
LOCUS       WP_119756233            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119756233
VERSION     WP_119756233.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121109
     Region          22..1102
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrllylsv ifvmigftay gqtvtgtvts ssdasalpgv svllkgsttg tttdsdghft
       61 iqvpegdnsa tlvfsfigfa sqevqvggrt tfdvaletdm tqlgevvvta lgisrekkal
      121 gyatstissd qitaagntnf asalygkapg vrittapgga tsavnvqirg insinakgnq
      181 plyvvdgvmi rnmeqsptgt nnggywddqk irgngildin padieslnil kgasaaalyg
      241 seasngvivi ttkkgtkhng lgvdfnynft vekvaftpky qntygpgydr etnttafgan
      301 eegfiptdvd gdgvnetvrp ifrawaqfgp rmdgrqvaww dgstraysaq pdnykdlyrt
      361 gsssnfniav snstdrgsfr lsytrldykg isrgsdlgrn tfnlnstvkl snkvsadivv
      421 nyinnkihnr peqinrlaan yggffsrady mdvylnkyqt sqgykyvtyd qpqknpaeai
      481 kyniravdll eylwrnvrdn ddeyqdriis sttlnyeiak glklrgrvgn dftsvrneie
      541 rhneyptsfn tssstgsysl stgrysifyt dalltyskdl nqdfafsvmg gfqsrsqnyi
      601 dqkssteggl vqenwfslnn sygvkstssa rtkatmyayl gmvnlsfkey lyleatarqe
      661 ytstlppghn gyfypsanlg fvfsdafqlp sfislgkirv sqariangss pyaanivysq
      721 qtlattqgtv tqlqaannyg nsniaperkt etelglemaf fqnklgldat vykntikdqi
      781 idqslapsng assvlanlge lsskgieigl satpynsgnf rwdtrfsfak svtrvmklap
      841 gmdemtfyna dagavlikak agdvlgdiyt htrdkdsngn yiinsdgyyq mstgnnyekv
      901 gnvlpkgvgg wsntltykgf glnflidyry ggqlvsaphl yaygagmyes tmqyrdaahg
      961 glsynvdgsg nkvlatngqy ndglildgvt ttgekntkil daanyyinsy ywasgwyeke
     1021 gvlkndyikm revsltynlp rsiaqklrfq nlkvsvigrn lfylyrtmkd ldpevaigss
     1081 wqrqgidegs laatrslgfs lngsf
//
LOCUS       WP_119757644            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119757644
VERSION     WP_119757644.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117198
     Region          27..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklyrcmgl plamlllfts malaqnrtvt glitdengtg mpgvnvivkg tsngtttdsd
       61 gkysigvpeg tatlvvsfig yatqevdvgs rtaidvkmas dvkqlnevvv talgierntk
      121 alqssvtqis gdnftqarev nmanglagrv agvnvtkias gpagssrivi rgakslntqa
      181 gamnqplyvi dgipmdntny gqagvwgggd qgdgtssisp ddiqsmtvlk gasaaalygs
      241 raaqgvilit tkkgtarkgv giefnsnfvf dkiynltdwq hsygsgaytg vgslanrvat
      301 kasnpedvqs afdngwydqa wgpkmdgstv yhfdgkahpy syqgdqwdkf yrtgtsftns
      361 laftggsetq nfrfsmanln sksvmpnsgf drvnlslasn skfgkkltlt tkimysneka
      421 knrpnvsdsp gnaiqsvyyi nndynideyr gdpnkpgavw tggptpldgk gngqelqgss
      481 nlwgqnpywa ayqfkntdtr drilasgqlr yditnflyaq vkggmdwstk rgsqltpegt
      541 gyqlpgalte yearareinl eyivgfnktf gkfninafgg gnkmtseyek sdlagngfnt
      601 pflasisnaa sktfnydyrk qginslfgsa eisfqnylfl tatarkdwfs vlnyphnnkf
      661 ypsigasfvf sdafaglpqw lsfgkirasw grvgnafsvv pystnlqytt glthlsrplg
      721 yyssanttnn gnlpnpdlvp yistetefgm dvrffesrlg idltyysqkt tedilnapis
      781 rasgfgttsv nlgeltnkgi ellitgqplr gavtwdisln faknnskivs lipgtnilnv
      841 eeprtrtvfv sqivgqpfgt ltgvkqkvsp dgqliydkdg apltdnnyyv lgkgvpdftg
      901 glnnsftykq fnlaflidfk sggkiysgtn vrmteagfhk qtlqgrdgea pltingvtev
      961 tdasgavtgy epinralapg eaqnywsqlg eraqdhfvyd asfiklrqvt lgynlprtll
     1021 sktpfqtasl sfvarnlail yknaenidpe ssytstnaqg ldyfgmpptr tygfnlrvsf
//
LOCUS       WP_119758252            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119758252
VERSION     WP_119758252.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117950
     Region          22..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskilllacl lgttllaraq ervvtgkvss medgsdlpgv nvvlkgtsfg tvtnadgvyr
       61 lsipgadagg tivfsfiglq tqevaigdrs vidiqlsadv tqlsevvvtg vgvatdkrrl
      121 aisvesvsgd rlptiptasi dqalvgkiag aqimsssgnp gapvsiqlrg intlsggtqp
      181 limvdgvemr stslnaldln nverievvqg asaatiygaq gangviqift kkgkqgpmhi
      241 dasartsvdq vlnignlhqp fnhsfttdan gnildnnggl ltqddlglwg qanwengpaa
      301 qnnkpyqnnt kyhdhiaqlf rnvhtsnynv alsggkensd yafsfsklrq esvvqgvldr
      361 tnfttnvgvd ilknlkfrst tqliytdntv npyyvsnapl ssamytypfa dldykdtdgn
      421 ytyqfggaga nnsnpkyffq yqnfkstvid viptlnlhyt ptkifeldyk lglnysvnnf
      481 aretqnqtgn asslannsfi gesiggglnk svtnnynins lvtgtikfdf dkdlgwkipi
      541 asttqlafdw rkssfhrqyl iytglpsyss iddingaqss snstteyedl fitygfllnq
      601 rfeykemagv sggfrsdyss tygdakspft fprgdaylrl sklnfwdgis svlpefkira
      661 afgeagiqpv gytldaskdl agpvpnhylr ipsyktgtvd ngfliysnpt fanaglkver
      721 tkefeygfdf gitptkngaw fnyiatnvsi wsrkstgvvw qrtqpvsqgs etiwdnyidl
      781 ksqgvqfsvd mdvysgdnlk wdfvtnfgtq sssldrtadg kdiplvwsna atytlkggek
      841 igtiygykal tsidqkdkng dpyinpanaa nyevvngrvv dkagkrvqft pdkyflgntt
      901 pkfnmafinn fsyknfltfs fqidwvygak tynqtkewmy seglhgdydk sltingetga
      961 wtayyksfyd asesngtkdy flenssfarl rnlsvgfdfa kffdmkgftr lqlvftgrnl
     1021 atitnytgmd pessqntsgg gttsaspqva tqrgldfwsf pnfksyqvgl nvsfn
//
LOCUS       WP_119758352            1191 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chryseolinea
            soli].
ACCESSION   WP_119758352
VERSION     WP_119758352.1
KEYWORDS    RefSeq.
SOURCE      Chryseolinea soli
  ORGANISM  Chryseolinea soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Fulvivirgaceae; Chryseolinea.
REFERENCE   1  (residues 1 to 1191)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1191)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1191)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1191
                     /organism="Chryseolinea soli"
                     /db_xref="taxon:2321403"
     Protein         1..1191
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132938
     Region          36..97
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          107..1188
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhvhrytgit grkiklllil lfagfaalae tvgkveslde ylhrleqqhh vsfvydgsei
       61 nrslkiettd atsleaclnl lraidityki vgdqvilqka krppviitge vtelvdgkss
      121 pmvgvsivek gtnngtmtds kgayrvlvkd hatlvfsmvg yktqeiivge ettlnvvlte
      181 dvsvfnevvv tgyqdvdkkl ftgstinlkg sdvkqdgitd vsrmlagraa gvsvqnvsgt
      241 fgtapkirir gatsitgdnk plwvvdgvvl edvvnisneq lstgdtktli gssvaglnad
      301 diesfqilkd asataqygar amngvivitt kkgrvgkpli sytanfstyr kpsyntfnim
      361 nsadqmslyd eldrkgwetf gnskrspngg vyvkmydlid qydktsgafg lrntpearaa
      421 flqgyarrnt dwfdvlfrns fmqehslgis sgteksqlyf sgsylqddgw tiadrvkrft
      481 gnaranfnit dklaiglitq gairvqrapg tvsrrsnpve gkydrdfdin pfsyaintsr
      541 tltpyddqgn leffkrnfap fniihelenn tldltmidlk lqgdvsykir pnlkyaflga
      601 vryaktnqeh kvyehsnmae afradgdati rqnnkflyrn pddpeaepvv vlpyggfynt
      661 tddylvsynl rntlewnktf ndthivrvfg sqelryadrq nkffygygyq fdkggvpyvd
      721 pniikqvveg nfdfygmgmt ydrflagmvn atysyrtkyn lngtlrydgs nrlgksrdar
      781 wlptwnvsgs wnvdaenfma sqsiinrltl ratygltasm gnatnsslvl stnkatrpyl
      841 peiesviniq dlenreltwe kqyetnigfd aaflrervtl tvdwyhrdgf dlisplrtsa
      901 iggqfvksan yadmtsrgie vtlggtlyqg dhsgwkvqlt fahnrnrvtn lkstptiwel
      961 vssdggpkeg ypyrglfsvd fqglnaengs pyfinekget snnvylqsdi tkylkyegpv
     1021 dptitgglyn sfryrnitls alitysagnk irltpafsss ytdldatpke flnrwmtsgd
     1081 ekftnvpsil dlrtlgsldg vnpyavynys dvriadggfv rlkqvslsyl lpeswtsrlg
     1141 atnlsvslia nnpmllyadk rlkgqdpeff nsggvatpip qqytlslkag f
//
LOCUS       WP_119769457             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Noviherbaspirillum saxi].
ACCESSION   WP_119769457
VERSION     WP_119769457.1
KEYWORDS    RefSeq.
SOURCE      Noviherbaspirillum saxi
  ORGANISM  Noviherbaspirillum saxi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Noviherbaspirillum.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Noviherbaspirillum saxi"
                     /db_xref="taxon:2320863"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55347
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msliigvpre ifpgekrvat vpdvveklik lgfsvavesg agdpanfsdd tyaaagasiv
       61 pdaaqlwsts nivfkvraps peevalirpg ttlisfiwpa qnpelmqqla akqvtvlamd
      121 svprmsraqk mdalssmani agyravieaa hhfgrfftgq itaagkvppa kvfvigagva
      181 glaaigaasg lgaivrandt rpevgdqvks mggefvavdy teegsgvggy akvmsegfqk
      241 aqrdtfakqa kevdiiitta lipgkpapkl ittemvqsmk pgsvivdlas eqggncelte
      301 pgtvvvrhgv tiigyadlps rlskqsstly atnllrltee lcknkdgtin vnmddevirg
      361 ttvikegnit wpppppklsa apagqaaqak pavapapkgh ghgasgapas gsriaivfgv
      421 aaalfwliga yapaaflghf tvfvlacfvg ymvvwnvtpa lhtplmsvtn aissiiaiga
      481 lvqvapplam gaerpgdwir wlavigivlt tinmfggfav trrmlamfrk
//
LOCUS       WP_119784135             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Noviherbaspirillum sedimenti].
ACCESSION   WP_119784135
VERSION     WP_119784135.1
KEYWORDS    RefSeq.
SOURCE      Noviherbaspirillum sedimenti
  ORGANISM  Noviherbaspirillum sedimenti
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Noviherbaspirillum.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Noviherbaspirillum sedimenti"
                     /db_xref="taxon:2320865"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38301
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaash avivqsgagi aasipdaayl aagatigtai
       61 eafacdlvlk vrapsadera qirpgtvvig mlnpfdadnt aamaaqglta faleaaprit
      121 raqsldvlss qaniagykav mlaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpyltdeer eiaqgvggya rpmpaawlar
      241 qaelvharaa qadiiittal ipgrrapvli sedtvkamkp gsvivdmave qggncplsel
      301 gktvtkhgvh iigeanlacl vaadasalya rnvldflkli idpagqlaip addeiiaatl
      361 lchggatlrk aa
//
LOCUS       WP_119779202             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Oleomonas
            cavernae].
ACCESSION   WP_119779202
VERSION     WP_119779202.1
KEYWORDS    RefSeq.
SOURCE      Oleomonas cavernae
  ORGANISM  Oleomonas cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Oleomonas.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Oleomonas cavernae"
                     /db_xref="taxon:2320859"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39296
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaipkerr snekrvaasp etvkklialg aevvveagag lsaavtdeaf agagatiapd
       61 lastlsgadv vfhvqrpvae elplmkrgav liaglnpyad rdsvkayada gidafamefv
      121 pritraqsmd ilssqanlag yravidgaae yaraipmmmt aagtvaparv limgvgvagl
      181 qaiatakrlg aivsatdvrp atkeqveslg gtfiavmdee fknaqtaggy akemskeyqa
      241 kqqaltadti kkqdivitta lipgrpapvl vtpemvasmk pgsiivdlav eqggncplsr
      301 pgeivvtang vkivghlnvp srtavdssql yaknllnfit plvsketkql aidwedeiik
      361 asiltkggav vhpafasa
//
LOCUS       WP_119773509             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_119773509
VERSION     WP_119773509.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53831
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgvv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_119784773             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Noviherbaspirillum sedimenti].
ACCESSION   WP_119784773
VERSION     WP_119784773.1
KEYWORDS    RefSeq.
SOURCE      Noviherbaspirillum sedimenti
  ORGANISM  Noviherbaspirillum sedimenti
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Noviherbaspirillum.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Noviherbaspirillum sedimenti"
                     /db_xref="taxon:2320865"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38353
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh aiivqagagl aasipddayv aagatigtaa
       61 qafacamvlk vrapsvdera lmapgtvvig mlnpfdadnt aamaaaglta faleaaprit
      121 raqsldvlss qaniagykav mlaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpylteeer eiakgvggya rpmppawlar
      241 qaelvharaa qadiiittal ipgrkapili gedtvkamkp gsvivdmave qggncplsel
      301 gktvtrhgvh iigeanlacl vaadasalya rnvldflkli idkegqlaip qddeiiaatl
      361 lcsggqslrk aa
//
LOCUS       WP_119785613             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Noviherbaspirillum sedimenti].
ACCESSION   WP_119785613
VERSION     WP_119785613.1
KEYWORDS    RefSeq.
SOURCE      Noviherbaspirillum sedimenti
  ORGANISM  Noviherbaspirillum sedimenti
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Noviherbaspirillum.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Noviherbaspirillum sedimenti"
                     /db_xref="taxon:2320865"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55078
     Region          5..528
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 malvigipre typgekrvat vpevveklik lgfavavesg agdaanfsdd tyraadaqvv
       61 egaaalwaaa divfkvrapd anelalvrsg ttlvsfiwpa qnpelmqqla arnvtvlaid
      121 slprqlsraq kmdaltsmag isgyraviea anafgrffng qitaagkipp akvfiagagv
      181 aglaaigtaa nlgaivrand trpevadqvk slggefvkvd yeeeasgggg yakvmsegfq
      241 qaqremyakq areadivitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 epgkavvkhg vtiigytdlp srlakqsstl yasnllrlte elcktkdgki dvnmeddair
      361 gltvikngev twpppppkls aapaasaakp aavpapkahg hghgapasgt siaitfgiaa
      421 alfwligafa paafighftv fvlacfigym vvwnvtpalh tplmsvtnai ssiiaigalv
      481 qvappleggt grpddwirwl avigivltai nmfggfavtr rmlamfrk
//
LOCUS       WP_119789525            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_119789525
VERSION     WP_119789525.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112178
     Region          23..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrilavlgv illsslsaaa qnrlitgivt daenkgivga sievqgkpfs aisdaegrfr
       61 mnvpegkvtl nvssigfqsq svavqekdtr vavtlvettq elkdvvvtsf gvkkqkkslg
      121 yavgelkged ltknkeinlg nalqgkiagv nvsapvtgps gssrvvirga tsasglnqpl
      181 yvvdgipidn tqqgnagmwg gadkgdgmss fnpddiasms vlkgsaasal ygyrgsngvi
      241 littkkgkng tgigvdfstn ssfntpasll kwqdqygaga pnasgvptrf tnlqelrdsy
      301 yfawgdkydg tpslsldgkt rpyqaygkdn venfyrtgys fsntlaisgg nestnfrlsf
      361 gntkdesimp ettfgrnnva lslnsapnkr isiesnaqyi sekshnrpyl ndsprnpsfp
      421 ttfmtpgsdi rwlsnpydan ggeedflgan vyhtnpyfat ksplnddlrk rfigsakvny
      481 nitdkiyaka vigiddinye yteieptgin ynpggsienr ietrsevnas gflgykgdia
      541 kdisldafig anrqhnrysg ikmkgnnfiv pfkyfygntq pdkteklfse sevnslfysa
      601 digykdflfl sltgredwfs tldpannstf ypsvsssfiy seviglpewm sygkvrvgwg
      661 nvggalpeay alaltyttpd gqtdslgqpi lgvngetipn rtlkpynvst iefgfentff
      721 nnrvstdltf yskkttndit dadvsqasgy rttkinvgei lnkgvefavn vkaiktpsfs
      781 wnvgynfayn hsevlnlsdk ittktlegnr dgranvvlek gqpfgvikay dylrdangni
      841 vlgtdgkflr gnliiagqgv aptsmglsnd fsyknftlsv fvdakfggei ysatnqlgtr
      901 yglseitlpg rengvqvsgt dvngnpvntn vsaynywrsy sdvtsnfvyd adfvklrais
      961 faynfpkayl qktpfqsvsl afsahnlwti ydkvpnidpe tnysnsnaqg merasmpltr
     1021 nygfalnvkf
//
LOCUS       WP_119789589            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_119789589
VERSION     WP_119789589.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110592
     Region          42..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiislnras fafilglllh stevqantig nslfsvrfqs sitgtvsdsr gplpgvtvmv
       61 kgtsiitttd fdgrytiqas kgdilvfsfi gysslektve advldiqlhe qaanlkevvi
      121 nagyysvknk ertgsiarit skdietqpit nvlaamqgrm agisviqnsg mpgggfqvkv
      181 rgqnslrsdg nnplyiidgi plssqsigss vtstnmpvqn splngvnpdd vesievlkda
      241 dataiygsrg angvvlittk kgrqektsfs anytggigkv tgyvdlmdtq qylamrrqay
      301 andkitrypa saydvngkws pdrytdwqke ilggtasynl lqttlsggsp qtqyllsgsw
      361 nrettvfpvd fkssrvnvrm nfnhsskdqk fkvsftsgya yqnsllpstd ltrdaqslap
      421 napdlytadg llnwdngtfs snpaakflrt itgktydlnt gvlfsyaltn slkaklnmgy
      481 tdlrqnqitv lpstafnpal grgsefssay yntlsrsswi iepqlvwdrs fgkaqleilv
      541 gttfqkqdgd qlvcmgenfa snsllenpas asiyrvmess qsvykyqaff grinfnwdgk
      601 yiinltgrrd gssrfgpgrq faefgaagva wlfseesflk glsflslgkl rasygttgnd
      661 qigdyqflnt ytvsgnayqg ikglapsrly npdyswetnk kleaalelgf ledritasla
      721 lyrnrssnql igiplpsttg ftqlianlda evqnsgveft lngqiansay fkwsaafnlt
      781 raknkllsfp glegssyanq fvigqplnii kvyqykgmdp qtgtytftdf ngdgnfsaad
      841 dkkvikdlnp dfygglqntl yfkgftldfl fqfvrqenfn emyrftmpgt msnqpsalvy
      901 nwqqvgdnaa yqgystnnnl kssaytryiq sdavisdasy irlknislsf dlphewtkgf
      961 scrislqgqn vltftkykgl dpeftssgyl pplrifsssl qlsf
//
LOCUS       WP_119790434            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_119790434
VERSION     WP_119790434.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115766
     Region          32..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiklkryaw icillisiav kaqdtkpliq sklegtvvda itkepiigas vtikgtthgv
       61 vtdtdgkfff qtgqkfpytl lisylgykke evvvnknait islteeqnal sevvvtalgi
      121 skekkslgyt tqalkgkela ttketnflng lsgklagvri tnsqgdmgss riiirgetsi
      181 agnnqplfvv dgvpvdnsql nfggatrdfr naiadlnpqd ietltvlkgp naaalygsra
      241 ahgvvlittk sgkgqksgyg vtfntgitvs qvatlpsfqn tfgqgsngrf syvdgkgggv
      301 ndgvdeswgp rmdgrlipqf yskgeavpfv ahpnnvkdff ntgltydnsv siakandkgd
      361 frlgvnnqkq lgtvpnsein ktnftintny qisenvkvgv nanyivtnap qlpggpsggr
      421 aagvmlqflw fgrqvdinel dkdwntnwnn syysnpywna yynttsqqrn riigdvhlda
      481 klaeglnfrf rtgvdyyndr rkytikygtn gtpfgsyaed aytvneqnte gifqytkqln
      541 ddfsldalag fnirnhsdan nyqkaprlav pdlytltnsr dpltssnsls rlrvysayas
      601 aqvgfrnyaf lnvtarndws stlpssnrsy fypsfngsvv ltdalnikss tldflkvrgg
      661 wsevgndadp yqlstvynfq tafdgnpiqt ssqkklnenl kpettrstev gleasfwknr
      721 lhfdvayynt nsfdqileik ttassgytsq linagkinnq gievqldgnp vqtenfkwnv
      781 avnysknksk veildyagdi knytigssgg vdvlasvgqa ygalygtayq rdasgnivvg
      841 anglpkadpt kkvlghytpd ylagltntlt yknlelsfli dasvggelfs gtnrtgnytg
      901 vlaqtlpgrg aengglsyyy pgnntanpkt lvsggaapsg vtvyddgmif ggvfadgtpn
      961 nkvisaqeyy kasyniseay iysstfvkmr eikltynvdk klvkklgleg asitaagrnl
     1021 ffiykdapni dpetafntgn aqgleslalp ttrnfslnln vkf
//
LOCUS       WP_119790840            1009 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_119790840
VERSION     WP_119790840.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1009
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111382
     Region          45..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnfsfyrgg rayyclifvw lcmsfsslfa kssyrqtnlf pqqhqiqgtv tdgtnplpgv
       61 tisikskknn avisdysgqf siscsphdtl vvsyisfktv mvpikgrklv dvqliydstt
      121 lqevrinagy ysvkdkektg siaritakdi ekqpvsnvla amqgrmagvs itqttgspgg
      181 gfdiqirgrn slrssannpl yiidgvpyas dpigvtatsa vlyggtspls glnpnqiesi
      241 evlkdadats iygsrgangv vlittkkgsm gdtkysakys rgfgsiahfa nlmktpeylk
      301 mreqafkndg yqsfpteafd vngiwdknry tdwqetllgg iadfidaqas vsggsnttkf
      361 figagynket tvlpaefayq krnlrvnlnh rspnqkftld ftagytaqgn nlpsldftsq
      421 armlapnapa lytetgdlnw enstfsnpla alegkyrgqt ydmvsnavlg yrikpnlqir
      481 anlgytalnh eesttipsti ydpsygvgse fsilnitntt rrswiaepql nykrdygnla
      541 ldllagatyq nldsgiltlr gtgfpsnsmi hnlgsatnvv vasnsetnyk yqafffrani
      601 nydskyilnf tgrrdgssrf gannrfatfg aigaawlfgk enwfkdsrti sfgklrasyg
      661 ttgsdqigdy qflntytttn vnyngiigla psrlynpnfg wetnkkleva ielgffndri
      721 fitgawfrnl sssqlvgipl pgttgfssvq anlgakvenk gieltlrtin irhsnfewst
      781 slnmsfldnt liefpnlqgs tyanqfvigk stnirkmykv kgvnpqtgiy efldynndgi
      841 itasdrqhva dftpkyfggl qnslryknfq ldilfqfvkq snysftvssg ppggmvnypa
      901 elnnswtqag dntslqiftt ginsaaiaay drfsssdaav vdasyirlkn fsfsyklpsd
      961 wlksiecrli aqgqnlltft kykgndpefi gngylpplrt vttgiqldf
//
LOCUS       WP_119790911            1236 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_119790911
VERSION     WP_119790911.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1236)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1236)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1236)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1236
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1236
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=137400
     Region          143..1235
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkpvvkqrl lhqimkitlf qfvlalvfss vtlannvngq kkldtkvtit vdnltldnal
       61 skieksahvk fsynsrlpql gekvsieanq etlssilnri lvpfnitfse vsnqivlqks
      121 avsfsnsnnh dslfeilafg piikgkvtdq sgsplpgatv lakgtktavl tdfdgnfsie
      181 mpanvdrlvi syvgmetkei gisnptptvv lteagqnlke vvvttgyekt skrtftgais
      241 kisgaelkvd gvvdvsrmie gkaagvtvqn vtgsfgatpk itvrgsssif gdtkplwvid
      301 gvvqediinv tfadlasgns atllssavag lnandiqsie ilkdasatsi ygsrslngvv
      361 vvttkqgrrd splkinysve ntvrtvpsyt qfdilnsqes msvfqemrtk gyldqssslt
      421 arfsgvygil akqinlydss ngqfgvrneq pyinqflkky elantdwfkv lfrpsitqnh
      481 slsfsgggkn ntfyaslgyy tdpgwtvadn vkqlsanikg tfyindklni tlstlgsvrd
      541 qeapgtyesk ndvvfgkvtr dfdinpfnyv lstsrtlrpy dengnleyyq nnwapmniln
      601 elenntldik vndirfqtdl dykinknlty nltasaryan tsrehkiyen snvvgaynag
      661 vgetlntqiq kdnvflyqnp ndltapkvsv lpnggflrky tndmtsynvr nsityrntfn
      721 ekhelegffg tefrsvdrnn dnftaagiqf ekgltafidp klieklvneg nsyydfgaer
      781 ertvgffgkv gytydrryta sftgrydgsn rqgdtgssrw lptytvsgkw nikeenfmkd
      841 vesvntlalr asygltatag patnslaiyk sfitdrfavg drenairied lqnkdltwek
      901 qyetnigvdl gmfrnrvqft tdvysrkafd lidyvitsgv ggqsvkqgnn admetkglei
      961 gfttqnivsk dfkwsstvnf siydqkitkl ankpavfdli atnggntvgh prnslysyqf
     1021 tglnneglpt filqdgaenn iteanfqdtn dvtkylkyeg svepnksigf antftyknls
     1081 lyvfivgsgg nkvrlnpvys ntyndqtvft kdfanrwinp gdenytnvpv iadkllnrny
     1141 gandlqiayn tynfsdvria sgdfvrlkni slgwefpsdy krklglttfn lkasavnpwl
     1201 iysdkklngq dpefrntggv afpitsqytf ainisf
//
LOCUS       WP_119790612            1186 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_119790612
VERSION     WP_119790612.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1186)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1186)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1186)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1186
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1186
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132456
     Region          52..118
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          132..1185
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkhnseky fseryhyyly lllmrsvtaf iwismcslya npslgqnkih vrfkntplte
       61 vfstlekqtn yvffynddvl ksantitldk datleeilnn aftnnnltfd iidkqvivkk
      121 nkkkaeqley eltgkvtdkn gapmvgvnvv lkgkqtwdit rkegdyrmrv spydtivfss
      181 lgyktvtvav nnkrvinatl vpdvmelhsv eipvsngyte ipkervtgai gvmtakelae
      241 vptvdiqsrl egklagvnvd prtgsisvrg tnnfsgtgsp lividgfpqs redfafskrg
      301 vpgtsilsfl npddvesitv lkdaaassiw gsmaangviv ittkkgkkge ptinfnttts
      361 igekidlgkl rvmntaqyid yekdlvnggf vvdnisnwqa lnpsaaqeim frqkrgeitv
      421 aqrdqllaql gqndnlgqin ryllrnsvtt qydlsinggn ekstyylslg ynkdqaamqg
      481 ndsksynitl nnsfqlksfl klntginyvp ttyqtntvan ealsnvsata lrpydmiade
      541 ngngisryyl frpevskafe akgylpwsyn fldelnysnv itkganirln asltatvtnw
      601 lnfeasgmyt sitnktksln eldsyytrnm inqatsvnta gklvygiplg sylyntnann
      661 dnqsmrfqmn inknfnenns lhflagtevr eerresssqr yygynvdtns gqsvnptvyy
      721 ttvygwqsii gasdnnigks rsrylsyygl gsydfmnryh vsgsvrfdda niigaskknr
      781 alplwsaggk wdinkesflr dvswlsslaf ritygkggss paggfgsqsp visiggvdfn
      841 tqlptasisi penpeikwet tttlnygldy gffnnrlrgs vdfyykkted ilanlpfnpt
      901 ygwsfvnynt atlkghgvdf slsgaiinaa fkwnstlnfs yntnevtdsr yvlnstnqyf
      961 gsspmvgnsi gtvyaynwag ldatgqsqvy kkdgtiikst qgitaidkdd lkkmgtsfap
     1021 yfggfmndfs fknfrlgvqi tyyaghvfrn tvlqnypsys gvqygavakd elvaerwrqa
     1081 gdeattnvpg ltninfnsln ryqyadinvl padnirlqqv slsynvpgqw lektfikals
     1141 fnfaarnlgl lwvkndlgid pqylsngnyn tlapqrnytl qfnlsf
//
LOCUS       WP_119791237            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_119791237
VERSION     WP_119791237.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116822
     Region          27..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkinfrki avlffvlltk ltfaqdrvvs givsdengvp lpgvsilvkg tqngsqtdfd
       61 gkysikaean avlvfsfigm qtkevqardk nvnvkmsags tqlqeivvta lglkrekksl
      121 gyatqeingd qltkintgnv snnisgkiag veirrnnnig gstnvvirgt tsltgnnqal
      181 wvvdgivlnn dntnsadqks ggnvggydyg naasdinpdd ietmnvlkga aatalygsra
      241 sngviivtlk kgsktkgglg fdfssgvnvg vvdkktlpey qnqygggygd fygtvdlgsg
      301 vhpytatdda awgpkfdpsl lvynwnsfyp elptygkatp ytavknnpns fyqnsltyin
      361 siafsaandq gdfrfgytny nqqqgilpns nnrkdnfnfs gsykvtpktr istsanylts
      421 naigmnetgy gdggnnylss vrqwyttnad fgdlkeayei tgknttwnvg spdnlavqfh
      481 dnpyfqrynn ynslkrdrff gnvvvktevt nwfdimgrga vdfyhqlqee riavgskrtp
      541 nalgqysryd knfreinldl vlnfktsitd ginfngmigg ntrrsvnnsi yavtngglvv
      601 pgiyaltnsi dpinspdemq qtlgtnsvyg masfnfldty flegtyridq sstlpkdndt
      661 ysypsitaty ifsnhikadw lsfgklrlny aetgndapfa vtstlypknt nfgpggirfs
      721 tdnsrsnsdl kseltkgvea glelkffknr lgvdfsyykt nttnqilsie tptqtgytra
      781 winggdvqnk gfevtvnatp iktkdfswqa tvnwstnkne vislggasqi slgsfqgvny
      841 vaevgkpvgq lvgsgftyln gekvirsngr ylqsagvvig nvapdwiggf nnvltyknia
      901 fnflidvkkg gdvysldqqy ghttgiyest vsnnhngvpq repvaqgggi lldgvkqdgt
      961 pnnvtasvtg tdgyyfynsm pqqqyvydas yvklreigls yklpkrflen tfisnmvfal
     1021 ngsnlwiihk nlpyadpeag assgnlqgfq tgvlpttkey sftmkvqf
//
LOCUS       WP_119791353            1122 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_119791353
VERSION     WP_119791353.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1122
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125067
     Region          55..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnfirikmg pngvsgfslk tklmlfcilf slsqvhgytl sskgaaksqn vqqqknitgq
       61 vndengmplp gvtilekgsk naaltdfdgk fslkvenena vlvfsflgyt ntevsvkgkt
      121 ivnvkmqrtt asleevvvvg ygkmkkkdlt gavvqvspdr lvnqnpqtvq dilrgtpgvr
      181 vgydpsakgg gniqirgqts vytagghnsp liildgmqfy gelseinpdd iaqldilkda
      241 saasvygsra aagvilistk kgktgkpmvs fstnttisnk sayrkvyspe gylkyredwe
      301 taqtygvnta tgqyeafiag tvangkpgyf snpndlskwg iteaqwlayq pasqttgkss
      361 kevwgarlgl nfdpslmanf lankthdwsn ssfrtginhd nnlsisgaad rvnyyvsfgy
      421 lksegaivgn dykaarsnmk vdakvtdwld lgvnvnfqdr sdgdvtpslg tnagdnnmmr
      481 tspfgtfida ngnyerqpmg knvsgqnyny yyerqfidke tgyttlntif nakvtlplgi
      541 tyafniapry qffhdryfrs tqnpnwpaat tgvnrnnstr fdynlnntit wdytiaqkhh
      601 iiatfvqeae errfwsdgmd ayniqpsdal gfhlvntatm ansalrsndt hetadalmar
      661 lfysfdnrym ltatvrrdgy safgasnpya vfpsfgvawn fknekwfnwe pmstgklrls
      721 wgkngnrsla dpyvslanlv ntgtmgylda sgkaleikyl aldrmanpnl ewekttstni
      781 gldlgflrdr itatldfyka sthdmimsqs lpgftgfsti atnlgevqnq gfelslntln
      841 mkkpyfewrt sfgisynenk ivslygnmvd vkddngnvig kkegndsang wfigrpisqi
      901 wdyrvtgiwq kdewkeaqky gqrpgdpkva nsytaddida vdsdgkpykk avynekdkqf
      961 lgnsnppvqw mlrndfkiyk nwdldismya nmggkslnsn ymntfndasl ykfnfnpyvn
     1021 pywtldnptn dwarldakgp agtpvapgrl ydrsfirldn islaytlpkd lmdkvhiksi
     1081 kiyasvqnva twaaskewky fgdpetggla trqfnlgfnf ql
//
LOCUS       WP_119792148            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_119792148
VERSION     WP_119792148.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123758
     Region          22..1111
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkilhalll flaiagysqe srtitgiiqd eadlspipga svfvennsis nktamagiih
       61 seaigttsdf dgkftlkigk nvtslrvtfm gyksytlels aqknytvnlt setaklqevv
      121 vtgyqkiekr kltaavskid msaiqqtgvs sidqllvgqi agvavstpsg apgapakiri
      181 rgtaslngtq dplwvldglp legndvpkny dkdnidqlnn fsiaglnpdd ikditilkda
      241 aataiygara angvivvttk kgkagkmvis fntntfitqr pdfdklnlmn asqkvdfelg
      301 lasradltyr ddageisril ngsnelaayr aggfsalspa tqqsindlrk nntnwgnliy
      361 qtaintqhgl slsgggeksd yyfslgyyde kgttigtgfk rynltlknnf eitdkfkvgv
      421 gifgsenktt syltdtdayt spssysrnvn pyltpynadg sykydqdisg ysdryvpfni
      481 leerantshd lktraikall daeykitrdl kvtsqlglql dnsssekfad kntyytrkek
      541 ersryftnga fnyflpeggi iqnantdffq ynlktmvnys ktfgekheie amvgnelrrn
      601 ytttiatkgf gfdkntlttk pimfpnssfa ndaiyrtyqk senenafasf fatasytynk
      661 kysvfgsvry dgsdlfgvdp kykylplwst saswavseed flkdnltlsn lrlrasyglq
      721 gnidkntspf vmgrysntti lpgqteqtis vesppndklr wekttntnlg mdlglfnnri
      781 sivtdfygrk stdliglrav pfengfeysn mnwaqvsnkg yeitlstrni drpnfkwnts
      841 infshnksnv drievrdtdl lpsregrpvn avfglktngi dengyplfvn kngetvntqt
      901 ffklydpyad ffpgeltess ltpaeyrdlf vylgdrdpkf tggitntiqv hnfdftvaaa
      961 fnlkqtvvkt ppysgtevdr gqnystdiln awsptntssn lpgivgkdsg tgdswmayqw
     1021 fssgtpldwn kyldtwvsem symrlssmrl gytfpkaftd hiniqsirls vearnlfvis
     1081 sdfkgyfdpe tygniyaqpv pksftigcnv tf
//
LOCUS       WP_119792953            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            anhuiense].
ACCESSION   WP_119792953
VERSION     WP_119792953.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium anhuiense
  ORGANISM  Flavobacterium anhuiense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Flavobacterium anhuiense"
                     /db_xref="taxon:459526"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116160
     Region          25..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqklkglmm lffililqss iaqekkitgv vsdnagiplp gvsvlvkgtk lgtqtdfdgk
       61 ymikassnqv lvfsyigmkt seitanssvi nvkmldagaq elesvvvtta mgikkqkrsl
      121 gyatssvsak dltdvtnvnv feslsgkvag adittpaqag asskvvirgf nslsnssply
      181 vvdgtpinns sngggttadg ksinstrsfd agngisdldp nniesmsilk gaaasalygs
      241 raangvvlit tksaknkski sidfltstdf nqvarvphlq nefgqgwsgl systwsgvan
      301 anntasneng swgakyngev rpwgaiingv qqakpyvalp nnikdfyttg ttftnsmris
      361 gggensnfsl nastvnsdgi fpttadaykr ntlginagis tgkftvrtsv nyinknqnvv
      421 ntgqggtegg tvaqalaqtp rdidvvglkd yknnpyntps nlyspyidnp ywdlqenstn
      481 ikgnrffgnv nlsykitdkl tatyqiggdy rnekiksyga imdyfpgsan adaskapvvg
      541 gvtektaeni etdtnfnlty vtpvgkdfsf ngmigfntnq rsgsslkanv tnldvpnfye
      601 lsnsilspiv vqddylrrsy gvfasveasy kekiyltvtg rndwtstlpq gknsyfypsl
      661 slsgvvldnt qhfvklrgsi asigndtgyy qtkssmipan aalgfgnill piggvngyel
      721 sgnlgnpnlk pertteyelg fesnffnkrv nldfsvyhkk ttdllfsrpl aastgftsqt
      781 dnildlqnrg vevvlnvvpv kvkkfqwdft ttfsknvskv ldiaygldkl tlasmygvnf
      841 vaekgqplgm ftaftprltp dgrpivspst gyytvgndqs nvgtsqrkfv mglrnnfkyk
      901 nftlgssfdw kqggkmysyt krinefsgng iettfndrnt yiipnsviev kdatgnitya
      961 entvpmttsk vtsfwntssn pgieaghvid ktfirlrdlf ltynvpttfv qkfkiatasl
     1021 siygknlfmw tpkanpyvdp elstygdgll seagefatnp sqrsygasfk vtf
//
LOCUS       WP_119806936             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            sp. JM45].
ACCESSION   WP_119806936
VERSION     WP_119806936.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sp. JM45
  ORGANISM  Paracoccus sp. JM45
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus sp. JM45"
                     /db_xref="taxon:2283626"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55259
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkdnh pgearvaitp asaghlgklg hevfiqtgag igagfsdedy tkanvtvcas
       61 saeligavdv vakvrqpsea eidqmregqt visffypaqn aellakakdq gvtaiamdmv
      121 prisraqkmd alssmaniag yrsvieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtsvslg aqvyafdvrp evseqiesmg aefvylefdq ptadgaatgg yaapsspefr
      241 ekqlakfrel apqmdivitt alipgrdapv lwtadmvaam kpgsvivdla aekggncelt
      301 vmderivsdn gvvvvgytdf psrmgaqase lygnnvrhfi adltpkkdgv idhnmeddvi
      361 rgatvvhdhd vtwpppppkv aaiaaqkpke kakvltaeer raaeaaafka dtkkqvgila
      421 ggglllllig lvapvsfmsh fivfvlacfi gfrviwnvah slhtplmait naissiiilg
      481 almqigsgsw wvvllgalav lmasinifgg fmvtrrmlam fqks
//
LOCUS       WP_119809947             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Massilia
            cavernae].
ACCESSION   WP_119809947
VERSION     WP_119809947.1
KEYWORDS    RefSeq.
SOURCE      Massilia cavernae (Mokoshia cavernae)
  ORGANISM  Massilia cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Massilia cavernae"
                     /db_xref="taxon:2320864"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38653
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr agetrvaatp etvkklaakh qvvvqsgagv aasnideaya aagatigsaa
       61 dafgcdvvlk vrapnaeera lmkpntvvig mlnpfdaeti aamaasglta faleavprit
      121 raqsmdvlss qaniagykav mmaanayqrf tpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpfisdeer eiaqgvggya rpmpadwmrr
      241 qadlvherak ladiiittal ipgrpapvli seetvkamkp gsvivdlave qggncplsel
      301 nktvvrhgvs iigepnlasl vaadasalya rnvldflkli idkdenlaid redeilkatl
      361 vcaggevlrk
//
LOCUS       WP_119815395             429 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. DCY119].
ACCESSION   WP_119815395
VERSION     WP_119815395.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. DCY119
  ORGANISM  Mesorhizobium sp. DCY119
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Mesorhizobium sp. DCY119"
                     /db_xref="taxon:2108445"
     Protein         1..429
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43891
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtifvpke vdlneprvaa spdtvkrlaa lgfdvvvetg aglasriida eftaagakig
       61 ktadaakadv vlkvrrpsda elkgyksgaa vlaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgaae ydralpmmmt aagtvpaaki fvmgvgvagl
      181 qaiatarrlg givtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk agsvivdlav erggnvegav
      301 pgkvvttang vkivghlnvp grvaasasll yaknlfafle tmidkgtkql ainreddlvk
      361 atmltdggkv vhpnfanaap apaepaakat rtaeakseaa pkkaaakkpa akkpatvkpi
      421 vpgknrgda
//
LOCUS       WP_119832367             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum cavernae].
ACCESSION   WP_119832367
VERSION     WP_119832367.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum cavernae
  ORGANISM  Azospirillum cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Azospirillum cavernae"
                     /db_xref="taxon:2320860"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39807
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,102,299,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,135..136,145..146,149..150,153..154,156..157,
                     159..164,166,168..170,173,196..197,289..290,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,135,138,141,182..185,205..207,239,250,
                     267..269,276,278)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(132..133,135,145,188..189,196,212..213,215..218)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(165..169,172,175,198,200)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvaipkerr agelrvaasp etvkklkalg levvvesgag lgsslpdavf eaagatiaad
       61 aasalndadi vlkvqrplls gegsdgvdel allkkgallf ailnpynsrd hvkayaaagv
      121 nafamefmpr itraqvmdvl ssqanlagyk avvdaageyg rafpmmmtaa gtvpparafi
      181 mgvgvaglqa iatakrlgai vsatdvrpav keqvqslggs fvavendefk qaetaggyak
      241 emsddykrqq aalvaehikk qdivittali pgrkapilvt aehvasmkpg svlidlaveq
      301 ggnvegsklg etvvtangvk ivghanypsr iaesasllya knllalltal ndkdkgvtin
      361 wddeivkaia ltrdgavihp aftg
//
LOCUS       WP_119837056             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Actinomyces].
ACCESSION   WP_119837056
VERSION     WP_119837056.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53623
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrtgipcekp gqalvaatpq tvsrlvrlgy evhvqrgagq aasfpdsaye eagarvtdea
       61 qvwdcevvlg vdapdeehla lmspgttyvg rlaparsprl vealrarglt glaldavpri
      121 sraqamdvls sqanlagyra vieaaahfgr vftgqvtaag klppasvyvi gagvaglaai
      181 gtasslgaqv rgtdvrpeve dqvrsmgatf ipvpsapghq eassdgyarq msaeqaelaa
      241 alyakeaaqa divittasvp grqapvllsr aalegmrpgs vvvdmaaang gnteltvpse
      301 vvltdggvti vgytdlagrl ptqasqlygq nlvnlltlmt pakdgvlrld ledqvvrgit
      361 vthageilwp ppavtvsaap tagagtvppa tqapdtsaas qeaaqnrars aararraglv
      421 aaalalaalv lvtpvavash yivlmlavvl gfyvisnvtp alhtplmsvt naisgiillg
      481 aisqvgndnl lvsavsflav vlasvnvfgg favthrmlam frkd
//
LOCUS       WP_119839684             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudooceanicola algae].
ACCESSION   WP_119839684
VERSION     WP_119839684.1
KEYWORDS    RefSeq.
SOURCE      Pseudooceanicola algae
  ORGANISM  Pseudooceanicola algae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudooceanicola.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudooceanicola algae"
                     /db_xref="taxon:1537215"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55624
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtptevf egearvamtp dsalqlqklg hecfiqsgag qkasftdaay eeagvtvlpd
       61 aatlfdtvdi vakvrapsdd eakmlksgqt lisffnpagn telldlckdq gatvlamemi
      121 prisraqkmd alssmaniag yravieagnn ygrfftgqit aagkvppakv livgagvagl
      181 aaigaatslg aityafdvrp evaeqvesmg aefvyldfee eqtdgassgg yasvsspefr
      241 eaqlakfrei apemdivitt alipnreapk lwledmiasm krgsvivdla aekggnaegt
      301 vpdekivtdn gvtiigytdf psrmasqass lyatnirhlm tdltpakdgv vnqnmeddvi
      361 rsatvthgge itfpppplki kaiaaqkpke kvkeptpeer raaetaafkk qtrnqvtllv
      421 igaalllgvg lvapasfmqh fivfvlsvfv gfqviwgvsh slhtplmavt naissiiilg
      481 almqigsgsw ivillgslsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_119841590            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_119841590
VERSION     WP_119841590.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109174
     Region          32..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnrygpafa lllagvlali svgpavaqte ytiegqvtde stsevlpgan vqiegtnfgt
       61 atetdgefsf taqlqpgeyr vrvsfvgyet atrmveltdq evvtldpfql gvsaarvdev
      121 ivtgqagpte rkelgnaiss ieaaklqdtp ksstlqslqg klagvrvqqs sgdpaggtdi
      181 rlrgtgtvlg aasplivvdg viisndspel iqvggttqnr lidinpndia rievvkgaaa
      241 aalygsrann gvvqiftksg qegetevtys trvktqavrk tldvnmaqne qgqfldnsgd
      301 plpegqrrfd fqdfifdray gteqylsisg ssgdtrffts ggylgsqgiv desgfqrfng
      361 tarlqhtvnd wfnvsagary afsksddvpn gglntlygal tgfifgpntf dprpneagef
      421 pddaafsnpl evqsrfdfgq ttdrfigdiq ldltpfdgls idytlgldty dqtgtafipr
      481 gvstpgfetg fsrraelsnl qlnsdlnvry easirdglts tsliggtlqh eseesfnaqs
      541 qdlppiaetv gggtssrefg efrspltvyg vfgqqsfgla drlfvtgalr ldasssfgeg
      601 drwqlypkvs tsyviseqdf wrgaigsvlp sfklrgsvgw sggltsigaf drftvynaqs
      661 fdgnpglqpa pqlgaqgvrp erqreievga dfslisdrls veftyynqrt edllltksla
      721 pttgfntela nigtvenngi elrargvaln rsdvrwvstv tyarnrnevt gipgetgrvi
      781 ipssfrvsaa qngepigsyf ggafarnedg evidtegnpm redddgywrp kncdvsesgc
      841 sgiparaeqd qiignpqpdf tlawanqvev gdnlsirfqv dgefgqdvfn ftrrigafps
      901 fgtledyere legdlpsgyg sgvfnifenw vedgtyvklr evavnytirl galpvesvrl
      961 naagrnlfsi ddysgydpev niggqrtgvr gfdfvvppvp rtfslgatit f
//
LOCUS       WP_119841793            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_119841793
VERSION     WP_119841793.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114332
     Region          29..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrysvlllg vllgalcfsp tssaqdpatv rgvvtdstga plpganvrvq gtqtgvsada
       61 dgayelaavr pgrrtivfsf vgfekvsrtl elsagdtrtl ditlgtgtvg lenvvvtalg
      121 vdreerslgy svervsgsdv aeapepnvmn nlsgkvagln vtggsgglas tprvtirges
      181 slagsnrpli vvdgipidnt pntqgsdaqt tqvdfgngls qinaqnisem svlkgpsaaa
      241 lygsraadgv ilietkdgse tdgigatvrt svtasrplrl pdyqneysyg nggefayvdg
      301 tnapgwnwgv rmdegverpq wqgprneage liptevtsap nkvrnffntg tnvstdvavr
      361 gggenssfra slsrsdrtgi vpntnldrts tslsasydvt daltvdanan yanttsdnlp
      421 ssgygsesim yyftwgarhv endllkdywq eegtqqahyd rnwtnnpyfq vnentngler
      481 drlyggvsar yeftdnlnlr artgldysnq gtkqrkafss itapngwlqe adrtftewns
      541 nlllnytrev gdftfepsvg anfmrqtrrn vqltaqalsv pdvynignar snvqaderde
      601 aqeilgvfas gtvsyqdmlf ldltgrndws stlpldnnsy fypsaslsvi vsdlvevpef
      661 lplsfakvra swaqvgndtd pfrltntytf gdawgstqtv vseadlanan lqpeitssye
      721 fgtnlrfydg raqldvtyyr sttrdqilsv plaqstgyns rlvnageirn tgvetrlqls
      781 piqdwsgfgw dvslnwtrnr stvveladgi dtfvlgegpf ggsaqaregg rmgdiygrvf
      841 drvedpnsph tgeiiyedgl pqltddvekv gnynhdwrgg igstfsyenl qlnvlfdvrk
      901 ggllysntha tgieggsleg ttrarnetvv gdgvvqnddg tysenteeae yvtwlrtyyd
      961 rpnvesnsfd atyvklrels lrynftpdwl tragvqnvgv svtgrnlflw tdvphvdpet
     1021 tisggdgqip gfevqqipst rsfgmnvqln f
//
LOCUS       WP_119842146             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Salinibacter ruber].
ACCESSION   WP_119842146
VERSION     WP_119842146.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40410
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maltigvpre tepgetrval vpdvadrlla tvddldirve egagqgayht dadydaagcs
       61 vvgrdatfda diiakvapps ddevdrlgee qvlvgflspl erpetaqala drgvtalame
      121 lvprisraqk ldalsamssi ggyraaigaa erlpaffpll ttaagtvrpa rvlvlgagva
      181 glqaiatakr lgakvfgydi reptreeves lgasfvelev dieadqdesg yaeqvekekq
      241 erqpellqph laeadvvist alipgqpapl lineeavaam dpgsvivdla apnggncalt
      301 etgeeivahn vqisgptnlp aempvhasel yaktvaamie egleadafap dfddeifaes
      361 cltrdgrvqn drvrgllgta eeaka
//
LOCUS       WP_119842179            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Salinibacter
            ruber].
ACCESSION   WP_119842179
VERSION     WP_119842179.1
KEYWORDS    RefSeq.
SOURCE      Salinibacter ruber
  ORGANISM  Salinibacter ruber
            Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia;
            Rhodothermales; Salinibacteraceae; Salinibacter.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Salinibacter ruber"
                     /db_xref="taxon:146919"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116248
     Region          27..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlipsvvf glallllpgl awaqqgtvtg titeaetenp lpgatvqvqd egtgaasgsd
       61 gqyriegvpa geqtirvsfv gyqpqertin vpaggtiran fqlrtsqael devvvtgvat
      121 gtdteklgfd vaqvsgdals evpatdpana lrgkvagaqi aegsgapgvs psiqlrgats
      181 itgdrsplvi vdgvitsggl sdismqdvts ievtkgaaas slygslagng viqiqtqdga
      241 qtgnldvtvr sevgasqvag dypsatrhpw tvegmevqlp ngdtetvsgd naqeqvrnfp
      301 dgtkilswpg rsnetfdeee dgtrlfdnpf pstfnnvena vtsklnttnf vsiagaqeef
      361 sykvsyenfq qdgilepvgs ynrntfrfng dyspegrlsv sanasyvtss gpvieeqgqd
      421 dnyfygllta dpyidmtekn dqgefafqpt gydvqqsnfs npyyvaqnrt wendqnrlfg
      481 gvelnfdild nwvltgrqsi drtnqrtelf ypkgyqtpdd dallasgldn reddqsqdli
      541 tevsttynde frdlaytata kylyeqretn nlflegagfp asgirsvgat dsenysigsf
      601 taeertenff fnldldyqdt yilsglvrrd gsslfgeder wqtyfrgsla yrltedfdip
      661 nvsklklrga ygtsgnrppf saqyetysat esglqvqnlg nselrsstit etsigidatf
      721 lqrfnltvny adsrteddyl qvplaggvgf snqfqnigev ksttweasld sqiltgddgp
      781 swsvgatfsr vrqeitdlgg apaftrdpan ldsdntdapa lslfrveegv pfgamygnkl
      841 ltsldqltvv dgevlnsggs srddftinnq gyvipegteg tpseqpvymv nedggtavtq
      901 igntrpdfqv glrsnftwkg fgvyglldws qggdvynysk qllyfnyrhe dqqdfaeqgk
      961 diaysdgssn iynqgspssh fvedatfvkl relsvsytld qdllqdafgt gaveriklsv
     1021 igrnlftitd ysgwdpevgl rsdannfkld eyaypnfrtf agsvsvqf
//
LOCUS       WP_119843586            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. MSK19-1].
ACCESSION   WP_119843586
VERSION     WP_119843586.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. MSK19-1
  ORGANISM  Reichenbachiella sp. MSK19-1
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Reichenbachiella sp. MSK19-1"
                     /db_xref="taxon:1897631"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111899
     Region          23..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlrvftlltl ffavvvsgay aqqtvsgkvf gelndplpgv svviagttqg titdlngeyk
       61 isvdgdspsl ifsfigyenq svevggrsvv ditmvtdvks ldevvvtafg veqkkkalgy
      121 avqqldskel mesqqtnivn alqgrvagvq insssgqpgs gssiiirgit slnpsannqp
      181 livvdgivms natdvpdilp ssgsnaansa eqgsstnrma dinpndiesl nvlkgaaaaa
      241 lygvraanga iiittksgka gktvvnfsat qgwdvlgnrp elqekyregr ygrlrfnsdg
      301 splrfqtqgp kvregteiyd nienffetgr rqeynisaqg gteqarffts igrldqsgit
      361 pesdwarttf rlrgditasd kltirsaisy tnsggnkals gdksimssms ymtnsfdvtd
      421 yinpdgsmkd ysdgiidnpl ylakyakytd dvnrisgnvg fnykitpwls adytigldqy
      481 ndnrnrfmpp gldgtsqtgg fivdanigrr einsnfllta tvdltedlna sltlgqqvvd
      541 insrsttrrg egflfsdfnd idntsnlfgs dnksqyrqvg fffdakanyk givylgvtgr
      601 ndissslsee nnsyfypgvn lglifsefls snhilsygkv raswaqvgkd aaphligfty
      661 sgasgfpfdg angfrkssva gdenlkpett tsfeigtdlr finnrlslda tyyvqnstdm
      721 itnvplsnst glsryttnag eienkgielm lnaqviktsa ftwdmnmnws kneatvisva
      781 dgideievyn egkseiiykl vpggnvgdly gntmartedg qviigsdgfp qratdpetga
      841 laiskignai pdfiagwnnr isykgislsa llewrkggdv mdmalingqr ngiwkdterr
      901 fedvifagvk nvgtaespvy edndivarld dggntyrasw layvgentlq daswlrlrtv
      961 tlgyqlpstl inkvgltsar itftgnnlfv ntpykgydpe snyfgsgsni vgftgmtvpg
     1021 tksylvtlnl kf
//
LOCUS       WP_119843506            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. MSK19-1].
ACCESSION   WP_119843506
VERSION     WP_119843506.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. MSK19-1
  ORGANISM  Reichenbachiella sp. MSK19-1
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Reichenbachiella sp. MSK19-1"
                     /db_xref="taxon:1897631"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110070
     Region          31..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknyylfnfr gllvlgalll ttaiqvyaqt kvvtgvikda elgdalpgvn vliqgtqtgt
       61 vsdfdgrysi sipsdetvlv fsfvgyqske ttvgsrsnid vtmdydvsal neivvigyge
      121 vekkdatgsi valgskdfnk gaistpqeli vgkvpgvvvt tgggaagtgs tirirggssl
      181 ranndplivv dgmplessgi sgmanplati npndietftv lkdasataiy gsrasngvii
      241 ittksgggdk lkfsyngnvs igvpvktldv ysgdeyrali qdritnhglt dvadntlgta
      301 ntnwqdeiyq naistdhnls vsgggeilpy rvsvgytnqd gilkknnmer tslnvlltps
      361 llndnlklsi nakgsiiend fsnpdaigaa vqfdptqpik ngntryggyt awttdpndin
      421 slpitiatsn pvaqleyrdn katgkrmilg gkaeyrlpfv dglkatvnvg ydyfnsvghd
      481 vmdtlaswsy repsnqvkky eqtkenslld fylnynkgle sidskidltg gysyqhfyne
      541 gfssnrpvam tdgvfeganr ddykneyyli sffgrlnytf kgrylltgtv rqdgssrfge
      601 dnrwglfpsv afawqikees flrdvdalet lklrvgwgqt gqqdigdtyy pyiptytgsq
      661 tgayyqfgns fyptqrpnay danikwettt tqnigldfgf ldgrisgsvd vyhretedli
      721 neipiaagtn fnnflvtnvg slvnqgveva ltgaiistpd ltwelsgnlt yneneitkmt
      781 lvddpsytga ptggisggen nniqinsvgr pintfymfeq iydqngmpie glyvdktgng
      841 gnvsgdnlnk yylqnpapey ligissrvny kgfdfsfsgr lnlnnyvynn nasnlgiyqn
      901 lynqagynan iltdvektqf mraqywsdfy lenasffrmd nitlgysfek fftdkvngri
      961 sftvqnafvi tdytgldpev sggidnnlyp rprtymvgln lnf
//
LOCUS       WP_119843596            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella].
ACCESSION   WP_119843596
VERSION     WP_119843596.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella
  ORGANISM  Reichenbachiella
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Reichenbachiella"
                     /db_xref="taxon:156993"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110650
     Region          23..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikrililsl alcttlfvqa qtrtvsgkvt dsadgaalpg vnvlvkgssn gtvtdiegay
       61 svevsdldvl vfsfigylta eqpvgaktvl dlgmepdveq ldevvvtalg isrdkkslty
      121 aaqevdgeel tkvkdanfmn sltgkaagvf vnrsgsgvgg strvvlrgns strnnsvlyv
      181 idgvpmnnfs psqpsdvwgq nfgvagsagt ggagrdggdg vaninpedie sinvlkgasa
      241 aalygsqaan gvilittkrg kagkvsvsas snftsesvlm mpemqfnygq tsagaldswg
      301 gsvdakdhvs dffdngktwi ntvsvaggne maqtyfsyan tdskgiipsn elqkhnvtfk
      361 eslslwqdrl kmdggvslit qstnnransg myfnpltgly ffprgldfde yknnyetfda
      421 nrnfntqnwv nnidvqqnpy wilnrnqned srnrvignig atlkiveglt frvrgnidks
      481 vdryeqrvha stqatlsdin gryvqqnaea tqmygdallm ynktfekfsv satvgtsitd
      541 sevktqffds kggddirneg ieglfyantf niqniaiggt alfneggshs qlqsvfgsln
      601 lgyngmlfld vtgrndwsst lpdtdffyps vgltavisem vdissvdllk vrasfaqvgn
      661 avnaydltsg sfnsiipygt vttptsrvep gqtlnpemqn sfevgaevsv ldqrvsldva
      721 yyntvtenqr ipivapaskg ggffyingge ivnkgieaal tvvpvstenf twtstlnftk
      781 ninevkalps eledgrlqlt apgvnsyamm ltegsqfgdi ygqkfarned gviivdadgr
      841 pqvqeggldy vgnpnpdymw gwnnnfnykg islgflvdar iggevmsite amndlygvsk
      901 atgdardagg vdmkavyadg taysgllpaq efyttvggra giteqyvysa tnirlremsi
      961 gyslpstvme klgpiktakl sligrnlffl kndapfdpdv smstgtglqg vhvfglpstr
     1021 sigfnlsltl
//
LOCUS       WP_119843649             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. MSK19-1].
ACCESSION   WP_119843649
VERSION     WP_119843649.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. MSK19-1
  ORGANISM  Reichenbachiella sp. MSK19-1
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Reichenbachiella sp. MSK19-1"
                     /db_xref="taxon:1897631"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110437
     Region          123..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnyikiamvl cavwgffpal lqaqntmnte ltasivpira qsgvdidlyk dnngeadkli
       61 asadtvanke vvllpgsdgy pvevafrqvg ekdlshdvsf vdmpsildkn yiinpldnme
      121 afvggfngnl wgqtdyltli dgvprdigsv lptevaqvtf lkgvsavaly gsmgargvvl
      181 ittkrgkihg qeitvrtnag vhvpkaypry lgsaeymdlf nearvndgld elysqeqiyy
      241 saqgtdpyry pdvdyystdy vqkaysryda tveieggnek tqyytnmgfy rtgtplnfgg
      301 atenhdkrfn irgnvdmnia nwltakvdaa vvfyngigsn tdywgaadtl tpnrytplvp
      361 idrieandqa sldlvgasqn iingqyllgg tqlqqstpig aiyaggtnny nsrqfqfnag
      421 anadlgavvq glslsttfgv dynstynvaf nneyavyqps wtsyagdnri asltkygnda
      481 ssgsqditds wytqtlsfna hldyqrtfdn rhnfsgmlla ygfqrsisal yhkpsnanlg
      541 lhlgynfkhk yyvdfdgalv hsaklpednr qsisptatlg wrlseeaflk dvsflsnlkl
      601 svsggilntd ldiqnvnned dasdyylyqq vynqtdgawv twkdgfsnqs tdsrrgsnpn
      661 ldypqrrels lgldfalfdn aivfegsffa sqtsgiavqn nvlfpsyfvs ngypsgsfvp
      721 ytnynnddrm gvdfnlrlnq nvgelalslg vsgiyyttea sqraemyeda yqnrqgqpld
      781 aiwglenlgf fadatdiqns pdqialgevq pgdlkykdqn ndgiinaqde vylgragwsg
      841 apltmgfnlt anyknftffa lgtyrsgayg mknnnyfwvn gqdkyseevr grwtedtqns
      901 atfprlttln gannfrnsdf wmystdrfdl srvqisydfp esllggpdsf irelgiyvng
      961 anlltispnr eilemnigsa pqtrfynlgl ramf
//
LOCUS       WP_119843673            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. MSK19-1].
ACCESSION   WP_119843673
VERSION     WP_119843673.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. MSK19-1
  ORGANISM  Reichenbachiella sp. MSK19-1
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Reichenbachiella sp. MSK19-1"
                     /db_xref="taxon:1897631"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122945
     Region          28..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkninkvla amllilssma ayaqspvtvq gqvldekgep ligvsiqvqn taigavtdle
       61 gnfrfqavvg dvivmrmlgm kqqqltvtns qplqitmved adqldevvvn gfqvvdrklf
      121 tgaaarlemd dvklegvada srmlegrvag vtvdnvsgtf gtspkirirg nssingnnqp
      181 lyvvdgvile dlsevntddf isgnantlis ssianinpsd iesyqilkda sataiygara
      241 angvivittk kgrsgalqvn ytgnfsvklr ptysqfnlln saeemsvyre mhskglidit
      301 taakaqtyga lgkhfvlinq kdipwgaggg lneqflnqye nantdwfdvl fndfglqqqh
      361 slsftsgtek stnyysisfl qddgqtiadq vqrltatarn nyfvsdkfnf glkltgsyre
      421 qeapgtsnre fdpisgtytr dfdinplsfa lntsrsmrpy dengdleyfr rnyapfnile
      481 elrynfidin vldvstqanf eftpvknlsi ngvfqvryan tkrdhtvher snqaeayran
      541 dtqffqdann llfsdpdnpg lnpvvvlpqg gfnyldqtdl lsffsrfsan wskdigldhs
      601 invlggtevr ysdrdersst amgviyesgg vvvtdpnive ffnlqnidin tfesnkdrfv
      661 gvfinggyay kgkyianftg rydgsnqlgk sqsarylptw nvsaawnidq erfmgrlefv
      721 dqlklratyg lsgnlppdas ailnlqsdvt irpsdvepyl yiedlsnadl tweklkefnv
      781 gmdmgfwesr vttsvdyyfr qsfdligqvl tsgvggqslk ygnfadmeah gfevtlntin
      841 fqrnsfswrt nfnigytrdr itnldygprl adaldqngta vlggprrglf strfagltsn
      901 gvptfygsnd evvveidlqe rddlagilqy egpseprggg gfantfqykg ftlnvllsyk
      961 fdykirlnds frssyndfvs lpgelrdrwv ttgdedktnv pviltsrqvn igsdvqaysl
     1021 ynqsnlrivn gdyirlksvr lsyqvpeqwv qkaklrnasl svegqnlall ysddrlngqd
     1081 peffssggva lpqpkmitfs lnigl
//
LOCUS       WP_119844472             937 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. MSK19-1].
ACCESSION   WP_119844472
VERSION     WP_119844472.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. MSK19-1
  ORGANISM  Reichenbachiella sp. MSK19-1
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Reichenbachiella sp. MSK19-1"
                     /db_xref="taxon:1897631"
     Protein         1..937
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103714
     Region          46..936
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyiqyiial atvlfgfaqv qaqqveevvl qdtlgankkq kvhlpfgdmd knrvvgatsl
       61 itqdqittad ldvesamigk amglnvfkns agpgsdnswl nvrglhtigd dgplvvvdgv
      121 snrsleslnf yeiesitvlk ditakslygp qaangvilvt tkrgevgvkk asinaeygfr
      181 kpthlpdfln sadyarlyne aqendgltpq ysdadiaaye sagindelpn vdyydrylks
      241 ftnyqriygt ysnadektaf yftagyageg gleaigeqtk ynsmnvrgnl dykindifsv
      301 qvdvaarlet tstnqmtysn ydgtpnnlgd nntvqgffst lsshrpneyp iyhnaptaes
      361 pgelgwgaak stniegellr agyrdellrq sqsnigldmd ftqwgiegls wknyvsfdty
      421 nflitrkkde yaryqadgtq vgddvqasgi skfddsayrn igmistmtyd rtfgdhafts
      481 hlnaiaqnre yqgtaqpykn vtygyrlnya fankyiaevd ltymgsnkle egsryeffps
      541 vglgwvlsee gflqsvdald ylkikasygq mgydrslqhf wyrdaygpng wvqfgsqnsn
      601 gssaynlira gnpaigfeia teynigleal imknlsvean yfneyrsdip mqvsslypdy
      661 fgdyipyiny gevsnqgvel glnysgqagd isygvggyvt yseaiyektg dltafshlnr
      721 dgqpldamwg ynsegfytda sevnvqstlg gdviagdlky tditedglit vedqkviant
      781 tpryqyslnf nfgykglgls vlgqgaaghd rmmswntayn gvaqgkyaan amnrwtpdnl
      841 dashprlttv ggahsyqgss fwlqdasyft irnielsyaf pekirnsira selrvfargt
      901 dlfsfsgnsd fnsdnaasgl sngflmktvs lgfnlsy
//
LOCUS       WP_119844645            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. MSK19-1].
ACCESSION   WP_119844645
VERSION     WP_119844645.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. MSK19-1
  ORGANISM  Reichenbachiella sp. MSK19-1
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Reichenbachiella sp. MSK19-1"
                     /db_xref="taxon:1897631"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117802
     Region          35..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnsillnpkn iklllqslvl vfvlmgsiva saqdrriegq vsdatgtavi gatvivkgne
       61 tvgsitdvng rysltipsga eklimtsigy atqevtigsr tvvdatlaen vkelhevvvt
      121 algveretka lgysvqevqg ddmtearetn mvsglsgkva gvqvtnsgst iggsarvtir
      181 gesslningn qplfivdgip isnqvqgasg sgnlevdygn aageinpddi atvsvlkgpa
      241 aaalygsraa ngailittkt gksskgigit insnttfenp lrlpewqnty gqgnngqfef
      301 vdgsgsgiad gvdeswgpkl dgqlisqfds prnidgfrgg dlnapagsti tptawspspd
      361 nindffetgv tltnsisias sndkgnirls ytnldqkgmv pntdlkrntl alntgvnltd
      421 klkinasiny intesgnrpa isygteslmy lwiwygrqvn tnnlknywmp gmegvqqfny
      481 nynyhdnpyf ttyentngqs kdrvlgnvsa tykftnelsl mvrtgtdfyn elrdrkrafs
      541 tqrfplgmyr edklyfnern sdflltynkq lnkdfgftvs aggnqmkqtf nynqtvapql
      601 lipgiynfsn savnlqvsqn dtekkinsly gyaqfayknm ifldvtgrnd wsstlpvdnn
      661 syfypsatls avisdmvalp spisfvklrg ayaqvgndtn pyslsnvyvs etawgstqak
      721 sessvlanae lkpektasfe lgadvrlfkg rlgldftyyd nrtsdqiipi aldiatgyns
      781 riinageiqn ngielmvnat pvqlangltw emgvnftrnr skvieltegl dtytmteing
      841 ayvqarvger mgdiygvgfa rvedenspyy gqiihsaegt plrgselekq gnynpdwmmg
      901 iqntlsfkgl slgvlfdirq ggivvsrtkt igstsgqlke tlygrengyd laldgngiis
      961 egviqnadgs fipnnvkvas rnwhnryyer nnveaakyda syvklrevkl sytmpskwfv
     1021 stpvrsikvs vvgrnlalwt enphfdpdvm amsggtlqpg ienmaypsar sygfnininl
//
LOCUS       WP_119844665            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella].
ACCESSION   WP_119844665
VERSION     WP_119844665.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella
  ORGANISM  Reichenbachiella
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Reichenbachiella"
                     /db_xref="taxon:156993"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119218
     Region          62..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkhyktqvr allgvkidtr qekdpgliss svsstsqswl kggltllvvl vlalnyaeaq
       61 vvisgtvadq adgsplpgvt vlmdgktggt vtdfdgnfkl naeegdvlif sfigylsqrv
      121 tvgsqtiidv elaedskqld evvvtalgie retkslgysv sqvdgdnlsr akevnvvnsl
      181 sgkvagvdvn lssagptgss svtirgkasl ggsneplyvi dgvpmdnraq gdgagqwggy
      241 dlgdgvssln sddiesvsvl kgpsaaalyg srasngvili ttkkgikrng igveftsnat
      301 fekvsarfdd yqtvygqgrd gqipdvddaq nttqsawgak mdpnltipiy ngqlkpygvv
      361 ednildffrt gstftntval tggseianmr vsvsdmrnkd iipgsemarn tflvngslkl
      421 adrltitskv nyiresatnr palsdnpnnv glsliglaps fdqkwlsedy kddedryvdw
      481 nggniyrinp ywstreisne ssrdriigyl qvdyrltdwl nlnlrggtdf yqsrftnfsp
      541 vstptletgs lteqsrfnre dnyqamlevh kdfnggfsls syvggnimty naetfnqagt
      601 giiledvqti qnflqvnngy snvrkqinsl fgavqlgykd tyfldatlrn dwsssldpdy
      661 nsymypslsg sfvfsnlles skflsfgklr asyaevggdt epyrlsqnyg vkdfsllgkp
      721 lgelsgvela kvdlkptrty syevgadirf fqdrlrldaa yyyqltrdqi ltlnipatsg
      781 ydiavinage ilnqgveiqm aatpiqvgdf qwnvtvnfak ninsipelhp esdtyllsna
      841 rwanaaivat eggkygdivg kkwlrdpdgn ivhnaaglpv lddeagqqvl gngqyefttg
      901 iindfsykgf tlralidyks gadvysmssg layangtske tlegrdawya seearlaagv
      961 tdiaawtptg gyvgkgvknt gtadnpvyet ndiptnpqny wgslytqspe lfiydasyvk
     1021 lrelvigysf pkkwlgnilt agsisfvgrn lwliysnvpn vdpesgynns ngqgfeygsi
     1081 psrrsygvnl slkf
//
LOCUS       WP_119845936            1090 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Reichenbachiella sp. MSK19-1].
ACCESSION   WP_119845936
VERSION     WP_119845936.1
KEYWORDS    RefSeq.
SOURCE      Reichenbachiella sp. MSK19-1
  ORGANISM  Reichenbachiella sp. MSK19-1
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Reichenbachiellaceae; Reichenbachiella.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Reichenbachiella sp. MSK19-1"
                     /db_xref="taxon:1897631"
     Protein         1..1090
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120675
     Region          21..1089
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrivyllfl lptivfgqnq kqvsgqvvdm dfkepvigas vyitmdavgs ersvvgaiad
       61 ldgnftfrap adantlvvsf tgyesqtvdi agmnstglli emkvsvemld eivmtgyqet
      121 tmrkttssma kveaveikqa gvanidqmlv gqlagvyvqp tngapgspak inirgtstln
      181 gssdplwvld giplegddip sdftdkdnid llksypisgi npddiesitv lkdasatsiy
      241 garaangviv iktkngqkgk trvnitantf vtqkpdfskl nlmnssekvd felymasrsd
      301 lryqqgqgev arilnesgey nnftnngfss ldpsvqaain glkdtdtnwg deiyqaainq
      361 qyglsmsggn drndyyfsag yfdekgatig aeqkrfnltl knnydltdnf tvgvalfgsq
      421 nrtssyltgi daytnpayya rtanpylglk dangdyiydp dliersdinl dynlleeran
      481 tsneliansm ksifsidyts eigikitsql glqldndaae qfsdqesyyt rkyeqksryl
      541 gdnsedlyym peggiiqntn anafqynwkt minygqvfyn khevdvlvgt efrednntmv
      601 rsrgfgynpn tlttvpitne raatnsnfdt ytksyssnay asffgtlsyt ydgkyslfss
      661 lrydgsnlfg vnpkyrylpi wsvagswdla kenflyssrl dilklrasyg iqgnvdktts
      721 pyvvgtygte svlpgiseei irasgapngd lrwekttssn igfdlgiwdg rlfisndyyy
      781 rkstdliglq svplesgynt istnwatvtn kgfelsittv nidhtdfrws tsfnisanrn
      841 nvdrveiqee sfkpslqgys vnaifaiktd gldsngiplf vkdgetmsav dfynllegtd
      901 gsqltreehr dlytyvgdat pkfsgginnt frykqfdlqi aanfnikqtv krnapyhmtt
      961 vnpgnnyste vfsagtgdlp gligfnsagi ntdlvyswfn sgdggntynd ldvwveeisy
     1021 lrinsirlgy slspaaaskl rvstvrfyle grnllvfgsd ytnyfdpety gsayaqplpk
     1081 lvsaglnlsf
//
LOCUS       WP_119857455             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodopseudomonas palustris].
ACCESSION   WP_119857455
VERSION     WP_119857455.1
KEYWORDS    RefSeq.
SOURCE      Rhodopseudomonas palustris
  ORGANISM  Rhodopseudomonas palustris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rhodopseudomonas palustris"
                     /db_xref="taxon:1076"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39002
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeqd paeprvaatp dtvkklkalg aevaiepgag lksglpdady aavgatvaad
       61 alsgadvvlk vkrpeaaels aykrgalvla imdpygndaa lkamadagvt afamelmpri
      121 traqvmdvls sqanlagyra vidgaeqfgr vfpmmmtaag tvpaakvfim gvgvaglqai
      181 atarrlgaiv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpaprlvta emvksmkpgs vlvdlaverg gnvegalpgq
      301 vvetngvriv gytnvagrva asasslyarn llsffetmvn kekalavnwd delvkatalt
      361 rdgavihpnf qpksa
//
LOCUS       WP_119887471             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            aestuarii].
ACCESSION   WP_119887471
VERSION     WP_119887471.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus aestuarii
  ORGANISM  Paracoccus aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus aestuarii"
                     /db_xref="taxon:453842"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55316
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkegf enearvavtp asaghlgklg hevfvesgag aragfrdedy rqagvtvlpd
       61 aaaligavdv lakvrqptea eigqmragqt visffypaqn adllaqakdq gitaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigasvslg aqvyafdvrp evaeqiesmg aefvflefde pvqdgaatgg yaapsspefr
      241 ekqlakfrel apqmdivitt alipgrdapk lwtadmvaam rqgsvivdla aekggncdlt
      301 vpderivten gvviigytdf psrmgaqase lygnnirhfl adltpgkdgv ihhnmeddvi
      361 rgatvvhdhd vtwpppppkv aaiaaqkpke kkkaptpeer raaeaaafka dtanqlkllv
      421 ggglllllig lvapasfmsh fivfvlacfv gfrviwnvah slhtplmait naissiiilg
      481 almqigsgsw wvvllgalav lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_119893789             233 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_119893789
VERSION     WP_119893789.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..233
                     /product="STM4504/CBY_0614 family protein"
     Region          <1..97
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl glepdkaise
       61 lnnlfhehgl kyryengriv rlrrikrlkn icyylyspge ygfveydlme aynrlmlndf
      121 acvvkechaa frsvllrihe rkgivyheqd slntlmanlm argvisaeyt hkfhflsdvl
      181 eseiflpmap ekshhhyamm lriseelacs iyyltersif fltqraeedg aap
//
LOCUS       WP_119878424             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter radioresistens].
ACCESSION   WP_119878424
VERSION     WP_119878424.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter radioresistens
  ORGANISM  Acinetobacter radioresistens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter radioresistens"
                     /db_xref="taxon:40216"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39968
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv igenrvaatp etvkklinag hsvviergag vkaayidsay eqvgatitdd
       61 ayqnsqiilk vrapkgeeiq klsphttvvs mfdpyrntel dqfasqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaneyqr mfpmlmtaag tvkparvvvm gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmsaeeq qraaeaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vesggnvegs
      301 kcgetvttsn gvkilgvpni patvateasa lyarnvfnfv etlfdqeknf tvnledeiqk
      361 allvthngqv llkrg
//
LOCUS       WP_119891631             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas cavernae].
ACCESSION   WP_119891631
VERSION     WP_119891631.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas cavernae
  ORGANISM  Pseudomonas cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas cavernae"
                     /db_xref="taxon:2320867"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38811
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletf tgetrvaatp etvkkligag hqvtvqsgag vnasvpdsay eavgakigsa
       61 aealgadlvl kvlapndael tqfksgavlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarilil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaigvggy arpmpaswma
      241 rqaqavhera kqadivitta lipgraapvl lkeetvkemk pgsvvidlaa aqggncplte
      301 aeqvvikhgv tivgysnlaa mvpadasaly arnlqdflkl vidgegkfhl nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_119898540             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            sigandri].
ACCESSION   WP_119898540
VERSION     WP_119898540.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus sigandri
  ORGANISM  Paracoccus sigandri
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus sigandri"
                     /db_xref="taxon:1276757"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55471
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkesf egearvaitp sssahlqklg hevfiesgag aragfsdedy raagvtveat
       61 aaelvaavdv vakvrqpteg eigqmrdgqt lisffypaqn aellevarqq gitaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtsvslg aqvhafdvrp evaeqiesmg aefvflefde avqdgaatgg yaapsspefr
      241 ekqlakfrel apqmdivitt alipgrdapk lwtrdmveam kpgsvivdla aekggncdlt
      301 vpderivtdn gvtiigytdf psrmgaqase lygnnvrhfm adltpkkdgv iehnmeddvi
      361 rgatvtrdhd itwpppppki aaiaaqkpke kpkaltaeek raaeiaafka etksqvtlla
      421 ggglllllvg lvapasfmsh fivfvlacfv gfrviwnvah slhtplmait naissiiilg
      481 almqigsgsg wvlllsalav lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_119944510             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neorhizobium sp. NCHU2750].
ACCESSION   WP_119944510
VERSION     WP_119944510.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium sp. NCHU2750
  ORGANISM  Neorhizobium sp. NCHU2750
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Neorhizobium sp. NCHU2750"
                     /db_xref="taxon:1825976"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55472
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvlkela arearvgmtp dsalalqklg ydclietgag kaagfadeay raagvtvvet
       61 adaliagsdv iakvrppeva evdklgpgkt lisffypaqn kdllerakar ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfke qqqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwtadmvalm kpgsviidla aerggncdlt
      301 vadervvsen gvivigytdf psrmaaqsst lystnirhmm tdltpakdgv vvhnmeddvi
      361 rgatvtkdge itfpppppki qaiaaqkpke kareltpeek rakevtafka qtknqailla
      421 vatvlllvvg ayapssfmsh fvvfvlscfi gfqviwnvsh slhtplmavt naisgivilg
      481 allqigsgnw lvvilgalsv lvatinivgg flvtrrmlam fqks
//
LOCUS       WP_119905369             218 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_119905369
VERSION     WP_119905369.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..218
                     /product="STM4504/CBY_0614 family protein"
     Region          <14..82
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 snlllktddk rkhidtiela fnyidtylrt yevtlglepd kaiselnnlf hehglkyrye
       61 ngrivrlrri krlknicyyl yspgeygfve ydlmeaynrl mlndfacvvk echaafrsvl
      121 lriherkgiv yheqdslntl manlmargvi saeythkfhf lsdvleseif lpmapekshh
      181 hyammlrise elacsiyylt ersiffltqr aeedgaap
//
LOCUS       WP_119908811             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Motilimonas pumila].
ACCESSION   WP_119908811
VERSION     WP_119908811.1
KEYWORDS    RefSeq.
SOURCE      Motilimonas pumila
  ORGANISM  Motilimonas pumila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadales genera incertae sedis;
            Motilimonas.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Motilimonas pumila"
                     /db_xref="taxon:2303987"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53754
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkell enetrvaatp ktveqllklg fsvsieasag elasfndqay idagasvesd
       61 tptlwqsdii fkvnaptfee idllkdgatl isfiwpaqne elmaklsskn invlamdavp
      121 risraqalda lssmaniagy ravieaanqf grfftgqita agkvppakvl vvgagvagla
      181 aigaagslga ivratdtrpe vaeqiesmga efllpdyeed gsssdgyakv msdgykqaqa
      241 emiaeqakdv diiittalip grpapliite emvnsmksgs vivdlaaqtg gncaftengk
      301 ivevngvkiv gysdlpsrlp tqssqlygtn lvnlmkllct ekdgninidf edevirgttv
      361 vkageiswpp paiqvsaapa qpapaaepap qveekpanpw lkpvaaalga laffwvadka
      421 psdflshftv fvlacivgyg vvwnvshslh tplmsvtnai sgiivigall qvgsesgvvt
      481 flsfigvlia tinivggftv tqrmlkmftk d
//
LOCUS       WP_119941440             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neorhizobium sp. NCHU2750].
ACCESSION   WP_119941440
VERSION     WP_119941440.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium sp. NCHU2750
  ORGANISM  Neorhizobium sp. NCHU2750
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Neorhizobium sp. NCHU2750"
                     /db_xref="taxon:1825976"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55559
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvlrera drearvgmtp dsalalqklg ydclietgag kaagfvdeay raagvtvvet
       61 adaliagsdv iakvrppeva evdklgpgkt lisffypaqn kdlleqakak ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfke qqqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwtadmvalm kpgsviidla aerggncdlt
      301 vadervvsen gvivigytdf psrmaaqsst lystnirhmm tdltpakdgv vvhnmeddvi
      361 rgatvtkdge itfpppppki qaiaaqkpke kareltpeek rakevtafka qtknqailla
      421 vatvlllvvg ayapssfmsh fvvfvlscfi gfqviwnvsh slhtplmavt naisgivilg
      481 allqigsgnw lvvilgalsv lvatinivgg flvtrrmlam fqks
//
LOCUS       WP_119952940             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas cavernicola].
ACCESSION   WP_119952940
VERSION     WP_119952940.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas cavernicola
  ORGANISM  Pseudomonas cavernicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas cavernicola"
                     /db_xref="taxon:2320866"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38789
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletf tgetrvaatp etlkkligqg hqvtvqsgag inasvpdsay aavgatigda
       61 aaalgadlvl kvvapnadel aqlkpgavlv gmlnpfnsen iaqmaergvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrmgavi easdvrpavr eqieslgakf vdvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkapvl lqedtvkqmk pgsvvidlaa aqggncpltv
      301 adqvviqhgv tlvghtnlas mvaadasaly arnlldflkl vldgegkfhv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_119956817             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas cavernicola].
ACCESSION   WP_119956817
VERSION     WP_119956817.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas cavernicola
  ORGANISM  Pseudomonas cavernicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas cavernicola"
                     /db_xref="taxon:2320866"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38658
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvgqg hkvtvqsgag isasvtdsay eaagatigsa
       61 adtfgaqlil kvvapsdsel aqikngsvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee rdcavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncplte
      301 adqvvvkhgv tivgltnlaa avaadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_119957259             247 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_119957259
VERSION     WP_119957259.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..247
                     /product="STM4504/CBY_0614 family protein"
     Region          <4..111
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 vyrricktlr keyglftlya hstsyldems nlllktddkr khidtielaf nyidtylrty
       61 evtlglepdk aiselnnlfh ehglkyryen grivrlrrik rlknicyyly spgeygfvey
      121 dlmeaynrli lndfacvvke chaafrsvil riherkgivy heqdslntlm anlmargvis
      181 aeyvhkfhfl sdvleseifl pmapekshhh yammlrisee lacsiyylte rsiffltqra
      241 eedgvsp
//
LOCUS       WP_119958046            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM32-11AC].
ACCESSION   WP_119958046
VERSION     WP_119958046.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM32-11AC
  ORGANISM  Bacteroides sp. AM32-11AC
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Bacteroides sp. AM32-11AC"
                     /db_xref="taxon:2292950"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112194
     Region          26..1023
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrimltlv clmaaiswva aqnspitgiv isaednepii gasvlvkgst tgavtdldgk
       61 ftitdapaga ttlqvsfvgm itqevpitpg tirvtlknda klldevvvta lgiakkeksl
      121 tystqvvngd elvrakdpnm mnalagktag vqinksssgl ggsskviirg nrsvsgnnqp
      181 lyvidgvpfg sstnentstt iggdndsgny drgdgisnln pddiesmnil kgpaaaalyg
      241 ssaangvvii ntkrgkegra sisfntnttf dmaaygipef qnnytgqtts wggkingspd
      301 ytddffktgv ttinslslsm gskamqtyfs yantygkgvv egnrlvkhnf nfretanffn
      361 nkltvdanvn amyqkgnnrt tsggyymnpl vglyhfprgg veggkdfnyy kdnyqvlntg
      421 rnimdqnwyk tsgtdmeqnp ywlinkvpne dtryrtlinl svkyqindyf siqargsady
      481 ivdkdntrmy agtspilcgm naagtgtngr ysyneqsels tygdvlftyq qqfenfsfna
      541 svggsindyn gngtgfdsyp gtlsipnvft mqnvtlnags lsdwrkhtqs qsvfftgqig
      601 lkdqlfldvt arndwtstla ytkyknkgff ypsvgltwll netlklpswi slgkirgaws
      661 qvgngldtyl snplntitkn gsisfnttsp fdelkpektt slefgtewrf fdsrlefdft
      721 yyktntknql ftlpapsgse yntyyvnagd iqnsgieimm natpvmtnsf rwktgvnfat
      781 nkneakalag ealgyfqfsg gesnnvwsrl evggsfgdfy gttferddng kikfgddglp
      841 lvnksdpkkl gnsnpdfnlg wsntltwkdf slyflidgrf ggkvmsltea dldqqgvska
      901 tgdardrgyv mleghkisge qaiqdfynlv ggragvteyy tysatnirlr elsigynlpq
      961 awltkigvik saqislvgrn lfffknnapy dpdgmlstsn rlqgvdvfgm ptnrsigfnl
     1021 kvnf
//
LOCUS       WP_119958058             988 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_119958058
VERSION     WP_119958058.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110781
     Region          2..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvisyigmqt qevdikpnik vfmrsdseml devmvvaygt akksaftgsa sviksetlek
       61 rqvsnlsnal sgtvsgvqtq stngqpgtsa tvrirgigsm yasnnplyvv dgipyegdis
      121 avnsqdiesm tvlkdaaaaa lygargangv ilvttkkgks gdtqisldar wgvnsrlvkn
      181 ydvlqnanty metaysalyn gylynsgyta erayqlantd lfpklgyqvy tipdgqylig
      241 rngklnpyaa lgysdgdyyy tpdnwsdemf qsnlrqeynl svsggsdkls yylsasylnd
      301 egiiensgfe ristrmnvdy qakkwlklgv nlsysnvtsr spgdqdtdaa tssgnaffvg
      361 nfiapiypmy vrnadgsfky ntntgyhvyd ygdgestnft rnfmsmsnpm sgflydteky
      421 lmdilngkwy akvdiidgls ltaslglhid ntrqhsvgnk yygqsasygg svmqyssrvy
      481 sldqqyllny kksfgnhnld ilagyesmdf nteshyilgy nmysdnnwta sniidrkngs
      541 gsyneyatig iitrasydfn ekyygsvsyr rdassrfhpd nrwgnfwsvs aawdmakenf
      601 isqydwinml klkasfgqqg ndnlyykgyt nyypyqdqft vsgsdgvfsd gvlyykgnkd
      661 itwetsnsfn vgvdfallgg ridgtieyfn rqtkdmlyyk pvamsngytq fpmnlgsvrn
      721 sgveielnyt piennnlkwv inwngtlmkn kilelhpdlk gemisgsyiy regeslyqmy
      781 ltkyagvdpd sgeaqywakg edgveyktwd wsaaynsnrq asgdllptiy ggvgttlefr
      841 gfdfsiqcay qlggtiydsg yqafmhggds hymgynwhkd ilnawtpenk ntniprvdai
      901 dkytnsssdr wltssdyfsi nnitlgytlp krwlrslgig slriygaadn valfsarrgl
      961 dprmsyttas tdrytpirti sgglkvtf
//
LOCUS       WP_119958571             980 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_119958571
VERSION     WP_119958571.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109293
     Region          2..979
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvisyigmkt qevvikpsvk vvmmpdteil devtvvaygt krkqdlvgsi ssvkneiisn
       61 sqatsvsnal egavaglqvv sssgqpgqda nivlrgigsi sasnnalivv dgvpfngkls
      121 dinptdiasv nvskdavsns lygsraaggv vmittktgrk dkvainfngs wgvaqraykd
      181 ydmatdpgef yrlswyglrn tywaagksie dsnlaasqdl lgelgnynay iipqgeylvt
      241 pdgklnpnar lryndsfada lfdnafrqey nvsasggndr tdyyvsmgfl dndsyvlgss
      301 yerftaranv nsllkswlkv gtnvgyskat qngvqenaga asnpfevars wapifpvhay
      361 daegnmkyye dgspmydagn getdgtskrp tatnqnvian mkediretvy nnltsrsyle
      421 isflknfkft anysydftns sqtvfytpli gdgqsfggrg tkgsyntttt nfnqilaysn
      481 vfgdnhhlsa kigheyykye yqylagqktn ffnpnnpeld nggqmqyins ytanhniegy
      541 fgmadydysn kyylsaafrr dgtsrfldrw gnfwsvgaaw risneafmeg tnswlndlkl
      601 rasygtqgne silseydyay vytpyqdqyt vtwngselgy spefygnpdl twekqktfdv
      661 gvdfrlfdrv ygsfeyfyrr tddmlfkrpv aystagrpyn wenlgamknt giefevnvdi
      721 fnqpdlkwtv slvgshyknr ivtlpeenre ngitsgpfnl regksrfeyy tymyagmdek
      781 gnamwymdet nekgevtgrt ttttyadatr yfigksalpd fngglsttfs ykgidlsiat
      841 afqiggyayd ysylsgmsss fyvghnkdmw ktfnpetgqg slpiwnadna snsftqqsdl
      901 nlikasyfsi rnitlgytlp knltqklgve klriyatadn lglwskrqgf dprvamagsd
      961 deyggyspmr visgginltf
//
LOCUS       WP_119962030            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_119962030
VERSION     WP_119962030.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116257
     Region          40..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnyclslv llalfgtamp faanaavesv lssqstqqak kitgkvldaa gepiigasvl
       61 vkgsgtgavt dvdgkfsvea pagstleisf igyktamlkv tnassysvtl qddsqtldev
      121 vvtamgikkd rkslgyaidd vdaeelmknk svnpinslag kiagvnitqg ggaagagsqi
      181 ilrggtsler dnqpvfvvdg viydnsttvv gnsafdgsls tastnsnrvm dinpedienm
      241 svlkgpaaaa lygsraaagv viittkkgke gavevnfstk yitqwatslp ktqrkygrgf
      301 aedqytdgky tgttyndfsy nswgapidne aatydniddf fqqggawdtn isvaggskns
      361 nfylsgsyyn qdgiipntgy ekatfrfnge qkwrmltfga nvaysqantd ktltsaglyg
      421 ssgsgtmtgv yrwsptddmk hylnedgtry rmfgdrldvv derdnpywil nknklkdnte
      481 rftgnfsika diadwwwisy rmgidsyttd dsktlaaggv yklawqkgmy sensyrykyl
      541 stnlmmnfnk qfgdfnfnlm lgtstddtrt wtnyrmawnf eipdfyafdn atndnrdfss
      601 srsqkrligt fgefradwkn tvfltvsgrn dwsstlpien rsyfypsvsg sivfteflpk
      661 idwlsfgkvr aswarvgkdt spysletalw psqsflgglt gvsnywtagn aalkpeites
      721 telgielrff nnrlkldyay ytnnsynqim sprlsnatgy ilrsvnagdv ynkgmelsig
      781 gtpiqtkdwt westinvsgn rgtvknlleg veilyvtdvq vgnakaasfp ngnfmaisgs
      841 ewkrddqgrv vldknglptk gtnanleign reptfsggwn ntitykgvsl nmlwdfrvgg
      901 hvyngteyam tlagvsefsa nrekievsgv ntngefvtnt feanktytyn gketsgktii
      961 anyyqdiypn etanfmtkvn alrlrtisls ynlpktllak tkvikrasit atannlllft
     1021 nyngdpevaa agsgavgsss vgidycgvpa tasfafgvnl tf
//
LOCUS       WP_119964313             535 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Simplicispira lacusdiani].
ACCESSION   WP_119964313
VERSION     WP_119964313.1
KEYWORDS    RefSeq.
SOURCE      Simplicispira lacusdiani
  ORGANISM  Simplicispira lacusdiani
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Simplicispira.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Simplicispira lacusdiani"
                     /db_xref="taxon:2213010"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55442
     Region          11..535
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqasptplgq rigvpreifp gekrvatvpd vvekliklgf tvavesgagd ganfsddayr
       61 aagaevlpda aalwaasdiv lkvrppstee valmreggtl igfvwpaqnp elmqqltarn
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgryfngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee dgsggggyak
      241 vmsegfqaaq rqmyasqakd adiiittali pgkpapklit aemvqsmkpg svivdmageq
      301 ggnceltvpg eavvrhgvti igytdlpsrl akqsstlyat nllrlveelc kakdgvavvn
      361 meddairglt vtkdgaitwp applkaapvp apktaavpva ekkgghghgs sgplpaktla
      421 ilfavaavaf wfigayapaa flghftvfvl acfigymvvw nvtpalhtpl msvtnaissi
      481 iaigalvqia ppeagvngrp dglilwlafa atvltavnmf ggfavtrrml amfrk
//
LOCUS       WP_119962246            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Bacteroides].
ACCESSION   WP_119962246
VERSION     WP_119962246.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bacteroides
  ORGANISM  unclassified Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="unclassified Bacteroides"
                     /db_xref="taxon:2646097"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117517
     Region          42..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkkckstl lystlvlclw ggfpqvrats fesfaieqqs nkvigtvkde fgpvigasvv
       61 ekgtsngvvt dlngkfslnv kpgatliisf vgykqqevka gnvplnivle edskmlgevv
      121 vtalgikrer kalgygvaev qgealtkake tnvinsmagr vpglvvtqta ggasgssrvi
      181 lrgstemtgn nqplyvidgv pldntnfgsa gtyggfdlgd gissvnpddi esmsvlkgpa
      241 asalygsras hgvilittkk ankdkisvey ngtmtfdtql akwddvqqiy gmgsngtypi
      301 navsntnmsw gakadgtnml kyfdgverpy livpdntsqf frtgftatns aiigvnngkt
      361 girftytdmr nkdivpkthm srdifnlran ttagkfdldf sanytredvk nrpalgdsks
      421 nigknlmtla ttydqewlkt yqdandeysn wngmdpynvn pywdvyknsn nskkdqfrfn
      481 gkvvwnitqh lkiqgtagae lnwftfedyk apttpgyesg ylqnnnfrnr mynfellaly
      541 nnswgdfdfn atlggnlykv nnqtivttak dmkirdvval msfnevsvep ysyrkqinsv
      601 ygavnlgwkh mlyfdatlrg dqsstlpvsn nmyiypsfsg sfvfsellkl gdklpygkvr
      661 mswaqvgsdt dpyqlglvyt kskfaypgyt igyisngtip nkdlkptktn sfemglelkf
      721 lknrigldft yysqlsknqi mgmassstsg ygyrlinage ienkgveial ntrpiqtkdf
      781 swnlnfnfsk nsnkvkklvd dmdmfeleka twldvqvaak vgenfgsivg pdfqrnengd
      841 ilidpstglp mydksnhvlg naswdwtggv ytnfsyknis lsavfdvkvg adlysmsara
      901 ahetgksmat legreawyks eearqaagya kdspdwiptg gfiapgvidn gdgtyrendi
      961 vinpekywms vcrnapsmfi ydnsyvkcre itlsytlpka wlknvvdglt isfvarnpfi
     1021 vwknipnidp dsnynnttgm gmeygslpsr ksygfnvnvk f
//
LOCUS       WP_119977295             209 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_119977295
VERSION     WP_119977295.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..209
                     /product="STM4504/CBY_0614 family protein"
     Region          <5..73
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 krkhidtiel afnyidtylr tyevtlglep dkaiselnnl fhehglkyry engrivrlrr
       61 ikrlknicyy lyspgeygfv eydlmeaynr lilndfacvv kechaafrsv ilriherkgi
      121 vyheqdslnt lmanlmargv isaeyvhkfh flsdvlesei flpmapeksh hhyammlris
      181 eelacsiyyl tersiffltq raeedgvsp
//
LOCUS       WP_119977637             466 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella algidipiscicola].
ACCESSION   WP_119977637
VERSION     WP_119977637.1
KEYWORDS    RefSeq.
SOURCE      Shewanella algidipiscicola
  ORGANISM  Shewanella algidipiscicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Shewanella algidipiscicola"
                     /db_xref="taxon:614070"
     gene            1..466
                     /gene="nrfA"
     Protein         1..466
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52102
     Region          1..466
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvknltkktf vvsalvaasl mtsgvmasdk teprnevykd kfakqynswh etaeseevvd
       61 mleevpslvv lwagygfakd ynaprghmya vtdvrntlrt gapksdedgp mpmacwscks
      121 pdvprmieeq gedgyfkgtw hkggaeivnt igcsdchekg ssklrmsrpy adramntlgt
      181 pfdkaskkdk qsmvcgqchv eyyfektkdh kgfvkfpwdm gttveqmevy ydsieftdwt
      241 halsktpmlk aqhpgyetwq lgvhgknnvt ctdchmpkvk naegrkftdh kvgnpfdrfe
      301 eacgschtqs kefmvnltee rkvkvndlka raeaqlvrah feakaawdag aseaemkpil
      361 mdirhsqwrw dyatashgva ahaadealri lgtavdkagd ariklaqlla vkgvkqpiai
      421 pdvstkakaq aalgmdmkkm nadkeefkkt vlpkwdaeak qreaty
//
LOCUS       WP_119979564             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            uniformis].
ACCESSION   WP_119979564
VERSION     WP_119979564.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides uniformis
  ORGANISM  Bacteroides uniformis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Bacteroides uniformis"
                     /db_xref="taxon:820"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109955
     Region          2..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 misyigmqtq evaikpsvkv tmrsnaeald evvvvaygta kkesltgsis vvdnkkiekr
       61 ittsvtgale gaapgvqvnn tygepgsaps irirgfgtlv sgasdplyvv dgvpfdgnma
      121 elnsndiesm silkdaasaa lygnraangv viittksgrn thkpsitlqm nqgmynrgip
      181 eydrldadrw meatwmakkn ammsnagmsa sdaaayatgh vvsesigrni ynaagdklfd
      241 nngkliatrl agyddldwqn aiertghrqe ynlsaatsge kynvyssigy lnekgyvkat
      301 gyerfsgrin ttytpnkwfk ggvnltgswt krdynsnasg nyyanpfyit rymapvyplf
      361 mhnadgtyql dadgnkiydt tssylsnrni ayemlynkqe svrnvlggqa fatislpygl
      421 sltvkgdlnn stsnnkkydn peigdgatng grltsyayqy ktvtlqeils wnyqfnqvhn
      481 veamvaheny swerkytsgm ntgmavdgnl tmgnflnnsy fsgsddedkt esylarvkyn
      541 ydnryfvegs frrdgssrfh kdnrwgnfys vgaswnmkqe aflqdvdwvd alklrasyge
      601 vgnnmgvsly ghmalytidk nggeaalvkq slsapdikwe ttqtvdvave grlfnrlnfq
      661 igyfdkrskd llfevrlpls agsypwvadt apmnltqykn igtvsnrgwe islnadvinn
      721 ndwkwnigvd atflknkivk lpdgkdilhg mqnyseghsi yewytyhfeg vdqmtgtsly
      781 tldpdkkaaa qeagalttin gtdyatatsy akrdwagsal ptvygsissa lswknwdlnm
      841 lftyslggkt ydgsyaslmg vsesgaagsa yhkdilnswk evpagmtets anridpngtp
      901 rtdfykssdl natsdrwlts ssyfvfknln lsyslpkrwl ksvgieglsl tagvenlftl
      961 tsrkglnpqy sfnggsddty vtarvynfgl tvkf
//
LOCUS       WP_119984494             951 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119984494
VERSION     WP_119984494.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 951)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..951
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105094
     Region          44..950
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miiqykkiwg lavaffslvt anaqlseshk idsskadssi nnlvdlglrk ekawrttgat
       61 ftlqgkeltq mfkgnllntl qgripgltvv tgsgepgydn ptlyvrgqss wniqgnqlvv
      121 lldgfqvdls alsalssnei esvtllkdaa atamfglkgg agvlsirtkv gkvlpknelv
      181 lnarygvqsl inhpevmday nyttfynqal vndgflpkyp npelykatnd pihpnvdwyn
      241 qmlnnssaiq dynlsfrggt ktaryfvlmd yenytglykn ataidkdfgt nakynkfnlr
      301 anveinlskn llvttnisgv tedrntpsgf tasqlfnnlm mlpsaafpvk npngtwgnss
      361 vynfnpvell qqngiyssht rtlqtdfsfk qkldaitkgl nfiggvsfnn qyagyyqtlf
      421 qvksyeitkd andmavldds gnvvyktigt nspgsstdvg tqhwnrntsr lgfnydrnfg
      481 kstitgvllg nrqsylhngq yyavrtqgls tnitydysqk yvvdfsgaym gsadfapghr
      541 yglfpavgia wiaskedflk nsnainylkv rasygstgni nenyrflyee mangangwiv
      601 gssntskggk aigqmanana swelkttfnv gidlqlwknl satidafsek rtgifqipsa
      661 dvpdftgfsl pyinsgivqn kgieavlgyk sngesfqyhv ngtvsfarnk iiqksenaqp
      721 fsrlyqagya igqekglvfd gfyqeadfnp dgslksgias ssfanvkpgd ikykdldgng
      781 iinqydmkpf gynnvpeitl glnlgfnykg fdfnafvqgv mnrtvnlltt aynythpfvn
      841 nnnitvfsan swtpetaqta ttprlstlsn annnqpsnfw lrngnffklr sielgytlpq
      901 kgalkkfnsi rlfvngtdlf tfnkidglep enlsmgyplt kvvnfgfnmk f
//
LOCUS       WP_119986475            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119986475
VERSION     WP_119986475.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120310
     Region          27..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklieftti llllffnqva aqntklisgh ifdaqtgqtl anttiravqs kqtvlssntg
       61 aftvaiksnd tlqithvgyn terirvtals qdikirlqqq nnaledvtin tgyqklkpne
      121 vngsyvvidn kklnqqtgln ildrlngvts sllfntgkqn gnpqnstgit irglstingp
      181 ldplivvdnf iydgninnin pndvesitil kdaaaasiwg aragngvivi ttkkghfnqk
      241 lqvdfnadlm vtdkpdlyyi pqissadyid fqqalfnkgy ynaqftnksh paippavqif
      301 qdrknglvsa edsaqqidal kkidnrqqfe kyfyrkgitq qyalnlrggs rnigwllsgt
      361 ydkemnnlra dynkinlrfe ntylpvknit vntgvyytns tntsgmtays tmseinskqf
      421 vpylnlagqn gqsvpiihny nqrytdtaga gnllnwgyyp lqdykhsygk tnieeltahi
      481 sigyhilkgl daslmyrydk qntnqtniqd tssyytrnli ntfsqlnrst gtvtyiiplg
      541 silnkdyssl nsynlrgqln fdrtfnqahr inailgvevr kewatsngai yygynanplt
      601 nssnldyidf ypnfvngaka kipygstlss tdnrflsffs nlsynyreky tvsasmrkdg
      661 snifgantnd kwkplwstgl gwqlskeafy plswlpflkl satygvsgnv dltktalpig
      721 iygqntfgti slpglsisai nnpdlswers yqtnikldfa trkntltgsl eyymkkgtdl
      781 yaptpydytt fgltstitan vadmkgkgvd itlhsvnink afrwttdfly synqsvttky
      841 yassssaiqs flghgnmimp vvgkplysia aykwggldan gdpqgyindt lstnynaisq
      901 sslnnglkgg sivyvgsanp tsfgaimnnf sfkgfelsfn ityklgyyll kpalayngla
      961 tngtngadya krwqepgdeh ktnvpafvyp lnasrdgfyq lseinvikgd hirlqfinls
     1021 ysflarrykl pfknlqvyfn ianlgilwra nhdhidpdfv naipdpktyt lgvranf
//
LOCUS       WP_119978479             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            algidipiscicola].
ACCESSION   WP_119978479
VERSION     WP_119978479.1
KEYWORDS    RefSeq.
SOURCE      Shewanella algidipiscicola
  ORGANISM  Shewanella algidipiscicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Shewanella algidipiscicola"
                     /db_xref="taxon:614070"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41417
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,96,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgllkesq adekrvalip anvtrlikkn lqilvesgag esagfsdqqy qeagaiitpr
       61 eqvfeqadii tvvnckgsqf deiktlakan qlfigmmdpl ahpdnatala atgttaiale
      121 lvpritraqs mdilssmati agykavllaa hkaprmfpmm mtaagtlkpa rafimgvgva
      181 glqacatakr lgavveaydi rpaareqils vgakpveldl etentetkgg yateqsddfi
      241 krqqqamtnv laqqdivitt aaipgrkapv littamvegm kpgtiivdla aetggncelt
      301 rldetvvhng vtilgpsnvp gtaathasqm ygtnienllk llvdndgqlh ldfddeivrd
      361 tvvvhqgdvv narirsllgm pdiavpeeaq
//
LOCUS       WP_119987314            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119987314
VERSION     WP_119987314.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118376
     Region          32..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrivsscrtl llrmfvivvl sasfsplyaq lktieghvhd skgeplvgas vmitgtkigt
       61 ttdlkghfsi ktkdgarlqi trigyndrnv iakdgidiil ianntdlsqv vvigygsqsr
      121 rkltaavsti sgddirdvpe asfdqmlqgr lagvsvqstt gepgakpniv irgstnldyg
      181 nanggntgpl yvidgiiydv ngmgtsygys dplslidpad iesidvlkda sataiygarg
      241 gngviivktr raktsrpqvt lsaytgvtgn ptfkkiltgd aernlklgll eselpygdls
      301 sgylpqqltd slnpafnndv dwqhmlirns aivnnediav ssnfgvgnsy rlslnhyseq
      361 gavkgygver fapsfnitiv pvkhvnlyge ftlssekhth gagmannpfl fsswnfptsl
      421 aqlngqeiqa ysgaggiydd drilsfignl rledtltknl lftssysann ytenynyfsp
      481 sylngiqnqa ysinnnnpnw twenylqytk hikknnftav agysaykesn ynsfaeaagi
      541 qvsgiytlqt vpsgsnlsvn tsnatkttes yyarllydya gkylftaslr rdassiyspq
      601 yqwgtfpsfs agwvisdesf fkpikkvvnf mklraswgvt gqdpgswyvk yqqlyndasy
      661 lggttgtivg nalysslggt pstyngttvv tpynygnnfi nygikssdnv rwekypqwdi
      721 gldwnmfndr ltfvadwyqk dadnkflwsv padattgymn ysgnyanvrn tgleltinsr
      781 nlgpksafqw ntsfnisfdk nwvtklpngd rdllygdpwf rkvitlgspl fsyklwqvkg
      841 vyateadvpt dpitgnkity fgtpmqagds rivdqngdyn idyedqvpdg ssplpkftgg
      901 ltntfsykrf sltvftsfsy gnkilngnls dalngsasyn swigvagpas fpnilnqfwa
      961 tsgdqtrypr liypsttyns tdawnisrsy flepggfiki kqvtlgynlp ndlmrrwkik
     1021 ginvygmven lhifkqakdi pdpelydptt gsdnityptg mkftfgtrin f
//
LOCUS       WP_119988080            1009 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119988080
VERSION     WP_119988080.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1009
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113717
     Region          34..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrylrigiil cllsisfsnt lwaqstlsfr lqakvydnnm hpikgaivqs rehddvksit
       61 dangvfsiiv spseelsiga ngyvtkylaa stllkeikln nidadtvqvs iafrkedkkn
      121 lfgdvsvvnv ksllkknyft ysldgmeafv pgyngnsnwg mgsyltlvdn vprdannvlp
      181 teidqisflk gvgaialygs taakgvisit tkrgeaynrr idirtnmgtf vpisypkylg
      241 saeymkyynq arendslpdl ydqntiynya sgenpyrypn vdfyssnylk naynrydata
      301 eisggndkak yytnigfytv gslldfgeak nertnrfnfr anvdiklney ltatidasat
      361 fyngkgvntd ywnnaaivrp nrfsplipis miepndessm lyvqnsnyvi dgkyllggtq
      421 ldqtnpfasi yaggtnqyis rqfqfnsgin adlrnvlkgl kfksniavdy stsynlayny
      481 syatyeptwn dysgtdliss ltkygndats gtqnvsnswy kqtiafyglf sydrtfnekn
      541 nfsgmllang yqqsesavyh rvsnanlgfh agynydhkyy vdfnsayihs aklpvnhrea
      601 lsptvslawr isnenflkna sdiindlkit asagivntdl disdyylyqg yytvagswfg
      661 wkdgsgfqat esrrgenanm rfpkrkeini gfdgqflkra levtgnffvn eiqgniiqas
      721 tlfpnyftts ypvssfipyi nyntderigf dfglnlkeqi gklglnlgvn gtyyntkaik
      781 raeiyaddyq yhqgkpldgi wglqslgffn sqedinnspk qsfgqvhpgd ikykdqngdg
      841 vintqdevyl gkggwygspy tfginltatw kkftlfaygi grygaygvkn nsyfwnygds
      901 kysevvrgsw teatkntaty prlttnssdn nfqtsdfwmy ktdrfdiakv qlsydltgll
      961 krkqvireln vyvsgsnllt ispekdilnm nigaapqtrf ynigikalf
//
LOCUS       WP_119989057            1122 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119989057
VERSION     WP_119989057.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1122
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122691
     Region          30..1121
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrktialrw afalcfffct svllaqtsli egrifsekdr tplggasisv vsthkgtfar
       61 pdgtfsveak igdklnisyt gyvaqtitin ghdsllislk evqsnldevv vvgygtqsrh
      121 dlsgavatvn prafksspts nigtvlqgtv pglsvsqstg qpgstpnivf rggndwggsg
      181 gplvvldgiv vpsvygidmd dvqsidllkd aastaiygar asngvllitt kkgknghsqi
      241 tytvrqttnf trknpsdylt aaqyislnre gigaryaadl adgntnaant dkgqlqgswg
      301 walnngfksp vglyttqllg ndnrqllntp gwkllvdpnp fvagqmdsil yreqtvadre
      361 nmifqqtntt ehhldfsgan eqgnfalglg lvkdngiiig sglkrlnmnf ngglnigknl
      421 kvsmntsayt vntsvpyndp sggggtggll qrfigvaptv rysndtsgva lpgpndptlg
      481 npaywstiyn nssteqrfmg gvnldwtilp ylhfkasgsg ymrydynnyf tksyqmgsgg
      541 aynnnrkasf snshdqqyty naffeynktl ngvhhlsama gaefydykyy yntgyaqgap
      601 tdlipwltas tvpsvvnggi qnpagassdf sawerlssai grinysykdl yfltanfryd
      661 gssrlssqnh ygffpgvslg wnmqkedffk nsniskivst frprvswgen gsiqsfkdak
      721 gnqiyfptaq vynnagiyng nggtyvgsyi ntdlkweksa stnfgadigl wndritligd
      781 yfirnvydki aslgidptsg fssyttnlge lqnrglelsl nariiqpiqp dglgidfnan
      841 fytvknyaik lpfnglpgnr qstmqvwdpn hpgqlmqvgg liegqrvgld evwapkwdgi
      901 ytsqdminad anvynaflpy knktlkqlgd akwhqvyknd tidsrqfvyv grttptvsgs
      961 fstnisykgf slyaafdyal gfvilnnekl rglsqvqgsq nstvdalntw sptnpngtlp
     1021 rfywanqgrn fatdasgnnp panmwekgdy valreltlsy dmtqnllkrv fvnkvkalrv
     1081 yvsggnlayf tpysgnfpet ggidngkypl prrltfgatv sl
//
LOCUS       WP_119988841            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119988841
VERSION     WP_119988841.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117426
     Region          74..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhlyikitrs lllsslavtl ivsntngqvt vpkkntenkv lrsdslfvqg vielastkar
       61 lsgislsvpd ysaaitdnkg rfkiavpsys svilisgdgf qqkqvalkgr kkvvvsmyee
      121 pytsqfdvtt lpfgdkpkdf ipyatqslna dnkweqstne tpmtylqgki aglnvirhsg
      181 tpgiganvtl rganslyatn qplivvdgvi ydnneygnsl itgnmynpls didvkdidni
      241 tvlksgnsty gtkgangvil ittaraqela tridfaaygg fnlspndlpv mqagdyrtyl
      301 sdllkttgmt qdeiqkmpym ndnmsspnyf ryhnntdwqk evmknsfnnn yylkvtggdn
      361 iakyalslgy lksqgvldnt dltrfqlrfn gdlnlskklt aavnlalvsn qensqiqgge
      421 nilsplslsl akapflpvhv igddgkispn ladydifnms npvaiaqnmq ganknyrftg
      481 svkfnykfnk slslqtllgi tfdkvqedlf ipqsgvvpdt latavaynrs gsnleryysl
      541 fndtklsyah tfnlvhklni dagfryqnnk seneyglgyn satdqfvsvg mgvaslrsvg
      601 gdigewnwln tyfhagysyl dkyfasfnls sdgssrfgkq apdgvniagn kwavnpslal
      661 awlmssenff snikfvqnlk lrasysrvgn ddignytarq yyisqnllgl eglvrgnign
      721 pqlewetvdk ldlgldasfl nerlnlsvdl yqnktyhmit idptnsatgi nyvianngtm
      781 snngielsid griinkgfkw dmglniaank nkidkfpngk lltsyadaty ltetgkasnl
      841 fygyktngif stqaeaaasg lqyqnadgtm spfqagdvrf vdvngdhvin dddrqvignp
      901 npkffggfsn tfswkrwald aiftfsegnd iynytraqle smsgygnqsl avnnrwrsdg
      961 qitniprvaw gdpagnarfs drwiedgsyl rlrtlslsyn lpikasalky lkvyatgnnl
     1021 itwtkylgyd pefsatnsvf gqgvdiglep iyktvqlgvr lgf
//
LOCUS       WP_119989179             978 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119989179
VERSION     WP_119989179.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 978)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 978)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..978
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108504
     Region          104..977
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlinrqvney nmlsilktks rkgilqlglv isfvlflnis vfsqvtnykr vdtaiskids
       61 aalqkedfls tkdsaeiqqe lgnttylknr ffigdrniqq qdnvaavsti yakdvsttpv
      121 rditnvmagr isglytlqts gqtgadaasf llrgqsplfv idgvvrsftd fnpndiksit
      181 ilkgalasam ygirssngvi sietkdkger nfelhfsaqg gissptvtpk ilnaydyakl
      241 ydkaqlndnp satpkytdsl lnayqngtnd pflspnvnwy nvvkkyvniq hynidmsgyg
      301 ksyhyfasle nfnqggnfvt spintyntnn kfnrynirln asvdfnkdis ldirlfgsia
      361 nsaepgssiq simssiystp playpvfnpd gslggstift nnidgqtlhs gyllensrtv
      421 ttdvklkykl ddllkglwas glvsinnqyh etinreksfa iyqysppqgg npasylkigs
      481 dgtvgngsyt lnsqyttsyy niqmgldrgw aksklhilga ynvendvatl nqlneiyrta
      541 sitanysydd kyiaelssay sglnyyppgh ryaflpsigl gwiiskesff nantvnflkl
      601 rasigqtang npgyfsyiqn yiingsgtni gatstnvtta yengianpni twekawkgdv
      661 glemamfdsk fssnidyyyn ryydqlitpp eqsgifgnty pqinvgktry sglelalgyn
      721 nndhkvqysi ngnvsiaank vlyaddpryp yswmyhsgip sgtmfgyqai gfyqtgddfq
      781 niphidgytp qagdikykdl ngdgvinfld ekplgttapl ityglngris ykgfdinvlf
      841 qgvqnsnlyi nptspliqef qngngivqai hldswtpqta staiyprlti ggnsnntaas
      901 sfwmkngsyv rlknvevgys vpqrwlnhak frqirifvna ynlvtwahls awnldpetgv
      961 nsyfadprvi nagislkl
//
LOCUS       WP_119989238            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119989238
VERSION     WP_119989238.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119504
     Region          27..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkikyiisi alllstqlic aqtqliikgn ikdavtgesi snatvhalgs gryalsdkeg
       61 sfviksksnd tllishigft pqkisvgsnh fisvllnetn tsladvtint gyqnlkpnev
      121 ngsyvvidnk klnqqtglni ldrlkgvtss llfnvgkqnn npqnktgiti rglstingpl
      181 dplivvdnfi ydgdinninp ndvesitilk daaaasiwga ragngvivit tkkgqfnqkl
      241 hvdfnsdvim tdkpnlfyqp qissadyidl eqylfnkgyy nsqlnsrshp avspavlifk
      301 ekqqglisat dsasqinalk qndsrrqfek yyyrkgltqq yalnlrggsq niawlisgdy
      361 dkdinnlsaq ynkinlrfen tyrpiknmtl nagvyytnsn nisglpsysn vislngtiqv
      421 pylnlagpeg qsiavpyayn tnyidtagag klmdwnyypl tdykhnvtta nteellanag
      481 lnykiiqglq lsllyqyqkq nvqtntisdt asyytrnlin tysqldrntg vinyiiplgg
      541 ilkkgyanlq synfrgqlnf drtfhqkhhi naiagmevrn ewasgsnaiy ygynpdplty
      601 tssinyntry ptfitgssay ipgtsslsst dnrfvsffsn adyiyndryi vsasmrrdgs
      661 nifgastnnk wkplwsaglg wniskenfyk igwlpylkls atygvsgnvd lsktalpvgn
      721 mainnitgfq derinyinnp dlswersyqt nlridfatak niisgaleyy hkkgrdlyap
      781 ipydyttwgl sstitanvad mkgngvditl hsnninrdfk wttdflwsyn tsittayhtd
      841 naasayyllq ggntinpiig kplyaiaayk wggldaqgnp qgyigdtlst dyagidvnay
      901 erglksgsfv yvgpasptif gslsnefsyk sfalsfnity kfhyylfkps lsytalatng
      961 tggidygqrw kqsgdenktn vpsfvyplns drdafyngst invikgdqir lqfinlsysl
     1021 lsnkknlpfn slqiyinaan igilwrannd hidpdyangi pnpktytvgi ranf
//
LOCUS       WP_119989340            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119989340
VERSION     WP_119989340.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117493
     Region          44..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyivtvlic fgllgfcgkq slfaqsnnss keittkssgd sviisgllkd sktnlplpsv
       61 sisvnypknk ivglsdylgk fsvkvkrgae llfsyvgytn gsynaskdnv sdveismvek
      121 aagglsdvvv ssfrtterat ftgastiita kdikdqpann vmellqgrva glniqnnngt
      181 pgvmgtvqir glstaavsgs gnnaflqpts plyvidgvpi dvntnyqygf nssapgvnpl
      241 slipaedves ievlkdaaat alwgskgayg viiittkrgn sqvpivqyis nytynavpkl
      301 rpviggreer dirlaeimny dtafyhglan inttpflsds lnsyydnstn wqaiyfrptf
      361 sttqnismmg gndkfnykin vgyqkssgii kgtgfdryni dmstmynpse kfkmsvsint
      421 glgktnygsg nafqqdnlsg vaqassllpp pnlyspisaa lgslvqndnk agnisgnldl
      481 efepvrnlrf ittssytins ntsrnftpsf lnggssigrw yndrnytlyn rqslnyntvi
      541 kdkhsflffi fnelnsssfr aataeayafp ndniqgptgy qhygamqgvl dnlsearsaa
      601 fggdfsynyd kkyvvefqlr edatsqngps vgytknptvs arwnfnkekf menltwldyg
      661 slrfsygkni vpqgdifday gkynfganfn gaqtvnvdfg ylpnhtfkpi qntqldfgye
      721 ssflngrlsl vydyyykmvd nqsfklalpn ssgftnintn avsqvnyghe vtlsvrplse
      781 hsafkwqlsf nithntnvls alpdglreyv ivlpdgaggs vpilyrlgsn tftnflyntk
      841 gvytsnsqvp vdpitglrqs irgvplmtgg pifsdvngdy kidandeqal gdpqpkyfgg
      901 fssylswkqw slstnvsftl drdvinesqs ylfnqyaspy tqnalppfng lnvytkngqi
      961 gatypnpynf lynayydpfr inqtlfmqdg syvkinqiti aytvipkfsk rygissarfy
     1021 ltgnniatfs pytgpnpeni tdlgrdnpnt ypnsrnytlg lnlqf
//
LOCUS       WP_119989648            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119989648
VERSION     WP_119989648.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117412
     Region          32..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkifpslff lfmlictisl pnglfaqgah fitirgvvtd nlnrpllgvt vqaqgaknat
       61 qtnasgafil kvpkgtellf tyigfenksv ligdqstitv qmmqskgeel nqvvvtamdi
      121 krnarelgys tqtisgadiq etqrqnfita lqgrvsglti nptsgmagas aqivlrgfns
      181 lslnnqplfv idgvivdnst fnetsnggsg iglasdranr tgdynnrisd inpndiasvt
      241 vlkgpeatai ygsqagsgai iittknpntn ggvsvnynns fqitnlnrfa ptnndfgpgs
      301 nglpaitlgs syysyfgpay pagtkmydni gnfikngfan tqnisadfgt knvgfrvsgt
      361 yfnqdgvipd ntykkvnfti anttkigkii tltpglsyta snnkspirgl yglmynlyrw
      421 pttdnmedyl tsdgqkrtlf ytnpntdfdn pywftknvhq gsendryiak lgvdihplsw
      481 laisgrfgyd tykengyefq gpesyelsta sggyldnyyk kyigynhtin itankkfgkf
      541 strlmvgtmw qdyktelyav sgsnlidsmp natdssntlq ssrirllrny ngepniseta
      601 qiayygeavl gydnvvfldf tqrfesssvf pkafrnynyp glslsaivsd ifpniksqng
      661 lnyfklrasm akvahiappy tnqsvfgqny assnypliys ygyfnnnfyl apefqktydi
      721 gtelrffndr ltfnadyyns hntnqinvgf rasyatgfvl ntqnaaetrn qgieftlgvt
      781 pvqnknwnwn lefnfahtws kvlalpnsid ssldyylsdt waagnarsga vrgypvteit
      841 gynykrnnqg qilidpksgl plintsfnpi gdrnphftlg tnsnlsyknw slsmlwdlri
      901 ggdifngtdq fltaigkskr tadrltprvl kgvladgmen sdnptinniv ltpyynnvyy
      961 tsdvnglpee afvqknvnyl slrdvtlsya fnkkvlkrik vfkslsaflt cnnlilitny
     1021 lgadpsvnin tagengvggf gfdyltpatp iaynfgirvk f
//
LOCUS       WP_119989700            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119989700
VERSION     WP_119989700.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119768
     Region          36..1086
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkeqgifil nkyvkafmll faifsscmay aqenvkitgk vvdskdhtpi skasiylngk
       61 kkgfftndng dftatvpsna iltisyvgyl piqenvdnrt dlviqlerdt talndvivta
      121 lgisrsgqsl gyavqtlkts dltqaqdpnl vndlsgkvag vqitnggagv gsssrivirg
      181 ensfsgsnqp lfvvdgvpin netyfnnave nssnqgtwae vdygngaaei npndiasiti
      241 lkgasaaaly gsraangvvv lttkkgkted glagvtinsn ttmetplklp hlqnqygagv
      301 nayplsgapn tyqylngggs aennipnwgl kfdpsllvnq fdgmvgsdgl qaadliargs
      361 sstpitatpw ighadhfkdf lqtgittqns vefggsnekg nfhmsfsnlf nkgilpntdl
      421 kryslslran hqfskhlstn vfldyinsss dnrpnigygs esvmytffgv ygmpmnidin
      481 slkkkwqvgq qdraqfrywn nhdnpyvtle dntnsfiknr lignaslkye fnpqfnlmlr
      541 sgidyytdnr eghrafgtvr fpsggfrtdd igyfenntdf lftyikpstg kfnmrlsggg
      601 nkfmqnityt rdianalitp glynfsnaqs qlptfyqken keiyslyafg dfdynkmlyl
      661 ditgrndwss tlpaannsyf ypsasfsaiv snmvhlpsai sylkvrlsaa qvggdaqpys
      721 inntyltntp ygsypltttn nilansnlkp sktntyeggi evrflqdrig ldatvyhslt
      781 kneivqlpvp vssgytnayv ngatianngi eimlnvtpvl tkdftwnssf nfshnvgtvk
      841 alpegiktyv yaqvtqydry yraiqydavv ggklgnmygn gfvrdskgnv vykngipqyt
      901 ssqntllgny npdfilgwyn tmsyknfdls ftwdwhqggk yysytelgvl aggmsvqtlp
      961 gretgiigkg vmddgtgnyv pntvrvsaad yynayynasn nealmydety lklrevrlgy
     1021 tfkhpfgrks nasmnvslvg rnlleftqnk dvdpetlalr gqqilpgief lsvpstrsyg
     1081 lslrvnl
//
LOCUS       WP_119990437            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119990437
VERSION     WP_119990437.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119611
     Region          24..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhfiillsi lfigvqyisa qenfivsgki tnennellpa vtihesnngr saisrekgif
       61 qikvqrfpdt llvsrigyql kkiivrnssa pltitlltdn valedvtint gfqqlktnev
      121 ngsyvvidnk klnqqtgvni lqrlngvasg vlfnlgkann npqnttgiti rglstingpl
      181 dplivvdnfi ydgdinninp ndvqsitvlk daaatsiwga ragngvivit tkqakfnqkl
      241 qvdfnsdlit tdkpnlyfqp qissadyidl eqflfnkgyy nssinsyyrp alspavevfl
      301 arqngaisaa dsatqintlk sidnrdaftk yfyrkgltqq yalnlrggss nlswlisgnf
      361 gkdannlkaa yqkanlhlen tykpiknlsl niglyytnst ntsgepdynt vsqingnvhi
      421 pylqlvgstg daiatphyyr lgyidtvgag rlmdwnyypl tdwthasakn niedviahvk
      481 lqyqivrgln lniiyqyqrq qthnkiifdt asyfardlin sfsqintqtg tvkyivpiga
      541 ilsetnsney aqdlrgqlnf drsfndnnql saiagfefrs tsnddknnyy ygyvqdplsi
      601 anvdvvnsyp tyvtgnysql tgagdpsqfy yrfvslfgna syiykhkyvl sgsfrkdgsn
      661 ifgantndkw kplwsaglgw elskesffhv hwlnhlklsa tmgysgnvdl sktalpvggs
      721 gtnnstqlpy irinsinnpd lkweqayqsn lridfttihn ilsgsleyyh kkgtdlyget
      781 pydyttwgeq stivknvaam vgngvdinlh snninrsfkw ttdfwmsynt dkttsyatda
      841 vsqlaslgsg ttitpivgkp lyaigaykwg gldnqgnprg ylndtlsedy isilqsnttd
      901 gikgnsfeyi gpanptfygs ilnefaykri slsfnitykf gyyllkpsls ylnlintgtd
      961 gadyakrwqq pgdenktnvp gfsypineyr dafyngadin vvkgdhirlq finlsysifk
     1021 dkdnaalkgl evylnaanlg ilwrankdgv dpdypntppv pkaytigfra nf
//
LOCUS       WP_119989960             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119989960
VERSION     WP_119989960.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108093
     Region          29..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkckqllqfl sfafllllgg sataqqthti sgvvtgqgnv pmagvsvlik etgkgtftdp
       61 sgvykilada naktlvfsyv gyrkqelpit sdhinaalyl dssshltdvv vigygavrkq
      121 dvsgavttlt tkdfqkgtit sfdqmiagka agisvtsngg hpgsggtirv rgistingss
      181 dplvvvdglp fsgyvnpndi atitilkdaa saaiygsqas ggvilittkk gtpgqvklnf
      241 ntqfsvakik kyvdvlsanq frnyintnpy fdstersleg tantdwqkei yqtalttnns
      301 lsisggvgkl pyrlsvgyln qdgilktdkm krttgslslt psflqnhlkv elnlngsltk
      361 nynanqgaig aavvydptqp vydpsniffg gyhqwmnggv lnpnaalnpv allmqrddes
      421 kynrgfgnlk ldysfqflpe lhfianfgyd vattngftre dstsanawka nndaargtnn
      481 iynnknqnvl aeytlnydkt fssikshina matyayqdtk ytnnnyrnyd fagdtipgst
      541 pvlyptglqq nslvsylgrl iytydekyvl tasirrdgss klapgyrwvt fpsvslawni
      601 akenflknsk tistlklrvs dgktanqggi gnyqfypgyy lsdnvskyqf gdnyynmytp
      661 spynealtwe tttsanagid fgflkdrisg sidvyhkhtk nllinallpv gtnftnqlig
      721 nvgemvskgv elnlslipiq ttdaqwtinf naaynnskit kltqnpdssf kgipvggisg
      781 atgqtiqeey vgqepnsflv ykqvynsqgk piegayadln gdgainpidd qyfyhspypk
      841 wtlgfstnft ykkwsfstvl ranignyvyn nvasnmgvar nmainnylan astdilntnf
      901 igsnsydmqs dyyvqnasfl kmdnigisyn lgkifhsdrt nltisgnvqn vfivtkytgl
      961 dpeiysgidn qlypnprvyt lglnlnf
//
LOCUS       WP_119990696            1049 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119990696
VERSION     WP_119990696.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1049)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1049
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112844
     Region          32..1048
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksnlrffk tfllavivlc mqnnsfaqtg yisgsvksnt gdplsgvtit vknskahdit
       61 kadgsfsika qrgatlvfty igyetqtlea nsdilnvvli paqaasagde vivtalgikk
      121 kskslgyavq evsgqtlada kepnlvndls gkvaglqiir sgngpgassq ivlrgnnsit
      181 glsqplivvd gvpydnftga snndfwnpsl dmgngladis aediasltvl kgpaaaalyg
      241 srggngvimi ttktgrkqng lginvsssig vesifanpdl qntysagtlg iygptasqsw
      301 gakiagqtvq daagnnvvlk phnnvanyfg ngiasnqsis fqqlinntsi ytsynrmddk
      361 siipgakltr nnittrvttk fgtdnrwsld akvqyinsaa nnrpqggaav qgnntffaty
      421 llppsiditq yrnavdsagk mrwyaggnaq npywaakyrl nsdardrflm hgilkyqfts
      481 wlnaqieggs dmytintenk myagspaskt gnygvgkstf retnystlit askdnvfgkl
      541 ggtisvggnl msqytsnigt svgllvvpdy fsvnngagnp tvssgytner insvygtael
      601 nyddyvfltg tlrndwsstl spanksyryp svslsyvftd minkvgghlp swisygklra
      661 syasagdglp pyslyntyii gkdpngntta qngsntlfdp nvkaeliksy eaglemrflq
      721 srigfdlsvy kdnavnqlir lpmnplsgys ykminagniq nkgieliada kildnptgfn
      781 wtstvnwstn dntiqslygd vktyslggyd nlavvaevgk kygeiygsyf drvtdktspy
      841 ynqliltntg lpqtapnqat kdlgnqqass llgftnsfsy knfhlsilld arfggkifsg
      901 tmdalelngv saltvvngsr dsmlvkgvid ngsgsytqnt qkvspqdywk qigatggnlg
      961 ineanmydas nirirniqlg ysfsrkmltk tpfqkamlsv smnnvwliss hmhgldpesv
     1021 yatstnatgf engaapttrt fyinlnlgf
//
LOCUS       WP_119990665            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119990665
VERSION     WP_119990665.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116432
     Region          25..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqklllllc fgmflfagka fsqdisvsgt vknakgeaia aasilvkgtk qgaitnsqge
       61 fslkvkngdy lvisaisyet qtvkvnssem dvilkeqdaa ltevvvtalg rslnkakigy
      121 stiaftadqi sknapvglld nlagkvpgaq isniggpgss tkvilrgyga iaggsnapll
      181 vidgvplann spagsdntdf gngindinpd dvesenfllg taataiygsl akngaiiitt
      241 kqgkagnlki ayngginfsk vgklpkmqdq fgngwgfefi pgengswgpk ldgvvrpwgs
      301 vvdnsqlikp fsfinnnird fyttgvegnn nvslsggneh nrfyfsygnv ssngviptqs
      361 dllqrntfsi ktntnygkfs fnsffnyinr kqnapntgqa sangggvfes llqipvdlpi
      421 kdfqlyknkf fnvdnyftpy aenpyyglne ngdqqrsdrl lgnleakyef tpsfsalyrl
      481 ggdfentrtq swnqpnapas gswngpnptn tegatrkvdp gsyekynqfy gtinmdfive
      541 ykhdlsntln ldiigggnyy qnsyeatdal vtnlvipgff nlsnsnqppt atgsttrsrs
      601 vglysqatla fknqlyltgn vrndwfstlp ieknsvfypg anlswvasnt fdlsnssisy
      661 lklraaygvt gsapsayqty nvlnatnigl gfgsltspfn gvssflvsnn ipnsqlkpii
      721 tkeleggfei kalhdrigld atfyhritqn qifqvpvaps tgyttlvqnl ghvrnqgiei
      781 afnatpiksn nfewninysf aknwnkvldl tggspnpiln taydaelrav vgksvaeiya
      841 ptpqlspsgq ivvspttgfp lvnttpntad nnitkrdygs alykytmgfy nswrykdvsf
      901 dfaldyrfgg vmysgtsdll nfvgnayntt ynerkpfivp nsvvantdgs gkttysenti
      961 aipsedmydy yyptknpala ydsriisksf lklrsvnlsy slpstwangi rvnkilvgiy
     1021 aknlllwtpa snafvdpeat nygtdlngel gefrtaplek efgfvlkvlf
//
LOCUS       WP_119991022            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119991022
VERSION     WP_119991022.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121849
     Region          28..1117
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnikhlqkis vavllvlfsc gvllaqerti ngivvdsasg qqlpgavvsv kgrpsnvaan
       61 aegkfaikvl psdsiivvsf vgyqrafvnv vgqdfvtvkm nstdkdlsdi vvvgygtqsk
      121 rditgsmatv dlkqiadipa asitellrgq vpglhvtgga qrpgdmatld vrqqfnygkd
      181 ggstspivvi ddviqvdpqs glpsqtalqn ldlsevasit vvrdaaaaiy gargsqgaii
      241 vttkrgsiga phlsysakfe rnnavsfgkv mnarqfgdys nkfnsaaghg tdpkymfsds
      301 ellsmdtldy nwlgnawkpa yaqqhsldvs ggtekatyft gasyytqgan lgsqnynrwt
      361 yragtnvkvl sglqlgatva annsdiaksf tkinfsdgya vggeqndysv llhmpqyipw
      421 iynvngvdqy ispplginkt gqaktgssls gwnyyallnn gsqtvtksfn ynvnfsltya
      481 vpyipglafk lnyglsqmss nteqdmfpql lyqdanivna dshlfselgs tdskwksyln
      541 tsgsrvtydn ttskneqsnf fvtydkqigd hsisamasve katntsddrf qiytspdpat
      601 yngtsvsagt idagntytnr faggslsylg rlnynyksky lfqfifrtda stifapqnyw
      661 gyfpaasagw visdekffkd hiswinflki radvgltgns nikpwhwlqt ynaypnkgfg
      721 fgsnggvyvn glvpgvtpna dvkwdrtlqr nfgldmsfln srlsvtfdqy fnsgrnllqa
      781 magalntpis vggafaeqny tninswgsel sigwrdhvgd ftyavgintg tsnykvlkyl
      841 dqpfaypsia ttrmavgneg itpvwgfetw kqtsghdgil rtdadinnyw nylsenaans
      901 giagaapnfm gitsesglkk gmlvykdvag plnannktia gpdgtitqdq dyvklkksnr
      961 tygftsninl gwkgislitq isvgwggtrr ldyikqgtss snatwsqpiy ltdmydsatn
     1021 pngkypniyy ydafggtnsd ffmlptfsav irslsigytl pvalvkkagi qsvrvflagn
     1081 nlwylnnpyp dkyrnmydap nvgyptlrtw alglnvgf
//
LOCUS       WP_119991156            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Arachidicoccus
            soli].
ACCESSION   WP_119991156
VERSION     WP_119991156.1
KEYWORDS    RefSeq.
SOURCE      Arachidicoccus soli
  ORGANISM  Arachidicoccus soli
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Arachidicoccus.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Arachidicoccus soli"
                     /db_xref="taxon:2341117"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121964
     Region          34..1097
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklpyircf avfiftllin sflfaqnaqk rvivrgtvkd aktqlplaga svmerdkdgr
       61 tlngtftdid gnfalrvndp annsiavafi nyvattefik drneinivlk gdnssledvi
      121 vrstntmdng tgmktserns tlatatinqk elenlsspni gsalegrlpg vnisvtsgdp
      181 gaglsirirg tatlngsanp liildgmpys ttippdfnfg tadvqgyaql lnvapsdiqd
      241 itvlkdaaat alwgsqaang vlvintkrgh agkpaisysf qgtyakqppa ipllngnqya
      301 tlipeevant gglpldinan kefsydptdp ywyynysnnt dwikaitqig ysqehdisms
      361 gggdkakyya svgyftqqgt tigtglnrit skinldytvs nrihfrsdft yahltnqldy
      421 ipnksyqvrs vaynkmpnms iyqydlygnq spnyfspesn iqgqypttyn pvalakngiy
      481 eqtgdritps fqlqyqaips vllttfdiqf dinnskshtf lpqnvsglss tdpssnsaga
      541 sdgdvydvyt ktnfiytpks ndenhqlqal lslqtddnky nsynvltsnt atsefqypfn
      601 gsvatnasaa lsstkgevrt vaallqgqyd wldryiinvg arvdgnsrfg psnryglfps
      661 lsarwrmsge kfmqkykkfi ddlsfrasyg hagtappnks iwnyfntyqp ysysyqgqsg
      721 vypsnielsn lkwqtlvgtn lgfnlwmfks rvrldvevyr nrikdmfydn ltipsytgfs
      781 tipanvgtmd nqgwelllnt iplktknwtv gfdlniarnt nvirsispfy pttntptlnv
      841 nglyktylqv gnpfgsfygf kylgvytnkd ativrnaqga evtdpsgqpl ymrfdypain
      901 ytfqpgdaky edvnhdgtid dkdvvylgng lpkitggfgl nvgfkdrlkl itffdyklgy
      961 dvvnqadmnt tnmysfnnqs tavlsrwrnp gditdvpral yrsgynwlgs sryvqdasyi
     1021 rlqavtlryt fsskildkmk irnaafyvtv enlvtftryk gqnpdvsiig nnspfaypvd
     1081 naltppsknv llginvsf
//
LOCUS       WP_119992861             986 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_119992861
VERSION     WP_119992861.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108799
     Region          33..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkslkrcl kkrmilllgf lmmtgvavaq qlqvqgkvtd atgegligas vlvkgttsgv
       61 itdidgnyvl lnvnpdaili fsyvgyqtqe lnvsgrnkid vvlhddqqvl eevvvvgygs
      121 lskkevsssi vqvdkknfnl gamnnpmemv sgkvaglnvn tqaaanpnss sslqvrgats
      181 vsasnspliv idgvaggdir niaaqdiesi tvlkdagsaa iygtrgangv ilvttkrgsg
      241 eagktvvtyd syiafnvakp spdilsadef rrsrrgtdyg adtdwyglit rdvaydtnqy
      301 isidgstkng fygasfnyks angldivsgr eefggrfsme qrvlenrlqf ngslsarrvn
      361 etwgndgffd raltmnptmp vynadgsyyq ptsptgatnp vaelalrdnn gqrmyllgta
      421 eaklnilqte khllnttlsy slhyndmkqq yyassagses ywngykgrae mkyqkwytnr
      481 lewlgnyaln lgdhnikavv gytyeksiwe qiggsnndfs fdntkywdlg sgsylkdgla
      541 slysgrsest ligffgrlny nwkdmlfasa slryegsskf ganqkwgyfp aaslawemme
      601 mgfmkntrkv ltslkprvsf gitgrsdfda ykslstyntn gsylfdgrwv tgyapssnan
      661 pdlaweksva inlgvdfvlw nrlrgsveyf drsskdllyt ytapqppfvy stilvnvgtt
      721 kntgievsld gdiltktavk wtsginysyg ktqltklsnd iykasyldly lkpgtgssey
      781 ffrvqeggei gqfygyeyag vdengnmlil ndkdeqipis qadakykryi gngapkhfls
      841 wsnnltwknf dlsvffrgtf gfdvfnmrky gmglqgcgtd nvlrsayled knirtgggvi
      901 ssyfledgsf iklenvtlgy nftpknrkll dnmriylsak nlftltgysg ndpsiidvng
      961 iqpgvdsnsa yptatqlslg vtlrfk
//
LOCUS       WP_119992766            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_119992766
VERSION     WP_119992766.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114982
     Region          43..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyttlytli lglfsigwtd cpedfmermq rpghseiqls kvtisgrvld esgfplagat
       61 iqeketanga iadsegkftl vvadnavlrv sfigyisqdi evegrstfhi tlredmield
      121 nvivtalgie kkenslsyat dlikneeltr vkmpnlitsl tgksagvrvn qvssglgasa
      181 kvsirgirsv asdnqplyvi dgvpilnsts eqaysaiggt anagnrdggd gisnlnpedi
      241 esisilkgap aaalygsqaa ngvilittkk gqshgqrsvs fstslmfdna falpkmqnry
      301 gvsdgvdswg eranlpeydn lrdffstgvt sitsislshg neklqnyfsy anttghgiig
      361 khnlskhnlt fretsvllns rlkldgsmnl mrqvvknkpt vggfymnplv glyrfprged
      421 isyykenfev ydegrnlniq nwhtsyedfe qnpywitnri lskenrmhvi vslsanlkin
      481 dwlslqargn vdyindkvrq qfyastapal agangryiem dyqetqyygd ailmmkkqwd
      541 afslnaalga sindktvnst rydsktaslk yanvfnlani imngsagldq kidarrqlqs
      601 lfataqlgyn efvyldlsar ndwsstlayt sheksgffyp svgfslifnk lmtlprwvsl
      661 akirgaysmv gndipmfitn psshitagge flasdaapfk dmepemthsf eagiearflk
      721 nriglnatfy ktntrnqffk lptlsgdkya yryvnagniq nvgwevslda vplltnhfkw
      781 ktevnfstnr nkiislheal keflygptsf sssyamklvk ggsigdiygk afvrddvgni
      841 vygtegdntg mplvegdgnt vkvgnanpkl mlgwnhmlsy knfsfyflvd crfggdilsq
      901 tqadmdmygv sevtarardk gyvmlegnri dnvkgfyknv vggragvtey ymydatnirl
      961 relsvgyqlp aawmektkvl kraqlsfsgr nlfffykkap fdpdlvlstg ndnqgievyg
     1021 mpttrswgfs lkcef
//
LOCUS       WP_119992974            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_119992974
VERSION     WP_119992974.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122946
     Region          24..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrvlivll cfvgalssaf aaekkvqgvv issednlpli gasvyvtaed lkkagsaqtt
       61 mgvitdvdgq fsiaipagit rffcsyvgyd vlevklvpgk ehyeitlhas sqmldavvvt
      121 gyqtverrkl taavskldis detigavksi dqalagqiag lsvsptsgap gapakirirg
      181 taslngtqdp lwvldgiple gtdvpepdel nditnmkqss iaglnpadie nitilkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs srftytptls ldrlnllnsa ekvglemdmi
      301 rnnyspdnhk ggvynilsny nelsafqngg wdalssdtqa ainrlksvnt nwgdilfrda
      361 fsqeynlsls ggtervtyyt sfgyykedgn vdgvgmdrfn lvgktsykvn silkvgasmf
      421 anrrkntnyl tdaygmsnpv fysrkanpyf elydkngnyn ydydiqnntd kdlgfnifee
      481 rqntsnesvv nsfssifdae lrfndkwklt sqfgyqlekt sreeiadwes yamryyykls
      541 eysqggetkh flpeggmqks yensnsqitw kamgeyrdsf ndihelevma gtelrktwye
      601 tlfsagygfd rktlttkpvi fpnesyatsf plhqttyken ayvsfystas ysllnrytvg
      661 gsirfdgsdl fgvdkkyryl plysvsalwr lsqepfmqqa kwvdnlvfra syglqgnidk
      721 ntspfllgty rsesilpgvs edviiinsap nkklrwektq svnagfdfsv lnqainlsvd
      781 yyyrkgtdli alrmlpletg ftsmnvnwas menkgveisl strnittknf swytnfnfay
      841 ngnkvlqeni peqqttpgre gypvgaifal ktagvnketg nmmfynpege kvtlkelyrl
      901 kdewgigias sdvtaaeert fysyigssda pytgglintf syknwelnvn fsltfggyvr
      961 tqpsydiinp dygknynvdv lnrwtpenpn aelpafmlsa snpeeyswyd sktiwrdldi
     1021 wvkklnyvrl qnlrlgyrip elltkrlgmn satvsiegrn lfvfgsgynn ymdpesmynp
     1081 yatpvpksvt fslnlnf
//
LOCUS       WP_119993110            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_119993110
VERSION     WP_119993110.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112418
     Region          26..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrimltlv cllaaigwva aqnspitgiv isaednepii gasvlvkgst tgavtdldgk
       61 ftitdapaga kilqvsfvgm itqevpitpg tirvtlknda klldevvvta lgiakkeksl
      121 tystqvvngd elarvkdpnm mnalagktag vqinksssgl ggsskviirg nrsvsgsnqp
      181 lyvidgvpfg sstnentstt iggdndsgny drgdgisnln pddiesmnil kgpaaaalyg
      241 ssaangvvii ttkkgkegra sisfntsttf diaaygipef qnhytgvsts wgsdikgspd
      301 ytddffktgv ttinslslsm gsqamqtyfs yantygkgvv egnslvkhnf nfretanfln
      361 nkltvdanin amyqrgnnrt tsggyymnpl vglyhfprgg veggkdfnyy kdnyqilnag
      421 rnimdqnwyk sqgtdmeqnp ywlinkvpne dtryrtllnl svkykfndlf siqargsady
      481 vvdknntrmy agtspvlcgm npagtgtngr yiygesssls sygdvlftyq qqftnfsvna
      541 svgasindyt gngtgfdsyp gilsvpnvft mqncslnkgs ltdwkthtqs qsvfftgqvg
      601 fkdqiyvdvt arndwtstla ftkyknkgff ypsvgvtwll netlklpswi dlgkirgaws
      661 kvgnglntyt snplnsitks gsinfnstap faelkpemtt siefgtewrf fnsrlefdft
      721 yyktntknql ftldapsgsq yaryyinagd iqntgvevml ngtlvmtkdf rwktgvnfat
      781 nkneakalag ddfgyftfsg gesnnvwsrl evggsfgdiy gttfvrdekg niqyepakeg
      841 qkdsdrlplv dktnpvklgn stpdfnlgws ntitwkdfsl yflidgrfgg evmslteadl
      901 dqqgvskatg dardrgyvml egrqitdveg fynqvggrag vtehymysat nirlrelsig
      961 yslpqawlak tgviknaqvs lvgrnlfffk nnapydpdgm lstsnrlqgv dvfgmptnrs
     1021 igfnlkvnf
//
LOCUS       WP_120006433             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Teichococcus vastitatis].
ACCESSION   WP_120006433
VERSION     WP_120006433.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus vastitatis
  ORGANISM  Teichococcus vastitatis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Teichococcus vastitatis"
                     /db_xref="taxon:2307076"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39395
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavlrerr sgetrvaatp etakklialg nsvaveagag lasgypdaay reagaevaad
       61 aagalsgagi vlkvraplaq gegdldelsl iprgalligt ldavsdpara gayaaagiea
      121 csmellprit raqsmdvlss qanlagyrav vegagafdkg fpmlmtaagt ipaanvfimg
      181 agvaglqaia tgrrlggrvs atdvrpaake eikslgasfv gyedeesraa qttggyakql
      241 saefyakqae vvaahiakqd vvvttalvqg rraptlitap mvasmkpgsv ivdiaadagg
      301 ncvmtrpgea ivtengvkil gyrnwpgria gaasalyarn lltflttfwd kdagaaklpq
      361 edeivrgvtl trggavvhpm laaqpaa
//
LOCUS       WP_120011816             429 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium waimense].
ACCESSION   WP_120011816
VERSION     WP_120011816.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium waimense
  ORGANISM  Mesorhizobium waimense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Mesorhizobium waimense"
                     /db_xref="taxon:1300307"
     Protein         1..429
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44050
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvtvetg agtasripde efakagaaig
       61 kagdaakadv vlkvrrptea emkgyrsgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 agkvvttann vkivghlnvp grvaasasll yarnlfafle tlvdkttktl aikrddelvk
      361 atmltdagkv vhpafakaae ppkgqhvepa aipaktmvaa asvkkaapkr aadkkvatgk
      421 saakpkgia
//
LOCUS       WP_120010744             898 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroidales].
ACCESSION   WP_120010744
VERSION     WP_120010744.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     Protein         1..898
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=98560
     Region          27..896
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgrvslclvi mfficsaqki daqvqnirek qdtisatksl ehirpeyikk gplnnaldvl
       61 sgqsagvnvt tngtdrlaml nsirvrgtts imggndplvi idgvtsdiat lstiypadie
      121 sftilknate tamygsrgas gvieiktkkg tgrgfeisyd gnygfesmyk hlqmlngpey
      181 iataealgld ynnggyntnf hdvitrtgli hqhhlafsgg sensnyrasf gfmdhntivk
      241 vndyrnlvvk ldatqkafdg rlvgdfgvyg ysskihdifd trmlfystaa qnptypagtd
      301 vngnwvknsa ashinhpgal lyekndseer nfnthlglkf nildnlilsa fgsysysstg
      361 naqfcptwvw aqgnvyrgef kgedyftnvs lsynnawgds hldavvgaey lkqvrtglwv
      421 qakgittndf synnigatss rpfggtsssy edpslasimg svtysykdry siaaalrgdg
      481 ssmvsdnntf gffpsvslgw dvkkegflsd tdfitmlklr tgygrsgnlg gitsyttlnt
      541 vkengivsin gaptvtmgsi rntnpdlkwe trstfnigfd lgiwdnrlml tselyysktt
      601 dmlyeydvpv ptfafdklma nigsmsnqgv elgisvvpiq rkdmemninf nmsyqknkll
      661 slsgeyngmh mtasditpig slygagqngg dnnvvyqivg qplgvfylph ckglkenelg
      721 gysydiedln ddgeidfsdg gdryiagqat pkvtigsnis fryksfdiam qingafghki
      781 fngtglaytn msifpdynvl kgapekniid qnvsdywlek gdyvniehit igynipmksk
      841 avkslrlsag isnlatitgy sgltpminsy vvsntlgidd krtyplyrty slglsiqf
//
LOCUS       WP_120025123             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis panacis].
ACCESSION   WP_120025123
VERSION     WP_120025123.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis panacis
  ORGANISM  Amycolatopsis panacis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Amycolatopsis panacis"
                     /db_xref="taxon:2340917"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38190
     Region          8..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maedgsrltv gvvtesrpge rrvalvpklv prlaqrdltt ivergagaga qltddaytea
       61 gaelgdpwqa dvvvkvatpt aeeiaklkrg avligfldpr gdpegiaale kagirafame
      121 avprisraqa mdalssqssv agyravllaa ekltrffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgaqttgydv rpevgeqvrs lgaqfldlgi eavgeggyar elteeeraeq
      241 qrrlteaitk fdvvvttalv pgrkaptlvt eeavrgmpag gvvldlages ggncalsrpg
      301 edvvvygvtv saplnlpagm pahaselyar nvtellellv tkegelrldf sdevvagacv
      361 agregses
//
LOCUS       WP_120028809            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120028809
VERSION     WP_120028809.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117332
     Region          25..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrklmlllv clfvsigfvt aqtstvsgvv tseedgepvv gasvlvqgtt lgtvtdidgk
       61 ftipgvpssa ktlrvsfvgm qqqevpikqg lmkitlkpdt evldevvvta mgisrsektl
      121 gysattvksd eiisarttnv analsgkvag lqvsstssdp gsvsnivirg fssingnnqp
      181 lyvvdgvplq nnmfsgsgkn vatggianvs sediesmtvl kgaaatalyg sraangviii
      241 ttktgkkgdg rnfsisyngs lqarqvsllp emqnefgqgw nggqtfieng swgpaldgsl
      301 qvygpvwnhq qliheysakk dnvkdffdlg wsqnhnials gvsgdskmny ylsysysndd
      361 gimpkdydtf erntiafrgs ydaadwlkvs sslnfartat davgsfqgts vidglfempr
      421 disivdmkdt sspfntpeay ftpygitnpy wslennynht askqiygkiq adikpikelt
      481 fsyrmgfdyt dydvkigspq ialddalidn dygyapsnmn qsgyvyaryg rhlelnhdfl
      541 anyadkfldn rldvninagv nmnersftri tgqtddltfh tgfwdlsnga tkttlgesqn
      601 krrlvglfgd vtlgwddmvy lnltarndws stlpidknsf fypgatlswi ftrlipenkv
      661 lsfgklrlay gktgndadpy qtgvtyiqgv angyygsgia qfpmngsnaf qasntkgsst
      721 lkpemtsefe vglnlqffng rlgidasyyn rttndqiftl pvdpstgysy mvtnfgkvrn
      781 sgvelvlntv piqtkdfrwn ldfnfaknnn kvialpesle ggkvsiysfs agndavymya
      841 eegkpmgqfy tylpkytesg qpivdangqp vlgtsvedtg knmnndwtgg vntaftykgf
      901 tlsaaldirk ggymfsrtkn lmqftgngia ttyngrrpfi ipnsvvdngd gtysenttpi
      961 yqhngsyqty fndygygagg eaylldrsfv klrnisltwd vpkawvrais lsslaltvfc
     1021 nnvftwtasd nnfvdpestt vsqatngdla tqfgelytnp scrtfgcsls vkf
//
LOCUS       WP_120028849             607 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides sp. AM26-2].
ACCESSION   WP_120028849
VERSION     WP_120028849.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM26-2
  ORGANISM  Bacteroides sp. AM26-2
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Bacteroides sp. AM26-2"
                     /db_xref="taxon:2292946"
     Protein         <1..607
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <17..606
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 grldarrtlk slvadlrvki ignifldlni wkgisartqf gldygnaynr avdgvwsetg
       61 grnsdgenyv gsyqshplsy vwtntlsytl stgkhnldvv lgteatrfvq egfsarregi
      121 yledrdfahi gvttgekynl gssadeytyf slfgkanyvy ngkyllsatv rrdgsslfge
      181 nnryatfpaf svgwrikdev fmedfdflsd lklraswgan gsvqglprgy tttpfttnyf
      241 gtsypiqgne sgplysgynr twlgnpdlkw etttqtdlav dfgffnqrlt gslgyyfkkt
      301 kdilvqtpyi avmgeggepw inganmnnqg lefevsfrnd psaefqytis anigtyktkl
      361 telpenvink ypgdgvrdfv igrspnvfyg lvadgifktq eevdnhaeqp gkaigriryk
      421 dldgdgrvde ltdrtyigta dpdffggitf dfkyrnfdln mffqgvfgnq vsndwkrqsd
      481 fwhisgsvpv gknhptrlld awsfdnpdsd ipamtnvmtn neqrmstyyi edgsylklrn
      541 ielgytfpak itnkmmmknl rvyasarnvf tlkkfwgddq ftsfdpemsg ygyltpftmt
      601 fglnvtf
//
LOCUS       WP_120029236             519 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            sinensis].
ACCESSION   WP_120029236
VERSION     WP_120029236.1
KEYWORDS    RefSeq.
SOURCE      Vibrio sinensis
  ORGANISM  Vibrio sinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Vibrio sinensis"
                     /db_xref="taxon:2302434"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54821
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp ksveqliklg fdvvveshag dlasfddasf ieagakvlak
       61 devwnsdvil kvnapqfdad kgidelalik dgatlvsfiw paqqaeller lttknitvma
      121 mdsvprisra qsldalssma niagyrsvve aahefgrfft gqitaagkvp pakvfvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv qsmgaeflev dfqensgsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgrpap klvtkemvds mkagsvivdl aaanggncey
      301 tvadkvittp ngvkvigytd mvgrlptqss qlyatnlvnl lkllckekdg titidfddvv
      361 vrgvtvvkdg eltwpappiq vsaqpeqkpa aqpkgpakkv depispkkki aalaiglcaf
      421 gwiasvapaa flahftvfvl acvvgyyvvw nvshslhtpl msvtnaisgi ivvgallqig
      481 qgngvvtfls fiavliasin ifggftvtkr mlemfrkdk
//
LOCUS       WP_120043402             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            panacis].
ACCESSION   WP_120043402
VERSION     WP_120043402.1
KEYWORDS    RefSeq.
SOURCE      Nocardia panacis
  ORGANISM  Nocardia panacis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Nocardia panacis"
                     /db_xref="taxon:2340916"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38054
     Region          16..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mettqsagdi sprgarvgvv resnagerrv alvpkiiagl lkqgvevvve agagagalip
       61 daayeaagar igdpwsaevv vkvappndae varlsagqtl igflaprdav nqigklkaag
      121 vqafameaip risraqvmda lssqanvagy kavlvaaqds trffpmltta agtvkpatal
      181 vlgvgvaglq alatakrlga rttgydvrpe vadqvrsvga rwldlgidaa geggyarelt
      241 edekaaqqqa ledaikgfdv vittalvpgr paprlvtaaa vagmrpgsvi vdlagetggn
      301 celtvpgqtv vehgvtiasp lnlpatmpeh aselysknva allelmlseg riapdfddrv
      361 ladscvtreg es
//
LOCUS       WP_120053166             259 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Salmonella enterica].
ACCESSION   WP_120053166
VERSION     WP_120053166.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         <1..259
                     /product="STM4504/CBY_0614 family protein"
     Region          <3..123
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 tlycyhnshs devyrrickt lrkeyglftl yahstsylde msnlllktdd krkhidtiel
       61 afnyidtylr tyevtlglep dkaiselnnl fhehglkyry engrivrlrr ikrlknicyy
      121 lyspgeygfv eydlmeaynr lilndfacvv kechaafrsv ilriherkgi vyheqdslnt
      181 lmanlmargv isaeyvhkfh flsdvlesei flpmapeksh hhyammlris eelacsiyyl
      241 tersiffltq raeedgvsp
//
LOCUS       WP_120060808             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides cavernaquae].
ACCESSION   WP_120060808
VERSION     WP_120060808.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides cavernaquae
  ORGANISM  Nocardioides cavernaquae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Nocardioides cavernaquae"
                     /db_xref="taxon:2321396"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52235
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigvlkeaq agetrvaatp atvvqllklg yevvvesgag elssfsdeay veagasigdp
       61 laadivfgvn tpsiaqrdgl rpgatliail narideetva dltqrpital amdavprisr
      121 aqsldvlssm aniagyravv esahqfgrff tgqvtaagkv npanvlivga gvaglaaiga
      181 agsmgaivra tdprpevadq vrslggeyls iespevevsa tgyakemgdd ykareaelya
      241 dqakiadiii ttalipgrpa priitaemva smkpgsvivd maaqnggnve gtvkgekvvt
      301 angvtiigyt dlagrlpaqa sqlygqnlvn llklmtpekd gqlvldfddv vqrgvcvvre
      361 gestwppppv qvsaapaaaa aaapveskpk kvtsqstkla rvaiaaavlf aliaispaal
      421 qihltvfala ivigyyvigh vhhalhtplm svtnaisgii vvgallqigq dndvitglaa
      481 vaillasinv fggfavtrrm lamfsrs
//
LOCUS       WP_120067186            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120067186
VERSION     WP_120067186.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116832
     Region          42..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mynivtkisr rfyfvllamg mlwgmmspkv faqevggtsi igkvvdqygn pvpdvtitmk
       61 nsdfkvitgi dgvftfqmkk gdvlrlshpe fihkevkvnk lkntervfkv tlneqfiknr
      121 etvsgpyepk nkknylgsaa tvytddlssm mgttilpalq grmaglnvsq yagarahqia
      181 ansrndligs vplfgegfys dntefgigsr gngpvvvvdg iqrelysldp eaiesvsiqk
      241 dalssmflgm rssrgallit tkepinegih lsftgrfgvq salktpkpls ayqyayllne
      301 alqndgkdpl ysyddfnkfr thsspythpd inwfdeilnk nattqaynln vtggnrvtqy
      361 fvsvgyqgek glfanptdnd ahdtnlsysr ymisskvnin itddftakvt llgrvedgnq
      421 pgvsygslln siyntpnnay piknpngtwg gnktfdnnlm sqsinsgyik dsardmvggv
      481 nlkydfgklv eglsvrmvgn vsiqnrsyvq rskrapvyay gfdkegkefy tlhgatntqs
      541 nffnsvtsyq qmygqiavdy nrrfgkhgvk atlmsdtrqt lvnydlpqlp sniigdvayd
      601 yaekyfvqaa lsesyfnrya pgnrwgtfya fgfgwdiske nfmedanwld qlkirgtfgk
      661 tgngmdnsgy ygyrqtfssn vaagypmgtn lgmgnltten tplanpyltw ekayklnvgv
      721 dlslfnnrlk ltadyyndky fdllqsrgks iqligqyypa enigkvrrfg gelsltyqdr
      781 vsnfnyyisa nwscdqskll ymdeqyvpee ylrqtgrpvg vmyglvadgf ftskeeiens
      841 pviegfkniq pgdikykdln gdkvinefdr tviggdkpys yfginlgfew kglefsmlwq
      901 gaynrdyylg dvtltegfqq ngqfygqaye nmlgrwtpet aetatfprlt aggnnynrgn
      961 gwnssfwlrs gnyirlknis lgynlpdsfc rnnlgglrvk lfvngqnlft ksacdlvdpe
     1021 vsftsyplqr cistginirf
//
LOCUS       WP_120067661             998 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120067661
VERSION     WP_120067661.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110702
     Region          36..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnihfktct cllgillmlf sgiqargasl evqqerkisg tvidekgepv igasvvvvet
       61 kqgtitnidg kfqvnapqng rlkisyigye tqevaikdrq slkivlkees talnevvvvg
      121 ygtmkrkemt saishvgakd lnqissldas mllqgkvssv svsntaladp nstgsiqirg
      181 issrnaglgp livvdgvpgg dmtninpadi esidvlkdga asaiygtrgs ngvilvnlkk
      241 gtrdgevhtt ysaavtfnka kkeldimnae eyrayrtvsn plsdmgastd wfdavtrlgv
      301 thmhtltfsg gnartnyrvt adyrkaqgid lrsdrreyga ratishttkd glftfaanmt
      361 prvidrnksa svygsviknn ptmpvydpes angyyrfpsg gdssniveql neeengteik
      421 llewnataav nllplfnpnn pnmvlksqvt vsqyqvdkfn gwfipstygp nvnsgvagka
      481 srdfdkntnn nlewvtnfst rikdhqiram vgysynygvs sgmgaenwdf ssdgltynnl
      541 gsgleaakeg ktmmssyknd hklisffgrv nydwkerylf tfslrhegss rfgenhkwgn
      601 fpavsvgwri sdekfmkgfs widdlkvryd ygvtgnqeig nyqslatyra ygwyqyggnn
      661 fhvwgpsknv nselrwekgh nqnigldfsl fkhkvtgsfn yfhrkqsdll gsysvsvppn
      721 lfstiyanvg tlrntgfeld itvnavrtkd ftysftlvga tnnnkfvsfs ndvykgqkyy
      781 stcnmanpnn pgylqrieeg erignyftyr yagvdkkgdw liydkkgnvi pvaqgteedk
      841 avtgnglpkf tgsmthnfty knfdltvalr gaagfdlfnv hdfyfglqsm stnqlttays
      901 knahittgkn vitdyfiepg dylkidnitl gytmnlnkky iekirlfgta nnlytftkft
      961 gvdpstyevn gltpgtfggg ynyypsafqf ilglqvsf
//
LOCUS       WP_120068268             914 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120068268
VERSION     WP_120068268.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..914
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101310
     Region          38..913
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvqharlify sllllvipce gtlaqkipva pidslitvgy atgslktlsg svekitetqm
       61 nkdqitnple airgrvpglt iqrgsngpaa ldavrlrgtt sltsgndpli ivdgvfgdls
      121 mltsiyptdi esftilkdas etaqygsrga sgvievttkk gmsgrtqvay ngsfgistvy
      181 knlkmlsgde frrvasergi sildkgnntd fqkeieqtgl qqnhhiafyg gssessyrvs
      241 lgfmdrqgvi lnedmknfts nmnmnqkmfd gflncelgmf gsiqknhnlv dyqktfysaa
      301 tfnptypnhk dpvtnswdgi ttasqitnpl awmevqddda tshistharl tfdlmeglkl
      361 slfgaytyni vensqylpts vwangqaykg tkkresllgn mmltykknwk khffdvlala
      421 elqketytgy yttvsnfstd kfgynnlqag alrlwegtns yyeqprlasf mgrfnytyad
      481 ryvltlnart dasskfganh kwgffpsasa awviseeefm kqfpvidnlk frigyglagn
      541 qsgidsyttl nlvkpngvvp vgnsaivslg dlrntnpdlk wevkhtfntg fdialfgnrl
      601 llsanyynsr ttdmlylynv svppftyntl lanigsmrnw gteiaigitp lktkdmelni
      661 nanitfqrnk llslsgmyng emlsaseyks lasldgagfh ggynhivyqm vgqplgvfyl
      721 phstglesdg nggytygiad lngggvsled gedryvagqa vpktilgsni sfrykrfdls
      781 lqingafghk iyngtsltym nmnifpdynv mkkapqqnik dqtatdywle kgdyvnfdyv
      841 tlgwnvpiek vqklkkyvrs lrlaftvnnl atisgysgls pminsstvns tlgvddkrgy
      901 plartytlgl sinf
//
LOCUS       WP_120069322            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120069322
VERSION     WP_120069322.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117052
     Region          4..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrisssrtl rityvgmkpq dvpikpgtik vmmksdsevl qevvvtgmqk mdkrlftgat
       61 kqldadnvkl dglpdisrgl egraagvsvq nvsgtfgtap kirvrgatsi ygsskplwvv
      121 dgviledvid vgpddlssgd aetlissaia glnsddiesf qilkdgsats iygaramagv
      181 ivvttkkgra gvskisytge fttraipsyk efnimnsqeq mgiykemeqk gwlnsadlfr
      241 tkdtgvygrm yrlideynns ngqrgllntp esrnaylrea emrntdwfdv lftnaisqnh
      301 svsvtagtek ssfyaslsam ldpgwykqsk vkrytanvnt tynlyknlsi nlisnasyrq
      361 qnapgtmsst ldiasgkmsr gfdinpysya lntsrtldps adyisnyapf nilheldnny
      421 ieinmvdvkf qgelkwkviq glelsalgav ryqtssqehn vlddanqava yrtgmddati
      481 reqngllykd pdnpyalpit llpeggiyqr qdrrmlgldf rgtlswnhlf aekhitnffa
      541 gmevnslkka yssfqgwgmq ysmgeipsyv yqffkngies gsryyslghs etrsiasfln
      601 atysydgryt lngtfryegt nrmgrsrssr wlptwnlsga wnvheeaffk alqptlsnlt
      661 lkasysltad rgpaevtnsq aiirsfspyr pftdiqetgl yiediensel tyekkhelni
      721 gidlgllenr infsadwyqr nnydligvvp tqgvggfink yanvatmksh gveftlstrn
      781 irtkdfswnt dfifsyakne vtqlkgltsm melvsgngfa regypvrglf sipfagldad
      841 gipqylidgk ltttgvnfqe rekldylkye gptdptvtgs fgnvftykgf klnvfmtysf
      901 gnvvrldpvf nykysdltam prefknrwtv sgdeaktnip viisdpqyqa ntslylayna
      961 ynysteriak gdfirmkeis lmyefpkswi apakisnlsl klqatnlfli yadkklngqd
     1021 pefvntggva spvprqftlt lrlgl
//
LOCUS       WP_120070144            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM37-9].
ACCESSION   WP_120070144
VERSION     WP_120070144.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM37-9
  ORGANISM  Bacteroides sp. AM37-9
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Bacteroides sp. AM37-9"
                     /db_xref="taxon:2292951"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116888
     Region          22..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknyflflff lvisvsgyaq gkritgkvtd aadgmpiiga tvvavdpdgk tnaksvgtit
       61 dingtftlhv pngcqelkfs yvgmetktak itglthinvs lastakalde vvvtafgvtr
      121 eakslnysrq svnaealaen ssgnlissls gkvagvtitp pgtsngsari virgtsslte
      181 nsqpvfvidg miienepgdt svtvdggtgs tdlgnpvadi npddiesiei lkgpnaaaly
      241 gsraaqgvvl vttkrsstfe ktkvsysgnf qfekvnqfld yqngwgtgen sylldhkltl
      301 qpngnrlqtd lpdfsgynss agaklrswga plwdqviygh dgvltthssh pdnvkdfyet
      361 ahrythtlav eggskknnyr vsytrskgns vvhginesfk difnlrlmnt itkwmtldsk
      421 mtyshekvdn rqymngsdkn piyafvtlpr slsidvlkhy kdengnemip igergynpyw
      481 niyentnsdt rdrvsgsmnl evkllpglka vgkagldayw wkgmeffnlg arsdvdggmk
      541 nwinnststn feallmynkt fhkisvnaia gisryernse krtesvnsil vpdfknisns
      601 neypsatqlq skkiirsayg svslgynsyv yldvtarndw sstlpldncs yfypsfgatf
      661 iftdafkiks pilsfgkira sfayagsdtd pyrinqtykl gsiyngsplq tisttlnndq
      721 llpernrsle lgadlrffhn rlgvdvtyyr sdaydlitkv alpvpsgysf kflntghvrn
      781 qgwevvlsat pvktklfewn aninwarnrs evikvvdgnp nvqllkssnv simleegmpy
      841 gvirgrawkr ddqgrklvds sgkilvtdnt qylgcaepkw tgsfgsnfri qnftvsflfd
      901 ariggtlysg twnrattagv vaesaegreg yylsnviyge ssakatsgyq ypdayfedgt
      961 pcllfvkpnn ryasfdersv fdasyikfre lsvayslpks ilkklpisgl rlavvgrnla
     1021 ilhqntpkgi dpeassssgn aqgieyggmp pvssvgfdik ltf
//
LOCUS       WP_120071044            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120071044
VERSION     WP_120071044.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125004
     Region          25..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkylcili clfanalafa saanrtitgv visgednepl igasvyvnad dlkkagasqt
       61 slgtitdmdg kfsisipekv trlhcsyigf eeqdivlqag kdtyrivlqa sshtlgdvvv
      121 tgyqelerrk ltaaiakvdv tdgmvgaaks idqalagqia gvavtttsga pgaparirir
      181 gtaslngtqd plwvldgipl egtdipeink dndndivnms qssiaglspn diesitilkd
      241 aaataiygar aangvivvtt krgktgkpvi nfntkltytp nlntsrlnll nseekvdlel
      301 qllkearfdi lwgltdpipv fpekgkvaai mkqynlidiy keqgwngltp eaqnainklk
      361 tintdwndil frdaftqeyn fsisggsekv tyynslgyvk engnvpgvsm srfnltskts
      421 yqinkilkig msifanrrkn ntfmtdtygl inpiyysria npyfapfdeq gnylydydvv
      481 rsnetdekqg fnifeerant nkesvttain sifdvqlrfn dqwkvysqig vqwdqlsqee
      541 yaginsynir niretnkywk ngvqtylipe ggmlkttnst tsqltwkiqg eykntfgdih
      601 diqimagsei rknwadnqas tgygydpkkl tfqnlifkde aqandwnlkt ksykenafas
      661 ffangsytlm nrytlggsvr mdgsdlfgvd kkyrflpiys vsglwrlsne sfirqykwvd
      721 nlalrlsygl qgnidkgtsp flvgkydnvn ilpgyseeni iinsapnskl rwektasynl
      781 gidfsvlnqa inlsvdyyyr kgtdligska lalengftnm sinwasmenk gveinlqtrn
      841 ittknfswyt tfnfaynqnk vlkvltdksq vtpslegypv gaifalktkg inpdtgqiyl
      901 enkegkavtv eelfrmtsne dglgtyqigp sseeqrdfys yvgtsdapyt ggflntfnyr
      961 nwelnlnfsy nfgahvkttp synvsdldpg rnmnrdildr wtpenttgkf palatynynp
     1021 adyylfstrn diyrsldiwv kklsfvrlqn irlayrvpse wlhklsigga tvglearnlf
     1081 vissnydnym dpesmgnlys tpvpksitfn lslnf
//
LOCUS       WP_120079138             942 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120079138
VERSION     WP_120079138.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105192
     Region          39..940
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtiinsiykg kryailltti ltfyapvlfa qriadsalve vaygqqpewr rtsaissirg
       61 edllkttsas lgnslqgqlp gltllqqsge pgydfsianl ylrgrtsyas gqkmlvyvdg
      121 feapieslst aeiesvtllk dasalalygm rgangvllvt tkkgcvsapq vsirlqtgiq
      181 qplgvpdpin aydyatlynq arvndglprl ytpeelnayq nntdpyfypn vnwkkailnn
      241 taplsmadls fkgggdvvqy yvmmnllqni gfykdtdkkr rensnayyas fnfrsnlniq
      301 iskhlstgln fsgsvgnrsi pggsssangl lgaiwrtapn afpvynpdgs yggnaaftnp
      361 vgnivsrgly kensrtfqli fmpkydlekl tkglsvsagi aynnymadss iknqnyarys
      421 lskgaggevl ytpygadspl esdegfrtdw srlnfkaqld ydrvfkqhql tasifflsdl
      481 yqkygsrddi kylnyagrvt ysynqkyige faasytgcdd yapgkrygff pafsagwils
      541 kenfmkninw veylklrasi glvgnnqnen grylfdqtys sngsyflgtg ssstggfrad
      601 mianpdiswe kervfnigld avllkglsve fdyfhkeryd ilsqpystip gfvgasygdi
      661 lpymnvgkvk nqgfegtiry esslknnfny yvetsawyak neivdmaeev klydyqyrkg
      721 rsvntpfvlv adglyqesdf dsngslkshl pvpqfgevnp gdikyidkng dgvvdsndsy
      781 pvgysnipew nyalkigfew kgidvealfh gvanrdiyls gplaysftdn gsasklalds
      841 wtpenpnasy prlstrtfen nyristywkr ngnyfrmkni rigytfpqsi araiklsrly
      901 vyanasnlft vshldgladp essslitypl trsynlgiki df
//
LOCUS       WP_120079053             925 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120079053
VERSION     WP_120079053.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..925
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102652
     Region          38..924
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkkyifia slisccvlak aqqatiageq alpdtlsigy gmdidkpsss ysvagvnsta
       61 fekfsginit kalygkiagl nvyqgtgasp dnvsslsfhg htplvlidgi prsvsditse
      121 eiescyllkd aaaaalygmk gangvllitt krgknarlnv kveynfgvsn qfrspefads
      181 ytyanalnta lgndglvaky ntqeleafrs naypyhypnv nwwdevlnkt gfthnlklsf
      241 nggndkfryf ttidyyrdrs mlkensvddr ydttptdtrl nlrtnidvsi testflkanl
      301 vgslketngt rygrsaiftp vyntpsaafp vqyeegiygg stiyneknpv allkdyghvr
      361 smagglladm rlrqeldalt dglsaevmvs fdnvgamqet sskeykymns yarmsddgtl
      421 itspivygkd setlghsvpf erllmrsdfq akiayerqfg khqvfgsliy dmqstiqqnr
      481 nnteknqsyi fnaaytyddr yslnvvfnrs gsaylpdgdk frnypavsaa wllsnekfmk
      541 gktpldmlki hasyglsgwd ggldhelwry tygsntgyif gynatsaggn segklpvtgl
      601 taersekvta gidlaafgnr lnfalegfye ersdilvsat nsisgivgig vgnlcegvnr
      661 ykgfdvslgw ndrigdfgyg isanasylnt eiinnneayq eydylyqrgn rigqayglea
      721 lgffgsqlei nqspvqtfst vapgdikykd qngdnridek dvvkmfgssv prfyfgfsln
      781 lsykaleita dfqgltgktv nllssplykp lvnngniskt fldretcwtp enkesatmpr
      841 lttlnnanny rssslwyrdg sfiklrnllv sytfpksmth fadvkvfvqg nnlfsldnid
      901 fadpeqlgis ypsvrsywag vklnf
//
LOCUS       WP_120079232            1071 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120079232
VERSION     WP_120079232.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..1071
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119021
     Region          30..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknryilllf llflgisdam aqrvqevets gvvydkstge tlpgvniicr daktkkrirg
       61 tisdleghfk iktpldvely ftnvamkpst yrvkkaaagv nifmvedvte ieetvivgqr
      121 rvnkasvtss nfvvraeela etpvanvmsl lqgrvaglni qlnnglpgaq gtmtirgisd
      181 isvvgnndtg wnlassaplf vvdgipqsev kdydsqglvs gsgvsplsti pfedianiqi
      241 lkdaaatsly gsagaygvil ietkkgnsvk pkvaysgnft vstpprlrdv aignaernli
      301 kwqilnndts riyhgyqdlm fmpqisdsln pywnnstdwq dqfyrvtynq shnvsfsggn
      361 dlfnykingn yytekgivkn tdfnrysltg nmnyrspnsk faigvdmkvg ftdnstgsgs
      421 avsqsgvasa asassllppp slytasvdal qvfgtsnsnv gsnysttvnl eyllpyriqw
      481 kgvfnysynv seseqfkpav lnndnyrsye enyssntsev yintylyrdf dlyianvglt
      541 agirynskkw tgntvsfkgl pndyilgpag yalsdgsasv senqstfali lnptfsfkgs
      601 rtfkaggeky iftptlspel ssvygkktkw lfnpslgfrw nigyegfmer fshfldnmsi
      661 ratwgrvvky satrydvygt ydinsnnlyd gesyipinfd rlpnvhldpv ttttwnlgye
      721 tslfnnrlst dinlyyrqvd nqlsdvrlpd hagfgnvrst evslvnygle vflrgkplpv
      781 qskwnlecgl nfsmnkdvvt klpnearqli nkdawvanrl ggsatamlly inkgvyatde
      841 dvpvdpvtgk rlrvgtstse eayfkagdpi wvdvngdyii dekdrvvagn aqplinggfy
      901 fnlgyknvsv hvntsftlkr dvinsvlant lksytypakr kiddlkkdaa ivpiesynfw
      961 tesnrynavy pnpynyhhnk eidpfreaqt lfledgsyfk intvsvsyrl pkswlsvlrv
     1021 ggvtlkasvn niwifsnysg ispesvnglg rdysggypna rtwtmgvvln l
//
LOCUS       WP_120079265             990 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120079265
VERSION     WP_120079265.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109184
     Region          2..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqisyigmqt qevvikpnlr vvlkadaqkl devvvtamgi srekkalgya vqdvksdalt
       61 raantdlaga lqgkvsgidi tpssgmpgas skitirgsrs ftgdntplyv idgmpiasta
      121 dvstsltdga ygtdyanrav didpndiesi nilkgqaasa lygmrasngv ivittksgkg
      181 adkgkptitf stnlsfdkis tlpklqqeya qgssgtfdps spfawgpkis elandptygg
      241 ntdnsytsqy gkqsgkyyvp qlaaagmnpw atpqaynnmk dffdtgvsws nnvnvaqrfd
      301 kgnysfslgn ttsngivpst gmdrynvkms aeaqlhpnwt tgfngnfvts kiskqstant
      361 svvatiynap vsynmagips hiegdpytqn tyrdnwidda ywavdnnqfs ersqrffgna
      421 fvkyttkfgt dnhkldikyq igddayttny seiygygstw aptgedseyh ytvnelnsll
      481 taaytwnine ewtldalign efvdkktkye yaysmnfnfp gwnhlnnasv fsneslynkk
      541 rtvgnfanls vawknmlyls gsirndivss mprdnrsfty psvslgfift elaplknnil
      601 tfgkirasya evgmagdytq syyytpsygg gfymgnpivy pingamayip yykvydpnlk
      661 pqntksyelg adltflnglv tlnytysrqn vkdqifevpl agstgassmi mnggkihtnt
      721 heltlgispv dtknfkldfa fnfskidnyv delapgvesi mlggfvtpqv ragigdkfpv
      781 iygksymrnd egkivvdqng lpmqgedavi gtvspdfrlg fntnielykf risavfdwkq
      841 ggqmysgtag emnyygvskl sgdmrknefi venavketgk dadgnsiyap ndikvtdaqa
      901 yftrrrside syiydnsyik lrelsvsypv fskkwlnvnv nvfarnilvw semkgfdpea
      961 sqgndnmgga ferfslpgta sygfgfnvkf
//
LOCUS       WP_120079343            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120079343
VERSION     WP_120079343.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121505
     Region          26..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmklvkyml iailvlgtge vaaqvqvvsg kvtemlgnqi epivganvni vnaqnrsvgg
       61 avtnldgdyr lqipaqennl tlvysyigmk tkrikytgqk vlnvklesnv etldevaita
      121 kriernnmgi ghkenvsatq kvmmedliat apiatveeal qgqlsgvdia lsadpgarss
      181 irirgtstln gsveplivid gvpytqeldd dfdfstanee dlgallniap tdiesvevlk
      241 daaataiwgt kgangvlsit tkkgktgktt fnfsskftak fepnsipmln gseyiamvqe
      301 alwnsanytg lnadtylkyl ydtpeinysp nwnyfneynv dtnwldevrq nafttdntfs
      361 msgggekaty rlslgylseg gttigtglkr fnsslrvdyn fsdklrfgad fyftqsdkdd
      421 nwapkdsnvr seafkkmpnk spyymdedgn rssqyfsyqt kdwegefkad nksashfnpv
      481 amanesyknt msrdsranfr idykilpclt ysayaslkms ttttdkflpq vatgvpwtsq
      541 yanqstaass esltlqtenk lifnknwkdk hnliatavfr ttqatssstt stsygnassg
      601 ladpitgssv yslgsgesea rsisgtglin ytlldryvfh tsatmdansa mgkserlgif
      661 ptvgiswnmq nepfmknted wmdeiklrfs igqsgnapkg taayygayts rgeymdmsai
      721 ypsrmqlnnl kwetsteynl ggdfsffhgk lrltfewynk yikdllqkep kmptttgfsk
      781 nkwynsgrme nkgwearidg vlyekkdwrv sayvnlsrnt neitelpetm npepytfkng
      841 eyairieegr pfgsfygyry kgvyqnqeat yardkegnvm ndvsgkpivm kngakqvcpg
      901 daiyedinhd gvineydivy lgncnpiltg gfgftvkykr lslnalfygr fgqkiinatr
      961 mdnesmynan nqskavlrrw rnegdntdip ralynegyny lgsdrfveda syvrlktlsl
     1021 syslpkkvcn ylgintlnff vtgydlltwt gytgqdpeas lptsasklsk dsantpcsrr
     1081 fscglnlnf
//
LOCUS       WP_120079351            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120079351
VERSION     WP_120079351.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116187
     Region          25..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktikiiftt lllllsvasv yaqgrkisgk ilsplnkpie gaiisavgsk daktgvdgtf
       61 kmelkenttq isvwaagyyp etrlvddnsq vvilmmpest ykynesailp mriessrpel
      121 tsavninkkd ftqgsmkidr alagqvaglk ttraggmpge gsymnlrgir sfvgsnaplv
      181 vingvpylpd sresqlingf srdifqayni qdiqnitvlk gaeasmygsm gsngviliet
      241 dgatsdnldt rvsfygqygv nwnnkrmpll tgndyksyls digmtyfgnm egffsefpfl
      301 sdpnskynyl ynnttdwqde iykngfvtdn lfrveggdai akydlslgya menglmdytk
      361 sqryhtqlnt nvliskwvem tatvglaylt gnyqqqgmdn vsnpilaays rapllspykk
      421 didgnildty styyygnstn mdfavsnpla ivntldgrnr qydvnfrlgl vykpfnglsf
      481 ngtfgmfyny nkehlfipgl sdksilpivd qygnaentvk egvgetlnif angnvryqrl
      541 fqgihhlnil agaqmlitqn kyeggagrnt pndfyqtlgd tktigryfyg yqekwnwanf
      601 yahadytyrd mvaaslnvaa dgassagtyg nhfyiypsgg vtllgkgwlp ltnstlvnrl
      661 nlraeyglsg nsrfssnlgk yyytslpymt tsgivranis nttlkpekni qfnlgldmsl
      721 lrnrlevtld yynnlskdvi favphtsalg slnyyancge iknrgvelav qaslvrtrdf
      781 ewiiggniar nesevkslgn tsqlinsysd gaqlvsrvge spyqfygyqt lgvfstqaea
      841 daanlvnqkg qayqagdihf vdqngdgrid skdrvslgsa apkyfggfft risyksfals
      901 aefsyskgnq ayngvrrsle slstfgnqsa avvnrwsleg qqtnipraqw ndpmgnndfs
      961 drwiedasfl rmknvtlsys fdkkflnffr sgtlyvtgen lltatkylgl dpefsysysd
     1021 amqgfdyakm mqpksikfgv nlnf
//
LOCUS       WP_120079623             923 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120079623
VERSION     WP_120079623.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 923)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..923
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104183
     Region          31..922
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mimnkslyiv afslafattg iaqnnegqdk vidlgtqttt elrktqavst iysneldkna
       61 atspynaiyg llpglsvmqn tswgtdksrl nvrgrgslng dtplfvvdgf arpleyinls
      121 eiesisvlkd gaatalwggr gangvvlitt krgiysqkdi kvdykfglgf pvnqpefada
      181 ytyakarnea lrydglqpdm deasflsggn sdlypnvdwq kealrnhtts hqlditfrgg
      241 gkrlryfsvl nykndmglln skytdytdry nsqmkkyfln lrmnldvdit datklklsml
      301 gmlretkrpt tseatlfeqi fntpsaafpv qtlngfwgsn nvlktnpian ladvgyykln
      361 qrmlqadlrl vqdlsvltrg lsaelaiayd nnatyqetak ksfmyqtiek gtdgepiytn
      421 ygnpndelei snkglanqyi hanfeakvny hrtwdkhdft asamfrqesm tltgannsry
      481 rqyiigtagy nfdnrymvdi vancfgssvl gkndkyrayp aisaawilsn enfmkeisaf
      541 dylklrasyg rsgydiydyd mdkqywvgsg ayyfqagnts agsslkegvl ameqldleva
      601 dkynigldms lfkgltfsid gfydkrtnil idgsglissa igvtipqmna gkvetkgtel
      661 samwkkeykd fnyyiganfs yakskvveng egyqpygyls kkgypvgqcf gweaigyfrd
      721 eadiksspvq kfsevrpgdv kyrdlngdnv idnndqkaig ystaipeiyy ginlgfeykg
      781 fgvdalfqgv ahysvmlnta svywplrnnt nisnwylndr irwteetkdi anvprlttld
      841 nannfrnstq wlengsyfkl rnlnvyynlp sswakkvkme kiqvyarann lfsldhvkym
      901 ncedlkinyp dmtsvyfgln inf
//
LOCUS       WP_120079584            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120079584
VERSION     WP_120079584.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116958
     Region          6..1038
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msssrtlqit yvgmksqdvp iksgtikvmm ksdsevlqev vvtgmqkmdk rlftgatkql
       61 nadnvkldgl pdisrglegr aagvsvqnvs gtfgtapkir vrgatsiygs skplwvvdgv
      121 iledaidvgp ddlssgdaet lissaiagln sddiesfqil kdgsatsiyg aramagvivv
      181 ttkkgragvs kisytgeftt raipsykefn imnsqeqmgi ykemeqkgwl nsadlfrtrd
      241 tgvygrmyrl ideynnsngq rgllnttear naylreaemr ntdwfdvlft navsqnhsvs
      301 itagtekssf yaslsamldp gwykqskvkr ytanvnttyn iyknlslnli snasyrqqna
      361 pgtmnstldi asgkmsrgfd inpysyalnt srtldpsvdy isnyapfnil heldnnyiei
      421 nmvdvkfqge mkwkvvqgle lsalgavryq tssqehnvld danqaiayrt gmddatireq
      481 nkllytdpdn pyalpitllp eggiyqrqdr rmlgldfrgt lswnhlfaek hitnffagme
      541 vnslqktyss fqgwgmqysm geipsyiyqf fkngiesgsr yyslghsetr siasffnaty
      601 sydgrytlng tfryegtnrm grsrssrwlp twnlsgawnv heesffkalq ptlsnltlka
      661 sysltadrgp aevtnsqaii rsfspyrpft diqetglyid dienseltye kkhelnigid
      721 lgllenrinf sadwyqrnny dligvvptqg vggvinkyan vatmkshgve ftlstrnirt
      781 kdfswntdfi fsyaknevtr lkgltsmmel vsgngfareg ypvrglfsip fagldedgip
      841 qylidgkvts tsinfqerek ldylkyegpt dptvtgsfgn vftykgfkln vfmtysfgnv
      901 vrlnpvfnyk ysdltampre fknrwtvsgd eartnipvil sdpqyrtnts lylaynayny
      961 steriakgdf irmkeislmy efprswiapa kisnlslklq atnlfliyad kklngqdpef
     1021 vntggvaspv prqftltlrl gl
//
LOCUS       WP_120079756            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120079756
VERSION     WP_120079756.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115246
     Region          45..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkiryirl iglifvlivg ssltfaqnks krksakkplv evvsivtdek gsplknvsii
       61 cgegavvlyt dakgrfqtkv endatvmvea lgyedkvykl tgsnivpeki vlkkeplflt
      121 eeslvnradg gktykgnevg atsvlengqf gtfpdltltn mlqgkmlglq vrstvsglgn
      181 ntpdlfirgq hgmsentaiv iidgverpaa dlipeeieri ellkdataki lygaraangv
      241 lwvttrrgka nrriynatae agvvqmtrtp dflnsyqyan lynearandg ltpyynqkql
      301 egyknskgvn dllypnvdly dqllnknany rkvsfdmtgg tdrvryalia gyvggsgfed
      361 vtytpqlhrl tlrgnldfnv tdfltisadv agrmemrkwg qldcgqvfta lsthrpneyp
      421 ltmsseetgl assdgiplfg asllrpmnay aetmyggytd erytrsqtni glkfdldmlt
      481 kglkagafls fdnydylqls lskvyptyai ktyrdfagee qimytqmkkt dvatsqsrks
      541 ttlqqtlgwn afaayentfn qkhdvsarlt ymyskttnqg vtqdiinany alrlnymydh
      601 ryaveadmal mgsnrfksgd kyffsaaggl awilsnedfl kdneyvnflk lktsagilgy
      661 drstehllye rawsqdgsfr fgttnngata yystfiragn pnlkwekaae wnigveglfl
      721 nnrlyteiny frekhtdiig svdasygdyt gnftyqdnmg svlnhgiegm ftwsdrindw
      781 aysvganfvw sknkvlkwnq vkhgeeyryt vgrstdammg lvaeglfgkd vvinghatqt
      841 fadyqegdia ykdlngdkii dgrdvkelgn sfprttlgid fnvsykgwgl ylqgyselgv
      901 htwatnayyw nngegkyskl aldryhpann ptgsyprltt tagennfrns sfwlkntsff
      961 rmknvelsyt fnqfsprsvv kkmkvfarga nlfvlssvkd ldpellnagv tnypvtrtft
     1021 ggvsfvf
//
LOCUS       WP_120079746            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120079746
VERSION     WP_120079746.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116914
     Region          22..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknyflflff lvisvsgyaq gkritgkvtd aadgmpiiga tvvavdpdgk tnaksvgtit
       61 dingmftlnv pngcqelkfs yvgmetktak itglthinvs lastakalde vvvtalgvtr
      121 eakslnysrq svnaealaen ssgnlissls gkvagvtitp pgtsngsari virgtsslte
      181 nsqpvfvidg miienepgdt svtvdggtgs tdlgnpvadi npddiesiei lkgpnaaaly
      241 gsraaqgvvl vttkrsrtfe ktkvsysgnf qfekvnqfld yqngwgtgen sylldhkltl
      301 qpngnrlptd lpnfsgynss agaklrswga plwdqviygh dgvltthssh pdnvkdfyet
      361 ahrythtlav eggskknnyr vsytrskgns vvhginesfk difnlrlmnt itkwmtldsk
      421 mtyshekvdn rqymngsdkn piyafvtlpr slsidvlkhy kdengnemip igergynpyw
      481 niyentnsdt rdrvsgsmnl evkllpglka vgkagldayw wkgmeffnlg arsdvdggmk
      541 nwinnststn feallmynkt fhkisvnaia gisryernse krtesvnsil vpdfknisns
      601 neypsatqlq skkiirsayg svslgynsyv yldvtarndw sstlpldncs yfypsfgatf
      661 iftdafkiks pilsfgkira sfayagsdtd pyrinqtykl gsiyngsplq tisttlnndq
      721 llpernrsle lgadlrffhn rlgvdvtyyr sdaydlitkv alpvpsgysf kflntghvrn
      781 qgwevvlsat pvktklfewn aninwarnrs evikvvdgnp nvqllkssnv simleegmpy
      841 gvirgrawkr ddqgrklvds sgkilvtdnt qylgcaepkw tgsfgsnfri qnftvsflfd
      901 ariggtlysg twnrattagv vaesaegreg yylsnviyge ssakatsgyq ypdayfedgt
      961 pcllfvkpnn ryasydersv fdasyikfre lsvayslpks ilkklpisgl rlavvgrnla
     1021 ilhqntpkgi dpeassssgn aqgieyggmp pvssvgfdik ltf
//
LOCUS       WP_120079806            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120079806
VERSION     WP_120079806.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117974
     Region          46..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqklnsgaln rillfvyils lstnaiaqnk nnsketyllp phgnyvygrv ieklskepmv
       61 gvtirldghs tgvitdingc yvltlpekgg lviysyigfe trkikvtsrq kvdvqmveat
      121 esiqevivtg ynsiqkesft gnttkieked llkvnpnnli saiqtfdpsf riqenlaags
      181 dpnslpqfvl rgqtgigett lgqtstssis revlsgnsnl pifildgfev dvekiydldm
      241 nsihsinilk daaatamygs raangvivie rrapeagkfr vqysgvlsae lpdlssynlm
      301 narekleter laglynsntp eidpytngyy qrlnnvltgv dtywlsqglr talnhkhsvf
      361 idggendvrw gvelgfrgte gvmkhssrkn anaafyvdyr igglqiknkv tytynkstdv
      421 pfnsfsdysh llpymrlyde ngdyvrrlek fdgasgtqvn plyeinfyns fdhsgydevt
      481 ddlslnwrit dglrlrgqfs vlmrnstgdl ykdpasasys astgningek testqkrtvi
      541 dgslslmynn tfkghnlnic lssnmrqtqs tasetryrgf pggdlvssny aaevygkpss
      601 sdnttrlvga lltsnytynn iyladltgri dgssefgsdk rwsmfwstga ginihnydfm
      661 ksnelfsmlk frvsygltgk tnfslysakd myqlqtdswy ptgygvflyq mgnpnlkwer
      721 kytldygvei glwhdkiylk asaydertid litdytipss tgftsykenm gkvkntgvel
      781 elrarlysdr nwlfqlygsf arnkntiiei sqamrdynkr veelfsgynp esssdskyak
      841 tylkyyegas ltsiygmksl gisptngkei ylrrngdvtd vwsadewtii gdtapkgqgs
      901 fgytlsykql smfasflytf ggdaynntlv syvenadikn dnvdkrvlld rwqkpgditt
      961 mkdirdrnvt tgassrfvqk nntlqwsslt msynfrpeql kklhlsglrl sftmndlfyw
     1021 stirqergld ypysrsfnlt tniif
//
LOCUS       WP_120079837            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroidaceae].
ACCESSION   WP_120079837
VERSION     WP_120079837.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidaceae
  ORGANISM  Bacteroidaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Bacteroidaceae"
                     /db_xref="taxon:815"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125189
     Region          25..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkylyvli cflvstlata naanrtitgv visgednepl igasvyvnad dlkkagvsqt
       61 slgtitdmdg kfsisipekv trlhcsyigf eeqniilqtg kdtyrivlqa sshtlgdvvv
      121 tgyqelerrk ltaaiakvdv tdgmvgaaks idqalagqia gvavtttsga pgaparirir
      181 gtaslngtqd plwvldgipl egtdipeink dndndivnms qssiaglspn diesitilkd
      241 aaataiygar aangvivvtt krgktgkpvi nfntkltytp nlntsrlnll nseekvdlel
      301 qllkearfdi lwgltdpipv fpekgkvaai mkqynlidiy keqgwngltp eaqnainklk
      361 tintdwndil frdaftqeyn fsisggsekv tyynslgyvk engnvpgvsm srfnltskts
      421 yqinkilkig msifanrrkn ntfmtdtygl inpiyysria npyfapfdeq gnylydydvv
      481 rsnetdekqg fnifeerant nkesvttain sifdvqlrfn dqwkvysqig vqwdqlsqee
      541 yaginsynir niretnkywk ngvqtylipe ggmlkttnst tsqltwkiqg eykntfgdih
      601 diqimagsei rknwvdnqas tgygydpkkl tfqnlifkde aqandwnlkt ksykenafas
      661 ffangsytlm nrytlggsvr mdgsdlfgvd kkyrflpiys vsglwrlsne sfirqykwid
      721 nlalrlsygl qgnidkgtsp flvgkydnvn ilpgyseeni iinsapnskl rwektasynl
      781 gidfsvlnqa inlsvdyyyr kgtdligska lalengftnm sinwasmenk gveinlqtrn
      841 ittknfswyt tfnfaynqnk vlkvltdksq vtpslegypv gaifalktkg inpdtgqiyl
      901 enkegkavtv eelfrmtsne dglgtyqigp steeqrdfys yvgtsdapyt ggflntfnyr
      961 nwelnlnfsy nfgahvkttp synvsdldpg rnmnrdildr wtpenttgkf palatynynp
     1021 adyylfstrn diyrsldiwv kklsfvrlqn irlayrvpse wlhklsigga tvglearnlf
     1081 vissnydnym dpesmgnlys tpvpksitfn lslnf
//
LOCUS       WP_120080231            1116 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120080231
VERSION     WP_120080231.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..1116
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126522
     Region          36..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          114..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnqaqkfi vlfllflfay swrveaqtgk ekqitmefkn eglpsifkrf ekvsgykvlf
       61 iydeissyts tgkvekatvd ealkviigkn plkyhidgqf initqkdskk ffsqvkgkvl
      121 seedglpvvg atiivedpsn irtitdnngn fqlsdvpkds rvrisyvgle tqflhpssym
      181 svvmksdtra ldevvvtgmf nrkkegftgs avtikgedlk kystnnvaka iaavapglri
      241 vdninmgsnp nglpdmrmrg sanmdmgtqs vdfnstsndv lavqgeyety anqpllimdg
      301 feisiqtlad mdpdrvasiv llkdaaatai ygsraangvi viesktpkpg riwvtyggel
      361 rieapdmtgy nlmnarekid aelksglyty ggetvekwql yqsklrevla gvntywldkp
      421 lqtafqqrht vtleggdeal ryrmyvgyns spgvmkdskr dvltgsldfq yrlkkvllkn
      481 sitldnsvan espwgsfsey trlnpylrpy gengeiqkrl dnfegvgges sylnpmyntt
      541 fnskdqsknf tvrelfkvey nptnelrfeg afnlsksvgh rdifrpaqht lfdnvtdptl
      601 rgdyrrsqse avswgidltg swnkqlkdhy ltanvrmsvl ennsetygny vtgfpndnmd
      661 nllfgkkyne kvtgderttr sigwmaaggy sykykysfdf nirldgssqf gknnrwapfw
      721 stglrwdlkk enfmkdvsfi sdfilrgtyg ttgsqgfdpy qahgyytysn lllpyyssda
      781 tgseilamhn eslkwqttks tnlalelgff dqrltarvey yrkitdnmvt sislapslgf
      841 gsylenlgki enkgweisls aipykntakq aywtitvngs hntdklleis eamkhrndmn
      901 asnltdtplp ryeegeslsr iwvvrslgid pasgdeillk rngemtsavn wsandvvpig
      961 nteptwqgyi nssftykgwg advsfryqfg gqvynqtlld kvenanlkyn vdrrvsqlrw
     1021 akpgdkaqfr tltpsgwetk atsrfimden ifqgsslsvy yrmdrtntkf ishwglssak
     1081 vtfnmedffy wstvkrergl yypysrqftf alnvaf
//
LOCUS       WP_120080341            1079 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120080341
VERSION     WP_120080341.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..1079
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117995
     Region          25..1078
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgkrihlfll alaigviqga aqvttvrgiv tteedgepvi gasvivkgts lgtvtdvngr
       61 felsgfppsa trllisyisl makevaiapq vsvtlksdth lldevvvtal gisrekkalg
      121 ytaqevkqna lvqgkdnnll nslsgkiagv ritntqgdvg ssrivirget siagenqplf
      181 ivdgipvdns qlnarssgrd fknaiadlnp ediktltvlk gpnaaalyga raahgaivit
      241 tkggdkrqkg igitlhsstq vsfvatlpef qnlfgqgagg rfsyvdgkga gvndgvdesw
      301 gprldiglli pqfdspldad gnrvatpwvs hpnnvrdyfr mgistnsgis vargddkyqf
      361 rvgynyekqv sivpdagtnk tnislntdyh lakwivvgat anyivytaps lpgsatpsgs
      421 nvrsnspmlq flwfgrqvdt nslkadytrn wnssyydnpf wsasyntqsq erhrligdlh
      481 aefrltdgln vrfrtstdwy ndrrkskvkw gsagagspyg syaedaytvk enntevlaty
      541 ikqlnknwgi dallgfnvrn kqyennyqaa prlavadlyt ltnsrdplts sndfyrlrqy
      601 glygsiqldy rrwaflnitg rndwsstlpv dnnsyfypsv tasvllseaf gwrskavnyl
      661 kirggwsqvg adanpyqlat vftsetafng nplqssstig mnpnlkpekt ssieagfeaa
      721 fwdnrlyldf tyyktdsrnq ilklattaas gytsqvrnag hirnrgyeiq lgtvpiqtsk
      781 gfrwnldlny gansskvvkl ddeglitsyq lyssgiqila svseaygtlf gtsyvrdang
      841 nvvvdanglp kisttnktlg kftpdwtggi sntfsyrsls lsflidasvg gsifsntnkt
      901 gkytgvlant lsgrdaehgg lwyytdamgn nvrlpespsy svssdglyya qvneqstrvy
      961 qdgimvegvt esgskneevv saekyyhriy siaeanvyda syvklreval syrlprlwtq
     1021 klhlqeasvt ltgrnlwtiy ksvpnidpes alttgnaqgv eayslpttrs fgvnlsvkf
//
LOCUS       WP_120080672            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120080672
VERSION     WP_120080672.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117065
     Region          43..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmekckyll fcgtlalwma gsfqqvyaat epssqaiqqq snkvtgkvsd atgpiigasv
       61 vekgtangti tdldgnfsln vkagatlvvs yvgykseevk agrgplnitl kedakaldev
      121 vvtalgikre rkalgygide vkgealtkak etnlinsmag rvpglvvsqt aggpsgstrv
      181 ilrgstemtg nnqplyvvdg vpldntnfgs agtnggfdlg dgissinadd venmsvlkgp
      241 aasalygsra shgvilittk rankdkisve yngtltfdtq lakwdevqqi ygmgsngtys
      301 ydaisntnks wgpkadgsnm lkyfdgverp flivpdntsn ffrtgitatn saiigvnsgk
      361 tgirftytdm rnkdivpqth msrdifnlra ntsagkvdld fsvnytredv knrpalgdsk
      421 snigknlmtl attydqewlq tyqtadgeys nwngmdpynv npywdiyknf nkskkdlfrm
      481 ngkavwnidp hlklqatlga elnwftfddy kapttpgfea grlqnsafrn rmynfevlal
      541 ynnhwgdfdf natlggnvyk vnnqttvtta qdmkirdvps ltsfneisvv pgsyrkqins
      601 vygavnvgwk hmlyldatlr gdqsstlptg nnmymypsfs gsfvfseltk lgdllpygkv
      661 rmswaqvgsd tdpyqlglvy tkskyaypgy tigyidngti pnkdlkptkt nsvemglelk
      721 flknrigldf tyysqisknq imgmasswtt gynyrlinag kienkgieia lstrpiqtrd
      781 fswdinlnfs knsnkvkeld gesdmfelek aswldvqvaa kvgenfgsiv gpdfqrnekg
      841 dilidpqtgl pqydksnhvl gnaswdwtgg lltnftyknl slvavfdvkv gadlysmsar
      901 aayesgkspe tlagrdawyr seeerlaagi akgadnwkpt ggfvapgvid ngdgtyrpnd
      961 iyinpedywm svcrnapsmf iydnsyvkcr eltlsynvpk swlknvvsgl tvsfvarnpf
     1021 ivwknipnid pdsnynnttg mgleygslps rrsygfnvnv kf
//
LOCUS       WP_120081079             914 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. OF03-11BH].
ACCESSION   WP_120081079
VERSION     WP_120081079.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. OF03-11BH
  ORGANISM  Bacteroides sp. OF03-11BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Bacteroides sp. OF03-11BH"
                     /db_xref="taxon:2292957"
     Protein         1..914
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101298
     Region          38..913
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvqharlify tllllvipce stlaqkipvt pidslitvgy atgslktlsg svekitetqm
       61 nkdqitnple airgrvpglt iqrgsngpaa ldavrlrgtt sltsgndpli ivdgvfgdls
      121 mltsiyptdi esftilkdas etaqygsrga sgvievttkk gmsgrtqvay ngsfgistvy
      181 knlkmlsgde yrrvasergi sildkgnntd fqkeieqtgl qqnhhiafyg gssessyrvs
      241 lgfmdrqgvi lnedmknfts nmnmnqkmfd gflncelgmf gsiqknhnlv dyqktfysaa
      301 tfnptypnhk dpvtnswdgi ttasqitnpl awmevqddda tshistharl tfnlleglkl
      361 nlfgaytyni vensqylpts vwangqaykg tkkresllgn mmltykknwk khffdvlala
      421 elqketytgy yttvsnfstd kfgynnlqag alrlwegtns yydqprlasf mgrfnytyad
      481 ryvltlnart dasskfganh kwgffpsasa awviseeefm kqlpmvdnlk frigyglagn
      541 qsgidsyttl nlvkpngvvp vgnsavvslg dlrntnpdlk wevkhtfntg idvalfgnrl
      601 llsanyynsr ttdmlylynv svppftyntl lanigsmrnw gteiaigitp lktkdmelni
      661 nanitfqrnk llslsgmyng emlsapeyks lasldgagfh ggynhivyqm vgqplgvfyl
      721 phstglesdg nggytygiad lngggvsled gedryvagqa vpktilgsni sfrykrfdls
      781 lqvngafghk iyngtsltym nmnifpdynv mkkgpkqnik dqtatdywle kgdyvnfdyv
      841 tlgwnvpiek vqklkkyvrs lrlaftvnnl atisgysgls pminsstvns tlgvddkrgy
      901 plartytlgl sinf
//
LOCUS       WP_120096523             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AF33-23].
ACCESSION   WP_120096523
VERSION     WP_120096523.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AF33-23
  ORGANISM  Bacteroides sp. AF33-23
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Bacteroides sp. AF33-23"
                     /db_xref="taxon:2292930"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109278
     Region          2..979
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvisyigmkt qevvikpsvk vvmipdteil devtvvaygt krkqdlvgsi ssvkneiisn
       61 sqatsvsnal egavaglqvv sssgqpgqda nivlrgigsi sasnnalivv dgvpfngkls
      121 dinptdiasv nvskdavsns lygsraaggv vmittktgrk dkvainfngs wgvaqraykd
      181 ydmatdpgef yrlswyglrn tywaagnsie esnlaasqdl lgelgnynay iipqgeylvt
      241 pdgklnpnar pryndsfada lfdnafrqey nvsasggndr tdyyvsmgfl dndsyvlgss
      301 yerftaranv nsqlkswlkv gtnvgyskat qngvqenaga asnpfevars wapifpvhay
      361 daegnmkyye dgspmydagn getdgtskrp tatnqnvian mkediretvy nnltsrsyle
      421 isflknfkft anysydftns sqtvfytpli gdgqsfggrg tkgsyntttt nfnqilaysn
      481 vfgdnhhlsa kigheyykye yqylagqktn ffnpnnpeld nggqmqyins ytanhniegy
      541 fgmadydysn kyylsaafrr dgtsrfldrw gnfwsvgaaw risneafmeg tnswlndlkl
      601 rasygtqgne silseydyay vytpyqdqyt vtwngselgh spefygnpdl twekqktfdv
      661 gvdfrlfdrv ygsfeyfyrr tddmlfkrpv aystagrpyn wenlgamknt giefevnvdi
      721 fnqpdlkwtv slvgshyknr ivtlpeenre ngitsgpfnl regksrfeyy tymyagmdek
      781 gnamwymdet nekgevtgrt ttttyadatr yfigksalpd fngglsttfs ykgidlsiat
      841 afqiggyayd ysylsgmsss fyvghnkdmw ktfnpetgqg slpiwnadna snsftqqsdl
      901 nlikasyfsi rnitlgytlp knlmqklgve klriyatadn lglwskrqgf dprvamagsd
      961 deyggyspmr visgginltf
//
LOCUS       WP_120125324             315 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas sp. LS-2].
ACCESSION   WP_120125324
VERSION     WP_120125324.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. LS-2
  ORGANISM  Pseudomonas sp. LS-2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas sp. LS-2"
                     /db_xref="taxon:2315859"
     Protein         1..315
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35305
     Region          5..171
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mpvydtyskr kkrlaglvpd vytydsiplg lrnqivfive divsgvfgdr qsesvydyls
       61 rilsrewgtk ylvahgehid rdeevkeair svtdadyvld iielllktaq nhakdernqv
      121 ttkakgalth yigelnhrfk ehgvgyeysd eqiiridsql lhsevvkpal qllsepgfeg
      181 ahdeylaahe hfrhrrykea lnealkafes tikviagvrg wtinkgdtan klvkacmdng
      241 lfpsyyqshf sgltnllvgg vpsirnaeag hgqgavvkei eshivaytlh mtaaaivlfv
      301 qsyqalpqvq tlpnq
//
LOCUS       WP_120128379             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. LS-2].
ACCESSION   WP_120128379
VERSION     WP_120128379.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. LS-2
  ORGANISM  Pseudomonas sp. LS-2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. LS-2"
                     /db_xref="taxon:2315859"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38680
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikkligqg hkvtvqsgag itasvtdsay eaagasigsa
       61 adafgaelll kvvapsdsel aliksgtvvi gmlnpfnnei iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee reaavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkapvl lsaetvsqmk pgsvvidlaa aqggncpltv
      301 adqvviehgv tivghtnlpa lvaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_120128526            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AF29-11].
ACCESSION   WP_120128526
VERSION     WP_120128526.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AF29-11
  ORGANISM  Bacteroides sp. AF29-11
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Bacteroides sp. AF29-11"
                     /db_xref="taxon:2292928"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112293
     Region          26..1023
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrfmltlv clmaaiswva aqnspitgiv isaednepii gasvlvkgst tgavtdldgk
       61 ftitdapaga ttlqvsfvgm itqevpitpg tirvtlknda klldevvvta lgiakkeksl
      121 tystqvvngd elvrakdpnm mnalagktag vqinksssgl ggsskviirg nrsvsgnnqp
      181 lyvidgvpfg sstnentstt iggdndsgny drgdgisnln pddiesmnil kgpaaaalyg
      241 ssaangvvii ntkrgkegra sisfntnttf dmaaygipef qnhytgqtts wggkikgspd
      301 ytddffktgv ttinslslsm gskamqtyfs yantygkgvv egnrlvkhnf nfretanffn
      361 nkltvdanvn amyqkgnnrt tsggyymnpl vglyhfprgg veggkdfnyy kdnyqvlntg
      421 rnimdqnwyk tsgtdmeqnp ywlinkvpne dtryrtlinl svkyqindyf siqargsady
      481 ivdkdntrmy agtspilcgm naagtgtngr ysyneqsels tygdvlftyq qqfenfsfna
      541 svggsindyn gngtgfdsyp gtlsipnvft mqnvtlnags lsdwrkhtqs qsvfftgqig
      601 lkdqlfldvt arndwtstla ytkyknkgff ypsvgltwll netlklpswi slgkirgaws
      661 qvgngldtyl snplntitkn gsisfnttsp fdelkpektt slefgtewrf fdsrlefdft
      721 yyktntknql ftlpapsgse yntyyvnagd iqnsgieimm natpvmtnsf rwktgvnfat
      781 nkneakalag ealgyfqfsg gesnnvwsrl evggsfgdfy gttferddng kikfgddglp
      841 lvnksdpkkl gnsnpdfnlg wsntltwkdf slyflidgrf ggkvmsltea dldqqgvska
      901 tgdardrgyv mleghkisge qviqdfynlv ggragvteyy tysatnirlr elsigynlpq
      961 awltkigvik saqislvgrn lfffknnapy dpdgmlstsn rlqgvdvfgm ptnrsigfnl
     1021 kvnf
//
LOCUS       WP_120130111             980 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AF29-11].
ACCESSION   WP_120130111
VERSION     WP_120130111.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AF29-11
  ORGANISM  Bacteroides sp. AF29-11
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Bacteroides sp. AF29-11"
                     /db_xref="taxon:2292928"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109357
     Region          2..979
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvisyigmkt qevvikpsvk vvmmpdteil devtvvaygt krkqdlvgsi ssvkneiisn
       61 sqatsvsnal egavaglqvv sssgqpgqda nivlrgigsi sasnnalivv dgvpfngkls
      121 dinptdiasv nvskdavsns lygsraaggv vmittktgrk dkvainfngs wgvaqraykd
      181 ydmatdpgef yrlswyglrn tywaagksie dsnlaasqdl lgelgnynay iipqgeylvt
      241 pdgklnpnar lryndsfada lfdnafrqey nvsasggndr tdyyvsmgfl dndsyvlgss
      301 yerftaranv nsqlkswlkv gtnvgyskat qngvqenaga asnpfevars wapifpvhay
      361 daegnmkyye dgspmydagn getdgtskrp tatnqnvian mkediretvy nnltsrsyle
      421 isflknfkft anysydftns sqtvfytpli gdgqsfggrg tkgsyntttt nfnqilaysn
      481 vfgdnhhlsa kigheyykye yqylagqktn ffnpnnpeld nggqmqyins ytanhniegy
      541 fgmadydysn kyylsaafrr dgtsrfldrw gnfwsvgaaw risneafmeg tgswlndlkl
      601 rasygtqgne silseydyay vytpyqdqyt vtwngselgy spefygnpdl twekqktfdv
      661 gvdfrlfdrv ygsfeyfyrr tddmlfkrpv aystagrpyn wenlgamknt giefevnvdi
      721 fnqpdlkwtv slvgshyknr ivtlpeenre ngitsgpfnl regksrfeyy tymyagmdek
      781 gnamwymdet nekgevtgrt ttttyadatr yfigksalpd fngglsttfs ykgidlsiat
      841 afqiggyayd ysylsgmsss fyvghnkdmw ktfnpetgqg slpiwnanna snsftqqsdl
      901 nlikasyfsi rnitlgytlp knlmqkfgve klriyatadn lalwskrqgf dprvamsgsd
      961 keyggyspmr visgginltf
//
LOCUS       WP_120130281            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120130281
VERSION     WP_120130281.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114886
     Region          43..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyttlytli lglfsigwtd cpedfmermq rpghseiqls kvtisgrvld esgfplagat
       61 iqeketanga iadsegkftl vvadnavlrv sfigymsqdi eveghstfhi tlredmield
      121 nvivtalgie kkenslsyat dlikneeltr vkmpnlitsl tgksagvrvn qvssglgasa
      181 kvsirgirsv asdnqplyvi dgvpilnsts eqaysaiggt anagnrdggd gisnlnpedi
      241 esisilkgap aaalygsqaa ngvilittkk gqshgqrsvs fstslmfdna falpkmqnry
      301 gvsdgvdswg eranlpeydn lrdffstgvt sitsislshg neklqnyfsy anttghgiig
      361 khnlskhnlt fretsvllns rlkldgsmnl mrqvvknkpt vggfymnplv glyrfprged
      421 iayykenfev ddegrnlniq nwhtsyedfe qnpywitnri lskenrmhvi vslsanlkin
      481 dwlslqargn vdyindkvrq qfyastapal agangryiem dyqetqyygd ailmmkkqwd
      541 afslnaalgv sindktvnst rydsktaslk yanvfnlani imngsagldq kidarrqlqs
      601 lfataqlgyn efvyldlsar ndwsstlayt sheksgffyp svgfslifnk lmtlpqwvsl
      661 akirgaysmv gndipmfitn psshitagge flasdaapfk dmepemthsf eagiearflk
      721 nriglnatfy ktntrnqffk lptlsgdkya yryvnagdiq nvgweislda vplltnhfkw
      781 ktevnfstnr nkiislheal keflygptsf sssyamklvk ggsigdiygk afvrddagni
      841 vygtegdntg mplvegdgnt vkvgnanpkl mlgwnhmlsy knfsfyflvd crfggdilsq
      901 tqadmdmygv sevtarardk gyvmlegnri dnvkgfyknv vggragvtey yiydatnirl
      961 relsvgyqlp aawmektkvl kraqlsfsgr nlfffykkap fdpdlvlstg ndnqgievyg
     1021 mpttrswgfs lkcef
//
LOCUS       WP_120130419            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120130419
VERSION     WP_120130419.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117283
     Region          42..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkvkkckntl lcgtltlclw ggfsqvraas fenfaieqqs nkvtgivnde fgpvigasvv
       61 ekgtsngvvt dldgkfslnv kpgatliisf vgykqqevka gnaplnivle edskmlsevv
      121 vtalgikrer kalgygvaev qgealtkake tnvinsmagr vpglvvtqta ggasgssrvi
      181 lrgstemtgn nqplyvidgv pldntnfgsa gtyggfdlgd gissvnpddi esmsvlkgpa
      241 asalygsras hgvilittqk ankdkvsvey ngtltfdtql akwddvqqvy gmgangtypi
      301 navsntnmsw gakadgtnml kyfdgverpy livpdntsqf frtgftatns aiigvnngkt
      361 girftytdmr nkdivpkthm srdifnlran tsagkfdldf svnytredvk nrpalgdsks
      421 nigknlmtla ttydqawlks yqdasgeyan wngmdpynvn pywdvyknsn sskkdqfrfn
      481 gkvvwnitqh lkvqgtagae lnwftfedyk apttpgyesg ylqnnnfrnr mynfellaly
      541 nnswgnfdfn atlggnlykv nnqtivttak dmkirdvval msfnevsvep ysyrkqinsi
      601 ygavnlgwkh mlyfdatlrg dqsstlpisn nmyiypsfsg sfvfsellkl gdklpygkvr
      661 mswaqvgsdt dpyqlglvyt kskfaypgyt igyisngtip nkdlkptktn sfemglelkf
      721 lknrigldft yysqlsknqi mgmassstsg ygyrlinage ienkgveial ntrpiqtkdf
      781 swdlnfnfsk nsnkvkklvd dmdmfeleka twldvqvaak vgenfgsivg pdfqrnengd
      841 ilidpstglp mydksnhvlg naswdwtggv ytnfsyknis lsavfdvkvg adlysmsara
      901 ahetgksmat legreawyks eearqaagya kdspdwiptg gfiapgvidn gdgtyrendi
      961 iinpekywmn vcrnapsmfi ydnsyvkcre itlsytlpkt wlknvidglt vsfvarnpfi
     1021 vwknipnidp dsnynnttgm gmeygslpsr ksygfninvk f
//
LOCUS       WP_120130501            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120130501
VERSION     WP_120130501.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116886
     Region          40..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnyclslv llalfgvsap faanaavesv lssqsaqqak kitgkvldaa gepiigasvl
       61 vkgsgtgavt didgnfsvea pvgstlevsf igyktvtlkv tnattytvsl qddsqaldev
      121 vvtamgikke rkalgysmed vksdelmkmk tanpisslsg kvagvnvtqs sgaagagaqi
      181 ilrggtsgae gkdnqplfvv dgvifdnsss vvgnsafdgs mrsasttsnr lmdinpedie
      241 smsvlkgpaa aalygsraan gvilittkkg kegvvevnin skftaswvks lpqtqrqyar
      301 gymedqydsk knytgtvfnd faytswgeks naatydnigd ffqggnifde sasvaggtkn
      361 skfylsgsyy dqvgvvpetg ykkyafrfng eqkvgiftfn asaaysdaht drtltgagly
      421 nssgngalyg vynwspfdrm thyqnedgtr yrlfgdrldp wderdnpywi vnrnhmyddi
      481 drfngmlsik adiakwwfvs ykigidrytq tasnrlaang vlkqvwqkgm msdntqqfry
      541 mshdfmsnms hkfgdfdlnl llgatmdetk tdrssmmawn fsvpdffsya naskdnkqft
      601 haatkkrlvg afgefraswk nmlyltvsgr ndwtstlple nrsyfypsvs gsfvftealq
      661 rlgwlddsvl nfgklraswa kvgkdtgvye letalwptgt yldgtvgvgn twtrgndklk
      721 pemtksteig velsffknrl hidyayytnn synqilaprg pqstgyifws inagnvynkg
      781 melsisgtpi qtkdwtwdig lnmagnrgtl dglpegmgvm yvtdvqyagm qaasfsggdf
      841 mgiagtkwkr ndagevildk ngmptydktl vavgnressf tgglnntltw knftfnmlwe
      901 frvggdvvng tqyamdnsgv sqfsadvrnr sltvtgvnsn gdpvtntwea dktytfngvq
      961 msgyniikdy yqnyyskesa nyitdvnslr lrsvslsyef pktwlskigf vkrasvsvaa
     1021 tnlllitnyd gdpevaaaga gvggsssvgf dycgvpatst msfglnltf
//
LOCUS       WP_120137871            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AF27-10BH].
ACCESSION   WP_120137871
VERSION     WP_120137871.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AF27-10BH
  ORGANISM  Bacteroides sp. AF27-10BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Bacteroides sp. AF27-10BH"
                     /db_xref="taxon:2292927"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113517
     Region          2..1012
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mvisyigmqt qevtikphvr vvmqsdtell devvvvaygt atkrsftgsa teikgdrian
       61 knpselskal tgevagvqvi stsgqpgsna sirirglgsv nssraplyvv dgipfgsdls
      121 gidpsdiest tvlkdatata lygsraangv illttkrgkk gktqveanvk ygintriipl
      181 ydtmenperf leltwegikn kymyrannpk deatakqyas edlfdadygi apvynmwkae
      241 gknlidpvtg rmkagvirkf tpekwedyif rtgekveanv kisggsdkls hytsfgylkd
      301 egyyigsdfe rfnarsnlsq ditswlksnv nmaysymeln kpgqgdnmnn gfqfinfmps
      361 ifpvfqrdad gnkikdnvvg gylydygmae gygrpyasgv npagaiqldk neyqshsfng
      421 namfeatflk dfkgtvnfgl qylgtknnel tnpyygdaeg lgrifknmst ffsftsnqil
      481 swkksfgvhn fdafvahest fykssdnygq kskivrpnnt ewsnavimdy mdsqtygfdm
      541 esyfgqiryd yndkyffhgt lrrdgssrfa kgqkwgtfgs igaawaitne nfmkdvswlk
      601 nlkyklswgv lgnqdfitnp tiagyypynd lytignlnde isfsfkykgn pdltwerset
      661 wntgiefnia dilegeveyy nkttkdmlfl kqvspslgya qypvndgkmv nkglefslva
      721 hlvktndisl dlrvngghyk nkmtqmpmdd ttgkekplei qgaygwskgh slydfyirey
      781 agvdpetgma lynsyynvka dgskdlitdm vtyqqnnkie rlevektsdy nnatkkyvgk
      841 sgiptlqggf gfdlavkgfe lnttfsyslg gyaydgvyat lmsnntpgsg nwhndienrw
      901 qkpgditdvp rltsgydeyt nasstrfits rsylnlsnvr lsytfpkkwm nrmnigslsv
      961 yvsgdnlmfi sarkgfvsma gntvstdpne dsggsdrsqy aplstimggi kiqf
//
LOCUS       WP_120138561            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AF34-31BH].
ACCESSION   WP_120138561
VERSION     WP_120138561.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AF34-31BH
  ORGANISM  Bacteroides sp. AF34-31BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Bacteroides sp. AF34-31BH"
                     /db_xref="taxon:2292931"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114858
     Region          43..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyttlytli lglfsigwtd cpedfmermq rpghseiqls kvtisgrvld esgfplagat
       61 iqeketanga iadsegkftl vvadnavlrv sfigymsqdi eveghstfhi tlredmield
      121 nvivtalgie kkenslsyat dlikneeltr vkmpnlitsl tgksagvrvn qvssglgasa
      181 kvsirgirsv asdnqplyvi dgvpilnsts eqaysaiggt anagnrdggd gisnlnpedi
      241 esisilkgap aaalygsqaa ngvilittkk gqshgqrsvs fstslmfdna falpkmqnry
      301 gvsdgvdswg eranlpeydn lrdffstgvt sitsislshg neklqnyfsy anttghgiig
      361 khnlskhnlt fretsvllns rlkldgsmnl mrqvvknkpt vggfymnplv glyrfprged
      421 iayykenfev ddegrnlniq nwhtsyedfe qnpywitnri lskenrmhvi vslsanlkin
      481 dwlslqargn vdyindkvrq qfyastapal agangryiem dyqetqyygd ailmmkkqwd
      541 afslnaalga sindktvnst rydsktaslk yanvfnlani imngsagldq kidarrqlqs
      601 lfataqlgyn efvyldlsar ndwsstlayt sheksgffyp svgfslifnk lmtlpqwvsl
      661 akirgaysmv gndipmfitn psshitagge flasdaapfk dmepemthsf eagiearflk
      721 nriglnatfy ktntrnqffk lptlsgdkya yryvnagdiq nvgweislda vplltnhfkw
      781 ktevnfstnr nkiislheal keflygptsf sssyamklvk ggsigdiygk afvrddagni
      841 vygtegdntg mplvegdgnt vkvgnanpkl mlgwnhmlsy knfsfyflvd crfggdilsq
      901 tqadmdmygv sevtarardk gyvmlegnri dnvkgfyknv vggragvtey yiydatnirl
      961 relsvgyqlp aawmektkvl kraqlsfsgr nlfffykkap fdpdlvlstg ndnqgievyg
     1021 mpttrswgfs lkcef
//
LOCUS       WP_120139279            1194 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120139279
VERSION     WP_120139279.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1194)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1194)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1194)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1194
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1194
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133502
     Region          32..99
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          111..1193
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkrflflfv lllslaisqa taqerqketi qltfdneews dalkkvgkaf gykilftydd
       61 vknrkatcsi kttsvgeaik aiignepfty tqngnfisii stdnkkdkqt rtvtgrvtde
      121 nsqplpgvav stpdnttgvi tnidgyfklq lpagatsinl tyvgmqplmv kaseqfmnlv
      181 mhedaqelqe vvvtgmqkmd krlftgastr lkseemklsg lpdisrsleg raagvsvqnv
      241 sgtfgtapki rvrgatsiyg nskplwvvdg vimedvtevs addlssgdae tlissaiagl
      301 nsddiesfqi lkdgsatsiy garamagviv vttkkgmagk srisytgefs lrlipsysef
      361 nimnsqeqmg vykemrqkgw lnfaetyras qsgvygkmyq lqnsydpitg tfalantpaa
      421 eneylrsaey rntnwfdelf nsnitqnhsv svstgtdkvs fyaslsvmnd pgwyqqskvn
      481 rytanvntty tisqqlslnl issasyrkqk apgtlsqsid pvsgevrrdf dinpysysmn
      541 tsrtldahtf ytrnyadfni rheldnnymn ldvvdlkfqg elkwkpikgl elgvlgaakf
      601 setgnehiik ddanqamayr amddatirdn npflyddpdy dydlpisvlp qggiyqktty
      661 kmlsydfrat anyntnfged hiinlfagte ansidrnkty fngwgmqysm geipfyvyqf
      721 fkksiedgad yyslantasr staffgnaty sykgkytvng tiryegtnrl gksrtarwlp
      781 twnisgaynv heetfweslr nsishlslka sysltgdpgp ssvsnsliei nsykpyrpgt
      841 niqesglqil nlandeltye kkhelnigme vgfldnrinl aadwykrnny dligiiqteg
      901 vggqiskfan vasmkshgve ftlstrnikt rdfswntnfi fshaknevtk ldsetevmsv
      961 vsgsgfalkg ypvrslfsyn fqglnqdglp tfidqdgnlt cngedinfqs qnlehlvyeg
     1021 ptdptitgsf gnifsykgfk lnvfmtysmg nvirldpvfs ssysdldamp kefknrwiaa
     1081 gnetvtqvpv ivsngqntnd rylkvlynay nystarvakg dfirmkeisf sydfpkrwts
     1141 kigisdlsmk lqgtnlfliy addklngqdp effrtggvsa pvpkqftltl kfgi
//
LOCUS       WP_120141129            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AF26-10BH].
ACCESSION   WP_120141129
VERSION     WP_120141129.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AF26-10BH
  ORGANISM  Bacteroides sp. AF26-10BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Bacteroides sp. AF26-10BH"
                     /db_xref="taxon:2292926"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114888
     Region          43..1032
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyttlytli lglfsigwtd cpedfmermq rpghseiqls kvtisgrvld esgfplagat
       61 iqeketanga iadsegkftl vvadnavlrv sfigymsqdi evegrstfhi tlredmield
      121 nvivtalgie kkenslsyat dlikneeltr vkmpnlitsl tgksagvrvn qvssglgasa
      181 kvsirgirsv asdnqplyvi dgvpilnsts eqaysaiggt anagncdggd gisnlnpedi
      241 esisilkgap aaalygsqaa ngvilittkk gqshgqrsvs fstslmfdna falpkmqnry
      301 gvsdgvdswg eranlpeydn lrdffstgvt sitsislshg neklqnyfsy anttghgiig
      361 khnlskhnlt fretsvllns rlkldgsmnl mrqvvknkpt vggfymnplv glyrfprged
      421 iayykenfev ydegrnlniq nwhtsyedfe qnpywitnri lskenrmhvi vslsanlkin
      481 dwlslqargn vdyindkvrq qfyastapal agangryiem dyqetqyygd ailmmkkqwd
      541 afslnaalga sindktvnst rydsktaslk yanvfnlani imngsagldq kidarrqlqs
      601 lfataqlgyn efvyldlsar ndwsstlayt sheksgffyp svgfslifnk lmtlprwvsl
      661 akirgaysmv gndipmfitn psshitagge flasdaapfk dmepemthsf eagiearflk
      721 nriglnatfy ktntrnqffk lptlsgdkya yryvnagniq nvgwevslda vplltnhfkw
      781 ktevnfstnr nkiislheal keflygptsf sssyamklvk ggsigdiygk afvrddagni
      841 vygtegdntg mplvegdgnt vkvgnanpkl mlgwnhmlsy knfsfyflvd crfggdilsq
      901 tqadmdmygv sevtarardk gyvmlegnri dnvkgfyknv vggragvtey ymydatnirl
      961 relsvgyqlp aawmektivl kraqlsfsgr nlfffykkap fdpdlvlstg ndnqgievyg
     1021 mpttrswgfs lkcef
//
LOCUS       WP_120141375             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AF26-10BH].
ACCESSION   WP_120141375
VERSION     WP_120141375.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AF26-10BH
  ORGANISM  Bacteroides sp. AF26-10BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Bacteroides sp. AF26-10BH"
                     /db_xref="taxon:2292926"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108765
     Region          33..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkslkrcl kkrmilllgf lmmtgvavaq qlqvqgkvtd atgegligas vlvkgttsgv
       61 itdidgnyvl lnvnpdaili fsyvgyqtqe lnvsgrnkid vvlhddqqvl eevvvvgygs
      121 lskkevsssi vqvdkknfnl gamnnpmemv sgkvaglnvn tqaaanpnss sslqvrgats
      181 vsasnspliv idgvaggdir niaaqdiesi tvlkdagsaa iygtrgangv ilvttkrgsg
      241 eagktvvtyd syiafnvakp spdilsadef rrsrrgtdyg adtdwyglit rdvaydtnqy
      301 isidgstkng fygasfnyks angldivsgr eefggrfsme qrvlenrlqf ngslsarrvn
      361 etwgndgffd raltmnptmp vynadgsyyq ptsptgatnp vaelalrdnn gqrmyllgta
      421 eaklnilqte khllnttlsy slhyndmkqq yyassagses ywngykgrae mkyqkwytnr
      481 lewlgnyaln lgdhnikavv gytyeksiwe qiggsnndfs fdntkywdlg sgsylkdgla
      541 slysgrsest ligffgrlny nwkdmlfasa slryegsskf ganqkwgyfp aaslawemme
      601 mgfmkntrkv ltslkprvsf gitgrsdfda ykslstyntn gsylfdgrwv tgyapssnan
      661 pdlaweksva inlgvdfvlw nrlrgsveyf drsskdllyt ytapqppfvy stilvnvgtt
      721 kntgievsld gdiltktavk wtsginysyg ktqltklsnd iykasyldly lkpgtgssey
      781 ffrvqeggei gqfygyeyag vdengnmlil ndkdeqipis qadakykryi gngapkhfls
      841 wsnnltwknf dlsvffrgtf gfdvfnmrky gmglqgcgtd nvlrsayled knirtgggvi
      901 ssyfledgsf iklenvtlgy nftpknrkll dnmriylsak nlltltgysg ndpsiidvng
      961 iqpgvdsnsa yptatqlslg vtlrfk
//
LOCUS       WP_120141559            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AF26-10BH].
ACCESSION   WP_120141559
VERSION     WP_120141559.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AF26-10BH
  ORGANISM  Bacteroides sp. AF26-10BH
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Bacteroides sp. AF26-10BH"
                     /db_xref="taxon:2292926"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122805
     Region          24..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrvlivll cfvgalssaf aaekkvqgvv issednlpli gasvyvtaed lkkagsaqtt
       61 mgvitdvdgq fsiaipagit rffcsyvgyd vlevklvpgk ehyeitlhas sqmldavvvt
      121 gyqtverrkl taavskldis detigavksi dqalagqiag lsvsptsgap gapakirirg
      181 taslngtqdp lwvldgiple gtdvpepdel nditnmkqss iaglnpadie nitilkdaaa
      241 taiygaraan gvivittkkg kvgkpvinfs srftytptls ldrlnllnsa ekvglemdmi
      301 rnnyspdnhk ggvynilsny nelsafqngg wdalssdtqa ainrlksvnt nwgdilfrda
      361 fsqeynlsls ggtervtyyt sfgyykedgn vdgvgmdrfn lvgktsykvn silkvgasmf
      421 anrrkntnyl tdaygmsnpv fysrkanpyf elydgngnyn ydydiqnntd kdlgfnifee
      481 rqntsnesvv nsfssifdae lrfndkwklt sqfgyqlekt sreeiadwes yamryyykls
      541 eysqggetkh flpeggmqks yensnsqitw kamgeyrdsf ndihelevma gtelrktwye
      601 tlfsagygfd rktlttkpvi fpnesyatsf plhqttyken ayvsfystas ysllnrytvg
      661 gsirfdgsdl fgvdkkyryl plysvsalwr lsqepfmqqa kwvdnlvfra syglqgnidk
      721 ntspfllgty rsesilpgvs edviiinsap nkklrwektq svnagfdfsv lnqainlsvd
      781 yyyrkgtdli alrmlpletg ftsmnvnwas menkgveisl strnittknf swytnfnfay
      841 ngnkvlqeni peqqttpgre gypvgaifal ktagvnketg nmmfynpege kvtlkelyrl
      901 kdewgigias sdvtaaeert fysyigssda pytgglintf syknwelnvn fsltfggyvr
      961 tqpsydiinp dygknynadv lnrwtpenpn aelpafmlsa sspeeyswyd sktiwrdldi
     1021 wvkklnyvrl qnlrlgyrip elltkrlgmn satvsvegrn lfvfgsgynn ymdpesmynp
     1081 yatpvpksvt fslnlnf
//
LOCUS       WP_120143389            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120143389
VERSION     WP_120143389.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118874
     Region          28..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknrytlllf flfsvvadsv aqqlervtis gtvydkaige aetfpgvnii cqdaktkkri
       61 agtasdlega fsikvpvgse lvfsyvsykp tiykvrkaas gisifleenv neieetviig
      121 nrkvskanat sahtvikade laqtpvsnvm sllqgrvagm evqlnnglpg aqgtfnirgi
      181 sdisvvgdke tgwdlassap lfvvddipqd dvsdynsegl isgsgvspls tialedidni
      241 qilkdaaats lygskgaygv ilittkkgns skpkvtysgn ftvstppslr evaignaern
      301 ilkwqilnnd tskiyhgyyd imfmpsvsds lnpyfnnntd wqeqfyrvty nhshnlsfmg
      361 gsdlfnykin gnyytekgiv kntdfnryal tgnmnyrspn skftigvdmk vsftdnstgs
      421 gnavsqsgva saanassllp ppslysasvd alqvfgitns tvksgysatv nlgyklpfni
      481 dwkgifnysy daseqekftp ailadnsyqs iaynysgnts kiyvsthatr sfdlkyirlg
      541 ltagirydsr tatgnsitft glpndyiigp vghgkssgna tvsenqstfs lifnpsinlk
      601 tkqsfraggd kyiiepsisp elssvygtkt kwninpgvgl rwnigyedfm rpfeswldnm
      661 nirltwgqvv kykatrydvw gtydikaent yngqsyipid faklpnaqld pittttwnlg
      721 ygfslfngrl sttldayykq vdnqlsdiyl pdhsgfdkmr stevslvnyg levaltgrpl
      781 ptrsnwnltc glnfainrdv itklpnearq ilnndawvan rlganttsml lyinkgvyat
      841 dedvpvnpvt gkrlkigrnd teeayfkagd piwvdvngdy videkdrvva anarpkvtgg
      901 fyfnlsykef smhvntsfvf grdiintvla rtfesysnpv kkkisdlrkn aalapieryn
      961 fwtennryna kypnpydyih ndiidpfree qtlfvedgsy fklntvslsy rfpkewlsff
     1021 rvsgvtlkas vnniwtfsky sgispesvtg lgrdnsggyp nartwtvgvv lnl
//
LOCUS       WP_120143614             937 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120143614
VERSION     WP_120143614.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..937
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104025
     Region          2..935
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklifsqait ltnaqpmkvt lgedtqvlde vvvtalgikr sekaltynvq qvkgdelttv
       61 kstnfmgala gkaagvqins sasgpgggvk vvmrgaksit qnnnalyvid gipmynrass
      121 ggdgamatqp ssesiadinp ddiesmsllt gpsaaalygy egangvvlit tkkgradktt
      181 vtysnnttfs dpmmmpkfqn tygnmtgemm swgletdkry dpanffntgs nvsnalslst
      241 gndksqsyis vattnatgim pnndydrynf sfrnttnfln nkfildtsan yiiqndknmv
      301 sqgqyfnplt slylfprged fsdvavyery ddlsgvntqy wpygdlggvs sqnpywimnr
      361 mnrendrrry klaaslqyni ieglnvqgrv sidnteskyt ekfhagtvgn fagpkgryke
      421 enrldrqvya dvlanfnktf nefnvtanlg asikdlrmel tslhgdlnnv tnhftienlt
      481 rsgyykvnad glkrqtqsvf anaeigwrsf lylsltgrad wdsslalser gnkpffypsi
      541 glssilsevi dlpewfsflk arfsftsvgn aydpyltkvr yvyddqldqy kaeslypnsd
      601 lkpeitksye aglnmrffkn tlnfdityyn sdtrnqtfaa plpassgyta vniqagsvqn
      661 qgiemalgyk newrdfgwss nftftynknk ikrladgvtn ritgepiemp yvdkarlggs
      721 tspvvrlteg gsmgdlyinr dfkrdnngyi yldaktglps mveteykkig sllpkvnlgw
      781 rnsftykglr lnillsgrfg glvvsntqaf ldrcgvseys aqlrqaggvt innrnvsakd
      841 ylgivaagtg egdhyvyeat nirlqevsle ytlpkkwlyn iadvtlglig nnlgmiycka
      901 pfdpelvass tstfytgvdy fmqpslrnmg fsikvqf
//
LOCUS       WP_120143394             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120143394
VERSION     WP_120143394.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112631
     Region          81..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnaiirfca ivallgfgne iravrssghl fllndsispd enngkvvgey dsiravyamk
       61 enavvyaskd tldlwrlscs pyislqqylk gtlpgiyvqe ttgepgsiqn mlirglsspv
      121 fskgdmssaq pvvylngipl ltndafvygi kstevnpigt atnilsglnl dnvesievvk
      181 daarlaklgp lavngailvn mkdgyyggsn mfiranggia ippsnvkmtn aandyafrmr
      241 fadycatkeq htaylnkmps wmrdirdmnf fgepgwadey ysisplynfs asmgsggsfs
      301 nyifmmgytg ndgvadetkf nkltanfaln mklleqlgvs clinlsrvsr dgnrnlrdry
      361 aeieylpdlt tplspvssvy rsyldiyeey kkndnlnnll ngylemnynw rglyvdtrlm
      421 ldyntnvrhv fwpmdlmesv nyvsnysgyn rrliwqssad ykfdflknhf fkiglqeiim
      481 ksvqhynytq gydgdddtkp ttsgggfkqm kryvdkmqnn mvstlfsidy ryrnffdvql
      541 vlradgssnv qkdnrwlftp aasasinlkd lllkdvkqls dlsmrgswar igryqdnnrf
      601 aagpqytgee ltgigqpvms syygyatiar pyntawvgyg lgwpysdkwn iglntsffnk
      661 rlsldveyyn ntdcdlitti pvneefgyky ryangmkvrn sgveltlsgk pfenpkgfsw
      721 dasfslaynk nellqlpenl nelvignrml kvghaidqfw lyqnegvyts dtevpvqngk
      781 klamgsipfa kndpkwkdqn gdnqindddk ilkghslppv tgsfinnfkl gqfdlginlf
      841 falghdainy rssqrynffa lentpslesl reiffwqstn dkddyplynq msgltpyrae
      901 qdlfmeklsy lklrsvtvgy tlpvkkkayk gggkkkvvsk nkleniyfyv tgnnlltftg
      961 fsgddpelid mdgyyrgygq plsrsvivgm kfnf
//
LOCUS       WP_120144024            1197 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120144024
VERSION     WP_120144024.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..1197
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134544
     Region          127..1194
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqqitlsr kkamrkvvwm kaaflllmfv ialhgraqnt dsklislelk eaplgealkq
       61 fsnvsgykvn fpsedvgayr vsvsihqlap laalqkileg kpfeyevkqh fitvrkvkpa
      121 sttrkvrnie grvvdekgep lpganirgid spfgaisdik gnftckvmee thtlevsfvg
      181 mqtekvsikg rthvnvimhe dkqqlgdvvv tgyqrisrer stasfgfids eqltrqmhtd
      241 lasslegqia glrmdinpnn gdmspilrgr gtfsndvgsh plivvddmpt dltlseinpy
      301 nvesitvlkd aaaasiygal aangiivvvt kqakeegahv ninadwfits kpnfnslnla
      361 stsdiidyqt dvfdanvaes gsasgflssy kagyynplfq lyldrengtl snneveatln
      421 qwrnndyyke yrdnawrtav tqrynvsvsq kvgknnhfls fnyendkgrt indkrnkfsl
      481 yyksnyaits wlnvnagvda rlgssdtpnt lftsytmqqr yerimdadgn rynspyvnvs
      541 gysggayngs vvskaegvsp yktfgfnvld algeggtksr nvsirpfvsl qarflkmfky
      601 nfmyqyewnh sksevfdaed sylmrmtyns midtngnsam pkggrffqne lssnrytvrn
      661 qidfdkswkn havtaiagle frenkipkpt rqlmygydpq tltsdiidwq ayrdgvgtsa
      721 lsgntitlsg lsptlqesrh ryasfyanas ysylsrynvs gsirwdqadl fgldirnqrh
      781 plwsvgaswi mseesfmkdi vwldflkarm tygingnvdq ssttyfvvkq ktqsnpiktt
      841 yltyddddlp npklrwekta tynvgldfrl fnnlvngsle yynrhssdll vrrymdptlg
      901 aksrvvnnge mrnrgiefsl tanlirkkdw nfavdfnfah nknkmlkvdh sdsdtstsfi
      961 mspqnyfmeg tsyntlwayr idriengypv avdkdgndlv tfnedgtvan ittgsslkgt
     1021 enlvnlgslt pkfngavslr lsykgialna ffvyaggnkl rnsvvsmsdq vgsqtlkdit
     1081 nrwsadapda nvrmyidmpt kvktyastfq dwwqygdinv kdagyvklrs lslgyslpsg
     1141 icrqirlnsl nlklqvnnlf twckagsdid pesyglnsgt rgmaspktys iglstsf
//
LOCUS       WP_120144152            1139 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120144152
VERSION     WP_120144152.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1139)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1139)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..1139
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125860
     Region          65..117
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          125..1138
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkttfekl pqantgrskn wktlraicll lflsvsftay sqitvnvkdi slraslkkie
       61 qvsnykffyn eslpelnrkv slnvknatie qtmqqllggm dlaykkeqdn vivlirkaqd
      121 ksitkkitgt vvdekgepvi gasivikges hgtitdfdgk ftladvpekg iltvsyigyk
      181 tvdlsaagqt fvkvvlqeds kmidevvvvg ygvqsqklvt tsiskvkmen idqgndynpi
      241 kmlqgrvagv nissasgtpg eapnvtvrgi gsvsggsspl yvvdgipsek ypnlnpndie
      301 nmevlkdasa aaiygsrana gvvlittksg qqgktkievs grygfaylas diemansmey
      361 mntmqaaidn ynvqmganlq lyvpsqiqet nwvkeisrkn sktgtgsisi sggnekttff
      421 aslgantqeg ylnkssydqy nmrakfthki nnlfklnmnl agsasrsdll eetstslkvl
      481 rtareeqpwy spykedgtsy kvngtdilrh npvmlineed wvakkyqlsg vfsidvtpfk
      541 gfkytptvsv ygildntskk lsdkhdarkn ssgwgalaeq kdqsfryvid nifsynnewn
      601 kliysvmlgh sfekytyeqf gaksdnyang afpssnfdli nagpniyagn isytsyales
      661 yfgrialnwd nkyilnaslr sdgssrfakn krygyfpsas fawrasneef fpknkyvnda
      721 klrlswgmtg smagvsnyap lslisaggas yngsagfqis qdaraltwek asqfnigfdi
      781 emfqsrltln idmfyqkttd llfkkpvnat tgyttlqsni gslenkglel alngkiftgk
      841 fkwdlggnis fvknkllsli egndmyivps sgsnllggsm halingqpis tfymlkmegi
      901 yqrddevpak lyakgvragd vkyfdynedg disdadrmnv gkaipdfygg itsnfsykgf
      961 dlslfgqfsv ggkvmsawrg vngsegtdhl glalsnvkvn drgesveqyf nvskevangy
     1021 wrgegtsnti prpvrigvht gydydynvqt stryledasy fklktvtlgy tlpesvvkkl
     1081 rvnslrvyvs adnlltltky sgydpetsfs gspgdsnygv dfglqpvlrt fifglnlnf
//
LOCUS       WP_120144394            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120144394
VERSION     WP_120144394.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117047
     Region          43..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnmekckyll fcgtlalwma gsfqqvyaat epssqaiqqq snkvtgkvsd atgpiigasv
       61 vekgtangti tdldgnfsln vkagatlvvs yvgykseevk agrgplnitl kedakaldev
      121 vvtalgikre rkalgygide vkgealtkak etnlinsmag rvpglvvsqt aggpsgstrv
      181 ilrgstemtg nnqplyvvdg vpldntnfgs agtnggfdlg dgissinadd venmsvlkgp
      241 aasalygsra shgvilittk rankdkvsve yngtltfdtq lakwdevqqi ygmgsngtys
      301 ydaisntnks wgpkadgsnm lkyfdgverp flivpdntsn ffrtgitatn saiigvnsgk
      361 tgirftytdm rnkdivpqth msrdifnlra ntsagkvdld fsvnytredv knrpalgdsk
      421 snigknlmtl attydqewlq tyqtadgeys nwngmdpynv npywdiyknf nkskkdlfrm
      481 ngkavwnidp hlklqatlga elnwftfddy kapttpgfea grlqnsafrn rmynfevlal
      541 ynnhwgdfdf natlggnvyk vnnqttvtta qdmkirdvps ltsfneisvv pgsyrkqins
      601 vygavnvgwk hmlyldatlr gdqsstlptg nnmyvypsfs gsfvfseltk lgdllpygkl
      661 rmswaqvgsd tdpyqlglvy tkskyaypgy tigyidngti pnkdlkptkt nsvemglelk
      721 flknrigldf tyysqisknq imgmasswtt gynyrlinag kienkgieia lstrpiqtrd
      781 fswdinlnfs knsnkvkeld gesdmfelek aswldvqvaa kvgenfgsiv gpdfqrnekg
      841 dilidpqtgl pqydksnhvl gnaswdwtgg lltnftyknl slvavfdvkv gadlysmsar
      901 aayesgkspe tlagrdawyr seeerlaagi akgadnwkpt ggfvapgvid ngdgtyrpnd
      961 iyinpedywm svcrnapsmf iydnsyvkcr eltlsynvpk swlknvisgl tvsfvarnpf
     1021 ivwknipnid pdsnynnttg mgleygslps rrsygfnvnv kf
//
LOCUS       WP_120144710             923 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120144710
VERSION     WP_120144710.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 923)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..923
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103209
     Region          33..922
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnsynrflk glfagifflg itsvanaqke qpdsvsavsr vnmdhlkkyp tlqlsnalqg
       61 qaagliaipn vggigydnst fyvrglhnng tseaiviidg ikrpiddilp eeiesiqilk
      121 datakimyge qatngvilvr tkrgkanerv irvgleygiq pvtrmpefld synyatlfne
      181 acvndgiqpf ysatdlegyk nskgvndlry pnvdyykefl rdastfrkat ielnggteka
      241 tyavtvgytg ssglekvsdr snlnrinarg nldlritdfl tasadvagri ekkdwgavdg
      301 atlfseistl rpneypfmia pedingrdgv ttdesslifg tsvrktnnly mdmayggnts
      361 eryvnsqtnl glkfdlkslt egltanayvt fdnysylrqq lrnayptysi erylddegee
      421 vlrfterkrl nlpkkqsiss ndtyrnfgwr anvnyehsfd lhdvlaeaaf rytteektgn
      481 tqdvkdgtft frgnyaynkr yflegvlsam gsnrfsgsnr yffayaigga wmiskedfmk
      541 dvkavnslrl kinyghlgya gntghflyrt nwkngdkfeh kpstggpttd lvrygnpdlk
      601 weysnelnig iegrffnnrl sgdinyfrem rkniigknta kyaavvgdfi paenigevmn
      661 qgidaqvrwq dkigeihynv gvnltftqne lrksdeldni enyrksvgra tstifglqae
      721 glfgkdvqla ghplqsygay qvgdiayadl ngdnmindnd vtdlgqsfpt ttmgidlsln
      781 ykgfglyilg tattgvtnil sssyywnngl dgysvlaldr yhpvnnptgt qprltttsga
      841 nnsrnssfws engsffrlkn velsytlank tgkfigkdfk ffvrgtdlfv lsgikdldpe
      901 rmlsgltnyp tyrtitggis inf
//
LOCUS       WP_120144734            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120144734
VERSION     WP_120144734.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122010
     Region          26..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkitifslt llfalilplf anaqvtvkgi vtdesgvplv gvsvrykelp qvgvttdidg
       61 kfsikemkeg ktlvfsyigm knvehllkga tpfikikmes atseldqvvv tgytqttfkk
      121 mtgsvgiisa dqlkdqaqpt vdalmqgkia gvavsaisgq pgstqkirir gtntitgdge
      181 plwvidgvpm qsgstdmpts aeiksgqfdd lfmngvagin psdiesitil kdasaaaiyg
      241 sraaggvivv ttkkgksgka qinysgnvsv tlppqrnysl mnsqeklaye qglwdefsap
      301 gfeagandyp vvgvvgiira grgkfagwsk eqqdtyieel gktntdwyde lfrnsvstth
      361 nlsingggdk ytyytslayt rnagllknnd ydrynltanl smhpsqkvki dfgasmsyqy
      421 skspalnsld pfqyayfanp yespynedgs yradetyyal geynnkktss kiipdcgfnv
      481 lremdetssr tkniktmvra gidysiinhl rfvglasyty stnrlkeiyg kntkaaldnr
      541 lsidnntnke yasilqrnvd nesymvrghf ayddsfgdhs vsliagaefr gsksdglysk
      601 rygydeitgn aitplpddpt gvgyeklkay laaidgsnge twseqrfvsf yasadyyykn
      661 kyvlnvsfrt dgssnfgsdk qfnpnwaaga awnvseedfm aslkpvlnrl tlriatgftg
      721 ninrsvspqm iisyyddyrn isnniyhigk vvsppnpnlr wektqdvkva ldfgmfndrl
      781 tgivegyyrk skdivtgvqv lsstgftqqk yntanidnkg ieatlngtpv ktkdfslsls
      841 aniaynknkv tkykasyssm gynnlwegyp vdaiysgryt gidpetglyt yqlrpdaeih
      901 tatdlnkpdn yryylgtsea pvtggfnvta eykgirlsvn gtfatgaknf efiksptsan
      961 tvsgngvfny tereqvfqnd lfahhlnvpk vaadrwtpnn tngtyprvwn pfgevygfgy
     1021 ynpmhkeith gafltnlsya riksiilgyt lpkklisnsa lsnvdfslsl nnfftftsys
     1081 gmdpetpgat ypisrsvmfs vnvgf
//
LOCUS       WP_120144901            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120144901
VERSION     WP_120144901.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119082
     Region          25..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnkwllsl avgllccgsa yaqttvkgki tsesgeplig atiavknstd gtvtdidgny
       61 slktkktlns kdlllfsyvg yktlqknytg ntmnvklaee sqqlndvvvt algikreekg
      121 lgyatetvkg dkitsalpsn wstalngkva glsvissggp lnssrislrg dvslnqngnd
      181 alvvvdgvpm sspmtnpgva ygagsnsels vdygngfsdi npddiesiqv lkgasataly
      241 gtraangvim vttksgagap kgigvsysgn fsiddvmrwp dyqyefgqgl psnigpagsi
      301 yegepyysyg kaedgsyast sgtssaygar fdanrkfyqy dpvtqgrase atpwvayknn
      361 rkdlfqtgyt itnsvaltgk sdrgsvrasi thtknewilp ntgfqritam isaqqqisra
      421 lrinfkssyt yrklnntpal gynsnsisyf lifqnpnvnl dwlrpmwrtg qenvkqlqpy
      481 ssfignpyvi lyesenpsek hsnvssvsan lrinskfdfm irsgiqlstd qreqhrpisd
      541 vvfgngffkk qnvfdyelns dalftyhdsf anglhvnasa ggnmmqqsyd mlaasvvgld
      601 ypgvyklang vsnpnvqtvi kkkalnslyf tanfaykdkl fldvtgrndw sstlpksnrs
      661 ffypsvsvsa vmnelflmpe pinllkvrgs faqvgndtdp yktspyygts dfpgsavvas
      721 tlynqdfkpe istnyeagfd lrmfqnrigl dftfyynrtk nqildapmdp ttgyskatin
      781 sgcvrnrgye iqldvtpvvs rdfrwnatft wsknenkiis laegadenql issignvsii
      841 grvggttgdl wgyklvrdpe gnvvindngl persgeieyv ataypkwkag lynefsyknf
      901 tlsvlldgqv ggkmyshshh kmteqgklah tlngrlpgtd fymskddpri ataglspqdg
      961 mymiapgvvk nddgsfsknt kvvtvesyyk efyrmanvet ntfstdflkl remrleyklp
     1021 gstlkktpfs kasiafyarn lfcitdyplf dpesaalngs smvtgvetgs lptartfgln
     1081 inlsf
//
LOCUS       WP_120144869             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120144869
VERSION     WP_120144869.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111047
     Region          37..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknihfktct cllgillilf sgiqvkgasw evqqeskvsg tvtdekgepv igasvvvves
       61 kqgtitdidg kfwvnvpkng hlkvsyigye tqevvvkdrq llkivlkees talnevvvvg
      121 ygtmkrkemt saishigakd lnqissldas mllqgkvssv svsntaladp nnqgsiqirg
      181 vssrnaglgp livvdgvpgg dmtninpadi esidvlkdga asaiygtrgs ngvilinlkk
      241 gtkdgqvhtt ystsvtfnka kkeldimnae eyrayrtvsn plsdmgadsd wfdavtqlgv
      301 thmhtltfsg gnartnyrvt adyrnargid lrsdrreyga raninhttkd glftfsanit
      361 prvidrnksa svysnaiknn ptmpiydses vngyyrfpsg tegsniveql neeensteik
      421 llewnataav nllplfnpkn pdmvlksqvt isqyqvdkfn gwftpstygs nvndgvtgka
      481 srdfdksttn nlewvtnfst rikdhqiram vgysynygvn sgmsaenwnf ssdgltynnl
      541 gsgleaakdg ktmmgsyknd hklisffgrv nydwkerylf tfslrhegss rfgenhkwgn
      601 fpavsvgwri sdekfmkgls widdlkvryd ygvtgnqeig nynslatyra fgwyqyngnr
      661 fhvwgpgkna nselrwekgh nqnigldfsf fqhkvtgsfn yfhrkqsdll gdysvpvppn
      721 lfstiytnvg tlrntgfeld vtvnavrtkd ftysftlvga tnnnkfvsfs ndiykgqkyy
      781 stcsmanpnn pgylqrieeg erignyftyr yagvdkkgdw liydkkgnvi pvaqgteedk
      841 svtgnglpkf tgsmthnfty knfdlsvalr gaagfdifnv hdfyfglqsm ttnqlttays
      901 knahittgkn vitdyfiepg dylkidnvtl gytmnlnkky iekirlfgta nnlytftkft
      961 gvdpstyevn gltpgtfggg ynyypsafqf ilglqvsf
//
LOCUS       WP_120144927            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120144927
VERSION     WP_120144927.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126654
     Region          36..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          114..1115
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknqaqkfi vlflfflfay swrveaqtgk ekqitmefkn eglpsifkrf ekvsgykvlf
       61 iydeissyts tgkvekatvd ealkviigkn plkyhidgqf initkedskk ffsqvkgkvf
      121 seedglpvig atiivedtnn iraitdnngn fqlsnvskds rvrisyvgle tqflnpssym
      181 svvmksdtkt ldevvvtgmf nrkkegftgs avtikgeelk kystnnvaka iaavapglri
      241 mdninmgsnp nnlpdmrmrg ganmdlnaqa tvdlnsasnd vlavqgeyet yanqpllimd
      301 gfeisiqtla dmdpdrvasi vvlkdaaata iygsraangv iviesktpkp griwvtygge
      361 lrieapdmtg ynlmnareki daelqsglyt yggetvekwq lyqsklrevl agvntywldk
      421 plqtafqqrh tvtleggdea lryrmyvgyn sspgvmkdsk rdvltgsldf qyrlkkvllk
      481 nsitldnsva nespwgsfse ytrlnpylrp ygengeiqkr ldnfegvgge ssylnpmynt
      541 tfnskdqskn ftvrelfrve ynptnelrfe gafnlsksvg hrdifrpaqh tlfdnvtdpt
      601 lrgdyrrsqs eavswgidlt gswnkqlkdh yltanarmsv lennsetygn yvtgfpndnm
      661 dnllfgkkyn ekvtgdertt rsigwvaagg ysykykysfd fnirldgssq fgknnrwapf
      721 wstglrwdlk kenfmkdvsf isdfilrgty gttgsqgfdp yqahgyytys nlllpyyssd
      781 atgseilamh neslkwqttk stnlalelgf fdqrltarve yyrkitdnmv tsislapslg
      841 fgsypenlgk ienkgweisl saipykntak qaywtitvng srntdkllei seamkyrndl
      901 nasnlkdtpl pryeegesls riwvvrslgi dpasgdeill krngemtsav nwsandvvpi
      961 gnteptwqgy inssftykgw gadvsfryqf ggqvynqtli dkvenanlky nvdqrvsqlr
     1021 wekpgdkaqf ralnpsgwet katsrfimde nifqgsslsv yyrmdrtntk fishwglssa
     1081 kvtfnmedff ywstvkrerg lyypysrqft falnvaf
//
LOCUS       WP_120144754            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120144754
VERSION     WP_120144754.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115161
     Region          45..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkiryirl iglifvlivg ssltfaqnks krksakkplv evvsivtdek gnplknvsii
       61 cgegavvlyt dakgrfqtkv endatvmvea lgyedkvykl tgsnivpeki vlkkeplflt
      121 eeslvnradg gktykgnevg atsvlengqf gtfpdltltn mlqgkmlglq vrstvsglgn
      181 ntpdlfirgq hgmsentaiv iidgverpaa dlipeeieri ellkdataki lygaraangv
      241 lwvttrrgka nrriynatae agvvqmtrtp dflnsyqyan lynearandg ltpyynqkql
      301 egyknskgan dllypnvdly dqllnknany rkvsfdmtgg tdrvryalia gyvggsgfed
      361 vtytpqlhrl tlrgnldfnv tdfltisadv agrmemrkwg qldcgqvfta lsthrpneyp
      421 ltmspeetgl assdgiplfg asllrpmnay aetmyggytd erytrsqtni glkfdldmlt
      481 kglkagafls fdnydylqls lskvyptyai ktyrdfagee qimytqmkkt dvatsqsrks
      541 ttlqqtlgwn afagyentfn qkhdvsarlt ymyskttnqg vtqdiinany alrlnymydr
      601 ryaveadmal mgsnrfksgd kyffsaaggl awilsnedfl kdneyvnflk lktsagilgy
      661 drstehllye rawsqdgsfr fgttnngata yystfvragn pnlkwekaae wnigveglfl
      721 nnrlyteiny frekhtdiig svdasygdyt gnftyqdnmg svlnhgiegm ftwsdrindw
      781 sysvganfvw sknkvlkwnq vkhgeeyryt vgrstdammg lvaeglfgkd vainghapqt
      841 fadyqegdia ykdlngdkii dgrdvkelgn sfprttlgid fnvsykgwgl ylqgyselgv
      901 htwatnayyw nngegkyskl aldryhpann ptgsyprltt tagennfrns sfwlkntsff
      961 rmknvelsyt fnqfspssvv kkmkvfarga nlfvlssvkd ldpellnagv tnypvtrtft
     1021 ggvsfvf
//
LOCUS       WP_120151901             938 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AF04-22].
ACCESSION   WP_120151901
VERSION     WP_120151901.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AF04-22
  ORGANISM  Bacteroides sp. AF04-22
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Bacteroides sp. AF04-22"
                     /db_xref="taxon:2292913"
     Protein         1..938
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104082
     Region          2..937
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 misfvgmqtq evtikphvkv ilksdselle evvvtgygtf kkasftgaas tvntstledv
       61 pvlsvadkls gnvagvtfgs sssnpgsvss irvrgmgsin agnnplyvid gtpvtsgdls
      121 eftysdagtd ilsslntndi esitvikdaa aaslygsraa ngvvvittks gkqgktnvsf
      181 rsdwgfsnma idyrpmldgd srrellwtgl knyglytgnm sdadaatfad qniedfaskp
      241 stgwtdwkdl lfrngshqny qlsvsggndr tkfytsvayt nqegiiykqg lerftgnanl
      301 thkfgdfevq vtsqfskvrq nktneatsyd gpvanyaffq spsstpyned gtlnngcgvf
      361 gvnplyereh ssdvytlmka fntikltyni wdklnlseki aydyaqgtnd vlwdrhsnng
      421 apggvmqriv nrndqlntqt qlsyinsfgl hnidallgfe tqdteyafny magqdypgdl
      481 yeltnagsts aetnrqsyrm tsflgranyn yadryylgls yrtdgssrla renrwgsfws
      541 vsgawrfide sflnpvksvl tdgklrvsyg vngtqpsdyy aymnlykygi iyngqsgmsi
      601 vgianpdlkw eknktwnigl dlsfidrisv tfdyyqrkts dliydlpvsq vggyydgnyg
      661 yttpqnigsl knsgfeltit stnfrnkdft wttslnmahn snkltkldgq qneivsgpli
      721 hrvgepyysy yvyeyagvda etgkemfyln dgtenarktt tniseankti vgkhqasieg
      781 gltnnlkwkf idlgftftys lggdafdyst wqhsnggsyl yggavptyyd iskmwtgpgd
      841 tdatlpkfey gsaaslssrw lmptdylrlk nltlgvsipq nyisklglsk ariyfsgsnl
      901 ltwkskdlfv dpemrvdglc tfetpalrty tfgielnf
//
LOCUS       WP_120144761            1023 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            sp. AM16-13].
ACCESSION   WP_120144761
VERSION     WP_120144761.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM16-13
  ORGANISM  Bacteroides sp. AM16-13
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Bacteroides sp. AM16-13"
                     /db_xref="taxon:2292938"
     Protein         1..1023
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114332
     Region          38..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrynkfifi lfvtailsgi atsleaqdkp kkkktaliev kglvtdntgk plsgvtvlsg
       61 egsiinytda ngkfalktka dgtllieafg ykdvvinlak eqptviklqn edlyaserdi
      121 heradggkty qrdlvgtvsk lsmenvlkyp dlqlsnalqg qaagliaisg dgglgyntst
      181 lyvrgqhnng tntalviidg ierpiddilp eeiesievlk datakilyga aatngvvlvr
      241 tkrgeahkri vrvgveygvq pstrvpkyld synysklfne arindgmnpy ytdtqlegyr
      301 nssgvndvly pnvdyynefl lnqniyrkgt iefnggnegv kyalvggytg gsglekvger
      361 saldrmnarg nldikitdfl tvtadvaarv elknwgakdg agifstlssn rpneypfiip
      421 netlsgqftp nedgtpffga strivdnlya dmvyggdtse ryvnsqtnlg anfdfnkyvk
      481 gltfnayvtf dnysylrqel rntyptyaid tysdldgeti trytqmkkld lpktqkiasn
      541 ntyryfgmra digyertlgv hdfsaigafr ytknemtgmt qdfkdanisl rlnysydkry
      601 laeltlagmg snkfdkndrf ffspavgasw iisnesfmke vkavnflklk asfgvlgytg
      661 ntgfflyqtg wnnngnynff qdqtdhkvsl arwgnpdltw eysqefnigi eglffnnrls
      721 telnyfhecr kdiigvnnaq yaatagnytm yenigqvtnq gidiainwkg nigrdflytv
      781 ganmtysknk ldkwneiegv esyrkaigrp tstifglqal glfgkdiple dhslqsygiy
      841 qngdiayadl nnngivddnd rmslgqsfpv ttwginvdlk ykgfglymlg tlhtgitqlc
      901 tnayywnngl ngyselalnr yhevnnpsgt mprlttttes nnfrdssfwt engsffrlkn
      961 ielsytfenk agrffankck lfvrgtnllt fskikdldpe rlnagitnyp aymtvtggls
     1021 vsf
//
LOCUS       WP_120151113             603 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides sp. AM07-18].
ACCESSION   WP_120151113
VERSION     WP_120151113.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides sp. AM07-18
  ORGANISM  Bacteroides sp. AM07-18
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Bacteroides sp. AM07-18"
                     /db_xref="taxon:2292937"
     Protein         <1..603
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          <13..602
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 arrtlkslva dlrvkiigni fldlniwkgi sartqfgldy gnaynravdg vwsetggrns
       61 dgenyvgsyq shplsyvwtn tlsytlstgk hnldvvlgte atrfvqegfs arregiyled
      121 rdfahigvtt gekynlgssa deytyfslfg kanyvyngky llsatvrrdg sslfgennry
      181 atfpafsvgw rikdevfmed fdflsdlklr aswgangsvq glprgytttp fttnyfgtsy
      241 piqgnesgpl ysgynrtwlg npdlkwettt qtdlavdfgf fnqrltgslg yyfkktkdil
      301 vqtpyiavmg eggepwinga nmnnqglefe vsfrndpsae fqytisanig tyktkltelp
      361 envinkypgd gvrdfvigrs pnvfyglvad gifktqeevd nhaeqpgkai grirykdldg
      421 dgrvdeltdr tyigtadpdf fggitfdfky rnfdlnmffq gvfgnqvsnd wkrqsdfwhi
      481 sgsvpvgknh ptrlldawsf dnpdsdipam tnvmtnneqr mstyyiedgs ylklrnielg
      541 ytfpakitnk mmmknlrvya sarnvftlkk fwgddqftsf dpemsgygyl tpftmtfgln
      601 vtf
//
LOCUS       WP_120154509             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter sp. B7].
ACCESSION   WP_120154509
VERSION     WP_120154509.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter sp. B7
  ORGANISM  Achromobacter sp. B7
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter sp. B7"
                     /db_xref="taxon:2282475"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38620
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkyvggk htvvvergag vaaryldday eaagatlgsa
       61 qdalgadlvm kvrapsadev phmkrgavii gmldpfdaeg ieqmaaaglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaegkggy aramppgwma
      241 rqaalvserc kqadivitta lipgrpaptl vsadtvaamr pgsvlvdlav erggncplse
      301 rgkivekhgv tivgltnlpg lvatdasaly arnvmdflkl iinadgalai qrddeivaac
      361 lvceggnvmq rt
//
LOCUS       WP_120173788            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            melaninogenica].
ACCESSION   WP_120173788
VERSION     WP_120173788.1
KEYWORDS    RefSeq.
SOURCE      Prevotella melaninogenica
  ORGANISM  Prevotella melaninogenica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Prevotella melaninogenica"
                     /db_xref="taxon:28132"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120130
     Region          120..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkikflqrv icvlllnllc fgplslpmsa qelngakvtl smhdatvedf anevakqtgl
       61 nvkfadedvk alkgvtldvr dqsvssllln lanqfplsyt vegntltlak keavqrkggv
      121 rgqvtdssge piigavirvd gvnggyvtdi ngeyeiktdl kevhmnvsyi gyktvtktvk
      181 ngatanitlr edskemqevv vtgyqtknkn sftgsqvavt rdqlmnvgtk nvlqsissfv
      241 pgmviaddnl kgsdpnkvae lnirgratfe gqantpvyvv dgaqvsaeyv admdmndiet
      301 vtvlkdasas alygakasag vivittktlk ggklklnysg tvrlstpdls dynllnasqk
      361 leyerlaglf tdtspatqyt ldkdyariyn dvqrgvetdw lskplhnais qshslsvdgg
      421 ddrakynlgi rygndagvmk gsdrtrlstn frlsyniagk ffvsnsstls svtsnvspyg
      481 dfsdwvkmnp yenpynsdgq lrsslyhdla nplydaslgs ysksnnfdfl nttsvqlwfg
      541 ekirldgdft vnrskqdrrt ftspfaysei rnksadqrgs ltdnwvnstt lqgkamlsyn
      601 nyffkklflt amgggsiest ssdaatytsi gfysdklghp afatsyaatr psgsdtqtrg
      661 vgffvnanti wdnkyfldli yryegssrfg knqrfapfws vgggwnvhne kfmkgtpvsl
      721 lklrasvgyl gninfnpyqa lttysynssy fygkgtgatp itignpdlkw ertlstnigv
      781 dftafrgrvd lsadyyiknt dnlllditka psvgvttsre nigevqnsgf elrlrtfpiq
      841 nkdwqwslgl tyaynknkik kisnslreqn eknksdngva plpiyeegqs ltalkvvpsa
      901 gidpvtgqei fikrdgtytf vydsndkvif gdtnplgtgs itsyltykrf alscsflysf
      961 ggslynetla tkvegsnpky nadervlndr wktpgtvaky kriddtttpy qtsrfveknn
     1021 flrmsslsls yevpttfiqk yglkrmflel ltndlfylst akrerglnyp ydrsfefslr
     1081 fsl
//
LOCUS       WP_120173570            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            melaninogenica].
ACCESSION   WP_120173570
VERSION     WP_120173570.1
KEYWORDS    RefSeq.
SOURCE      Prevotella melaninogenica
  ORGANISM  Prevotella melaninogenica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Prevotella melaninogenica"
                     /db_xref="taxon:28132"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117094
     Region          25..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlmmflv glflslgtal aqteisgtvv stddgqpvvg asilvsgtqt gtvtdvdgkf
       61 rlsapagvkl vvsyvgmktk tvtatnnmkv slapddknle evvivaygta krqsitgsva
      121 vvdskkigdr isttvtgale gsapgvqvnn sygepgatpk ihirgvgtlv kdadqplyiv
      181 dgtpfegnia elnpsdiesm svlkdassaa lygnraangv vlittkkakf stkpnitlkm
      241 dqgfyrrgia eydrlnanew measwvamkn yalsggiast eaaagtyatq hlvpdyvkrn
      301 iyngaddalf dangkltaam rtgyddldwq kavertghrq eynlsaavas dkyniyssag
      361 ylneqgytln sgyerftgri ntnynankwl elglnlsgts svrsynsnan gnmyanpfyi
      421 trymapvypv ylhnadgtya ldadgnkqyd ttseylgnrn lpyemtmdmd rvrrnvldgl
      481 iytkitlpyg fslsgkvnln hantnrqtyn npvigdgasn ngrlseyanq yisytgqell
      541 nwdhnfnlhh vdvllgheny swnrkyarvm ntnaaiaglr alsnfvlntd tegyfedyrt
      601 esylgrlryn fdekyffdfs lrrdgsskfh kdkrwgnffs agvnwnikke kfmekvkwvd
      661 alrarasyge vgndaavnfy gyqalyyitk nggnpalvrq klaaldlkwe ttqtldfgve
      721 gtlfdrlnfs lgyfdkrskd llfevrfpls agsffgndai enltqyqnig tisnrgfeim
      781 lsgdvvrskd wtwnlsfdat tlknkvlklp kgedilhgqq nyseghsaye wytyhfvgvd
      841 qmtgkalydl dpkkeaaasa agdlveingt kyttstsqai rkwagtalps vygsfssnlr
      901 wkdlsltmlm tyslggktmd gsyrtlmsta sastaaalhr dvlnswsgap ngmtatspnr
      961 idpngtpild fngsndnnai sdrwltsssy limknimlty rlpkalvtkw glsgvsvkag
     1021 venlftltgr kgmnpqysfa ggsddtyvsa rvfnfgltvd l
//
LOCUS       WP_120173837            1161 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            melaninogenica].
ACCESSION   WP_120173837
VERSION     WP_120173837.1
KEYWORDS    RefSeq.
SOURCE      Prevotella melaninogenica
  ORGANISM  Prevotella melaninogenica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Prevotella melaninogenica"
                     /db_xref="taxon:28132"
     Protein         1..1161
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129191
     Region          124..1160
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyhqhmfrt lrslpslvfl tafilmisws spasaqtpgk kfsisfkdks vaqildfist
       61 kgdykinysd dvkndtlllt isfedvdels avekllshss fvynidgkvi dvfkmknatq
      121 gqytirgtvk dkdglgvpfa ivqikgtsqg vtadidgnfs mpvekeegtv tissvgydak
      181 tlkyhtgkam nviltssaia mgevtvvayg krntreqvga iasvkvedlq kaptasienl
      241 lqgrmagvdv snlsgspggg gsritirgfs slnqkgindg splyvidgip vsssagdatg
      301 ginplsgldp ssiesvqvlk daasaslygs ragngvilit tkkgksgrse vsfnvsqsls
      361 wlpstpmqtl gkgerdiall laksqrgahy dyitdklvyp gsykdsygwd adndgaydyl
      421 wrngkvldse rrlpgiaqds lntfynnrtn wwkyafrvgr vtkadmllag gtdnirymvn
      481 agvydetgim issnfrrfsl lsnldfnlst klsaftrinl tyatqkagad ggrvqgltfd
      541 pkrtstllpg kgstaeqval rqlkdidktn snynvrlsvg lnynilkglk fsstysldhy
      601 ftrvytftpd ylkydkksev qasniamtnv qteniltynl alpsehklel magmtynydl
      661 lqnlsgtakg gptnsikyag egwpslfndg gtvraaqsfl tnqqeqslls flgraaysyk
      721 krymaelsir adgssvfgkd vrwgtfpsvg lgwafseerf mkkfwwlsfg klraswgksg
      781 qkfqepylal gvmeesnifn gslglipqsm ankkltwees dqydlgldlq lldyrlkfkl
      841 dyyykysskl lmqsylpgnv flatnmwdna saisnegief eaqydvirkk nwnwsvgfnl
      901 shnknmlrkt yngedlndkv lgrpvygiyt fkdegivqke edipmylnas gkqiplyfqs
      961 innplrvggr kikdqnydgv iddkdlyyag stlpavyggl nshlewkgls fdvlfsytis
     1021 rkvmnmykns aftftkdfgv imnyfhsgdf wttsnrdaky pslefadkdy vgqfdgnvds
     1081 nienisflrl kqlvigyqip knwlkgsfik danvylsgen lflltnysgv dpeiinpysg
     1141 kddgtqypln rkvtlglnlk f
//
LOCUS       WP_120174436             936 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            melaninogenica].
ACCESSION   WP_120174436
VERSION     WP_120174436.1
KEYWORDS    RefSeq.
SOURCE      Prevotella melaninogenica
  ORGANISM  Prevotella melaninogenica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 936)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Prevotella melaninogenica"
                     /db_xref="taxon:28132"
     Protein         1..936
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104337
     Region          29..934
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkykihiigg almlsslsgy aqeitdttvv nvaygvqssk tqsaaistvk gerlmeitsp
       61 tvgnslkgml pglsilqksg epgydfymen mftrgvssfn skqqmlvfvd gfeapldnis
      121 aeeiesvsll kdaaalaiyg srgangvlli ttkkgyhssp kigfrmqtgi qmptimdtpm
      181 daynyarlyn qalendgkaa lytnealaay qsgsnqylyp ninwknqlyk nttpltmgel
      241 sfrgggggln yyvmaglmhn dgiyrgtdsk qrenanvnya rynfranldv ditkyfrtfl
      301 ysgvsfaekt tpgaggaddy lksvwttppn afpvynpngs iggtslytnp vanllnrgly
      361 kensrslqvi fglqydfsal vrglsakvmf gyynfmaess pktrdyarys laqtgvdaqn
      421 npvynytqyg sdaaltateg frtsqsrigl qgqidyqrqf gdhgvhamll mhndryqvyd
      481 vrddecyvnf agrlsydyqk ryiaevvasy mgtdnyargr rfgifpamsa awvvssesfm
      541 kslswvdflk lrtsygltgn nqtsaryiyd esyggsgsyl fgtgssqssg ftektlanpf
      601 vtwekkrvfn vgidatlwkn lsvnfdvfhe vqsdilaypy aqvlgivgas ygsilplmnv
      661 gkvtnhgfel karyqgkvrd nfsyfaeagt wyamsrvdeq gedvkpesyl ykkgnsvwkp
      721 ivleadgyyt andfdsngkl nanlpqprfg rvapgdikyk dynndqvvde ndahpignst
      781 vpawnymfsg gfkykgfdfs vmfqgvaqrd iylrganiys fqnngtasnl aldswtptht
      841 dasyprlstm nfsnnyrtst fwrrngnflr lrnvqvgyel ansvtralrl ssvyfyvnat
      901 nlftldhlgk lgdaeqdnll syplmrtvsv glklaf
//
LOCUS       WP_120174759            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            melaninogenica].
ACCESSION   WP_120174759
VERSION     WP_120174759.1
KEYWORDS    RefSeq.
SOURCE      Prevotella melaninogenica
  ORGANISM  Prevotella melaninogenica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Prevotella melaninogenica"
                     /db_xref="taxon:28132"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113904
     Region          54..1035
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrmiheakqk hlyfsvafal sialaptsay avgnpvgspe asmpqavqqn gnhkvtgrvv
       61 dpagepliga timvegtkdg tvtdidgnft inttskaklv isyvgytaqt ilvgdkttid
      121 vtlkevantm nevvvtalgi kraekalsyn vqsvgsnelt rnkdanfvns lngkvagvsi
      181 sksasgvgga trvimrgaks iegdnnvlyv idgipifnfs ggrdsgimge grvssegiad
      241 lnpediesis vlagpsaaal ygsnaangai littkkgkeg rvdisfsssa dfsspllmpe
      301 fqntygnklg syeswgekla tpssydpkkd ffrtgtnfin altlnmgnef nqtfasvatt
      361 nsrgivpnnt ydrynftirn ttrmfknkvq ldlgasyikq kdnnmvsqge ywnpivaayl
      421 fprgesfegi ktferydnvr nfptqywpis dsrfanqnpy wtayrnlapd dkdrfmfnag
      481 ltynifdwls vagrirldkt fitserkiya ssfnyfaken gaydyydykd hqtyidaian
      541 inktfgkfsl aanvgysysd yasltrgygg nlvlvpnkfs lnninpsdsk iregggdskv
      601 rnvaafasae lgwrsmvylt ltgrndwnsr lvnsseesff ypsvglsgii semtklpsfi
      661 sylkvrgsyt evgspvsrsg mtpgtittpi vggslkstdi ypftdykaer tksyefglta
      721 rfwkklsfdf twyksntynq tfigelpess gykavylqag nvenrgvema lgyndnfggl
      781 qwssslvysk nvneikemvk dyhhplspkp inipevskdn grvllkvggs indiyarkvl
      841 akdnqgfvnv spsggmslet vepiylgktt pdftmgwnnn ftyknfglsf linarvggiv
      901 tsstqalldr fgvskasada rdaggvmipn qglydakkyy tlvatgendl agyytysatn
      961 vrlqeltlsy kfnsrlfnnv ikdltlsfva tnpwmiycka pfdpeltast gtygqgndyf
     1021 mqpslksygf svkfkf
//
LOCUS       WP_120174801            1125 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            melaninogenica].
ACCESSION   WP_120174801
VERSION     WP_120174801.1
KEYWORDS    RefSeq.
SOURCE      Prevotella melaninogenica
  ORGANISM  Prevotella melaninogenica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Prevotella melaninogenica"
                     /db_xref="taxon:28132"
     Protein         1..1125
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126094
     Region          31..1124
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myrliklnri ltvvfflftv ltaaaqtagm vsgmvkdeqg ealigayiqv letkakavtd
       61 vdgnftikal agqtiqasyv gmvsksvkvt nghtlniilk sdsrqidevv vtgyqnirnr
      121 vytgaatsvk mddiklegia dvsrmlegrv pglsvqnisg tfgsaprini rggasiignv
      181 qplwvidgav yedlvhlsld qlasgdavtl issavsglnp adiqdiqvlk dasatsvyga
      241 ralngvivit tktgrrdspm rvtystenti rmrpryssfd llnsqetmsl yqemndkgyf
      301 gisnslygrr sgifyqlyka vstinpatge yylpntpear ldflrqreya ntdwfnllft
      361 lnpvtnhait lsgggknsat yasigyyhda gwtiadkvsr ltanlkntfy indkltttls
      421 vqgnirsqka pgtmpqrkns tigvferdfd inpfsyslgt srtlspyned gslsyyrnnw
      481 apfnifneya nnkmnidvld fkiqgeatyr lnnnfaiktl lstrhahtst nheihegsnl
      541 vqafranenp fvaqqniylv hdkdnpqlqp kvglpnggiy nkteatlksf larlafdfdk
      601 risehdlkaf afsefrsavr ttnpfqgygi qydrgnqvyt dplifnklin egsdyfnlhk
      661 rtdrgitfsf ngtygyagky vfntvlnveg sntsgkgara lwlptwnvgg kwnidqedfl
      721 kenktisrla lrvsygltak mneeainana iyksgivnrh slddreskfn ilhlenrdlt
      781 wekmyelnig aelglfdnri sttldiyqrn tfdlidlvrt sgvggqyyky anfgdmrtrg
      841 ielgihtkni vtedfkwsts ltvsamdqki trllnspnaf dmvagrgrgn ivdyprgslf
      901 sfnfqglnnq glptfdfgry psnqselski agadfldaqy aksyliyhgp ieprviggls
      961 ntlkyknwel sffltvqagn kirlnptfdp efadlnifsk syynrwlnpg deyktdvpvl
     1021 psqeliaavg kenieraynt ydysqqrvad gsfvrmknis lvytvpesfl kkirlhsmnl
     1081 nlnmtnpfli ysdkklkgqd peyyksggvs mptpkqytvt lnvgf
//
LOCUS       WP_120174851            1102 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            melaninogenica].
ACCESSION   WP_120174851
VERSION     WP_120174851.1
KEYWORDS    RefSeq.
SOURCE      Prevotella melaninogenica
  ORGANISM  Prevotella melaninogenica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Prevotella melaninogenica"
                     /db_xref="taxon:28132"
     Protein         1..1102
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122802
     Region          24..1098
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekritlflf glilslgtaf gqakingtvv sqgdgeavig asvmvqgttm gtvtdidghf
       61 tidvpagkkl vvsyigmvtq tvtakdgmkv vlsndnhqlt evvvtgmtqq dkrlfsgaat
      121 kidaskakld gmadvsrsle graagvsvqn vsgtfgtapk irvrgntsif gsskplwvvd
      181 gvimedianv dasslssgda ktlissaiag lnaddiesfq ilkdgsatsi ygaramagvi
      241 vvttkkgkag qshlsytgey tlrlkpsykn fnimnsqdqm evyrelekkg ylnyaeiana
      301 stsgvygrmy qliseydatk gqfglentqa ardaylraae yrntdwfdql fsssimhnhs
      361 vsasggtdkg qyyaslsamy dpgwykssrv qrytgnintt yninkkigln lianasyrkq
      421 rapgslsrti dpstgavsra fdinpysysl ntsrtldpte sytrnyapfn ifnelnnnym
      481 dlnvhdfriq tsidykpitk lkltalvavk saastmehiv rensnqalay ramgtttird
      541 anpylytdpd npfslpesil keggildrsg nhffgwdtrl saayndvfnd thivnlyagv
      601 esnsvdrkat fdrewgmmfd ageiaklnyr afkmfqeqgs dyyglsnthi rslayfgtgt
      661 ysykgryqmt gtfryegtny lgkatsarwl ptynvsgawn aheegwfnkm fkqalthatf
      721 rlsysltgdr ppvtnslpif satvpwrpft siqetgykeq fgnknltyek krefnlgfdf
      781 gfldnrinlt tdfywrrnrd ligyvshpql gsynlanvas mksngmelsl nthniktkdf
      841 swesnfifsw thneitslft harvidlvqg tgyslvgypv nsifsipfag ldgeglptfm
      901 nedgrrtnss lnlqerdqek ikylkyegpa dptttgsfgn ilryknwdln vfvtysfgnk
      961 vrlnhifsnr yddmdalpke frnrwtysgd eavtnvpvia arrqnrnnpq ldvaynayny
     1021 sdvriakgdf vrmkeislgy tfpaamirsi gvsslalklq atnlflfysd qklngqdpef
     1081 fntggvaapv pkqftmtlrl gl
//
LOCUS       WP_120174999            1125 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            melaninogenica].
ACCESSION   WP_120174999
VERSION     WP_120174999.1
KEYWORDS    RefSeq.
SOURCE      Prevotella melaninogenica
  ORGANISM  Prevotella melaninogenica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Prevotella melaninogenica"
                     /db_xref="taxon:28132"
     Protein         1..1125
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123926
     Region          49..1124
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msifketkqk hlyfsaafal slalaptgvy agtntstavq svqqngnhkv tgrvvdsage
       61 pligatvlve gttngtvtdi dgnytlntta naklvfsyig yaaqtipvgg kgtidvtlke
      121 eantmnevvv tamgimrkek sltyatqqvk aedlmkvqdp naanslegkv agititpsag
      181 gaggaskivl rgnrsilgns splivvdgvp msngirgqqg mdasgfgstg tsegsdplsl
      241 inpddiesin vlkganaaal ygsraangvi mittkkgreg kvdinvtsni tfdsplltpk
      301 iqkvygstvd pttgalslnn wggkiadrss sdlilrspld erwvgyaeeq igvdaqknpi
      361 marrhnvylr nsagddvadf frtgvttnns islsggteia rtyvslansh atgmmrnnsy
      421 nrnsisfrqt ynffkrlhid aslnyteskt knrpgggtvg nplyhlyttp qninmdyyrd
      481 hymisegqwl snpgsyykln gsnfawtqga rttltgpqqe waflshpnnn pywllnmans
      541 qqkesrlfgt lqanidiydg ltfqarvnys qlryknrslr yattflpasm edygrfwdsd
      601 ekttefytdy llsynkafgd ysvsatagfv ghtvkgeskg tdavatyydr lmrklptmvn
      661 yfdtsaggyg vtntdkssnw drsylftgqv gwketvylda syrrdwyrpf ryfkqlgkid
      721 tdnygyfgvg anaivsqlvk lpewfnflky rvsyssvgns ipnkaygams rnlqtgalsg
      781 nkyldfspip eetgsfetgi eslflnnrls fdftfyntiv knlymelgsl ggstellnsa
      841 kvrntgfett igydfkfank lrwrtsynvs yndneiletg ydkdgtsrky qqtvgeakvi
      901 yqkggsigdi yagdflrdan ghivltakge ptfdktgsnd rflgnmnskw qmgwtntfny
      961 kefqlsflin griggkvlsl teayldyiga sertadarln aeknnivatn ygnvpgmeln
     1021 dgsgrivpvq tyyqalgass npssylyngt nfrlrelslg ytfrdvfgqn rnltlsfiar
     1081 nlffiykdap tdpdvslstq nglgafesfn mpssrsfgfs lkanf
//
LOCUS       WP_120174933            1104 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Prevotella
            melaninogenica].
ACCESSION   WP_120174933
VERSION     WP_120174933.1
KEYWORDS    RefSeq.
SOURCE      Prevotella melaninogenica
  ORGANISM  Prevotella melaninogenica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Prevotella melaninogenica"
                     /db_xref="taxon:28132"
     Protein         1..1104
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122478
     Region          24..1103
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskkllmcfa mlfmcinaal aqtkisgtvv aaednepvig atimvvgtks gavtdvdgkf
       61 slttdvanpl itvgyigmas qtlkgttdmk vvlksstqtl nevvvtgltr tdrrlftgat
      121 dkvdaekarl sgvadisrsl egqaagvsvq nvsgtfgtsp kirirgatsi ygsskplwvv
      181 dgvimedaan vgaddlasgn petlissaia glnaddiesf qilkdgsats iygaramagv
      241 ivvttkkgkq gqahisytge fttrlvpsys nfdildskeq mgiyreladk gwlnfsdvln
      301 gseygvygkm yelinkynan tgqfalentt earnrylqra efrntnwfke lfssnimqsh
      361 sislsggtqk snyyasfsal ldpgwykqsn vnrytlnvnl tqhltdklsl nliggaayrk
      421 qrapgtlgqd vdvvggevkr dfdinpysya sntsrvldps atyvanyapf nifnelnnny
      481 idlntldarf qlelkykpik glelsllgaf kymtstqehf vkdnsnqala yramsngiir
      541 dankylykdp nnpyvlpmtv lpygglyhkg dnrmsdydir atanysrtfa ekhimnlfgg
      601 melksierqr nafegaglry dagmvpfyiy qyfkravesg ntyytinptn srsvafygnt
      661 tysyqgryvf ngtlryegsn qmgrnssarw mptwnvsgaw nvheenwfnk lsplnkltlr
      721 asysltgtpp dasysnstai itastpfrlf aedqepqlel selanstlty ekknelnlgf
      781 daslwnnrlg vtfdyytrrn fdeigpmita glggeiiraa nvaemnsngl elsissvnik
      841 kknfswttsf iysyatteit klfnqgnvms lvsgngfakk gyparalfsi pfvglnsegm
      901 pmvlnekgqv ttddinfqer tktdflkyeg ptdpthtgsv gnmfsyhgfr lnvfftyafg
      961 nvvrldpkfr aryndlvsmt nafknrwmaa geeketnvpg ilsksqyman tnvrlgynay
     1021 nysdtriakg dfirlkeisl gydfpaqmfq ksmiknaslk lqatnlflly adkrlngqdp
     1081 efynvggvas pmpkqftltv klgl
//
LOCUS       WP_120180068             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pelobium
            manganitolerans].
ACCESSION   WP_120180068
VERSION     WP_120180068.1
KEYWORDS    RefSeq.
SOURCE      Pelobium manganitolerans
  ORGANISM  Pelobium manganitolerans
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pelobium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Pelobium manganitolerans"
                     /db_xref="taxon:1842495"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108091
     Region          29..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksymikha lllllflvai rvhgqsgdis gkvvdendap lpgasvtvmq tnkgtvtdas
       61 gnfrlvglsg nvslavnfig yetatrnltl kgdqqinfkl kpsatqlnel vvigygster
      121 knltgavstv tskdfrqgti ttpaeliqgk vagvsiiqns gqpggastir irggaslnas
      181 ndplivvdgv plsgnsigna psplslvnpn dietftvlkd anataiygsr asngvilitt
      241 kkgtagkarv svssnnsvat vakkvdilta deirayvadn pganygtdgn nnpllfsdlv
      301 gtantdwqde iyrsafttdn nlsvsgttkg vpyrisgnyl sqqgllltdn frrgtanivl
      361 spsffdkhlk vdlnlkgalt kshfandgai gaaiqfdptq pvhatnafgn yfewlrsdgs
      421 vnpnaprnpl gllelrdnng kakrsfgnvs fdysfhflpe lhanlnlgyd vsegtghitv
      481 ptfaaqaigt lgeisqsrnt esnkfsefyf sydhnftdik sniaatagyg yydnskttyf
      541 ferykgtgev lttpkfpyat drdkllsyyg rlvytlndky ilsgtlrada sskfapenrw
      601 gyfpsvaftw raisesflan sqslsdlklr lsygltgnkd gigytdylsk yyantnngqy
      661 nvggtyydyy sparydpdlr westntynvg vdygflkgrl ygsldayyke tkdllstvni
      721 pvgtnfsnll ttnvgnmevr gfeaninfka iatekqnwdl glnlavnkrk vtnltlspdp
      781 gsrvsagdit ggtgitlkyn avnhipgsff vykqvydqag kpveglyadl nhdgvvntdd
      841 qyfykspdpa ftlgfntsys inkwtvrtsl ranvgnyiyd nvssnfgvrs nilspagvin
      901 nagvdfrntn fqnnqflsdy yiknasflkm dnlgisydfg klgatganls lsancqnvft
      961 isnykgldpe stsgidynly prprtftlgl nlgf
//
LOCUS       WP_120180270            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pelobium
            manganitolerans].
ACCESSION   WP_120180270
VERSION     WP_120180270.1
KEYWORDS    RefSeq.
SOURCE      Pelobium manganitolerans
  ORGANISM  Pelobium manganitolerans
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pelobium.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Pelobium manganitolerans"
                     /db_xref="taxon:1842495"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117771
     Region          23..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklvqsffi llliatsvla qdrritgkvt aaedglplpg vsvkvtgekq gtqtdangnf
       61 tlnlpagaks leisyigfvs qvvsigtktn vnvalvndtk alsevvvvgy stttqqaftg
      121 sakvvssenl erkavsnvsq alagevsgvn vintsgqpgt tatirvrgfg svngnraply
      181 vvdgapiatn tintvnplsa inpddidnvt vlkdaaatai ygargangvv vittksgkgk
      241 psfievngqt gtnmsllpry dviespeqyi glvweglynq avitgktdpt atansrifnp
      301 nysvsskynm wnvangaali dpvtrtvkpg vtrkynpedw edygfqnssr neanikfggs
      361 sdatnyyssf gylkdkgysv gsdyerlsgr lnlnqkikpw ltgsvnlaya rseanrggqs
      421 edsgsifwfv dnipsiypvf lrdatgsivt dpifggnqyd ygqgrgfgal tnaiadatyd
      481 iqrdnrndln gvgslkidiv kglsfetrlg iqyfsniynl rnnkyygsaa gqngslfqrr
      541 tdftssnfln llrytksfge hsiealaahe stdfkynisa fssynlvdpd lldfnnavvs
      601 npnsgytnay kldsyfsqvn ynykstyyls gsirrdgssr fvknkwgtfg svgaawilsn
      661 esfmqqsndl fpylklkasy gligdqegvg yypgydlyai nnlednpafs fdtkgnpdlt
      721 wetakifqtg vefdfkkyis gsidyfiknt ddlifdrrvg psigyaiikv ndgklrnqgl
      781 efdltghilk kadyrldlgv ngafyknklt qmpidpvtgk qkpidiqtay gysvghsiyd
      841 fymrnfegvd padgtsmwtr yyndannngv ldagegiasl tqyladnptv sesslktttt
      901 ktysnatqyy igksaiptvr gafnltagyk afdlsvqmly glggysydya yatlmnndav
      961 gsnnwstdil nrwqkagdvt dvprisneed anvnarssrf ltkanylvln nvrlsyglpk
     1021 tylskigltd csvwvsgdnl wissardgfn pmisesgasd iytysplsti tlglkvrl
//
LOCUS       WP_120182956             969 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pelobium
            manganitolerans].
ACCESSION   WP_120182956
VERSION     WP_120182956.1
KEYWORDS    RefSeq.
SOURCE      Pelobium manganitolerans
  ORGANISM  Pelobium manganitolerans
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pelobium.
REFERENCE   1  (residues 1 to 969)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 969)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 969)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..969
                     /organism="Pelobium manganitolerans"
                     /db_xref="taxon:1842495"
     Protein         1..969
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107728
     Region          63..966
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqikigiaf cltlatglsg lnsakaalni nsklssqits ratdlktnqi dsipttgtkd
       61 slvqvafrki aqkdllggvs vldvdglmek nyetyslenl ealipgfhgn iwgnnsylvl
      121 vdgvprdann vmpseidqit vlkgvgaval ygsnaakgvv yittkrggny aqkvnvrgna
      181 gvfvpksype ylgsaeymtl ynearandgl aplysnddiy nsgsgsnpfr ypnidfyssd
      241 ylkstynryd itteisggsn kaqyytnlgf nsngslldfg eatksrgadr fnlrgnidmk
      301 lnriiklnvd vsasfytakg vnanyfgsaa tvrpnrfspl ipismieesd dpsmvyvnns
      361 nhiidgkyll ggtqldqtnv fatiygggsn kninrqfqfn tgidfdlngi tpglafktsl
      421 aidyltsftq sfnnnyavyq aqwnnyagfd qisgltkfgd dsksgnenis nsyyrqasal
      481 sgqfdynrtf nkrhnvsail lgygyqiges gvyyktnnsn lglqvgynyd hkyyadfssa
      541 yaystklpeg nrggisptls lgwrisqedf mkdvsvidnl kltasagiln tdleienhyl
      601 yqgyytynda awyswndgql vhsfdrrrgn nynmsfpqrr einfgiegsl lkslitfsgn
      661 vffsemkgkv vqpnsiypny fytgwpvysd ipyvnydsdk rqgydfnlnf nkklgavawt
      721 lgfngtyyet eadirvgdsq yefayqnrsg rpldaifglq sdglfmdqpe idnspsqsai
      781 asgggvkpgd ikyidqnedg iidsrdevyl grggrygspf tlginltakw knftfyalga
      841 grmgakamkn snyfwvdged kysvvvrdrw tedtkttatf prltaansdn nyyssdfwmy
      901 stdrfdlakv qisyqlpkal lgksfikdlg vyvngfnllt vakekdilel nvgsapqnrf
      961 ynlgvkamf
//
LOCUS       WP_120183056            1094 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pelobium
            manganitolerans].
ACCESSION   WP_120183056
VERSION     WP_120183056.1
KEYWORDS    RefSeq.
SOURCE      Pelobium manganitolerans
  ORGANISM  Pelobium manganitolerans
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pelobium.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Pelobium manganitolerans"
                     /db_xref="taxon:1842495"
     Protein         1..1094
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121276
     Region          32..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrilinkll lltfvfcals tsnlfaqtpa tvvkgkvtdk ldkqpvpgan vaeldkdkrt
       61 vtatttding nyslrlsnpn nqisisflgy ktflsgavkd rkeinvaldi asnqlqevsv
      121 vgrheatvsd lpisarnstr atstinaeki dqmsvgsidq alqgrltgvd fgttsgdpga
      181 gmsirirgts singssqpli vldgmpyete ipddfnfgta ddqgyaqlln iapsdildit
      241 vlkdaastal wggraangvl lintkrgkmg kpsvnynfkg alsnqpdalp fltgnqyatl
      301 ipeevmnatg vpldflgqng qnkafqydpl dayyyynysn ntnwidlitr tgvtqdhnis
      361 isgggdktry ygsvgylnqt gttvgtdltr ittkinldye vsdkmkfrtd ltythvnnnl
      421 nytsslrnva ynkmpnmspf eydeygnitg vyfspeeniq gkysgtynpl amanegsskl
      481 ygeritprfn lsynilpqnk lyftgdvvfd innnksktfl pqiatgrpsn etsvnrasds
      541 dgdsysiqtk lnlvytpfst eknswqnlis fqtsdsrsss ysattsntas sylqdpsips
      601 vtngsglsln sgqsqsrsmg lvfqsqyqwl dryilslnar idgnskygpd nrfgifpgis
      661 arwrvsgepf mkkfehfldd fsirasygst pnapgsnyay ysryspfsyt yldnsavgrn
      721 nmaltqlkwe tivgknlgfn lwmfnnrvrl daeiyqnttk dlyfndlsip nitgytsvdm
      781 nigtmnndgw eiglnttplk nktwqvdldf nisrnansiq sisefypres vvglpglgky
      841 ksylvegnpf gsfygfkylg vyktaedtka kdadgnvivg pngqdkymry nyptvdyvfq
      901 agdaiyedvn kdgnideadm mylgngipkf nggfgaavgy kgqfklsaff syrygfdvvn
      961 gaqitttnly gfnnqstavl rrwrnpgddt dmpralyndg ynwlgsdryi qdgsfirlst
     1021 vtftynlgkq flqtlnlksa rvyltgqnly twtkytgqnp dvdirgkntp faypvdnalt
     1081 ppsrtytlgl tvgf
//
LOCUS       WP_120183060            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pelobium
            manganitolerans].
ACCESSION   WP_120183060
VERSION     WP_120183060.1
KEYWORDS    RefSeq.
SOURCE      Pelobium manganitolerans
  ORGANISM  Pelobium manganitolerans
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pelobium.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Pelobium manganitolerans"
                     /db_xref="taxon:1842495"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116263
     Region          45..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhiskksvka lwvpslmlll satptiaqtp knqktntsqt dkkgikisge vkdaisgkpl
       61 tginitvpgf saaitgdngk ftvhvpdlrg siivsganyq qkevalkgqs svsvrlydes
      121 fnsvydlavl pfgpelknhi pyavntvnvn gayhksnetp dtylqgsfag lnvqrksgtp
      181 diganmylrg ynsiyatnqp livvdgvifd nnaygaslie ghqnnplanl dvkdinnitl
      241 ikdgtsmygt rggngvllit tnkakdaatr ldfsasggin inpknlpvmn aadyriylse
      301 ilksqglsda qiqakpymdd nanpdfytyh nntnwqnqvr esgtsqnyyl kvtggddiat
      361 yalslgytdn dgvvknnnlt ryqtrfnadl nlskkikaft nlafsrseqd lnhqglgskk
      421 apvflsliks pflspnemse tgiaspnlsd idifgfsnpa atvsnsliak sasyrfngsv
      481 ganyaispkf tlntilgitf nkvrensflp svgiasdtls tavgynqtaa aiqrlfsvyn
      541 dtwlnfkhaf ngsqkidani gfrynsskse ydtglsynta sddfvtlnsg qntlrtiggs
      601 lgqwnwlnty lnlkysaysk yflsanlsvd gssrfgqkip dvlslgnyry avlpsvagaw
      661 lissenfman nkfvetlklr lsyglngndd ignytaktyy vsqnflgrqg lvrgnignpe
      721 lkwetiakfn agldasflke rlslsfdfyh nnitdmiiye ptltatgfdy aitnngamqn
      781 sgvelgisar ainkqdfkwd lgvnlahnkn eintlpgnad lmtnfggati ltrvgqpanl
      841 fygyktngvy atdaeaagtg lmnktaegal vpfkggdvrf vntnndnvid eqdrqiigda
      901 npdlfgsfsn tlsykrftln alftfsignd iynglranle slsgyenqtp nvnnrwrnng
      961 qvtdvpaarf gdpmqnsrfs drwiedgsyl rlrslslsyn iptksnfirs atvyaianni
     1021 ftatkylgyd pefnanesvf argvdlgmnp lyqsmqlgvr igl
//
LOCUS       WP_120183065            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pelobium
            manganitolerans].
ACCESSION   WP_120183065
VERSION     WP_120183065.1
KEYWORDS    RefSeq.
SOURCE      Pelobium manganitolerans
  ORGANISM  Pelobium manganitolerans
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pelobium.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Pelobium manganitolerans"
                     /db_xref="taxon:1842495"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117035
     Region          43..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msnykilsls aalvvalgst qpiysqnksa eavekskets klkvkgkvvd gltgapivga
       61 svsvpqytak itdqngafei svptmqinle vaivgyqtvv vpanktdltv tlypegtksf
      121 yaetytpfah dvkhvsqmvg avdvvdfqga weqnsetvdn ylqgklagvn vtrksgtpsm
      181 ganiairgln slytqnqply iidgliynae ihsssitngh ennplqnidv rdiesvtvlk
      241 davataiyga kaangvivit thrakelttk idfevssgfn qtpkripvmn afnyrsylnd
      301 vlatstltge eiaalpfnnd skgfidypvy hnetdwqnkv fkteldksyy lrvtggdnia
      361 kyalsvgfnd dngviantqq nkytarfnsd lsltkrlkaq tnislgygqq klkdqgfapn
      421 tnpiflaltk apffntnela pdgtvspnya padyfgysnp lqliyngvnd kksyrflggv
      481 nfdfkltdhi nlsnttgity dkaqenffip akgiaseiin ntvvtsrlgt qvaryfsitn
      541 dfraayakti ndkdkfnaiv glryqhhdae qdyalgynsa tddlvsigns daakrtfggn
      601 igewanvtfy glanyaidnr fiinaaisld gssrfgseae ggvnvfedhp fgvfpsigga
      661 wiissenflk dnkninllky risyglvgnd dignynakqn yvsqnflgvq glvrdgvsnp
      721 ylrwetvrkf ntgfdlsmfk erfnlsidyy nnqtdkmlay qngntlsgia yyldnsgkme
      781 tngldlslfg kittgkvkwd aglsvgtykt kvtslpetvy tniggatyit kvgeapnafy
      841 gyqfkgvfst qaqasaagls rydeagnkia feagdaifad kdnnkviden dryvigdpnp
      901 dfyggfnnsi sykkwslgal ftfsvgnday nytranlesg nglynqtdal lnrwradgqv
      961 tniprvtyed pmgnarfsdr wvedasylrl rqlslaykft fnksivnyln iyatannlft
     1021 ltkylgydpe fsmntdvyrq gidatlepqf ksfqlgvrlg l
//
LOCUS       WP_120183310            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pelobium
            manganitolerans].
ACCESSION   WP_120183310
VERSION     WP_120183310.1
KEYWORDS    RefSeq.
SOURCE      Pelobium manganitolerans
  ORGANISM  Pelobium manganitolerans
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pelobium.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Pelobium manganitolerans"
                     /db_xref="taxon:1842495"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118387
     Region          24..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknlsilil llgsvagqql raqqtlsgvl sdagtgqpva gayltavnnk sraitnakge
       61 fslalrllpd tvkvlalgyk gqthvvkntn qlrislqpde mllqevvist gyqqlkpseq
      121 ngaitsiskq qlgqqtstni lqrlesispg ltvarnkaen pqnntgirir glgtingsld
      181 plivvdgfiy egnidninpn dvesvnilkd asassiwgar agngvivitt rkgtyrqplr
      241 mgfntnvtts gkpnlmelpd mgtasfidfe kqlfesgyfn sqitgspyla ltpavkvfyq
      301 rqqnqitaad saklinlyln sdrrsqalsh yyspaltvqn nfslsggseq tkylfsaayd
      361 qtrgnlyeqn srislrsdla frlfpkleln tgviftgans qsgrdtytat rygsrltayl
      421 pifdaqgnel paeseysray lnanadprll dwayyplqdy khrdlstkrq elyataalay
      481 rplnwlkatl smqyqnqqsk nenafdaesy yarslvnsyt qvsagnisyv ippggvlnln
      541 nsevnsytgr fqldgnwqkn dhelsgiaga elrqaqaegs gqyyygyqsd plnytavdyv
      601 ntyphylngn dgnptaaprl sstvnrfvsl yanaaysyrk tytfnasirr dasntfglst
      661 ndrwtplwsa gagytisnas ffkvkaidfl klsitagysg nvdlsrtala vanagtysvs
      721 glpfirvtqi nnpelrweki rqinysldfa vlnrrlsgni syyvktgkdl ygetqydyta
      781 wgrsaeittn iasmqgrgwd islqsnnltg klswqtqlll nyntnkvtdy fspaasryss
      841 llssgtsiyp vvgyplyavg ayryaglnsq gqaqgflngq pstdydqlyn tldteglksn
      901 iiryfgsaep lyngslintf gyknlslsfn igyrfnyylq kntvnyqslv slgighsdyd
      961 rrwqkpgden ftdipaltfp lssqsnafya tsertiirgd hirlnyinld yrvkiaqgnk
     1021 likglniyan asqlgvlwhq nkegidpdyi nslsprtsyt lgvrtqf
//
LOCUS       WP_120185593            1146 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            lutimaris].
ACCESSION   WP_120185593
VERSION     WP_120185593.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum lutimaris
  ORGANISM  Tenacibaculum lutimaris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1146)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1146)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1146)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1146
                     /organism="Tenacibaculum lutimaris"
                     /db_xref="taxon:285258"
     Protein         1..1146
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126486
     Region          35..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          116..1145
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqfkktrlf vigiflifqa nygfsknldn ekislelnda tlvtvfeqmt nltqfkftyg
       61 dyiannsnky tvsfqnkevt iilddlskkv gfdykieenn iiigkreqqk ektiqqkisg
      121 kvvdktgepl pgatvsikgt sigvstdfdg nfqleltnea ktlvvsfvgf etkeinigse
      181 tvfnitlled aqvldevvii gygeqsrakv vgavgelkne eltkvasasi eqqiagkmsg
      241 vvvnqfngqp gaasqivirg tgtltaganp livvdgyplt egsslnsins ndisdisilk
      301 daasaaiygs raangvilvt tkkgksdqkt sislhtymgi qeqssgvelv daykhaqflt
      361 earnwgyvsk dplnrsesdp nsvrvtkkin grnidgrely ldylqpyldg eqglintnwm
      421 neafraapmy nydlsisggn kktryytslg yfhqegivig sglkrysatl nldskisdkv
      481 kfginikptf tvqdalnqss rssgalalip lnfpsyspyk fdgslnisdq lineqreieg
      541 vringtpven lvatsrkvid qkdrfrtfgn iyldaeifkn lkykfsmggd ydayvrnyyy
      601 psdvgsyrtp aprsdadate rklnrynylv entlnyqlks nkhslnvlvg htfqkekiss
      661 ttvkatgfad nniqniaggs sftvdntldi wtlesylsrv qydynskylf saairadgss
      721 rfgsnnrwgy fpsvsagwvf nreeffplkd iitfgkisgs wgqtgnnqig nyssqalvtd
      781 snyvfdggla pgyitttapn pdlgwevass lnvgldlglf hkvnlsaayy ktntrdllld
      841 vpvpqqtgyt tvlanigeme nkglelqlsg qdfslgnvkv gfnanltsyn nkvlalgpgq
      901 keiatgtdqn fvtkvghsia eiygyevdgv fktqeeidnt phlpgtltgd ykvkdmngdg
      961 vinvddkvsk gsympdftyg fganlqyegf tfsfgfngvk grtlmdgdms sltesgegfa
     1021 vpttyyfenr yhpennpngf lgqpnfgnfs nsrkllrssv vvernngdyi rlrdvrlayd
     1081 fsesllnklk lsklqvyvsg nnlftstdyr gwnpdgtsgn iltsgfnngg nypvaktylv
     1141 gvrvty
//
LOCUS       WP_120186432            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            lutimaris].
ACCESSION   WP_120186432
VERSION     WP_120186432.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum lutimaris
  ORGANISM  Tenacibaculum lutimaris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Tenacibaculum lutimaris"
                     /db_xref="taxon:285258"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116678
     Region          26..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlhlknvic vlfffsfmln inaqekkiig vvsdsagplp gvsivikgtv kgtetdfdgn
       61 ytmnvktgdv lvymflgyak vekvvgesst invamkedan ildevvvsva yaakkkkdii
      121 gavsvvsake vgdlkvttvt ealqgtsgls mvnasgqpga sptirirgvg slqgnvdpli
      181 ivdgaqfagn lnsinfndve sysvlkdada vslygnrgan gviiiktksg vntngegiie
      241 intsygfsdk atddysylsa eqivttswqa irnerldqgd aaeqaaifas snvmtdlavn
      301 pysinepvdt ngkiksnarl lyetnyydil tqkatrqdvs lvlrggnekt ryfvsgafld
      361 segfslnskf rryngrvnls sdvkswlsvg anafvtises nvptqsgsty anniqyvrsv
      421 ssiyplykrn adgsfisdnn gnkqydfaeq rgffgnynpl aetygsvkly erntfnfspy
      481 ltvkfndkin lksqfnytny lyegnlfnnh fvgtpkeqvd nrystkernt tktwnvintl
      541 sykntfdekh tltgllgqem ydntynrvsa tstgyafanl peldngvlpt gassiteknr
      601 lysffgrldy nfdekyyfgt gvrrdassif akenrwgtfw svaagwsiyd eflkgnglvn
      661 slklrasygt vgnqninqqf tfldqnglgf nilanpglvp taianpdlkw ethnklnigv
      721 dfaffnskvy gsleyydnrv tdllyfdvpa pstgsegagi dgnnesralg kwrnfgemsn
      781 kgfefnvnsv nvendkfrwt ssfaistnqn riedikqien rgsfrweagr dryefymrew
      841 agvnpttgap ewykdvvdts gkvtgrekts tyseatryyt gksalpdfeg rlgtkfeyng
      901 idltlnfnyk fgnyiyntdf sslmkarnlg eqsssetlka wqkegditdv pkltteaddf
      961 nsrstrwlqr gdfirlknis lgynlnqeml dklkirklrv ylsadnywtw krennlddpe
     1021 qafngitdnr stvlktlslg vnisl
//
LOCUS       WP_120186505            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            lutimaris].
ACCESSION   WP_120186505
VERSION     WP_120186505.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum lutimaris
  ORGANISM  Tenacibaculum lutimaris
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Tenacibaculum lutimaris"
                     /db_xref="taxon:285258"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117183
     Region          25..1068
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfngilt lllalvvqis faqdrtisgt vsdetgplpg vtilkkgttq gtetdfdgny
       61 sinaktgdvl vfsfvgmkta ertvgasnqi svllegdnll devvvvgygt ttrqsytgta
      121 kvvkteniaa ksfsnvsqsl agevagvnvi ntsgqpgsta tirirgfgsv ngnrdplyvv
      181 dgvpfsgsin sinpgdiest tilkdatata iygargangv ilittkkgra gsssidvsik
      241 sgvnfsglpr ydvikspeey ietsweaman rgldinpnad gaayantnlf ssrginakyn
      301 mwnvnsvsdl idpatgkvra gvtrkydpen wgdygfqtsf rtetnlnmsg gnddtkyfss
      361 fgylndkgyi igsdynrytt rlnlthkpak wltatanigy aysknttngq ssdsgsifwf
      421 vdnipsiypl yerdangali ndpyfggfkh dygvgrgfga ltnsiadaky dtnqskrhel
      481 ngnislnfqi adgltfenty gaqyfmikad ninnpfygsa egqggsifrr fsevtsqnfl
      541 nllrykkqlg ndnleillah etnqyefdts taskenlvni wggneslnny iitsspstgy
      601 tneaniesyf gqvnysindk yyftgsvrrd gssrfvdnkw gtfgsfgasw ilskenfmas
      661 ssfvnflklk asygligdqa gvglynyqnn ydignlnnei slsvrpignp altwetskmf
      721 qvgteftlfn niidgsvdyy vkntddlife rrdapstgda iltvndgqlr nsglefdlts
      781 hiikkdnfkl dfsingeian neliampidp atgeqkvldi agsygravgh siydfymrew
      841 agvdptngyp lwtqyyhdan nngsldageg iqslyeyqta npnnavsktt tstydeatek
      901 figksvipdv rgafrlsgqi hnfdfstqft yslggyaydg ayaalmdndq vgnnnwhtdi
      961 rnrwqnpgdi tdvprlmsnr npqvnslssr fitstdylsl nnlrvgytip kkfiensgvs
     1021 nvniwmsgdn lfllsdrkgf npstsetgaa ntyryspltt itlgvnvkf
//
LOCUS       WP_120202297            1037 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Ichthyenterobacterium magnum].
ACCESSION   WP_120202297
VERSION     WP_120202297.1
KEYWORDS    RefSeq.
SOURCE      Ichthyenterobacterium magnum
  ORGANISM  Ichthyenterobacterium magnum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ichthyenterobacterium.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Ichthyenterobacterium magnum"
                     /db_xref="taxon:1230530"
     Protein         1..1037
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113057
     Region          25..1036
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkltglma lfmvlvmqfs faqektitgt vtsigdglpl pgvnvivkgt srgvqtdfdg
       61 nyaikasnge tlvfsfiglk dneikigssn iinvqmqedi asldevvvva ygdtsslrts
      121 pasigtvkae vledranasa iqnlqgqiag lnistgtgqp gadstiilrg pgsingniep
      181 lfvvdgipvd ednfrsinpn dietysvlkd aaaaniygnr aangaivitt krgkynqalk
      241 frystsygyn elqdqpfelm nsreilnwqr sngaglgfgm tdseiaaisn qvntnwadvf
      301 frrgttlshd lsissggets nnftslqyfe qdgifigskf krfsvrnnfs grssddkfsy
      361 nlnlslgfsk tdevgdsags gstffnpfsa alqglpylsp ydpdgsittd ggispgdina
      421 ilgrgasnfp yvllnslsln tdreeeikil tsfnanwnfa knltagiqvg mdlstesrle
      481 ilhpnsilgp fqdrvgnnpa tifggiqeet ytrdfrfnti sslnysntfa dkhqldvtay
      541 feylkghldg fdydqfgldp rligdgsafv pgtttevlgg atvnpyidtl nsftttvgni
      601 svfgaldyey dgkygfsagv rrdnsfrfid dnawgtfwsi agrwnidqea fmsdsafdll
      661 klrashglsg ndrirggyyg atnetrnlyt agtgyngtvs tvpgqvants lrweettqsn
      721 igvdfsvfnr klsgsidvye kttddlfqnn nisllnatgg tiesnlgtmv nkgielqlry
      781 niyddsdwki svnangsynk neiealppss nglvnlggst algegeslgs fylveyagvn
      841 psngnplfvk adgtltetll dadrvfsdrs iypvwqggfg sdikykgfef ttqwsfvadv
      901 yrnnldfasl qdvsvgsven grnrsvtlfn awqnvgdite vprvgsslgg vdyinqtdry
      961 ledasflrlr nvtlayslpd svleqlpisg mrlyiqgenl ltfskyrgwd pesnfrttdr
     1021 gqfptpkiyt fgatinf
//
LOCUS       WP_120202470            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Ichthyenterobacterium magnum].
ACCESSION   WP_120202470
VERSION     WP_120202470.1
KEYWORDS    RefSeq.
SOURCE      Ichthyenterobacterium magnum
  ORGANISM  Ichthyenterobacterium magnum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ichthyenterobacterium.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Ichthyenterobacterium magnum"
                     /db_xref="taxon:1230530"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115722
     Region          25..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lllafvvqmt faqektisgt vsddsglplp gatvlvkgts tgastdfdgk
       61 ynikantgst lvfsfvgyat qevsvgasnt invqlaedte aleevvvtaf gkkkqkrslg
      121 yaatavsgek ltevatlnpf eslsgkvagv disapnqpga stkivlrgyg slngsgplyv
      181 idgtpissas nssslsgltt dvnrsfdggt nindldansi asinilkgga atalygsran
      241 ggaiiittkk grsgqklkve lnssidflev ariphlqqrw gqgwngvdfs glpnggqgat
      301 nengswgplf ngnlrvwgqi vnasqqikpy enlednikdf ydigntftns lrlsggsdka
      361 dfsliytrvd tdgiiptdad alnrntlsln sgiagdkfrl rvnanyaqtr qnavntgqgd
      421 nagegesfmq eliqiprgvs vldladytnn pfnnndnfyt pysrnpywvl nenettldre
      481 rfygninmsy dlatnlvgtl qigadisngt rhshgaviny tpgspqallg gttnaggvte
      541 ytdqrrqyet flsfdynksl sedfgleasl gasmnnryfn slqvsitnld ipnfyeisns
      601 avlpittqnn sqlkgysafg aatlsykeri ylnvtgrnew tstlaigsns ffypsvnlsg
      661 iaidngehfl klragyasla nsapiyltes salqasavay fgninfpfag lnsfeiartl
      721 gnldiepeft deyeigfegr ffnnrvtadv ayykkttdgs itslllpnst gynrifgnfm
      781 dienkgieva lglvpvrtdd fswnidytft knenkvtklp egldkllins afgvnfyaie
      841 gqplgefqar vpllnedgqv vvdpntgipq qsteeqkign sqrdfvmglq ntfkyknwrl
      901 sfgidwkegg emysytsrll nftgnalstt yndrntfivp nsvvdngdgt ysenvtpitf
      961 gavtgyysas nnpsteavnh vidktfirlr dmsisynfpe kiigntglss lslslygrnl
     1021 alwtpdenpy vdpevttfgg ndivtefgef agnpaqrtyg faikmsf
//
LOCUS       WP_120212211             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Epilithonimonas arachidiradicis].
ACCESSION   WP_120212211
VERSION     WP_120212211.1
KEYWORDS    RefSeq.
SOURCE      Epilithonimonas arachidiradicis
  ORGANISM  Epilithonimonas arachidiradicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Epilithonimonas.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Epilithonimonas arachidiradicis"
                     /db_xref="taxon:1617282"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109526
     Region          32..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrllsv gvlfftgqal maqkakkdta stkdieevvv ignikldpaq kvgsyntvsk
       61 anfestpfss idevlngrva glnfssasgd pgssnlviir gvssligtpn plyvidgvvi
      121 gkgadnaqvm eswnplaaid pnaiesvdvl kdasatalyg srgangviiv ktkkgkfnqk
      181 trfefstetg iqdrafdklk vmndeeyiky gsilmwnsrg iktsadliqn mddarryfls
      241 vyeptyynng elkntntnwt kavnrnnsvv ntynfgvsgg dsntsfrigg syyqnkplvl
      301 tagfdrisln aavnhkasek lkfgmnvnys nikrstyfgg ratanpvtqs imlsplrpiy
      361 nddgsynqel sddvgarsgf npvsilnear qdsrintfia sanmdysfak dfsfnstfgt
      421 qtqfmkemtn iqaghpvyti mednqgflgd hrttifeynw vnslsynkvi adkhtigaaa
      481 gieyqdhiyn vlsaqtftmn npdpyfqysn eqfvsnddlq wrqlsyfgkl sysydkrysv
      541 tgqlrrdgns tlgnekfgtf wslggswnva qesfapalfs tfnlrasygv lgnipyadqw
      601 gpqynsatnl fynytygwgg npgyagfnna gnpnlswees khldiggeig ffndrlkftl
      661 dyyrkitdkt ifdfypaaes ggpgaqyani gklnnsgfel viegspikns nfqwnvsang
      721 aysktmvdrl egqklvtfng dtsdssnelv alaeghvlge yyvvqwagia qqddptkgik
      781 agdalfytdg sktdvtnvrt daqrawmgks afpiynvgis nefkyknlsl sfllsgqfdf
      841 yvsngvhsyt ihdgafptrn qitdalydsw tdapgmenfn asnpkailtn pstsrlessr
      901 flnkgdhirl kemriayslg dvfkksvgln nftiylrgtn lltyvfdkdl nydpesntns
      961 wswlgkgryw yaspvlrtvs mgiqlgf
//
LOCUS       WP_120212670             962 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Epilithonimonas arachidiradicis].
ACCESSION   WP_120212670
VERSION     WP_120212670.1
KEYWORDS    RefSeq.
SOURCE      Epilithonimonas arachidiradicis
  ORGANISM  Epilithonimonas arachidiradicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Epilithonimonas.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 962)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Epilithonimonas arachidiradicis"
                     /db_xref="taxon:1617282"
     Protein         1..962
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105646
     Region          34..960
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklkifsg igalfftgqa laqnvkndtv pteksiaevv vlgysrtttk aksneavttv
       61 gaetlenrpn vsflnslqga apgitvnsms gspgsgkfni lirglsslna stdplyvidg
      121 lissgtqfrn lnaediasvs vlkdaqatav ygnrgangvv vintknaryn sglkinynal
      181 ssfstfpkps yntanakefl qiqknygage gnlltqaqid nwagadtdwg keffqtgmsq
      241 shnlgfrfgg envavysslg yqdvegimks tdfkrftfrn nitgkssngr ftynsqlaas
      301 ysrrhqfdee tntainanvv qnplfgslmg rptispyrya ngrglfaaig tntagnnalv
      361 lsdiinggir nrftemgvla nlnlnykltd ylsignkvgv dyknsdrvla rdpngflsla
      421 vavpsgipyg gsetmnntsd ltfsnvtnit fnksfglhtl taaaymdylk vhwqfkqqtq
      481 ngldpinwkf gagtgyvpfn tatptlylpa vsgrqinggt layfgtldyd ydgkygiagv
      541 vrrdgsyrfl panrwetfws asarwnidke sfmentnfrm lklrfsagtt gnqnlgvpad
      601 ntnpltlnas nyldyygttl tassfmglpg ylmsnlsntq lrwekvtqyn agldfaykfv
      661 egnidvyrkv tsrmfndlvv sapagppsti ntttkfirgn ngemenkgie allrfnvinn
      721 dnvkfsvfvn gaynkneiis ldredttgdf vnvvggpayq whlypyigvn sangnqqfld
      781 ingaitetpv aedrrltgks ylpkftggfg fnaeyngffl dtlfsfqqgg wiydnfyqwq
      841 mtpayagany nvsadllnaw tptntsanvp slsasnigre gqsdrflyrs dfirlknisl
      901 gysftrnqlg nlpisgfkif aqaenlitws dwkgydpepm nryslnifpn aktvsvgfnv
      961 ef
//
LOCUS       WP_120212672            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Epilithonimonas arachidiradicis].
ACCESSION   WP_120212672
VERSION     WP_120212672.1
KEYWORDS    RefSeq.
SOURCE      Epilithonimonas arachidiradicis
  ORGANISM  Epilithonimonas arachidiradicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Epilithonimonas.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Epilithonimonas arachidiradicis"
                     /db_xref="taxon:1617282"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110983
     Region          31..1008
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklttsvla vvlsssfavv saqtvqdtak tqdiegvvvt algikrekra lgysttevkg
       61 dqvssvpvan vsdalagqva glniqqsgtm ggstnmvirg iksltssnqv lvvvdgvpin
      121 ndtynqagmq sgqgsydysn gmadlnpndi esvnvlkgaa asalygsrgm ngvlmittkk
      181 gkrtkkigve fnsaltlgtv dkttlpkyqh eygggytgss fysgdingdg tvdnnivyty
      241 ddasfgtafn pnmmvynwds qypqlpgylk ptpwvagkdp nsvwgpsaty qnsvafsggn
      301 engrfrlgyt nfnqdgglpn msirrntidf tadynltdkl nvfgsitytn trgkgriytg
      361 yesrnpmqgf rqwwnmsvdl ekqkqaylmt gqnltwnikd yesqavgytd nfyfnryenf
      421 qtdnrnryfg nfglnykltn wlsfmgrytf dvydelqeer vaigssdqgr lsnggngeyy
      481 frdqrvyemn ydaifnvdkd fgdnfnlngn fgfnyrrngr vgnsavtngg lkvpglysit
      541 ntaepltenn lsqfdikksv dglfaqaslg ykkmlyldgs vrtdrssalp tdnmrywyys
      601 gatsfvfsel fankdivnfg kvrfnyakvg ndtgayqlyn tytfipaist eagnafgasl
      661 pqvtnnpnlr aefmheleag lemaflknri sfdlsvykqk tedlitptdi ssgsgftgmw
      721 vnsgdienkg iearltvvpf ktkdfswelt anwsknkskv tringdipfl efasmwnvts
      781 gallgestgt irgtnyvyln gervvgangk ylisddpqev igdavpdwrg svmntlrykn
      841 lslsflidvk qggdvysqdm afglatglya etaglnelgn pvrntvangg giilpgvkad
      901 gspnttrtqm snytnglgyy ggpeamhvyd gsfvklrnvt isyrfpketl glsfidsmtl
      961 sligrnlwii hknvpyadpe aglgagnaig fqngahptfr efgaslkvef
//
LOCUS       WP_120213098             954 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Epilithonimonas arachidiradicis].
ACCESSION   WP_120213098
VERSION     WP_120213098.1
KEYWORDS    RefSeq.
SOURCE      Epilithonimonas arachidiradicis
  ORGANISM  Epilithonimonas arachidiradicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Epilithonimonas.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Epilithonimonas arachidiradicis"
                     /db_xref="taxon:1617282"
     Protein         1..954
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104320
     Region          39..953
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlfhlsktn raalffamtl lptglvyaqs krdtvqkekq ieevvvigyg tqkkeavtgs
       61 vaslsgnalk evpsanvtda lqgrvagldi grtstkpgav qqirirgers ltgsndpliv
      121 ldgipfigsl gdispsdiks ldvlkdasat aiygsrgang viiittnrgg kgqkakfsyn
      181 gytgyqtifs kypmmdgpkf aklradanlf tngpdeandv ntdwqdlyyg vglmmnhdig
      241 vtggtekggy nfgvayfqqn gvvplqsykr lsirgaldqe vnswlkvgfs tnsnfsindf
      301 ngvsgapvlg ysplgkpyle dgsprlrttf anldqtaiqt rtilqslgda yadrtnafss
      361 ynnlyseikf pvdglkyrln vgltyrnsns gyylgtgaln fqpatlssas ignslttqwv
      421 lenlitydkt fgkhkinava lysaeqtrfn sssigardvp idafqyfnlg qaqgeitinp
      481 anqgywrrgl mslmgramyq ydnrymltat vrsdgssvla kgyqwhtypa vsigwnvane
      541 sflrdsryin mlklragfgq tsnqavdpym tfgslsttpy nfgsnyavgn fvnrapnysl
      601 gweysktwny gldfsilnkr isgtieyyvt ntekllldkv lpqssglgvv lqnvgasqnk
      661 gleislngvi idnpegfswe vggnlaanrn kitalasgqd rnvgnlwfvg yninaiydyq
      721 niglwqqgdp ylnilepqsg aapgmikvly tgaynadgtp trainesdrq iintnpdfvg
      781 gfntrlaykn ldlsivgafq sggvlvstiy gsagylnrlt grannvdvdy wtaenpnvry
      841 pkpggllsgd npkyastlal fdgsfvkirt itlgynfnkt ilddlgvsnl rlyvtlqnpf
      901 vfaspyyrhs gmdpepnsrg denqavnsyk rnqlvigtnn pstrnyllgl nltf
//
LOCUS       WP_120213495             957 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Epilithonimonas arachidiradicis].
ACCESSION   WP_120213495
VERSION     WP_120213495.1
KEYWORDS    RefSeq.
SOURCE      Epilithonimonas arachidiradicis
  ORGANISM  Epilithonimonas arachidiradicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Epilithonimonas.
REFERENCE   1  (residues 1 to 957)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 957)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 957)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Epilithonimonas arachidiradicis"
                     /db_xref="taxon:1617282"
     Protein         1..957
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107376
     Region          34..956
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrknyvklpl liaalyfgsd lhaqstqdtv akenkieevv vigygtqkkv dltsaittvk
       61 aadivktpsg qatqalqgkv agvqiiangs pgeapkmnir gvhsingdnq plyvvdglfv
      121 nnieflnpnd iqdftilkda sasaiygvla angvvvittk ggsfnrkpkl tydsyygaqy
      181 annvikmana eqytnfales gsqfeidaia naiqrfgrsr inpnlpnvnt dwykealria
      241 piqnhslavd ggsdkvaysl gghyfsqdgi lnmknsyerf nirakvdvka tdwlnvgasm
      301 nytrgekydd egsawqqvyy avpimpvydp lftsatykpy adarvlgyrs sdnpfalmdn
      361 vdklgiqknl ifnayaeisl lpkeltfkst lsynsrtfne rlmelpyfvn nfaggfqrti
      421 enssitrnna tyedyiwdnv ltwnktlgdh dftlmggtsf adqlysfmsi kgffyqgspf
      481 srynestwyi nntadtgrit ndgrddvkps rfyrtsyfgr lsykfkdryi lyatlrnegs
      541 nkypnqktin lpafglgwva seesflkgvs wmnllkfrgg wgrlandnvp nnrpstaesv
      601 nsvfadtylp afqfttfldd vrreyteetn igisaeflnr rltlegdyyv kdtkemvigv
      661 pptigtavsy rnvgtmrnkg feislgwrdk igedwgysin anftnndnnv tklvdnasfi
      721 argsgdfpqr lvvgqpmdvf ygydvigvyq nqaeinadpt avaynatnss spikpgyfky
      781 rdmngdglid dkdrmylgsg iptyyfggsl avnyktwdls iafygqggnv ilnrnraevi
      841 rttgrnidad fainrwhgeg ttneyvsseg yrnswnnqkl skfwlqdgdf friqniqlgy
      901 tlkadgipem rfsvtadrpf mwtkaenlmn peigingvnl dvyptpsvvs fgysikf
//
LOCUS       WP_120230676            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. AG363].
ACCESSION   WP_120230676
VERSION     WP_120230676.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. AG363
  ORGANISM  Chryseobacterium sp. AG363
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Chryseobacterium sp. AG363"
                     /db_xref="taxon:2183997"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114993
     Region          130..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklcravll ilvlsigcqg lyaqeklstk rvnfetgktt aseavgkfls envkdkiysn
       61 ddlkdysvqp tkcknelvmd clnkilrdvp veifidnnsv iirpkkdspk asttelsqqs
      121 tahrdtvses sdihtideit inagyykvrd kdktgsiakv sardienqpv tnvlstvqgr
      181 msgvnivqns gvpgagfeiq irgqnslrtg sfteqngnvp lyvvdgvpfs eispqksqis
      241 stiipggnin plntinpndi esievlkdad ataiygsrga ngvilittkk gksgkvslnf
      301 stnygiseti snltllnkeq ylnmrrtayk ndgiatypan aydvngvwdq qneidwqkil
      361 igkkattsnt qlsanggskt tnflvslghn eqttvygqdf kytsnnfssn lshrsennrf
      421 qinvsnlftq qknnviysdl ttraftlspi spqlynpdgs lnwanntftn plaaynasyn
      481 ndtklfqtnl nseyklfkdf klkvntglny ttidelalqp ntiynpnigs glssansqar
      541 qkkqnifsfi iepqinwses wgnhnlqilf ggtfqsmvrd teeelgfgfe snqfisniaa
      601 aktlmklens nieykyaaiy grlnyqfkdk yilnltgrrd gssrfgpnnr fanfgaigaa
      661 wnfskenllk nlewlstgkl rasygsagsd nigdfqflnn yivsstliyn nitglspsrl
      721 ynpdysweit kkmeaavelg ffknrlnlst alyrnrsssq lvgyqlsavt gfssvmanln
      781 atienkglei eitgrpiakk dlqwessfni sfpsnellsf pglagssyan qyvigqptni
      841 vklyqfegid pstgqyrfkd fngdgkitsp edrqvvadig ikyfggwsnn fryknwdlsi
      901 lfqfvkkkgw nynsimslpg tmsnqptqvl dvwspqnptg yympystvnt nihnlfrtst
      961 aavsdasfir lkniqlayti plaegifkna kiyfqgqnll twtnffgvdp ealtsgflpp
     1021 lrtysfgiqf nl
//
LOCUS       WP_120214767             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Epilithonimonas arachidiradicis].
ACCESSION   WP_120214767
VERSION     WP_120214767.1
KEYWORDS    RefSeq.
SOURCE      Epilithonimonas arachidiradicis
  ORGANISM  Epilithonimonas arachidiradicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Epilithonimonas.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Epilithonimonas arachidiradicis"
                     /db_xref="taxon:1617282"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110739
     Region          126..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktvmsvil lvatglpiay gqagqtppva mkkenrvsii kvfdklskss kipflysstd
       61 fkdvfvndsa inysslessl kylkkfypie yeiknntvvl rktnvklisq senfpipkdt
      121 isvqekkide vviigygkvk ksdatgsltt vkidsendgs pvsaqealtg kaagvniisp
      181 ggapgagsti rirggsslsa sndplividg iaidnsstsg ssnilgminp ndietytvlk
      241 dasstaiygs rasngviiit tkkgskktrf qyssntkvsy npkmldvlsg deyrsfikdy
      301 yagnntiing lgtgntdwqk eiyrtsvsnd qnfsmtgavk dipyrlslgy tdqqgiirkn
      361 syermnasla inpsffdkhl ninlnykpsi enndfisnpa ssavgfdptr pvydnssqyg
      421 lgyfiwkdas gkpitiasan pvsvlnlrkd eskvvrhign iqldykihgf edlklnanag
      481 fdilksngdi fvpdnaplaw tsigndgqgl ienytqkknn tqldlyanyt ktlsdhkidv
      541 mggyswqkfw qsyddnqtnv sgnkvyqnii skseyylvsf ygrlnytfkd rylftatlrn
      601 dgssrfskdn hwglfpsaaf awkineesfl kdssffsdlk lrlsygktgq qdiggdyewm
      661 qtytfsqsna lyqlgnqyyq tirpngydpn lkwettstyn vgldfgilkn rvsgsievyk
      721 rttddllnki svaagsnltn miftnigsme nkgvevslnt ipikttdwqw sldanitfne
      781 skitkltlvd spnygvnign vsgstagtiq thsvgyspyt fylyqqeyde agkpiegkyk
      841 gglvkdknpm pksflgissk lsyknwylgf nghanfgnyv ynnvkskdyk tkatlgngty
      901 snllsytaeq gfdnlqlysd fflekasffr mdnitlghnf knisdkfdlg vnlsvqnvfv
      961 itkysgldpe vylgidnnmy srprsflfgl nvnfk
//
LOCUS       WP_120231241            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. AG363].
ACCESSION   WP_120231241
VERSION     WP_120231241.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. AG363
  ORGANISM  Chryseobacterium sp. AG363
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Chryseobacterium sp. AG363"
                     /db_xref="taxon:2183997"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110981
     Region          29..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknsyynigg iffglmftav sigtkaqtrt isgtvtssgk plsgviisqe gsdqitmtgn
       61 ngtytlqvsa entillfrhp dyaeekftlt nqtvvnisle qkvkgieevi lnagyykvkd
      121 kertgsiakv sakdignqpv lnvlsaaqgr vagvnivqns gmpgggydiq irgknslral
      181 gnnplyvvdg vpvggemasq fsgavlpass inplnsinpa diesieilkd adatsiygsr
      241 gangvvlvtt kkgkngkvga gaggagnlgl nagtsyavss visnltmmkt edylrmrrqa
      301 yqndgisayp anaydvngvw dqgrytdwrk eligntadaf tanvslnggn drtsflvgyg
      361 hneqstvfsk gfkykadnla anishssedk rfqlsvssrf slqknnvlse ditrqaylmv
      421 pyapalylpd gslnwennsf nnpaglynss ysyenkqflt ninvqyellk ywflkfsggl
      481 nyqsfdersl kpntmynpas yqgqssassq syrsnqdrfs filepqlswq mkkgrhaldv
      541 lvgttfqrdt gnqgsmigig fesnafieni gaartriitd qikteyryaa ffgrvnyqya
      601 gryilnvtgr rdgssrfgps nkfanfgavg aawifsqegf lknkkwlsfg klrssygttg
      661 sdnigdygyl dtydlseyly nntaglnpsr lynpdyswek ttkleaalel gflknrinli
      721 tawyrnrsss qlvgyqlpsi tgfpsvlanl davvensgwe lelsgrpfsg gafqwesnvn
      781 isfpknklva fpglagstya ntyvigqpit svkvyqyegi dpatglyrfk dfngdgkita
      841 pddrqaveni gvryfggwnn tlryknwnls flfqfvkqrn wnynnimpip gtmnnqpqev
      901 ldvwsaenpg gsympyssgs ngirnqlhvf fmnstatvsd asfirlknle lgyqvpvkgt
      961 fksvkvyfqg qnlltftryf gpdpefrnig flpplktysm gvlitl
//
LOCUS       WP_120214088            1001 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Epilithonimonas arachidiradicis].
ACCESSION   WP_120214088
VERSION     WP_120214088.1
KEYWORDS    RefSeq.
SOURCE      Epilithonimonas arachidiradicis
  ORGANISM  Epilithonimonas arachidiradicis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Epilithonimonas.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Epilithonimonas arachidiradicis"
                     /db_xref="taxon:1617282"
     Protein         1..1001
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110377
     Region          29..1000
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknsyynigg iffgliltav tthskaqtrn isgtvtssnk plsgviisqe gsdqvtmtan
       61 ngtytiqvsa enpillfrhp dyaeekitlt nqtvvnisle qkvkgieevi lnagyykvkd
      121 rertgsiakv sakdienqpv nnvlsalqgr mtgvsitqns gvagggfdik irgrnslrgy
      181 sttgydgnkp lyivdgvplp lvndfnsgmt asilpynetn plnainpddi eslevlkdad
      241 ataiygskga ngvilittkr gkkektevnl rtsyglgqmt nlpkmmnlee ytamrklafa
      301 ndgvavpsna ydingvwnpn kttdwqkyfv gntssvsdvq lgvsggsgnt qfsvsgghne
      361 ettvfpgsyr ykrnnlgvsv nhtsadrrfq igfngtaalq dnvlpptdfn ivypvlapna
      421 pdlytssgmi nwenntfnnp mgpatqtfsv ktkslnanmt ssyqfgsgfs anlnsgysty
      481 nsyeqkifpk ttynpssnig ssssslrkaq klneswilep qlnyekrlek hqfsalvgas
      541 fqeqksdniv ilgrnfpsdd lltnmaaaas itvpsasesl yryqavyarl nygynkryfl
      601 nltgrrdgss rfgserryan fgavgaawlf seekpfkdrs wlsfgklrts ygiagndqig
      661 dyqyydtyqs tggsyggnsg lvpqrlynkn fgweltrkfe aalemglfke rlnlnigyyh
      721 ntssnqlvgi pmpatvgfss iqanldatvr nrglevsves vpvktkhwkw ttslnftlpe
      781 nhlmkfpnld kstyasrfei gksislvkly qytgidpvtg lytfydtnqd gkintadrtv
      841 skeikeywyg glqnsiqykn wsfdlllqfv sqsqynvksm ygnignmsnm paiftdywtp
      901 gnpdaefqkp sagyntaaat asslfllsda tvsdsftvrv knatlsyrip sdsngklkar
      961 lfisgqnlfv fssykegnpe fmaagytspl rvvsfglslt y
//
LOCUS       WP_120231640             949 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. AG363].
ACCESSION   WP_120231640
VERSION     WP_120231640.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. AG363
  ORGANISM  Chryseobacterium sp. AG363
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Chryseobacterium sp. AG363"
                     /db_xref="taxon:2183997"
     Protein         1..949
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104365
     Region          32..948
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqsnlkysg liavlyfgmn vnaqvtqdsa kvqkidevvm igygsrkkvd nttaissisa
       61 eevtrtkvln asqaiqgkaa gvqviasdap gstptvmirg lgtvlggrtp lyvidgmyad
      121 ninninsndi ltydvlkdaa alaiygnraa ngviiittks grgklsvsyd glvgfrtplk
      181 tikmangsef anynnagkas tylnpnqpyn tdwfkeitrt giynqhnvsi sgsseaakyf
      241 lslsnydeqs ilkgtnynrt tvrtnnefri tkgirlaqtl satftndtpk sygaftnayk
      301 qsplvpvyyp ngkygqpiyn kttgnidyeg grfnnvgnpv mqlaydnqkg knfllqgglk
      361 ldidiykdlk ftsqfsgeyn nykyynfvns kafwldsdpm rvdsgydtsl pltrltnksq
      421 nyfnwvlnny ltytkkvgnh dieivagtea svangletlt inrknvpvsq dywnldgvdy
      481 ygnlfsdntt kaiesikgnr nttisyfgrl qykfmnryll sgtfrrdgss qfaeghrwgt
      541 fpsfgagwii seesfmqdgf fdllklrggw gklgnqkvpl nylplssgat ynygfgtspv
      601 sngitvnqgy dpslgwevte etslgldfai lnkrlsgsfd vynrktnnli lgvvpylatg
      661 isevnfshmg svvnkgaeis lnwadkvged ftysiganys ynknklasid lskpvsqlvg
      721 gnlgngqdtk ifnakavgya lgsfylwead gydangnlkf kdlngngvtg sadpgdrrff
      781 gsyipkstlg vnfsmsyknw dfalsgygaf gfkvyngkka qrnggenvea svandfwtpt
      841 ntnaanpvnp anipiastfy lesgdyfrin nisvgytfkn vtdymksikl yvsainpivf
      901 qkysgyssel sgynpadpta egdpikragv eldayptlrs fvfgvnlnf
//
LOCUS       WP_120231737             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. AG363].
ACCESSION   WP_120231737
VERSION     WP_120231737.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. AG363
  ORGANISM  Chryseobacterium sp. AG363
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Chryseobacterium sp. AG363"
                     /db_xref="taxon:2183997"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108793
     Region          36..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkqcklgv lalllfaeyg faqskdslsg etsikevvvv afgkqkkeei tgsvqslkak
       61 dlsnlqngni lqgiggkvag vqvissgqpg sqptirmrgi gsinassdpl ivldgipysg
      121 nlnsiaasei esisfledas snalygsrga ngviivntkr gkskgvsiea dvktgvnfrs
      181 iedysvytsp qdyytayynr arigeiarlk qpgavpsgps phdvglsalt klgynvynvp
      241 fnqliskegs fnpdakllyq ddwkkllfrp alrreatvgi nangdqiksy tslnylddkg
      301 ylissgferf girsnvdyai tsklkltsal sytyskqdfg eaggfsnpfq farniapfyp
      361 vflrdnnyqr lydsygnaly dygdgqgpng atrsyavfen pvgnlqknks qtvsnvtnln
      421 lglnyeiikg ldftynfgay lennrnlqfg nteggtsssv ggtisqgsnf kytlnhqqll
      481 tyqkklgnhs fnllagheln kikdngfsgs kqqlllpdsq afdnavkitg lsgsgyeyav
      541 egyftrllyn ydgkyffnan irrdgssvfs pesrwgnfyg lglawniake dflkdnsvin
      601 slklkasygq qgndnillgg ssrdyyayqd iyginnfgnd kpvlslkkqg nkdlkwetsk
      661 nlnagfeisl lknrinlnad yferkvsdmi ytlplppsna gsyvkygnig dmtnrgvqan
      721 vnvdilrgde fqwsfyanat hyknkitrlp aeqrntglvs glfilteggd rytyflkefa
      781 gvnpengdal wyhttinptt qkeertvtnn ykeatdyntg ksaipkvygg fgtdfsfkrf
      841 nlsvnfayqf ggygyddiyr slfhsdsygs nystdldktw tpenptaalp rvdltatnqn
      901 gnstlyliks dyislqdvtl syqlpdgfaq qaglsglkiy vtgnnlylws krkgydpras
      961 ltgvsdsyry sllssvslgf klnf
//
LOCUS       WP_120232236            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. AG363].
ACCESSION   WP_120232236
VERSION     WP_120232236.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. AG363
  ORGANISM  Chryseobacterium sp. AG363
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Chryseobacterium sp. AG363"
                     /db_xref="taxon:2183997"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124065
     Region          22..1108
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlillpl laaniamaqq kktitgkied gntsqvitga sikietqsvs tktelegiie
       61 svsvgtvtdk dgkfileipt dtktvlvsyp gyesrviqln egqtnytirl tseisdknki
      121 qeviitgyqk iekrkqtsav stvkmdnisq agvasvdqml agqiagvavt petgapgspa
      181 kirirgtasl sgpqdplwvi dglplegndv pnftdkdnid qlqnfsiagl npndiediti
      241 lkdaaataiy garaangvis ittkkgkkgs lklnfsadtf vtsrpdfdkl nllnasekvd
      301 lelmlakrad ltyradkgev mriltqnnql dafrnggfda lnsftrqqin glrnnntdwg
      361 kllyrnaink qyglsvsggs dradyyfslg yydeegttig tgfkrynltl knnyklsdkl
      421 nagisifgtq sertsfvtda dasinpvnys rnanpymkpf nadgsynydr dmdgfedryi
      481 pfnfleeren tnyslknnsl kaildleyka skslrftsql glqydankte kfaaentyft
      541 rkmkentryy kdgkynyflp agavkqnwdn dffqynwklq aaystkinkh eidlmagtei
      601 rktednttit rafgydpatr rataivfpns sfaadkryet yreaapiena yasmfatasy
      661 tydqkytffg svrydgtnlf gvnkkykylp iwavsgswlv tkedfmknis avsnlrlras
      721 yglqgnidrn tspffigeyn datilpggke siinvlsppn dklrwekttn tnlgldlglf
      781 nnrvsltadv ysrkgtdmis mketpletgf eytmmnwgsl tnkgfelais trnvnhdnfk
      841 wtttinfahn ksrvlseqpr dnallpsreg lpvnavfalk tagmdeqgnp lfwkgdqkis
      901 aaeffklydv yadflpgqlv dtklsnaelr slftyvgdrd pkftggiint fkvsnfdlti
      961 satfnlkqtv mrtpsyrgme ldrgrnytrd iyeaggslpg itspdmeanp dgwmankwft
     1021 gnrsnaysll dvwakeisyi rissirlgyt lpkeftnpmg itslrlsveg rnlfvfsngy
     1081 kgyfdpetyg niyaqpitks vtvgfnvsf
//
LOCUS       WP_120232472             988 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Chryseobacterium].
ACCESSION   WP_120232472
VERSION     WP_120232472.1
KEYWORDS    RefSeq.
SOURCE      unclassified Chryseobacterium
  ORGANISM  unclassified Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="unclassified Chryseobacterium"
                     /db_xref="taxon:2593645"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107585
     Region          31..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkavipvlf vfsltanaqe kktadttktt sieevvvtsl gikrqarslt yssqqiggde
       61 ltevktpnll nsingkvsnv qinrtngvgs svrvvmrgdk svnsaqplyv idgipiingt
      121 gksadigqys nmpdpgdvls sinpddiesi nflkgasasa lygsaggnga ilittkkgra
      181 gkssitysss ltvdrayslp klqhsylsyd psvsgsqpgq sveswgakgs skdylkdflq
      241 tgttwvnsls fqsgnersts yfsignttnk gvvpmsyfdq ynvsfrnssk flddkltlda
      301 nfigslqesk nrqtpgasfs pltslywlpr gvdfdqygpd nytylnkerf lpaqnwwevn
      361 pdgsfkgnpp tqnpywilnr npvtvsnknt ygalslsyqi npwltarvrg nyswnisdsq
      421 rdiaafsapt llavkeging rilkntyens stygdvllig spkisesfsl dftlggsint
      481 trnkigqidn ayltnpnlft vsnlewgkkr spgdgyhniy tnmkkqvqsv fasatvgykn
      541 mfyvdmtfrn dwdsslaltg rtgfdyesvg anavlssvfk lpevisfwkv rgsyatvglg
      601 lptnisnami eynkgytvgv dagtlvfpks sfitdpkykd lfpkpefnkt fevgtelrmf
      661 snklsfdity ynsntsnqll etkidsyfgg iapgsyyina gkirntgfes slsykvfsse
      721 kfgwtttlna sankntivel fppslpisen qlfsltggge ytklklggsf gdlygikfkr
      781 ddqgrilvne kgiplaegtp sylgnpnpkf imgfnnsfni gklgisflid gkfggkvlsl
      841 tekandiygv sqstadarda ggvsipnavy apgtpnagqa ytgltnakdy ykavgttegf
      901 gkgideayly sattirlrqa sisytfdiqs kymrnatvsl vgtnlfffyk kapfdpeqvs
      961 gntpggvgvd sfglpvtrsi glslkanf
//
LOCUS       WP_120232664            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Chryseobacterium].
ACCESSION   WP_120232664
VERSION     WP_120232664.1
KEYWORDS    RefSeq.
SOURCE      unclassified Chryseobacterium
  ORGANISM  unclassified Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="unclassified Chryseobacterium"
                     /db_xref="taxon:2593645"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118195
     Region          22..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlatfav fllplyfsaq einisgnvks engssvsgvn itdkntgkta ttdengnfti
       61 sanpkdilef fapdfsvytv evsskkqysv vlkkqnekqi egvvitalgi akkkekigys
      121 tqevgtkqfe tittpsignl fsgqvaglnv snptgmqqap qftlrgnsnl vfvidgvive
      181 kevfqnldpn nieninvlkg atasalygsr grygavlitt knakkkgfsv efsqntmita
      241 gftnlpktqt eygngshgky efwdgadggv ndgdmiwgpk fvpglqiaqw nspirdkvtg
      301 qvvpwygavt gtqyddksry ervpidwkyh dnlstflkpa vinnnnfais yrsnkdvyrf
      361 sgnfmnyddr vpnsylqkyg infssenhlg dkltfdtkfn fnqaftpnip nydynpsghm
      421 ytiliwmggd vdgkalknhm wipgkegraq anwnyawynn pwfgaeyykn qnrtniinaq
      481 tgleykatkd lsvkgkislv enhskteils pysyfnydap rsggyilkdn ktwnlnydvl
      541 atykkkisen fdftinaggs afyyknnnne rstdglkipe vytfensiga lknytylkek
      601 liysaystid iglynaffin vsgrndwsst lpkanrsyfy psasisavis nlvkmpesin
      661 mlklsaswak vaydfqpysi rnyylnnggi tfngnptyyy pttlnvensl kpeqtksyel
      721 glsagflnnr itldatyfrt ldynnilqfp aaessgftsq yvngneyttk gfevslglvp
      781 vktsdfswkt linwstyeqk ltsiydnmpn ykniklgerm dsyydytwqk spdgkvilda
      841 ntgmptrann psnlghfnpd wtfgfnntfk ykkftlnigi dgsiggvmrs qvvekmwwgg
      901 khpnsvayrd leyanpgtyy fvpdgvnynp atgtytphtk aisyqdwaqn ypyrarvtqd
      961 eseefanvfd rtfvklrsvv leydfsslln prgmvkgfta nisaynlamw kksknlysdp
     1021 dfqtktdndi qdpssrwfgi gfnlkf
//
LOCUS       WP_120232542             959 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. AG363].
ACCESSION   WP_120232542
VERSION     WP_120232542.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. AG363
  ORGANISM  Chryseobacterium sp. AG363
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Chryseobacterium sp. AG363"
                     /db_xref="taxon:2183997"
     Protein         1..959
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106528
     Region          35..957
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlsa galffmgavt yaqttkkdtt qtkqidevvv qgyrtvskkt avgasqqika
       61 etiesraqsn vlnavqgqla gvnisagsgq pgakptviir gvgtlsastd plyvidgfps
      121 nsdafrnlns ydietfevlk dpaalaeygn rgsngvivit tkrgsstggk lsfhynsqtg
      181 vnflqknkyn iansrelltl ekrlntgkgv dmtdqeindf nintdwldyf ynpgiftahn
      241 lsvesgnerv rtfttagyln qdgtlagtsl qrftlrnnis gksenkkfdy figmaavfsk
      301 nsdqpsegda eainqnpilg aqmgvpylsp smysngyqlf qdyassggsl lytplflidk
      361 vetfyrrfnd yrfdvnsels ykilpglvar trtnaqliyq rlvsvqrpes fnsllfsptq
      421 gvpsylggay ngtesinnny nfsfnqlaql gytksfgkht fnltgnmeyn myqfqqsiqt
      481 qrglnpknyv pdtgqgyvtd taandwyvpt isnvksrldl lsyfgsfdyd fnktygivas
      541 irrdgtsrfg ddrkwgtfws vggrwnidse sfmdnvsfvd vlklrgsygv ignqrvvagt
      601 iyqglnppky ydvytpitta ggsynsgfgm giafgdpllq westklynvg idfeffnrrl
      661 tgsfdkygkk tenmyytdpm apvlgtgaid hntnmflynr gyelslnyta lktedltlni
      721 rangsinnqe lggiagggyi dsgtqfivrq qngmlpfmpy vyhylgvnpa ngellfedan
      781 gnptenptfa drktrkynyl pkyqggfgfd vnykgfyast tftyvagier fdgdwstmya
      841 gdnigqfnvs rdlldswtpt ntgaslpslt aanrsldass drflvdasyl rlrnaqigyk
      901 ipkrmldgtf lssasiyvqg enlatwtkwr gydaesnrns daanyptakt ftigfdfrf
//
LOCUS       WP_120232848             983 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Chryseobacterium].
ACCESSION   WP_120232848
VERSION     WP_120232848.1
KEYWORDS    RefSeq.
SOURCE      unclassified Chryseobacterium
  ORGANISM  unclassified Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="unclassified Chryseobacterium"
                     /db_xref="taxon:2593645"
     Protein         1..983
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108671
     Region          33..980
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkitmsllv vvlsssvaiv naqqkkndta tqtkeiegvv vtalgikrek kslgystqqi
       61 kadaitegvn tgnianqlvg kaaglnistt tnfggsaniv irgnksivsn nqalivvdgv
      121 pldnrnnysd rydygnnlsd inqadiesin vlkgaaasal ygeragngvl littkkgrsk
      181 qgrvgvtlss eiqvgtidkt tfakyqdkyg agygqyfded dagnlyapfy ddasigmpfd
      241 pklmvyqwds ydpnspnfgk ayswtaakht pasffetatn yvntvslesg sndsnilvny
      301 tnflsngvlp nseqkkntis akfnhkfndk fdvtaytslt iqntkgrnst gygdniitgf
      361 rqwwqnnvdv yslrdayrns grnitwnrts andgnpkywn npyfdryeny qtddrtrffg
      421 yvllnykvnp nltitgrass dsydqknqtr kqlgsmpesf glsgksvssg yelenlrsse
      481 lnfdlygayn kkfenelsln gllgasyrrn smegvrnste gglilpnvwa lnntaeaplp
      541 tqedlaksvt mgayiqaalg ykdtyfiegs yrvdkssnlg qnnnvygyps vsasiilsnl
      601 inqdwlsflk lrgnfakvgk stdnyrlqdq yrilgifgki pmvsnstvkn nrdlkpessn
      661 efevgveanf fknrigfdva yydtrttdqi vradvststg yaskwinage iqnkgieval
      721 natpfksdnf swdininwsk nkssvlklte gldnlllqqv qgevtynayv gqpfgiikgt
      781 dyvyvngqpv vedgvyarke dqvigninpd wiggirntft ykgvslsfli dgqkggdifs
      841 tdlyygmgtg iypetafpdr nnivlagvnp ngtpnttpip iadtgelmgg isvmpakafv
      901 ydasfiklre asltfnlpkk wydrtfindm kfsiigrnlw iihknlpyad pesglragll
      961 srgysvgamp tvrtfgfnft akf
//
LOCUS       WP_120232947             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. AG363].
ACCESSION   WP_120232947
VERSION     WP_120232947.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. AG363
  ORGANISM  Chryseobacterium sp. AG363
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Chryseobacterium sp. AG363"
                     /db_xref="taxon:2183997"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109536
     Region          35..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrketqkllv lsllglvsvn laaqqkakkd tikgldevvv talgikrhdr algyvaekvd
       61 aktfeetqnn nwaqsmegkv aglkiqtaga gplgtsritl rgeksimmdh nyalivvdgv
      121 plgnsttgsg taaygagsgg dvpidlgngl nsinpddies vtvlkgasaa alygsraang
      181 almittksgk tkngklrvtf nssssfdsvl kwpdwqyeyg qgtlatntag nfyysyglsp
      241 dgpntggtss afgpkfagqy yfqydpnvmg qskerqlwrp yennikgfwr tgstysnsis
      301 vessnektsf rssltylnne wmmpntgfdr fnfalsfahq ltqklkistk fayntttsdn
      361 lpatgynnqs isyfmifqnp nvdlewykpi wkpgqeqvdq ihpfssyidn pymiayemln
      421 gvrkktitgn itadyqfnkn fsvmlrsgie ilnekrttkr pwssanylkg fyreqfiknq
      481 eynndllfsy kadwnkfsis asaggsiryn eyllndyqai glktageysl tnalsipvky
      541 paprdkhvds vyglltlgyd nkifvditgr ndwsstlpkq nrsffypsvs tsfilsdifn
      601 lksnnlnlwk lraswakvgi dsdpylldny ytasnitgsv vapttfnnps lkpekntnie
      661 agmdfslfkn rlnlnltayq nfsenqiipv smptesgysk riinagkirn rglelsadil
      721 aikgkdfswk vggnwstnen rvmtlpegfd givsnvgdvv fykmevggsl gdmygfkllr
      781 tpdekviygd nglparpadi ekvgnafpkw raglqndfri knftisfsfd gqyggiaysq
      841 shhkmseqgk lkstlpgrdn pggmivgdgv vqnpdgsfst ntkgvlvssy ygdyyrranv
      901 etnsfstdfi klrdariays fpketiqsig lddltiaifg knlwmwtkfp mfdpevatld
      961 natitpgvem gqlpaartvg fqlnlkf
//
LOCUS       WP_120233057             996 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. AG363].
ACCESSION   WP_120233057
VERSION     WP_120233057.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. AG363
  ORGANISM  Chryseobacterium sp. AG363
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Chryseobacterium sp. AG363"
                     /db_xref="taxon:2183997"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110311
     Region          29..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknsyyhigg iffglmftav sitvkaqtrt isgtvtssgk plqgviisqe gsdqvtmtgn
       61 ngtytlqvsa entillfrhp dyseekftlt nqkvvnisle qkvkgieevi lnagyykvkd
      121 kertgsiakv sakdienqpv tnflstiqgr magvnitqns gvpgggysiq irgrnslrty
      181 anseidgsqp lyivdgvpvg sgmtavygan ilsdanlnpl snispndies ievlkdadat
      241 aiygsrgang vvlvttkrak kgslelsvnt syalsnslsn ltmmnteqyl gmrrqayand
      301 gisvypatay dingtwdqnr ytdwfrtllg ntsvtsnvql slsgggerts flvsyghneq
      361 ttvfakdfry ktntllgnls hrsadnrlnf tmstlfskle hnvisldntg salflapnap
      421 alydsqgnin wqnntfdnpl aaynstysnn nvqfmnnfta gyeflknvqi rlnggisyqt
      481 fdelslqpst iynpslgigp ansralqsnk srlsytlepq lnwtfkkgrh qvdvlaggty
      541 qadlntqgai qgygftsnaf ieniaaattk lisdqvktey kytavfgrln yqfdrryiin
      601 itgrrdgssr fginrkfanf gavgaawlfs nesfmkelsw lsfgklrgsy gssgtdnign
      661 yqyndtfits tlgynnvtgl vpsklfnpnf swektvklea aleiglfkdr lnvtashyrn
      721 rssnqlvgyq lpsvtgftsv lanldatirn tgwefeitgr pltgtfkwea sanlsiprnk
      781 llsfpglegs tysnsyaigq pvnilklyhl eginpqngqy iftdyngdgk isspddrqvi
      841 knigveffgg wsnnfsyknw slsllvqfvk qqsrnfnyqm sspglmrnlp vevlnvwspn
      901 npnglympyh ataspqhslf qmsdatvsdg sfirlkniql syriplqgkl ikeakiyfqg
      961 qnlytwtryf gldpefsslg flpplktysf gmqinf
//
LOCUS       WP_120233144             912 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. AG363].
ACCESSION   WP_120233144
VERSION     WP_120233144.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. AG363
  ORGANISM  Chryseobacterium sp. AG363
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 912)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 912)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 912)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Chryseobacterium sp. AG363"
                     /db_xref="taxon:2183997"
     Protein         1..912
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=102376
     Region          31..911
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqkkltts vcfflmtgfi aaqttkktds leekkiddiv iigykaqkrs sltaavsvis
       61 dkklqdsntp svsgllqgka agvqilpggg sagsvatvki rgtstingps salwvvdgvv
      121 mpyapnldpn qiesinilkd aastalygsk aangivqvft ksgnsgkgil saslnnsfnv
      181 fnngrfklmn gtqlydyfts lkgapeipkt lrndgynwlk ggtqtgvvqn ytidfrggsd
      241 hsktyisgny ynetgtikgd eynrlsfrin heqtikpwli vkpkvslsyt tgkdtqasly
      301 qmylnmpwdn prdangnlir vdedyadwyg rdkssylydl qwnygksnql dlignldaev
      361 rftdylkfit tnnvtyknyd dmyytdprsi sgtsnkgelt enyqkdiskf fnqmlrfdkd
      421 fgnhninala ayeytdrfyk ssragvygvv pgtdifntga stgqkptgrk fdraynaflf
      481 nteyvydkky fiqgslrses ssafgannrn glfyaysvgw nihkenffki kpvnewklra
      541 srglvgntps pdygwqdlyr ltekydgqig atwyqlgnpa ltwesiyqnn igtdikvfnn
      601 rltlnidyfn nktknllmlv plpsltgvdr qyvnigdvrn kgwefnvnys iirsedinwd
      661 lgfnistykn nvlstrnngt qvldnyhvai qgydvnsfym rkwlgvnpen geaqweiinp
      721 dgsrsatsky nlatvqvvga atpdyygsvs tnlniknfyl aanlyfsqgg qvynsyrelf
      781 dsdgaypyyn qmvlkdgwtr wekpgdiath paavynnnsl tnkpssryle dasfvklrsl
      841 rigynlpasl tekmkiksan iyimgenlft itkfsgvdpe vgnadnqsvy sgnagaiypi
      901 prrfslglnf sf
//
LOCUS       WP_120238622            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Marinifilum
            flexuosum].
ACCESSION   WP_120238622
VERSION     WP_120238622.1
KEYWORDS    RefSeq.
SOURCE      Marinifilum flexuosum
  ORGANISM  Marinifilum flexuosum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Marinifilum flexuosum"
                     /db_xref="taxon:1117708"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112959
     Region          24..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslvstli lmfiglqgll aqsrevsgiv tsaedglsip gvsvivkgtt igtstdfdgk
       61 ysinvpeges ilvfsfvgmt aqelavkgst mnvvmqpasv dvdevmvvay gtakkesftg
      121 sasvvkkddi vkvsggigkv iqgkvagvtv mggdirirgf gsfsassspl yvvdgvvgap
      181 kpndedienf tvlkdaasta lygsrgangv iiitskkgkk dkkptfevky qhsvekmiep
      241 ewelmnagey yqhqfkgmvn yvgesrayty fnyymnnknp ynmaepfnld gslkegakll
      301 ydtnwkdeal enaskdeiyv aasggsensn yhwsarmyky dgfvrtsksk gantrfnyti
      361 dlrdnlkvnv nstisyyegs gtyttkanen nhlylsyvls paapmyqlnq idngdgthsy
      421 eyvldkqgnr vydysnpnyk nynpiglmea dfddnygfsa ffapsityev idgltlkgql
      481 sgrlntrrgd sfqnpyygsg stenglstke tyhtmdwtmh tsanykfevg ddhsfdvivg
      541 yeaadydyqd fyatkngysl gdistelstg nspryagsst tevglisyls nlnydfrdky
      601 ymsasfrrdg sskfgednkw gnfwsvgfsw riseenflsa dwitnlklrt sygvlgtndi
      661 gnykfgdyys lganyggitg vshtnlpnaq lgweesdnfs vgvdfdlfds klsgtieyfn
      721 kntdgllynv plptttgfps vlmnigemqn sgfemelsgk ilsgefnwna dltmtyikne
      781 ikslpvdqvi qgtkrwiagd sryeyyirew agvdpedgra qwymdqenad gtvekvktks
      841 yskatrynmg qstpkfffgl nnnlsykgfd fsvqtvaafg hkiydgqyqt fmhdgsgkat
      901 nlakdalnsw tpentntdip kyrwanntss nstssrwlvd gdfvkiknit lgytvperfl
      961 dkmflnyarv fmtvdnvhsf sdyksgdpei slagvsngys fnpattyrmg inikf
//
LOCUS       WP_120239032            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Marinifilum
            flexuosum].
ACCESSION   WP_120239032
VERSION     WP_120239032.1
KEYWORDS    RefSeq.
SOURCE      Marinifilum flexuosum
  ORGANISM  Marinifilum flexuosum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Marinifilum flexuosum"
                     /db_xref="taxon:1117708"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118503
     Region          24..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkmiglfvc lvlmglqivn aqskqvtgtv tnaedglgmp gvsvvikgtt vgsstdidgk
       61 ytieaspndi lmfsfvgmit qeitvgdktv idvvlqtesi gvdevvvtal gitrekkalg
      121 ysvtdlggde vskvkqqnlv nslsgkvagv qirqsnnfgg stnmvirgns sifggnqplf
      181 vvdgvpisgs tfnsaaqrgg stgydygnal sdinpddian msvlkgaaat aiygsrgang
      241 vvmittkkgk kkkglsisin sgitigkidk etfaeyqdey gagygpyygs tgyfedldvn
      301 gdgtddlvvp tyddasygak fsgqqvyhwd sfvpesanfg kayeykaaan tpvdffetev
      361 gytnnveltg gnedgtfrls ytnfhtngil pnsklnrntv sfngdyninp klkvgvsanv
      421 slqdtkgrns tgysdnlmsq mrqwwqvnvd vkaqediykq tkknyswnhq estgdgvlnp
      481 lywdnpywtr fenyqtdsrd riygnafftf dafdwlditg rvsldhytsl reerravgsv
      541 aapfgvlrtd eksgyqryei gftevnydfm anyntslsdd itlagvvgis irdestdryq
      601 astlgglvvp nlyslsnsvn tpsapietle ekrvygmyaq atfsykdily ldltdridks
      661 salpkdenty nyysiaasyl fsthtelpwl nlgklrmsya tvgndtspln vydtyvkndn
      721 fgkytlfsyp ntknnielkp eytkefevgl etkmfnnrag idvsyytket edmlipvevs
      781 katgysfnwv naatvenngi evalygnpik teafswdinv nwarnrnkvl dlyndveniv
      841 insyqggisi natkgqplgt irgtgflfdd ngnkvvnssg yyisqsdqii gdqnpdwtgg
      901 isntfsykgl tlnflidiqk ggdvysldmh ygqgtgvlkh taglnelgnp krdpvseggg
      961 ilnvgvtedg spnttrarad yyggayywgn ssrnpgaltv ydasfvklre laltynlpkn
     1021 lisgfaqnvs lslvgrnlwi ihknvpyadp esglssglaq gylsgsyptv rswgfnvkvd
     1081 f
//
LOCUS       WP_120239488            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Marinifilum
            flexuosum].
ACCESSION   WP_120239488
VERSION     WP_120239488.1
KEYWORDS    RefSeq.
SOURCE      Marinifilum flexuosum
  ORGANISM  Marinifilum flexuosum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Marinifilum flexuosum"
                     /db_xref="taxon:1117708"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115238
     Region          57..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkcylsnlh siltnplsfg rkisslallv avlsspfaan anvnslsedn savavqkivt
       61 gtvteesgvs lpgvsvvvkg ttvgtvtdid gkfqiavdes svlvfsfvgm ttqeitvgsq
      121 svidvvmaad alqvdevvvt algikrekka lgyavqdvka edltkagdgd lvsslqgkva
      181 gvqinqtggg vggssridir gvsslvgnne plwivdgvpf dngnsndgsv wggtsragga
      241 fdlnpddies vsvlkganaa alygerggng vilvttkkgk rnkglgisys gsmtlseaay
      301 mldlqdkfgq gingeyytte taswgpemkg qqveswtgem ipfedqgnll kdftrtgiah
      361 khnvsfsggn ddgsfrmslg kdiingiydn hkvekttfdl radydinswl nvesklsffl
      421 tegeqrpevg nysyvsyfnt mprnirpsdl kpgydiiagk hvekiysdas pgnrnpyflq
      481 eqyvnndkkn rtfgfiaanv kltsdlkakf kygmdffqfs sldgyqyadn inpnrpdynp
      541 tqsnfkeeny efllsynkdl nedftislnv gantmkrhfk qlrsfsgkls seddfylgag
      601 snikavesit esevrsmygf gqvayknmif ldftarndws stltsadtef dnsyfypsvs
      661 lsallsemfe lpkfvsyakv rgslaqvgka adpyqtsqty kiesgdfdls kgkvpdvlvn
      721 kdlkpeists weigtdirlf snrigldfty yqedtknqil klstdqttgy pyrlinagli
      781 rnkgvevmlt tvpvktedfk ltvgfnfakn kgtleelyed mpvykfddne gfvglpgkrl
      841 giirgskydr nengdiivdn nglmklsnee hnilgnvqad wtgainlnae ykgfylsalv
      901 siqqggdils tseqaavsag takrtlennr malfvdgvtv dggannvmis aqdywrkvaq
      961 adeefiydas hiklkelaig ynlpktilnk ipnnpiqsak vsligrnlfy fhkntpgtvp
     1021 dasaysssfv aqaydfapvp svrtygfsln lgf
//
LOCUS       WP_120240544            1181 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Marinifilum
            flexuosum].
ACCESSION   WP_120240544
VERSION     WP_120240544.1
KEYWORDS    RefSeq.
SOURCE      Marinifilum flexuosum
  ORGANISM  Marinifilum flexuosum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1181)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Marinifilum flexuosum"
                     /db_xref="taxon:1117708"
     Protein         1..1181
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129469
     Region          69..120
                     /region_name="STN"
                     /note="Secretin and TonB N terminus short domain;
                     smart00965"
                     /db_xref="CDD:198033"
     Region          133..1180
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknhdfghc ssnawrktlr vmklttilff laiftvaaeg ysqgtrismk medaslkevf
       61 relkslsdyt fvysegmvad vkideidlqe vsvedaltec legtdleyyi ennvvvirkk
      121 aiefkqpieq ekkiingkvt ddsgspipga siyikglqkp lgtitnidge fsldlrgmee
      181 atlivsfigm etqeivvtsq eyinitllss tegldevvvv gygtqkrsev ssaistvsse
      241 kledniasna sfdralgglv kgvqvvqnag apgsgvdini rgitspfggs dnnplfvidg
      301 vpfqtnpvgl atvsnpllsi npndiesidv lkdasataiy gsrgangvim iktkkgrkge
      361 dlkvslsast tfgepintld yanttewkaf andlfnesfk afekgqinss altrfgfman
      421 fdtepdplpw dptntkivgy nslkedyfgt antnwadeiy rnkaltqqyn atltggtekt
      481 nmllslsytd qeglikeenf eqfnvrmgid anvnditsvg anitigsssn esgyasasti
      541 nansviptln arpditpykq dgtfnryqsv difgqstsvp npvallssqd nnstdftalg
      601 nfyvevrpik dlklkselsa srfgnrtrnf dpaksltgvi tddgfgtiti pkstlfdaht
      661 vntnkilnlt atygrtfndh svsgmigysw drskavstns fyqgfpddkv ltdpksaeev
      721 vktnsseiei gmnsifarlt ysydsryyft anfrtdksvr fapskrrayf psasaswais
      781 neeflsssev innlrlrtgw grtgsnnipn faylqffgin ngagdvvynq nqavglngtl
      841 pnpeikwelt eevnlgvdfg lfnnrlrgsv dvynrkskda lmpslyples gatsftsnfa
      901 ditnkgfefe vggdiirnen lvwsasfnis knknsldkfa atalndntrd rfevgreinf
      961 ingyvtegii qnqaeldaln agapdntyqe agtgvgdykf adlnndgevt sedqtylgsa
     1021 qtdffggfnt nvaykgfels ayfnfsagge svvpnslfpa pdknierrfl drwtenntna
     1081 lyprailsdp nqnsrmssah vystsyirlk nvqlkynipa dvlskigvek ghvfvagnnl
     1141 wtktdfpgid pelvggfssg gntsnpypla ktwsvgvnln f
//
LOCUS       WP_120241158            1108 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Marinifilum
            flexuosum].
ACCESSION   WP_120241158
VERSION     WP_120241158.1
KEYWORDS    RefSeq.
SOURCE      Marinifilum flexuosum
  ORGANISM  Marinifilum flexuosum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Marinifilum flexuosum"
                     /db_xref="taxon:1117708"
     Protein         1..1108
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123749
     Region          24..1107
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrmltllli llpafvwaqe mklikgkvls esdgdvliga svyidkatig aetgmkgiie
       61 nislgtitdf dgnfslevpk qlntiscsfl gfetqvvdik gksfvtiklg estselgevi
      121 vtgyqkiekr kvtsavvkvn adniqqagvv svdhmlsgql agvtavtqng apgapakiri
      181 rgtvslsgsq dplwvvdgmp legndvpdfs dkdnidqlyn ssiagfnpsd iaditilkda
      241 aataiygara angvivvttk ngkqgsmrvs fssnttftqr pdlsqlnlln snqkvdlelg
      301 laartdysyr ngnggvaril dqyndrqnyl dngfsgisnn aqadinalra intnwedlly
      361 qtavnqdqsl svsggnefat yyfsagyhge kgttigtsld rinltskirl klnekmnfga
      421 avflsqrktk gyltgsdlft npayysrtvn pyqkvfnadg syaydrettg algtpldfni
      481 ieerrntsne ltsrninaif dfdykiskgv kystqlgiqt edrrteqiat kdsyigrrtk
      541 hnsrytgknd kgedvtlydi negfikvwda dffqynlkni ievnksined hefdlmlgne
      601 iranetttiy sanyafdrss nssvaidfhn adaakrfkgf nksfvkntfa sffstlsysy
      661 khkytlfgsi rydgsnlfgv dkkykyqplw alsgswnate eeflknvtwl nslkfrasyg
      721 lqgnvdksts tnlignkarv eilpgmveev lrvdnpqnpy lrwektrtyn agfdvaifkn
      781 airasvdfyh rkstdlinlr alplengfnf apinwaavtn kgfeigistr niynkdfewt
      841 tnfnisrnid kvdniqvrnd swfpsgvgrp vnalyvlktd gldengmpvf vkdgkkmnlq
      901 efagielkwg fwptptlspk efrelftyag sadpkfsggi intfkyknfd lsiacnfnlg
      961 qkvritppyn mteydralnt ttdilnawtp entnthlprl igastadgav svehqlysnn
     1021 dpinylkyld iwikemnylr ctnirlgysf pkhilekvnl ssarlsvear npfvisnnyd
     1081 gyfdpetfgn iyaqpiaksy siginvgf
//
LOCUS       WP_120252614             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Sphingobium].
ACCESSION   WP_120252614
VERSION     WP_120252614.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium
  ORGANISM  Sphingobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sphingobium"
                     /db_xref="taxon:165695"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54819
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreks lgearvaltp dsagqlqklg hiclvesgag qqagfadday raagvtvvad
       61 adalwaeadv ivkvrppeae etarltpgkt lisffypgqr geelaainat ganilamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigaatslg aitlafdvrp evaeqiesmg aqfvyldfse eqqdgaatgg yaapsspefr
      241 eaqlkkfrel aptvdivist alipgrdapv lwtkdmveam rpgsvivdla aerggncelt
      301 vtdqkivsan gvtiigytdf psrmaaqsss lyasnvrhml adltpgkdgv ivhdmeddvi
      361 rgatiafegq vsfpppppki kaiaaqkpkp kaeeltpeqk rakdiaafka qtrsqvtlli
      421 vaalllmgvg avapasfmah fivfvlacfv gfqviwnvsh alhtplmavt naisgivvvg
      481 avlqvgssst ivlvlatisi liasinivgg flvtrrmlam fqrs
//
LOCUS       WP_120257266            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120257266
VERSION     WP_120257266.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112269
     Region          36..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miaridskhl ffvgligcyf flftkgahaq pstrigkvis ttdqrpllgv tvlnlstqla
       61 ehtdqegnfs iraavgdrlk fsligyksae lpvtaagllt vglaqenfti devvvtalgi
      121 kretrgltya tqqlsgsavn dardnsgnim ssltgkvaga vittaasgpg asarvvlrgn
      181 ksisgnnnal ivvdgvpydn ssaqqatgtt ynygtsdgaa ninpddvesi nvlkgpsaaa
      241 lygsraanga ilittkqgks grytidyngs affdqvnllt efqntygrgn ggvsgtnige
      301 swgpkaqtyk nnvkdfyens atfnnsisty ggteklqgyv syannkiggi iqgnslkrns
      361 lnlrvnteli pklktdvkln yvnqqidnrp rlgdmgipve ayiiprdmdk nelmdyetid
      421 pntgqplrky wsgsaiydnp ywsinrtsvn evrdritalg satyqlrdwi simgrysfdk
      481 yidntdgsff astvsvgdvr kggkyyetna ryqesnldfl ingknplteh iaitynlgas
      541 tlrrkyssfq nmanglsipn efslkmattp eflaiagyer rlnsvyastq lsfdntifld
      601 mtarndwtst lkaphsyfyp svgmsaifne llqmpawvnf gkirasytqv gndadpyllr
      661 qlysfglgag ngfisrspik aipdlkpelt ksfeagldmk ffgnrlgfdl tlyksntvnq
      721 llflglpmas gysrqyinag dienrglelq lmatpikseh fswettlnfa sntnkiialh
      781 dktkranitd nnryatvvvn egekygdlyg yawkrdpqsg kfvvdgsglp vveanqklgn
      841 fnpkallgws nsfsykgftl ntlvdarigg eivsgtsayl aafgvadyts myregglvld
      901 avdangaant qaitaqqlwt rvsqngrdgw gefftydmtn vrlrelsity rldlkntsvf
      961 knaglsltgh nlffiyrgks kldipgigkt knpidpeaal gagnyqgvev glppsvrtfg
     1021 lnlkltf
//
LOCUS       WP_120257154            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120257154
VERSION     WP_120257154.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124421
     Region          55..1106
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkqskslta lldkvvnipc iqitlfvilf llismfslsa qtprkdsgad gllsisgtiv
       61 savdgkpiqg vsirvegekg rassnkdgsf slrvanpngt vsfshvgfkr letsytagvs
      121 msvkliplen qleevevvst gyqkipkera tgsfefvdnk llnrkvstdi lsrledvvpg
      181 isreksadrg klpfinvrgv ssmrsyawpl ivvdgmpyqg dlnwvngtsy wgnfnninpn
      241 diesitvlkd aaassiwgaq agngvivitt kkgsynqpvq vdvntnlsie grpdlyalpq
      301 msskdyieae kylfdkgayd fklgreftrm spvqrllfqq kqgllseaev eqelarlakv
      361 dsrdqflkyi yrqaskqqyy tqlsggsatv rynfsagydk nlekivnsgy drvnlksfaq
      421 mvpvknlslg mgltytssvf depngsgvqy gnliasnypy tlladgngna ltlpgtvnpf
      481 fldtlsaynk lldwqyrpld elgkttskvn mhdilmdfna eykfpfglda svlynyrnlq
      541 qdqelwksvs syamrdmins ftlwdespik ynlpmgdnmy lvntrgtmhq grfqlsynrt
      601 fsdkssisai agaeikdmkt itnstnywgy dkekltwqpv dlvsifpwan giigyskins
      661 lqesqnrtnr ytsyftniay tynnryiasg slrkdasnlf gvktndkgqp fwslglawlv
      721 snesffksqq vldflklrat ygyngnvnnt vsaypimdvs pypdyvtgnn ygtistppnp
      781 llrwenvgml nlgldfglkn nrltgsvefy vknstdliap aqidptsgft tlninsadmr
      841 gkgvdvslqs vnikgehfkw hsnlvfaynr tkvtksyisn dagryfvsgt riltpiegmd
      901 vyaalgydwk gldpengrpi glfngqeskd ynkiynstkv qdlismgsmq pvyfgsfrns
      961 fnyrswelsf nisyqlghkf rrqsfnafqf ydaesghkdy alrwqkagde lhtsvpsfvy
     1021 pvdnnesqfy kystaliepa sqvkwrdiqi gytvsglswk gikslrlygy vnnvatiwra
     1081 nkwgidpeyg qnypdpmsfs vginckf
//
LOCUS       WP_120257634            1126 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120257634
VERSION     WP_120257634.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1126)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1126)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1126)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1126
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1126
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126898
     Region          78..1125
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnfirtgig iacskqaaqy vnlinaqptc ienkayslre lliirtllvi atlfhmfsls
       61 aqtprkdsga ngptrhelkg qvlshddkpl qgvsirvdve nlqirsandg tfqllvnnqk
      121 gkikftyvgf ksqevrytar tdlvirlipe dnkleevevv stgyqkipke ratgsfefvd
      181 nkllnrkvst dfvsrledlv pgftsnktgn srgsylnvnv rglstlfsek fplividgvp
      241 ydisnpglgp giftninpnd ienvtvlkda aaasiwgaqs gngvivittk rgkfneqtkl
      301 sfnsnisika kpdlyyypqm sssdyidaqq yifdqgkyns wfknkfrnpq pvlwlmyark
      361 ngtlseadfn eqiallkaad lrddflkyiy rqavnqqyni qlqtgsdkvn tlfsvgydkn
      421 lndvvtssfk rlnlksntqi kpvknmildi glsytdskne nsyftvaynr makgvknypy
      481 mrladangnp iavdisglnp tfrdtiaggr lldysyvpld qlndsketqq irefftnina
      541 sysfdfglkl nllyayqrtm npteiwkgig tfqlrdeins faswnnnavt wnlpvgdflg
      601 ivnwdsynhq sratadyskk wnekheislf agmevrkneq kvtssqysgy dpetgafksv
      661 pygiqvpmln glfgtstitd vnvfkrfrnn fvsyfangay tyanryllsg sfrkdasnlf
      721 gvksndrgqp fwsvgaawil snepliangv fnflklrtty gyngnvnnsv saypimsiqs
      781 eahymtnqny gmimtppnpr lrwerigitn vgldfslrnn slsgsieyyv knakdliapd
      841 ridpstgfst lmvnsgnirt kgwdislnsi pvqqknwtws snlvfsyart kvlksyvqne
      901 ngkdfissaq sgtmtpiegm dlysqlgykw agldpgtgep rayingeisk dytailglnv
      961 rdlenygstv plytggwrnn vryktvelsw nisyqlghkf lrnsfdnslf lnsdightdy
     1021 alrwqksgde lhtdvpafky padlgsqvym rssallengg qiklrdiqls vslpslsrfk
     1081 vhnakiygyi qnvgtiwran kfgidteygf nipdpmmsal glsfnf
//
LOCUS       WP_120258139            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120258139
VERSION     WP_120258139.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119009
     Region          25..1075
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrsiaila snilvcsaly aqtavkgkiv dqdgkpipgv svsikdgpgt qtgadggfsl
       61 tytngtvlni saigykpkqv qinnqtvvnv tlesmmenld evvvtalgit rekkslgyat
      121 qevnakeltd agqhsltgal agkvagvqvn qfggavgssa risirgntsl qsdqqplvvi
      181 dgipvtnnaq rtgdntysgv dygsglndin pddiesinvl kggaaalygm ragtgvimit
      241 tksgkraeng vqisydgnfs idraanlpky qnlygqgsrg deysyktngg glsyqdyvlk
      301 nsfsyvdgtg sngvndgide swgprmdmgl lipqfnspvv ngvrqatpwn shknnvkeff
      361 qtgfsqnhnl sllsksdrss trasisfrdq rgtvpntdqk kytaqlnndy kisdkvsydi
      421 manftrtesn nlvtqgydsa npmngliwfg rqvdmqdlkk nwdqrdaqgn ytyynwnsay
      481 hmnpfytmhe srnalkmnri fgktslfyqp fdflkfegrv gldyynthmf ettyynydnk
      541 dgkfneikns nsdfnadfia nfnkqfgdls lsgivganyr dyqfetntlg akglnvlgvy
      601 tiankigday tvmdhakgrs nsiyaqanlg wkdqlyldlt arndwsstlk ksffypsasl
      661 swlptttfeg lksdylnfwk lrfnvigvgn atrpyqngny yyaqtdaynn lsqmyksmty
      721 aieglepeai tsyeigtelg mfkdrlhldl tyyqkinknq llpvptsnvv gfsniflnag
      781 eirskgveiq lrgdilrnen glnwtttvnf skdknkvvel ypqldlndlr lgwtwgisnm
      841 asigqpwgtl vgpgydrved gpmkgaikva anglidkpls aqvlgnvvpd flasmrndft
      901 ikdfrfgfml dfrkggdiws qtmshgyttg iaeitaadgi reraivagkd vmknerfamk
      961 vgdnwventi etsaqswyel ggvaemyvfd gsflklreay isynlpkaly srikgikran
     1021 vsitgtnlal lwvhksntmr ldpesggvss dsrgvgfeqa svpnsrsigl klgftf
//
LOCUS       WP_120258593            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120258593
VERSION     WP_120258593.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117075
     Region          28..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkeilkmhlr llgivfmllq shhvfsqiki sgtvidsekr tplagatvvi vgaqgnsals
       61 svqtdavgkf aittnegssl kasmigyrti tvmgkqgivi emvptavtld etvvvgyttq
      121 kkgllagsva svkfkeadie ipttsvgnll agrmpglyvs tpsgipgaqp dirirtassw
      181 nasptlyvid gkvtidaaef nnlspneiee vsilkdaatt aaygaragag vvlvttkrgk
      241 agkvsinysv ntgrdvrgkn meltsimewg qiqnriwgea ggpantpwte takayfkdrd
      301 fgggkgygfd klrdvyvnps itthnlsasg gtdklqyfig asyvnqetfi kntnekkynv
      361 rtnitanltk nvsvfaglsl nnnkfnspeg dwsgdmfpkl llwqpympsf tasglpvdyf
      421 wisnksgeaq glsgynkseg lksvvnlslt ykmpflegls akvgyiktfn nsnqkiyshp
      481 ftyyqlaqie pvvwdlnniv gqrltyhtpg iqkmaawnqe dqtnlqlnfe rdfgqhhvna
      541 alvyerqers ydgidating fpiymtdqww astggsgivn gtatkrinna ygflptvgrk
      601 syigqfaydy adkyvatfay rydgsanfpk dkrwgffpsv saawvisken ffknvngies
      661 lkvrasvglt gndfvainps ggkddanakr wqyedkyvtg nsaifgetpt lnpgiqydvl
      721 pnanitweky lnknfgvdis flkhfnatae ywetrtydil striqstppt fsrplpsvny
      781 gemkangvdl svnyanrtgd lnyniglnft ygnswytird lnitydyqnl igngrssnmi
      841 tgytvdkllr tqsdvdalla ahpgynfkgn apkpgqfayr dfngdntine nditvlnksn
      901 npkvvglnls adwkglsisa nfngslgykk sfnnlsdgve wnrmwrpwaa eswspentga
      961 wlpyrysand evrvvntsgs nfwladasfv rlkflniayn lpqswykkya nnirfyvsgs
     1021 nlfviskfnk kfydpemdrg tsfpivksfn agisltf
//
LOCUS       WP_120258762            1115 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120258762
VERSION     WP_120258762.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1115
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125694
     Region          64..1114
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mthfykggse lpigtqcscp qltksnclkl tilfwgivms smfslsaqtp rkdsgadgln
       61 nlilqgtvvs atngkslqgv sirvdaqkqr ttskedgsft lpvkhrngli kftyigyrpf
      121 eveystevsl tikmiplenq leevevvstg yqkipkerat gsfefvdnkl lnrkvstdfv
      181 srledvvpgl ssakmspdlr gnylninvrg estlspdkfp llvidgipye skfaayglan
      241 fnninpndie nvtvlkdaaa asiwgaragn gvivittkkg kfnektnidf nmnvsikdkp
      301 dlyyypqigt sdyidligdl fnrgrynatl gywgnnvepi vqrmkdhkdg eiseeqlkae
      361 ldqlrgydmr ddfrkyiyrk avnqqysvri naggdkvnas igvgydknln elvtssynrm
      421 nlqgnmqfrp iqnllinlgl tyseskknds fygvgynalg ngianapymr laddngnple
      481 vyipafnptf qdtvaggrll dwsykplkel ydsrseqinr eimsnlsvqy afpfglsiqg
      541 lyalqrninp ivewkgintf qqrfeinnfv twddkqvywn mpvgdyryel nassfshqgr
      601 ltadfnrswg kghqvsllag fdirevgqdm rasqyfgfdp edgtfqpmql greiqmmngl
      661 lgvnnlpdrn vfdqlrnrfv syygngsysy lkryilsgsf rkdasnlfgv ksnnkgqpfw
      721 slglawvvte eeflkdspfs llklrstfgy ngnvnntisa ypvmkvetip ngatgqnyaq
      781 invppnpklr wervgilnlg mdfglkgnrl ngsvqyyhkt pkdliadgqv dptvgfaslm
      841 mnvanldtkg wdislngkpf vtgnwewnsn lvfaynrtkv vkaflsndna qynvskalsf
      901 qktaiegmdl yslltyrwag ldpedgavra ylngevskdy iailnakvss lqnhgsqmpl
      961 yfgsfrnsir fknvelswni syqlghkfir ttfnnysfln vgaghtdyah rwqnpgdeqh
     1021 tdvpafiyps nsaasniyvs ssalvenagq iklrdiqcsl qlpqlarygf knmriysyiq
     1081 hvatlwrgnk kgidpeygkw ipdpmmisfg lnfnl
//
LOCUS       WP_120259167            1016 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120259167
VERSION     WP_120259167.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1016
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111653
     Region          23..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mskilsflll wlviiplahg qqrvlkgslv dlatnaplgg atvrlestnv gtstddqgkf
       61 tlnvpqgavk llvtlvgyed trrtitaqen disikmtsks ssletvvvta lgiqrkaksl
      121 tystqvvkgd eltkvkdvnp mnnltgkvsg vqinrsssgm ggsvnivlrg fksnrnnqpl
      181 yvidglpitn tngsgndgaf ggatdrgdil stlnaddias invlkgasas alygsqgang
      241 aimittkkga egnlkidlss gftadkafyl pklqyrygqt tpsseeswge kgtfadpvkd
      301 fyntgttfin tlalsggtnr iqnyfsyant snkgilptnt fkqhsatfrn smnffddklf
      361 fdgslmysrq nihnrpssgl yfspiaglyl fprgqdfdky knfeyfsesr nfylqdwwni
      421 nadakltgth hqqnpywvln riptdqkrdn iigqaqfryv ltdwlsvsar gtlnkrwdhw
      481 erriyagtqg vlsglpidgk lgdngryntd rsestalygd llltgnkqwa eqldlnftag
      541 tsindlrsng tvldlarlav ankflmsniy rdapmqsate tisrrqiqsl fasanlgyre
      601 kvyldltarn dwastlantp kehkgyfyws agvstvlnel fklpsfitys klrlsfaqvg
      661 ndvaaystip vntlntgilt pnvsgpyrgi plkpeisksv elgyegrfwk drvnldialy
      721 ktntrdqyfe yqgpvgvvnt tvflnagnve nkgieaalgv taikkehfnw ntgfnftanr
      781 nkilklapnl gntyplggnf nvlrlggsfg dfwapmfkrd qngtiivddn grpqiapagy
      841 ignntpkaiv gwtnnvtykd fglsftidgr fggkvisitd gylnsfgvse esaaardrgg
      901 vdiaavkmdg tawegllpaq ayysavgnrd giiegqlysa tnirmreial syklpikwqg
      961 ikqpsisltg rnlfffrnda pydpelnttt gvggqgydsf alpttrsygl nlkvsf
//
LOCUS       WP_120259356            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120259356
VERSION     WP_120259356.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120340
     Region          19..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknyillvfl laccsvnaqi tgyvfdedgn plggatvkfl ksrssvqtrq dgyfssvnat
       61 tpdslliqfi gyhdrktlim snsgnlriql eknpyaleev qvvntgfyki pkeratgsft
      121 tidnkllnrs vggdilqrld gvasgvqfvt pngtktsdir vrglatiqsd asplivvdnf
      181 pydgditsin pndienitvl kdgasasiwg aragngvivi ttkkgqynqs grlslnsnvt
      241 lgqkpdllyn rkrllseavm eiekekyeng gyyiedgsqt sfpeyvemli alnngsitqq
      301 efdrkeailk stevrkeamk ylyqssiyqq yalnarggge rftyyvsggy dhnranvigd
      361 knnrinlnsq ntfkpfkqie isssfwftqq gsygngisls elagaakhvg mspynrlmde
      421 ngialpiiye yrkpyiedat knglldweyr plderglter kvsdqeiran msvkysfmkl
      481 fdftgtyqyl kgsrdnaiey deksyyvrnl vnsftqmdgs kvipeggifr ylspentvsh
      541 sgrmqlnynq dfgaehqvna ligseiretv vktspgstly gydpellmgs snfdytksyp
      601 vrpdsysgip slsvenaqft drylsyfgna sytyrmryil sgslrwdgsn lfgvktnqkg
      661 tplwsigasw evskeswfep tyinylrlrt tfgsagnvnk tvsayptirh svndritgyn
      721 wanlttignp slrwervntl nigldfralr erisgsleyy vkdandliga dvllpntgvs
      781 rggtainsnl inyanlrtrg fdlqinslnl ngvfqwntnf lfsytknkir dykankstml
      841 fsyfenspvp vegksrdily alpeyrldpd dgtvlmylng erernaieyy nsftvdqlvn
      901 mgvsvpplfg slrndfswkg lalsvlvswk sgyvfrrsth spglehtivy syhmdyldrw
      961 rkkgdeahty ipatssiste nfgpdinkfa nfvskgdhir lqdirlsyvf pkharlfsgi
     1021 rnmsinayar nlgilwksnk qgidpdyves dyiaprtfal glqvdf
//
LOCUS       WP_120259378            1178 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120259378
VERSION     WP_120259378.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1178)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1178)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1178)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1178
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1178
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132036
     Region          129..1177
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhhfmkyrr vksillgggv wllilsplgg lkaqiniaak qkslisvfrq vekqskyvfl
       61 ydkavenspa isfdcancsi erviqlleqq tklefkisgq qvlvkkrttk gtgetkaaal
      121 tlqaaqkdti qgkvvdergn pvvgatllik gtrigtatdr tgtfkllrpa dgqqvlcncl
      181 gyhpeeihva gqttlmltlr vkaqqlddvv istgfqkrer nklignissi kgedlqasgi
      241 ttvdkalrgk ltgvyvrsns grpgeagsii irgsntmtgs sepliildgm plqnggvagt
      301 dktssninsl ltngignipp ediasidilr dataasiyga raangvivit tkrgeagkdy
      361 inystkqsln mqpgnafnfm nsaeklafet qlykdfhpvy ggranqlllq vdngaisaae
      421 aqqqinqlsm intdwinvly npayqqshni amsggstklq ynvslnyqda ngtlmennnk
      481 qggmnvkltr nindkllvdf nlystikknk egqsamdpfr yalfanpyer pyqedgsyaw
      541 dktyrdlsgk vgetaylnye tfniikelre ntlttdyanv rsqfglewkf lngfqyrgsa
      601 vvnytnvsta desragtyrs faqnwlnvar tsgsgvlpkf nygfleensg rtldytvrnt
      661 ieynktfadk hyvqaffane vsertnnrff hynpiylqdy rmagypswdd vppanykkld
      721 lsrlggtyye kdrsvsfiss atysyanryv fnanfrsdgv diigsknqft plwsvgakwn
      781 gheekfvkeq lpwlnrfvls agfgytgsin rsvypfhtyt lsalvyddvv kaqafkygnp
      841 vlkwekkrdi nygaqisvln srlnieanyy dnrvtdlldn vvlpvsvgrt ssvvnagils
      901 nkgwelsarv ellkktdwlw evggnlttvk nnldkvyykk eptvsnltpq nvenyamrsw
      961 fgykydhidp nnghmmvkaq rldaagnisg eeiidlskis sadlqskyrt yylgqqdpkl
     1021 yggfntrlry ksmtfstnfv fadgnmikgf qdrregpsgm tddvtagrtn rlkeqqyrwr
     1081 qygdvtdipy ysptasnyvn ylidrdiesg myikcteigv nwranpavlk kmikqlqigv
     1141 fannlftisp ysgsdpetqm afgypttpsy sfslnigf
//
LOCUS       WP_120259543            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120259543
VERSION     WP_120259543.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124895
     Region          22..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkflipltf mcvqmahaqe skelkgkvld avtlkpvvga tvvvessava edigvpnqvq
       61 qsalgsltda sgefrlkvpg nlkyvtisyv gyqriqvpvf qdhrtillqp sgesldeviv
      121 tgytdikkrk nttaynkinv adikqtgvas idemlagqva glqlsnfngg pnsapqirir
      181 gtvslngtqd plwvidglpi egtelpnrid kdnlnslnnl piaginpddi aditvlkdaa
      241 atsiygaraa ngvivittkr gksgpaklqv santfvterp dyaqldmmna nekvdfellm
      301 anrtdlnyrs dkgaimrils nanaldayrs gglaalspdv qqsinqlrtq qtdwgkelyr
      361 qalnqqysas isggndghry ylssgfydek gatkavdlrr ysltlnndfn indrfkagin
      421 llgsvsnrqn piqdrdaftn psyyvrsvnp ylsvydqsgk ynydpdiegf ekdtyipfna
      481 ieerentkys ltnkalkais yleyaivpql slrtefglqf dengtekfad qesyntrkfr
      541 aatryydtas ktykyflptg gtienthnsi fqynwktylk ytkswqdrhe levmggtelr
      601 rstnkivttk gfgynpatlt tqnidfpnsn yqndprfrqy skgfiensya sfygnatytl
      661 drkynvygsi rydgsnmfgv dpqyrflpiw slsgswnvle eefikgktal sdlrvrasyg
      721 iqgnvdrnty pfivgkygnt nllpgstegt vvvdmpandk lrwertqsyn agidlglwkn
      781 rlnitvdyyn rkstdlisys alplengfqn vqvnwasarn qgveltissr qiqtekfsws
      841 tdfniahnnn kllkvvnnpk ayapetqegr pinglyvlet agldkdgvmq frnldgsvss
      901 fedfyglydp wadflpgyts qtdmtaaeyr skfkykgskd pkfiggmtnr fryanfdlai
      961 savfnlerwv srtptynpak vdrgqnytkd llmalqgnka lpalgsisse lnerwmaygw
     1021 mesndpinsf nqydiwakkm syvrinsirl gytlpaalsk kigasnlrvn vegrnlfvfg
     1081 anydgyfdpe tygdyyaqpi sksfafglsa sf
//
LOCUS       WP_120259629            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120259629
VERSION     WP_120259629.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115383
     Region          24..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkllslfv gsmiltsvaf aqerkvsghv tgvdgkplag vtiavqgsnv atqtdangny
       61 sisvpngkvl vfrsigysdk tlivkegqsa fnislsnddh aldevvvtav gisrkskslg
      121 yattninnee itrtspvsmf dglqgkiaga titsqsgapg astkvilrgy ssiggnnqpl
      181 yvidgvpvnn tslgsagstr sadygnqand inpddiesin ilkgagatsl ygsraangvi
      241 vittkkgkag kikvdlgtsa tyssilmlpk lqntfgqgws gvfsyiengs wgpkfdgidr
      301 lwgnvvnnqq qvkpyvglkn nirdfyttgs eyntnvavsg gteastfyls ygnissdgiv
      361 ptdadsygrn svslrgstvy nkfkasasln yvnrhqkfva tgqgsntgat mfqeliqipr
      421 dmsiidfkdy kyifnnldny ftpyaqnpyf vlnengnnyn sdrfygntel nyeftdwlsa
      481 tarvgadltn vrikdwqais rpdptspnss rqadvggvte dsnylgeing dfllnfkkni
      541 ledltfdgll gynfnqretr lhnssvaglt ipnfyylsns snapvttvni tkrrlmgaya
      601 qanfgyrnyl fltlnarkdw sstlpigknt ffypaanlsf vlsdltdlkp ygvsfakfrt
      661 sigrtgndan vyllqsvltp gnvamgfgnv ifpiggvtaf elgntignnn lepeltteye
      721 fgtelkflnn rlgvdftfyn ketdgqilsi piaatsgytf qvanfglvrn rgyeltlsgt
      781 pvktdkfswd mtytfaqnrn kvlelpdgle qvsifsgydv dfvaikgrpl gvfkgptekt
      841 dpngniivnp dnglplqade kveygtsqrd ytmglvntfk ykdwafgfsf dfrkggqfws
      901 ytsqlnyfvg naqrttyndr ntyiipgsvn eikdgdkvvg yqenttpiay gdianywsng
      961 qntqsvsrns vldktslrlr dvtlsynlpk svaakikadr vslgvygrnl flwlpksntv
     1021 idpdastynn dlrgelgefg agpttrsyga slkvsf
//
LOCUS       WP_120259625            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120259625
VERSION     WP_120259625.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116916
     Region          24..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqtllsflv ggmiltsvaf aqekkisgrv tsadgkaipg vtvvvqgtnq atqtdtdgny
       61 slnvpagkvv vfrsvgfddk tiivnnnstv fnvsmenhdn aleevvvtan aikrekrslg
      121 ysaptiksde ltegrnssai nslagkiagv nitstsnapg sssrvvlrgg ssiagnnqal
      181 ivvdgtpidn tskvggtndl asvdfgnrgn dinpddiesv tvlkgpaaaa lygsrasnga
      241 liittkggkk gakssitfss tntlssilkl pefqneygqg yagydsktge fsgyvndpre
      301 ngswgapftg eiqewgqein gvrqkkaysa vkdnvkdffd lgiasdnnls fsggsdkstf
      361 ylglnalnsn gvypgkkdny nkygvrfngt tefsdkfsag vsvnynrins nnigggqgpg
      421 svynnllqtp rdidivglkd lsnpynahgy tdangvvnnd rygyygsytm npywilanyn
      481 nyndvnritg nfnlnykple wltfqerigl dnytdrrrte spkysfipvd tksgnysssn
      541 irsnpgqyri dqynvneivh dfmatathkf nddwdasfml gnnirqrkts nnitatnasg
      601 glvvpgwynl snsngpldli edtwsnrrlv gvygdlnvsy kniaylqata rndwsstlpk
      661 knnsffypsv sgsfvlself kpelkskfny aklranwaqv gsdtdpyqli ttfarsevns
      721 gfgkttfpfg nvsalmssnt ignaglkpei ttsfevgtel gffnnrlyad ftyynnnskn
      781 qilsipipls tgyglalvna gkvqnngvel tlrgtpvktd nltwelygtf tknnskvvel
      841 mpgveqvsig gfsgmnivaa vgrpygefyg vtnatdaqgr tivdkgsgmp latdkpqyfg
      901 tynpdfqasl gtnlsyknws msalfdtkqg gvfysrtrdi lafvgtsaet ggerigqifp
      961 nsvyldadgn svvnttstyd kgnyfptrea gtnivdatyi klrnltfsyk ftkdqlkntp
     1021 fgaasigvfg nnlfiwtpse nkyadpevns sgagnaqgfd ftaqpslrny ginvkvsf
//
LOCUS       WP_120259795            1076 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120259795
VERSION     WP_120259795.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1076
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121009
     Region          24..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfvcnlfia lflcganvaf aqkqkvtemh givkdknnee iligvnfktk qgvflnkshv
       61 ggrvtlsvpr nadslivsli gyqrvtvahd yfmhsdvlll ekqdyylaea vvntgyqalr
      121 pnevtgavdv lsnkmlneqt gtnilqrmrn ivpafrydnk pvqnpevnkl nisvrglsti
      181 ngsldplivl dgfiyegdid nidpnsieqi silkdaaass iwgaragngv ivitskkgrv
      241 ndggtrvsfn stfsiqgkpd yqslytidns sfmevekmlf dngyyknaln ttkyiavtpy
      301 vdlldkrsrg iisvsdsarw tdyykaqngv ynysdnfvsk pitqqyalnl nggnkfhtyg
      361 fglgythkss elgagdqkin irlnngfrlt erlqvdasll ltdqksksgk palnslsysg
      421 ksvpymafyg pdgevvpfer efrklfldqn yqngyldwsy yplsdyrhst sevklrevfa
      481 slgvryklts fldlnlsgqy qnqrtdkrnl ddensylarr ainqysevnq qtgvakynvp
      541 lggilnngiv sgtsytlrsq lnisktfqkh rivgvigaem renrtegssf tsygynddpl
      601 istavdhvtr fktipsntnr titgapaysh tnnrfvsaya nfsyiwqeky glsgsfrkdg
      661 anvfgastnd kwsplwsagl fwelrkenfl rsyeqtvdql klratygtsg nvdlrktrdp
      721 igtistdsyt rfptiiitsl ndpslrweki atvnlgldfs flnrriagsv dwyfkkgkdl
      781 ygltdydytt wgyqptitkn vasmqgkgvd lvlnslnlnk tvkwssrlll sfnknkttky
      841 fnangntlln flndgsgitp mvgyplnglg afkwmgisad glgqgvldgn isaeyakirs
      901 svalnpense silfvgsskp qlfgniintv swkniemsin isytgdyyfr kpvtsyanly
      961 qkgvaypdfd krwqqpgder ykdvpkmtyp vlsgadsfyq aadinvlkad hlrleyislg
     1021 wnreimfndh ksklmlylni snlgilwtan klridpefpy klapqsvysl glkidy
//
LOCUS       WP_120259872            1158 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120259872
VERSION     WP_120259872.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1158
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131964
     Region          123..1157
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqkttqlaw ksmrspmakk lgiaflslyl lqsnpaysfg qtievhakaq klakvfeqlk
       61 hengyhffwe gkdfsqtlit vdvkgdihev ldklfsklpf kyriqqktii veadpnkkiq
      121 estyrgrvln elgnpiqgat iiyddgsgqk ttvtnskgqf aftvhqgpvh viissvgyqp
      181 qeysvdnpek sifvqlelsn nrieevvist gyqrlnknna sgsttsldsn yfkkrnntsl
      241 etalegavpg lsfykdekga sdmrirggss lragtqplii vdgfassiip nineiegvtv
      301 lkdaaaaaiw gsqasngviv ittkkgnrgk tsvtysgnlr vqmrpdykal qransaeiid
      361 yekeqydkef vidiydgnss gytqsigift aydrkeisle erdrrlaala glnnqdqink
      421 lllrkavnqs hyigisggsd kfshmttvng qfdlsglqgt stktfnfsnr lqydlakfvs
      481 lttnvgflyg wdqqgindls geiralqpyq mlmdeqgnyi rsyagynkve ndrlmslgyr
      541 dnglnlyeen qlannrsrsl airslfglnw kiidglrltn nfvyertttn grnqydkdsy
      601 atrsfmnryt vldknnsika yipygdyldt rsdqstflsa rnflnyekkf dekhyinvla
      661 gfdlnrkine gdrnrlygyn dqllnsqnid lialnvgikd wegrtytydh ssyvrnnyve
      721 nreysfystl aytydnrytv tgswrndhsn lfgsdpkfkr tplwsiggkw lidnehffni
      781 dwisqlnlra tmgltgnfdr snqsstylva rrffnamand yvarvdsppn aklrwertkt
      841 ynigldlgil kdritlnady yhkfsydllg sqdldptvgm tnsyingadm inkgvefgln
      901 aailknsafq wsstlnlaln kskvtknkit dsdptnnrpk ntvpflegyp reslwsyrwa
      961 gldeqgrpqt fdaegnktrv pvlesliyhg ssrplytggw snefrykgfq lsiytvfnwg
     1021 hyarkempem nsltwsssyn nqiakrwrsp gdelitdipt fpgwedlsne ylflttrssn
     1081 svidaaylrv remslsytfk rpqlqgklpf seirlvsqfn nlwlwkanks gidpealvaa
     1141 rldlpqprvf tfginvtl
//
LOCUS       WP_120260007            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120260007
VERSION     WP_120260007.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117161
     Region          26..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maknnidfvv laalclstgt lyaqstikgk vvdnnnspiq gatiteiisk kqvqtdangl
       61 felpssgnsi siqvqyigfd sktvqtnpgg lttiqlspts sqldevvvta lgisrekksl
      121 gyavqevksv elqtrptnal salsgkvagl qvttsggnmg gsshvllrgi nsiagnnqpl
      181 yvvdgtpidn tdlnssstin gsagkdvgnm iqdinpddid nisvlkgpsa aalygsraan
      241 gvilittkra skgekidisl ntgvdfeniv rlpkrqhlyg qgystafqtq ningtdykiv
      301 dyaadeswgp kldgtpvlqw ynlnpedesn ylnpspwlyp kndvsyffrt gvantnnfai
      361 agnsgntnyr fsytnknvkg ttpnsslgrn tfnfsggtql gklkinsnfn yirnasvgrp
      421 wtgasnrnii leafqwgavq vdykllenyk redgtplawn rtgwqntpta eatrfidnpy
      481 wsayesymed nrdrfygnig lqydlnswls lgakvhgdiy sfqsqdriav ysrstsqyee
      541 tsnklneyny eflatakknw dkfslignig anlrdqqrkq dyaitqggli ipnyynlkna
      601 nsvkidnfky hrriasvygs fslgyndlly ldgtvrndws stlptdnnsf iypsltgsfv
      661 fsqlaafkql dwlsfgkirl gwaqvgndtd pyqlykvyep eqsyegqasy glpsikpnan
      721 lkpeitsswe tglnvqlfkn rlgfdityyn nnsrnqilpv pvsssfgyas kvfnagkinn
      781 kgleivlngt piknenftwd atinwaknkn kviklddqvn tlslsnslve lvaregesyg
      841 qflgydfvya adgqrvvqad gtymktsqlv plgsilpdft fgfqnsfryk nfslgflvsg
      901 rvggkffsqt ykvgmysgil dktaannire tgvildgvkg dvtfhsdgty avenvqqntt
      961 nitaqqwarn eyngpttfsi fdatyvklre vtlgynfkla nakviknigv nvygrnlwni
     1021 ytkskyidpe ftssggnvqg ieggnipvpv tygfnvnlkf
//
LOCUS       WP_120259882             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120259882
VERSION     WP_120259882.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107906
     Region          27..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkllaqcv mmpalllttf favaqtrvlk gkvvdetqsp ltgatikvkg sttatttdad
       61 ggfsinistd akslevsyig yatkevpiag ndmtialepg snqgldevvv igygtarkrd
      121 ltgsmvtiga knfnkgimts pdqliqgktp gvmvinntgq pggsttvrir gnssirasnn
      181 plfvldgvpm sgnsplpegr ggfssdrgnp ltylnpgdia smdilkdasa taiygsrgan
      241 gvviittkkg kvgppeisvg asagvstmre ypdvlnasrf realnyytps evansdfggn
      301 edafkaitrk aitqnyyadv aggtehgkyr lsggylnqng iirgsqlkky tanfsgnfrf
      361 lenkrlgldf aafltqmdnk yapinatvgs egnvisqalq wnptrplrdd kgnltfvsst
      421 trnpltsiea fkdvattntm vvnlapyyki tddleyrfiy samrqtgnre gmyraglidp
      481 savnneqafi snngetnlqm thmlsynkqi nddwsvnava gyeyldynyn nnisfgggfk
      541 ymgldyfdyl qystvstrei asyrsptnql qsfflrggfn yldrylftat arrdgstkfg
      601 annkyamfps laiawnvaqe dflkssgifd qlkvrigwgk tgnqefpsga slnrftfgnq
      661 svgranfqnr dlkwetsttl nagidfsvlk grlygsidyf nkkttdalfe qtlaqdgpag
      721 riwvnldgei vnkgveialt gtivkndnwt wdltgnatfl knsvsglvgy yetgalrgqg
      781 fsgvlgqrmv ngqplnvwyl adyqgidpqt gtsmyrghdg sinttndpas nkfymnspnp
      841 ttllgistnv sykqfslaan mngalghylf nntaattlgi snlssrnigs affntsvkes
      901 tsnsasastr ylekgdylkm anltlsykvg nvgktlknln vsltgqnlfi itkytgfdpe
      961 vntdgsnngi pslgieylpy pparnillgv nfsl
//
LOCUS       WP_120260198            1158 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120260198
VERSION     WP_120260198.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1158
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126606
     Region          30..1156
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mesklkhysl vlcvtmlmgm pftlvaqiak tiqghvvnsk ngqpiagvsv kevggknass
       61 tnengdftls vsnnkvvlsv qyvgymtksv egivgtplrv elqedntild evvvvaygea
      121 kkkdltgsvs tidnralnmq snstvsrale gaapgiqvsa vdgqpgidmg irvrgigsas
      181 qntsnalvvi dgvpaqndnp latlnpkdiq sisvlkdaas talygargan gvvlvttkkg
      241 msgktrisfe gklgvnqvgp yqfdkisdpk diyefawlsi ynsarygvdg tgiskryttn
      301 vqnpnmsheq aaefasahlf dyigsttkfq rnslgnwmly dvpgavytps gtgadasstm
      361 sgsylvntdg klnpnarllf sdryddylle nrlrqdydls asggnekvsy flsggyledp
      421 syirgssfkr yngranfdaq vntwlklgan igysnrttqs patrfgrnpg sstanvfrfi
      481 ngqnplvqly ardqngalin engenkvhvl agdtysplgl tsaalsstnv ltvldndldr
      541 rvsddwttrv ygqakflndf tftanvsmdk fnemrtrywn sesgqaagig afgktasntt
      601 ilnlqqllny sktiglhnfe gllgheydsf kneqlnyrss yslidefpsy infvgrydgg
      661 tfpnpgggee krtmesyfsr inynyndryf fqgsvrrdgs skfklkdkrw gtfwsvgggw
      721 ridsesfmqn aknwidllki rgsygvignq ngisnysgyq twsysatytq ttngtgipan
      781 itlnqnayvn dqltweniht mdagidfsfl grvrgsldyy nrvtvnaiwn qpiaiskgqs
      841 siatnsakig nkgfeidlsv diikkpdfnw tvstngthyt tklkavpngv gsdalggnwt
      901 agtdawaaag tsavtnityl rgvnkdffnl ymlkyggvdq atglplfyhq vtkadvdagt
      961 ypgykegesl tttdyskasr yemgsalpkw iggfstslry knfdlylala yqlggkffst
     1021 eygnnlyvse dpgkalssel igntwtpnnt gakfpmvmyg ntygngattg swlysdlglf
     1081 sasylnfkni tigytlpenv lakmkikklr ifasgdnlfm ktahsgidpr qslvggfeva
     1141 aysyptmrtf sggvslef
//
LOCUS       WP_120260341            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120260341
VERSION     WP_120260341.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111977
     Region          23..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkklllfcs gvmlstslwa qtktitgkvt nasdggsman vtvsikgkpv stqtnpdgsf
       61 tikaepgdil ifravgskek qqavgtdatv nialsgseea leevvvtamg ikkekkalgy
      121 avqdiksdel mknknpnvin slngkiagln itnsggapga sasiiirggt slerdnqplf
      181 vidgmpidns tgvgdmsafd gstnisttsg nramdinped iesisvlkgp taaalygira
      241 aagaivittk kgkdgavsig vnsrvsanwv nklpkqqgiy kqgtslsgtv dpnsnfswgn
      301 kfadgetvyd nlrdffktgy tydnnfnvtg gnkngnfyls ggnlkqtgii pttdydrtnf
      361 rlngeqrlgi mtfggnaafs qskttktltg tglwgtggng ylesiiaypr nanmknwqna
      421 dgsqnlllpa isleanidnp ywtvnmnpqt dktnrflgtf ytnakftdwl dftyrlgldn
      481 ytstytskis agssvveqyq kgmlsqnitq ytftnhnfll nahkvvaqdw dlslllgaat
      541 edlntktnat kaqrfilpnf yafnnaadkd kfvydnltqi rrlgvfgdfk vgyknfaylg
      601 atlrndwsst lpvqnrsfmy psfsgslifs ellpkndvft ygklraswae vgkdapayqt
      661 nsyleipqnt igggfrnswt lgnsnlkpek tqsfeigtdl kflrnrlgve ftyynnksvd
      721 qilsprvdna tggifqyvna gnlqnkglel tinatpikre nfswdlalnm shnkgkvnal
      781 pgglsilyvt dvqvadgkaa sfndgdfmgi sgkkwrtnen gellldwttg ypssdgnaty
      841 qvgnrepkfl gglnnsftyk nwnlsflfdf rkggdilngt eyqlayygls kntenrgdkm
      901 lltgvatnpa tkqleqvtre itldqyyyqn iyaqqtanfv etvnwlrlrs vnlsydlpss
      961 vfqsvkwikg anftlnatnl llftnysgmd pevsaagagv rgsgsvgvdy agvpntksvt
     1021 fgvnlkf
//
LOCUS       WP_120260338            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120260338
VERSION     WP_120260338.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113611
     Region          22..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrsllllms llcmyctafs qkvitgkvtd tkgealkgvt vqekgkntqt atssigayki
       61 tvsdgatlif rsvgytstee niqgrsvinv vlsdnsaaid evivtaygik rdrkslgyst
      121 pivsgedvsd tqresffqgl qgrvpglsin stsglpgasa qivlrgfasi sgdnnalivv
      181 dgipinnsti nendlasnga nqsldysnra mdinpddiet ytvlkgpeat aqfgsqgagg
      241 ailittkkgk agkftanytf sgrvesvnkf perqyvyaqg lngsydgtas talgprypeg
      301 vhiyednvkn ffttgynqkh slafeggtek vtyrwsneyn nntgvvpntl ykrfstrlns
      361 takfgdklef ntslnyiysk ndkvrrgasg ylmtlmsfnp ifdvrdwidd kgnrvlhnsd
      421 ifnerdnpfw dvyrntaydv vnrvlatsni syranswlsl ngiigidfsn tlgqsvyhpq
      481 sfsgsgssta mrngsineyt vngrilsgsf manvkknlsk dfsfranlga efkdydfltn
      541 sqygedfydp dfysinntfp ssrlvrsaaa nfrtvgfmaq tgfgylddmv ylnltgrlda
      601 asrmmpnnpy faypsaslaf nftdldffkd kvswmtngky risvgttgka pyksyytlsn
      661 fepknttggg faygvnggnp nlkaektrdf etglelalld rrltfdfsyf nrlstgqiim
      721 prlsygsgfv lrmmnggevk tygtelqtti npirrdnlkw dltfnftqyk gkvlslaedl
      781 pelyesdtqv lggvrsgvvp gysigtltgt rfkrndrgdv linaqtglpi agtdryypig
      841 dripdftlgi vnkltykdfy ltflwdwrkg gdvlngldyr lyingmsskt lnreeprvia
      901 gvledglqns enptinriav tpysssgyyt vntepqmfie kdiytvrlrd vtlrynlpkh
      961 ltrkigaqag lsvfftatdv flftnytgld pesnmntpgl ggiggygidf gnmakprgfn
     1021 fgltlkl
//
LOCUS       WP_120260346            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120260346
VERSION     WP_120260346.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111231
     Region          31..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnklyttlk mlsivptmlf sasllhaqss qvkgtvvdak sktplvgati kvlgtstass
       61 tdskgtfqin vddknrvlni stigyenktv tlgpgettvt isldeqtqql esvvvtalgi
      121 sraqksltys tqqvsgdeln kvkstnlann lngkvagvni assssgpggs akvvlrgnks
      181 asgnnqvlyv vdgvpinnqt lagqpdnvfg gqrdggdpia minpedveni svlkgasaaa
      241 lygsqaangv ilittksgkq grttinfsss aqieqavstp kfqsqygqgs kgknsntsvf
      301 swgdktngan ydnvgeffrt gsnftnsltl sggneknqty fsyantlakg ilpendlmrh
      361 nfnlkesatf fddkltveas anyitqkldn aptsgfyysp lvglyllprs lniadyktye
      421 kfnpsrslne qnwftlsdde ttqqnpwwia nrnstrstrn rlllngsaky kiapwisvqa
      481 rgsvdrtsev wdrkayagtq kilarengay sytnttitqq ygdvvanmnf nvsdklqitg
      541 lvgtsitdwk tegtdfttgk dglkvpnqff iqntttpvts tlsanrrqlq svfasanlay
      601 dnwiyldlta rndwsstlaf tgtksffyps aglgivlndk lnlpefvnma kirgsyavvg
      661 ndlppytsll tntvnpyavl tvndiaflkt lkpektksle igtewrmwnn rlnvdvtyyk
      721 tnttnqffkv aashaslnkq yainagniqn qgiealvsld aikndnftwn tsvnftynkn
      781 kiieladavp efnltgegrn nfasklevgg sfgdiygqdf vrdnqgriii sadgipqknn
      841 vytklgnsnp iwqmgwnnsf nyknfnlsfl idgkfnydvm svtqslldgy gvskvtgdar
      901 anggvivngv tpdgkavtkv daeqwytsta gmgpvssqyi ydgtvvrlre ltfgydfnik
      961 dsffkklrvn avgrnlfyis kkapfdpevt mstgnalsgv difmmpatrn ygltlnatf
//
LOCUS       WP_120260606            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120260606
VERSION     WP_120260606.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117139
     Region          33..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksihsqryi iglrgslill lnlftillfa qnktitgkvk deqgkplega yiielaskhg
       61 trtdkegsyt lknvapntki ratfigrime ekevksnett vnftlkqrvn sinevtvntg
      121 lykrpvgnft gsaktysgee lkmvnprnai qalavvdpsv rmlqdnqfgs dpnhlpniqi
      181 rgannlslnp agtsngtpvs ngdimssyls npnqpliild gfettlqtfy didinliani
      241 tvlkdaaatv aygskaangv ividtkqpaa gklrvsysvn asaevpdlts yklmnaeqll
      301 eaqrltgiys dpanqyndla kkqwydyrla qvrkgvdtyw lsqpvqtglg lshslslagg
      361 sgplrysfgl nyntsegvmk esgrdrygmt ynfsygiknl klsnaiavgy trgnntpwgt
      421 fdsyiklfpy frsvddngnp ikilepdfne lgfsinapgg tftnpmynat lnvkdytatl
      481 nltnntnlew sltddlkltg slgwmsnapn aeafypadht rftssaialf pnlgsynhts
      541 gknssingrl nlsyrlalgr ntilanigss fqktssnaln vrvfgipndy lgemgmangf
      601 dyqstkpstq nnqtknisnf lslsynydnr ytaeftvnqs gssqfgsnsr fapfyaggla
      661 wnignekffk qnniiqsakl nasigitgnq nfssdmaqqt yqynlmnnyr lmlgantlsy
      721 anpnlkwqqt lksniglqlg llkgrlnani effrettdnl ilpldmalst gfesyqnnlg
      781 atknegyeis ltapvikdak rnifwtvgin aghysnvita lspaiiaine afnkgtdpnn
      841 plnsryqtrp lprfevgesm nriwavpslg idpatgkevf vkldgsrtft wdardkrava
      901 dataklkgaf nsnfnyknfi lnfifsyqyg gymynqtlvd rvenvdlvtg nadlrvfter
      961 wkqpgdhssf kalvangasg lqqtnvtsrf vqkdnflela sltvgynipa narwvkaarl
     1021 saprimitqn nllrfgtirt ergtvypfsr sfnlglstnf
//
LOCUS       WP_120260698            1129 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120260698
VERSION     WP_120260698.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1129
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127293
     Region          75..1128
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnfirtgkc iacskqtiqy iklkkaqser idckaysskg vltkrvllii avvfhmfsls
       61 aqtprkdsga ngpltvsgtv isilnskpih gvsvriedek grassksdga fsvpvlahkg
      121 tvkfshmgyk plalpysvgv sltvkliple nqldevevvs tgyqkipker atgsfefvdn
      181 kllnrkvstd ilsrledivp sisrdksfdr gklpfinvrg vssmrsypwp livvdgmpyq
      241 gdlnwvngss yfgsfnninp ndienitvlk daaaasiwga qagngvivit tkkgrynqpi
      301 qvsfntnltv eakpdlyylp qmssrdyidv erfyfdngay dykksqifnr fspvqilmmk
      361 kekgllstde ldrkldqlaq idtrdqflky vyrnavkqqy htqlsgggts lrylfsagyd
      421 knldnmvnsn fdrinlkssa qlspvknldl gvgitytkst ltdpsgnntq ygnllagnyp
      481 ytllanaggk lisidgagvn pffldtlaay nklldwryrp ledldlitnr vdvsdivldf
      541 naeyklpfgl rasvlynyrn qqqdqeywks vnsfvmrdki nsftewdysp vkrnlpfgdn
      601 lyilntkgtm qqgriqlsyd hqfsenhlvs aiagmeikdm ktrtystnyw gynrdqltwq
      661 pvdlisifpw gngilgrski yspqesqnrv nrftsyfana sytfksryia sgsirkdasn
      721 lfgvktnnkg qpfwsagaaw lisnepffkh qngidflkvr ttfgyngnvn ntvsaypvmd
      781 ispypdyvtg ntyaaisnpp npnlrwenvg mlnlgldfgl knnvlsgsie yyiknstdli
      841 apamidatsg fgtlninsan mrgrgidinl kslnirsdnf qwmsnlvfay nrtkvtksyi
      901 snddgknfvs gnriltpieg fdvyaalgfe wkgldaengr piglvdgves tdyaaiynnt
      961 kvkgmanlga mqpvyfgslr nsfsyrsfef sfnisyqlgh kfrrksfngy qfwqtdaghk
     1021 dyalrwqkpg delhtdipal afpldyygdl fysmssalie padqiklrdi qlgynfpskq
     1081 nrlfkelrvy gyvnniatiw rannwgidpe fgenfpdpks fsigmsckf
//
LOCUS       WP_120260728            1209 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120260728
VERSION     WP_120260728.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1209)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1209)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1209)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1209
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1209
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134384
     Region          158..1182
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myhfftkkdv gdffcvvptd eqstgeksvs riftnalmki slssllllgm mgvqantmaq
       61 rvninkknvs lrkilqeini qtgyhylwaa pnidpltcts vsfnnlplqe alktlekntp
      121 iffelekdmi mvkqrqseig giqlketill lnlkdqskir gkvvdengnv lvganvmiqg
      181 rkkgtitngn geftldnssv gtniiisyig yesitipvtn nlgvitlalk tgtlneatve
      241 vntgyqklpk drvtgsfsyv sgeklerkla tdlksalegq ttgltidkag kieirgvstf
      301 naqktplivi dgypvettid dinpmniasi tvlkdgvaas iygsraangv ivvttksgqn
      361 sepkisysgf vniiqkpqlk ylnkattsdy idaeidlfnl npngpstmdp ynmsrvtyll
      421 mqeregkish qdamteingl rginalnqiq dlffrnkvth qhniniaggs pkssynfsvn
      481 yqqtkdnlin ndskrlitdf knewqlfpfl tagaaanfty nkgnstsfty stiygpelvg
      541 dnyqslvgfs ggsmimpytn lldgngnpaa iwgisqykvn tykntpgmks wdyvpledmg
      601 kmpsysnvyn frmsgflran ivegltaevg gnwvkgtanv kniqradsyn ariayndgts
      661 ksnpanhyip dgsildefkn inetwtlrtq lnyrknfsdn khllhalvgn eirkitsdnn
      721 rlatragyne nagsfipvni kdftagiyna dmlfpngsvs ltdgsltygd nrfvswyang
      781 syeydnrfil sgsirldltn ffgtdkkyry kplwslggty klsnekwwdk avfsklnirg
      841 sygingnisl rngpflilsv gsyspttggv sygvssppnk qlrwektnia nagidfglfn
      901 naiegsfdyy nknssdllaa daadptlgfs sltknvgkmt nhgfelglnv haiknsrfsw
      961 dilpnisfna nkvkhynvnr pytgsyttpg gimvagypsd glwgyrfagl nelgqtqvyt
     1021 rdnqvvlasn aevtdlvyqg tfrpkwdlal tnrfsyqnwd lsfmfiaklg hkyrkdtfsg
     1081 snyqnrhvae rwrkpgdekn tiypvleewn mdmfsfpfad vnvgnasyak lrditlsynl
     1141 eklskriglt narifvqgrn lfritakgvd idpettefnv sggtgagtdq gftslplpre
     1201 ifiglrfgl
//
LOCUS       WP_120260898             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120260898
VERSION     WP_120260898.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111215
     Region          69..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqfyminla ffmllfessa vkagdpgltp gpkiakerag rarmksksnv dsltakskfs
       61 tipvlgsdti svvelskypl vtleqilkgn isgvyvqeps aepgtvqqnm lvhgitrpvf
      121 tarnfkenrp livvngiqii detsliyniq neetqpigaa tnilslfdld niasievlkd
      181 agqiakygpr avngvvyvtt ktaqagdkki singysgfav pnnittvnae ferdfrqtfy
      241 dkyagaeqia aypsylsdss ntnyygpsnw vdqyykltpl ysingalmgg tnrsnfrffa
      301 nhtqnasgad dtkfnrtygg fsinmlpttw fkvsgniqig rlardrnrsl terytetkyt
      361 pdlstplapn kslynlylrn fdkltldnny ntsvlaslgl dinimpgldv tsrialdyne
      421 nrrdvfwpst lmegnnytsn ylgynerlsf dnnisyvkel ntgkllfeag lqiqadrqky
      481 nylqayrgpn dyikinkveg dknkanylvs igfipyiygd ktihhlinty frttyewngl
      541 klsglirrdg sswqqlserw ytsyavngey dlsskiendk idilkfrgsy ghignlpnsd
      601 teaagpqyss qlswdkntgi msyngvgtvs rpysygwvgy dvpwsftdmy nigvslsmak
      661 qfglhvdfyn kttknmllpv ptvaesgykf eyasgmdvqn rgvdvslnyt mprstggfcw
      721 nsafniaynt nelkklpnql daivvgknkl qvgeridqyw llqnrgsyqs daevpvrdgd
      781 nrvmtyngtd mkggdprwvd qdgnfdinne drilmgniip kwtggftnqf ayknfdlsfl
      841 lyfnlgreii nqqaskkydf anvaesknly gvreitswek sfdetaypiy npwssvvpyq
      901 aeqdlfmedg sfvklknlsv gydltkvvnn kklnrlyvyv tgsnlltitk ysgrdpelvn
      961 fygydtgtgi rypkmytlgv kldf
//
LOCUS       WP_120260901            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120260901
VERSION     WP_120260901.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118086
     Region          24..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkryiilisc vltsvmshgq tkvtvkgmvl davtnrpmvg vsvrsaktdk vlsasgstga
       61 ysvsttsndd lifsftgyta srisltgrns fvinvkmsta qnmleetvvq gfsrrsrqtl
      121 tgssvsisgk dlqdnpvani tellqgkvag lnvqmnngtp gtrgtvllrg lsnlgtvgsg
      181 vdtyliptsp lyiidgvrvd dntnfeygyg gagtgispls lippedieev qilkdaasts
      241 lygtrgsygv ilirtkrgrs evpriqyttn qflsippnlr nvlggkderl srinqvynya
      301 dsywqgrddi nkhqvltdsl npyfnnstnw qgvfykptyn qshnisasgg ddkfsykvng
      361 nyykengivq ntgfnrytld mntqytpner lrlfasmsgk igeqqlgggt svsqggvasa
      421 atassllpsp sqgfvtsdli aalngrndnk stnligmvel efdilknfra kntfsynyst
      481 drtdtykpai annnrssfyn ydsqtnslnn mfflsylkei gkhtfntyvf neldmkdnlr
      541 keylkdgfan dqlegpfgls aakggvtgvs dyrsagfgas fsynynlkyv vdltyridkt
      601 sttgaekpwi knpsvavrwn meregfmknl kdagyvnsla lrgswgrnit ptgtvfdafg
      661 kyiytgyfnn nptigfdwkn mpnadlkpat ttsmsfaleg dffdnkfnti qevyykqven
      721 elmqidmadh nafgkqqsnd lahvtygyef tlayrpfdrg sdwnwrieln gainkealte
      781 lpnsrrlhia ydeayntyhq ayilgrnpfs hvlydyrgvf stdgdvpvnp ssgermkmin
      841 gntvyyfqgg dpnwtdvngd yiidekdmvy vgnsqprvtg ginsflsykn wslnmmfsyv
      901 rgrdiinevl atqlnsyfdp fmtdkdrngr qnaallpldr ydfwlregdv atypnpfdyq
      961 rqggmkpfrp nqtlfmedgs ylkfnsatlr fsfprewikr yklhglntyl tanniytfts
     1021 ykgvnpegvs smgydrsdgy pnrrsftlgi saqf
//
LOCUS       WP_120261050             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120261050
VERSION     WP_120261050.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110269
     Region          64..975
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrlfcflfl vpmcpnvkan hlnfwaskqd tseinevdkr llrgrlatll qkqgvrdsln
       61 lrnvetlpvv sipevlkgqv aglyvqeatg epgapknmvl rglgsplfei kdainvqpav
      121 fvngipiard nnfaysiqqy qfnrigpgtd nfagidlatv esievikdpv klaklgplaa
      181 ngaiwiltkp gregerqifi ntyvglatkp vvtpvnaqye nmfrsvfynk ygsatdrlny
      241 pgylsdstnv nyygpanwne eyykttpiyg gslgirggnd ranfsfvggy tknassadkt
      301 nierynalfn vnmapfkwln fgatinasrs lrdrnrslrd rfgeasyvpd lsvpispgkd
      361 myaqyldiyk aaldkntvnf lnslvtldly flknlkfnts lgidysegar qaffpgslme
      421 tnnymssyfg fnqrlvynnr leynlefqeq hkldltlgss ytqdlyryny araydgpndf
      481 ikvnvvdgdp qkgsylvpig glyvnrysnr edfrlhslyl aanykyknll dlnavlrydg
      541 sstmqpdsrw lmtpsfaaky hlipenednl fnhlgvkasw arigkpvfts kfaigpnyta
      601 dlnwgseksl vsyngfavas rpysegwvgy dikwpftdha eltvdgtlle kkidfevsly
      661 qkkdvnqlin spipaeygys gqivnglsvk ntgvdlnlsa kvlsnpetlq wntslnlnyn
      721 qnkltalpgg rkqlkvgnrl lkvgeaidqf wlyenqgsyd tegsipvqng qkiqfdgvdf
      781 aagdpiwkdq ngdfkinded rvlkgnampk ltgsfqnyfk fkgfdlnmqw yfalghkaln
      841 qrasnkynfv ntentnsldg irevfhwqqd vdlnkypiyn pwspivayrv dqdlflenas
      901 flklrsltig ydlaqlnnvk dkmktirray vyvsgtnllt iskfsgadpe lidfngyytg
      961 yglplspmvs lgvklel
//
LOCUS       WP_120261055            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120261055
VERSION     WP_120261055.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116534
     Region          23..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrilpmitl vllsyfhvfg qsipvegivr ggkgqplagm tvtergttnq astnqqgsft
       61 lsvkslpitl vysgvgykkq evrvttqqap svvlssddss lgevvvvgyq kqsvkkttsa
      121 vqvisgksie dlpapsfesl lqgrvagvni qnftgepgar ntftvrgntt ispdlnsevd
      181 lantmssply iidgmplsvs dlggssatgt nyiaginind iesivvqkda aatavwgsrg
      241 angviviktk rgrvgipsir asyyrgiter pqlqrtlgga aerrtkmdil sqyaswsqmg
      301 gftqpltdsl nssynnatdw qdlfyttgni dnadasisgg sesvnyrlsa gyynedgvvr
      361 ntgfkrysir gnfgftlspi iksdfmvsaa rinrkrglgr gidqvvpvnq gempssfvgl
      421 gqadydfylg qydklkddnq tdninifskt yvdiidglqy slegsvqanl dsrnqfqpre
      481 lnqginyaas tgrnaytyni anvlnyiktf ndkhtinlta lqsfqydkql shktegfnlp
      541 tddihviqgv atkdliastn kvesgllsym gqfsydyksr yifnaswrad assrfgvntk
      601 wgsfpalsga wvisdesfme kfdwvnlfkl rgswgrsgvl pedfyapynv walssdtyng
      661 ttfavpsfak pltlknltwn kseqtnigfd lglfndrltv tfdayrkvlk dpimgfsfpy
      721 ytgytklsfn vpmsvynegi dltimtknls ktsalqwntn lnmtfnknri gslpfgdrsf
      781 yadsrgynqq llytvgspiy rwaqmlyqgv yshqdqipvn pvtgkpltvf kgnypvkpgy
      841 piwtdvnqdw dtwsdedkga adgdlmltgn pnpritggly nefiykgfsi smlntftigr
      901 diinnlksnq fnaiggnvtk ftnnrlpdle gldywtpeka kdpnyqanfp sispygsyfy
      961 qylpfstmfn engtyfkikt isvgyllpkh iverlkigar nirfygmldn lhtfqkasvp
     1021 daelvtpqge ysggayplpr kytiglevnf
//
LOCUS       WP_120261189            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120261189
VERSION     WP_120261189.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117012
     Region          66..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfnqpslhlp kiavltcilt tlsakgfaqs qtfqgklids vsqdaihgat irnshlsklv
       61 ssdqagnfsi qaqigdtlri gfmgylpksf iisnqgplqi slspnqqsln evvvtalgik
      121 kekqaigysv qeikgkdlvk arepnaissl agrvsgltit pstnlfgdpg itlrgrsnil
      181 ivvdgmpint dswnlspddi esysvlkgan aaalygnrgq ngaivittkr aktegkgfqv
      241 efnsstqlqt gynaipkiqt eygpgsnfqy afkdgrgggi ndndyniwgp rfegqlipqy
      301 nspidpktga lvplpwearg kdnlkkflqn gllstnniai ssktergdir lsasqmfqrg
      361 ttpntklggt ninltggina gsklridasi nynkqyspny pniaygpnsp iyiltlwgga
      421 dydindlrny wqpgkenvqq ynreytiydn pwmtayenlr tydkddiygy vsanykwnsh
      481 lsfnartsas twnrnrtiki pisanlynyn iggsrvggyq etydtfwenn tevslkyqnr
      541 isedigftgs vfgnlrtvsa kslfartdrg ltvpgvydls nsvmptvstn dralrqvgst
      601 ygfvdldykn mlflnltgrf dksstmpikn ntyfypsasl savisqmvsl pkvisslkvr
      661 gayanvasdf vnetaqydiy kllpaytnyg rwansmtgvt ytdvlpnpdl vaervktaei
      721 gletrlfnnr lgvdlavfrn legpriiela tsvtsgvkar qtngltllrk gielsidata
      781 iqrerfswnv lvnastnhaw lhdidghqtr sgdvrigerw dsfyvndfqr dekgnlivgt
      841 nglpaynpyv skigysdnkf tasisnsfry rdfnfsflvd grfggliknv qdakqwgsgt
      901 hpesansyrl kdwenrdskd ykgsvmtegl kivkgqlstd qdgkiisdtr efapndipvl
      961 wqnwatnyyq sgpisakdrt fvklreivfs ynlptsllkn srflrsasvs lvgrnllyft
     1021 gkgtknmdld qftaassdyq tpsvksfgln inatf
//
LOCUS       WP_120261358            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120261358
VERSION     WP_120261358.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117368
     Region          25..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqfsiiltf icalfvgdaw aqtmvkgvvk gndnralsgv sirlenpkrd lgktgedgrf
       61 visvpnsgvm vfsyqgyrte kytivagkke ynvtlestaq eleetvvvgy qqrkretltg
      121 svvtisgkei qdipsgnfvd llqgkvagln iqnntgspgm rgtmavrgms nfnvsgsgdn
      181 tfvtptsplf vidgvpiddn sgyeygfesa gpgvspismi ppedieditv mkdaqatamy
      241 gsrgaygviq vrtkrgnskv pivqyqgqff lsavpqlrrv iggkgermvr ldqilmndtt
      301 laaairrind spiladslnp yynnstdwqs yfyrntmnqt hnvnisgger vfnykanmny
      361 ydengiiant gfkrytlqsn mqyepsdrfr mmtninvnva qnkmgsgnal mqtgvgksvn
      421 ttslypspsl fsgsmgalsa lgvddqnktg nyvgqlelqy vpikdlrasv tlnynyttst
      481 kdrytpeill gnssevysyy snkskvynrn qlsyvkaikd khlfnlygft emeisassed
      541 lskirgtand qfqtgisynt rntlggllns lnnfrsvaya gsfsynydsk yildltyrvd
      601 gssltggatp wtknpsaglr wnfkkekfme nvdwwdtgfl rgsvgrtisp sgslsdiygw
      661 ykiddgrynn rpttsldlei apntglvpqs ttqwsmaael gffnsslyvt yetyykqsdk
      721 ilrkkpianh nafanvltne samvnrghel siqyrpklas sewelnanat fainrdyvts
      781 lpdgarqlvq pdgsgydlpq fyrlgrnaft fvlydykgvy ksddqvpvnp ltglryragg
      841 emnggkffra gdpiftdlng dyvldendlv yvgnsqpait gglylytryk nwslrtqlsy
      901 tidrdilnta ltdrfrnysd psgqnygdga pgayvplday nvwrqlgdna dypnvsdftr
      961 ltlynpyryn stmfmedgsy vkintitvgy nfdrrwarrf gvssarvnlt annvytfsny
     1021 sgpdpelvtg vgrdgsngyp srrtyslgvs vqf
//
LOCUS       WP_120261467            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120261467
VERSION     WP_120261467.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112148
     Region          26..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfykkatg lalctifsas alyaqqtitg kvsddkgpvs gvtvavkgtt katqtnasgs
       61 fnidaapget irlsivgykt qeivvgstkt invtltadas tlgevvvtam gikrekktlg
      121 ysfqevkseq ltdaketnva nalvgkvsgl qvikgsagpa sstkitlrgn nsltgdnqpl
      181 iivdgvpmnn flggmkgngd knndmwnpat dmggglgdin pddiesmsvl kggaasalyg
      241 sragngaivi ttksgkaqkg agitysstig letifmtpkl qnsygqgkdg vynpisttsw
      301 gdkatkvydn igayfntgvn htqnlafqqq lgetniyssa tylndqskip gsslerinlm
      361 tkvtssfgpd krwttdvkvq ymnmnaknrp isgqnnsnvy stlftmprsm nildfknpln
      421 avgdmawygt senktmnpyw lekyrlnndi rdrfimngni kykfndwlda earfgrdqyt
      481 tnyenktygg splitggsyg vgkntffenn ftvalnarkd nligkwggsa svfgqimktr
      541 stgidastge lqvpnlfyin nsksfptieq sllqkqinsl yataeinydn ylffnvtgrn
      601 dwssalgldn rsffypsvsg swvisdmink tggslpswls faklrgsyae vgndlpsfql
      661 ynvynigkdp ngnttagmgn tkyspsilse liktiefgfd trlfnnrlgl dfawyktnat
      721 nqlidlpmnp ysgyeyekin agniqnsgfe ivldgriltn kdqltwnssl nfsrnrnkii
      781 sladgvdmyp lgsydnvsir alegglygdi ygtkflrved pnsefngqli lngsglpqaa
      841 sglhklgnqa pkalvgwnnn fayknfglsf qvdgrfggef fsgtnlnlqa ngnaevtapn
      901 gernpfvvdg viasngsytk ntiqttqqly wtqvtstsgn ygiteqnvyd atnirlrnvt
      961 lsynfpksil gnsivqrakv sltgnnlwmi ksyangvdpe svfainsnat gfenfstpts
     1021 rsfflnvtlg f
//
LOCUS       WP_120261463            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120261463
VERSION     WP_120261463.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118083
     Region          28..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfykrtag lalctlfsat slyaqqsitg ivsdangpis gvtvtvkgtt kgtqtiangs
       61 ftiqaaqget lrisivgykt qeivvgsnka invtltsdaa aldevvvtam gikreskalg
      121 yavsnikade itkagntnfg salygkapgv kittapggsa savnvqirgi nslnyqrqpl
      181 yvvdgiiirn dqqngaagan nnnfdrdqri rgngmldinp adidnisilk gaaasalygs
      241 daasgvivit tkkgtkgrgl gvdfnytgsl eraaflpkfq neygpgydag invtngatae
      301 gwildpksps grrpyfrsya sfgpkftged vlwwdgqvrp yvarknnyyd vfdkgynsta
      361 nvgisnqtek lnyrlsatrm dykstspgsk qtkntfnlns slklsnrlst divanyintn
      421 thnrtyllgq vlgsfdgffs rtedmaamkk ayqtsdgyky sklgtgrped fiytmrasnl
      481 ldyfwnqykn sydevenril tsatlnwdvv dhlkfrgrig ndftsatstn kqytenatky
      541 nspssstggy sttkgaysil ygdlmmtysn kinenfdysa svgfqsrsen yddqssstas
      601 glvtenwfsl snslaqattt narkemlkya yfgslnigyk gfayldgtyr seysstlptq
      661 nnnyqygsls gsfifsdafn iksdkftygk lrasygivgn daaiyeania ytqaplltvn
      721 gaipaltykn rygnldlrpe rkyemefgle lkflknrlgl dasyynnyie dqilglttpa
      781 stgatsqlln igkianhgle lsingtpiqn enftwtsrln ysfnrskvke llsgvdelvf
      841 ysadanslki takagetlgn iyvydiakda ngnnlisdeg fyvmdkskyk mvgnimpkai
      901 ggwtntfnyk nfsldftady rfggkmvsen lkygmasgly entlpyresg itlpgvnant
      961 gktndvhlsg aeyyfntfnw gddswsekga vydnnfiklr elsigyqipd sftkrikmnn
     1021 lrfsligrnl fyfyrtlknl dpeapvgnaw waqgvdvgss aatrsfgfsl hanf
//
LOCUS       WP_120261470            1123 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120261470
VERSION     WP_120261470.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1123)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1123)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1123)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1123
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1123
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123398
     Region          28..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfqkraag lalctifsvt slyaqqsitg tvrdangpia gvsvsvkgtn ratqtnengs
       61 ftiqasqget lrisivgykp qeiqvnatkt idvtlsndds sldevvvtal gikreakslg
      121 ysvqkvggre ltqtnaptva tglmgkvsgm nismsngveg gsqrvvirga asltganqpl
      181 yvidgmpidn nqitskgndi tkasgsyqdw gsilnfinad diedvsvlkg ptaaalygar
      241 ggngvvlitt kkgklkeglg idynysfrsn dpyryqemqn kygyggaial ysaiptlpvd
      301 angqlrypga dpwsgtnitd qkwlshgtvp ggkntwdyfs wygtgaswga emkgqeilww
      361 dgtkrnyspq pdniqsfyrt gntqthnvaf sganelgsvr lsytrqnnts iipnsnfnnn
      421 tfnlgtnvki skkvtadvsa syinfyrlns pdvgnsdnsw gkfstygmsr dyknlekdiy
      481 rnpdgsknll dgsvynmgyp yggygrnqyw nifmnnteln rdqllgtvkl naeltdwltl
      541 mgrasgnfss defdkksypt dkeglqgkyg helykttdrn ldflatvhke nlngskfsgs
      601 fsfgasswks nyrgiqgfnd gpfndpflfy laninkngsv sgfipteerm eqqinslfgi
      661 anisydnflf fegtfrndwa stlpsktrsy nypaaslsyv ftekwaskps wfdygklraa
      721 faksaigtkp yqtsyiygtg tfngqpirki snnllpvdll kpqrstsyel gtdlsflknr
      781 lgltftyykv nstdqiidln vapssgvtgv rtnsgelqnq gieftlrgtp iktqdfswdl
      841 tlngahnrnk lvklapgine yyldemfgsy gvtmkvkvgd nfgtiygsdf eyyensdrrl
      901 vervldgkgn ptgtrykvtg dqvpignanp kltgglgtnl rykdfslyal adfkwggdiw
      961 sgsystamgn glspqtller dggglpytyp dgskanhgvi ldgvfadgte nkdvvhymwk
     1021 yagsyaawsd ikmprslavl enswaklrev rltyqipksv vqktkffqgm sasligrdlf
     1081 yiytslpenl npeaingign aqgiefgalp gvrsfgfsis asf
//
LOCUS       WP_120261864            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120261864
VERSION     WP_120261864.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115650
     Region          45..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrgsmhaqal mtlaltlnla ptiaktgsks isfanhgnsf vvfqqtirgk videkgqgig
       61 gvtvrnstag ttaqsapdgs fsiaakpgdq lefssvgydr qrntvsgsgp ltivlankst
      121 vledvtvtgy tnyskkqsan vsttvkakdl eqvpmasvdq mlqgrvpgms vmassgqpga
      181 tasvvirgig singisdply vidgipiats elknfsandf esvnvlrdat gkslygsrgs
      241 ngvivittkk gksgqlavnf nsqyglsklt rpkfqmmntq qrlqfeeelg pfvdpdnneg
      301 igpgwtyspk npevaggtsa ykaraaqild slrginvdwr dyffrngkfm dqqvnisggg
      361 ehvrfyssag yykqegvair sgldrytlkn nvdfdkgkls ggvnvtlgyt nskftegvga
      421 srvgssmasv yyalpyeypy apdgtlihfg neddyfildq regsaglerl lnssssself
      481 ntnvglnlny qllptlkvht rlgidynttt gqdyinpdsy ygsrdrdptl ggkglfaedn
      541 lrstnvistt gltyqntfde khnlelsayf eylyrrnraf gykgygidsr lpenpngvtv
      601 sptylpailg grtkyalasy malgrytydn rysltasyry dgssrvaean rwhgfysfga
      661 nwnvkeeefl ksnefiqgls lrasygttas tingdfnyla tfrkditygg etairpydpg
      721 npnydweyvd efnagfdlel fpskrlrvam dyynkitknm ffdqpislts gfldrklpls
      781 tgkmrnrgve mslsgdvikr edwgltlgvn asynkntily lsdaltevld gdtrimrvgl
      841 pygtyyapew agvnpqtgda qyynrdgsit teydetsqav tksgsmfpkw vggfnttvrw
      901 knlsldalfa fvsdvrrwnn edfynenssy mtsnqsirml tdrwkqpgdn ailqridipr
      961 eytskdiqda sflrlrnvnl vyqfpktlfg dqkvikgari ffqgqnlltw tswrgldpen
     1021 segisrfnyp aprtytagfs vnf
//
LOCUS       WP_120261896            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120261896
VERSION     WP_120261896.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125550
     Region          117..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtnyylkl mggallfqsl alqtmatqfk tgegigkila kmeqkfnvkf gydasisdqk
       61 inelvnlekl kkeeiaqfir tisdghlevr kiddklyvvs kkektasesk klhaaqkelr
      121 gkivdqetnl piggatirvk gtaiaattdq mgafklsnvs dqailqvsfi gyelsevpat
      181 saslirlsks sealeevvvt algikreqka lgyavqdikg dqlakvkgvd vgttltgrvs
      241 glrvmnstef nrapdiqlrg kspllvidgv ayenmslrdi avdnienisv lkgstaaaly
      301 giegaggaim vttkkglsqk gveitvnsnn mffagylalp nvqssysagy ggkyntddev
      361 wgdkldigrk ykqwnpftkq mddvetelts kgknnfqnfl epgfisnnsv sftnqgengs
      421 irtsishiyn kgqypntkln mtnisvaget kisdkvnlet rlgynrrhap ndfgsgynnq
      481 gyiynilvwt gpeydltqyk dywqtenvsq nwlykawydn pylsayekis aelvnklnaa
      541 vtlnykmtdw gnfllrsgyd yygnsreqtn pmgiygtrgg fdgsggydnr gkywsrkqdg
      601 fsttndfift akknfgdfgi dalvggsify rrdntmtast vngltipgfy slrnstgpvs
      661 avegktkemr ngiysrlsls wrnavfiegt arndwysmlp dksyfypsvs gsvvvsdliq
      721 kpnwlnllkv rgswastvyp pdpyeinqtf gvsnnvwdgm ttasypniik dysinptked
      781 maefglewav lnsrltgnyt yyarrrynik adisnsnysn ishttgfrar linlkeermt
      841 rgheislggv pirrenfews vngnlsqnlq yyhkldpdyt adalyikegm rtdhyvtrdw
      901 erspdgeiih naagmpisav htarlfgyta pkwfwgitnq fqykdfslsf sfdgrikgls
      961 ysnmnarlwq tgahpdsdtk eryeevvngk rtfvgkgvki vsgevsydky gqiikdtrvf
     1021 apnetvvsye nywkraysgt qniwdetfik lrevslsynl prevasrfka kkasigvtgq
     1081 nlflwtkeyr fsdpdagsed lnspsmrylg fnislsf
//
LOCUS       WP_120261473            1101 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium detergens].
ACCESSION   WP_120261473
VERSION     WP_120261473.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium detergens
  ORGANISM  Sphingobacterium detergens
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1101)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Sphingobacterium detergens"
                     /db_xref="taxon:1145106"
     Protein         1..1101
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121743
     Region          26..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msvfykksag lalctlfsat alyaqqtvsg svsdktgplp gatvsvkgsi aktltnehgs
       61 fkinaekgqt irismigykp qeivvgsasa ikillesdes sldevvvtal gikrdkkslg
      121 yatatvtsdd llkagatqnp flamygkaag vginigsggp tggvnirirg aaglesgtnt
      181 rplfvvdgvp lydestsmes rgydplnsfd mgsgindlns ediesieilk gakatvlygs
      241 qalngvvlvt tksgrktrgl giqvnqqisi dkpftyidfq ndygsgastn diqyadingk
      301 kirklplsrf sfgpkfdnsd imlydstmst yhaypdnfin ffktginnrt niavsgggei
      361 gsarasyttn tyndilpgfk qkqntfsfng nfmpskfasf efvnnlysvn tknrrpniqq
      421 wvatglnrdy dynwikgfyh daqgyrkdle pyglaggspg fwpnatsnil weqndnldkd
      481 tkfhlvssik ttlqfsphvs figqasidyt ntdvvtenki trmvpdrigg gykwtkrntt
      541 vqnyqglmky ensfnkdwnv fgfiggayqk itdnnmftst gnmgllypdw yslnnanian
      601 wptagargqv mgngrgsdvl ysmlgsatis ykeshylelq arndwnstlq spnnsyfypg
      661 lsytwnfsnd fkipklqygk lrvawanvgg gpstatgdry fannvfsvgq lpysygpvtv
      721 tppsslflem ikpfrkreie igfntrwfqn srleidysfy nnntydqiis qplssstgys
      781 sakintgnlr nwgheifika apianekfrw dltftaanqf skvialypgi tqkyitgnsg
      841 fqvfaeegkr igeikaydyk rddsgnkiig pnglyqlsdd vsyigknvnp difggfmndf
      901 ffkgfnfhlg ldykfggsvf sytnnylmgt gvikqslpgr deenggvayy idknnkfiqt
      961 qhnaaapsds kdgiiyhdgi ildgvmesng syvknnqivs aptyygtyin dlgtswppdr
     1021 lfkndyikfr eisvsytipq qwannlklqk ltltaaarnl gylyksipni daeaalgaqs
     1081 yiensfypsv rtftfgvnvs f
//
LOCUS       WP_120269624             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Stappia
            quadratibracata].
ACCESSION   WP_120269624
VERSION     WP_120269624.1
KEYWORDS    RefSeq.
SOURCE      Stappia quadratibracata
  ORGANISM  Stappia quadratibracata
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Stappia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Stappia quadratibracata"
                     /db_xref="taxon:2762596"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39355
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklavprese agetrvaatp dtvkrfvslg fevsvetgag tlsrvvdady qaagatiakd
       61 akatlegadl vlkvrrpsaa elglmkkgai viatmdpygh edavkamaea gisafamefm
      121 pritraqvmd vlssqanlag yqavidgaae ydrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqveslg akfiavedde frqaetaggy akemsdeykk
      241 kqaelvashi akqdivvtta lipgrpaprl itkemvasmk pgsvivdlav erggnvegav
      301 pgkvaqvgev kivghlnvpg rlaasasaly aknlvafaet lvdkeakaia vnwedelvka
      361 tvltrdgkvv hpafapaag
//
LOCUS       WP_120271677            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120271677
VERSION     WP_120271677.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110721
     Region          22..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklpilfli fslmaaapai aqkitgtvis ggdkeplpgv tvlekgttng ittdfdgnfe
       61 fnlkdasdqv lvfsfvgyqt qevpvngqtk idvvlqesdi avdevvvtal gikrdkkals
      121 yssqtisded iantqgvnfa sslsgktagv elressagag gstkitlrgt rnitssnqpl
      181 fvidgipman yqtsdasgfy ggrdsgdgls ninqddiesm tilrganaaa lygsqgsngv
      241 ilittkkgkn gttkatfssn tsitqafdlp dlqykygqts egsesswgee gdyddsfvkd
      301 ffqtgvttkn gitlsggndk tttyfsysna ysegvvptnt fkknnltfkq sskffddklt
      361 vtsdvmltqq kvhnkilngy ywnpllglyn fprsldfddy knnykvwdsd rnmwtqnwai
      421 sgnsegemnp ywilykdqnd ektnriignv sldyqlaegl nlsargsydy trqiyelkan
      481 agsssvlvsd ngryiysnle syqaygdlml tydhslsddl dlhavigtsy qnktigdgva
      541 idsdtygltl anvftiqnis sikafssgnv mdsrlikesa fanislgynn mlyldlsgrn
      601 dwssslaytg nlsyfypsvg lsailsqmiq lpeaisfakv rgsyarvsne ipafktnpvn
      661 gvdvdnlisr nsvtpftdlk pemqdsyefg lemrflnnrv gldasvyqid tkdqylelda
      721 psgsyydtyy vnaghirskg leitlsttpv kgkkfswdsn vnfttntnki mklsddldgy
      781 ytmggggegy dmyvveggkm gdiyvyqyar dddgniildd dtyvptkntt krkvgnaspk
      841 wmmgwtnsfs ykkfnmsfqv dgkfggnfvs mtnayldang vsqatadare aggvkvkgvl
      901 sdgsayegtv daqtyytsta gragimeqyv ygstnvrlrq vslgynfdlq kytnlinnin
      961 lslvgsnlff fyneaptdpd itistgngsq gvenfgapts rslgfnlqvn f
//
LOCUS       WP_120271780            1130 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120271780
VERSION     WP_120271780.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..1130
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124141
     Region          27..1092
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkgllqtli vglfafisis syaqsrvtgt vkssdgellp gasvvikgts igvitdfegr
       61 ynievpqsdv vllfsfvgmd akeeplqgrl svdvilqtss igvdevvvta lgisrasksl
      121 gysvsevsge nlenatqenv lnalsgkvpg vtinstgaag ssvsmvirga tsltsdnqpl
      181 fvidgvpvnn tlnnvssigs dnnvdygnai sdlnsndies msilkgpsaa alygsragng
      241 vvlittkkgk kakglgvsis sstvldipyk yvdtqslfan gsrpytptny psnsygsmvi
      301 aedasgwvgp elnkgytaiq wpytpeeles gipvskelks ynnaenffet gitstnsvsv
      361 anqtdkinyr vsftnmqnkg yipnsdlhkn sissnislnl tdnftissvi nyskngsdnr
      421 pagnrganpl qalyninshi nvldmkdywe egkegiqqss pytwgdydsr efnnpyflan
      481 evnnsfnrdr ifgnidaswq itpdlsvkar yahdefkekr etkiaysyte eangaygiin
      541 lerferntdf lvtykkrlde vdfsvsaggn amyqkgsnny mttksggsgl itpgiysltn
      601 ispdnldygs swwekaiysv yalasfgykd mvyldltarn dwsstlpedn rsffypsasl
      661 slllnnmlal psdvsllklr ggwaqvgndt dpyklypvlg negawgnvtr lsasgellsp
      721 dlkpeiqtsy efgadlnfyd srlrlsgtwy hsdnknqvls idlpassgas skqinaglis
      781 akgweatlgl tpiansnwkw dlnfsftrnr tilkeladgm tyiklwgdak ggaytwvgde
      841 igqiidrkmv rvedpdseyy gypildsdgy dqsnskvydd dgnrvapvig nfnpdlmvgl
      901 qtslsykrft lsanfdwrig gqfvsqtlry gesdlhsqrw ldrtlklnnl ddipaylkeh
      961 adeylspdgm fyvvvggpta dtggfehteg gitlndgvfm pgvyeddngn yvenlgggdt
     1021 kyvryqdfyg wsytrtatfd adfiklrdvs itykipekiy ssigiqnasi svfsrnlilw
     1081 tkakinidpe nafqpesstq asgiqfkqgi erynvnpwvi pvglklnlnf
//
LOCUS       WP_120272129             954 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120272129
VERSION     WP_120272129.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..954
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105435
     Region          66..953
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnklrltkpl caliilmciv ptfvsaseth asklssvess vqtfaddslk adslhfrvdl
       61 ldlkeslned vlrkfpqlnv adflqgtvag levlnstsgv ggsvavtlrg qrslsekstp
      121 lfvidgipmv nnlgeqpnmw ggldegdgls qinpddiasi efikgtsgav lygsqaangv
      181 vlittktakd eqlrvilnst tlfekviwep elqfkygtda eteswsmtag nypdnyvsdy
      241 fgtgmtaqns iaisgggkns tlyatfants akgvvennry qrnnfalrnv shlfqnrlni
      301 qagisyadet vknryatgyy lnpltglylf prnggvpind malgrqpfsy fksnysipnt
      361 ytsadeqnwf vydhlqsnpy wllnkqpqed qtqrllanls aefklsgdfd lqvrsgydya
      421 dksfeqqyyd ggnpinigtn grwrykkytd kliyldgslt yhhrfnklgv eavaganykk
      481 tdfnngyqid sgitglnspn iftednlpsn igredlyhwe leqkgiyasv aldynrslil
      541 elglrndvts siisegheah wfptaklstl lnewinfpav vshsqvyisa sssyrdlsss
      601 lmqlyghsai tssnsvgptd dlspekikaw eagtnwsfwn nnlsvdlayy qttnsdqasl
      661 rsasatqqsf ylyifvnmgd ivnkgfeatv aakpitgsdl nwqtklnfys ntsevkdlas
      721 nnesyfvdlg stegyysrvy aggkigdlyg ykflrnesgq lvldestgtp rktssieylg
      781 nlnpdfclgw gnslnyknis ldlqlnanig gkafsqtesm ldgygvsqrs aaardkgyva
      841 idgiqgetlv tqidpelyyt tvggrngige nylydrtnir laqaalayhf nveslglplk
      901 aasvslvgnn lfflykkapf dpemalstgl gsqsmdsfsv pasrmygfnl rvtf
//
LOCUS       WP_120272131            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120272131
VERSION     WP_120272131.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111798
     Region          22..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklsllffv lvllgtvsam aqtvtgrvvs egdneplpgv avlekgtnhg aatdfdgnyt
       61 fnlqnsegav lvfsfmgyet qevsvdgrss idvvlksnni avdevvvtal gikresktlt
      121 yssqevsgee mmkardvnfm sglsgktagl eirksssgag gstrtvlrgs ksvnsvsdpl
      181 yvidgipmvn nkgdqagmwg gtdegdglsq lnpddiesis vlkgatasil ygsqgangvi
      241 iittkkgkeg kttvsfnssa ifesvietpd lqfsygadgg taeswsytkg nyesdyvddf
      301 fetgynlint vsvssgnekm styfsygntg aggvvpnnsy qkhnvtfkqs akmlddkltl
      361 tsnvmltser sknrpgagyy lnpltglylf prsgatplsd sslgaqpfsy fkdnyqyfmt
      421 srnmnwqewh ikadnqsnpy wlinkqpktd ltkrviaslt ldyqiteklk fqargsydya
      481 nktfeqkfya ggntvnisen grwnykkfad kqlysdgifs yqnefgdlsl savagasyqe
      541 svygdgvsvd ngtndllypn efyfqnvpdn vaiksiyggk iikegvfgsv qlgfkdmlfl
      601 dlsgrndwss tlaatgnesy fypaagltgi lsqmvtmpef isfakvrasa sqvnnevpwg
      661 liqvnhsina sgsvdrntvk pftdakpeql vtwelgtdwr ffngrlgldf tyyhitstnq
      721 alsktlsgsk qdnyytsmyf nageivnkgv eivlnstpvk tsdfewnssl nfsknnnkvv
      781 elypgepsky idlgssegyi nriytggsig dmygiqfrrn dagqillded gtplktasds
      841 pvylgnlepd fslgwnnsfd ykrftlsfli nakiggkafs qtesildgyg vsqrtadard
      901 kgyvavngit eesgtvmtqi dpqlyystvg grngiaeayv ydrtnirltq lalsydldvk
      961 slglplqaas fsvvgnnlff lykkapfdpe lsmstdlgsq sldnfnvpat rtygfnlkft
     1021 f
//
LOCUS       WP_120272270            1143 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120272270
VERSION     WP_120272270.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..1143
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126053
     Region          50..118
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          133..1141
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknglwysn syrinvplil kkmkltilmi clgiitsfgs vysqnsnltf kltnqslknv
       61 lseienqtnf sflyqaksin heqrvsidmt naditdildq lseqahfqyk ildnsvivlt
      121 gggesgsvqq ptkvtgkitd dtgfplpgvt vvvkgttvgt vtdgngeyil tdvpadaili
      181 fsfvgmraqe lpvagksnid vvleeesigl devvaigygt vskknlttai skvetddiqk
      241 sassnmsqlm vgraaglqat vtsaqpggav disirgggdp iyvvdgivmp ssslesgsgg
      301 sttvvpssvn rgglaglnpe diesvevlkd asaaiygiga angvilittk kgkkspmnid
      361 ysgsysfvkn ypytkslnat dymglvntfs keqylynhdm gaygnnaydn gwtpafsdse
      421 ianaksydwv devlrngavn nhnlvirggs ervtyyvsgn yynqegtvmn ssmerfsmrs
      481 nlslqltdfl klstianvnr nkygnssvgg assgrgsqaa galtaalsyp sylpikdedg
      541 nytqfsyipn avsmqdidda tnsdgtylnf iadialvkdm lnaklvygnn kemtdryvyi
      601 pstvyfdqmy qsrgniaydg renqtfeatl afnkefgefm nmdvvvgvgk ylnsskglsf
      661 aydtqndvig nddvsavtgn mnpdsykned ekrsqflran fdildryvia ttlrrdgtdk
      721 ffpdkkyayf psvsvawkmt nenfmknihw ldllklrasy gttgddnlgs slygtyspsl
      781 vikfdegnev yssyvqdgvd ypnvtwektv mknigldfyl fknrisgsfd vfrndvtdml
      841 gdantaglsm fgtypinggh irrqgwdasl ttenikttdf lwksvltlsr ynslwkerfp
      901 nydyndyqir ddepvnaryy yktagminad lsnipssqpe dyakagfpii vdnnndgeit
      961 vddvvmsnev pkiyfgfgnt ftyknwdldv fvysqlgvnk ynyawewada aslanqtnne
     1021 nkfafdlwss etnqggrlpg yayeassvsl pggagidvmy qnasflrfrn itlgynlsgk
     1081 qlgsvvgkwv knirlyvdaq npititnfeg ydpevrsggs qktfsaeypq artftigaki
     1141 nfn
//
LOCUS       WP_120272310            1088 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120272310
VERSION     WP_120272310.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..1088
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120673
     Region          25..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkikyliiv fillfsgmlq aqntkvlsgr vfemvngekq pipganvvva nnqnrfltgv
       61 atgpngeynf rvpaneegln iifsfiglks kkipytgqpt idvvlesedk vvtevvvqgr
      121 hvdrvtgite kqqtaatqrv dmdeimsvsp vtsleealqg qlggvdiisg gdpgakssir
      181 irgtstlnas adplividgi pysttisddf nfatanaedf gqliniaptd iesievlkda
      241 aataiwgtkg gngvlmittk kgskgktrft fssklttrfe pepiplldgn eyvalmqdai
      301 wnaanakgla nsqdlvqlly dtpeinyspn wryfdeynqn tdwldeivrt sivsdnnfsm
      361 sgggdkaiyr fsvgylndqg ttigtsldrf tsllsinynf sqklrvdvdy sftqteknsn
      421 ydsgssswrn arseamakmp nkspywiged gertdeyfsr qnsdefqgaf tgqknynpva
      481 lvnegyntss irenritfrl nyyitpelty tgytsmklss nrnekflpqv atgvtgvsay
      541 anrssdavsd gfnlitenkl lyrknwsekh nlvamglfrt eqaqgssyys qisgaasagl
      601 adpttggtvt degsgtsetr smsgianahy tfmerymvna tvnfegnssl gkserwgafp
      661 avglawqaqe edfiknlgwv dqakirvsyg vsgrspsgas pyigsfqald enymdmaaia
      721 pikiqldnlk wetskeldfg adfifmenkf kftfdwynkk tndllqknvs vpastgftti
      781 awynsgeitn tgielrgdye iyknrdwrit vnaninrnvn kivalpdnlt qesytfgngn
      841 yaqrletgvp vgsfygykye gvyqnvaety ardaagnimn dvdgdpivmq ngtlqafpgd
      901 akykdtnndg vinqydivyl gnsmpvftgg ggfqvkyksw tlttffhgra gqkvinqgrm
      961 ntesmygrdn qstatlrrwr segdvtdipr alynygynyl gsdrfvedas firlktlsls
     1021 ynmprdfvqk lgmqslnvfl tgydlftwtk yagqdpevkm psatnalvkd esstpisrrf
     1081 algvninf
//
LOCUS       WP_120272464            1150 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120272464
VERSION     WP_120272464.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..1150
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125738
     Region          52..1136
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtllrsrh yglkrslklm mvvlglcamt taqasspank tdlvgeqqnq gkvvsgtvtd
       61 sngepligva vavegtskgl itdfdgnfkl evpdensvlv fsfvgfetqk vtvgqlteid
      121 vvlkdniqqv devvvtalgi kreakalgya mtelkgddin inainpvdal qgkaagvdvs
      181 qsdggmfgst rilirgassl nsssnnqpif vvdgvilens tadagdadws stsgdygnel
      241 knlnpddfas vsvlkgapat alygsrglng aviittksgk aqkglgisvs qtfgvdyvyk
      301 qpdlqnvygd gaisgyvdyg etddsgsyya wgnqsqfyln sndekkfnqw gtgfgpkfdg
      361 ssilgydnkm ttynavknny rdmydlgfnt ntnvaiqggn dkttfyssvs ykhakgtlgk
      421 nefnrlsflt kashkladnv lleasvnfae stpknpqpni geyfisgtfe reydpsyykn
      481 kykgthggla nssvgdeyas ypgislywal nenssiqtet sfrpdltlti dlndwlkwks
      541 eanynyyytn revknpnsgi srtyelgagq ysmtqttkkq tnantalmfn kdvnadlnvs
      601 gfvrgeyydn tqtymytsts gglvvpdqyf iansvdnady dsyvtgkkrm lsvagqasaa
      661 yknrlfldvt grndwssamv ysdatgtysy fypsvslsgi vsdmvdlpdw vsfgkvrlsw
      721 aqvgndtray linsayslns tykdgdyiss eelsstmyet nlqpekktsw elgldwrflq
      781 srvgidatyy kentrnqims isvpsvsgvs sqlvnagnmq nsgieialht tpinngdwnw
      841 dvdftytrnq nkiislhenv adyilldgyt nygnyrigsv akvggaygtl mtdskaklda
      901 ttglpllsws dtrrfaymsr sgeeeeigsv npdflgsvss slryknftls vgldmrfggy
      961 vasygskygt aygyteaslk ysapeyggit wtsqydnqty sdgvvpegif aggtsitlps
     1021 gssytvadgg etyaalyekg viepthasaw tyfknswsrg vvnddwvkel nyislrqvsl
     1081 syncskqfas kigakslgfk lsghnlgyll ntapggenpe svrgttaysf rmrsysafta
     1141 symfsinasf
//
LOCUS       WP_120272570             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120272570
VERSION     WP_120272570.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40203
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigvlkdae pehrvalipe nvksllarkv svlleqgagt nafypdesyi eagatiltrt
       61 evleksdllv qisepdetli atlktnqvwl sefkplwhkn lvnaflragi ssfsmdavpr
      121 ttraqamdvl ssmatiagyk avldaashlp sffpmfmsaa gtirpanvli lgagvaglqa
      181 iaiarklgaq veafdvrsav keevmslgar fvevegaked aaaggyaieq teeykrkqqe
      241 aidqhaakan vvictaqipg rkaplliske vvarmqpgsv iidlasstgg ncelsednks
      301 vvhhgvtiig qsnypaqmpk daskmfgknv snfldllite dgqmslnfdd eivrgtcith
      361 qgeiinervk svid
//
LOCUS       WP_120273279            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120273279
VERSION     WP_120273279.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112603
     Region          32..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkvnwlrk cltllaaffl gvgallaqev nlsgivtsse dgsplpgvsv lekgtnhgtv
       61 tnvdgqysis vpqgatvvfs figmeikeit asssqtldvv ldpeteglge vvvtalgitr
      121 ekkslgysva evgsdevatv kdvnpmnsls grvagvtitq gsfgpgsssr vvirgnnsit
      181 gnnqplyvvd gipmsnsgyg sangsdtgey sksdygsgis dinpddiasi svlkgpnaaa
      241 lygsraangv imittkkgsa rkgvgvtfts nttfespmll pdyqneygqg tegyipstva
      301 dlksaggswg prmdgsnqly ytgetkaysp qpdnvkdffe tgstlintla ltagndevnv
      361 rfsytnteaq atipnskiqr hnfnlrgfak ltdrlsvdak atyfkqygkn rptlgteglm
      421 stlyniprnv dindyktyqd petlssvsat slganpywsv yhdqredwkd rlqgfakiqy
      481 dftdylsayv rvgtdmstmn ietvnqyghw ysttgafsyt esqeqetnad fllmfkkdlt
      541 dkinlnaslg gnhmystnrg hsvsgsqfri pdgpplsaas vvtagftple ekeinslygt
      601 vsfaydrwfy ldlsarndws stlpetnwsy fypsasasil indlleiens vlsyskvras
      661 waqvgndtdp yqlydtysla aasssylget tmsrsdvkya sdlkpedvrs ieiggefhff
      721 ndrlytdmsy yditskdlim nvpiskstgy symkenvgei rnkgfemmlg gvpvktddft
      781 wdvsvnfatn knklnelieg tddytfstin sgnvivkatv gggfgdiygt twekdddgni
      841 lvldngkpqv ssdkvllgny qpdwtggmtn tfsyknwkms flidarfgge vysgtdaamd
      901 aagtskrtla yreggvvvdg mlddgsanat sisaeeywga vssiaseyvy dqtnvrlrei
      961 sliwnlpskw lentivrnas igvigrnlff fykdtdnfdp easysvssfs qgvvyyplpt
     1021 srsigfnlnv nf
//
LOCUS       WP_120273439            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120273439
VERSION     WP_120273439.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109863
     Region          23..1019
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrliflfl scwiaimata qdrtisgvvq ekttkdplpg vtiqekgttn gtvtdmsgkf
       61 tlsvkpgavl qvsfigmesq evavgnstsl qiqleastee vnevvvtamg ikketkalgy
      121 avqevkgadl vkvkepnlvn slngkiagvn vtnsggapgs ssqiiirggt sltgdnqplf
      181 vvdgipidns avggdsstgg lsatstysan rgldlnsddi esisvlkgpa aaalyglkaa
      241 agaviittkk gkagvpqvtv sskfrmdvan kypeyqkmyg qgnngvaddg tasswgapvs
      301 gsiynnmedf fqtawsydvt gsvsggneng tffismnrsd qngivpttny iknsfrfnge
      361 qtkgiftvgm ntnyiysqsn ktltgdglyg ssgdgamisl ylwpvnnnms nwleggsrvp
      421 lvnnvepvdd vdnpywtvnr npvtddvhrf igsgyvtidp tdwlsgtyrl gvdhynmytr
      481 silypgsava dtytdgsvse iqrennilts nltlsankkv ndftlglllg hnyeqttyyr
      541 nkqqaiglls dflsinnade dnksysnyrs tkrlysffge fsadykgiay lsvtgrndws
      601 stlsaenrsf fypsvsgsvi vselfsdelk dkfsfaklra swsqvgkdap vyqtatylnd
      661 pvttvgggys nsytggnpnl kpettestel gldmrflkgr fgvdftyydt rskdqiispr
      721 vsmatgyifq yvnfgtvink gvevtltgkp vkskdwtwdt slnishndgt vtdlpegvtl
      781 lyvtdvqigp aksasigegd flgltgqrwt adengktild sdtglpitst datnivgnre
      841 pdlllgfnns itfknwnlsf lidirkggdv ynateyamvy sgtsketenr gttgqfsgvm
      901 vdsngdyqda tssveldqsy yqneyvadas hfitdvnwfr lrsasltysl pgsfcdklgf
      961 vksadislsg tnlllftnyk gmdpevsagg sgvvgagsta idyagvpatt svafgvnikf
//
LOCUS       WP_120273967            1098 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120273967
VERSION     WP_120273967.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..1098
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119610
     Region          23..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkialllai faiglqsvla qtkeitgtvt saddgstipg vsvsvkgttl gtitdldgny
       61 smkvpqdakt lvfsfvgmqt levviegatv naalqsdvvg inevvvtalg isrerkslgy
      121 avqevsgeev nntkgdnfvt slsgrvsgiq vknntnfggs tnviirgsss ltgnnqalfi
      181 vdgipidnan tnnsgqttgr sgydygnaaa dinpndiesi svlkgaaata lygsraangv
      241 ilittkkgkd sagkgpqvkv ssnvtiskid kktfpeyqts ygagygdyyy sdgdhpgley
      301 yadvngdgvt dyttpyyeda srgekfdasl mvyqwdalya dspnylkatp wvagangpes
      361 ffetgvstsn svdvsggddq ttyrfnytyf dqsgvmpnsh ldkhnlmfng shkildnlki
      421 tssanyirts gkgrpstgys dnimssfrqw yqvnvdlglq eqmykkthqn itwnpvaydd
      481 lapaywdnpy wvryenyetd grsrligyaq ldwditsdls amgrysidty eelqeerkav
      541 gsgagefgvd rpdvtsgysr ytkaftetnl dlmlnyhksf tedldftail gmnvrrtkne
      601 tvyastnngl aveglyalsn svdamlppee vfyrvgvngi fgsvslgykn tlfldgtlrr
      661 dqsstlpean ntyyypsvtt sfifsnlaea dwmslgkvrl nyaevgnsap alstkdvysa
      721 nspfsgtslv tlpntkknst lkpertkswe aglemnfvkn rvgfdlafyk tnttdqlmpv
      781 tvsyatgfss nwvnagelqn kgielaimgt pvkskdfrwd arlnwstnkn evislykdes
      841 gnqitnlqla sfqggvstna rvgqpygtil gsdfqyadng gkivsqttgr ylktstndqv
      901 igdtnpdwna glsnsfkykn lalsflidwq kggdvfsldl wygmgtglyk etaglndlgn
      961 ekrsaiekns dgtyastsgg tinpgvdadg npntvrvsnq nygadgwavs pnkkfvydas
     1021 yiklrevtlt ydlpksivnk lylenasigi vasnlwiihk nlpyadpeas qgsgnyqgwq
     1081 sgvmpanknf gftlnlqf
//
LOCUS       WP_120273443             981 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120273443
VERSION     WP_120273443.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..981
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107888
     Region          22..980
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktfllifl laflinafaq gkmvsgvvts asdgttlpgv nisvkgttkg tvsdidgkys
       61 levaegdvll fsfigmktqe vkvgasavld vamaadalgl devvvtgaga ltkkkqlgna
      121 istipaidiq esgaisvgsa lsgklagaqv mqnsgnpsgg isvrlrgast vlgssdplyi
      181 idgvvvnnes relinlggyt qnrlvdiepq diervevikg aaaaaiygsr asngvvqiwt
      241 krgsserldi nvnsqlsvse vrktlpyndv nliwdgdgtt stnadgtpvk rynyqdlifh
      301 tavgtknyvs lsrakgdtky ffsashfdne givngtnfkr ttarlriddk ltswmdmsvg
      361 tsisyntsqn qfnnedfnyg lltsllfadn svdmrptdgv ypsfgwitni qeaidlvdaq
      421 qinkraitdf klalhpfkgf smdytfgydy snslgklyvp vgfnttpqgv sqkesldemk
      481 lnndlnarym fninedivst taagyslqye kyqilslsae nlipavessn agtvtgrndy
      541 maeksirgyy lqqtfgykdk lfltgairvd essvfgdder rqtypkvsgs yvvsdndfwk
      601 essfgnivnt fklrsswgqa gnmtaieayd rytnystvsi dgttglikps tlgnkdvkpe
      661 rqtefevgtd leflsgrlgl emtyykqdie dlllertlsp stgaeyrven vgtmtnkgfe
      721 lllkaaviqk kdlnwdltat fstnknkvdg iegdiityaw gesaakngyp lgvfygyyya
      781 rnddgslllt adglpqrekg hyennepvse rdangqptge nlkkvigdpn pdfiasline
      841 vrykkwsfrv qfdavqgydv iswdkrilnr yaggdgyake lrgdrpkgwg vaeysiydsf
      901 iedgsfvklr elslgyrikp avdwcesikl sltgrnlfsf dnyygmdpev nregqsnvvr
      961 gndmanvpip rtiifgvnvn f
//
LOCUS       WP_120274175            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mangrovibacterium diazotrophicum].
ACCESSION   WP_120274175
VERSION     WP_120274175.1
KEYWORDS    RefSeq.
SOURCE      Mangrovibacterium diazotrophicum
  ORGANISM  Mangrovibacterium diazotrophicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Prolixibacteraceae; Mangrovibacterium.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Mangrovibacterium diazotrophicum"
                     /db_xref="taxon:1261403"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113961
     Region          24..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqyrialti lflllvcgls aqnisvkgkv tssdkigisa avvtisgteg vvqtnengef
       61 evevvdpegt ltvsaegfye vsqpllgrte vfvvmvdlak pkynedlvfp frnltsgtqt
      121 saaknlaskd fdqvhtiena lqgeisglrv tnksgmpgeg aylnlrgirs mvsknmplil
      181 vngvpympdt eespiiggys rgmlaglnvs diqnitvlkg aeasiygsma angvilietn
      241 gasatdklet qislnsqfgv nwndrrlpvm ngdeyksylt digltyydnm adlisnfpfl
      301 vddpeyyyny lynnktdwqd eiyapsmvsn nvlrveggda vakydvalgy mteggvvdgt
      361 krnryntqin tsinvnrkle lvasiglaym qadlqeqgmi eetnpvlvay sklpmlspyk
      421 kdpdgsilad ydvyrygvsn pvaivntlta edrqhnvnlr fganykltsd lllsgtfgly
      481 ynydqenifi pgrssativa mnnglaentv rsgvgevknl yynvnanykk ilsngnlfna
      541 yggiqmltsk keydagsgyn tandfyqtld fvesgttqfy gyidewnwmn myahgdytmn
      601 nllrasvnva ldgtsssgvd asrlgvfpsa gltfmaknlt slenssfvnk lnlrveyglt
      661 gnsrfssnyg knyyestpfl vlsgivrssi pntnlkwett kqldlgadis lldnrldlgi
      721 gyfnakssdv lfakpissvl gsstyydnva eisnsgiele lsaallktkd fewiiggnis
      781 tlnnevkslg gttsttmelp dgaelitavg enpysfygyk avgvfasqae asaanlkdwr
      841 gesyeagdvh yqdvnndgqi sdedkqilgs atpdffggfn tyvryknisl saeftytsgn
      901 eayngtrrsi ealdsfnnqs raavnrwqld gqqtdipkav ygdpmnnnaf ssrwiedasy
      961 vklkyvtlay efdkavlnff rsgkiyvtge nlftwtnylg ldpefaysyd dalqgvdysk
     1021 vvlprtvkfg fnlkf
//
LOCUS       WP_120285686             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Dietzia
            kunjamensis].
ACCESSION   WP_120285686
VERSION     WP_120285686.1
KEYWORDS    RefSeq.
SOURCE      Dietzia kunjamensis
  ORGANISM  Dietzia kunjamensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Dietziaceae; Dietzia.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Dietzia kunjamensis"
                     /db_xref="taxon:322509"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53798
     Region          17..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkpdsdvrda gvapsvigvv aesnpaenrv aatpetvakl iglgyrvvve hdagtraefa
       61 daayaeagae ladgdaawsa dvvmkvavpt eaevarvrsg atlvgllapa qnehllglla
      121 ergvtalamd avprisraqs mdvlssmani agyravieaa hhfgrfftgq vtaagkvppa
      181 kvlvagagva glaaigaass lgaivratdp rpevadqvgs iggeylpvev peeekvvstd
      241 gyakatseay draaanlyse qaadvdiiit talipgrqap rlitaadiat mkrgsvivdm
      301 aaaqggnveg svpdqvvvte ggvtiigytd lagrlpaqas qlygtnlvnl tklvtpdkdg
      361 awaldmddvv qrsvtvtrgg eimwppppvq vsaapaaaaa pepvepkpek kkmsagaklg
      421 liaagmalll lltavapgdi prhitvfvla ivigyyvign vhhalhtplm svtnaisgvi
      481 vvgallqvgi dntlglalaa vailvasinv fggfavtrrm lgmfskga
//
LOCUS       WP_120287134             376 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Tardiphaga].
ACCESSION   WP_120287134
VERSION     WP_120287134.1
KEYWORDS    RefSeq.
SOURCE      Tardiphaga
  ORGANISM  Tardiphaga
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Tardiphaga"
                     /db_xref="taxon:1395974"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39183
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaisp dtvkkfkalg vdvaiepgag iksglpdsey tavgatisad
       61 avkdadivik vkrpevsela gykrgalvia imdpygndaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra vieaaesfgr afpmmmtaag tipaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf laveddefkn aqtaggyake mskeyqakqa
      241 altaehikkq diiittalip grpaprlvta emvasmkpgs vlvdlaverg gnvegakpge
      301 vadvngikiv gytnvagrva asasslyarn lfsfietlvn ketkalavnw ddelvkatal
      361 tkdgavihpn fqpkta
//
LOCUS       WP_120297693             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. BL23I1N1].
ACCESSION   WP_120297693
VERSION     WP_120297693.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL23I1N1
  ORGANISM  Paraburkholderia sp. BL23I1N1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia sp. BL23I1N1"
                     /db_xref="taxon:1938802"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39365
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatlv gmldpfnaen ssklaaagit afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpnetdee reaaqgvggy arpmppswla
      241 rqsalvhera kqadvvista lipgraaptl isvetvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvtkhgvqi vgytnlasmv padasslyar nlldflklii skegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_120280935             321 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Rhodococcus].
ACCESSION   WP_120280935
VERSION     WP_120280935.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34171
     Region          8..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttsptihdl iivgsgpagy taaiyaarae ltplvfegtq fggelmttte venfpgfkdg
       61 imgpelmdqm reqalrfgad lrtedvdemd ltgavktvva ngetyrshav ilamgaepry
      121 lgvpgesqll grgvsacatc dgfffrdqdi avvgggdsam eeatfltrfa rsvtlihrre
      181 efraskimle raranekirf vtnakvaevq gensvtnlvl edtvtgersd lpvtglfvav
      241 ghdprsslvk gqvdlddegy vkvsapstat svpgvfaagd lvdhtyrqai taagtgcsas
      301 idaerwlvan reveaptlae a
//
LOCUS       WP_120325122             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Altericroceibacterium spongiae].
ACCESSION   WP_120325122
VERSION     WP_120325122.1
KEYWORDS    RefSeq.
SOURCE      Altericroceibacterium spongiae
  ORGANISM  Altericroceibacterium spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Altericroceibacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Altericroceibacterium spongiae"
                     /db_xref="taxon:2320269"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34889
     Region          6..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mathntkmli igsgpaglta aiyaaragme pivvqglqpg gqltittdve nypgfrdviq
       61 gpwlmqemqa qaehvgtrmm wdtiidvdia ngppyvakgd sgdeyvghtl viatgaqakw
      121 lgvpgeqels gkgvsacatc dgffyrgkkv avigggntav eealyltnhs ddvtlihrrg
      181 elraekilqe rlfahpnvtv lwnkrvekfl gnplqggltg leladtitgd isefdchggf
      241 vaighapste lfrgklemde sgylvveagt pktshpgvfa cgdvmdhtyr qavtaagtgc
      301 maaldaerfl atldfvrnee raeqvae
//
LOCUS       WP_120328322             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora globbae].
ACCESSION   WP_120328322
VERSION     WP_120328322.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora globbae
  ORGANISM  Micromonospora globbae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora globbae"
                     /db_xref="taxon:1894969"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33670
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlkp lviegvqsgg almttteven fpgfadgilg
       61 pelmdnmrkq aerfgaeflt ddvtrvelvd tgdvgsnaas tvwvgetayr aravilatgs
      121 awrplgvpge qeylghgvss catcdgfffr nqhivvvggg dsameeasfl trfadsvtii
      181 hrrdsfrask imadralnnd kikvewntvv eeilgsdgkv sgvrvrnvht getkvldvtg
      241 vfvaighdpr selfrgqvel ddegyvkvqa pstrtsvpgv faagdlvdht yrqaitaagt
      301 gcaaaldaer fiatlqg
//
LOCUS       WP_120312490             302 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Mycobacterium mantenii].
ACCESSION   WP_120312490
VERSION     WP_120312490.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium mantenii
  ORGANISM  Mycobacterium mantenii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Mycobacterium mantenii"
                     /db_xref="taxon:560555"
     gene            <1..>302
                     /gene="trxB"
     Protein         <1..>302
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..300
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 igsgpagyta alyaaraqla pvvfegtsfg galmttteve nfpgfrdgit gpelmdqmre
       61 qalrfgadlr medvesvsle gpvktvttae gqthrarsvi lamgaaaryl gvpgeqellg
      121 rgvsscatcd gfffrdqdia vigggdsame eatfltrfar svtlvhrree frasrimler
      181 arandkitiv tnkaveaveg eqtvtglrlr dtvsgevstl avsgvfvaig hdprselvre
      241 vletdpegyv lvqgrttats iegvfaagdl vdrtyrqavt aagsgcsaai daerwladhe
      301 et
//
LOCUS       WP_120305772             338 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paraburkholderia sediminicola].
ACCESSION   WP_120305772
VERSION     WP_120305772.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sediminicola
  ORGANISM  Paraburkholderia sediminicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Paraburkholderia sediminicola"
                     /db_xref="taxon:458836"
     gene            1..338
                     /gene="trxB"
     Protein         1..338
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35519
     Region          8..318
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtlrqrhtdv lilgsgpagy saaiyaaran lrpllisgia kggqlmtttd venwpgdpdg
       61 vqgpdlmarl cqhaerfese ivsdhvhavd lgvrpfrltg daglytcdal iiatgasaqy
      121 lglpseqayl gkgvsacatc dgffyrgrev avvgggnsav eetlylsnia srvtlvhrrn
      181 alraepilid rlmekvaqgk vvlmwehtvd qiigdhsgvt amsvirntdg mattlpvhgv
      241 fiaighrpnt elfagqlemd ngyidtsggh sgsatatsvp gvfaagdvqd hvyrqaitsa
      301 gtgcmaalda qrylesrkas aavlpvappp vtearspa
//
LOCUS       WP_120312691             272 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Mycobacterium
            marseillense].
ACCESSION   WP_120312691
VERSION     WP_120312691.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium marseillense
  ORGANISM  Mycobacterium marseillense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Mycobacterium marseillense"
                     /db_xref="taxon:701042"
     gene            <1..>272
                     /gene="trxB"
     Protein         <1..>272
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..272
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 dviivgsgpa gytaalytar aqlapvvfeg tsfggalmtt tevenypgfr daimgpelmd
       61 qmreqalrfg adlrmedves valegpiksv ttaegetvra ravilamgaa arylgvpgeq
      121 ellgrgvssc atcdgfffkd qdiavigggd sameeatflt rfarsvtlvh rreefrasri
      181 mldrakandk itivtnkave avegadtvtg lrlrdtvtge vstlavsgvf vaighdprse
      241 lvrevletdp dgyvlvqgrt tstsiegvfa ag
//
LOCUS       WP_120332247             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora globbae].
ACCESSION   WP_120332247
VERSION     WP_120332247.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora globbae
  ORGANISM  Micromonospora globbae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Micromonospora globbae"
                     /db_xref="taxon:1894969"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32665
     Region          5..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpdpyrliii gsgpagytaa lyaaranltp lviegaqsgg almttteven fpgfpdgitg
       61 pelmdnlrkq adrfgaqflt ddathvdltg pgpkivhvge qayradavil atgsawrplg
      121 vpgeqellgh gvsscatcdg fffrdqdiav igggdsamee atfltrfars vtivhrrdtf
      181 raspimaera ltndkiriaw nsiveeiign ngavvgarlr dvhtgktril datgvfvaig
      241 hdprselfag qvdldpdgyv tvespstrtn vpgvfaagdl vdhtyrqait aagtgcaaal
      301 daerylaalp
//
LOCUS       WP_120313394             302 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Mycobacterium mantenii].
ACCESSION   WP_120313394
VERSION     WP_120313394.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium mantenii
  ORGANISM  Mycobacterium mantenii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Mycobacterium mantenii"
                     /db_xref="taxon:560555"
     gene            <1..>302
                     /gene="trxB"
     Protein         <1..>302
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..300
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 igsgpagyta alyaaraqla pvvfegtsfg galmttteve nfpgfrdgit gpelmdqmre
       61 qalrfgadlr medvesvsle gpvktvttae gdtvraravi lamgaaaryl gvpgeqellg
      121 rgvsscatcd gfffrdqdia vigggdsame eatfltrfar svtlvhrree frasrimler
      181 arandkitiv tnkaveaveg eqtvtglrlr dtvsgevstl avsgvfvaig hdprselvre
      241 vletdpegyv lvqgrttats iegvfaagdl vdrtyrqavt aagsgcsaai daerwladhe
      301 et
//
LOCUS       WP_120332346            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120332346
VERSION     WP_120332346.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120502
     Region          21..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mriaiilswl llsltinaqv tfkgkvvdgs gkpipgttis nkdgkkviks ddrgqfqwtd
       61 qadtatlrfh hlgyndrnis lfketgftti tlellettld evqintgyqq lpkeratgsf
      121 elidnkslnl rtgnnilerl eglspalqfd rrregevsln irgintldpt magpliildn
      181 fpyqgdlgni npndiesvsi lkdaaaasiw garagngviv itskkaakkq rialeysstm
      241 disekpnlfy spdlnaadfi everflfdkg fynasyngtp rvknntiysp ivellfkqle
      301 gkvgadvvdr eiarlgrvdy rremldlfys tpqtqqhyfa lsnksdkfsn rlsmgfdrai
      361 gnnkgsennr fnirsvsrld ltpklsiegv laydyrkgqs ypdlmdndyv igggktnlyp
      421 yaqfrdqehn alpiprtynl dyvkglaads plqnwlyypa deigtakaen nrhhfqaqvs
      481 vnyrpiegma inmtynvene tydnellyrq hsfyarnlvn rfsqvsdgkv kyivplggik
      541 nstsestray nlrtqgsyqk rfndqhdini lmgaeisnrq tdsksfrvyg ydeetmlsqv
      601 vdyvnaypiy dglasnarip aaegfnrmyk rfvsmyinvg yqyrdkygls fssrkdasnl
      661 fgvntndkwn plwsaglswr adkeffmsql swldllklra tyghsgnsgg vanplplisy
      721 sspinslnpl lkaavltpan pdlkwedvrt vnvgldfavk ggiltgsvey ynkkstdlls
      781 ldaldittgy gtatrnvatl igkgidirls snyrlgslql rstlnfsksr tkvakfygti
      841 vagssyavnt grtinpvldk eiypvfayyf egldpangdp qgrykgevsk eynrmvldsv
      901 qnlryygtal ppyygsfiqe lnwknftftm lfsykfghyf qketisyssl fnswsghsdy
      961 qrrwrqpgde ahttvpsmvy pavsardrfy gaaepniqkg dlirlqdial nygfktkigk
     1021 hqinaniylk annlgllwra nrfgldpdyy dlpparryaf glnvkf
//
LOCUS       WP_120332424             959 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120332424
VERSION     WP_120332424.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..959
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107850
     Region          54..956
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkykklrial clglswiata egmakeslnp tirqhknifp erstfvgpds igtdsttlvq
       61 vafrkvqkkd lmgnvqsinv pqlldksynt yslenldafi pgyngniwgm ggylvlvdgf
      121 prdannvmpt eidqvsvlkg anaialygsr aakgvisitt krgksgsqqi kiransgina
      181 amsypqylgs aeymtlynea rqndglsply saetiyqhaa gtnpyrypnv dyyssdyikd
      241 hynrydatae isggnqraqy ytnfgfwseg sllnfgqakk ngganrfnmr gnidvkvndl
      301 islnvdaaas fyiskgvnad ywgaaatvrp hrfsplipid mieegdvnsm vyvnnsnfli
      361 dgkyllggsq ldqtnafanv yaggtnryln rqfqfntgln fdlknilegl vfktnlavdy
      421 qsnynqsynn nyavyqaswn nydgkdliss ltkygddris giqnisgsty rqtiglngsl
      481 nfnrtygndh hvsaillana fqiaasgsyh ktsnanlglq lgynysskyy vdfssayshs
      541 aklpqgnrra lsptlalawr lskenflvds kvvnelrlsa sagilntdld isdyylyqgy
      601 ytyndaawys wrdgdlvhtf drrrgdnpnm kfpkrkefni nlegglynnl itfntsyfvn
      661 rmsgglvqaa tqypmyfmty wpvysdlpyv nfndderrgv dfginlnkqi nktfvslgfn
      721 gmyyttkavk rdelyefayq nragkpldai wglqhdgfyn sqseidqaaf stfgevkpgd
      781 ikykdqngdg tidtrdevyl gkggwagapl tlgcnltvkw nnftlfaaat gqfgakamkn
      841 ssyfwvdaed kysvvvrdrw testketaty prlttfnsdn nfrssdfwly ktdrinlskv
      901 qlsydfpkrl fnakfihelg iyatgsnllt iakeketmql nigqapqmrf fniglkalf
//
LOCUS       WP_120332372             993 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120332372
VERSION     WP_120332372.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109577
     Region          33..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkngvkllly wgayvlicll fietgygqsr slvtgtvvne ankplagvtv nadengnqaq
       61 rqttatdang mfrftdlkvg ipynlsftyl gyhpqelpef ivksgdnnsv lirmkiseat
      121 nlsevvvvgy gtqkkqnitg siatvkaedl tdvaspnvgs llqgkvagle vsnssgqpga
      181 mpkvkvrgis sisasqvpiw vvdgviqhdv pnlnpqdies isvlkdaasa alygsrgang
      241 vivvttkaak agittvnfsg ktgisvfntg qfnvmnsqql ydfwsafpnt kdipswfnss
      301 ltdvntdwia mgtqhgvvqd ynlsvsggtd ktrvyaagny fqekgtvkgm vydrftgrln
      361 ldqklgdkit fspklfasyt ktdnrqhdin alftylpwdr pyddkgnvin aqaagsgwrg
      421 rdlsnyyydl qwnytqgnry namvnldfsy kilpflefks tnnltylvdk gliytdpqsi
      481 sgqadngrik nsnayrttrf snqmltfnkt fglhslnala ayeyndykyd dnsatgigiv
      541 sgitvlsgas kasgvtgtan hyafqsmlmn anysyddryv lqasfrrdgs srfgsntkyg
      601 nffsfsgawn ihreaffdss tvnflrlkaa yggvgntpet lypqyelfsv naqyngtptv
      661 fpsalgnknl tweksystni gvetglfdrl nltlelyrkn tsdllhfvpl pdvsgykgyw
      721 dnigrvmnkg aeltidaklv rgaafswdlg fnlginrnkv melyggsrqi ngnqvieegn
      781 dintwymrkw mgvnaengtp qweiidnktg eksltgnyaa aslqkvgrat pdyfggistk
      841 mnynhfylta nmaftkgiqv ynagrelfds dgayatynqm dlksgwsrwt adhtnathpq
      901 alfggnnrsn gtssryledg sylrlrnvtl gykwtgkmle rlkvkgintn isidniftit
      961 nysgidpeaa asggttspyp lpkrimfgld iqf
//
LOCUS       WP_120332551            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120332551
VERSION     WP_120332551.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119511
     Region          49..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpiklpqfr ktaqvtlaia llnaahvdsv wanfanettk leiadqaiik givkdqdgkp
       61 idggtiinet skqstrtefn gkfnlkgqvg dqirvsslgy ktatitatdg dlvvvlekdd
      121 skldevvvta igikqqkkqi gyatqevkld vlkesktmni gtaltgqvsg livnnptgif
      181 qapsfqlrgk splivvdgip vesdfydmss qnieninvlk gtaasslygs rgkngailit
      241 tksaksdrle fsvgtsnmfs agftvfpesq kefgsgsngk yefwdgadgg isdgdmtwgp
      301 klnsgikvaq wnspirdkqt gevipwwgdv sgtkyndksr yervpidwva hnnledflgt
      361 glitennatl syrsekvsif gtgkyayqkg qvpntklstg glnlntsyrf tpevqldlnl
      421 synkvkspny prygygpknh mytillwmgn dvngqelkdh lyipgqegyr qanynyawyn
      481 npyfaaneln qvydqdilag qtaltwrisp eftikgraaa rqknlfqdmq spksymnygd
      541 srngdyknwd skqlnfdadv latyikqlsd nfgvtvnags stfkrdyrel yqttdglvvp
      601 fvynlgntqg pvkatnttte kiirsayasv nlnvfkstyl nfsgrndwss tlskanqsff
      661 ypsvslssvi sdyfklpaqi dfvklysswa svssdldpys iaatykkdvt ygstpsvtyp
      721 agiinpdilp qqsisleiga smaffknrls advtyynvvd knqiidlsis qasaftsrkv
      781 ngnkyrtkgl eisltgniik neqfswtstv nwsraiqrle eiynnqakyg nlkkgdrads
      841 yygtvweksa dgkvilnsnt gmptknpfpq ylgyfqpdwq fgfanqfkfk gfqvnldldg
      901 siggvmnstt iekmwwggkh pssvlyrqeq ydagkpvfvp dgvivtggel trdvngnits
      961 dtrtytsntk avdwqawsqn ypyqarvtes esklfanvfd rsfvklrrls vgydvnkvfk
     1021 lkqltalnas lfgynlamwk kvpyidpdfg vgndgnlqdp stryigfsld fkf
//
LOCUS       WP_120317627             307 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Catellatospora].
ACCESSION   WP_120317627
VERSION     WP_120317627.1
KEYWORDS    RefSeq.
SOURCE      Catellatospora
  ORGANISM  Catellatospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Catellatospora"
                     /db_xref="taxon:53365"
     gene            1..307
                     /gene="trxB"
     Protein         1..307
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32984
     Region          7..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 menvrnliiv gsgpagytaa vyaaranlkp lliegvesgg almtttdven fpgfpdgvmg
       61 pelmdqmrkq aerfgtefit dnatrvelsg evksvwvgdr eyraravvlt tgsawrplgv
      121 pgeqellghg vsscatcdgf ffkgqrivva gggdsameea tfltrfaehv tiihrrdefr
      181 askimaeral anekisvewn tvideilgtd gkvsgirvhn vitnesrelp atgvfvaigh
      241 dprselfrgq velddegyvk vdapstrtni pgvfaagdlv dhtyrqaita agtgctaald
      301 aerflah
//
LOCUS       WP_120332992            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120332992
VERSION     WP_120332992.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124674
     Region          120..1111
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtnyylkl mgsallfqsl alhtmasqfs tsegigkilt rmeqkfnvkf gydasisnqk
       61 ineaadldkl kkeqivqfiq tisdgnlevk kideklyvis rktgndtkvk nekpvsnvak
      121 eirgkvvdqe tgqpiagvtv rvkgstqvtt tdqqgtfrfv nvaddaillv syigyqtsev
      181 sasnadvikl gksseelgev vvtalgikre qkalgyatqs ikgddltrvk gvdvgttltg
      241 risgvrvlns tefnstpqiq vrgltpilvi dgvayenltl rdvpvdnied mnvlkgatat
      301 alygsmgagg aimittkkgl aekgteisvn snnmffsgyl alpevqhgys sgeggkfnnd
      361 dyvwgdkldi grtakqwnpq tkqleemell srgkdnfknf lepgfisnns vsftnqgehg
      421 sirtsinhiy nkgqypnqkl nmtnmsvagq tkisekvdie trlaynrrsa tsnfgagynd
      481 qgyiynilvw tgpeynlqdy kdywlikdqs qnwmykawyd npyltayekv tpelvnkmna
      541 altlnykvsd wgklmvrtgy dyygqrreqr npmgiygtrg gysgfdskgk ywmqnqdgfs
      601 ttndviftak kkvgdfgfdg llggalfyrr dnavtattvn glsipgfysl rnsidpvstv
      661 esktkemvns tygrlsvswr naifveatgr ndwssalske qrsyfypsvs ssivvsdlig
      721 nkpawldmfk irgswavtkt vpspyeinqa ftisnnvwdg lptasypnsi kdysisptqr
      781 dltefgfdfg lwknrfygny tryyrllhnv ttyatisgss gftsrlintq eekmtkghei
      841 tlgtaaikke nfqwdiilnm sqnleffhkl dpvysadaly vkkgartdyi tvkdwerspd
      901 gqivnnasgm pisakyaaql ygytapkwfg gltnqfrykd fslslsvdgr ikgmsysgmn
      961 arlwqtgahp dsdnpyryee vvngnktfva pgvkivsggv tydkygqiae dtrvfadndk
     1021 vvsyetywks aysgrrnywd etfiklrels lnyrvpekla skfkakrasv gvtgqnlllw
     1081 tkeyrfsdpd vgsedlnsps mryigfnlnv tf
//
LOCUS       WP_120333019            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120333019
VERSION     WP_120333019.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117084
     Region          31..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqfkifynsc mllilcvfls tkvfaqtvim sgkvtdnkgr plagvtvrfg ksgkeatstn
       61 ssgafsltta tgtsvafrli gydgttmtvk adrnvvvqlk eidnqmdevv vrgyvkrpre
      121 tttgsstkis gkeiqdipsa nvenllqgkv aglniqvntg apgfrgstqi rglstisvtg
      181 sgdqsfltpt splyvidgvp mdadranelg lsqqgpgisp lslippedie sievlkdaqa
      241 tslygslaay gviiintkrg nsevprvryt gnfflktppq lrptlggnle rrlkllqvyg
      301 nalsqddldr isqtpmlsds lnayynnstn wqdlfyatty nqthnvaidg gnqklnykan
      361 lnyynengii kntgfdrymt nmrfeyypne kfkftaqisa slgskskgng lgilqsgvat
      421 ngmastllpg psfylassgy nsalktrndn ssksikpfie asyeiiqglr atttmsyest
      481 sdnentftpa aangqfaqvy ayygrynsly nrnsinysht fnekhtvffn lfneiralek
      541 qanatlqart pndqfegplg fdgyfskggg llrrgfgker glsfaiagty dymkkyvvdl
      601 syrmdgssqn gfgnlytknp avglrwnayh enflrdvdwi nllsirtswg vnvmpnstle
      661 rvygkydiag syndkigigi nyeqipnpdl kptttsqynl gldlaffqnr feltydtyyk
      721 kvnnilfeel lssslgfekv nsnsaaiany ghelsvmlrp ltegrftmsi gvngaynrdv
      781 llklpehygg qfvrwenndk ykqhvvfrvg tstmsnymll nrgvystdad vpvdpatgrr
      841 yrmangtefq agdpifadld gnyvldendy artgnsqpli tggmqlnfny nhetlgsfgl
      901 nlyasytakr tilnnalaer lqlmsdpygd ravvplddvn mwmkpgdiak ypyaydfrry
      961 ssvnpfrmdq dlwaedgsyf klnsvtlsym ftknairryg lerlrvyvsa enintfskys
     1021 gpnpenvstm grdasggypv prqynvgvni df
//
LOCUS       WP_120333533            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120333533
VERSION     WP_120333533.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118015
     Region          26..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfykkatg ialctlfsat slyaqqtitg tvtdakgpvs gatvsvkgta kgtqtnasga
       61 ftiqaapgev lrisivgyrt qeitvtsaks ikvsltedas aldevvvtam gikreskalg
      121 yavsnikaee itkagntnfg salygkapgv kittapggsa savnvqirgi nslnyqrqpl
      181 yvvdgiiirn dqqggatgan nnnywddqri rgngmldinp adidnisilk gaaasalygs
      241 daasgvivit tkkgtkgrgl gidfnyngsi eraaflpkfq niygpgydaa tniangasae
      301 gwftdansps grrpyyrsyg sfgpkftged vmwwdgqvrq ykarennyyd vfdkgynsni
      361 nvgisnqtek inyrlsatrm dykstspgsk qnrntfnlns tlklsdklst divanfintn
      421 thnrtyllgq vlgsfdgffs rtedmsamkn ayqttdgyky skfgtgrped fkytmrasnl
      481 ldyfwnqykn sydetenril tsatlnwdvv nhlklrgrig ndltsatsin kqyneyatay
      541 nsttsssggf atskgvysil ygdvmatysn kinadfdysa svgfqsrser yddqssstag
      601 glvtenwfsl snsyaqatts nsrkemlkya yfgslnigyk gfayldgtyr seysstlpss
      661 nnnyrygsvs gsfifsdafd iksdkfsygk lrasygivgn daaiyeania ynqnplltin
      721 gavpsltyrn nygnlnlrpe rkyevevgme lkflknrlgl dvsyynnyid dqilglttpa
      781 stgatsqiln igkianngle lsingtpiqn enftwnsrln ysfnkstvkt lapgveelvf
      841 ysadenslki takegeklgn iyvydiakdq ngnnlisddg lyvidktkyk yagnimpkai
      901 ggwtntftyk nfmldftady rfggkmvsen lkygmsagly entlpyreng vtlqgvnant
      961 gkandvhlsa aeyymntfgw gadswtekga vydnnfiklr elsvgyripd sftkrlkinn
     1021 lkvsllgrnl fyfyrtlknl dpeapvgnkw waqgvdvgss aatrsfgfsl nanf
//
LOCUS       WP_120333535            1106 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120333535
VERSION     WP_120333535.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1106)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1106)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1106)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1106
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1106
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121810
     Region          28..1100
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfykktag lalctlfsat slyaqqsisg ivsdangpis gatvsvkgts rgtqtggngs
       61 ftiqastget lrismvgyks qevvvgsnkt invsltsdqs nleevvvtam gikkaprelg
      121 yamstidske ltktgspnfa galygkapgv rittapggat sgvninirgi nsitgnsqpl
      181 viidgvpmrq nkfdnsnywg dqrargngle dlnpedietv silkgasaaa lygseamngv
      241 vlittksnkg gtgfsidfna nythdqiayl pkfqnvrgpg yslayanggq aedkffyyga
      301 dravdgvtrg vlpatvnfgp kfdglptvaw dgkvrpyeaq naygkffnnp nntslnlalg
      361 hatetsnvrf sltrqdnqmt sfdsynkkni vnfnstfklw nklttdvvvn yinqhthnrp
      421 fmtdrlinnf tgmistfdnp dwyadryqts lgykyvtgtn qsltpgenli hngykvdvld
      481 yywntrakts deysnrligs ftntyqitdd lsvrarfsad vtsarfedrs pnrfpllygf
      541 dtesgfttkn qnqnvyytdl lasykkqvtk diklgaavgy tatknqdfsv sgwtngglsq
      601 rnwydlsasv ndsrssqari wslrdatfgt lnfsfkdywy vegtlrreli sqmhpdknvl
      661 yypsvnssli lseafklpei fdyaklrgsw givgnypnif qsalsfsqkt lgdqgtgsvi
      721 ytqvptsgfg nerikpetkh eiefgletrl lkgrlgfdit yyngqirdqi ldfslpmttg
      781 assivanvgt lrnkgwefvi ngtpvqsenf kwnttvnlaf nrnkveqlag gatelehrfi
      841 dgdaakiisr vgeplgdiya rpvktddqgr mvvdanglyq ldnttykkvg nampkaiggf
      901 insfsyknft ldalidfrwg ghimptginw mksrglleet legmdaehgg lsyylsggkg
      961 iattgstgpn getvyhdgml ldgvlldgtk naniisqaty fnstynwggp qyggnsryel
     1021 yveknnyikm relslayrlp kdfarklkak nislsafgrn lffiyrtakh ldpeqmtggs
     1081 hwsqqitnag sgpatrtygl mlrasf
//
LOCUS       WP_120333557            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120333557
VERSION     WP_120333557.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112665
     Region          24..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqkliyfll gilfaihvqa qssrkvggiv sapdgtplag vsirventke atqtgrdgqy
       61 sirvaasekl ifsfigyqvr hidlkgrssl dvvllkeesv ldevvvsagg ilrtpreqgy
      121 attqvtgenl tqgksptiag glqgkvpglq inqissgvnp nyrlvlrgnr sllgdntali
      181 vldnavvssd llnninpadv envqvlngas gaaaygaegs ngvliittkk gqagrtainl
      241 sntftleeis ffpklqdkfg agstsgsqiy npeenqqygp afdgstvaig nplengeqqy
      301 gtysarndrf dfwnvgrnnq tdlsissgnd kssqyiagqy ltgrgttpgd kynrisfrln
      361 gtrafypnlt ldysasyven fyditsatss iytqltqtpa nipllsykdy vnnpfatpdg
      421 wynpwylnpy wtadnyrskt knsyltakie lkyrpttwle ftyrpsisnr wydsksvspk
      481 qtyssysvnt igrtnlaggv sdteynsari nhdlqigikk dvndfsfnfn ltgtaisrry
      541 ksvavsasgl eipglynvsn rigeagases ntlartfavw gdllvgykdy lflhatgrnd
      601 wtsvlskanr syfypsvdls fiptdafkql kdnsivnywk lrgglsrtgy vnvdpyslvp
      661 tfssvtgyss gtffsqgsri issnlkpeit tgvefgtdfr lwdnridani tyyhtgttgq
      721 aipagiaiss gysqfyvntg kvtnegieta lhitpirsrd fqltvggnyt hnknilqdly
      781 pgldrising ssviygqkgl elnqiivsdy ardeqgrviv dvntgypsva seskilgntt
      841 prhrlgldls lrwkdfsfst lfeyrggykf aaidlgstld fggssarsay ynreafvfpn
      901 ssyldatsgq yvtndhitvs dggagfwtsg tynrgvysny visgnywkwr easlsyrlpq
      961 rvlsrlkgvk aasvsiqgrn lllftpksne ytdpdysand nnaigvsttg qtpptryfga
     1021 tlsltf
//
LOCUS       WP_120333968            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120333968
VERSION     WP_120333968.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123299
     Region          54..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miklsksfta lldkvvnipv iqitllvivs llvsmfslsa qtprkdsgan gllkvsgtvl
       61 sasdgkpiqg vsvriadekg rastksdgsf svpviasagt vkfshvgfkp ltlpysagvs
      121 ltvklillen qleevevvst gyqkipkera tgsfefvdnk llnrkvstdf isrledvvps
      181 ittmktyqpa rgkllnfnir gqstlrsnvw plivldgmpy qgdfnninpn dienvtllkd
      241 aaassiwgaq sgngvivitt kkgkfgqpiq lsfnsnitvg arpdlnyqpq mssadfieae
      301 ryffdkggyd fkfedifnrl spvllllken rdgtlsdvdl eaklndlkki dsrddfskyv
      361 yrkavkqqyn iqlsagsdkm snlfsvgydr nlnnvvtssy drlnlrnnfr vnplknlsfg
      421 ldilyiegrn keygysnqnq ynmlfggnyp ytrladdqgn pvevigngpl piyqdtagng
      481 rllswkyfpl keldqsseit ssrenifnld gkwemmpgln lsaiynyrrs ltktenwqga
      541 dsyymrqlln syavyddnai kwniplgdkm tffnqegvah qgrvqlsydh kwndkhhlhs
      601 iagyeirqnt asqnsalyyg ydknrltymp vdyvnqlpfa ngylgtnriw gempllgttn
      661 rftsyfanas yaydgkyils asarkdasnl fgvksnnkgk pfwsvgaawv ltnegflkdh
      721 pifsslklra tygfngnvnn ttaafpvmti qsqvhgitgl pyaqimsppn pslrwetvgm
      781 lnfgldfall nnrisgtley frktprdlvs ttkldpttgf ssmnmnsadi lgkgldlsiq
      841 srnvvnrlfs wttnlifsyn rntitrsyls ntkglnyisg pqtnfrtpvv gadlfgqytf
      901 kwagldpqtg eprgyvngei skdyptiyng tqvsdldywg stvpvyfgaf rntftyknwe
      961 asfnisyqlg hvflrnsfnn smfwdyetgh sdyalrwqkp gdenwtdvpa lsypvnsgsm
     1021 fyslssalve kadqiklrdf qlayrinssk viknpqlyly mqnlgtiwra nnwgidpefg
     1081 knspdpfsvs lginfsl
//
LOCUS       WP_120334725            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120334725
VERSION     WP_120334725.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114651
     Region          52..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mwysdkiklv taskkwiipl valatsytqv qaaaalsalk gnsnflnfqq sisgvikdaa
       61 tgnpisgvtv likgttvvtq tdaagrytia akpgqillar fvgydnqeit vgesksvdiq
      121 ltassnqige vvvtalgimr ekkslgystt svkgdqftta rdpnlgnals gkvagvsvag
      181 natglggssr vvirgnasmt gnnmplyvvd gipldnqnqg sagqyggmdm gdglnsinad
      241 dieniqvlkg aaasalygyr ggngvimitt ksgkgaqgig idfnnnltvn tiydyrdfqd
      301 iygqgvqgtk pttaaaandt ynqswgakmd gsqavnkfgn sytyspidnw knfyrkglsn
      361 qtslavsgsd ekssfrlgln nmyegsilpn aksnqrganl nttykitpkv qlginanymf
      421 efvnnranls dgngntnasl lylansydvr wlepavdefg kelqpgnnvy fnnpyflqyr
      481 kfnestkkrl tggfnlrydi tdwlyvqgaa trdgfnlafk qvqpkgasad pngyineynk
      541 efeetnfnyl igfkkklsdf sisatvggns qktrnqtwgt dggirpfivd gvyntgnvaa
      601 gtrtfkklyd eyqvrsiygt adfgykdflf lnlsarndwy stlnpesngy lypsvslsyv
      661 ftdhlklpdw inmgklrlsr aaasngtkay qtalayrtls yelqsqpvgt inndvvpnan
      721 lkpvrisewe agtnlefwgn rmgidlavyq kttkddivrv ttstgsgysv aiqnigelrn
      781 kgievliygd iirandfkwk ssvnfafnds kvlslgnqks ltfeggvsrs gnasvqnivg
      841 lpygqivgyk yktdasgnri fddkglpvrs davevlgngv yrftggfrnd ftyknfslgm
      901 lldvklgaki fsgtnlnlyg sglhkatleg regnivgkgv nlnggtntta vdaqtywkyv
      961 vdqsfteefv ydagfvklre isfgyslpkq mlsktpfraa slslvgrnlw tihkntpnid
     1021 pesaynnsna qglelngypm trnigfnlnl kf
//
LOCUS       WP_120334815            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120334815
VERSION     WP_120334815.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119208
     Region          32..1054
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkfnrlifv sfsflcmlll stgivysqgt gkelkgivkt ndgrflekvt vlvkgtstgt
       61 vtdsygrfsl klqqstakvt lsfthtgyss keldvevgre ieitlseste nldevvvigy
      121 gtakrkdvtg aivsvqtekl ekeaprsvqd llrgnaagli igqgnsakgd aslqvrgkgt
      181 lkagssplnv vdgvifdgtf adlnpndiqs idvlkdasat avygakaang vilittkkgk
      241 kgkpsitfng nfgmvesagm prvmtadefl kyrydfevgr rtadylkahp emfvdprlls
      301 gtnqldwyny dqktpvtnvt edqlirswls rlelktpeie nymnnkitdw qdlvfqkgiq
      361 qdyavavsns nenanyyfsl nhvdregvvv gsrfknfrtr lnletkitsy lkvgantnfa
      421 vrnegflksd wkqsavispf gsnnlddpss iyqrlptgdv tpvnpffdnq frdrknnynt
      481 lnsslygvit lpfgielqsn ftpsftwhey ynhdssknpe wkakggsser sfektynwql
      541 dnvlrwkrrf dvhnfevtll qnaekgqfwq tkatasqfvp sdvlgwhrlq agtiplnesn
      601 dtyrtgdalm arlfysfkdr ymltasvrrd gysafgaqnp ratfpalafa wdftaedfmk
      661 ntkswldygk lrlswgrngn rdielyeals dmtsglhpyi dasgnlylss qlyvnrmanl
      721 dlkweskssy nagldfsifh grlsgaldfy tattqdllvd relpeiigfs svaanlgels
      781 nkgfdislns nimnkgdfsw nataifmlnr rkivklygdm vdvkdsegni vgqkeaddvk
      841 nrwfigqdpd riwaykrngi wqigeeemaa kygnqpgdfk yidqngdgvl tdadrvfqgy
      901 ttprfrwsfr nelrykelsf sfliysnwgh ygdfyqaann snfadrstdy alprwtpdnp
      961 indyarigsk nngtnyvnms fmrldnmvls ynlpksllqs lriqqlrisa svrnvayltk
     1021 dfkfgdpers wksdaladvg dpaprtynls lnltl
//
LOCUS       WP_120334832            1202 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120334832
VERSION     WP_120334832.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1202)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1202)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1202)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1202
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1202
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=136080
     Region          150..1201
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myknyaqlgr alhdqtqqmk nsdhpdiwgr pqwrgnimri slttimmscc llhvgaktyg
       61 qdisiheksv slrkvfsein kqtgysyvwa attidpdtkv nltvkkeslg nalgkllddl
      121 dldfeikgki ivvheksqqt qrsianqlmt vkgfivdynn rplqgatirv kgvpkgtvtd
      181 qnghfeingv ssnsflditm vgfapltiaa ksdlgtitlr aldeqlqevn itvntgyqki
      241 skeraagsia qvtakdmegr lqpnlldrid gllpglnlvr ntsspqnnkn nlgievrgrs
      301 tinaqaapli vvdgmpyegd ltainpndia sitvlkdasa asiygvrssn gvivittkig
      361 sagktkidys ntlsfrglps rsylnqmssa elvnfqkemf nyrsgdyavi dprkamndvy
      421 rilydrkggv iseeemekrl dvyrnrdrfs qmdkflnttr fdqqhnlavs ggsdrytyhy
      481 slnytqpgdy nkgratnkel gfslknnfkf tdwfslranv lgknqnregd igfnfydnym
      541 ggkasyylle nengspaqwy nsksqfeidr lnalgledet yiplkhvaai hekfynkyln
      601 lnfaanfklf kgldfdlsyq sertegyngt lnrknsqsvv gmvndatqig kdgaikrnip
      661 qggqfaeqrn dvnsytlrgq fnyqynswdk heiiaiagae rrqinnrytn iykygydess
      721 lvykgineel fgiqiqntqa lfnsytiskk etgfkdlvdr fvsfyangsy tydrkltlsg
      781 sirmdqsnlf gtniknqykp lwsigalyhl pkidwepldr wsvratygvn gnvpkdngpy
      841 lisrvnnnln yfngemqayi dsppnpllrw ertkvfnvgf dfslfkdrlt atldiynkkt
      901 sdllgntpld ptlgwdmvll nyadmqnrgi elglngkviq renfswnsti nfsynknkit
      961 dlyveqntpy yyyyapqnrv gipmgslysi dyaglndkgr plarkadgsl vettqkltvd
     1021 dliyegttvp pytvsfrngf rykdltlsfm fifngghvmr gvhpeflsky aelnynsnfd
     1081 klwlnywknp gdesnpdiap afvsaasgni sdifnaahkf vqkadyiklr dislsynlpa
     1141 qwiaptklsy vrltgqvlna wrwvankdnl dpevwagyst vtspsrgiqa piiynlgvsv
     1201 gf
//
LOCUS       WP_120335112            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120335112
VERSION     WP_120335112.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114345
     Region          23..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkfllfcs gvmlstslwa qtktvtgkvt nasdggtmpn vtvsikgksv stqtkpdgsf
       61 tinaepgdil ifravgsqer qqlvgtnati nvalsgseea leevvvtamg ikkekralgy
      121 avqdiksdel mknktanvvn slagkiagvn vtqssgaaga gaqiilrggt slerdnqplf
      181 vvdgiiydns tpiggnsgfd gmqatstsns nrvmdinped ienvsvlkgp aaaalygsra
      241 aagavvittk rgsegrveig fssrfsanwa nrlpeqqgky krgyynsagt ldnyttqswg
      301 eafkpgekvy dnvgdffrta tvfdntvnvt ggnkngsfyl sgsrfdqqgi ipetgygkta
      361 frfngdqkfg klsvganvay tlantdktlt saglygsgga gaissvygws rsddmkkyln
      421 ddgtkyrmfe glqelqddve npywtinrnk ltdnteritg sinanmnifd wwnvsyrvgm
      481 dsyltknstl iaengavkql wqngmmsend lkfnywssnl msnfnkkigd fdlgamvgyf
      541 aeetkvntnr rmgydfvvnn fysfgnidka nklfdevtsk krlyglygel rasyknflfl
      601 nvtgrndwts tlpvanqsyf ypsvggsfvf tellkdkgld wlsfgklras warvgkdatp
      661 yatntylwtp reslggiiat gnswtkgnpn lkpettgsfe vgaelrflng rlgvdyayyt
      721 nnsynqilsp rlgqsvgyif vsvnagdiyn kgmelsltgk pikrenfewd vtlnmsrnkg
      781 tvdnlisgvd ilyvtdvqvg nakaasfngg sfmgisgsky artpdgklil dantgmptsd
      841 nattynignr epkligglnn sltyknfnls flldyriggd iyngtdyamt lnglsmrtle
      901 rdeltlsgvv ntgtaaapvy edktftfnan esylvsgaqt sgkkiiqdyw gvhyikesan
      961 fmtktnwlrl rtvsvsydfg nsllkksnvs kvikgltatl tgtnlwlltn ykgldpeasa
     1021 agsgvtgsss vgidyngvps tagvtfgvnl kf
//
LOCUS       WP_120335302            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120335302
VERSION     WP_120335302.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124700
     Region          22..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkflipltf mcvhvahaqe srelkgkvld avtlkpvvga tvvvessava edigvpnqvq
       61 qsalgsltda agefrlkvps nlkyvtisyv gyqriqvpvf qdhktillqp sgesldeviv
      121 tgytdikkrk nttaynkinv adikqtgvas idemlagqva glqlsnfsgg pnsapqirir
      181 gtvslngtqd plwvidglpi egtempnrid kdnlnsltnl piaginpddi aditvlkdaa
      241 atsiygaraa ngvivittkr gksgpaklqv santfvterp dysnlnlmna nekvdfellm
      301 anrtdlnyrt nkgaimriln kadaldayrs gglaalspev qqsinqlrsq qtdwgkelyr
      361 qalnqqysas isggndghry ylssglydek gatkgvdlrr ytltlnndfn indrfkagin
      421 lmgtvsnrqn piqdrdaftn psyyvrsvnp ylsvydqsgn ynydpdiegf egdtyipfna
      481 veerentkyk ftnkglkais yleytilpql sfrtefglqf dengsekfad qesyntrklr
      541 aatryydaas ktnkyflpvg gtienthnsi fqynwktylk ynktwndrhe levmggtelr
      601 rtkntmvttk gfgynpatlt tqtiifpnst yqndsrfvqy kkafiensya sfygnatytl
      661 drkynvygsi rydgsnmfgv dpqyrflpiw sisgswnvle eefikgktal sdlrvrasyg
      721 iqgnvdrnty pfivgkygnt tllpgntegs vvvdmpandk lrwertqsyn agidlglwkn
      781 rlnitvdyyn rkstdliays alplengfqn vqvnwasarn qgveltissr qiqtdkfsws
      841 tdfniahnnn kllkvinnpt ayapetqagr pinglyvlet agldkdgvmq frnqdgsvas
      901 meefyglydp wadflpgyts qtdmsaatyr skfkyagskd pkfiggmtnr frygqfdlai
      961 savfnlerwv srtpiynpak vdrgqnytkd llmalqgkta lpalgsisse lnerwmayaw
     1021 mesndpinsf kqydiwakkm syvrinsirl gytlpaaisk kigtsnlrvn vegrnlfvfg
     1081 tnydgyfdpe tygdyyaqpi sksfafglsa sf
//
LOCUS       WP_120335310            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120335310
VERSION     WP_120335310.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117375
     Region          26..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maknninfvv maalslstga lyaqttikgk vvdnnnnpiq gatvtetssk kqvqtdangl
       61 fefpstgssl sisiqyigfe trtvqtnttg fttvqllptt sqlnevvvta lgisrekksl
      121 gyavqevksv elqtrptnal salsgkvagl qvttsggnmg gsshvllrgi nsiagnnqpl
      181 yvidgtpidn tdlnssstin gsagkdvgnm iqdinpddid nisvlkgpsa aalygsraan
      241 gvilittkra skgekvdisl ntgvdfeniv rlpkrqhlyg qgystsfqtq ningtdykiv
      301 dyaadeswgp kldgtpvlqw ynlnpedean ylnpspwiyp kndvsyffrt gvsntnnfai
      361 agnsgntnyr fsytnknvtg ttpnsslgrn tfnfsggtql gklkinsnfn yirnasvgrp
      421 wtgasnrnii leafqwgavq vdykilenyk redgtplawn rtgwqntpaa eatrfidnpy
      481 wsayesymed nrdrfygnig lqydlnnwlt lgakvhgdiy sfqsqdriav ysrstsqyee
      541 annklneyny eflatakknw dkfslignig anlrdqqrkq dyaitqggli ipnyynlkna
      601 navkidnfry hrriasiygs fslgyndfly ldgtvrndws stlpinnnsf iypsltgsfv
      661 fsqleafkkl dwlsfgkirl gwaqvgndtd pyqlykvyep eqsfdgqasy glpstkpnan
      721 lkpeitsswe tglnlqlfkn rlgfdvtyyn nnsrnqilpv pvsssfgyag kvfnagkinn
      781 kgievvlngt pikhenftwd atinwaknkn kviklddqvn tlslsnslve lvaregesyg
      841 qflgydfvya pdgqrvvqad gtymktsqlv plgsvlpdft fgiqntfryk nfslgflvsg
      901 rvggkffsqt ykvgmysgil dktaannire tgvvldgvkg dvafhsdgsy dvsniqqntt
      961 nitaqqwarn eyngpttfsi fdatyvklre vtlgynfklt npkiiknigv nvygrnlwni
     1021 ytkskyidpe ftssggnvqg ieggniplpv tygfnvnlkf
//
LOCUS       WP_120335315            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120335315
VERSION     WP_120335315.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121498
     Region          30..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mysnlklrtl ltlsvlmgnm llaqaqdhav rgkitdaktg ellgnvtvki kgsnqslqtn
       61 tdgtfsistn pntilvitst gyrpyevkvg qlnqldikle skveqmdevv vvgygkmkks
      121 nltgsvssld kkvletgvrs npasalagti pgirvqqtsg rpgavptvvl rggttygggg
      181 tplvivdgli rngfndinqn diesidvlkd asataiygar aangvilitt krgkegvsni
      241 tlsskvgvnk lnnpfdflsa rdylnwsrkg vqvsgqyqps qlnqltsvgp fgtgnkykdd
      301 kgnildgnlt snavwstmll ddtnrellqq gwqtmidpvt gkelifkdfd yakyalrdas
      361 ltqdynialq ggndkgkyyg svgkynekgm pintfydrtt fvlngeykvk pwlhslsgvn
      421 faytkwrdai ngegnymtra lgapptmrgt nangdllvgr dyqdgnpvvn ddkfirknln
      481 qkltltqaft inflenlslr vsgnwffnqs tsesfnrdyl aspgnyvrtr nssasydkiy
      541 nqtynavlny rteiasshhi damlgseffd tynngftaag sgaptddfmd lgltspdank
      601 rsidsyhdrq rimsyfgrvn ydykekyllt ltarrdgyst llnnrwgtfp gvsigwalhr
      661 edflkdylgt dkivntlklr asyggngnvs gigsytlqgs ygtnkydgqv gytmstlsip
      721 nlkweslitk evglesriln kidlslayyh rttkdkiasl slpasagftt ittnngdmqn
      781 qgveigvnyq ilrrkdldls fnwntaynkn kilklpfngv ennrqgglqv ydpkskelvw
      841 vggnqegqdp nvayayeaig iirtkeqlds yalqlkdlig artlvhpdvy nvmssseknl
      901 yyplalgdvm wkdvngdgii nsydrvymgn tvprwtggfg aalrwknisl strfdyalgy
      961 vaydgprawf lgmmqgtfnt ttsvfdtwtp enpnakypty ywadqlfknn tsressmfyn
     1021 kgnylafrei nvsyrlpksi anrlkmedls isatgqnlhy wskntlfspe sgsvgqnggg
     1081 yplpktfilg lqltf
//
LOCUS       WP_120335386            1053 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_120335386
VERSION     WP_120335386.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..1053
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114288
     Region          24..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhkllsfll ggailtsvaf aqekkvsgrv tgtngeglpg vtiviqgtnq atqtdangny
       61 sinvptgkil vfrsvgysdk titvaqgssl ynvqlndnes vldevvvtga glqasrrsvg
      121 vaqttikaed lmqakpsnvv tgltgkvagl lvqgvtsgvn pnfrvmlrgm rsltgnneal
      181 ivvdnvivps silgnlnpdd iedvtvlnga naaalygsqa angalivttk kgkgslgfqi
      241 dlentttfes vnflpkmqkl fgsgsendiq sydphenqqy gpifdgvirp igdklqdgsi
      301 qnipysyagk kgkdgfwdtg vtnmtnlsis sqsensslrl sgqyltstgt vpgdkynras
      361 arlsgtrkll egldltysty yaqnryntts vagdiyervl ntpgqipltd ykdwknnpfa
      421 spdgyfnayy nnpyfmadny rsrtrndyfi gnlelkykpi ewfdvlgrvg vttsnqsfkn
      481 ttgvytfsdf tkswagtsty kyqnilggvt dgfnystriv sdfiahaynk agdfkidytg
      541 ifqfiqneys gmsanvsgla vpgiynlgns tnnpgasqas ylartfgltg kidvgykdyl
      601 fltvtgrndw vsilepnnrs ffypsaalsf iptdafeglk dfkaldflki rgswskvgqv
      661 nlgsstdfga yrllptfsqg sgypyngvgg htvgnqlvqd glkpemtrsf evgfesawak
      721 rrinwdftyy dnrttdnvvp tgvstatgys sylvnagttt gkgvetrlnv ipirtdnwel
      781 slggnyayfn nkvesiaegl evlqlgayts gssagagsya vagqdfpvlr gtyykrddlg
      841 riivdpvtgy pssdgslkil gkampthtlg lnldltwkdl sfhtqaeyrt gnyiynaggs
      901 tfdfsgagyn tglynrdrfi ipnssywdaa sqsyventsv tvrdggpgyw tiagprtgiq
      961 enyitsgafw kiremsvsyr ipksalagqn vikaarvsvq grnlfiwtpk tnvytdpeys
     1021 dgngssngna igltnlgqtp psryigfsvn ltl
//
LOCUS       WP_120335510            1107 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120335510
VERSION     WP_120335510.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1107
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122855
     Region          144..1058
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnekffkrsp aflnpellsv klttlmtigl lscsiqqsfa qrihidttkk plktvlkqie
       61 eqsgysfvyd agiventamf qisldedgiq aalsklakel hvdykivnkt itltrikeke
      121 gtillkgrvs iddqdgksps yqagvsvaik gtnkvtstnn igefslevpm eativvsyig
      181 yksreipakd irknlaivlq ksmdyldevi vtaygtkear enqtgsafti trkdldnrpa
      241 lrldallegv vpgvefnsqd ggtnssarsr ystrirgess tvggttsnep lwvvdgvply
      301 tggttnsipg mqnsisplty inpndiesvt vlkdasatti ygangsngvi littkrgkga
      361 pkltysfrtg inrrpsshln qlngrqylnl vkdmgmvdql gkidtsqdtr wadvynrtgf
      421 tnlhslglsg stdavhyfls aniydekqti ignstkrydv rsnvsgnvgk rlvlnstlaa
      481 syskddmfnp gnayfqyspl ispfgpngey ierdpnggll qgmpglidqn eqkqatahvl
      541 gtlgftyqlw dglvftnlng adftsanedq yfsmynytgs ssngeayrgq sqvlnlistn
      601 tlafkrtifk gdfdvvlgie arkeerrsvs atgsnfpndy irevgfvstd nrlgttsrdk
      661 qtllsyfgra gyvydkryai nytyrkdgss nfgkdvkwgt fssvgaawti sneafwpknk
      721 ivdflkfkas ygnngnsrfn sayasgiyky dsnysyggss gttmsrgvnd glkwettkml
      781 ntgidfrllg rwnvaaeyyr nvthdmidda yvsmvtgfrr tyqnvgkmqn agvelsvnga
      841 ilqkenfnwn atfilssnrn kvlqlnedid rvsgntimrk gynsrsyylv rwagvdpstg
      901 dpmwydldgn vtkvyntenr vlvgnstpqy yggltnyvny knwnfsiffk yskggyyfdq
      961 atrnngldgl nilsgnqsid mlnswyfpgq latsprlsnt stssimnstr flldktylkl
     1021 dnisvgytfn sglirrlkld hisvtamasn iamwtpyssk kgsiknyevl akqygvtngs
     1081 vvdntyanml sessrvlnys lginigf
//
LOCUS       WP_120335766            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120335766
VERSION     WP_120335766.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120430
     Region          24..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrclisllvi lcysltvsaq grysgkvmdq hgkpianvni rlektgqsfk tdkngifvia
       61 nvpkplavav smlgfetqrl lwndytdklk vdlmqkeqll dvvevntgyq sfakerstas
      121 fsqidstklt trisnnilqk leylapglqf dnrtgksvin irgintfsdn lmqpliivdn
      181 fpysgdiani npndvesvtl lkdasaasiw garagngviv inlkknskgy nkmefthnlt
      241 fgekqdlfyl rnisstdfid vermlfdkgf ykaslnsvns rllvfspvvq llyqqskgli
      301 smeeadrqin sfrnhdyrre lmdnlyrnpi rqqyhlsndl ardkftnrfa lgydrnteqq
      361 qasnnqhltl qtsnrydfsd qlqlqvgmaw snqkstsspt fpsfpinplg gkaalypyaq
      421 lksddgssla ipynynlyfv qnipetqlld wtykpledyk esqsnsntkd ivlnatltyk
      481 pfpflslsgl ynyenqsvdt ekrngvnsfy trdlinrfsq vengvikriv plgdimqnnt
      541 srmlshkarf qassdfslqe dwkfnlfaga eishastdtr lntaygyden tmtsinvdpi
      601 ntypiysnls gnsripfytg fgrnsnrfvs lfgnaavtyk nryianfsar rdasnlfgvk
      661 tndrwnplws aglawvvsne kfmdklnwid llkfrttvgh sgnlggvstt lpiiyydnpr
      721 ndleterkas vgelpnpnlk wedvrmnnfa vdfaflngrl sgsfdyyrkk stdllateki
      781 dptlglynmr rnvgelkgrg fdlnigyrqa lnkslkigve alfafstdkv tkykgtvsna
      841 lfyasaggra lmpyegrgly pvfsypfkgl dpntgdplgw yrgevsknys gmlydsvqnl
      901 nyhgrglpty qgslrpsiqw kgfqaslnlv ykfgyffqke tinyaalfks wkgnadfadr
      961 wqqpgdeart svpsmvypan asrddfyans smnvlkgdhi risdirlgys faaktahkpi
     1021 aiavngyvnn mgiiwrknky gldpdsygip airtyglnin vky
//
LOCUS       WP_120335465            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120335465
VERSION     WP_120335465.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123144
     Region          51..1115
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhnylpskhs iltmlllrsn iradvnwalr lglmgllsts yllanaqqna tingvikdet
       61 gkpipsatvt irnatsgmkk tttsrpdgtf sldqipagqg yqisvssigf ksrelldyti
      121 tdrdklaini slessaqnlq evvvtalgik rekkalgytv aelkgdeltq gketnvanal
      181 sgkvagvqvs raasgaggss kvvirgnnsl ignsqplyvv dgvpidnqni sspnqsggtd
      241 ygdgigninp edietmsvlk gpnaaalygq rgsngvilit tksgkagktr fsygtdfslg
      301 nglvlpdfqn vygqglngtf thfrkddgti vsmsealkng ysgmpkmsag rdrttraswg
      361 akmegqtyed aygnilqltp kpdtyssffq tekqfvnnls iyggtdkvny rfsfantdvk
      421 gyiptntlkr nnfglrtqak itdkfhidik anyiaqkgqn rptladaadn paylfisqpr
      481 slgndimaqy kwtaqeisrq lgfsgltegl ektyatnsst anpfwtihen hnedrrdrii
      541 gllrlsydfa pwlkvtatgg tdfytdqrfr yrpintyqsl nrkgdireev irarednfdv
      601 lassnfkltd diklsanlga shqsrylrmt gnsgnqfivp nlfvinnttt nsyifdlies
      661 kinsaylsgq fsykdywfvd fsarndwsst lskennsffy psvssslvls dafkwqsdal
      721 sfakirgswa qagssgnpyq ltgayslnqy thggvpmasy teiipdpnlk nelttsieag
      781 adlrflknrl sfsftyyqak tknqildvpi apsslyvknr inageisnrg iefvlgatpi
      841 ksesgfewnt tfnynrnrnk veslypgves fllatdrgin vvaevgkpfg qligtqfawi
      901 kddqgnrlid pttglplrta grvetdlgna qpdwlggfan tfkykgfnly alvdirqggv
      961 ifsqsnreqi iygtskktle grdgtyvaeg mvgqkdgsgn wtstgtknsk qvaaqdywnm
     1021 vasdkevmvs eemindmsyi amreislsys fpkklmphkl vnslklgvyg rnlfyfqrkt
     1081 dgfspeasaf nvnnssigie stslpmmrtf ginltvgl
//
LOCUS       WP_120336055            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120336055
VERSION     WP_120336055.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111460
     Region          30..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlnkknpqkk nllifallsa glthvhaqqq qvkgavqnek geflpgvsvk aiqvnggpsv
       61 ttstnsqglf hfqnlvehag yrfvfsavgf qsdtlsgyvv earkplslsv klqqsavkld
      121 evvigygrvs rkdltssist ikaedanvgv ftspaqmlqg kvagltissn nsnpnatpsv
      181 slrgastlrs geamepyyvi dgvpgaslal vapddiasid vlrdasatai ygskaangvi
      241 ivttkrgksg qtninyngyl aidkvakhye mmnaaqyqsy vndngfsmep tddlgadtdw
      301 qravertgis nnhnisilgg aektqysisl ntiknngvik gtdmgrqiar aflqtkalnd
      361 rltasfnvna sitkqndvla ldqglsvyda myyylpvspv rntdgswfek adrsqyanpl
      421 slieentnfs ktkvlqahak lgyeilpglt ynidlslqnr qfnnaqyysm fsmaargqng
      481 ksiraavede rkvmemnlsy ektfagkhkv aalagyswee nnnndgfqlt tsdyysddls
      541 yynpgmanvv dllgfgnyyl stlrmisvyg rvnyaynnky llqatvrrdg ssafgtnnrw
      601 atfpsvsaaw rlseesfire tgifddlklr agfgvsgnsl gfdaftaqsv rgasskffdy
      661 vsadgqvspl rtlmvlrnsn pnlkweatsm inlgldfgfl knrltgslev ykkktsdliy
      721 dyqvskskyi yptltanvge ienkgielsl nakaidkedf kwntglvlsh ntnkvvsian
      781 eqftqdyiel sdlggagqtn vfqqrltpga pigqfytwew agyndegvsv fytrdektge
      841 rtgettttpq kkdqavtgsp qpkltlgwnn sfsyknfsln gmfqgafgqk imnatrarhs
      901 nvvgnagqkn vlasvveter mtdinahyls drylengsyl rlayvtlayt ipmknipikn
      961 lrvyatmnnv fvltkykgid pevglggltp gidnrqtypr trtfmfglnf nl
//
LOCUS       WP_120336144            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120336144
VERSION     WP_120336144.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121464
     Region          34..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkilkpninl illftfltlp lafvqgqqnv yifkgkvids ltkkgiaavs irdiatgrna
       61 ttdqkgefqi qyqsapkkav vfsilgyetk aindngvgky ltvelapkel rleeatvstg
      121 yqikprervt gsfelvgrsq idrrihqnvl eqlngrvasi rfdvpnvssn vtpkmnirgr
      181 ntifsndqpl yildnmaydg ditlinsndi esitvlkdaa assiwgarag ngvvvirtks
      241 gkandrptvs fnsslaytpk pdlsrlkris ssdfidfetm lfnkgyydsq ltrpypvaqt
      301 pvvetlvllr nglidaqtas sridklrkid vrddveryly tnklvqqygi nikggnnvlr
      361 yflsanydhn kedkvknsnn rfsirsntsy qlgkklelts nivfsqktlt nlypstlndl
      421 tsfslgsgkf lypyaelaae dgaylslpng lrdtfkksam ekglldwtft pldeiyhnts
      481 nstnksteyl fnpsllyrpi egvslvanyq yqkqvgnqqt lrdrnsydvr nlinrfaqvs
      541 atgvvsfpvp vgdilqtead eqrsqqgriq anfersfdtn hhldamlgme vrenkivdhs
      601 niaygyaerg lvsvpvdyvt rykyydasgs gnipygvsmt sttsrffsyf gnlaytykgr
      661 yslsgsarvd qsnlfgvktn nrkvplwsvg glwhihqedw lkrdwvnkls lrstfgysgn
      721 vgdavgitti tlsnayltna pradvqnppn eslrweknrl lnfgldfgff knrlsgsley
      781 yakrntdlls nsdidpttgl gnlsgksvfl gnvatttgng vdltlnavni rqpkfgwest
      841 ivfsvnhskv keyysqstta qsyinsnnav tpligypvyt vfgyqwagld pengmprgyl
      901 dgeisneysk imnapvgtla yhgpakatvf galtntlryg dlsltfnldy rfgsyfkrss
      961 isygmmatsw aghadyadrw qqpgdekrtd vpalvypfng natsfyigss alvekadyia
     1021 lhdvyldytv rpellkrygi kslvlkgyvs nlgylwlans rgldpfyent irpqksftlg
     1081 lnltf
//
LOCUS       WP_120336188            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120336188
VERSION     WP_120336188.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122680
     Region          38..1096
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqqfstgkrp akgallllla iafgqkgfaq qsgelvvivq dakskglana tvtiknkssn
       61 lkrsgqadqq gkavfnnlpv dsnycilvty tgllpkeecq yivtsgkrss vvfqltdaas
      121 nqmdevvvvg ygtqkktnls gavdqisgdv lesrpisnaa qglqgispnl niqfnsgapg
      181 aepkinirgi tsinggdpli lvdnvpisaa eliriapqdi esftvikdas aaaiygaras
      241 fgvliittkt gkgdvkvnys nnftwntptv mpdkitdpyv fsrlletstd ntpwdnvnys
      301 dqfyqyaker sdnpsiagvr inpsdskvwe ymgnrdwtry flsdwnatnt hdlsisgsne
      361 kvqyyisgsy nrqnspvkla edyfdrynlr skvnyrlsdf isfgnntvig strrltpsqm
      421 slpdiynifp tsfdknpdgt wanssagiia aqmvdggksd rkrldvqstf ntelrffgnk
      481 fkvnadytfq rnslnrnwyt kqyeigygpd dvrkegttga yreagfsyyn vyniygtylq
      541 sfnkhqvnav lgfnqedyry evitaeragl isesfptiqf atgtmkmgea idtyalrgaf
      601 yrlnytyddk yivefngryd gssrfpkskr fgffpsgsaa wridrekfms svagldllkl
      661 rvsygqlgnq svsnygylps mekkdadylf gsergiyigv pplvspnytw ekvntvnfgl
      721 dvavlknkls asfdyysrrt lgmltlgrdl pnilgasepr enaadlktng weltvnfqdr
      781 felanaplrf naklllsdsq skitrfdnpn ksilqyyegm qmgeiwglqs nglfkdeaei
      841 akldqtsiip wgalsivpgw ptyvdqdgng kiekgytlgd tkdlkiigns tpryqfgidl
      901 sadwkgfdlr affqgigkrd yypldylywg tyqqpygnfy ghlldfyrpg sdsdidrakh
      961 sqaylnlgla dqnlnaaypi lqswladrnl gtridqaqgl aipqtnylln aaylrlknlt
     1021 igytlpksit srakisnlrv ylsgeniiew savkryfdpe tlnentytnp tagsdrvgng
     1081 ltypfqrsfs agiqvtf
//
LOCUS       WP_120336361            1055 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_120336361
VERSION     WP_120336361.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..1055
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117249
     Region          66..1052
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfklsysisp kvtgltlsla mlaaqgfsqt rsfqgrlvds lsqgaihgat irnshlaklv
       61 ssdhsgkfvi dahigdtlri gymgylpkvf ivgnqpssvi slipnqqsln evvvtalgik
      121 kekqaigysv qeikgkdmvk arepnaisgl agrvsgltit pstnlfgdpg itlrgrsnil
      181 ivvdgmpint dswnlspddi esysvlkgan aaalygnrgq ngaivittkr aksqdkgfqv
      241 efnsstqlqt gynaipkiqt eygpgsnyqy afkdgrgggi ndndyniwgp rfegqlipqy
      301 nspidpktgq liplpwearg kdnlkkflqn gllstnniai stkndhgdlr lsasqmfqrg
      361 ttpntklgst ninltggina gsklrfdasi nynkqyspny pniaygpnsp iyiltlwgaa
      421 dydiddlrny wqpgkenvqq ynreytiydn pwmtayenlr tydkddiygy vsanykfndk
      481 lslnartsas twnrnrtiki pisanlynyn iggsrvggyq etydtfwenn tevslkyqnr
      541 iaedigfsgs vfgnlrtvsv kslfartdrg ltvpgvydls nsimptvstn dralrqvgsv
      601 ygfmdvdyks mlflnltgrf dksstmpvkn ntyfypsasl savisqmvsl pkvisalkir
      661 gayanvasdf vnesaqydiy kllpaysnyg rwansmtgvt ytdvlpnpdl vaervktaei
      721 gletrlfnnr lgfdfaffrn legpriiela tsvtsgvrar qtngltllrk glelsidgtl
      781 iqqkdfswnv mvnastnhaw lhdidghqtr sgnvrvgerw dgyyvndfqr dekgmpivgt
      841 nglpaynpyv srigysdnkf tasisnsfry rdfsfsflvd grfggliknv qdakqwgsgt
      901 hpesaneyrl kdwenrdvkd ykgtvmtngl kivkgqlntd qdgkiisdtr efapndisvl
      961 wqnwatnyyq sgpitaksrt fvklreivfs ynvpanllkn srffrsasvs vvgrnllyft
     1021 gkgtqnmdld qftsassdyq tpsvksfgln lnatf
//
LOCUS       WP_120336579             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120336579
VERSION     WP_120336579.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108025
     Region          27..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkllaqcv mtltfllvsf ivvaqtkvlk gkvvdetqgp lagatikvkg gtaatttdte
       61 gsftftvpse aktlevsfig ytlkevpivg nditialeps agqgldevvv igygtarkkd
      121 ltgsmvtiga knfnkgimts pdqliqgktp gvmvinntgq pggsttvrir gnssirasnn
      181 plfvldgvpm sgnsplpegr ggfssdrgnp ltylnpgdia smdilkdasa taiygsrgan
      241 gvviistkrg kvgqpevsvg asagvstmre ypdvldaarf realkyytps evanadfggn
      301 edafkaitrk aitqnyyadv aggteygkyr lsggylnqng iirgsqlkky tanfngnfrf
      361 lenkrlgldf avfltqmdnk yapinamvgs egnvisqalq wnptrplrdd qgnltfvsst
      421 trnpltsida fkdlattntm vinlapyyki tddleyrfiy samrqtgnre gmyraglidp
      481 savnneqafi snngetnlqm thmlsynkqi nsdwsvnava gyeyldynyn nnisfgggfr
      541 ymgldyfdyl qytpvstrei ssyrsptnql qslflrggfn yldrylltat vrrdgstkfg
      601 snnkyamfps lavawnvnqe eflkstgifd qlkvrvgwgk tgnqefpsga slnrlvfgnq
      661 svsqanygnp dlkwetstti nagidfgiwg nrlygsidyf nkkttdalfe qtlaqpapag
      721 riwvnldgei vnkgvevalt gtiikndnwt wdltgnatfl knsvsglvgy yetgalrgqg
      781 fsgvlgqrmv ngqplnvwyl adyqgidpqt gmsmyrgqdg sistandpai nkfymhspnp
      841 ttllgistnv nykqfslaan mngafghylf nntaattlgl snlssrnigs affntavkes
      901 tsnsaapstr flekgdylkm anltlsyrvg nvgrtlknln vsltgqnlfi itkytgfdpe
      961 vntdgatngi pslgieylpy pparnillgv nfsl
//
LOCUS       WP_120336653            1135 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120336653
VERSION     WP_120336653.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1135)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1135)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1135)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1135
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127818
     Region          145..1131
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklnvyhfek kvaatdlpkd vgkylsklvl sglllsvtmg vshaqnitlk ehkssmyqvl
       61 ekirkqanad ligdlallkn skpisiqadn knivqvlkei senqpvdllf qnntilvrrk
      121 qpaatgpvsd qrprqgaers veqhirvrgr vqdntgkplv gvsikvvgsa nsgvlsgeng
      181 vffvviskkt ellfsmvgye skrvevsspe pltvileqvt nkieetvvtg ytkvrrdnft
      241 gaatmvtrqd lekfnstnif tvlqaldpsf kvdervtags npnvmpqini rgvssvgeya
      301 vnapliimdg fevplttlyd idvnriesis ilkdasstsl ygsrggngvv vietrlpkdg
      361 kftvtydmkp svamvdlsdy nlmnaaeklq yekladlyts rsgdpswdli qqesynnlla
      421 kreqdvaagv ntywlkqpvr ntlsinhslr megggngvry sleggyfdnk gvmkesgrtr
      481 gnagftliyr ipnvitfrnv gtylyskayn spygdfktyt tlnpyeriyd drgnynirfg
      541 elgqwyswgp tlynplynag lgfrdeqvsq tlqnnmsiew yalpklivra sgtivrtvtd
      601 ldrykspfht dfttvtdanl rgaytfgnqn ftkyegkvdm qysnkfgkhq lvanaiteir
      661 nqntvgnlnt vtgyvddrfm tpqmalqyav gslpkstslp vrsvgflgsl fytydnkynv
      721 sgtlrsdgas iygsqnrfgt fwsagfsynm hnekwfknsf ltklrwylna gtsstvsefn
      781 vgmvstaynf ftgqnyynqy aaiytgqgnp avrwpeqqqr siggefgikg dllrldvsyy
      841 dritnrmist vnvapsfgfy kdkffqnlgk vqnkgfeama nlrvlnntak dfswyisvga
      901 vqnrsklkei snelrtlnes lvkkdnkgnv irpsqfyqeg qslsviravp slgidpangr
      961 elyrdrngnv tyqwdannqe vvgnaeptly gnvgttvnyk glsvqiigny slggdiynqt
     1021 lmdkiennsp ylnadrrvle erwkqpgdls rfkaigdqsv tqpssrfvqt esflrlstin
     1081 vnysfsnail kryklerlrl nfsmndmfrw stvrmergid ypyarefnfg vmvqf
//
LOCUS       WP_120336731            1054 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120336731
VERSION     WP_120336731.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1054
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117399
     Region          32..1053
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtmyenlpkk cltgifmlll lvcqqlyaqq qrtvtgivkd ekgiplsdls ilekgirnat
       61 ktdadgkfsl plksanptli fsyvgyvrqe kqlragentl qitmkedgtg ldevvvmgyq
      121 dvqrrkttga iatvkgkdfe ntpyatfdam lqgrvagltv lstsgepgtn nivnirgtsn
      181 lgladnqlqa plyvidniiy dvsdiqaayg nasplqainp ndiesvdilk dasasaiyga
      241 raangviiik tkrpavgkpe irisayngvs srpamkpitv gaaerrlkmn llyqggsydw
      301 fnngsispml tdslnpafnn ntdwqglflq saninnvnvs igatmekfly rfsaqryyeq
      361 gvmmgfenen ltprlmlqan ptdnfqfetn lfagftkakh gsgddtkypf stwgfpssfy
      421 qitdvdqqiy tgrydgmmdr dnsfslngnf agtlkkflin gltlrsqfsf nvnnntrdlf
      481 rpklltgnrn yaqnwvnqnk rwewetyfny iksirnthni savlgtgier ntsnenymyg
      541 yndngtyvkt vtgipsgpdl yattsisers rvsvfgrfgy dykdkyllsa syrmdassry
      601 skdnrwgifp sisagwvlse epffqgakna isffkirgsy gitgrdpgsy yarytgltfd
      661 asyagsvlen gisgsvlsyn gkptvspdya aaatsptirw erspqfnagf dmnllhdrvt
      721 vtadfyvrds kelvynltmp atsgystvsn nfisvrnsgv emtlisrnma pssafqwttn
      781 fniaynknyv tslpdggkei qvgdvwmqra lnvgqpifpf kvwdtdgvya tnadvpvdpl
      841 tgkrlthfrg nsyqagdprr rdvngdyvid yndkidmgnp npdlvggfin qfsyknfsls
      901 tlvsfvfgrs lwngylsdkl qdagssalys twgtnsaiag dfkpsdfwmk dgdqtkyptl
      961 frntvdnwhi anstfvenas fvrlkniqls ytfpqamikk lklkmlriyg vvdnvavksw
     1021 ssvpdpeave angystgngy pipkkwtigl dvtf
//
LOCUS       WP_120336741            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium siyangense].
ACCESSION   WP_120336741
VERSION     WP_120336741.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium siyangense
  ORGANISM  Sphingobacterium siyangense
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Sphingobacterium siyangense"
                     /db_xref="taxon:459529"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120744
     Region          28..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfmrmlcils vwmcwltsys qvrernivrg vilssedsrp lqgvtvqnmf tnmrlksean
       61 gsfgisgdlr dtlrfsamgy qelrvlvkdv lakgrvlmav kdnyleevqi ntgyqilkpn
      121 ettgsasvis ndmlnqqtgt nilnrlnnva sglrfenqps tvsdrqklnf svrslstidg
      181 nldplivldg fiyegnvani dpnsiesvtv lkdaaassiw garagngvvv itskkggqga
      241 gkmmnttfss tlitkakpnl dqvyqlsnkd fidaesmlfn kgfydwlgng fqyisvtpai
      301 difdrtkrgl ltpadsadli nelmtkdgrk syrdlflesp fsqqyslnls ggsrqynygf
      361 sggytreide yagrsrklnl qltnsfqpte kldiainllf tnsisesgkp kfeslhyngk
      421 qvpymdfynn dgsqrafype frgtymteny gtpyldwgyy plsdykqavs ttrlnewyst
      481 isgkykilpf ldvsvgfqyq iqqtdlqgly neesyyarkn inqfmevsng gssityhipr
      541 ggikskdfss grsytartql nmnkswglhr ligmaggeir etaskgenyw vygykekplq
      601 avpvdfttyf tivpslvpmg itgspsftdr vnrfvslysn wsyifkdrya wsgsfrkdgg
      661 nifgaktndk wsplwstgls wdigkesfit hkdvdrlklr atygysgnvd lrktpqpias
      721 vtagtytrlp altisklndp slrwekvstf nlgldfslfk grlsgtvdhy iktgkdlygl
      781 tdfdytawgk sntvtknvas mrgkgwditl stnnldkavk wnsrlllnln knkttayyra
      841 lnggvssflg dgntitpipg mplnalsafk wmgldsegnp qgilrgevsk dyiginnaaf
      901 ndgleggsiv fygsakpqvy gslintfgwk swtlslnvsy kgdyyfrkpa tsyynlfnrg
      961 tafpdfetrw qqagdelkts vpsvqypled frdalyvqse vnvlkadhlr leyiniswdk
     1021 tlrlkkralr vkfygnvsnl gllwtankqn idpefpyris ppttlsfgcq lny
//
LOCUS       WP_120338586             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Cryobacterium soli].
ACCESSION   WP_120338586
VERSION     WP_120338586.1
KEYWORDS    RefSeq.
SOURCE      Cryobacterium soli
  ORGANISM  Cryobacterium soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Cryobacterium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Cryobacterium soli"
                     /db_xref="taxon:2220095"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34302
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqiiiigsg pagftaaiya aranmkplli assveaggel mnttdvenfp gfadgiqgpe
       61 lmakmqeqae kfgteviydd vtklefgdtv ksvtlgnget healsvifat gsayrklgih
      121 deerlsgrgv swcatcdgff fkekviavvg ggdsameeat fltrfaskvy iihrkdtlra
      181 skimqeraks hpkiefvwnt evvgidgeea veglrlrdtv tgaesslpig glfvaigndp
      241 rthlvhnlld ltsdgtiava grssktsqag vfaagdvidp tyrqavtaaa sgtvaaldae
      301 hylatlpedl laqagdpefa tvtn
//
LOCUS       WP_120338589             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cryobacterium soli].
ACCESSION   WP_120338589
VERSION     WP_120338589.1
KEYWORDS    RefSeq.
SOURCE      Cryobacterium soli
  ORGANISM  Cryobacterium soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Cryobacterium.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Cryobacterium soli"
                     /db_xref="taxon:2220095"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38658
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvgigrerr dgekrvaatp etvlqltalg vdvtvesgag lasgysdaay ekagahlapv
       61 fdattfdvlc hvrplspela atlpagtitv glaspaselp tvaalaaarv tsfalelvpr
      121 israqsmdal tsqalvagyr avleatirfp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsaydvrpas adevtsmggt fialdldave gaggyatela edravrqrel
      241 lapyvakadv littaaipgr papllvtrem vaampagsvv idlaaetggn vegvlagedq
      301 rvptsagdgv vtlvgmrdaa samasdasrl yaknvanlla lmttdgqvvp dfadevvaga
      361 cltsggevrh aptaaalegk n
//
LOCUS       WP_120347583             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia fungorum].
ACCESSION   WP_120347583
VERSION     WP_120347583.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia fungorum
  ORGANISM  Paraburkholderia fungorum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia fungorum"
                     /db_xref="taxon:134537"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39491
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatlv gmldpfnten ssklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvetvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltetd qvvvkhgvti vgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll ardgevtrks
//
LOCUS       WP_120346075             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paraburkholderia fungorum].
ACCESSION   WP_120346075
VERSION     WP_120346075.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia fungorum
  ORGANISM  Paraburkholderia fungorum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paraburkholderia fungorum"
                     /db_xref="taxon:134537"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35236
     Region          10..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpatstkhak vlilgsgpag ytaavyaara nlspvlvtgl aqggqlmttt dvenwpadah
       61 gvqgpelmar flehaerfnt eiifdhihta kldekpirli gdsgeytcds liistgasaq
      121 ylglpseeaf mgkgvsacat cdgffykqqh vavigggnta veealylagi akkvtvihrr
      181 dkfraepili drllakekeg vveikwnstl devtgdqsgv tglrikntkt gdttdialqg
      241 ifvaighkpn tdifagqlem kngyiitkgg lngfatatnv pgvfaagdvq dhvyrqaits
      301 agtgcmaald aqrylesiee igehvmsaea dr
//
LOCUS       WP_120342556             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia fungorum].
ACCESSION   WP_120342556
VERSION     WP_120342556.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia fungorum
  ORGANISM  Paraburkholderia fungorum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia fungorum"
                     /db_xref="taxon:134537"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39639
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigipaesr agetrvagtp etvkkltaqg htvlvqstag erahfpdtay eqagarivgp
       61 aealtadlvl kvqtptevel qhmrrgailv gmlnpfdvdq varilaagva afalesiprt
      121 traqsmdvls sqaniagyka vllaasvyqr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqveslgarf ldvpcetdee reaaqgaggy arpmpaswia
      241 rqsalvhera kqadivitta lipgrtaptl laeetvremk pgsvivdlaa gkgssvgdrh
      301 ggncpltead avvlrhgvhi agytnlpamv atdasslyar nvfdflklii dtdgnlkidt
      361 gddivaatll ghdasmlkta
//
LOCUS       WP_120349537             295 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_120349537
VERSION     WP_120349537.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>295
                     /gene="trxB"
     Protein         1..>295
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..295
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vqgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqa
//
LOCUS       WP_120351711             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sulfitobacter sp. D7].
ACCESSION   WP_120351711
VERSION     WP_120351711.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter sp. D7
  ORGANISM  Sulfitobacter sp. D7
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Sulfitobacter sp. D7"
                     /db_xref="taxon:1968541"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35658
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maetrktkvl iigsgpagyt agvyasraml epilvqgiep ggqlttttev enwpgdsevq
       61 gpdlmirmqd hakamgteii gdiitdldls srpfhakgds gttyvadavi latgarakwl
      121 gleseekfkg fgvsacatcd gffyrgqeiv vigggntave ealfltnfas kvtlihrrde
      181 lraekilidr lmknpkiepl wfheleevyg tdsplgvegv kvkhvktgei tdipakgvfv
      241 aighapsnel vkdtlethmg gyvvtkpdst etsipgvfaa gdltdhkyrq avtsagmgcm
      301 aaleaerfla evgdvegkdt slplgygaev kedv
//
LOCUS       WP_120353856             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Alginatibacterium sediminis].
ACCESSION   WP_120353856
VERSION     WP_120353856.1
KEYWORDS    RefSeq.
SOURCE      Alginatibacterium sediminis
  ORGANISM  Alginatibacterium sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alginatibacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Alginatibacterium sediminis"
                     /db_xref="taxon:2164068"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33810
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvqhhkli ilgsgpagyt aavyaaranl npvlitgiqq ggqlttttev enwpgdakgl
       61 tgpvlmdrmr dhalefdtei iidhitsvdf sqkpyrlkgd sveyscdali ictgasaryl
      121 gleseeafkg rgvsacatcd gffyrnqkva vvgggntave ealylsnias evhlihrrds
      181 frsekiltkr lmdkvaagni ilhldqtlde vlgdemgvta vrtqhvatge tkdievmgaf
      241 iaighspnte ifadqldmen gyiqihsgit gnatatskeg vfaagdvadh iyrqaitsag
      301 sgcmaaldae ryldsl
//
LOCUS       WP_120356679             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Alginatibacterium sediminis].
ACCESSION   WP_120356679
VERSION     WP_120356679.1
KEYWORDS    RefSeq.
SOURCE      Alginatibacterium sediminis
  ORGANISM  Alginatibacterium sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alginatibacterium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Alginatibacterium sediminis"
                     /db_xref="taxon:2164068"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53840
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipkesf dnesrvaatp qtvvqlialg fevlveegag skasftdqay ldsgatitqq
       61 qqildcglil mvnapnqdel qaikagttvi sfvwpaqnpe yleaaraqgi nllamdmvpr
      121 israqsldal ssmaniagyr avveaahnfg rfftgqitaa gkvppakvlv igagvaglaa
      181 igaagslgai vrafdtrpev aeqinsmgaq fleldfeeea gsgdgyakvm skafieaema
      241 lfaeqakdvd iiittalipg kpapelitea mvksmkqgsv ivdlaaatgg ncaltepgev
      301 vqregvtiig ytdlpsrlpa qssqlygtnl vnllkllspe kdgnidlnfd devirgvttv
      361 reqeitfppp aikvsaqakp qpakavnapv veeapkrpwl kpllaaiavf gfakvanaap
      421 veflqhltvf vlacvvgyyv vwnvshslht plmsvtnais giiivgalvq mtaqasgivl
      481 flsgiailia siniaggftv tqrmlkmfrk d
//
LOCUS       WP_120359449             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bifidobacterium pseudolongum].
ACCESSION   WP_120359449
VERSION     WP_120359449.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium pseudolongum
  ORGANISM  Bifidobacterium pseudolongum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Bifidobacterium pseudolongum"
                     /db_xref="taxon:1694"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33202
     Region          6..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseirdviii gsgpagytaa iylgraglkp lvvagaltpg gqlvntteve nfpgfpdgim
       61 gpdlmenmqr qaerfnaeiv fddvestrld etvktvtcsg gdvyqaravi iatgsyyrhl
      121 dvpgeekysg kgvsfcatcd gfffrgkpiv vvgggdsame eagflsrfgs svtllhrrdq
      181 frasqimvdr tlenpaidvm mntvvering dgkgvtsvsi rnvvsgetge lpangvfiaa
      241 gqvpqtaflg gvlelddhgy ivvegastrt nvpgvfaagd cadpvyqqai saagtgcraa
      301 ldvqaylesl vaeaaea
//
LOCUS       WP_120367460             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter cumulans].
ACCESSION   WP_120367460
VERSION     WP_120367460.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter cumulans
  ORGANISM  Acinetobacter cumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acinetobacter cumulans"
                     /db_xref="taxon:2136182"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33537
     Region          8..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdahglt
       61 gpalmermqe haerfgteii ydhinevdls qrpfvlkgdm deftcdalii atgataqylg
      121 leseaaymgq gvsacatcdg ffcknqkvmv vgggntavee alylsniash vtlvhrrdsl
      181 rsekilqdhl fekvkegkis iiwnhqvdev lgdaqsgvts vrlkstqdds tqnvdvtgmf
      241 vaighkpnss mfegqltlrd gyvqvqsgta gnatqtsvag vfaagdiads iyrqaitsag
      301 sgcmaaldae kyldal
//
LOCUS       WP_120368560             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter guerrae].
ACCESSION   WP_120368560
VERSION     WP_120368560.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter guerrae
  ORGANISM  Acinetobacter guerrae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter guerrae"
                     /db_xref="taxon:1843371"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39798
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv tgenrvavtp etvkkligag hsvviergag vkaayidsay eqvgatikdd
       61 ayqgsqlilk vrapqsdeiq klsanttvva mfdpyrnpdl dqfasqnvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak eqveslggkw ldvpmspeeq aradeaakng ygwtpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 kvgetvften gvkilgvpni pstlsteasa lyarnvfnfv etlfdadknf sinpeeeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_120375108             316 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Acinetobacter].
ACCESSION   WP_120375108
VERSION     WP_120375108.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33593
     Region          8..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdahglt
       61 gpalmermqe haerfgteii ydhinevdls qrpfvlkgdm deftcdalii atgataqylg
      121 leseaaymgq gvsacatcdg ffyknqkvmv vgggntavee alylsniash vtlvhrrdsl
      181 rsekilqdhl fekvkegkis iiwnhqvdev lgdaqsgvts vrlkstqdds tqnvdvtgmf
      241 vaighkpnsg mfegqltlrd gyvqvqsgta gnatqtsvpg vfaagdiads iyrqaitsag
      301 sgcmaaldae kyldal
//
LOCUS       WP_120370069             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter guerrae].
ACCESSION   WP_120370069
VERSION     WP_120370069.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter guerrae
  ORGANISM  Acinetobacter guerrae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Acinetobacter guerrae"
                     /db_xref="taxon:1843371"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33554
     Region          8..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk pvliaglqlg gqlttttevd nwpgdpeglt
       61 gpalmermqa haerfgteil ydhinevdlk trpfvlkgdm geytcdalii atgataqylg
      121 leseaafmgq gvsacatcdg ffyknqkvmv vgggntavee alylsniash vtlvhrrdsl
      181 rsekilqdhl fakekegkis iiwnhqvdev lgdntgvtsv rlkstqdest qtidvqglfv
      241 aighkpntdm fegqlelrdg yiqvqsgtkg natatsvagv faagdvadni yrqaitsags
      301 gcmaaldadf yldsi
//
LOCUS       WP_120375394             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Acinetobacter].
ACCESSION   WP_120375394
VERSION     WP_120375394.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39797
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaetv vgehrvaatp etvkklisag hnvviergag vnaayidsay eqvgakitdd
       61 aytgsqiilk vrapkgdeiq klapntavia mfdpyrnsel dqfatqqvsa falellprtl
      121 sraqnmdvls sqanlsgyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptar dqveslggkw ldvpmspeeq qkaadaakng ygwmpgeeyi
      241 rdqaiivdka vsnadivitt allpgrdapr likaetvakm kpgsiildma vetggnvegs
      301 vcgenvmtan gvkilgipni pstvsteasa lyarnvlnfl dtlfdaeknf ainpeeeiqk
      361 allvthsgqv llkrg
//
LOCUS       WP_120379588             329 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Clostridia].
ACCESSION   WP_120379588
VERSION     WP_120379588.1
KEYWORDS    RefSeq.
SOURCE      Clostridia
  ORGANISM  Clostridia
            Bacteria; Bacillati; Bacillota.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Clostridia"
                     /db_xref="taxon:186801"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36056
     Region          19..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maelftrkea nrmsdikmyd viiagagpag mtaavyasra nletlmierg ipggqmante
       61 dvenypgydh ilgpdlsnkm fehakkfgae yaygdikevv dhgeyktvva gqkeyhtral
      121 iittgaqykk lgipgeeels grgvsycavc dgaffkdknl vvigggdsav eegiyltrfa
      181 nkvtivhrrd qlraqrilqd rafendkidf iwdtvvekin esagkvgsvt lknnntgety
      241 dheidgvfvy igmvplsepf qalgitnedg yiptnenmet kipgifaagd irektlrqiv
      301 tatgdgsiaa eqaikyvedl meelktaqs
//
LOCUS       WP_120384193             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter rongchengensis].
ACCESSION   WP_120384193
VERSION     WP_120384193.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter rongchengensis
  ORGANISM  Acinetobacter rongchengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter rongchengensis"
                     /db_xref="taxon:2419601"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39891
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv tgenrvaatp etvkklisag hsvviergag kkaafidsay eqvgakitdd
       61 ayagsqiilk vrapygdeiq klaagttvva mfdpyrntel dqfasqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparivim gvgvaglqai
      181 atakrlgavv eatdlrptar dqveslggkw ldvpmsdeek qkaadaakng ygwmpgeqyi
      241 kdqaiivdka vsnadivitt allpgrdapr likaktvakm kpgsiildma vetggnvegs
      301 kngenvvtdn gvtilgipni pstvsteass lyarnvfnfi etlfdqeknf vinqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_120386321             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vreelandella alkaliphila].
ACCESSION   WP_120386321
VERSION     WP_120386321.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella alkaliphila
  ORGANISM  Vreelandella alkaliphila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Vreelandella alkaliphila"
                     /db_xref="taxon:272774"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33639
     Region          3..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 metrherlii lgsgpagyta avyaaranlk pllitglqag gqlttttdvd nwpgdaqgvq
       61 gpelmermkq haerfntevl fdhinevslg ekpytlkgds giytcdalii atgasarylg
      121 lpteqqfmgq gvsacatcdg ffyrnqeviv vgggntavee alylsniask vtlvhrrdtl
      181 raekilqdkl fekveagkia lewfyevdev lgdntgvtgv rvkstkdgst keihapglfi
      241 aighspntgi fegqlamngg yikvksgleg natatsvpgv facgdvmdhi yrqaitsags
      301 gcmaaldaer yldgia
//
LOCUS       WP_120384540             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter rongchengensis].
ACCESSION   WP_120384540
VERSION     WP_120384540.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter rongchengensis
  ORGANISM  Acinetobacter rongchengensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acinetobacter rongchengensis"
                     /db_xref="taxon:2419601"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33771
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliagmqlg gqlttttevd nwpgdpiglt
       61 gpalmermqa haerfgteil ydhinevdln vrpfvlkgdm eeytcdalii atgataqylg
      121 leseqaymgq gvsacatcdg ffyknqkvmv vgggntavee alylsniaah vtlvhrrdkl
      181 rsekilqdhl hekvkegkis iiwnhqvdev lgdstsgvts vrikstqdds tqdvdvsgmf
      241 vaighkpnts mfegqlelrn gyiqvhsgta gnatatsvag vfaagdvadd vyrqaitsag
      301 sgcmaaldad ryldgle
//
LOCUS       WP_120402993             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter tianfuensis].
ACCESSION   WP_120402993
VERSION     WP_120402993.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter tianfuensis
  ORGANISM  Acinetobacter tianfuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter tianfuensis"
                     /db_xref="taxon:2419603"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39610
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipaetv vgenrvaatp etvkklisag hnvviergag vnaayidsay eqvgakitdd
       61 aytgsqivlk vrapkgdeiq klapntavia mfdphrnpel dqfaaqqvsa falellprtl
      121 sraqnmdvls sqanlsgyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmspeeq qkaadaakng ygwmpgedyi
      241 rdqaiivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 vcgenvvtan gvkilgipni patvsteasa lyarnvlnfl dtlfdaeknf ainpeeeiqk
      361 allvthsgqv llkrg
//
LOCUS       WP_120403101             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter tianfuensis].
ACCESSION   WP_120403101
VERSION     WP_120403101.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter tianfuensis
  ORGANISM  Acinetobacter tianfuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acinetobacter tianfuensis"
                     /db_xref="taxon:2419603"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33582
     Region          8..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdahglt
       61 gpalmermqe haerfgteii ydhinevdls vrpfvlkgdm deftcdalii ctgataqylg
      121 leseaafmgq gvsacatcdg ffyknqkvmv vgggntavee alylsniash vtlvhrrdsl
      181 rsekilqdhl fakekegkis iiwnhqvdev lgdaqsgvts vrlkstqdds tqnvdvtgmf
      241 vaighkpnsa mfegqltlrd gyvqvqsgts gnatqtsvpg vfaagdiads iyrqaitsag
      301 sgcmaaldae kyldal
//
LOCUS       WP_120430637             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter baylyi].
ACCESSION   WP_120430637
VERSION     WP_120430637.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baylyi
  ORGANISM  Acinetobacter baylyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter baylyi"
                     /db_xref="taxon:202950"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39817
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigipteti agenrvaatp etvkklisag hhvviergag vkaayidsay eqvgatitdn
       61 ayqgsqlilk vrapqsdeiq klsanttvva mfdpyrnpdl dafadqnvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgavv eatdlrptak eqveslggkw ldvpmspeeq aradeaakng ygwtpgeqyi
      241 kdqaaivdka vsnadivitt allpgrnapr likaetvakm kpgsvildma vetggnvegs
      301 kvgetvften gvkilgvpni pstlsteasa lyarnvfnfv etlfdqdknf ainpeeeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_120427178             300 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acutalibacter sp. 1XD8-33].
ACCESSION   WP_120427178
VERSION     WP_120427178.1
KEYWORDS    RefSeq.
SOURCE      Acutalibacter sp. 1XD8-33
  ORGANISM  Acutalibacter sp. 1XD8-33
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Acutalibacteraceae; Acutalibacter.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Acutalibacter sp. 1XD8-33"
                     /db_xref="taxon:2320081"
     gene            1..300
                     /gene="trxB"
     Protein         1..300
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=31716
     Region          2..281
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mlivgggpag ytaalygara glsvlllekl apggqmgttd mvdnypgfpk gvngfdlamq
       61 mkecaerfga ktaleevsal eltgevklah tpkhiyqart vvlamgshpr elgleregdl
      121 rgrgvsycat cdgmfyrgkt vaivgggnta vsdglylsrl cdkiylihrr dklraplpqq
      181 kaleqagnve flwnsevtal lsgdrlsglr vrnkktgevq elacdgvfia vgqvpdaqla
      241 vgqvacsedg yvlagedtrt nlpgvfaagd lrkkplrqiv taasdgavaa amaqeyldgr
//
LOCUS       WP_120430643             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter baylyi].
ACCESSION   WP_120430643
VERSION     WP_120430643.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baylyi
  ORGANISM  Acinetobacter baylyi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acinetobacter baylyi"
                     /db_xref="taxon:202950"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33746
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mqkrhsklvi lgsgpagysa avyaaranlk ptliagiqlg gqlttttevd nwpgdpeglt
       61 gpalmermqa haerfgteiv ydhinevdls vrsfvlkgdm eeftcdalii atgataqylg
      121 lesevkfmgq gvsacatcdg ffyknqkvmv vgggntavee alylsniaeh vtlvhrrdsl
      181 rsekilqdhl fakekegkis ilwnkqvdev lgdhtgvssv rlkstldgst qdvevqglfv
      241 aighkpntgm fdgqlnlrdg yiqvhsgtsg natatsvagv faagdvadsi yrqaitsags
      301 gcmaaldaek yldqlsn
//
LOCUS       WP_120440819             337 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paracoccus yeei].
ACCESSION   WP_120440819
VERSION     WP_120440819.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus yeei
  ORGANISM  Paracoccus yeei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Paracoccus yeei"
                     /db_xref="taxon:147645"
     gene            1..337
                     /gene="trxB"
     Protein         1..337
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35766
     Region          17..322
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mshvpaeiad avlpahtrll ivgsgpagyt aavyaaraml qpvliqgmqp ggqltittev
       61 enwpgetqvq gpdlmvrmea hakamgarif vdtvvrldlk arpfvaelds garvtadavi
      121 latgaqarwl gleseekfkg fgvsacatcd gffyrgrevv vlgggntave ealfltnfas
      181 kvtlihrrds lraekilqer lfrhpkvevl wnhqlaeveg ttaplgvtgv rvrhvatgee
      241 rvvpadgvfv aighapasel vrdqlelhng gyvkvepgst rtsipgvfaa gdltdhiyrq
      301 avtsagmgcm aaldaerwla ehamagapnp egaeipa
//
LOCUS       WP_120441865             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            yeei].
ACCESSION   WP_120441865
VERSION     WP_120441865.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus yeei
  ORGANISM  Paracoccus yeei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus yeei"
                     /db_xref="taxon:147645"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55398
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkesy egearvavtp ssaahlkklg hevfvesgag vragfsdaay qaagvtvept
       61 aaalindvdv vvkvrppema eiaqmrrgqt lishfwpaqn aelleaareq gitaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv livgagvagl
      181 aaigaatslg aqvyafdvrp evaeqiesmg aefvyldfkd qvqdgaatgg yaapsspefr
      241 eaqlakfrel apemdivitt alipgrpapk lwtedmvaam kpgsvivdla aerggncdlt
      301 vpdqrivten gvvvigytdf psrmgaqase lygnnirhml adltpgkdgv ivqnmeddvi
      361 rgatvthdgd vtwpppppkv aaiaaqkpke kpkeltpeek raaevaafra qtksqvtlla
      421 vgailmllvg mfapasflsh fivfvlsvfi gfqviwnvsh slhtplmait naissiiivg
      481 allqigsgsw lvvllaalsv lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_120459439             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            parahaemolyticus].
ACCESSION   WP_120459439
VERSION     WP_120459439.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54733
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvviesqag vlasfddaay eaagakvvss
       61 devwasglil kvnapivdee kgideiallq ddatlvsfiw paqnaelmeq lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaefltv dfqedsgsgd gyakemsddf
      241 nkkaaelyae qakdvdiiit talipgrpap klitkemvds mkagsvivdl aaanggncey
      301 tvkdqvimtd ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvikeg eitwpappiq vsaqpqakqa qpvkkepkve eptsptkkli glvaavgafa
      421 wiasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvsflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_120463476             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus aceti].
ACCESSION   WP_120463476
VERSION     WP_120463476.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus aceti
  ORGANISM  Paenibacillus aceti
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paenibacillus aceti"
                     /db_xref="taxon:1820010"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33938
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myktiiigtg pagltaaiyl aranmkplvi egpqpggqlt tttdvenfpg fpegimgpvl
       61 menmrkqaer fgaefrtgwv nsvdmskrpf klqvdglgel eaeslvlstg asakylgipg
      121 eqdnvgrgvs tcatcdgfff rnreiivigg gdsaleeagf ltrfaskvtv vhrrdelras
      181 kimqdrvrsn ekvewalnrt plevitnemg vtglkvrnna tgedeiipat gvfvaightp
      241 ntgflagqid tdengyilvk pgtsetnipg vfacgdvqds ryrqaitaag sgcmaaidce
      301 kyiealeheq keltak
//
LOCUS       WP_120464220             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus aceti].
ACCESSION   WP_120464220
VERSION     WP_120464220.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus aceti
  ORGANISM  Paenibacillus aceti
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paenibacillus aceti"
                     /db_xref="taxon:1820010"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33763
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksivvgtg psgltaaiyl aranlhplvi egaqpggqlt tttevenfpg fpegvlgpel
       61 mermrkqaer fgaefkngwv eevdfsgspl klileggeel tsetvilstg asakylgipg
      121 eqeyvgrgvs tcatcdgfff rgkriivvgg gdsameeagf ltrfassvtv vhrrdelras
      181 kimqervren dkvkwalnrr pleiatddgg tviglkvrnn angqeeliea egvfvaight
      241 pntgflsgav atdeqgyivv apgttrtsap gvfacgdvqd tryrqaitaa asgcmaamdc
      301 ekyldgdmvh dwskml
//
LOCUS       WP_120467037            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            caecimuris].
ACCESSION   WP_120467037
VERSION     WP_120467037.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides caecimuris
  ORGANISM  Bacteroides caecimuris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Bacteroides caecimuris"
                     /db_xref="taxon:1796613"
     Protein         1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123601
     Region          32..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknrkegftp rvglflllvt fclgaiqaqs skitgyvkdq sgepligvnv mekgttngtv
       61 tdlngfysiv vkasnavlnf syigyknqei pvagkklinv tmkddsetld evvvvgygtm
      121 rkkdltgsvv qvrpdkiane npktvqdilr gtpglvvgyg egdagakggg emkirgqrsv
      181 ytdgghnnpl iildgmffqg elseinpddi gqidvlkdas aaavygaqaa ngviiittkk
      241 gkkgkpvvnf tasvgltqka ayrdrwqttd eylqhyvdwk ekntygvnae tgeyaaysrp
      301 gneytskpey frnpnnlsgv sleqwrnyst nregesdlsi warrlgfryd taaldnlllg
      361 ktvdwqdeaf rlgfnqdynv sisgagdkvd yylslgylrn egafvddtyr airanlklna
      421 kvtdwfevga nvnfqdrsdg eigmdkggfm enspyamlkd engnytqdpl myqydranek
      481 nwyfekqyiq lekgyttlnt ifnakvklpf nityqfniap rfqffydryf tsaerpnsnp
      541 ndrgtnreqa krfnwslnnt itwdqtfank hhviltlvqe aeerqywsdr iearnilpsd
      601 algfhntqng dkavstfrtd dnhqtadalm arafysygdr ymvtgtirrd gysafgannp
      661 yawfpsggla wsftnedffq kythimnsgk lrvsygkngn rslenpyeal anlypgggkm
      721 qgyitssgdl ylmrylmaqr mmnpnlqwek tqswnfaldf gflndritgt leyyrmstkd
      781 mimrqplsnf tgfenittnl gqvdnsgfev alntlnidkk nfqwsssfsl synknrikhl
      841 fgdrqdivda ngtvvgsrea dyvaagwfid kpisaiwdyk vtgiwqkdev eeakkygqvp
      901 gdpkvwnnpa ndqydadgnl vkviynnddk vfqgqtaapv twalrndftl wkdltlsvni
      961 ysrmghksle smylnndddg ggmtyrlvnk nakeywtvdn ptnkyariea qgpegakgar
     1021 rlynrsfirl enisvgytlp rawtekvqid rvkvygsvrn aavwakdweg ygdpetgnfa
     1081 sriwtlglnl tf
//
LOCUS       WP_120467520            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            caecimuris].
ACCESSION   WP_120467520
VERSION     WP_120467520.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides caecimuris
  ORGANISM  Bacteroides caecimuris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Bacteroides caecimuris"
                     /db_xref="taxon:1796613"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126640
     Region          36..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          114..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkknqaqkfi vlflfflfay swrveaqtgk ekqltmefkn eglpsifkrf ekvsgykvlf
       61 iydeissyts tgkvekatvd ealkviigkn plkyhidgqf initkkdskk ffsqvkgkvl
      121 seedglpvig atiivedpss nirtitdnng nfqlsdvpkd srvkisyvgl etqflnpssq
      181 msvvmkadtk aldevvvtgm fnrkkegftg savtikgedl kkystnnvak aiaavapglr
      241 ivdninmgsn pnglpdmrmr gganmdmatq savefnstsn dvlavqgeye tyanqpllim
      301 dgfeisiqtl admdpdrvas ivvlkdaaat aiygsraang viviesktpk pgriwvtygg
      361 elrveapdmt gynlmnarek idaelqsgly tyggetvekw klyqsklrev lagvntywld
      421 kplqtafqqr htvtleggde alryrmyvgy nsspgvmkds krdvltgsld fqyrlkkvll
      481 knsitldnsv anespwgsfs eytrlnpylr pygengeiqk rldnfegvgg essylnpmyn
      541 ttfnskdqsk nftvrelfrv eynptnelrf egafnlsksv ghrdifrpaq htlfdnvtdp
      601 tlrgdyrrsq seavnwgidl tgswnkqled hyltanarms vlennsetyg nyvtgfpndn
      661 mdnllfgkky nekvtgdert trsigwvaag gysykykysf dfnirldgss qfgrnnrwap
      721 fwstglrwdl kkenfmknvs fisdfilrgt ygttgsqgfd pyqahgyyty snlllpyyss
      781 datgseilam hnenlkwqtt kstnlalelg fldqrltarv eyyrkitdnm vtsvslapsl
      841 gfssypenlg kienkgweis lsaipyknta kqaywtitvn gsrntdklle iseamkhrnd
      901 mnasnlkdtp lpryeegesl sriwvvrslg idpasgneil lkrngemtsa vnwnandvvp
      961 igntepkwqg yinssftykg wgadvsfryq yggqvynqtl idkvenanlk ynvdrrvsql
     1021 rwakpgdkaq fralnpsgwd tkatsrfimd enifqgssls vyyrmdrtnt kfishwglss
     1081 akvtfnmedf fywstvkrer glyypysrqf tfalnvaf
//
LOCUS       WP_120468331            1205 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_120468331
VERSION     WP_120468331.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1205)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1205)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1205)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1205
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..1205
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=135234
     Region          127..1204
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkrlneerr erpciqswky lvgfllmfaf vaglaaqeke kkvtmkcvne kltdalkrve
       61 kqsgykivfs ynelhsirvn asiqelaape avkkliaghp vkssvdgryi hvflkkdkke
      121 tlekgllrgq vvdendeplp gvsvrvkngr stgtltdlng gfsipvkegq samltfsfig
      181 kktvekmvnd gwgvqvklee mvnavdevvv tgyqvmdkrl masatstvkm ddikiptins
      241 vdkmlqgtip glmvqnssgs pnatprirmr gsstiygnas plwvvdgivy edpidlsnde
      301 lnnvlmgsdm ldqvnqnatr sllgnaiagv npndiesitf lkdasataiy gtraangviv
      361 lttkkgkigk psisfsaslg ftgrprysqy nlmnskervg isrevvekgy lydympyatg
      421 fegalfdfys mkitksefde qvakyetmnt dwfkllcrna lnqdysasis ggnekvnyyt
      481 sigynnskgt tkgdnstsys ltsnisaylt kkvraytrls fsdqksdgfy ttnpytyalq
      541 ttraigpdey yttqintidg lsnnylltyn ifnelahtgn eaksrnfsgn vgidvkiwkg
      601 ltlqtlfglr yvnstnyqwa dersyyiagi rgydygtvip ngeeekkskl phggilnyns
      661 mnnvgytara qlsyattfge mqqhaingmi gyeaisnqyd gfndveygyy pdrgmavsye
      721 ydkesagsev lnnsslekht vsrkntknna vsayatlvya lknryifnan lrgdasnrfg
      781 qytnhkflpv wslaarwkin deswfrgwka ldnfsirfsy gqqgniptsv gpnlvaqyma
      841 lavnrfsgny qlgikrlpyp dlrwektvtt nygldfslln grisgtvdyy vrkgkdlifn
      901 lpvaseygtt qtfrngasmk nygievgltf ipvqtrdftw tltpiysknt nnisntakqd
      961 ytyldylagn afengkpvna lyawefkgld hetgramfeh cstnesevek sndpksylky
     1021 cgstdpkfng glstslrykn filnaqfaya fghvkrlnfl fsgtmkmptp qtnlttdflh
     1081 cwrepgdeeh tdipgiafde arnyfvytpi anatqqntyd mynysdvrvv kadffrcrnl
     1141 mltytlpdkw lqplniagms csfnvtnlft lcsskfngqd pevdstgsva lpitrtysfs
     1201 vslnf
//
LOCUS       WP_120469694             993 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Bacteroides acidifaciens].
ACCESSION   WP_120469694
VERSION     WP_120469694.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         <1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          4..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 ssaktlqisy igmqtqevai kpqlkvilka daqqleevmv tavgiqraer slgysvskvd
       61 adeaiqkaep dlirsldgki pgvsinspsg aagsatrmti rgnssflgnn qplyivdgvp
      121 ysntevassn qateaggayg sgistldpnd iesmnvlkga aaaalygsra angvvlittk
      181 tgsknkkkag kgmeitlnas ytieqiaglp eyqnsfgtgn dfipggangs wgaaftdvte
      241 vplsiyannv ygkaypnlpq tvpykayknn vkdlfdlggi ydlslnfnky tetgnftatl
      301 skmdqdsyip yadfsrysis vggnqtlang vriggnvsfs rneqngpmfg nnqsngigas
      361 sfaralilgr nwdmslpyet pdhkslffvg dqadnpiwsw kyntintqmd rtianvnmgy
      421 ditkwlsvdy rvgindykmd rkevlnlgsr alggkgrilv stydtqeies tlllrfnipv
      481 hkdfglkatl ghnvnqftan etltkgmnim spgvyninnt esqtseeyyt rtrlwalfgd
      541 vtldyknyaf lnitgrndfs stlpknhrsf fypsiagsfv ftdafhined iikfgkvrls
      601 wakvgndaga yykngtftlg qpfngqpils lpssmfdpdl kpeftsevef gaelqflksr
      661 vnvdftwynr nstnqiapls lpystgygsy ytnfgkmnnh gieiglnvip ilnkdfkwdm
      721 yftytqnrse vkelaegver vslntgfatp kavlevgkpy gmlvgqvfar deegnylvdp
      781 nsgayliade egdlgdpapd cklslnntft ykgfslsfmf daqiggcvwt syipdllgrg
      841 vtkdtedryg srilpgylad pstkkplldg ngnkipnnvq mkeldlwfsp gsgvstfatn
      901 gvdeasvyea ttfrlrelsi gyqlpkswla ktfigsatvs fvarnlwyfa pnvpkysnyd
      961 ptassygggn vqgidytsap ntrrygfnik ltf
//
LOCUS       WP_120482990             307 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hominisplanchenecus
            murintestinalis].
ACCESSION   WP_120482990
VERSION     WP_120482990.1
KEYWORDS    RefSeq.
SOURCE      Hominisplanchenecus murintestinalis
  ORGANISM  Hominisplanchenecus murintestinalis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Hominisplanchenecus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Hominisplanchenecus murintestinalis"
                     /db_xref="taxon:2941517"
     gene            1..307
                     /gene="trxB"
     Protein         1..307
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32885
     Region          5..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdkvydllii gsgpaglaaa iyaqraklst vvlekeyisg gqvvntyevd nypglpging
       61 yelgvkfreh adqlgaefvt aeveeiiiee tvkkvessag eyrakalvla mgaahrelgv
      121 pgekelagmg vsycatcdga ffrgrrvavv gggdvaveda iflargcekv vlihrrdelr
      181 aakslqerlf acenveiiwd tavreinged hvesirlenl ktgekrsldm dgvfvavgvi
      241 pnsriikelv gvdengyila gedcassvkg ifaagdirkk plrqivtava dganavtavq
      301 eyllsvq
//
LOCUS       WP_120485909             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Anaerotruncus sp. 1XD42-93].
ACCESSION   WP_120485909
VERSION     WP_120485909.1
KEYWORDS    RefSeq.
SOURCE      Anaerotruncus sp. 1XD42-93
  ORGANISM  Anaerotruncus sp. 1XD42-93
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Anaerotruncus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Anaerotruncus sp. 1XD42-93"
                     /db_xref="taxon:2320853"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32904
     Region          4..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqydaiiig agpagltaai ylqragwrtv vleayvcggq mantpeieny pgysrisgve
       61 lstslynqav eqgariefdg vsavrlyeae ktvetqsgra fraravivan gakrrklgip
      121 geeelagrgv sycatcdggf ykgkhtlvvg ggntavedal ylsnlcervh iihrrdefra
      181 grvltdalqk renitihydt ipveirqaeg kpmvgeieve nvktggrtgi pvqgvfvavg
      241 fepdnqlfag qltldpsgyi vagedtrtnl dgvfaagdtr tktlrqivta agdgaiaafe
      301 aggylaaqa
//
LOCUS       WP_120488454             948 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bergeyella
            cardium].
ACCESSION   WP_120488454
VERSION     WP_120488454.1
KEYWORDS    RefSeq.
SOURCE      Bergeyella cardium
  ORGANISM  Bergeyella cardium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Bergeyella.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Bergeyella cardium"
                     /db_xref="taxon:1585976"
     Protein         1..948
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103659
     Region          19..947
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msvklkvlsa galfflgiqt idaqkkktds lvekkiedlv ivgfgqkrav keltgsvgki
       61 ggqdvantss asidkalsgk vagvqggmnt gqpggaanlr irgiasingr nnpiyiidgv
      121 rvaqgdltrn tttanilanf neadiesvtv lkdavstavy gadagtgvii ittksgkkgn
      181 arfsfsnetg vafkavkgee plstsewldl liagyantvn arkedvlaal qngtipptnr
      241 lgsvyakrhi ntnwqketek tggayfqkfn fsvsggsdrl tylsslgyfn qngvvkgtsf
      301 nritntnkis ykatdklnls tdlqfsygki ntvsdgatfs npllgwyylq ptdpvrnadg
      361 syyfgkggkl snnlfnvaal qeleyqtakt arvfanfqad yklaknlayk fvfapefini
      421 eednyrsplh gngynyggsv layssryfnf nvqnilsynf klgesnnfsa sliqeayksd
      481 vrkvggsanv vgspyletmn nfvvpreayg iksissrggy aatlhydydk lflldvsgrq
      541 dklsnfwpgk ktgyfwsaga gldlarleal kssntisqlk lsasygkvgn ladvspysly
      601 qytfnyndqa garvtgvdnq dlkwetlspf nvgldlglfn nrlsigaayf hkltkdlife
      661 lplspsqgat sqyqnigemk ntgfeftida kiiknagdgf nwnlggnvst lnnaitklyg
      721 gqdivindlr ihregevass fymrkwagvd ptngnplwyk ngvdgettsn yneaqkavqg
      781 saiatlfggv dtklsykgfs ldaqlsfgfg nkvydqfarl tqsdgamtlt ypgyrsqldy
      841 wspenpnasn pkpilgrgnk nanshssryl ykgdylrlrt vklayniksd alkqtgingm
      901 qiyilgdnif tynfdknykf dpdlqingyv nlqippmkty slgvninf
//
LOCUS       WP_120488756             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bergeyella cardium].
ACCESSION   WP_120488756
VERSION     WP_120488756.1
KEYWORDS    RefSeq.
SOURCE      Bergeyella cardium
  ORGANISM  Bergeyella cardium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Bergeyella.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Bergeyella cardium"
                     /db_xref="taxon:1585976"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33712
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meknildcvi igsgpsgyta aiyaaradlk pelytglqag gqlttttevd nfpgypdgvt
       61 gtqlmmdlqk qaerfdtkvh fetitkaefa tqkgrvhtlw agdkeilart viistgasak
      121 ylglddeqky agggvsacat cdgffykgre vivvgggdta aeeatylakl cskvtllvrk
      181 gefraskamv hrvmntenie vkfhheligi egennlvera vvinnqtket akievhgifi
      241 aighkpntdi fkgqinlden gyiltekgss htnipgvfaa gdvkdpvyrq aitaagsgcm
      301 aaidaeryla eleg
//
LOCUS       WP_120488862            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bergeyella
            cardium].
ACCESSION   WP_120488862
VERSION     WP_120488862.1
KEYWORDS    RefSeq.
SOURCE      Bergeyella cardium
  ORGANISM  Bergeyella cardium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Bergeyella.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Bergeyella cardium"
                     /db_xref="taxon:1585976"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112939
     Region          28..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrlnfnvlsa gvlfflgsqv ataqkvkkdt vrdidelvlv gyskvnrnef vgtatqintk
       61 sidnkavsnv sqalageaag vrvinttgqp gtsakirvrg fgsvngnrdp lyildgmpye
      121 gnisvinpdd iatmtilkda tatsiygarg angvvvintk kgranrssiq feskigmnls
      181 llpryeviks peeyislvwe glynqgkinp ailaqygfrt aeeyannilf sdygitplyn
      241 lwnvegkdli dpvtrqvrng vtrkytpenw qdyaykpalr tehnlsmsgg sdkttyytsf
      301 gylkdggysi nsnferystr lnlgfqpknw lrgtynmgya ftksqnngqt sdsgsvfwfs
      361 dsipsiyplf lrdangnrip ettlggyiyd ygyngrnfgf gtnaiadaty dkltntkhel
      421 naslnleadi tkhltfetrl sgqyfnnsrd nyknpyygsm assggsiski kheaftwnfl
      481 qllryknkfg nhgleafaah eandyeykyl ggdktglvdp ytgefnnaik tvalnsyien
      541 yklesffgsv sydyqnkyla sasvrrdgss rfsthkwgtf yslglgwvls renflkensf
      601 fsnmklkasy gtvgdqagvg yypgydvydi gnfmdapsas ynrkgykdlt weksrifqtg
      661 ldfsifknkr legsidyynk ttdnlifdrr lapsqgnaie ktnggalvnq giefnlighi
      721 ikkddfyldl svngeilrnk ltkmpidpvt grpkvidlse sgfgraqgys iydyylrewa
      781 gvnpntgaaq wtmhyvdvnk ngvydtgdea inslyeyqqn npgavisqtl tesyadatqk
      841 figksaipdl rgginlsvgy knislgaqml ysiggyaidy syatfmtnpt agnanwhkdi
      901 hnrwqkpgdi tnvprlsnsn rgdrnfsnqs srfltktdyf ilnnvniayt fdrdflrgtg
      961 ldgltislsg dnlwikskrk gfnpstseng essryayapl stftigikan f
//
LOCUS       WP_120489937            1198 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_120489937
VERSION     WP_120489937.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1198)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..1198
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134816
     Region          130..1195
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkqqitlle krtkkklvwm rtaflllvft atalqgwaqn aenrqislem kneplgsalk
       61 qfsnvsgykv nfpsedvapy rvtvsiyqma pfaalqkile gkpfeydvkq nfitvrkvka
      121 tsttasgkfr nvggqvvdeg gnplpganik vlnspfgaia daegnfickv pvdvhtlevs
      181 fvgmqsekvs vkdrnnvrvi mhedkqqlgd vvvtgyqris rerstaafgf vdseqlnrqm
      241 hsdlassleg qiaglrmnin pntgdmspil rgvgtfsddv gtnplivvdd mptnlslsei
      301 npynvesitv lkdaaaasiy galaangviv vttkqaqkeg ahvsinadwf ittkpsfksl
      361 nlastsdiid yqtavfdanv aekgsaanfl ssfqynyynp lfqlyldqan gditssevna
      421 tlgqwrnndy ykeyrdnawr taitqrynvt vsqkagnsnh flsfnyekds qrvisgksnk
      481 islyyksnya vtnwlnlnag vdvrmgrsht pnssytsytl qqryerilda dgnhytspyv
      541 nvgaypsyng svvrkaegvs pyrtfgfnvl daleesitks hdvsirpfvs lqarflkmfk
      601 ynfmyqyewn kgkselfese ntyamrmlhn smvdtngkaq lpqggrfsqt eveskrytvr
      661 nqidfdktwk dhavtaiagl efrenkiptp arqllygydp qtltsdfmnw qayrdgvgts
      721 alsdrtitls glsatlhesr hryasfyana gysylsrynl sgsirwdqad lfgldirnqr
      781 hplwsvgasw ilseesfmke iswldylklr mtygingnvd qasttyfvvk kktqsnpikt
      841 tyltyedddl pnpklrwekt atynigldfr lfknlisgtl eyynrhssdl lvrrymdptl
      901 gagsrvvnng emrnrgvels lsaniirkkd wnfavdfnfd hnknkmlkvd hsesdnaslf
      961 iksplnyfme gtsyntlway rihriengyp vavdkdgndl vkfnedgtva sitsgsslkg
     1021 tddlvnlgsl tpkfsgsvgl rfnyknfdln affvyaggnk lrnsvlkmdd qlgtqtlkgi
     1081 anrwtaddsn aqvrmyldip aqvktyastf qdwwqygdin vkdagyvklr slsvgynlpf
     1141 tvcqhlrlss lkvkvqvnnl ftwckagsdi dpesygmndg trgiaspkty siglstsf
//
LOCUS       WP_120490048             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            ovatus].
ACCESSION   WP_120490048
VERSION     WP_120490048.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides ovatus
  ORGANISM  Bacteroides ovatus
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Bacteroides ovatus"
                     /db_xref="taxon:28116"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108783
     Region          1..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtdvdgnfnl snvpssaktl qisyigmqtq evvikptlkv vlksdsqnld evvvtamgik
       61 rsekslgyav ssvkgdeitk aresnvlnsl sgkiaglqia qssgtvggss siqirgassi
      121 gsvssplfii dglpidngsy npdrtngivd vgnragdins ddiesinvlk gaaatalyga
      181 rakdgaivit tkkgkknspv fvtvnsstrf envlklpdfq neyaqgsygv ynvkmlngwg
      241 pkissvqdqq ftdykgdkvt lkanpdnvkd fyetgmsyin nvsvagggek adfrlsftst
      301 nqtgvvpgsd ynkyafsvna gmnftknftg risaqyirsd segrpaqgan dsnlliplin
      361 glprtidihd iqknwideng kqitldpegk snnpywiink nkftnnldrm ignitltykp
      421 iegltitnna gtdfytegrr kvyakgtvga lngkfqtwnl ykriinndlm vsyektfand
      481 yhfkvmmghn lyqeewknen vqaqnlvvdg lytytnakst tpvnyyekkr lvglygdisl
      541 gykdmlfvnv tgrndwsstl pinnrsyfyp sisgsfifte lmenkdilnf gkvrlsyanv
      601 gsdedpynla fkytpastyf lqylgdvntf phmglvgftg prvlpnenlk pqnqssfevg
      661 adlrffggki rldmtyysni tknqivsidv plstgyfann inagkiankg vevtlgltpv
      721 etrdfkwdld atfasnkqtv eelaegldey tltsglsglq ikaakgdsfg lygtgwkrdd
      781 qgnyvinskt glretvnnvr lgdvypdftm ginntftykg vtlsflidir hggslysetv
      841 anlrssglaa etiahredas fiepgvilqd dgtyrpndvp vksmqdywqh isnssnnegn
      901 iynasfvklr evqlsysfpr kwfksffvks ldlgfearnl wiikdhvphi dpeanffgps
      961 qigggvefns ipstrsfgfn vrltl
//
LOCUS       WP_120490063            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_120490063
VERSION     WP_120490063.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118915
     Region          40..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklrflmac allaflwseg syanttlent gssqqqqywk ikgkvsdekg ealigatvki
       61 knathgtvtd vngnfeivlp pgsvliisyi gyreqelkin sqrtydivlk eetagldevv
      121 vtalgikrdr kalgyavsdv kgkelekake tnvinalagk ipglvisqta ggpagstrvi
      181 irgntsltgs nqplyvvdgv pldnsnfgsa gayggydlgd gissinpddi esmsvlkgpa
      241 asalygsraa hgvilittkk aqknqnrrai gvevnstvtf ekqlteyddv qtefgqgwdg
      301 rinlndddak sacaswgpry degiafkyfd gvtrpfiyrk dnikgffntg vtatnslils
      361 sakennsirl sytnltnkdi mpnakisrnt idlrtffkla eklevdfkvn yvneyvknrp
      421 aladsrtnva nnlmnlagnf dqvwlkdnym hsdgtyydwn rgdvwninpy wvqyamkntt
      481 qkdqyfavas fkysvnknly fkltgggenv nfsfmdyipy stpstllgql qkstfenksy
      541 nvefianyqn sfkrfnygit lggnvyhvdn kshtitaknm smhetvalqs flqkeitegs
      601 wrkeinslfg mvnlswkdll yadvtlrrdq sstlpvnnnv yfypsvggsf lfselikpnp
      661 ilsfgklras waqvgsdadp fmldlnyimt dktfgnystg yistgtipnk dlkpsktnsf
      721 eigvdlkfln nrigldftyy kqnsnnqimn vatsvtsgyg tklinageie nsgveialnt
      781 tpvqtkdfsw dfnfnfskns nkvkslstgi eslelaaarw lgvkvlavpg eeygvimgqd
      841 flrneqgdvi inadsglpei tsdmkklgka twdwtggltt tfrykqftls aifdikvgad
      901 iysmtargla ksgkaaytvr grdewhksee qrleagvaeg nwqstggyva egvvkqvdaa
      961 gnvswvkntk aiapydywgy icdktaspfi ydnsyvkmre ltfgytfpkk mieryvesls
     1021 vsfvarnpfi iyknvpnidp dsnyntsaig leygslpsrr sfglnvnikf
//
LOCUS       WP_120498805             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Kiloniella sp. EL199].
ACCESSION   WP_120498805
VERSION     WP_120498805.1
KEYWORDS    RefSeq.
SOURCE      Kiloniella sp. EL199
  ORGANISM  Kiloniella sp. EL199
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Kiloniellaceae; Kiloniella.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Kiloniella sp. EL199"
                     /db_xref="taxon:2107581"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33808
     Region          7..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msethrtkvl iigsgpagyt aaiyaaranl epilvqglqp ggqltittev enypgfadvi
       61 qgpwlmeqmq kqaehvgtkm hfdiinevnf derpfvctgd sgnsyvadtv iiatgaqarw
      121 lglqgeetyn grgvsacatc dgffyrgkev avigggntav eealylanic skvtlvhrrd
      181 alrcekiled rllknekidi qwnkvvddvl gtptdgvtgl klrdtqndsf seldvsgmfv
      241 aighdpatai fkgkldldde nyilatpgta ttnvpgvfaa gdcvdkiyrq avtaagmgcm
      301 aaleaerylt emnd
//
LOCUS       WP_120500720             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseovarius sp. EL26].
ACCESSION   WP_120500720
VERSION     WP_120500720.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. EL26
  ORGANISM  Roseovarius sp. EL26
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseovarius sp. EL26"
                     /db_xref="taxon:2126672"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55448
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevl egearvamtp dsalqlqklg yecaieagag asagfsdany eaagvevikt
       61 paalwkacdi vakvrqpdtt elkrltkdkt lisffnpggn eegmelaksk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvfldfee eqtdgaaagg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvaam kpgsvivdla aekggncklt
      301 vmdekivtdn gvtiigytdf psrmaaqsst lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgstvtfege itfpppppki qaiaaqpkae apkeltreek laqeaaafka qtknqvtllg
      421 igavlllgvg lvapasfmqh fivfvlavfv gfqviwgvah slhtplmavt naissiiilg
      481 almqigsssf lvillaglsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_120502144             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Roseovarius sp. EL26].
ACCESSION   WP_120502144
VERSION     WP_120502144.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius sp. EL26
  ORGANISM  Roseovarius sp. EL26
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Roseovarius sp. EL26"
                     /db_xref="taxon:2126672"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33568
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetrhtktl iigsgpagyt agvyasraml epilvqgiep ggqlttttev enwpgdtevq
       61 gpdlmvrmea hakamgceii gdiiteldte srpfvakgds gtvytadavi lctgarakwl
      121 glpseeafkg fgvsacatcd gffyrgdeiv vigggntave ealfltnfas kvtlihrrde
      181 lrsekiledr llkhpkiepl wfheleevlg ddmpkgvtgv rvrnnqtnev seipckgvfi
      241 aighapasel vkgkvemhhg dyvkveagst rtsvpglfaa gdltdhtyrq avtsagmgcm
      301 aaldaerfla eqd
//
LOCUS       WP_120505224             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfitobacter mediterraneus].
ACCESSION   WP_120505224
VERSION     WP_120505224.1
KEYWORDS    RefSeq.
SOURCE      Sulfitobacter mediterraneus
  ORGANISM  Sulfitobacter mediterraneus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Sulfitobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sulfitobacter mediterraneus"
                     /db_xref="taxon:83219"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55284
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif egearvamtp dsalqlqklg hdcvvetgag aaagfddasy kaagvevvkt
       61 aaalwkaadv vakvrapnda elkrlradqt lisffnpagn tegmeaaakk gatviamemi
      121 prisraqkmd alssmaniag yravieagnn fprfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvkam kpgsvivdla aekggncklt
      301 vadekivtdn gvtiigytdf psrmatqast lyatnirhlm tdltpekdgv inhdmeddvi
      361 rgatvthake itfpppppki aaiaaapkke apkeltaeek aaqevaafkq qtknqvtlla
      421 vggalllavg lvapasfmqh fivfvlavfv gfqviwgvah slhtplmavt naissiiilg
      481 almqigsssf lvillaalsv fmcginifgg flvtrrmlam fqks
//
LOCUS       WP_120511327             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Photobacterium salinisoli].
ACCESSION   WP_120511327
VERSION     WP_120511327.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium salinisoli
  ORGANISM  Photobacterium salinisoli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Photobacterium salinisoli"
                     /db_xref="taxon:1616783"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34186
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msnakhskll ilgsgpagyt aavyaaranl npvmitgmqq ggqlttttev enwpgdaegl
       61 tgpalmdrmk ehaekfntei ifdhinetdf sqrpfllkgd ngeytcdali iatgasakyi
      121 gleseqafqg rgvsacatcd gffyrnqkva vvgggntave ealylanias evhlihrrdt
      181 fraekilidr lmdkvnngni vlhtdrtlee vlgddmgvtg vrlketqsdn tedldvmgvf
      241 iaighqpntg iftgqlamen gyikvqsgle gnatqtsvpg vfaagdvmdh iyrqaitsag
      301 tgcmaaldae ryldalnsk
//
LOCUS       WP_120514384            1119 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120514384
VERSION     WP_120514384.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1119
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123834
     Region          140..1118
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfffakieik prmwlivkpl limklsffli lvaslqlsae tygqrvrlky dgadlatvlr
       61 diqratgfnl agkynlvkta rpvtisrdsv dlaealrlle vgqdlrlslm grsilinerf
      121 aiataeppni vddtsrrsgf pitgliigeg dvplsdvtvq nlttgkgtyt kasgvfilqn
      181 vnlgdrvrvs yvgyadqlft vgsnrevnlr lkvetvglna vqkegyqits krysnanvtt
      241 vkgtvieryp vaniatalqg rvpgltvtpt sgyksgpfrf virgesting psdplividg
      301 vplnpltivt danvvseysg fnqsgitgps ggqsplysls psdiesievl kdgeataiwg
      361 srggkgvimv ttkrgkpgkt rfditassgv nfvprnypml dtktyfemrr eafandgiap
      421 desnaydlkl wdstrytdwq ryfwngtsnl tqadvsvsgg dklttfrvsg sfvnfqalnt
      481 lagsdqkitn qiaiehksln rklslsfvny fsfmksdmis mvgsvvlppn apevfdeenr
      541 lnykgwypis drypfgsiwq pytakttyin sqlsasykil qpllfkidfg ysqnfqnqim
      601 ifpiasknpl dnptgssiig qansgriiie pqlefrkffl ngdfraqvga tyqtvaqngs
      661 nsrgdgfvnd nlirsienap iqygsnvgge ykyaaafgri syiwksklta nltgrrdgss
      721 rfaagrnign fysaglgyii sednyfkrsl pfvnfakirg sygvtgsdri adykyltrwq
      781 slpsaatyls svtyrsvqha npylewqtdk midfgiqlgi lddrigieas wyqrrsgnql
      841 lefalpsatg fqsvtanfpa tvqnrgiels vsfnpirksn idlkiyanaf snknillkyp
      901 gieespyasi fevgqpikit rvlkltgvdp qtgnytfedr nkdgridyna fsadndlisk
      961 dlsirsdggv gidfryrkfe isiffqfria dgqnalyrgl vpgeaanipk evydsrwqkp
     1021 gdiaksarlr viqqesdvaf qisdgvitna nfvrlnnlef rynlpegask klgmtscnvf
     1081 irgnnlllit gykgsdpelq sfgslpimsa ltagaklsf
//
LOCUS       WP_120514284            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120514284
VERSION     WP_120514284.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109585
     Region          35..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnysniyklf fpllcilffq eayaqsgvkq dhaftgivld ekkvplqgat vsvqegnava
       61 ttnargefsi naglrdvlif kmpgflsgql tisntdvirm tlleagidag ddddvyipfg
      121 irkkrqvsaa ittvksdavp qaplgdvknl fsgrvsglyl pqsntapgdd gtgmfirsrn
      181 sfgdksakgy vdgvqrefgd mdiaeiesit vlkdaaslaw yglrggngiv lintkkgnas
      241 ksyinfdtqi gvqtssnlqt plnsydyaql yneaalndga avapfsaadl eayksgadpf
      301 rypnnnysrd ylkkssivqr yvlsagggsn siryfallsy fnqgglldqt kapsfnsnag
      361 ykkfnfrgnv dfdvnkylti alnagmrten rlspgsglsd vlgaiyetpp nafpilnedg
      421 slggtadyts nprgllqqrg yisnlqrvll atlnvkqkld fwvpglsanv lfsydgsgty
      481 tsgitqqytv ydaqlgksyl tstpttyraa gysannlqne lwigldydri fgahtinasv
      541 rgqrfaekqp erldsrnqgi sarveygfkq ryflslvggy sgsenispek rygffpavaa
      601 gwvvseepfl knnsvlnyfk vrasygtvgn deiggsrfaf esfynrnatg ggypfgnsfa
      661 atnsttesnl gnpdltwetv kmanagfdar flnnalsita dfyhtrredi ltanvipgil
      721 gqnigmvnag iveskgidas vfytrtfgkl sitlngnlll sdskviaeng qnglpeyqqt
      781 lgrfpgaylv flsdgfyqdq aeidnspaks tlagkivpgd iryrdiggpg gkpdgiinnd
      841 drvrinkasn phtyygfgan lrygmvdfsv qfqgvegrti dvesyvnsgp fdlnqesfyr
      901 wtpataatak yprlgledrg nntadsdfwl rsgdflrlks veaginlpvt kagplrmngl
      961 rifvggynlf tsnsldvnvd peipgsgrge aypylktwtv glnakf
//
LOCUS       WP_120514781            1127 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120514781
VERSION     WP_120514781.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1127)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1127)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1127)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1127
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1127
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125454
     Region          126..1126
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrqspvlslr glamlcmvlf lhlatranvh qfdfkvtlka eqvalknvmk diekqtglyf
       61 mysatgglki ndpvsihvtn akledvletl levrgiswsi idkaivlksg avknkenket
      121 keamfrtvsg svldkdgqpl pgatvqikgt nigtttavtg ifslanvptk qlviqarytg
      181 yesqekvlte gnivfnlnps vsnldetvvv aygtstkrsv tgavsvvkge eirtlpnrsf
      241 dkslqglvpg lrisngtgqp gggvsnmivr gistgtealg gstvrnpliv idgmqvtqdi
      301 fnrmgpsdpf tpltnplaqi npddiaeisv lkdaaaialy gskasngvim vttkrgrsgk
      361 tkfnfshqtd asmrpasipk mlnqsqylel lyetyrntdp ttwtdeaira dlfkkfpyqt
      421 igndtsfypq aewdneiynh paitlsnnls vsggtpnqtf ylnfeytkqn giikstgyer
      481 aslrvnldnr itdwlkfgis stfsynlqka gyqsegpyag apstdilspl lpirtsdgsy
      541 ikeftwgtll ntvypnpife rdynlnktsa frglttmnad vsflrhfnft tslgvdymqt
      601 enkqkidprl snsgggyird ydtrnanllw msilkyqtqi grhhhidvla gqeaqiqnnk
      661 nlylsvkgsf gqqtnpyytd vvnpeyvmdv flggtlkrts lsqfvhlnyd yrkkynisgs
      721 wrrdgasvfg dsnpfgnyws lggawiisee nfmqpiknvi pflklrgsig lagnagavnh
      781 llryhllsrq lfmkdpavmp gtspgnptik wektsqwngg lqagllnnrl tadvdlyykf
      841 tknliyqtil psftgyasvm dnigdirnsg ielslsgdii rrkdlrvalr gnwsknsnkl
      901 lkankniysv snimsneegr emnsyfmpvw agvnpangmp qwldssmkpt qqynlalkqf
      961 vgrsqpdafg sitstvtwkn lelqamfyyq ygglfynevn sllltdglra yhnvpvtaln
     1021 rwqkpgdiae npvrllsnnn sgaenstryl qksdyirfqn lkltwriprk wlsparvqdl
     1081 sidgqvnnla lwataddvdp dnvnlggrgg faypnsrtys irlnvsf
//
LOCUS       WP_120515048            1039 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120515048
VERSION     WP_120515048.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1039
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113537
     Region          26..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrllllwa fllclyqlsf sqstpitgki sgmdgaplpn vsvqvkgtst gaitnaqgtf
       61 slqagtdail iissigylpq qvalkgrsfi altletdnkt lndvvvigyq starknvtts
      121 issvsakdie pytsgtvata iqgklagvqi maadgsvgsq prilvrglss itantnplvi
      181 vdgmeigynf mntinpldil sidvlkdasa asiygarsgq gvilittkkg kgaptinfsa
      241 vygitqspnv klagaqeyag lmnqiatnsg atlpfpdvks lsntnywdet fgqgnrqnyn
      301 lsisgggngl svfgslgyys eesyagkqag qwkkitgrln vdwdinkvvk tginisprye
      361 nypfaplnlt wgafamdptv apfrseadvi aslppltgvf adfmtafnpa ysvpgrslfn
      421 glinpefnkr tnfdkreyfg gqfstyleik pfkglvlksv ldatanfsqq nnyapkyyfa
      481 pnsynaktav tsataqnsrv kitstadytl plpeehsvnv llghsydsys tkgtnasren
      541 ipfdsepfry inagnlvtga sggyqpgaap fgkmlsffgs lrynykekyy ltgtmradas
      601 slvnplyrwg yfpsvsgawv isqesffdpl kdhvsflklr aswgksggnl pgsvgdymsy
      661 vnmityvdat gkvingytpg sinnpelkwe iqqdftvgld aalfndklni sidrytrnpk
      721 nlllpvrvdp slgypqgyip tqyanvgemt tkgwdvavgy kdnitrklsy gvnltltqfk
      781 sevdylsssd piiggennev istfrsrttv ghapgawwgf tvdgvfqtdq eassyvnkng
      841 erlqpqatag dlkfrdfnnd gkidnndmsd lgspypkfsa glaltlaygn fdfrtelygv
      901 fgqqnfnqyr rnmiaggnyn fisgfqdqyw hgegtsnsfp vlrktdlngn ftkmstffle
      961 kgnflranlm qigykvpegl ikgiknlrvy vsaqnlftis nysglnpdip wystisyagn
     1021 dnyqmvpprl ytfglnlal
//
LOCUS       WP_120515056            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120515056
VERSION     WP_120515056.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116675
     Region          39..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhesftklca slpvvalfcl lladasarea gkrhteavqv tgivtdarqe alpgvsvsek
       61 gtsngtatdi ngrftitvtg aaavlvfrsi gfqakelaag sgilnvqleq dvrnlnsvvv
      121 talgirreek algysiatld gsqvntvkev nitnalagkv agvnvrggsa dpgattlvvi
      181 rgqgsfqgyn qplyvvdgvp lasairmpvq pvgesavdfg stisdinpdd vasitvlkga
      241 sasalygnra ingvilittk agsglkkglg itvnssvmfd qpwlfphfqd qfgagdrpgt
      301 eetvseaswg prinvgtkhv qwnsptdaag dpiptdwvsf pdrhkdffet ghtltnniam
      361 tagnedgnfr lsytnlankg mvpntdldrn tlnlaatykl hpkvklatni gyaksssdnr
      421 paynrgsvgn ivytttpnvd ikqlrdywmp gregvqqfsh vpgsmdnpyf vayefinsyd
      481 rnrltgnvel slqltkdlsl tgrtamdmft etrenkrpfs sirnplgaya ieteyfreqn
      541 tdflltykka lssdffisvs gggnrmdqhg rttlqstesl ispgvysinn aragtvydnt
      601 yrfrkrinsl ygmgqlafrn yafldltarn dwsstlpaah nsyfypsvst slvlsdmlni
      661 qqgalsyakv raswaqvggd tgpyelynty tfgqdwgnvk raylddvmkn sslkpliats
      721 yelgtdlrff ngrlgldfty yntinrnqil nvpttmasgy ghklinagsi rnrgveislh
      781 avplagtfrw dfqanftrnr nkvlkltegl nsfllggaeg vryevregte mgdfyalgwa
      841 tvpdgkykgq pllnadgsyq qinnyvkign ynpdfmlgft ntfsykkftl sllldwrqgg
      901 effsyvaknl lsdgrtvttl pgrdpatggl pwtdaagnqr tdgmilqgyi gqasgnyvln
      961 dkitdpenyy geyywsfngr stfdatyvkl reaslkysft qkalsklpvh nlsisliarn
     1021 lftwtaadqg ydpetamtia ngsfspgvas wslpytrsfg asvgfnf
//
LOCUS       WP_120515315            1061 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120515315
VERSION     WP_120515315.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1061
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116620
     Region          23..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrhflkltll llmtnltiya qsrkitgkvs tadgqplpgv tvfikgtgtg tisagdgsys
       61 ldvpdnatel tfsligmetf tqplsglasy nvtlktgdkq lqevvvtalg isratkalgy
      121 avqevksael qtrptnalga lsgkvaglqv issggnmggs trvllrgins isgnnqplfv
      181 idgitidntd mntkstinss agkdvgnmiq dlnpddieni nvlkgpaaaa lygtraangv
      241 fvittkkgka gkgfdvtlns gleferltrl perqhlyggg ksntfqtati ngttynivdy
      301 gmdeswgpel dgtpvlhwyn ldpeyaddyl kpqpwlypks dvedffrtgl assnnisisg
      361 gnenqafrls ytnravrgti pnsslhrntv nlsgssrfgk flatanvnyv knqstgrpwt
      421 gasnrnimle ayqwgqvqvd ydklreykrp dgtprawnrn syentaagra tkyidnpfws
      481 afesyleenr drfygnigls ydvnswlqls skvnadlydy qnqdriavfs rsqssyneys
      541 nnfsefnyef lanakkrwnd fslsafaggn imnqkrrisn aatqggliip dyynlknass
      601 vlnesnsfhk siyslfgsvs lgyksflfld gtlrndwsst lpldknsfay psvstsfvis
      661 elgelksssw inllklrlsw aqvgndtdpy qlqqayeatq afngnpgykl psifanpelk
      721 peitssyeag vsfkafrnrl gldvtvytnd srnqiinipv stafgyesrf inagkinnqg
      781 vevnlnvvpv tnqdfnwdvn lnwstnknkv vkltedassy pindptgtli tlvaregesy
      841 gqflgydfvy dndgnkviga ngaylrteqm vplgsilpkw qfgigqrfty krwdagilvd
      901 grvggkvfsq tykvgmqtgv lkptaengir englvldgvn gtvtfnpdgs ysvsntkvnt
      961 trisamdwal gfsngpttqs ifdgtyvklr evtagytipf sktsivrqvr vsaygrnlwn
     1021 iytvndyidp eltnsggniq gveggnlpvp atfgfivqvk f
//
LOCUS       WP_120515405             975 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120515405
VERSION     WP_120515405.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 975)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 975)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 975)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..975
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105813
     Region          25..974
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkflkgils ciclllplvi qaqnqtvrgk vtdvagqplp gasvvvqkgr qgtvtnaegf
       61 felsvpsgtk ltinftgyrs rtltadpaap lqvvleedia kldeiivtgl atsvkrrnaa
      121 nsvatvsake lsgtapaqtl daalsgkvtg anitassgap ggglsfklrg vssiygtiqp
      181 lfvidgvivs nrsvstglnt fteassggsa tsaqdnsasr iadinpadie nveilkgasa
      241 saiygsqasa gvviittkkg ragktrfqfn qdagfasvsr lmgtkleltg ddidargwss
      301 adsleyenar ragklydyek emfgnkgfir ntnlsvsggn ekttfhisag tkkeegivrn
      361 tgyenhnirl nlnhrasdrl kfglstaymn taadrgifnn dntgvsvtga ltalrpfydl
      421 hpnadgvypd plggnnvlet ialmtnseki nrvitganme ailqqsnvsv trfsgragvd
      481 fyhgktqalf pgrlhfeqaa gtngrnnqgs tydlntswaa flvntltpga grssftttlg
      541 lthefgsfdq lmtiaqnlvg sqtsqgqass lraqqsrqsf rndgiffqee fayneflnlt
      601 agvrfdkstn ngdykkyniy pkvnaswnit rmadwnssil gdlklrvayg essgfptfss
      661 rfttmpsenv egipgtgtgi tlgnpdigpe rqteleggvd isffngrlsl eatvynkvik
      721 dllvaadwpi stgfsskwin ggslrnrgle lslrtvpvnn rnirwnsnvn fwlnrskvlt
      781 ldvpmfdmgd gfgssygafy ieqgrsatqi liehepgvlm pignsepdfq lnwfnevtlf
      841 rdftfrallh ykkggdninl tqllrdwggv srdwdnrddk gertgvsrad dhrtliqdas
      901 ylrlrevalf yrlpikskti eniqvgvsan nyfistnydg ydpevsnfgs tfgtgvdvnp
      961 ypaskrlqfh lslnf
//
LOCUS       WP_120515285            1130 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120515285
VERSION     WP_120515285.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1130
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125764
     Region          50..1129
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqlkvyacda gkrrrklpvl filllfaaft paytfgsett afqdsvpssq irgrvmdaee
       61 kialpgvtve nlvnrkgilt dangnfvlag rmgdsirfsy igkrvqvaiy rgqpiniqla
      121 slggvlsevv vtgfqdldkr kfsgaattlk gdevkidgla dvsrmlegra agvsvqnvss
      181 afgaapklri rgatsihgdn kplwvvdgvv leeiinisnd qlssgdpttl lgsavaglna
      241 ndiesfailk daaatalyga ramngvvvit tkkgrvgkpl vsytgnfstq lkpsyadysi
      301 mnssqqmsvl aelerkgsle pnildradyg vygkmydlft qvdangnfil pntpeskaaf
      361 lkryaaantd wydllfnnsf iqehslsisf gtdksqsyfs tsyygdngwt vadrvsrytl
      421 nfrnnynfsd rlsvgfstla svrqqrapgs lsrqenpveg qfdrdfdinp fsyalnasrt
      481 ltaydengdr eyfrrnfapf niltelenny lninvadlrl qgdlkykitp altfefvgal
      541 ryvkssmehq iteranmana yradgnstir qnnrflyrdp enpeaepivv lpyggfynrt
      601 edqlvsydfr nslnyiktfn nlhavnllag mqvksadrqq asntgfgyqy dnggipfvdy
      661 rivkqtiesn fpyygmskdy drfvafygsa gytfkqrynf tgtvrydgsn rlgksttarw
      721 lptwslaasw nadrepfiqn ltwidyltvr asygltasmg patnssivlr ninttrpfft
      781 evesvirlan lenseltwek aytanagldl glfknklnit mdgyyrqsfd lisiirtsgi
      841 ggesekaany admeswgael mvggpvitrr dwgwktnftf gynenqitnd rsrpqifnmv
      901 qaeggnrqgy parslfslef kgldprrgdp lftnekgetg sgvylqdrdi shlvyqgpvd
      961 pivtggwsnt fnyksfslnv fvtaqggnki rlyeafktsy tdldaapkef lnrwllpgde
     1021 kvtnvpsilg aleqstlnge ypynnynyst ervasgafvr lktvsltynf qpallnrigl
     1081 nsasvagaai npwliysdkk lrgqdpeffn sggvalpvqk qftltlkvgi
//
LOCUS       WP_120515421            1016 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120515421
VERSION     WP_120515421.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1016
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111049
     Region          21..1015
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiyllsla cmmsvgamaq qvirgtvrds ltkapipgat ikvvngsggv tanekgefel
       61 rvpanaqlri ssigfepvli patavmrpim ltttalllna pvvvgygtqq rpllttsiss
      121 lnakklapen nivsdvgkal qgriagvfva ntsgtpggtp niqirgvqsa rasdanpliv
      181 idglvmegsg islnsinpqd ietidvlkda asaaiygarg stgviiittk kgrqgakptf
      241 svnaytgfnn vpstrrmlst peyeaafkda rnnrlgdiek qltdpaltpt qisqlqsert
      301 rltsqvnalk madrstdwid rvknkqapvn niqasmtggg eknsyymsig rysevasigt
      361 gqferytgki ditqqvgswl klngninlsq gvnknnaypl vsafnarpdt peepirlpng
      421 qldyyigqqn hplgemlenk nkrrtqtwfg nlsadvklhr tlqfrsvfsa nkynvssndy
      481 qsplgylgkf nkgylkvngi dnfnynfdny ltytnrfkql gvnavagytf ysveqnssgy
      541 elngfpavag itggsaaaay gsvasissln gssletseaw fgrvnldwnq kyllgaslrt
      601 dgssklnpdn ryswfpavsa gwdiakenfm lrqkaisflk lrasygisgn irplanfate
      661 dlmtgttylg eaalkirdli gnpsvrweqt kqvdagidlg lfqqrlnvtv dyynkttdgl
      721 lssrfipwef gaqsipynvg sirnygmdle lslssaptsk vmwrvetnmn lnrnkvlsla
      781 dsvinygtfi fggpqsnvki gqsvgsvqvy nslgvdpqtg dmvyedrnkd glinikdmiy
      841 vpialpkftg gttltagykg vtvealfnyv vgtsiydyye qslrnydmdf fgvmpnkfdi
      901 vnsrwrkpgd itdvpravlg qhgagkttdw nyrpstqfvy nasylrlrnl mvsydlpqrl
      961 lskasisrck vycsaqnlft itkyigfdpe aannsgivss nlpnaramvl gidvsf
//
LOCUS       WP_120515610             989 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120515610
VERSION     WP_120515610.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..989
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106802
     Region          27..953
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhlskqftll vllllmtvat faqqqrvtgt vsdasgnpvp gvtvrvqatn rgtvtdgqgr
       61 ysieavngnt lifsytgyks qnnvingptl nvtiqedyan ldevvitgla tsvkrsnlan
      121 avatisakql ygvapaqtfd aalsgkipga litantgapg ggisvkmrgv tsifsnsqpl
      181 yvvdgifisn isvpaglnli tgaatagnpq nqdnpssrva dinpddieni eilkgasaaa
      241 iygskaaagv ilittkkgtg igrtivrlrq dlgwgearkl lgvrqfteqt afdkggaaar
      301 dmfiaarnag klydyekemy gekglisntn asvnggtert gmyfsanrrs eegiiknsgy
      361 lnnavrmnid hqlsdrisla lrasymntsa drgltnndnn svtygvslat vpqylelhpd
      421 angvypvnps aanpletrdk mrnnettnrf itggevratl htndrtntkl ivrggvdffn
      481 lkteaifprt lqfmkggleg asiqgntnnl ntnlagvlvn sfaanndlnf ttslgatlet
      541 nsldhilaia tnlipdqsnv dqaassqlqq frqkyrdngi fiqeevlimd aitlsagvrf
      601 drstnngdyk kyfvlpkasa swnlakmpfw sietvnsfkl raaygqagnv apygakflal
      661 tssniggqpg slvdnqfgnp dieqerqtel eagldvsffn grltfegtyy nkkiydlllr
      721 rnvasssgft qqwvnggdlr nqgveigiga ipvntkrfrw naqlnfwknk sqitkltipa
      781 fpmgafgntl gnffieegks atqiigtlgg gkgvgvlgns epdfqlsfyn dltfltnfsl
      841 rvmlhwkkgg dninltqyls difqttydyd ddqngngikd gvdrmaaaaa tdasvrvqda
      901 syvrireigl yynipipknn iisavnvgis annwftwtdy dsydpetsnf gsntistats
      961 rgsngissgv evtpypavkr amfhlgvtf
//
LOCUS       WP_120515944            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120515944
VERSION     WP_120515944.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111079
     Region          34..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnplkkqhg rwktfpllll lqlvatlama qvrisgkvta adgspvpgis vqlrntttga
       61 ssdangqynf taniqpgsyt leftgigfkt vhkaisvsga aasadaimee dvlnmdeivv
      121 igsslrqsrk qlgntvnsvn akqllntgsg nigaalqgkv pgaqitqtsg dpsggisvrm
      181 rgtstikgss eplyvidgvi vsnattnvnn lnvsaaagvv ssnpptnevg tnrmadinpn
      241 diekidiipg asasaiygsr asngvvlitt ksgkagrlti dfstgiimnq lrkkvyisty
      301 gkqfgsaalr lgnisdgpgn iitytrpdgq vrklstdlvd vtrydyqddi fqtglgtdny
      361 islgggtekt kyffsggfyk negiirntdf rrfnfktrie qvindyitva ggvaytnsfs
      421 nekpngnvfw spinsvnitn nlynieerda agnlkgvept rvnplsvied mdltqavsrt
      481 isdlqikikp vrglsidyil gidnfsqegs nlikrypyis aqeglgyvss amvnsflinn
      541 dinisynaql gdfssltttg fnhqyqkitg lvnqgrdlln gittingaat kldpqysydq
      601 rqvfggflqq tfgyknivfl taagridgst sfpedtrtyf ypkvsgswni sdmgfwkdmg
      661 gkwfnsarlr aswglagnlt gigsyerfsn yisgslngva tynintalgn alvepersse
      721 fefgtdlsfl nnrlgilftv ynkkivgnsl lvdrvlapss ggstrvenvg dltnkgwelg
      781 inampvntkn fswnvggsls rnknlvtass qvtpislana agsgsvilag esvgvfygny
      841 ferdgkgtma ldaegrpiaa inaqkvllrk vignpnpdwi lsfnslltyk klsfsflfdg
      901 algqdvfnad rrtrqgvgig dysereikge lprgyifsvy nteewrieda syvklrevsl
      961 syelpafakf irtssvslvg rnlvsfdnyd gfdpetnagg nssvlrgidf gnvpiprtfq
     1021 ftfrasf
//
LOCUS       WP_120516095             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chitinophaga barathri].
ACCESSION   WP_120516095
VERSION     WP_120516095.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33886
     Region          12..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 menktsqehv hvliigsgpa gytaaiyaar anlkpvlyqg iqpggqltit tevenypgyp
       61 egiqgpemmv dfekqatrmg adiryglata vdfssqpykv eideektita dsiiiatgas
      121 akwlglpseq rlngsgvsac avcdgfffrg keaaivgagd taaeealyls kicsnvhmlv
      181 rrhemraskv mqdrvlktsn imvywntetl evtgenkveg vrilntqtke ektipinaff
      241 vaighqpnsg ifagklemdd qgyiktipgs trtsvegvfa cgdvqdktyr qavtaagsgc
      301 maaldaeryl sakgh
//
LOCUS       WP_120515936            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120515936
VERSION     WP_120515936.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114143
     Region          23..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmrrlflfll llgiipavqa qntvrgtvta aedraplpgv tvriqgtstg vasdangnys
       61 iaaspgqvlv fsflgyvpkn vtvgnnntih vellvdqknl qefvktayni skdprslsss
      121 vqkvdgadva qtqrenfing lagrvagati tgtsgapgss sqivlrgats iggnnqplfv
      181 vdgvpfdnqt lnqeslisgq svsfanrnsd ygnramdlnp ediesitvlk gpeaaalygs
      241 dgasgailit trrgksgrat vtydnnfrfe dvymfpdvqt tysrglngva ddnatvnpfs
      301 fgamsaffgp kynmdttqfy dnfdnffqsg fqqrhsltvd ggnekytfrm sssyldqkgv
      361 vpntsfsrgt vrlsgsakvs pvfdmngsft ytnsttdkgs kgagsyfltl ltwpvdddvr
      421 nymnpdgsrk tlrgvaynse fdnpfwdvnk nvsndhterf tgnltlnlnp tnwltfsgia
      481 sadiyttdgf fmthpqsryg fasngflsgq diltrnfsgi irgtanktwg kfgniltagf
      541 afddfttein aykgerfyep efisinntdp lsrdakltys nirkmrffgn yevswnrlly
      601 lslagsregn stfmsrfvdk dpffnygaag lsfvfsdllk nwkwlsyaka risyattgkg
      661 patpyvidyt mqsqittggg yaygftgnnq glvpektknf efgaelkffd nrlgiditry
      721 slrssnqils arasygtgyv ikylngglve nrgleiqltg dpiqttnfrw hvlanfdrnr
      781 gqilempasl ptyydsdtwv fgnlrsqayk gaftgnlsgy slrrnskgql linpssglpv
      841 ssgdfvivgd rqpdfkvgli neftykdwsl sfnldfrkgg dvfngneyyl ylaglskrtl
      901 nreeqfving vlldgleesa kptpnniavn pyyrtdywns tsateadfie svdwmrlrdv
      961 tlmyrlprtl larqkvisna svfitgtdlf mitnytgadp svnantasnr gyggagidfg
     1021 slstprginf gvkvqf
//
LOCUS       WP_120516471            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120516471
VERSION     WP_120516471.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112935
     Region          31..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mansyfsryi svlaclvlal cgsvraqqpg tvaglladny gqpvagaaif vkgtndstst
       61 daagrftvra avnntliiqy pgyytiehkv rdtkpltlrm eevyipapqr ipvlygeasp
      121 ksmvgavgtv ytnqlsttpa tlyayalpgr laglytqqss gfrnpatgdn fdvdifvgni
      181 prpgalepnd ntemglilrg qvpvtivdgv qrdvfsidpe niesisvlkd glstillgqr
      241 ssrgvllvtt kraragkprv sftaqtgvqq slnlpkplpa wqyayllnea lqndgkeply
      301 keadfiafrd ysspythpdv nwydailrdn aplsrynlni ngggnvarys vslnytdqqg
      361 ifrtspanny ntnaglkryl intdvsidvt eslnismqlf grlqegtqpg agtsdilgal
      421 latpnaaypi rnlngswggt nnlntnllsq tlnsgyiqdn skdvmanvdi rydlgdwlpg
      481 lsvkgkgnls iqsanaidrs krelvyrmgv tqgdtlysky gdavaqrnnf msvfnaqyff
      541 gqvslnydrq fgrhglnavv ladsrqtifn ydlpgkatni sgkvaynyan kyfvegalnr
      601 sgynrympgk qygtffaggi gwdlaqedfl kgnagwmdql klrgtyahtg ngidnsgyyi
      661 wrqdfsenng igggvyaqgi arspasafqe nglanvnisw etarkldvgi dvslfnnqlq
      721 itgdyyhdry enllqirgks ialsganypp eniginqyeg geltltyqgr vndfnyfita
      781 ngsieqsksi frdeqrreye wnkrtgqpvg mpfgyiadgf fqsaeeaegs atiagykplp
      841 gdirykdlng dgtinqfdea pigtykpriy ygvnigfawk gieasallqg vanrvnyvan
      901 fateagfqfl nftygqayeq itgrwtpeta atatyprlta dannsynkas ssfwvrngny
      961 frlknvslay nlpyswtrrv klgsvkifan aqnlfthaay dfvdpevgvg aypiqrvlnt
     1021 ginvkf
//
LOCUS       WP_120516638            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120516638
VERSION     WP_120516638.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115739
     Region          23..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqallfitm mmvsvslafa qqrqvtgkvv gddgapiafa tvqikgttsg ttadqegnfs
       61 lsvsgtnvtl ivrsvgylak eiplgsltsv svslapdaks leevvvtalg mnrqkkslgy
      121 avqeikadki tqtkqadlnt aiagkvagvq lrggsgakfg tmqirlrgvn nltggnpiyv
      181 vdgvitpnta inpddvaslt vlkgpaatal ygqrasegav vittkktsgg gigltvnhtt
      241 tfenvyvlpd yqneygggss qdwrtfvyqp gthnpalakl dgakyynyev deswgprmdg
      301 tihapwyawd ptvspsdfgi qkpfvpqpdn vrdffktgia nnttvsfaks sdvmtnrfsf
      361 tnltrsgvip nskqqknwlt yygslnltnk ltlstninyv neylfnvpre gygtqttgsf
      421 nqwfhrnlet nklkeyykre dgsfrswnmt gptnvtpkyw dnpyteayen irnnyiqtvy
      481 gqvtlnynfm ngfkagviar gtfenfnsdn rvasytlnpp sfsteedkrt evsylgnley
      541 ektikdfslr agvwgelntr tryrvtsata ggfilpdvyn vsnslnekvt tnliqerkvn
      601 slfgyagvgf rdmlfldatv rndisstlps fnnsyvygsl stsfvftell ntrdwlsfgk
      661 lrasiarlgt dtdpyaiqet falgtnfpks gsatysrmsv pdtrpndslr palstsyeig
      721 telqfannrv rldvnyfyrk nidqivdvtv psssgysark insgeminkg weftigatpl
      781 kmqdfswdid vnfafmkntv vsiapdvenl qvaldgsals fgfvgspras lnakkgssyg
      841 limgggfqrd eatgkmlvdd egypllnnsv elgyvtpdwt ggvssgvyyk nfslnfsldf
      901 qkggkfvsis kmfmsgsgls aetaglndkg npkrdpvasg ggvkldaisa ssgkqnevya
      961 etkdlyqsyl fslwenwtyd asyvklrela igysfptrml gnspfkginv avigqnlwli
     1021 hsatkgldps elesswiegg qlpgtrsigf nvkvtf
//
LOCUS       WP_120516723            1095 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120516723
VERSION     WP_120516723.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1095
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119602
     Region          27..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrilllatl lsfcfapiaw aqekkavsgt vkdvngqllp gvtvmekgtq ngtmtaadgs
       61 fkisvapngt lvftfmgyaq qevsasaasf aivlkedskn lnevvvtalg fkreqrklgy
      121 avtelkgsev aktnainpva alqgkvagld isgaaggpqa asrivlrgak slngkdqpif
      181 iidgtifene dadnavnfgn vlknfnpddf esvtvlkgaa atalygtrai ngailittkk
      241 gttrkglgve fsqtaqfeqv yrtpialqne ygagynpffn tdadgnvvew aggfsfgpkm
      301 dgtmakiing dvvpfsaqpn nwkntyqtgk yfntnvaveg gnekanfrfs yshvdnnsvm
      361 pnngfkrdaf slkssavisk flsaeggvtf tssestnptr qggdytnenv grkwiyifpr
      421 nydpgywqar ymgpdpgkqd lnsylgqypg adywfslend nwvrkekllm gnlsltgtat
      481 ewlkfiargn fsyeqnaddr rqlgwgpnyt gnrglfvlsg qnktqytftg mavitpklgs
      541 dftaslnlga etwtsgigns frtattnglr ipgmyamtns egpldaqakt laqkrinslf
      601 faasfsykna wfldvtgrnd wssalmypdg hgtpsyfyps vsaaweftes lkssmpswvs
      661 ygklrasyaf vggdmmpwen nsgyvtssvw ngaanilpin eyyqsntlpn lnlkpstsss
      721 vevgadvrfl nnrlgldvaw yrsiikdqii kipvamesgv kdrfinagkf rnsgieiain
      781 arpiesknfs wdltlngskn nnkiislygn ekeyemgsdq dvrvlaivga aygviqtnyg
      841 ytpyvgkdan dpnngkpvis pnsadqpykf krgaavvgni tpdfnlglsn nfnyknwslg
      901 fllqariggd mfsashqygt grgtvastie grdaehggva wtdnsgrsrn dgmipegvfe
      961 dgykithngt evdlggmtyr daysrgyvkp mspyqyysmv gdwgigirea svfdasyval
     1021 revsigytmp skiaekirmn kvrvlligrn lgylynnlpd ninpeslrnn stsafseygg
     1081 tpfvrnmavt lqlgf
//
LOCUS       WP_120516948            1118 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120516948
VERSION     WP_120516948.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1118
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123399
     Region          32..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnliqsistl wrlslivsii llphlagaqs avtgkvtdst graiefasvq vkgttkgtft
       61 aadgsfsiaa pgnailvisn mgfisrevpv ngqsslnvql qtnnrtledv vvvgymqqsr
      121 tktsasiskl npaelkntsn pnpvqamqgk iagvsipiss gqpgagasni iirggtklnv
      181 ygtglgtsgg nlssvsggsn vlfvidgifr nsmndvnpdn iesiqvmkda astaiygaqg
      241 angvvviktk sgkfgskmnl sinhrttwet kardykylna tdylrlartt vqstsdridk
      301 nnllnnggfs agtrvytakg qygknvnlta lydnivaveg qayvddllsk gwmvmddpin
      361 pgtrllyadn qyqdliwntg ltnntnvsvd ggsekanynv slgytdqagt fvgtnykryd
      421 vlgnfgfqaa dnfridasvn yqnvlpnyve nftneltrgt rltplirimk ddgnpavgel
      481 ysarnrlhti kyddvrsnte rlisrlagdw tiikglhfrp svsyllqdyr ymfmrkktpe
      541 deiqpstqrq knertdnfrq vmidqvlqyd fslqnrhnft ilggfnftkk nnsrinigsq
      601 raandyiyti eelpvisign vptsnvtdfg telveersas ffgqvnydyd skyivgatlr
      661 ydgfsnfapg nkyayfpsvs aawnihrekf whikpvsslk lraswggsgd snlgitdtyg
      721 gystvnyglg sgivrsnlsn pnlkwetttt tdiaieagfl enrinvtvdw ynkltkdqla
      781 smplpseapf psiiynngvl qntgweveig gtvlrkgdft wntnfsfsyn kqrikelpgn
      841 grdknrqggd rvwdpaqgke ievggyaege rpfglwaykv egvfstdeea qkwnqthrdl
      901 lsspqgqlvg kragdfifad lnsdgvidtk dqvfmgyrtp dkiggwqnsf sykginlrvs
      961 ldyatghmis ngalarslgq grafnegape qalgadiwqk pgdvgkkyar fsfadydfgq
     1021 rnylrntslg vnnsyssdvs amiekgdfla lreitlsydl pkawmqkirs tsmnvffsvf
     1081 nigyltkytg inpetytgfd aiayprprqf slggtlrf
//
LOCUS       WP_120516546             974 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120516546
VERSION     WP_120516546.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 974)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 974)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 974)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..974
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..974
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108970
     Region          22..973
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkvllmlfs vlsclqmtaq trpvkgkvtd srdgsvllgv svmvkgtttg tttnvdgvys
       61 lnvadnatli fnfvgyevle vpvsgkstvd iqmnldvktl aefeistgyv skrkgtitga
      121 idvidgkrie srpsgnfnhl lqgqaagvyv manggrpgaa pqifirgtgs insglaplyi
      181 vdgqpvspsd fatisqndie sfnilkdasa tavygsrgan gvilittkrg ksgkatldyr
      241 gfygvteiae pkvrmmntke rldyevaigl rqandpaipe llksdynqvk eilkpalaqs
      301 htisvrtgtd ktsiymsgey ydqkgvyydn dfsrvgarln vdntttdwlk tglnmyvgym
      361 eealpnetrn stgnpgmmay lvmpyenlrs esgnwreilr hggytnvrsn lwsrendftg
      421 sgndhlkflg nvfaeatiip dlkfttrysm nlsdyvtktf nqpllaaadn gnatrrfsrw
      481 nngtwtntln yrktfarnhs vnavvgseyn yltdydftat arntsspllq efgtmlnpvs
      541 tggslskyrm fgvfgnvnyg fkekyyldls irrdgsskfg rnqqwgtfws vgalwnakse
      601 pfiaqyewis dlrvrssigl tgnddigfyp sydlyggtty egrpglipsq agnpdltwek
      661 rrkfnvgvdl gihnrvsvti dhyreltydm vldapvsylt gftqvkgnmg kmsnngveft
      721 vkgdvlknrd falrvegnlt ynknkirdly gyrdellgsg tgiltkvgyp rgqfkynrfs
      781 rinpdnglel wldkngketd kfddadaviq egktmyapwy ggatadfswk glgifmqwnf
      841 megkysvnnt tawlvwnnas wsnynrvhdl gekmwkkpgd vakypkygsg tqfddryled
      901 asfvrlrelt vyynvpknvl skvkvlrsvr ayarannllt ftewtgydpe yfnnlelgiy
      961 pvsrsytfgi digf
//
LOCUS       WP_120516965            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120516965
VERSION     WP_120516965.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117099
     Region          27..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkikwllwlk lllaittvts aqsvavkqis gevrsdkgei legvtvavkg tpngtvtdst
       61 gkfsikvpdg gnlvfsftgf nsreipvngq qhvaivlqys igqldevvvt algikstkks
      121 inysvqnlkg gevtatkepn ivsalsgkva gvqinnssgq pggsatirir gsasvlgens
      181 plfildgmpi dnsntglaiq nanqivnqsn ravdlnpndi esiavlkgpa aaalygiras
      241 ngavvitskk ggngkeprkl kvslyssltf esiarrlqpi qrkfaqgsgk ryvvpgqngs
      301 edswgplldt ltysstpskw dvngtivgks nplsngipvn lydnignffe rgytndnals
      361 vtgktekfgy yfsfgrlyqq gvvpttdffr ntarfgatfq asdkldfsls vnyfntgsgn
      421 rmlpggapgg alrslintpa nfditnglkn paddprsytf edgsqrayag gtfgfdspyw
      481 slnnnphtdn nnrvvlveet nyklfnwlta tfrvgtdiyn ekrmalfnkg svafpagvli
      541 nytflnrdin tdlyltaskk lsdrfglkvi aghnyfdhql datvnqgnnl nlpgfenisn
      601 gstfnvqqat tqrrlvagya saeldyknwl ilnvtgrnew tstlakgkns ffypsvslgw
      661 ivneslnwdv pwldylklra syaqvgndaq pyslgtyyss ttlngsaqgq tlnfpfngla
      721 gysldatlgn knlkperits yeggleawff knrlgveaty yknesrdqil svsipastgy
      781 ssfitnagli tnsgveaiit gvilnkrnfr wttvlnfshn ksfvheltgd nsmislmstn
      841 ggtqiiapgy afsviygral rtnadgqvli ddreqingap nsnyglpvae atpsvigdpn
      901 plwnaglrnt lsyknialsf lldnrqyfdi ynstlaqmvn ngvaketenr ydqvvfegvg
      961 lssgkqntik vvpgeawyks tinygsvyie kdlwwlrlrd vnlsysfpks llqkirlsel
     1021 eltltgrnlf twtnytgsdp dvnlrggstn gygsdffnyp ttksygaalk vsf
//
LOCUS       WP_120517698            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120517698
VERSION     WP_120517698.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116416
     Region          24..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkgltvlfl llvclsgqvl aqsrtikgkv taaedgtpii gatvlakgtn vgtvtntegd
       61 ytlnvpdgvn elvvkfigmk dteakingav vnvvlstdvr tltetvvtan airrdkrslg
      121 yaaptvkaee itrgqsvspl naltgkvagv nitstasapg sssrivlrgg ssitgnnqal
      181 lvvdgvpidn esiigggdsr saidfgnrgn dinpddiedi silkgpaaaa lygsrasnga
      241 liittksgkk ggnkkqeity tsaltlsnil klpdfqndfg qgfhfepdpl enfswgpkfd
      301 gamtewgqei ngqrlskpys aqpnnvkdff emgkawnnnv slaggnekst yylslnalns
      361 ngvmpsnvdr ynkygvrfng stelsnkfst sigvnyskin snmiqggqgd gsvydnvlqt
      421 prdiplqdmg dlnnpyysyg dvlqdadgnp qygyygaytn spywvlrdfr nlndvdrvtg
      481 nftvtykpld wlniterlga dvysdrrrik qakadllpad pgwtdkhltg ayeenkinls
      541 divhdlmita khdfskdfna slmvgnnirq rtlttleagt nsaglvipgw ynldnsngsp
      601 vatnfysqrr lvglyaqldl ayknmlflga tarndwsstl paanrsffyp svngsfvfte
      661 llkdskigdf lsygkirasy asvgndadpy llrnyyvrtq ilggfantlf pfdgipgltv
      721 gntignpnlk pertnafevg telnmwnnrl sldfsyyqnr skdqilpapi apstgftnei
      781 lntgevenkg veigfrvtpv ktssgftwel fgtytknknt vvsllpgvdq vivggvsgms
      841 ivaavgrpyg tfyardylkd dqgrmvinae tglplltdda ryfgsynpdw maswgtnlsy
      901 kgfslsvlfd tkqggyfysr tsdimtfvgt tprtvvndrq pyvvpntvie dpanpgkyia
      961 ntsvetqwmd fwtnqssvpd aahiidgsyi klreasisyr vpksllsrtp fgdasigffg
     1021 nnlwihtpke nmfadpevns ggagneqgfd ftaqpslrnf gvnlkvsf
//
LOCUS       WP_120517739            1123 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120517739
VERSION     WP_120517739.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1123)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1123)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1123)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1123
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1123
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122017
     Region          28..1122
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtshaflml tlllfgitss lsaqqkptvg gsivdsksap viaanivekg tknralsdae
       61 gfyrisvspg atlviscigf atkevvvgtg ttlnvtlqdd qralnevvvt gfgesrakrn
      121 lgysvtqvsg ddirrtaavn pisalqgmvp glqvtpnsgg pqastrflir gsanldpygn
      181 qplvvideiv mdeqvilpnr ggeqdfgnil kdinpddies isvlkggavt alygsrasng
      241 viliktkkgf sqkglgvsft qtlmferayk tvdlqdrfgs gyhandwtkl ggdslaintd
      301 syylsfgpem kgqmfrditg lyrrndvgyn dvldmyetgi nrntnvgisg gndkttfrfs
      361 ysnlgassat pnndlnrnsf nfrathrpvk avlldintay tqsktknpal lggnsllyrs
      421 sygvprnydi nywmdnyidp vnggytnrde sgasnafwym yqnqyeqken nlrgslnlra
      481 dltnwlrldg sasvntfetn ytakirgtsa gfangeyrvn nnsvkqyryr galnyiksig
      541 kfdllvqggg elnqssqvgt eartngfitp dvfrlsntke rpvlvenkpm kmqnaslffq
      601 ssigfkdylt lniygrndwn stlvyndghg eysyfypgad lafvftdlfk lpkavefgkl
      661 rvsyveaggg ttpyrtstgs faaygayqda yggtilrygf snnslpnqnl vpvrnakiea
      721 glefklfgnr lggditvyqq dsknqiqdft ipivsggnta linegkvrnk gvelqlygtp
      781 lkindfswdv mfnyarnkns vlslpfnska alldgndgiy svayvggdyg sirsnygyas
      841 yqakgaggan vnsplngmpv igfgatrgal ggpvmyylra gtynpsvgge sdpvvgstmp
      901 dflgsirntf nykrlalsvf ldakiggdvy sttygygsqy gqlahtlngr tadlggleyq
      961 sntnyngqgp gkrndgilpv gvfadgtvip asasadgqeh nvggmtvada yskgwvkpvm
     1021 asdyydhtyg wangirqasv fesswvsvre vslsydlptn ianklklnnl rasvigrnlf
     1081 flynnapdhv npdnlsstsa gafvenggtp yfrqfgfsln anf
//
LOCUS       WP_120517771            1038 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120517771
VERSION     WP_120517771.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1038
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115274
     Region          29..1033
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqsnlkrwm lglfclvlys tsmyaqekil vkgvvtdslg aplpgasvsq tdgekinvaa
       61 daegkfelnv apgarlrvsm tgyeqamvtv sgasirivlr qsatslkdfv vtgygsqrrd
      121 lvtssvatmk mdedrrnfpt tsvanllagq mpgvfvstps gipgsspgvr vrvgtsfnsq
      181 nalfvidgmi asgddfnala pndidnisvl kdaaaasvyg araaggvivi ttrrgasgra
      241 risysfntgf skrgknaert saietgeifn rlnpgsnttw sqsdfdyfrk inngwgydql
      301 nevyndpsit shnlsvsggs ekikyfvsga yikedavmkn ltfdrynfra nltaditpel
      361 qafagvslan sltygppnta vagnpndlyr kqllwqpeqp vwtdngnpid ygwianvgae
      421 argdggyikr nwlspninlr lqykvpripg ltasgqffks ysynrskafe kqydmwvmkt
      481 tgvrqistad adrvaikkss qigknflqed yawmssytln fqlnydttfn kvhhvramvl
      541 fekshwesgg istgrdnfpv yltdqwwats gdrldsyngg nteqangrrs wvgqlgydyd
      601 gryiaafsyr ydgsmqfayd krwgffpsas agwiisrenf fssvkniqfl klrgsvgitg
      661 ndavggwqwq qsyqngssay fgndgktntg itygpivntg ltwektlsyn agvdvnfldh
      721 fnatlelykm ktydilgqrl asvpptfsrt lpsanygeme akgiefsigm nreagdfkyf
      781 ananmgygaa kyitrdenit ypwqktvgyn anrvvsrvvt gmlrtqadvd afmsknpyyk
      841 yygispqpgq ltykdisgpn nqpdgliddw daevlkpnnn pvtvglnlgg ewkgialqas
      901 fsgnfhqwrm vnnlvdgnve wnrmwrkwyt dgwtpeapga elprrysand garrvtndas
      961 dfwmkdasfm rlrflaasys lpysitnrvg iaglklyfng snlfviskfg keyydpemad
     1021 gftypimkaf nfgailsl
//
LOCUS       WP_120517837            1163 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120517837
VERSION     WP_120517837.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1163
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130031
     Region          65..130
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          147..1162
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkerpqpnvg pfrslflmlc icltvmglpg lqaqhiyaan tgttgtqqak etqkpldkri
       61 slqvkdtrlt dvlekieqqt ayvfvfsnde ipaarkitln vkdkrleevl emicsplair
      121 yelisnkiil kqgnaastvn sqqddvtisg rvvsdngegi pgvnvrlqga ptigtvtneq
      181 gnftlkipds atdgtllcts vgflpaavpi srrtsitill ttdskelsev vitaygsqrk
      241 kqvtaaisti stkdiesrpv snmfqalqgt apnltlqqnt aepgaamvln irgvgsltgn
      301 apliiidgvq agneglrnln pydvesisvl kdaassaiyg sqaangviyi ttkkgkkddk
      361 psvqyngmyg wqmptalprq vegwefmtlk nealvnsgkt pqytpehisy wenrgsepay
      421 vremlrkytp qqnhslsltg ggksssylls lgyvnqgnml qnkyipsdid fnykrynara
      481 nisvdvskyv kvdmnlaytk sfynkqvadi gllirdairt priypvkdsl gnyvvpslns
      541 nnviaqlalg gynreewdnl lgglnititp anhftvnlna sgtysiknyk trvnkysyap
      601 yyttanppvn nvqaqaeykd latnvyatae yentfgkhyv kaqvgvrsda vneyygfsat
      661 ryagtnlddd wtigggyipk pdgtldyati gtynsivnpn lfalnslfgr lnyvfkdkyl
      721 aeftwrydgs sklapghrwq ffpafslgwr atdemflenf rdrfgnvkfr yswgqvgnsn
      781 iggfnyqarv nlnpnkypfn ntanpgadft pynellewei stmsnygvdv dffnnklsas
      841 fdffnkrttg iyltqevpgt agigsslqnv gevenkgwel tvnyrgrtgp vshtvganls
      901 dnlnrvirfg qesirgadya yiiregfpia syfgyrsdgl yqnlddikna pkvpfaynqq
      961 vqpgdvryid rnedgvidad dryvfgnpfp rytfgftyna vwknwdftmf wqgvgrrsqf
     1021 lrgdiveafh nnedhayvqh idrwtpmnpg asyprltigt anannfaysd ywmfdskylr
     1081 lknlqlgysl pksvtgivki qsarlyftsq nlltftprrf relgvdpeft qyddklgfsn
     1141 ynaiagrnyp naatfafgld ikf
//
LOCUS       WP_120518282            1083 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120518282
VERSION     WP_120518282.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1083
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117067
     Region          87..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mavnvllrtg wyspvarsrm yrfirnaaly llllsvcvmq smaadhptig knivktvsip
       61 llekvagngv aeegtvssrr ifkeediavk givtgeggia lpgvsivvkg gtrnaitdea
      121 grysisvpen avlifsytgy erkevpvnga elnvslqpav ksleavvvta lglerkkrtl
      181 tystqgvsak eltearelnm vnalqgkvag lninsgssgv gsqarvtlrg nrsisgnsqp
      241 lyvidgvvvr aspadintdn iaslnvlkga naaalygsag qngvivietk rgksginvtv
      301 nstymaekai lstpyqyeyg qgvsgnylkt sesswgpkld gtmvdtwsld paeagnkyaf
      361 lpdrkardni frtghnwatn vsvsagsdkg rtlftythtd gagvlpgndl srhnaalrit
      421 nqltsrltld vkldymkqki dnrldegess fnplrqvatm panirdqdat rfefidpvlg
      481 vmrqnywspg titganpywt lyrnlrynkv drlmglasls yqfsenfraa irgsfdgenn
      541 aleeksyygt yrdpsgryav gkgsallvng dfllsytkki nadwnvtana ggeirhikdd
      601 alsastgtgm sipnffalsn lalapaatya pgvaietqsl yanaqlgwkd avfleltgrn
      661 dwsstlaann rsyfypsagi saviselaql petftylklr gswaevgnga spgllqrfaa
      721 ssaggnlgyl slnttlpnkn lkpemtrsle aglelrmfnd rvgidvtayr tntnnqiflq
      781 alpvgsgals fytnggdven rgvevilntt pirttnfnwd lnvnfarntn tvkelsdeip
      841 sltvggdtym rnfvleegkp fgqiygkgfv rdnkgrvivg vnglpqttpg ktvllgnvnp
      901 dwtggvsssf swknwsagfv ishkqggdia sftdailyge glveetlqgr dggllfgkni
      961 lqnipgvkad gsentvavna qqlwqylggr tapvgemfvr satntrlref tlgyklpesl
     1021 frkgplasiq lslvgrnlff lyreakgpdp dytegtgtis egfqsfalpp srsfganiki
     1081 nfk
//
LOCUS       WP_120519059             983 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120519059
VERSION     WP_120519059.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..983
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105683
     Region          27..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkmrllkal lfcpliflat evlaqtkpvs gkitddrgei iigasvqvkg tstgtvtdnn
       61 gifklnvpas attllvsfig ytqqevsian tsevnvvlqt enttltdvvv vgygtarkkd
      121 ltgsvaslka kdfnkgiana pdqliqgkva glmvvntsga pgaattvrir gvssvrsgnq
      181 plyvidgvpl dgrvarpnin anglgitpda nplnfvnafd iasmdvlkda sataiygsrg
      241 sngviiittk kgsegpakld fnysvgmssi mkklkvldan efrdvlksyn ltsgdggane
      301 dgmkaitrtg itqnfnlgis ggsenaryra sfglmnqegi vrksglkkyt gnlsgqfkfl
      361 eskklgldfn lmaaqtveql apisnnadfr gsligqalqw nptvplykad gsfnqlggns
      421 ainpiamsea wddkpnisyi lgsispyfki tddleyrflf sinrqtgirr temkgyitip
      481 gveglgqayy gnaelttklf thtlsynkql stafnlnavv gyeyqdfayq gvdlgalgft
      541 tdalpytsil qnalqsntfi ssfvnpqsel qsifgrvtan lhdkylvtat mradgsnkfg
      601 knnrygyfps faakwnisse gfmkggtffq nlalrlgwgi tgnqefpaga aqeqyalaga
      661 ggarqvnvan pdlkweksnq inagldfail gnrltgsvdy fnkkttdllf nytaivpgpa
      721 snlwinmpgd itnkgveval rgdiirgknl nwgigvnatf isnelqnytg pdvltgaisg
      781 qgvtgatvqr fanghplnvf yvrkyegldk dglaqyadng ntmyymgdpn pkqllgistd
      841 lsykkwyvav nfngafgqdi ynntantvlp vnnlssrnia aalkgnnenl anpittssry
      901 iengdflklt natisyslgs igktfknini sltgqnlfvi tnysgfdpev ntdksingvn
      961 sfgieyspyp tarniilgvs vsl
//
LOCUS       WP_120519015            1156 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120519015
VERSION     WP_120519015.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1156)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1156)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1156)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1156
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1156
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127316
     Region          118..1154
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtiprscm mpallwlclt istatraqqk vysfnwenta lssvfrqieq aanvrfsynp
       61 sgikedmpik lridsqqlda vvarlcqain snyriteniv mirpsgesat aadyrlhgkv
      121 tnekneplpg vtvhnqrlkk avhtladgvf sidaapgdqi eftmigferq vqkagaegsl
      181 lnitmkekvt dlgtvvvtal girrearalg yahaevsgdd mkraretnvi nslagkvpgl
      241 iinstaggpa gssrviirgn tsisgnnqpl yvvdgvpidn snygqvsgdk yssgfdfgda
      301 isainpddie tisvlkgpsa salygsragh gvilittkkg slkkalgiei nstatmekql
      361 trfddyqyey gqgtggtipr drdqarttmf snfgarldpt lmvasfdgkq rpyglvrnni
      421 enffrtgstf tntisltsat dntafrlsls dlknndivpt sdmrrntanf ssnskfgkrl
      481 svdakvmymr eevnnrpala ddagnignaf vglannidqs ifssgykndn gdyvdwggge
      541 yrlnpywvin emsnktkkdr imgnivanyq fadwialqgr fstdityfky rkysppstpg
      601 sitgryegid qkfqtteadv lltlqkqftp nwygaarlgs slsqysrpgt nllgtdmale
      661 eisinsfndr vateiesrqr tnsfyglfsg ayknwayldv tlrrdatstl pksfnsylyt
      721 sfsgsfiftd afkmknkvlt ygklrgsvae vgsgtdphml nlnyallqqk ingeaaggis
      781 ttvlppgdlk ptrtrsyeig temkfldnni gldvtaytqd srdqinyvpi ptssgfrtml
      841 vnagviqnkg ieiaisatpv rtenfrwdis vnaarnkntv kslaegipfl tlsdarwlgv
      901 svvaqpnapy gailgydyqk dpsgniilds itltpvptde rkvmgkgtwd wtggmttsls
      961 yknftfnail dmkqgadlfs mtnlfavlrg shettlegrq ewihseeerm aanktpvewq
     1021 qsgnvrgyvp qgvvrngldn sgkpvyvknt ramdpgqyws lfyadakgit tpflydasyi
     1081 kvrelsltys lpqsmlrkak igavtvsvvs rnpfilhknv pnvdpdsnyn ngngqgleyg
     1141 slpsrrswgl nlnvrl
//
LOCUS       WP_120519228            1080 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120519228
VERSION     WP_120519228.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1080)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1080)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1080)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1080
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1080
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119394
     Region          25..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkkllfllv vlmgmvysva maqdrkvsgt vkdskgeplp gvsireagts ngtasdvsgk
       61 fsltlkganp vleltflgya kttikvdnrs dysivmqsda qqlkdvvitg yeqkkrktlt
      121 tsvtrldaee iqnipaasvv nllqgrvagl svvnnggmpg vgapvfirgn asvassfndd
      181 rifsdplfvv dgiqvpadra sakgftanal gtgnspiswl npndiesidv lkdaaaaavy
      241 gsrgangvii iktktaktgk pkidlrayng infapslfpi lggksereak vdiwnrfapy
      301 darmsgmpiq mtdslnpffn nstdwqsmyf qtgriqnyda sisagnemgn yrigggyyse
      361 dgivintgfk rytanftgrl lpnkkttivm qtylgrtdrs rgnskngqgv ssqgiwsips
      421 stymipdksp ygggmldayk lnrdknftnt vnsslqlmya ftpeiiftst gslsyandkr
      481 dyffasvann nssdagqyna lsngytwtnq lswnhytpnn dhnfgaflvq efnkntievt
      541 qidakggssd liqivqgfsp srtvtktgyg anatssvlgk vnygyrekyl idasiradgs
      601 sklspnkrwg yfptvsaawr iaeeqwvkdn ltwlneakvr lswgktanqy venfasvssl
      661 ngnaggfnep sysyvssygg skvaiqnfnq mqnldlqwey sdqtnlglel talkgrisli
      721 adlyqryteg gtydeqlpts sgysiikrng idmlnkgfel tlsvnvldpk savswttrfm
      781 larntsqvak lpnnnrpfml dnvtmvkvgs apygfvfmvn dgvwqsnsev pvdpftgkkl
      841 ffdygylpyr egaprfvdln gdykindlng dgarevndrt wvgdptpkid ggwvntvswk
      901 gftldmmfnf rwgvkvvnsa lqrywnstkv tggynpnytt fdyfngnsld wggippmsef
      961 diygfapgdr ggkdarfptl dywtgsiqtf wniydyksaf vedasflrlk nvmlsynlps
     1021 kflkrfgier vmaygntenv fiitkysgrd peaiefpsgy drgrnyplsr kmtlglnvtf
//
LOCUS       WP_120519275             971 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120519275
VERSION     WP_120519275.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 971)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 971)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..971
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108023
     Region          22..969
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkylllfssf lfcmlqaqaq qrtitgsvad ssgspvpgat vlvkgtnigt aaggdgryai
       61 qvpndnavli ftsigfqdre vtvgretvln vrllqggkdl navvvmgfsk verqhvassv
      121 aqmdmkqakt rpviklqeaf sgtiagvtmq qgtnlpgavp gtisirgist lqnaeplviv
      181 dgmeqsltdi dpnqvksiti lkdaasasmy gsrgangvii ietergttgk fkvdlntwya
      241 iqkpidlpkf vngaeymrln neartlqgqt ptfsadsirk mesgqipsvd wldevmqrns
      301 nsqntalsvs ggggvgtfnl mlghlrengl nniegsrkys arfntninia dkfvlladfy
      361 ahrlqvdrlf andngnslya dawkmnasqq lfyeddrgqn ipehyilhnn lnpaasierg
      421 girnylhdhs ainlrpkyni nknlniegnv sylitksaek wkratfkfyd gngkpvttwg
      481 nivdalqrvs tsqvtgrvla nytsslrrgk dkiyftagae amswnytdfr evskssffgk
      541 lnysfdnryi leftpradgs skfapgnrwg ffpsgalawn vtnenfmkpi vrsgklnnlk
      601 frvsyglign envdpylwee ivntwgwtmr lpnpafswek qkqanlgmea tlldnrltit
      661 advykkhsfd liysdfpvpp ltgshtlesa vnigevdnkg felsatwsdn igdlkysigg
      721 mlfdnrneim kagykandtl ifkdnndkvw yrgialdnyy gykadgfyrd aaevegspar
      781 fpntlpgdir yvdqnkdgvi nnedrvnlgd pyphmnysvn lnlsykrwdf avlgqgvger
      841 tgrlngmegy pvlvdgatna lgaprqyyad nrwtpenpns rfprvwtgts tntnlsdvwl
      901 snaayfrvkm iqlgytipri gsqirnvriy vnaqdaitft nweglepern ggngnyprma
      961 nfsiglkatm f
//
LOCUS       WP_120519280            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Chitinophaga
            barathri].
ACCESSION   WP_120519280
VERSION     WP_120519280.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117115
     Region          23..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfkrtlqlmf llllslhgaa qeqkvtgtvk dktgsalpgv tiadkgvkns gtvtdangnf
       61 sltvkgtart lifsiigynn qevdvagkts invvmevntk tlgdvvvigy qevsrrknta
      121 siatvkgeti anlpapsvdm mlqgrvsgvn vqnfsgepgi rntivvrgns svlrgydear
      181 alsaplyvid gvptsatefg gidasgtgtn aiaginpndi esldilkdas aaaiygsrgs
      241 ngiiiiktkr akkgkpefnf stymgiskkp qltevvagae errmkmavmd lyngpiddet
      301 lpmmltdsln pdfnnatdwq syfyqngmin nydlsmsgan dvinyrisvg hykedgivkn
      361 tgfkrytimg tigsqlapwl nnqtrfrvtr tdrprsiner tgsffafdsy slpssfyklt
      421 dntreyllgn dsrqdkninn nvlfttafna nvakglnfnv tanyenrasn rdyyqpsvvr
      481 dnkqgyayfy sdkteiasly ttleyskafg ahhlnliggq nleytkwvwn sgdadlipnd
      541 yawavnvsnk lfsntsssiq etglqslfar vnydfkdryl lsasftgdas skfgadnrwg
      601 afpsvsagwi vsdepffqdl nwlsflkirg sygitgnqpe knylgynnyn vnragfgdnn
      661 dvtsyngtsv itpnyrdgia qkdlsweesk qgnigfeagf fkdrihvvvd aykrettkgf
      721 fsyllpnasg yteaqtnaig trnaglevti ntrnlnpkse lqwytdltfs ynqnmitalp
      781 nggrsivfny ntgvygsdyl lsvglpanqf yvfeykgiys rqedipfnll tgqplknfvg
      841 wdyyagdpil vdqdgnfdlk epmdqivggd pnpkfyggvl nnltwkgftf gvflnytfgr
      901 dilnsynnrr feylfeatgd egernlakra imdidklnyw kkpgdkadlp tfslvngqrs
      961 pyrfldkstm yiengdylri ktitfgynfn ehmlrnlkik rlrlygvidn iytfqhsnvp
     1021 daeavnaygv ydgdgypipk kftfgldfgf
//
LOCUS       WP_120519311             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga barathri].
ACCESSION   WP_120519311
VERSION     WP_120519311.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga barathri
  ORGANISM  Chitinophaga barathri
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Chitinophaga barathri"
                     /db_xref="taxon:1647451"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40088
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milavlkeks genrvslvpe vvkqlvqqhv evwveegagq gafypdtmft eagavikprs
       61 ellqkadlll slrqpspqdw eqvppgkiwm glyqplynvp lmqqwadkkf tvfsldtipr
      121 ttraqsmdvl ssqaniagyk avllaaytys ryfpmlmtaa gsippakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgak fvevegaada skaggyaveq sadyqakqta
      241 riaesaakad iiittaqipg kpapvliska mlesmragsv vidlaaatgg ntaltkdast
      301 ivhngvtiig nsdlagaapa dasklyarnv lnflklmltk egainlnfed dlvkgtcivh
      361 ngeivndrvk qlqpaav
//
LOCUS       WP_120520123             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter celericrescens].
ACCESSION   WP_120520123
VERSION     WP_120520123.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter celericrescens
  ORGANISM  Arthrobacter celericrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Arthrobacter celericrescens"
                     /db_xref="taxon:2320851"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53527
     Region          3..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivael gretrvaatp atvkqllglg ydvvvekgag esasfrneey aaagasivga
       61 edawgsdvvl rinpptenei nrlaegatli smlspglrpe lvealaarpi talaldavpr
      121 israqsmdvl ssmaniagyr avieaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksiggt ylkveveeem kssdgyakat seaynrraae
      241 iyteqardvd ivittalipg rpapklltad dvaamkpgsv ivdmaagqgg nvegsvager
      301 ivtengvvil gytdlparlp aqasqlygtn llnllklltk dkdgqltidf ddvvqrsvtv
      361 vrdgektwpp ppvqvsaapa aqadatraee gpageaaktg lspagkagli aagiaflfgi
      421 navapaplpq hftvlllsvv vgfyvigkvh halhtplmsv tnaisgiivv gallqitses
      481 livqalsava vllasinifg gfavtrrmla mfskgnkaqg
//
LOCUS       WP_120520730             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arthrobacter celericrescens].
ACCESSION   WP_120520730
VERSION     WP_120520730.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter celericrescens
  ORGANISM  Arthrobacter celericrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Arthrobacter celericrescens"
                     /db_xref="taxon:2320851"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33695
     Region          13..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msnaentasq vrdviivgsg pagytaavyt aranlkplli agsvtaggel mnttdvenyp
       61 gfpdgimgpd lmenfekqaa rfgteiqfed vtelelegdi ktvtiatget frarsiilst
      121 gsayrelgle nekrlsghgv swcatcdgff fkdqdiavig ggdsameeal fltkfaksvt
      181 vvhrrdtlka skimgdraqa hekinfvwnt avedviggdk vtglklknlv dgtvselpvt
      241 gvfvaigndp rselvkdkle ltpegtiavq grssktsikg vfaagdvidp tyrqaitasg
      301 sgcvaaldve hyladlhg
//
LOCUS       WP_120521173             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arthrobacter celericrescens].
ACCESSION   WP_120521173
VERSION     WP_120521173.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter celericrescens
  ORGANISM  Arthrobacter celericrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Arthrobacter celericrescens"
                     /db_xref="taxon:2320851"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33995
     Region          6..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msteqliiig sgpagytaai yaaraglepl vvagavtagg almntteven fpgfpggiqg
       61 pelmdglqeq aekfgakivf ddavsvelkg hlkrvaigag etyaapavil atgsaykelg
      121 lpeekklsgh gvswcatcdg fffreqdiiv vgggdsamee atfltrfaks vtvvvrreel
      181 rasrimaqra kdnpkisfaw nsavtaihgn akvtgvtlrd trsgekreha atgifvaigh
      241 vprtelltgq velddegyik vaspttvtnl rgvfacgdav dhryrqaita agsgcaaald
      301 aerylaaled adsiatalve epths
//
LOCUS       WP_120522742             391 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter celericrescens].
ACCESSION   WP_120522742
VERSION     WP_120522742.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter celericrescens
  ORGANISM  Arthrobacter celericrescens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Arthrobacter celericrescens"
                     /db_xref="taxon:2320851"
     Protein         1..391
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39980
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiarerr kgerrvaatp dtvkqlaalg levlvesgag lesghpdeay qdagawivdt
       61 ldpgnldlll hvrpldpdsv rslkqgavtv glaspsselp tvqaladagv tsfalelvpr
      121 israqsmdal tsqalvagyr cvleaatrlp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandirpas adevasmggt firldvetae asggyarels adrgalqrel
      241 laphvaaadv littaavpgr rapllvtlam vqamrpgsvv vdlaaesggn vegvvagedt
      301 viptadgrgt vtlvgmkdaa salpadasrl yaknvaslle llvrdgafap dwedevvags
      361 clthdgavrh gptaealaal ttaesatega n
//
LOCUS       WP_120545329             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corallococcus terminator].
ACCESSION   WP_120545329
VERSION     WP_120545329.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus terminator
  ORGANISM  Corallococcus terminator
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Corallococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corallococcus terminator"
                     /db_xref="taxon:2316733"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34617
     Region          8..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdkiqkvt iigsgpagyt aaiyaaranl epvvfaggpt lehpqrvpgg qlmvttdven
       61 ypgfaepitg pelmerfqkq aerfgtalhm enitkvdfsq rpfllesesg mkvrsetvii
      121 stgatakwln vkgedtyknr gvsacatcdg afykkqdvlv vgggdtamee atylakivnh
      181 vtlihrrdsl raskvmqera lnnpkisflw nsaveevvgn nkgmtgavvr nlktndsqlv
      241 tatglfvaig htpntelfqg ilethqggyl ktipgstrtn ipgvfacgdv qdsyyrqait
      301 aagtgcmaai daerwlieqg e
//
LOCUS       WP_120529871             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corallococcus exercitus].
ACCESSION   WP_120529871
VERSION     WP_120529871.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus exercitus
  ORGANISM  Corallococcus exercitus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Corallococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corallococcus exercitus"
                     /db_xref="taxon:2316736"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34626
     Region          8..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdkiqkvt iigsgpagyt aaiyaaranl epvvfaggpt lehpqrvpgg qlmvttdven
       61 ypgfpeaitg pelmerfqkq aerfntvihm enitkvdfsq rpfllesesg iqvrsetvii
      121 stgatakwlg vkgedtyknr gvsacatcdg afykkqdvlv vgggdtamee atylakivnh
      181 vtlihrrdsl raskvmqera lnnpkisfmw nsaveevvgn akgmtgavvr nlktgdsqlv
      241 naqglfvaig htpntelfqg ilethqggyl ktipgstrtn iegvfacgdv qdsyyrqait
      301 aagtgcmaai daerwliehg e
//
LOCUS       WP_120537816             321 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Corallococcus].
ACCESSION   WP_120537816
VERSION     WP_120537816.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus
  ORGANISM  Corallococcus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corallococcus"
                     /db_xref="taxon:83461"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34617
     Region          8..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdkiqkvt iigsgpagyt aaiyaaranl epvvfaggpt lehpqrvpgg qlmvttdven
       61 ypgfaepitg pelmerfqkq aerfgtalhm enitkvdfsq rpfllesesg mqvrsetvii
      121 stgatakwln vkgedtyknr gvsacatcdg afykkqdvlv vgggdtamee atylakivnh
      181 vtlihrrdsl raskvmqera lnnpkisflw nsaveevvgn nkgmtgavvr nlktndsqlv
      241 tatglfvaig htpntelfqg ilethqggyl ktipgstrtn ipgvfacgdv qdsyyrqait
      301 aagtgcmaai daerwlieqg e
//
LOCUS       WP_120557457             308 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Corallococcus aberystwythensis].
ACCESSION   WP_120557457
VERSION     WP_120557457.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus aberystwythensis
  ORGANISM  Corallococcus aberystwythensis
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Corallococcus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Corallococcus aberystwythensis"
                     /db_xref="taxon:2316722"
     Protein         1..308
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34800
     Region          5..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 manidiyskr kkrqegsapd vfvydkvpea lriqivhmwq difrdhvrgg tfaydcykav
       61 hdilcreygv fylsndiagm mddygtrcrk filscdpdrv ldiveltfkv arlkigdrdt
      121 pghlsvrfmd etiaelnsrf rehgvgyqfe sdaimrvdss llhaevvrpa lrllmeeefq
      181 gaeeefrsah ehyrhgkyke alveslkafe stmktvcgrk swvvaenata rvligalfdh
      241 glvpapmaah fsalrttlea gvptlrnrlg ghgqgeepve vpdylaayvl hltaanivmv
      301 veafkamk
//
LOCUS       WP_120560381             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corallococcus aberystwythensis].
ACCESSION   WP_120560381
VERSION     WP_120560381.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus aberystwythensis
  ORGANISM  Corallococcus aberystwythensis
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Corallococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corallococcus aberystwythensis"
                     /db_xref="taxon:2316722"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34647
     Region          8..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdkiqkvt iigsgpagyt aaiyaaranl epvvfaggpt mehpqrvpgg qlmvttdven
       61 ypgfpeaitg pelmerfqkq aerfntvihm enitkvdfsq rpfvlesesg mkvrsetvii
      121 stgatakwlg vkgedtyknr gvsacatcdg afykkqdvlv vgggdtamee atylakivnh
      181 vtlihrrdsl raskvmqera lnnpkisfmw nsaveevvgn pkgmtgavvr nlktgdsqlv
      241 natglfvaig htpntelfqg ilethqggyl ktipgstrtn iegvfacgdv qdsyyrqait
      301 aagtgcmaai daerwliehg e
//
LOCUS       WP_120565006             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corallococcus sp. AB011P].
ACCESSION   WP_120565006
VERSION     WP_120565006.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus sp. AB011P
  ORGANISM  Corallococcus sp. AB011P
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Corallococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corallococcus sp. AB011P"
                     /db_xref="taxon:2316735"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34538
     Region          8..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdkiqkvt iigsgpagyt aaiyaaranl epvvfaggpt lehpqrvpgg qlmvttdven
       61 ypgfpeaitg pelmerfqkq aerfgtvihm envtkvdfsk rpfllesesg iqvrsetvii
      121 stgatakwlg vkgedtyknr gvsacatcdg affkkqdvlv vgggdtamee atylakivnh
      181 vtlihrrdsl raskvmqera lnnpkisfmw dsaveevvgd gkgmtgavvr nvktgdsklv
      241 nahglfvaig htpntelfqg ilethqsgyl ktipgstrtn vegvfacgdv qdsyyrqait
      301 aagtgcmaai daerwliehg e
//
LOCUS       WP_120572527             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Micromonospora].
ACCESSION   WP_120572527
VERSION     WP_120572527.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora
  ORGANISM  Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora"
                     /db_xref="taxon:1873"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33784
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlkp lviegvqsgg almttteven fpgfadgilg
       61 pelmdnmrkq aerfgaeflt ddvtrvelkd tgeigsdavs tvwvgetayr aravilstgs
      121 awrplgvpge qeylghgvss catcdgfffr nqhivvvggg dsameeasfl trfaesvtil
      181 hrrdsfrask imadralgne kikvewntvv eeilgddgkv ngvrvrnvht geskvldvtg
      241 vfvaighdpr selfrgqvel ddegyvkvqa pstrtsvpgv faagdlvdht yrqaitaagt
      301 gcaaaldaer fiatiqg
//
LOCUS       WP_120577034             321 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Corallococcus].
ACCESSION   WP_120577034
VERSION     WP_120577034.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus
  ORGANISM  Corallococcus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corallococcus"
                     /db_xref="taxon:83461"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34593
     Region          8..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdkiqkvt iigsgpagyt aaiyaaranl epvvfaggpt lehpqrvpgg qlmvttdven
       61 ypgfpeaitg pelmerfqkq aerfgtvihm envtkvdfsk rpfllesesg iqvrsetvii
      121 stgatakwln vkgedtyknr gvsacatcdg affkkqdvlv vgggdtamee atylakivnh
      181 vtlihrrdsl raskvmqera lnnpkisfmw dsaveevvgd gkgmtgavvr nlktgdsklv
      241 nahglfvaig htpntelfqg ilethqggyl ktipgstrtn iegvfacgdv qdsyyrqait
      301 aagtgcmaai daerwliehg e
//
LOCUS       WP_120616044             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corallococcus sp. CA053C].
ACCESSION   WP_120616044
VERSION     WP_120616044.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus sp. CA053C
  ORGANISM  Corallococcus sp. CA053C
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Corallococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corallococcus sp. CA053C"
                     /db_xref="taxon:2316732"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34609
     Region          8..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdkiqkvt iigsgpagyt aaiyaaranl epvvfaggpt lehpqrvpgg qlmvttdven
       61 ypgfpeaitg pelmerfqkq aerfgtalhm enitkvdfsq rpfllesesg mqvrsetvii
      121 stgatakwln vkgedtyknr gvsacatcdg afykkqdvlv vgggdtamee atylakivnh
      181 vtlihrrdtl raskvmqera lnnpkisflw nsaveevvgn pkgmtgavvr nlktndsqlv
      241 tatglfvaig htpntelfqg ilethqggyl ktvpgstrtn ipgvfacgdv qdsyyrqait
      301 aagtgcmaai daerwliehg e
//
LOCUS       WP_120630028             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corallococcus sicarius].
ACCESSION   WP_120630028
VERSION     WP_120630028.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus sicarius
  ORGANISM  Corallococcus sicarius
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Corallococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corallococcus sicarius"
                     /db_xref="taxon:2316726"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34595
     Region          8..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdkiqkvt iigsgpagyt aaiyaaranl epvvfaggpt lehpqrvpgg qlmvttdven
       61 ypgfpeaitg pelmerfqkq aerfgtalhm enitkvdfsq rpfllesesg mqvrsetvii
      121 stgatakwln vkgedtyknr gvsacatcdg afykkqdvlv vgggdtamee atylakivnh
      181 vtiihrrdsl raskvmqera lnnpkisflw nsaveevvgn pkgmtgavvr nlktndsqlv
      241 tatglfvaig htpntelfqg ilethqggyl ktvpgstrtn ipgvfacgdv qdsyyrqait
      301 aagtgcmaai daerwliehg e
//
LOCUS       WP_120620191             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corallococcus sp. CA049B].
ACCESSION   WP_120620191
VERSION     WP_120620191.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus sp. CA049B
  ORGANISM  Corallococcus sp. CA049B
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Corallococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corallococcus sp. CA049B"
                     /db_xref="taxon:2316730"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34588
     Region          8..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdkiqkvt iigsgpagyt aaiyaaranl epmvfaggpt lehpqrvpgg qlmvttdven
       61 ypgfpeaitg pelmerfqkq aerfgtvihm envtkvdfsk rpfllesesg mqvrsetvii
      121 stgatakwlg vkgedtyknr gvsacatcdg affkkqdvlv vgggdtamee atylakivnh
      181 vtlihrrdsl raskvmqera lnnpkisfmw dsaveevvgd gkgmtgavvr nvktgdsklv
      241 nahglfvaig htpntelfqg ilethqsgyl ktipgstrtn vegvfacgdv qdsyyrqait
      301 aagtgcmaai daerwliehg e
//
LOCUS       WP_120632028             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Ruegeria sp. EL01].
ACCESSION   WP_120632028
VERSION     WP_120632028.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria sp. EL01
  ORGANISM  Ruegeria sp. EL01
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Ruegeria sp. EL01"
                     /db_xref="taxon:2107578"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33411
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 madtrhtkvl iigsgpagyt agvyasraml epilvqgiep ggqlttttev enwpgdtevq
       61 gpdlmvrmqd hakamgcevi gdiisdlnld qrpfvakgds gttytadavi latgarakwl
      121 glpseekfkg fgvsacatcd gffyrgqeiv vigggntave ealfltnfas kvtlihrrde
      181 lraekilqdr lfkndkiepl wfhqleevvg tdaplgvegv rvknvktgev teipckgvfv
      241 aighapanel vkdkldshmg gyvvtkpgst etsipgvfaa gdltdhiyrq avtsagmgcm
      301 aaldaerfla eqd
//
LOCUS       WP_120635941             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ruegeria
            sp. EL01].
ACCESSION   WP_120635941
VERSION     WP_120635941.1
KEYWORDS    RefSeq.
SOURCE      Ruegeria sp. EL01
  ORGANISM  Ruegeria sp. EL01
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Ruegeria.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Ruegeria sp. EL01"
                     /db_xref="taxon:2107578"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55770
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeil dgenrvamtp dsavqlqklg ydcaiekgag qaagfsdaty eavgveivkt
       61 aaslwksadi vakvriptea emkrltkgkt lisffnpagn eegmelaksk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvqsdefr
      241 eaqlakfrel apevdivitt alipnreape lwtkdmveam kpgsvivdla aekggncklt
      301 vadekivtdn gvtiigytdf psrmasqass lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgstvthqge itfpppppkv qaiaaqpkae vkeltpeekr aqevaafkaq tkqqftllgv
      421 ggvlmllvgl iapasfmqhf ivfvlaifvg fqviwnvshs lhtplmaitn aissiiivga
      481 lmqigsgsfl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_120639921             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Teichococcus wenyumeiae].
ACCESSION   WP_120639921
VERSION     WP_120639921.1
KEYWORDS    RefSeq.
SOURCE      Teichococcus wenyumeiae
  ORGANISM  Teichococcus wenyumeiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Roseomonas.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Teichococcus wenyumeiae"
                     /db_xref="taxon:2478470"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39502
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,76,101,298,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,134..135,144..145,148..149,152..153,155..156,
                     158..163,165,167..169,172,195..196,288..289,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,134,137,140,181..184,204..206,238,249,
                     266..268,275,277)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,134,144,187..188,195,211..212,214..217)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(164..168,171,174,197,199)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavlkerr agetrvaatp etvkkliglg itavavesga glasgypdaa yreagaeiap
       61 daaaalagaa illkvrapla agegevdels liprdtlllg tlealgnper akayadaglq
      121 acsmellpri traqsmdils sqanlagyra viegavafdk gfpmlmtaag tipaanvfvm
      181 gagvaglqai atarrlggrv satdvrpaak eeikslgasf vgyedeeska aqtaggyakq
      241 lsaefyakqa evvathiakq dvvvttalvq grkaptlvte amvdsmkpgs vivdiaadag
      301 gncaltvpgq aivtgngvki lgygnwpgri agaasalyar nlltflttfw dkdakaprlp
      361 eddeivrgvv ltrggavvhp qltqaa
//
LOCUS       WP_120647473             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corallococcus llansteffanensis].
ACCESSION   WP_120647473
VERSION     WP_120647473.1
KEYWORDS    RefSeq.
SOURCE      Corallococcus llansteffanensis
  ORGANISM  Corallococcus llansteffanensis
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Myxococcaceae; Corallococcus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Corallococcus llansteffanensis"
                     /db_xref="taxon:2316731"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34649
     Region          8..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdkiqkvt iigsgpagyt aaiyaaranl epvvfaggpt lehpqrvpgg qlmvttdven
       61 ypgfpeaitg pelmerfqkq aerfgtalhm enitkvdfsq rpfllesesg mqvrsetvii
      121 stgatakwln vkgedtyknr gvsacatcdg afykkqdvlv vgggdtamee atylakivnh
      181 vtlihrrdtl raskvmqera lnnpkisflw nsaveevvgn hkgmtgavvr nlktndsqlv
      241 tatglfvaig htpntelfqg ilethqggyl ktvpgstrtn ipgvfacgdv qdsyyrqait
      301 aagtgcmaai daerwliehg e
//
LOCUS       WP_120651280             316 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Pseudomonas].
ACCESSION   WP_120651280
VERSION     WP_120651280.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33601
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli vlgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmermq khaerfdtei vydhihtael qkrpfilkgd sgtyscdali latgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvvc vigggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfekaangnv rlhwnhtlde vlgdntgvtg vrlkntadgt tkelslagvf
      241 iaighkpntd lfkgqlemrd gylivqggle gnatatsipg vfaagdvadh vyrqaitsag
      301 sgcmaaldae kflddn
//
LOCUS       WP_120653730             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_120653730
VERSION     WP_120653730.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38852
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikklvsqg hqvtvqsgag vsasipdsaf eaagatignd
       61 saafgadlvl kvvaptegel ahmragavlv gmlnpfsnev iarmnargit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahhypr fmpmlmtaag tvkaarilil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvikhgv tivghsnlaa mvpadasaly arnlldflkl vidkdgqfhl nleddivaac
      361 lmcrdgqvvr nng
//
LOCUS       WP_120654669             315 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Pseudomonas].
ACCESSION   WP_120654669
VERSION     WP_120654669.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33239
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgpalmqrmq ehaerfetei vfdhinavdl agkpftlvgd sgtytcdali iatgasaryl
      121 glpseqafmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlvhrret
      181 fraekilqdk lkariaegki elrlnaevde vlgddmgvtg vrlkrndggt delkvdglfv
      241 aightpntsl fegqlalkdg ylvvnggrdg natatsipgv faagdvadhv yrqaitsaga
      301 gcmaaldver yldah
//
LOCUS       WP_120656091             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Butyrivibrio sp. X503].
ACCESSION   WP_120656091
VERSION     WP_120656091.1
KEYWORDS    RefSeq.
SOURCE      Butyrivibrio sp. X503
  ORGANISM  Butyrivibrio sp. X503
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Butyrivibrio.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Butyrivibrio sp. X503"
                     /db_xref="taxon:2364878"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33388
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydliiigsg paglsaavya kraglnmlii eknpvsggqi idtyevdnyl gipgvngfdl
       61 amkfrehadk lgaefadgtv tgikcisegs dtkapvykie tdsgeyetht vilaaganhs
      121 klgvpgeeey igkgvsycat cdgafyrgkv tavngggdva vedaiflsrf aekvylihrr
      181 delraakilq delfgiknie viwdnvvkei kgkdkvnsll ienvnnkeek elpvdgifva
      241 vgihpstdvf adlvkcdeng yviagedgat nvpgifaagd lrkkrlrqii tavadgantv
      301 tsvqdflvgk aks
//
LOCUS       WP_120661738             506 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus opacus].
ACCESSION   WP_120661738
VERSION     WP_120661738.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..506
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52182
     Region          1..505
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgvlkear agetrvaatp ttvaalqklg yqvvvepgag epagftdgay aeagaelrdp
       61 laadvvigvn pptlaqrdrl qpgatliaml nprlddgiva dlaqrpital smdavprisr
      121 aqsmdvlssm anvagyravv eaahefgrmf tgqvtaagki pparvfvvga gvaglaaiga
      181 asamgaivra fdvrpevaeq vasmgaefve idfeaevsad gyakemtaeq eiataamyde
      241 eacaadivit talipgrpap kliteetiaa mrngsvivdm aaanggnaal tktderivtd
      301 ngvrilgytd lagrlaaqas qlygtnivnl lklltpdkdg elvldfddvv qrgitvvrdg
      361 estwppppvq vsaaprtpaa atvpaaepka pmspgkrlgv vaavaavlfl ligvapaqlq
      421 lnltvfalai vigyyvighv hhalhtplms vtnaisgiiv vgallqigkg dtaitvisfv
      481 avllacinif ggfavtrrml amfsrs
//
LOCUS       WP_120664535             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Rhizobium].
ACCESSION   WP_120664535
VERSION     WP_120664535.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34526
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mparhtkvli igsgpagyta avyaaramlq pvliagmeqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlq qaqhvgaeiv ndlvtevdts qrpfvartds gqvwtadtlv iatgakakwl
      121 gieseqhfqg fgvsacatcd gffyrnkdvi vvgggnsave ealylsniak svtvvhrrds
      181 fraekilqer lfakanvkil wntevaeitg tpakppmpps vtgarlrdvr tgavtdmpid
      241 gvfvaighap atelfkgklk lkdngylwta pdstatnveg iyaagdvtdd tfrqaitaag
      301 mgcmaaleae ryltghmpva vaae
//
LOCUS       WP_120666882             387 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Rhizobium].
ACCESSION   WP_120666882
VERSION     WP_120666882.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhizobium
  ORGANISM  unclassified Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="unclassified Rhizobium"
                     /db_xref="taxon:2613769"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40660
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msnlvfvake svteetrvaa svetvkkmrg lgfdvvieac agassripdv eyevvgarig
       61 sikdakaadv ilkvrrpttk eiagyksgai iiaimdpygn eaalaemara gltsfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg alvsatdvrp aakeqvaslg akfiavedee fraaetaggy akemsreyqa
      241 kqavlvadhi akqdiiitta lipgrpaprl vsrdmlkamr pgavavdlav erggniegae
      301 ygkvaevegv rvigypnmag riaasasaly aknlvtflet mvdkdskslg lnradelika
      361 tmltddgevv hpsfvdpdqp tvnkgdl
//
LOCUS       WP_120665240             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Moraxella catarrhalis].
ACCESSION   WP_120665240
VERSION     WP_120665240.1
KEYWORDS    RefSeq.
SOURCE      Moraxella catarrhalis
  ORGANISM  Moraxella catarrhalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Moraxella catarrhalis"
                     /db_xref="taxon:480"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33742
     Region          5..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqhhrliil gsgpagysaa vyaaranlnp viitglqvgg qlttttevdn wpgdahgltg
       61 nglmermksh aerfgtkliy dsitqvdlhn rpftlvgdkg vytcdaliia tgataqylgl
      121 eseqkfmgqg vsacatcdgf fyknqkvavv gggntaveev lylsniasev tlihrrdtlr
      181 aekilqdqlf ekvkdgniki ewnhqikevv gddmgvtgvm iestqdgsik qldimglfva
      241 ighkpntklf dgqlnmqdgy ivvnsglngn atatningvf aagdvadhty rqaitsagtg
      301 cmaaldaeky ldslti
//
LOCUS       WP_120667068             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Caldibacillus debilis].
ACCESSION   WP_120667068
VERSION     WP_120667068.1
KEYWORDS    RefSeq.
SOURCE      Caldibacillus debilis
  ORGANISM  Caldibacillus debilis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Caldibacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Caldibacillus debilis"
                     /db_xref="taxon:301148"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34392
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 maeekiydvv iigagpagmt aavytsranl stlmiergvp ggqmvntgev enypgydsil
       61 gpelsekmfa hakkfgaeya ygdikevidg kpykrviagn keykaravii atgaeykklg
      121 vpgemelsgr gvsycavcdg affkgkdliv vgggdsavee gvyltrfark vtivhrrdkl
      181 raqkilqqra fanekidfiw nhtvkrinek dgkvgsvtlv stvdgtekev aadgvfiyig
      241 mvpltkpfek lgitnengyi vtnermetki pgifaagdvr ektlrqivta tgdgciaaqs
      301 aqlyvenlae esekanis
//
LOCUS       WP_120672525             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Moraxella catarrhalis].
ACCESSION   WP_120672525
VERSION     WP_120672525.1
KEYWORDS    RefSeq.
SOURCE      Moraxella catarrhalis
  ORGANISM  Moraxella catarrhalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Moraxella catarrhalis"
                     /db_xref="taxon:480"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33758
     Region          5..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqhhrliil gsgpagysaa vyaaranlnp viitglqvgg qlttttevdn wpgdahsltg
       61 nglmermksh aerfgtkliy dsitqvdlhn rpftlvgdkg vytcdaliia tgataqylgl
      121 eseqkfmgqg vsacatcdgf fyknqkvavv gggntaveea lylsniasev tlihrrdtlr
      181 aekilqdqlf ekvkdgniki ewnhqikevv gddmgvtgvm iestqdgsik qldimglfva
      241 ighkpntklf dgqlnmqdgy iivnsglngn atatningvf aagdvadhty rqaitsagtg
      301 cmaaldaeky ldslti
//
LOCUS       WP_120674104             543 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces hoynatensis].
ACCESSION   WP_120674104
VERSION     WP_120674104.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces hoynatensis
  ORGANISM  Streptomyces hoynatensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Streptomyces hoynatensis"
                     /db_xref="taxon:1141874"
     Protein         1..543
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54648
     Region          8..542
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msqprpqrlg vvaesapget rvaatpssar rlralgyevv vepgagaasg fsdaayvaeg
       61 aqlgdawace vvlkvnapde aevrrladga tligllspal rpdlvealas rrltalalda
      121 vprisraqsm dvlssmania gyravieaah vfgrfftgqv taagkvppak vlvagagvag
      181 laaigtavsl gavvratdpr pevadqvrsl ggeylavdaa qeasadgyak atsaaydrra
      241 aelyraqaae vdivittall pgrpaprllt eadvaamkpg svivdmaaaq ggnvagtvpg
      301 raivtgngvt ligytdlpsr lpaqasqlfg tnlvnllkll tpgkdgrltl dfddvvqrsv
      361 tvvrdgektw ppppvrvsaa papaaapgaa ttapraagaa atgaaagaaa apsagaaagg
      421 aparrtarlt agvryaaaaa galglfllta fspdqligni tvfalsvvig yyvigkvhha
      481 lhtplmsvtn aisgvvvvga llqighadtp itvlsflail lasinifggf avtrrmlsmf
      541 skg
//
LOCUS       WP_120683083             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora musae].
ACCESSION   WP_120683083
VERSION     WP_120683083.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora musae
  ORGANISM  Micromonospora musae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora musae"
                     /db_xref="taxon:1894970"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33682
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlkp liiegvqsgg almttteven fpgfadgilg
       61 pelmdnmrkq aerfgaeflt ddvtrvelvd tgdtgsgavs tvwvgetayr ahavilatgs
      121 awrplgvpge qeylghgvss catcdgfffr nqhivvvggg dsameeasfl trfadsvtii
      181 hrrdsfrask imadralnnd kikvewdsvv eevlgadgkv tgvrlrnvht getkqldvtg
      241 vfvaighdpr selfrgqvev ddegyvkvqd pstrtsvpgv faagdlvdht yrqaitaagt
      301 gcaaaldaer fiatlqg
//
LOCUS       WP_120685002             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces hoynatensis].
ACCESSION   WP_120685002
VERSION     WP_120685002.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces hoynatensis
  ORGANISM  Streptomyces hoynatensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces hoynatensis"
                     /db_xref="taxon:1141874"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33753
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslnp lvfegsvtag galmntteve nfpgfkegim
       61 gpdlmdgmra qaerfgaelv pddvvsvdlg gsvkkvtdsa gtvhearavi vatgsqhrrl
      121 glpnedtlsg rgvsycatcd gfffreqdia vvgggdtame eatflsrfar svtivhrrda
      181 lraskamqer afadpkisfs wdsevaeihg tdgklsgltl rntrtgdtse lpvtglfvai
      241 ghdprvelfk gqldldedgy lsvdapttrt nipgvfaagd vvdhsyrqai taagtgcaaa
      301 ldaerylaal tdaetvasdv aa
//
LOCUS       WP_120690085             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora musae].
ACCESSION   WP_120690085
VERSION     WP_120690085.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora musae
  ORGANISM  Micromonospora musae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora musae"
                     /db_xref="taxon:1894970"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33696
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlkp liiegvqsgg almttteven fpgfadgilg
       61 pelmdnmrkq aerfgaeflt ddvtrvelvd tgdtgsgavs tvwvgetayr ahavilatgs
      121 awrplgvpge qeylghgvss catcdgfffr nqhivvvggg dsameeasfl trfadsvtii
      181 hrrdsfrask imadralnnd kikvewdtvv eevlgadgkv tgvrlrnvht getkqldvtg
      241 vfvaighdpr selfrgqvev ddegyvkvqd pstrtsvpgv faagdlvdht yrqaitaagt
      301 gcaaaldaer fiatlqg
//
LOCUS       WP_120686537             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Butyrivibrio sp. XB500-5].
ACCESSION   WP_120686537
VERSION     WP_120686537.1
KEYWORDS    RefSeq.
SOURCE      Butyrivibrio sp. XB500-5
  ORGANISM  Butyrivibrio sp. XB500-5
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Butyrivibrio.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Butyrivibrio sp. XB500-5"
                     /db_xref="taxon:2364880"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33519
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydliiigsg paglsaavya kraglnmlii eknpvsggqi idtyevdnyl gipgvngfdl
       61 amkfrehadk lgaefadgtv tgiecvekgs dtkapvykik tdsgdyetht vilatgahhs
      121 klgipgeeey igkgvsycat cdgafyrgkv tavngggdva vedaiflsrf aekvylihrr
      181 delraakilq delfgiknie viwdsvvkei rgedkvnrll ienvnnkeek elsvdgifva
      241 igihpstdvf adivkcdeng yviagedgat ntpgifvagd srkkrlrqvv tavadgantv
      301 tsvqdflvgk aks
//
LOCUS       WP_120692796             389 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudarthrobacter phenanthrenivorans].
ACCESSION   WP_120692796
VERSION     WP_120692796.1
KEYWORDS    RefSeq.
SOURCE      Pseudarthrobacter phenanthrenivorans
  ORGANISM  Pseudarthrobacter phenanthrenivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Pseudarthrobacter.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Pseudarthrobacter phenanthrenivorans"
                     /db_xref="taxon:361575"
     Protein         1..389
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40086
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,286,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,276..277,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklgiprerr egerrvaatp etvkqlaalg veilleedag aaagypdiay sqagarlvpa
       61 ldlaqldvla hvrpldpdta qalkrgavtv glaspsselp tvqaladagv tafalelvpr
      121 israqsmdal ssqalvagyr cvleaairlp rffplymtaa gtvpparvlv lgagvaglqa
      181 igtakrlgar vfandirpas adevasmggt firldletae aaggyarqls sdagtrqrql
      241 laphvaqadv littaavpgr rapllvttem vqgmragsvv vdlaaesggn vesvvpgqdi
      301 pvptadgkgh vtlvglkdap samasdasrl yaknvanlla lmirdgalaa dfgdevltga
      361 clthggevrh qptaellaer astwregvl
//
LOCUS       WP_120692835             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudarthrobacter
            phenanthrenivorans].
ACCESSION   WP_120692835
VERSION     WP_120692835.1
KEYWORDS    RefSeq.
SOURCE      Pseudarthrobacter phenanthrenivorans
  ORGANISM  Pseudarthrobacter phenanthrenivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Pseudarthrobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudarthrobacter phenanthrenivorans"
                     /db_xref="taxon:361575"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33364
     Region          13..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtiaentase vrdviivgsg pagytaavyt aranlkplll agsvtaggel mnttevenyp
       61 gfpdgimgpd lmenfekqaa rfgteiqfed vtaldltgpv ktvtiatges fqaksvilst
      121 gsayrelglp nekrlsghgv swcatcdgff fkdqdiavig ggdsameeal fltkfaksvt
      181 vvhrrdslka skimadrala hekinfiwns tvedvlggek vtgltlrnli dgtvsnlavt
      241 gvfvaigndp rtdlvkdvld ltpegtiavq grssktsipg vfaagdvvdp tyrqaitasg
      301 sgcvaaidve hyladlpa
//
LOCUS       WP_120694695             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Moraxella catarrhalis].
ACCESSION   WP_120694695
VERSION     WP_120694695.1
KEYWORDS    RefSeq.
SOURCE      Moraxella catarrhalis
  ORGANISM  Moraxella catarrhalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Moraxella catarrhalis"
                     /db_xref="taxon:480"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33728
     Region          5..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqhhrliil gsgpagysaa vyaaranlnp viitglqvgg qlttttevdn wpgdahgltg
       61 nglmermksh aerfgtkliy dsitqvdlhn rpftlvgdkg vytcdaliia tgataqylgl
      121 eseqkfmgqg vsacatcdgf fyknqkvavv gggntaveea lylsniasev tlihrrdtlr
      181 aekilqdqlf ekvkdgniki ewnhkikevv gddmgvtgvm iestqdgsik qldimglfva
      241 ighkpntklf dgqlnmqdgy iivnsglngn atatningvf aagdvadhty rqaitsagtg
      301 cmaaldaeky ldslti
//
LOCUS       WP_120695552             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces radicis].
ACCESSION   WP_120695552
VERSION     WP_120695552.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces radicis
  ORGANISM  Streptomyces radicis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces radicis"
                     /db_xref="taxon:1750517"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33892
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytsa lytaraslnp lvfegavtag galmntteve nfpgfkegim
       61 gpdlmdnmra qaerfgaelv addivsvdls geiktvtdta gvvhqakavi vatgsqhrrl
      121 glpqedelsg rgvsycatcd gfffreqdia vigggdtame eatflsrfak tvtivhrrda
      181 lraskamqer afadpkirfv wdsevaeihg tdgklsgltl snrktgetsa lpvtglfvai
      241 ghdprvelfk gqldlddegy lqvaspttrt nvpgvfaagd vvdhtyrqai taagtgcaaa
      301 ldaerylaal sdaesiasdv sa
//
LOCUS       WP_120697397             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Moraxella catarrhalis].
ACCESSION   WP_120697397
VERSION     WP_120697397.1
KEYWORDS    RefSeq.
SOURCE      Moraxella catarrhalis
  ORGANISM  Moraxella catarrhalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Moraxella catarrhalis"
                     /db_xref="taxon:480"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33728
     Region          5..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqhhrliil gsgpagysaa vyaaranlnp viitglqvgg qlttttevdn wpgdahgltg
       61 nglmermksh aerfgtkliy dsitqvdlhn rpftlvgdkg vytcdaliia tgataqylgl
      121 eseqkfmgqg vsacatcdgf fyknqkvavv gggntaveea lylsniasev tlihrrdtlr
      181 aekilqeqlf ekvkdgniki ewnhqikevv gddmgvtgvm iestqdgsik qldimglfva
      241 ighkpntklf dgqlnmqdgy ivvnsglngn atatningvf aagdvadhty rqaitsagtg
      301 cmaaldaeky ldslti
//
LOCUS       WP_120701199             304 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptococcus].
ACCESSION   WP_120701199
VERSION     WP_120701199.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32680
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigag pagmtaalya arsnlkvall eagipggqmn ntsdienypg yanisgpela
       61 ekmfepleal gvehlfgrae nivdqgnyke ittddgllqa ktviiatgsn hrllgvpgee
      121 elnsrgvsyc avcdgaffrd edlmvvgggd saveeaiflt qfaksvtivh rrdalraqkv
      181 lqdrafanek ihfawntvve eikgdnrvts lvlkdvqtge vreqaaggvf iyvgldpvsd
      241 fakdlgildd qgwvitddhm ktsvpgvfav gdvrqkdlrq vttavgdgav agqeaykyit
      301 ehee
//
LOCUS       WP_120701629             306 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptococcus].
ACCESSION   WP_120701629
VERSION     WP_120701629.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     gene            1..306
                     /gene="trxB"
     Protein         1..306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32724
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiivgsg pagytagiyl sraglknrli tgyseggqlt tttlvenypg fengiegnkl
       61 vqtmrrqaeq fgtemtfgfv qkiegesspf kvhldngeii dtkaviiatg ssakylgieg
      121 eeeavgkgvs acatcdaffy kerevlvvgg gdvameealy ltrfaskvtv vhrrnelras
      181 dimvkraqan dkihwmlnyt pvkvtsnlmg mtgldvrnne tgdiehiqad glfvaighqp
      241 ntdfldgkla lddkgyiqtq agtaktsvag ifaagdvqdp kyqqaitaag sgaiaaldtl
      301 ayidnl
//
LOCUS       WP_120705448             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            jaguaris].
ACCESSION   WP_120705448
VERSION     WP_120705448.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium jaguaris
  ORGANISM  Rhizobium jaguaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rhizobium jaguaris"
                     /db_xref="taxon:1312183"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40336
     Region          5..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnlvfvake tvadetrvaa svetvkkmkg lgfdivveag agapsrirdg eyeaigarig
       61 svqdaaqadv ilkvrrptgd eiagyksgai viaimdpygn eaaladmara gltsfamelm
      121 pritraqsmd vlssqanlag yqavieaaav ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aqvsatdvrp aakeqvaslg akfvavedee fkaaetaggy akemskdyqa
      241 kqaalvaehi skqdivitta lipgrpaprl vsremlkamr sgavavdlav erggnvegve
      301 fgtvahvegv kvvgypnmag ripasasaly aknlvtflet mvdkntrslg lnradelika
      361 tmltdggevv hpnfvdpdqp tvnkgdl
//
LOCUS       WP_120706402             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhizobium jaguaris].
ACCESSION   WP_120706402
VERSION     WP_120706402.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium jaguaris
  ORGANISM  Rhizobium jaguaris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rhizobium jaguaris"
                     /db_xref="taxon:1312183"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34484
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtarhtkvli igsgpagyta avyaaramlk pvliagleqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlq qaqhvgaeiv ndlvtevdtn qrpfvartds gqvwtadtli iatgakakwl
      121 gieseqhfqg fgvsacatcd gffyrnkdvi vvgggnsave ealylsniak svtvvhrrds
      181 fraekilqer lfakpnvkvl wntevaeitg tpakppmpps vsgarlrdtr mgvvtdvtid
      241 gvfvaighap atelfkgklk lkdngylwta pdstatsvag iyaagdvtdd tfrqavtaag
      301 mgcmaaleae ryltghmpva vaae
//
LOCUS       WP_120710475            1006 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacterium
            marinum].
ACCESSION   WP_120710475
VERSION     WP_120710475.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacterium marinum
  ORGANISM  Ulvibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacterium.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Ulvibacterium marinum"
                     /db_xref="taxon:2419782"
     Protein         1..1006
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109225
     Region          24..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitllrslv magallcfgl sqaqevsgtv sdavgplpga svvvkgttng tqtdfdgnyt
       61 idgldddail vfsyigysnq eipvagqati dvvlqedaqa ldevvivgyg sqakkeitss
      121 vvsvstedfn qgvvqeptql lqgkvaglsv vnrggnpnqe pvirlrgist vggnqqplvv
      181 idgilggsln svdpadieni tvlkdgsaaa iygsrgsagv ivvttkrgka gqplrvsyng
      241 qlgvstianq ieimdrgefl avggndlgsd tdwrdevtqt giaqvhniaa sgggesfnyr
      301 vaanirdtdn ilinsgfqqf nfrtnftgll fddklkidvn aaftqrdsqi gfnealryat
      361 synptapvfg ddapfpfnsa qfggyfetlg lfdsfnpvai aelnrndrfa ttlnygvnln
      421 yrvtdnltvn lnyaaqnike daniyypttg ywrgnalspt rrgradfgnl errfrllegy
      481 aaytnsfadk fnftvtagys fqendfnyny fqigdfppgv dfdfsnnisa aqdlleagri
      541 eadsgredgd riirffgrvn mtfddaiyfd asisregssr fgtenqwgif pavgagadln
      601 kylelpnvnl lkvragwglt gaippavgly qqifnvqngv dgqsgaattq dngraanpdl
      661 kweeksefnf gvefamdrfg atadyfirdi rdfvtfanvd aaefngfsqr wqnsgqlgvt
      721 gfelsanydv irndkltynt gviftqnknt leenpqgdqv dgnlgspgqn ntnvirikeg
      781 eevgqiwgpv fsgnvdangt pilldingdg elvtgqgsal ddnadfrvlg tgipdfeigw
      841 tnqvtfgnwd anvffravvg hslvnsfraf yepiigsqas ynfvntklqr ddirtaqfsd
      901 yyvekadflr ldnmsigynf dlketsyikg lrlslaaqnl ftitgysgvd pepslqdggl
      961 pagellgddp tdqideiqan pliagierre ayftsttitl glnvnf
//
LOCUS       WP_120710930            1132 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacterium
            marinum].
ACCESSION   WP_120710930
VERSION     WP_120710930.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacterium marinum
  ORGANISM  Ulvibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacterium.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Ulvibacterium marinum"
                     /db_xref="taxon:2419782"
     Protein         1..1132
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123597
     Region          25..1093
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrknlsfla lffcsvftvy lygqqqvsgv vssddgellp gvsvvikgtt tgvssdfdgn
       61 ytinvpnaqs vlvfsylgme tqevvvggrp tinvtmitss ealdevvvta lgitrekksl
      121 gyavsevdgd aldnvpqena lnalsgkvsg vsinstggpg ssvnmvirga nsltgdnqpl
      181 fvidgtpifn tlnnvsgfgd rntvdfgnpi sdinpddian vsilkgasaa alygsragng
      241 vvlittksgk akkglgitvt sstvfdipfr yinshrrfas gdrpytednf psnafgalli
      301 negasawagp eldkginaiq wpysqqeies gvpvarelrs ysnpenffqt avtatqnisi
      361 enssenisyr lsvnnmdntg fvpntdlkrt gislnssvkl seqvtvssnl nyvkngsnnr
      421 pggdrgvnpi halyqlsphi dvrqmedywl dgfeglrqhs pysfgedptd isqnnpyfla
      481 nealnsfkrn rifgnikvdw ellpglnlmg rytydgynee retkissgyd raingtyglq
      541 nidqreinad fllsyrkayd nwdfsvsagg nirdaksans lignqnrtgl evpnlfrisn
      601 iapgnlryen eeshrkinsl ygvlnlgfan tlfidltarn dwsstlpegn nsffypsisa
      661 sllvnelvdl gpkvsllklr sgyaevgndt npyaitnvls nggywgsapt lsvpgtllnp
      721 sysaelsksw eagielaffq nrlradatyy sarntnqifn vdfpsstgys sqlinagets
      781 segfeaslgl tivdndvwnw dmsfifntnv skivdlpegt pfirlwndar ggayswegde
      841 igqivdarmv riedpnseyf gwpvidqggf essdrtlqda dgnrvadvig nfnpdfnagm
      901 ttsisyknft lsmnfdwrkg gqfvsqtyry nesdmrtqrw ldklvdlsgv ddvpgflran
      961 adqylspdgd fyvlvggpta emgglehteg gitlndgvfm pgvivdddgn iigenlggpg
     1021 tittryqdhy gwdftrnatf dadfvklrei sftyalpnky lksigftkas islfsrniil
     1081 wtaadigidp evafqpstgg vgdtgvlfkq gierynanpf aipvgvrlnf gf
//
LOCUS       WP_120710961            1134 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacterium
            marinum].
ACCESSION   WP_120710961
VERSION     WP_120710961.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacterium marinum
  ORGANISM  Ulvibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacterium.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1134)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Ulvibacterium marinum"
                     /db_xref="taxon:2419782"
     Protein         1..1134
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123647
     Region          37..1094
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdiilkrvke krsfkgfsls llfllfgigg llaqnlqvtg tvtaeedgmp lpgvtilvad
       61 snngettdfd gnysisvlan atlefsyigf etkyvavnnq ssinvalsvs aealdevvvt
      121 algikrsdks lgydvekvgs eeltrvaqen vlnslsgkvt gvtlnntggt gssvsmvirg
      181 aislssdnqp lfvidgvpve sslnnvggfg nrnrvdygna isdldpnsie dvtilkgasa
      241 aalygsragn gvvlittkka kkgqkmtinv vtntvfdipv rfldaqhqfg sgflsyspes
      301 qggsyilpda lpaggnggpe ldrgyyavqw napldangqp iptelvshpn nvenfvntgi
      361 tttnsitvsn ssdvlnyrlg vtnmantgii pnsdikrnsl slsvsselnk kltistninf
      421 vnsyadnrpa snrganplew aykvpanidi rdlrdydlpg tevlglgnas fnnpwflane
      481 innsfsryri ygnvglewkl spnfsirssy nlnyfnqtqe tkmapgyare anngtygiak
      541 tdgletnvdi latytkdfgn fdfsisgggn lmyqrqtgli nsafngagli apnlftvdni
      601 aagslnyssf lrerginsvf gtgtfgfmdm lyldvtarnd wsstlpvenr syfypsasvs
      661 flvselvdip kvdllklrag waqvgndtsp yrlgtffnng gqwgnsilfs gegtlntpdl
      721 epeqatslef gldlnmfnnr lrfegtyytv enknqiinvp lagssgfssv sinagilest
      781 gyelalgftp vrtenwdwdl ninytsnesk ileltegvdf iqfwsenrsv srgyaqnaat
      841 gedglvgniy srkilrvtde nspyfnypli epgegerlan teeyfkvgny npdfimglqs
      901 slrfknftln mtfdwrsggq ymsqtsrymv edgygqqlld nivnpgipdv gpemrqwvld
      961 radqlllaes fprvggtpgn gglpetlggq lvfdgvfvpg vvgeydadgn fvlisenlgd
     1021 egtfvmpfsi snpwtfgtph mfdadfiklr eislgydlps kftsrvgidk lsfavysrni
     1081 mlwtkdsafg vdperafeae tssgnrgtqf kqgierynve pwvipvgiri gitf
//
LOCUS       WP_120711000            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacterium
            marinum].
ACCESSION   WP_120711000
VERSION     WP_120711000.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacterium marinum
  ORGANISM  Ulvibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacterium.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Ulvibacterium marinum"
                     /db_xref="taxon:2419782"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113543
     Region          23..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtrklivflv lvlgayplla qnktvtgtvt dtsdgsplpg vnvlvqgttn gtqtdfdgny
       61 tievaegnvl vfsyigmraq sitvgssntv dvqmvvdenq ldevvvtalg lerqskslsy
      121 snqqveteel tkarainvte glsgkvaglt varsatgvgg gtrvllrgir sidgssqply
      181 vvdgillngd innippddiq eisilkgana aalygsraqn gaiiittksg kgaregvsat
      241 vgftsqmssp ihllefqney gqgaggtysp qattsygprf dgsqvahwsn dpnypdfggt
      301 ytyeaqpdnv edffrighei atnvgvnvns eksnvflgyt ftnaggiipg ndlnrhsitt
      361 rinsnitekl qvdaklnyir ddftnvltpg esydnpvryl yktprnirtq dfenfqfine
      421 egklrqhyfl pqfngggnpy wvannvkrpr ldervlglls lkyditddls ilarsaidrt
      481 srsedqlwyn dtytvaqfgr yqktasnqyd wntdvlinyn knitddfkid lnvganqrvf
      541 ernqirgngt nftienffal sntqnplate qfdkfevqsv yglaefsykn aiflnltarn
      601 dwsstlpedn rsyfypsvgl ttvvtdlvdl sssplsflkl ranwaevgnd tqsfrlsrra
      661 dirfgsldin ptqpnpdlrp etteslelgf darfldnrlr ldftyyktnt fdqifrtptp
      721 vgsgvseifq nggdiqnrgv evvlgasiid npdfswdldl nfatyktevl eiaegfdrlt
      781 itsdfirdyv lvageefgdt ysrgyqrddq drvivddtgl plitpgrnev kvanfnpdwt
      841 ggirnslryk nfnfsalidi rqggtvtsft eailardgvl dyttegrdgg lvfgdnffgg
      901 etavrqdgsp ntiavtaeqf wnrvggrntp vgeafvrdas nirlrelvig ytvpqsilsk
      961 tfftsanisl vgrnlffitn kaenfdpevl tsvtndptss nngeisgggr eafapptsrt
     1021 fgvslnfgf
//
LOCUS       WP_120711877             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Ulvibacterium marinum].
ACCESSION   WP_120711877
VERSION     WP_120711877.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacterium marinum
  ORGANISM  Ulvibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacterium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Ulvibacterium marinum"
                     /db_xref="taxon:2419782"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34287
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msekierlkt viigsgpagy taaiyaarad lkpvmytgme pggqltttte vdnfpgypeg
       61 idgptmmvql qqqaerfgte vrigmvtave lsdetggihk ltidsdkvie aetviistga
      121 sakylnlpse qrlrgggvsa cavcdgffyk gqdvaivggg dtaaeeasyl anicnkvtml
      181 irkdhmrask amqhrvnslk nidvryntei devlgdqvve glrmvnnqtg kkeeiaitgl
      241 fiaightpnt gifkgqldmd etgyiltkgk stktnkpgvf asgdaqdkey rqavtaagtg
      301 cmaaldaery latvetpeev v
//
LOCUS       WP_120711953            1137 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacterium
            marinum].
ACCESSION   WP_120711953
VERSION     WP_120711953.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacterium marinum
  ORGANISM  Ulvibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacterium.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Ulvibacterium marinum"
                     /db_xref="taxon:2419782"
     Protein         1..1137
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124541
     Region          54..117
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          140..1136
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkpntmewl skiipeldlk mkltfffliv alfqiqansg ysqntkisld ltqvtlaevf
       61 seiesktefr ffyknedvnl drkltlkirk erihvilnri fqngkvsyev fnkhivikka
      121 nnstssqvqv vplpesyqlq vngtisdsng tplpganive kgttngtqsd fdgnfslsvt
      181 dqnavlvvsy lgfttqevqv agqttiaiil qedagaleev vvvgfgtqkk inltgavevi
      241 dddalenrpv nnvsnllagq asgvtafsgg gqpgldesni sirgnttfgg snspliivdg
      301 vestlnnidp idiasisvlk dassaaiygv rggngviivt tkrgrsgalm vnyntslgfq
      361 eftetptftn sfdyatlrne alvndgnape ftdeqlqafq ngsapntdwl galltpngft
      421 qrhhlalsgg sdtfnysasl gyldteglip ntnyrrysfr lnldqkindr ltlgynvalt
      481 rrdieeprgg vgsiysknfr ehptepirns dgnfvafine hnsvaeaneg glqrtledkl
      541 lgsvsaefki leglnikgia avnqdyrnfn dfdkflqlyn vdgseaiglp srisvtesrr
      601 tninlqallt yektfgkhyi kallghnsiq ddfkltqtar tglpssnvsd elalgdpdta
      661 tntsdvelyr lesyfgrlny nfddrylfef tlrqdatsrf aeanrkevfp sfslgwnlan
      721 enfftieevn qlklrgswgq lgnqevivng avsnfayapt fragagyqag gqlqtsfreg
      781 lianpdlrwe titksnvgld aalfnnsfrf sfdyfsenrd dilavvplpg sfgasappsn
      841 vassiargie msfnyngsig ddfnysigyn mtnflkapti dalpetgevp grsvgdpinn
      901 ifgyealglf qneaeiasap dqtalggtpv pgdiryadtn grdengnltg qpdgiidpdd
      961 rtslgtftpk lfygfnfgad ykgldlslff qgvgrvqnsl idraahpfsn ggktlanhld
     1021 rwtpentnas yptlhsanag rnqvtssfft ynasylrlkn iqlgyslpes finkfglqkc
     1081 rvyvtadnll titnsefpdg fdpetlgnpd pdalnpgnng eiypqvktya iglnvtf
//
LOCUS       WP_120712437            1085 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Ulvibacterium
            marinum].
ACCESSION   WP_120712437
VERSION     WP_120712437.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacterium marinum
  ORGANISM  Ulvibacterium marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacterium.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Ulvibacterium marinum"
                     /db_xref="taxon:2419782"
     Protein         1..1085
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117558
     Region          27..1081
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngilt lflalivqls faqekavsgt vtdqdglplp gtsvvvkgtt tgtqtdfdgn
       61 ytlnteegav lvfsyigqrt qeitvgsant idvqmvedaq aleevvvtaq giqreerslg
      121 yavttvdeeq vssrpeadig rvlqgkvagv nitnnnglsg sgtniiirgf ssvtqsnqpl
      181 fvvdgipids gtntqtsfld gntessrfld idpntiasvs vlkglsatvl ygnrgrngvi
      241 littkgaatg eapsktevtv nqsvfvadai lpkyqdnygg gfhqgfgyff snwgprfdrt
      301 dddgisqarq fvgdgpggva ilqhphnfia dqtliagfed llddpypyqp yngveeffrt
      361 gfvtstsvnv rgggekasfn lnygrtedrg itpgntllrn nfnlggnarl snkltisgvf
      421 nfirtgfksp pnavstgsga afnggavfgd ilytprsvdl tnlpfqaadg rsvyyretnd
      481 iqnpywtvan vktsqdtdrf igntsltyei ndwmnltyrl gldtysefnf ygqnkggvdg
      541 pvigllrtns vrntiwnhdl ilsadkdlse nlnlkaiagl nsrrdeyeqd giesqgqlvf
      601 gvlehfnftt psaqnsltrs gnnpnlnqnf eqnlvgayld ltlgykdwlf lnavgrndws
      661 stlerennsi fypgasisfv ptsafegiqg nflnyaklrl gygssagfpd pfttrsvlgl
      721 tarslvdvng nvissnsvdn tlgnadlkpe riqefevgld trlfnrlnln vslfdkrttd
      781 litdrtldss tgftsttvni geiqaqgvev dfdlailkef esgiginiag nwttiettvt
      841 dladgtnnil ltdaiaqeaa nyavegrpfg vllgsdfvfd ddgnrlvnda grylfdptir
      901 eigdpnpdwq taliptitfk nftlsanlqy rhggdvysvt tsaligrgvv dddnpidrea
      961 nyilpgvkas dgtpndtais stelgfntyf ggninplsif dgstirlqea slgyslpskm
     1021 lektpfgslt ftlsgqnlwf kainfpdnvr ydtnssstgv gngqgidfft gpsvrrygft
     1081 vrasf
//
LOCUS       WP_120715043             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Moraxella catarrhalis].
ACCESSION   WP_120715043
VERSION     WP_120715043.1
KEYWORDS    RefSeq.
SOURCE      Moraxella catarrhalis
  ORGANISM  Moraxella catarrhalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Moraxella catarrhalis"
                     /db_xref="taxon:480"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33770
     Region          5..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqhhrliil gsgpagysaa vyaaranlnp viitglqvgg qlttttevdn wpgdahgltg
       61 nglmermkah aerfgtkliy dsitqvdlhn rpftlvgdkg vytcdaliia tgataqylgl
      121 eseqkfmgqg vsacatcdgf fyknqkvavv gggntaveea lylsniasev tlihrrdtlr
      181 aekilqdqlf ekvkdgniki ewnhqikevv gddmgvtevm iestqdgsik qldimglfva
      241 ighkpntklf dgqlnmqdgy ivvnsglngn atatningvf aagdvadhty rqaitsagtg
      301 cmaaldaeky ldslti
//
LOCUS       WP_120715914             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tsuneonella amylolytica].
ACCESSION   WP_120715914
VERSION     WP_120715914.1
KEYWORDS    RefSeq.
SOURCE      Tsuneonella amylolytica
  ORGANISM  Tsuneonella amylolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Tsuneonella.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Tsuneonella amylolytica"
                     /db_xref="taxon:2338327"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34604
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mathktklli igsgpaglsa aiygaramme pivvqglqpg gqltittdve nypgfkdviq
       61 gpwlmqemea qavhvgtrmm wdtivdidis ghpfratgdn gdvyegdtlv iatgaqakwl
      121 gvpgemelgg kgvsacatcd gffyrgkkva vigggntave ealyltnhsd dvtlihrrde
      181 lraerilqdr lfkhpkitvl wnkaverfag dplagglthl elrdtvtget sdfaadgafv
      241 aighapstel fkgklpiddg gylivepgtp ktavpgvfac gdvmdhtyrq avtaagtgcm
      301 aaldaerfva gldidleghv ekaeeaa
//
LOCUS       WP_120718854             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus chosunensis].
ACCESSION   WP_120718854
VERSION     WP_120718854.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus chosunensis
  ORGANISM  Streptococcus chosunensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus chosunensis"
                     /db_xref="taxon:2707003"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32973
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehiygyve nvedhgdfkt vltddqtyet rtvivatgsk hrplgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdraftnek isfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldplsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrlkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_120722433             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces hundungensis].
ACCESSION   WP_120722433
VERSION     WP_120722433.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces hundungensis
  ORGANISM  Streptomyces hundungensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces hundungensis"
                     /db_xref="taxon:1077946"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33715
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgim
       61 gpelmdnmrg qaerfgaelv pddvvavdlt gdiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedklsg rgvswcatcd gfffkdhdia vvgggdtame eatflsrfak svtivhrrds
      181 lraskamqer afsdekikfa wdsevaeihg dqklsgltlr ntktgetsel pvtglfiavg
      241 hdprtelfkg qldlddegyl kvdapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala dnekaaagv
//
LOCUS       WP_120730913             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora endolithica].
ACCESSION   WP_120730913
VERSION     WP_120730913.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora endolithica
  ORGANISM  Micromonospora endolithica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Micromonospora endolithica"
                     /db_xref="taxon:230091"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32698
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdrrpliii gsgpagytaa vyaaranlap lviegsqsgg almttteven fpgfpdgitg
       61 pelmdnlrkq adrfgaqfvt ddvtrveltg dvktvwvgeq ayparavila tgsawrplgv
      121 pgetellghg vsacatcdgf ffrdqdiavv gggdtameea tfltrfarsv tiihrrdtfr
      181 asrimadral sndkirvawn svveeilghd gavtgarlrd vhtgqtrdld vtgvfvaigh
      241 dprsdlfrgq vtldddgyvt vdapgtrtnl pgvfaagdlv dhtyrqaita agtgcaaald
      301 aerylasla
//
LOCUS       WP_120729109             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora endolithica].
ACCESSION   WP_120729109
VERSION     WP_120729109.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora endolithica
  ORGANISM  Micromonospora endolithica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora endolithica"
                     /db_xref="taxon:230091"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33707
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlrp lviegvqsgg almttteven fpgfadgilg
       61 pelmdnmrkq aerfgaeflt ddvtrvelkd tgetgsdavs tvwvgetayr akavilstgs
      121 awrplgvpge qeylghgvss catcdgfffr nqqivvvggg dsameeasfl trfaesvtii
      181 hrrdsfrask imadralgne kikvewnsvv eeilgddgkv sgvrirnvht gestvldvtg
      241 vfvaighdpr selfrgqvel ddegyvkvea pgtrtnipgv faagdvvdht yrqaitaagt
      301 gcaaaldaer fiatlqg
//
LOCUS       WP_120731164             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_120731164
VERSION     WP_120731164.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38735
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsty eaagatigsa
       61 sdafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet itrlaehgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_120736572             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nocardia yunnanensis].
ACCESSION   WP_120736572
VERSION     WP_120736572.1
KEYWORDS    RefSeq.
SOURCE      Nocardia yunnanensis
  ORGANISM  Nocardia yunnanensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Nocardia yunnanensis"
                     /db_xref="taxon:2382165"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34809
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpvrdlii vgsgpagyta avyaaraele pllfegtqfg galmttteve nfpgfrqgim
       61 gpdlmeemre qakrfgadir tedvdaldls gpvkkvtvgg evfeahavil amgsaarylh
      121 vpgeqellgr gvsacatcdg fffkgqdivv vgggdsamee atfltkfass vtivhrreef
      181 rasrimlera knndkirfll nsevigvhgd tavthltvrd trtgetsela atglfvaigh
      241 dprselvrgq vdldgegyve vkgqstytsl pgvfaagdlv dhtyrqaita agtgcraaid
      301 aerwlaeqgd ittntldhag apvevnn
//
LOCUS       WP_120737077             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Nocardia
            yunnanensis].
ACCESSION   WP_120737077
VERSION     WP_120737077.1
KEYWORDS    RefSeq.
SOURCE      Nocardia yunnanensis
  ORGANISM  Nocardia yunnanensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Nocardia yunnanensis"
                     /db_xref="taxon:2382165"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38839
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdttqsaqta aprgarvgvv retnpderrv alvpkiipal lkqgvevive agaglgalip
       61 deayteagat lgdpyaadvv vkvappndne iaklrsgqtl igflaprnad tkigalkdag
      121 vqafaveaip risraqvmda lssqanvagy kavllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rttgydvrpe vadqvrsvga qwldlgidaa geggyarels
      241 eeeraaqqva lenaikgfdv vvttalvpgr paprlvtaaa vegmkpgsvi vdlagetggn
      301 celtepgktv vrhgvtiasp lnlpatmpeh aselysknia allelmlkdg alapdfddqv
      361 ladscvtrek aetevka
//
LOCUS       WP_120739481             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Butyrivibrio sp. CB08].
ACCESSION   WP_120739481
VERSION     WP_120739481.1
KEYWORDS    RefSeq.
SOURCE      Butyrivibrio sp. CB08
  ORGANISM  Butyrivibrio sp. CB08
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Butyrivibrio.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Butyrivibrio sp. CB08"
                     /db_xref="taxon:2364879"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33149
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydliiigsg paglsaavya kraglnmlvi eknpvsggqi idtyevdnyl gipgvngfdl
       61 amkfrehadk lgaefadatv tsivckeegs dtkapvftvv tdageydtht vllatgahhs
      121 klgipgeeey igkgvsycat cdgafykgkv tavngggdva vedaiflarf cekvylihrr
      181 delratkvlq delfalpnve viwdsvvkei kgedkvttlk ienvkksees dlnvdgifva
      241 igihpstdlf asfvkcdegg yviagedgat svpgvfvagd srkkrlrqiv tavadganav
      301 tsvqdfmvgk sk
//
LOCUS       WP_120750262             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus ginsengarvi].
ACCESSION   WP_120750262
VERSION     WP_120750262.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus ginsengarvi
  ORGANISM  Paenibacillus ginsengarvi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus ginsengarvi"
                     /db_xref="taxon:400777"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33751
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myktivigtg pagltaaiyl aranlnplvi egpepggqlt tttevenfpg fpegimgpel
       61 mdnmrkqaek fgaqfrtgwv nevdmskrpf klkieggeel vaetliistg asakllgien
      121 ekdnigrgvs tcatcdgfff rnkkiivvgg gdsameeanf ltrfgsevri vhrrselras
      181 kimqdraken pkvvwslnkt plgviagekg vtglkvkdsd tgieevletd gifvaightp
      241 ntgflkgqln tdelgylvvn pgtsetnvpg vfacgdvqdh kyrqaitaag sgcmaaldce
      301 kfleghsvhd wsvsl
//
LOCUS       WP_120752456             726 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein, partial
            [Aquimarina sp. BL5].
ACCESSION   WP_120752456
VERSION     WP_120752456.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. BL5
  ORGANISM  Aquimarina sp. BL5
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Aquimarina sp. BL5"
                     /db_xref="taxon:1714860"
     Protein         1..>726
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
     Region          32..>726
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklnsrahfk khlvvflcli tfgvinaqsk aiqgkvtaeg iplpgasviv kgtsngastd
       61 fegnyqidan addiiiftyl gyitqevavk dqttinvnlv edaseleavv vigyqtqrkr
      121 evsgaissvk sevlerqavt nfsealqgqv agvniqaesg apgarinvqi rgtnsltgtg
      181 tagqdplggq inpndnalnp lfiidgvpfp eppsispnei esieilkdaa ttaiygvrag
      241 ngvviittkr akpgpikvnl stftsinrit ssvptlntrd yialnrqyve nngqsfesng
      301 vfvnnpnald ndtdwqdlil ndnaitynyn lrlaggsdks nfslvldhin qdgtlinsdf
      361 ertnlrlnnn fkkdrfslft svflsrddsd repwailyda ivspateagp driednnsvs
      421 gdpnqfnvlg nilrklqets krksnttsis lqfkyllakg lnakvnisgs rnssestffr
      481 pgfifldedt geiipgrera aisiltests lfeqgtiesi ldyktnignh nisllggvta
      541 eqrtfnttrt evqefrsntp iptidqaidt dvvtvqgnes pnrlfsvlgs lgydydgryl
      601 iranvrrdgs snfqpdfryk tfggvsvaws iaresffkns nalsfindlk lrasygevgn
      661 qnigsfrtsr lignnfnipi gndivngltq tdifnqdlqw etsitsnlgi dlslfksafn
      721 ltaeyy
//
LOCUS       WP_120754988             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_120754988
VERSION     WP_120754988.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34391
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfrdgim
       61 gpdlmdnmra qaerfgaeli pddvvavdls eeiktvtdsa gtvhrakavi vttgsqhrkl
      121 glpredelsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtvvhrrdt
      181 lraskamqer afadpkisfv wdseiaeihg egklsgltlr nvktgetsel pvtglfiaig
      241 hdprtelfkg qlelddegyl kvdapstrtn ltgvfaagdv vdhtyrqait aagtgcsaal
      301 daerflahls dsehvrepek ta
//
LOCUS       WP_120755242             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter baumannii].
ACCESSION   WP_120755242
VERSION     WP_120755242.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34813
     Region          8..326
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdpeglt
       61 gpvlmdrmqa haerfgtelv ydhinevdln vrpfvlkgdm deytcdalii atgataqylg
      121 leseqkdvhx gleseqkfmg qgvsacatcd gffyknqnvm vvgggntave ealylsniae
      181 hvtlvhrrds lrsekilqdh lfakekegki sivwnhevee vlgdntgvtg vrlkstkeds
      241 kqevqvqglf iaighkpnts mfegqlnlrd gyiqvqsgts gnatatsvag vfaagdvads
      301 iyrqaitsag sgcmaaldae kyldnl
//
LOCUS       WP_120760119             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter sp. P255].
ACCESSION   WP_120760119
VERSION     WP_120760119.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter sp. P255
  ORGANISM  Campylobacter sp. P255
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter sp. P255"
                     /db_xref="taxon:1979368"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33161
     Region          3..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldlaiiggg paglsaglya trgglknvvm fekgmpggqi tssseienyp gvaqvldgis
       61 fmapwneqcm rfglkhemvg veqvsrnddg sftikleggk seqakavivc tgstprragf
      121 kgedeffgkg vstcatcdgf fyknkevavl gggdtaleea lylanicskv ylihrrdefr
      181 aapstvekvk nnnkielitn avvdevcgdn mgvnkikigm kdgskreldv pgiftfvgln
      241 vrneilkqdn geflctmeeg gqvnvdlkmq tniaglfaag dlrkdapkqv icaagdgava
      301 alsalayies lh
//
LOCUS       WP_120762170             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Protaetiibacter intestinalis].
ACCESSION   WP_120762170
VERSION     WP_120762170.1
KEYWORDS    RefSeq.
SOURCE      Protaetiibacter intestinalis
  ORGANISM  Protaetiibacter intestinalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Protaetiibacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Protaetiibacter intestinalis"
                     /db_xref="taxon:2419774"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33513
     Region          4..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrhliiigsg pagytaaiya aranlnplvi assvefggel mkttevenfp gfpegimgpe
       61 lmvrmqqqae rfgaeivydd vtaldltgdv krvtlgdgsv heahaiiyat gsayrklglp
      121 deerlsgygv swcatcdgaf frqkkvavig ggdsaleeat fltrfadvvy lihrrdsfra
      181 saamqerafs dpkiqviwnn evkhvygdek vtgigivntv dgtettldvq gmfvaigadp
      241 rthlvhgqle lapegtiavq grssrtnipg vfaagdvidp sykqaataag sgvvaaldae
      301 hylaeiadaa kaaavpa
//
LOCUS       WP_120770015             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus gwangjuensis].
ACCESSION   WP_120770015
VERSION     WP_120770015.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus gwangjuensis
  ORGANISM  Streptococcus gwangjuensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus gwangjuensis"
                     /db_xref="taxon:1433513"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32941
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvgli egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehiygyve nvqdhgdfkk vitddqtyet rtvivatgsk hrplgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdrafanek vsfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldplsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrlkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_120761628             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Protaetiibacter intestinalis].
ACCESSION   WP_120761628
VERSION     WP_120761628.1
KEYWORDS    RefSeq.
SOURCE      Protaetiibacter intestinalis
  ORGANISM  Protaetiibacter intestinalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Protaetiibacter.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Protaetiibacter intestinalis"
                     /db_xref="taxon:2419774"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52443
     Region          3..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtrigivaep agenrvavsp attarivalg yevavergag tassfpdeay adagatvvdr
       61 aeawgadvvl aitaptpadi arlrpdatfv gllspalrpe lleqlaargv talaldavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvrsigge ylavvvpeeq qevssdgyak atsdaydrra
      241 relyseqaae vdvvittali pgraaprllt asdialmkpg svvvdmaagq ggnvegsvag
      301 ervvtangvi ilgytdlagr lpqqasqlyg tnllnlltll tpgkdgrltl dhddvvqrav
      361 tvtqggavtw pppavavsaa paaappapas aparrapnpr arlglaiagi talflvcvfa
      421 ppplpqhflv ltlsvvvgfy vigkvahalh tplmsvtnai sgiivvgamt qlgsasllvq
      481 llatvavlva sinifggfav trrmlamfrk gdak
//
LOCUS       WP_120771899             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lactococcus allomyrinae].
ACCESSION   WP_120771899
VERSION     WP_120771899.1
KEYWORDS    RefSeq.
SOURCE      Lactococcus allomyrinae
  ORGANISM  Lactococcus allomyrinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Lactococcus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Lactococcus allomyrinae"
                     /db_xref="taxon:2419773"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33638
     Region          6..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maenmydvii vgsgpagmta amytarsemk tlllergvpg gqmnntaeie nypgygtimg
       61 pelsmkmaep leglgvenay gfvtsiedyg nykkiitedd effaksliia tganhrklgv
      121 pgeeefgarg vsycavcdga ffrnqdilvv gggdsaveea lyltrfgqtv tiihrrdqlr
      181 aqeiiqqraf dnekvnfiwd svveeikgdd kkvqtvvykn vktgesteka fggvfiyvgl
      241 dpvaefaqsl gitdeagwvv tddhmktnvp gvfavgdvrq kdfrqittav gdgaqaaqea
      301 ykfvteldn
//
LOCUS       WP_120774373             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Microbacterium].
ACCESSION   WP_120774373
VERSION     WP_120774373.1
KEYWORDS    RefSeq.
SOURCE      unclassified Microbacterium
  ORGANISM  unclassified Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Microbacterium"
                     /db_xref="taxon:2609290"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34482
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqviiigsg pagftaaiya aranlkplli assvevggel mnttevenyp gfpdgiqgpe
       61 lmakfqeqae kfgtevlydd vtelevdgtv krvtlgsgav heahtliyat gsayrklnve
      121 geerlsgygv swcatcdgff frqktiavvg ggdsameeat fltrfadkvy vihrkdtlra
      181 skimqerafa nekiefvwns evaevlgada vtgvklrstv dgtltempld glfvaigndp
      241 rthlvhdklk ltsegtiwvd grtsvtsvpg vfaagdvidp syrqaitaag sgtvaaldae
      301 hfladledas vevpaaeaae ilta
//
LOCUS       WP_120776020             325 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Microbacterium].
ACCESSION   WP_120776020
VERSION     WP_120776020.1
KEYWORDS    RefSeq.
SOURCE      unclassified Microbacterium
  ORGANISM  unclassified Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="unclassified Microbacterium"
                     /db_xref="taxon:2609290"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34073
     Region          7..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msiqevelvi vgsgpagyta avyaaragla pivlagsvta ggalmtttev enfpgfvdgv
       61 qgpelmesmr aqaerfgari llddavsvdl dgpvkiietg agetfrsnav iltmgsayrk
      121 lgiadeerlt grgvswcatc dgfffheqei vvvgggdsam eealfltrfa skvtvvhrrg
      181 efraskimaq rvldhpkiev awnsevaglv gaekveavtl rntvtglkre lpatgvfvai
      241 ghdprselvt givdtdadgy vlvdhpstrt nlagvfaagd lvdhtyrqai taagtgcgaa
      301 qdaqhylagl detasiptmt eevfa
//
LOCUS       WP_120782865             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora costi].
ACCESSION   WP_120782865
VERSION     WP_120782865.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora costi
  ORGANISM  Micromonospora costi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora costi"
                     /db_xref="taxon:1530042"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33636
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlkp liiegvqsgg almttteven fpgfadgilg
       61 pelmdnmrkq aerfgaeflt ddvtrvelvd tgdagthats tvwvgetayr aravilatgs
      121 awrplgvpge qeylghgvss catcdgfffr nqhivvvggg dsameeasfl trfadsvtiv
      181 hrrdsfrask imadralnnd kikvewntvv eeilgadgkv sgvrlrnvht getkvldvtg
      241 vfvaighdpr selfrgqvdl dgegyvkvea pstrtsvpgv faagdlvdht yrqaitaagt
      301 gcaaaldaer fiatiqg
//
LOCUS       WP_120784628             307 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Apilactobacillus bombintestini].
ACCESSION   WP_120784628
VERSION     WP_120784628.1
KEYWORDS    RefSeq.
SOURCE      Apilactobacillus bombintestini
  ORGANISM  Apilactobacillus bombintestini
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Apilactobacillus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Apilactobacillus bombintestini"
                     /db_xref="taxon:2419772"
     gene            1..307
                     /gene="trxB"
     Protein         1..307
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33109
     Region          5..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mmekydvivi gagpggmtaa lyasranlsv lmidrgiygg qmnntaeien ypgfksilgp
       61 dlakkmyess tnfgakyayg tvesvedkgn tkivktdqds yetssviigt gsqyrklgvp
      121 geeeysgkgv sycavcdgaf fknrevvvvg ggdsaiseal ylagivakvt vihrrdqlra
      181 qkvlqdrafa ndkidfvwnt nvteimgdnm kvtgvktvnn etneektida ngvfvyvgnn
      241 pvtdvfsnln itdekgwikt ndrmetsvkg ifaigdvrvk elrqvstavg dggiagqnaf
      301 eyvsslk
//
LOCUS       WP_120789067             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gryllotalpicola protaetiae].
ACCESSION   WP_120789067
VERSION     WP_120789067.1
KEYWORDS    RefSeq.
SOURCE      Gryllotalpicola protaetiae
  ORGANISM  Gryllotalpicola protaetiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Gryllotalpicola.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Gryllotalpicola protaetiae"
                     /db_xref="taxon:2419771"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34808
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mndltengvr dviiigsgpa gytsaiyaar aelkplvias sveaggeltk ttevenfpgf
       61 pegvmgpdlm ikmqeqaerf gaevvyddvv avelagetkr vvlgsgethe artvivatgs
      121 ayrrlgldde erlsghgvsw catcdgfffr qkniavvggg dsameeatfl trfadkvtvi
      181 hrkdtlrask imqerafane kiefawnkev vaisgseavt gvtlrdtvdg teselaldgl
      241 fiaigndprv hlfhgqlklt pagtiavdgr ssrtnlpgvf aagdvidpty rqavtaaasg
      301 tvaaldaehy laeldqaeas vdavfapan
//
LOCUS       WP_120786609             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Macrococcoides caseolyticum].
ACCESSION   WP_120786609
VERSION     WP_120786609.1
KEYWORDS    RefSeq.
SOURCE      Macrococcoides caseolyticum
  ORGANISM  Macrococcoides caseolyticum
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Macrococcoides.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Macrococcoides caseolyticum"
                     /db_xref="taxon:69966"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33411
     Region          7..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseikeydvi ivgagpagmt aavyasranl stimiergmp ggqmantadv enfpgfdlit
       61 gpdlstkmfs haqkfgaeyt ygdiknitve gddkivdlgd kqlkakavii atgaeykkig
      121 vpgeselggr gvsycavcdg affkqknlvv igggdsavee gvyltkyadk vtivhrrdtl
      181 raqkilqera fkndkidfiw nstlksinek dgkvgsvtli dnegketdfe tdgvfiyigm
      241 qpltkpfqhl gitdevgyim tneemetnip gifaagdvrq kklrqivtat gdgsiaaqna
      301 qhyieslnd
//
LOCUS       WP_120793030             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium paragordonae].
ACCESSION   WP_120793030
VERSION     WP_120793030.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium paragordonae
  ORGANISM  Mycobacterium paragordonae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Mycobacterium paragordonae"
                     /db_xref="taxon:1389713"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53065
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl sgetrvaatp qtvgqliklg ysvvveseag aaasfldsay deagadigsp
       61 eqawtadivl kvnapnddei aalrdgatlv slispglhpe lveklttrki tvlamdavpr
      121 israqsldvl ssmaniagyr avieaahafg rfftgqvtaa gkvppakvlv vgagvaglsa
      181 igaagslgai vratdprpev adqvkslgge yisvddseae vsatgyakem sedykareaq
      241 lyaeqcqdvd iiittalipg kpapriitad mvagmtpgsv ivdmaasngg nvegtvkdql
      301 vvtdndvtii gytdlagrlp aqssqlygtn lvnllklmtp ekdgqlvlnf ddvvqrsmtv
      361 vrdgestwpp ppvqvsaapa vpaaaapvke shakqpmsnk rrltttliaa avlfgliais
      421 paalqvhltv falaivigyy vighvhhalh tplmsvtnai sgiivlgall qigkenlpit
      481 vvscaailla sinifggfav trrmlamfsr s
//
LOCUS       WP_120795674             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thiocapsa rosea].
ACCESSION   WP_120795674
VERSION     WP_120795674.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa rosea
  ORGANISM  Thiocapsa rosea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Thiocapsa rosea"
                     /db_xref="taxon:69360"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34065
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msetkhcrll ilgsgpagyt aavyaaranl spvlvtgleq ggqlmtttdv dnwagdpdgv
       61 qgpelmermr rhaerfetei ifdhvnavdl gtrpfkltgd savyscdali iatgasamyl
      121 glpseeafrg rgvsacatcd gffyrnqkva vigggntave ealylsnias evilvhrrda
      181 lraekilqkh lfekaehgnv kiawnhtlee ilgdatgvtg mrikstldda tqdidlqgvf
      241 iaighkpntq ifdgqlemag gyikvnsgid gnatatsvpg vfaagdvmdh vyrqaitsag
      301 tgcmaaldae kyldalaaad k
//
LOCUS       WP_120796212             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Thiocapsa
            rosea].
ACCESSION   WP_120796212
VERSION     WP_120796212.1
KEYWORDS    RefSeq.
SOURCE      Thiocapsa rosea
  ORGANISM  Thiocapsa rosea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Thiocapsa.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Thiocapsa rosea"
                     /db_xref="taxon:69360"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37993
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipleta sgetrvasip evvkkligkg fevmveagag aragypdddy aaagaqltdr
       61 agafdvdlll kvrrpdtadv ealrpgglyi gllescgdde ilsamlakgm rvlgmermpr
      121 tsraqsmdal ssqsniagyr atleaaaryg rflpmmmtsa gsakparliv lgvgvaglqa
      181 iatarrlgad vyaydvrpet qeqirslgak pieldlgesg ageggyakel seeakakqqa
      241 alsdqlakah iiittalipc rpapvlvted vvkrmrpgsv ivdlaaangg ncpltvagei
      301 verhgvtivg ltnfpalvpa dasafyarnl anlieimvap sesgpvikdl aedditaaml
      361 vkpaa
//
LOCUS       WP_120800909             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120800909
VERSION     WP_120800909.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33379
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed dsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120801956             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120801956
VERSION     WP_120801956.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33275
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnektelvv pglfifvgyd
      241 vnnavlkqed nsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120803842             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120803842
VERSION     WP_120803842.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33365
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdiqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120808664             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120808664
VERSION     WP_120808664.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33436
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yrnkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120812254             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120812254
VERSION     WP_120812254.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33396
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy aveeikgdaf gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120812706             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vogesella
            indigofera].
ACCESSION   WP_120812706
VERSION     WP_120812706.1
KEYWORDS    RefSeq.
SOURCE      Vogesella indigofera
  ORGANISM  Vogesella indigofera
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae; Vogesella.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Vogesella indigofera"
                     /db_xref="taxon:45465"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40031
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqiaiaterl agelrvaatp etvkklvamg htvvieagag rhaaapdaay seagatltas
       61 raaalgqgdi vltvrplpad aiaelkdgav ligqlapyhn dtfpllaakq vsafamellp
      121 rttraqsmdv lssqnniagy ravllathyy prfmpmlmta agtvkparvl imgvgvaglq
      181 aiatakrlga vveatdvras tkeqveslgg kfievpmsee ekkandgvya kemsddykqr
      241 qaelvakhar qadiiittal ipgkkaptll saevvqamkp gsviidlaae aggncaqtvp
      301 gevittdngv tvvgltnlpg mvaadassly aknlftflgl mlskegftln leddllaatl
      361 vthagevrfp aanvanpakk etshg
//
LOCUS       WP_120813309             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120813309
VERSION     WP_120813309.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33381
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdts gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120814136             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120814136
VERSION     WP_120814136.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33279
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsvvvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120815701             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120815701
VERSION     WP_120815701.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33411
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkstvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvisaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120818107             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120818107
VERSION     WP_120818107.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33407
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmn tniqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120819083             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120819083
VERSION     WP_120819083.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33307
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120822416             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120822416
VERSION     WP_120822416.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33336
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsvvvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120823940             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120823940
VERSION     WP_120823940.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33379
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgnas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120827226             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120827226
VERSION     WP_120827226.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33410
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn nnkiefltpy vveeikgdaf gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120828493             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120828493
VERSION     WP_120828493.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33407
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdts gvsslniknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120828691             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120828691
VERSION     WP_120828691.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33272
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy lveeikgdas gvsslsiknt atnkktelvv pglfifvgyd
      241 vnnavlkqed nsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120830708             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120830708
VERSION     WP_120830708.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33394
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsvvvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120831767             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120831767
VERSION     WP_120831767.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33350
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvvlaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120832040             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120832040
VERSION     WP_120832040.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33351
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdvs gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120833627             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120833627
VERSION     WP_120833627.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33380
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehaks ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120836086             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120836086
VERSION     WP_120836086.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33363
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkieflipy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120838208             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120838208
VERSION     WP_120838208.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33407
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnkkrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120841100             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120841100
VERSION     WP_120841100.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33386
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh q
//
LOCUS       WP_120841206             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120841206
VERSION     WP_120841206.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33438
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsvvvdfsmk tdvqglfaag dirifapkqv vcaasdgtta
      301 alsvisyleh h
//
LOCUS       WP_120844226             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120844226
VERSION     WP_120844226.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33334
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120844476             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120844476
VERSION     WP_120844476.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33336
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlghakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120846123             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120846123
VERSION     WP_120846123.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33342
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi igsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemva vqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeti ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnihglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120847078             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120847078
VERSION     WP_120847078.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33336
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknail fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120848734             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120848734
VERSION     WP_120848734.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33322
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrngfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120849631             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120849631
VERSION     WP_120849631.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33396
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksmiiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120847726             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120847726
VERSION     WP_120847726.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33363
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apialehakn ndkiefltpy vveeikgdas gvsslsvknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120851912             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120851912
VERSION     WP_120851912.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33321
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atdekreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120856056             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120856056
VERSION     WP_120856056.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33321
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgki feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsvvvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120857048             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120857048
VERSION     WP_120857048.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33319
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvl pglfifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120860521             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120860521
VERSION     WP_120860521.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33286
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt vtnkktelvv pglfifvgyd
      241 vnnavlkqed nsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120859179             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120859179
VERSION     WP_120859179.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33320
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120867411             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120867411
VERSION     WP_120867411.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33307
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120868756             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120868756
VERSION     WP_120868756.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33480
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskrdsh fvilaeddkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn nnkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120871976             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120871976
VERSION     WP_120871976.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33323
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120872176             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120872176
VERSION     WP_120872176.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33378
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnveglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120877573             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120877573
VERSION     WP_120877573.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33312
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeti ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnsavlkqed gsmlckcdey gsvvvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120876955             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120876955
VERSION     WP_120876955.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33334
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gstlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120879861             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120879861
VERSION     WP_120879861.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33394
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdts gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120881583             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120881583
VERSION     WP_120881583.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33408
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt fearsviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120881971             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120881971
VERSION     WP_120881971.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33384
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed dsmlckcdey gsivvdfsmk tsvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120887781             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120887781
VERSION     WP_120887781.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33422
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120884921             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120884921
VERSION     WP_120884921.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33306
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120889175             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120889175
VERSION     WP_120889175.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33320
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120890225             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120890225
VERSION     WP_120890225.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33354
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed ssmlckcdey gsivvdfsmk tnveglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120892008             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120892008
VERSION     WP_120892008.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33360
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgififvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120893212             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120893212
VERSION     WP_120893212.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33340
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmlggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120894873             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120894873
VERSION     WP_120894873.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33381
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dvrifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120897341             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120897341
VERSION     WP_120897341.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33408
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaeegkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120897184             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120897184
VERSION     WP_120897184.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33397
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsiivdfsmk tnvqglfaag dirifapkqv vcaasdgtta
      301 alsvisyleh h
//
LOCUS       WP_120898921             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120898921
VERSION     WP_120898921.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33318
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkhtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeav ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120899955             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120899955
VERSION     WP_120899955.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33408
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsvvvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120901017             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120901017
VERSION     WP_120901017.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33351
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnveglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120903491             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120903491
VERSION     WP_120903491.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33392
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdaf gvsslsiknt atnkktelvv pglfifvgyd
      241 vnnavlkqed nsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120904057             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120904057
VERSION     WP_120904057.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33393
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn nnkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120902495             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120902495
VERSION     WP_120902495.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33380
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv ttcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120905417             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120905417
VERSION     WP_120905417.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33394
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknail fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn nnkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120910198             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120910198
VERSION     WP_120910198.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33264
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vvgeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgtta
      301 alsvisyleh h
//
LOCUS       WP_120908470             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120908470
VERSION     WP_120908470.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33364
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120910663             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120910663
VERSION     WP_120910663.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33365
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120911796             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120911796
VERSION     WP_120911796.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33336
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffvfvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120914519             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120914519
VERSION     WP_120914519.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33351
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff ykskevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120912963             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120912963
VERSION     WP_120912963.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33351
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120915580             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120915580
VERSION     WP_120915580.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33323
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnveglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120919329             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120919329
VERSION     WP_120919329.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33292
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa vqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn nnkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120917804             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120917804
VERSION     WP_120917804.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33353
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeti ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120921555             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120921555
VERSION     WP_120921555.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33287
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pglfifvgyd
      241 vnnavlkqed nsmlcecdey gsivvdfsmk tsvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120922534             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120922534
VERSION     WP_120922534.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33302
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt vtnkktelvv lglfifvgyd
      241 vnnavlkqed nsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120923141             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120923141
VERSION     WP_120923141.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33382
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed dsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120925483             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120925483
VERSION     WP_120925483.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33411
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tssseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed dsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120926589             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120926589
VERSION     WP_120926589.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33349
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnekreliv pgffifvgyd
      241 vnnavlkqed gsmlcecdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120926753             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120926753
VERSION     WP_120926753.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33364
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffvfvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tniqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120931913             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120931913
VERSION     WP_120931913.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33338
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnktrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120934908             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120934908
VERSION     WP_120934908.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33307
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsvknt atnekreliv pgffifvgyd
      241 vnnavlkqed gsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120936380             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120936380
VERSION     WP_120936380.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33395
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120937342             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120937342
VERSION     WP_120937342.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33224
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvsqkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnsavlkqed gsmlckcdey gsvvvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120942785             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120942785
VERSION     WP_120942785.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33327
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknagl fekgmpggqi tgsseiekyp gvkevvsgld
       61 fmqpwqeqcf rfglkpemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120941163             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120941163
VERSION     WP_120941163.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33422
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaeddkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120945526             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter labacensis].
ACCESSION   WP_120945526
VERSION     WP_120945526.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter labacensis
  ORGANISM  Helicobacter labacensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Helicobacter labacensis"
                     /db_xref="taxon:2316079"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33516
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midlgiiggg paglsaglya trgglkevvl fekgmpggqi vqsseienyp gvkeilsgmd
       61 fmqpwqeqcf rfglrhemas vvrlgwqgkf ytiqledgrs vearsvilst ggrpkkagik
      121 geeefwgrgv stcatcdgff yknkevavlg ggdtaleeai ylskmcskvy lihrrthfra
      181 apitiehakq nskiefltpa lveeiqgdas gvgalvikht esgalqtlqv paififvgye
      241 vnneilkqed grmlcacdey gsvmvdlsmr tnlkglfaag dvrsqapkqv vcaagdgata
      301 alsaiaylda hp
//
LOCUS       WP_120945573             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120945573
VERSION     WP_120945573.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33323
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120946836             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120946836
VERSION     WP_120946836.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33438
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeti ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120948474             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter mehlei].
ACCESSION   WP_120948474
VERSION     WP_120948474.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter mehlei
  ORGANISM  Helicobacter mehlei
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Helicobacter mehlei"
                     /db_xref="taxon:2316080"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33229
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midlaivggg paglsaglya trggvkdvil fekgmpggqi ttsseienyp gikevlsgid
       61 fmqpwqeqcf rfglkqemva vskistqdkh ylihtddgkv tparsvilat ggrpkragik
      121 geneffgkgv stcatcdgff yknkevavlg ggdtaleeal fltkmcskvy lihrrdgfra
      181 apvtieharn npkiefitpa vveeikgdgn gvnavvlknt qtgtiqelvv pvifvfvgyd
      241 vnnevlkqed gsmlcacdsy gsvlvdlnmk tnlpgffaag dirtnapkqv vcaagdgata
      301 alsciaylds hh
//
LOCUS       WP_120949192             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120949192
VERSION     WP_120949192.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33349
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvnfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120950184             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arthrobacter oryzae].
ACCESSION   WP_120950184
VERSION     WP_120950184.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter oryzae
  ORGANISM  Arthrobacter oryzae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Arthrobacter oryzae"
                     /db_xref="taxon:409290"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33948
     Region          5..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteqliiigs gpagytaaiy aaraglaplv iagavtagga lmnttevenf pgfpagiqgp
       61 elmdglqqqa ekfgarvvfd dvtdvtlagh lkrvvtggge theapavila tgsaykelgl
      121 peekrfsghg vswcatcdgf ffrdqdiivv gggdsameea tfltrfgksv tvvvrknelr
      181 asrimaqrak dnpkirfawn saitkihges kvtgvtltdt rtgdtrelaa tgifvaighv
      241 prtellhgqv eldaegyikv dspttvtnlt gvfacgdavd hryrqaitaa gtgcaaalda
      301 erylaaleda dsiatalvee pths
//
LOCUS       WP_120951231             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter sp. L8].
ACCESSION   WP_120951231
VERSION     WP_120951231.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter sp. L8
  ORGANISM  Helicobacter sp. L8
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Helicobacter sp. L8"
                     /db_xref="taxon:2316078"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33530
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midlgiiggg paglsaglya trgglkevvl fekgmpggqi vqsseienyp gvkeilsgmd
       61 fmqpwqeqcf rfglrhemas vvrlgwqgkf ytiqledgrs vearsvilst ggrpkkagik
      121 geeefwgrgv stcatcdgff yknkevavlg ggdtaleeai ylskmcskvy lihrrthfra
      181 apitiehakq nskiefltpa lveeirgdas gvgalvikht dsgalqtlqv paififvgye
      241 vnneilkqed grmlcacdey gsvmvdlsmr tnlkglfaag dvrsqapkqv vcaagdgata
      301 alsaiaylda hp
//
LOCUS       WP_120953307             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arthrobacter oryzae].
ACCESSION   WP_120953307
VERSION     WP_120953307.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter oryzae
  ORGANISM  Arthrobacter oryzae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Arthrobacter oryzae"
                     /db_xref="taxon:409290"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33600
     Region          13..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msnaentase vrdviivgsg pagytaavyt aranlkplll agsvtaggel mnttdvenyp
       61 gfpdgimgpd lmenfekqaa rfgteiqfed vteldldgdi ktvtigtget fkarsiilst
      121 gsayrelglp nekrlsghgv swcatcdgff fkdqdiavig ggdsameeal fltkfaksvt
      181 vvhrrdalra skimadrals hekisfvwnt gvedvlgqdk vtglqlknll dgtetqlavt
      241 gvfvaigndp rtdlvkdkle ltaegtiavd grtsktsiag vfaagdvidp tyrqaitasg
      301 sgcvaaldve hyladiha
//
LOCUS       WP_120953189             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120953189
VERSION     WP_120953189.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33383
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gmsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnveglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120953997             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter oryzae].
ACCESSION   WP_120953997
VERSION     WP_120953997.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter oryzae
  ORGANISM  Arthrobacter oryzae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Arthrobacter oryzae"
                     /db_xref="taxon:409290"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38286
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqvgvgreqr agerrvaatp dtvlqltalg lnllvesgag teagfadaaf keagatvisd
       61 lpfealdvll hvrpltpqat arlrpgtvti glaspgselp tvralaaggi tsfalellpr
      121 israqsmdal ssqslvsgyr avleaavryp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandiraas adevasmggt finldlaaae egtggyaral gedraarqrs
      241 llaphvaaad vlittaaipg raapllvttd mvtgmragsv vvdlaaesgg nvegviagqd
      301 ilvpvdggsv tlvglqdaas ampsdasrlf arnvsnflal itregtvapd fdddvvagtc
      361 lthggavrha ptaaalggea
//
LOCUS       WP_120958254             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120958254
VERSION     WP_120958254.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33364
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy iveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120962540             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120962540
VERSION     WP_120962540.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33384
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdts gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed ssmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120965792             540 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Comamonas
            sp. lk].
ACCESSION   WP_120965792
VERSION     WP_120965792.1
KEYWORDS    RefSeq.
SOURCE      Comamonas sp. lk
  ORGANISM  Comamonas sp. lk
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Comamonas.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Comamonas sp. lk"
                     /db_xref="taxon:2201272"
     Protein         1..540
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56363
     Region          16..540
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mstnpsqtss gagtqrigvp retfplekrv atvpdvvekl iklgfsvsvq agagdaancs
       61 deayraagae vlpdaaaiwa scdiifkvrp ptqeevaqmr egqvlidfiw paqnpelmqq
      121 laakkvtvla idslprtlsr aqkmdaltsm agvsgyravi eaanafgryf ngqitaagkv
      181 qpakvfiaga gvaglsaigt aaslgaivra ndtraevadq vtslggefvk vdyeeegsgg
      241 ggyakvmseg fqaaqramya qqakevdiii ttalipgkpa pklitaemvq smkpgsvivd
      301 maaeqggnce ltvpgeavvr hdvtivgytd lasrlakqss tlyatnllrl teelckakdg
      361 valvnmedda irgltvvkng eitwpappla qvakpaakpa eapvvqkksg hghgasgplp
      421 aktlaiifav aalafwfiga yapaaflghf tvfvlacfig ymvvwnvtpa lhtplmsvtn
      481 aissiiaiga lvqiappdga aggrpdelir wlafaavvlt avnmfggfav trrmlamfqk
//
LOCUS       WP_120977836             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Cohnella endophytica].
ACCESSION   WP_120977836
VERSION     WP_120977836.1
KEYWORDS    RefSeq.
SOURCE      Cohnella endophytica
  ORGANISM  Cohnella endophytica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Cohnella endophytica"
                     /db_xref="taxon:2419778"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33362
     Region          5..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrktiiigtg pagltaaiyl aranlnplvi egpepggqlt tttevenfpg fpdgimgpdl
       61 manmrkqaer fgaefltgwv nkvdtskrpf tltvegkgel taetliistg asakylgipg
      121 erdnvgrgvs tcatcdgfff rnkkiivvgg gdsameeahf ltkfasevvl vnrrnelras
      181 kimqdrarsn pkiswnlnrt plevvsgplg vtglkvlnne tgleetiatd glfvaightp
      241 ntrfldgqld tdetgyllvt pgttetnvpg ifacgdvqdn kyrqaisaag tgcmaaldce
      301 ryleevhtpv hv
//
LOCUS       WP_120978487             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Cohnella endophytica].
ACCESSION   WP_120978487
VERSION     WP_120978487.1
KEYWORDS    RefSeq.
SOURCE      Cohnella endophytica
  ORGANISM  Cohnella endophytica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Cohnella endophytica"
                     /db_xref="taxon:2419778"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33833
     Region          2..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhktivigtg pagltaaiyl aranlsplvi egpepggqlt tttevenfpg fpegimgpdl
       61 manmrkqaer fgaefrtgwi nnvdmskrpf tlsleggetl qaetliistg asakymgipg
      121 erdnvgrgvs tcatcdgfff rgkkiivvgg gdsameeanf ltrfasevtl vhrrdemras
      181 kimqdraren nkilwglnkt pievvagdng vtglkvrnnv tgeeeildtq glfvaightp
      241 ntkfldnqie tdelgyikvk pgttetnvpg vfacgdvqdh kyrqaitaag sgcmaaldce
      301 kflegsathd wsqsl
//
LOCUS       WP_120980624             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120980624
VERSION     WP_120980624.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33409
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120987763             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120987763
VERSION     WP_120987763.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33409
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed dsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120983111             539 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Corynebacterium xerosis].
ACCESSION   WP_120983111
VERSION     WP_120983111.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium xerosis
  ORGANISM  Corynebacterium xerosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Corynebacterium xerosis"
                     /db_xref="taxon:1725"
     Protein         1..539
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55407
     Region          1..536
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipiepd arqplvaatp dtvakliklg ydvdvqagag dhaaypddly vaagarlvge
       61 dvwradiitt ldtppreyrn lmkpgamlvs rlapgrnpel vddlasshft alamdavprl
      121 sraqsmdvls smaniagyra vveaansfgr lftgqvtaag kvppatvyvi gagvgglaai
      181 gtanamgaiv katdlrpeag eqvesmgaef ipipvaseks tdgyakemtd dqataaakly
      241 aeqsaaadiv ittanipgrq sprlltaddv ramrpgsviv dmaaanggnc eltvpgeviv
      301 tdngvtiigh tdlagrlpgq asqlygqniv nlfklitpdk dgtpildldd eivrgitvtl
      361 ngassskggd tgnveaettg aatdtrilwp pppvqvsatp aaaaqeklaa aataeapekv
      421 sfmggskaki glglaialga avilaspasv svnymvltla ivlgfyvisa vtprlhtplm
      481 setnaisgiv lvgailvvss tnvivsslaf laivlssini fggftitdrm lgmfrkeea
//
LOCUS       WP_120987814             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aliarcobacter cryaerophilus].
ACCESSION   WP_120987814
VERSION     WP_120987814.1
KEYWORDS    RefSeq.
SOURCE      Aliarcobacter cryaerophilus (Arcobacter cryaerophilus)
  ORGANISM  Aliarcobacter cryaerophilus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Aliarcobacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Aliarcobacter cryaerophilus"
                     /db_xref="taxon:28198"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32834
     Region          3..292
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldlaiiggg pagltaglya trgglanvvm femgmpggqi tgsseienyp gqgsvmtgmd
       61 lmaswpeqcq kfglkhemaq vetitkngdt fkiltndnre feakavlmat gsvprragfk
      121 gedeffgrgv stcatcdgff yrgkevavig ggdsaleeay ylskmckkvy lvhrrdtyra
      181 apstiahikn aenieevtnv sveevygdns gvlglkvkcn ktgeirdlpt pgvfvfvgrn
      241 vlnaplkqad gsflcdvies gevvvdlkmr tttkglwaag diridaakqv vcaaadgata
      301 avdiieylg
//
LOCUS       WP_120992328             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120992328
VERSION     WP_120992328.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33322
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn nnkiefltpy vveeikgdas gvsslsiknt atneareliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120995318             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Stutzerimonas urumqiensis].
ACCESSION   WP_120995318
VERSION     WP_120995318.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas urumqiensis
  ORGANISM  Stutzerimonas urumqiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Stutzerimonas urumqiensis"
                     /db_xref="taxon:638269"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33645
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdpegl
       61 tgpvlmermq qhaerfdtqi ihdhihtael rskpltlhgd ngtytcdali iatgasaqyl
      121 glpsedafag rgvsacatcd gffyrnqvva vvgggntave ealylsniar evhlihrrdk
      181 lrsekilqdk ileksrsgni rlhwnhtlee vlgdssgvtg lrlrsttdgn ekrldvsgvf
      241 iaighkpntd lfvgqldmrd gyllvrggsn gdatatnipg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylde
//
LOCUS       WP_120995838             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Stutzerimonas urumqiensis].
ACCESSION   WP_120995838
VERSION     WP_120995838.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas urumqiensis
  ORGANISM  Stutzerimonas urumqiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Stutzerimonas urumqiensis"
                     /db_xref="taxon:638269"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32732
     Region          2..313
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msvrharlii lgsgpagysa avyaaranlk pllitgmqag gqlttttevd nwpgdphdlt
       61 gpalmarmqa haerfdteiv fdhinaadla grpftlrgds atytcdalii atgasarylg
      121 lpseeafmgr gvsacatcdg ffyrnrpvav vgggntavee alylaniass vtlihrrdgf
      181 raekilqdkl rervaegriv lkldaqvdsv lgdasgvtgv rlatpagaed iqvdglfiai
      241 ghtpntglfe gqlalregyl vvnggrdgna tatnvpgvfa agdvadqvyr qaitsagagc
      301 maaldaerfl dgll
//
LOCUS       WP_120996449             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120996449
VERSION     WP_120996449.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33351
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_120997260             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas urumqiensis].
ACCESSION   WP_120997260
VERSION     WP_120997260.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas urumqiensis
  ORGANISM  Stutzerimonas urumqiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas urumqiensis"
                     /db_xref="taxon:638269"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38878
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletr agetrvaatp etikkligqg hqvtvqrgag isasvpdsaf eavgaslgda
       61 aaafgadivl kvtapdasel glmrsgavlv gmlnpfdndt iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmvaanqypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaegvggy arpmpaswma
      241 rqaqavhera kqadivitta lipgrraptl lkeetvqqmk pgsvvvdlaa aqggncplte
      301 adqvvvrhgv tivgytnlaa lvpadasaly arnlldflkl vidkdgqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_120998959             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_120998959
VERSION     WP_120998959.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33310
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknvvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqgvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnveglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121000923             330 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Saccharothrix australiensis].
ACCESSION   WP_121000923
VERSION     WP_121000923.1
KEYWORDS    RefSeq.
SOURCE      Saccharothrix australiensis
  ORGANISM  Saccharothrix australiensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharothrix.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Saccharothrix australiensis"
                     /db_xref="taxon:2072"
     gene            1..330
                     /gene="trxB"
     Protein         1..330
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35154
     Region          7..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnlivv gsgpagytaa vyaaraqlep lvfegsqygg almttteven ypgfrdgimg
       61 pdlmeqmreq akrfgaelra edvesveleg dvkyvtangt ryaakavvla mgaaarylhv
      121 pgeqellgrg vsacatcdgf ffrdhdiavv gggdsameea tfltkfarsv tiihrreefr
      181 asrimlerar anekikwlln aevtevvgeg svsavktrdt rtgevtehaf tgffvaighd
      241 prselvrgqv dvddegyvkv qgqstytnva gvfaagdlvd htyrqaitaa gsgcaaaida
      301 erwlaehgta aaavtaehvg ggysepvtts
//
LOCUS       WP_121005430             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121005430
VERSION     WP_121005430.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33422
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy iveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121010159             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121010159
VERSION     WP_121010159.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33420
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeti ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdaf gvsslsiknt atnekreliv pglfifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121009182             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hydrogenivirga caldilitoris].
ACCESSION   WP_121009182
VERSION     WP_121009182.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga caldilitoris
  ORGANISM  Hydrogenivirga caldilitoris
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Hydrogenivirga caldilitoris"
                     /db_xref="taxon:246264"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34056
     Region          6..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 madiekvvii ggapagltaa vytsramlep lvfgghmfgg qlmlttdven ypgfpegiqg
       61 pelidrmrqq aekfgariiy envvkvdfkt kpfrlwagek eylaesviva tgarprmlgl
      121 eseallmgkg vsycavcdga ffkdmdvvvv gggdsameea lhltqharsv tvihrrdklr
      181 askimqdraf snpkikfvwn svveevydvn kgkvtgvlvk dvktnelrei kcegvfiaig
      241 hipntdiftg qleldsqgyi kthdfvktsv egvfaagdvh dkryrqaita aafgcmaale
      301 cerylaekgi i
//
LOCUS       WP_121015169             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121015169
VERSION     WP_121015169.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33406
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvrnavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsiivdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121012511             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hydrogenivirga caldilitoris].
ACCESSION   WP_121012511
VERSION     WP_121012511.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenivirga caldilitoris
  ORGANISM  Hydrogenivirga caldilitoris
            Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
            Aquificaceae; Hydrogenivirga.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Hydrogenivirga caldilitoris"
                     /db_xref="taxon:246264"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34975
     Region          16..315
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mgvgfglnyq peelydviii gagpagstaa iytsraglkt lvlyraeadg algvtqqien
       61 ypgvpgpvsg yellkimreq aksfgtqfvr gkviatdfsd evkkvftidg refrgkaiii
      121 asgamerank fkgedeflgr gvsycgvcda affkdqpvav vgeddygvee aefiarfask
      181 vyfvapgski kapaevieef ekldnvevll rhrvleivgd qlvkglklkd vakqeeklle
      241 vngvfiflgg tkpsvdflmg qvemtdgdci vvneemmtsv pgvfaagdvl ctnikqavia
      301 aadgckaala vdkfinkkak itsqw
//
LOCUS       WP_121021462             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Litoreibacter meonggei].
ACCESSION   WP_121021462
VERSION     WP_121021462.1
KEYWORDS    RefSeq.
SOURCE      Litoreibacter meonggei
  ORGANISM  Litoreibacter meonggei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Litoreibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Litoreibacter meonggei"
                     /db_xref="taxon:1049199"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55523
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapketf egearvamtp esalqiqklg hscvietgag alagfsdkay kdagvevvkt
       61 aaalwkaadv vvkvrqpdat eskrlregqt lisffnpaan eagmeaakka garviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqvesmg aefvfldfee eqadgstsgg yasvsspefr
      241 eaqlakfrel apeidivitt alipnreape lwtedmvkam kpgsvivdla aekggncklt
      301 vmdekivtdn gvtiigytdf psrmgaqast lysnnirhml fdltpekdgv inhnmeddvi
      361 rgatvtfdke itfpppppki aaiaaapkka kapeltheek aakevtefkq qtktqvtlla
      421 vgavlllgvg lvapasfmqh fivfvlavfv gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgsf lvillaalav fmtginifgg flvtrrmlam fqks
//
LOCUS       WP_121023104             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Litoreibacter meonggei].
ACCESSION   WP_121023104
VERSION     WP_121023104.1
KEYWORDS    RefSeq.
SOURCE      Litoreibacter meonggei
  ORGANISM  Litoreibacter meonggei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Litoreibacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Litoreibacter meonggei"
                     /db_xref="taxon:1049199"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33456
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msatrhtkal iigsgpagyt agvyasraml epilvqgiep ggqlttttev enwpgdtevq
       61 gpdlmvrmqd hakamgcevi sdiitnldtt srpfkatgds gtlytadavi latgarakwl
      121 gleseekfkg fgvsacatcd gffyrgqeiv vigggntave ealfltnfas kvtlihrrde
      181 lraekilinr leknpkiepl wfhelvevtg teaplsvegv kvkhtktgei seipckgvfv
      241 aighapsnel vkdvlethmg gyvvtkpdst etsipgifaa gdltdhkyrq avtsagmgcm
      301 aaleaerfla ene
//
LOCUS       WP_121033862             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Terracoccus luteus].
ACCESSION   WP_121033862
VERSION     WP_121033862.1
KEYWORDS    RefSeq.
SOURCE      Terracoccus luteus
  ORGANISM  Terracoccus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Terracoccus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Terracoccus luteus"
                     /db_xref="taxon:53356"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54101
     Region          1..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpresr aretrvaatp ktvgqlvalg ydvviesgag laatfddaay taagarvaps
       61 devwgsdvvh kvnapdefem rrlrpgtvlv slmapaldpe lvarmqtagv talamdavpr
      121 israqsldvl ssmaniagyr avveaahefg sfftgqvtaa gkvpparvlv agagvaglaa
      181 igtarslgav vlatdaraev aeqvesmgae flavrlpead pahgpgdgya kemgedynrr
      241 aaelyaeqlp svdivvttal ipgrpaprli taemvatmkp gsvivdmaas nggnvegava
      301 dervvtdngv tiigytdlaa rlptqasqly gtnlvnlmkl ltpgkdgqlv ldlddvvqrg
      361 mtvtrdgell wpppaiqvsa aakpaatasa pvaapekrpp dprrryalma lgavlfglva
      421 wasppeflgh ftvfvlavvi gyyvighvhh alhtplmsvt naisgiivvg allqlgtaqt
      481 spvsqiviiv lsfvatlvas inifggftvt rrmltmfrkg
//
LOCUS       WP_121029095             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121029095
VERSION     WP_121029095.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33440
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gmsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121034516             358 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Terracoccus luteus].
ACCESSION   WP_121034516
VERSION     WP_121034516.1
KEYWORDS    RefSeq.
SOURCE      Terracoccus luteus
  ORGANISM  Terracoccus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Terracoccus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Terracoccus luteus"
                     /db_xref="taxon:53356"
     gene            1..358
                     /gene="trxB"
     Protein         1..358
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=37257
     Region          7..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa tyaaranlhp lvfegavtag galmntteve nypgfkdgim
       61 gpdlmdgmra qaerfgaelv tddvtavdls gavktvtdgs gtvhrahavv lamgsayrel
      121 glprekelsg hgvswcatcd gfffrdqdia vvgggdsave eatfltkfar svtivhrrge
      181 lraskimaer ahsndkirfa wnsevaeihg egklsgvtlr dtvtgetrel avtglfvaig
      241 hdprnellta eaatgpdagg lvelddagyv lvqgrstrtn vpgvfacgdl vdhtyrqait
      301 aagsgcsaal daehylaala dtatpeaaqq eateideadp vetpaegslp tepvgara
//
LOCUS       WP_121036344             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121036344
VERSION     WP_121036344.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33334
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tssseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskknsh fvilaedgkt feaksviiat ggspkrtgik
      121 geleywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakk ndkiefltpy vveeikgdsa gvsslsvknt atnktselvv pglfvfvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvifyleh h
//
LOCUS       WP_121038294             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121038294
VERSION     WP_121038294.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33456
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgday gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121043056             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Herbaspirillum huttiense].
ACCESSION   WP_121043056
VERSION     WP_121043056.1
KEYWORDS    RefSeq.
SOURCE      Herbaspirillum huttiense
  ORGANISM  Herbaspirillum huttiense
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herbaspirillum.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Herbaspirillum huttiense"
                     /db_xref="taxon:863372"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38863
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaipaesr dgetrvaatp etvkklvaar hevmvesgag vkssipdeay vavgasigsa
       61 eavytaeill kvrapdeaer arlqpgtvvi gmlnpfdadn iaamaaaglt afgleaaprt
      121 traqsldvls sqaniagyka vlmaantyqr fmpmlmtaag tvkaarmlim gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpflteee keiaqgvggy arpmppdwmk
      241 rqaelvhera kqadiiitta lipgrkapvl iseetvkamk pgsvildmav dqggncplse
      301 pgktvikhgv hiigegnlaa lvaadasaly arnvldflkl iidaegklvi nkeddivaat
      361 llcqggeilr k
//
LOCUS       WP_121049283             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingosinicella
            microcystinivorans].
ACCESSION   WP_121049283
VERSION     WP_121049283.1
KEYWORDS    RefSeq.
SOURCE      Sphingosinicella microcystinivorans
  ORGANISM  Sphingosinicella microcystinivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingosinicellaceae; Sphingosinicella.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Sphingosinicella microcystinivorans"
                     /db_xref="taxon:335406"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33597
     Region          9..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mgetkqvrva vigsgpagyt agvyaaraal npviirglqp ggqltittdv enwpgesmil
       61 gpdlmdkmaa qakhvgaeiv ddlvsdvdfs qrpfrltlds gnvyladtvv iatgaqarwl
      121 glesegrfrg fgvsacatcd gffyrgktva vvgggntave ealfltnfaq kvylihrrde
      181 lradktnqar llanpkveav wnvevaevtg asdplgvtgl klrgtngaad rtldvdglfi
      241 aighdpatsl fkgklnmdge gyiltapdst atsvpgvfaa gdvkdkvfrq avtaagmgcm
      301 aaleaerfla hheaglaeaa e
//
LOCUS       WP_121049530             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121049530
VERSION     WP_121049530.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33410
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121052833            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Lacinutrix
            venerupis].
ACCESSION   WP_121052833
VERSION     WP_121052833.1
KEYWORDS    RefSeq.
SOURCE      Lacinutrix venerupis
  ORGANISM  Lacinutrix venerupis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lacinutrix.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Lacinutrix venerupis"
                     /db_xref="taxon:1486034"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117052
     Region          20..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhiylcvml lvssfsfaqi titgtvtnat dgetlpfvni tsgkngtttn qngeylieip
       61 skdnqlqfsf lgyktqtitv gnktiiniel tedtstldev vitalglere rkelgyavqs
      121 lkseglnevk svnfldnlsg klagvtvsqg atgvgssski tirgeasfsn nnplfvvdgi
      181 pinnntvfnf tneaaagfqe idfgngamev ntddikevsv lkgpsaaaly gtrasngviv
      241 ittkdgkktk glgisinssl fidtafrlpd fqnsygqgns gmfefvdglg ggtndnisys
      301 wgprldtgif apqfdspvll engsivrggd tslysgntit ptelksnpdn lkdfyetgit
      361 tinniaisng fdngnyrlsf tdlrsesiip gvnldrqtva lklnfeptek ttfsssiayt
      421 nsssdnrpsn gygsenvnys lvawgprsln innlknywqp glenvqqysf nytffdnpyf
      481 ilyenrnafe rdrvfgnial khnftnnlsl qvrtgmdyss ekrelrrafs snrfkngaya
      541 ehdvtyrein tdfllnyntl fgdfkvdvsl ggnrldqtas tkqvqtvnla qpgifslnna
      601 aspievfqyk skkrinslyg iakfgykdyl flditgrndw ssalatpfsv dqtsffypsa
      661 sasfilsnvt mlpesvsfak irasvaqvgn dtgayqtsga fvsqtpfnse ptfsdqnfip
      721 nsnlkpestt syefgadlrf lndrfrldft yynaitkdqi islpipissg ynqqvvnggk
      781 vtskgveiia gltpiktnnf twnttfnfat ntatitqlpq adgrltlays riydsqnqtv
      841 wfqveeggri gdfygtgylk nengdfiidd ngnyiadnnl qklgnynpdf tlgwnndfky
      901 knwtasflfd wrqggelvsr tsalgnvggq laeteyrpee giiaqgvtqt gapntvaisa
      961 esyyrqfydr nheennvyda sylklrqfsi gygfklsdgf lglkeggtid lsligrnlfv
     1021 itenphfdpe qlavqgngfi sgvedmsyat srsfglkasl nf
//
LOCUS       WP_121052509            1019 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Lacinutrix
            venerupis].
ACCESSION   WP_121052509
VERSION     WP_121052509.1
KEYWORDS    RefSeq.
SOURCE      Lacinutrix venerupis
  ORGANISM  Lacinutrix venerupis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Lacinutrix.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Lacinutrix venerupis"
                     /db_xref="taxon:1486034"
     Protein         1..1019
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110174
     Region          25..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfsgilt lllafvvqlt faqgktisgt isdgdnlplp gvnvlvkgts ngtttdfdgk
       61 ysisantgdv lvfsyvgntv ektvgasndi sfvmnenale evvitvlgve rkadeltsst
      121 qivkaetltq asnpnviqsl agkvsglkin ttnngvnqst rivlrgnrsl tgsnealivi
      181 dgaissantl anlapeiies tnvikgaggs alygsqgang viivttkrgt adekiniavn
      241 tsisfedisf lpqrqtkygq gwngghvtye nggwgpefdg siqpvglaqa dgsyimapys
      301 piednieqff qtgtiaqtgv sisggdtnsy allsvnrqnt efvvqddklg rtnvlfkagk
      361 kigkwdiggn inyvnsktet ttsslftell qtatnvpveq fansgneghw tsyyrspywm
      421 rdnirnttes drfngiinlk yeindnisls sltslrtfss nfvgytneyt dtsgvgggdh
      481 stvsqfatnn qesknfyndi fvnfnymltd dlsfkatlgn nvqdnwsslt svngsnvtip
      541 nfynisnitg ipgvsnssfr srsyalfgsf dfgfkdylfl tltgrndwts rlaadrnsff
      601 ypsvgvsfvp ttafpslkeg gvlnyakisa nlarvgndrv gtyetnstln qvagypyggl
      661 nsfaidatva dpllvnefid skevslnlaf fkgdritlga syyitnnkdl vtnvststas
      721 gltnstinig etetkgyeid lgitpirtad frwdinmsls sdetivkkvs dntdevslgn
      781 gnadvgifat vgepfplikg tgyqrdpqgr vlidpstgnp lktsefinlg vanpdyivgl
      841 ntsltykgfr lagvfdyrtg hqfwagtkdw lswsghlves aengrrgfif pnsaietspg
      901 vyqantnvvt ggttyanyld yfsneyrdvs enfvldataf kvrelslsya fnkdvlnalg
      961 fsdfrigina rnpfvvlpke nrgyadpefs nttgnaqgls vtgqypatrt ygmtvnltf
//
LOCUS       WP_121053486             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121053486
VERSION     WP_121053486.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33350
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsvknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121056702             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium telephonicum].
ACCESSION   WP_121056702
VERSION     WP_121056702.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium telephonicum
  ORGANISM  Microbacterium telephonicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Microbacterium telephonicum"
                     /db_xref="taxon:1714841"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34441
     Region          3..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrkviiigsg pagftaaiya aranleplli assveaggel mnttevenfp gfpeaimgpd
       61 lmakmqeqae rfgtevvydd vveldvagpv kkitlgsgkt aeaeslvfat gsaprkigie
      121 gesrlsgrgv sycatcdgff frekaiavvg ggdsameeat fltkfaskvy vihrreelra
      181 skimqerafa nekiefvwns evadilgdda vtgvvlrdtv tgaerelald gvfvaigndp
      241 rthlvhekld ltehgtiwvd grtsrtsvag vfaagdvidp tyrqavtaag sgtvaaldve
      301 hylasladag apaadvaeid glpdadaa
//
LOCUS       WP_121055638             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121055638
VERSION     WP_121055638.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33379
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 vpitlehakn ndkiefltpy vveeikgdvs gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121060934             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium telephonicum].
ACCESSION   WP_121060934
VERSION     WP_121060934.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium telephonicum
  ORGANISM  Microbacterium telephonicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Microbacterium telephonicum"
                     /db_xref="taxon:1714841"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51991
     Region          3..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 marigivaeq agesrvaasp vtvqkiidlg yevvveagag sassfpdaay tdagalivda
       61 atawgsdvvl kiaaptdaei alltpgatlv allspalrpe llsalaargv tglamdavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvli agagvaglaa
      181 igaasslgai vratdprpev adqvksiggt ylevvvpdeq kevssdgyak atsaaydaaa
      241 aklysdqaad vdiivttali pgraaprlit aadvasmkpg svivdmaaaq ggnvegsvag
      301 ervvtangvt ilgytdlagr lpqqasqlyg tnllnllkll tpgkdgslvl dhddvvqrav
      361 tvtqdgavtw ppppvqvsaa paakaaaeia paapkktmst gaksaltvvg iavlflvcaf
      421 apaplpqhfl vltlsviigf yvigkvahal htplmsvtna isaiivvgam sqiivpdplv
      481 qvlaavavll asinifggfa vtrrmlamfq kgdqk
//
LOCUS       WP_121061818             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chachezhania antarctica].
ACCESSION   WP_121061818
VERSION     WP_121061818.1
KEYWORDS    RefSeq.
SOURCE      Chachezhania antarctica
  ORGANISM  Chachezhania antarctica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Chachezhania.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Chachezhania antarctica"
                     /db_xref="taxon:2340860"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55758
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf egearvamtp dsalqlqklg heclietgag laagftdaay ekagveiikt
       61 gaqlykaadi iakvrpptet evkrltpsqt lisffypgsn aelmelaask gatviamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvflefde paqdgaatgg yaapsspefq
      241 ekqlekfrel apdidivitt alipnrdapi lwtkdmvelm kpgsvivdla aerggncelt
      301 vkdekivtdn dvtivgytdf psrmatqsst lyatnvrhmm tdltpekdgv vnhnmdddvi
      361 rgatithdke vtfpppppkv aaiaaqkpke kvpeltpeek rakevaafka qtksqvtlla
      421 vgtglilllg liapasfmqh fivfvlavfv gfqviwnvah slhtplmavt naissiiilg
      481 almqlgsgsf lvlllaaisi fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_121062857            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            vaceletii].
ACCESSION   WP_121062857
VERSION     WP_121062857.1
KEYWORDS    RefSeq.
SOURCE      Maribacter vaceletii
  ORGANISM  Maribacter vaceletii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Maribacter vaceletii"
                     /db_xref="taxon:1206816"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111661
     Region          25..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkifkktci ifigflvqis faqekpisgt iydqdglplp gvniliegts ngtqsdfdgn
       61 ylitgnqgqt ilfsylgqke irvaiktqtt initmeedaq aleevvvvgl gqsknpskla
      121 ysvatvdtek mldahetdfv nalagkttgv qinsssglag gssrilirgv sslnydntpl
      181 yvidgipvsn tenqfdsrde dqalfygsts ggsidispdq irnitilkga aasaiygsra
      241 angvividth kgnknssaqf nfkssttist iiepkrqqiy tqgsggnyrt gepgdqtsls
      301 wgpkiselgi sqynpydifr tgitkdnils vrggsesaty yasvgifnqe gtvptnsfdr
      361 ysflfnsshd itkklsvnak lsytnsinkr pfegngrtsi mwtiagapis ynllpatned
      421 gsqrlyrtnr nnpyhllent gltsktnrfq psisltynil ewiklkatss mdynlsnars
      481 iensgiigty ssgrvlqtdr tnrdfntdii ltinknfsek itadyligyn lldrknssly
      541 aegasfvipd fydlsnttsl qtdeettikr nysfygqanf syddylfltl tgrndwsstl
      601 psnknsffyy sgslgidlak tfdlhgtlnr amlrtsysri gkdapeysti tgnikanpgd
      661 gqrgninfpf qgsgsyvqsa ikgnpeltpe ftneieisad lqffqsrlgi efnyydrkse
      721 dqifevplaa atgfssifkn agsienkgie iatnvtpiet enfswdigvn yskndskvie
      781 laegvesvrl sgftnpgifi rkgepygviw ttlykrneeg qllldddgyi qfgevgnagt
      841 atpdwtgglt tnvrykgfel sgvmdirvgg kiynldefyt sfygtsilta drekdviidg
      901 iiessgevnt ipikkdfnyw nayagdeefv qktdfiklrn vtlaynipsr litktgfnsa
      961 klslsgrnlw iktddsftgs dpelslygsg ngqgitnfqi psnksysltl nlsf
//
LOCUS       WP_121062861            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            vaceletii].
ACCESSION   WP_121062861
VERSION     WP_121062861.1
KEYWORDS    RefSeq.
SOURCE      Maribacter vaceletii
  ORGANISM  Maribacter vaceletii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Maribacter vaceletii"
                     /db_xref="taxon:1206816"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118743
     Region          25..1087
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtklngilt lllaliahvt laqektvsgt vsdqdglplp gvnivvqgst sgtqtdfdgn
       61 ysinasegqt lmfsyigqkt ataivgasnt vniqlqedae aleevvvtam gmsrekkslg
      121 yaaqeikgdq vstvkvdnvv nslsgkvsgv qikannnfgg ssnflirgvs slkgnnqplf
      181 iidgipisnr innttaqegg stgydygnaa sdinpddvas inilkgaaas aiygsrgsng
      241 aiiittkkgr sgnakvtvss gitvgsidks tfleyqdeyg agygpyygin edsyfqdida
      301 tgdgitdivv ptfddgsyga pldgslvyqw dafvpehany qtatpyvagk ntpvdffets
      361 yqynnsvsva ggnekmtyrl gytnfeqkgm lpnsnlnknt fnlngtlkvn dklqvgsnan
      421 fiiqrtvgrn stgysdnlms qfrqwwqvnv dvkeqqaifn etgqnyswnh eggfvqggsa
      481 lqphywdnpy wsryknyqnd rrarfygnlf atysltnwld vtakgavdsy delreerrav
      541 gsvaapfgll rddessgydr kdisfreyny dlmfnvntaf nddltltgva gvnlrsetys
      601 fyhqataggi ivpelyslsn svnavpkpke tlekkkvagy yaqaslgykn mlyldltdry
      661 dvssslpsgn nkynyyaiss slifsnlida swlnfgkirg gyaevgndlp annvydtfti
      721 nnnfgssviv sypgtkqnse lipertkeie fglearmfnn rvgfditayk kntedqlmdv
      781 slstttgftr rwvnagemen kgievglnft pvetnnfawn vnvnwsknen kvvslfggqe
      841 nlqlnsfqgg isinatvgea ygsirgtgfd yhsngqkivd angyyvakad qvlgnvnpdw
      901 lggvsntlry kelslnflid iqkggdvysl dthygqgtgl pyytaglnel gnpkrdpvts
      961 gadsggvlnp gvtedgqpnt traradyfgg ayywgnssrn paaltvydas yiklrelslk
     1021 yqmpvdkwlk gkfvsaatis lvgrnlwiid knvpfadpes glgagnvqgy lsgsyptlkt
     1081 vglnlnlef
//
LOCUS       WP_121062906             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chachezhania antarctica].
ACCESSION   WP_121062906
VERSION     WP_121062906.1
KEYWORDS    RefSeq.
SOURCE      Chachezhania antarctica
  ORGANISM  Chachezhania antarctica
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Chachezhania.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chachezhania antarctica"
                     /db_xref="taxon:2340860"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33429
     Region          8..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdprhvkvl iigsgpagyt aavyasraml epvliqgiep ggqlttttev enwpgdsevq
       61 gpdlmvrmee haramgteiv sdiitdldls erpftatads gavykadavi latgarakwl
      121 gipseekfkg fgvsacatcd gffyrgqeiv vigggntave ealfltnfas kvtlvhrrne
      181 lraekilidr lmknpkiepl whhvleevvg tdsplgvesv kvrhvdtgvv seiptkgvfv
      241 aighapsnel vidqlethmg gyvvtqpdst atsipgvfaa gdltdhkyrq avtsagmgcm
      301 aaleaerfla ene
//
LOCUS       WP_121064251            1067 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            vaceletii].
ACCESSION   WP_121064251
VERSION     WP_121064251.1
KEYWORDS    RefSeq.
SOURCE      Maribacter vaceletii
  ORGANISM  Maribacter vaceletii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Maribacter vaceletii"
                     /db_xref="taxon:1206816"
     Protein         1..1067
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116984
     Region          20..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkytmllfvl fasalghsqq tisgtittif gdpisnvnit lvgtskgtas ntkgayaidv
       61 pnfqgalqfs algyttqvip ihynetvnav leesseqlee vvltalgfkr etkelgyavq
      121 sinakgvtev ksanfldnls gklagvtinq gatgvgsssk itirgeasfs nnnplfvvdg
      181 vpinnnsvfn ftneaaagfq eidfgngame vnpddieevs vlkgpsaaal ygtrasngvi
      241 liqtksgaks kglgisynts ffvdsafrlp dfqneygqgn sgqfayvdgl gggtndnity
      301 swgprldagn lvpqfnspvt langtvvrgg dtalynglpi tatpftsnpd nlkdfyetgt
      361 tainnlaias nfdkgnlrls ftdlrsesii pgvnldrqti aarlgfhpte klhinssisy
      421 vnsqsdnrps sgygsenvny slvawgprsl nikdlknywq pglegtqqys fnytffdnpy
      481 filnentnsf nrdrvfgnls akyditdnls atirtgmdys selrqlkray ssnrfrngay
      541 aehdvffrei ntdfllnykn nfgdfkvdis lganrinqka vtnqsqttsl aqpgifklsn
      601 aaspievfef askkrinsiy glakfgykny lfldvtgrnd wssalatpfs vdntslfyps
      661 vsssfivsev vnlpqeisfa klraswaqvg ndtnpyqttg afvaqtpfng qptfsdqnti
      721 ananlkpeqt ssfeigadir ffkdrlsfdi syynavtkdq iislpigiss gftqqvvngg
      781 evrskgveii lnatpvhttd fswnttfnfs rnratveslp qdgglltlay sriydsqnqt
      841 vflqaeeggr igdlygtgyl knengdfvlt negryipdnn lqklgnynpd filgfnnqfs
      901 ykkwdlgflf dwrqggiivs rtralgnvgg qlaetafrpe egiiaqgvvn vgtidnpvye
      961 pnttavtaes yyrqfydrnh eenntydasf lklrqvslgy tfdnlkvfkn datlrvslig
     1021 knlfaitenp hfdpeqlavq gqgfisgied msyattrsfg ikagfnf
//
LOCUS       WP_121065329            1078 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Maribacter
            vaceletii].
ACCESSION   WP_121065329
VERSION     WP_121065329.1
KEYWORDS    RefSeq.
SOURCE      Maribacter vaceletii
  ORGANISM  Maribacter vaceletii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1078)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Maribacter vaceletii"
                     /db_xref="taxon:1206816"
     Protein         1..1078
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116287
     Region          26..1077
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlktklsli aillfnitlf aqdgyvlsgt vsdadnvpip ganviilgtt tgtatdfdgn
       61 fqitvksgde lqfsyigyvt ksvsvtgqes lnmilaedaa qleevvvvgy gtrkkshltg
      121 avakiggddv aavqtarvdd alagklpgvl iqnqdgspga apkiqiraas sissasnpli
      181 vvdgypisgg ldtvnpndiq slevlkdaas aaiygsrgan gvvlvttkkg ksgkakfsyn
      241 aytstsskya dnilmnasew antietnvan gtfdisnvdn typgmydyrl nalknspgai
      301 speewlfqng sstshdfsms ggnddvnyfa smgyqnaegv vrtqgyerln arlnvdaklg
      361 ekfksgvsfn gftskrdilg hdmrdllray gvhpvyhtae siafvqqldr daqalglagm
      421 dagyrgsgye assiyelepg maaqdwhygr aqnggndglg rrdangiggs gdagpaakld
      481 ntdawektff gnvsgylqys iidglnlktv lggdlrdtqa yshrllgfds rardsqtymn
      541 qtdlkvstvl settlsyakv ignhdisava gieyqstsir gtalagsnvp dtaiqnfnll
      601 apadivvter detraresif grvnyayddr ylisaslrrd gdsrfgankr yetfpaislg
      661 wnvhnesfle dnetlsqlkl rfstgslgta sflgsydsqs llqaaptafg tgflipdnvq
      721 nddltwqtnt etnygvdlgf fnnrlrigvd yytsdiedil inqsvsevlg tpsivlnsgd
      781 vrssgleiel nasivnsenf rwsmganlst veteitdlgg ldelpqavyg qsgrgpvfrn
      841 yvggeigemw gletigevem ihvadptlni ginsgeqyvv dqqspgedgf geidftrtve
      901 dggdlvkigq atpdfywgmt qnfnykdfdl sfqfqgshga elynidplyy nsqwgrrlpy
      961 svfdansdgi adhngehytl trnrtdamiq dasfialrnl tlgytfqsdl tdkiglnsvr
     1021 iygaasnlly fmasnytsyn pegvktsgsd ylgpttygaq vgaspvvksf tlglnvnf
//
LOCUS       WP_121068697             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Maribacter vaceletii].
ACCESSION   WP_121068697
VERSION     WP_121068697.1
KEYWORDS    RefSeq.
SOURCE      Maribacter vaceletii
  ORGANISM  Maribacter vaceletii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Maribacter vaceletii"
                     /db_xref="taxon:1206816"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34383
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdsierikt liigsgpagy taaiyasrad lkpvlytgme pggqltttte vdnfpgypeg
       61 idgptmmvql qqqaerfgte vrigmitate lsdkvggihk vtvdndkvie aetiiistga
      121 takylglpse qklrgggvsa cavcdgffyk kqdvaivgag dtaaeeasyl snicnkvtml
      181 vrkdymrask amqhrvesip nieikyntev devlgdqvve glrmvnnqtq ekediaitgl
      241 fiaighkpnt difkgqldmd etgylltegk ttktnlpgvf acgdaqdkdy rqavtaagtg
      301 cmaaldaery laaietpeev a
//
LOCUS       WP_121071188             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121071188
VERSION     WP_121071188.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33292
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121074830             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Leucobacter aridicollis].
ACCESSION   WP_121074830
VERSION     WP_121074830.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter aridicollis
  ORGANISM  Leucobacter aridicollis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Leucobacter aridicollis"
                     /db_xref="taxon:283878"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33823
     Region          3..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mreviiigsg pagftaaiya araelspqlf asqvsmggel mnttevenfp gfpegiqgpd
       61 lmqkmqeqae rfgtevvydd itevdfsgei krvtdttgtv hearsiifat gsayrklgve
      121 geerlsghgv swcatcdgff frdktiavvg ggdsameeat fltrfakkvy vihrrdslka
      181 skimqqrafd nekiefiwns evteihgdas adrlslrntv dgsvselpie glfvavgndp
      241 rthlvhgkld ltedgtiave grtsltsvpg vfaagdvidp syrqavtaaa sgtvaaldae
      301 rylasvedal asaavag
//
LOCUS       WP_121075082             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121075082
VERSION     WP_121075082.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33377
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakk ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121082755             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121082755
VERSION     WP_121082755.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33310
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffvfvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgtta
      301 algvisyleh h
//
LOCUS       WP_121085896             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pararobbsia silviterrae].
ACCESSION   WP_121085896
VERSION     WP_121085896.1
KEYWORDS    RefSeq.
SOURCE      Pararobbsia silviterrae
  ORGANISM  Pararobbsia silviterrae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pararobbsia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pararobbsia silviterrae"
                     /db_xref="taxon:1792498"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34089
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqvkhakvl ilgsgpagyt aavyaaranl npvlvtglaq ggqlmtttdv enwpadangv
       61 qgpelmqrfl ehaqrfntei vfdhihtaki tekpirligd ageytcdsli iatgasaqyl
      121 glpseelfmg kgvsacatcd gffyrqqeva vigggntave ealylsniak kvtvvhrrdk
      181 fraepilidr llakekegkv eikwnhvvde vqgdtsgvts lrikhrdtga tqdielagvf
      241 vaighkpntd lfegqlemkn gyivthaglg gnatattvpg vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq rylesleah
//
LOCUS       WP_121086282             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121086282
VERSION     WP_121086282.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33317
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pglfifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121089054             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121089054
VERSION     WP_121089054.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33352
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsvknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlcecdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121089156             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pararobbsia silviterrae].
ACCESSION   WP_121089156
VERSION     WP_121089156.1
KEYWORDS    RefSeq.
SOURCE      Pararobbsia silviterrae
  ORGANISM  Pararobbsia silviterrae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Pararobbsia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Pararobbsia silviterrae"
                     /db_xref="taxon:1792498"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39791
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaevr egetrvaatp etvkrlasas hqvlvqagag ahafftddaf raagaeivda
       61 saafgadivl kvrapsdael pymkpgtvli gmldpfdteq adrlaaarlt afalesaprt
      121 traqsldvls sqaniagyra vlmaaalyqr fmpmlmtaag tvkaarvvvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetaee eeaaqgvggy arpmppawlk
      241 rqaaavherl kqadivista lipgraaptl ideetvkamk pgsvivdlaa grgieqphgr
      301 ggncpltead ktvvrhgvqi vghtnlpatv aadasslyar nlldflkliv dkdgrltidl
      361 dddivaatll ardgerarka
//
LOCUS       WP_121093049             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseinatronobacter ekhonensis].
ACCESSION   WP_121093049
VERSION     WP_121093049.1
KEYWORDS    RefSeq.
SOURCE      Roseinatronobacter ekhonensis
  ORGANISM  Roseinatronobacter ekhonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Roseinatronobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Roseinatronobacter ekhonensis"
                     /db_xref="taxon:254356"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55276
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkvgalkeik pgearvaltp dsaaqlqklg heclvqsgag eaagfndaty eaagvtvvad
       61 aaalvdgadi vikvrepeea evkrlragqt lisffwpaqn eamldaakdt gatviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkipparv livgagvagl
      181 aaigtstslg aitmafdvrp evseqiesmg aefvflefde paqdgaatgg yaapsspefr
      241 ekqlekfrel apttdivitt alipgrpapk lwtedmvkmm kpgsviidla aekggncdlt
      301 vmdervvten gviiigytdf psrmatqsst lyatnirhmm tdltpekdgv vnhnmeddvi
      361 rgatvahage itfpppppkv aaiaakpkek vkeltpeekr akevaafkaq tkqqvtliav
      421 aavlllavgl vapasfmqhf ivfvlsvfig fqviwnvahs lhtplmavtn aissiiilga
      481 liqigsssll itvlaaagif masinifggf lvtrrmlamf qks
//
LOCUS       WP_121096126             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Roseinatronobacter ekhonensis].
ACCESSION   WP_121096126
VERSION     WP_121096126.1
KEYWORDS    RefSeq.
SOURCE      Roseinatronobacter ekhonensis
  ORGANISM  Roseinatronobacter ekhonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Roseinatronobacter.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Roseinatronobacter ekhonensis"
                     /db_xref="taxon:254356"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33792
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttsrhtrll iigsgpagyt aavygaraml epvlvqgiqp ggqltittev enwpgdtmvt
       61 gpelmvrmea haremgteii sehiasldls arpfravgds gaiytadavv latgaqarwl
      121 glpseekfqg mgvsacatcd gffyrgkevi vvgggntave ealfltnfat kvtlvhrrds
      181 lraekilqhr llnhpkvevi wdhtleevlg ntngggvqga rlahttgget reiacdgvfi
      241 aighspasel vkdqlkmqsg gyvwvepgtt rtsipgvfaa gdltdhvyrq avtsagmgcm
      301 aaldaekfla eqgqdmaae
//
LOCUS       WP_121100517             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121100517
VERSION     WP_121100517.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33317
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ngkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsvlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121100572             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Litorimonas taeanensis].
ACCESSION   WP_121100572
VERSION     WP_121100572.1
KEYWORDS    RefSeq.
SOURCE      Litorimonas taeanensis
  ORGANISM  Litorimonas taeanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Litorimonas taeanensis"
                     /db_xref="taxon:568099"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34406
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtvhhkvl iigsgpagyt aavyaaraml epgivaglqp ggqltittdv enypgfpeim
       61 gpelmdkfke halkfgtafh edtiidvdft krpftmkgds gtvytadavi iatgaqakwl
      121 glpsedkfqg fgvsacatcd gffyrgkevv vvgggntave ealfltnfas kvtlvhrrdt
      181 lraekilqer lfnnekveil wdtaleeilg dedplgvtgv qlkntktgel fkrdthgvfi
      241 aighkpstav feghvqmneg gyittapdst atnipgvfat gdvsdetyrq avtaaglgcm
      301 galeaerfla ehqiasvqea ae
//
LOCUS       WP_121102477             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Litorimonas taeanensis].
ACCESSION   WP_121102477
VERSION     WP_121102477.1
KEYWORDS    RefSeq.
SOURCE      Litorimonas taeanensis
  ORGANISM  Litorimonas taeanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Robiginitomaculaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Litorimonas taeanensis"
                     /db_xref="taxon:568099"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39033
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhiavikdag paehrvaatp etvkgyvksg hsvsvtkgag qdanysdady keagakiats
       61 natcvksadi vfsitggdak lvaglkkgag itglmnptdn pkyaeacaka gvtafaleyi
      121 prisraqsmd vlssqsnlag yravvegagl ygrampmmmt aagtvapakv fimgvgvagl
      181 qaiatarrlg avttatdvrp atkeqvaslg akfiavenee fkaaetaggy akqmspeyqk
      241 lqaeltashv akqdivitta lipgrpapkl vskdmlanmr pgsvlvdlav erggnvegak
      301 kgeivttkng vqivghlnwp srmasdasam faknlkaflp litsedgqya pdweddiikg
      361 caltkdgevi herllg
//
LOCUS       WP_121104786             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. WPR_5_2].
ACCESSION   WP_121104786
VERSION     WP_121104786.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. WPR_5_2
  ORGANISM  Pseudomonas sp. WPR_5_2
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. WPR_5_2"
                     /db_xref="taxon:1907371"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38625
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpkemh agearvsatp etikklisqg hkvtvqsgag vnasvvdsay eaagasigsa
       61 ndafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaaavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlas avaadasaly arnlldfmkl iftkegqfei nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_121111091             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhodococcus sp. P1Y].
ACCESSION   WP_121111091
VERSION     WP_121111091.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P1Y
  ORGANISM  Rhodococcus sp. P1Y
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rhodococcus sp. P1Y"
                     /db_xref="taxon:1302308"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34758
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpkvhdli ivgsgpagyt agvyaarael qpllfegtqf ggalmtttev enfpgfregi
       61 mgpdlmeqmr eqakrfgadi rtedveelql dgeiktvsag getyraravi lamgaaaryl
      121 gipgeekllg rgvsacatcd gfffrdqdia vigggdsame eatfltrfar svtivhrrse
      181 frasrimler aknnekinfl tdtkvlevlg dssvtgvaie naltgekstl avtgmfvaig
      241 hdprnelvkg qvalddagyv tvasptsats vagvfaagdl vdhvyqqait aagtgctasi
      301 daerwlaeqg dittntleha dqpvdavsa
//
LOCUS       WP_121116960             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. P1Y].
ACCESSION   WP_121116960
VERSION     WP_121116960.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. P1Y
  ORGANISM  Rhodococcus sp. P1Y
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rhodococcus sp. P1Y"
                     /db_xref="taxon:1302308"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38554
     Region          18..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(31,86,105,298,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(60,138..139,148..149,152..153,156..157,159..160,
                     162..167,169,171..173,176,199..200,288..289,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,138,141,144,185..188,208..210,238,249,
                     266..268,275,277)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(135..136,138,148,191..192,199,215..216,218..221)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(168..172,175,178,201,203)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msisqsteng tnsgastrvg vvresveger rvalvpkvva sligkgvrvv vesgaglsal
       61 ipdelyveag aeigdpwsad vvvkvapptd aeisklsngs tligflaprn adnkiealaa
      121 agvqafavea iprisraqvm dalssqanva gykavilaas estrffpmlt taagtvkpat
      181 vlvlgvgvag lqalatakrl ggrptgydvr pevadqvrsv gaqwldlgid aageggyare
      241 ltederaqqq qaleeaikgf dvvittalvp grpaprlvta aavegmkpgs vvvdlagetg
      301 gnceltepgq tvvkhdvtia splnlpatmp ehaselyskn vsallelmld enavlapdfs
      361 devlaqscvt rkaea
//
LOCUS       WP_121118740             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Croceibacterium ferulae].
ACCESSION   WP_121118740
VERSION     WP_121118740.1
KEYWORDS    RefSeq.
SOURCE      Croceibacterium ferulae
  ORGANISM  Croceibacterium ferulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Croceibacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Croceibacterium ferulae"
                     /db_xref="taxon:1854641"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35320
     Region          6..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtthttrmli igsgpaglta aiygaragme pivvqglqpg gqltittdve nypgfrdvvq
       61 gpwlmtemqa qaehvgtrmi wdtitdvdid sgtpfrakgd sgdeyvgdvl viatgaqakw
      121 lgvpgeqalg gkgvsacatc dgffyrgkkv avigggntav eealylthha eevtlihrrg
      181 elraekilqd rlfvhpkikv lwnkrvesfe gdpmagglth lvlgdmetge fsdfacdgaf
      241 vaighapsts lfqgkvemdd ngyivvepgt pktnrpgvfa cgdvadhtyr qavtaagsgc
      301 maaldaerfl atleyvrneq aahhkveaea ae
//
LOCUS       WP_121120546            1180 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121120546
VERSION     WP_121120546.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1180)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1180)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1180)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1180
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1180
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=127498
     Region          52..130
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cl21470"
                     /db_xref="CDD:473874"
     Region          197..1179
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmhplnhtll iacgfvlfch sgqahtteik yrtnvvgrtk plsflavdti gisgkvtdsl
       61 gtalagvvvt ekktgnsgls dqtgafrlsa dpngvlvfik tgfaikevpv nnqklievvl
      121 spgtaevqtd stansrdsss tvaagrdstt kvtagrdsit vagqdstkna tgnqdstknv
      181 agnpngsgav aagkasvkgt vtgpkgplpg vtvavvgtnv sastdesgkf qiaagpknel
      241 rfsslgfeav tqlvgdrkdi qvvlsgetkv ldsvqvvavg ygtmdratlp savssigane
      301 ikdevlpsit qaiqgkaggv qvtqksgspg ggisirvrgt tsinassdpl yvvdgipvns
      361 ttnftggstf dfgggtqgin vlssinpsdv qsieilkdaa sssiygsraa ngvvlittkk
      421 gvagqsefnf nmyegfsqvp keryydfmnt eqyqdymkdy ykilqqqdpk avipeqifsn
      481 pnvntnwqda ifrnagtrny elssrggsek tqyytsvgym kqggvllgsd fnrlsgrinl
      541 dhqhneklrf stainltrav nkrvqeensk egatksgifs ppnlavrdet gnfvydqvra
      601 trenpvamlt lptneaqtfr vlanasaeyn ivpelllkts fgtdisfide tffmppvglr
      661 syasqggiga rrntrdqlwi nettltydkk fgdhsinala gfsvqesrle fvhgqrsnfp
      721 nndipyitag gvitgansyp eewaiasgfa ratyiykdky ilnanvrsdg ssrfgadnrw
      781 avfpsfagaw rlteedflkd skvlddlklr aswgitgnqn ignyasrsly ssgynymgla
      841 gfvpnvlgdr nlkwettnqw nvgvdagflg nrisvladyy ykkttdllig lpiltssgyl
      901 trftnsgdie nkgfefeltt knlvgefkwt tslnmtfnrn kvvalpeglt emrggvgdln
      961 raivgqplgv fygwqatgvn pqtgmidylg adgsavtptd ykdqrmigdp npsffggitn
     1021 nfayknfdls vqgqftygnd ifnynlasgl egfnpssnqf vdfvdrwrap gditdvprpa
     1081 pgdlsngais srfvedgsff rirnitfgyt lpssiaekik mkklrwyatv qnafvftsyr
     1141 gydpevsssh ggantgliyg ydygsypqpr ifttgvnvtf
//
LOCUS       WP_121120646            1084 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121120646
VERSION     WP_121120646.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1084
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119748
     Region          46..1083
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnqlifpsks skrlaqllai gimtggiips ysygvnlseh nlnffknitg kvvdqngkpl
       61 agvtisikgs ktatstdadg tfrlnlpvgn eilvlnfvgy krleipvgnq nvlnirmeae
      121 sqeleevvav gyttqkkahl tgsvvaikae eiedlpstnv aaglagrllg vnvsggvsrp
      181 gskatlgvrr smaagkdggt seplyvidgv iqvngqnqpd atqfnnldps eiesisvlkd
      241 gaaavygvra adgvilittk rgkigapris yngsyainde ayrtkvmnay qygmyfnimn
      301 gpngnntdps rpgfekaffs qdeldyfknh synwlddawk ssyltkhsln isggadkaty
      361 fanvaynkqn gnlstldydr wnfragsdiq vasnfkaaiq vfgnvgdlqk tfnkiggend
      421 dndyrnllla spyvpayvng lparlpgtsg dlsayhffel qklnnlatsd srqfgvnlsg
      481 eyqapwlkgl vlrgsyarnf tssrgtqvgt kyqtytftng gdnshiydlg tnpvaatfsn
      541 gnrvyfsnsn gnnyqanfta iydkkwkqht fsglfsiekg eanssqedvw kddplantng
      601 qfgtafgavd grtaayesgt lgyvgrlnyr ygekylaevl frsdastkfa penywanfyn
      661 isagwvisee dffkvngvdf lklrfshgkl gsdkiplwnw lqrysyqtgk gavfggnsga
      721 ttgmkmeksp nrdatwsaey knnvgidarf lrsrlsatie gfyykghdal iertgnipit
      781 vggsvaaenf gkennygief elgwqdkvnd fsygistrfs wsdgrviqgn fndidmlypw
      841 kprpnassdl gawgydylgm fktqadidny vsqynitqvf dqsvdklrpg mlyyrdvrga
      901 lqadgtfaep dgiindndli qlakrkdnhy tlgttlrvgy kgltaeavit gsfggyseit
      961 ernklnndis rvytnlpviw gdvydpvlnp tgtmpnpqws siynqpssfw tvsafrmrma
     1021 sfnvgyklpe ritqylrvsn arvylsamnp msiynpysyk dgngsawdvy pnlrtysfgv
     1081 nvtl
//
LOCUS       WP_121120838            1153 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121120838
VERSION     WP_121120838.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1153)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1153)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1153)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1153
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1153
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126638
     Region          76..1152
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkfvlfsva lglsfpsesy sfvkkegals sanltgallr sssktsvqnt vqgtvtdgkg
       61 pvsevsvsvv ggsastktda qghfkitaav gsklrfssig yisqdvivts ntlnvvlvdd
      121 nqsleevvvv gygtqkkgnl tgavssinvk dnlqgraiad vgrgiqgttp gltvvvpsge
      181 vgsdpvmkir gqigsiagqs nplilldnve ipsiqlvnpa dvesitvlkd aaaasiygak
      241 aafgvvlits kkgakggdtf nisynnnfsf qnsavdynmg dvnalkysle aaerigetea
      301 gafykvnrqs ydlavkwkek yggtigandp tvygrdwyvn paeptkkygv rtynvqdymi
      361 rkaaptsqhd lsisgtsgkt dynlsmglln qsgmmkptdh dqfrrtnaal rlstelnkyl
      421 tvrggaivsr rkkeypyttn sttadpwlyl yrwsslypmg ydengkmirs pwsevssant
      481 asfqnnylnl nlgatvnimk nwkvdfdytf snqeeittqp gtrftaadsw iagvarkdaa
      541 gapvyvnadg qvvpagtqga saaydlnyym ytanganpdh flraagnrrn ntinavttyn
      601 lninddhefk flaginrvtl dydmnssqtf nlldiknpql gfgvntssqq akgdalweaq
      661 lgyfgrvnya yknkylfean irydgsskfp knlkwqwfps fsagwvasee sfmewakptl
      721 nqlkfrgswg sigdqtvlps lytstlipgd inwlgadgsr yynigtpsav lsslgwqrie
      781 ttdigldmrm fknkfgvvfd wyrrdtknmi vpsgnvsatf gapppqgnfg alrtqgwela
      841 mdfnhrfeng lgfnvrgtls dakstilkyt dtkvisdyyv gkdvgeiwgy rtdrlyqasd
      901 feydasgkmv eidinqkkfn klsdpngayn tfstdskfrw gpgdvkfvdl ngdgkidkga
      961 etlsdhgdle iignetprye ygfrlgldyk gfdfsaflqg vgkrqlwgng fltipgynss
     1021 dgampaaiad nfwskdhtda fypaafnnaa sndannlvkq srylldmsym riknitlgyt
     1081 lpssltnkay iktariytsl enfftfdklk glpvdpeain gfsifnekny nsgrtgvgtp
     1141 mfksvsfgvq vnf
//
LOCUS       WP_121120848            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121120848
VERSION     WP_121120848.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113859
     Region          22..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrsllllmg llcmcctafs qkiitgkvtd lkgealrgvt vqekgkntqs atnalgvyki
       61 tasddatlvf rsvgyvsree vvrgrsvinv vlsdnnasid evvvtaygvk rdrktlgyst
      121 pivsgddvsd tqresffqgl qgrvpglsin stsglpgasa qivlrgfasi sgdnnalivv
      181 dgipinnsti nendlasnga nqsldysnra mdinpddiet ytvlkgpeat aqfgsqgagg
      241 ailittkkgk agkfttnytf sgrvesvnkf perqyvyaqg lngnydgtal talgprypeg
      301 mhiyednvqn ffttgynqkh slafeggtek vtyrwsneyn nntgivpntl yrrfstrlns
      361 takfgdklef ntslnyiysk ndkvrrgasg ylmtlmsfnp ifdvrdwidd kgnrvlhnsd
      421 ifnerdnpfw dvyrntaydi vnrvlatsni tyrannwlsl ngiigvdysn tqgqsvyhpq
      481 sysgsgsasa vrngsineyq vngrilsgsf manlkknlsk dfsfranlga efkdydfltn
      541 sqygedfydp dfysinntfp ssrlvksaaa nfrtvgfmaq tgfgylndmv ylnltgrlda
      601 asrmmpnnpy faypsaslaf nftdldffke kvswmsngky risvgttgka pyksyytlsn
      661 fepknttggg faygvnggnp nlkaektrdf etglelalld rrmtfdlsyf nrlstgqiim
      721 prlsygsgfv lrmmnggevk tygtelqatv npirkdklnw dltfnftqyk gkvlslaedl
      781 pelyesdtqv lggvrsgvvp gysigtltgt rfkrndrgdv linaqtglpi agtdryypig
      841 dripdftlgv vnkltykdfy ltflwdwrkg gdvlngldyr lyingmsskt lnreeprviq
      901 gvledglqnt pnptinriav tpysssgyyt lntepqmfie kdiytvrlrd vtlrynlpkh
      961 lirkigaqag msvfftatdv flftnytgld pesnmntpgl ggiggygidf gnmakprgfn
     1021 fgltlkl
//
LOCUS       WP_121120866            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121120866
VERSION     WP_121120866.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111455
     Region          31..1019
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnnklyttlr mlsivptmlf sasllhaqsn qvkgtvvdak skaplvgati kvlgtstass
       61 tdskgafqin vddknrvlni stigyenktv tlgpgettvt vsldeqtqql esvvvtalgi
      121 sraqksltys tqqvngdeln kvkstnlann lngkvagvni assssgpggs akvvlrgnks
      181 asgnnqvlyv vdgvpinnqt latqpgnifg gerdggdpia linpedveni svlkgasaaa
      241 lygsqaangv ilittksgkq grtvvnfsss aqieqpvslp kfqnqygqgt ggkndntsvs
      301 swggktdgtn ydntgqffrt gsnftnsltl sggneknqty fsyantlakg ivpendlmrh
      361 nfnlkesakf fddkltvegs anyitqkldn aptsgfyynp ivglyllprn ldianykqfe
      421 tfnssrnlyd qnwytlvddq ttqqnpwwvv nrnpnsskrn rlllngsaky qiapwisvqa
      481 rgsvdrtsev wdrkayagtq silarpnggy nytnttitqq ygdlianmnf hvndkfqitg
      541 lvgtsitdwk tegvnytsgt agleypnqfi iqnsktptpt glsnnrrqlq svfastnlsy
      601 dqwlyldlta rndwsstlaf tdtksffyps vglgvvlndk lnmpefinma kvrgsyaivg
      661 ndlppyttll tnslgpyavl tlndisflks lkpekthsle igtewrmwnn rlnvdvtyyk
      721 tntknqffki aanqaslynq yainagdiqn qgvealvsld aikndnftwn tslnftynkn
      781 kivklddrvs efaltgdglf gnyaskfkvg gsfgdiygld fvkddqgril vdaagkpqtt
      841 sqyvklgnsn piwqmgwnnt fsyknfnlsf lidgkfdyev msvtqalldg ygvskatgda
      901 ranghvaing vttagaavts vdpqawyest ggmspvssqy iydgtvvrlr eltvgydfni
      961 kdsffkklrv navgrnlfyi tkkapfdpev tmstgnslsg vdifmmpatr nygltlnatf
//
LOCUS       WP_121120854            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121120854
VERSION     WP_121120854.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109862
     Region          23..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkklllfcs gvmlstslwa qtktisgkvt nasdggsman vtvsikgkpi stqtnpdgsf
       61 tikadpgdvl ifravgskek qqlvgadati nvslagseea leevvvtamg ikqqarslgf
      121 avqnvsskei sesnqanvvn aiqgkvagvq vtnsggspga sanimirggs slsgnnqplf
      181 vvdgipidnt tpvsqgglga gtapasnrgv dinpediasi svlkgpaaaa lygiraasga
      241 vvittkkgss gkglitygtt fsidnvnrlp klqsiykqgl qgkydpqsyl swgpkfdqsd
      301 kiydnlgeff qtsvsqvhdl taggsterss fyasaslldq ngivknmdfd rksfrlnadh
      361 kifdnlkiga nmnyinsgrt yfsqgsangv mgaiywplnv dmkdyvnvdg tqkllsqnsd
      421 gavdnaywti nkkpitnkvn rfmavgdisy dplswlnlty rigtdyyten fqsvtaptsq
      481 tsvtgylaes tannqittst flanakrsyg dfnfnltvgh nlestyrqtt tstainfidp
      541 dfvginnsiq adrtvsksin rrrimgvfgd lnmdwknivy lnfrgrndws stlpksnnsf
      601 fypsistsvv ltdlvkeiye sestgilsya kvrgawaqvg kdapahvlrt tlgtyindft
      661 inprgfitni tdyfgnpnlk peftnsyevg adlrfinnrv gldvtwyktk sddqilgtrt
      721 ppssgsflay lnggaienkg wegiiniqai kkenfqwsfd lnfsanrakv lnlpgsldrv
      781 elsdawvtdn aaqaaaflng tvfgingnvw ktndqgqyll dnngrpqias smqlvgdrnp
      841 dwiagitntf kyrdfglsfm wdfrqggdvf nataytlvns glspltqnrd nmvipgvies
      901 tgqvngltip lnqdyyqtly aknsknfved gswvrlryvs lnykapssla kklrlqnlqf
      961 tltgrnlllf tdysgvdpev sgsgagvggs gsfgfdnlgv patrgidlgl kfsf
//
LOCUS       WP_121120926             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Otariodibacter oris].
ACCESSION   WP_121120926
VERSION     WP_121120926.1
KEYWORDS    RefSeq.
SOURCE      Otariodibacter oris
  ORGANISM  Otariodibacter oris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Otariodibacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Otariodibacter oris"
                     /db_xref="taxon:1032623"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33560
     Region          2..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mtvkhaklli lgsgpagyta avyaaranln pvlvtgmqqg gqltttseie nwpgefneit
       61 gselmnkmqq haekfdteii fdhihsvdls krpftlngdf ntftcdalii atgasakylg
      121 lpseeaykgr gvsacatcdg ffyrnkpvav igggntavee alylsnvase vhlihrretf
      181 rsekilidrl mkkveegkii lhlnsvldev lgdnsgvtgi nikstndged klitldgvfv
      241 sighspntei fanqlelnng yivvksgldg natatsvagv faagdvmdhq yrqaitsagt
      301 gcmaaldaer fleg
//
LOCUS       WP_121122221            1099 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121122221
VERSION     WP_121122221.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1099
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121863
     Region          40..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msektklffa ltlvassgya fgvhampnta ntieykvtqq eitgrvsdkn gpivgasvsv
       61 kgsaiatytd qqgrfklskl npgsiivvsy vgygskevky egqsnlsisl datstdldev
      121 mvvaygttkk stftgsatvv kkeqlekigg sgfaetlqgm spgvnvtnne gnpggdsriq
      181 irgissmsgs snplyvvdgm pydgqltsia psdiesitvl kdaaasslyg sraangvivi
      241 ttkkgksakp tlnfksawgt sdnaignptk atpeeqllnt wegmyndqfy rynrtskeag
      301 dwasanvlgk llkkssagvy vspfkdinen yvlhdgngna yinpklqkiw nesdydyyga
      361 vfsrklrqey nldvsgtagd gktnyflssn ylddkgyamn qyfkrygfra nvtsqvtdwl
      421 qlggnmsfss srqnlsgasr aldfsttlts pwlrnadntd wvysektgrr mydygtygnn
      481 ffgihvlnng gdywdnpnde gftnnqrnmi saryfagikl pynlnfkssi sidnnvykef
      541 tygsavhgpg qqapygtsvl tsggsagrvn netravtfnn iltweqdfgt hhlsalagqe
      601 sytrnvvgdn gygegimqlg qyeltstttn wsvgsykdry allsylakvd ynyddkyfas
      661 vsfrrdgssr fhpnnrwgnf lsgglswkis kenflkeatw ldnlsfrssy gttgndrliq
      721 rqlngvagge flyayqayys adnlyglpgl npktvaapdl qwernkqfnv aadfaflkrf
      781 ygtieyysrn ssdllfykef plsaqagaan gqnmnlgnlq nsgfefslga difrkdhfnw
      841 kvdgnlstlk nevtylpsga ftfnnrgagy rleeghslyd fymvknagvn pdngnmqywv
      901 kddkggwkis edyvgevtsd dyqwigsalp kvygsltnsf kvhgldfsfm fyyslggkmy
      961 dysyserstl rggvgvtqel vqdrwrkpgd hallpkwsdd nyastrrasd fyifdndyvr
     1021 lrnitlgysi pkstlqrlgl anvrffvsad nlltfgsakn rytepetgls gnnyngnadt
     1081 dngrqgarri ytgglqvtf
//
LOCUS       WP_121122217            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121122217
VERSION     WP_121122217.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116506
     Region          25..1031
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqhvlttlc liacssmqsl yaqqiqiagk itdsngnpvg gvtinvkgss qgtstneqgl
       61 ftlnansnat lilsavgyna qevqvngrkt isitlvsneq aldevvvtal gikrsqksig
      121 ysaqqvkgdd ltftketnvl gslagkvaga qvtgssganl ggtqkikirg vnsvtgggqp
      181 lmvidgtpis nsnfssstgn gvdlgnvgqd inpedietin vlkgptasal ygmrgqygvi
      241 mittkkgkkg pkkidigfns atswektgnf mplqniygvg nnqtflklas geyyvngnde
      301 swgpkmdgtp vrmyysfypq dvdfgkttpf spqpnnikdf yntgfttnng ltiaggnena
      361 airfsynnty ikgvipntsl krnnfglngt lditskllvg aninyannng qrpvqgyqgs
      421 ftgatqwfqr nidinrlrny kyadgtilnw nvnpntstgi itnnkpsdwn npffdayenl
      481 nndsrdrvfg dvnvsykifd nlkvsgfvrk dfftqnlssr tafggrldea fsvgkyqnde
      541 snyeflaeyn nkwndfslna nlgtniytrd ysyvsqatvg glatrgfyni aasidrpett
      601 syklkkqirs lyamasfgyk diyfidasir qdvssalpkn nnsyvypsvs gsflfselfd
      661 skvlsfgklr asyaiagsdv dpysallnyq mgtayktstg tittvsvpdk lknanlepsf
      721 ahtfeigtdl kffndrlgld ftyyqqrnkk qvidlsqssa tgyesefvna gdienngiei
      781 slsgtpaksa nftwnttlnf arnnskihel idninsyqld lntyssqtvy lradrgkafg
      841 tligpgylrd qatgkillda nnmpiqelnk dfgsvlpnft ggflnsiryk nidfnamidf
      901 qsggkffsws kmlavksgqa eetaamnskg knvrdpladg ggyeisgisq atgeavnafv
      961 darsyfrnqi gtkfyeewlf nasyiklrev slgytfsent lkktpfksir iaaiarnpwm
     1021 iwqkapkgid pselsmgsas iswiekgelq tvrsygvnls fkf
//
LOCUS       WP_121122378             988 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121122378
VERSION     WP_121122378.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109318
     Region          28..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkqllrpfw alnmllgvsa safaqqatlr grvmdqkgss lvgatvrfed iqkslstnan
       61 gdfsldrlqm gklrlkvsmv gyasldtliq vkdgsnplnl ylksnesele evvvigygtq
      121 kkseltgsis tvtakdfqkg qisspeqlim gkvpgvqitt sggqpgaest irirtgasln
      181 asndplivvd gvplaggsvs gianplslin pndietftil kdanataiyg srasngvili
      241 ttkkgsrsgt qinfstqnsl atvankvkll nadqirdyvn angsdamkkl lgtantdwqd
      301 viygnafttd nnvniaskag nmpyrvsagy mnqdgvlknd nlkrttaala ltpkfldnhl
      361 sldvnvrgtw skskfatqda igtaiqfdpt qsvyvedkns fggyyewiqg gkpnpnaprn
      421 plalldlrkd ngdvfrsign akvdysfhfl pelhanlnvg ydlarskgnt ftpaiaarnf
      481 neggerteyk tdinnktlef ylkydkelpa iksnidatvg ygyyknstks ynfartneag
      541 evltsvnlpf drpenllisy ygrliytydn ryvlsgtlrt dgssrfsqdn rwgyfpsvgf
      601 twraknesfl kdqqtisdlk lrlsygktgq qdgianysym pnytiggdqs myrfgneyyy
      661 lyspvvydgd irweststyn agidfgfhnn tvygsvdyys kktkdllsti piavgsnfsn
      721 flltnvgnme nqglevnlhv vpvksehstl dfginftynh skvtnltlsd dpnfiietgg
      781 irggtgnniq ahmvgytpys frpfqqvyde agkpveglyv drngdgvisd sdrymykspl
      841 pkyllgftaa ysykkwsatt tlranldnyv ydnvssnfgs synvidqasl vinnapvdfl
      901 nsnfkekqlq sdyyiknasf lkmdnfnvsy qfgqflrnsk anlsisatvq nvftvskykg
      961 vdpeisngid drfyprprty vlginvnf
//
LOCUS       WP_121122493            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121122493
VERSION     WP_121122493.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115818
     Region          48..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mfnhyiklsv vgvllviadk qtaqaswypr lretasgnek raigkfpkiv deygkpisga
       61 kvydagrqlv getdengdfs psghvthevl wveypgyyrk rikggseksv slvpavlqrt
      121 dslhigydkk kssellgavs vvynsqikdm ptplylnalt grmpglftqe vsgfrspsmt
      181 aitsndlags lpsdavkyrs sigdnteigf nlrgqspvtm idgvqrdiys idpeniesvt
      241 vvkdalssil lgqrssrgil qvttkkgqag pprisftaqt giqqslkmpq plnayqyayl
      301 yneallnagr qpvyssddfk afrdgtnslf fpdvnwydav vrdnnpttky nlgvkggikn
      361 aryalslsyl nqyglfksdd kfdyetnvqn krylinsaid vdvtddltig lqffgkiqdg
      421 rqpgaktgti lstlyntpnn aypifnpdqs yggssvyrsn lyqlatgsgy lldntrdlla
      481 nldfnykldk fvpglyakgk lnvsstsssl idrnrqqpvy dlsyneqkel vyvrygtiad
      541 qpnsfattst anffyfqgal gydkqvsekh rvgaklfmdr qtanyqfdlp aiytnfaata
      601 nyayqdkyfa evalnysgfn rfmpgnqygl fyafglgwdm lqedflkekt dwlsqlkwra
      661 tfgrtgntne aalgyyswra sygqdgangy dfgseyaytn sliekglani egtwekgnkf
      721 nigldaafwh stlkltadyf rdtyfdllqq rgstidligi gypnenigkn ryegqeislt
      781 yqnnfgefny fitanasrmk tqvlymnevf qqydwnrrtg mpvgqtfgyr angliqtqde
      841 adhapllsgn kvypgdvklv dlngdgiinq ydqtaigntk plvyfgttvg fnvagfdfsv
      901 llqgvlnrsy qqtdysfgnt gdgqgfdyml grwtpetgta atyprltlgp dptntqniss
      961 ywtrsgeylr irnldvgytl pfnwtkrakl ssvrifanaq nlftftpygr ldpeissgta
     1021 ypaqriisfg vnvkl
//
LOCUS       WP_121122364             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121122364
VERSION     WP_121122364.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108343
     Region          27..993
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkllaqcv mmpalllttf tavaqtrelk gkvvdehqsp ltgatikvkg sttatttdae
       61 gafslnipnd akslevsyig ytlkevpiag ndmtialeps sdqgleevvv igygtarkkd
      121 ltgsmvtiga knfnkgimts pdqliqgktp gvmvinntgq pggsttvrir gnssirasnn
      181 plfvldgvpm sgnsplpegr ggfssdrgnp ltylnpgdia smdilkdasa taiygsrgan
      241 gvviittkkg kegspevsvg asagvstmre ypdvlnasrf realkyytpn evddadfggn
      301 edafkaitrk aitqnyyadv aggteygkyr lsggylnqng iirgsqlkky tanlsgnfrf
      361 lenkrlgldf glfltqmdnk yapinatvgs egniisqalq wnptrplrda qgnltfvstt
      421 trnpltsiea fkdlattntl vinlapyyki tddleyrfiy samrqtgnrq gmyragliep
      481 snnedeqafi snngetnlqm thmlsynkqi nedwsvnava gyeyldynfn nnimfgrgfk
      541 ymgldyfdym qyskpanrei asyrsptnql qslflrggfn ylnrylltat vrrdgstkfg
      601 snnkyavfps lavawnvaee dflkssgifd qlkvrlgwgk tgnqefpsga srdrlifnnq
      661 sisqanygnp dlkwetstti nagidfgilg nrlygsidyf nkkttdalfe qtlaqpapag
      721 riwvnldgei vnkgveialt gtivkndnwt wdltgnatfl knsvsglvgy yetgalrgqg
      781 fsgvlgqrmv ngqplnvwyl adyqgidpqt gtsmyrgldg sistendpav nkyymnspnp
      841 ttllgistnv nykkfslaan mngafghylf nntaatglgl tnlssrnigs kffdtsvkes
      901 tsnsaapssr flekgdylkl anltlsyrvg nvgktlknln vsltgqnlfi itkytgfdpe
      961 vntdgstngi pslgieylpy pparnillgv nfsl
//
LOCUS       WP_121122632            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121122632
VERSION     WP_121122632.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119541
     Region          26..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrsikiygll llaivifplf iqaqekkvsg iiiergsgka iagaalklrn gkggtttdtk
       61 gkfeinvnnr ansvslqiss igfraidtvl tlgaghrvem vsaaigidev vvstgysaip
      121 keratgsfsf vgkdrineqi nfnimdrlpa vasglvvdrn aksgkeqflv rgmstikget
      181 qplivldnfp fegdlnsinp ddiqnitilr daaaasiwga ragngvivit tkkgttdqkl
      241 kidlnllttv qqkpdlfsld risssdmidv etmlfdkgyf dasinsaqhp vlspivelli
      301 rkkasqdqne iagieqeinr lrnvdvrndf ekylyrvglq qqttvglsqg tdkliwnasv
      361 gnglqidnld nrvrrnnvlm naklllskal tleggmnisf qnmrsgrpgf gsvtaynggl
      421 fpyaeladan gnalplvkdw rgtylqqqad kglldwryyp ledykhsvqk qqmqntilst
      481 altyklpkwf glslryqyqa esgrteklsd iesyearnmv nsyaalntat gradfkipkg
      541 glfdqsnsml rshnvrgqld fnwatgqhkv yallgselrn vsskgsgnrl ygynednlsy
      601 alfdltvpyv hyvtgaknyv mdglsisqke nrfistylna sylfdekyta tfsarrdasn
      661 lfglnvkdkw npfwsaglgw tvsnekfwnk dlisylklrs tygktgnlnp amvalttiky
      721 agpnpytqtp yarfdnyvnp elkwesvstv nigldfalkn krisgslegy lkkgsnlygi
      781 apvdytsgig pfvmknvaam eskgldlnmn svnttgqlrw tsdvnlsfns dkvtkyhmet
      841 raatlfisgi nlisgkegap vysmysykwm gldpkdgaal glldgqpsre yrkftgtnat
      901 vddlvfhgsi lpkifgslgn tiawrdwalt mrwtfkfdyy frretiryss lfstwnghgd
      961 fnkrwqqpgd eqktdipamf ypvlsgaenf ypyaepfver gdqvrfeyln layrikgapk
     1021 slfkdvllsl nvnnlgliyr knkagidpdf skssstgfsp skiysfnikc sl
//
LOCUS       WP_121122884             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingobacterium puteale].
ACCESSION   WP_121122884
VERSION     WP_121122884.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34202
     Region          12..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mefkqevehv qcliigsgpa gytaaiyaar admkpvvytg ivpggqltqt tevdnfpgyp
       61 kgitgpvmme dlreqaerfg tsvrfgyvtk vdftgdvhrv eidgtvqvta dtviiatgat
      121 akwlgleseq kyngfgvsac avcdgfffkn qevaivgagd taaeeatyla klcskvhmlv
      181 rrdefraska mvhrvmntpn ievhynsevk evlgdgqvvt girvinnkdq sekdldvtgf
      241 fvaighkpnt elftgvldmd etgylitkpd statnipgvf acgdvqdnif rqaitaagtg
      301 cmaaleaery laakesge
//
LOCUS       WP_121123019             959 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121123019
VERSION     WP_121123019.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..959
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107708
     Region          54..956
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkykkltial clglswtatt kglakashdp svilhknifq efltttipds sstdsttlvq
       61 vafrkvqknd lmgnvqaini pqlldksynt yslenleafi pgyngniwgm sgylvlvdgf
      121 prdannvmpt eieqisvlkg vnaialygsr aakgvisist krgmaggqkv kiranaglna
      181 risypkylgs aeymtlynea rqndgltply naetiyqhaa gsnpfrypnv dyyspdyikd
      241 hynrydatae isggnqraqy ytnfgfwseg smlnfgqakk ngganrfnmr gnidvkvndm
      301 islnvdaaas fyvlkgvnan yweaaanirp hrfsplipid mieegdvnsm vyvnnsnfli
      361 dgkyllggsq ldqtnafani yaggtnryln rqfqfntgln fdlknilqgl vfktnlavdy
      421 qsnynqsynn nyavyqaswn nydgkdriss ltkygddris giqnisnsty rqtiglnssl
      481 nfnrtydnnh hvsaillana fqiaesgsyh kvsnanlglq lgynysgkyy vdfssayshs
      541 aklpagnrqa lsptlalswr lskenflans nvvndlrlsa sagilntdld isdyflyqgy
      601 ytyndgawys wadgalvhsf drrrgdnpnm kfpkrkefnv slaggfynnl itfntayfln
      661 rmsgglvqat tqypmyfmtg wpvysdlpyi nynsdqrqgv dfgvnlnkql nqtfvslgfn
      721 gmyyttkavk rdelyqfnyq nragkpldai wglqhdgfym sqsdidnsaf ssfgevkpgd
      781 ikykdqngdg tidtrdevyl gkggwagspl tlglnltvkw nnftlfaaat gqfganaikn
      841 ssyfwvdaed kysvivrdrw testketaty prlttfnsdn nfrssdfwly ktdrinlskv
      901 qlsydfpkri lsskfihelg iyangsnllm iakeketmql nigqapqtrf fnvglkalf
//
LOCUS       WP_121123001            1124 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121123001
VERSION     WP_121123001.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1124
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126566
     Region          126..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklscfsqat rpflwllfav lvqlghkvna qtvtyagrni plmdvlqvvk lqtnyevlga
       61 kkilesakpi sikadkmplk lfldkilipq eigytieskt iflekktssr rsepksppqg
      121 eksfqrqirg qvlgkdrmpl sgvnisqlgn tiavadqegr fsfvstmqpl tlsrvgyknf
      181 tlalvenkde ysivmeeean aleqvvvtgy qvlkkdsytg taitksgdel rqvnpqnvlq
      241 amqvfdpsfk ilpnnlagsn pnalpninvr gssalpsgst dvlrrdnvtt tmnlpafild
      301 gfevslekvm dldmtriesv ttlkdaaasa iygsraangv mvivtkapkd gklqvtythe
      361 tnvnmpdlsg ydllnapdkl ayeklaglyd gqkqrqsqdv ldelyyhkla nvlggidtyw
      421 lsqpvrtavg qkhgvflegg aktfrygvdm ryqtrpgvmk gsgrnqysgg lnfsynpknk
      481 irfqnelsit vvdgrespyg sfenfvkmnp yyrlkddqgn itqlsdrwir vdpsgnrnee
      541 yvlnpaydat lssynksgyt ellnnlsadv dlgkglrlrg llsllkrmnt gddfrsplsn
      601 efysyetsra dergsygsys nnelywdgni rlnwdrnigk hyfnmiagan irtesydery
      661 fkaigfpndr ftdigfakgy eegkspqtnv gasrlfgsfl sgnysydnry lfdatlridg
      721 sskfgankrt apfwstgigw nihnekwfat kvisqlrlra tvgltgsvqf dpymsrvtys
      781 ydknnwyssg lgstvrnygn enlawqrtqs vdlgvdigfw snrltfslrn yskitkdila
      841 diniapstgf ssykenlgdm enkgielgvn wqaiktekwt lsllanlvqn rnkivrisna
      901 lksyneradd eqqkdeykav pllryeegqs mdaiyavpsl gvdpesgrev fvkrdgtlty
      961 twdprdiavv gvatpkmegs fggtlryqqw mlvayfqtrm ggktynqtlv drvenadpry
     1021 nvdarvleer wknpgdhtff ksiedlgrse lssrfvmpdn llalqslnis ydakqafanr
     1081 lalaslrvgl igndifrwsn vkeerginyp farsvtltlq arfk
//
LOCUS       WP_121123800            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121123800
VERSION     WP_121123800.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119524
     Region          24..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrksiamla atvlvssavy aqtvlkgkvv dqdgkpipgv titlrdgtgt qtgqngefti
       61 nykqagqlsv saigygrkev nltnqttlev tllsdernld evvvtamgit rekkslgyat
      121 qeikasaltd agqhsltgal agkaagvqvn qfggaigssa risirgnssl qkdqqplivv
      181 dgipitndaq rsgdntytgv dygsglndin pddiesfnil kggaaalygm ragagvimit
      241 tksgkraang vqisydgnfs idraanlpky qnlygqgsrg deysyntlgg gesyqdyvvk
      301 nsfsyvdgtg efgvndnide swgprmdigl mipqfnspvv ngvrqatpwn shknnvkqff
      361 qtgfsqnhni sllsktdkss trasisfrdq rgtvpntdqk kytaqlnney klsdkvsydi
      421 msnftrtesn nlvmqgydsa npmngliwfg rqvdmqdlkn nwdqrdevgn ytyynwnsay
      481 hmnpfytmhe sqnalkmnri fgktslhyqp fdflrfegrv gldyynthtf ettyfnfdnk
      541 ngkfdemkns nsefnadfia nfnkqfgdls ltgilganyr dyqfetntlg arglnvlgvy
      601 tisnkigday tlmdhskgrs nsvyaqanlg wrdqlyldlt arndwsstlk ksffypsasl
      661 swlptasfeg lksdylnfwk lrfnivkvgn atrpyqngny yyaqtdsynn laqmyksmty
      721 aieglepeai tsyevgtelg lfkdrlhvdf tyynktnkkq llqvatsnvv gfssiflnag
      781 eikskgvelq lrgdilkred glnwtttvnf srdknkvvel ypqldlkdyr lgwtwgisnm
      841 asvgkpwgtl vgsgfdrvek gpmkgaikvg nnglvstpld gqdigqavpd flasmrndft
      901 ikdfrfgfml dfrkggdvws qtmshgyttg iaeitaangi reraivagrd vmtnerfams
      961 dgkdgwvent ietsaqdwye nggiaemyvf dgsflklrea yisynlpkhl yskikgikra
     1021 nisvtgtnla mlwvhksntm rldpeaggvs sdsrgvgfeq atvpnsrsig lklgftf
//
LOCUS       WP_121124143             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121124143
VERSION     WP_121124143.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110964
     Region          58..975
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrlfcflfl fpvfqksqah twlnwnaqkd tseisevdqq llrgrlktll kkqgvrdsln
       61 tsnietlplv sitqmlkgqi aglyvqeatg epgapknmil rglgspvfet kdavnvqptv
      121 yingipiard nnftysiqqy qfnrigpatd nfagldlsvv esievikdpi vlaklgplaa
      181 ngaiwiltkp gkegkreisf dayvglatkp avtpvnaqye nlfrstfynk ygtasdrlny
      241 pgylsdstni nyygpanwne eyykvtpiyg gnlgirgggd ranfafmggy mknassadkt
      301 nierynalfn vnmapfkwfn fgttvnasrs lrdrnrslrd rfgeaayvpd lsipispnke
      361 mygqyldiyk raldnnsvnm lnllvnldly llpnlkfntn lgidysegsr qaffpgslme
      421 tnnymsgyfg fnerltfnns lnynftlqqq hkfnfilgsn ytqdlyryhy araydgpndf
      481 ikvnvvdgdp nsgdylkpig glyvnrwtnr edfrlhsffl sgmyswkdkl dvnavlrydg
      541 sstmqpdsrw lmtpafsaky hlinpeehav mdnlnikasw arigkpifts kyavgpnyta
      601 dlnwgseksl vsyngfavas rpysegwvgy dikwpytdht eimldgsmld krlnfaiaay
      661 qkkdvnqlan mpipaeygys gqivngmtvq nrgidldlni nvlsnpeglq wntalnlnwn
      721 qnkltalpnd kqelkinnrl lrvgeavdkf wlyenegiyn tetdipvrng qklqfdgvdf
      781 aagdpiwkdq ngdfkiddkd rvlkgnampk lvggfnnqfk fkgfdlnmqw yfavgqkaln
      841 qrastkydfi ntentnsldg irevfhwqqd vditkyptyn pwspivsyrv dqdlflenas
      901 flklralsvg ydlaqlnsik dkmktirray vylsgtnllt iskfsgtdpe lidfngyytg
      961 yglpmspivt mgikldl
//
LOCUS       WP_121124151            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121124151
VERSION     WP_121124151.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118031
     Region          26..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqlcilifl fanvltnsvl aqtgmvkgtv kgannrplag vsiklenpkr dlgktgddgr
       61 fvismptngv mvfsyqgygt vkqpvtagkt eynilmeske qeleetvvvg yqqrkretlt
      121 gsvvtisgke iqdipsgnfv dllqgkvagm niqnntgspg mrgtiavrgi snfnvsgsgd
      181 ntfltptspl fvidgvpidd nsgyeygfet agpgvspism ippediedit vlkdaqatal
      241 ygsrgaygvi lvrtkrgnsk iplvqyqgqf fmsavpqlrk viggrdermv rveqilmndt
      301 tlaaairrin dspmladsln pyynnstdwq syfyrntynq thnvnisgge rvfnykvnmn
      361 yydengiian tgfkrytvqs nmqyepndrf rmmanvnanl aqnqmgsgna amqtgvgksv
      421 nttslypaps lfsgsmgals alnvddqnkt gnyvaqvelq yepiiglrat stfnynytts
      481 tkdrytpell lgnsseiygy ydnkskvynr nllswvkaik ekhvinlygf temeisqsss
      541 tlnkirgtan dqfqagisyn trqtlgglln nltnyrsiay agnasynyds kyivdltyrv
      601 dgtsvtggas pwtsnpsvgf rwnfkkekfm erfswwdtgf frgsvgrtiq ptgtlsdlyg
      661 wykvdagryn nrpttsldlk napntelvpq tttqwslgme lgffnsalyl tyetyykqsd
      721 kilrskaian hnafenvltn eaamvnmghe vsinfrprlr ngdwdlsgta tfalnrdytt
      781 alpdgvrqli qpdntsgynl pqffrlgrnp ltfvlydykg vyktddevpv npltgqryra
      841 ggefsagkff ragdpiftdi ngdyildend lvfvgnsqpa mtgglsvftr yknwslrtqf
      901 sytldrdiln taltdrfrny dtptgviegk pdyvpgayvp ldaynvwrql gdnadypnvs
      961 dftrltlynp yrynstmfle dgsyvkinsa tlgynfdrkw iqrygltsar inftanniyt
     1021 fsryagpdpe lvtsvgrdgs ngypskrtys lgvsvqf
//
LOCUS       WP_121124191            1121 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121124191
VERSION     WP_121124191.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1121)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1121)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1121)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1121
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1121
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126035
     Region          119..1120
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrtnyylkl mggallfqsl alqsmasqfs asegigkila rmeqkfnvkf gydasisdqk
       61 inatanvdhl kkdqivqfiq tisdgnlevk kiddklyvvs kkniavsrne ngrtinaqke
      121 vrgkvvdqet glpiagvtvr ikgsnlastt dqnglfklsp atesavlqis ylgyetvdip
      181 vaqagtvklv kssealeevv vtalgikreq ralgyatqsv kgedltrvkg vdvgttltgr
      241 vsgvrvlnst efnktpeiqv rgltpilvid gvayenmdlr dvpvdniqdm nilkgatata
      301 lygskgegga imittkkgla dkgteitvnt nnmffsgyla lpevqhsyss gesgkfnndd
      361 yvwgdkldig rtaeqwnpit kayevqqlts rgknnfknfl epgfisnntv sftnqgehgs
      421 irtsinhiyn kgqypnqkln ltnisvtgtt kindkldlea rlgynrssss tnfgsgyndq
      481 gyiynilvwt gpeydlrdyk dywlvkdqsq nwmykgwydn pyliahekit pelinkvnaa
      541 vtlnykindw akfmlrsgyd yygknrtqrn pigiygtrgg fsdfrndlsv fggfdskgky
      601 vkandngfst tndailtgkk sfgdfgldgl lggsifyssd qtlvtgtmng lsipgfyslr
      661 nsigpvssve irprqmrngi ygrlslswrn alfleatgrn dwvstltken rsyfypslsa
      721 savvtdllas kpmwldmfkv raswavtksv ldpyevhsaf tvkgnvwngm ptasypniik
      781 dysisptqrd ltefgfdfam lknriygnyt ryyrllhnqi vkakiskttg feerlintke
      841 eemtkgheit lgttaikrvn fqwdatinls qnlryfhkld peyskdalyv kqglradyie
      901 ykdwerapdg qlvlnssgmp isaqyanqlv gytapkwfwg fsnqfrykdf tfgfsldgri
      961 kgmsystmna rlwqtgshpd sdtkfryeev vngnktfiap gvkivsgtvk ydkygqited
     1021 trvfekndqv vsyegyykra ysgrwnywde tfiklrelsl syrvsdkfas klkakkasvg
     1081 ltgqnlllwt kefrfsdpdt gsedlnspsm ryigfnvnlt f
//
LOCUS       WP_121124226            1157 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121124226
VERSION     WP_121124226.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1157)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1157)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1157)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1157
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1157
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129586
     Region          172..1151
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkftltpfnk rekdfhsttl aanavpnpwr syekhspffa rplsrslmri nlitlmiglg
       61 lsqvdantya qqitlkkqka sleailkkie kqsgytffyk kneinqvidl sadikeapfk
      121 qvlniifnka nlsydffdkt vvikkrttap slhaittisp ekvvntsiqh gikgrvvdeq
      181 gnpvegasir qkndekrsvk tnadgvfnlp italneilvi sfvgyenqei katlsvsgml
      241 vklrkkdnti eevvvtgtgi nrnkdsftgt ttkfsgaelk avsnnniiqs lktldpsflq
      301 iennlagsnp nvmpvievrg kssipsstlt dqfgadpnqp lfvldgfptt iqtivdldmn
      361 rvasvtilkd aastalygsq asngvvviet vkpkpgelqf tytqdfrfem pdlsaynmmn
      421 atekleferl sgrynssssp tqqvyldsly nqhlsfvkkg vdsywlsepl qngfstnnsi
      481 naaggdetfi ynlglnyrkg kgamigsgrd sysgsinlty rknkvninni tyirgnktte
      541 sqyglfstwv ntnpyyeknw enpyleisrk snssvdfyia nplydamlpq ynksknlevq
      601 nnfnanydik sylranaalq mtkgttegki ykspemsdff etptlrkgry tdnrnnnfsy
      661 qgnfmltfyk tfaqkhqlna nwrntiaenk ndayttvaeg fpagntgnpr faysylldga
      721 pvassstyrs vnttlsanys ydnrylfdvv yrldgstayg snkqfspyya vglgwnihke
      781 afakkmpwin slrltgnvgi tgnqnfanis sislynytst nynqfgqgvt lnmlgnpnle
      841 pqktqqists ldfslfnnrf tgyinaynkk tdplivpvdl psstgvfsyp ynignltykg
      901 letkltiypi ynlekgitwn igltaasyks qyggfgdilr tlnkqqetsk slvryidgns
      961 aeaiwatqsl gidpttgkev fltkdgqytf dysaadvanv gntapkvegv istnlrikgf
     1021 tfglglryrl ggdifntalf dkveninftn vvnnqdkral ydrwqnpgdi aqfkaisqta
     1081 ttpissrfvq slntlssetl nigylfdksp wlesmklktl svnlmandfl yfstvrrerg
     1141 isypyartfa fsfrasf
//
LOCUS       WP_121124291            1042 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121124291
VERSION     WP_121124291.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1042
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115414
     Region          44..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrgsmhaqal mtlaltlnls ptiaksgnsi ssanygysfl glqqtirgki ldeqgqaigg
       61 vtvrnltagt taqsapdgnf siaakpgdql efssigfdrq tvsvngsapl aitlvnrstv
      121 ledvtvtgyt nysrkqsanv sttvkakdle qvpmasvdqm lqgrvpgmsv massgqpgat
      181 asvvirgvgs ingisdplyv idgipiatse lknfsandfe svnvlrdatg kslygsrgsn
      241 gvivittkkg ksgqltvnfn sqyglskltr pkfqmmntqq rlqfeeelga fvdpdnnegi
      301 gpgwtyspkn pdvaggtaay karaaqilds lrginvdwrd yffrngkfmd qqvnvsggge
      361 hvrfyssagy ykqegvavrs gldrytlknn ldfdkgklsg gvnvtlgytn skftegvgas
      421 rvgssmasvy yalpyeypya pdgtlihfgn eddyfildqr egsaglerll nssssselfn
      481 tnvglnlnyq llptlkvhtr lgidyntttg qdyinpdsyy gsrdrdptlg gkglfaednl
      541 rstnvisttg ltyqntfyer hnlelsayfe ylyrrnrafg ykgygidsrl penpngvtvs
      601 paylpailgg rtkyalasym algrytydnr ysltasyryd gssrvaeanr whgfysfgan
      661 wnikeeeflk snefiqglsl rasygttast ingdfnylat frkditygge tairpydpgn
      721 pnydweyvde fnagfdlelf pskrlrvamd yynkitknmf fdqpisltsg fldrklplst
      781 gkmrnrglem slsgdvvkta dwgltlgvna synkntilyl sdaltevldg dtrimrvglp
      841 ygtyyapewa gvnpqtgdaq yynrdgsvtt eydetaqavt ksgsmfpkwv ggfnttirwk
      901 nlsldalfaf vsdvrrwnne dfynensgym tsnqsirmls drwkqpgdna ilqridiprn
      961 ytskdiqdas flrlrnvnlv yqfpktlfgd qkvikgarif fqgqnlltwt swrgldpens
     1021 egisrfnypa prtytagfsv nf
//
LOCUS       WP_121125121            1178 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125121
VERSION     WP_121125121.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1178)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1178)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1178)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1178
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1178
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132047
     Region          149..1176
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtnrsnlmsa lldkvahlvp ingdgknnlk kvlfewdkky pldcivyslr wimsactpvp
       61 mpksvkgviq lslnlyflvf naiiclskal knkhallila clcfnkvicl skalknttml
      121 ltciavfhmf slsaqtprkd sgadgllsis givlssvdgk piqgvsirve gekgrassnk
      181 dgsfslpvan pkglvsfshv gfkrletsyt agvsmavkli plenqldeve ivstgyqkip
      241 keratgsfvq vdnellnrql sanlldrlng vssavlfdks avsntnqagi sirgrstlfs
      301 ndepliildn fpysgdinai npndiasisi lkdagaasiw garagngviv istkkgikst
      361 vpqinfvanl altakpdlyy paqmtssefi dferflyekg ryntiinngy geispvvtll
      421 ekerkgeisq stleqnlldl sktdtrndle rwyrtalrqq yalnlrggsd rytyfgsygy
      481 drdqqtlstd nnrrhsfnfn sslkladhwl nltnfiqfsd qlsrnnsqsf tpnypyldli
      541 gasgealavs dgtlnmayaa npgsnqlldw syrpwnenna nysaatqsir igagleikpf
      601 dwltgkteym lqrsnsqnel lygkdsyyvr nmvntyshld plkntlirpv pwgdmldqts
      661 lntvsksfrt sltvdkwigr khsingilgw eirddnasry rnyfygynee trvnqnaaid
      721 yvstypfwfg ngsgrisnnd nstasvdrfl syffkgsysy dnkyilsvsa rkdesnlfgv
      781 ksnqrgvplw svggrwnain hsrserklls rlalrssfgy sgnvdrslsa yltaqpsvgl
      841 tpwnannltv vnppnpslrw ekvknwnmgl dlalyndile ltadyfikdg ldlmgtslla
      901 pqtgvtqfrg ntastrtqgl dlilkstldf nkvkwtmslq psfmrskvik nyvsnrtnas
      961 iasnnrenpq edypyfalfs fqwaglddmg npqgikdgqp sidyasllna ndlgqliyhg
     1021 slsptsygnf mhtinyrnfn lsfnlvykfg yyfrrnnvfn gssvsyrqeg fsdrwqeqgd
     1081 enatfipsls yplnnnrgtf fnlserlvep adhirlkdir igysfrqlpa gikslelfgt
     1141 vtnvgllwkr tkvrqdpdfn niipapkiil lganlnin
//
LOCUS       WP_121125159             996 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium].
ACCESSION   WP_121125159
VERSION     WP_121125159.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium
  ORGANISM  Sphingobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Sphingobacterium"
                     /db_xref="taxon:28453"
     Protein         1..996
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110025
     Region          36..995
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrsinltkkr inwcglivls tallpcpgya qeqvalkgrv egqngkplsg vtiyskttak
       61 gavtsndgef tipsaaadtl tfsfigydtq kvgvggrsnl viklipnneq lsevvvigyg
      121 qqrkgdltss vatvtsenfv kapvqdagql lqgkvaglsv gttsgnptgg sqillrgntt
      181 lfgansdplv iidgipgtln tvapediesi dvlkdgsaaa iygvrgtngv iiittkrakg
      241 qetnvidyag svstqsilrk pqlltasdyr qqisegirda swdlgsdtdw lkeisqtplt
      301 hihnltfrgg ssktnylasa nyrylegilk rsdnetfsgr idvnhtmldn klkfnlslln
      361 qtnsftqtqd ggtfngytyr qalifnptsp vynekgkwfe qpsnfnyenp larlyesdgq
      421 trsvnsrmag titynpiadl klsslfsysr nnitagyset knhisnlrds rngyaalgnr
      481 liidrlmelt aeytktigkh rgsilagygy qenensssfi qnwdfptdvf gynniglgna
      541 ikdgkgaigs dkfetnlisf fgrltysydd rylllasvrh egasqlvgak spwgtfsais
      601 ggwrisnesf medqtvfddl klragygvtg nppsnlflgq aqlgyggyiy snghwvqslg
      661 ptsnpnpnir weekresnfg ldfsllkglv sgnidyyird ikgllydyqv psppnlvttt
      721 ranvgtmrnn gievllniap vrkpnfewnt sllfstntnk lkslsnelyq ttndyfttgg
      781 tgepiqtftn ivyigqqigd fygfkavdid dngkwiyega dgarvayndf ghtfedkkvl
      841 gnglpkyyag wnnnfrykni dlsvtmrgaf dyqilnfqrm ylenpslqny nrlassedlv
      901 fgkakltapl efnsyyiedg dhwkidnitl gytfrnmksk wlnnariyas slntfvitgy
      961 kgidpevnrl glspgnddrd kypttrtftf gvnvsf
//
LOCUS       WP_121125162            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125162
VERSION     WP_121125162.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116295
     Region          31..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksrssiqsl vagiacsvfm vqvnplfaqq iqvrglvkds ktglplsgvs irinnqakgs
       61 sdskgqfvlq ansgeniefr ligyevqsqk aqgsmsvalk stegtleevv vvgygtqkra
      121 tltgavetvs sktfedravt nvalalqgqt pgltvtrtsp rpgneglnls irgassings
      181 kplividgvp alndysflnl nsddienisv lkdgaaaiyg sraangvllv ttkkgkgklk
      241 vdyngnfrfn tnglvgysps mqeyatmwle ankeetvpnw wvwgednvrk maqgiegkyd
      301 lyntdfyifn anriqemfst rysyqhnlsl gsgndkssyr lsfayadnqa nlataydgqk
      361 qwnarfnyty nltdklkles nisainants mpsrglgnil ysfdmpfypa knpmgqwlap
      421 fngidagsnr naaattsdag rfdkksltsr vdlratydiw ngisleaaas lqnerytges
      481 yvvpvklynw ygdyvanayn tdgtnntysa gtfnglsqyy eallrynktl agkhnisamv
      541 ginaekfnsq tinatrlgyd dlgiydiglg ktegmtnsgg kslngrysyi srftynyaek
      601 yllelvgryd gnsrfakghk fkgfgsvqag wvfseesfma plkdivsfgk lrgsyastgn
      661 aadnlrdfdy lslvnigtsv lglpaslqtn sglsnnglis ydrtwetviq anagldlkfl
      721 rnrlsatfda yekrnigmlt qvvypsvlgg tapqtnsgkf ytrgwelsig wkdqkgdfgy
      781 nvavnmgnan tkvdqvenad tynagrnnvv ngypfrswfl fktdgyfkdq advdayyaay
      841 gnsealkgle ktnpqktlrp gdtkrvdvag tgnitaggnt qsslvymgda mphytyginl
      901 ggswkgfdln affqghlkqn imrtgymayp fralytnqnp sflghtwtee npnaefprlt
      961 snvdraawny anndfmlqns ryirlkslvv gyslpkslid rvklqkvrvy fsgndlweat
     1021 aikdgfdpet genatdgdna gypfartwsf ginigf
//
LOCUS       WP_121125183            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125183
VERSION     WP_121125183.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115981
     Region          40..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkrrilyys aylllaglae qplvtyaqdt pktiinasfr gqvvdaengq piegatvkly
       61 gvthavttdr kgnfafvtgq klparvvvss vgykeqivli eeqgdtvrll redrtleevv
      121 vvgygtqkrk dftgaastis aeaikdipvq sfdqalagka sgvsislpng llnnppvirv
      181 rglnsislss yplividgip vntgnigtsn vannpladin psdiesidvl kdaastsiyg
      241 sraaggvliv ttkkgkqgra kvtydvwgsa vsatrlpkll nasqyidikn eavlnnkils
      301 gngtndkvas alffpqydan dklvetnwyd hvyntgyshn hslavsgana ntqyyfsgny
      361 sdqegffakn sfdrkglrfn iehkvndwfs lgsnltynnt fndaknsgsl pssqllligg
      421 arlalvlppn vsaykddgsy nlsstgllgp ganlftntly npealfaysk yttgndhilg
      481 nlhaslnllk nlkftttyav drnlsttkty lspnlgssgy tnggsvtnvs slrnnwnftn
      541 slsydqvfae khaltllagy diqkydndsw nasqnnasdp ffenfqgnwt tlsgaggsvt
      601 erfyrstfvr atynynkryf ltanfrrdgn salganskyg dfggvslgws vfeedfykns
      661 slanllgdlr frgswgkvgn gnlsayesln lyssslygta ptwsmsqagd pdlgwetseq
      721 tnfglsldla qkrlhvdvdy frnnvnglil dvpqspskgi pgnsilknvg smynrgiefa
      781 isgdivkkrd ftwnaslnft hvknkvtals dgnadiigyt httteannit rvgyavgsly
      841 gavtdgvnpe ngqrifinkn gervqysaav asgqsnwtyl dgrvaspitv adyqvlgtal
      901 ptyyggfnns frykafdaav nftfaggnkv mngtrgtlld qrfynnsvev lnrwttagqq
      961 tdiprlvynd visngsagfs idqnaekadf lrlqqltlgy tlrgnlfnki gvssiriygq
     1021 asnlflitgy sgtdpesssn gnsntsigve knsigqgrtw taglnvsf
//
LOCUS       WP_121125221            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125221
VERSION     WP_121125221.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124278
     Region          48..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgnycklkqs hrissswllc lvafgspata lnanaalksi trpivqnrei tgkisdgkgq
       61 plsgvtvsvp gsimstasra dgsysisvsp haeklvfkll gyksqeislt gakvlnvvln
      121 ssadeleevv vvgygtmrkk dltgsvtqil pdrianenpk tvqdilrgta gmnigfdasa
      181 kgggsievrg krsvydsnsg hnnpllvldg mifygelsei npddieqidi lkdasaaaiy
      241 gskaasgvii istkkgkqgk ptinmtmnag atqlsnyrkr fnpaaymqhr adwytkntyg
      301 inpetglyea yqtrddngnl avpygfylsp dqlpsslsle swralstnen gesdqsiwgr
      361 rlglqgnalq nflngkavdw adhtfrtgfn qdynasisga sdkvnyylsm gylknegavi
      421 sdtykavran mkinahvnkw lelganvnfq drsdgnidid ldqalrnspy adyadangnp
      481 iqyplseqfs qrgynydflq nyleldkgyt vlnsifnakv klpfnitysf nasprlqyfh
      541 dryfmsaelp gsnpadrgan reqtkrfdws lnntinweht fadkhrlmlt lvqeaeeqqs
      601 wkdriearni lpsdalgfhn tkngskensn fdsydshqta dallarlfys yddrymltts
      661 irrdgysafg tsnpyatfps valawnftre kffkwtdvmd ygklrasygk ngnrqladpn
      721 lalanlyags gkmhgylnsa gelvqyrylm vdrlanpnlq wekttawnfg ldfgflknri
      781 sgsleyylmq thdmimeqkl pnftgfgsit tnlgqvdnkg ieltlntvnl qkdnlkwstt
      841 fsfsynknqi vhlyknyedv ldangnvvgr kemdeisngw figqpigaiw dyqvtgiwqa
      901 neaaeaaryg qapgdpkvan pytaddvvnd agrkpvynnn dkvflgqtdp rfrwamrnef
      961 tlwkdlsfsf niysymghks lsgnylnndd dggrmaygla nlpakeywtp dnptdrygri
     1021 eakgpvgaeg arwlydrsfi rldnisvgyt lpasltsryn lnrvklygtv rnvatwtkdw
     1081 efgdpetfhp dnnpqgwasr vftfgvnlsl
//
LOCUS       WP_121125288            1028 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125288
VERSION     WP_121125288.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1028
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112984
     Region          20..1027
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkhilyllil sltsgnvwgq vvtgvvtdtq kkpiagvsva laesglktst dsrgrfsisi
       61 daalrdaklr fkamgfqpqt vtvnghrnls vvlivstsml devqviaygt tsqrfnvgsv
      121 akvkaediar qpisnpleal qgrvagltvs atsglpgssf kiqvrgqntl pkataafgsp
      181 apmdnplivi dgipfapqne nvnqfgslas pgniallnnq qggfsplnsl npsdiesiev
      241 lkdadataiy gsrggngvil ittkkgtggr tgfdmdvrqg vsfmgktmrm mntkeyltir
      301 reaisndgls pnltlwdnaf apdllafdpd kytdwkdyfl gksasntaft gavsggsqnt
      361 nfrlglglnr tsyifpgdfa dkrmsfssnl hhnsenkkfs ldltttysyg knnsagnanl
      421 ltayrldpnf pdlidregnl rwdyngiqlg mgipdnpisy lhntyqmknt llnsnlllay
      481 kltheltlrs sfgynafhgd eyagnpflaq npylspeats sfgknsygtl iaepqlefkk
      541 ttgrnafevl lggswqyntn ereqvtgrgy thdglitsin garnryatda yseykyvgaf
      601 grlnykyhnr yiaglsvrrd gssrfgpgkr fgnfgsvglg wifseedfmk nklgflsygk
      661 lrasygvags datgdyqyis rwgtssypye gvvglqplnl fnadlswast kklelglelg
      721 fmddrllvss syyrnrssnq llsyylpsqt gfssvaenwd atvqnsglei tlqskniarg
      781 nfswntafnl slprnrlvaf pgletssyat rymigkplna iyafrytgvn petglfefsg
      841 aggeltsnpq rpsgisfndf nyigttdpay fgglqntlty knfqldlfve fkkqtgsnyl
      901 kqvyngavgq eynlpaamld rwqrpgdrae fqrytttfgs dvfkagqsya lsdavysdas
      961 yirfktlnvs ytldkkitea lrvkvlriyg saqnlftitn ylgndpetqg lytvpvlksf
     1021 viglqlsl
//
LOCUS       WP_121125528            1040 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125528
VERSION     WP_121125528.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1040
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113755
     Region          28..1039
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfykktag lalctlfsat slfaqqsisg tvsdakgpls gatisvkgtt ratqsnsnga
       61 fsiqaaqget irislvgykt qeilvgatkt invtltneas aldevvvtam gikrekktlg
      121 ysfqdvkgdq lvdakennis naltgkvsgl qvvkgsngpa ssskiilrgf nslkgdnqpl
      181 ivvdgvpmnn ragnpdknnd fwnpstdlgn glgdlnpedi esmsvlkgga aaalygsrgg
      241 ngvivittks gkaqkgsgit ysstigietl fmrpdlqndf sqgtdgsfvn tttnswgaki
      301 egqnvtnwdg tniplksydn ignffntgin htqniafqqq lnnntniyts atylndksii
      361 pgssmtrlnl mtrvssnfgp nkkwfsdvka qymkmnaknr pisgqnqsnm yntlflfprs
      421 lditqfsdai qpngnmlwfg tgnqvnpywl ekyrlnndir drfllsgslk yqfndwlnte
      481 aklgsdmyyt tidnrtyags plttdgkgsy sfgsnnfyen nymlslnark dnlwgkwgga
      541 asifgqimtt kseykvtdig qlivpnvfnp nngisnpair atpskkqins lfataelsyd
      601 nfwflnltgr ndwssalskk nrsffypsvn tsliltdlit ktggtlptww nyakirgsya
      661 avgndldpyq lvntyklekd pngntvtsre dvkyneniks eliktieagi etrffnnrlg
      721 ldftwyktna tnqiidvpmd pfsgfqrqyi nagnienkgi eislnakiln apeklnwnmd
      781 infsknknri lelsdvtkty nlialenisi kadeghdyge ifgstyqrvt dpssqffgkm
      841 ilganglple gastflgkqn psallgvtns fsykniglsf lvdgrfggkf fsgtnaalqq
      901 agvaavtvvn gsrdkfvvdg vvsdgkggyv nnttevnpqq ywaaignpnl giternmyda
      961 tnirlrnlsl syslpnsilk nsivqrakis ltannvwmik shangvdpes vfaissnavg
     1021 fenfstptar syflnvtigf
//
LOCUS       WP_121125531            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125531
VERSION     WP_121125531.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118733
     Region          28..1079
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mslfykktag lalctlfsat slyaqqsitg ivsdakgpvs gatvsvkgtt rgtqtgangs
       61 ftiqasqget lrvsivgyka qeivvgstka inikltedas aldevvvtam gikreakalg
      121 yasstisske ltqagttnig salygkapgv qinsapggas savniqirgi nslsnnrqpl
      181 yvvdgvmirn dqqagskgln ntggitdpgg qaiwsdnrir gngmldlnpn diesmtilkg
      241 asatalygsd aasgvivitt kkgvkgkglg idfnytgsie taaflprlqy eygpgydaat
      301 nlqsgateeg wmtnplfpgd rllnynawgq fgpkydgqdv rwwdgslrky sankgnygdi
      361 fdtghnsnfn lsisnqteki nyrlsasnmd ykaivpgskm nkstfnlnss ikladrldld
      421 vvasyistit knrpglmgdv lgsyagffsg aedvekmknq lyqtsdgyry npfgsnrpga
      481 fpvnyravnl lnyfwqqkrn syeekenrfl gsatlnwgil dklkfrgrlg tdftglnien
      541 kehneyavqy netnstgkfe vskgiykiiy gdalltyadk lsddfdfsls ggfqsrmeny
      601 ddqmsrtegg lvsanwfsln ntfgqavtth vrkelikyay fgllnlsykn ylflegtgrk
      661 eysstlpakn npyhygsvnt sfvfsdafkl pdffsygklr asygivgnda piyasnlafk
      721 qtslitvngp vpslatnsay gnedlkpekk tekeigldlk flknrlgldv syysnfiddq
      781 implttahst gastqflnvg kisnrgweis lsgtpiqken frwnarlnfs nnkskldali
      841 sgvpklifyd adqssirmea rpgetlgniy vfpratneng eflisdegny vidkstyvka
      901 gnimpkaigg lsntfnyknf sldftadyrf ggqmistphk yaygagrles tleyresgit
      961 ldgvnqntga kndvhlsgae yyinnfywgn nawnekaavl dnnfiklrev vigynlpesf
     1021 tqklklnslr vsligrnlfy fyrsikdidp eapvgnywys qgidigsnaa trsfgfslna
     1081 kf
//
LOCUS       WP_121125727            1186 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125727
VERSION     WP_121125727.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1186)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1186)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1186)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1186
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1186
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131991
     Region          109..1185
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkllvplv clmsttgsfa qkraslsqal sevtriygtk fsyeeglird afvnsdmipk
       61 nkrlpvetvl kellypnnyl flyvqnnyft iirdsrdkrd nhsddrfwkv itgkvkdskg
      121 apligvtvms dghavrtgvt sssdgsytlr ltdpadalif symgmepqrr vigssnqinv
      181 tmeqivnvld dvevvsmgyt kipkdratga fgtvtakqiq etpainvmer iqglvpgmyv
      241 dprtnkieir ginsygtgga prdplividg fpmaenddns ftltnkgntq ssggailsri
      301 npndiesitv lkdaaassiw gakaangviv ietkkgrntp psinfsssls maspadlnkm
      361 drmssaqyid fekqlvdegv igdnieksdw epfntkrphs eslewifrvk rgtataqerd
      421 aaleklaatd nrqqikdyll qnatsqqhnl slsggankst yfvsanyskd vpvfrankae
      481 sfnlttnltn mmfndrvrla tgvnynygns ignsaainal ssnissggll pydllkdeng
      541 nnirryiqfr pevsqdfenk gyldwaynpi eelsaanynd qshairmhmd intkltswad
      601 lsvmgqwqrq lnntenidgv nsygqrnqin igttfndngn yvygyplggr lgisnyngsq
      661 yvfrtqlnid kafgqssqhn lnflagaewk qnsrrsssda ylgfiedtys yavinprgsy
      721 ntiygwdnyf ssngsiaknr dralsyysna afsafngkyv lsgsirfddf tlvgasrger
      781 gkplwsiggk wdakkekflk datwadalgl rltygvngil pksvgrvvvi ntstdnisne
      841 vtadiaypan kqitwekvks lnvgldyaiw nnrlqlnvdy ytkkssdivy sfpfngtygw
      901 tllqfnsatl eghgvdiglr aawlqstvkw ntlfnfgynt nkvtdsrftd pvnvinytda
      961 stpilghptd ylyayrwagl dnqgrsqvyk kngdivnada panalvaedl vemgrttppy
     1021 vgglfntfsf kdftlgvrvt yemghvlrrl svqnypdyag ysgaigmqsd lakrwrqpgd
     1081 eaftnvpgls tqgyqynsls ryansdalvi sgsnirlqqi dlgynfpfkt lehtpfksvn
     1141 vnasvrnlgl iwrknkdgvd psyrtlnsys nlppsptyfl slnvsf
//
LOCUS       WP_121125717            1206 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125717
VERSION     WP_121125717.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1206)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1206)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1206)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1206
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1206
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134609
     Region          125..1205
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkitenrwqp ircllmvpvt sllftagqqt faqqklslkq aikqieqrfn anlsyehnll
       61 ngktvdpeml kgnrleevlk kvlypnqlvf lyvdersysi vrrsaedrda stvrygtdpe
      121 mmdrvagtvl saggkpipla svwvkdtrkg aksdengrfl iydikptdvi mitavgyest
      181 aitagnrsql tftmqekdhl leeavistgy qkiskeratg svslitakel ekipsanliq
      241 rlegqvpgvq vtigtgdrtf tynnnqlgiy sstrtigqnd ygltvrgvgs idsdtekspl
      301 ividgaissi dlamlnpndv dnitvlkdaa aasiygvraa ngvivvttkk gsvtgvpkin
      361 fsmnttfsgk pdlgylrtmn saqmidyqee lvaknilngn niatnlysys tyypgevaaa
      421 airlkngqmt qadydalvnp lksidnrsqi qqyllrpmss qqynlsisng tennnyfysa
      481 syanenpytk gengkrltln lnnnwklfki atlstsirgt ffrnrqngig lsqiydtggs
      541 tllpyqllad ehgngiaydr ltpgfvdvlg paykdwryny lqelelmdrs lknnnysavi
      601 nlaipiykgl kgsvmysner sfgnnrtyng egsyanrsll nrftpigast nsiginkggi
      661 nniintdvnn ytvrgqlsyd allgqkhdis aiagseirqt etgqgnityy gynmqtgfnt
      721 avsylpnayp siqgfneslg gapqqadrrr rflsyfsnaa ytydgrftfs gsvryddynn
      781 fgldrsfrat plwssgfkwn lrkesfmnsl hwlnqlgfra tygvngnitq dvrpftyisl
      841 ddasrnptaq psasiiaian pqlrwektyv tnlgldfgll dnrlsgtldy yvkkgrdlly
      901 gfpiaapyvg tinagslkrn tatmsgrgid lglngillrs adwqwdmtan fsyntnkitd
      961 nrfdpadist ftysytpigi sylegypsdk lfafrhagld angltqiynk egdivsvket
     1021 lksvddlkym grtvapyfgs lktnlrykqw sfyalmtyqf gsvfmkpsie symtpsrgft
     1081 lpkfdlsadi adrwrqagde vttnvpavta diygqyslyr ysysdinvlk gdyirlreis
     1141 lsyalpkdfl rrikieqvsl tgsvrnlgli wtankegidp dfanyvgntt nlrpvpsynf
     1201 sinvnf
//
LOCUS       WP_121125793            1077 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125793
VERSION     WP_121125793.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1077
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117143
     Region          24..1076
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqtllsflv ggmiltsvaf aqekkisgrv tsadgkaipg vtvvvqgtnq atqtdadgny
       61 slnvpagkvv vfrsvgfddk tiivnnnstv fnvslsgqdn aleevvvtan aikrekrtlg
      121 ysaptinsee ltsgrnasai nslagkvagv nitstsnspg sssrvvlrgg ssiagnnqal
      181 ivvdgvpidn ssviggassl asvdfgnrgn dinpddiasv tvlkgpaaaa lygsrasnga
      241 liittktgkq gggktdisfs ssntfssilk lpdfqneygq gastydskgn lvfvddpken
      301 wswgapftge mkewgqaidg krlskpysav knnvrdffst giasdnnlsl sggsekstfy
      361 lglnslnsng vypgnkdtyn kygvrfngtt efsnkfyagi sanynkinsn nigggqgdas
      421 vynnllqtpr dipvtdlkdl nnpyfgygyv gadgvdhsdr fgyygaytmn pywvlqnynn
      481 yndvnrvqgn fnvgykpfew ldikervgvd hysdrrrses pkytffpadn ttdnysdsnv
      541 rtsngqyrld qynvtevihd fmvtanhkfn edfdaslmig nnirqryatv nstatnasgg
      601 lvksgwynla nslgpldlie dswekrrlvg vyadlnlsyk nflflqatar ndwsstlpkk
      661 nnsffypsvs ssfvfselms pdakrilsyg kvraniakvg sdtdpykllt tyrrgeidgn
      721 fgsttfpfgn vyglmansti gnselkpeit tsfevgtelg ffqnrlsvdf tyyknsskdq
      781 ilsipianst gfgfsvvnag kitnngvela lrgtpiktqd ftwelmgtft knnnkvvelm
      841 egvdqvtlgg fsgmsivaak grpygefyai anqkddqgrt ivdqetglpi ptteaqylgs
      901 ynpkfqaslg ttlsyknwsl ntlfdmkhgg vffsrtkdim aftgtsaetg gerfaqifpn
      961 svyldengns vvnttakydk vdyypyleag envvdasyik lrslaisykf kkdqlkntpf
     1021 gdvtvglfgn nlfiwtpken kyadpevnsa gagnaqgfdy taqpslrnyg vnvkvsf
//
LOCUS       WP_121125866            1112 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125866
VERSION     WP_121125866.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1112
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125040
     Region          22..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkflipltf mcvqmaqaqe skelkgkvld avtlkpvvga tvvvessava edigvpnqvq
       61 qsalgsltda sgefrlkvpg nlkyvtisyv gyqriqvpvf qdhrtillqp sgesldeviv
      121 tgytdikkrk nttaynkinv adikqtgvas idemlagqva glqlsnfngg pnsapqirir
      181 gtvslngtqd plwvidglpi egtelpnrid kdnlnslnnl piaginpddi aditvlkdaa
      241 atsiygaraa ngvivittkr gksgpaklqv santfvterp dfgklnlmna nekvdfellm
      301 anrtdlnyrt gkgavmrild kanaleayrs gglaalspev qqsinqlrlq qtdwgkelyr
      361 qalnqqysas isggndahry ylssgfydek gatkgadlrr ysltlnndfn indrfkagin
      421 llgsvsnrrn piqdddaftn psnymrlvnp yltvrdqsgk ynydpdiegy ekdtyisfna
      481 ieerentkya ltnkalkaig yleytiipql slrtefglqf densmerfad qesyntrklr
      541 aatryydsvs ktfkyflptg gkiennhnsi fqynwktylk ynktwnekhe lelmggtelr
      601 rskntmvssk gfgynpstlt tqnivfpnsn yqddkrfnpy kkgfiensya sfygnatytf
      661 drkynvygsi rydgsnmfgv dpqyrflpiw slsgswnvle eefikgktal sdlrvrasyg
      721 iqgnvdrnty pfivgnydns tilpgypegt vvvgmpandk lrwertqsyn agidlglwkn
      781 rlnitvdyyn rtskdlians alpmengfqd vqvnwasarn qgveltitsr qiqtekfsws
      841 tdfniahnnn kllkvmnnpk ayapetqegr pinglyvlet agldkdgvmq frnqdgsvss
      901 feefyglydp waeflpgyms qtdmtaavyr skfkykgskd pkftggmtnr fryanfdlai
      961 savfnlerwv nraptynpal vdrgqnytkd llmalqgnka lpalgsisse lndrwmaygw
     1021 mesndpinsf kqydiwakkm syvrinsirl gytlpaglsk kigannlrvn vegrnlfvfg
     1081 anyegyfdpe tygnyyaqpi sksfafglsa sf
//
LOCUS       WP_121125860            1044 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121125860
VERSION     WP_121125860.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1044
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114302
     Region          26..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 maknnidfvv laalclstgt lyaqstikgk vvdnnsspiq gatiteiisk kqvqtdangl
       61 felpsnsnsi siqvqyigfd sktvqtnpng lttiqllpas sqldevvvta lniskekktl
      121 gyaiqelkgk dlseakesnl vnslagkvag vqitnsqgnm gssriiirge tsiagnnqpl
      181 fvidgtpvdn sqlgtsgnrd yanaisdins ediesmsvlk gpnaaalygs raaagvilit
      241 tksgkkrkgl ginvnsnnti erlavlpdyq nvfgqgadgk fsyvdgkggg lndgvdeswg
      301 pkmdgrlipq fyskgeavpf lphpnnvrsf fgtgrtlnng isiadatdki dyrfsynnsn
      361 qtgiipnssi eknnfnintr ykitedltlt ananyvrtns gnlpgvggfr sngymlqftw
      421 fgrqvdvarl knyrdengnl vnwnnsyysn pyfiaeentv qqqrdrifgn vglnykinkf
      481 ltanfrsgnd yytdrrkiri aygtngtpyg syeedaytvn ennteftlny nrplsddftl
      541 dilgggnirs qsrqrnnqka prlavpdvyt lansrdalis tseysplkay svfssaqlgy
      601 knyaflnlta rndwsstlpv dnlsyfypsa nasvvltdaf piqgdilsfw klrggwskvg
      661 kdtdpfnlid sypfstpfnn npilsvndik knpdlkpett tstelgtela ffknrvrldl
      721 slyninsinq ilavdvspst gykkqlvnag kinnkgleiq lgvtpvkken fqwdinvnfa
      781 tnkskvveld ekgllqsyii gssgtvqvla avgkpygtly gtgflhdsqg rlvlsdgtpt
      841 adpvnhyfgk ftpdwlggit nqfryknfdl sflvdikhgg klysgtnatg rgtgvlastl
      901 pgrdaehggl nyttvdkltn etiahddgil vdgvnadgsk nttvisaqqy ykalyrvnep
      961 nvfdasyikl revklgyqlp ghwvskigfq gasfalvarn lwiihkntpn idpetafntg
     1021 naqgleslql pttrsfgfnl nfkf
//
LOCUS       WP_121126037            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121126037
VERSION     WP_121126037.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112149
     Region          33..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mivhihsnrr vaigttlgcl flwtgiaaaq tttikgkvss ttdqtalvga tvsnlmnkla
       61 tktdkqgnfs isanagdklk isllgfktie iavpatgdlq vtletesqqm eevvvtalgi
      121 krqvrgltya tqqldgatvn nardnsgnvl ssltgkvaga vvttaatgpg asarvvlrgn
      181 ksitgnnnal ivvdgvpydn ssaqqasgtt ynygtsdgaa ninpddiesi nvlkgpsaaa
      241 lygsraanga ilittkqgra gryqidyngs asldqvnlls rfqnsygrgn ggvtgtnvge
      301 swgpqgrtyk nnvrdffena atfnnsvsty ggtekvqgyv sytnnkiggi ipgndlkrns
      361 lnlrvnteli pklktdvkln yvnqqidnrp rlgdmgipve vyvmprdmdk aelqdyetid
      421 pvtgepqrky wsgsavydnp ywstnrtsvn evrdritamg satyqltdwl nvmgrfsydk
      481 yidktdgsfy agtvsigdvr pggkyfetha ryqernfdll fngknsisea vkitynvgas
      541 sldrryssfq nmanglsipn efslkmattp efllingyqr rlnsiygsaq laffdnifld
      601 mtarndwtst lksphsyfyp sigvsaifne wlklpawvsy gklrasytqv gndpdpyllq
      661 qlysfglgag kgfisrspik mipelkpelt ksyetgldmk ffanrlgfdl tlyksntinq
      721 lltlglpmas gysrqyinag nienrgievq ltasplkken lewqttvnfa antnkvielh
      781 ektkratite ntkyasvvvn egerygdlyg ykwkvdgqtg kyvvdnsglp vveanqklgn
      841 fnpkallgws nsvryknftv nalidtrigg eivsgtsayl aafgvadyta dyrdgglvld
      901 avdasgaant kaitaqqlwt rvsqngrdaw gefftydmtn vrlrelsvsy kfnlkntaai
      961 ksaqlmltgr nlfffyrgks kldipgigkt dnpidpeaal gagnfqgvev glpptvrsfg
     1021 lnvkltf
//
LOCUS       WP_121126316            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121126316
VERSION     WP_121126316.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111662
     Region          24..1019
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqtllsffv gsmiltsvaf aqekkvsgrv tgadgkplvg vtiavqgsnv atstdangny
       61 tltvptgkvi vfrsvgfadk tlivkegqts fnmvldnkdn aleevvvtal giskssrgig
      121 ystskvsgdd lvksgeanii qglaakasgv qitssagtpg asskivlrga asftgdnqpl
      181 ivvdgvpidn glnntkagdd pynqslsgvq vanraldinp ddietvtilk gpaaaalygq
      241 aagngaviyt tkkgklgsgl gitfsssyem qkvnklpefq kkygqgsggt ytdrtadswg
      301 enliaagkpi ynnvedffkn gnvfnnnlai tsggekttmr fsvgstnntg iiphtsynry
      361 tsrlnaeskl ndritvggnf sfttantraa qngsniagvm lallrspvdf nlkdykdelg
      421 vqktyfasyd npyfsternp ykeennrflg nvyadiklnd vfsvswktgl dsyatngnqi
      481 ytigsngddd sagwgeikrt nvnyrniytd lllkfnkkis edfsvsgllg gnfnyvqsia
      541 nfargknlli pdyynlnnar tlyasnseey rnskaiflda tfdyrnilfl tltgrnewst
      601 tfgrnakgff ypkadisyvf sdlfkdseiv nfgkvrlays nvgispkpys drtyftspli
      661 adgmtngysf pyqgqlgfai snefiaenlk pernvgyeag lemkflnnrl gfdftyyqqr
      721 asnllismpv dptsgfayyy nnfgkmknsg ieltlnghvv ksenfnwnat lnwsknsnev
      781 telapgvdkl sigdafsspq sfaivgqpfg viyaqkfqrn aqgqvlidpn sglpmyesdl
      841 gnvgstipkw lmninnefsy knwsfsflwd frkggklwgg tnavlinrgk aaitedrerk
      901 yvidgvygsg snegqkntte ltafnyfkny lgnsssevsi qdgtwarlrs idlnyrfnkv
      961 skaiqyiqvg vnlrnpilit kykgidpets ltgsdqnfag ydffnnpgtk sysinfrvgf
//
LOCUS       WP_121126809            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121126809
VERSION     WP_121126809.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111547
     Region          31..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlkktnpqkk nllvlallsa glghvhaqqd qvkgavqner geflpgvsvk aiqvnggqsv
       61 ttstnsqglf hfqnlvergg yqfvfsavgf qadtlsgfvi earkplslsv klqqssvkld
      121 evvigygrvs rkdvtssist ikaedanvgv ftspaqmlqg kvagltistn nsnpnatpsi
      181 slrgastlrs geamepyyvi dgvpgaslal iapddiasid vlrdasatai ygskaangvi
      241 ivttkrgksg qtnisyngyl aidkvakhye mmnaaqyrsy vkdngfsmep tddlgadtdw
      301 qreverigvs nnhnisilgg tektqysisl ntiknngvik gtdmgrqiar aflqtkalnd
      361 rltasfnina sitkqndvla ldqglsvydg myyylpvspv kkadgswfek pdrsqyanpv
      421 slieentnfs ktkvlqahak lgyeilpglk ynidlslqnr qfnnaqynsm fsmaargqng
      481 ksiraavede rkvmemnlnn ektfagqhkv salagyswee nnnndgfqlt tsdyynddls
      541 yynpgmanvv dllgfgnyyl stlrmisvyg rinyaynsky lfqatvrrdg ssafgtnnrw
      601 atfpsvsaaw rlseesfire mgifddlklr agygvsgnsl gfdaftaqsv qgasskffdy
      661 vnaqglispl rtlqvlrnsn pdlkwettsm inlgldfgfv nnrltgslel ykkktndliy
      721 dyqvsqskyi fpiltanvge ienrgieltl nakaidkeqf kwntglvlsh nsnkvvsian
      781 qqftqdyiel sdlggagqsn ffqqrltpga pigqfytwew agyndngvsv fyardektge
      841 rtgettitpq kkdqtvtgsp qpkltlgwnn slsyksfslt gmfqgtfgqk ilnatrarhs
      901 nvvgnagqkn llasvleter mtdinahyls drylengsfl rlayvtlayn lpvknipvkn
      961 lkvyatmnnv fvltkykgid pevglggltp gidnrqtypr trtfmfglnf nl
//
LOCUS       WP_121126823             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121126823
VERSION     WP_121126823.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108853
     Region          41..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkgfafkssl lglsllsclg etqlqaatga esrwiglmqq qdirgvvrne qgqgmagvtv
       61 lvagttvgts tasdgsyria lpkgksqllf smvgyssqtl tvagttlnvn mlpagnvlee
      121 lvvvgygstt kkdltgavnt vgskdfnggl vgspeqling ktagvqvmsn sgspssgsti
      181 rirggaslsa sndplivldg vpletggisg nsgnflslin pndiesmtvl kdasstaiyg
      241 srasngvlli ttkkgkgdal rlsfssivsm qqalgvadmm srdefaelin skgtaaqkal
      301 lgnsstdwls evfqqamgtd nnlslqgkmg kvlpfrasvg yynqqgtlrt dktermtgal
      361 vvnptffnkh ltvnlnvkaa rnnnsfantd aiwsavafnp tqpiysgvda yggyyegldn
      421 aglpatganl nplgllkqek hrstvnravg nldldyklhm lpelkahvtl gydyakgngs
      481 nlipasaann ftvggafdry eqtlknrlft gylnynkffs dikstidvta ghdyqywsak
      541 rppivyynea gdnirstaia sderhtlisw ygrinynyds rylltatirk dgtsrfspen
      601 rwgtfpsval awrlsqesfm kgisflndlk lrasygvtgq qegignyeyl pvynlgtaya
      661 qyrfgdqyhl vyrpsvynrd lrwettkafn ygldfalwkn risgsveyyt rkthdllanv
      721 pvaagtnfdq natinvgnve srgfefqlnt vpvekdnlrw evnfnatnqh tkvtnialvq
      781 danavgtyvg pnvsgrgiqi lttgyqpnmf yvykqlynea gkplegvyad lngdgainek
      841 dlyryqspaa kwlfgfntql tykkwtaatt lranvgnyvf nntkmnlsaw etlqyvdpai
      901 nnlhrdyfnt gfqtrqyysd yyvenasflr menlsvnynf gkvgkisslr vgavaqnvfi
      961 vsnysgmdpe vpsgfdssfy prsrtfslsl nldf
//
LOCUS       WP_121126847            1097 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121126847
VERSION     WP_121126847.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1097
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123287
     Region          56..1082
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkklklqan ssvllqiqil kitilvilyl lvsmfslsaq tprkdsgavg lkqellrgtv
       61 vssldgeplv gvsiripgek gnaktdktgn ftipvtnrkg avalshigyn dqlvdyqvdi
      121 klnitlflke ntldevevvs tglqqipker aagsfefvdn kllnrkvsmd fisrledvvp
      181 sistvkmlde nrgkfpninv rgrssissni wplivvdgfp ysgnfnninp ndienisilk
      241 dasassiwga qsgngviiit tkkakrnepf kvsvnanttv enkpdlyyfp qmstsdfidv
      301 elmlfekgfy nsrmydrmyt mtpvvqllkd rqegkltdaq ltdkinalra idmrddfsky
      361 iyrkavkqqy nvqlagggqk lsnifsagfd knrgavvtns sdrlsfrnqt aykpidrlel
      421 nlstqytqyt tkdamvpiky nemgagygny pymrladeng nplevetvgl srdfrdtvag
      481 grlldwnyrp laelyetqik dntkemmfsf ganyqilpel rlsllynfrk adskqenwrg
      541 igsmhqrdei nyfaswdkqs vtwnypvgdy lyilngssda qqgrvqldyn rkftdahevn
      601 vllggeirqd hstahssvff gydpttlsyq eadlvhdhpy lngilgvrki nnyprlaevt
      661 nrftsyfana sytfkqryif nssmrkdasn lfgvsandrg kpfwsigaaw llsnesfmtd
      721 gpfstlklrm tygkngnvnn atsaypimlr stqnhfltgl pyasmqsppn pdlrwetvgm
      781 fnlgmdfslk ggrlsgsaef yiktpkdlis atqidpttgf aslnvnsanl kakgidlsih
      841 svnisatdfs wrsdlafsyn rtkvtksyla dqlgryyrsg aysmnvtpie gadlnsiisy
      901 kwagldpqtg kprgyengei stnytsivng tlladmqnsg salplyfgsl rnsftyknwd
      961 csfnisfqlg hkfmrksiny stlvannvgh adyaarwqkp gdekitdvpv ftypanaqea
     1021 nfymysaalv spadqikwrd iqigyspknr wlkdlrvyay aanimsiwra nklgidpefg
     1081 nnppdpfags lglsfsf
//
LOCUS       WP_121126863            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121126863
VERSION     WP_121126863.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119605
     Region          48..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkpiklpqfr ktaqvtlala llnaasvdtv wanltnevia feipdqsvik givkdqdgkp
       61 idggtiinet skqstrtefn gkftlkgqag dqirisslgy ktttitatds plevvlekdd
      121 skldevvvta igikqqkkqi gyatqevkld vlkesktmni gtaltgqvsg livnnptgif
      181 qapsfqlrgk tplivvdgip vesdfydmss qnieninvlk gtaasslygs rgkngailit
      241 tksaksdkle fsvgttnmfs agftvfpesq kefgsgsngk yefwdgadgg isdgdmtwgp
      301 klnsgikvaq wnspirdkqt gevipwwgdv sgtkyndksr yervpidwva hdnledflgt
      361 glitennatl syrsekvsif gtgkyayqkg qvpntklstg glnlntsyrf tpevqldlnl
      421 synkvkspny prygygpknh mytillwmgn dvngqelkdh lyipgqegyr qanynyawyn
      481 npyfaayeln qvydqdilhg qtaltwrisp eftikgraaa rqknlfqdmq spksymnygd
      541 srngdyknwd skqlnfdadv latyikqwsd sygvtinags atytrnlrev slstdglvvp
      601 fvynvgntqg pvkgansite kttrsvyaav nlnvfkstyl nlsgrndwss alpevnqsyf
      661 ypslslssvi sdyfklpkdi nfiklygswa taasdldpys isatykkdlt ygstpsvsys
      721 eklvnpailp ektisletgv smaffdnrls tdityynvve kdkifdlnis qssgftsrkv
      781 ngnkyrtkgl evsltgniik ndqfswtstv nwsravqrle eiynnqakfg nlkkgdrads
      841 yyatvweksa dgkvilnpnt gmptknpfpq ylgyfqpdwq fgfanqfkik gfqvnldidg
      901 siggvmnstt iekmwwggkh pssvlyrqeq ydagkpvfvp dgvivtggel trdvngnits
      961 dtrtytnntt avdwqawsqn ypyqarvtea esklfanvfd rsfvklrrls vsydvnkvfk
     1021 lkqltalnas vfgynlamwk kvpyidpdfg vgndgnlqdp stryigfsld fkf
//
LOCUS       WP_121126876            1160 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121126876
VERSION     WP_121126876.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1160)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1160)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1160)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1160
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1160
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=130020
     Region          141..1159
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksqtlskl ffllaglnls yplsaaeivq fvhmdatkqp vsfqdllanl ekkfnvrfnf
       61 segmigsfmv dsagidglkk tqiknfleki sdgkvkieqv demlyvilpk ktvkkedktp
      121 svpisspprk nnnpgqqqqe rtvtgriidq ntglalegvt iriqgkniss nsspsgqfsl
      181 skvgdndvlv fsilgyndlq vpvqgesefs velnpknigl devvvtalgv krekkalgys
      241 iqevqgssln takeanlmsn mtgkvaglsi qnppglfedp kislrgssnv lvvvdnvpve
      301 tnfwnissdd iaevsvlkgp aaaalygsrg kngailittk rgggkdgkve isinssvmfq
      361 psfvylpktq skygtgqwgq fewvdgaggg vydndyvwgp kldqrdpntk sgfvelpqwd
      421 spidpatgkr iptpfisrgk dnirnffntg niisnniaig astektnyrf sftqldqkgi
      481 dpgaridast vafsgghkft dkfsietsin ynkqysdnyp rtsyfadnnm ynigvwmgad
      541 vdvrglkdyw epgqegikqr nynyqyynnp yyianefrqe yskdvvygfa nfayqftpel
      601 klsyranlnw htrytaqkrp kgfvgynpdy mdggfypdyn ydfelnnevl lnydkrlssl
      661 wsisalagan nrnnnwrnms lsasalsipg vynignskvp itgtnntykk lvnsfygsat
      721 igyhdalylt ltgrndwssg mpvkknsyfy psvsfsgvvs elvempsfis fakaraawir
      781 vggdmspyss rptysygtrw ggtptlslgg tlypqdiepd fkntiefgad irllknrigf
      841 disyfedtyt nqitqasiss ssgytsrlin sdkktrtkgw evtmnstpvk senfswdlal
      901 nwsrtrdwli qaesgkngrd gyvkegekyg ylyyrnefet tpdgqfvyrn glpvksngvt
      961 nlgfgpsnwv ggltssfkyk dwflsfsvdg rwggllysrl nqklweagkh insaneqyrd
     1021 adnrdektyi aegqkivsgn ltfdeegfik edtrvfeknd vpvyyrswan ayynqsiytt
     1081 smfdatylkl revilsytip tewtkklglk gasvafigrn lflwtkeesy mdpdvqggsg
     1141 etrlyvptpr nlgfnvklnf
//
LOCUS       WP_121126904            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121126904
VERSION     WP_121126904.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118962
     Region          48..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnyqfftrsl lkrsikllcp lialspsplf anpftaspil lsskfagitg rvldpdgkpv
       61 ygatilvkgs kagvktgedg vfhinlpadn qviivsyigy kvqeidmtgk tnitirlesn
      121 tsidevvvvg ygtkkrgevl gavasvdpke iqdipaania aalrdrvagl gvsessgrpg
      181 aavtlnvrna fasdqaklqg vtneplyvid giistsdvfe nldasmveni silkdasaai
      241 ygasgakgvi lvttkrgqag ktqlsyngym gisdatvkpk mlsayqhakl lnetyalnna
      301 qptlffsded laylktnpyk swydelwkss rmerhnlsis ggsekvtffa ggsyqkengn
      361 yagmsqqkys frsgfnaeii dglkadvafn vnntktnsqn slsddrdqnf yqtlittpqw
      421 vpiqidglpv nfnninansn tnplaiinsg yyqkqnntny sinaslnyap kalkgfnari
      481 qvshsgtsss gqeylpaynl yefvrsgnnn qlytntvdkv frmegnktri mpslgkgssy
      541 qgnivlqyan tfgdhsmaim agaeqsatnt eglsaywtnq qllnldeywa fdqstftnns
      601 rtideavkrs vfgrfnydyk kkylvevitr ldassrfakg niwglfptva tgwvvseenf
      661 fkdlnyisyl kvranyglvg edrvnarlwq drfsvdpvnt gylygetpva slnptiianp
      721 diswekhrtf nfgiesrwfd nklsfgfeyy frdsydvfdk gndenfpmya gfkapvvnyq
      781 krkgwgtefs lgyqntfsng lklstnmnfg ysgsyttqmy fnkfqlydfs ypdwkvemgt
      841 dsrkyntgny gliyvdmlrt qqdvdnflak npnytidgkv pqvgwtvyed tngdgkitek
      901 dlttmfents pifstgvtig layksfslnt nfravfggka fyesqamtap tdkvnvpsfw
      961 edhwslenpd grfpryddaa mmkkwnstfw aedgttirin nmvfnwavpk nftdkinvrs
     1021 lklmlsgnnl wtivapfkhr dpyatslyny ptirtlsfgl nfgi
//
LOCUS       WP_121127137            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Sphingobacterium puteale].
ACCESSION   WP_121127137
VERSION     WP_121127137.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium puteale
  ORGANISM  Sphingobacterium puteale
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Sphingobacterium puteale"
                     /db_xref="taxon:2420510"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120844
     Region          27..1070
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiklvfilf lfnsvvttsl faqqtvking rvvdgiaakp vggvsvqipg gmvlartdsl
       61 gqfqvllsta intlvfshvg yrpdtiavkq gdhhllikln srstileeve vlntgyyqip
      121 keratgsfgf vskediarvp atnildrldg ivnsltmdrs ntngeraadp klrlrglssi
      181 qsnsepliil dgfpyeqgla tinpsdiasi tvlkdaaaas iwgaragngv ivistkkgtt
      241 nqptriqyas vfqlqdkpdl yyapnylpaa tvldiedemf arsnylernq tpiplytewl
      301 ikhrdkkisd qelmnfrdql aatdtreesl syfyqkgfnq hqdiaftggg kgyafrssas
      361 ydknrsflkg dtytrwnanm qgtihwggkf kimpsiwytq qfnvqngigf tsftgggnsv
      421 vpyyrfqdgn gqslpivkgl rygyqesapg lglldwmyrp ldelklndnr ssdqelrmqm
      481 glsyefskli rwevfyqyln nlngqsalyd kdsyyardlv nkftqadmtk vipygairre
      541 ggrtgarshs irtqlsgewn hrnqhqlnyl lgaelldrit ttspfawsyg ydrdlltgrv
      601 nfdytkrytt rptgtalipa asgsyglnty rflsyysnla ysyrdkylat aslrwdasni
      661 ygvktnqkgv plwsiglgwq maqesffqnd iipslklrat ygssgntnpn vstfpiisym
      721 iddltnntaa vltsvgnpsl qwervntlnl gidfgtrnnr ltgsleyylk kgnnligadl
      781 mdpttgiidn vyptivnrin yanlqtkgwd itvnsknivg afnwdtrlql akvnnkvthy
      841 ntnditsati fidsrppvvg qsldviyafp whglnnegkp viyqngeltt dyinyyndyp
      901 ieeltkiggr iptltagmln tfrwkhwsvs anivwksgyy fqrttmdpgg ettgayhkdy
      961 yrrwqkagde aftdvlpkap anspeiraig smttnssllw ergdhlrlrd itlsyhwink
     1021 nraavvksln fgwsmanigi lwrrnkygld pdiprapypn pritsfsmni el
//
LOCUS       WP_121128238             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Oceanobacillus bengalensis].
ACCESSION   WP_121128238
VERSION     WP_121128238.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus bengalensis
  ORGANISM  Oceanobacillus bengalensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Oceanobacillus bengalensis"
                     /db_xref="taxon:1435466"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34461
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseeliydvi iagagpagmt aavyasraql stlmiergip ggqmantedv enypgfdsil
       61 gpdlsnkmfe hsknfgaeya ygdiksvedh gdyklikagn keykaralii ttgaeykklg
      121 vegedelggr gvsycavcdg affkkkelvv vgggdsavee gvyltrfadk vtiihrrdel
      181 raqkilqqra fdnekidfiw dtvvkkingp egkvssvtle nvktkeeydf eadgafiyig
      241 mvplsepfks lgitndegyi ptnedmetnv kgifaagdir ekqlrqivta tgdgsiaaes
      301 aikyveelve glqtsns
//
LOCUS       WP_121130301             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121130301
VERSION     WP_121130301.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>305
                     /gene="trxB"
     Protein         1..>305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..305
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstvdgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcma
//
LOCUS       WP_121145450             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Orbus hercynius].
ACCESSION   WP_121145450
VERSION     WP_121145450.1
KEYWORDS    RefSeq.
SOURCE      Orbus hercynius
  ORGANISM  Orbus hercynius
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Orbales; Orbaceae; Orbus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Orbus hercynius"
                     /db_xref="taxon:593135"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34112
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mknkhsrlmi lgsgpagyta aiyaaranlh pvlitgmqeg gqltttteie nwpagavdlt
       61 gpdlmskmre haerfeteiv ldniervdfs qkpfklygge tlytcdalii atgasaqylg
      121 lasedvfkgk gvsacatcdg ffyrnqkvav vgggntavee alylaniase vhlihrrdef
      181 raekilisrl mekvaqgkii lhthqtldev lgnemgvtav rvrstqdmtk teqidvlgvf
      241 iaighkpntg ifgdqleldn gyikvksglk gnatqtsieg ifaagdvmdh tyrqaitsag
      301 tgcmaaldae hyldnl
//
LOCUS       WP_121145841            1082 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            discolor].
ACCESSION   WP_121145841
VERSION     WP_121145841.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum discolor
  ORGANISM  Tenacibaculum discolor
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Tenacibaculum discolor"
                     /db_xref="taxon:361581"
     Protein         1..1082
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118171
     Region          25..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfngilt lflalivqis faqektisgt vsdgtgplpg vnvlikgttt gvetdfdgkf
       61 sikaktgdil vfsfvgmkti ekkvspsstf nismssdnvl devvvtslgi krakkslgya
      121 sqeikgdkvs tvklnnvvns lsgkisgvqi kannnfggss nflirgvssl tgnnqplfiv
      181 dgipisnqie nsanqkngrr gfdygnaasd inpddvesin ilkgaaasai ygsrgangvv
      241 iittkkgkeg nmkvnvssgi tlgkidrstf lkyqdkygag ygpyygstgy fedidvngdg
      301 tsdlavptyd dgsfgapldg slvyqwdafv pehpnfqtat pyvagkntpa dffetshqin
      361 nsvsisgseg kvsyrlgytn fqnkgilpns kldkntfnfn gtlkvsdrls tgananfinq
      421 dvtgrnstgy gdnlmaqfrq wwqvnvdikd qkyiydltgk nyswnhvgsv ggsplkpqyw
      481 dnpywtryqn yqsdnrnrff gnafatykin dwldltakaa vdtysevred rravgsvpte
      541 fgltvgdqgs gyqrtqinft efnydlmlnf nkdisdklsl ngvlgmnirk eknqywrast
      601 ngglanpgvy slrnsvlpvn lpverlaekq vngyyaqatl gydnklfiel tdrydvsssl
      661 psdnnsynyy avsgsfifse linadwlnyg kfragyaevg ndlpannvyd tysvidhfgs
      721 valssfdgtk knenlvpert keielgietr flsnrlglnl swykkdtenq lmpvtttaat
      781 gftsrwvnag tiqnkgfevs ldgkiiktnd fkwnttinws kndnlvkely adveniqlas
      841 fqggvtinat kgqpygtirg tgfvyddngn kvvdsngyyk aqanqiigda npdwnagitn
      901 tlsyknlsls flidiqeggd vysldlhygq gtglptytaa lndlgnpvrd pvtsgpdsgg
      961 ilnpgvtedg qpnttrapad tyagafywgn ssrnpaaltv ydasyiklre lslkynfpkt
     1021 wlqnsavsdv tislvgrnlw iidknvpfad pesglgagna qgylsgsypt vktvglnvnl
     1081 ef
//
LOCUS       WP_121145847            1038 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            discolor].
ACCESSION   WP_121145847
VERSION     WP_121145847.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum discolor
  ORGANISM  Tenacibaculum discolor
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Tenacibaculum discolor"
                     /db_xref="taxon:361581"
     Protein         1..1038
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113306
     Region          25..1037
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrtkfngilt lflalivqis faqektisgt vsdetgplpg vtilkkgttq gtetdfdgny
       61 siqaksgdil vfsfvgmkta ertigssnqi nvllesdnvl eevvvtalgi skkekglgvs
      121 igkvkaeslt varssspina lsgkvsglki tqqsgtpggs asiivrgats lsgdnqpifv
      181 idgmpisnqs inadgiaggv dggnragdln pddiesisvl kgasasalyg arakngaivi
      241 ttkkgkrnsg isveinsslr tdsplklpky qneyaqgtgg tydkdrvngw gpkisdvqdq
      301 tfedfkgdqv tlsakpnnvk nffqtgitki ntiaisggde ksdfrasytn tdvegivprs
      361 sykknnysvn ygrifnekfs trvnvnyihs gsrgrtqqgs ndsnviipsi lgisrtvsfd
      421 dlannyidet gaqigltert nnpywvlnkn pfstkldrii asaefnynit dnlkivdrig
      481 tdfynenrqk lyakgtlgnl ngqftnwdyy nqiinndvyl synnsfdngi svsailghnl
      541 yqtqynrttv eatsiivpgl yslantekqv atdfksrrkl hgiytdinld ykntyflnit
      601 grndwsstlp kennsyfyps vngaivftel fekndiinfg kirggyaevg sdaapysldf
      661 gfapatsyfv qyslsnnipq ggiigfqapr tlpnanlkpq rkkeyevgld lrlfrnivdl
      721 kftyynsdte dqliavdvpl stgffrksvn agsvnnsgie ldlnisplkt lntdlkwdig
      781 vtfnknkqkv eslaeglqef qlqsgwsglt ikaspgeefg lygtafkrnd egeyiinkat
      841 glkevvanqr lgntapdwtm ginnsfnykg fnlsflvdik eggtlfsgts aslrssglay
      901 etltnrgesf vdagvnevta pdgtvtyeen ttpvqnqeey wgnesatsnt egnifdasyi
      961 klrevalsys lpskfledkf ftgirfgvea rnlwiiqdhv phidpevnff gtggpaatve
     1021 fasvpsiksv gfnvkltf
//
LOCUS       WP_121149355             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium sp. AG1240].
ACCESSION   WP_121149355
VERSION     WP_121149355.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. AG1240
  ORGANISM  Microbacterium sp. AG1240
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Microbacterium sp. AG1240"
                     /db_xref="taxon:2183992"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34529
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msgienvvvv gsgpagytaa iylaraglnp ivltsaveag galvntteve nfpgfptgim
       61 gpdlmenmra qaerfgarii yddatalglt gpvktittgy gdtyqahtvv lamgsayrkl
      121 gipgeqhltg hgvswcatcd gfffkgqdia vvgggdsale eamfltrfad svtlihrrdf
      181 lraskimqdr alanpkirvl wdtevteavg tdrltglrlr ntvtgeesel aatglfiaig
      241 hdprselvlg qvdvdadnyv rvsspttetn lpgvfaagdl vdhryrqait aagtgcaasa
      301 daehylaang lasyaqqeta elddaltr
//
LOCUS       WP_121146414            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Tenacibaculum
            discolor].
ACCESSION   WP_121146414
VERSION     WP_121146414.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum discolor
  ORGANISM  Tenacibaculum discolor
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Tenacibaculum discolor"
                     /db_xref="taxon:361581"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124332
     Region          23..1110
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskfmltlf ivllgritya qeksisgtvs dttgplpgvt vliknttkgt dtdfdgnyti
       61 kvnqgdvlvf rfvgkkttei kvqnqtvinl vleddsniln eveviatgyd kinkktftgs
      121 aisvgiddlk idgvvdvtrm legrvagvni qnlsgtfgta pnitirgsss ifgnntplyv
      181 idgvvqedvi eqdldqltsg dpstlisssi aginasdikk idilkdasat siygararng
      241 vvvittksgr kdsplklnyn leqtirdips ysnfdllnsk esmaifrene srgffqlpsv
      301 srgryggvyy irataldnyn estgmfelgn tpeareaflr kyelantnwf ktlfrnsslm
      361 qnhslslsgg sennsyyasv sllhdpgwti adkvtrfttn lkntfyfsdk fnatlavnas
      421 irkqkapgtf sresdpvtgd isrefdinpf syalntsrtl rpyndtggye yyrnnwadfn
      481 ileelannsi dinqrdirfq ldasykitdn itydfngagr fvntvrehnv rensnvvray
      541 nadsstvlrd dniflyqdpt dpdalpvavl pnggiyfknd dylttfyarn sfkydntfne
      601 khnfnallgq eirfvnrnsd rftgyglqyd ngltaftdpr ileklingge ayfgltkere
      661 rtvaffgkat ysyddkyvfs ltgrydgsnr qgrssssrwl ptgtvsakwn askesflens
      721 ntfsnlqfrt syglvatpgn atnalaifts qiadrllpad renflnital qnseltwekq
      781 yelnfgvdlg lfnnrvnlit dvykrdifdn idfvrtsgig gqfikqgnna dvetygieft
      841 ldtknivtdn ftwssninfs yfdqeitkld ntpiafdlvd qtggnvvgyp insmfsfqfa
      901 glnneglpqf inkdgevasv ldfqnnenlt dylkhegsvn pnisvgfsnn ftyknwdlgv
      961 litgsggnkv rlnpvfssty sdtsifsksh vnrwlnpgde nitnipvvpd psafqrnsnl
     1021 rtvynaynys tervadgdfl rmknislgyk fnnelveklg lshlkvkfqg tnlfllysds
     1081 klngqdpefy qtggvalpit rqytfslnlg f
//
LOCUS       WP_121154871             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingomonas paeninsulae].
ACCESSION   WP_121154871
VERSION     WP_121154871.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas paeninsulae
  ORGANISM  Sphingomonas paeninsulae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sphingomonas paeninsulae"
                     /db_xref="taxon:2319844"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34060
     Region          7..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpathstrml ilgsgpagls aaiygaragm spivvqgiqp ggqlmtttdv enypgfkdvi
       61 qgpwlmeqmq aqaehvgaqm mwdtivdidl sqrpfrligd ggtvytgdtl viatgaqakw
      121 lgldseealk gkgvsacatc dgffyrgkkv vvigggntav eealyltnhs hdvtlihrkd
      181 hfraekilqe rlfkhrgikv lwnkrvdkfv gggdpeglig ldlidtvtge ashigtdggf
      241 vaighhpate lfrghlelda dsylkvetgs trtsvpgvfa cgdvmdkiyr qavtaagtgc
      301 maaldaerfl aeadfeavta
//
LOCUS       WP_121157758             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora pisi].
ACCESSION   WP_121157758
VERSION     WP_121157758.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora pisi
  ORGANISM  Micromonospora pisi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora pisi"
                     /db_xref="taxon:589240"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33448
     Region          7..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlnp lviegvqsgg almttteien fpgfpdgilg
       61 pelmdsmrkq aerfgaefit ddvsrvelad tgkpgsdavs vvyvgetayr akavilstgs
      121 awrplgvpge qeylghgvss catcdgfffr gqeivvvggg dsameeanfl tkfassvtiv
      181 hrrdsfrask imaeralane kirvewnsmv eevlgadgkv sgvrlrnvht geakvldvag
      241 vfvaighdpr selfrgqvel dengyvrvna pgtttsvpgv faagdlvdht yrqaitaagt
      301 gcaaaldaer flatlev
//
LOCUS       WP_121161421             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. BEA3.1].
ACCESSION   WP_121161421
VERSION     WP_121161421.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. BEA3.1
  ORGANISM  Pseudomonas sp. BEA3.1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. BEA3.1"
                     /db_xref="taxon:3083251"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38918
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 myigvpleta cgetrvavtp dtvkrlvasg hqvvvqrgcg llscitdsaf eavgatvgea
       61 sdafgaevvl kvvapndqel elinsgsvli gmlnpfnsel ivkmagrgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaaqyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrmgavi easdvrpavk eqieslgakf idvpyeteee racaegvggy arpmpeswil
      241 rqaqavhdra kqadivitta lipgrkaptl lnigtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgltnlpa qvgadasaly srnlldfmkl lfdkdgaldi nleddivaac
      361 lmcrdgqvvr kns
//
LOCUS       WP_121165972             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Roseovarius spongiae].
ACCESSION   WP_121165972
VERSION     WP_121165972.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius spongiae
  ORGANISM  Roseovarius spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Roseovarius spongiae"
                     /db_xref="taxon:2320272"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55593
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtprevl dgearvamtp dsarqlqklg hdcaietgag eragfsdaay keagveiiks
       61 paalwkacdv iakvrvptdt evkrlrkgqt litffnpaen daqmkqaadk gatviamemv
      121 prisraqkmd alssmaniag yravieagsn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvyldfee aaqdgaetgg yaapsspefr
      241 ekqlekfrel apemdivitt alipgraapv lwtrdmveam kpgsvivdla aekggncelt
      301 epdekivtdn gvtivgytdf psrmatqsst lyatnirhml sdltpekdga ivhdmeddvi
      361 rgatvthgge vtypppkpkv aaiaaqpkkp aakeltpeer raqevaafka qtrnqvgmla
      421 iggglllavg avapvsfmqh fivfvlavfv gfqviwgvah slhtplmavt ngissiiilg
      481 allqigsgsw lvlllamlsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_121164964             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Roseovarius spongiae].
ACCESSION   WP_121164964
VERSION     WP_121164964.1
KEYWORDS    RefSeq.
SOURCE      Roseovarius spongiae
  ORGANISM  Roseovarius spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Roseovarius.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Roseovarius spongiae"
                     /db_xref="taxon:2320272"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35665
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maetrktkvl iigsgpagyt aavyasraml epilvqgiep ggqlttttev enwpgdtevq
       61 gpdlmirmea haravgcevv gdiitsidft arpyvcqsds gteyvadaii latgarakwl
      121 glpseekfkg fgvsacatcd gffyrgqeiv vvgggntave ealfltnfas kvtlihrrde
      181 lraeailqdr llknpkiepl wfhtldevyg tddplgvegv kvkhvktgei tdipckgvfi
      241 aighapanel vkdalethmg gyvvtkpdst etsipgifaa gdltdwkyrq avtsagmgcm
      301 aaleaerwla eqddaprsev teplgygaev aage
//
LOCUS       WP_121169426             306 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thermovibrio guaymasensis].
ACCESSION   WP_121169426
VERSION     WP_121169426.1
KEYWORDS    RefSeq.
SOURCE      Thermovibrio guaymasensis
  ORGANISM  Thermovibrio guaymasensis
            Bacteria; Pseudomonadati; Aquificota; Aquificia;
            Desulfurobacteriales; Desulfurobacteriaceae; Thermovibrio.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Thermovibrio guaymasensis"
                     /db_xref="taxon:240167"
     gene            1..306
                     /gene="trxB"
     Protein         1..306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33298
     Region          20..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mevwdtlivg agpaglaagi yagrsqlktl ildrmpggql liteeienyp gfhggitgfe
       61 lsekfrqhae kfgakiengh tvtevtldge ifvvktdyge fkgrtliwaa gsnprklgvp
      121 geaefvgrgv sycavcdgaf fkdrvvavvg ggdsaleeal yltkfakkvy lihrrdkfra
      181 vkiiqdrvkr nekiepvlnk vvvsingkdf vesltledtr tgekmelpvd gvfifignep
      241 nvspiihfvd tdpsgfiltd eemrtktpgl faagdvrskp lkqvitaasd gavaamsatr
      301 yleeke
//
LOCUS       WP_121172605             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Kushneria sinocarnis].
ACCESSION   WP_121172605
VERSION     WP_121172605.1
KEYWORDS    RefSeq.
SOURCE      Kushneria sinocarnis
  ORGANISM  Kushneria sinocarnis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Kushneria.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Kushneria sinocarnis"
                     /db_xref="taxon:595502"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34759
     Region          9..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetqhhgli ilgsgpagys aavyaaranl kpllitgmem ggqlttttdv dnwpgddsgv
       61 qgpelmermr rhaerfdtei qldhieevel gqrpyvlrgs sgtyscdsli iatgasalyl
      121 gleseerfkg qgvsacatcd gffyrnkevv vvgggntave ealylsnias kvtlvhrrds
      181 lraekimqqk lfdrvdngsi elawnsvvee vlgddsgvtg vrlkstedgs trelmapglf
      241 vaighkpntd lfqgqlemrd gyivvksgld gnatatslpg vfaagdvadh vyrqaitsag
      301 sgcmaaldae rflddldpsv phsaw
//
LOCUS       WP_121181635             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nocardiopsis sp. Huas11].
ACCESSION   WP_121181635
VERSION     WP_121181635.1
KEYWORDS    RefSeq.
SOURCE      Nocardiopsis sp. Huas11
  ORGANISM  Nocardiopsis sp. Huas11
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Nocardiopsis.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Nocardiopsis sp. Huas11"
                     /db_xref="taxon:2183912"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33247
     Region          7..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa vyaaraelrp lvfegsitag galmnttdve nfpgfpdgim
       61 gpdlmdnlrk qaerfgaelv pedvtevdlt kpvkevtagg etflahtvil atgsgyrelg
      121 vpgekelsgr gtswcatcdg fffrdqdiav agggdtamee alfltrfaks vtvihrrdel
      181 rasrimaera landkisflw ntevkevlgt ervtglkvfd nktnetstld vtglfvaigh
      241 dprvelfnkq ielddegyvr vdapstrtnr agvfaagdvv dhqyrqaita agtgcsaald
      301 aeryladmgn
//
LOCUS       WP_121188836             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microbacterium sp. AG790].
ACCESSION   WP_121188836
VERSION     WP_121188836.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. AG790
  ORGANISM  Microbacterium sp. AG790
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Microbacterium sp. AG790"
                     /db_xref="taxon:2183995"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51749
     Region          3..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 marigivrer dgetrvaasp ttvgkiralg ydvvveagag aassfpdaay taagatvapr
       61 deawgadvvl svaaptdaei allqpgatlv gilspalspd llaalaargv talamdavpr
      121 israqsmdvl ssmaniagyr avveaanefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvasiggt ylevvvpdeq kevsadgyak atsaaydaaa
      241 aklysdqaad vdivittali pgraaprllt aadvaamrpg svivdmaagq ggnvegsvag
      301 ervvtangvi ilgytdlagr lpqqasqlyg tnllnllall tpgkdgqlti ddtdvvqrav
      361 tvtrdgavtw ppppvqvsaa pttpgtdaaa sapapaakkg lstgaksgli vagiaalflv
      421 cavapaplpq hilvltlsvv igfsvigrva halhtplmsv tnaisgiivv gamsqivvpn
      481 pvvqvlaava vllasinifg gfavtrrmla mfqkgdqk
//
LOCUS       WP_121189981             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium sp. AG790].
ACCESSION   WP_121189981
VERSION     WP_121189981.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. AG790
  ORGANISM  Microbacterium sp. AG790
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Microbacterium sp. AG790"
                     /db_xref="taxon:2183995"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34262
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqviiigsg pagftaaiya aranlspllv assveaggel mnttevenfp gfpegimgpd
       61 lmakmqeqae kfgtevvydd vvkleltgdv kkivlgsgae heaesvifat gsaprkigie
      121 getrlsghgv sycatcdgff freqaiavvg ggdsameeat fltkfaskvy vihrraelra
      181 skimqerafa nekiefvwns evvdvlggda vsglllrdtv dgterelavt gvfvaigndp
      241 rthlvhdslq ltehgtiwvd grssrtsvpg vfaagdvvdp iyrqavtaag sgtaaaldve
      301 hylaargdag apekdaaeid gledaa
//
LOCUS       WP_121192064             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Motilibacter peucedani].
ACCESSION   WP_121192064
VERSION     WP_121192064.1
KEYWORDS    RefSeq.
SOURCE      Motilibacter peucedani
  ORGANISM  Motilibacter peucedani
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Motilibacterales; Motilibacteraceae; Motilibacter.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Motilibacter peucedani"
                     /db_xref="taxon:598650"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34118
     Region          6..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mgdvrevviv gsgpsgytaa iyaaraglrp lvlegsvtqg galmntteve nfpgfpegit
       61 gpdlmdalra qaerfgaelv tddavsldlt gpvkavvdge gtehrakavi latgsaykei
      121 glpnekrlsa kgvswcatcd gfffreqhiv vvgggdsame eatfltrfaa svtvvvrrdt
      181 lraskimqer aldnpkitfa wnsevadilg edkvtgvrlr stvdgserdl dvtgvfvaig
      241 haprsellhg qvhldengyv ltegrstrtn lpgvfaagdl vdhtyrqait aagsgcaaal
      301 daerylasle dvaltgdavq aavli
//
LOCUS       WP_121195495             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_121195495
VERSION     WP_121195495.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33692
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstvdgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_121196210            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121196210
VERSION     WP_121196210.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110015
     Region          38..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meifirkknl ylllllllcv splmvtaqte lpatinskle gqvldvntke plpgavisis
       61 gtthsvstna egrfnfvtgq kfpytliitf igyerqeiqa sgspikillk qklnqlnevv
      121 itdgyttqtk ksytgsatti ngaenenkpf ssplaalqge vaglnitltn aqpgatpsvq
      181 lrgvgstaln snplyvidgm ilsnpnsvln ginqddiesv tvlkdasata iygsrgsngv
      241 ivintkkgka gktqvdfste agrtiniplp aagqplnadq fatlfiegvt nagntpaqva
      301 alatnyglns gqsndwqkit hkdgsqqqyn vsvrggnent kifasagyft qqattlnsdl
      361 kritslfnid qkiskrigft tginisnnyq ntpvgdvgsw anpvfaseil rpfqlaynpd
      421 gsiasssssn igfpahynpl wiaahdnhgt setrilfntt lnwniwdqlk fssyvsadye
      481 atqastflnp vlgdgsssng qatetntrny tlltrnqldy rydipgikdf yvtaavgyea
      541 qkantytasa sgvgfpltqp tlvvlsdaat atgassstsn itfnsiyarl ssnyknlfsi
      601 sgsfrrdgss vfgannpygn fwsvggawni dgndffkdqr ifssaklrls ygktgnaqgi
      661 gaysaqplss ygsnyttgng qnyntvgnpd ltwesakkfd igadigffkd rllftvdyyr
      721 diidgliqsv pisgttgfnt vpyanigamq ntgyelsikg tavqtqafsw issfniavnk
      781 nkitqlanga gangdyyfqv gydyhtyytp lwagvnpadg talwytddtq tktttnygsa
      841 akepyktatp kffggfnntf nyrgitlavd fyynfgnytk dywstrfydg syytfnkyqr
      901 eftnrwttpg qitdvpkyia gggtqssssa yssrfiynas firlknatlg ydlkklnvlk
      961 nvtgvskvyi yargtnlwtr tyddrlpydp etgavtipaf rtytlglnvg f
//
LOCUS       WP_121196254            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121196254
VERSION     WP_121196254.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116258
     Region          28..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgkrilflml cylfstclit araqinstvt glvkdnegkv vpgatvaekg mpgngtitdq
       61 egkfqltlkg tsktitisli gfrrqeikae gkpitvmlqi qenslsdvvv vgyqkqnrre
      121 vtaaisslsg kdianipqss fdqtlqgrla gvsvlsstge lgskpaivir gsanidfgna
      181 nggntgplyv idgvifdvna mgsaygnnnp lslinpndie sidvlkdasa aaiygaragn
      241 gviivktksa kqgkpqvsis ayvgsvtkpn fikvstgaae rslklallqq ltygdrqlga
      301 iplaitdsln safnndvdwq gllvrqqalv nsqdvaisai tgstsyrisi nhyneqgvlh
      361 gyglekfsph lnltikplkg meltadllms sqrqqhgvgg aganlfgawn fptsftpltq
      421 aqydvytgkk hyydddrafs iigslqlkqq itsdlvfnst ygstnytnky gyfspvelng
      481 tlntaydiya snpswsfenf lqynkrigkh nflmaagasl ysyenyynya saagitvsgi
      541 stvqtvpagt nlnastsyqr kttesyyarv nydyagkyll tasirrdass iysptyrwat
      601 fpavaagwia sdesffeplk kavsffkira sygitgkdpg qwyskyqslf ndasyfagtn
      661 gtinnfgglg gnattyngts vispfaygnn flnygtkass tvrwerdpql dfgadlelfn
      721 grvnltvdwy rkdskdvffy nvpaqatsgy qyqsgnyvdl rnqglefatn fnvlgpkspf
      781 qwnfnfnisf nknlvtklpn nnrdflfdvp wfyktltlgk pifsyrvfht ngvyatdaev
      841 pidpttglke tangvplkag dpryvdvngd yninnddkyd ggnpnpkytg gfgstfrykr
      901 vslsffasyv fgrkilngal sdalngskyp gsygttagaa tyvsllnqfw qnpgdqtrya
      961 rlvysnadar vkdpwnigne yfvedgsfvk lknvtlgydl pdrwtkklgm trfnlyvmgd
     1021 nlamwkkaks iadpelvdpt tgsanviypt aakftlglni gf
//
LOCUS       WP_121196342            1179 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121196342
VERSION     WP_121196342.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1179)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1179)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1179)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1179
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1179
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131040
     Region          129..1178
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlpklrsilk iksivltaaa scfinlalat glahsqglek ritidvqnkp lkqtldqiaa
       61 saqmviiysn tkgiiekpvt ihekdqpvsr ilnelllpls ltyeviddri vikfdnassr
      121 ppsrekppfp vkgkvtdang lplpgatvki kngpavattn sngdfqitnv adstilqvsf
      181 vgyvtkeivv rkaefltivl eigsaqlnev vvstgyqtlp keratgsfvq innellnrrv
      241 gtdiisrleg vvpgllfnrn tingtagavd isirgtntly anaqplivid gfpydgdfnn
      301 inpndvesvt vlkdaaaasi wgvrsgngvi vittkkgkrn eklnvemnan vtignkpnly
      361 yspnflpand vinleqtlfn kgyfdsnlss gyspvspvvq ilanqragti saadatsqin
      421 alrntdvrdq lnqyfyqkti nqqyalnlrg gnsnsdyvfs lgddqdrsyf kgnqngritl
      481 nslynfyplk dlqisagfny tqvaattnnp iynnggrltf nndniypyak lvdvsgnala
      541 ipkdyslsft snadgklldw ayrpldelnn edntskmvdn rislgmqygf lkdfrinlky
      601 qyehavtnql rnfssdtyya rnlinqytqi gsggsltypi pvggilqqtn ayltsqrgra
      661 qlyynhswnq khelsaiaga eiseainesn sntsygydkn tgtsygtidy sdsfnitpyg
      721 ygqripnslg fgkttdhyis yfsnasytyn nryilslsgr idksnlfgvn tnqksvplys
      781 sglawdlske dfyhlswlpy aklratygyt gninksatav ttirqfsnsy ysgnpyaivi
      841 npgnpelrwe ktrminfgld yafknsiiag sveyyikkgt difgdsplap stglttffgn
      901 tadikgngvd ivintkning tnfrwttnfl lshvvdivtk ydvtlasssy iqlsnassvy
      961 pltgkslygl ysykwaglth ntgdpqgyvn gqvstdyaki lsgtsiddmv yngssrpttf
     1021 gsfrntfsyk dislsfniiy klnyffrrss ytssalpyng ntdfykrwqn pgdesstnvp
     1081 almyppyntn rdqfyqnssv lidkgdhirl qditlsydlt kqqwkkspft kfqlytylnn
     1141 vgilwranhd hldpdlstns tfgsyplprm lsfgikanf
//
LOCUS       WP_121197076            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121197076
VERSION     WP_121197076.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118508
     Region          23..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklllvslc flfysmqifa qnrtvtgtvt akddggpmpg vsikgvgtdv gvvtgadgkf
       61 sislpatvka lqfsfigygt vtksitgavl nielessskv lgevlvtgaf gikqtsrsas
      121 saaqvvsgdd lntvrqanin nalagkvagi qvrsqstaal grgtevrlrg asgfgtgspa
      181 lyvvdgtimt nsddinpddi esstilegaa agalygsqga sgvivitlkk akkkdglnvd
      241 lnlgsrwdma yilpnyqnty aggnnpdltq ynwkagdpta wqalsgkyyp dysddsswgp
      301 kmvgqeyipw yawypgtqys fktatlnpqp nnardyfntg vtlnnniaig katddynirf
      361 sygnqyiqgl vpnsdlrknt mtltynlnln khfilganin yvnqkqdglv ndaysnqtsg
      421 sfnqwfhrdi dmgimkelrg lksptgayas wnhadpntyd pnnanafyag nywynfytyq
      481 dlvqnvnqrd rlygnislty kvnndlsfkg tyrkmqnttf gytqfssdla tsgvqttgne
      541 arnkgyyany ttylnrenye fltnytkkik dfkidanagg dfynanyndd santnnglsv
      601 pnvftisnsv dpasygntra kerynalfvt anigwkdmly lngslrddwy stlnpsknlv
      661 tsksiggsfv fsellksqst wlsmgklras ygeipsalgq ngsvfgssse sfgfgrypgs
      721 vyttsankfv snllqtandg ivdpnlignt vkekelgidl affnerlglt atywdgsnen
      781 lagsvglnga sgltsittnf gkitkngldf tlygtpvkik nfewrinaty snllhdyvde
      841 isnkygikti avgfntysal pglyqvqgqs wgqiygngil rnangvpilt sagmyqnnpa
      901 vsfgsalpkh tggiqnsfiv ykdfainvni dyqfggkfss lsdlwgsysg ltartaalnd
      961 kgipvrdpvg ngggihqigv sasgatidmy vpaydyyqnn ynsktgdefv ydltfiklre
     1021 lgisyripvk klgiasyvkn atfqltgtdl wllyaktkdf dpsqisavsg esgqlpgtrg
     1081 igfnlkvgf
//
LOCUS       WP_121197160            1206 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121197160
VERSION     WP_121197160.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1206)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1206)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1206)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1206
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1206
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133209
     Region          41..103
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          115..1205
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mdenfykklk lkikpflvll mavaiampka naavdwqtrt erletvlkki eqqyrvsfvy
       61 dateinknld ikvvetsktv dlflqqlgsy giaykvvgnk vilkksastl kdtpikgkvv
      121 ektgsgkesi pgvtvmekgt knvvstgpng dfaitvkdga vllftavgyk tkevvvgsqt
      181 tievvmeanv nnlsevvvtg yqsldkklft gaattlkged vkrdgisdvs rmlegrvagv
      241 svqnvsgtfg aapkirvrga tsisgdnkpl fvvdgivled vvnisneals tgdantlvgs
      301 svaglnpddi esftilkdaa ataqygaram ngvviittkk gkdtkgkpnv sytgeftsyl
      361 kpsystydil nsadqmnvyl emrdkgwlne gvtannangg vftkmyntmy synaasdsyv
      421 lrndapsekq flqryangnt nwfdvlfkns lqmqhslsvt sgteksqlya stsflkdngw
      481 tigdnvsrft gslrgtfkis dklsfelltl gsvrdqaapg tlsrvsnpvf gqydrdfdin
      541 pfsyaintsr vltaydangg leyftrdyap fnivselknn tlnltqidfk gqigvkykvl
      601 kqlqysfdga yrfaktnqeh kvtensnqan ayraginpan atimannrfl yhdpdspdgl
      661 pvtvlpyggf yntvgdnitn yyfrnalewn ttfnkdhlvn vfaaqelryi drqhvtfdgy
      721 gyqydqggvp yidpnivksn vesnlnyysm gytyerylny qlraaysykg kyslnstvry
      781 dgsnllgesp tarwlptwnv sgawnmdled fyqksslikt lnrvtwraty gltaslgpat
      841 nsslvlqsqs tsrpviteke talyikylen sqltfekqye tnlgvdlgfl qdritltvdv
      901 ydrkgfdlig kittsgigge adkianyanm rskgievtig atpvkhkdft wntnlnfakt
      961 sskitnlqsq ptifdlvnqd ggpqlgypqr glfsidfvgl shdrgipqfi kedgtvgtnv
     1021 ylqsivtkyl kyegpvdptl tggffnsfky kqlslgvlvt fsagnkvrld pvfkssytdl
     1081 datssiflkr wekpgdeltt nvpsildkys aaqldgypyn nynyssarva dggfvrlktv
     1141 slsyaikpqy laklgitnaa lsfatnnvwl iysdsalngk dpeffgsggv alpiprqftl
     1201 slkvgf
//
LOCUS       WP_121197439            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121197439
VERSION     WP_121197439.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118121
     Region          36..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmlrnksiti yscvalilll wsismdagaq vstaavitgt vteaktkati pgvtvvevne
       61 ndrqvaaavt nidgkytikv sskshkirfa yigfqsltlp igdktvinaa lkeaesnelm
      121 avevtaksak kistgygdvs erdkigavst vtsemlqglp atsidqmmqg qaagvqitsn
      181 sgdpgggatv tirgqgsisa gndplyiidg vpiistpfdn tnggnnyarv spiadinpnd
      241 iekidilkda naaaiygara angvivittk rgkpgatsiv lntqfvllqs prpipvlnas
      301 eykvmrleae qnngninpss ntllplvddp tyqfywlyqa ntdwpaalrq lgltqnynmt
      361 lqgggesary sfgtsysdak gsmintgfkr ftgrfnldyk vsnklrftan iaftrskvna
      421 lanngggtly fnslvrspal piydvsyvdg sslpnymsyg gfygfqdnpv afaatsinas
      481 ystnlkpnir aelevaknlk fvstasldfv genatyfqpa aatgviwnsn qfnrldtrdf
      541 erlqmisdsy ltytktfgrk lvtnyllgnt fntfksnqls aqayatadfa mqtlgnsggy
      601 nsvysanate ailsqfakld mvyddsygln ftirrdgssk fggdnkygyf pstgaywris
      661 nlkalkyskv itnlklrasw gqlgnsgipn yayisqfgqg anylglsgvs qtnpqlnhlk
      721 wetsestnig ldagffndrl gltvdvynrv tkdllynlpv passgipips gaqsatiltn
      781 lgnirnrgie vnltgtpiaa knftwnasfn iatninkvls lpggtvttsd sfggftsqik
      841 egdalgtyyg lvfkgvyard adavvhdkng nivyelngtt prlmhigset gnvykggdai
      901 yedfnhdgvi ndqdkvrigd anpkffggmn ntftyknwsl rcfiqyqygn niidgmrlql
      961 esmtntnnqa asvlrrwrtq gdvtdmpral stdtrnvlps trwvedgsya rlksltlsyr
     1021 fspafvrklh lsnldmfvtg nnlytltnyl gadpeiyvgn npafvgvdqg ytpqtknylf
     1081 glnvkf
//
LOCUS       WP_121197442             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121197442
VERSION     WP_121197442.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107453
     Region          60..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mikfrlhaic ffcaaatcfg lwspalgqsk qpipklsktd sliraltlqk dvqdqqnpdv
       61 gylgvkrqps igvvstlldn rykeltaqsi sallqaqsag vhvvntsgap gsgalvnirg
      121 vatlnagttp lyivdgipir sirnqsplal nadndpladi nphdiasitv lkdayatapy
      181 girgsngvvi intyggtsgk tlldvtvnsg vsfapkelsv lnadqyrnmi ieqetsrgqt
      241 aaqiqsgmgr ylllstptnq lwrynnntdw qkqmlrsgsl ndfnlllrgg davakyslla
      301 gyvnqggvis ntnysrfsar fnfdykvgrk ltflntlsyv rsdktlkdeg sssntnplll
      361 atlksptlts lqhdnfgntl rdpdsadyag rnnpyavinr mrtenstnri lgkitaqytf
      421 spnlflhigl agdfdrlnei rfvpsagfap vtyvtrysaq gnstelmain entlnyekts
      481 asgisvisay vgnsfqttsl dskylkains tadqfvlntg dpnfldslas sqptwrllsf
      541 fagaqysyks kysiganira dgssrfaqgh qwgyfpsvag swhlskegfl aqnklisdlt
      601 lrtsygitgn ddvgyyagyn slvaspyqgy savklgilgn pnftwektqq fdggidigff
      661 kngveltany ynrttndlln ainlpgisgf ktytvsegsm rnrglelsla trvkkgafgw
      721 tsgfniafns ntilslpdki npivnysggy asilavgnsv gayygynavg vysktsdvhv
      781 kngasnsapf kggdvmfedv dhngvidtnd rkvignanpk ffggfhntfs ykmfdlaifm
      841 dfaygnqvyn aqraalesms nydnqstsil nrwrqegdvs smprlqygdp egnnrfssrw
      901 iedgsylrfk avtlgynmpl ksarlssifk svriqvtgqn lytftkykgy gpevgsainq
      961 vqysadyasl pqsriiylgv klgl
//
LOCUS       WP_121198424            1179 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121198424
VERSION     WP_121198424.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1179)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1179)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1179)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1179
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1179
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=129312
     Region          132..1176
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlknlrsilr yksfvltvat tcflncalat eiarsqdlnk risidvekkt lketldqvsk
       61 qahvgiiysn argvlknpvt ihakdqpvsk vlndllsplt ltyeiigdqi vvkfdnissr
      121 ppsqgqpvkq sipikgkvtd dkgsplpgat ikikdgpala ttdsngefei snvsdstvlq
      181 isfvgyltke ivvtnanylt islkngsnql nevsvvstgy qnipkeratg sfsqpiktef
      241 earvatdvls klngitsgll fnanttaarn gidinirgrs tifandqplv vvdnfpysgd
      301 inninpndve svtvlkdaas asiwgvragn gvivittkkg klnqslkigf nanitvfdkp
      361 dlnynpnqlg assfigleqf lfgkgyydsn ltntstypvi spavellaan ragslssndl
      421 asqlntlrgi nvndqlsnyf yrkatnqqya ltlsggsdka tyylstgydn nlpglkgntn
      481 qritinslnt fylvknlels aglnivqdyn kidntlsqfn trvfpysqia dasgnplaip
      541 fnysrnyvqs apangfldws yyplkelgat nhstkdldir lttglkyafi pgltgeikyq
      601 yersnsqdrd yqsqqtyftr nyinqfsiln ngqvtgynvp lggilslana nmvtnnvrgq
      661 lnfnrtwgnn nvsaiagyel sqttvesngs nlygynddla tfinvdptts fpinpsgsts
      721 insglgiggt lsrirssfan aaytymdryt lsgsaridgt nyfgvatnqk niplwsagak
      781 wniakenfyt ldwlpvlalr asygyngnld qsitgvttfr ysnlatyltn lnyaaisnig
      841 npdlrwektg itnlalgfgt knnvltgsle yyfkketdll gyktfpensg ittlegnysd
      901 mtgkgfdlsl tsqnlkgsik wtttllfsha tdkvtrydvn pltstvvssg sgiavpvvgk
      961 svfgiysykw dglngqtgnp vgfvngtase nyatittktp isdlvyagpa rptyfggfnn
     1021 rlsykgfsla vqinykfgyy frsptinyyq itssgsflrv nrdfdnrwlk pgdekntnvp
     1081 sliypstqar dnfyqfseat vekgdhvrlq dislsydlnk smfhrlpfnn iqlfiyanni
     1141 gviwranhkg ldpdavpasg dintmpnprs isfglkgsf
//
LOCUS       WP_121199033             993 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121199033
VERSION     WP_121199033.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107158
     Region          29..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrifyfkkyl llsafifipy llfaqsgsis gkvvdenkqp lpgatvsvig gtqgaatetn
       61 geflikglka gkytleakfi gyapmqsvvt vtsgtaivnf nlkpdsknln evvvigygtq
      121 skrevsgais tvsskdfqtg tvtsadqlvq gkvaglsitt ngspgsgsti rirggaslns
      181 sndplividg vplspngisg aasalslvns ddiesvtvlk daastaiygs rasngvllit
      241 tkkgakgaaq vngstensig tlarriqvls adqvrayvaa nkpslsstlg tantdwqdqi
      301 fqkaftsnnn vnvsgsvknm pyrvsvgyld qngllktdni krtsgalrln ptffnnslkv
      361 dinangtyqq srfantgaig aalsfdptqp vydpkspyng yyesyntpgl issglnpntp
      421 rnpvgllfdd qntsqvyrsf gnavvnykfp flkalsasan fgydvskgqg vtsipasaaq
      481 afnslgnntp ylqknqnttv eyylnytndi ksikstinaq agygyynfln tnynfqalsa
      541 nnqpqpnssa plypysqgey tiisyygrli ytydekytlq gsirsdntsk fspstrqgif
      601 pagafsyrvs dedflkdskt isdlklrvsy gvtgqqdgig yygylpiysl ttndtryqfg
      661 ntyyngytps aydtslkwet tntfnagidy gffhqrlygs vdfysrktkd llatvpipsg
      721 tnftnqlttn vgnsishgve lninaipvkt knlswtlnyn iaynkvsitn lylvpnptsv
      781 gvqtggisgg tgnyvqlnal nqtpgtfyly kqvygangkp legvfadlng dgaitaadry
      841 lyhsaappvt mgfstqvnyk kwslstvira nignyvynnv danlatggsi innvgvvnna
      901 ttgiygsgft gynylsdywv qnasfvrmdn aglgynfgnl fnnhinlraa fncqnvfvit
      961 kytgldpevy sgidnntypr prtftvglni glk
//
LOCUS       WP_121199000            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121199000
VERSION     WP_121199000.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117689
     Region          23..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiylfiil vsdlfyasaq ttkitgtiid aeshqplqga siilkknaqy tisdidghfr
       61 isltradtli vthigyarla mpvssanssq llismkstys qlkevtvstg yqtlpkerat
      121 gsftqidnkt fneqvstdvi srleavansv svsrktagnt aqlmvrglst iqgvkqplii
      181 vdnfpydgdi nninpnevqd itilkdaaaa svwgtkagng vivittkkgk fnqktavegn
      241 aittitdkpn lfylpqmssn dfinveqflf skgyrfsdta stghppfspv yeillkqqng
      301 qlsqaaataq inalrnldvr ndlnkyfyqk avnqqysinm nggsnniawl vfagydknin
      361 elnakndrln irtqntfsla knlqlsvgav ytqtnntsgk psysdistsi gsippytqia
      421 dangnplpva kdyrlsyins agsgklldwn yypltdyqhv nktikgndll anlglnykit
      481 swlnadikyq fekqqvtnnt iydansyyar nlinqftqin qtfntvlnvi pkggiydlsi
      541 nnitsndvrg qlnfnktsgk fdisaiagge isqkaldqns yrvygydgni ltttnvdyan
      601 syptfvqgiy sfipsnvnfl knlnryvsty anaaltydek ytlslsgrrd asnlfgvstn
      661 nkwtplwssg lswdiskekf ynsklvpylk lratygysgn vnpdatavtt vaynitspyt
      721 qtptavidkf ynpdlrwekv gilnigldfk mlnnrisgsl eyyrknatdl fgsvpvdytv
      781 glvnttivkn vasmqgngad lelnsinldg avkwltninl syyrdkitny ylssyqgsnf
      841 vnggqliagi igkpvysifs ykwagldpat gdpqgylngq vskdylnitg sgttindlky
      901 ngpafpvifg smgntvsykn lsitarvlyk fgyyfqrqsi sysslfannv ghsdyslrwq
      961 ktgdekatnv psivypadpa rdafyngsea lvdradnirl qyininysfk lrpsasgfnk
     1021 lqafvvfnnl giiwkathap vdpdynssvi ppsksislgi kgtf
//
LOCUS       WP_121199127             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mucilaginibacter gracilis].
ACCESSION   WP_121199127
VERSION     WP_121199127.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34632
     Region          9..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqeqehvkc liigsgpagy taaiyaarad lkpvlytgml aggqltqttd venfpgypkg
       61 imgpemmedf rlqaerfgtd irfgyvssvd fstlphqvvv detktiladt viistgasak
      121 wlgldseqky ngfgvsacav cdgfffrgqd vaivgagdta aeeatylakl crkvymlvrr
      181 defraskamv hrvmhtpnie iiyntettei vgdgqnvtgv rvlnnqtqqe rildvtgffv
      241 aighhpntdi fkgqihmdet gyiithpdst qtniegvfac gdaqdhifrq avtaagtgcm
      301 aaleaeryla gkehivtad
//
LOCUS       WP_121199485            1204 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121199485
VERSION     WP_121199485.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1204)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1204)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1204)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1204
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1204
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=132134
     Region          134..1203
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklrdqfrsg hsaclynqiv rtmkltilii tsvllqvsan glaqkvtfnk kdvtlkqlft
       61 eirkqtgynv fwqdgrvdds qkinadfrna sledvlnnvl epqsltysiv nktvvvkkke
      121 ktffekikev fsnidvsgkl idaetgqpip yvtvtlkgtn rkvftnesgt fffakvpeng
      181 slvftsvsye titktlsatm vvkltvrvlk lddvvistgy qqirkgastg sysiltdkdi
      241 estpsvnlle rldgkvpgvh fdvrnnaiqm rsingyvkns pplividgfp aanqnlvnis
      301 ssvidgnpln gnksylnpdq pgtsgnavmd ninpndiesi aflkdaaaas iwgaaaangv
      361 ivittkkgkr napsinysvt vstsapgnfs nakamtsaqy veleqemfnk gfftdpitdf
      421 rnapiseaqe wmfrvkrgta taaqrdsaln ilsnrsnrdq fkkyllqrat sqqhslslsg
      481 ggnnntyyia anynkdvpvy rsnygetyal tsnlsndfln kritvntgin yqytksqvns
      541 aalaalgtgs fgyapyemlv daqgnpinka vtftqrvtds lsnlgylpwg ynavnelnys
      601 ntilsknsir lnsaikgnit dwlnvtvsgq yqrnlanqdf lqnqnsfatr nlintgttls
      661 gktliygvpv ggvyktsstt yddysvrgql ninktfnqhh idflggseir qyqytggtqt
      721 rygynedlst saavnptvsy atvtrstssl gysdgnifkd skrylsyfal anysfqnkyf
      781 asgsirfddy tnqgldrsqr avplysgglr wnihqenflk dvkwidglnl rasigtggsi
      841 ptagtsyati sigsndpytt lptasivvpa nsqltwettr tinegidaef lhgrlslsad
      901 iyqkrnynll islpynatyg fttlqynagd akgygeefii tgqpisttny nwtssfnfsy
      961 atnvitdqrl attntsggia eitagypsdn ifvyrwagld naghsqiygt dgtvlkssgs
     1021 rsvtnadlvy ggrttppyfg gwtntfryhd lslivratya lgykflltdi ntssyptgtg
     1081 fgglivnsar latrwrnpgd eattdvpgla gnsfnsvsrf lgadinlrda gnirlqqvsl
     1141 syrlpqsftr gqyikaitvg ataanlgliw rankdgldpd yqvtgtytnl ppsatflfnl
     1201 nvsl
//
LOCUS       WP_121199541            1064 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121199541
VERSION     WP_121199541.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1064
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118123
     Region          25..1063
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkyypflw lfllvftksa fsqvkmirgq vssatgqtla gvtltlsisr tssasdtngh
       61 fsiairsspd tlrityigyk tlrlpvssat ilplriqmep liselnevvv stgyqdipke
      121 ratgsfykld nqllnqrvgs divsrldglt sgllidkrdp nqstiqirgl stlnydaasp
      181 livldnfpya gdinninpnd iesvtvlkda aassiwgara gngvivintk kaklnqplkv
      241 sinsnitlsa kpnlfsanql svgsfiglek ylfaqgnydn lfndpthppi sqvveilqqq
      301 kqgtlsqaqa darinqlagq dvrndmtryl yrpatvqqya lnltgsgnni ryllsagydk
      361 nlsslqgngn qritvrsnnv idltkrwqlq tdvifthtda tanspggygn ysftgnispy
      421 arlvnsdgtp aavdlfyrgq ytdtaghgkl ldwkyrplqe lanndnttta ndillnagts
      481 ykvlpwlsad lkyqyqqswn nttnnnslal fstrdlinrf sqltatgvdy ivpkngilkt
      541 rdvlnraqsl rgqlnvnnnw gdkhelsaia gaeiretrsh istsnlygyd antattvgvd
      601 ysnpyptfdg iygnsyipdg ssidnltnrf vsvyanaayt ynrkytlsgs arrdasnifg
      661 vntnqkwvpl wsagllwrid qeqfykvgwl pqlsmrltyg vsgnlsltas altkiqyndp
      721 srspinlpsv dilsppnpyl rweqvktwna gfdfgsansr ltgsvdlykk natdlinnvi
      781 ldptvgmtga lqnsaaidsk gfdvvlntln vnreikwrst llvnyvsykv sknlnppsad
      841 glvsdgnyif pvvgynpyei vsyqwagldp qtgdpmgyvn gqvskdyqai aknpvqqqvv
      901 sgsalpplfg tfrntvdwhh fslavnityk ldyyfrrpsl nyttlftygt gyseydqrwm
      961 kpgdekltnv pslvypanal rdnfyhyadi nveradnvkl ndiylgydwv pqhpmlglks
     1021 vqfylyasql nlliwkanks gidpdilygv kppvtfsagl kvnl
//
LOCUS       WP_121199894            1050 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121199894
VERSION     WP_121199894.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1050
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113409
     Region          23..1049
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkifllffv mlaigitvqa qnrtvtgtvt skddngplig vtivikgsta atstdvngky
       61 sikvtnlqnv vigakylgye yqevslkpge lkvdfalvat nsslnevvvt gygttvkgki
      121 lgavseikaa efedlpvanl gtalrnrvag vgvsvtsgkp gaattlalrn pvtftgssti
      181 gqtsnplyvi dglistiddf nnldaslvet isflkdasaa iygasgdkgv vlvttkkgki
      241 gktqinysgy sgtstaaqap kmlsafqqat llndgwaasn tantsrfsqa dldflstnpy
      301 dswyqdlwhs sttqrhtinl sggtekilff aggsyyyetg nygninstky nirsgmtakl
      361 teditayisl ntnysksfsn slksasstdt etsqilalit tpqwvpltin glpngygdvs
      421 gnstwnpial ynsgtynktn aqtinlnssl ewrpkfvkgl tikeqfgknn qtsgsnqwlv
      481 pytvynftrt gqnsklfstv plaskpsqin snsdqlqqgt gynnsyelit sadysrvigk
      541 htfdimalsd ltegssgsnl lyrttaqipg vdqfyaypss tttvqlnpga nvgkqsylgk
      601 msydyagkyl mqlitrvdgs tnfpadkrwg afpdlglgwr vseekwfkpf tkyvnslklr
      661 lnvglvgddr itpytyvavn tpasnnyifg sgntvvngiv asttfanpdv twekqrqtnf
      721 gidatfldsr ltatieiynk htydgfvdfs slgivpqftg qsltavnngi annwgsefdl
      781 sfvqpvskdw tvranvnfgf sdnnivqvay apgkigtvda ltgitigqss htytssnigy
      841 iatgiiktqa dvdailaknp nytiggvkpq pgfmnyqdtn gdgkidandv glmypsvnsp
      901 fsggitlgas yktfsfsing lfviggklqt dgqakkpatt tlnvpvfwad hwtpdnvnaa
      961 fprtdaplid qnstfwtvsa tqlrinnmai swslpkrise klgipnlrvl asgtnlwtii
     1021 npysykdplt ssysdyptlr tlslglnvtl
//
LOCUS       WP_121202165            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Mucilaginibacter gracilis].
ACCESSION   WP_121202165
VERSION     WP_121202165.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gracilis
  ORGANISM  Mucilaginibacter gracilis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Mucilaginibacter gracilis"
                     /db_xref="taxon:423350"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119655
     Region          120..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlvftgisfa ntskgqglld krvdyniqnt sltnaiqqle kvtnlkfvyr knlvenefgl
       61 sidakqeklg avlsklltpr gitfdiigdq ivlakavtaa kqpdaantde penaslavtk
      121 titgkvtddh dqplpgvsvs ikgttmgtqt dangkytlni pdneiekail ifsfigfnsq
      181 eipaggrsvi nvrlvasqss lnevivigyg sqrkgdvtss vatvkaenfv kgpvldagql
      241 lqgkvaglsv sapsgdptsg svillrgntt llgansdplv lvdgvpgslk tvvpedieti
      301 dvlkdgsaaa iygvrgtngv iivttkrass nftnavdysg yvstqtlare pklftaadyr
      361 aqiaagtrdk sydlgsstdw lkaisnnlpi ttvhtltlrg gnsktnylas vnyrslngif
      421 qksdnrtfsg rvdinhymfd dklkinfgll qqdnaftqtq dggsfngyty rqailqnpta
      481 piknadgtyf eqpsifnyqn pvsmiynsdg ktsnttskyn stitltpfdg lklsalgsyt
      541 rfnqtagyse nkqnisnird hlngypgvgs tqsidrllel taeykktmgd hsfsvlggys
      601 yqdndtfsff eqnhdfptdi fsynniglgr aaanglgves ssrsetnlis ffgratynyk
      661 drylllasvr reaasqlyga kepwgtfpai qvgwritkes fmkgqhvfdd lklragygvt
      721 gnqpaqgflg vgllgygnyv lsngqwvqtl gpsqnpnpnl rweekhetdl gldysllkgm
      781 itgsvdlynr kiegllydya vpsppnlyps tranvgtmqn kgiefllnit pirkadfqwt
      841 tsfnfstnsn klislsnety qttsnyfttg gtgepiqtft nivtvgknig dfygfkvtgv
      901 sadgqwiyed rngnsvaykd fthsfedkkv lgnglpkyya gwnnsirykd wdfgvtmrga
      961 fgyqilnfqr myyentsvqy ynrlksandk vfgtavlnkt mplefnsyyi engdfwkidn
     1021 inlgytfnsl kskyihaprv yvstlntfvi tgykgidpev srsgldpgnd nrdkypttrt
     1081 ftlglsanf
//
LOCUS       WP_121203182             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Oceanobacillus halophilus].
ACCESSION   WP_121203182
VERSION     WP_121203182.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus halophilus
  ORGANISM  Oceanobacillus halophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Oceanobacillus halophilus"
                     /db_xref="taxon:930130"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34354
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseermydvi iagagpagmt aavytsranl dtlmlergip ggqmantedv enypgfdhil
       61 gpdlsnkmfd hskkfgaeya ygdiqeivdh gdyktvkagn kefntraliv atgaeykklg
      121 vegeeelggr gvsycavcdg affkeknlvv vgggdsavee gvyltrfakk vtiihrrdel
      181 raqkilqqra fdnekidfiw dtvvkkingp egkvnsvtle ntktgeisdf vadgvfiyig
      241 mvplsspfns lgitndegyi ptnehmetsi pgvfaagdir ekqlrqivta tgdgsiaaea
      301 aikyveelae kvkatns
//
LOCUS       WP_121206742             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Marinobacter nauticus].
ACCESSION   WP_121206742
VERSION     WP_121206742.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter nauticus
  ORGANISM  Marinobacter nauticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Marinobacter nauticus"
                     /db_xref="taxon:2743"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34044
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msetrhsrli ilgsgpagyt aavyaaranl nptlitgiev ggqlttttdv dnwpgdndgv
       61 qgpelmqrmq khaerfetsi vydtineadl nnrpfrlkgd ngeytcdali iatgasamyl
      121 gleseekfkg qgvsacatcd gffyrkqkva vigggntave ealflsniad evtlvhrrdk
      181 lraekilqdk lfekaengnv niiwdhtlde vlgdgtgvtg mrirntkdgs tqdlelagvf
      241 iaighkpnts lfegqldman gyirirsgld gmatqtsipg vfaagdvadh vyrqavtsag
      301 fgcmaaldae kfldqqg
//
LOCUS       WP_121208198             385 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Marinobacter].
ACCESSION   WP_121208198
VERSION     WP_121208198.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter
  ORGANISM  Marinobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Marinobacter"
                     /db_xref="taxon:2742"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41008
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mmigiprerq dgenrvaiip sgvstlleag yevvvesgag saahftdddy rhagaiiadd
       61 adalyrqatv ilkvrapsse earliqqdat liclldpwfn qplleqlagq nvqafaldlv
      121 prttraqsmd vlsamagisg yravlsgama lpryfpmlmt aagtihparv lvigagvagl
      181 maiatarrlg avveaydlrp evkeqveslg adfieievpe sdttgdsgya kaqseafyta
      241 qrqqladcva radlvittaa vpgkpapkli dqemihrmks gsvivdlaad kggnvdgtvl
      301 nqkvdvdgvt lvghanhpsr vpvhasqllt rnitafllnm tedgrvvpkl edeivastlv
      361 vqhgsvrhna etrdtpqtst qkdtd
//
LOCUS       WP_121209631             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Maricaulis
            maris].
ACCESSION   WP_121209631
VERSION     WP_121209631.1
KEYWORDS    RefSeq.
SOURCE      Maricaulis maris
  ORGANISM  Maricaulis maris
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Maricaulis.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Maricaulis maris"
                     /db_xref="taxon:74318"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38670
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,92,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriailkerh agetrvaatp dtvkkfvaag hevaiekgag ltaavtdeaf tdagakigta
       61 aatlkgadal favrspdeat laklkgvllv ahlsphgntk maeglakagi nalamefvpr
      121 itraqamdal ssqanlagyr sviegaelyg rafpmmmtaa gtvapaktfv mgvgvaglqa
      181 iatarrlgai vtatdvrpav keqvaslgak fvaveddefk qaetaggyak qmspeyqakq
      241 aelvashiak qdivittali pgrpaptlvt kamvesmkpg sviidlaapn ggnceltkld
      301 evvehkgvki agygnlagrl aadasalyak nlanllpllv neegglaphw ddeviqgmal
      361 tkdgavvhps lvkega
//
LOCUS       WP_121211039             302 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121211039
VERSION     WP_121211039.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>302
                     /gene="trxB"
     Protein         1..>302
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..302
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv hlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 ag
//
LOCUS       WP_121214702             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Ureibacillus endophyticus].
ACCESSION   WP_121214702
VERSION     WP_121214702.1
KEYWORDS    RefSeq.
SOURCE      Ureibacillus endophyticus
  ORGANISM  Ureibacillus endophyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Ureibacillus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Ureibacillus endophyticus"
                     /db_xref="taxon:1978490"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34096
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 maeekiydvi iigagpagmt aavytsranl stlmiergip ggqmanteev enypgfetil
       61 gpelstkmfe hakkfgaeya ygdvaeiidg edykvikags keyktrsiii stgaeykkig
      121 vpgekelggr gvsycavcdg affknknlvv igggdsavee gvyltrfank vtivhrrdkl
      181 raqkilqdra fanekvdfiw nhtikeinek dgkvgsvtlv stvdgseqef qtdgvfvyig
      241 mdpltapfkn lgilneqgyv vtdekmqtsv kgifaagdvr dkmlrqivta tgdgsiaaqs
      301 aqvyveelke kisq
//
LOCUS       WP_121216817             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Oceanibaculum indicum].
ACCESSION   WP_121216817
VERSION     WP_121216817.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum indicum
  ORGANISM  Oceanibaculum indicum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae; Oceanibaculum.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Oceanibaculum indicum"
                     /db_xref="taxon:526216"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34977
     Region          7..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mptekhtkll iigsgpagyt aaiyaarani spimvqglqp ggqltittdv enypgfadvi
       61 qgpwlmeqme aqarhvgtei ifdiitdvdf srrpfratad sgdvyiaetl viatgaqarw
      121 lgleserkfq gggvsacatc dgfffrgkev aivgggntav eeaiyltnha skvtlihrrd
      181 slraekimqd rlfrnpkvev iwnhtveevl gtenpnqvtg lrlkstvdgt ertlsadgff
      241 vaighdpats lfkgkldmds egyiitrpds tatsipgvfa agdvkdkvfr qavtaagmgc
      301 maaleaerfl aahedgsvep aatvaaq
//
LOCUS       WP_121222703             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121222703
VERSION     WP_121222703.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>313
                     /gene="trxB"
     Protein         1..>313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..313
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali latgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkntidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kyl
//
LOCUS       WP_121220165             382 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Oceanibaculum].
ACCESSION   WP_121220165
VERSION     WP_121220165.1
KEYWORDS    RefSeq.
SOURCE      Oceanibaculum
  ORGANISM  Oceanibaculum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Oceanibaculaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Oceanibaculum"
                     /db_xref="taxon:659693"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40338
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mivaipkerr pgetrvaasp dtvkklidlg ldvvvekgag qaaamtdeay kaagatiakd
       61 tktvlekadi vlkvqrptgs ddktdevalm kegavllcil nayndkplld qlaarkvttf
      121 gmefvpritr aqsmdvlssq snlagyksvl daaaefgraf pmmmtaagtv pparvmimgv
      181 gvaglqaiat arrlgaivsa tdvrlatkeq veslgatfvm veseeakqae taggyakems
      241 deykkqqaal iaetlkkqdi aictalipgr kaptliteem vksmkpgsvi vdlaveqggn
      301 cecsepgkvv qkhgvtvvgh lnvpgrlpvd asalyaknll nfvtllidke tkalkidled
      361 eivkgtlvtq dgqvvhpalk aa
//
LOCUS       WP_121223946             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Saccharothrix variisporea].
ACCESSION   WP_121223946
VERSION     WP_121223946.1
KEYWORDS    RefSeq.
SOURCE      Saccharothrix variisporea
  ORGANISM  Saccharothrix variisporea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharothrix.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Saccharothrix variisporea"
                     /db_xref="taxon:543527"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35359
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnlivv gsgpagytaa vyaaraqlep lvfegsqygg almttteven ypgfrdgimg
       61 pdlmeqmreq akrfgaelra edveqleleg dvkyvtangk ryaakavila mgaaarylhv
      121 pgeqellgrg vsacatcdgf ffrdqdiavv gggdsameea tfltrfarsv tlihrreefr
      181 askimlerar andkikwlln aeavevlgeg gtmsglkvrd trtgeitehp ftgfflaigh
      241 dprsdlvrgq vdvddegyvk vkgqstytnl dgvfaagdlv dhtyrqaita agsgcaaaid
      301 aerwlaehge sdahltpefv gggygdsad
//
LOCUS       WP_121228845             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121228845
VERSION     WP_121228845.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>309
                     /gene="trxB"
     Protein         1..>309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..309
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv hlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaalda
//
LOCUS       WP_121230103             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Saccharothrix variisporea].
ACCESSION   WP_121230103
VERSION     WP_121230103.1
KEYWORDS    RefSeq.
SOURCE      Saccharothrix variisporea
  ORGANISM  Saccharothrix variisporea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharothrix.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Saccharothrix variisporea"
                     /db_xref="taxon:543527"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52044
     Region          1..505
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvlkeaa dgetrvaatp atvpalrklg yevvvepgag vaadftdday ldagasvgsv
       61 aeadvvlgvn apttaqldal edgatviaml spalrpdlve dlakrpital avdavprisr
      121 aqsldvlssm aniagyravv eaahefgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgavvra tdprpevadq vkslggeyla isspevevsa tgyakemged ykaaearlya
      241 eqcadvdiii ttalipgrpa priitaemva smkrgsvivd maaqnggnve gtvagekvvt
      301 angvtilgyt dlpgrlpaqa sqlygtnlvn llklmtpeqd gelvvdfdde vqrsitvvra
      361 gevtwppppv rvsaapapvv qepvaevpak rvsplvkwgl pavglalffl vlatapapip
      421 rhfttlmlsi vigyyvighv ahalhtplms vtnaisgiiv vgalvqlgsa dptvtvlaav
      481 avllasinif ggfavtrrml amfrkgd
//
LOCUS       WP_121234531             299 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121234531
VERSION     WP_121234531.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>299
                     /gene="trxB"
     Protein         1..>299
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..299
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsa
//
LOCUS       WP_121239521             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sulfurisoma sediminicola].
ACCESSION   WP_121239521
VERSION     WP_121239521.1
KEYWORDS    RefSeq.
SOURCE      Sulfurisoma sediminicola
  ORGANISM  Sulfurisoma sediminicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Sulfurisoma.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Sulfurisoma sediminicola"
                     /db_xref="taxon:1381557"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33929
     Region          11..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtantlprhs kllilgsgpa gytaavyaar anlkpvlitg laqggqlmtt tevdnwpada
       61 dgvqgpdlma rfekhatrfn teiifdhiht akltekpmkl igdsgeytcd aliiatgasa
      121 qylglaseqa fsgrgvsaca tcdgffyknq kvavigggnt aveealylan iashvtvvhr
      181 rdkfraekim qdklfekera gkvtikwdsv ldevlgdksg vtgmriknvk sgatedidlm
      241 gvfiaighkp ntdlfagqle mengyivtqg gregnatgts ipgvfaagdv qdhvykqait
      301 saatgcqaal daekyldnlg
//
LOCUS       WP_121239574             528 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfurisoma sediminicola].
ACCESSION   WP_121239574
VERSION     WP_121239574.1
KEYWORDS    RefSeq.
SOURCE      Sulfurisoma sediminicola
  ORGANISM  Sulfurisoma sediminicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Sulfurisoma.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Sulfurisoma sediminicola"
                     /db_xref="taxon:1381557"
     Protein         1..528
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54862
     Region          3..528
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpltigvpre tfagekrvat vpevveklik lgfavsvesg agdaanfadd tyraagaeiv
       61 adaaglwans divfkvraps atevglmkeg atligfiwpa qnpelmqqma arkvtvlaid
      121 alprmlsraq kmdaltsqag vagyraviea anafgrffng qitaagkvpp akvfiagagv
      181 aglaaigtaa glgaivrand traevadqvv slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqremyakq arevdiiitt alipgkpape litaemvksm rpgsvivdma aeqggncelt
      301 epgqavvkhg vtiigytdlv srlakqsstl yatnlfrlte elcktkdgii dvnmeddair
      361 gltvikqgev twpppplkpa aapaqvkpap vaakksghgh gagepmagss lamifgigaa
      421 lfwvvgafap asflshftvf vlacfvgymv iwnvtpslht plmsvtnais siiaigalvq
      481 iapplsglte grpsglilgl avlalaltai nmfggfavtr rmlamfrk
//
LOCUS       WP_121257280             355 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Solirubrobacter pauli].
ACCESSION   WP_121257280
VERSION     WP_121257280.1
KEYWORDS    RefSeq.
SOURCE      Solirubrobacter pauli
  ORGANISM  Solirubrobacter pauli
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia;
            Solirubrobacterales; Solirubrobacteraceae; Solirubrobacter.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Solirubrobacter pauli"
                     /db_xref="taxon:166793"
     Protein         1..355
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36594
     Region          1..352
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,70,89,284,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,122..123,132..133,136..137,140..141,143..144,
                     146..151,153,155..157,160,183..184,274..275,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(117..118,122,125,128,169..172,192..194,224,235,
                     252..254,261,263)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,122,132,175..176,183,199..200,202..205)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(152..156,159,162,185,187)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpkerl drerrvaivp dvvrrlraae hevvvesgag ltagapddaf vaagasigdp
       61 wgcevvakva pplddevtrl ssstilvgfl nplgnpagle aiaatgatal amekiprisr
      121 aqsmdalssq atvsgyravl iasielprff pmfmtaagtv ppaqvlvlga gvaglqaiat
      181 arrlgavvta fdirsavkeq iqslgarffe vegigdaeaa ggyareltpe eqqlqrdals
      241 vqmgksdviv ttalvpgrpa pklipasave gmkpgsvivd laaeaggnce ltrpgetfvt
      301 dggvkvvgpl nlpsemaeha sslyarnils lvelgfdfdd evvagatvvr ggkvv
//
LOCUS       WP_121254010             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nocardioides ferulae].
ACCESSION   WP_121254010
VERSION     WP_121254010.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides ferulae
  ORGANISM  Nocardioides ferulae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Nocardioides ferulae"
                     /db_xref="taxon:2340821"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34861
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpetrnvivi gsgpsgytaa vyaaraalqp lvfegsvtag galmntteve nfpgfrdgim
       61 gpalmdemra qaerfgaelv addvvevdlt aepkvvktat etytaravil amgsgyrklg
      121 lpredelsgr gvswcatcdg fffrdqhiav vgggdsaiee atfltrfgsk vslivrrdel
      181 raskimqera fadpkleilw nsavaeinga drvesltlrd tvsgetrelp atglfiaigh
      241 dprselltgq vdlddngyvv ashpstgtnl pgvfaagdlv dhiyrqaita agtgcaaald
      301 aerylaeldh aasgpadaqa radaealspt l
//
LOCUS       WP_121258588             337 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Solirubrobacter pauli].
ACCESSION   WP_121258588
VERSION     WP_121258588.1
KEYWORDS    RefSeq.
SOURCE      Solirubrobacter pauli
  ORGANISM  Solirubrobacter pauli
            Bacteria; Bacillati; Actinomycetota; Thermoleophilia;
            Solirubrobacterales; Solirubrobacteraceae; Solirubrobacter.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Solirubrobacter pauli"
                     /db_xref="taxon:166793"
     gene            1..337
                     /gene="trxB"
     Protein         1..337
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36236
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 madvenviii gsgpagytas lytsranlnp lciegfmwgg llqqttdven ypgfpegimg
       61 pemmqkfrdq aerfgtrfit dnvtkfepgs ggephtvwvd deaykartvi lamgaehkkl
      121 gvpgedelgg rgvsycatcd aafykdrtti ivgggdsame eaiflakfss kvtivhrrde
      181 fraskimler akaveniefl tpytvkaflp gdngqldrad lintetgeel vvpmagafia
      241 ighepqsaiv dglidvddeg yvkvdgrstr tnipgvfaag dlvdhtyrqa itasgsgcqa
      301 aldaewylrd npavptpaal egtgnlaeeq wapvars
//
LOCUS       WP_121270365             293 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121270365
VERSION     WP_121270365.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>293
                     /gene="trxB"
     Protein         1..>293
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..293
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqhpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyr
//
LOCUS       WP_121276829             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Trinickia fusca].
ACCESSION   WP_121276829
VERSION     WP_121276829.1
KEYWORDS    RefSeq.
SOURCE      Trinickia fusca
  ORGANISM  Trinickia fusca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Trinickia fusca"
                     /db_xref="taxon:2419777"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35402
     Region          8..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mstrkhakvl ilgsgpagyt aavyaaranl spmlitglaq ggqlmtttdv enwpadangv
       61 qgpelmqrfl dhaerfktei vfdhihtakl nekpirligd sgeytcdsli iatgasaqyl
      121 glpseesfmg rgvsacatcd gffykqqhva vvgggntave ealylagias kvtvvhrrdk
      181 fraepilidr llekekegvv eikwnhvlde vkgddsgvtg lrikhtqtge atdvalqgvf
      241 iaighkpntd ifagqlemkn gyiitnggln gnatgtsvpg vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq rylesihelh qdhvmsaevd r
//
LOCUS       WP_121277156             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trinickia
            fusca].
ACCESSION   WP_121277156
VERSION     WP_121277156.1
KEYWORDS    RefSeq.
SOURCE      Trinickia fusca
  ORGANISM  Trinickia fusca
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Trinickia fusca"
                     /db_xref="taxon:2419777"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39673
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr thearvaatp etvkkyvgsg hrvtvergag gaasfpdeqf aavgaelvda
       61 atalgaelvl kvqspnetel aqmkrgavlv gmldpfnadn aarlasagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaadlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atarrlgavi easdvrpavk eqieslggkf idvpyetdee reaaegvggy arpmpaswla
      241 rqalqvnera kqadivitta lipgrdaptl lselavqamr pgsviidlaa grgaelagqp
      301 gvrggncplt epdkvvvkhg vtivghtnlp amvaadassl yarnlldflk livtkegaln
      361 idmtddivaa tllardgava rkaa
//
LOCUS       WP_121279447             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121279447
VERSION     WP_121279447.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33311
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvifaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121282048            1140 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121282048
VERSION     WP_121282048.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1140)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1140)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1140)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1140
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1140
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125137
     Region          117..1137
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqiyllvll vlgsqllmpr panaqspaai kitlklqhqn lrtalssiqk asgiqvvfne
       61 elvlpyhnis vnvsnvsvst vltqvlkdtk lkyiaqanki vilakqgned gsqetsisgq
      121 vsdetgkalp ganikliels khtttnssgf fqlavqpgty tleishvsye tkqiqrvktg
      181 gssihielsg hehtlenvvv talgikreek slgyavtkid geeisktvpg nwvnalsgkv
      241 pglnisraga gpggtvritl rgqnsldldk geplividgv pvlsgmvgnn glsygatgnt
      301 eppvdygnal sdinaedikd vtvlrgpsaa alygsraasg ailittknna erkerlnvtf
      361 nssanlegvl hypdfqyeyg agntintyfs ygaspdgpst nstrsfgpaf sgqlyyqydp
      421 vtktrgiekt pwvadknyvk dafvtgvtyn ntlsltggds knsvrlsynd vrnkyilpnt
      481 gytfnrlafs snsklknfql stgfnyyhkq sdnlplsgyn tnsfmyglmy rsanipasyy
      541 kdywdikdvd qnnllnpsvd npyfilyenl ntldqdrifg nvtatynlsk kmslmlrggi
      601 dqnssfrttr rpyssirfav gryqeqtvmm qeqnydflyk ydekllnnld lsfsaggsif
      661 knkiqnnlit aerlstpgiy tlgnakdrpl ivlspankev qslyalaqfn yknflfmdlt
      721 grndwsstlp kannsyfyys fsgsaiasei fdlsafrals ylkikgsvsq vgndtdpyrt
      781 gyyltpsefg gsytnpttlp ggdslkpeii tnrelgldir ffknclgfdl tyynanssnq
      841 iltvpndpat gftgrifnag linnrgiela vnasllhkks klqwktmlty ssnrslvkel
      901 apnvseiima tgprgfvkai vggsigdiyg sgylrapsge ivhddrglpl idtenlkilg
      961 savpdfkagi qnqlsynqfs fsflfdgqkg gdiysfshsv lggagklkss lpgrydgiig
     1021 egvvqnadgs yrkndivatp gdyynqkylr dnaeanifda sfiklrevsl eyrfsakllk
     1081 slgansasfs lygrdlllft kfplydpeia tlnrnriepg fetgqfpstr sfgatlkasf
//
LOCUS       WP_121282160             972 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121282160
VERSION     WP_121282160.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 972)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 972)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..972
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107817
     Region          50..967
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrknivtcc lclvafllri tqtaaqeqkd sivkvpfrnv saqlpndslv rtafrivare
       61 dllggvstvn iaallkksyg srgldnlqsf vggyngniwg qaplilvdgi prnaadvrmv
      121 evqsvtvlks asavmlygst aakgavlitt nrgsvkplsi nvrantgifv pkayptylng
      181 adymtlynea ltndgiatsg agftqqqidn tragtnpyry pdvdffssdy lknaysksdl
      241 ttevsggnef aryytnigls ynnslikyge qqknsdfgfn vrgnvdmnit kwltasadav
      301 aissnnyagr gdfwgassti aptfnrfspl ipidrldpgn palqtfvkns nhvidgkfll
      361 ggqstnptnv fsdmlaagyv rtktstflyn vglkadlasl vkglsfttat smdyaslyse
      421 aynlpyatyr ptwstvnged vitalekfge dknstneyvg rstytqtmsf rsqfdyarvf
      481 andhsvtatv lgwwyktqfs sdidnqggsd yqpvlntnlg fqtgynfkrk yyldftgalv
      541 hsaklapgkr nalspsisig wriskerffk envsfvddlk fnasyasvnq dldvtgyran
      601 nvnepvdyyl yqgyysntaa lggyyqwrdg vaggrttlsg qsenldltfi krnewrvgld
      661 asffknlltl nlnyfsqntn gllargvtiy psyfsgsgdf rpwinfnqdk rqgldfslnl
      721 nkhigevqys lglsgmfyns qavkrdeivd qaylaragrp ldayygyvse gffqnqadid
      781 ahakqtfgvv kpgdlkykdl ngdglidgrd qqdlghtgwa aspftyglnl tvryknftlf
      841 algsgsagav gfknssyywv ggsgkysevv ldrwteatkl tasyprlttn snnnfrnstf
      901 wlyktnrfdl nrvqltydfd rkflkdsfvh glslyvqgdn llvisnerkl metnigsapq
      961 trffnlgara sf
//
LOCUS       WP_121282187            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121282187
VERSION     WP_121282187.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113481
     Region          25..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkiftslff lftlltglst maqvktitgk itavddggpl pgasvkikgs ttgtstdsng
       61 sftiqvpstn avlvisligy ktqeitvgsk ttvnvglasd aqelqevnis talgitrqak
      121 slgyaaqsvk sedlnynhqp nllnalqgki agatisstgg gpgqgasiri rgvnsidpni
      181 sgdplyvidg vqidnststv ganpdgtayg srgvtnrasd inpedietin ilkggaatal
      241 yglrgangvv vittkrgkqn gvsvnfnssy gfdevlkspd vqteytqgvl gaytnppggi
      301 gpawgptiae aklidpthpd qlfnnydraf gtgqqvknsi svaggseaik ffssisqlyq
      361 kgmmpntdnk nfsgrlntdf tispkfkaav nmnftnsggy tysadrfges laywsprydv
      421 adyqnadgsq kyfgtnnpiw gtannrlkgd vnrfiggasl sydpakwlnf syrlgvdtyn
      481 dnrvrtargp myateamydn aqgfygeynt kfrtinstfv atltskltdd itgtlrlgqe
      541 lydrkskeig tlgsilgvyn ffnlanagvl tptqnlrqkr ligyfgeatf dyknylflti
      601 tgrnditstl pkasrsffyp saslsyvfsd qfklptvinq aklrlsyari gkdaseystf
      661 tgyspytqlp tgtggltiap nlgnpglrpe ftntyeagle msffknrlgf dftyyyslsk
      721 dqiiqtqvss avgyvtksin agdirnrgve lvlngkpivs kdfrwdvnvn fsanrnmvls
      781 mpngiseivy gaargygnag vtmkliqgqp ygniygsyfn ryygstpedp ivldknlpll
      841 igangfpsis ggkqkllgns qpnyiigmgn tfkyknfsln vlfdarlgfe kynwledfys
      901 afglpdytad rrsykvfdgv langtpntkp vwlgqntvdg vnygegyyri yyrnvsepfv
      961 sdaswvrlrs asltynlpen wlpaksikna slsvtgnnlw lwtkyygvdp esssfdsgsn
     1021 ndgsagftyp sartimftln vgf
//
LOCUS       WP_121282500             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_121282500
VERSION     WP_121282500.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53571
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yynkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_121283090            1092 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121283090
VERSION     WP_121283090.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1092
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=120525
     Region          29..1091
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mehfyphlkr ltllmvyclc pfillaqtki sgtvndgtnq plpgvsvmlk gtktgtttdi
       61 ygrfiinana gqilefrflg fvsrevpada tnpmvitlmg dnknlgevvv talgvkkdnr
      121 kigyavstvk gedltlardp npvtgligkv aglsvgpsae llgapnvsir gntislyvvd
      181 gfpintdtyn ispddiesyt vlkgpaaaal ygnrasygai littkkgnkn kkgltidvns
      241 stvfnkgfla fprvqhayga gentfyqfvd gkggakggvd adydiwgpyf ngqliaqyds
      301 pvingvrqpt pytargannl nnflrtgsqt nnnialtsng enytirfsas qqhqnsyipe
      361 qyldianani yasfnpsprw kfegninfnr qttdnfpdvq ygpnsliynl aiwtgadwdv
      421 napdikavwq pgkvgiqqqf aeytryhnpw fmveewtrgh hknnttgyll anyklndhln
      481 atirsqidty gilrtekmpf sahpygregn egdyredrrd lfdnntelml nydytiknfl
      541 nlsgliggnm rnmsynsswv stdylnvpev yafsnsknpv qatsfssdmr vlsayyslda
      601 sfgkyatvst tgridkssaf qvpttyfyps lslatvvsdy ikmpsfisyl karasysnir
      661 sdatsttigp apfssitafg ggtaaslfnn plgygttyts pyngpdysln tsyatskpyn
      721 nqtagyasdy lyqngiktst rinyeegfdi kflksrlgfs gtafqyidgp rilpnaista
      781 tgytieylna lktkktgyeg slsgdvfqnp ngfswnvlan istykevyke lpqgqstyat
      841 ffkegdrtdk lygtafvrtp dgkiindaag kplvnptaqf lgneigkfsw siynkfqykn
      901 yslgvqfdgs vggviidymh nktmrggsna etaegalgaa ryqdwqnfgk agyngsyige
      961 gvvisnggsi nydsntgavl nygalqyapn tqvafvqdyv skyynvdean lmsktftklr
     1021 evtlgytfpk ellaktfiqk asvsvygrnl lyfykdkrfk dvdldqynya tastslqspt
     1081 vrsyginlnv sf
//
LOCUS       WP_121283178            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121283178
VERSION     WP_121283178.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109651
     Region          26..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtrlkitlfi ltmlccvqiy gqtplisgki idvsgqpipg isvkvkgtav gsssdakglf
       61 siksgnpatl vfsgigyttk efayngqsni titlsedqqn lneivvtalg vkrekrnlty
      121 ssqevkgeql tqtkepnlvn alagkvsgvq itsssgtpgs ssrivirgan slfgnnealm
      181 vidgipvnnd etgnlnmgpg tnriadldpn iiesinvlkg gaatalygsd gakgviiitt
      241 kagslnkkps lsfsssfsme kpllpeiqnk yslgsngvyf dgvnqktsts wgarmdtlki
      301 ngqpaqvydq sdlffktgkt ytntvavngg gaynsyfisy tnfaqdgtvp gtsfdrntvf
      361 gkfsteilkd lnitfslnya ntknnrlpeg yalespvwti ftapvsynlq palnpdgtqr
      421 lfrfsrnnpy wvldnisnts vvnrflptfn adykvlnwlt iterfgadvy veqgkyhesl
      481 lsvsnpngri vnnntnfrqy nndliigank sfgdftidal lgnnilstyt etayanglgi
      541 tvpgfdnigs tsninfkets yltrkigfyl qsnidykkfl ilsltgrydg tsvlaknnsf
      601 ypygsaatsf ifsnffskel sdimsfgklr lsystvgnas igpynlltpy eslpirnitf
      661 pyqqqagfli sqtlgnpnlk nerinefeig letgffknrl slevtyfdkk tnngiipnva
      721 lapstgfnat svntavmrnr gielllnakp iktenfswdl tlnysrirnk vlsinnnler
      781 ldngftvifp nqpygvifgt ryarnsegkl ligndglpfa adeqgiigdi npdwmggivn
      841 nfkykqftls fsfdmkkggd iqnnvdgygy fygtpkvted rgprvvegvn attglpntvs
      901 vsgqayyqra ngvlesviqd gtyvklrnvs mgynlkptwl qktpfktigl qvtgrnlwiy
      961 aphftggdpe vssfgssngs qgiysfstpt srsvdfslrl tl
//
LOCUS       WP_121283781            1074 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121283781
VERSION     WP_121283781.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1074
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117274
     Region          101..1073
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknillrttg flclvllscp qlfakiksek knfnryyfqq dttkkqdttk kapvakpads
       61 vkvppnplgg srpvttpapv paatapatpa stapaasagq ktitgtvvde qkiglpgvgi
      121 kiqgktggtv tqengkfsin vtaptdvlvf syigyqsksv pagngaaplt inlapsgaqn
      181 lsdvvvvgyg tmkskevtsa vahidtaqfr qsgarspldl iqgkvaglni tragssnpns
      241 gpsvqlrgvv svagsasply vidgipggnp dllqqddils vdvlkdgsga aiygtsanag
      301 vilittkkgk pgpptfnyss yirkefiqnr ldflsaeefr akinsgeina rdygasedly
      361 gslinrdnls qnhnlalsgg tdktsyrasl nyrdlqgial engrkeytgr lninqkgfdd
      421 klniqlnlat ninnanllsn gatseffnne lnrsgweeel gknptkpiyn pdgsyyydnq
      481 stnqyarlfn ntsyrkqqtt sadlkadfdi tkglkasvfg smqrdnyldg gyatlaseds
      541 fensdypsgg yafknnflsq ayafeptlqy ntvvadkhsf talagysyry nieegarmst
      601 rgflndqfne dnmgvgqala dgkasmgsyk ndntliaffg rvnyafdnky llqlilrreg
      661 ssrfgdnnkw gnfpavslgw nvteekfmen vkwvnylklr agygvtgnsg fannasrvtl
      721 gpggkylypd gsyretygpt rnpnpflkwe skretnigad ftlfnskltg sldlfdrttk
      781 dlldlyttpq ppyiqsqiya nvgnissrgi elalsyqaik tkdftfsmdf tgstikntln
      841 sysndafavk fktfggigga gdlgdaitty egedvgifyg krfagfdadg kwlffnrngq
      901 avrndqinns kdknltdlap lgnaipkyya sytanftykn fdfrvflrgk fdykilntta
      961 ltygnpfvtg snylrdafgk yseindtfmy sdyylengtn vkidevtlgy nfklktkfir
     1021 nlrvyatgqn latitgysgn dpdfvqdtgl gpgidsrgay pstrsflfgv nvgf
//
LOCUS       WP_121284129            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121284129
VERSION     WP_121284129.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118543
     Region          26..1060
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkstiyivm amlcfflkve aqvkkiaikg ritnekglpi anatikvkes ktttiangeg
       61 lfelnnvqlg ttliissigy kttelqniqk deflnvrmlt edngleevqv vstgyqnipk
      121 eratgsfvql enktlnrnvg vnildrldgv ssglilnkgl tngannpkis irgrstlfas
      181 aeptivldgf pyegsieqin padilsitll kdaaaasiwg akasngvivi ttkrggknqk
      241 lqvelsstlt iggkpnlyyq dqmsssefid leeylyakgy ytsainsgyr pvseaieifn
      301 nrklgkiskv dstnsinnlk erdvridlkr yfyrpsvyqq yqlnlnggge fnryylsggy
      361 dknmetsvsn afdrftlkan ntfslfkdhl eivgdigfas gntysasqpy lpyspydqiv
      421 sangeplsvi knlrsayvdt vgngklldwh ykpidelkan svlkqvqyki nlginynile
      481 eltlsakyqy lkesnsnenn ypqqsfytrd linryssivg ntlnrpiplg gilensvrnl
      541 iskilrfqld yhksfgsehd inaiigfegg dtrgnstsqs yfgynpetlt ngngtinpli
      601 fypyyyapst sqqiptapsl gsqtditqsy ytnisytykk kyiisgsarr desnlfgvka
      661 nqkgvplwst glawiidken flnsewissl klratfgyng nldknisgll tltntgsine
      721 wgsnysrvrn ppnpflrwek vktynlgldy vvlknrisgs idfyqkdaed lignnpiamq
      781 sgvfqfkgng aslrtkgidl ilnikniega fqwstaalfn yntdkvtsyk ikqtsngnii
      841 sgnynnpleg ypyyaifsyp sagldnsgap qgylngaisk nyseiislld tkqlkfhgsa
      901 spkffgsiin tfsyknlels fnviyklgyy frklsvfsgs nnysytsrdy sqrwqksgde
      961 lstkipalty pangamdsff lnsedlvdra dhirlqdirl syhltgqkis sflfknasff
     1021 lyaknlgilw ktnelsidpd ygtfnipqpf sgtvgfnlkf
//
LOCUS       WP_121284659            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121284659
VERSION     WP_121284659.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116297
     Region          28..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnlkflrkis lplllmlmas tmlfaqdrkv tgkvvdqadg qgipgvnvsl kgipsnvstn
       61 adgnftiqvk sdadvlvfsy igyvrqqiav gakttltvrl vsenkdlddv vvvgygtqkr
      121 atltgsvvdi kaseiedlpg tnvaaalsgr llgvgvsggi arpgvpakit irnpnaifsk
      181 dggstdplyv idgviqidgq gkpdatnfgn ldaseietms flkdasaaiy gtrggngvvl
      241 ittkrgrvgk prisysgsya vndeayrtkm msayqfgqym nilnganssn pklpgvdnff
      301 sndeleyfkt idydrledaw ksasdvrhtl svsggadkat ffasasynkq ngnlatldyd
      361 rwnfragtdv tvatnfkvgv qlsgnsgnlv ktfnkvsgeg veddyknlll apryvpdyvn
      421 glpvklpgtt ndlsryhfge inrlnnlatt ksnlfsvnvy aeyelpyikg lkarlayarn
      481 agnsvgdqvg tfytlyefnr lgenkhiyeg stvlsslkvt ngdrlyysnt nqkseqtnfv
      541 lnyardfgkh svsglftvek sesenaqqvv fkaspiaatn gqfnsatgai dgstsaneag
      601 slsyvgrany ayankylaef lfrsdastkf apenywgkfy sgsvgwvise esffkvpavn
      661 ylklryafgv lgndqtkawl wrqrytfqdg kggvfggnsa ttagfkmeaa pnrdatwste
      721 yknnigidak flknrlgvtv egyynlarni lieptaslpv tvggtvasin mgsadyfgye
      781 lgiswddkig kdfnygvsar fgwsddkvkv snfnandilk pwmpkpgess dngmwgydyl
      841 gmfktqdevt nyinqnkitq vfgvaanqlk pgtlyyrdvr gplqsdgsfa gpdgiidend
      901 qvqlskkatn hygfgitlka gykgfsvdav iagsfggwse iderkplnas iarnftslpd
      961 iwgsiydpai npggvmpnps fesinltpts nfykvnamri ripsfnvnys ipkiiveklk
     1021 innarvfvsa lnpvnlynpy tykgpdgawd aypnlrtlsf gvnltl
//
LOCUS       WP_121284757             318 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Pedobacter].
ACCESSION   WP_121284757
VERSION     WP_121284757.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter
  ORGANISM  Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pedobacter"
                     /db_xref="taxon:84567"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34042
     Region          10..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqenehvqc liigsgpagy taaiyaarad lkpimytgmq aggqltqttd venfpgypqg
       61 imgpemmedf rkqaerfgtd irfgyvssvd fsstphkvvv deiktitadt viiatgatak
      121 wlglpseqqy ngfgvsacav cdgfffkgqd vaivgagdta aeeatylakl cktvhllvrr
      181 defraskamv srvlatpniv vhyntetqei lgngknvtav kvlnnktgve sdiavegffv
      241 aighkpntdi fkgqldmdet gylttkpgst ltniegvfac gdvqdmyyrq avtaagsgcm
      301 aaldaeryla akehpvea
//
LOCUS       WP_121285092            1035 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121285092
VERSION     WP_121285092.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1035
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115113
     Region          139..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknictaall llsgvtling qqqdlskikv nysvgkisae damkgflaen kiksfaysnn
       61 dlekhriqgt kcinesvlgc ankilkglpl ealifnntli irqkilkvse madteelipl
      121 aaipqkrnds metsrketki eevvlnagyy kvkdkertgs iakisakdve nqpvtnvlas
      181 aqgrmagvni tqnggtaggg yqiqirgqns lrtisnsgid gnqplyvvdg vpisgqapsq
      241 fagpalpggs inplnsispq diesfeilkd adataiygsr gangvvlitt kkgksgrlgl
      301 sfnsqysfsk alsnldmmdt qeyiamrrka fsnngvsvyp ataydingtw dqnrytdwrk
      361 elignlasas ntqlsltggn etttflvsfg hqeqgtvhak dfkyktnnis tnlnhqskds
      421 rfrlnisslf snqknnvine dltktaytla pnapalyhpd gglnwqnntf tnpvaaynas
      481 ysnnnvqfmn nynaeyellk nvsfkfnggf nyqgfeewsl rpntiynpaf vtgqssaysq
      541 askfnqhrfs yilepqlnwn fqkgshqfdi lvgatyqqdv srqgsitgig fesnsfieni
      601 aaaqtkvigd qisskyryaa lfgrinyqln kkyilnvtgr rdgssrfgpn nkfadfgavg
      661 aawlfskeni fkdsrwlsfg klrgsigtsg sdnigdyqyl dtytilstsv yngvtglips
      721 rlynpdfswe kttkmemale fglfksrlnl taayyhnrss nqlvgyqlpa vtgftmvnan
      781 ldatvqntgl eleanahpiv tgdfqwqtsf nisfpknkll sfpglsgsty antyvigqpv
      841 diirlyhleg ihtqtgqyqf tdynqdgkvt stddrqiien lsvqyfggws nqfryanwdl
      901 sllfqfvkqk srnynasmas pglmnnlpke llnvwspenp sgyympyrss vntlhslfqn
      961 sdatvsdgsf irlkniqlsy riplkesslf rdvkiyfqgq nlwtwtryfg idpesgtssf
     1021 lpalktyafg iqfnl
//
LOCUS       WP_121285112            1203 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121285112
VERSION     WP_121285112.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1203)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1203)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1203
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=133900
     Region          150..1198
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mifssncryp ngyspavyws pvphreqtth lkkilmrlhf illlllftvi valaddvkaq
       61 sitleakatp myqvfkqiek qtgylfwykg kmlgkntpit asinnlqlkp aldkifanip
      121 fsyeivdeti vvtekllpqk skekqnkqgi tgvvndengq plvgasvtik gttqttmtds
      181 egkfaidnvs dnsllvisyv gyksveikaq nnksisvtln lisgklddis vvstgyqnip
      241 keratgsfvq idntllnrri stnildrldg itsglifnkv agpvgiaptn eklginirgr
      301 vtidskvsad plvvldnfpy egdinsinpn diesitilkd aaaasiwgar sgngvivitt
      361 kkgklnealk idlntnitig espnlkysrn flnssdyidi ekylysqnyy nqdlanttty
      421 pvispvvall arntaeanqq idalrsidvr deaskhlyqk slsqqynlsl rggsaksthl
      481 lslgydknry nnigagfdrl tintsntyrp iknlevsaav vynksnqssa yiynplypyl
      541 kladadgnpl svpvgfnnty lesaqalgym dwklrplqer dlfdnvakin nlllrtsvry
      601 qflpflsaev qyqyqnengn trylqsidsy nvrntiniys qrntttgvft ypvpkggils
      661 mtdrkleaen frtqlnynqn fagkhnisai tgaelrdiet tsynrlsygy nddfgtavtn
      721 lnyttffpls pagtgsrtvp apdgtvngtv nrfisyyana sytfkdryta tlsgrkdgan
      781 ifgantndki tplwsaglgy eiskeafynl plipylkvra tygyngnvyn assyltatys
      841 tssltgaqta titsapnpel rwekirnknl gldfatkknr lngtveiydk lgtdliedal
      901 lapstgfnsf kgnaasvntk gvdiilnsin lngdfkwytn flfsynkdkv isydtkytts
      961 yltsnasnia dparqglyik egnsifgvys yksagldpss gdpvgylngi esknytails
     1021 nnnpddviyh gssrpthfga lrntfsykgf slsanvtykf nyyirkksts lnytetilpv
     1081 yansdyalrw qkagdenitt vpsmvfavnt nrntfyqnse vlvekgdhir lqdiglsydl
     1141 nqnllrkmpf sslqiysyin nvgilwrank ngidpdvsdy rsgnynvfpn pityafgvra
     1201 nfk
//
LOCUS       WP_121285195            1045 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121285195
VERSION     WP_121285195.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1045
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113504
     Region          37..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meksylkwss gffvillipf llllftekaq aqnkrytisg kvtdasnnep ipgvvvkiln
       61 tslatstnsn gaytfavdla sgkyqiqfsy vgykskaqsi dlasgdqvql stslnadavg
      121 ldevivtgts qgttrkelgs yvstvkgddl nkapsgnvls slqgktagaq isqnsgdpag
      181 glsvrlrgis svnssseply iidgvivnns ttrvtntsan ydggnfvgsi gqnrmvdinp
      241 adierievln gaaaaaiygs ransgviqif tkkgvsgaaq vnfstsltls hlrkqvevne
      301 spvrfgtpin fptqdviqtv gdppflqtqk ipatrynyqd yifqsatgtd ntisvsggne
      361 ntkyytsaay fsnqgiiknt dftrynfran idqkitewak fsaglnyirs sanekpdgns
      421 ffspmnsvti ignihdifar dangnlmavg ergrvnpvsv iedikqrqet nriiananlk
      481 lypvknltld ftlgvdnsgq sgstyippfa ynvnpdfygg gaaldgtlng yasaatnnaf
      541 qfnnefnaty qaklseliss ttqvgysfqy ektryqlvng rglaplietv naaatqlpsv
      601 dgrtelsvsg gyiqqnfkyk dhlfvtgalr vdqssvfgad nrtqeylkgs lsyvlssady
      661 wksfgvsdww dtfkiraayg esgnltgiga ydrinaystq sflgraslfs satlanenvk
      721 perqrelelg tdlsffknrl glqfnwynkk vsdlliasvq apstgfssll dnigslrnkg
      781 ielvlngtpv dgkdfkwnts vvfnrnrnta ldvgglrlfs tnpgapvaii ngeaigvfyg
      841 tffarnpdgs lltnaagipq iekgiqnsat tftpqrdang lptgttlrkv ignpnpdynm
      901 sfvndftykk lnlhvqfdav qggdvwnadw rtrqgvgngk vaeqeqlgql prgyvagvya
      961 ieewriddgs fvklreisls ynigklkflr dltvtvsgrn liswdnykgy dpelnsggqs
     1021 tilrnidfgs vpiprtfslg lqvkl
//
LOCUS       WP_121285479            1073 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121285479
VERSION     WP_121285479.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1073
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115866
     Region          23..1072
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllpslfi cmlfalsala qdrtitgtvt ssedklpipg vsvkiqgatg gtstsadgkf
       61 sikvasdaki ivfssigftt qskpigssnv inailssdan aldevvvtal gqvrkkntls
      121 yaaqqvkgee ltltrssnav salsgkvsgl qiiqgnaigg stnvvirgsk sltgnnqalf
      181 vvdgvpvdns nnnstnqttg rggydygnaa adinpddies vnvlkgaaas alygsrgang
      241 vimittksrk skgmgitins gltvgtidks tfpeyqteyg agyssgyesg dgfllidvqg
      301 ngvkekvvpt sedasygakf dpnllvyqwd afdpyspnyk kktpwvaaan npstfyetai
      361 snnnnilfsg asdkgtiklg ytrsddrgtl pnskiiknil nfgstyqitd rltasalany
      421 skveglgryg sgysglnvnq nfrqwyqtnv dmmaqkdayf rnkqnvtwnw sdpstpeglv
      481 pkytdnyywt ryqnyqndtr srifgnasln ykatdwlnil grvsldtyne fqeervavgs
      541 qgaasyartd rsvsetnfdl ianfdknvtk nlnlkaligg nirknllnsv fsttnggliv
      601 pglysisnsv gavaapveky eprevdgffg gatltynefl tldgtfrrdk sstlpgvgna
      661 ynyysvagsw lfsqqlkdkv dwissgklrv nyatvgndap fgsiknvyts qnlfgssilf
      721 aypfttnnps lkpektesse iglemaflnn rigfdasyyl tksknqiipv avsaatgftn
      781 tyvnagvirn ngvevslygs piktqdfswn ininwtknns kvlelyndsk nlqlgsfqag
      841 isvnatlgqp ygtiqgkdyv ynangqkvig adgyykitts ttnvigninp kwiggiynsf
      901 kyknvslgfl idirsggnvw sldqfyatyt gilpntvgln dlgnpvrnpv tnggnsggvi
      961 ldgvtengqv ntkrvvidan sptlpqsafs ydasyvklre atltysfpka miskwgpvkg
     1021 idlsvfgrnl wiihknlpys dpeenlssgn vqgiqsgayp ttrtiginak lsf
//
LOCUS       WP_121285483            1070 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121285483
VERSION     WP_121285483.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1070
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115863
     Region          23..1069
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfm lmlcaisata qertitgtvt aqddklpipg vsikvlgttl gtstdpsgky
       61 tlkvpstaks iefssigftt qtreigsqtv invalssdsk qlgevvvtal gvsrekktlg
      121 ysstqvgtde inrgaptnav aglqgkvagv disttsgspg gsskvilrgf ssvggnnqpl
      181 yvidgvpinn srpggtsapg tvgdisenyd fgngandinp ndietisilk gaaasslygs
      241 rasngvilit tkkgkagalk idlsssasft nvaivpsiqd qygqgwskqn wlaengswgp
      301 kldgmtrpwg pivdgdqetk pfvavkdnfr dafdtgqefn nslalsggne tstfhlsygn
      361 iysngilpga ndtykrnnfs lsgstkykgl tvsgsanyvg kntravqtgq avsgigssfy
      421 edllqipvdy pftnfkdynn kfynvdnyfs pfsqnpyysv yengsrfksd rfygnvdlky
      481 katdwlsfqf qqgadltnna skfwnaknnp aigswagggn degytrqesv gnviegsery
      541 feydsklnal ftkkfgndfd ingligvnyn drgyrsvytg venlaipgfy qinnsandpt
      601 stsaenerrl fgayasatlg yknyafltln arndwsstlp adnrsffypg anlavvlsda
      661 ldlssakisf lkvraavgqt gsdtdpyrif ntlsrtsaal gfgniifpia gvpgysvsdi
      721 lnnpdlkpei stetefggei rffnnrlgld vsyynrvtkd qiipvvtaps sgvtsrivnf
      781 gkirnrgvei altgtpvkne nftwdigytf trnrnvvlel pdgldklvln taydaqfvar
      841 vgqplgvlea pvpkydpqgr ivvgsngfpl ladnngsygt sqrdfimglt nsfkfkeftl
      901 gftldyrkgg vfysgtadll nfvgndiktl yndrrtfiip nsvvqvnnpg ggisyventt
      961 pisegnvnal yytnngkava yqnrildktf lkvrditlsy slpksiaqki radratltvy
     1021 grnlitwlpk enrtidpevs nfgndltsef gefrtgpsvr nvglslnltf
//
LOCUS       WP_121285489            1089 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121285489
VERSION     WP_121285489.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1089
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118119
     Region          23..1088
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfi llflastaia qdrtitgtvt sqddklpipg vtvkvkgasa gtvtdsngky
       61 svsvpsgsni lefsyigyvt keqvisanav initlsadak tltdvvvvgy gtttkqaftg
      121 saktisadql gnkrasnlsq alagevsgvr vitqsgqpgt eakvrirgig svsgnrdply
      181 vvdgvpfygs lnsvnindie sttvlkdaaa taiygsrgsn gvilittrsg rgksafiegd
      241 vnfgtnmall prydvikspe efiglawegl ynqgrglatp ltdaaaitya narifgptgg
      301 glpaasniwn stganlidpa trqvrsgitr kfdpenwedy afqnssrtea nvriggssdk
      361 tsyftslgyl ddigysiksn ykrlnarlnl thevkpwlvg gmnlgytnsk rnfggqtsds
      421 gsifwfvdni ppiyplflrd tkgaivqdpi fggnqydygn agrrfgsltn aiadtqyntd
      481 rddrnelngn vsltakiipg ltfentfglq yynnesvsrt nkyygsaasq ggsiylents
      541 lmsynllnlv rykktfgens lealaahevt dwklktlqas rynlvlndse dlnngtvtnp
      601 snsyseqykl esyfgqinyd yqkkyflsgs lrrdgssrfk tnrwgtfgsv gaawlvssee
      661 fmksqnifss lklkasygli gdqggvgyyp gyntfnidnv ndqpglsidl vgnpdltwet
      721 skmfqtgief nlgtyltgsv dyylkntddl ifdrrigpss gyaivkvngg slrnqglefd
      781 ltghifkkkd fyldlginge ifsnkmtamp idpstglqkp idvqgnyaws vghsiydfyv
      841 rkytgvdaad grstweayyl dannngvpdg gllenqagey igslgsylaa npgkeaqlkk
      901 tttktyqnat qqydgrsaip dvrgainltt gykgfdlsvq mlyslggyvy dgayaglmgn
      961 gliannnwhk dilnrwqsps qpgdgivpri snnqdanvss assrfitkad yfslnnvrlg
     1021 ytfptkitgk lgltglsvwv sgdnlylgts raglnpmtae panstetggs ntyrysplst
     1081 isaglrvkl
//
LOCUS       WP_121285498            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121285498
VERSION     WP_121285498.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113327
     Region          23..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkllqslfi llfiatsaia qdrtitgtvt gkedgmplpg vsvkikgasg gtttgadgky
       61 svkisqqata lefssigfls qsrnigssns invtlesdak slnevvvtsf gvqrdkkslg
      121 ysttkidadv ltaskatnit nqfsakvpgv rvqgsggaft gasviirgmt tftgsnqply
      181 vvdgvpidns ggntplqtgp slsnraidin pedvenvvvl kdaaatsiyg srgasgvili
      241 ttkkgkkgek gtitfstnya igninrlpey qneyaqgnng lltqanigna tvlgsgvsts
      301 wgpkivgqti tnslgqkeil qaypdnvkdi fkqsynlqnn lsfsggteks tfriaygnst
      361 etylldnnkl krnnltfsgt tdvtskltvg asitytntss irtlqgnqls nplfrayftp
      421 rsynltdlpf edangnqlwf ggednpywsi kynkyndevn rvlgnvnaky kftdwlnadl
      481 kvgsdffnlk skgfdeignr gggfagansr lvggivdqvn nvrnvssyft vnanktfgnf
      541 nlsgtignei nqnyignaqv tgytlvvphf nnlknaltyn pvfgssktrl mgvfadfvad
      601 ykgylslnvk arndysstlt qanrsifypa aalsfvatda fpelkseryv nliklrasig
      661 evgkgasays tetyydksaa sdgtgaiinf pynglagftl ndgagnpdit peftreisfg
      721 telgffrnrl tvdatyyirn trsvilsvpy satsgitsvv knagklstkg felliggtpl
      781 ktadfswdvs vnytkyksiv eelapgvtvi tlggfttpni rlvagdeygq iygsayqrna
      841 egkllisptt glplasadvv kignpnpkyt mgisntftyk sfslftlldi rkggdqysrn
      901 iadvqrngva aetgefprfe adgvtqtkpy lfegvyasga nagkpntinv raqdyygntg
      961 kyvaaegyiy dtswfrlrea slsyrlpsgl igknifksie lgvfgrnlyl kaknyphfdp
     1021 eqnalgisna qglefnslps trtfgvnlki vl
//
LOCUS       WP_121286274            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121286274
VERSION     WP_121286274.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113702
     Region          53..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmkkkllplv ftctvltvfi lfesasasag elktvifsks lpakklklap igitgkvtde
       61 qgvglpgvsv aekgtrnati tnssgsytis vantnavlvf tsigykpvei tvnaktvvnv
      121 smltvtnaln evivtalgik reakslgysa qkadvealqt nrttnlansl egqiagldis
      181 ppaagpggst kirlrgqssf tadnsplivi nglpmsqgas ssngytqnvd qgdnmqginq
      241 ddiesmtvlk gstaaalygs ravngaiiit tksgaknsgi giefnsnftv nqaldytdfq
      301 yeygqgenni rpssvgtaqs sgawsfgvpf dnvptyqfdg vqrpyapvkg riktffrlap
      361 swsntvalsg gndkgsfrvs lsnqdaqgii pnndyhkkif nvginyklte klsaqfyvny
      421 dhqfnnnppl igvqgnaipt siyrlansis fdvlkagaid angnetptsr fatitnpywi
      481 lakqfqrqtk dhllgtavvr yqffdwlylq granmdllqt tyesntptgt lavsaaptgl
      541 yngsygists ntrqnnfdfl lggghkwkdf sfnatvggnn fplitstfne avtnfyirdl
      601 ytigngvtan ssynltkqtv nslygtaefs ykdllylnvt grtdwysvla rdidhyfyps
      661 isgsfvfsel lpktkwlnfg klrvavaetg saqgvgayna ltfllaqnsf nglplgsing
      721 taspntqikp fgvnekeigi elrmfnnrvn ldvaaydkkt tnqavpisls aatgyattlv
      781 nlgglankgl efnlelvpvq nknftwktaf nsafnsskvl slannqsqlv vgspeffgsi
      841 vhmvglplnq ivgstykrda sgnivlsggk pvasdkpvsf gsglptatgg wlntlnykgf
      901 tfishidyka ggkllsstsl nllreglske slpgreggvi fpgvnatdgl pnttavnaed
      961 fyanyrstni ldpfiysssf vklrslslgy dlskfinkky vkslvlsavc rnvliikkyt
     1021 pnidpeaias sgdnltgyeq aslpttrtyg fnlnikf
//
LOCUS       WP_121286634            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121286634
VERSION     WP_121286634.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116976
     Region          23..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrlllmivl lfcaslvgaq eslrgvvrdv sgkavsgvsv kgaavevfsg edggfvlsgk
       61 agkvrlsfsa mnfdkldtlv slpfsgllev vlvgmerqle tvevstgyqr lpkeratgsf
      121 lqlsgkvlne qvgtgiiarl egitsslsvd rksnggegyg iiirgigtlq gprsplivld
      181 nfpyegdinn inpndvesit vlrdaaaasi wgaragngvi vintkkarfn dklkvsfsgs
      241 lkvtgkpdqy yqskisvddf idlenflfdk gyytsfevgt araplsevve lriaardgli
      301 nagdaksrid vlrsydlrrd ldryvfqnat aqqyslqmga gsekrnwlls agfdhnvssl
      361 aapfsrynlk aeqnfkvtsr ltltgnlmlt ytnskngrtd psqinsatgm lppytrlade
      421 ngnslpvitd yrtgyissag ngkfldwryy pledykytrs vnnvndvlas frasyqvldw
      481 lkvaatyqfe qqdgkiksvn tpqsylvrnl vnifssidag gtlkrniplg sivdqdysll
      541 qghnmraqad idkvmgrhal sgiiggeirs ngtetnagrv yglnestltt svvnyldpvk
      601 tfvtgnleyi tnrdafgktl nryvstfanl aytfddrytl slsgrrdasn lfglktndkw
      661 nplfssgfsw diskekfwrs slisflklrt tfgasgntdp rstavttity agfnsvftqt
      721 pyaflsnyan pelkwervfm fnaaldfgfr enrikgsley yrkksvdlla ltpidltagv
      781 gativknsgv iqgdgvdlel ssrnltgkfs wttdfflnyy kdkvlknyns tfngrgklng
      841 nvsytglvgy plygmisfkw agldpatgdp qgilngavsk nydalmgssl kfedmvyhgt
      901 alpifsgglg nsfsyagftl svrlsfklry yfrknaldyg slfigregna dyakrwqkpg
      961 delitsvpsl iypnsnvrde fywgsevnvl kgdhirmqyv nlgydfkpag lkktgfsrlq
     1021 lfvvasnlgi iwrankegid pdymgipdar siafgfkssl
//
LOCUS       WP_121287229             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121287229
VERSION     WP_121287229.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33311
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkctgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121287246            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121287246
VERSION     WP_121287246.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113017
     Region          110..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnfvqriill iglifplcap aqtkvtlnfn ganfeqvvea iqqqtvyhfa yseskipkhq
       61 vsikveeeda vkvidqllln sgytysllpn hlivirknag gmetdsvrfl kevvitalgi
      121 ekdndkvgya lttikgssit karesnlima lqgrvaglni tdvnggpgsa arvlirgvss
      181 mtaasplfvv ngvpidnsir gsaneyggad ygdgisninp ddietitilk gsaasalyga
      241 raangvilin lksggentka kfeyntnlaf dvpvnstdfq ylygqgtqnk rpadlynais
      301 tgllswgemm dgkltpqvdg smrpyapvkn niqtfyriap aftntlslvg gntknnyrvs
      361 vsnldynsil sngalnrktl nfygtvalsp kislsltgny iyewnknksy lsdgplnpny
      421 gisalatsld qsilapgfda etgfesrwna deyktnpyfl mnkqadhasr nryissavlk
      481 yqlaswasvq grigydsskd elvsilptgi afsinrqggi naydqnltse lnsdilfsat
      541 rnlsdklnle lsmganyrer kgnseklkgs qfkvpylytp enlitstktl aisrivtesa
      601 yytadlsyqh flnfsvtgry diystlpann rgifvpgvsg sfifsdllkl kalnfgklrv
      661 dfaktsgepi vpyttqiyyt iddqvngipv gsfssdlpny nlkpftlnei eagldlkffn
      721 srldidftyf nrvthneiin akqsvttgft sayvnlgetr nagielalgy tpiltttskw
      781 qvnlnltkvk ntllsidgns nytltgtyrp lnantalvvg kpitqvmayd ylrdaggnii
      841 igsdgipkrg nfipmggtmp tlyggitnsf nykqfsfsfl idyrfgnkil sateyysyvl
      901 glnkatlvgr etgivadgvl engqkntinv payayypela tnisalavln gsfvklrqat
      961 lgytfnnifl krtpfssigi dlvarnlftl lkysknidpe sqfsptlgya giegaslpat
     1021 rtfgvnfnfk fk
//
LOCUS       WP_121286905            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121286905
VERSION     WP_121286905.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117883
     Region          55..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkrftypas fslkkslwvt clfiaifnsa fsipktneeg vpkplqqkkt aenakvikgh
       61 vtdekkmgip gvsvlikgtn tgtvtnqegd fsikaddgdv lvfssigyvn keikvdhsdt
      121 yqivmtedak alsevvvtal gvkkersklg yvaqtvqges lvkareanli ssltgrvagl
      181 nitnstdlfq dpgislrgrk plividgipd qsadlfrvna ddvesvtvlk ganasalygs
      241 igqngaimit tkrgkgnnls idvnsstqiq psfiripkvq teygagykgk ytyvdgsggg
      301 pegsgwiwgp kldqpdpttp sgffetpqfn spkdpitgkl vplpflsrgk nnvedffqtg
      361 lissnnisit qssekgsfra sashiyqkgi vpntdlnnss fnvsgnykls daftidarln
      421 ynrqftknfp etgygptnyl ynlilwtgad vsvqdlkdyw vpgkegiqqr nynvsyynnp
      481 yfqayeylrg ydkdntygsl nlnykispaf svqfrnglnt yglnrtykep msyigygnks
      541 rgqftvatqn yidlvtdlig dynhtfsdkf klhaqvggsn yyrnhkygst ntdglsipgf
      601 ynlsnsanpl qgsnaveerr tssvyaildl eflngiylta tgrndiistl ptnnnsffyp
      661 sigssvvvsq ltklpdwfsy lkargswsrv ssgtlgddty tygylpafdk gtswnstpal
      721 tfgrllkqvn ltpqtsdswe vgldtkffkn rlsveatyyq tsdfnniasp disitsgygs
      781 qlvngnvyqr kgmefvvngt llksndfqwd mavnlskyrr ylkeiyggae tlgnlrvgdr
      841 tdriygsvyq tnnqgqiiyg sngfplndnf srfigneapd wtygientfn yksftlkflv
      901 dgrigglmys ttnqkmwwgg thpgtvnqyr idanagkatf vgdgvvvtsg aatydakgni
      961 tsdtrvfapn akavnyidym ietsngaynn ynyfsqtflk lrevtlgwqv ptkllgksfv
     1021 kgldfsvvgr nlllfskmpn idpdpakdnl qtpstrsfgf nvnlkf
//
LOCUS       WP_121287344            1036 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121287344
VERSION     WP_121287344.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1036
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111033
     Region          40..1034
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkslqltcl llyasaglya atpadhskra vsyhsvyqdv ikgtvkdetg npvpgvtiti
       61 kgaqggtqtn tsgqysiaak tgdilvfsfi gyqskevtvg tqstldislt pdsknletvv
      121 vtalgikrse ksltyttqqv sgeelnkvks pnlvnslngk vagmtispss sgvggsakvi
      181 lrgsrsvsgn nqplyvidgv pisnngnana qqnsifgggq dggdgisnln pddiesltvl
      241 egasaaalyg sqaqngvili ttkqgkagkt qigfsssltf dkiaykpefq nsygpasttt
      301 rdswggpisn ttdnldqffq tgtnatnsin fsggseiaqt yfsyantyas giqegnklnr
      361 hninlretak flnnkltvdg nvnyinqrin nspsiglynn plvglylfpr gvditpykdn
      421 yllagnvgta rqnwlggsad inqnpwfltn lnpntairnr fllsgnvkye ftpwlnlqvr
      481 gnidrttddf enrrysging nfnsngkgyl sqntqtfiqk yadailnvtv plkgsdfkin
      541 gliggsindq kttglslagd lsavdlftpn ntivanagty tsdilnttka ndafhsqlqa
      601 vfananlsyk dwafltltgr ndwssnlaft pnisyfypsv glsfivsqma klpeaityak
      661 irgtyaevgn avppyltfvq ntlgnggaln intnrafael kpertksfei gtdmrflanr
      721 lnfsftyykt ntknqyipvk pappglvgtg ylnagdvqnq giqftlgadv lkgdglnwnt
      781 gingslnrnk iidvaasqgl nsidltgggn nayisriaag gsygdiygyt lqrdangrii
      841 lsgdgtaanp yfpvksgdys liananpkfq lgwnnsfnyk dfslsflvdg kfggkvlslt
      901 ealmdqagas kvsgdaraqg gvkidgvdas gkavsatinp qsyysflgdr ngvtgeyvys
      961 atvvrlreas igynlplkgt fksmrlslig rnlfyfykka pydpevtmst gnglsgidvf
     1021 nqpvtrsfgf nlnvlf
//
LOCUS       WP_121287534            1069 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121287534
VERSION     WP_121287534.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1069
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117733
     Region          31..1067
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mektstkhcy vkfltatlfy llipwlafaq ktikgtvvdq tnkpipgvsi iekgtkngta
       61 tnadgkftlt vqkdnaiima rivgyrslek pasasgtlnf sleednntln evvtigyqki
      121 trkkttaais sisgkelanl paasfdqllq grlsgvnvqn ftgqpgvapt vsvrgnstgs
      181 tgydqynvvr splyvvdgvp qssddyvppg tgtgtnymag lnpsdiesid vlkdasaaai
      241 ygsraangvi littkkgvgg dtkvsfnsyy gmvqrpnlrq atmgtterrq kmevlqrqls
      301 ydqrvqlpyi ltdslnpafn ghtdwqdlff qtgkindnnl sisggsdngt tyrfsggyyn
      361 edgivkgtgy tryttrlnlt sramnkklmi npifyyssss rgrgnedpnd pskptkigsg
      421 nlpsslfsis pekldyyvsk dgenlnknva nqfgvnlnls yefnknftln sqssytndnt
      481 rrdvsmsnll nsgfgnssss fsssamglrt snylayngsi kkhsfsavag qdieynlfqt
      541 tqasgyggas dniqtvtgfk qenifgfssy aahglvayyg rfnydydgky llsgtirtdg
      601 ssgfgennky gvfpsisagw llseenfmkn lsnnpftlik irgsygatgn edrrnayvqy
      661 nrylvnnggf egngtangvf ygisgatsyn gvtaitpnfv ngvaqkdlsw ekstqwnigt
      721 dleidngrya isfdvynkev kqklfnvdlp vtsgynsayt nafavrnagm dltltanpir
      781 kefkwfstln isyvknqims lpnggrdiil sgdrfdknhv lsvgspinaf ylyrtkgvfs
      841 tsadipqnpy tgelyrnsng tfnagdfyla dldgdyfldv fndginpdka pigdpnprft
      901 ggwtnnfsyk nfslsifvnf tfkrdvlnlf dsdrfansqa ggavnnfayf stpdldrlni
      961 wrnpgdqaey akfdlgtyry yytgaqtffl ekggyarirs inlgydfspk lvrklglsql
     1021 klyaiadnvy mfqqskklpd aeavngygey ngtgypiprk ytlgvqvqf
//
LOCUS       WP_121287682            1048 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121287682
VERSION     WP_121287682.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1048
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116218
     Region          28..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrnillytl livciiyctn aysqekniiv ngrvldketk qgvpgvsvvl qstnkgltqt
       61 ngdgkfsvnv pvggtllfkf lgyntssvki tnqtnitvti sedrkdlndv iivayqnrpk
      121 ettagsvtvl sgkdvsdipv snietllqgk vpglniqnnt gapgfrgsvq lrglsslsis
      181 gsgndsflqp tsplyiidgv pldadkaaef gfqtqgpgvs plslipqedi eniqilkdaq
      241 atsmygsrga ygviiittkr gnskvpriky vsnffvnapp klretlggns erqlkiqqii
      301 lnaetinqir gisntpflad slnayynnst dwqdvfyqtt fnqshnlald ggdqkfnyka
      361 nmgyyaekgv ikntgynryn lnmnmefkpn dkfrffgfvn gsvgkqnkgn gagllqsgva
      421 sngqastllp ppsfyqasgg vlsalqtlnd nnsrnlrani daryefipgf aasstlsydy
      481 tsdtettftp aaangsfakl ydyngrnfql ynrnaityak tlgekhnffi ntfneiykqg
      541 sqssisrqer ipndqlqgpv gfdgyysrgg gvlssyknat iasfagslsy dydkkyvaef
      601 syrldgtsss glenpyskns siglrwnfnk enwltdqkwl dygslrltwg qnivptgnlq
      661 siygiynlng nynntqtigi nydlipnpal kptttsqynl gfdigflnrf sivvdsyfkk
      721 vdnllfdril snttgfnkls sndlgianyg teinlivkav tskdfdlsfs ingaynrdvl
      781 lklpeeyngq yirfdgsgyl qhnvfrvgrn tlsnylrinq gvyktdadvp vdpvtgkryq
      841 tnntffyggd pilkdvngdy ildgrdyeit gnsqplitgg lsitmrykkw glnmyasyta
      901 drtilnnala driaimrdpy alnavvplgd lniwqrpgdv akypypydfs rygniqplra
      961 dqtlwqesgt ylkinnltls ymfdkklirr fglanlrifg stnnlitfsk ytgpnpenvt
     1021 algrdisngy pvprtynigl nlelntgn
//
LOCUS       WP_121287693             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121287693
VERSION     WP_121287693.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108085
     Region          29..994
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrvfyllkqg flvllvfsal mvkaqtgsvs gkvldetglp lpgasvivkg ttrststdad
       61 gnfklaglsn gsvtlsasfi gyqtldkavs istnatvnfq lvpdaqklne vvvigygtae
      121 kknltgsitt vgakdfqkgt ittpeqliqg kvagvniiss sgqpgvgsqi rirggaslna
      181 sndplividg vpfsgksidn apsplslinp ndietftvlk danataiygs rasngvilit
      241 tkkggtgapv infstnnsva tiakkvdvls adqirtfvna nptaaydvgk tfvsllgkan
      301 tdwqneifqn afasdnnlsi agkfhgvpyr vsagyldqqg llitdrfnra tgaitvsprl
      361 ftdhlkidls lkgtlteshf andnnnaian aiqfdptqpv tatnqfgnyf ewlradgsln
      421 pnaprnpvaq imlrnnngna arsfgnvrfd ysfhflpelh anlnlgydvs kgtgrifvpa
      481 faatsfstng sstqslntsn nkvsefylny akdvasirsr fdatagygyy dnaktnfsfn
      541 eysatgvlrt tpkfpfsvdr nkllsyygrl vytladkyil sgtmradass rfaeenrwgy
      601 fpsvgftwri agenflkesk avsdlklrls ygetgnkdgd tvgdysylak yysnsntgqy
      661 qigdtfydyy apsaydpdlk wettttynag ldygffkgri ygaidvyykk tkdllatvni
      721 pvgtnfnnnl itnvgnmdvr gaefslnfaa iktenvswdf gfnaaynkrk vtnltlnpdp
      781 gskqgagdit ggtgvtikyn avnqlpgafy vykqvynsag kplegvyeds ngdgvvnssd
      841 qyfykspdpk itlgfntafs ykkwtistvl ranlgnyvyd nvssnfgirn nilssaglin
      901 naavdflntn fttsqylsdy yvknasflkm dnlglaydag klfknsntsl ritancqnvf
      961 viskykgldp eltdgidfkl yprprtytlg lnvgf
//
LOCUS       WP_121287988            1150 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Pedobacter
            alluvionis].
ACCESSION   WP_121287988
VERSION     WP_121287988.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter alluvionis
  ORGANISM  Pedobacter alluvionis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Pedobacter alluvionis"
                     /db_xref="taxon:475253"
     Protein         1..1150
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=126695
     Region          127..1149
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkksavtsql ifsvmrfftl iyimlstmlf vgqaspvnaq qlnvkvsini kkgsltelfk
       61 tiekktglyf vytnkdaiek qnlsgfkaen eavsalldrv lppfqltyli eknqiiikks
      121 irikgkvtde kglpvpgvnv iekgsnnats tnlngefnln vlnnqallif kmigyqsrev
      181 alngetelni slspdetals dvvvtalgik raekalgysi atvkgsdvnt vkevnvinsl
      241 agkvagvnvv stgadpgsss fitirgqssi atdnqplfvv dgvpvahslr atsevgrssv
      301 dygspiadis pddvesitil kgasaaalyg sragsgvvli ttksgsvnkk glginfnsna
      361 mydqawmfph fqhtfgggey tddpasstts awgprldagt khlqwnspld asgkpiatdw
      421 vshpnnpqdf yetgatytnn isisgknadg nyrlsytnls nkgivpntdl krntlnlsat
      481 yvlhpklkis tnigyvnnks dnrpsayres vtqmlyslpp nmnindlkny wkpgrenieq
      541 fsaddsdnpy fvayehtngy drnrltgnvq avyditknls lmvrtgldmy neahetkrpf
      601 sskrfkfggy gvdnsffkeq ntdfllsykk llnqdwslsl saggnqmnqt nrstaqktes
      661 lsipgvynia naqagtivns qynsrkrins iyglgqvsfr dmvfldltgr ndwsstlpag
      721 nnsyfypsas lstiitdvfk iksdvlsfvk lranwaqvgs dtdpyqlynt ipfnqdwgdv
      781 kratiefnlk nnflkpeiat syefggdlrf fksrvgidvt wyktnkrnqi inipttiasg
      841 ssnrlinagn iqnsgweigl navpfdgsfk wetnvnftkn enkvielsdg lkeysmgsad
      901 gdnirylike gtkigdfytp sytkvssgpn agaalldktg hyirnnseyi kvgnynpdft
      961 vgfnntfsyq nftlnvlldw rkggnfysyv vkslinaglt dntlagrdae tgglpwtdsq
     1021 grkrndgmii pgyiadangn lsqntviiaa sdfynntynk yyerltysas flkireaslt
     1081 yvfnkkvtgk lpisnlslsl igrnlytwta nglgydpett msvtegfklg vghwtlpgtr
     1141 sfgfklscnf
//
LOCUS       WP_121293473             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121293473
VERSION     WP_121293473.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33365
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdef gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121288372             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121288372
VERSION     WP_121288372.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33279
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnsavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121294366             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121294366
VERSION     WP_121294366.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33394
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffvfvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tniqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121297007             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121297007
VERSION     WP_121297007.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33367
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121298720             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_121298720
VERSION     WP_121298720.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33421
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tniqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_121306450             333 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paraburkholderia sp. BL17N1].
ACCESSION   WP_121306450
VERSION     WP_121306450.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL17N1
  ORGANISM  Paraburkholderia sp. BL17N1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Paraburkholderia sp. BL17N1"
                     /db_xref="taxon:1938798"
     gene            1..333
                     /gene="trxB"
     Protein         1..333
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35357
     Region          5..320
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpatstkhak vlilgsgpag ytaavyaara nlapvlvtgl aqggqlmttt dvenwpadpn
       61 gvqgpelmgr flehaerfnt eiifdhihta kldekpirli gdsgeytcds liistgasaq
      121 ylglpseeaf mgkgvsacat cdgffykqqh vavigggnta veealylsgi akkvtvihrr
      181 dkfraepili drllakekeg lveikwdstl devtgdqsgv tglrikntkt gatedialqg
      241 lfvaighkpn tdifagqlem kngyiitkgg lngfatatsv pgvfaagdvq dhvyrqaits
      301 agtgcmaald aqryletide mvgehamsqe aer
//
LOCUS       WP_121306640             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. BL17N1].
ACCESSION   WP_121306640
VERSION     WP_121306640.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL17N1
  ORGANISM  Paraburkholderia sp. BL17N1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia sp. BL17N1"
                     /db_xref="taxon:1938798"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39435
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqsgag tgasfpddaf taagaeivda
       61 atafgadlvl kvqsptdael pllkrgatlv gmldpfnten ssklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvdtvqamk pgsvlvdlaa grgaeyegqr
      301 ggncpltead kvvikhgvti vgytnlasmv padasslyar nlldflklim tkegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_121308808             532 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp. BL17N1].
ACCESSION   WP_121308808
VERSION     WP_121308808.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BL17N1
  ORGANISM  Paraburkholderia sp. BL17N1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Paraburkholderia sp. BL17N1"
                     /db_xref="taxon:1938798"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54844
     Region          3..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligiple aaagerrvat vpevveklik lgflvavqsg agaganfddd ayraagagia
       61 ataaelwsgs divfkvrpps teevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvr slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl ygtnllrvie elckgkdgti nvdfdddair
      361 gltvikegnv twpppikqav vapkpaaaap aaaapakskg hghsgepmsa kslaivfaig
      421 alaflcvgqf apasflshft vfvlacfvgy mviwnvtpsl htplmsvtna issiiaigal
      481 vqvapplgel anagdrpsgl ilglavgalt ltavnmfggf avtrrmlamf rk
//
LOCUS       WP_121311689            1015 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121311689
VERSION     WP_121311689.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1015
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112017
     Region          25..1014
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwift lllalsmqfs faqektvtgv vsdktgplpg anvvvkgttr saqadfdgkf
       61 sitakagevl visftgynns svtvgaanny vvtltdgikl devvvegyrn ttkgttvvaq
      121 ttvnaktien rpnasfiqtl qgqvaglnit sgtgqpgaas svvirgagsl tgntdplyvi
      181 dgiptnainf rsinptdies vtvlkdaaat aiygnrgsgg viivktkrgg tgdaktsfry
      241 ssttgytelq kakysfadsr elltlekryg vgrgnsltdd eiaaygintd wvnyffsqak
      301 stdhqlsiet sgknlnsyts vsyldqegil qntglkrftl rnnlsgksnn dkftyslnts
      361 lgfsksqqav slgtgsinqn yvlgatlgap yispdeyvss qqvfdlyntd gtllytplfl
      421 idkantfsnd tdevrmsagv dlgynlfknv tarsrtsfen ietrivqwqh pisfnsflfl
      481 npgqefggte siafrrefrf nqlwqvewkk tfaekhtvta lgnaeyygsq vntdfqnqrg
      541 ldprtfvpgt gagyladita hdfygptgna skikyallsy fgvldydfnd rlgvvgtvry
      601 dgtnrfaedy ywgtfwsvag rwninkekfm ensgfqvlkl rasygttgne riqagtewts
      661 lqppltrdty ansatvpgqy ngaasyavtl gvddlrwett tqwnvgidfe ffknrvrgtl
      721 dyynrltvdl lntepispit gqtlinrnsd ieltnkgfel slaydvvrne nfkftvrgnv
      781 sknnttvngi peaqggeqnl gltinrnglq pyefylypya gvnpdngnll feaadgtlte
      841 tpsiaddsra tgktstpiyq ggfgfdldyk gffastnftf vqdvyrfdyd lqglydpgsl
      901 gqfvvsddll nawtptntdt nvpslnatny gaeansdrfl kdasyvrlry lqvgyrvpkk
      961 fldktfitgl sfyvqgenly twtkweglda esnrgndqaq yptprifsfg vdlkf
//
LOCUS       WP_121312604             978 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 102].
ACCESSION   WP_121312604
VERSION     WP_121312604.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 102
  ORGANISM  Flavobacterium sp. 102
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 978)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 978)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Flavobacterium sp. 102"
                     /db_xref="taxon:2135623"
     Protein         1..978
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107221
     Region          25..977
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykkllf lflllpfgal aqsslsgvvl dsksnqplpg vnvivqgans stttdfdgkf
       61 qlgglkngdk vvfsfigyds ktvtfsgqnt vnisleesan qlqevvvqvg ygtvkkkdat
      121 gsvttvgakd fnkgsnvtae nllngrvagl tvntsgapgs gseirirggs slfasndpli
      181 vidglpienn adnnrgttsv laalnpndie sftvlkdasa taiygsrasn gviiittkrg
      241 gkklavdynf qygsgrlvdk isvfngdayr dlitdlrpgd vsmlgtantd wqdkiyrrtd
      301 yvdnnisikg nlfniiparl sfgntyqegl rltntfnrnt vstalnpsff ndhlkirlna
      361 tytneknrfa dgvegsalrf nptqpvydpa spfggffeyy npdgtlqlgt rnpvaqllqt
      421 ddrgvnnrvf gnfeidykfh ffpalravin lgfdeanger tklmgadaas gpsnnnlpyg
      481 kneyeesiar nklfdaylvy tktfgkidfe aqagysyqir qnqiqstgni ldpnlpsnfp
      541 ettiftdnvl lgyfgrtkla indtylftft vrrdgssrfp snekygtfps aafawklknv
      601 afkdskvisd lklrlgygit gqqefggfne rnfylqqytt gsgssqyifg tsptpiaisn
      661 pynpalkweq tttynvgfdy glfndritga ldlfykvsdd livnaafadg gnfsnagfqn
      721 igsfstkgie fsldaqvikn dnfnwnvnfn ttafkrride laygadiftg dtgagtggta
      781 qilregytpy sfyvykqlyd asgspiegay adlngdgiin gddryiykna dpkvtfgfas
      841 tmnyknfdfs fnarasygar iynavnagra qynslingvl envptsvlnt gftttadvvl
      901 sdiyvengsf irldnvtlgy tfpkwiegka slrlftgvqn allitdysgl dpeitnngrd
      961 ntiyprqrsf lfganikf
//
LOCUS       WP_121313275             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium sp. 102].
ACCESSION   WP_121313275
VERSION     WP_121313275.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 102
  ORGANISM  Flavobacterium sp. 102
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Flavobacterium sp. 102"
                     /db_xref="taxon:2135623"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33766
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaaran mnpvlyqgtq pggqltttne venfpgypdg
       61 vtgpemmvql qeqakrfgtd vrdgwatkvd fsgpihkvwi ndtielhaet viistgasak
      121 ylglpseqhy lqtgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rsekfraski meervrkten itilmnhdtv evigdgqvvn evkalnkttg eeitipatgf
      241 fvaighkpnt difaeyitld etgyiinvpg tsktnvagvf vagdaadhvy rqaitaagtg
      301 cmaaldaery laald
//
LOCUS       WP_121313838             993 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 102].
ACCESSION   WP_121313838
VERSION     WP_121313838.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 102
  ORGANISM  Flavobacterium sp. 102
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Flavobacterium sp. 102"
                     /db_xref="taxon:2135623"
     Protein         1..993
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109836
     Region          20..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkiflsyfll ltiscfsyaq elngkvvden glplpgvnii akdkninstt dydgnfviqa
       61 vagdvlvfsm igyetltrna qsnmvitlke snqlltevvv igygtkksgs itgsvaqika
      121 tdivktpsqs aiqaiqgkaa gvnivtndep ganpsirirg lgtvlggrdp lylidgveat
      181 glnglnpnei atidilkdas slaiygqkaa ngavivttkk gkkgkirvny dsyygqkfiq
      241 kkvemadsyr fayynnvaag sstyysfdqp yntdwldeit ntgevisnyv sfsggnenas
      301 yyfgatnyke kgiligteye rnninsrnef kifddrlkis qnfnlaiann tpkpvsaftn
      361 aykqspivpv yfpngrwgvp lrnpatglid ingndrfnnv anpvaqltyf nersknivms
      421 gsvaaeiall kelkytsnfg atytlnkgyn fssnadiyls qnatqtlqdy edsfgdnpik
      481 yntlqqyksd dymwnwdnyl tykksfnkhd ftliagmsrt tknngeylsg trfnvpessn
      541 ywyldlasfn adappgsvvs nnhstpivsi ayfgraeyef ddkyllsasi rregissfqd
      601 vkkwgyfpav sagwvisnet flekikfvny lkfragygev gnanslnaln ipvfaagyny
      661 afgdsqtifp gsnqpyqvdp nltwetmkef dfgldfkvln nrlsgsvdvy drtssdvilp
      721 vslppvlspg evtvntgevn nkgvelslrw dteindnlky wvagnfshnk neltkvdnay
      781 fsrliggglg ngeytkqvlv gqplgsfyvy dvlgingdga fiysdervia gsylptytyg
      841 lslggsyrnf dfsvdtygvg gnkvyngkka qrfggeniey syldsfwtps npnttnpkpy
      901 netprpstyf iedgsflrin nitigytipk fynkiekvrv yitavnpfvf tkytgyspev
      961 vggdnanplg gagieldayp tnktflfgln isl
//
LOCUS       WP_121314145             998 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 102].
ACCESSION   WP_121314145
VERSION     WP_121314145.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 102
  ORGANISM  Flavobacterium sp. 102
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Flavobacterium sp. 102"
                     /db_xref="taxon:2135623"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108427
     Region          36..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkislykar apllyalfis lvycnalfaq ntqpttitgt vsdvngvlpg vtitvkrtqn
       61 stisdsagky sltaqtddtl vfsyigfkti eigvngrall navlsddatn lkevtvnagy
      121 ytvkdkertg siakitakdi dkqpvsnvla amqgrlagvd iiqdsgtagg gfqikirgvn
      181 slradgnspm yvidgvpyss etigysstts gmpsttspln sinpkdvesi evlkdadata
      241 iygsrgangv vlittkkgka gkarfsvsss tgygkvakfi dlmnteqyla mrrdayandg
      301 ittypgtayd vngtwdqsry tnwqkellgg taeihelqas vsggsdqtqy llsgssrqet
      361 tvipgdfkyr rtgihftmnh atednrfkms faggytlqdn kqpatdlsrv arnlapnapa
      421 lydengnlnw enntfqnpla alrsfstvdv kdllanvvls yaitpsltak vnlgytdvkn
      481 heqkivpstm anpssgvtsa vsslidnate rqsqlfepql qwkkdfknss ldilvggtaq
      541 eqttsrlfis gtgfasnami tnlgsanars ilgsevleyk yqaffgriny nykdkyivnv
      601 tgrrdgssrf gpgkqfatfg avgaawlfsn esflkentil sfgklrlsyg tsgndqigdy
      661 qylntygnng lnyqgvvgle pirlfnpdfg wesstkfeaa letgflkdri fltlvwyknl
      721 ssnqlvgvpl pgttgftain anldatvenr gvegtlrtvn cngkhfkwtt nltvsaarne
      781 lisfpglvas tyanryvvgq ptsiikvyey tgvnpqtglf evadlngdga fntagdkqkt
      841 idltpeyfgg lqnqfqyrnw qldlffqfvk qktydytpns pggamvnqsv ayanawqqag
      901 dvvpyqmnts gansaasaaf yryvesdalv vdgsfirlkn isvsydvplk akgvtcklsl
      961 sgqniltfth ykggdpelrf tgylpplrvf tggvqltf
//
LOCUS       WP_121314417            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 102].
ACCESSION   WP_121314417
VERSION     WP_121314417.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 102
  ORGANISM  Flavobacterium sp. 102
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Flavobacterium sp. 102"
                     /db_xref="taxon:2135623"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110451
     Region          44..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnknslykar vpllyvlfis lfycnavfaq ktdlviksnv eslkvngvvs dangalpgvt
       61 itsngtltst itdnagkftl ttssdailtf tyigyaavtv avdsrsvini tmtedattlk
      121 evtvnagyyt vkdkertgsi skitskdiek qpvtnvlaam qgrmagvdit qttgmpgggf
      181 dirirglnsl rtagnapmyi vdgvpfssda igyaqtstnt ptptsplnti npsdiesiev
      241 lkdadataiy gsrgangvvl ittkkgkagk tqftasasta tgqitktvdl lstpeyialr
      301 kkafandgiv nypgdaydvn gtwdqtrntd wqkeltggta emttvqasvs ggsaqthflv
      361 scnsfsqtsv fpgdfvykkk gahvnldhes edklfkitfs gsydiqdndq pardltrisr
      421 nlapnapaly dangnlnwen stwenplaal naealyktns lvanstlsyk lpygftakan
      481 vgftnlyhhe trtdpstiyd pvyeagaeys aiflttsrre swiiepqlqw qrkvsqgkid
      541 vlvggtfqnq vsnrlvqygs gftsnsllyn lasasmsqty fddetiyryq alfgrvnfsw
      601 kdkyivnltg rrdgssrfgp gkqfanfgav gaawlfseek avaerakfls fgklrasygi
      661 tgndqigdyq yldtyqsstg vydgtvglap irlfnpnfsw esnrkieaav elgffkdrif
      721 ftgsyyrnrs snqligmplp attgftslqs nlaatvqntg leltlrtinv qgdffgwttn
      781 fnltlpknkl iafpglatst yrnqyviges iniqklyhft gvdpttgvyq fedvngdgll
      841 sfaddaqtvk dfspefyggl qnqlrykrfq lefliqfvkq lnwnaasqfp vpgafanqpt
      901 svlgawqqag dlsttqlytn glnsaatnay qrynasdaav sdasyirlkn isltytipth
      961 lkglecrlnv qgqnlllitp ykdgdpefrs fnylpplrvl sfgaelkf
//
LOCUS       WP_121316545             380 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Paraburkholderia].
ACCESSION   WP_121316545
VERSION     WP_121316545.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39539
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvtqg hrvtiqsgag aaasfpdeaf taagaeivda
       61 atafgadlll kvqsptdtel pllkrgatlv gmldpfnaen arklaeagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlt
      241 rqsalvhera kqadvvista lipgraaptl isvdtvqamk pgsvlvdlaa grgaeyegrr
      301 ggncpltead qvvlrhgvqi vgytnlasmv padasslyar nlldflklii tkegalnidl
      361 addivaatll ardgavtrta
//
LOCUS       WP_121316803             333 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paraburkholderia sp. RAU2J].
ACCESSION   WP_121316803
VERSION     WP_121316803.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. RAU2J
  ORGANISM  Paraburkholderia sp. RAU2J
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Paraburkholderia sp. RAU2J"
                     /db_xref="taxon:1938810"
     gene            1..333
                     /gene="trxB"
     Protein         1..333
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35402
     Region          5..320
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpatstkhak vlilgsgpag ytaavyaara nlapvlvtgl aqggqlmttt dvenwpadan
       61 gvqgpelmar flehaerfnt evifdhihta kldekpirli gdsgeytcds liistgasaq
      121 ylglpseeaf mgkgvsacat cdgffykqqh vavigggnta veealylagi akkvtvihrr
      181 dkfraepili drllakekeg vveikwnhtl devtgdqsgv tglrikhtqt gettdialqg
      241 lfvaighkpn tdifagqlem kngyiitkgg lngfatatsv pgvfaagdvq dhvyrqaits
      301 agtgcmaald aqryletine mvgehamsqe aer
//
LOCUS       WP_121319556            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            piscisymbiosum].
ACCESSION   WP_121319556
VERSION     WP_121319556.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium piscisymbiosum
  ORGANISM  Flavobacterium piscisymbiosum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Flavobacterium piscisymbiosum"
                     /db_xref="taxon:2893753"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109952
     Region          22..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiflifmi vftaqvslaq vksvkgvitd sdglplpgas vavqggqkga ttdfdglytv
       61 evqkgqtlvf tyvgletqki vvgdaatinv kmavaasnal tevvvtslgl kktrksltys
      121 aqelkgeelt rvkdanvint iagkiagvav tkssggtggs tkvlirgnss imnsqplyvi
      181 dgiplyngss nqqgnynasn dsfgstaggn rdggdvvsli npddyegmtv lkgaaasvly
      241 gsqgangvil lsskktkent snlavssvtt fesvhslpef qyeygtanaq kswggkvssn
      301 dfvkdffntg vtqitsaaft tgtdvsstsl syantsasgv iegnglkknn fgirqtgkff
      361 dnkltvsada kytsqtidnr pvnglysnpl tgvylfqrgn dfnyykdnfe tfipsrnlyg
      421 qnfysapnad iyvqnpywli nrnksvdkdn ffngnlaley kannwlsiaa rysynrvend
      481 ydkkiyattn tslsningry invgtlstqr ygdliakint nfnedfsfna ivgasinntl
      541 anqsttldsg ivgglvnanl ftlgnfgeas gldnlslqat gssrevqsif gsatfgyknm
      601 lyldvtgrnd wsstlvntdt gsyfypsvgv tallsemttm pdwinfgkvr gtyaqvgndv
      661 safvtspkst vqggnlippt vgprpgdglk pelksefefg tewrmfnnrl gfeisyynse
      721 tknqyiqipa patnpygytn yginagsien kgfevvltgk iiagdkfswd ttinysqnrn
      781 kvkeipeelg gtipltpvnn inyryvlteg kpfgviegkh ivkndqgeiv lddkgnvale
      841 aglrevgnan pdfmlgwsnt fkfgaftanf lidgrfggdv msitesmndf ygvskrsgda
      901 rnaggvavna vkpdgtkvts mpaeqyyttv agvngataey vydatnvslr evslgytfnk
      961 kvlpfvntat lsliarnlff iykdapfdpn ialstgqglq gvdiyglpst rsiglnlnvt
     1021 f
//
LOCUS       WP_121325614            1010 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121325614
VERSION     WP_121325614.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1010
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111019
     Region          45..1009
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnyfsfykgg ktlycltlta ilfsfsssfa gntyrkfssi fqqhqvhgti tdgtaplpgv
       61 tivvkgrasv taitdytgqy sinvtasdtl ivsfigfktl kvpvsgrski ditlqydttt
      121 lrevkinagy ysvkesertg siaritskdi etqpvtnvla tmqgrmagve itqntglpgs
      181 gfeiqirgqn slrfngnspl yiidgvpyss qsigsnmtsg nmpaenspln sinpgditai
      241 evlkdadata iygsrgangv vlistkkgkq gktafsttys ygfgqvahfm dvlrtpdyla
      301 mrreafgndg yneypdyayd vngtwdqnrn tdwqkeligg vatysnlqss ltggtertsf
      361 llsgnysret tvfqgsfdyv kagghlslnh esqdsrfkis fssiytsqsn slpaiditst
      421 alllapnapa lydgsgnlnw enntfdnpva alegkikgqt ndlvanallt ydlgagftak
      481 gnfgytfltq kqlnlrpsta lnpaygagse ssivftnslg rnswiiepql nwnhkfgkls
      541 ldalagttfq qqkgtrqvny aigfannslm enpasasrnl vlssdenlyk yeafyarlnf
      601 nwesryllnv tgrrdgssrf gpgnqfanfg avgaawvfsq enmikddmpv lsfgklrasy
      661 gttgndqigd yqyldtysva aakyqgisgl qpsrlfnpdf gwetnkklev aletgffndr
      721 ifstvawfqn rssnqlvgip lagttgfstm qanldavvqn rgleltlrti nikngefswi
      781 tsfnitsnkn rlisfpglda stfknqyvig hslnitkvfh ytgldsssgt yqfldvdgdg
      841 svnfgddqkt ikdlspkyyg glqnqlrykn ieldflfqfa kqenynpnsy spmpgtmanq
      901 psavlsrwqn pgdtgpyqaf sdsdasrtia yyqfsssdaa isdasyirlk nisltyqlpq
      961 sltkkfncki glqgqnvfti tkykgidpef kytgylpplr vftttiqltf
//
LOCUS       WP_121326365            1008 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121326365
VERSION     WP_121326365.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1008
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112534
     Region          30..1005
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mryiqlkivl cfvlfaflps kifaqidqki nlagvvigae gkpienativ skednitatt
       61 dnngsysisv tantdieisa igyntlivka tadindinld kensnlvqia frkqeskdlm
      121 gaisfinlpe ildknyttfs ldgvqafvgg ynngniwgms gylvlvdgvp rdintvlste
      181 ieqitflkgv saialygsra akgviyittk kgkvqkqqit trfdngvsip knlpkylgsa
      241 eymhyynqar andgldptys detiynystg knpyryadvn yyapeyikkf yfnydanvei
      301 tggnksaryy tvvnfstqed plqdfgeaak nnnnrfnvrg nvdlrindri satiganaiy
      361 snsrgvntny wssaatlrph lfsplvpism iepsddasma lvknsnyivd gkyllggtql
      421 nptnpfaaiy aggyntyisr qfqfntginv elgdvvnglt frtdfgvdys nsynqsynns
      481 yatyeaswnn yagkdqitsl tkygkdsktg iqnisgsala qtvsfsaqfn yvkkinennn
      541 vsamligsgf qqsfsgvyhk tsnanlglnl aynfdqkyfa efngafvhsa kfaegnreaf
      601 sptmtlgwki seenfmkdlt avnslklnvs agvlntdldv snyylyesiy sqtdgawfsw
      661 rdgalnrstd arrgenldlg fakrkelsvg legaffknfi tlntnffane vtgnviqast
      721 lypnyfvtnf pntsflpyin ynndkrigfd fdlrfnkkvg nvdlalgftg tyidteaskr
      781 aelysdsyqn rqgkaldafw glksagffrd aqdissspsq tfgqvkpgdi kyidqngdgi
      841 idnrdevylg kagwngapft fginftskwn hftfftiftg qtgahamkns syfwmdgedk
      901 ysvnvrdswt eankdtalyp rltslngdnn frssdfwmys tnrvnlskvq ltydfpkktl
      961 qktffnelsv yalganlltl sqnrdimeln iggapqtryy nlglkalf
//
LOCUS       WP_121326259            1004 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121326259
VERSION     WP_121326259.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1004
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111663
     Region          44..1003
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktfslnkgl aglwypfifg fylfctpala rntlffsvlq qqtqvhgivt dgtlplpgvs
       61 isvknqkkav vtdfdgkfti tvsphdilif tyigfkttei pvagrlvinv qmkedatslq
      121 evkinagyys vkesertgsi aritskdiet qpvtnvlatm qgrmagvnit qntgvpggnf
      181 dikirgqnsi rvdgnaplyl idgvpyaset igynqtstiy psptsplnsi npdtiesiei
      241 lkdadataiy gsrgangvvl ittkkgkagk ttftvtastg agtvtkfmkl mnteqylamr
      301 reafkndgip ynswdydvng twdqnrytdw qkeliggtas itdlqaaisg gsektqflis
      361 gnyhtqssvf pgdfiykkgg sqfnlnhrse dnkfrvtfsa gynsqnndqp afdftydars
      421 lppnapalyd sngelnweng twdnplrnln aefesktndl iansvlsyei ssglliksnf
      481 gytdlstvet rtapssvynp aynissanss lylnntdrss wiiepqiswt kelglgkldl
      541 lagstfqnqt ttrlfqsgtg yssnsliynl asakyinvll ndetiykyqa ffgrinysfd
      601 kryiinltgr rdgssrfgpg nqfaifgavg vawlfsnenf lknsswisfg klrssygttg
      661 sdqigdyqfl ntytttginy ggnvgleptr lynadfgwet nkkleaalel gffhdkiftt
      721 aswyqnkssn qlvgvplpgt tgftvlqsnl naevqnsgle ltlrtnnfsn anfswttsfn
      781 ltfaknklls fpvlesspys qkyrldkpln ielvyeykgv nsqtglyefe dinkdgkitf
      841 pedrqkavdl npkyygglqn qlryknwnld flfqfvkqkn rinpmgfagq msnqpvsktd
      901 rwqafgdipa yqlyttgnns eavtadylyd rsdasitdas firlknisls yllpmrsntv
      961 qckimlqaqn lltftkykdg dpeftssgyl pplkvttagi qltf
//
LOCUS       WP_121328837            1075 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121328837
VERSION     WP_121328837.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1075
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115900
     Region          25..1074
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv lllvlmaqls faqertvsgt vsdnagmplp gvsvlvkgtk sgtqtdfdgk
       61 fsikastsqv lvfsyigmkt qeiaassslv nvklgdaaqe legvvvttal gvkrekkslg
      121 yssqlvtaeq vnssptnnfl nnlsgkvagl eikansnfgg stnivlrgvk sitgnnqali
      181 vvdgvavsna nlndtdsqng rqgfdfgnsa sdidpnnies invlkgaaat alygsqasng
      241 aimittkkgk knsalgvsvs stvsvgaidk stmpryqtqy gegyggedss ytadvfgnpn
      301 glvastgdda sygnkfdpni mvyqwdafvl gnpnygkatp wvaakndpks ffqksttytn
      361 nvnlsggdek gaynlgftni nntgvlpnsl lnknslngnf srdlsdklts tafftftdqn
      421 ttgrnntgyg dnfiggfrqw wavnndikel ereynrtgqn ttwnqtdpts gnlapafwnn
      481 pyfdryqnye qdsrtrflag tslsykitpd fvllgratid ysndqqelrk avgshaetfg
      541 isgandgsgy slykrdfmqq tydfiatynf hlnedigaka lggytylrsd aysiqssttg
      601 glaspglysl ensnvflpar esqiayeksg lyaqlsldyk kflflegsfr ndkstalpte
      661 nsnynyysig sslifselvq adwlslgkvr inyaqvgndp aagrlgakvn nygidgnplf
      721 gnsptyldfa nlkpetqkaw eaglemsmfk nrlnfdlsly ktntedqifn vpqststgrn
      781 fatvnageie nkgielalsg kviktqdftw dlgvnwstnk ntvvslnqgr dnlllatfqg
      841 gaslnatvgq sygtlrgkdy tydangnkvi dadgfyvlas nkvigntqak wlggisnkfs
      901 yknlslnfli dvkkggdifs ldqaygqetg iydlgindlg nsvrnplttg adsggvilag
      961 vhadgtpntt ridastsggt afssdvnptk ayvydgsfvk lrevgftytv psqildklkl
     1021 kglsfsvign nvwiiqknlp ysdpeagssa gniqgfqsgv mpatkvysfn vklnf
//
LOCUS       WP_121328607            1051 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121328607
VERSION     WP_121328607.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1051
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113926
     Region          37..1050
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklislvf iggvifstna kevaitkhlf eqkssqievt gqiigqddgm piagatiyae
       61 snskiatisd engrfklnvp eneshvvisy mgyqttnfpl iqttnltirl kpaenvldqv
      121 lvtalgvkkt skaisyavte lkgteftkak etnianalvg kiagvnvsst atgpngstrv
      181 virgngslng nnqpmyvvnd lpidntqlnl pgigngpgst rinvdrgdgt svinpddikt
      241 itvlkggtaa alyganaang viliqtkrgt aqkgigveyn tsftfetpsi ipdwqyeygs
      301 gangkkpttq aeavaagrws wgakmdgtdv iqfdgvarpy vaqknniknf yetgttfins
      361 ialsggteka tgrlsfsntd nqgvvpnsdf nrkslniasn vnmtdwlkfd vvaqynveks
      421 nnrvtvsdae anpnwgtymi antvdirnla pgydangvee awnpvavatn pyfvvnkikn
      481 sdtknrflgm vnvklnftpd lflqgrigqd ftnydffgyi pkttlnnpig yaqgsrvkls
      541 nlnseailny tkkniyrdfs lnallgvntr ttlrdetrve gsgfvlddfy altnlstlty
      601 sypygktktn svygavdldy knvvflnftg rqdwfstlsk dnntvfypsv gtsiivsdil
      661 kmpdfvsfak lrtswaqvgg atpdpyalnq sysmvqgghn gqqlqtptgs rvpnatlspl
      721 tsttfeigtd lgffnnrlnl dfayynratt ndivettisn asgastalln lgkmrnkgve
      781 fllsgkiins enfswdasfn gsynkntvea ltdqlnsitm atsvngyvti tsdvgrpysi
      841 ikgykplkda ngntvynvsg gsatiargpl eelgqgvhpw aagisndfky knisfsflid
      901 gkfggslysg tdlygtrmgl tkltldgres glpikgvdtn gnpidmviap enlrtyydgl
      961 rnisstfvyd asfiklrqvi igyqlplekl kglsklqgas isfvarnlfi lykktpnvdp
     1021 esvfsagnaq gveqfgvpkt rsfglslnvk f
//
LOCUS       WP_121328990             315 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Flavobacterium].
ACCESSION   WP_121328990
VERSION     WP_121328990.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34077
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaaran mnpvlyqgmq pggqltttne venfpgyvdg
       61 vtgpemmiql qeqakrfgad irdgwatkvd fsgdihkvwi ndtielhcet viistgasak
      121 ylglpseqhy lqmgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rsekfraski medrvrkten ieilmnhdtv evlgdenvvh aikaknkttg evfdipatgf
      241 fvaighkpnt difkeyitld etgyiintpg tsntnvpgvf vagdaadhvy rqaitaagtg
      301 cmaaldaery laske
//
LOCUS       WP_121328979            1068 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121328979
VERSION     WP_121328979.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1068
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116855
     Region          27..1066
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkfkffqrkt vvlffvllaq fafaqervvs givsdnagmp lpgasvlirg tktgtqtdfd
       61 gkyslkassn svlifnyigm ktqeimaant tvnvvmaggs eqlqeivvta lgvkrekksl
      121 gyatqeikge dltkvntgnv ansisgkiag vqirrnnnig gstnviirgt tsltgnnqal
      181 wivdgiplnn dntnsedqks ggnvggydyg naaadinpdd ietmnvlkgs aasalygsra
      241 sngvilvtlk kgskskgglg vtfssgitig vvdkktlpey qnqygggygd fygtvnlgsg
      301 vhpyaatdda swgpkfdpnl lvynwksfyp qlpgygkatp wtavqenpns fyqksvtyvn
      361 nvavagsnen gdfrfgytny nmdqgilpns dnrkdnfnls asynlkpktk isasanylka
      421 nakgmnetgy gdggnnylss irqwystsvd fkdlrdaynl tgqnttwnva gpndlavqfh
      481 dnpyfqrynn ynslardrff gnvnlttqvn dwfditgkga vdyyhqlqee riavgskrtp
      541 nglgqysryd kdfreinfdl ilnfktgite gikfngmvga nsrrsvsnsi yartngglvv
      601 pgmyalnnsi dkinspdere itlgtnsvya nasfnfldty flegtyrvde sstlpkdnnv
      661 ysypsitgty ifsnhiktdw lsfgklrlny aetgndapfa vttatypksd nfgdggirfs
      721 tendksnanl kseltkgvea gielklfknr lgfdfsyykt nttnqilsie tpsqtgytra
      781 winagdvqnk gfevtmnvip vktanfswev kvnwstnkne vislgeanri slgsfqgvgy
      841 vaevgkpvgq ligsgftyln gqkvirangr ylqtagatig dvnpdwiggv nnvltyknft
      901 fnflidvkkg gdvysldqrf ghttgiyest vtnnhlghpq rdpvasgggi llpgvkedgt
      961 pndkivsveg angysfynsm peqqyvydas yvklrevgls yrlpskflak tfmssiifaf
     1021 ngsnlwiisk nlpyadpeag mssgnlqgfq tgvlptskey nfnmkvqf
//
LOCUS       WP_121329673             980 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121329673
VERSION     WP_121329673.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..980
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108012
     Region          24..979
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkriktkfll lllllpfcvf aqntisgivl ekstkqpipg anikvlgtni ststdfdgkf
       61 qlsgvkadsk ivfsytgytn qtvavagqkn itvnleednn qlkevvvqvg ygsvkkkdat
      121 gsvtalttkd fnkgnniste nllngrvagl tvnstgapgs ssqirirggs slfasndpli
      181 vidglpldns tnvgassfma slnpatvesi tvlkdasasa iygsrasngv iiittkkgsk
      241 tlsvdynvqy aagsltktvd vfsadefrsv iadrrsddls klgtantdwq raiyrntgti
      301 dqslavrgsl fniiptsltl gntdqqglrl tnefkrntvg lvmnptfldn hlkmrlsany
      361 aneknrftdg vegaaigfdp tqpikvegap yggyfeyttg vdangnyplv staarnpvsq
      421 llntndrgkn drffgnfevd ykfhffpalr avvnvgfdes ngerrrlvga dagsapsnnn
      481 ipygtneyte amrrnklldt ylvynktfks lnfemtggys yqkfqsskfe tgnilnpdlp
      541 stfpettldt dvvllgffar tnlnfrdkyl ltlsyrrdgs srfeeanrwg nfpsvafawk
      601 mkedffkdst vlsdlklrls ygitgqqdip epngylqkym vgggnaeyyf gtspvpvalp
      661 skrtnnlkwe etssynagld fgflnnrlsa gldvyykesk dllvnaaisd gsnfsnrvyq
      721 nvgsfttkgv eftinanaik tldfnwnmnf niskferrik nlvngtdifl gdniagtgtp
      781 gqifregytp ysfyvykqly nnegkpidga fadlngdnik ndsdkyiynn pdpdftlgfa
      841 snmnykkfdf sfnlrasign rifnavdasr aqydamengg vlsnipsqvt qtnfqttsnv
      901 vlsdlyiena sflkmdnitl gytlnnwvns kaslrvstgv qnvfvltkyt gldpeitnng
      961 vdktiyprqr svlfglnlkf
//
LOCUS       WP_121329387            1114 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121329387
VERSION     WP_121329387.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1114
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123666
     Region          21..1113
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknlfymlsf llalsgyaqe rtikgtvvda kdglpipgvt vfvensavsn ntqqkgviqs
       61 sslgtvtdfd gtfefkinsn mkslrvtymg ylpytidits qnnytislks daaelkeivv
      121 tgyqkiekrk ltsavaqvem adikqagvas ldqmligqva gvavtqqtga pgtiskirir
      181 gtaslngaqd plwvldglpl egndvpqnyd kdnidvlsnf siaglnpddi kditilkdaa
      241 ataiygaraa ngvivvttkk grkgnmkvdf nvntfvtqkp dfsklnlmns sqkvdfelsl
      301 asredltyrd tageisriln qanelgayrs ggfsslsptt qnsinslrnn ntnwgdllyr
      361 aafntqygls lsgggersdy yfslgayned gatvgtgfdr ynltlknnfd vtdklhvgvg
      421 ifgtqskkts ylsdtdgftn psnysrnvnp yltpfnadgs yrydkdikgy gngtvalpfn
      481 fleerentny elitrsvkal ldvdynitkn lkastqiglq fdnnssekya gkdsyytrke
      541 rektsvfsng tynyflpvgg iiqnsntdff qynwktmvny nttlggkhel efmvgnelrk
      601 nkntsiatkg fgfdpktltt aqiifptasy aadsnyrtyl ktenenafas ffatasytyd
      661 rkytffgsvr ydgsdlfgad pkykylplwa vsgswavsee nflkdndvis nlrlrasygl
      721 qgnidkntsp yvvginqtav ilpgqtepil tvlsppndkl rwekttntnv gmdlglfknr
      781 inivtdvygr kstdliglqs lalengfeyt nanwaqvtnr gyeislstrn idhpnfkwnt
      841 tinfahnksn vdriqtrsns ylpsreglpv navfalktag idengyplfv nkkgetvnsq
      901 tffalfdpya dffpgvlsqs kltdaetrdl ftyvgdldpk ftggfmntfk vhnfdltiat
      961 tfnikqtvve kptfngtsld rgqnyttdal nawsptntgs hipgitspts gtgdswmayq
     1021 wyspgaaple mynyldtwvh emsfmrvssi rfgyslpkka inslfmenvr fsiegrnlfv
     1081 issdykgyfd petfgniyaq piprsislgc nltf
//
LOCUS       WP_121329723            1062 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121329723
VERSION     WP_121329723.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1062
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115465
     Region          22..1061
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqimlifmi vftaqvslaq vktikglvsd hnglplpgvt viiqgtktat qsdydgkyti
       61 qastgdvlvf syigiktqav tvagsatinv vltedaqnln evvvtalgik rqkkelgyav
      121 qdvkgdqlsk vittnvasgl sgriagvdvs lpatgiggss rviirgissi gesnqplyiv
      181 dgvpidnsgl nndsaaaskw fdgrdngdgi ssinpnnies ltvlkgaaas alygsralng
      241 vilittkkgs kgklqvelts gvsfdrvnak ykdfqgdygs gshgvlpdpt kapeelygyt
      301 tsawgpkfsn sigqqvkifd gsmkpyarvd nniqdffrtg ftttngials ggsetayvrf
      361 gynnlknddv ipnsglernd aslnatlkse kftldanvny miettanrpg lgdspnnvgy
      421 slsslapnid qawlqhykne atgeiykwnn niyqlnpyft vdanhnsskk nrfmgnvagt
      481 yqlakwvglt frsgldtylf takdfmspgg twparetgyl glnditvsem ntdvianfse
      541 iklatdltfs gilganrrdf rrqenssfgt niiepgteyi snfsnqtina psvtktrtns
      601 vygsakldyk gylyaeftgr ndwfsvidkd afypgaslgf ifsdafniks dtfsygkfra
      661 swakvsnapg ayknslnytt yssydgqsvv nvkntsapna nltyqtkkgi efgletawfk
      721 nrlraditvy redtsdqtld lassatsgye flsvnagelr negieiflsg tpiktkdfew
      781 gidlnfsknk nsilslhpdi ntytisearw anaaivaqvg gqygsiigrd fertpqgemi
      841 vganglptyt enkvvlgkgv pdwaagltnr fsykgitlqf lldmkfgmdv ysmtnslaaa
      901 kgllditteg rdefiaartq aaasdpnfvf kdwvptagyv angvvntgta dnpvyvkntk
      961 pvdpqeywrs vtdatpapfi ydasyvklre vslgytipks vfegakinsi yfsvfarnll
     1021 tfnkdlpnid pesmytsgng qgfeygslps rqsygfnikv tf
//
LOCUS       WP_121329726            1012 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121329726
VERSION     WP_121329726.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1012
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108970
     Region          22..1011
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkiflifmi vftaqvslaq vrnvkgvitd sagmplpgas vavqggqkga stdfdglyti
       61 evqkgqtlvf syvgletqti vvgdastinv kmqqassnal nevvvtslgl kkskktltya
      121 aqevkgeevt rvkdanlmns lsgkvagmiv gkssagagga vkvtirgnss atnnqplyvv
      181 dgipllnsts amsnqvfgdt aggnrdggda ismmnpddie smtvlkgasa aalygsqgan
      241 gvilittkkg kegkvtanyn ssvfvdnvvs lpdfqtnygs apssdlswgp akkspdhvkg
      301 fyntgvtmin siainggsdk attsltyant nvdgviptne fkknnialrq siklfddkvt
      361 vdaslsyaeq kinnkptngl yfnpltgvyl fprgndfady yknyeqfnst rnlmdqrwps
      421 atsdiiqnpg wilnrnasid knqslissaa isykannwls fkarggynrl yntfdkrmya
      481 gtnetlapst gryiysdses yqlygdliat intkfnddft fsatlgtslt kstvndayvs
      541 dsgqknglin anwfntgnfv saernahtig gkkevqsvfa satfgykdml yldvtgrndw
      601 sstlvntdnl sffypsvgls ailsqmvtlp eaisyakvra syaqvgndvs afltspvnti
      661 vggqvtpplv gpkpgtslkp emqnsyefgt ewrflnnrig fdftyyrnet knqlitapap
      721 ipnttgyqny afnagsienk gfeitltgka iandnfswdl glnyasnknt vldlgagang
      781 gvntvvltng dpnsykyvle vgkpfgeiqg knivrnaqgq ivldkdkniq ktdfvdlgss
      841 npdfmlgfsn sfkykkltln llidgrfggh vmsmteamld yygvskksgd ardaggvkin
      901 avdqdgnavt tmdaqkyysq vgnragatge ymykatnvkl gevslgytfd fsketvfktv
      961 nlalvgknlf ffykdapfdp nvtlssgegl qgvdifgaps trsigvnlnl tf
//
LOCUS       WP_121329835            1111 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121329835
VERSION     WP_121329835.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1111
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=121234
     Region          26..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllyesll vflmvlcsqg vsaqnktisg vitdsanmpi pfvtvkekgt kveasadeng
       61 afkisvkega tiivsfigfk ttelkavdgm kiklatatne ldgvtvtalg qtkknksigy
      121 atsvikadal vktasptian glygkapgvr isstpggaga iniqirgins itgrnqplii
      181 ldgvpirdge vnnndywnqq rvknngladi npedienisi lkgasaaaly gseavngvvl
      241 itsksgrgkk glgidfstsy sgneiaylpr fqyergpgwt nanystgyla pdgfahydvd
      301 gngtfetrgv snsgnnygpw fdgkpvmtwd gvirpysaqk dgyknmfqns wdsttnfalt
      361 nstenssirf sytrieseal smgnnnkknn fnlnasfktg klktdvivsy mnqnlqnrtf
      421 atdrlvnnft gmlspfdngd wykakyktsl gykyvvgkdt qsltpseniy rngfrsdiad
      481 yfwntgakqq deitnrlias vtetlsvtkd ltlrgrvstd ltainienkn pvevplvyef
      541 gnegdrsgsf mmegqdynil ygdllatynk kinedfgvna vvgysatret yrtlsrstkg
      601 glsvegwydl kssigiatsd skreetlkda vfgtlsgsfr nylfvegtir rdrtstmnpn
      661 nnaftypsvn ssfvlsdavk lpdfisyakm rgswgivgsy psryganvaf iqntlgtqgt
      721 snpvlttnsq dkygnegikp emkneyelgf etkffdrrlg ldfsyynaki kdqildltla
      781 pttgassila nvgelsnkgf evaltgspfr tanfswdvtl nwakninkvv klangatell
      841 hadydgsaaq lksvvgdpmg giyahpvktd asgkdmvdsd gflmidgdkw vkygsaipkg
      901 vggllnsfty ksftldvnid ysyggslmpt ginwmtargl teeslkystn erggltyymd
      961 ngkgvqvpns atagpggqvl yrdgmlmngv tadgspntnv isqagyynmt ynwggpqyss
     1021 sryelyiqkn dyvklrevsl afnvpaayas kfgatklsls ffgrnlfyiy rtikdmdaea
     1081 ttagtkwtqn vnnagltpst rsygvmlras f
//
LOCUS       WP_121329848            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121329848
VERSION     WP_121329848.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=122995
     Region          73..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknqfnpvna elltkqkkif lwtkknsiff fvtlcsissf ghtvklerve vinhaketka
       61 esnlnfavdv dpitgkvtge lgeslfgasv kikgtnkves tdvdgsfsia akegdvlivs
      121 yvgfitkevt vgnqkqlnir lksaqndlsd vviigyqkvh kknvnaavst isskdlqdip
      181 visvssiigs latgiqtptq tgapggrgsl virgntsmsg sgyssplyvi dgvqtsledl
      241 agyntsntdf laslnpndie kidflkdasa aaiygsrgan gviiittkkg galdkpeftf
      301 slntgispip nlvtmnigsa ernakmgmly kwwksddvqt shvpmvlsds lnpafnnkvd
      361 yqglfyrtgi snkynlsmrg gsettnyrls lgydnvegvi knsgfkrytf sgninskvgq
      421 nfenqfrvnl lqtdnqtgqg npdggrfqfn ntlptdpsnl nsslfyvsdd kikslqgels
      481 dklntdetiq vtlsdfmkyd ftpafsinaq fnyvyssekk nyyepstvre egdgfasyal
      541 ynrknlssdl yanyykkfgn htvtgvlgqk tdynkyedmf myakgfgvda ikvindrytq
      601 gqingytsie snallsyfgr lgyrfkerym vdvafsrdgs srfgedvrya nfssialgwi
      661 isdepfikki tgnvlsyakl rasygvngne idenflrygs yrlgyggnpl wsnlmnvsty
      721 ggttgvvtdy ntignpnlsw vnskqwdigf dmdlfnnrin itfdaynkkt enllfetlfp
      781 aysgfnqaks nvagvmnygw eamvkwqifs vgnpwkleis tgmsqnknfv tklpngnkdy
      841 ygydagrdrs ygyvvgmpli lpvqfkneyi vdnlsqlpin pytgeilhgk sawgtiapgt
      901 piwkdyngdy lldeagdykl dtsfkptpdf tglfninlky kgwylqaysq fsfgsdiids
      961 stqkyldnyd rgddwavkgl qdlsglsfwe npgdgaagah ypalyparpn ttpyyrfrsg
     1021 qslwkesgdy wkisnasigy tidksrvleq ihisrvriyg svinpyqwqr skvvadasqv
     1081 demgytlgng ypqsktfslg ldikf
//
LOCUS       WP_121330136            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121330136
VERSION     WP_121330136.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111302
     Region          25..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mmqkvfkllf vfclcsfqfa kaqttvkgti tdavsgipip ganvvvkgtr tsassdfdgk
       61 ysikvpnqsa vlvfsyvssa pkevavgtqt tvnvalgaat qqlgevvvta lgikrekkai
      121 tysaqnisvg elsearslnv anslsgkvag lnysttsngv gsssritlrg nrsltgnnqp
      181 myvvdgvpis ngtttgnpdi dtggttqpdg isninpedia smtvlkgpsa aalygtrasn
      241 gvivittksg ksgktsvsls snfmassayd ltnfqneygq gsqgvynpts vsswggkldg
      301 sqvsawqlvr npnykgpatt dyspqpnnvm dfyktgynla ntltitagne kaqgyfsytn
      361 tkaegivggn qldrhnlnlr ltskvsdkls ldvktnyiiq didnllrtge esigtsayll
      421 prsikfneyk nyeytdaagq lqqnyfvdea gspggnpyws alrddsrkdk rnrfiglasl
      481 kydftktisl qvrtgldqmt nknvrnryat vafnnnlgsy sesyetvsef ntdallsyne
      541 kfgdfsvgin aganalqqns sslssggvls krnffalsnv stiqsvstas ekrinsiygf
      601 sqigfrnylf ldltarndws stlpaanrsf fypsvglsgv isdmvtlpev isfaklrasy
      661 akvgndtdpy qtssrlsyig gnggmlyaqt taanpnlrpe msssvefgge vrflknrlgl
      721 dvtyfqtntk dqifyintpe ssstsravvn ggeiqnkgie vvltatpvqs effswdvgvn
      781 fatyrsevks iyggreelvl gegrlvrskv iqggeygdly ikgfqrspdg kiivnsagip
      841 latnsfdvra gnfnpdwtag lkntfkykdf slsflvdfri ggevisytqa reaglgvsdv
      901 tlpgrnggiv vdgvvagpgg tytqntvsin aeqywtaigq rtpiaepfiy datnirlrel
      961 vfgyslpkrv lynsgftsid fslvgrnlff fenkakyfdp eagagtgnlq giesfnipst
     1021 rdygvnvkfg f
//
LOCUS       WP_121330284            1096 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121330284
VERSION     WP_121330284.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1096
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119783
     Region          43..108
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          126..1095
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myfklsylnl krifflvlal laiqngyskt nftehskvkn ktekatlvsi fsklskqtdy
       61 kfsygqaiia dnttytvdfs ddsvslilsd lskkanfnyn ingklvliqk teapktisrk
      121 aidrvkvkgk ivdenkvpip gafiketnss nsttsnfdge feitvgegkt ievtymgykt
      181 ktvvtqsgfm tiqlepntae lsevlvvgyg kqakkdvtga vtqlqassfr qgvnvsadnl
      241 lqgkvagvrv vstsgepgag vnvtirgvgs irsgstplfv vdgmplsndd vspsgtnvgf
      301 gsstaknpln flntsdiesi tvlkdasasa iygargsngv vlvttkkgsk gegtltydsy
      361 mgvsnvahkl dvlsaseyrn aikdksfdhg gntdwqdvif rsaittnnal sfakqtesgn
      421 yyasvaqmdq qgiirnsnfk rlsgrinaae sfldnkrlkl kvnltasqtv ddgvptsddg
      481 gsngqlviht lmanptrsvf dangnytnfn mnahynpayl lsiyedqtnt lrvlgnleas
      541 frivngleyk lnvgvdrsts ernttiypni tdiskigkyv qnnldsknsl iehyltyngt
      601 fgkhkvealg gfsyqkfers gtsfsiegit ekgvgvkpei npgfkgilpv lsgyaqenel
      661 qsyfgrlnyt fnerylltas mradgstrfg dnnkygyfps falgwniske nflqnieain
      721 nlklraswgq tgnqevenki tkaayslsga dgyylyddln lvngvsvvrt pnpdlkwevv
      781 tqsnlgldfn lwrdklygtl dyfkktttda ilnvtsplls ptntvwtnls nhgkivnkgf
      841 efmlgskvvd tkdftwnvdv ngatlnnkie dlpiseiltg tisgpgqsgv naniyksgya
      901 agsfyllqhi gfdskggnif kdqngdgkid nsdrviiega lptfyyglns dmryknfsfs
      961 fsiigqtggy llnntglnal ninnlasdrn vstnyyesga nptnspilst lfleksdfir
     1021 lntarigynf dlkglnwlng ltlyvtgnnl vtithysgfd plinspkpsa gnqsigidya
     1081 ayptsrtfsf gatlkl
//
LOCUS       WP_121330473            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121330473
VERSION     WP_121330473.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117693
     Region          45..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkvksknv klskivlllc lmslfkvssi raetinlsfe qsqdrtvkgk vvdeigtplp
       61 gvnvivkgts kgtvtdknge fsidlpekkd vlvftfismk dqevivngkn ditvvmtdqs
      121 eslkevvlig yqsvqkktvt gamttvkskd ienvpyasid qilagkvagl tslstsgepg
      181 artvtnirgs nsvglggvsy plyvvdgiiy dindmpssyg nnplaslnpn eiesvdvlkd
      241 asasaiygsr gangvilikt kqgsknqrpt frvnaytgig lkpslrkvtv grmerqlkld
      301 airrnfkdmd qnfhmaltds lnvsfnnntd wqdlfiqnar isnvdasvsg afgknqykvs
      361 lgyynetgvi igyqlkrfsp tmflslnltd kinftinmmp symdtnhgfg ngetfpfgtw
      421 gfpssfwgis dkqkkqyqgq agnldedkri gllantrlni nftkdllfts sfsynffenr
      481 rdqfqssqiy atdkdaavse hyatninele nyltytksfn erhnfsailg qqiseqdnks
      541 sylrgqgvlg stvfdispgp dlsgnsymet kkrmgifgrf sydykekylf sssyrrdgss
      601 ryntdkrwtt fysvaggwla seetffkpvk dvvnflkfrg sygvtgndpa syyaqyniyt
      661 gnasydnssf ginnpavatt yngvptvsqn yggfagskdi twekypqvnf gidlnmfnnr
      721 iqinadwyar dskdifytnl vapatsgygf ysgnavdirn tgyeftvstv nlgnnstfkw
      781 ntsfniafnd nyvtrlpdgg kdltvgepwl qytltegmpl fnyrvwdvkg vyssdsdvpt
      841 dpltgqkmkf ygetikvgdp kyvdqngdyi idnldkkyag spnpkatggi indfryknws
      901 msifcnfvyg rkiwngyvsd rlngsksaap wsdwgsratv gtiqdinyyq gpgdttaefg
      961 tlftnysnvd rfhiansqfi edgsffrikn irlgyavpen fgkkiglsal qfyamadnva
     1021 lftkstlpdp eavgadgftt gnnyplaikf tlglsatf
//
LOCUS       WP_121330409            1129 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121330409
VERSION     WP_121330409.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1129
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123546
     Region          52..117
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          131..1128
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mtkkqmrfiq ncqsikksvl dkallfvalf figltakaas vdigkrvtlk venesmknvf
       61 qkiekqvdvh fmyetnqvna nqkislklnn vtleqaldki csnfllkyei vsnnivikks
      121 qkvadneqnk inisgtvysa tdgmplpgvg ikdkgsdvat stdfdgtfkm einsseavlv
      181 fsyvgyvnqe ikvtpadkni kvklvadmkq lqevvvmgyg svkknavlgs vgsvsmkets
      241 srtynsaael lqgtvagvtv lnnggdptae ptinirgigs lnaetplivl dgiiysgsln
      301 tlnpndiasi svlkdaasaa iygarasggv ilitskkgvs ekvninvnyq ggfqnvakkl
      361 dvlnaaeyad amnlardnag mpripafdpa feptarttkt nwmdeifhtg eiqdlslsin
      421 gkteksnffv sgsyrknegi llntfgeryt aranssfkia pnftigenls ysltngqsan
      481 tssgytgail aaifyppnat iyredgsghf ggvpekyigs ygdvinpvay lkrldnrnpv
      541 stilinpyae weivkglkvk tnwgytriqd nakdfavkit epgkifdfnr ltqksitttd
      601 llgeqtisye rslgkhnfka lagytyqetk rdfytiegtg fdnedpsqry llnakliqqt
      661 aaglsdeiis syvgrlnydf nqkylfsgiv rrdgtsklls enrwkvypsv sagwliseee
      721 fmknigpivs nlklraswgq ignlgnlgpy qfsvplnqtq aligstpvin ygyaegelsn
      781 pnlkwesseq tnigldftmf nnmltgsvda yvkknkdmlv rdqlpgvsgt pqgrivnsgd
      841 venkgleasl tyqksrgefk fdvtanaafl snkivsikdg ltsleplnis rvrslplani
      901 yqvgspvgay ygyatdglfq snaeakayvn stgavyqpna vagdikfkdv ngdgvinnsd
      961 rvvlgnpfpk ttyslnanfr ykgfdmnvff navagnkvfn avkytglnas fpgynllads
     1021 knawsptntd tnipvlsstd nnnnfgrisd fyiedasfir lknvsigytv kdswlngkak
     1081 lrffisgqnl ftitkysgmd pevglsnfgl dlgkyplsri ymtgvnatf
//
LOCUS       WP_121330615            1007 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121330615
VERSION     WP_121330615.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1007
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111808
     Region          45..1006
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnifsfykgg kalyclfftg illsfssahs kyylpndsli fqqhqiqgtv tdgssplpgv
       61 tisiksrins tvisdyngqy slsaspydtl vvsfigfkta lvpikgrtkv dislefdttt
      121 lqevrvnagy ysvkesertg siaritskdi etqpvtnvla amqgrmagvs iiqnsgvpgg
      181 gfdikirgqn slrsdanapl yiidgvpyas dpigynqtst tfptvtspln sinpdtvesi
      241 eilkdadata iygsrgangv vlittkkgkg gktaltvkst tgvgtvtrlm klmntqeyla
      301 mrrqafkndg lslypsyayd ingtwdqnry tdwqdeflgg taqinniqav lsggsdttqf
      361 mlsssyhtes tvfpgdfiyk kgglqfnlnh rsqdnkfkft fssgytiqdn dqpafdltas
      421 srylapnapa vynekgelnw enntwqnplr llyahsgsks ndlvsnavls yeiipnlilk
      481 gnfgftdlrh ketrtspstt ynpaynltsa yssvyfnntd rqswiiepqi nwekelsigk
      541 igmlaggtfq nqttdrlyqf gtgftsnnli ynlasaavtr vlysdntqyk yqaffgriny
      601 nwqdryilnl tgrrdgssrf gpgnqfanyg avgaawifsk enfikenall sfgkvrvsyg
      661 ttgndqigdy qflntytssg lqydsnvglq psrlynpdfg wevnkkleaa leigflkdkl
      721 fltaawyqnr ssnqlvgvpl agttgfqslq anlnatvqnt gweftlrtin fntlkfnwtt
      781 slnltlsknk llsfpgleas synqkyrige plnielgyqy tgidpqtgiy lfsdknkdgt
      841 isfpedkqti mdlnpqyfgg lqnqlsykgw kldflfqfvk qknrtyytdf agqmanqpar
      901 lvgswtqpgd nalgqiyttg yngaaltady lfsqstgsit dasfirlkni alsydlplnl
      961 kttkcqlllq gqnlltftky qdgdpefina gylpplkiit agiqltf
//
LOCUS       WP_121330560             315 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Flavobacterium].
ACCESSION   WP_121330560
VERSION     WP_121330560.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33975
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msntiekikc liigsgpagy taaiyaaran mnpvlyqgmq pggqltttne venfpgyvdg
       61 vtgpemmiql qdqakrfgad icdgwatkvd fsgdihkvwi ndtielhcet viistgasak
      121 ylglpseqhy lqmgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rsekfraski meervrkten ieilmnhdtv evlgdnnvvh aikalnkttg evieipatgf
      241 fvaighkpnt difkdyitld etgyiintpg tsktnvegvf vagdaadhvy rqaitaagtg
      301 cmaaldaerf laskd
//
LOCUS       WP_121331120            1063 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121331120
VERSION     WP_121331120.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1063)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1063
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115891
     Region          32..1062
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkklnryay lcillisigi kaqetkpliq sklegivida atkepvigas inikgtthgv
       61 qtdfdgkfyf qtgqkfpytl ivsflgykrl etvvnqnsvv ieitqeqnal sevvvtalgi
      121 skekkslgyt tqavkgkdlg etketnflns lsgrlagvri tnsqgdmgss rivirgetsi
      181 agnnqplfvv dgvpvdnsql gsvggatrdf knaiadinpq dietltvlkg pnaaalygsr
      241 aahgvvlitt ksgknqkglg itvntgitvs qvttlprfqn sfgqgsngkf sfvdgkgggv
      301 ndgvdeswgp kldgrlipqf nsngvavpfi ahpdnvkdff ntgltydnsi siaksddksd
      361 frlgvnnqkq lgtvpnsevn ktnftintny qiskgvrvgv nanyivtdap alpggpsgnr
      421 aagvmlqflw fgrqvdteev qrnrnvnwnn syysnpywna yynttsqqrn rligdihlda
      481 klaegfnfkf rtgidyyndr rkyeikygtn gtpfgsyaed aytvseqnte giftytkkln
      541 ddfsldalag fnvrthsdan nyqkaprlav pdlytltnsr dpltssniys rlkvysayas
      601 aqfgfrnyaf lnvtarndws stlpsnnrsy fypsvngsvi ltdalnlksn tldflklrgg
      661 wsevgndadp yqlstvynfq tafdgnpiqt ssqkklndnl kpettrstev gleasfwknr
      721 lhfdfayynt nsldqileik ttaasgynsq linagkinnh gveiqldgnp vqtenfrwnv
      781 avnyaknisk veildydkqi qnytigssgg vdvlasvgqa ygalygtayl rdangnivvg
      841 anglpkadpq kkvlghytpd ytggvtntlt yknlelsflv dasvggqifs gtnrtgnytg
      901 vldqtmpgrd aangglsyyt tasngsvkts lpagttapsg avvyddgmif kgvyadgtpn
      961 ttllsaqeyy kasyniseay lysstyvklr evkltynvdk klvkklglag asftasgrnl
     1021 ffiykdapni dpesafntgn aqgleslslp ttrsyslnvn lkf
//
LOCUS       WP_121331366            1000 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121331366
VERSION     WP_121331366.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1000
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109239
     Region          23..999
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfifsfla llllpaymsg qaikgkvvds sgmgvpgavi sapqsrtsad adfdgnftin
       61 akegetlkvs mlgfdavtii atsgamtitl keagdtalke vvvigygtrk kidntsavss
      121 ikseeitkmk vinasqaiqg kaagvqvsts dapgstpsvv irgagtalgg rnplyvvdgm
      181 ptdninnint nditsyevlk dasslaiygt rgangvimit tkagkgkltv dvesfagfrt
      241 plksvkmana deyvrysnaa fskdypsgrf sanqpyntnw fdeitrtgsy tqnnisisgs
      301 senvkyffsv gnyeekgiln gsdygrttfr nnnefklsdk vkltqnfsvs sikntpmpls
      361 aftnayrqsp lvpvryadgk ygvpfvkdgi vgetgdsfnn vgnpvaqldy tneqqqtvtl
      421 qgglkldydi ikslkftsqf ngefytykqy nyvdnialws aadptrivad ypkdlnintl
      481 trsrdqyfnw nlsnyltfnk vfadihdiev tagieanvqg trekltidrk nvnansnyws
      541 lkdvnvasnv tglkdealnq rrlasyfarf qyklmdryll tgtvrrdgss qfaddkrwgt
      601 fpsvglgwiv skesflsnve pinllkirgs wgrlgnqnvp lntqlltsgl dysnlgsgtt
      661 insqvdpnls weiveelsgg fdfevlnsrl kgsfdvydkn ttntilnvkp ystsgitvat
      721 pshigevsnk gyeislrwdd kindklsywv ggnfshnkne ltslknvqln piiggslgng
      781 qntkildnts vgqplgsffm yeyagvdptn gqmlyykadg skvaqtglde lkdkkyvgsl
      841 lptsnygvsl glnyksidfs vdgygtggak vyngkkaqrf ggenieasva rdfwtptnat
      901 ssnpapsnat pvastyyles adffrinnit lgyklplrdd qfisfcriyv nainpfisqk
      961 fsgfspdvts dgklvegtqg veldaypslr sfviganlkf
//
LOCUS       WP_121333750             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_121333750
VERSION     WP_121333750.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53579
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltf
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_121333937             356 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Pseudomonas aeruginosa].
ACCESSION   WP_121333937
VERSION     WP_121333937.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..>356
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..356
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddiv
//
LOCUS       WP_121335002             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Pseudomonas aeruginosa].
ACCESSION   WP_121335002
VERSION     WP_121335002.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         <1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          2..359
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(9,67,86,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(38,118..119,128..129,132..133,136..137,139..140,
                     142..147,149,151..153,156,179..180,275..276,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(113..114,118,121,124,165..168,188..190,225,236,
                     253..255,262,264)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(115..116,118,128,171..172,179,195..196,198..201)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(148..152,155,158,181,183)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 lethagetrv satpetvkkl igqghqvivq sgagvnasqp dsayeaagat igsaaeafga
       61 dlvlkvvaps aaelaqmksg avlvgmlnpf dneniarmae rgitafalea aprtsraqsl
      121 dvlssqania gykavmlaan hyprfmpmlm taagtvkaar vlilgagvag lqaiatakrl
      181 gavieasdvr pavkeqiesl gakfvdvpye tdeerecaeg vggyarpmpa swmerqakav
      241 herakqsdiv ittalipgrk aptllheatv aemkpgsvvi dlaaaqggnc plteadqvvv
      301 rhgvtivghs nlaalvpada salyarnild flkltlnaeg fsvnleddiv aaclmcrdgq
      361 avrkng
//
LOCUS       WP_121337675            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 123].
ACCESSION   WP_121337675
VERSION     WP_121337675.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 123
  ORGANISM  Flavobacterium sp. 123
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Flavobacterium sp. 123"
                     /db_xref="taxon:2135627"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118230
     Region          27..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngflv llvvlmaqlt faqeravsgt vsdnaglplp gvsvlvkgtk tgaqtdfdgk
       61 ysikatssqt lvfsyigmkt qevkasatsi nvklkddsve lgevvvttal gikrekkslg
      121 yatqevkaad ltagagsgnf lnelsgkvag vnikrnnnfg gstsaisrgv kalgqtneml
      181 ivvdgmpinn antnsnqgnq tagrgttydy gnngmdinpd diesinvlkg aaasalygyl
      241 agngvimitt kkgkaktgmg itvssevvtg gidkstfpky qnkygagygp yyedpsglfl
      301 yrdidgdgnd dlvvptseda sfgaafdpnk lvynwnaftp ysdsygkatp wqaakngpit
      361 fftsplsisn svsfedgnek tsvvfnynnt kqngimpnse lkknsfslkl nhqftdklsl
      421 stfanysqqn tigrnstgyn dniagmfrqw fqtnvdiqel kqvyersggq nvtwnwsdpt
      481 dlrpiywdnp yftryqnyqn dtrnrftgya kldyiltdwl tatgkvssds yaeireerra
      541 dgsvpaefgi nrndegsgyq rynrnfseqn ydfiltfkkn isedfsfngi lggsakrssv
      601 nsilastegg livpgiyslt nskstvpfpl egatkdgvns yyasvslgyk dmffldatsr
      661 rdafsvlpkg nnslfsnsvs gsflftklvn kdwlsfgklr agysesplgt pslslvdtyt
      721 kydpfngqql ysvnsiknnp nlapiktvaq eiglemqffn rrlgfdvsvy knensgeavn
      781 vpfststgys skyinaadiv nkgievqfnv tpiktndfaw dvfvnwsknn sevvalapgi
      841 enlqlnsfqg gvslnavvgq plgiikgtdf tyldeqkvva angryklnts tnniigdina
      901 dwiggirnkf tyknfsfgfl idmkkggdiw sldqsygqat glyaesagin elgnpirnti
      961 angggiilpg vqadgtpntv rtpspnqygn mqgyrrmpnk afiydagfik lrevnityvl
     1021 ptsvvskmhl temkfslvgs nlwiidkslp yadpesglgs slassgystg slpttrnigc
     1081 nvtfkf
//
LOCUS       WP_121338133             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 123].
ACCESSION   WP_121338133
VERSION     WP_121338133.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 123
  ORGANISM  Flavobacterium sp. 123
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Flavobacterium sp. 123"
                     /db_xref="taxon:2135627"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109612
     Region          21..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnfifsfla lillpaymsg qvikgkvldq ngigipgafi vasdskttad tdfdgnfnin
       61 akagevlkis mvgfdalsik atsepmtikl keskdtelke ivvigygtrk kidnttaits
      121 lkaeeisktk vlnasqaiqg kaagvqviss dlpgstpsvv irglgtalgg rtplfivdgm
      181 pteninnint nditsyeilk dasslaiygt raangviiit tkkgkgdkvs vefesfagmr
      241 eplkkvkmag snkysyysnm alqsttfsqd qptntdwfda itrtgsykqn nvsvsgsten
      301 ikyffslgny eekgilngld ysrttfrnnn eykiskkltl nqnfsfgstk stpkpldaft
      361 aaykqspivp vrfpngqygv sfvgddgfag ttgssfnnvg npvaqldffn eqqksimlqg
      421 glkldyeiik slkftsqfng eyyswknynf edtkniwlaa dpsrvasays ptanvnlltk
      481 greqyfnwnl snyftynkvf adihdvelta gietsvkgsr ekltiarknv nadanywsls
      541 gvnyvgtvtn yndevfnqnk lasyfgrfqy klmdrylltg tirrdgssnf gkdyrwgtfp
      601 afglgwiisk eefmanvkgi dllklrggwg klgnqnvpln sqayssglss ylggsilyeg
      661 ttinsqvdps lsweiteess vgldfellnk rlkgsfdvyd ksttnvilnt kpyltsgisn
      721 sspahvgevs nkgyevalrw ddkitdnlty wvggnysnnk nkltglkdat lapinggglg
      781 ngqwtklldn ssigqplgsf ymyeyagfda tngkmlyfds tgskvaqdvl adkdkkyvgs
      841 ilptstygvs lglnyknfdf svdgygtqga kvyngkkaqr ftgenieesl atnfwtvnnt
      901 tasvaapfnq vpvastfyle sgdffrvnni tlgyklplkg efinscriyv nainpfitqk
      961 fsgfspelng ngdpygtqgi eldayptlrs fviganlkf
//
LOCUS       WP_121337825             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium sp. 123].
ACCESSION   WP_121337825
VERSION     WP_121337825.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 123
  ORGANISM  Flavobacterium sp. 123
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Flavobacterium sp. 123"
                     /db_xref="taxon:2135627"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33864
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaaran mnpvlyqgmq pggqltttne venfpgyvdg
       61 vtgpemmmql qaqaqrfgad irdgwatkvd fsgdvhkvwi ndsielhcet viistgasak
      121 ylglpseqhy lkmgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rsekfraski meervrkten itilmnhdtv evlgdeqvvt avkaknkttg eifdieatgf
      241 fvaighkpnt difasyltld etgyivntpg tsktnvagvf vagdaadhvy rqaitaagtg
      301 cmaaldaery iaake
//
LOCUS       WP_121340953            1086 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 120].
ACCESSION   WP_121340953
VERSION     WP_121340953.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 120
  ORGANISM  Flavobacterium sp. 120
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Flavobacterium sp. 120"
                     /db_xref="taxon:2135626"
     Protein         1..1086
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117903
     Region          25..1084
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngilv llvvlmaqlt faqersvsgv vsdnaglpip gvsvlvkgtn sgtqtdfdgk
       61 ysikaspsqv lvfsyigmkt qevtassasv nvklatdsqe lsevvvtalg ikrdkkalgy
      121 atqevkgdav skvkssnfvn slsgkvagle iktsgnlggs tqvvirgnns iagnnqalfv
      181 idgvpidnsn snsgdqkagr ggydygnaas dinpddiesi nvlkgaaata lygsrasngv
      241 vmittkkgks qkgigitiss sltlgtadke tlpryqnkyg agygpfygpn edsyfneadv
      301 ngdgvpdltt pftedasyga afdpslliyq wnsiypqlte tygkatpwva gkanpnsvwg
      361 tgstavnsvs ldggddkssf rlgftnllqe gslpnssikr ntisfsgshn lteklkasas
      421 fnfvktdgkg rngtgyssgn vmqqfrqwnq mnvdfdeqka ayfltrdnit wnpnsttnlk
      481 piysdnpywt fyenyqtdtr sryfgnvale dkltdwlsil grfsfdtyae lqeerinvgs
      541 advskysryn nnvseynydl mlnfnkdlte klnlegnigy nvrnnlrnsi faatngglnk
      601 srlfslsnsf apilapqeye assmvdgayi raslgyddfa ylegtyrtdr ssnlpkannr
      661 ygyysvsgsl vfskyinaew lsfgklrany aevgndttpy rvfntyeigt pfdgtgvasn
      721 ngtlanpnll perqksyefg lemaffkrrl gfdvsyyrdl nvnqitsipl stgtgydsav
      781 lnagtienkg fevqinatpl ktdsfkwdln lnwsknkslv vellngienl qlaslqggvs
      841 inatpgqpyg tirgsdfiya engqpivnqt gsatrigtyq rtsasnvvig dinadwkagl
      901 nnsftyknfn lsflidmqkg gdvfsldtwy gyatgmydfs aadnelgnpv rnpivgtpgn
      961 ygansggfil pgvapdgtpn qvraagdiyt tawgyarapn klhvydagyv klreasltyn
     1021 fntktlektp ftnivvslig rnlwiidknt pyadpeagls sgnvqgyqsg aypsireiga
     1081 slklqf
//
LOCUS       WP_121341150            1029 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 120].
ACCESSION   WP_121341150
VERSION     WP_121341150.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 120
  ORGANISM  Flavobacterium sp. 120
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Flavobacterium sp. 120"
                     /db_xref="taxon:2135626"
     Protein         1..1029
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112377
     Region          25..1028
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkilgqkllf flfvfsvhli ngqtktitgk vtdqsglplp gasimvketk lssisdldgn
       61 ysiktengkt lvfsfmgfkt keiltsegsk idvvlddnsl tlgevvvtal gikrdkralg
      121 yasqelksdd inrvnstnfv snlsgkvtgv qitgsgngit sssrvvirgd kslninnnsp
      181 lfvvdgipin nntygvggns tnqrdlptdy gngaseinqe dvesvnvlkg aaasalygsr
      241 aangvivitt ksgkknkglg vsisssymts ealrlpeiqg vygagsklty dpgadtnlgp
      301 rldaglsilq ngspgysvgq gvalpfqfry dlndffrkgs sisnsvsitg sdektnfrls
      361 ygkttsediv pnsnlkrdni slnlnykisd kwkvitiaty tksgsdntpv tgygsqglmy
      421 nllwnhtnvd ldwlkdywit kdvqqnsmfs wgdnpfkiay eninafkkgr lygniastyd
      481 fnenlslmvr mgmdnsndfr wsrrpigssr ypqgmyreqs iafteynada lltydrtfgd
      541 fstklslgan rmnqytsegk iegqgisipg iynlqninvm piqsrniykk rinstygman
      601 igyknylyld ltarndwsst lpadnnsyfy psaslsfipt slfemnknid flkfranaas
      661 vgndtdpyrl vktyengala gtltnpstil nsnlkpeiat syevgveaqf fnkrvtldas
      721 yyitnsknqi vgldvsqatg stsnvinagk iqnkgieigl gitpvksenl ewsinanfsq
      781 nrgvvkelte gissyiiaqg pnggtvearv germgdmygr gylrspdgqi vfdntgspil
      841 dtqikkigny npdwmlglst nlrfknvtln alfdvrhggk iysmtnaigm esgilavslp
      901 gretgivgdg vvqnsdgsys pnttvisaen wyysnafrrd nieansfdas yvklrevsln
      961 yrfpqklika anvqnisigl vgnnlalwtk vpnidpetqs lsggtllpgf evlqlpssrs
     1021 ygvklnvsf
//
LOCUS       WP_121342142            1021 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 120].
ACCESSION   WP_121342142
VERSION     WP_121342142.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 120
  ORGANISM  Flavobacterium sp. 120
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1021)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1021)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Flavobacterium sp. 120"
                     /db_xref="taxon:2135626"
     Protein         1..1021
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113169
     Region          56..1020
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkfsfykgk wwipiflwvy liftplfsyg sicvvkskie shkvipstal gmtqsiviig
       61 tvrdsqgvlp gvtvsvqgks tatitdyqgk ysitatatdi lvfsfvgytt lnipiagrtv
      121 vsvhlqedat qlqevkinag yysvkesert gsiakitakd iekqpvtnvl atmqgrmagv
      181 nvtqttgvag ggfdiqirgq nslraggnep lyivdgvpfa sevignsntt gvlprsaspl
      241 siispteies ieilkdadat aiygsrgang vvlittkkgk qgktqytanv srgtgtvtrf
      301 mdlmhtqqyl emrkeafand gittfptsay dvngtwsptr ytdwqreltg gtseltdvqt
      361 svtggsqrnq fylganyhke ttvfpgdfnf nrtsvrgsfs hasederfra nfsvgytmqg
      421 ndlpatdltr dsrilapnap alydaegkln wengswnnpl rllyasylak sqsliansql
      481 syriveglef rtafgftdlr hnerrtnpst lnnpslgygs sysslyrntn nrqsysiepq
      541 ldfnrqwnds kiavlvggtf qqqegnqlll fadgftsnsl lntlaaasav yvaaddasqy
      601 kyqaffaran ytykdryivn ltgrrdgssr fgpgkqfatf gavgaawlfs reafftnnsi
      661 lsfgklrvsy gttgsdqigd yqfldtystt sngyqgitgi qptrlynpdf gwetnrklei
      721 aletgflkdr ifltwawydn rssnqlvgvp lpgttgftsi qanldatvvn sgtelslrtv
      781 nlqkkdfswt tdfnisfmkn klvsfpnlaa styrnqfvig epinikllyh ytginpetga
      841 ytfedvngdg vltaekdkkt ivdfnpsfyg glqnqlryqr lrldflfqfv kqqnystdyi
      901 farpgllsnq pvsvtdrwqk agditpyqmy ttnsnsdagk afnnfqasdg vvtdasyirl
      961 knvslsydlp qnwigqlqcr lyvegqnllt ftpyegtdpe fkttgflppl rmlsagvqlt
     1021 f
//
LOCUS       WP_121342272            1024 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 120].
ACCESSION   WP_121342272
VERSION     WP_121342272.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 120
  ORGANISM  Flavobacterium sp. 120
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Flavobacterium sp. 120"
                     /db_xref="taxon:2135626"
     Protein         1..1024
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110072
     Region          25..1022
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miqkvfkllf vfclfsfqla kaqttvsgki tdgstgmslp gvnvvvkgtt ngvstdfegk
       61 ysinvpsrsa ilvfsfvgya ekeiaftgat tlnvsltena nqlgevvvta lgiskdqrkl
      121 gyavttvggd nldkaretnv anglagrvsg lvvrgtnsga ggtskvllrg isgitsggsp
      181 lfvidgipid ntqrgsagew ggadqgdgig ninpddiekm tvlkgqsasa lygaravngv
      241 iiittkkgkk ggdyaitfns nfmadapvdy tdfqdqygqg tggskplttg aalatnrnsw
      301 ggkldgssvi gfdgqqysys kakesyidfy ktgtnltntv svskglgdga frlsfsnlds
      361 ksivpnsglk rttinlsadq nitdklnvaa svnytdersn nrpflsdgpk npnnflllap
      421 nvdhnifapg ydpitgaevv fsddnyvtnp yfivnqgved ptrkrtisvl stkysftddi
      481 yamvrlgndv sndtefsvnp wgldyttnkr gsldskgqst rselnldglf gakfkigtdf
      541 svdalaggni rqnkyeriki gggpfvlpyl ytpnnvvnin reynytgses hsafysfdfg
      601 ykkyltlstt grydvyssls saassdnavf tpsvsgafvf ndllhidald fakvrlsyav
      661 tsgeatpytn slyfnsgnsl vrngvsyatg sipstlptll kpftvdevel gldlrffksr
      721 ltfdlsyyek tshdeilnae ysrstgfatg vvasasiqnk gleiavtgip vktdnftwtt
      781 slnttnfknk vlatnadetp ivlgsnrgtl gnavtayvvg eagpqirayd yayntdgsiq
      841 vdaaglpvrg efknfgsvlp tfyggwnnef kyknfnlafl vdfnygnkvi sateyysrlr
      901 glnqatlvgr etgvtnsgit ataenyyqae arnitstsvv sgdfiklrql sfgysfpksv
      961 mgkisflegi disfvarnla ilmrkadnid pessfgsnvk yygiegtslp strsfglnvn
     1021 fkik
//
LOCUS       WP_121342382            1002 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            sp. 120].
ACCESSION   WP_121342382
VERSION     WP_121342382.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. 120
  ORGANISM  Flavobacterium sp. 120
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Flavobacterium sp. 120"
                     /db_xref="taxon:2135626"
     Protein         1..1002
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109683
     Region          21..1001
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrniifsfla lillpaymsg qvikgkvldk dgigipgami vaadsktstd tdfdgnfnin
       61 akvgevlkis mvgfdavsvp atatpmsiql qeskdtelke vviigygtrk kidnttaits
      121 lkaeeisktk vlnasqaiqg kaagvqviss dlpgstpsvi irglgtalgg rtplyivdgm
      181 pteninnvnt nditsyeilk dasalaiygt raangviiit tkkgkgdkvs vefesfagfr
      241 aplkkvkmag snkyshysns alqtttfsqd qpvntdwfda itrtgsytqn nvsvsgasen
      301 ikyffslgny qekailngld ysrttfrsnn efkiskkltl nqnfsfgsan stpkplsaft
      361 naykqspivp vrfsngqygv syvgadgfag tsgssfnnvg npvaqldyfd eeqrsitlqg
      421 glkldydilk slkftsqfng eyyswknynf edtktiwqsn nnpgqlssii ypadknvnll
      481 tkgrnqyfnw nlsnyltynk vfadihdiel tagietsvrg areqltvark nvnadsnyws
      541 lagvdyvgtv vnykdevfne nkiasyfgrf qyklmdrylf tgtirrdgss nfgkdyrwgt
      601 fpafglgwvi tkeefmanak gidllklrgg wgklgnqnvp lnnqayssgl tyylggsiln
      661 egttinsqvd pslsweitee tsagldfell nnrlkgsfdv ydktttnvil ntrpyitsgi
      721 snsspahvge vsnkgyeial rwddkltdnl sywvggnfsn nkneltglkd atlapitggd
      781 lgngqwtkll dntsvgkplg sfymyeyagf datngkmlyy tatgakvtqd aldanadkky
      841 vgsilpnsty gvtlginykn fdfsvdgygt sgakvyngkk aqrftgenie dslatdfwtv
      901 nnttaskpgp fnqvpvasty ylesgdffri nnitlgykip lkgeflnscr iyvnainpfi
      961 tqkfsgfspe lngngdpygt qgieldaypt lrsvviganl kf
//
LOCUS       WP_121342714            1020 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [unclassified Flavobacterium].
ACCESSION   WP_121342714
VERSION     WP_121342714.1
KEYWORDS    RefSeq.
SOURCE      unclassified Flavobacterium
  ORGANISM  unclassified Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="unclassified Flavobacterium"
                     /db_xref="taxon:196869"
     Protein         1..1020
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111159
     Region          25..1018
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskftwilt lclaffiqfs faqektvsgt vtsksdqmtm pgvnvvvqgt srgvqtdfng
       61 efsikasvge rlvisivgsk pvtvvvgaqn rinvqleddt tvlenviveg ynvtktkaks
      121 nvasvtvssk tiegrpnasf iqtlqaqvsg lnitsgtgqp ggnsqiiirg tgsingkvep
      181 lfvidgipln sdnfrsinpd diesvsvlkd agatsiygnr gangviivkt kkgsfdsals
      241 vkytsttgfs tlqktdynlm nsqelltter aygrgrgftn gpnggpmtda qiaaavntdw
      301 tdyffrtgvt qnqvvslagg gknmtsftsl gyfdqqgilk gsdlkrfsfr snitgksnnd
      361 kftystttsi nfsrrneana igtggvnqny vlgannsapy ispkdystsq qllldyqtqg
      421 gtllltplfl vdklktfenr idelkglini dggykitkdl sigtalaldy tqqnsytwqs
      481 ptafntllfs aaatasdten qfferdlals sntrlnynrs fnekhtinag ayieyikahr
      541 naftftqrgl npkttspgag tgyiidgpan drnvptvsaa kqetglfsyf gtadydydsk
      601 ygfgatirrd assrfaddyk wgtfyslsgr wnidkeafmq gsvinalklr gsygtsgnqd
      661 ilngtysaln ntrelyttgv gyngtqsfvl sqlavpdlrw ektaqanigl dfevfkgrlt
      721 gsfdvyqkkt tdlflrvpls gvnaadgina nfgalknegv eatlnyglfk sdkvggfnla
      781 lnfngsynkn tildvagttg vidngttviq egktideffl tryqgvnpan gnllflnaag
      841 eitenpnvtg drvltgksrv plyqggfgfd ssykgffltt nfsyaaevyr idfdlqglqn
      901 ptnnvgvfnv sadllnawtv dnrvtdipal raanyaaqnn sdrylvdasy vrlrfasfgy
      961 dvpkkllert pfktvkafiq genlvtfskw rgwdaesprt adqyqyptpk ifsvglqlef
//
LOCUS       WP_121344026             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gillisia
            mitskevichiae].
ACCESSION   WP_121344026
VERSION     WP_121344026.1
KEYWORDS    RefSeq.
SOURCE      Gillisia mitskevichiae
  ORGANISM  Gillisia mitskevichiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Gillisia mitskevichiae"
                     /db_xref="taxon:270921"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106719
     Region          27..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrhnqlssin lmlflfifpv avfaqetltg ktinestgea vpfvnviqkg tsngttsdld
       61 gnfslsvesl patlvfsyig yetqervvtq nspinvsfve aaaaldevvv tglatsikrt
      121 nsanavasis aeeligttpp ptldgafygk fagavvnans gapggglsik lrgatsiqgn
      181 tqplyiidgv yvdnssiaag lntvsaaasg gsasnqdnpt nriadinped ianieilkga
      241 saaaiygsga aagvviittk rgkagetkfr fsqsmgwtea inllgvrdyt eqrvldsfge
      301 adraayvaar dagtlvdyed eiygekglin itnfsmsggs ektrffagvt yndedgivkn
      361 tgyektslrl nldhtptdfl klslssnfin sssdrgffnn dnsgatigia ltatrpwdal
      421 fpnengiypd hpnntsnplq trdlvknnet vnriimggsa nldiykadns nlelilrggl
      481 dyygqktral fpkalqgqkl ingglngvsv qgdtqnknyn lsgflvhnyf tdsninfrtq
      541 lgitreyfdq ntelitatgl vasetnvdqa antgsdqtrl lqensgifaq eevnykdmfi
      601 atlgvrgdks snngdatelf yypkaslavn lnefefwnsn siwnqfklrv aygeagnfpp
      661 fgalftsyda fstdgvlgis lvgirgdanl kserqkelef gtdvnflngr iglsatyyvk
      721 tvddlillad lepstgftrq yvnagslenk gielsldtrp ivtedfqwdl ginffknksk
      781 itelrvppfn lgafgaglgs frieegksat qiigsfpegl rvvgdaepdf qmafnnnley
      841 knfqftmlwq wkqggenvnl ttlltdlnqt shdfddfgad pdgelpngqf rpganasvht
      901 edasyvrlre vglyytiqse tleailngsi nsiklgfsgt nlinifdyns ydpevsnfgg
      961 gsiftgvdvl pfpsskrflf nlsvnf
//
LOCUS       WP_121344194            1030 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gillisia
            mitskevichiae].
ACCESSION   WP_121344194
VERSION     WP_121344194.1
KEYWORDS    RefSeq.
SOURCE      Gillisia mitskevichiae
  ORGANISM  Gillisia mitskevichiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Gillisia mitskevichiae"
                     /db_xref="taxon:270921"
     Protein         1..1030
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113385
     Region          22..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrlllill cfigmqafaq ermltgtvmd gkglpvtgas vyikdtnkgt vtnmdgkftl
       61 napenidail visslgfdtq elklgtqttf nvtlvenleg ldevvvtalg ikrekkalgy
      121 svteikgeai aetqrenfvn glagrvagve vnstsglpga stsivirgis slsgsnqplf
      181 vvdglpisnn ttstaifass vsgtsfdnrg vdftnraadi npediesvti lkgpeaaaly
      241 gieaasgaiv ittkrgkagk tridysnsfr idriveypdi qqtydrgagg ytnegneely
      301 yfgepypegt kfydnvknff qdaytqkhnl sisggneksq yrisashtda egfvpttgle
      361 klnlstaita efndflsadv tfdytrsdnd qtfrgsggpl lhlllwpstd dasnyltpgg
      421 arrdyadysn avenpffnvn knifnsltdr yklntqvtat plkwlkfvgq vgvdyfttkn
      481 tivrhpesnt gkdyggifdq alvttrnltf qyytqitppn lfndklktdi kigsavydyn
      541 tfsaaaggqd fqapdlwsin ntdldthraf nnlterrlvg afaslnasyd nmlyltltgr
      601 ndwsstlpkk nnsffypsag lsfiftelea lkpfkdvlty gklrasvaqv gkdarpysir
      661 pfytnalttg ggfrygftgp sldlkpemtt syeygielkl fnnklgidat yfnknsvdqi
      721 vqnlrlsyat gfvlmtfnag eiqnegielq lnatpveten fswdvlanyt knwselvslp
      781 gdvsefynsd twlygnvrvg srvggslttf tgydyerneq gdvlinpsng lplldtsewi
      841 vvgdrnpdft mgvtnslryk nlslnflldf rvggdvynat ehylttrgls krtldretpr
      901 ivtgvlkdgn entgtptenn ipidlyrnst ywssiyphqs fiekdinwmr lrdvtlsynf
      961 pasalerakf irsasvfvtg tdlflwtnys gldpvasgns aavggaggag ldygnfplpr
     1021 glnigmrvgf
//
LOCUS       WP_121345465             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gillisia mitskevichiae].
ACCESSION   WP_121345465
VERSION     WP_121345465.1
KEYWORDS    RefSeq.
SOURCE      Gillisia mitskevichiae
  ORGANISM  Gillisia mitskevichiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Gillisia mitskevichiae"
                     /db_xref="taxon:270921"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35028
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtverikc liigsgpagy taaiyaarad mkpimytgme pggqltttte vdnfpgypeg
       61 idgpammvdl qkqaerfgtq vrfgmvtevq fnnepggihk acvdnstwie aesiiistga
      121 takylglpse qrlrgggvsa cavcdgffyk nqevaivggg dtaaeeatyl anicskvtml
      181 vrkdemkask amqhrvtntk nivlkyntqv devigeqvve glrmvnnvtg ekeeieitgl
      241 fiaighkpnt difkgqlemd dmgylitkgk stktnipgvf asgdvqdkey rqaitaagtg
      301 cmaaldaery lssveelies naeanl
//
LOCUS       WP_121345723            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gillisia
            mitskevichiae].
ACCESSION   WP_121345723
VERSION     WP_121345723.1
KEYWORDS    RefSeq.
SOURCE      Gillisia mitskevichiae
  ORGANISM  Gillisia mitskevichiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Gillisia mitskevichiae"
                     /db_xref="taxon:270921"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113512
     Region          20..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkiitrlii lfcsyfsfgq titgkvtdin gtllpgvsil vvetnkgttt nfngeysita
       61 qegntlkftf igmrtqnvtv tndatldivl iddieqlnea vvtafgikke krsvgyavqe
      121 igneelnrnn ntdvlgglqg kvagvninas sgaagagssi virgitslnp nannqplfvv
      181 dgipisneap tgsllpstgs nspssseqfs ftnrgadinp ndiesvsilk gpaatalygl
      241 raangvvlit tkkgksgetk ynfktslgfn evsvvpeiqk kwregisggi vstpndnapd
      301 gydyedgrtf gfwtlgpeya egepiydnfr dffrtgltfn nsfsasggge sytyfgsisr
      361 lddkgivpnt dfdrtslkls gsinvtnkft iepsisyiks egrlpnggdk simsslsywt
      421 ptfdvndyll pngneknyta gvadnpryfa evsyldsqvn rilantqfky eftdwasvqy
      481 qigidnyhds rrrfvppdid pgsatqgfiv keglnynewt snlfvtlshe fnedfsgsll
      541 vgnqisdiet rrltnraegl spenlgsfdq atnffidegg terkivglfg dlrldykntl
      601 ylnitgrndw sstlpkqnrs ffypsfnlsy vlsqtlrdae slpnfmtyak lrasyaevgk
      661 dapafvgiyy dnptnfpfgt vdgfsrdsqg asnklkpert salefgaefk ffesrlgfdl
      721 tyyiqkskdq ilpvpvaqss gfdtfvlnag eienkgfeal vnivpiktdn fnwditlnfs
      781 tvdaevlslp egideiifad sgfpgivsrl evggapgdlf gyiwerdang nriiqedgfp
      841 rvlanspsdr vkvgnalpdw igsigssiky kglalsflle rkeggdlyds gqrngirngn
      901 lkitefrdqe vilegvledg spnnipvvit edyyrssaiy nraseilvqd aswwrlrnvt
      961 lsydlskkil drsfinratl sftgtnlwid tpfrgydpeg sqfsagtnay gftglnipnt
     1021 rnylfginln f
//
LOCUS       WP_121346447            1072 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gillisia
            mitskevichiae].
ACCESSION   WP_121346447
VERSION     WP_121346447.1
KEYWORDS    RefSeq.
SOURCE      Gillisia mitskevichiae
  ORGANISM  Gillisia mitskevichiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Gillisia mitskevichiae"
                     /db_xref="taxon:270921"
     Protein         1..1072
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116226
     Region          27..1071
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktkfssilt lllafvvqit faqqqsvtgt vtdedglpip gvnilvkgsn tgtqsdfdgn
       61 yaiqasqgdv lvfsfiglvk teqtvgtsnt isvvmkgdaa qldevvvtal gikrekkslg
      121 yatqevdgsa vsdvptsnfm nslsgkvagl niktsgtigg ssnvvirgss sitgnnqalf
      181 ivdgtpisna ntngsnqqag rggydygnaa adinpnnias invlkgaaat alygsraang
      241 vviietkkgn kgkgigvsvs sslmisdids etlpvyqdqy gagygayyes edgyfnlfdv
      301 dgdgnldett pftedasfga afdpnrmiyq wnsifpsltd tylqatpwva akntpndiwe
      361 tgytainsva ldggsdtgsf rlsannllqe gnlpnseikr ntitfsatqd ltekftastn
      421 vtftktdgkg rygtgyssgn pmqqfrqwfq tnvdiyeqrd ayfatgenit wnpngpdnls
      481 piysdnpywt ryenyetdtr sryfgnlnln yaindifsvv grfsfdtyde lqeerinvgs
      541 advasysrfn nrvaeynydl ilnfnkditd dlnldgnigg nlrrnqrnyi qaatngglnk
      601 agfyaltnta npmlaptevd yttmvdgvya raglgfknty ylegtirrdr sstlpiannt
      661 fyypsvstsi ilsnlfdasw lnfakfrany aevgndtnpy nvfntyivnp gfggegsasn
      721 taslknldlt aetsksyevg leanfldkri gldlsyyrtr tfdqitavpv snatgrdskl
      781 lnagtvqnkg levllnlnpi rtenfnwnmt inwaknesev ieltdgidnl elaslqggis
      841 inaapgqpyg airgtdyvyd dngnkivgst gyylktgtsn eiigniqpdw tggvsntfry
      901 knlslnflid vqeggdifsl dtwygfatgm ydrsvgtndl gnpirntian gggvilpgvt
      961 adgqpntvra rtdyyanpfg yardankghv ydasfvklre agltynfgek vldalpftna
     1021 sisltgrnlw iihknipysd peaglssgnv qgyqsgaypt areigasvkf nf
//
LOCUS       WP_121351084             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_121351084
VERSION     WP_121351084.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33724
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqmvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstvdgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_121346487            1060 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Gillisia
            mitskevichiae].
ACCESSION   WP_121346487
VERSION     WP_121346487.1
KEYWORDS    RefSeq.
SOURCE      Gillisia mitskevichiae
  ORGANISM  Gillisia mitskevichiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gillisia.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1060)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Gillisia mitskevichiae"
                     /db_xref="taxon:270921"
     Protein         1..1060
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116718
     Region          24..1059
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknkitllaf mvifqftnlf aqektvtgkv teindgmtlp gvnvivkgtn qgtvtdmdgf
       61 ysinvdenqi lvfsslgfet kemkvgsqtt inigmvanle gldevvital gisrdkkslg
      121 yatqevaged lnltneqnvi gslsgrvagv qvtgasgasm ggtqkikirg vnsigggdqp
      181 livvdgtpis nanfagsdes dygnlgqdin ptdiesvnvl kgpaasalyg irgqygvimi
      241 ttkkgskgvk dvqvqvnssf tveragnfmp vqnmygggss qqfrtlangd pyvdlsvdes
      301 wgpkmdgtpv rqvfsfypqd deyqqltpfv ahpdnikdyy etgynfnkgi tvsggnentt
      361 yrlsfndtri egvepntyld rnnlglnasl dlskkltvst ninyarndaq rpkqgseygt
      421 gyftqwfqrn idmnrlkdye yedgtylhwn lrrpdsntge idnlsplywd npyfdayent
      481 nkdsrdrffg nvglsykvlp elelsaavrg diytqnietr tafggkrtpd ftigkyenke
      541 mnyeflalyn kkwddlsing tlggnifnrr ysslyqgtvg glsspgfyni dasidrpnvs
      601 nyllrkqirs mfgmlslgyk dtyfvdasir ndvssalped nnsywypsis gsmvfselvd
      661 wdtlsfgklr asyaqagsdl dayqtslpfg vgtvyngtnt lfvpdnlnnp nikpsfahsy
      721 eagidlrffk srlgidftyy vqknknqiis ldvsgasgys sstinagliq nkgyeiavta
      781 kpivmdnfkw dvnfninrnk sevvelapgi dvytygstty ssvnsylnsy vgeafgslvg
      841 qayqrdeatg killgsdnmp lytdathnfg svlpdfnggl qntfsignfn iaamidfqgg
      901 gqffsrskml avrtgqdplt vatndngmnv rdpledgggv kvtgvsaetg edvtayvdar
      961 syyrnvlgrr iyeewlydas yiklsevrlg ytfgekimqk lpfksvaval iarnpamiwq
     1021 eapegidpsa istgsqsisw yesgqlvsvr syglnlnitf
//
LOCUS       WP_121352503            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121352503
VERSION     WP_121352503.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115673
     Region          24..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllcfvas flllgsafaq kvevsgkvlg ensqplpgvs vqekstsngt stdangnfrl
       61 svarnatlvf ssvgydrkea avgadprgvt itltpasnai sevvvtalgi rrekkalgya
      121 vttvdrkqle qrpeaditrv lngktpgvdi gatsgisgsg tnivirgiss itgettplfi
      181 vdgvpfdast naqsdfrfgn qtssrfldld pnniesvsvl rglsatvlyg eqgrngvili
      241 ttkngsnrrv gnkaeitltq stfankvasl pdwtnayggg thlstgfqfy snwgaafqnp
      301 pvtllhpysr sayaaafpel qgvkipfeah pdninsffrt gwinttsinv agspgansnv
      361 sgnftfyndk gfipgndlrk ytgglggstk lsnrftvsgv vnfantdyqt ppnsastgsg
      421 pqyanypgif advmytprsi dlmnwpfedp ttgasvyyrp sndiqnprwt akyvkftesv
      481 qrvygnlalr ydllknlnim yrigldnfsn fntlqspkgg vqvplgvyrt tnirntilnh
      541 ellanyntrf sqnwdlsvta gsnlrrtlyr qdgmfsqnql vfnlfnhnnf inhtnkgedg
      601 snldfrseye slgvfaegnl gykdflyatv ggrnswvstl eeanrslfyp sgslsfipta
      661 aveglknnkm lnyvkmrvgy atsarfpdpy rtrqalsigs nvfvtqngtq vnsnsipnrl
      721 pnpdlkpell reveagletr lfnnkvnldf twynrlskdq iisqqldpst gytekeinvg
      781 gvrnrgievg lniapvkgrn fgwdftvnft rnrnevtsla dgvkqipvag ftdlgsfaip
      841 gkplgimqgy yvqrdpktgq rivdnqgnyl ssteigiign pnpdfktsli nnltykglsf
      901 rmqwdytqgg diysatirsl largetkdte fdrtlpvilp gvkqdgtpnd iqvdafiayf
      961 nslgfgasdv svfdgtvirl reaslsyslp sglisktpfg gisltfsgqn lwykapntpk
     1021 hmnfdpetsg lgassyrgfe fitgpssrrf ggsirvtf
//
LOCUS       WP_121352999            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121352999
VERSION     WP_121352999.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114094
     Region          27..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkllqlltl vlllivllpw qgmaqqrtis gtvrtenqnp legatitikn tsritqtgdn
       61 grftiqaatg etlvitsvgy epqevkvnng savavtmkas gnnmnevvvt algirrerka
      121 lgysvsdlna qelmknkntn vvnslvgkvp gvnitqfsgs agagasitir ggnstsegrq
      181 nqplfvidgi iydnsttvtg ntgtdglsrs nttysnrimd inpedvetls vlkgaaaaal
      241 ygsraadgvv iittkkgaeg rvtvnvnski stswanklpe vqtvfgpgvy ssngvlntan
      301 tynswgakip sdstiydnig nffrhgliyd nnvnvsggsk ngsfylsgsn fnqtgivpgt
      361 gykkttfrfn geqkygrltl nanvaysnan tdrtlttagl ygsgvgsmqs lyswpvtfdi
      421 knylnpdgtq hrvyagtlal esdrdnpywi inqdnltsqt rrftgginan fkitnwwdit
      481 grlgydqyat ndytfiapgs alaplyqngr lskdlydyty itttvmsnfh ktfgdfdthl
      541 mmgttsedtk ivsqnhwgyg ftipgtisfn nipttskfls dgttrkrlvg aygeagvsyk
      601 dllyltatgr ndwsstlpve nqsyfypsis gsfvftqllp antllsfgkm raswarvgkd
      661 anayatntyv npsisigsyi gvgnqwaagn pnlipeiqns wevggefrfl kgrigldyty
      721 yhsqtenqig qprlaqsggf ifstlnsgsv inkgmeials gkpivqknfs wdvmlnfsyn
      781 kgrlgafipg vayfyptdaq fgtvkaasip ngsyflgmtg qsyyreldsk gkeisngryq
      841 vdpttgfyki nannpvvgnr epdflggfnn tlrykkltls flldlrkggd vfngteyalv
      901 vnglskqtll ndrqsvtvtg vnsvtgadft qtynanqsyt vgsttvsgyd miqrywanya
      961 ansynfitsv nwlklrslsl tydfsglvkn qkvikgisat avgtnlltwt nykgmdpevs
     1021 aaggtggsgs tgidylgvpa vasltfglnv tf
//
LOCUS       WP_121354076            1058 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121354076
VERSION     WP_121354076.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..1058
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117072
     Region          21..1057
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkvqfllcm llltavafaq rtvtgrvada qgnavpfasv tvkgtntgva addngrfsiq
       61 apanstlvit asgfqatefk vgnqtnvnit iggqtnlsev vvttalgikr rpkelgysat
      121 nvtteeltvg rspqvaagls gkvsglaifn vdnsvdpqtk ivlrgyrslt gsndalivid
      181 gipntsqsvl slinpndies vtilkggqaa tlygsqgvng avvittkkgq agkgritfss
      241 sanfdklswl psfqdqygng saytagygta gylpnyldrm kdnwrpfenq qfgdpyngep
      301 rilgrvledg sklivpyaai pgerrkqwnt gytfnnqaay sggdagntyy lsiennnthg
      361 ivphdksnrt gvrfaaskqa drlsmnfagn yvqanfdrtt sdfyfdvlnt aahvplstlr
      421 dwktnkfanp ngyyndyynn pyfnadnnrq vytdynlngs fdlnynfakw lsahntvgli
      481 nnnrvrknyt gqffytdwak nsayvpapwd wandydgidr astdiqggvy drtltetvmt
      541 nnfavtaskd fgdfrnklil gqqlyqrktk diavgsgslv qpglynvgnr rgelsggean
      601 slerkwgyya dfttgwkeql fvhaslrydg tsrfyasgrt aslyqypyyg vdvsyiltda
      661 ipslksstfn yaklraswnk nandnipvyg ldlqfnptgg fpfgntvgys vgdvlpdqnl
      721 kpefvytsev ggefqfwnsr vnleataywq rsvdqvltvk vsnttgspyl rlnvgesknw
      781 gyetdlrvqi ikarnlswem sarysynqnk vtdlyqgvdq fayggyayaq tyviknqsfp
      841 qmkatayvrd patsrvivdk ttgypilssd lvqfgrttpp hiaglgtrlr vqnftltana
      901 eyrggnvifh qlgrdmtftg aggwtsertp hifpnsaynd gtgkyvpntt vnvreseyal
      961 wvnyyrliae nfvtpgwfik lrdvnlsynl pgnlirgski lqgasvavyg rnlftivdkk
     1021 nvftdpefsy ttgngqginn slntppvrqy ginlnltf
//
LOCUS       WP_121354375             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121354375
VERSION     WP_121354375.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106381
     Region          25..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkkidlmam vlllllpfga maqvvvsgtv tdaanapltg vsvrlrnspa aavtdaagrf
       61 slsvpsasgt leftyvgfat qtvalspgvt tytvklqeae grlnevvitg lassvkrsnl
      121 gnavasvsak eltgttvqpt mdaalygkft gsnisansga pgggislklr gitslvansq
      181 plfivdgvyy dnssinagln svskaagqgs tnfqdnpsnr iadldpddid rieilkgasa
      241 aaiygsraaa gvvlittkrg rtgkpriela qsigaqwqlk klgqrdwtee kvnasigpna
      301 vplfraangk vynyeeelyg ntgtmsntri svsggnentk yytgftyksd egivkrtgyr
      361 kssfrlnldq kitsfidgsf nanyvssrad rgyfnndnts ttlgvsfvst psfinlypda
      421 ngnypdnpla psnflqtrdl vtnrenvdri llggtatvri lngskhnlrf iarggldqyt
      481 lntialfpre lqfekngngt ngasingtti skgknlsafl vdnvdvskln frtqvgltae
      541 dldqnnvvnt atqmigsqsn vnqagsikad qavlkqndrg ffvqeevnyq dkliatlglr
      601 gdkssrngna nklyyypkas lalnvhrffs lntgafsqlk lrsaygqsgn fapfgaiyls
      661 lppvifnnta gsvvdltrgn paleperqke welgldagff ndraslefty ynktvedlll
      721 kvvvplssgy tdawrnvaai enkgveialn atpvvsrdlh wnftanfwkn takvtrldvp
      781 afntgafgat lgtyrvelgk sptqivgigt addkidpvtk lavygngepd fnlssyndvf
      841 yksfelsflv hwkkggnnin lttllsdifg tspdydkksl dpsgqktnge yrlaalgsta
      901 rpwvedatyf rlreiglsyr lpkslfrnaa dvrvgvsgrn linvfkynsy dpevsnfgsn
      961 aissnvevtp fpsaksvhft vnltf
//
LOCUS       WP_121354429            1032 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121354429
VERSION     WP_121354429.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..1032
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113106
     Region          32..1029
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 msihltksgg skrtfwlllf qllglslwaq vqisgrvtgp qneglpgitv qiqatrfsts
       61 tepdgtysls aplkpgsyqi qftgvgfkaq tksiqvsgsa aqtvdaqlee dalkmdevvv
      121 tgtsagttrr qlgsyistvk adeltkgatg dvlaalqgkt agaqisqnsg dpaggisvrl
      181 rgvssinsss eplyivdgvi vnnatnrvtn tqnsydgsnf vgtigqnrmv dinpadieri
      241 evlngaaaaa iygsranagv iqiftkrgrs gapvvnfsts imvnelrkkl avnqapvkfg
      301 gspdvqtqdi ltttlttttp vtrydyqdyi fhtgvgtdnn vsvsggseks ryyvsgsyfy
      361 nqgiirntdf rrynfranfd qtfnrvfsmt mglnyinsaa nekpngnsff spmnsvtiig
      421 nfhniferda ngnikavger grvnpvsvie dfkqrqetnr viaslgaklr pfngftfdyt
      481 lgidnygqng ttfmppfayn vntaffgggp tlnptlngya stgndyffqi nnelnanyqf
      541 ditkdlgstt qvgysvqyek nryallqgrg lspfvetvng astilpstde rteisisgay
      601 lqqnfkymnk lfltgavrrd gssvfskdqr nqmyykgsvs yllseedfwk ksmpwwntfk
      661 lraaygesgn ltgigayarf nlyssnsyld rsalqssnqk tnenigperq releigtdls
      721 flnnrvgvqf nwynkrveni nisrqvaptt gftsvldnfg elenrgielv lngspvankt
      781 vnwnltaifn rnrnkmvnig qaltllstng gapvallqgy pvgvfygtff avdangsqvk
      841 nstgfpqiek gkqvsatvye vqrdgsglpt gttlrkvigd pnpdwtgsli nevgykrfnl
      901 rvqldavqgv dvfnadfrtr qgvgngkvae qehlgilprg yvnsvyqiee wrvddgsfvk
      961 lrevslsysl gkmrffndls iglsgrnlvs wdnykgydpe vnaagqstll rgidfgavpi
     1021 prtyrlsina rf
//
LOCUS       WP_121354990             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Flavisolibacter nicotianae].
ACCESSION   WP_121354990
VERSION     WP_121354990.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39984
     Region          1..358
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,88,283,309,311)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,121..122,131..132,135..136,139..140,142..143,
                     145..150,152,154..156,159,182..183,273..274,316..317,321,
                     324..325)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(116..117,121,124,127,168..171,191..193,223,234,
                     251..253,260,262)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,121,131,174..175,182,198..199,201..204)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(151..155,158,161,184,186)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mivgilkepa vetrvsflpe avatltkkgm tilvetgage rsaatnadye kagaricere
       61 evlsqseill sihppgdtls pakilighyq alyepalmtr waqqgltvfs mellprttra
      121 qsmdilssqa niagykavll aanlypryfp mfmtaagsiv pakvlilgag vaglqaiata
      181 rrlgavvevf dtrpavkeev qslgakfiev egaadastag gyaveqtqey qqrqqqkike
      241 slakadivit taqipgkkap vlvteemlng mrngsiiidi aaatggntpf tknnetvvyn
      301 gisivgesnl patmpsdask lygknilnfl qllttkegti qlnwdddlvk gtcvthngei
      361 vnervrslva qpqi
//
LOCUS       WP_121355293             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavisolibacter nicotianae].
ACCESSION   WP_121355293
VERSION     WP_121355293.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34151
     Region          11..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdkqlaekth lliigsgpag ytaaiyaara nlkpmlyqgi qpggqltitt evenypgfpe
       61 giqgpelmih fekqaqrmga dlryglatkv dfsqkpykvw ideekliead aviiatgasa
      121 kwlnieseqr lngygvsaca vcdgfffrgk evaivgagdt aaeealylsk lcstvhmlvr
      181 rdemraskvm qdrvkntpni kiywntetde ilgektvdgm riknhvsget qeipikgffv
      241 aighnpnsdi fkgwldmdea gylitqagta ktniegvfaa gdvqdkiyrq avtaagsgcm
      301 aaldaeryls algl
//
LOCUS       WP_121356196            1065 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121356196
VERSION     WP_121356196.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..1065
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117548
     Region          26..1064
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mqkdlqrfif llgmllacsv vfaqqrtitg vvtndeskep lsgvsisvkg tdrvtstnek
       61 gqfsilvsgn esvlkissvg ylykeitvgg qnsvsislak dvkqmdevvv igygtqrkth
      121 ltgsvgtvdv kriedfpggn lsqalkgqvv gvsvsggysr pgeaatisir npisfskdap
      181 kdplyviddi irtkadfdll dateienisv lkdasaaiyg imgsngvivv rtkrgragap
      241 visytasagi sdatsmpkmm tgyqqalymn dylngsknwd qaavaqlsgi ytqdevdyfk
      301 thnydwlkna wqkayntrha lnvsggsdra tyfagftyss ensnfdglgy krysfrsssd
      361 iklaaglklg lalsgnlsdr kntfnkqgne sldndwktli genqgytpyi nglpilipga
      421 gtssnintyh yfavhelnny tssyntglnf qgqlsyeipf ikglkaavny nknianswgk
      481 qygtkytvyd fnklgsnghi lgdsviktyt wsngdrvrln ptitktyqln ttvnydrtfg
      541 khqigalfvy eqaeafsdgv agqvdgvvvg gldnqnfavg tstnpdgssn etiseagrma
      601 yigrlnysfa nkylfeanlr adasqnfape nrwgyfpsls agwvvsdenf fdnltktvny
      661 lkirgsvgfm gidntksyqw lrsyaiqtgk aavfggnsdr glatvmnidl anravhwdnq
      721 dkydigldar flrnrlsist dwyinksynm lssltsspsi ligtalpten fgkanvfgye
      781 lsanwrdnig knwsynvttn fnwndnrvlv advpkgdigt fkdqngksnd mgfygyhslg
      841 ilrtqaevda yvaqynitdm lgykpgtnnp irpgmlafad vrgkqnattg kydgpdgvid
      901 vndqdflkak qdnhyglgin wgvsyktvsl nvvmgmswgg issvesaark vgtaysnrps
      961 fwsdhwtpdn inaaypspyy tstydvasdf wwrssftfrv ttfnlsytlp rdltrragln
     1021 nvrlflngtn pvnffnpydy kdningsydv fpqlrtfnfg lnvnl
//
LOCUS       WP_121356272            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121356272
VERSION     WP_121356272.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114784
     Region          24..1043
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkiqalllc fallvtglaf aqtrqvkgvv tdsagaplpn vsvqvqntrv gtrtnetgtf
       61 vidlppgsnt llltsigfep qqvnvagkdd vsvtlntarq namqevvvta mgitrtqksl
      121 gysttnlkgd elikaresnv vnslagkvag vrvtsqsgtp ggsskiilrg qssfsdpsgg
      181 qpifvidglp idnssqqlat tpsavpqgsa gvdfgnragd inpddiesvn vlkgaaatal
      241 ygarakngai iittkrgkrg asvvrfnssv rfdkplrlpd yqneyaqgny gvysinstng
      301 wgpkisevqd rtfpnflgqq vklqaypdnv kdfyktgnty insisfeggg esgdfrlgyt
      361 nyyqtgivek esfgrnsinl nagravsakf dvrttlnyvs sigknrpiqs snnsnslvqi
      421 vqflprtvds ralkanyvdp vtgqqitltp trtgnnpywv iynntsennv eriygnavls
      481 ykpiswltis nnfgsdvyne frklvtrpgt agqlqgnffq anlfnrilnn dfiitadkrv
      541 tndlnirala glnnyeayyr rdqadaqqlt vdelytfsna atvtnsntsn krriigvfge
      601 vglsyknyly lnatgrndws stlpvenrsy fypsvstsfv ftelwkpkpl sygkiraswa
      661 nvgsdtdpyq lafnytavsq vfaqygqgsq fpfggllgft ipptipnaql kpqnqqsyea
      721 gidlrflkdr aridftyynt ktadqiiala lpqstgfatk rvnagaikne gieltlsgrp
      781 lmlksfnwdi dvnftknrqt vedlpadikq ytlasayngl qirarngeqi gmwgtgferd
      841 psgnivinpn nglrrvvtdq rfgnvfpdwt mginnsfsyk glnlsflfdf rqggvfysgt
      901 vgtlrslgla ketaidrdki iidkgvllda atgkyvpntv pvqsmqdfwg qfgnntasep
      961 avfdasyikl reavlnysfp akwftnqafv kglslgvegr nlwliksnvp hidpevnlfg
     1021 sasvgegvef ynlpstrsfg inlratf
//
LOCUS       WP_121356579            1108 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121356579
VERSION     WP_121356579.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..1108
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=124204
     Region          49..1107
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknflrfrkr dftrdkyaqe qprslgfllv fflalclpfg llaqvssmtv sgqitdmans
       61 plsgasvvlk gtkrgvttnn egkftmpqvp gngvlvisys gytsqevavn grssinisle
      121 ggtsnmnevv vigygqarkk dltgsitqir pdkiadenpk tvqdllrgtp glsvgfdpsa
      181 kgggtirirg qrsvytdggh ndpliildgt ifygelsevn pddieqidvl kdasaaaiyg
      241 aksangvlii ttkkgkkgkp kinltsnlgi stmasnrkvf gpegymqyrq dwykaptygi
      301 npatgkyeay qtpvsatqnk nlpgfydrpt denlaqygit vdqwkaytaa tngtasaeei
      361 wakrlllqat sltnflngqt fdwynqsfqt gisqdhnisv sgatdqlnyy mslgylsneg
      421 vargntysav rsnlkldaki tkwldigani nfqnrtdgdl avdwgaqilr nspyaaykda
      481 ngnltvhpmg dgsvanygyn yafnrqyldl dkgymvlnti lnakvklpfn itysfnaspr
      541 yqffhdrywe ssqhpdwkgt nglvnreqtq rfdwslnnti nweqtfarkh rvnvtlvqes
      601 ekrqrwqdri earnilpsdv lgfhetfygd knkstyntdd iletadgmla rlfyaydsry
      661 mlttsvrrdg ysafgssnpr atffsaalaw tftnekffhw qplstgklrl swgqngnral
      721 anpylalanl gigagatmgy ldpsgnllqy ryllmdrlan pdlsweksea fnagldfgfl
      781 nnritgtfdy fitptvdmim nrslpgfsgf gsittnlgkv enrgfelsvi sqnirqknfn
      841 wnttfgfsky kntikhlyyd yvdvldaqgn vigskerddv gngwfigqpi gviwdyrvtg
      901 iwqpneaaea akygqrpgdp kvannntand vknpngtitp vydnndkefl gqtnppimws
      961 lrnefnyknl dfsfnmysyw ghkslsgsyl nqdngtsqvt ymqntyekty wtpenptnev
     1021 arldsrgpsn lnspgklydr sfirldnvtl gyaptlgfla krgieklkly asvrnvavwk
     1081 kdktwkywdi etgglapriy tfglnvsf
//
LOCUS       WP_121356669            1047 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121356669
VERSION     WP_121356669.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..1047
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115059
     Region          22..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrklvyflsf llltmqalaq ekkvsgkvtn kgendkplvn atvqvkgtti atqtnaegry
       61 tisvpndssi lvvsfvgfqa aemptsgatv vdvslnqlpl emnqvvvvgy tsqrkkdmtg
      121 avavvdltpv knnssgntmq alqgrvagly iekdgspnga ngkilirgan tlgnndplyi
      181 idgipttrpe vfqtmnpani asvqvlkdas aasiygsras ngviivttkn ggntnskvvf
      241 qfdnsvsvqs ekysrfkvlt aeergralwq asvndrqdpa agygeiynfd wngdfnnpvl
      301 rsvtakpfvg gdpntpagnt dwqdvmykka fvtnnsltvs agnrtsslei nlgyynnsgm
      361 lrytgyqryn gsinaitraf ndrvtfganl rmsnsderlv akdlggestt ylavtlapti
      421 pvyqkdgqtf agelgagysd rnnplhmqyl arwnntnrls tfgnvfaeiq piknlffksn
      481 igadkadyln kviaptfteg alsrstnslt ydqnrflslt fsntlrynwn lhadhrfnfl
      541 vgteyiktdl nfqttkkegf alqtkeyftl naatgntnvs ggstgnrlfs qfgrvdynfa
      601 drylaavtvr rdgssrfgte nqygifpaas vgwridkegf mknnrfvsel klragvgrvg
      661 nqqigdlarf glfdtrygtt laqlvggfwe qymnigtays lngantgtlp sgfvqiqaan
      721 pglkwestee intgvdftvf qnkifgsfdy fsrkttgili tppvasalge gqskavngas
      781 ktnqgwefvi gyrgdrvgql kynvqanfah frdkitdlpe avrpaypgnl vntiighsqf
      841 difgyktagl fqsqdevtka ptqigaapgr iryvdinndg vindldrtwi gttlpkleyg
      901 irvdltykqf daslfgsgva grngfdaytf fnnlmhsren vgpgvfdawt pqntsthvpa
      961 ltlkdnnneg rtsdyfivst ayfkmrniql gysltpkavf srlrffamge nlflvkskdy
     1021 qgpdperidi rpipipktlt lglnasf
//
LOCUS       WP_121356996             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121356996
VERSION     WP_121356996.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106392
     Region          29..988
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mhrkltlyla tlvatflfft hsllaqnrvt gtvtdatgka vagatvilkg tntatqtnes
       61 geftitapaa gtlvisavgf gtqevavqsr ttipiqlttq esnlnevvvi gygtarrkdi
      121 tgaissvqak dfnrgvittp dqllqnkvpg lqvttnsgqp gsattvkirg nnsiragsna
      181 lyvidgvpld grsarpnfgn afgstpdanp lifvnpndia ridvlkdass aaiygsrgan
      241 gviaittktg tagapklefn tsvgvnaglm krfdvltase fktalskynv anqdfggnvd
      301 amkelqnkka tqnyslafsg gsengrfras flaseingyl knstldkyvg nfggqysfld
      361 krltlgfnit aghttedlvp vantsgstgn iissilqwnp tasfrgtngl fyyptngsgn
      421 pvallsgfsd vahvnsvlgn vsatvriiqg ldykflyavn nsvgdrytni ygflqgysgl
      481 sgsgqaaign arltsqtfdh tlnyrtalts qlnlealvgy eywttryqns nvsaqgfntn
      541 lsettftgip ytsmlqngnv qnppgtfvdp kvelqsvfgr aslnyankyf vtgtlradgs
      601 skfgsnnkyg yfpsvgvrwa vnnedfmkgt slfsnlalra swgitgnqef pagasqeqfa
      661 fgsynnasqi nvanpnlkwe etksydigld lstrggkvnf nidyynknts nilfqstaiq
      721 papasiyfin lpanlinkgv eiglgvnvid hkdltwdigg yyahndnklt nftqngkdiq
      781 iitgqingqg vsgtlaqvit nnypvneyfl kefqgydqng nqtfganpiy agnpnptnsf
      841 gvnttlnyhk fgfvvnggge sgyliynnta tsvtniagis ngrnidknsy ssvekptspv
      901 aantrflesg nyfklrnatl syrvgdigry vrnmnvyvtg nnlfvitkfs gfdpevnidk
      961 ssnnypsrsi eyipfptart isvgvnltlq
//
LOCUS       WP_121357122             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121357122
VERSION     WP_121357122.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108698
     Region          29..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkyapckg llpltmllft givviaqpki sgivrgaegl plagvtiaiq gtpvatssaa
       61 dgsfsilakk gdvlifstvg rekamvklld qvflnislpf nsksledvvi igygtsqkrd
      121 ltgavakita gdfnkgnvtd plqlvqgkia gllitkpggd pngeltvrir gatslegqpp
      181 lvvidgmaid dfykaistln padvesftvl kdassaaiyg srgangvlli ttktsriakp
      241 vvaydgwcgv eqisrrfqvl nasqwraata alggasldqg admdwqsais qrafshshti
      301 sirggtdamn yrgsmgyinq egviintgke vmtgrlnihq kslneklavd yninasvtnr
      361 tllfdqwstg ltrtggsftf dvasgylpvw psynpdgsyf niannsylnp lfllkeidrk
      421 qrenffqtsv kadytllkgl nagilgalsr antvhdyfyp gvrerndkae askfnnnkqn
      481 fsgdihvhyq ksfrkqtaei tgvyeynrfi ndgfgvtarg flvpqllnnn lgtatnvqtg
      541 dlssyknevk lisflgrlvy tydnriifta nfrrdgsskf gsnnrwgnfp sfafawrldr
      601 agflknskwl ndlklrvsyg ftgnqenlpp yayqqlygpt gpylyngqvl qsyavvqepn
      661 pdlkwevrrs lnigadftlf ndrlhgtidv fhdktsdmlf lydlpqppfl sdkvsanaat
      721 atnkgtevtl datplltknw kwdlhfnigt lknritnlsg qfngtslsit nrhygyaega
      781 gfsgtyvsel kpgypagvfw lpqfagldad ghalynnydg ngklsgtsmf ytdkdrvfid
      841 ptprfswgft tnltykrfdl sfflrgvqgq kifansllnl gtsvflparn vgvdaltngf
      901 adqpqpssyw vkdgsfvrld nvtagyrfkg tkdlailrly vtasnllllt kykgidpeir
      961 tegaqryidn qyypktkgfl lgvnmaf
//
LOCUS       WP_121357422            1052 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121357422
VERSION     WP_121357422.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..1052
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115029
     Region          32..1051
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkenaklrfc tgffkllfsl llfsfstitq aqtitgtvtd eggknlagvs vtvkgtaggt
       61 ttdlqgryri naganatlvf syvgytnsev pvdgrsqvnv slspnaqnms nvvvtalgit
      121 kqtrglgysa ssvkpeeltv nrtanpinal egkiagvnit slgtgpggss kirirgqssi
      181 sgggsplivi ngvpfdnsny ngntvgvngg gvysdggdgl ssinpddies mtvlkgapaa
      241 alygsraqng vimittktkg rgkgigvsln tnymsetpld ftdyqneygq genglrptsa
      301 nptsgewsfg ekfqpgmtqv lfnnltvpyq pqgsrikeff rhgqnfsntv tleasgdngg
      361 lhmslnntdn wgimpnnkfn rkvlnlgysy nlspkfsfag ninysrevnk nppnianqdn
      421 sipttlmals tsmplsvlea nkynaqgney vwsrfmnrtn pywvlaeqfh nikrdrifgn
      481 vslkynilpw wwiqgragqd yysrdedvnn fptghasrpa aqagffngvy tqesrrfret
      541 nfdfltsank sfgsldvnvt fggnqmrrrf dvnnvqvtdf vvrgvyavqn graknpvydi
      601 nergvnslyg sadlswnrtf yltgtlrkdw fstlaaenng ilypsvsgsy vfseslkgtl
      661 pwlnfgkirl gyaevgsdad vspyadqlfy gissntinnp agtavtvgns gavlpnkhlr
      721 pmriketeag ielkmfnnrv nidaavykkl tidqivsvqi sdasgftstl insgesqnkg
      781 fegllnlvpi lnkdfrweft antaynitkl nrlatdkpge rfttgthpfn geirlvvgqe
      841 laqiagygya rdikgrmifq snglplrtpd fvlfgsglpk wtggflnnfn ykginlsvli
      901 dyklgnnvls gtnfnairhg lhkmtlegre tgfvtgngvn qsggentaqa kvqtywehlr
      961 sqqiveavvy nagywklrqv slgydftryl pakwpvkgmk ldfvannvli fkkwidnidp
     1021 esvgygtdam aglespglpt trglgfnlni kf
//
LOCUS       WP_121357620            1087 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121357620
VERSION     WP_121357620.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..1087
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=119960
     Region          31..1085
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqvypkvkl llllfvsfsf sfqlfaqtap irgkvtdvqt aapiagatia vknskavttt
       61 naageftira ndgdiltvsf igyqtisski tgdfvpialv qndarlnevv vtatgikkev
      121 krlgyatqtv dagrltqare pnplnslkgn vaglsvninp emghapgisl rgdgapmyvv
      181 dgvpmtsdty nvnpddiesf tilkgpnaaa lygfagqnga iiittkkgsr nkkgftvefn
      241 tsnqfskgfi alprvqdeyg pgeygtyafg dgkgggvndy dydggwgpkl dgrllpqydg
      301 pfdpnqtytt kfengltytg hvkptlwvar gkdnlqrflq tgllsttsla lssssektds
      361 rfsvgntyqr givpntslnn fnatanltqr ftnrltltty lnynrqstpn lpdvnygpns
      421 iiynmtlwgg adwniadmrd ywqagkvgvq qkyaeywryn npyfmsyewl rghymnneyg
      481 yvalnyklnn nidflvrpsv naydffnsek vpysansyrs aswgdyredr rslfqtniea
      541 qaryqrnril gfldvqgllg anlrnfkfns nytttnylnv pgiyafsnsl navqatsfns
      601 gmkvlsgyys fdmgygsyvt lnatgrvdks stlptnnnty fypsfnlatv iseyvklpea
      661 isfvkarasf aeskaggtas tfspnisglp gseygyayps pydgpsyqfs rtytlspsyn
      721 ninsasysnq sidpliktns rkaweygldl rflknaigvd itryhyrntg ivskgmsaas
      781 gdysnltngn tytndgweva vnatpfknpn gfnwnvaanw ftfkkvwvnn snpnnyvkng
      841 trtdliygna fvrtpdgqlv hdaksglllr ysdlgvtaqk vyghadpdwq wgvvntlgyk
      901 nlslrfqfdg mvggvmedyv rkktlqggrh ietaegafgd arpndargsa aysyvgqgvv
      961 ltgapivldp itgeitnmkg ltvspntnpt svqgyvsrma sipdldmisk tyaklrevsl
     1021 syafpstlfg nkaffkqasl slvgrnllyf fpsrykdvdv dqytqdsgsn lqtpttrsyg
     1081 vnlnlvf
//
LOCUS       WP_121357561             995 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Flavisolibacter nicotianae].
ACCESSION   WP_121357561
VERSION     WP_121357561.1
KEYWORDS    RefSeq.
SOURCE      Flavisolibacter nicotianae
  ORGANISM  Flavisolibacter nicotianae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Flavisolibacter.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Flavisolibacter nicotianae"
                     /db_xref="taxon:2364882"
     Protein         1..995
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110036
     Region          32..991
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnyikigvaf cglfsclsgn vnaqnasshn ftstvynnqg lpvsgalvan segkavattd
       61 vtgqftvtvp dktllviaan gfqpqrvrvd tvpekitllq aatnpvdvvy kkvqkqdlpg
      121 aisvlnpety idqdynltve ggmngrvagl lwsnniwgme naivmidgvr rdfsditlne
      181 vdqitvlkgv navalygsqa akgvilitsk rgdansrkig vrvnsgvalp kalpqylgsa
      241 eymtlynear rndglaelyd aatiqnyrtg nsyrfpsvdy ysseylkkfq tatdanaefs
      301 ggnniarfys nigwansstl lnagegkneg dnrfhvrgni dlklndyiss sislstvfnd
      361 srrgrtnyws naatllpnrf tpliplsmia pgsttaqayi kasrniidgq yllggtqqfp
      421 tnpladlyvg gydkfirrsf qvtdgidfnl knllqglsfh tlfnldynns yiqstpntya
      481 tyaptwsata dsvnglakfg adlrpgtqni sgttqlqnig lsawlnyeks lnethnfsat
      541 llgfgstikt ndvyqatsna hlglqlnyny khkywvdfss ayvnstklpd gnrtafsptv
      601 slgwllsses flaqskvvdy lklsasagil ntdldisgfy lydnvfnrgt tftwndgvqa
      661 gnqttfsnft gnpalafpkr kelnaslega ffnnlltlqt tffvnrmdgl ltqqfsrypg
      721 ymssfipytn ynankrsgfd lmlnvnkkvg avglnlglna tyadskvvkr delfadayqn
      781 rtgrpvdaif glrsngffad qadidrsakq lfgevkpgdi kyvdqngdnl idqrdeimig
      841 rfiapfaygi tfgasyknfn lfvlgtgnng gtglknndyy wafgdkkyae vvrdrwtptt
      901 kemakfprls sqqnnndfrn sdfwtyktnr fnlqkvqlty nlsgnilrkt ffkdlgmyva
      961 ganlitfskn reilnlnist apqfrsytvg vrarf
//
LOCUS       WP_121363797             991 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            limicola].
ACCESSION   WP_121363797
VERSION     WP_121363797.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium limicola
  ORGANISM  Flavobacterium limicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Flavobacterium limicola"
                     /db_xref="taxon:180441"
     Protein         1..991
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108754
     Region          24..990
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktiykklli lllllpfsil aqntvsgivl dkvsgqpipg vnvnvqgaan gvstdfdgky
       61 qltkikkgdk ivfsyigykn tvvdyvtqns lnvsleedan qlqevvvqvg ygtvkkkdat
      121 gavtvlaakd fnkgqnvtae slitgrvagv sitgggspga kanirirggs slnasnepli
      181 vldglplsna vpngstsils tidpndietf tvlkdasaaa iygsraangv ivittkkgsk
      241 dglkvsfnsq tglstvantv dvlsadefra lvnangsaaq kaklgtantd wqdeifsnvf
      301 tsdnniavsg slfkklpari svgntntpgi lkntsfertt tslslnptfl dnhlkiding
      361 nlsfgknqfq degrvigsai gfdptqsvyq dgsryggyfe wleangdvnl laaknpvall
      421 nqnnrrstst rkwgnirvdy kfhfleelra vaelgidkfd sngfeetspn sitgfqlntf
      481 ssgqwtnvgd ykkytdtrqn knlnaylnyv kefgkfkvdl tggynyqmfe regyvsgdlr
      541 rpnpaqdvat dpdinlqsyf granlgydsr ylitlnyrrd gtsrfseenr wgnfagaafa
      601 wniaeesflk dnetvsglkl rvgygttgqq disasydylr rvtlgtvnsn yifgstayqv
      661 aktegynkdi kweetseini gldyglfndr ingsvnyfqk eandlladia ypdganlrns
      721 gfsnigsvtt kgiefninad vvknenlnwn lafntayihq eitdlgltvp gfqgyetgdn
      781 iaggsnnkvk insvgfnpga fyvfeqlydt nkrpiqgayv drnadgkidn sdryrfhkpn
      841 adytfglfst lnykkfdftm swraslgnfi fdninsdkgy lqaalrrdsd lanitpdyya
      901 tgftfedngt qrylsdyfvk dasfikldnv tvgysmdksl lkdvslrfsl gvqnalvfsk
      961 ydgldpenfs gvdgsvypra rtfvfgvnan f
//
LOCUS       WP_121364550            1022 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            limicola].
ACCESSION   WP_121364550
VERSION     WP_121364550.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium limicola
  ORGANISM  Flavobacterium limicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1022)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1022)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1022)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1022
                     /organism="Flavobacterium limicola"
                     /db_xref="taxon:180441"
     Protein         1..1022
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=112746
     Region          25..1021
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwifs llmalsmqfa faqertitgt vsdatgpvpg vnvtvkgtkv gvqtnfdgty
       61 sikaktgdvl vysfvgmtdt srsvgttnvv nvsmqdsakv laevvvqgyr tgtkksaiaa
      121 vatvaaatie nrpnanvvnt lqgqlagvni tsstgqpgak stviirgygt ingntdplyv
      181 idgfptnadn frsinpndie sltvlkdaaa tsqygnrgsn gvilittkrp algeakssfr
      241 yssnfgvisl qnpkydyana netlriernf gngrgagltd aqinanttdt dwvnvffkqa
      301 tsvthnlsfe tssenmssft sfgytnqdgv lettglqrfn lrnntggksa ngkftyqvat
      361 gfgysknnea tnlgdgainr nyvlgaflgl pyyspdeyqg sawtydlynn tpgleatpfm
      421 lidklktydq etsetrvdva tdfaykvskd ftlrtrvngl flenrffqae fpnsfnallf
      481 sstpgvssle ggnfngiedi nnrrefnfnn lyqvafnkei gkhtinasvn yeynfattnt
      541 dnqrqrgldp iffvpdtgag yvndnaandf ygptgnasrl rndllsyfal adydfnnkyg
      601 lsgtfrrdgs srfdkdyrwg nfwsiggrwn ideeafmdna tfinqlklra sigttgnqri
      661 vngtvfagvi ppaftnsysl tnntynggqg ygfnfgfpea qwevteqyni gldfdmfkrl
      721 rgtidfynkk tidlfidipt saafgattlr gnsdadvtnr glelnlaydl iqkedvlltl
      781 rfngsynknt vggiksnngq iittdtagyt fitqnggsif epyvykylgv npdngnllfe
      841 dasgnptetp tsfdrkatgk nfvpvyqggf gfdfqykgff aastftyvld ayrfdtdeen
      901 lfdignigqf rnsrqmlnaw tstntntdvp sldatnlpst gdsdrflrda sylrlrnaqv
      961 gyrvpakllr gtfinslaft lqgenlftvt kwkgfdaesn rtsdfyqypt pkiytfgvdi
     1021 kf
//
LOCUS       WP_121365895            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            limicola].
ACCESSION   WP_121365895
VERSION     WP_121365895.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium limicola
  ORGANISM  Flavobacterium limicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Flavobacterium limicola"
                     /db_xref="taxon:180441"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110973
     Region          46..1007
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkisfykgr lafwyliiig fslsytpaqa skilrqnqyq qqqnqisgti tdgtnplpgv
       61 tisikgkatt gtisdfngqy rltaspndtl vvaflgfkti tvsisgrkii niqlqeditt
      121 lqevrvnagy ysvkekertg sivsitaati ekqpvtnvla amqgrmagvs itqttgvpgg
      181 gfdiqirgqn slrpdgnrpl yiingvpyas dpigfnasat imptltspln nlnpgdiesi
      241 evlkdadata iygsrgangv vlittkkgka gktsytahys hgfgkvtrfm dlmntdqyvq
      301 mrkeayandg ytkypasaye vngtwdqtrn tnwqkeltgg sstitnlqts vsggdeqtqf
      361 iingnygket tvfpgdfgyk kgnvrinlnh latdkkfgit fssgytvqdn nqpstdltti
      421 srklapnapa lydtagqlnw enstwenpls nlngkslskt ydfvansils yalpyhlelk
      481 ssfgftdlkh tesstfpsti ydpaygldsa fssiftttts rqswivepql nwhtdigrgk
      541 iavlvgstfn qltgqqlvls gegftsnsli ydlasastvs imssgsteyk yqaffgranf
      601 swkdqyfvnv tgrrdgssrf gpgnkfatfg avgaawlfsk sfidngspsf lsfgklrasy
      661 gttgndqigd yqyldtysss gnpyqgvvgl eparlfnpdf gwesnkkfei atelglfndr
      721 ifltagwfrn tsssqlvgip lpgttgfnsi qanldasvqn dgieltlrtv nfqkknfgws
      781 tnfnisilnn kllrfpdles stysnkyvig splnivkvyh ftgldpatgl yqfedfngdg
      841 qlsakddkqy lidlnpefyg glqnqlhykg iqldflfqfv kqlnynsast lglpgsrnnq
      901 ttdvlarwqn pgdtgpfqqy stganaavan aytkyrdsda titdasyirl knvalsyqlp
      961 pswlkgveck lniqaqnvlt ltsyrgadpe fktrgvlppl kiittgiefi f
//
LOCUS       WP_121366106             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium limicola].
ACCESSION   WP_121366106
VERSION     WP_121366106.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium limicola
  ORGANISM  Flavobacterium limicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Flavobacterium limicola"
                     /db_xref="taxon:180441"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33993
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaaran mnpvlyqgmq pggqltttne venwpgnpeg
       61 itgpemmvgl qaqaqrfgtd vrdgwatkvd fsgdihkvwi ndtkelhcet viistgasak
      121 ylgmpseqhy lkmgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rsekfraski meervrkten itilmnhdtv evlgdeqvvt gvkalnkttn evfdipatgf
      241 fvaighkpnt difkeyitld etgyiintpg tsktnvdgvf vagdaadhvy rqaitaagtg
      301 cmaaldaery laake
//
LOCUS       WP_121370616             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Frondihabitans australicus].
ACCESSION   WP_121370616
VERSION     WP_121370616.1
KEYWORDS    RefSeq.
SOURCE      Frondihabitans australicus
  ORGANISM  Frondihabitans australicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frondihabitans.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Frondihabitans australicus"
                     /db_xref="taxon:386892"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34291
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqviiigsg pagytaaiya graglkplvv assveaggel mktteienfp gfpeglqgpd
       61 lmfkmqeqae rfgaevlldd vvsvdlegdv krvtlgsgdv eealtvifat gsayrklgie
      121 geerlsgrgv swcatcdgff fkekniavvg ggdsameeat fltrfatkvy vihrseslra
      181 skimqqrafd ndkieflynk tvtevvgdek atgvvltdtv dgststldld glfiaigndp
      241 rvhlvhgqld ltsagtiavd grssktnltg vfaagdvidd tyrqaitaag sgtvaaldae
      301 hylaglpkdl ldqatgaapa epvtasa
//
LOCUS       WP_121376213             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium endophyticum].
ACCESSION   WP_121376213
VERSION     WP_121376213.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium endophyticum
  ORGANISM  Flavobacterium endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Flavobacterium endophyticum"
                     /db_xref="taxon:1540163"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33571
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaarad mkpvmytgme pggqltttte vdnfpgypeg
       61 idgptmmvql qqqaerfgte vrigmatave fskekggwhk vtvdgnkeih aqtviistga
      121 takylglpse qklrgggvsa cavcdgffyk nqdvaivgag dtaaeeatyl anicksvtml
      181 vrkdamrask amqhrventp nlkvlfntev devigdqvve glrmvnnftg ekseiaitgl
      241 fiaighkpnt difkgqldmd dtgylitagk ttktnlpgvf aagdvqdkey rqaitaagtg
      301 cmaaldaery latle
//
LOCUS       WP_121366230            1031 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            limicola].
ACCESSION   WP_121366230
VERSION     WP_121366230.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium limicola
  ORGANISM  Flavobacterium limicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Flavobacterium limicola"
                     /db_xref="taxon:180441"
     Protein         1..1031
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111319
     Region          25..1030
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklkfngilv llvvliaqlt faqervvtgi vsdntglplp gvsvlvkgtk tgtqtdfdgk
       61 ysiksspnqv lvfsyigmkt qevlasqsti narllddsie legvvvgalg ikrsknalts
      121 stqvvatkel tqaanpnvvq slvgkvsglq inkssngvna tnrivlrgsr sitgnnealv
      181 vidnsistsa alqqlppeli envnvikgmq gaalygeqgv ngviivttvk gkekgkitvn
      241 vnsaidfetv sfmpktqqky gqgwdgvhyp eengswglpy dgvlrptglp qadgiefeqp
      301 ysfikdnvea fyqtgttyqn gfsinagsed syallsankv ktefvvngdv lernsflfka
      361 gkkigklsid gnvnysyqks setspdlldd liqtpgnvdl nlfknsgneg nytiyfknpy
      421 wtvdnnrnda trtfintiaa lkydinknin vtytgnlqft nraaqshine yretaalaga
      481 ganrnqtsey fasqsslrty ygdllvnfdy dltddlslka nvgsnmqdrn fritsqggqn
      541 ldipgwyhin nvlspanpst ldnrsqksnr asvlanvdlg yknylflnlt grndwtsvls
      601 kennnffyps agvsfiptla fdglksetls ylklsanivk vgnsssiqpy atseigvfpt
      661 gfpygqlgsy iinqrptdkn ikpefvttke vnlniglfnn ritidgsayi sdtkdlitaa
      721 tassasglat sqsnigdmtt kgleidlgli piktkdftwn lrasyatnks vinslaagan
      781 einllsdvat gtgifaqvge efplikgttf lrddngniiv nqfglptrss snsilgkatp
      841 dyilglsnsf tykgltltav mdyrtghqii sgtkydltwp grleesaafd revgfilpns
      901 vvetapgsgi ytpntsvysa aghgpngiid yygtlsrage hnvinatafk vrelalsysl
      961 ptstiekfgl tslrfginar npftvlaksn kgytdpeasd stanngngqg ysgtgqypnt
     1021 rtfggsmnlt f
//
LOCUS       WP_121375073            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Flavobacterium].
ACCESSION   WP_121375073
VERSION     WP_121375073.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium
  ORGANISM  Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Flavobacterium"
                     /db_xref="taxon:237"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115537
     Region          25..1044
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrskfkwifa lllafsmqfs faqektisgt itdsqglplp gvavvvkgtt rgtqtdfdgk
       61 ysiaasqgev lvftyvghkt stvtvgasss vnvalqeeat sletvvvdsy rttskkrsan
      121 avatitsetm egrpnvsflq tlqsqvagln iatssgspgs akidvilrgl ssvngntepl
      181 fiidgvaanq nvfrsfnsed ieridvlkda gatsiygnrg angvivvktk rgsynsklkv
      241 rytattgftn lqdhdykltn aqqlltleni vgagmgatlt peqvagwnsp ltpelsvglt
      301 enqikywgtn tdwqkvffrt gisknhnlsf tqgsenmtnf tslsyfdqdg ivpntgfkrf
      361 tfrtnftgks adgkftygtn ltaayskrvq leqetrtdin antlqnplqg llasqpylnp
      421 aqyvngqqlf defgapsfei npfmlmdyln penipssfee tkilanatat ynftdalsft
      481 ttmgidyvln qrlfarapqs ylaivatpag aqfggieqqq tdrdfsfnlv nklsynktfn
      541 dkhtvevsvf neyikahrra enwtqqgldp rtwslgagtg fvpfnpatpt lynriigglk
      601 rdaglfsyfa tasydydsky gveatvrrda sykfiqdntw gtfwsvsarw nidqeafmen
      661 sifdvlklra sygttgnqnv laaayganpl ylannnvrdl nssqagynna aslgvatian
      721 vdlqwettkq anvgidftmw krlsgsldvy rkktidlfdd nyvsavnqly tiaantqssi
      781 insgvelllr ydvfkegdfk ldlfvngsyn knewadlvyp npandfiqva dnfvqqngsq
      841 intyfvvpyv gvnpdngnll fldrnnnlte tptnedrrns gksmipkyqg gfgfntsykg
      901 ffvnanfsfv adiyrfdfdl lnlsnpasgi gtgpvvsell nawtptntgs nvpsltatni
      961 naaetfsdry lvdadyirmr nlsfgyefpa klldktlfsg vkfytqleny ltwskwrgfd
     1021 veglnssnqg gypspkvisf gvdlqf
//
LOCUS       WP_121376833            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Flavobacterium
            endophyticum].
ACCESSION   WP_121376833
VERSION     WP_121376833.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium endophyticum
  ORGANISM  Flavobacterium endophyticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Flavobacterium endophyticum"
                     /db_xref="taxon:1540163"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111863
     Region          25..1026
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktklngllt lvlalimqis faqertisgt vadesglplp gvsiaikgtt ngtqtdfdgk
       61 fqikasptdi lvfsfmgmat qevpatatnf niilkddatq letvvvtalg irrnpkelsy
      121 stqvvksdel nqakavnaat alvgkvsglq intinsgvnp qtrvvlrgar sisgnneali
      181 vidgvpsaln tlselnpndi esttilkgan aaalygsags ngaimittkk gkngkmtlqv
      241 nstitfekvq fipdrqtkfg qgwageldpv entnwgapld gslvqvgpel adgtirefty
      301 tarknnikdf fnvgttkqng fsisqgdens nlffsaqdvk tegiipgdvy hkntfrlnts
      361 ktsgnwnvag nvsyftdktd vagnltgsdd essffsepdg grsvysqllq tpiniplevy
      421 sqgdlqdyft nyaynpywil knsrqvsysd rfqgsidlgy kvndwfnvly rgglslltst
      481 fkntnnghif tdgsgredln qgvsdgsnye rrinsdlmfn fdfklnddis akitlgqnir
      541 diktkelgir gdnlvvegly nvsmrtgelr gaefnsrlrs iglygsaeig frdylflnvt
      601 grndwssali kennsffyps ygvsfiptsa fpelkgnvlt fakvtasytk vgnstsayan
      661 qntyirsvgf pygdltsfnl sntvalanlk pefttskefd lnleffkkri sldasyyisn
      721 stdqiinaaa ssssgatral lnagelqtkg feldlgftpi qtedwnwdlr vsysapktev
      781 ksllpgvnel slggfttagv yavvgeeypi ikgtayerdd qgrviidqat gnpiqssalk
      841 nlgkttpdyi vglstnlnyk gfrlsavfdy rtghvfynei gqmldftgss vqsaqsgrlp
      901 fvfpnssyqs apgvytpnts ittssggqpf wdsvysnise nyvvdatafk creiafsytf
      961 skkmldnspf egitiganar nvfmilpkan rytdpefgft tgnavgvgsv devpptrtyg
     1021 fnvtltf
//
LOCUS       WP_121380250             302 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121380250
VERSION     WP_121380250.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>302
                     /gene="trxB"
     Protein         1..>302
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..302
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgptlmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 ag
//
LOCUS       WP_121385834             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_121385834
VERSION     WP_121385834.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38581
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vsasqpdsay eaagatigsa
       61 aeafgtdlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_121380564             298 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121380564
VERSION     WP_121380564.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>298
                     /gene="trxB"
     Protein         1..>298
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..298
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv hlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaits
//
LOCUS       WP_121389143             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinokineospora cianjurensis].
ACCESSION   WP_121389143
VERSION     WP_121389143.1
KEYWORDS    RefSeq.
SOURCE      Actinokineospora cianjurensis
  ORGANISM  Actinokineospora cianjurensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Actinokineospora.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Actinokineospora cianjurensis"
                     /db_xref="taxon:585224"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35122
     Region          11..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpaeadqirn liivgsgpag ytaavyaara qleplvfegs qfggalmttt evenfpgfrd
       61 gimgpdlmeq mraqagrfga elraedvdtl eldgpvkyvv ahgtryaaka vvlamgaapr
      121 ylnvpgeqel lgrgvsacat cdgfffrdqd iavvgggdsa meealfltrf gktvtiihrr
      181 edfrasriml erakanekir wqlnsavtev lgdgkvqglr lrdtvtgees vldvsgffva
      241 ighdprsqlv agkvdiddeg yvltegrtty tnvdgvfaag dlvdhtyrqa itaagsgcaa
      301 aidaerwlae hgtaaaevap elvgggyapt n
//
LOCUS       WP_121393101             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinokineospora cianjurensis].
ACCESSION   WP_121393101
VERSION     WP_121393101.1
KEYWORDS    RefSeq.
SOURCE      Actinokineospora cianjurensis
  ORGANISM  Actinokineospora cianjurensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Actinokineospora.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Actinokineospora cianjurensis"
                     /db_xref="taxon:585224"
     Protein         1..362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36846
     Region          6..358
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(19,74,93,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtantvvgvp aetaggerrv alvpkvverl aarnisvvve pgagsaalip ddayvhsgaa
       61 lgdpwsadvv vkvavptdde iarlragavf igflapltqp ekaealraag vtafamesip
      121 risraqsmda lssqanvggy raallaaehl trffpmltta agtvppakll vlgvgvaglq
      181 alatarrlga httgydvrpe vadqvrsvga qwldlgieat gsggyaralt dderaeqqrq
      241 lakaitgfda vittaqvpgr taptlvtaea vqgmragsvv vdlagesggn celtspgavv
      301 vehavtiaap lnlpatmpeh aselyarnva alldllvakd galaldftde vvagacvtgq
      361 ev
//
LOCUS       WP_121395133             360 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Pseudomonas aeruginosa].
ACCESSION   WP_121395133
VERSION     WP_121395133.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         <1..360
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..353
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(3,61,80,279,305,307)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(32,112..113,122..123,126..127,130..131,133..134,
                     136..141,143,145..147,150,173..174,269..270,312..313,317,
                     320..321)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(107..108,112,115,118,159..162,182..184,219,230,
                     247..249,256,258)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(109..110,112,122,165..166,173,189..190,192..195)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(142..146,149,152,175,177)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 etrvsatpet vkkligqghq vivqsgagvn asqpdsayea agatigsaae afgadlvlkv
       61 vapsaaelaq mksgavlvgm lnpfdnenia rmaergitaf aleaaprtsr aqsldvlssq
      121 aniagykavm laanhyprfm pmlmtaagtv kaarvlilga gvaglqaiat akrlgaviea
      181 sdvrpavkeq ieslgakfvd vpyetdeere caegvggyar pmpaswmerq akavherakq
      241 sdivittali pgrkaptllh eatvaemkpg svvidlaaaq ggncpltead qvvvrhgvti
      301 vghsnlaalv padasalyar nildflkltl naegfsvnle ddivaaclmc rdgqavrkng
//
LOCUS       WP_121410379             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_121410379
VERSION     WP_121410379.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38608
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmkssavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_121410524             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Pseudomonas aeruginosa].
ACCESSION   WP_121410524
VERSION     WP_121410524.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         <1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..358
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(8,66,85,284,310,312)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(37,117..118,127..128,131..132,135..136,138..139,
                     141..146,148,150..152,155,178..179,274..275,317..318,322,
                     325..326)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(112..113,117,120,123,164..167,187..189,224,235,
                     252..254,261,263)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(114..115,117,127,170..171,178,194..195,197..200)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(147..151,154,157,180,182)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 ethagetrvs atpetvkkli gqghqvivqs gagvnasqpd sayeaagati gsaaeafgad
       61 lvlkvvapsa aelaqmksga vlvgmlnpfd neniarmaer gitafaleaa prtsraqsld
      121 vlssqaniag ykavmlaanh yprfmpmlmt aagtvkaarv lilgagvagl qaiatakrlg
      181 avieasdvrp avkeqieslg akfvdvpyet deerecaegv ggyarpmpas wmerqakavh
      241 erakqsdivi ttalipgrka ptllheatva emkpgsvvid laaaqggncp lteadqvvvr
      301 hgvtivghsn laalvpadas alyarnildf lkltlnaegf svnleddiva aclmcrdgqa
      361 vrkng
//
LOCUS       WP_121413141             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_121413141
VERSION     WP_121413141.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33611
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv hlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kslddh
//
LOCUS       WP_121417821             293 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121417821
VERSION     WP_121417821.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>293
                     /gene="trxB"
     Protein         1..>293
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..292
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv hlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvvsy thl
//
LOCUS       WP_121419152             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121419152
VERSION     WP_121419152.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>315
                     /gene="trxB"
     Protein         1..>315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali latgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkntidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kyldd
//
LOCUS       WP_121421490             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. 94].
ACCESSION   WP_121421490
VERSION     WP_121421490.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. 94
  ORGANISM  Acidovorax sp. 94
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Acidovorax sp. 94"
                     /db_xref="taxon:2135633"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55439
     Region          11..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqttpvpqpq rigvpretfp gekrvatvpd vvekliklgf avtvesgagd gakfsddayr
       61 aagaqivgda aalwaasdiv fkvrppssde valmregstl idfiwpaqnp elmqqlaakk
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rkmyaeqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg qavvrhgvti vgytdlasrl akqsstlyst nllrlteelc kakdgvavvn
      361 meddairglt vvkdgaitwp applkqapap apkaaaapva akksshgpga pmsaktltiv
      421 favlavlfwa igayapvafl ghftvfvlac figymvvwnv tpalhtplms vtnaissiia
      481 igalvqiapp dagingrpdg lilwlafaal vltavnmfgg favtrrmlam frk
//
LOCUS       WP_121429693             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Azoarcus sp. DN11].
ACCESSION   WP_121429693
VERSION     WP_121429693.1
KEYWORDS    RefSeq.
SOURCE      Azoarcus sp. DN11
  ORGANISM  Azoarcus sp. DN11
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Zoogloeaceae; Azoarcus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Azoarcus sp. DN11"
                     /db_xref="taxon:356837"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33580
     Region          2..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mttkharlli lgsgpagyta avyaaranln pvlitglaqg gqlmtttevd nwpadadgvm
       61 gpelmsrfqk haerfntemi fdhihtvkla ekpfrligda geytcdalii atgatakylg
      121 lpseekfsgr gvsacatcdg ffyknqdvav igggntavee alylaniakk vtvvhrrekf
      181 raekilidkm mekvaagkie lalnsaldev lgdntgvtgm rvkdintgat kdvalqgvfi
      241 aighkpntdi fegqlemegg yivtkggreg datstsvrgv faagdvqdhi yrqavtsagt
      301 gcmaaldaer yldalgs
//
LOCUS       WP_121431057             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121431057
VERSION     WP_121431057.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>312
                     /gene="trxB"
     Protein         1..>312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..312
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae ky
//
LOCUS       WP_121432836             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinomadura pelletieri].
ACCESSION   WP_121432836
VERSION     WP_121432836.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura pelletieri
  ORGANISM  Actinomadura pelletieri
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Actinomadura pelletieri"
                     /db_xref="taxon:111805"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33944
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa iyaargdlkp lvfegsvtag galmnttdve nfpgfpdgim
       61 gpdlmdnlrk qaerfgaelv tddvtevdlt vdpkvvkvgd ethlaktviv atgsgyrelg
      121 lpdekrlsgr gvswcatcdg fffreqdiav vgggdtamee aifltkfars vtvihrrdql
      181 raskimqdra fanekikflw dsevtaihgd drvtgvtvrn tksgeqsale itglfiaigh
      241 dprselfagq letdtdgyll vdapttktkl pgvfacgdvv dhtyrqaita agtgcaaaid
      301 aerwlqdrda aetvpqv
//
LOCUS       WP_121431242             296 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121431242
VERSION     WP_121431242.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>296
                     /gene="trxB"
     Protein         1..>296
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..296
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqai
//
LOCUS       WP_121439231             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Salisediminibacterium
            halotolerans].
ACCESSION   WP_121439231
VERSION     WP_121439231.1
KEYWORDS    RefSeq.
SOURCE      Salisediminibacterium halotolerans
  ORGANISM  Salisediminibacterium halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Salisediminibacterium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Salisediminibacterium halotolerans"
                     /db_xref="taxon:517425"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34739
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseetiydvv iigagpagmt aavytsranm stvmlergmp ggqmantedv enypgydsil
       61 gpdlsqkmfd harkfgaeyk ygdvkeiidg keyktivtgs gelkarsvii ttgakykelg
      121 vpgekelggk gvsycaicdg affkdkelvv igggdsavee agyltkfask vtiihrrdel
      181 raqrilqdra fdndkiefmw shvvteinek dgkvgsvtve strdgsrsef atdgafiyig
      241 mlpisepfln lgitnedgyi etdeemktsi pgifaagdir ekhlrqivta tgdgsvaaqn
      301 ayhyveelke emkeaakqt
//
LOCUS       WP_121441554             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Alkalispirillum mobile].
ACCESSION   WP_121441554
VERSION     WP_121441554.1
KEYWORDS    RefSeq.
SOURCE      Alkalispirillum mobile
  ORGANISM  Alkalispirillum mobile
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Alkalispirillum.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Alkalispirillum mobile"
                     /db_xref="taxon:85925"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34139
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseprhvpll ilgsgpagyt aavyaaranl npvlvtgmem ggqlttttdv dnwpgdaegv
       61 qgpelmermk ahaerfntev vfdhihtahl tdkplrlegd agqytcdali iatgasaqyl
      121 glaseqafmg kgvsacatcd gffykqkpva vvgggntave ealylsnias hvtlihrrdk
      181 lraekilqdk lfekvaagai tvrwdttlde vlgddsgvtg lrlrstrdds tdelavdgvf
      241 iaighkpntd lfegqlemen gyiqvrsgln gnatassvpg vfaagdvsdh vyrqavtsag
      301 tgcmaaldae ryldnldhdt r
//
LOCUS       WP_121441912             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Alkalispirillum mobile].
ACCESSION   WP_121441912
VERSION     WP_121441912.1
KEYWORDS    RefSeq.
SOURCE      Alkalispirillum mobile
  ORGANISM  Alkalispirillum mobile
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Alkalispirillum.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Alkalispirillum mobile"
                     /db_xref="taxon:85925"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34153
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msetkhckll ilgsgpagyt aavyaaranl epvlvtglem ggqlttttdv dnwpgddqgv
       61 qgpelmermk rhaerfetei vfdhihtahl kekpirlegd agsytcdali iatgatakyl
      121 gldseqafmg kgvsacatcd gffyknkpva vigggntave ealylsnias hvtlvhrrds
      181 lraekilqrq lmermeagkv diiwdhnlde vlgddagvtg lrlkhtksda trqvdvhgvf
      241 iaighapntg lfqdqlemng gyivvksgln gnatatsipg vfasgdvmdh iyrqavtsag
      301 tgcmaaldae kyldalhle
//
LOCUS       WP_121442854             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Alkalispirillum mobile].
ACCESSION   WP_121442854
VERSION     WP_121442854.1
KEYWORDS    RefSeq.
SOURCE      Alkalispirillum mobile
  ORGANISM  Alkalispirillum mobile
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Ectothiorhodospiraceae; Alkalispirillum.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Alkalispirillum mobile"
                     /db_xref="taxon:85925"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39937
     Region          3..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavkvavpke trpgerrval apaalrqfek lgvelllqkg aglesgfdda dyknvkivds
       61 eeellgqadv vmkvqpptek evgmmregav llgylapheg dsrikalckr nvtslsmelv
      121 prisraqaid alssqgaisg ykavliaaer sprffpmltt aagtirpskv lvigagvagl
      181 qaiatarrlg aqveaydvrs ataeqveslg akfvdtgvka egeggyarel taeekkkqae
      241 vlndhiaash vvittaaipg rpapkiidka tvermgrgsv ivdlaaetgg ncelteagkd
      301 vdhngvvvvg ptnvpasvav hasemysrnl ynlltlliqe gelhlnwdde viadsclthg
      361 gevkhdptra rlegdks
//
LOCUS       WP_121444127             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Brockia lithotrophica].
ACCESSION   WP_121444127
VERSION     WP_121444127.1
KEYWORDS    RefSeq.
SOURCE      Brockia lithotrophica
  ORGANISM  Brockia lithotrophica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillales
            Family X. Incertae Sedis; Brockia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Brockia lithotrophica"
                     /db_xref="taxon:933949"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35349
     Region          20..322
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvggfgftig glggpetkey dvvivgagpa gmtaalyasr aqlstllvek nvhggqmtnt
       61 eeienypgyp sikgselaai mfehalkfga ehthgevtgl ekegdrwavf taegsrylay
      121 avilatgadn krlgvpgedr lagrgvswca vcdgaffkdk dvivvgggds aveeatyltr
      181 farkvtvvhr rdkfraiktl qdrffrnert dviwntvvte ilgdkrveav rlknvvtgee
      241 wvrptdgvfi yigvepnsaa frslgitdeq gyvltdesmr tavpgifaag dvrkkelkqv
      301 atavgdgsva amsalayvea ikegrpvhp
//
LOCUS       WP_121451596             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Desulfofundulus salinus].
ACCESSION   WP_121451596
VERSION     WP_121451596.1
KEYWORDS    RefSeq.
SOURCE      Desulfofundulus salinus
  ORGANISM  Desulfofundulus salinus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Peptococcaceae; Desulfofundulus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Desulfofundulus salinus"
                     /db_xref="taxon:2419843"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33064
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydvaiiggg pagltagiya araklksvli ergmtgglaa ttefienypg fsegiggpel
       61 msrmeaqarr fgleilnsnv edlkkdnlnf ivktedaeik trtvivatga qpqrlnvrge
      121 etfhgrgvsy catcdgaffk dkrvavvggg daaveeamfl tkfatrvfii hrrgelratk
      181 ivqerarqnp riefiwhsvv deimgketvt gvrikdvrtg qtselpvdgv fiyigyspns
      241 sivkelvkld ewgyiltdan mqtscpglfa agdvrqkslr qvvtavadga iaavsaekyl
      301 ehnr
//
LOCUS       WP_121453545             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. 106].
ACCESSION   WP_121453545
VERSION     WP_121453545.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. 106
  ORGANISM  Acidovorax sp. 106
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Acidovorax sp. 106"
                     /db_xref="taxon:2135637"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38281
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mfigvpaetv agetrvaatp etvkkltalg hslrvqsgag laasvtdaay eaagaeitda
       61 agawgaplvl kvrcpseaea pwlrsgttlv gmlnpfdaag lqrlaaagvt ayaleaaprt
      121 traqsmdvls sqaniagyka vmiaadryqr ffpmlmtaag tvkaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvggy arpmppswle
      241 rqkievakrv aqadvvitta lipgrpapvl vtpemvqamk agsvivdlaa pqggncplte
      301 pgstvvkhgv tlvgetnlpa lvaadassly arnvldflkl iinkegalhv dmqddivaac
      361 lmahegtlkr a
//
LOCUS       WP_121458886             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Azonexus fungiphilus].
ACCESSION   WP_121458886
VERSION     WP_121458886.1
KEYWORDS    RefSeq.
SOURCE      Azonexus fungiphilus
  ORGANISM  Azonexus fungiphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Rhodocyclales; Azonexaceae; Azonexus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Azonexus fungiphilus"
                     /db_xref="taxon:146940"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34260
     Region          10..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mskttrhtpl iilgsgpagy taavyaaran lkpvlitgma qggqlmttte vdnwpadadg
       61 vqgpelmqrf ekhatrfdte iifdhihttk ltekpftlig dagtytcdal iiatgasamy
      121 lgleseqafq gkgvsacatc dgffyrnkpv avvgggntav eealylania shvtvihrre
      181 kfkaekimqd klfqkekegk vtilwnstld evlgddsgvt glrvkstkdg stqnidvhgv
      241 fiaighkpnt difagqlemd hgylvtqagr ngnatqtsip gvfaagdvqd qiykqactsa
      301 asgcmaalda eryldnlghq a
//
LOCUS       WP_121459967            1003 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium defluvii].
ACCESSION   WP_121459967
VERSION     WP_121459967.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium defluvii
  ORGANISM  Chryseobacterium defluvii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Chryseobacterium defluvii"
                     /db_xref="taxon:160396"
     Protein         1..1003
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109378
     Region          32..1002
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltagvlt lvlssslava naqetkndtv ktqdiegvvv talgikrekk algyssqevk
       61 gediskaptt nflnnlsgkv agldikqgtn fggstnvvlr gyksilgdnq alfvvdgvpi
      121 insninstdq ktarggydyg ntasdinpnd ietlnvlkga aatalygsra qngaiiittk
      181 kgskrnkgvg veysssftvs fvdkttfpey qteygqgylg qgfgsyqgfp rvsfghdasy
      241 gpkydgslvw qydafipgsp tfgqrtawev akngpieffn vgtntvnnis lnggndvaty
      301 rfsygntyat dimpnsklnk nnfagnasyk ftdkltanly anfitqrtqg rsttgysdni
      361 msnfrqwwat nvdlkeqeal ynmshqnytw niksvsdirp qywdnpyfkv yenyqtdsrd
      421 rlavnaslny dltpdislmg rvgrdgytmk veerravgsv aapfglndvd qpsgyavsny
      481 nvsetnydfl atykktlndf ninallgtnl nvqsneinqq stsggllipg lytisnsvst
      541 palpflsete krifgvfaqa slgykntyyl egtirrdqss alpddnnvyw ypsvsgslvf
      601 snlikqpwls fgkvraayaq vgsdtnanll snvylaqnpf lssmyaynti aknkdlkpqr
      661 ldnielganm effknrlgfd vawfknkafd qilalpvstg tgsgsqykna gtletkgfei
      721 sghvvpvkts dftwnidvnw snpntkvvel apgieniqlg slqggvsina plnqdygtiw
      781 gadfvyangq kvvgengayl stdssdknlg sfqakwmggl rnsltyknls fsflidvkqg
      841 gkvfsldqyy gygtglypds vglndlgnpi rntlangggv ilpgvmvdpn npnnyivntt
      901 rldksqssqv lgtdpppaaf vydasfvklr evaisyklps svlastflrd ltvglvgtnl
      961 wiihknlpya dpeaglssgn iqgyqsgpmp atrniaftlk anf
//
LOCUS       WP_121460588             964 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium defluvii].
ACCESSION   WP_121460588
VERSION     WP_121460588.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium defluvii
  ORGANISM  Chryseobacterium defluvii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 964)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 964)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 964)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..964
                     /organism="Chryseobacterium defluvii"
                     /db_xref="taxon:160396"
     Protein         1..964
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106012
     Region          30..963
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnrfyfnksn kaalffamtl lpsgiaysqv kkdtvikenk idevvvigyg tqrkeavtgs
       61 vatvkgdvlr evpsanitqs lqgrtagvdi sqtstkpgat mqirirgtrs ltgdnnplvv
      121 ldgipfvgsl gdisssdiks idilkdasat aiygsrgang vilvttnrga kgqkprftyn
      181 tftgvqtlfs kypmmdgpkf aqlrayaipa gnttplysng adennsvntd wqslyykpam
      241 mtshdigvsg gteggnynvg lsyfkqnali piqsyerfal rmaidqqvgs ifkfgfttnt
      301 nysisegngv npgavlgysp ianpynadgt pkrvmstagg idqtwiytrk sleslgdkyv
      361 detkafasyn nlygeaslpi kglkyrlnvg ldfrtsnsgn ytgvgvfntn plgpsaagrg
      421 nnqtyhwvle nlltydrtfg khkinavaly saeenkytss ymsaknvpad ffqyynlgqs
      481 pqaditvrpe dqiywktgll samgrvmyty nnkymltatl radgssrlap gnkwhtypal
      541 slgwnvtnes fmenikvinl lkfragwgqt snqavdpyst mgrynvapyn fgsagstgiy
      601 gsqppnpnlg weysktqnyg vdfgilnnrl tgsveyykth tfdlltqksl patsgwssiv
      661 snvaetenkg levslngiif dnpdgftwea ginfytnknk ilslasgter dvnnlwfvgh
      721 ninslydyqy iglwqagdpy qsilepgtpa dvigsikvly tggynpdgtp vraigpddrq
      781 ifdtapkyqg gfnmrfaykn felstvgafq hggilvstiy gsasylnrlt grgnnvdvdy
      841 wtenntdayf prpgrhlsgd npkysstlam fdasylklrt itlgynvdke flkdlkvnsl
      901 riyftvtnpi vlfspyhkfs gmdpepnsfg nenqavsgyq srqlvigtnn pstrnylmgl
      961 nltf
//
LOCUS       WP_121460642            1189 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium defluvii].
ACCESSION   WP_121460642
VERSION     WP_121460642.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium defluvii
  ORGANISM  Chryseobacterium defluvii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1189)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1189)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1189)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1189
                     /organism="Chryseobacterium defluvii"
                     /db_xref="taxon:160396"
     Protein         1..1189
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134271
     Region          148..1185
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnntinnngs fisfqqkknd kipmitkwrv mllralflcl liflyslsmg qkislelssa
       61 sfkstiqqiq kqsgysfsin drhmriskpv nisaknqdil evlpvifnqq pfgysvdgki
      121 visidrknnl gkekekvnps gfrqpafrgk vvnergeplp gatirikktg eqfstdsegn
      181 feipiqfrne elqisyigys slekigedat htvlvplqnt lgiaevvstg yqtipkerat
      241 gsfaivdnkl fnmrvspnli drlegnvpgl ifhkntssst engvdinirg hstlfasdqp
      301 liildnfpyd gdlrrinpnd ienitvlkda aatsiwgaks gngvivittk kgkrnqkpni
      361 elnsnvtiga kpdvyynknf inaddfinie qelfdrgfyn ndlaslsmpv ispvvdildk
      421 kkrniissse aekaiselrn vdvrkeieky fyqksvnqqy svnikgggdn idyfvslgad
      481 hnrsnlvgnt dsrytvnvkt ninltkrlla sinymfvqsg skqnytlgnl spysksvypy
      541 mklsdenggh latikefntn yidtagggkf ydwqyrplde lgyandksrs tdnlvnlslk
      601 ydfskslsae ikyqfgksts qskgysseqt ystrtlinkf tyfdesgnpv ypvpkggmld
      661 qtystlttkn lraqinynks wnvheltaia gaeindvvke sdfntyygyd lntgsfttpd
      721 fvtnfetnps ssslipyypk itkftdhfis yfsnaaytyd gkytfsvsgr idksnlfgvn
      781 tnqkgvplys iggswnlske sfyhldwipy lrlrttygys gnvdknvtav ttirqlnnyy
      841 ysrtpyaqvv npgnpdlrwe kiktvnfgvd yasknnrisg sieyfiktgl dlfgdmplag
      901 stgwpnfrgn yartkgrgwd vvlntknivt tnfewntqlq lskaqdfvtk ydvkeadlny
      961 ltygsgnfga implegkplf aiyafksgpl thdtgdpqgf ldgklttdys sifnktplds
     1021 mvyagpsrpt vfgslrntlt fkrfslsfni lykfnyyfrr nsifysslfn swnghedfsd
     1081 rwqkpgdenv tnipsiqypp mntfregfya nseslvtkgd hirlqdimls ydidksaesr
     1141 lpfahlqlyc yinnigiiwr snkqgldpdl fgnglpqprs ialglranf
//
LOCUS       WP_121460722             945 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium defluvii].
ACCESSION   WP_121460722
VERSION     WP_121460722.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium defluvii
  ORGANISM  Chryseobacterium defluvii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Chryseobacterium defluvii"
                     /db_xref="taxon:160396"
     Protein         1..945
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103927
     Region          25..944
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqsdlkysc liavlyfgmn vnaqvtpqdt itqetkinev vligygarkk idnttsissl
       61 naeevtktkv lnatqaiqgk aagvtvvasd lpgstpsvii rglgtalsgr nplyvvdgmf
      121 vdninninsn dilsydilkd asalaiygnr aangviivtt ksgrgkkitv eydgftgarm
      181 plkkvkmags nlfsyytnta lgttkfsqdq pvntdwfdai trtgtynqhn lslsgasdna
      241 kyflslsnyd eksilngsdf nratvrtnne fkitkgiivs qtfsvafnnt tpkplsafta
      301 aykqspiipv yfpnglygvs fvgadgfasp tgssfnnvgn pvaqlnfnne rqksvlmqgg
      361 ikldmdiikg lkftsqfnge yynfksynfv dskaiwlaad ptrvlnntpy pasdptnllt
      421 nekkdyfnwi lsnyitynkk fgqihdleat igmevsersg enviisqrkn miansdywdi
      481 ygtgsdplny ldqlvkynsi nynnnrtnsy faraqyklmn rylvsatirr dgssqfsegn
      541 kwgnfpafgv gwviseedfl kdnsvinslk lrggwgklgn qnvplnilpf atggdynynf
      601 gsgsiangtt idkindpnls weiteesnig ldyemlnnrl kgsidvynrv tknvildqvp
      661 lmtsgislag lshlgevtnk gievnlgwdd kinenwsysi ngnysfnknn lnklananvn
      721 dirggglgng qytkllseia vgqplgsfwl wevagkdang nftyvdtdgd gktgandldd
      781 rkfmgsyipk stfginiglk yknvdfsang ygtlgakvyn gkkaqrfsge nveyniannf
      841 wtpgntgsen papfnavpla sdyylesgdf frinnitlgy tltkpieyls slrlyisain
      901 pvvfqkfsgy spelnadgnp ynltgvelda yptlrsfvfg vnikf
//
LOCUS       WP_121461228             990 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium defluvii].
ACCESSION   WP_121461228
VERSION     WP_121461228.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium defluvii
  ORGANISM  Chryseobacterium defluvii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 990)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 990)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 990)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..990
                     /organism="Chryseobacterium defluvii"
                     /db_xref="taxon:160396"
     Protein         1..990
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110871
     Region          29..989
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkenqkllv lsllglvsvn maaqqkakkd tindinevvv talgikrqdk slgystetik
       61 seeilktqnn nwaqalegkv aglkiqtaga gplgssvikl rgdismnmdq nnalivvdgv
      121 plnntttgtg fsaygagska dlpidygngi nsinpddies isvlkgstaa alygsrgagg
      181 aimittksgk skkgklqvtl nsyssydtvl rwpdyqyeyg qgtmqkdtkg nyyysygasa
      241 dgvntgstss afgpkfagqy yfqydptveg qsatrqlwrp ykdnikgfwq tgttfsnnva
      301 letsnentsf rtsltylkne wmmpntgfdr fnaslsfdhk ineklkvglk fnynktksdn
      361 lpatgysnqs isyfmifqnp nidlswyepi wkkdkyqidq ihpfssfidn pymiayemln
      421 gvdknfitgn inlnyklakn fevmlrsgme ltneertqkr pwssanylqg myreqhiklm
      481 dlnndllfty kntfndfdfs asvggsirys eytmydymad gllkpgiytl pngignitkf
      541 atpsdkqvns tyglvtlayq nkifldltar ndwsstlpkd nrsyfypsag msfilsdifk
      601 mtssqfnywk lraswskvgn dtnpykliky ynnsvfsgsv eapslypnpn lrpemltnie
      661 agmdfsflkn risynftvyq nnskdqivdi palletgysk rtinageirn rgvemtlntf
      721 pvknknfsws vnanwsmnrn kilslpeefh gepytmgsvg gvvyynavvg gslgdmygyg
      781 lmyspdgqvv fgsdgltakp tqmkkignay pkwragiqne fryknftvsf sfdgqykgma
      841 ysqshhkmte qgklghtlig rdnpngliig qgvvqnadgs yspntkgvav sayyadyyrr
      901 anvetnsfdt sfvklrdari sysfpksvte qlkltdltla lfgrnlwmwt kfplfdpeaa
      961 tlndnlitpg vemgqlptar tigiqlnvkf
//
LOCUS       WP_121461687             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium defluvii].
ACCESSION   WP_121461687
VERSION     WP_121461687.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium defluvii
  ORGANISM  Chryseobacterium defluvii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium defluvii"
                     /db_xref="taxon:160396"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33651
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypagit
       61 gpemmmdlqk qaerfdtkvh yemitkvels kevggvhkly agnkeifakt viistgatak
      121 ylglddekky agggvsacat cdgffykgkd vvvvgagdta aeeatylakl ckkvtmlvrk
      181 dvfraskami hrventpnie vkfhheligi egenslvera vvinnqtqet skidvdgifi
      241 aighkpntdi fvgqidlden gyiltekgst rtnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 aamdaekyla elh
//
LOCUS       WP_121462097             983 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium defluvii].
ACCESSION   WP_121462097
VERSION     WP_121462097.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium defluvii
  ORGANISM  Chryseobacterium defluvii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Chryseobacterium defluvii"
                     /db_xref="taxon:160396"
     Protein         1..983
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107995
     Region          35..982
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mklrlslitt avlffaggqv veaqrtnkdt tttekqidev vivaygsqkk etlvgsntei
       61 kakqfadrpi snigqaidga spgvkvstgt gqpgsapsiq irgigsygis tsplyvvdgv
      121 iytgslsain tndiasfnil kdaastslyg saaangvvli ttksgrkgtd vlnfnmstgy
      181 vgrsipeydr vdvyqyypli weamrngrlt svpgttvaaa nayattnlis gvlktnvfnv
      241 adnqlvvdgi lnpnaqlkyt dldwqgplmk tgfrqsyeln ysggtnktty fssvgytnet
      301 gylaksdfer fnarlkvdsq ikswlklgts isgvssngnn sidgadnnss yinpyswtrt
      361 mgpiyspyah dpntfatlyd aagnivydag sargadaaag rnviqetlln kdisknyyii
      421 srayaefkvd pyltlstnvg ydirnnrrsr yvnkligdaa pagaaekttf teqtltwnql
      481 lnykrkfgvh nfefllghen ykymyeyfna ykqgqtvddn delinfvtpt tvtsqtdnyr
      541 kesvfsrlny dykskyllsg sirwdassrf aedvrwnsfw svgagwrika edflsassti
      601 selklrgsyg evgndgtnsy ymykstyslg ynnaqepgil fgfladpsit wesnkqtdlg
      661 ldfgflnnri tgsvdyynrv tddlifpvpl pvsggvpgns isknvgtmyn rgfefaisad
      721 vvrndnftwn inanastlkn evtelsagit eiingtkkvs vghsvydywl rqwygvdpad
      781 gsplflvada yagttasdir tvngtqvttn fnkakydysg taipdlfgsf gtsitykqws
      841 lstmftyqlg gmtydsnyqs lmssysqgga lskdildrwt tpgqitdvpa lnsstytnsn
      901 aassrwlvks dfitfrqatl gysfspesis qygltslrll lsgeniwskt arkglepaqs
      961 fngtttnryt parivtigfn lsf
//
LOCUS       WP_121462262             946 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium defluvii].
ACCESSION   WP_121462262
VERSION     WP_121462262.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium defluvii
  ORGANISM  Chryseobacterium defluvii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 946)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 946)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 946)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="Chryseobacterium defluvii"
                     /db_xref="taxon:160396"
     Protein         1..946
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105622
     Region          32..945
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlsa gvlffmggqt llaqtkqdti pkqetkidev vvvgyravsk ktavvstaqi
       61 keetingrpn snlmnvvqgq lagvnistgt gqpgakptvi irgvgtfsgn tdplyvidgf
      121 ptnsdsfrsl npndvesmev lkdasataqy gnrgsngviv iktkqgrygd rtafnyrsqi
      181 gvsmlqdary nlanarqllt lenrygagvg admtqeeinn yqtntnwldv ffrpsflqsh
      241 dfsvttgakn insytnvgyl qqdgilensg mkrftvrnti ngktndnkfk ytfgtaigft
      301 rndqigslgt ggvnqnmvlg ayqgaphlsp slyqnsqqlf nlyetegtll ytplflidkm
      361 ktfytgldem rldvtselsy qilpsltarm ranaqlitqn gltwqhpisf nsflfqngte
      421 avgtetiaes rqfyfnnlwq leysksfgdh tinaagafef nnamlksstf tqrglnpltw
      481 vpgagtgyvt dtsnddfnvp tvgagqsrln mfsffgnldy dynkkygiva nirrdassrf
      541 sedqrwgtfw svggrwnvde esfmdnvkwv nsfkirgsyg vtgnqrivdg tvwaglnppp
      601 yldtfsivnn vynglmgmgi tlgyadlrwe ttkqwnigtd felfnrklrg qfdvydrkti
      661 dlfddwaqsp tsgvlsirqn tpqdlrnsgy elslaydlik ngnltftlrg ngsinkqrvy
      721 dlpdgilreg tqpmvysqng slyqapyvyh ylgvnpsngn llfedingnp tetpttadlr
      781 plkyntvpky qggfgfdldy kglylsttft yvaglyrydy dmsgfydptq lgqfnvssdl
      841 lnawtptntn tnipsltasn ydaqalsdrf lvdasyvrlr niqlgynipk sllngtfvre
      901 lritlqgenl atwtkwqgyd aesnrgadqs qypspktftl gfdvkf
//
LOCUS       WP_121462372             977 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium defluvii].
ACCESSION   WP_121462372
VERSION     WP_121462372.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium defluvii
  ORGANISM  Chryseobacterium defluvii
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Chryseobacterium defluvii"
                     /db_xref="taxon:160396"
     Protein         1..977
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106550
     Region          9..976
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkivvpvvl afsvsgyaqe skasdtaktt diqevvvtsl gikrqarslt yssqqiggde
       61 ltevktpnll nsingkvsnv qinktnggvg gsvrvvmrgd kstrnsqply vidgipiinn
      121 tgvtgtggpn vdyfnsmpdt gdvlstinpe diesinflkg asaaalygaq gsngailitt
      181 kkgsagrssl sysssltfdr vynlpelqhs ylqttpydpa ngntgsydsw gakgsskdyt
      241 kdffqtgvtw insvsfqagn ekstsffslg nttnkgiipt snldqyniny rttskflndk
      301 lvldanvmas lqtsknrlsp gsyfspitnl ywlprgvdfd hfaqnysyfd qtryldaqnw
      361 wavkpngefa dnetqnpfwi lnknpvitkn knvygsaals ytinswltak vrgnynyfns
      421 dsqrnvaays qptvlgskds ngkiykntle kttiygdall ignpkinddi sldftlgasi
      481 sdlkynitti ennklfvanl falnnldwgn eqgqgvygng rsyiithpqr qdqsvfasas
      541 lgykskvyld ltfrndwsst lagtgnngid yesigangil teifnlpeai sfwklrasya
      601 tvgnaldpts tipqpefnag vitgsyssap vsnamfsdlf pkpefnrtfe agtelrmfnn
      661 klsfdftfyk svvsnqylkg vdaatnfgvq sgkvdinagk ienigfessl sykvfnrekf
      721 rwtttlnasa nkntikellp lkyypdpekl fvlngggfnm lkvggsfgdl ygtafkrdtq
      781 grivvdangv pikdsnekqy lgnpnpkfml glnnnfsigr fdvsflidgr fggqvlgftq
      841 svndglgvsq asadsrdagg vsipnavyen gtpytgltda edyykvvggr ggineayiyk
      901 atavrlrqas isytlktnsk ifrdatlsvi gtnlfflykd apfdpeqvsg vnpggvgvdm
      961 fgmpitrslg fslkanf
//
LOCUS       WP_121463238             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arsenophonus endosymbiont of
            Aleurodicus dispersus].
ACCESSION   WP_121463238
VERSION     WP_121463238.1
KEYWORDS    RefSeq.
SOURCE      Arsenophonus endosymbiont of Aleurodicus dispersus
  ORGANISM  Arsenophonus endosymbiont of Aleurodicus dispersus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Arsenophonus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Arsenophonus endosymbiont of Aleurodicus
                     dispersus"
                     /db_xref="taxon:235559"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34924
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mnktnhsrii ilgsgpagyt aaiyaaranl npvlitgfqp ggqlttttev enwpgdhtdl
       61 mgpilmerml qhtkkfteek niindhihkv dlqqrpfqls gdkeiyscda liiatgastr
      121 ylglpseeaf kgngvstcat cdgffhrkqk vavvgggnta ieealylsni asevyvihrr
      181 gefraekili qrmmekvktg nivlytnyti dkvlgndsgv tginlrstqn nnietlfvtg
      241 vfiaighmpn tsifidqlvl knsyiqvksg tkgnatqtsv egvfaagdvm dhiyrqaita
      301 agtgcmaald aerylealyg k
//
LOCUS       WP_121482174             335 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Brevundimonas naejangsanensis].
ACCESSION   WP_121482174
VERSION     WP_121482174.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas naejangsanensis
  ORGANISM  Brevundimonas naejangsanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Brevundimonas naejangsanensis"
                     /db_xref="taxon:588932"
     gene            1..335
                     /gene="trxB"
     Protein         1..335
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35586
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttprtvrva iigsgpagwt aaiyaarasl npvmiaglqp ggqltittdv enypgfaeti
       61 qgpwlmeqmq aqamhvgtev lhdivvkadl sqrpfrltld sgtellaetv iistgaqakw
      121 lgleseqkyq gfgvsacatc dgffyrgkqv vvvgggntav eealfltnfa etvtvvhrrd
      181 efraekilqd rlfahpkikv vwdsavdeil gvseagashv tgvrlknvkt gdlteipadg
      241 vfiaighaps selfkgqlev nsggylrvkp gtastaiegv faagdvtddv yrqavtaagm
      301 gcmaaleaar flaeedhkaa hhpishkeae kigaw
//
LOCUS       WP_121482434             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brevundimonas naejangsanensis].
ACCESSION   WP_121482434
VERSION     WP_121482434.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas naejangsanensis
  ORGANISM  Brevundimonas naejangsanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Brevundimonas naejangsanensis"
                     /db_xref="taxon:588932"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38309
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavaiavtre rrdgetrcaa tpetvkklia lgatvtveag tglgssipda dyaeagagvr
       61 pdlaavlaga dvllkvrgpt aseisalkpg avvvglldaw rdkatvealr ganatafame
      121 fvpritraqv mdvlssqanl agyravieaa yaygkgfpmm mtaagtvaaa ktfvmgagva
      181 glqaiatarr lgavvtatdv rpaakeqves lgakfvaved eefkaaetag gyakamsaey
      241 qakqaeltaa hivkqdvvit talipgrpap rlvtaahvas mkpgsvivdl aveaggnveg
      301 skpnevvtts ngvkivgwsn lpgriaadas alyarnlvaf lglmvkdgal svdleeeilk
      361 aavvthggav vhegvrg
//
LOCUS       WP_121486375             954 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 7].
ACCESSION   WP_121486375
VERSION     WP_121486375.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     Protein         1..954
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=105045
     Region          33..952
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklrvlsa galfflgqva faqtakkdtt sktkqidevv vlgysktatk akstaastti
       61 sekvledrpn asflnslqga apgitinsss gspgsgridv rvrgigslns tmdplyvidg
      121 mstngtqfrn lnpddiatis vlrdaaatsi ygnraangvv iittkngtyn sgmklsygst
      181 igfsaypnhk ynlvngsqyr slqnefvfgp deqyspeevq napntdwkkq yfqtgmtqqh
      241 nlgltfggkn vsvysslgyf dmtgivkstd fkrfsfrnni ngksndgrft ygsqlavgys
      301 krhqldqetn vaglvanplq nplfssilar pdlepnpytr gsdmykaiga aysdripwvt
      361 qdiinggiqn vytetsvlan vnfaykltdy ltvghksgid fkesdrafar apygylalva
      421 kagndpyggl evlnnvkdfn insitnltfn kswgdhtlev gayldyikah yrtkqyqqng
      481 lnpltwvlga gtgyvpystt tptlyvpnvt aqnvnagala yfatadydya gkygftgmvr
      541 rdgayrfske nrwntfwavs grwnidkeaf mdgsvfdmlk lrssygtqgn qnlgitvnnl
      601 nplvnpnttt lfrnvyqtst aylnqqglsm tvlgnpdvrw etqkmfnvgl dfiafdrkle
      661 gnfdyyiktt nnlfnklnis aasngvftid gnngsmrnng vegslrynif nkgdfrlsvf
      721 angsfnknki ielpygyspt dnvnaagsla fqwnlvryag vnketgemqf ldkngniten
      781 pndsdrvltg ksfypkyqgg fglngsfkgv fadvlfswqa ggwqfdnlyt wlvdpnsigt
      841 gnnvsadlfd swtpdnknas lpsitasntg adgssdryly ktdfirlkti sigysfpkaa
      901 leklpikglk lfvqgenlvt wsswkgldpe pvtdyslsvy pnpktfsigf nvef
//
LOCUS       WP_121486478             985 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 7].
ACCESSION   WP_121486478
VERSION     WP_121486478.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     Protein         1..985
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106752
     Region          29..984
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrkavipvlf vfsisanaqe kksadttktn sieevvvtsl gikrqarslt yssqqiggde
       61 ltevktpnll nsingkvsnv qinrtngvgs svrvimrgnk svsnsqplyv vdgipiingt
      121 gksadisqys nmpdpgdvls sinpddiesi nflkgasasa lygsaggnga ilittrkgki
      181 gkssisysss ltverayslp klqhsylsyd psdptqspgn nieswgakgs skdyvkdflq
      241 tgttwvnsls fqsgnekstn yfsignttnk gvipmsyfdq ynvsfrnssk flddkltlda
      301 nfigslqdsk nrqtpgasfs plaslywlpr gvdfdqygpd sysfidkkrl lpaqnwwevk
      361 pdgsfkgnpe tqnpywilnr navtvknkna ysavslsyei npwltarvrg nyswnssdsq
      421 rdisaysaps llaggqngri lknvyensst ygdvlligsp klsesisldf tvggsvntts
      481 nkvtqidnay lsnpnlfain nlqwnvdrsp gdgyhniywn lkkqvrsvfa sasvgyknmf
      541 yvdmtfrndw dstlaltgrs gfdyesvgan ailssifklp evinfwkvrg syatvglglp
      601 anisnamvay ynaysygvda gtivypkssf vtsrpdlipr pelnktfeag telrmfsnrl
      661 nfdltyynsn asnqlletti gsnfggipsg syyinagkir ntgfeaslsy kvfgtekfgw
      721 tttinasank ntivelfpss lpisenqlfs ltgggdftkl rlggsfgdly gvkfkrddqg
      781 rvlvdengvp lgttgdpqyl gnpnpkfilg fnnsfnigkl gisflidgkf ggkvlsltek
      841 andlygvsqa tadardaggv sipnavyapg tplagqayng vtdakayykr tggaggigtg
      901 ideaylysat tvrlrqasis ysfdiqskym rnatvslvgt nlfffykkap fdpeqvsgnt
      961 pggvgvdsfg lpvtrsigls lkanf
//
LOCUS       WP_121486864            1014 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 7].
ACCESSION   WP_121486864
VERSION     WP_121486864.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     Protein         1..1014
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111214
     Region          44..1013
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 myhkinffkf kklipialif lvanqadakg ftlnypvfsq vnetisgtit dqkgsaiegv
       61 kitvvetgdt astdasgnft isanigqtls isyegygtqm vkisstsvav qlepqkgsts
      121 ieevtlvgyg sqkksdltga vsqlkaenfk egmnisvdnl mqgkiagvri vqssgepgag
      181 vnvsirgigs irsgstplfv vdgvplsnda vsatgpnigl gnaqaknpln flntsdiesi
      241 tvlkdasaaa iygargsngv vlvttkrgrk geplftydty lgfssvikkl dlmsadeyrs
      301 aginklydhg gntdwqdeif rnavssnhsv sfskstetgn yfasishmdq dgiilnsgfk
      361 rttarlnaee sffdnkrlki klnltasdik etgipngana gsdgqviiha lmanptrsvy
      421 dengnftnfn mnahynplyl lsvyndktnt frvlgnteat lrilpglnyk fnlgidktms
      481 ernttmypni tdrtpkgmyv qanldsynvl lehyltydls lnkhnfsllg gfsyqkfktt
      541 gtyfgvknia nqgagispei npgysgeafi paagyaqene lqsyfgrvny nfdkkyllta
      601 slradgstrf gqnnkygyfp svavgwtvsn enflkdsqii nelklrgswg qtgnqevpnk
      661 itqassslsp sggyylydnl nlingvvinr tpnpdlkwev veqtnigadf slwrnklygs
      721 leyynkvtkd pilnipsrpl sptstvwqnv dakivnkgfe fslgseiikt enftwnfdin
      781 gatvnnvvkd lpvsaiysge vsgpglsgvt aniykngyea gsfymlnyqg vdangkyiye
      841 dvnndgridq ndrkifegai pnftfginsy mrykkfdfsf sfigqtggyl vnntaldlni
      901 nnlasdrnvl knfyesganf tnqpqlssly leksdfirln nvklgytfdt sqlkflrsin
      961 lyvsaqnlft ltsytgydpl vdtnkqvsgn qslgidytty psaktfilga tvkf
//
LOCUS       WP_121486889             987 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 7].
ACCESSION   WP_121486889
VERSION     WP_121486889.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     Protein         1..987
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109451
     Region          9..986
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrketqkllv lsllgfvsvn laaqqkvkkd tikgidevvv talgikrhdr algyvaekvd
       61 aktfeetqnn nwaqsmegkv aglkiqtaga gplgtsritl rgeksimmdh nyalivvdgv
      121 plgnsttgsg taaygagsgg dvpidlgngl nsinpddies vtvlkgasaa alygsraang
      181 almittksgk tkngklrvtf nssssfdsvl kwpdwqyeyg qgtqakntag dfyysyglsa
      241 dgpstggtss afgpkfagqy yfqydpnlqg qskdrqlwrp yennikgfwr tgstysnsis
      301 vessnektsf rssltylnne wmmpntgfdr fnfalsfahq ltkklkistk fayntttsdn
      361 lpatgynnqs isyfmifqnp nvdlewykpi wkpgqeqvdq ihpfssfidn pymiayemln
      421 gvrkktitgn itaeyqfnkn fslmlrsgie ilnekrttkr pwssanylkg fyreqfiknq
      481 eynndvlfsy kadwnkfsis asaggsiryn eylmtdyqai glktageysl tnalsipvky
      541 paprdkhvds vyglltlgyd nkifvdvtgr ndwsstlpkq nrsffypsvs tsfilsdlfn
      601 lksnnlnlwk lraswakvgi dsdpylldny ytasnitgsv iapttfnnpt lkpenntnie
      661 agmdfslfkn rlnlnltayq nvsenqiipv slptesgysk rvinagkirn rglelsadil
      721 avkgknfswk vggnwstnen rvmtlpegfd givsnvgdvv fykmevggsl gdmygfkllr
      781 tpdgrviygd nglpgrpadi ekvgnafpkw raglqndfri knftisfsfd gqyggiaysq
      841 shhkmseqgk lkstlpgrdn pggmivgdgv iqnpdgsysp ntkgvtassy ygdyyrranv
      901 etnsfstdfi klrdariays fpketiqslg lddltiaifg knlwmwtkfp mfdpevatld
      961 natitpgvem gqlptartvg fqlnlkf
//
LOCUS       WP_121487425             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium sp. 7].
ACCESSION   WP_121487425
VERSION     WP_121487425.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33652
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypagit
       61 gpemmmdlqk qaerfetkvh yemitkaefs kevggvhkly tgnkeilakt viistgatak
      121 ylglddekky agggvsacat cdgffyrgkd vvvvgagdta aeeatylakl ckkvtllvrk
      181 dvfraskamv hrvestpnie vkfhheligi egenslvera viinnqtqek stvdvegifi
      241 aighkpntdi fvgqidlden gyivtekgst rtnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 samdaekyla elh
//
LOCUS       WP_121488265             942 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 7].
ACCESSION   WP_121488265
VERSION     WP_121488265.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     Protein         1..942
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103849
     Region          35..941
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkqsnlkysc liavlyfgmn vnaqtakkdt atkeqkieev vligygaqkk envtgsigmv
       61 sakdladkpn anpvssiqgk lagvnitntg tpggsprvdi rgvgslsgnt vfivdgmitt
      121 disflnpqdi esmsvlkdps slaifgaqaa ngaviiktkt gkgkpvfsvn sylgikkvtn
      181 ipkmvnsdqy velyneklln dnngdptgsi sranfpadtn wyneifrtsi insndfsatg
      241 sigklnyygs vgylqdegnl aagyginsgs gfnrfntkln lsykitdnit igdnfsfskm
      301 rtdvaqnpll naynappifs vmnpatgdyq ffngysipnp rarldlyrsq vrqerllnni
      361 wgelkflkdf tfrisyssdn yspsqyeytp tlnyvpissq vasslitrnf rnrnyvwdnt
      421 inwkksfgnh nfdilagfsr trtslsqdyw aaknvnydgt ngslniangt dlvhvegvdr
      481 ddavvsgvfq dqqriqsffg rinydykgky lvnasirrda ssqinvdrsk tfpaisagwv
      541 iskedfmseq nvfnllklra sygelgnpnv grgysantti igggayygnt gypaqtidkf
      601 idpnigwett tgkdvglema lfnnklkida ayynkdsknv vygvnqgtvs gasnwnnfvt
      661 naysfnnkgf evsvnyntkl sehvtfgiyg nftslkneit svyggsylet gaslfgnsiv
      721 rlqsgqpvgs yygyqvagvf qtdaeaaasg qpgakagwfk fadqdgngti dsrdktflgs
      781 pipkgtygfg vnfnvydfdi avdfqgvfgn kiynynreqr fgnetwdldm ynnrwhgagt
      841 sntnamitsn qsiilpnsfy vedgsyirlr nvqvgynlpk slaqslsltk lrlyvsaqnp
      901 wtsfkyngfs peitntdrvq mgidnniypi saiytfgmnl tf
//
LOCUS       WP_121488589            1110 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 7].
ACCESSION   WP_121488589
VERSION     WP_121488589.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     Protein         1..1110
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123955
     Region          22..1109
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlillpl laaniamaqq kktitgkied gntshiitga sikietqsvs tktelegiie
       61 svsvgtvtdk dgkfileipa dtktvsvsyp gyesrviqln egqtnytirl tsevtdknki
      121 qeviitgyqk iekrkqtsav stvkmdnisq agvasvdqml agqiagvavt petgapgspa
      181 kirirgtasl sgpqdplwvi dglplegndv pnftdkdnid qlqnfsiagl npndiediti
      241 lkdaaataiy garaangvis ittkkgkkgs lklnfsadtf vtsrpdfdkl nllnasekvd
      301 lelmlakrad liyradkgev mriltqnsql dafrnggfda lnsftrqqin glrnnntdwg
      361 kllyrnaink qyglsvsggs dradyyfslg yydeegttig tgfkrynltl knnyklsdkl
      421 nagisifgtq sertsfvtda dasinpinys rnanpylkpf nadgsynydr didgfedlyv
      481 pfnfleeren tsyslknnsl kaildleykt skslrftsql giqydankte kfagqntyst
      541 rkmregtryy kdgkynyflp agavkqnwdn dffqynwklq aaystkinsk heidlmagte
      601 irktedntti trafgydpts rrgtaivfpn sdfasdkkye tyrenppien ayasmfatas
      661 ytydqkytff gsvrydgtnl fgvnkkykyl piwavsgswl vtkenfmkni tavsnlrlra
      721 syglqgnidr ntspffigey ndatilpgvk egvitvispp ndklrwektt ntnlgldlgl
      781 fnnrvsltad vysrkgtdmi smretpletg feytmmnwgs ltnkgfelal strninhdnf
      841 kwtttinfah nksrvlseqp rdnsflpsre glpvnavfal ktagmdehgn plfwkgdqki
      901 saaeffklyd vyadflpgql vdtklssael rnlftyvgdr dpkftggiin tfkisnfdlt
      961 isatfnlkqt vmrtpsyrgm dldrgrnytr diyqaggslp gitspdmdan pdgwmankwf
     1021 agnssnaysl ldiwakeisy irissirlgy tlpkeftnpm gisslrlsve grnlfvfsng
     1081 ysgyfdpety gniyaqpitk svtvgfnvsf
//
LOCUS       WP_121488606             932 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 7].
ACCESSION   WP_121488606
VERSION     WP_121488606.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     Protein         1..932
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103378
     Region          30..930
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvklhvlsa galfflgqaa faqkskndsv lkenkidevi vtgyqkkkad eitqaqavvg
       61 gdeirrnspt tsignslqgr asgvfvqstt gqpgaaatiq vrgvagvggs septyvvngm
      121 ymnarqfsai npadvesisi lkdaaataqy gargangvvv vttkagkagk thysfetkfg
      181 fseklrdkny tmmnsrelld fqnqlgylgf kprtqqeidr laaydhnwqk dllkpssiqs
      241 ylfsaqggsr estfyyslgy dsdngiirdi dglkrytgnf gftnklsekl nvginlgvqy
      301 qetqnfmdrn ntqnpfgamy kyapyepvyn adgsynqtmr agsnvveqir nyrlddqrlr
      361 ipvtlfaeyk iidglkfktn fnglfdwymg tqwlkkgsnl dltlnnkipt gslnknsfyt
      421 fnytwnnsin ykksygghnf dflgfieynd nynetmngga yglkspvinv psittpsdrn
      481 tftgvkvrnt lfslagilny dyegkylvtg slrrdassrf gannqsgifw sasaawniak
      541 edfmkggfin dlklrgsygt tgndgtlpdy ynvnnisygl ygtngtsypg tvskgnyiig
      601 nnnlkwesna itnlgvdftm wnrrvrgsve vyqnkrkdfv qlvpldkqeg gyyqyinagd
      661 msqkglevel svdvikqkdf qwnlhanisf qksvldrlad gqternlgdt ylkvgetpyv
      721 fynvrfagvd psngkalyyd kagnitdvys asnavpltdk spfpksfggf gttvqykgld
      781 fsadfafklg gytynnmyla avdptlavag rnmaqaaaqi wqnpgdtgvf qkvdsngmrd
      841 sdqwieksdy lrlrsltlgy tfdkaflgeg spinklrayv qgqnlftvtk fhgepevslg
      901 sadstalfvp gaynlytypa vrtilvglql ef
//
LOCUS       WP_121489065             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 7].
ACCESSION   WP_121489065
VERSION     WP_121489065.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=107353
     Region          19..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkltasllv lvvsssiava naqqkndtvk tkeiegvvvt algikrekks lgyaseevka
       61 aeltggttnt gnvasllsgk vaglqvntnn nfggsanlli rgykslnggs plividgspv
      121 nnttvttgap fdygnflsdi nqediesinv lkgaaasaly gergsdgvil ivtksgrgnn
      181 dgswgvtlns gitagfidks tfpkyqtryg agyggeswne apgpggynya nfgddasygp
      241 afnpnslvyq wdsfdpsspn ygkatpwvaa kngpikffet pvtyintitl ekgnktsnls
      301 lsysnmlsng lmpnselrkn tisakfshdf tdklhasvft tltlqgtrgr netgysdniv
      361 sgfrqwwqtn tdvyalrnay qnngnsnfsw nrtsaddgtp qywnnpyfqr yqsyqsddrt
      421 rvfsyaqlky dvsknfgitg klsyddlqmv veerlmngsl pqvfgasgln vgsgyartnv
      481 knsemnfdlf anykfditpd lnvsgiaggn vrrnlidnvy mstegglskp glfaisnsvr
      541 tilppdenya kfvtsslyat asfgyknflf vdgtfrvdqs snlpkgnnsy sypsvtgsli
      601 lsefvkqpwl sfwkirgnya evgsstsnyr lantfkarge glfdqpyfla npdlkpqrsk
      661 etefgmeaqf fknrlgfdia iyktktidqi inlpvssatg yrtflvnagq idnkgieiql
      721 ngtpfksdnf twdinvnwsk nenkvislng nsqnylmaty qngvslnarv geafgalvgs
      781 dyqydangnk ivdpvsgnyl rnnnqvigni tpdwvggirn sfrykdfsvs flidvkqggd
      841 vyspdmaygt atglyeetay yresgvinpg vnpngnvntt vagdptsags vdgygvmpnk
      901 rfvydasyvk lreasigysl pksilantsi rdakisivgr nlwiihknlp yadpeagtgn
      961 glaakgqsig vlpttrdigi dltlkf
//
LOCUS       WP_121489393            1046 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 7].
ACCESSION   WP_121489393
VERSION     WP_121489393.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     Protein         1..1046
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118179
     Region          22..1045
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkktlatfav fllplyfsaq einitgnvks engssvsgvn itdkntgkta ttdengnfti
       61 sanpkdilef fapdfsvytv evsskkqysv vlkkpnekqi egivitalgi akkkekigys
      121 tqevgtkqfe tittpsignl fsgqvaglnv snptgmqqap qftlrgnsnl vfvidgvive
      181 revfqnldpn nieninvlkg atasalygsr grygavlitt knakkkgfsv efsqntmitg
      241 gftnlpktqt eygngshgky efwdgadggv ndgdmiwgpk fvpglqiaqw nspirdkvtg
      301 qvvpwygavt gtqyddksry ervpidwkyh dnlstflkpa vinnnnfais yrdnkdiyrf
      361 sgnfmnyddr vpnsylqkyg infssenhlg dklifdtkfn fnqaftpnip nydynpsghm
      421 ytiliwmggd vdgkalknhm wipgregraq anwnyawynn pwfgaeyykn qnrtniinaq
      481 tgleykatqd lsvkgkislv enhsktevls pysyfnysap rsggyilkdn ktwnlnydvl
      541 atykkkisen fdftinaggs afyyknnnne rstdglkipe vysfensiga lknysylkek
      601 liysaystid iglynaffin isgrndwsst lpkanrsyfy psasisavis nlvklpesvn
      661 mlklsaswak vaydfqpysi rnyylnnqgi tfngnptyyy pttlnvensl kpeqtksyel
      721 glsagflnnr itldatyfrt ldynnilqfp aaessgftsq yvngneyttk gfevslglvp
      781 vktadfswkt linwstyeqk ltsiydnmpn ykniklgerm dsyydytwqk spdgkvilda
      841 ntgmptrana psnlghfnpd wtfgfnntfk ykkftlnigi dgsiggvmrs qvvekmwwgg
      901 khpnsvayrd leyanpgtyy fvpdgvnynp atgqytphtk aisfqdwaqn ypyqarvtqd
      961 eseefanvfd rtfvklrsvv leydfsslln prgmvkgfta nisaynlamw kksknlysdp
     1021 dfqaktendi qdpssrwfgi gfnlkf
//
LOCUS       WP_121489678             917 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Chryseobacterium sp. 7].
ACCESSION   WP_121489678
VERSION     WP_121489678.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 7
  ORGANISM  Chryseobacterium sp. 7
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Chryseobacterium sp. 7"
                     /db_xref="taxon:2035214"
     Protein         1..917
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=100594
     Region          30..915
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfttvlki apafllastv mhaqkkdslp qekkidevvl igygkqkksd ltgsitsvta
       61 kdfnggatsa gqliqgktpg vqitnnsgap gsgtkirirg tsslsgensp lividgvpqd
      121 fvgmngvsdp lslinpndie tfdilkdasa taiygnrasn gvilvttkkg tagkfklnfs
      181 tvasvstkmg kvdvlnaqef rdfvnayapa gyktklgnan tdwqdqiyqa awgtdnnval
      241 sggikglpyr lslgyneqng ivksnsfrrt svglnlnpkf ldnhlsvnvn lkgtftdnrf
      301 vdgevikaat yfdptqpvys gnsnyggyye wldpgsatgy nvngnknpvg lingirdvss
      361 vtrglgniql dyklhflpdl hfnvnagydy tksdghkfkd gnlragfedk gssnfysmek
      421 knklletyfn yvknisaidt gvditagysy qdfnilipga vtyrgtgins qdldfetrnt
      481 lisfygraif tiankyvisg sirrdgssrf yngtrdnvwg vfpgvslawk lneenfikni
      541 ssistlklra gwgktgqqel paldgnkpnn ypafaaynps yqgagyqfgn efyfmyrpan
      601 ynpnltwett ttknlgldfg fnknritgsi dvfrkdtkdl lvyadepagg lsnaswqnvg
      661 dmknegiegs itvvpvknqn ttwevsfnat hykpiitklk dradesfnme vggiegaagn
      721 kiqahavgya pnsfwvyqqi ydtngkpvdg afvdrngdgv istkdmyyyk sttpdailgf
      781 stkvshknwd falsaravlg nyvynnaasn ssiqsastne ylqnvfatap qyqfsipqyk
      841 sdiyvenasf lrldninigy nfgeiftkgs nlkvyamaqn vfvitkysgv dpevfggidn
      901 gyyqmpriys lgfnfqf
//
LOCUS       WP_121495909             298 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121495909
VERSION     WP_121495909.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>298
                     /gene="trxB"
     Protein         1..>298
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..298
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaits
//
LOCUS       WP_121490522             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cupriavidus plantarum].
ACCESSION   WP_121490522
VERSION     WP_121490522.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus plantarum
  ORGANISM  Cupriavidus plantarum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Cupriavidus plantarum"
                     /db_xref="taxon:942865"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39461
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipletr agetrvaatp etvkkyvaqg hqvtvqtgag vrasqpdgay eavgarigsa
       61 aeaygaeivl kvrapddaer almkpgtvli gmlnpfdien narmtaasit afsleaaprt
      121 traqsmdvls sqaniagyka vliaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfltdee reiaqgvggy arpmpadwmr
      241 rqaelvhera rqadivitta lipgrkapvl lkeetvqqmk pgsvvvdlaa aqggncpltv
      301 adevverhgv ilvghtnlas mvaadasaly arnvldflkl vidkdgrytl nleddivaac
      361 lmcrdgqlvr qaa
//
LOCUS       WP_121508279             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. 93].
ACCESSION   WP_121508279
VERSION     WP_121508279.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. 93
  ORGANISM  Acidovorax sp. 93
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Acidovorax sp. 93"
                     /db_xref="taxon:2135632"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55483
     Region          11..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqttpvpqpq rigvpretfp gekrvatvpd vvekliklgf avtvesgagd ganfsddayr
       61 aagaqivgda aalwaasdiv fkvrppssde valmregttl idfiwpaqnp elmqqlsark
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rkmyaeqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg qavvrhgvti vgytdlasrl akqsstlyst nllrlteelc kakdgvavvn
      361 meddairglt vvkdgaitwp applkqapap apkaaaapva akksshgpga pmsaktltiv
      421 favlavlfwa igayapvafl ghftvfvlac figymvvwnv tpalhtplms vtnaissiia
      481 igalvqiapp dagingrpdg lilwlafaal vltavnmfgg favtrrmlam frk
//
LOCUS       WP_121497205             301 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_121497205
VERSION     WP_121497205.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>301
                     /gene="trxB"
     Protein         1..>301
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..300
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 p
//
LOCUS       WP_121517882             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. Z26].
ACCESSION   WP_121517882
VERSION     WP_121517882.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. Z26
  ORGANISM  Streptomyces sp. Z26
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces sp. Z26"
                     /db_xref="taxon:2500177"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34709
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegsvtag galmntteve nfpgfsegil
       61 gpdlmdqmra qaerfgaelv addvsavdfs geiktvtdse gtvhrartvi vstgsqhrkl
      121 glpqedelsg rgvsycatcd gfffreqdiv vvgggdtame eatflsrfak tvtivhrrdt
      181 lraskamqer afadpkinfa wnsevaeihd kdgklasltl rdtttgetsa laatglfvai
      241 ghdprtelfe gvlefddegy lvvdspstrt kvpgvfaagd vvdhtyrqai taagtgcsaa
      301 ldaerylaal adgasspest pepdkvaav
//
LOCUS       WP_121521876             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Oceanobacillus piezotolerans].
ACCESSION   WP_121521876
VERSION     WP_121521876.1
KEYWORDS    RefSeq.
SOURCE      Oceanobacillus piezotolerans
  ORGANISM  Oceanobacillus piezotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Oceanobacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Oceanobacillus piezotolerans"
                     /db_xref="taxon:2448030"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34360
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtnenvfdvi iagagpagmt aavyasranl rtlmiergip ggqmantedv enypgfdsil
       61 gpdlsnkmfd hskkfgaeya ygditevidn gtykiikagn keyktkafii atgaeykklg
      121 iegeedlggr gvsycavcdg affkqkhlvv vgggdsavee gvyltrfadk vtiihrrdel
      181 raqkilqqra fdnekvdfiw dtvvkkingp egkvssvtle nvktgeqfdf dadgvfiyig
      241 lvplsgpfvs lgitndegyi ptnehmetkv pgiyaagdir ekqlrqivta tgdgsiaaes
      301 aikfveelee etkvaks
//
LOCUS       WP_121531326             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter cumulans].
ACCESSION   WP_121531326
VERSION     WP_121531326.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter cumulans
  ORGANISM  Acinetobacter cumulans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acinetobacter cumulans"
                     /db_xref="taxon:2136182"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33558
     Region          8..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdaqglt
       61 gpalmermqe haerfgteii ydhinevdls qrpfvlkgdm deftcdalii atgataqylg
      121 leseaaymgq gvsacatcdg ffyknqkvmv vgggntavee alylsniash vtlvhrrdsl
      181 rsekilqdhl fekvkegkis iiwnhqvdev lgdaqsgvts vrlkstqdds tqnvdvtgmf
      241 vaighkpnsg mfegqltlrd gyvqvqsgta gnatqtsvag vfaagdiads iyrqaitsag
      301 sgcmaaldae kyldal
//
LOCUS       WP_121530290             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenirhodobacter hankyongi].
ACCESSION   WP_121530290
VERSION     WP_121530290.1
KEYWORDS    RefSeq.
SOURCE      Paenirhodobacter hankyongi
  ORGANISM  Paenirhodobacter hankyongi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Paenirhodobacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenirhodobacter hankyongi"
                     /db_xref="taxon:2294033"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33429
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mgetkktrvl iigsgpagyt aavysaraml npvlvqgiqp ggqltittev enwpgrtave
       61 gpelmvqmee haramgteii sdtitslklg drpfvalgds gttyvadavi latgaqarwl
      121 glpseetfkg fgvsacatcd gffyrgkevv vigggntave ealfltnfat kvtvihrrds
      181 fraekimqdr lfrnpkvevi wdsvpeeilg tdaplgvtgv rirnvktdae tvvpcdgffv
      241 aighapasel vkdqlelhhg gyvkvepgtt rtsiegvfaa gdltdhiyrq avtsagmgcm
      301 aaldaerwla eqe
//
LOCUS       WP_121541563             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mariprofundus sp. EBB-1].
ACCESSION   WP_121541563
VERSION     WP_121541563.1
KEYWORDS    RefSeq.
SOURCE      Mariprofundus sp. EBB-1
  ORGANISM  Mariprofundus sp. EBB-1
            Bacteria; Pseudomonadati; Pseudomonadota; Candidatius
            Mariprofundia; Mariprofundales; Mariprofundaceae; Mariprofundus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Mariprofundus sp. EBB-1"
                     /db_xref="taxon:2650971"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32848
     Region          9..307
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseavhhrli ilgsgpagyt aaiyaaranl apvviqgqqa ggqlttttdv dnypgykdgv
       61 qgpemmedfk aqaerfgtel iwdhineadl skrpftlkgd dgtytcdali iatgasakyl
      121 glpsedefag rgvsacatcd gffyrgkdva vvgggdtave ealylsnlcn kvtlihrrda
      181 lraepimqdk llatenieva wnsttdsilg detgvtgirl nstvdgssrd vdvhgvfiai
      241 ghkpntdfla gkldmdetgy lntvgksttt svegvfaagd vadpvyrqav tsagegckaa
      301 ldaerwlaaq e
//
LOCUS       WP_121533325             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paenirhodobacter hankyongi].
ACCESSION   WP_121533325
VERSION     WP_121533325.1
KEYWORDS    RefSeq.
SOURCE      Paenirhodobacter hankyongi
  ORGANISM  Paenirhodobacter hankyongi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Paenirhodobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Paenirhodobacter hankyongi"
                     /db_xref="taxon:2294033"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55933
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapretf egesrvamtp dsalqlqklg htcfieagag daagfsdeay rkagvtvipt
       61 vaelfaevdf ivkvrplvtd eehgwlrkgq tvisffypgq hpdrlelake tganfiamdm
      121 vprisraqkm dalssmania gyravmeaan nfgrfftgqv taagkvppak vlivgagvag
      181 laaigtttal gaityafdvr pevaeqiesm gaefvyldfe ektqdgaaag gyaapsspef
      241 reaqlkkfre lapdmdivit talipgrdap klwladmvaa mkrgsvvvdl aaerggncdl
      301 tvpgekivse ngvtiigynd fpsrmatqas qlyatnirhm itdltpgkdg vivhnmeddv
      361 irgatvafeg avtfpppppk ikaiaahkpk ekakeptpee rkaaekeafr katrqqvmll
      421 aigtallllv gsvapasfms hfvvfalscf vgfqviwnvs hslhtplmav tnaisgivil
      481 gallqvgsgs wlvvvlaals vliatvnivg gflvtrrmla mfqks
//
LOCUS       WP_121544167             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mariprofundus sp. EBB-1].
ACCESSION   WP_121544167
VERSION     WP_121544167.1
KEYWORDS    RefSeq.
SOURCE      Mariprofundus sp. EBB-1
  ORGANISM  Mariprofundus sp. EBB-1
            Bacteria; Pseudomonadati; Pseudomonadota; Candidatius
            Mariprofundia; Mariprofundales; Mariprofundaceae; Mariprofundus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Mariprofundus sp. EBB-1"
                     /db_xref="taxon:2650971"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39554
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mliavpaesq skekrvaatp dsvgrfiaag cdvvvqknag taasypdaay qakgaklvds
       61 fagvcadadl vlkvralqad eigalkkgaa iaslvapfsn pllqqyadag ityfcmemvp
      121 risraqsmdv lssqaniagy ksvllamehy qrffpmlmta agtvqpakvl vmgagvaglq
      181 aiatarrlga sveafdvraa akeqveslga kfvevaadad aedaggyake mdddykrrqs
      241 eliaahaaka diiittalip grpapvlite emvktmkpgs vivdmavemg gncpiseldq
      301 vvekhgvtlv gvvnipalma tdasslyarn lvnfitpmld kesgalvinm ddevvessli
      361 ckdgaflkpq llnqgdas
//
LOCUS       WP_121546697             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_121546697
VERSION     WP_121546697.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34136
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqegim
       61 gpelmdnmra qaerfgaelv pddvvavdlt geiktvtdta gtvhkakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkisfv wdseiaevqg dqklsglklr nvktgelsdl aatglfiaig
      241 hdprtelfkg qleldeegyl kvdapstrtn itgvfgagdv vdhtyrqait aagtgcaaal
      301 daerylaals deeqaepekt sv
//
LOCUS       WP_121550474             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesotoga sp. BH458_6_3_2_1].
ACCESSION   WP_121550474
VERSION     WP_121550474.1
KEYWORDS    RefSeq.
SOURCE      Mesotoga sp. BH458_6_3_2_1
  ORGANISM  Mesotoga sp. BH458_6_3_2_1
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Kosmotogales;
            Kosmotogaceae; Mesotoga.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Mesotoga sp. BH458_6_3_2_1"
                     /db_xref="taxon:1437446"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34551
     Region          35..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msffelgsak kadlkeyydv tiigggpggi tagiyavqag lkpiivekal dggqmnntqt
       61 venwtgftti sgmelsekma dharafdvpf vyaevvdiet nglekavvld ngkriksrvi
      121 ivatgsnprk lgvkgeeefk grgisycatc dghffsdkhi avigggnsal deslylskmv
      181 skitviqnlp kltadrllqt klndtgkvey iyssvvdsve gdsqvrkvni kdvnssetts
      241 lgvdgifvfi glipntqflk gklemnefgy ikaddfmetr tkgvyaigdv rekevrqivt
      301 aaadgaiaiy haarnyfnd
//
LOCUS       WP_121581396             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp. YM1C-6-2].
ACCESSION   WP_121581396
VERSION     WP_121581396.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. YM1C-6-2
  ORGANISM  Mesorhizobium sp. YM1C-6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. YM1C-6-2"
                     /db_xref="taxon:1827501"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34565
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtvkhapvli igsgpagyta aiyaaramlk pvlvaglqqg gqlmittdve nypgfaepiq
       61 gpwlmeqmmk qaehvgaeiv ndiitevnld vrpfrakgds gteytadalv vatgaqakwl
      121 gipseriyqg fgvsacatcd gffyrnrdva vigggnsave ealylsniak tvtvihrrde
      181 fraerilqer lfqkenikvi wdttvdeitg npgkaplpps anglvlrnvh tgavsrlpid
      241 gvfvaighap avelfvgklk qksngylwte pgstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagieahr eaae
//
LOCUS       WP_121579907             430 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. YM1C-6-2].
ACCESSION   WP_121579907
VERSION     WP_121579907.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. YM1C-6-2
  ORGANISM  Mesorhizobium sp. YM1C-6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Mesorhizobium sp. YM1C-6-2"
                     /db_xref="taxon:1827501"
     Protein         1..430
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43719
     Region          7..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqiafipke veageprvga spetvkrlag lgfeviveag aglgsritdd efakagaaig
       61 kaadagradl vlkvrrptea elkgykpgaa viatmdpygh daavaamaka gitafamefm
      121 prisraqvmd vlssqanlag yqavidgaae ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegav
      301 agavitldng vkivghlnvp grvaasasll yaknlyafve tmvdkttkaf avnredelvk
      361 atmltdagkv vhpafadaaa aaekaaaeqk sadepaagge pakaekkpaa rkskkaasgp
      421 tsgpasggea
//
LOCUS       WP_121584097             315 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Mesorhizobium sp. YM1C-6-2].
ACCESSION   WP_121584097
VERSION     WP_121584097.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. YM1C-6-2
  ORGANISM  Mesorhizobium sp. YM1C-6-2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Mesorhizobium sp. YM1C-6-2"
                     /db_xref="taxon:1827501"
     Protein         1..315
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35366
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mpvyetfakr qkrekgeqpd vfvydtmptp lrvqivqifd etlgdqdafd dhyghgpkvr
       61 rlyisaikll rrelgvfelp hapsydknai kefrsyilgv kdveqclsai eigcrlienv
      121 askfdyrnrp kapkeamaai eeinarfkeh gigysydgei irvdsqliha eavkpalrll
      181 nskqyegaqe eflsayehyr qgktkealnd clkafestmk aicdkrgwgy dpkataktli
      241 dillanglip sfwqtqmgsl rtllesgvpt grnrlgghgq gsvstevpgy laaymlhmta
      301 stlvflveae kaspq
//
LOCUS       WP_121585843             308 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Anaerotruncus].
ACCESSION   WP_121585843
VERSION     WP_121585843.1
KEYWORDS    RefSeq.
SOURCE      Anaerotruncus
  ORGANISM  Anaerotruncus
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Anaerotruncus"
                     /db_xref="taxon:244127"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=31944
     Region          4..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mndydviiig agpagltaai yvqragyrsv vleeyvaggq mantpeveny pavgkisgve
       61 lgmnlynqvl eqgaqvefdg vasadltgkv ksvvtqsgrk itagaviian gakrrklgvp
      121 geeeysgrgv sycatcdggf ykgkttvvig ggntavedal ylaniceevh lihrrdafra
      181 gkvlvdslls renivihydt vpvevlpdeg gkvvgalkvk nvktgaetei paqgvfvavg
      241 lvpdnkvfeg qvdldpagyi aagedthtnl pgvfaagdtr tkalrqiita agdgavaase
      301 agsylmqg
//
LOCUS       WP_121605659             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Virgibacillus].
ACCESSION   WP_121605659
VERSION     WP_121605659.1
KEYWORDS    RefSeq.
SOURCE      Virgibacillus
  ORGANISM  Virgibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Virgibacillus"
                     /db_xref="taxon:84406"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34496
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msenhmydvi iagagpagmt aavyasranl etlmiergip ggqmantedv enypgydhil
       61 gpdlsnkmfe hakkfgaeya ygdikevidh gdyktivagn keyntralii ttgaqykklg
      121 ipgeeelsgr gvsycavcdg affkeknliv igggdsavee giyltrfadk vtvvhrrdal
      181 raqrilqdra fdnekidfiw dtvvekined ggkvgsatlk nnktgetyey sidgvfvyig
      241 mvplsepfks lgitndegyi ptnenmetti pgifaagdir dktlrqivta tgdgsiaaea
      301 aikyvedlqe elkttns
//
LOCUS       WP_121611073             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesobacillus foraminis].
ACCESSION   WP_121611073
VERSION     WP_121611073.1
KEYWORDS    RefSeq.
SOURCE      Mesobacillus foraminis
  ORGANISM  Mesobacillus foraminis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Mesobacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Mesobacillus foraminis"
                     /db_xref="taxon:279826"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34097
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseekvydvi iigagpagmt aavytsranl stlmlergvp ggqmanteev enypgfdhil
       61 gpdlstkmfd hakkfgaeya ygdvkeiidg kdyktvvags kqykgraiii sagaeykkig
      121 vpgeqelggr gvsycavcdg affkgkelvv vgggdsavee gvyltrfask vtivhrrdel
      181 raqpilqdra fandkidfiw shtvkeinek dgkvgsvtlv stkngeetef kadgvfiyig
      241 mvpltkpfes lgitnsngyi etnekmetkv agifaagdir ekslrqivta tgdgsiaaqq
      301 aqhyveelke elkaka
//
LOCUS       WP_121616913             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus aureus].
ACCESSION   WP_121616913
VERSION     WP_121616913.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33484
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteidfdiai igagpagmta avyasranlk tvmiergipg gqmanteeve nfpgfemitg
       61 pdlstkmfeh akkfgavyqy gdiksvedkg eykvinfgnk eltakaviia tgaeykkigv
      121 pgeqelggrg vsycavcdga ffknkrlfvi gggdsaveeg tfltkfadkv tivhrrdelr
      181 aqrilqdraf kndkidfiws htlksinekd gkvgsvtlts tkdgseethe adgvfiyigm
      241 kpltapfkdl gitndvgyiv tkddmttsvp gifaagdvrd kglrqivtat gdgsiaaqsa
      301 akyiehlndq a
//
LOCUS       WP_121625562             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Xanthobacter tagetidis].
ACCESSION   WP_121625562
VERSION     WP_121625562.1
KEYWORDS    RefSeq.
SOURCE      Xanthobacter tagetidis
  ORGANISM  Xanthobacter tagetidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Xanthobacteraceae; Xanthobacter.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Xanthobacter tagetidis"
                     /db_xref="taxon:60216"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34160
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtthhkkvvi igsgpagyta aiyaaramle pvlfegiqpg gqltittdve nypgfadviq
       61 gpwlmeqmra qaahmgtqii adhvasldls rrpfrmtteg getyladvvi lstgaqarwl
      121 giaseeayrg fgvsacatcd gffyrgkevv vvgggntave ealfltnfas kvtvvhrrds
      181 fraekilqer lfahpkvnvv whaelaeivg aeeptrvtga mlrdtrtgel trlaadgvfi
      241 aighapstel vkdqlrlkpn gyvwtapdst atsvagvfaa gdvaddvyrq avtaagrgcm
      301 aaleterfla hhqvsqaae
//
LOCUS       WP_121628568             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Poseidonibacter antarcticus].
ACCESSION   WP_121628568
VERSION     WP_121628568.1
KEYWORDS    RefSeq.
SOURCE      Poseidonibacter antarcticus (Arcobacter antarcticus)
  ORGANISM  Poseidonibacter antarcticus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Poseidonibacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Poseidonibacter antarcticus"
                     /db_xref="taxon:2478538"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32813
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mldlaiiggg pagltaglya trgglgnvtm femgmpggqi tgsseienyp gqseivtgmd
       61 lmsnwpeqcq rfglkhemnq ittitkegdt fklsavdgke yeaktvlmat gsvprragfk
      121 gedeffgrgi stcatcdgff ykgkevavig ggdsaleeav ylskmcskvy lvhrrdtyra
      181 apstiehmka asnieevtnv dveevfgdms gvlglkvksk engeirdlpt pgvfvfvgrn
      241 vlneplkqed gsflcdtnna gevvvdlkmq tsvkglyaag diridaakqv vcaaadgata
      301 avniieylg
//
LOCUS       WP_121621341             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Xanthobacter tagetidis].
ACCESSION   WP_121621341
VERSION     WP_121621341.1
KEYWORDS    RefSeq.
SOURCE      Xanthobacter tagetidis
  ORGANISM  Xanthobacter tagetidis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Xanthobacteraceae; Xanthobacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Xanthobacter tagetidis"
                     /db_xref="taxon:60216"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39388
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavpaevd lgeprvaatp dtvkrlvalg aqvaveagag vksgildady eavgatiaps
       61 gadvvagadv vlkvrrptea elssykrgal vlaimdpygn daalaamana gvasfamelm
      121 pritraqvmd vlssqaniag yravidaaae fnralpqmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg aivtatdvrp aakeqvaslg akfvavedee fkqaetaagy akpmsaeyqa
      241 kqaalvadhi kkqdivitta lipgrpapkl isaamvasmk pgsvivdlav erggnvegai
      301 pgqvvqvggv kivghlnvpg raaastsply aknlfnflet mvdkqakala vkwddelvka
      361 tlltrdgavv hpnfapknps pegaa
//
LOCUS       WP_121630626             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tropicibacter alexandrii].
ACCESSION   WP_121630626
VERSION     WP_121630626.1
KEYWORDS    RefSeq.
SOURCE      Tropicibacter alexandrii
  ORGANISM  Tropicibacter alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Tropicibacter.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Tropicibacter alexandrii"
                     /db_xref="taxon:2267683"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35020
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtrhtkvl iigsgpagyt agvyasraml epilvqgiep ggqlttttev enwpghteiq
       61 gpdlmvnmea haramgteii gdiinkldld trpfvahgds gttytadavi latgarakwl
      121 glpseeafkg fgvsacatcd gffyrgkeiv vigggntave ealfltnfas kvtlihrrde
      181 lraekilqdr llkhdkietl wfhqleevig ddmpkgvtgv kvknvktgei sqidcagvfv
      241 aighapanel vkdvlethmg gyvvtkpdst etsipgvfaa gdltdhkyrq avtsagmgcm
      301 aaleaerwla eqdaagepat dvanepesa
//
LOCUS       WP_121634368             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tropicibacter alexandrii].
ACCESSION   WP_121634368
VERSION     WP_121634368.1
KEYWORDS    RefSeq.
SOURCE      Tropicibacter alexandrii
  ORGANISM  Tropicibacter alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Tropicibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Tropicibacter alexandrii"
                     /db_xref="taxon:2267683"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55625
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpteve agenrvamtp dsalqlqklg yecliqsgag aradfsdsdy eaagvtvvpd
       61 adalwaqadi iakvripqda eldrltpekt litffnpggn aeglekakak ggnviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee eqqdgsatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreapk lwledmvkam kpgsvivdla aekggnvegt
      301 vkdekvvtdn gvtiigytdf psrmarqssl lystnirhmm tdltpekdgk vnhnmeddvi
      361 rgatvayqge itfpppppkv aaiaakpkek vkeltpeekr aneiaafkaq tknqvtlitv
      421 gavlllavgl vapasfmqhf ivfilsvfig fqviwnvahs lhtplmavtn aissiiilga
      481 liqigsssvl itilaalgif masinifggf lvtrrmlamf qks
//
LOCUS       WP_121636290             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Planomicrobium sp. Y74].
ACCESSION   WP_121636290
VERSION     WP_121636290.1
KEYWORDS    RefSeq.
SOURCE      Planomicrobium sp. Y74
  ORGANISM  Planomicrobium sp. Y74
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planomicrobium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Planomicrobium sp. Y74"
                     /db_xref="taxon:2478977"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34208
     Region          8..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteaekiydv viigagpagm taavytsran lstlmiergi pggqmantee ienypgfehi
       61 lgpdlstkmf dhakkfgaey aygdvkgivd geeyktitag skeykaravi lttgaeykkm
      121 gipgetelgg rgvsycavcd gaffkqknli vvgggdsave egvyltrfad kvtivhrrde
      181 lraqkilqdr afandkidfi wshtvkeikg engkvsgvtl vstkdgvete keidgvfiyi
      241 gmlpltkpfa dlgilndegy vvtnekmets vpgiyaagdl rektlrqvvt atgdgsiaaq
      301 aaqhyieelv ekigqnv
//
LOCUS       WP_121638592             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudoalteromonas agarivorans].
ACCESSION   WP_121638592
VERSION     WP_121638592.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas agarivorans
  ORGANISM  Pseudoalteromonas agarivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudoalteromonas agarivorans"
                     /db_xref="taxon:176102"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34000
     Region          6..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msthrkliil gsgpagytaa iyaaranlep llitglevgg qlttttdven wpgyptgiqg
       61 pqlmrqfkeh aenfnteivh dyithvdlqq rpfvlkgqqt ytadaliist gasakylglp
      121 setefkgkgv sacatcdgff yknqsvavvg ggntaveeal ylaniashvt lihrrdslsa
      181 ekvlqqrlfd kvaqgkvtik wnnqvdeivg dangvtgiti kstlaehnre tlsvngvfia
      241 ighqpntdif kdqldmrdgy invysgfeng etltnipgvf aagdvsdnhy kqaitsagsg
      301 ckaaldveqy ftrlga
//
LOCUS       WP_121645459             418 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Notoacmeibacter ruber].
ACCESSION   WP_121645459
VERSION     WP_121645459.1
KEYWORDS    RefSeq.
SOURCE      Notoacmeibacter ruber
  ORGANISM  Notoacmeibacter ruber
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Notoacmeibacteraceae; Notoacmeibacter.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Notoacmeibacter ruber"
                     /db_xref="taxon:2670375"
     Protein         1..418
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42481
     Region          4..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,289,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtvfvpke sladegrvaa spdtvkrika lgldvvvete agrasrilds dyetagarig
       61 sasdatsadv ilkvrrptte eiaaykqgai vlatmdpfga eealsamada glsafamelm
      121 pritraqvmd vlssqanlag yqavidaaea ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatakrlg gvvsatdvra aageqvaslg gkfimtealk dasgeggyar eltddekkaq
      241 selvaghiak qdivittali pgrpapklid admvasmkpg svivdlaver ggnvegskag
      301 evvvtkndvt iighlnvagr iaatasqlya knlyafletm vdgesgsvai dredelvsat
      361 llthggkvvh erfggastea paaapddgas pegeaapave pgtgdsdagk gntsegka
//
LOCUS       WP_121648785             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mycetocola tolaasinivorans].
ACCESSION   WP_121648785
VERSION     WP_121648785.1
KEYWORDS    RefSeq.
SOURCE      Mycetocola tolaasinivorans
  ORGANISM  Mycetocola tolaasinivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Mycetocola.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Mycetocola tolaasinivorans"
                     /db_xref="taxon:76635"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33275
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrnviiigsg pagytaaiya aranlnplli assvqaggel mnttevenfp gfpegiqgpe
       61 lmakmqeqae kfgtevlldd vteldlsgdi krvvtgysge feaesvifat gsayrkigla
      121 deerlsgrgi swcatcdgff fkektiavvg ggdsameeat fltkfaskvy vihrrdtlra
      181 skimqeraha nekiefiwna evtgisgena lsgvtltdtv tgeerelald glfvaigndp
      241 rthlvhgkld ltaegtiava grssktnvag vfaagdvidp tyrqaataag sgvvaaldae
      301 hylaaresav qapaha
//
LOCUS       WP_121645270             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Notoacmeibacter ruber].
ACCESSION   WP_121645270
VERSION     WP_121645270.1
KEYWORDS    RefSeq.
SOURCE      Notoacmeibacter ruber
  ORGANISM  Notoacmeibacter ruber
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Notoacmeibacteraceae; Notoacmeibacter.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Notoacmeibacter ruber"
                     /db_xref="taxon:2670375"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35017
     Region          10..318
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpasaqhtsv lvigsgpagy taaiyasral lepvliagle qggqlmittd venypgfadp
       61 imgpqlmeqm rqqaenvgar lvsdivtdvn ldirpfritc dsgavwtads viiatgaqak
      121 wlglpseetf kgfgvsacat cdgffyrgkh vlvvgggnsa veealylani aekvtvvhrr
      181 defraerilq drlfrqknve ilwntevdem lgtqpkaplp psvnavrlkd vttgetremd
      241 idgvfvaigh apavslfegk lkqkpngylw teadstrtsv pgvfaagdva ddiyrqavta
      301 aglgcmaale aerylagias etevqaae
//
LOCUS       WP_121654158             316 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Micromonospora].
ACCESSION   WP_121654158
VERSION     WP_121654158.1
KEYWORDS    RefSeq.
SOURCE      unclassified Micromonospora
  ORGANISM  unclassified Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="unclassified Micromonospora"
                     /db_xref="taxon:2617518"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33602
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlkp liiegvqsgg almttteven fpgfadgilg
       61 pelmdnmrkq aerfgaeflt ddvtrvelvd tgdagsgavs tvwvgetayr arsvilstgs
      121 awrplgvpge qeflghgvss catcdgfffr nqhivvvggg dsameeasfl trfadsvtii
      181 hrrdsfrask imadralnne kikvewnstv eeilgadgkv tgvrvrnvhs getkvldvtg
      241 vfvaighdpr selfrdqvel ddegyvkvqa pstrtnvpgv faagdvvdht yrqaitaagt
      301 gcaaaldaer fiatls
//
LOCUS       WP_121651187             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agrobacterium fabrum].
ACCESSION   WP_121651187
VERSION     WP_121651187.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium fabrum
  ORGANISM  Agrobacterium fabrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Agrobacterium fabrum"
                     /db_xref="taxon:1176649"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55750
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtpkely egesrvgmtp dsaqalqklg ydcvieagag kaagfsdday raagvtvvds
       61 adalyagsdi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qqqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvaam kpgsviidla aerggncdlt
      301 vpdqrvvsdn gvivigytdf psrmaaqast lystnirhmm tdltpakdgk pvhnmeddvi
      361 rgatvtyqge itfpppppki qaiaaqkpke rvkeltpeek hakeraefka qtksqvgllv
      421 igtaalllvg lfapasfmsh fivfvlacfi gfqviwnvsh slhtplmavt naisgiviig
      481 allqigsgnw lvvilaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_121659110             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mycetocola zhadangensis].
ACCESSION   WP_121659110
VERSION     WP_121659110.1
KEYWORDS    RefSeq.
SOURCE      Mycetocola zhadangensis
  ORGANISM  Mycetocola zhadangensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Mycetocola.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mycetocola zhadangensis"
                     /db_xref="taxon:1164595"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34272
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrnviiigsg pagytaaiya aranmnplll assveaggel mnttevenyp gfpegiqgpe
       61 lmskfqeqae rfgtevildd vtevsldgdv ktiktgysgd feassvivat gsayrklgla
      121 deerlsgrgi swcatcdgff fkektiavvg ggdsameeat fltkfaskvy vihrkdtlra
      181 skimqerafa nekiefvwns evvgisgena vngvtlrntv dgteshlelg glfvaigndp
      241 rthlfhgqle ltsdgtiavd grssrtnlpg vfaagdvidp syrqaitaaa sgtvaaldae
      301 hylasleqea hhnpeiasav aasv
//
LOCUS       WP_121663501             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Metabacillus litoralis].
ACCESSION   WP_121663501
VERSION     WP_121663501.1
KEYWORDS    RefSeq.
SOURCE      Metabacillus litoralis
  ORGANISM  Metabacillus litoralis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Metabacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Metabacillus litoralis"
                     /db_xref="taxon:152268"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34637
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseekiydvi iagagpagmt aavytsranl stlmiergvp ggqmanteev enypgfdhil
       61 gpelstkmfd hakkfgaeya ygdiqeiidg eeyktvkagk keyktraiii atgaeykkig
      121 vpgekelggr gvsycavcdg affkgkelvv vgggdsavee gvyltrfask vtivhrrdel
      181 raqkilqqra fdnekidfiw nhtvkeihdv dgkvgkvtlv ntqngeeqef ktdgvfiyig
      241 mvplskpfes lgitnemgyi etndrmetrv egifaagdir ekmlrqivta tgdgsiaaqs
      301 aqhyveelve klkvsk
//
LOCUS       WP_121666618             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesonia aquimarina].
ACCESSION   WP_121666618
VERSION     WP_121666618.1
KEYWORDS    RefSeq.
SOURCE      Mesonia aquimarina
  ORGANISM  Mesonia aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Mesonia.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Mesonia aquimarina"
                     /db_xref="taxon:1504967"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35251
     Region          10..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtatkterik cliigsgpag ytaaiyaara dmnpvmytgm epggqltttt evdnfpgypd
       61 gidgptmmiq lqkqaerfgt qvrmgmvtev efskevggih racidnstwv eaetviistg
      121 atakylglps eqrlrgggvs acavcdgffy knqqvaivgg gdtaaeeaty lanicekvtm
      181 lvrkdemras kamqhrvtst knidlrynte vdevigeqvv eglrminnet gekedieitg
      241 lfiaighkpn tdifkdqlem ddtgylitqg kstktnipgv fasgdvqdke yrqavtaagt
      301 gcmaaldaer ylatveseae etekvsa
//
LOCUS       WP_121667399             986 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Mesonia
            aquimarina].
ACCESSION   WP_121667399
VERSION     WP_121667399.1
KEYWORDS    RefSeq.
SOURCE      Mesonia aquimarina
  ORGANISM  Mesonia aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Mesonia.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Mesonia aquimarina"
                     /db_xref="taxon:1504967"
     Protein         1..986
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=109926
     Region          28..985
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkflfrsclr lsiflvlssw aipctgqqqi sgtvtntdkm pipgvnitfk nkpggtstnf
       61 dgqyelnaqa qdslvfaylg yqtqtiavan qtqinitlqe eenslgdlvi nagyyttter
      121 ertgniakvt aeeielqplv splqalqgrm agveitpgnd lpgsaptiri rgqnslraeg
      181 nyplyiidgm pinsapvesn snlsftgidp lstlnlsnie sievlkdada taiygsrgan
      241 gvilittkkg tpgettvqar istgfsevpn qiellntndy lkvrqrafen dgiapnenna
      301 ydllvwdqer dtdwqeeffg gqaeftqanl siaggssttr yringsylnq gsvypggany
      361 hkatgnaqln hkgkndkfsl dmsltygtdr nytvgigavi pqvfslapna prifnedgsl
      421 hweewsqvgr enpfqgypnt sevkthnmvt nlnlsyrlfe klelstnfgy thlnsneltk
      481 rpkesfnpey aefidhesah legqraswii epqlsyqkni gklgikalag ttlqeqlnrq
      541 tgvtgtgyat rsmignlaaa ttlsrginqe tkyrymaffs rlgidwdtky finltgrrdg
      601 ssrfgpqerf anfgaigaaw ifteetwmak qlpwlsfgkl rgsygstgnd qigdygyldi
      661 yeatqgpggl yptrlanpfy sweinkklea aiqlgflkdr lhlnvsyyqn rssnqlvgys
      721 lpsitgfssv qanlpatven rgweieanak vlntrhwkwq salnltlpkn elvsyanleq
      781 ssyantyrvg eplnidllyq yegidpetgy yqiadvnedg rldyedrvvv kdrnpefygg
      841 wqntlqyknf nlqflfqfak kegefalfda grigalrqed ylelegnefq eistqlnair
      901 gynnvtqtal pytdasyirl ktlslsyslp vtplqkigik ncsvfvhgqn lftltnyrgm
      961 dpemalgqgt afgalrtftt gieinf
//
LOCUS       WP_121670620             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium agaricidamnosum].
ACCESSION   WP_121670620
VERSION     WP_121670620.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium agaricidamnosum
  ORGANISM  Janthinobacterium agaricidamnosum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium agaricidamnosum"
                     /db_xref="taxon:55508"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38689
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qvvvqsgagv qasipdeaya aagaqigtaq
       61 eaygcaivlk vrapdagera mmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvlkhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_121673265             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mycetocola manganoxydans].
ACCESSION   WP_121673265
VERSION     WP_121673265.1
KEYWORDS    RefSeq.
SOURCE      Mycetocola manganoxydans
  ORGANISM  Mycetocola manganoxydans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Mycetocola.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mycetocola manganoxydans"
                     /db_xref="taxon:699879"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34154
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrnviiigsg pagytaaiya aranlnpvll assveaggel mnttevenyp gfpegiqgpe
       61 lmtkmqeqae rfgtevildd vtevslggev ktvktgysgd feaasvivat gsayrklgla
      121 deerlsgrgi swcatcdgff fkqktiavvg ggdsameeat fltrfaskvy vihrkdtlra
      181 skimqdrafa ndkiefiwns evvgisgena vdgvtlkstv dgteshlelg glfiaigndp
      241 rthlfhgqle ltldgtiavd grssrtnlpg vfaagdvidp tyrqavtaaa sgtvaaldae
      301 hylasleqea nhnpeiasav aatv
//
LOCUS       WP_121679709             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Falsibacillus albus].
ACCESSION   WP_121679709
VERSION     WP_121679709.1
KEYWORDS    RefSeq.
SOURCE      Falsibacillus albus
  ORGANISM  Falsibacillus albus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Falsibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Falsibacillus albus"
                     /db_xref="taxon:2478915"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34200
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseeqiydvi ivgagpagmt aavytsranl stlmiergvp ggqmanteev enypgydhil
       61 gpdlsnkmfe hakkfgaeya ygdikeivdg eefktvkags keyktrsiil atgaeykkig
      121 vpgekelggr gvsycavcdg affkgkdlvv vgggdsavee gvyltrfank vtivhrrdel
      181 raqkilqqra fdnekidfiw nhtikeinds ngkvgsvtlv stengeekdf ktdgvfiyig
      241 mvpltkpfan lgitneagyi etndqmetkv ngifaagdvr ektlrqivta tgdgsiaaqs
      301 aqhyveelne alkak
//
LOCUS       WP_121690673             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Agrobacterium fabrum].
ACCESSION   WP_121690673
VERSION     WP_121690673.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium fabrum
  ORGANISM  Agrobacterium fabrum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium; Agrobacterium tumefaciens complex.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Agrobacterium fabrum"
                     /db_xref="taxon:1176649"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55794
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtpkely egesrvgmtp dsaqalqklg ydcvieagag kaagfsdday raagvtvvds
       61 adalytgsdi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qqqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvaam kpgsviidla aerggncdlt
      301 vpdqrivsdn gvivigytdf psrmaaqast lystnirhmm tdltpakdgk pvhnmeddvi
      361 rgatvtyqge itfpppppki qaiaaqkpke rvkeltpeek hakeraefka qtksqvgllv
      421 igtaalllvg lfapasfmsh fivfvlacfi gfqviwnvsh slhtplmavt naisgiviig
      481 allqigsgnw lvvilaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_121697882             944 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Heminiphilus
            faecis].
ACCESSION   WP_121697882
VERSION     WP_121697882.1
KEYWORDS    RefSeq.
SOURCE      Heminiphilus faecis
  ORGANISM  Heminiphilus faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae; Heminiphilus.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Heminiphilus faecis"
                     /db_xref="taxon:2601703"
     Protein         1..944
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104156
     Region          42..943
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 miskykiill aalgssvcag dayaaseesa dslnaenqiq layrtidknd vlggvevldv
       61 ealmqknyin eisnstisgy vsgfngnslw gmdadndagf lvlidgvard mnnvsstevq
      121 sitfmkgaqa tvlygsraak gviyittkrg hegplrinvr antgwhvaks mpeylgsaey
      181 mtlynearan ddlgpaytad qiyntatgtn pyrypdvnmy sseylkkvyn rsdatveisg
      241 gnqrarfytn inyyrlgdyl nfgeaknnyt drfsvrgnid vniaewvkay vnadatfyga
      301 rsahgnywes astfrpnrit plipismvnp daveslglin gsnnirdgyf lagtqidptn
      361 ifadylakgy tkftsrqfqf dagvnldlgm lakgltfgtr fsvdyatsyn tsytdsyatf
      421 ipvwsnfngk deitsvnkeg kdehsgvqnv tgsasrqtls wsgqfdynrt fadvhnfhal
      481 alaagwqrtv ageyhrvssa nigfevdyny dhryyadlsl vglhsaklap ghrqgwspsa
      541 tlgwrisqed flidnpvvnn lmlsvsasdv ksdmdipgfy lysthfttgg wyswggsggq
      601 aaayparggn pglgyisrke ftasvrgtff nnlmdvnaqf ftykmdglvi nnsskfptff
      661 styypassla tylnndantr tgfdfgvnlk ktvgevdlqm gvtgtyyktk askrdeirey
      721 ayqyregkai dgiwgykclg ffatdeeaaa vdqsalgssn lkagdlkyad inndgkinqd
      781 dqvmlakggw ygapffmgvn lsakwkgfti fvhglgsygg hgmlndnlyy kmvgdnkysa
      841 marerwtpat aatatmprlt ttngannyva sdfwlystdr fdidkiqlty dfpssiihgi
      901 vkglqvyvsg ddlltigknr kimemnvgsa pqsrfyniga kvtf
//
LOCUS       WP_121698461            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Heminiphilus
            faecis].
ACCESSION   WP_121698461
VERSION     WP_121698461.1
KEYWORDS    RefSeq.
SOURCE      Heminiphilus faecis
  ORGANISM  Heminiphilus faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae; Heminiphilus.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Heminiphilus faecis"
                     /db_xref="taxon:2601703"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115157
     Region          23..1042
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklflffva vmaalmvsaq tmrtvtgqvv saadgealvg atvmpigggq gtstdmsgef
       61 rlsvpdnvki lqvsyvgmet vkaeikaghm tialrstdns ldevmvvayg takkssftga
      121 astisssaie klqvsnvska legaapgvqv amqsgqpgts atvrirgigs insssnplyv
      181 vdgmpyegni aainpndieq invlkdaast alygsraang vimistkkgr dqknkvtfea
      241 rigsnsrgip nydiitdpgm wmttqwtvlr nraiaggate aeagaqasas lygnvgynpf
      301 rcdnnaivda ngnltsapll wydnwsdeai snglrqeynv avqggnergt hflslgwled
      361 egiiknsdfs rlsmrasgdy lvtkflking nvsysrgvqn slnisslsny sntfafiqqv
      421 apvypvyayd adgkriyaed gspvfdfgsg qygtrkyapn snvvasdkan qnkvltdnfa
      481 srfgvtldiw nglkfqangg ydvtntqqdr fmtptfgdaq nvngrgykyr trletytvne
      541 lltytntfad khnidvlagh enykmkynyl nasktnffdp aipefdnain mdnissytdt
      601 ytveswlgrl nydydnryyl sasvrgdgss rfakgnkwgt fwsvggswrl sqeeffkgvt
      661 wvdnmsiras ygsvgnddiy ypmtttsnyy psktqygvsn sdgqfavsky yegnpditwe
      721 tsynfnagvs allldnllni dieyfnkrtk dmlynvpqpp ssgvsyisrn altmvnrgie
      781 ftltvnvplp tdfmwswtft gthyknkvtd ipvdkqvegi thdayynire grsvwdfyyy
      841 rfaglddsgh atwyrdqtda dgnvemvpvt dytqatkyyi gtaipdfqgg ittnfawkgi
      901 dfsiatnyqi ggdiydamya gmmhagsmqg ynwhkdilna wtpqntdtdv pvldgsqnan
      961 tfsdkyliga dyfnlrnitl gyslpsawlr kaylekarvy vaadnvalfs rrkgldprqy
     1021 vygqsqanys airtvsfgls ltf
//
LOCUS       WP_121698711             994 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Heminiphilus
            faecis].
ACCESSION   WP_121698711
VERSION     WP_121698711.1
KEYWORDS    RefSeq.
SOURCE      Heminiphilus faecis
  ORGANISM  Heminiphilus faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae; Heminiphilus.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Heminiphilus faecis"
                     /db_xref="taxon:2601703"
     Protein         1..994
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110144
     Region          32..992
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mknfnlrell pafrivlcll lcgitpalwa qqqvsgtvid senepvigat vwekgtkdnr
       61 tvtnadgrfs isvqpgavls isyigyktve vtanngkplh iamneeshml ddvvvigygs
      121 iskkevtsav shvsgkdmlq igngnpamqi qgkvpglsve nstgadpnss vsmqvrgvss
      181 rnaglgplvv idgvpggsld ninendiesi dvlkdgaasa iygtrgsngv vvittkkgav
      241 dgnvhtsysg finitdpire ldvlsadefr kynrgddyga ntdwfksisk tgvshshtlt
      301 vsggtsrtny ratvdykdtd gidlragkrq vgarmtvnht gkddlykiil nvtprnvkyn
      361 nadydafrea iminptipvm dkdnpgkyty itayatnnpv erlkieqngg ertflnwdgt
      421 lkvnlfpalc kderhslstq itlaqqiiqn dyswfrpsts tvaqesgfdg eakrsydknk
      481 qqslewlvny gfsnaknrva fmggysyqyf vndglsaenk dfasdllgad nlgagaymga
      541 tagrkgmssy rndskliaff grlsysfndr yfltasirhe gsskfgannk wgnfpavsag
      601 wrisqenfmr ginwindlki radygetgnq dfasyqslat masydlifyk gqyiqgwgin
      661 snpnvnlkwe kgknwnagid fsllnykleg svnyynrkqs dllgtysvpv ppnviansyv
      721 nvgtmkntgi eielrynavr tkdfdytlsf igstsdnkfv sfsnrlyegq kfywmdgfpt
      781 ypgnpgpvqr ieegqrvgnf ytfryagvdd ngnwlvydks gekipvsqgt dadkcvvgng
      841 mpeftasltn nfryrnldlt lyfrgafgyq iydaqdlyyg vmgaapgtnv lksaysenah
      901 itegknvhss yfvhdgdfvk ldvatlgytw kinryiekvr fyltgrnlfs irsynrglap
      961 daycvnglqp gipysktgyy pstrqylfgv qidf
//
LOCUS       WP_121699246             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Heminiphilus faecis].
ACCESSION   WP_121699246
VERSION     WP_121699246.1
KEYWORDS    RefSeq.
SOURCE      Heminiphilus faecis
  ORGANISM  Heminiphilus faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae; Heminiphilus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Heminiphilus faecis"
                     /db_xref="taxon:2601703"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33751
     Region          6..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttentkcli igsgpagyta aiyasranis pilyeglqpg gqltttseve nfpgypegvm
       61 gaqlmedlrk qavrfgadvr tgiitkvdfs nrpftltsdd gtiikadtvi vatgasaryl
      121 glpdeqrfsg lgvsacatcd gffyrgrtva vvgggdtace eamylsnlak kvylivrkdy
      181 lraskvmqqr vmtkenikvl fntqtrglsg teflerahlv efagtdneke ldididgffl
      241 aighkpntdi fkgqlmldeq gyivlsghdq stsvegvfaa gdvadpnyqq aitaagtgcr
      301 aaldaehfll ehqs
//
LOCUS       WP_121699796            1105 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Heminiphilus
            faecis].
ACCESSION   WP_121699796
VERSION     WP_121699796.1
KEYWORDS    RefSeq.
SOURCE      Heminiphilus faecis
  ORGANISM  Heminiphilus faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae; Heminiphilus.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Heminiphilus faecis"
                     /db_xref="taxon:2601703"
     Protein         1..1105
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123109
     Region          23..1104
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekrllllls gliigiglfa qvkvtgvvls asddepliga tvsvkgtkta vatdldgkft
       61 itapstnsql evkyvgmktv tvkvqgtpmh ivmesssqel eevvvtgmqk mdkrlftgaa
      121 tkvdaqqari sgmadisrsl egraagvsvq nvsgtfgtap kirvrgatsi ygsskplwvv
      181 dgvimedvle vsadelssgn aetlissaia glnaddiesf dilkdgsats iygaramagv
      241 ivvttkkgta grnsinytge ftmrlkpsys tfnimnsqdq mdiyqelakk gylnyaeian
      301 asssgvygkm yqllseydat tgqfglpntp earaaylraa eyrntdwfde lfstsvmqth
      361 svsissgtek aqhyvsasam ydpgwykqsr iqrytanlns tfnisdkvsv nlisnasfrk
      421 qrapgtlgsd vdmvsgevkr dfdinpysys mntsrtldag efytrsyapf nilhelknny
      481 mqlgvndfrl tgiltykpir kvelsllggv qktttqqehf itddsnqaqa yramptaair
      541 dknpllytdp dnvyalpvti lpnggiyera drdmfkwdmr aaaryndvfn edhivnlyag
      601 metnsvdrhs twfrgwgmqy smgeipnyay qafkrgqeen tpyysltnah qrsvaffgnv
      661 tysyksrytf ngtlryegtn qlgksrssrw lptwnisgsw nlhneswfer fvptwshmtl
      721 rasysltgdr psisnaysil maanpwrpfa gvgesslyid dlangsltye kkhelnlgls
      781 tgvldnrinl efdwykrnnf dligvattqg iggqitklgn iaemkshgve lslttrnivt
      841 rdftwttnfi ysynknevtk letskrmfdl isgngfaqeg ypvrslfsip fkglneeglp
      901 tfldqdgnis ttgiyfqtsd peklkfleys gsidptdigs fgnifrykgl tlnvyitysf
      961 gnvirldpvf rneyddltat pkefknrwgv agdenrttip tiaskrqnkn dsnlsyayna
     1021 ynysteriak gdfirmkeis vnydfpqkvl nalrlarlsa klqatnmfli yadkklngqd
     1081 peffntggva aptpkqftlt vnlgf
//
LOCUS       WP_121700059             999 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Heminiphilus
            faecis].
ACCESSION   WP_121700059
VERSION     WP_121700059.1
KEYWORDS    RefSeq.
SOURCE      Heminiphilus faecis
  ORGANISM  Heminiphilus faecis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae; Heminiphilus.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Heminiphilus faecis"
                     /db_xref="taxon:2601703"
     Protein         1..999
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111135
     Region          22..998
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkklflmlcg llmvavvsaq trtvsgtvva aadnepliga tvvpvgggsg tatdidgkfh
       61 itvpgsvkev kvsyvgmktv tlpltdgmvv klemsdnrld evivtgygtg kklgsavgsl
      121 nvvnedvfan spapnfvdal qgqvpglsif sntgepsatp anirirgvns ldasntplfi
      181 ldgapvtssv fttlsmndie svtvlkdavs taiygsraan gvivitskkg kfgqkakvtv
      241 ranvgwsspv enkikmmnsq qyiefrdkin qpvtaevrel vekygistdw qkemikdnam
      301 tyslegqvsg gsdnlsytis lnhydqdgli assgmrresl rasleskvnn wlrigfqgnl
      361 gyreyetnsa aaadgtfytn npivqsymmm pydspyyyti engdivygdk avwykytgdg
      421 danwltklnk gkrssvtanl llsevitpik gltirsqqal daydyrnssi wtavdnfvtp
      481 mgdvtdfgqy ttrqrgesfe ryysfvytnt aeyrfsinnl hnisvlagqe siinksnqfn
      541 vattgqpnns qmlltngtdi dlknnvgqei eettinsyff nasydfdnry fldfsirrdg
      601 sskfapdhrw stfwsagvmw naksesflqp ytwiddlkfr vnygttgnsg ignykyfgti
      661 gsgnlynggn tlilgqapny dlkwetvrsf dvgfsfgfld klygsadfyv kntedmlmei
      721 pysfttgyds gsgnigsmrn tgvdvelgah iiktrdwywg vrvnfnynkn eitglfngkq
      781 fysmpdygly yeigkdanql rtvmyagvdp rdgqqmwydk dgnltkefnr erdavstgks
      841 fiapwtggfg tnlrwrnisl sadfnwaaek yifnwahqmv saayratstn qcvdmlnvwt
      901 kpgditdipn adqqpqadsr ylenssfvrm knltlqydfe kklinklgvq glalhftgrn
      961 lltftpsgyt gtdpeyenng vrfsypntrq yefglevtf
//
LOCUS       WP_121717683             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. E5N91].
ACCESSION   WP_121717683
VERSION     WP_121717683.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. E5N91
  ORGANISM  Streptomyces sp. E5N91
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Streptomyces sp. E5N91"
                     /db_xref="taxon:1851996"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53349
     Region          13..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtghqsahrp prrvgvvaes lpgekrvaat pstvrlllgl gyevvvesga gaasgfgdea
       61 yaeagagvge awaadvvlkv naptadetaa lrdgttlval lapaqrpell ealsargvta
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaavg aasslgaivr atdprpevad qvrslggeyl avdmaqeesa dgyakatsad
      241 ydraaarlyh eqardvdvvi ttalipgrpa prlltaadva amrpgsvvvd maaaqggnve
      301 gtvagrtvvt gngvtvigyt dlaarlpaqa sqlfgtnlvn llrlltpgkd grividfddv
      361 vqrtvtvvra gtvtwppppv avsaappata ppaaspaapv ggrprlltpa grfgliglgm
      421 latfllvafa paqlaqnftv falavvigyy vigkvhhslh tplmsvtnai sgivvigalv
      481 qighestlvt vlsfvaillt svnifggfav trrmlsmfsr ggsr
//
LOCUS       WP_121726378             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter labetoulli].
ACCESSION   WP_121726378
VERSION     WP_121726378.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter labetoulli
  ORGANISM  Helicobacter labetoulli
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter labetoulli"
                     /db_xref="taxon:2315333"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33164
     Region          3..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 midvaiiggg paglsaglya trgglknvvl fekgmpggqi tgsseienyp gvkevvsgmd
       61 fmepwqeqcf rfglkhkmse vkkitkdngi fgihladgsv eqakavifaa ggspkranlk
      121 geneywgkgi stcatcdgff ykdqevvvlg ggdtaleeai ylsricskvh lihrrnefra
      181 apstithakn nekihfitpa vieeilgdss gvsgvrirht dsnetevisv yglfifvgyd
      241 vntatlkqdd gsmlcecdew gsvkvdlsmk tsveglfaag dvrtqaskqv vcaagdgata
      301 alsaiayleh k
//
LOCUS       WP_121727843             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. 1608163].
ACCESSION   WP_121727843
VERSION     WP_121727843.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. 1608163
  ORGANISM  Acidovorax sp. 1608163
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Acidovorax sp. 1608163"
                     /db_xref="taxon:2478662"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38362
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mfigvpaetv agetrvaatp etvkkltalg hslrvqsgag laasvtdaay eaagaeitda
       61 agawgaplml kvrcpseaea pwlrsgttlv gmlnpfdaag lqrlaaagvt ayaleaaprt
      121 traqsmdvls sqaniagyka vmiaadryqr ffpmlmtaag tvkaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvsgy arpmppswle
      241 rqkmevakrv aqadvvitta lipgrpapvl vtpemvqamk agsvivdlaa pqggncplte
      301 pgstvvkhgv tlvgetnlpa lvaadassly arnvldflkl iinkegalhv dmqddivaac
      361 lmahegtlkr a
//
LOCUS       WP_121732521             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas prosekii].
ACCESSION   WP_121732521
VERSION     WP_121732521.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas prosekii
  ORGANISM  Pseudomonas prosekii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas prosekii"
                     /db_xref="taxon:1148509"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38582
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag vtasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vfnkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_121735003            1056 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides distasonis].
ACCESSION   WP_121735003
VERSION     WP_121735003.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     Protein         1..1056
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115209
     Region          42..1055
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlknfkpisl ilcmgalfls ggvyanivpv eqgtsisqqa gkvigtvedd fgpvagasvv
       61 vkgttngtit dmngnftleg vkngdviqvs figystievt ysgqslgvik laedtqklde
      121 vvvtalgikr ekkalgyatq elkgdelvna resnianals gkvsglqvvr sssgpggssk
      181 ivlrgnnslt gsnqplivvd gipmdnftgg vddawgnsgv dmgnglsdin pediesmnvl
      241 kgasaaalyg sragngvili ttksgkkqsg lgitvnagvt vesmflkpel qniygqgtng
      301 iynvkdrssw gpiadgsvti drwdgqkvqm ytydnidayf qkgtsfnegv sfqqsydgta
      361 vfasinrsdd kgivpgasln ktsltlrgts efgpdkrwkl dakanylnnn aknrpiqgin
      421 qsnafstiyn lprsldirdl encldengnm iwwdtestpq enpywikdyr tnqdsrnrll
      481 gtislsykit dwwnlelkgg tdyytttttn kvysggnvnp kgrysekset fyennysfls
      541 tfkkdnlfsk fggfvtvggn lmmqrrkkle agtgdllipn lfsmsnaadk nnmthtsedv
      601 qrkmnsiygs lqmnwdgwlf lditarndws stmskenqsy fypsvslsgv isdmvekvgg
      661 tmpewmsfak irasyaevgn dldpyqlytv fkvdkdpngn ptaalgttly dstvrselik
      721 sweagidlkf fnnrlgidaa wyksnatrql ldlamdpfsg yskrkinagn iqnsgvelml
      781 ygtilqnpkg fnwettlnas fnknkiidly dgvneygikt fddlkivart gsyygdiygk
      841 kfqrvesgeh agkiivdaqg lplvtsddhy lgnqqpdcml gwtnsfsykn islsflidar
      901 iggniysatt anlykagnaa gtvingtrse fvvpnsvvsd gnggyttntn avtpelywgr
      961 aaggnigvge aflydatnir lrnitvgydl ekkwlektpl qkvrvsfvan nvwmivnhle
     1021 gidpesisat ntnatgfeng saptsrsftf nvtvgf
//
LOCUS       WP_121735004            1142 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides distasonis].
ACCESSION   WP_121735004
VERSION     WP_121735004.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1142)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1142)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1142)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1142
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     Protein         1..1142
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125442
     Region          42..1141
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mlknfkpvsl ilvagamalp tsayanlipe kldvsisqqs gkvagtvedd fgpvagasvv
       61 ikgttngtit dmngnfsldg vkdgdviqis figystqeiv ykgqalsikl aedtqkldev
      121 vvtalgmkrs ekslgyamke mkgdelntnl inpvaalqgk vagveisgsd ggmfgsskvq
      181 irgastlgkn nqpiyvidgv ildnsikegn pdwdsnpndy gnelknlnpd dfesvsvlkg
      241 aaatalygsr glngaivitt ksgksgqglg invsqsfgmd aitqtpsfqn efgngiiagn
      301 vsygdkdang nyyiydnfgq yptnaegqfs lmndqgmswg pafdgrdvqy ydgstraysp
      361 vknnfrkayq kgfssntnva isggnekttf ytslsykhvd gttpnnsfdr lsflgkathm
      421 ihpkvkleas mafanstpkn spinlgenfa ngvwgrsydp stakdkykgs hgglanskyg
      481 dewgnmpgkd twwnvyenef rqketsvrpn vklnidlldw lkfnvegsyn yyytryeekk
      541 pgsgyanegg yyglsqttke qsnlnanfmf nktfgdftvn gfirgeyyen fqqaqsmntn
      601 ggliapnqyf ienskqtpay kakiqdrkkm lsvafqagvs wkdqffldvt grndwssalv
      661 yadghgtysy fypsvngswl itstyrdqlp ewisfakvrg swaqvgndts pyiinsayni
      721 ntstlggtny ygmslpetmy dqnlkperkn aweigldwrf lnnrigldat yykentknqi
      781 meisvpsvsg ikkqmvnagn iqnkgvelal ntipfqnkdw ewtldftwtk nmnkivelhe
      841 nvadyivlag diaygnyrvg svakvgsayg tlmtdsyykf dessglpmlv wtdgtrrshy
      901 lrneaeivei gsmipdflgs vstglkyknw slsialdmrf ggkvasynsr ygtaygymee
      961 slkgtpghgg iswtskydgk tyndgiipeg iipsgtqitq pdgsiytvgs ggvstagqsy
     1021 qelinqgvie pthasawtyr nnawtmagrn ygvvndswvk dlnyialrdi slsyrlpnta
     1081 cekfkakhcv ltlnghnlgy llnslpnnin pesvsgtaaa efrirsltgv tssftftvnv
     1141 gf
//
LOCUS       WP_121735079             988 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides distasonis].
ACCESSION   WP_121735079
VERSION     WP_121735079.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 988)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 988)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 988)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..988
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     Protein         1..988
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=108119
     Region          1..987
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkskevvvsp nvnvtlmsdt qnldevvvta mgiskekkal gyavqdvksd eltqgantsl
       61 sgalqgkvsg idiasssgmp gasskimirg arsftgdnsp lyvidgmpia stadvntdtm
      121 nngsvsgady anravdldpn diesinilkg qaasalygmr asngvivitt ksgkgarkgk
      181 pqisfntnla fdkvstlpel qteygqgneg aynpysgfsw gpsisdland pvyggnvqne
      241 ytkgglhngq yyvpqraaag ldpwatpqay nnakdffqtg vtwsnsvnva qsfdkgnysf
      301 slgnttsdgi vrstgidryn vklsgeaqlh dnwttgfngn fvtskikkqg tandgvtatv
      361 ytapisytma gipshiegdp ytqntfrenw iddgnwacdn nsftersqrf fgnaflkyst
      421 kfgtdnhkld vkyqigdday ttnysdiygy gttgytngya seygftvnem nslltftynw
      481 ninedfvfda llgnelvdkr isntqavgys fnfpgwnhln nasvfnsshe ykrkrtvgnf
      541 aslslawknm lylnvtgrnd ivssmprdnr sffypsvslg wvftevealk ndiltfgkir
      601 gsyaevgmag eyvpsyyytp gygggffqgt pimypingnm ayipyfvvyd pnlkpqntks
      661 yelgadltfl nglvslnyty srqnvkdqif evplagstga ssmmmnggkm hsnvheitlg
      721 ispvdtknfk ldfafnfski dnyvdelapg vesimlggfv tpqvragigd kfpviygvgy
      781 krdgegrivv nekgipeage tqvigkvspd frlgfntnie lykfrlaavf dwkqggqmys
      841 gtagetnfyg tsklsgevrk sdkyhfdyaa veqkgvdadg kpvyvpytgg vkgsdaeeyf
      901 ksvrgideay vydnsflklr elslsypvyk kdnlnvnvnv farniivwse ikgfdpeatq
      961 gnnnmagafe rfslpgtssy gfgvnvnf
//
LOCUS       WP_121735049            1066 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides distasonis].
ACCESSION   WP_121735049
VERSION     WP_121735049.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     Protein         1..1066
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=117593
     Region          24..1065
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkrltflllc lfigigvata qtmkitgnvi ssedqqpvig aavvvkgtti gtvtdfegnf
       61 tldvpgdakt ifisyvglkt kevavapvvn vmldsdskal devvvtamgl trekkslgya
      121 lqevksedit kagqmnvans lsgkiagvqv taqggqigas qnivirgnss fgnnqplivv
      181 dgvpmtndnp tgsavilgsg lndintedie sisvlkggsa alygmragng vilittksgk
      241 kdkgisvsyd gditmdriyn lpglqnkygq gyygsefdwk asgfdgsyqd fassmgysyv
      301 dgngsgindn adeswgprld iglqlpqfns pvvngvrqat pwvsqpnnik dffqtgysts
      361 htisltaate ksstrasisy rgqegttpnt dmqryaasln tkmnfnkyie fdlsanyvrt
      421 tsgnlpgtgy dganvmqsll qwhgrqidmn dlkanwdqkd etgaythynw qksyatnpyw
      481 vlnknlnkyk rdrmfgkssl wykptdwlkf egrvgldtyf ssqlsniews idypdgyfrd
      541 ydrrttevna dfiayfnkqf gdfqvnalag anyrdydyfi ktigadeltv pglytvanak
      601 gsvyasenhe trrsnsvyan asigwrnqay vdisvrndwd stikdaffyp sfsaswimte
      661 tlpsltesgw lnflklrggw akigsatdpy lsnayysvls apfngtslyy npitfpathl
      721 rpemvktwev gveanflrnr lhldvayyqk tttdqimqar vstatgyrsm minageisnk
      781 gvelqvsgdi iqnkdgfnwt atlnwskdks kivelytdpi tgesldayei gsswscynya
      841 kpgkswgtlv gtgfvydedg ailvrdgmpm yeenkeigdv apdwlmgfnn efsyknwsfg
      901 flldfrkggd vysisqafgt ytgiydftae gdlrekgvva gqnvmtdkvf knedgsinnt
      961 avsaedffgn yyticemavv dgsflklrea hltynfpqsi lkktkylkaa hvslvgtnla
     1021 llwvhksnqi hldpesttga ananvgfesn syppsrsfgl kvgvtf
//
LOCUS       WP_121735113            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides distasonis].
ACCESSION   WP_121735113
VERSION     WP_121735113.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=111006
     Region          23..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrksfillla fflcvtgyaq kltisgvvid kdlnepltgv nvlvkgtttg titdfdgkyt
       61 leadansilv fsylsmktie epvngrtkid vtmvsdaeal devvvtamgi kresktltys
      121 aqtvggkdln eiknvnmins lqgksaglqi tpnstgaggs skilfrgnks isgsnqpliv
      181 vdgvpmmmnv sdsqidgsyg gsrdggdams tinpddiaqi tllkgasaaa lygavaanga
      241 imvttksaqs gkvainvssn ttvetpmvlp kfqnsygvsn qgtfswgdkl asaspnyakd
      301 yynlgyttnn sislaggndn issyfsyanv ssngivpent ymshnllakv gfnlwtklhv
      361 dvsarynnqh ienqptagyv gnptlgaylf prgedwdyyk ssyevydgtr ninvhnwtnt
      421 aqeqfsnpyw mlnrqkpvsy rnryefggsv kydimeglsv tgrlryergd etwnlneyas
      481 stagrnllgt mkdtrvnseq tygdllaqyn ktwedtysls vtaggsyqkt knssleligw
      541 gdsqfsvnda gvitsgayyp nifspanyyk lqttktlaek rlnsvfataq fgykeglfid
      601 vsarndwsst laftdgvsff ypsvgasvll drfvdfgknv dlfklrtsys ivgndvpigv
      661 tnerytlgdq galnppekss frtlkpektn slevgfdgtf fqnrfnvnlt yyktntknqy
      721 fdisapwetg lksryinagn vqnqgfevsl gwynqftdnf swstnfnfsy nnnkiielad
      781 elsewnltsy ctgakvllke gghfgdlyvr dlqrddngkp ivsdtgapvl agsdnkdlvy
      841 agdmnakvnm gwtntfhykd ftlsflidak vggkvlsmte atmdgwgvse rsglardagf
      901 vevdgaqfdp qlyysttggt synsniltsq yvydatnvrl relsfgytfr nlfgagknlt
      961 asiigrnlff fykdapmdpd vaagtgngwq gidmfalptt rsfglnlkln f
//
LOCUS       WP_121736337             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Parabacteroides distasonis].
ACCESSION   WP_121736337
VERSION     WP_121736337.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33791
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdsvnekvr cliigsgpag ytaaiyasra nlspvlyegi qpggqltttt evenfpgypd
       61 gitgpelmed lkkqavrfga dirfgiataa dlgeapykit idgekviete tliiatgasa
      121 kylglpdehk yagmgvsaca tcdgffyrkk tvavvgggdt aceeaiylas lakqvylivr
      181 kpylraskvm qervfktpni tvlfehntlg lfgengvega hlvkrmgepd eekvdiaidg
      241 fflaighkpn sdifkpwvdt devgyivtvp gtprtkvpgv faagdvadph yrqaitaags
      301 gckaaieaer ylseigk
//
LOCUS       WP_121737472            1011 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides distasonis].
ACCESSION   WP_121737472
VERSION     WP_121737472.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides distasonis
  ORGANISM  Parabacteroides distasonis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Parabacteroides distasonis"
                     /db_xref="taxon:823"
     Protein         1..1011
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=113160
     Region          57..1010
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mekssktskl lclgllkpsv mllttgflsm afspalasve pvvdlgpkme svtqkgktit
       61 vkvsdsmgel iganvlvkgt tignvtdmsg vvilqdvpeg ailevsyigy vtkevpvggs
      121 slvsvtleed sqkldevvvv gygsmdkkqv tsaitsikad dlmvgvsgsd istalqgkig
      181 glvmnnlgsa ngatsfqlrg mtsinsgksp lividgfpgg dirsltqedi ksidvlkdgs
      241 agaiygtraa sgvilittks gsntdgkvkl tysteltkkq nynapemlsg reyaeygigt
      301 dygsdvnwwd eminknnfsq khhlalelgt ekaqvytsff yeknegiain dsrqdfggri
      361 nasfklfddw levrpavdyr qaarnnkfpn fqqamrnnpt rspydadset gynvwtnesl
      421 dynvvadsyl rdyygldkwf kpevtlklni kpvpglsfqq ilgyenrqwe nhtynpsthr
      481 keieesrkga aylgfskten ltsegyftyl kefkgghsin atagysyfek ngegfnmtny
      541 nfsvdgikyw dmnqgsflrd gkaamssskd iseklfsvfg rvnysyndky masasirheg
      601 sskfaadnrw anfwsvtagw risneefmke idwlqdlkvr fgygvtgnnd fdasymanll
      661 gsdtnwmlpn gvwaysygkt qnvnanlgwe qkkewdlgvd ysffegrlyg kfdyyrrkid
      721 nllysvkvpq ppytigtqyq nigsmeskgw efevggdiir tkdftwtsni nmshntgkil
      781 tlwgnntyyn gngfvapgtp gdaarmeegs tigsfflwkf agfdddgnfl lynkdgevip
      841 aadktendkq ymgnytpkli lawnntlsyk nfdlginmrs widfdvynti nmyygiqgrg
      901 ntnvlkdayg kfnhikgekq icdyyledgt flkidaitlg ytlpmkkytn nlidririya
      961 tvgnvctitg ysgmnpevki dgwdkgtekf wdveyfyplt rtytlglqfn f
//
LOCUS       WP_121739359             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Alcaligenes aquatilis].
ACCESSION   WP_121739359
VERSION     WP_121739359.1
KEYWORDS    RefSeq.
SOURCE      Alcaligenes aquatilis
  ORGANISM  Alcaligenes aquatilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Alcaligenes.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Alcaligenes aquatilis"
                     /db_xref="taxon:323284"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33806
     Region          8..318
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msttkhakvl ilgsgpagyt aaiyaaranl npvlvtgmeq ggqlmtttdv dnwpadaqgv
       61 qgpdlmarfq ahaerfetel ifdmvssadl strpltlngd sgtvytcdsl iiatgasaqy
      121 lglpseqefm grgvsgcatc dgffyknqdv vvvgggntav eealylsnic ktvtlihrrd
      181 tfrsepiltd klmdrvqngn irlklhselq evlgdasgvt gvriinkqtq atedlavtga
      241 fiaighkpnt gifegkldmh dgyittrsgl kgmatmtsvp gvfaagdvqd niyrqaitsa
      301 asgcmaalda qrwldenk
//
LOCUS       WP_121748008             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_121748008
VERSION     WP_121748008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34145
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgim
       61 gpelmdnmra qaerfgaeli pddvvavdls geikkvtdta gtvhqakavi ittgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkisfv wdsevaevqg dqklsglklr nvktgelsdl avtglfiaig
      241 hdprtelfkg qldldpegyl kvdapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaalt dedkaepekt tv
//
LOCUS       WP_121756546             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter felis].
ACCESSION   WP_121756546
VERSION     WP_121756546.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter felis
  ORGANISM  Helicobacter felis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Helicobacter felis"
                     /db_xref="taxon:214"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33208
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midlaiiggg paglsaglya trgglknvvl fekgmpggqi tqsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemva vvhlslegeh yrihledgns learavilct ggrpkrtgik
      121 geaefwgkgv stcatcdgff yknkevavlg ggdtaleeai yltkmcskvh lihrretfra
      181 apvtlehakk npkiefitpa vveeikgdvg gvnalsikdl ktgavrelsv pglfifvgye
      241 vnneilkqed gsmlcacdsy gsvlvdlsmk tnlkglfaag dvrtqaakqv vcaagdgata
      301 alsaiaylda hs
//
LOCUS       WP_121763961             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter burdigaliensis].
ACCESSION   WP_121763961
VERSION     WP_121763961.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter burdigaliensis
  ORGANISM  Helicobacter burdigaliensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Helicobacter burdigaliensis"
                     /db_xref="taxon:2315334"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33765
     Region          4..309
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mlelaiiggg paglsaglya trgglkevvm fekgmpggqi tsssemenyp gvaevksgfd
       61 fmqpwqeqcf rfglkhemae vkyikrkdsh fvlvlsdgke veskavivat ggspkrsgvk
      121 gedtywgkgv sscatcdgff yknkevvvlg ggdtaveesi ylakicskvt lihrrnefra
      181 spitlerakn epkinfltpy vieeicgste agvtglklkn ledestmdlk idgifvligy
      241 nvnnkvlmde ngnsicalde ygqavvnlkm etnipglfva gdlrkdapkq vvcaasdgat
      301 aalsaieyve hhk
//
LOCUS       WP_121765156            1205 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121765156
VERSION     WP_121765156.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1205)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1205)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1205)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1205
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..1205
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=136920
     Region          113..1204
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkikfalmf illlctlqqi waqdkkisfd fqnepmpsal rkiaqtynqk isfshedisl
       61 ykanasvhak dvqdalrqtl vgtpllfkek gefitvfldp tsteaikrkn lcvitgsvhd
      121 elgdplpgat vtithesqqw ggstdidgnf tvyaprpiie kekcfiqasf igfkkerlai
      181 npqklniklv lqtssneine vvitgygnid arrntsaits lkmddilmpg mtsieqaleg
      241 rvpdmifman sgevgatarm rirgtstlvg nreplwvldg ipltdpvdvt teqlndpdyi
      301 nyignaisgi npqdieridv lkdaaataly gtraangviv ittkkghiga psinysgelk
      361 iiarprytdh ninlmnsqer vqfgkdlcdl hyafpaqmsm vgyegayydy ikgnttfdef
      421 qnqvrwfenv ntdwfkilah dalthnhtls vsggnrstry yaslgytsed avvrtqyndr
      481 ytgtlnlqst inksfqvnfr mngniakkny lpseidalgy aynttralpc ynpdgslyyy
      541 krhaynierk edssykynyn iinemnnmsq tydsnqlita ldlqyryehi ldatmtmsyq
      601 rsasttetwy gektnyiahl kngeledtpl kgddgkcalp yggvlntsnn itdnitfraq
      661 vnyhqgvgan qkhllganlg yevsayknkg ftdqtrgyfk ergmkyleem tleeilqypd
      721 yaqwtiqphr tvqstktnki sgyltmtysy dnyftvnmng rfdasnkfgs rsnkkflpiw
      781 svsgmfnike tlcknfeaad emrlrfsygk tgnmvdgqtp nlllrqgsmn yyfgenyakv
      841 yaypnpnlrw eqtdeynlgf dlsffqnrlt igsdfyykkt kdafttvpvs tvnglseyvm
      901 nggditnkgf siylsgypir neewqwylst nyslykntvn ndvinnykid dylngtaivg
      961 gesigtfysy eflglnptng vpmfddyndr rhllenksle divktvlvks gtrepkfngs
     1021 lystltwkql slstnftynl gnkirkfaly sdivkgvsse nnvrkefvnr wrvpgdehkt
     1081 vypslispsd pqysnyinhy saqggnfsni pkyadnlwsm ydysnirvvs gsyfrlssls
     1141 lryrftpkml qktpfktasi nfstnnvfti cskeldgqdp sqsgfsttta lsirpsytmg
     1201 vqvsf
//
LOCUS       WP_121765316            1173 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121765316
VERSION     WP_121765316.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..1173
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=131690
     Region          32..98
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          117..1172
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mndrrnsffr lfllillcmg vqslgaqtvt kvfkneplka vlkeverqtk ysiiyktdev
       61 nenkkitasf qqatvnnvla avldkdveyk lqnrmiiitk ktvrniaaap sqslhrvtgk
      121 vvdvngepvi gasvqvvgqs mgtitnldge ftlssvpvna vvvvsyigfe kkeikvpelq
      181 kssrvmlred tatleevvvi gygtqkkinl tgavavvdsk tmedrpvpra sqmlqgtvpn
      241 mnvtfgsgyp gasatinirg vnsisgnasp lvlidgiegd idrlnpndia sisvlkdass
      301 aaiygarasy gvilvttkeg sarkttvsyd gryswsnqtt stdfetrgyy sagindlfyt
      361 nyngkpytny teedyrqlwl rrndktenpe rpwvvtdqrd grdtyvyygn fdwynylyrk
      421 nrpmwehnis vsggndklny ylsgntvdqt gifrqnpdky kvynfrskis akitprltis
      481 nntkyhynsy sypglsginn nfntavnhal asfvpvnpdg savyltslsn savldgmgai
      541 laygkhkned qryefsttfe asfnvmknln vranysylhy nyqtmnrtvn vpyskypgei
      601 sylttgngvn qlketqtnhw yqafnvygdy mldiadhqfk imagynyetk rlkdikvsrq
      661 gllsddlndl nlavgdamtm sggqneyall gafyrlnysy kggrylfets grydgssrfr
      721 sghrfgffps asvgwrisee pffgnlkkni dnvklrlsyg slgnqqvgyy dyiqtintng
      781 tmnyifgdek kgsyasvsdp nsadltwetv stwnvgldlg ffnnrlnlta dayirdtkgm
      841 qtsgkklpga yganepkqna anlrtkgwel mltwndafkl ankpfrynls vgladntsei
      901 tkfdnpskil sdyyvgqklg diwgyvvdgl frtdeeaasy nidqsavnfv intaqvnpgl
      961 hagdvkfidl dgdhkissgs ntaddpgdrk iignslpryt ysiqggfdwy gfdfsiylqg
     1021 vghqdwypgt nsvffwgpya rpyssfiprd flsnvwspen pdayfprpig ylalgnnrsl
     1081 gvvndrylqn laycrvknit vgytipvvwt kkvkierlhi yfsgenlftf splksdyidp
     1141 eqasaensik sangnaklyp wsktysfgvn vtf
//
LOCUS       WP_121765484             920 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121765484
VERSION     WP_121765484.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..920
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=103099
     Region          48..918
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 meksikliit gllcssiaaa qvadsiqhyg rgisfskkea ttaggmatad elghrtstva
       61 snalfglipg lqvlqnggne wengatlyvr gvgttssksp lilidgyers idnlavqdie
      121 svsvlkdaas lalygmrgan gvilittkrg hvgkpvitfd yefkmgtphr lpefvdgyty
      181 aqamneglkn dgtttprysq reldafrdqt ypefypnvdw mdealrdhsf gnnvnfslrg
      241 ggdvvqyftq lnylndkgil qpteenegys tqfkysklnf mtnldiklgn ttklqlnmrg
      301 nfaednrpyt ttadifdmly kvpsgampvk tssgrwgats iygsnpiami sdtgyergqt
      361 rnlyadinfa qdlsfitkgl satarlgfdn earywernqh kyateqatmg wdgeensykk
      421 lteetaldfs ssikdvvrrl tinaqvnydc twnaehklna tvlysmdklm krgqntgraf
      481 mdivgqvhyt yknrylldfs lagsassild pddrwgifps vgagwilsee nalkadwlnm
      541 lklrasygta gradygvqlf rgsysgggsy yfgetpasis gmkearlavd gltyekshkl
      601 nagidfmawn rlslsidgyy dhrtdilvdg dgalssvlgi aapdinsgiv nsygveiaan
      661 wndkignvty qlggqfsfnr nkikemnevy rpydylkrtg rsvnqyfgye vegiyqswdd
      721 iekrevkqil devrpgdlkf kdqngdkvid eydqvalgyn kicpeiyygf slgaeykglg
      781 fiasfqgvan ysqmldtrsi yrplvnnntv sqhyydnrwt dsnpdgkypr ltyngsknny
      841 ntnslwvada sylklrtlev yydlpqrwvn klpgvnhmrl farghdlfsi dkmdgvidpe
      901 mtatghplmt qytfgvnlrf
//
LOCUS       WP_121765662             316 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Bacteroides].
ACCESSION   WP_121765662
VERSION     WP_121765662.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33697
     Region          8..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeiekvkcl iigsgpagyt aaiyagranl cpvlyeglqp ggqlttttdv enfpgypegv
       61 sgpqlmedlr aqasrfgtdi rfgiataadl skapykitid gekeietetl iistgataky
      121 lgledekkya gmgvsacatc dgffyrkkvv avvgggdtac eeavylagla skvylivrkp
      181 flraskimqe rvmnhekiev lfehnavgly gdngvegvnl vkrlgepdee ryslpidgff
      241 laighkpnsd ifkdyldtde vgyiitdggs prtkvpgvfa agdvadphyr qaitaagsgc
      301 kaaieaeryl sakgii
//
LOCUS       WP_121765667            1197 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121765667
VERSION     WP_121765667.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..1197
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=134287
     Region          112..1196
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkertrfcgi rwlcllillc gsvmegraqa dknvtvqlkn aslrnvfdki keqanvgfiy
       61 snsaistlpr kdydfqnvai skviaysltg smltfeiedn kniiikkkkg mkditgvvvd
      121 aqgepiigaa iqekgtlhgt ttdldgrfal esfgnkdiql vvsyigmkrq vvtwkgntlr
      181 ikmeddaqni nevvvtgyqt idrrkttaai ssvkmddvlm pdmttidqal egripdllfs
      241 qnsgnvgata rlrvrgtstl vgnreplwvl dgfilqdpvn vsieqlndpd yinyignais
      301 ginpqdieri dvlkdaaata lygtraangv ivvttkkghv gtpvirysnq tklvvrphys
      361 dkninlmnsq ermqfgkdlc dlhyvfpqym tmvgyegafh rfqtgvisye qflnevknye
      421 ttntdwfdlm crnavthsht vslsggtest ryyssvgytr engtvnteyt erytaalnlt
      481 tniskqlrtn frinaniqkk nhlpgevnal qyayettral paynpdgslf yhqkhgysvg
      541 enkkannqyn ynilnement ssdysgntfn asgevkynll dmidftaggs ysrsstaqsv
      601 wfgentnyva ilkngeakdi pqtgesgvce lpyggvyntt ntitesitgr lqanfhrfld
      661 sentslitat lgyeasayrs naiadetrgl yqkrgmqyat megadlddfp yyknwlakgh
      721 rqitaaktnt isgyltlaye yknfftvgmn grfdasnkfg srsnekflpv wsasgrlnvk
      781 etmlnkcdwl dlfdirfsyg ktgnmldnqt anmlikqgtm dgyygqyise vvafpnpnlr
      841 weqtgttnlg lelslferrl tlsgdvwfkh ttdafssini stvngissyq mnngtidnkg
      901 ysfyisgypi rtkdwslyls tgyswadntv rsgtnenfsl ddylsgtaiv ngqaigtfys
      961 ykylglnpnt gipmfedyrd rrhllankkl adviplvmtt sgnrdpkltg sfyttlkwkq
     1021 lsanlsfnyr igskirlfnl ygpiskgiss dknvrkefln rwmkpgdekh tnipvllsps
     1081 dpnyestmsh wcltasakvn ekipafagnt wsmydnsdlr vvsgnylqls nlvfsydfrp
     1141 eqlketfika lrmslsttnv ftiaskkldg qdptqagfag vsmstrpsyt fninisf
//
LOCUS       WP_121765712            1109 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121765712
VERSION     WP_121765712.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..1109
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123374
     Region          25..1105
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnkkvmlllv clftsvglmi aqtpkkvtgv viseeddqpv vgasvlikgt tlgtvtnidg
       61 qftidnvpss artlkvsyig mksqevaika gtikiilqpd sevleevvvt gmqkmdkrlf
      121 tgastkltad nvklsgmadi srglegraag vsvqnvsgtf gtapkirvrg atsiygsskp
      181 lwvvdgvime dvtevgadel ssgdaetlis saiaglnadd iesfqilkdg satsiygara
      241 magvivvttk kgkagtnkis ytgeftmrmk pnyrnfnimd sqeqmsvyrd leaagylnfs
      301 dsyrastsgv ygkmyhlins ynatngtfgl intpeardlf lrqaeysntd wfdllfsnsv
      361 sqnhaismst gtdkasyyts lsvmtdpgwt krskvsryta ninalynisk avslnligna
      421 ayrqqaapgt lgsqtdpvsg evkrdfdinp ysyalntsrt ldpneyyvrn yapfnifnel
      481 nnnymdlnvl dtkfqgelkw kpinkvelsa lgaykysttt qnhyvkdysn qawayramdd
      541 atmqqanpwl ytdpdkvntl petvlpvggf yretkyamns ydfratasyn dvfkenhiln
      601 ifagmelnat drsktwfngv gtqygmgtlp sysylyfkqg neentdyyti detrsrevaf
      661 fgtgtysykg kytlngtiry egsnklgksr sarwlptwnv sgawnaheen wfeslqpals
      721 hatlkasysl tadrgpanvs nsyviiksyn pwrpsadvqe sglqisetqn nsltyekkhe
      781 lnigidlgfl dnrvnlamdw ykrnnydlig iintpgiggq iakyanlasm kshgieftls
      841 trnivtkdfk wntdfifsna knevtdlqsn atvmdlisgn gfamqgypvr slfsmdfkgl
      901 neegiptfin esgelttsdi nfqerdrkgh liyegstdpt itgsfgnift ykalklnvfi
      961 tysfgnvvrl dpqfhnkytd ldatpkefkn rwmksgdenr tnipaiadar mntqdtylsr
     1021 aynaynystv rtakgdfirm keislsydlp ktwlshlkls taslklqatn lfliysddkl
     1081 ngqdpeffnt ggvavpvpkq ftltlrlgi
//
LOCUS       WP_121765865            1027 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121765865
VERSION     WP_121765865.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..1027
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115150
     Region          45..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnkiryirl iglifvlivg ssltfaqnks krksakkplv evvsivtdek gsplknvsii
       61 cgegavvlyt dakgrfqtkv endatvmvea lgyedkvykl tgsnivpeki vlkkeplfla
      121 eeslvnradg gktykgnevg atsvlengqf gtfpdltltn mlqgkmlglq vrstvsglgn
      181 ntpdlfirgq hgmsentaiv iidgversaa dlipeeieri ellkdataki lygaraangv
      241 lwvttrrgka nrriynatae agvvqmtrtp dflnsyqyas lynearandg ltpyynqkql
      301 egyknskgan dllypnvdly dqllnkntny rkvsfdmtgg tdrvryalia gyvggsgfed
      361 vtytpqlhrl tlrgnldfnv tdfltisadv agrmemrkwg qldcgqvfta lsthrpneyp
      421 ltmspeetgl assdgiplfg asllrpmnay aetmyggytd erytrsqtni glkfdldmlt
      481 kglkagafls fdnydylqls lskvyptyai ktyrdfagee qimytqmkkt dvatsqsrks
      541 ttlqqtlgwn afaayentfn qkhdvsarlt ymyskttnqg vtqdiinany alrlnymydh
      601 ryaveadmal mgsnrfksgd kyffsaaggl awilsnedfl kdneyvnflk lktsagilgy
      661 drstehllye rawsqdgsfr fgttnngata yystfvrvgn pnlkwekaae wnigveglfl
      721 nnrlytemny frekhtdiig svdasygdyt gnftyqdnmg svlnhgiegm ftwsdrindw
      781 aysvganfvw sknkvlkwnq vkhgeeyryt vgrstdammg lvaeglfgkd vvinghapqt
      841 fadyqegdia ykdlngdkii dgrdvkelgn sfprttlgid fnvsykgwgl ylqgyselgv
      901 htwatnayyw nngegkyskl aldryhpann ptgsyprltt tagennfrns sfwlkntsff
      961 rmknvelsyt fnqfspssvv kkmkvfarga nlfvlssvkd ldpellnagv tnypvtrtft
     1021 ggvsfvf
//
LOCUS       WP_121765982             929 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroidaceae].
ACCESSION   WP_121765982
VERSION     WP_121765982.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidaceae
  ORGANISM  Bacteroidaceae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales.
REFERENCE   1  (residues 1 to 929)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 929)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 929)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..929
                     /organism="Bacteroidaceae"
                     /db_xref="taxon:815"
     Protein         1..929
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=104242
     Region          61..928
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnyikllii gtlcsstawa qvsdsisdkt rdemakrvey grgifydake ntaatavata
       61 delshrtsvn asnllygllp gvqvlqnann awndgasllv rgmgtmssks plilvdgfer
      121 pldylnssei esvtvlkdav stslygikga ngvilvktkr gvesapeidf syqfnmgtpr
      181 rlpdlvdgyt yaralnegle ndglqpryda kalkafqdgt ypdfypnvdw mnealrdhsy
      241 gdnvtfsarg ggkyvkyysq lnfldergil qptdlndgys tqfkysrlni rtnldikvsn
      301 stqlklnmfg nfsehnrpgt etsvifdaly kvpsgafpak tknnvyggtt tyannpigyi
      361 agtgyarsqg rvlyadmelt qsldfitkgl tfgarisldn yatywdnnak sfgyesatid
      421 fatgeetykt lrnegvlsfg ssvgdvsnhf nlearvnyeh swekdhklnv almysmdknt
      481 qkernestaf idaiaqahyv yknrymldvs fsgtaasvle pgnrwgifpa lglgwilsee
      541 nylkrnwlnl lkvrasygia granydmnlf nsvygvgsgy yfkdnitslg gmkesrlgvt
      601 gftyekshka nfgvdlvawn rllvtadafy dhrtdilvda sgtmstvlgi aapkqntgvv
      661 dnygvelaak wndrigdfty qagamfsysk neivemneqy rpyeylrrtg kslgqifgye
      721 vegiyqnqke iddrevkqyl sevrpgdlmf kdqngdnrid eydqvalgyn stcpeiycsf
      781 dlgaeykglg fyalfqgagn yskvlnvnsv yrplvsnntv sthyyenrwt kenpnalypr
      841 ltysgsnnny ntnslwvada sflklrtlev yyqfspkvmk kvsplrnarl farahdlfsw
      901 dkidimdpea vkaghplmtq ytfgvnltf
//
LOCUS       WP_121765993            1043 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121765993
VERSION     WP_121765993.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..1043
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=116346
     Region          59..1041
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnvdrpvltr vkcslflslg krtkyfclvf illgsvatna vyaqqtvtgg ketarspqrt
       61 vykgivided dlplagvnvt lkgdksigvt tnenghfqia lpegknvlvf syigmasqev
      121 rvhegksvtv rmlpdaqqlg etvvtgiytr kmdsftgaas tykaeelkai gnqnilqsls
      181 aldpsfviae nnlagadpns mldisingkt singlsdtyg tdpdrplfil dgfettleri
      241 sdlsmdrves itilkdaasa aiygskaang vvvvetkkpe agrlrftyng nyqvswadls
      301 dynlmnaaek lefeklsgry galdengeil mdanralyys ryrnvvggld sywlseplrt
      361 afvhdhslna eggdaafryg ltlryknaeg vmknsgrqni dgtvnlgyri drfnfsnqtn
      421 iyytktdnnv vsfsefssan pyyakydeng evykvlesyq vlggteyayn plwdfqqksf
      481 nrgdqltlnn nfnvefrpfd kmrivgkfgf tttrgktevf kspfdssfts veelkrgtfs
      541 rsdnnstsyd gsllasygda igvhtynfvg gaqlsenntt mgayltqgyi sdnfynpnfs
      601 nsypdggkps ssvakarsas fylngnyayd mrylfdfnvr sdgasvfgvn npfsttyslg
      661 vawnihnekf frqsklvntl rlrytfgnpg nqnvdaklan nvytyytkyp npfglaaias
      721 kwgnknlkwk rtqthnigln atlfdrrlav aldytlrksd pelinveqpt stgtsfipmn
      781 igatknnnvs mtlgydiirr rellwkvtan llhttttyyn igdlleklnq egragqtlir
      841 yydgasatal wairsmgidp mngnevfqkk dgtytykwds aeevecgdst pkiqgnlgtt
      901 vrykgfslgv nfayrlggqt vlqtllnkve ninnvavryn qdkralhdrw qkpgdvaqfk
      961 riddtsetki ssrfiadent lqctsislgy edttsdwikk aglssvtfri ytnnifrlst
     1021 vkeergldyp fsrsvsaslg lrf
//
LOCUS       WP_121766053            1026 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121766053
VERSION     WP_121766053.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..1026
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=114040
     Region          49..1025
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mktnptlrrt srtlfllflf calsvqltaq nadkkinets tktnkgniir gvvydtdglp
       61 ligatvrnlq nqsgtvtnnd gvftlagtke svrllisyig kkpqeiratt gksikviled
      121 dnsalkevvv tgivtkkkdt ftgssatfsg eelksvgvqn piaslktldp sfnvldndlf
      181 gsdpnrlpni eirgkssmlg mrdelsedpn qplfildgfe sslaaiynld inriasmtil
      241 kdaastaiyg skaangvvvv etvkpkagql rlnysgsmdv sfpdlssynl mnseeklrfe
      301 qmmgkytsnn sieemisydn iyqkrladiq sgvdtywlse plrtginhrh slyvdggseg
      361 flfglgvnyn gvegvmkksq rdvmganidl tyrvgrlqft nkftaqqtkt dnpivsfsey
      421 aaanpyfkky deegkvskll dnnriegavg nplyndsqns rnegkdlmls nfliaeyspi
      481 tdlklrarfg lthtnskgdn fispddtrye tvnilkrgsy ghsemeqtry egeataiyak
      541 vlkeahrfnv alganiseqk sltqgysasg fpsgdftyps fsngyteggr psyyesvsrs
      601 vsaymtggys lldrylmdvs yrvngasvfg snkkyintws vglgwnlhne kfirdnlrfi
      661 nyfkirgsvg npgnmnysss mslttfrysy aaynyfglss vlsqlgnddl kwqttldkni
      721 gldltmfnnr lvltldyyhk ttdplligig lpssagltsy ntnlgkqisk gftgiaqyyi
      781 frdfnkrltw svrgtirlas skldgignal eklnkygqsr stvryydgad pddiwtvrsa
      841 gidpangrel fikkdgtyty dfsydeeviv gntrpnaegt igsnfgykgf tvgatfryrm
      901 gaetfnnavy skvenigmag ltknqdkral ynrwqkpgdi aqfkniadat ntpmssrfvq
      961 kentlslesf qigyefdpql agklgisgmr inaymnnifr lstikeergt sypfarsvsl
     1021 alsftl
//
LOCUS       WP_121766226             914 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121766226
VERSION     WP_121766226.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..914
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=101114
     Region          1..912
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mgedtqtlde vvvtalgikr atkalsynvq evkgdeitav kdanfmnsla gkvagvqiss
       61 gatgaggaar vvmrgmkslt kdnnalyvid gvpifntgks ggeglfgdmg gsdavadlnp
      121 ddiasismmt gpsaaalygs saangvvlit tkkgqtektt itvsnsttfs kayimpdmqn
      181 rygtssglfs wgeltdrryd psnffetgtn vinsvalstg nsknqtylsa sttnsggilp
      241 nnsynrynft arnttnflnd rltldigaqy iiqnnknmvs qgqyynplpa lylfprgdnf
      301 deirlyeryn tnygymeqyw pygdaslslq npywvqnrii rtsdkkryml naslkwkvtd
      361 winivgrvnl dnsdyrnkne ksastlttfc gvsggfedam rqerslyadv lanidktfgd
      421 fhltanvgas iyhtsmdqly fagdlvipnf fqvnninfss nykpdptgyk deiqsifasa
      481 elswknqlyl tltgrndwds klafskqksf fypsvglsal lsemvelpel ityakvrgsy
      541 tvvassfdrf ltnpgyeyns qthnwanptv ypmenmkpek tksweiglnl kfwenrfsld
      601 atyyrsntln qtfkvdipss sgykqaivqa gdvqnqgiel algfsdkwag fgwssnatft
      661 lnrnkvkrla sgsvnpvtge aiqmdemnvg wlgkenvapr vilteggsmt diyvynqltk
      721 dnngnikvdq ngnlgitssn tpvkvgnlda dfnlgwinhf tykgidlgvv lsarvgglay
      781 satqgildyy gvsevsasvr dnggtpinng kvdaqkyyqt istgeggygr yylysatnvr
      841 lqelslnytl prkwfknvan vtlgvvgrnl wmiyckapfd pelsastssn yymnvdyfmq
      901 pslrnfgfnv kvqf
//
LOCUS       WP_121766425            1117 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121766425
VERSION     WP_121766425.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..1117
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=125333
     Region          25..1116
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrikflciii clfvnalasa saanrtitgv visgednepl igasvyvhad dlkkagasqt
       61 slgtitdmdg kfsisipekv trihcsyigf eeqvialqgd krsyrivlqp sahaladvvv
      121 tgyqtlerrk ltaaiskvel sdamvgatks idqaltgqia gvavtntsga pgapakirir
      181 gtaslngtqd plwvldgipl egtdipkmds nssdndivni gqssiagisp ndiesitilk
      241 daaataiyga raangvivvt tkrgrtgkpv vnfntkltys pnldtsqlnl lnseekvnle
      301 lqmmkeqpfd yggwgfmfyp vypekggvvn ilrkyelldt yrqngwdglt peaqnainrl
      361 ksintdwndi lfrdaftqey nlsisggsek vtyynslgyt kensnvpgvs lsrfnltskt
      421 nyqlnkllki gisifanrrk nrtfmtdsyg ltnpvyysri anpyfepfdn ehnylydydv
      481 tgsvtdekrg fnifeerdnt skesittain sifdtelrfn dqwkltsqig vqweqlsqee
      541 yvglnsfnmr nmredntyyk dgvrtyiipe ggmlkttgat tsqitwkiqg eykntfsdih
      601 diqimagsei rknwyenhvs tgygydpktl nfrnlnfkde tqaneskwkl kneisrenay
      661 asffangsys lmnrytlggs irmdgsdlfg vdkkyrflpi ysvsglwrls nepfinqkwi
      721 dnlalrlsyg iqgnidknts pflvgsyknt silpggtyed yitidsapns klrwekttsy
      781 nigldfavln qainlsvdyy yrkgtdligy kllplengfe smainwasms nkgieinlqt
      841 rnittknfsw ytsfnfaynq nkvlkvmtqk sqvtpslegy pvgaifvlkt kginpetgqv
      901 mvenkngesv tieelfkmap sgnndgqysi gadteeirgf ysyagtadap ytgglmntfs
      961 yrnwelnlnl synigahvqt tpsyyiadld pginmnrdil drwtpenvng tfpalatyht
     1021 npadyylfss rrdlyksldi wtkklsyvrl qnirlayrlp sewlqkvris gatvglearn
     1081 lfvfgssykn ymdpesmsnl ystpvpksvt fnlslnf
//
LOCUS       WP_121766481             953 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121766481
VERSION     WP_121766481.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..953
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=106765
     Region          40..952
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mnniknkisv wavfaclmvp staswgqeat ssavrtsdee evidlgyltl pkravtgavs
       61 svsgtelrks pdaslpktfa grfsglttre tdaelsrggf stetmgmsww irglstvngt
      121 tpmvildgvl cpntnyvyls pdeiesvtvl kdaavlslyg iqgangvisi ktkrgrvgkt
      181 dvtvtfdqsl qqmtrrplfv nsgeyvdlrn qagcndglgk ysqfspsdve qfhaggnely
      241 pnnnwydmfv rpltfmsrag vtvrggsekv qyfsnvnymh qqspfkttee pgsqynpepk
      301 ndwfnfrsnv dvkftsylkg flrlagnvkn ekttgysnaa vydhlftlpp tmygpltpsg
      361 deyenggqvi thddegtpvy gmlnrsgyiq nlyvnitaqa glnmdlgflt kglsigglma
      421 yqtstlnqtl ttqdferyir tkdmsglyft kkgsslnspl kysksstmdy nlnlyahany
      481 srtfgdhsid amgyifyqkq elqksnlpyk resmgataty gyknryfika dvgysgseqf
      541 hpdkryvatp aisgawivsd eafmkdiewl nylklrasyg itandqfgga rylylddidi
      601 ngneglkgnp slsaekmkkq nygielglfn elsisldwyk srcdnmlvss sgtipqyqgv
      661 plnyypktng gkmenygyei eamyekrlnd dwsfhvggsf sfnknkvisv nespyssdya
      721 yrlrtegyts gqvwgylidy sngngmfnfk eeleasglty afgtprlgdf iyqdlngdkv
      781 idekdiapig ysiiprqsyn ltagfkykgl evsllfqgvn kvstvasgig vyehayqgvf
      841 ndihqhawtq erwnngekie ypalslnest nhvansffvw nasylrlknm eiaytlpkhi
      901 skkvcaenir fslsgqnllt fdkmrskyid peigtmgdfq pyrvynigvs ltf
//
LOCUS       WP_121767290             984 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121767290
VERSION     WP_121767290.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..984
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110075
     Region          39..983
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkyiqigmcl cmglacfmqp iraqkqsqvr veavvrtpqg epipgavins neikaytvad
       61 aagtfslnis aggkfivkav gykdqvvdaf rtverrdlqg gvsyidlpef mkkdyttysl
      121 dglqsyiggy tgaiwgqgal vlidgvprda sadirpseie qitvlkgvga valygsraak
      181 gvvqittkrg kaydraidvr antglyvpkr ypkylsswey mtlynealrn dglsslyddh
      241 ailnhwkgen pyrfpsidfy ssdylkkayn ksdatvevsg gterarfytn mgighentll
      301 nfgegknegn lrfnvrgnid fkfnevlsaa vdasvilnnn ryangnywga aatlrpnrfs
      361 plipvsyiet dntaallqaq nsnhlidgky llggsqldqt npfadvyagg yaknnsrqfq
      421 ltaglnfnle kllkgltfkt qfavdysssy vesytnsyav yepswytpeg qvyidrltky
      481 gedrsngkqn vggswyqqtm aftaqlnyer aienkhnina illatghqrt etgiyhktsn
      541 anlgihlgyn yqhkyyadfd gaiihsakma pkkrnafspt vtlgwrisse dfladspiid
      601 dlkltasagi lhtdidfssy ymyqgyytqt ngayygwgdg aytmqstdsr rgdnmdlgfv
      661 krkeinigle asllkklltv nanffvnrme gmpvqpytay pgwfstgwpn ssfipyvnfd
      721 idqrigvdfa vnlnkrmgqv dlglgltgty ltskaikrdd lyndtyqnra gkpldamwgl
      781 vsngfyesee dianydatps ygevkpgdik yvdqnndgvi dskdevylgh gsapfsfgis
      841 ltakwknftl fargtgfigg ygmkssnyyw vygdgkysee vlnrwtedtk atatyprltt
      901 msgdnnfrss dfwmyktnrf dlaklqltyd fsrellknsi vhelgvyisg enlltlsker
      961 kvmemnigst pqcrffnlgv katf
//
LOCUS       WP_121766021            1108 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein [Bacteroides
            acidifaciens].
ACCESSION   WP_121766021
VERSION     WP_121766021.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides acidifaciens
  ORGANISM  Bacteroides acidifaciens
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Bacteroides acidifaciens"
                     /db_xref="taxon:85831"
     Protein         1..1108
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=123223
     Region          44..108
                     /region_name="DUF4974"
                     /note="Domain of unknown function (DUF4974); pfam16344"
                     /db_xref="CDD:435289"
     Region          123..1107
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mksmrerfil qglvmliaft lslatpfkah aqsgqkerit imvkqkplee vlkklskeyn
       61 yqlfynnslv kgirvsvsiq kaginqtmdv llagtglqys ikektivitt ipsrntakek
      121 kllsghvvdk egraipgvni ftgdktqgav sdidgnfafa splkhgtlln ftsigmkpqh
      181 ivyggestlk ivmvedvnel eavvvtgvvn kkresftgsa stftadelka vgtqnvissl
      241 ktldpafnvl esgefgsdpn rmpdieirgk sslistrdel aedpnqplfi ldgfesslea
      301 iynldmnrva sitilkdaas taiygskasn gvvvvetvrp ksgklhltyn gsaniswadl
      361 ssynlmnase klrfeqmvgr ytsstpsqqi eldqlynnkl advargvdty wlaeplrtgi
      421 nhrhslyaeg gegafqfglg lsyngitgvm keskrdnlsg nidltyrlnk lqfvnkfsmd
      481 ntasgnpivg fseyaganpy ymkynengev erwleyndyv eagnplynaa qnsynkgksl
      541 sisdkfimey tpiaamkira rfgithtnsn teaftsplds dyskvdftkr gsynygetes
      601 nkyegeltvt ygktfnkahl vniaaggyls qldskshgya avgfpvgdft lpsfangypd
      661 ngspsyyent srsvsayaig nyafnnryll dfsyrvngss vfgtdkhyig twavglawnl
      721 hnekfvsdni dgismfkira signpgnqnf sssstittfr ynfnsfnyfg mttslaqlgn
      781 pdlewqttid rnigfditil ndrltltgdy yykttdplli gidmpastga tgniiyknfg
      841 kqttkgfnaq atyyiirqmd krfwwsvrgt lrhgsselng ignrlesfnt sgregdqngq
      901 nkstkryfdg adpdaiwavr sagidpatgr eifikkngel tydfsyddev iigssrpkve
      961 gvlgssfswk gfsmnfdfry rmggysfnsv lynkvenitt sqlkynqdkr alydrwqkpg
     1021 diakfkniad sqstpmssrf vqkdntltle slrvgyefkp eiarkvgvss lrlnaymndi
     1081 frissikqer gtsypfsrsv sfnlsltl
//
LOCUS       WP_121768541             998 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: SusC/RagA family TonB-linked outer membrane protein
            [Bacteroides].
ACCESSION   WP_121768541
VERSION     WP_121768541.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides
  ORGANISM  Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Bacteroides"
                     /db_xref="taxon:816"
     Protein         1..998
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=110701
     Region          36..997
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrnihckmct cllgillmlf sgiqargasw eaqqerkisg tvidekgepv igasvvvvet
       61 kqgaitnieg kfsvnapqng rlkvsyigye tqeiaikdrq slrivlkees talnevvvvg
      121 ygtmkrkemt saishvgakd lnqissldas mllqgkvssv svsntaladp nstgsiqirg
      181 issrnaglgp livvdgvpgg dmtninpadi esidvlkdga asaiygtrgs ngvilvnlkk
      241 gtrdgevhtt ysaavtfnka kkeldimnae eyrayrtvsn plsdmgattd wfdavtrlgv
      301 thmhtltfsg gnartnyrvt adyrkaqgid lrsdrreyga ratishttkd glftfsanmt
      361 prvidrnksa svygsviknn ptmpiydses angyyrfpsg gdssniveql neeengteik
      421 llewnataav nllplfnpkn pnmvlksqvt lsqyqvdkfn gwftpstygp nvnssvagka
      481 srdfdkstsn nlewvtnfst rikdhqiram vgysynygvs sgmgaenwdf ssdglmynnl
      541 gsgleaakeg ktmmssyknd hklisffgrv nydwkerylf tfslrhegss rfgenhkwgn
      601 fpavsvgwri sdekfmkgls wlddlkvryd ygvtgnqeig nyqslatyra ygwyqyngnn
      661 fhvwgssknv nselrwekgh nqnigldfsl fkhkvtgsfn yfhrkqsdll gsysvsvppn
      721 lfttiyanvg tlrntgfeld vtvnavrtkg faysftlvga tnnnkfvsfs ndvykgqkyy
      781 stcnmanpnn pgylqrieeg erignyftyr yagvdkkgdw liydkkgnvi piaqgseedk
      841 avtgnglpkf tgsithnfty knfdltvafr gaagfdifnv hdfyfglqsm stnqlttays
      901 knahittgkn vitdyfiepg dylkidnitl gytmnlnkky iekirlfgta nnlytftkft
      961 gvdpstyevn gltpgtfggg ynyypsafqf ilglqvsf
//
LOCUS       WP_121773016            1081 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides sp. CH2-D42-20].
ACCESSION   WP_121773016
VERSION     WP_121773016.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides sp. CH2-D42-20
  ORGANISM  Parabacteroides sp. CH2-D42-20
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Parabacteroides sp. CH2-D42-20"
                     /db_xref="taxon:2320086"
     Protein         1..1081
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=118997
     Region          24..1080
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mrrltflllc lfigigvata qtmkitgnvi ssedqqpvig aavvvkgtti gtvtdfegnf
       61 sldvprdakm ifisyvglkt kevpvasvin vvldsdskal devvvtamgl trekkalgya
      121 lqevksdelt kagqqslats lsgkiagvqi tsqggqvgas qnivvrgnss fgnnqplivv
      181 dgvpiandna kgatvnlgsg lndinpedie sisvlkggsa alygmragng vilvttksgk
      241 kdkgvsisye gditidrvyn lprlqnkygq gyyaseydwk eaqageysgd yqafalengy
      301 nyvdgmgsgi ndnadeswgp rldiglnlpq ynspvidgvr qatpwvsspd niknffqtgy
      361 smnhtvalsa stdktstras lsfrdqggtt pntdqkryam avntkmtfnk yidfdlsany
      421 irtksanlpg tgynstnalq simqwfgrqv dlkdlknnwd qvdeygkyth ynwiqsfhan
      481 pywtlnkntn sydrnrfygk tslyikptdw lkfegrmgld hydsnqfsri lwnidypngy
      541 frsfdrsmte fnadfiayvn knfgdwalng laganyrdyq taimgtgade ltaeglftva
      601 nahgtpytln dhekrrsnsv yanasigykn mayaevsvrn dwdstikdaf fypsfsgswi
      661 ltetfpglqn gdylnflklr ggwakigsat dpyrsnayys lisssfngtt lfynptilpp
      721 tnlrpesvkt wevgveanlf nnrlhidaay ynkvtsdqim nanvatstgy tsmyinagki
      781 snkgvelqvs gdiiknpkgf nwtatlnwak dksridelyt dpvtgqslda yqigsswsvk
      841 nyamvgkswg tlvgtgyvyn edgsilvedg ipvyeagkei gdvtpkwlag fsnefsykdw
      901 sfgflldfrl ggdvysvtqa fgsqtgilkh taegdlreng vvlgqnymtd kvfktadgki
      961 ndvavnaedf fynyyticem svfdgsylkl reahltynfp ksilektkci kaahvslvgt
     1021 nlallwvhks niahidpest stggddpett atsrgfnsgv gfesnsypps rsfglklgvt
     1081 f
//
LOCUS       WP_121773454            1057 aa            linear   BCT 07-JUL-2024
DEFINITION  SusC/RagA family TonB-linked outer membrane protein
            [Parabacteroides sp. CH2-D42-20].
ACCESSION   WP_121773454
VERSION     WP_121773454.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides sp. CH2-D42-20
  ORGANISM  Parabacteroides sp. CH2-D42-20
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Hall,L.M., Fawell,S.C., Shi,X., Faray-Kele,M.C., Aduse-Opoku,J.,
            Whiley,R.A. and Curtis,M.A.
  TITLE     Sequence diversity and antigenic variation at the rag locus of
            Porphyromonas gingivalis
  JOURNAL   Infect Immun 73 (7), 4253-4262 (2005)
   PUBMED   15972517
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Wei,B., Dalwadi,H., Gordon,L.K., Landers,C., Bruckner,D.,
            Targan,S.R. and Braun,J.
  TITLE     Molecular cloning of a Bacteroides caccae TonB-linked outer
            membrane protein identified by an inflammatory bowel disease marker
            antibody
  JOURNAL   Infect Immun 69 (10), 6044-6054 (2001)
   PUBMED   11553542
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR04056.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Parabacteroides sp. CH2-D42-20"
                     /db_xref="taxon:2320086"
     Protein         1..1057
                     /product="SusC/RagA family TonB-linked outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=115238
     Region          25..1056
                     /region_name="OMP_RagA_SusC"
                     /note="TonB-linked outer membrane protein, SusC/RagA
                     family; TIGR04056"
                     /db_xref="CDD:274948"
ORIGIN      
        1 mkkkltsvll flalsagvvs aqtskvtgkv igedgepvig asiivkgttv gtvtdfdgnf
       61 elevpangkq lvisyigmks qevaatsnvn vklladtqnl devvvtamgi skekkalgya
      121 vqdvkadelt kgantslsga lqgkvsgvei spssgmpgas skitirgsrs ftgdntplyv
      181 idgmpvasta dvdtgssvsg tdfasravdi dpndiesini lkgqaasaly gmratngviv
      241 ittksgkgar kgkpqvafnt slsfdkvstm peyqkvyaqg tngkyspyas tswgplisel
      301 pndptyggnt dneftkqygk hegmyyvpqr aaaglapwaq pqaydnikdf fnvgttwsns
      361 vnvaqafdkg nysfsigntt qdgiipntgm drynakmsae aqlhknwstg ftgtyvnski
      421 skqssanngi latvygapss ydlagipshv egdpytqntf rstsgfdgay wavdnnefle
      481 rsqrffgnty lkystkfntd nhkldvkyql gvdsyttnyt dswgyghang ygeidhygys
      541 itelnsllta aytwninedw lfdalvgnel venqrkfyes yganynfpgw nhidnattmv
      601 aseslrrkrt vgnfasisls yanmvyfnat vrndivsnmp rnnrsftyps vslgwiftel
      661 eplknnvlty gklrasyaev gqagdyydsy yttpvygggf ygstpiqypm sgitaftpya
      721 rvydpnlkpq ntksyelgvd ltflnglfsl nytfsrqnvk dqifevplag stgsaelvtn
      781 ggaihtnahe itlginpint knfkwdmafn fskidnyvde lapgvesifl ggfvdpqvra
      841 nigdkfpviy gttflrndng divvdedglp qigsegvigk vspdfllgfn tnfeiykfri
      901 gatfdwkcgg qmysgtlntl nyygtsmesv esrtaetfrf shpavkqled gsyvandidi
      961 kgedalsyyd rmtliseagi ydsgflklre lsvsypvwdk nginvnlnvf arniilwsel
     1021 kgldpeasqg nnnmgggfer fsmpgassyg fglnvkf
//
LOCUS       WP_121775639             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Acinetobacter].
ACCESSION   WP_121775639
VERSION     WP_121775639.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33722
     Region          8..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliagmqlg gqlttttdve nwpgdaeglt
       61 gpalmermqa haerfgteil ydhinevdlk vrpfvlkgdm deyacdalii atgataqylg
      121 leseqaymgq gvsacatcdg ffyknqkvmv vgggntavee alylsniash vtlvhrrdkl
      181 rsekilqdhl nekvkegkis iiwnhqveev lgdsnsgvts vrlkstqdds sqdvdvsglf
      241 vaighkpnta mfegqlelrn gyiqvrsgta gnatatsvag vfaagdvadd vyrqaitsag
      301 sgcmaaldad ryldgle
//
LOCUS       WP_121783798             315 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas putida].
ACCESSION   WP_121783798
VERSION     WP_121783798.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas putida
  ORGANISM  Pseudomonas putida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas putida"
                     /db_xref="taxon:303"
     Protein         1..315
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35280
     Region          5..168
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mpvydiyskr kkrlaglvpd vytydsiplg lrnqivfiae divsdvfghq msddvydyvs
       61 rtlsrewgte ylvahgefid rdeevkdair kvteadnvld ivelllqtaq nhakddrnlv
      121 sargksalar higelnqrfk ehgigyeyse eqiiridsql ihsevvkpal rllsepgfeg
      181 ahdeylaahe hfrhrrfkea lnealkafes tikviagvrg wtinkgdtan klvkacmdng
      241 lfpsyyeshl salsnllvgg vpsirnkeag hgqgavvnei dphivaytlh mtasaivlfv
      301 qsyqalpeap nepne
//
LOCUS       WP_121787892             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces dangxiongensis].
ACCESSION   WP_121787892
VERSION     WP_121787892.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces dangxiongensis
  ORGANISM  Streptomyces dangxiongensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces dangxiongensis"
                     /db_xref="taxon:1442032"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34284
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmra qaerfgaelv pddivsvdls geiktvtdta gtvhqakavi vttgsqhrkl
      121 glpkedalsg rgvswcatcd gfffrdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfv wdsevaeiqg dqklsalklr nlktgelsel pvtglfiaig
      241 hdprtelfqg qldlddegyl kvaapstrtn vtgvfaagdv vdhtyrqait aagtgcsaal
      301 daerflaala dedqaepekt aav
//
LOCUS       WP_121792687             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aeromicrobium phragmitis].
ACCESSION   WP_121792687
VERSION     WP_121792687.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phragmitis
  ORGANISM  Aeromicrobium phragmitis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Aeromicrobium phragmitis"
                     /db_xref="taxon:2478914"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33935
     Region          7..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msevrnviii gsgpsgytaa vyaaranlep lvfegsvtag galmnttdve nfpgfpdgim
       61 gpelmdkfra qaerfgaeli addvthvdlt gpiktvalad grtfsaravi lamgsgyrkl
      121 glpgedelsg hgvswcatcd gfffrgkeia vvgggdsave eatfltrfad kvtlihrrde
      181 lraskimaqr alanpkidfa wnsevaeihg tgsleavtlr dtrtgetrrl pvsglfiaig
      241 hdprsellvg qvdlddegyv ltqpgstatn lpgvfaagdl vdhtyrqait aagtgcsaal
      301 daerylasfe eagepapaaa lte
//
LOCUS       WP_121792805             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aeromicrobium phragmitis].
ACCESSION   WP_121792805
VERSION     WP_121792805.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium phragmitis
  ORGANISM  Aeromicrobium phragmitis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Aeromicrobium phragmitis"
                     /db_xref="taxon:2478914"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52577
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigivtesa agetrvsatp atviqllklg ydvvvesgag arasftdday adagatvvap
       61 deawasdvvl kvnapddeei arlrdgatli sllspglnpe lveklaarpi talamdavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksigge ylaveveeqm essdgyakat seaydrraae
      241 iyseqaqdvd iiittalipg raaprlitaa dvasmkpgsv ivdmaaaqgg nvegsvpgek
      301 vvtdngviil gytdlagrlp tqasqlygtn lvnllklltp gkdgelvldf ddvvqravtv
      361 ardgeklwpp ppvqvsaapa aapavaepve kkeprklter grivavaaaa avlfgliais
      421 paalqghlvv falavvvgfy vignvhhalh tplmsvtnai ssiiivgall qigsddavit
      481 tisfvavlla sinifggfav trrmlamfsr s
//
LOCUS       WP_121807605             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nocardioides mangrovicus].
ACCESSION   WP_121807605
VERSION     WP_121807605.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides mangrovicus
  ORGANISM  Nocardioides mangrovicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Nocardioides mangrovicus"
                     /db_xref="taxon:2478913"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34836
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtdvrnviii gsgpagytaa vyaaranlap lvfegsvtag galmntteve nfpgfregiq
       61 gpalmdemra qaerfgaelv addvievdls geiktvrted gtfsaravil amgsgyrklg
      121 varedelsgh gvswcatcdg fffreqhiav vgggdsalee atflsrfgsk vtlvhrrdel
      181 rasaimqera fadpkiefaw nsevaslegd galsgvvlrd tttgelrtmd atglfiaigh
      241 dprselvrgq vdlddegyvl vehpstatnl dgvfacgdlv dhhyrqaita agsgcasald
      301 aerwlaardf aassagspal tqaevssgvg va
//
LOCUS       WP_121829140             327 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Streptomyces].
ACCESSION   WP_121829140
VERSION     WP_121829140.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34561
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmra qaerfgaelv pddvvavdlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedtlsg rgvswcatcd gfffkdqdia vvgggdtaie eatflsrfak svtivhrrdt
      181 lraskamqdr afadpkisfa wdsevttihg dqklsgvtlr dtktgatrel pvtglfiavg
      241 hdprtelfkg qlelddegyl kvaapstrtn lpgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala dtekvaepek laetpvv
//
LOCUS       WP_121830088             507 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Streptomyces].
ACCESSION   WP_121830088
VERSION     WP_121830088.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52041
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgvlkear agesrvsatp atveqirklg ygvvvdpgag vaagftdgay eaagatvgda
       61 vaadvvlgvn apapdqldrv rpeatvialf apafdpamve dlgrrpftal smdavprisr
      121 aqsmdvlssm aniagyravi eaahefgrff tgqvtaagkv ppakvliaga gvaglaaiga
      181 sgslgaivra tdprpevadq vrslggeyls iespetevsk tgyakemgdd ykareaelya
      241 aqcrevdivi ttalipgrpa ptlitaemva amkpgsvivd maaanggnve gtvkgertvt
      301 engvtiigyt dlagrlpaqa sqlygtnlvn llklmtpdkd arlvldwddp vqrsitvvre
      361 gesawppppv qvsaapapap aapvepapkk ppmtagqkfg gvalgalalf laaafapaal
      421 lphvtvfvla ivigyyvigh vhhalhtplm svtnaisgii vvgallqigh tstavtvlss
      481 vaillasinv fggfavtrrm lamfnrs
//
LOCUS       WP_121836324             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus hillyeri].
ACCESSION   WP_121836324
VERSION     WP_121836324.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus hillyeri
  ORGANISM  Streptococcus hillyeri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus hillyeri"
                     /db_xref="taxon:2282420"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33068
     Region          2..300
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvatl eqgapggqmn ntsdienypg felisgpels
       61 mkmfeplekl gvenlygivt giedkgdyki vktddeeyqt ktviiatgak hrhigvpgea
      121 efnsrgvsyc avcdgaffrn qdllvvgggd saveealflt rfassvtivh rrdelraqkv
      181 lqdrafanek isfiwdsivk eikgdaikvr svdienvktg evtnhefggv fvyvgldpvs
      241 dfvkelgitd engwiptddh mktsrkgifa igdvrqkdlr qittavgdga magqqayqyi
      301 vdnd
//
LOCUS       WP_121838724             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Parashewanella curva].
ACCESSION   WP_121838724
VERSION     WP_121838724.1
KEYWORDS    RefSeq.
SOURCE      Parashewanella curva
  ORGANISM  Parashewanella curva
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Parashewanella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Parashewanella curva"
                     /db_xref="taxon:2338552"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53708
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipkeqg gehriatspn svtqliklgf dvvvengagi dssftdqafi eagaktaskv
       61 whaamifkvn aptpdeieqi qagtilvsfi wpaqnpelvq lladrditvl amdmvprisr
      121 aqsldalssm anisgyravv eaahefgrff tgqitaagkv ppakvlviga gvaglaaiga
      181 agslgaivra fdtrlevaeq iesmggeflk ldfsdedggs sdgyakvmsd efiaaemalf
      241 aeqakdvdii ittaqipgkt apklisqemv dsmkpgsviv dlaagsggnv epsvagrkiv
      301 tdngvtvigy tdlagrlstq ssqlyatnlv nlmkllckqk dgeieldfdd vvtrnmtvch
      361 qksimfpppp isvsaapaqp kpeavkpaev kedkpssmky wfaglgalaf taiaatapaa
      421 flshftvfvl scvvgyyvvw nvshslhtpl msvtnaisgi ivvgallqig hgsvvinila
      481 fsailiasin ifggftvthr mlkmfrkdq
//
LOCUS       WP_121840034             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Parashewanella curva].
ACCESSION   WP_121840034
VERSION     WP_121840034.1
KEYWORDS    RefSeq.
SOURCE      Parashewanella curva
  ORGANISM  Parashewanella curva
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Parashewanella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Parashewanella curva"
                     /db_xref="taxon:2338552"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34238
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mtearhckll ilgsgpagyt aavyaaranl qpvmitgmqq ggqlttttev enwpgdaddl
       61 tgpalmdrmq khaekfntei ifdhihetdl serpfrlkgd sgeytcdali iatgasamyl
      121 gleseqafmg kgvsacatcd gffyrnqkva vigggntave ealylsnias evhlvhrrdt
      181 frsekiltdr lmkkveegni ilhldqtmne vvgddmgvtg lklkstkdes itdlevagvf
      241 vaighkpntq ifkgqlemnn gyikvesglq gnatqtsveg vfacgdvmdq hyrqaitsag
      301 agcmsaldae rfldaqe
//
LOCUS       WP_121844001             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_121844001
VERSION     WP_121844001.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36006
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqiikiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkgits qspgdaviel nerfrehgvg yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel vsymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_121850681             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Euzebyella marina].
ACCESSION   WP_121850681
VERSION     WP_121850681.1
KEYWORDS    RefSeq.
SOURCE      Euzebyella marina
  ORGANISM  Euzebyella marina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Euzebyella.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Euzebyella marina"
                     /db_xref="taxon:1761453"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34368
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeniervkt liigsgpagy taaiyasrad lkpvlytgme pggqltttte vdnfpgypeg
       61 idgptmmvql qqqaerfgtd vrigmvtsvd lsdeiggihk itvdnskeie aetiiistga
      121 sakylnipse qrlrgggvsa cavcdgffyk gqdvaivgag dtaaeeasyl anicnkvtml
      181 vrkdymrask amqhrvnslk nievryntev devlgdqvve glrvvnndtg ekdeiaitgl
      241 fiaighkpnt difkgqldmd etgyiitkgk stktnkpgvf asgdaqdkey rqavtaagtg
      301 cmaaldaery latvetekev v
//
LOCUS       WP_121845507             346 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Kocuria tytonicola].
ACCESSION   WP_121845507
VERSION     WP_121845507.1
KEYWORDS    RefSeq.
SOURCE      Kocuria tytonicola
  ORGANISM  Kocuria tytonicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Kocuria tytonicola"
                     /db_xref="taxon:2055946"
     gene            1..346
                     /gene="trxB"
     Protein         1..346
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36084
     Region          40..345
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msnqsgifss avnlgvtgaa rsapadashp aadagddavh dvvivgsgpa gytaaiytar
       61 anlkpvvlag svtaggelmn ttevenypgf idgimgpelm dnmqqqaerf gadiryedvv
      121 sveldgevkt vttedgtvlr aravvistgs ayrklglpde erlsghgvsw catcdgfffk
      181 gqnvavvggg dsaieeatfl tkfadkvtli hrrdqfrasd imkqralddp kieilwntrv
      241 sgirgenkva aleledtvtg easelpvtgv fvaigsdprv dlvkdqlelt vdstiavdgr
      301 ssttslpgvf aagdvvdpty rqaitaagsg cvaavdvehy laalds
//
LOCUS       WP_121852733             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Parashewanella spongiae].
ACCESSION   WP_121852733
VERSION     WP_121852733.1
KEYWORDS    RefSeq.
SOURCE      Parashewanella spongiae
  ORGANISM  Parashewanella spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Parashewanella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Parashewanella spongiae"
                     /db_xref="taxon:342950"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33819
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msqarhckll ilgsgpagyt aavyaaranl npvmitgiqq ggqlttttev enwpgdaddl
       61 tgpalmermq khaekfdtei ifdhinetdl sqrpfklkgd sgeytcdali iatgasaryl
      121 glesetafqg kgvsacatcd gffyrnqkva vigggntave ealylsnias evhvihrrdt
      181 frsekiladr mmkkvadgni tlhlnqtmde vvgddmgvtg lkmkstsdgs isdlevagvf
      241 vaighspntg ifdgqlemnn gyikvqsglq gnatqtsveg vyacgdvmdq hyrqaitsag
      301 agcmaaldae rfldsqd
//
LOCUS       WP_121853020             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Parashewanella spongiae].
ACCESSION   WP_121853020
VERSION     WP_121853020.1
KEYWORDS    RefSeq.
SOURCE      Parashewanella spongiae
  ORGANISM  Parashewanella spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Parashewanella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Parashewanella spongiae"
                     /db_xref="taxon:342950"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53732
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipkeql enetrvaatp tsviqlkklg fdviveqgag laanfddnlf lqsgaqlsds
       61 vlnadiifkv naptdseikq mkpgtilisf vwpaqhpdlv dllakqqitv lamdmvpris
      121 raqsldalss manisgyrav veaahefgrf ftgqitaagk vppakvlvig agvaglaaig
      181 sagslgaivr afdtrlevae qiesmggqfl klefdnkegd asdgyakvms defiaaemal
      241 faeqakdvdi iittaqipgk tapklissem vasmksgsvi vdlaagsggn vepsvagkki
      301 itdngvtvig ytdlasrlas qssqlystnl vnlmkllckq kdgqvaldfd dvvtrnmtvt
      361 hqseimfppp pisvsaapsk pkvtekvetq apkqpsktky vigtlgiaaf maiaatapad
      421 flshftvfil scivgyyvvw nvshslhtpl msvtnaisgi ivvgallqig hdsllikala
      481 ffavliasin ifggftvtqr mlkmfrkg
//
LOCUS       WP_121855908             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Enterobacteriaceae].
ACCESSION   WP_121855908
VERSION     WP_121855908.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae (enterobacteria)
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53602
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gtteaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_121856181             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Escherichia coli].
ACCESSION   WP_121856181
VERSION     WP_121856181.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36100
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiiniyskr qrkirgevnd vyqynnipha lrvqifkiit dsigfpssne rytsyrnead
       61 kvyayiheil skeygvfslk efakndfdal vdfflkernt ekcldfieic fqilvshvak
      121 nhyefkdits qspgdaviel nerfrehgvs yqfeseeiir idsqlihadv vkptlillsg
      181 eplfegande flaahehyrh krykeclndc lksfesimka ihdknnwkys pndtasklin
      241 sclsqnlipa ylqsqftslk tmletgipti rnknaghgqg adikevpeel asymlhltat
      301 nllfllkcek nik
//
LOCUS       WP_121860631             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia sp. Nafp2/4-1b].
ACCESSION   WP_121860631
VERSION     WP_121860631.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Nafp2/4-1b
  ORGANISM  Burkholderia sp. Nafp2/4-1b
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia sp. Nafp2/4-1b"
                     /db_xref="taxon:2116686"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34249
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlvtgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfq ehaerfntei vfdhihtakl heqpirligd sgeytcdsli iatgasaqyl
      121 glpseeafmg kgvsacatcd gffyrnqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegvv dikwdhvlde vtgedsgvtg lriknvktge kqdltvqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglq gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_121862944             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Nafp2/4-1b].
ACCESSION   WP_121862944
VERSION     WP_121862944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Nafp2/4-1b
  ORGANISM  Burkholderia sp. Nafp2/4-1b
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia sp. Nafp2/4-1b"
                     /db_xref="taxon:2116686"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55036
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatgerrvat vpevveklik lgfsvavesg agaganfddd ayraagasia
       61 ataaelwsgs divfkvrpps aeevallreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvrtm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvve elcknkdgti nvdfdddair
      361 gltvikegnv twppppikqa vvapkpaaaa paaaapaksk ghghagepms akalaivfai
      421 galafllvgq fapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapplge lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_121863936             346 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Kocuria tytonicola].
ACCESSION   WP_121863936
VERSION     WP_121863936.1
KEYWORDS    RefSeq.
SOURCE      Kocuria tytonicola
  ORGANISM  Kocuria tytonicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Kocuria tytonicola"
                     /db_xref="taxon:2055946"
     gene            1..346
                     /gene="trxB"
     Protein         1..346
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36170
     Region          40..345
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msnqsgifss avnlgvtgaa rsapadvshp aadagddavh dvvivgsgpa gytaaiytar
       61 anlkpvvlag svtaggelmn ttevenypgf idgimgpelm dnmqqqaerf gadiryedvv
      121 sveldgevkt vttedgtvlr aravvistgs ayrklglpde erlsghgvsw catcdgfffk
      181 gqnvavvggg dsaieeatfl tkfadkvtli hrrdqfrasd imkqralddp kieilwntrv
      241 sgirgenkve aleledtvtg easelpvtgv fvaigsdprv dlvkdqlelt vdstiavdgr
      301 ssttslpgvf aagdvvdpty rqaitaagsg cvaavdvehy laalds
//
LOCUS       WP_121872821             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhodococcus sp. SBT000017].
ACCESSION   WP_121872821
VERSION     WP_121872821.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. SBT000017
  ORGANISM  Rhodococcus sp. SBT000017
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rhodococcus sp. SBT000017"
                     /db_xref="taxon:1803385"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35055
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkvhdli ivgsgpagyt agvyaarael epilfegtqf ggalmtttev enfpgfregi
       61 mgpdlmeqmr eqaqrfgadi rtedveeldl tgpiktvsag getyraraii lamgaaaryl
      121 sipgeekllg rgvsacatcd gfffrdqdia vigggdsame eatfltrfar svtivhrrse
      181 frasrimler aknndkirfl tdtkvlevlg dtsvtglsle haetgekttl dvtgmfvaig
      241 hdprnelvkg qvelddagyv kvaspssats vegvfaagdl vdhvyqqait aagtgctasi
      301 daerwlaeqg dittntleha dqpvdavna
//
LOCUS       WP_121873691             372 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Rhodococcus (in: high G+C Gram-positive
            bacteria)].
ACCESSION   WP_121873691
VERSION     WP_121873691.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
  ORGANISM  unclassified Rhodococcus (in: high G+C Gram-positive bacteria)
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="unclassified Rhodococcus (in: high G+C
                     Gram-positive bacteria)"
                     /db_xref="taxon:192944"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38033
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqstekg sgsttvvgvv resgegerrv alvpkivasl tgkgveivve sgaglgalip
       61 delyvaagat igdpwsadvv vkvappsdae iakltsgstl igflaprnae nsigalkaag
      121 vqafaveaip risraqvmda lssqanvagy kavllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rptgydvrpe vadqvrsvga qwldlgidaa geggyarelt
      241 edervqqqka leeaikgfdv vittalvpgr paprlvtaaa vegmkpgsvv vdlagetggn
      301 celtepgetv vkhdvticsp lnlpasmpeh aselysknis allelmlvdg klapdfsdev
      361 lagacvtrek en
//
LOCUS       WP_121875051             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Providencia].
ACCESSION   WP_121875051
VERSION     WP_121875051.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Providencia"
                     /db_xref="taxon:586"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53476
     Region          8..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 makiinrtly llslvagiwl ltpavhaqta skeasstint knesfaqahp dqyhswrats
       61 eqsqredala edprlvilwa gypfsrdynk prghayalid vretlrtgap kdaqdgplpm
      121 acwsckspdv arliqeqged eyfhgkwakg gpeivnvlgc adchktdspe faqgqpaltl
      181 trpyaarame aigkpfdkas rfdqqsmvcg qchveyyfag enksvkfpwd ngtkvedmev
      241 yydniafsdw tnslskapml kaqhpeyetw sagihgknnv tcidchmpkl qnekgelyts
      301 hkignpfdnf eqtcrnchtq skqelqavva erkqaiqemk ikvedqlvha hfeakaawda
      361 gatkkemapi ladirhaqwr wdlaiashgi hmhapeeglr mlggamnkaa dartklvrll
      421 gakgitheia ipdistkeka qqaigldmqk inaekqeflk tvvpewdaqa rknnllsq
//
LOCUS       WP_121876417             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Umboniibacter marinipuniceus].
ACCESSION   WP_121876417
VERSION     WP_121876417.1
KEYWORDS    RefSeq.
SOURCE      Umboniibacter marinipuniceus
  ORGANISM  Umboniibacter marinipuniceus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Umboniibacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Umboniibacter marinipuniceus"
                     /db_xref="taxon:569599"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33828
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdikhhrli ilgsgpagys aavyaaranl npviitgmqq ggqlttttdv dnwpgdaegv
       61 qgpelmmrmq ahaerfdtei vfdhilkadl sqrpfvlqgn etyscdalii atgasamylg
      121 lesetefqgk gvsacatcdg ffyrgqkvav vgggntavee alylsniase vtlihrrdsl
      181 rcekiladkl fekekngnvt ilwnhtldev lgdemgvngi rlndlsnnts knldiaglfi
      241 aighrpntel fvdqlemnsg yltiqsglqg natqtsipgv faagdvadqv yrqavtsagf
      301 gcmaaldaek yldel
//
LOCUS       WP_121885264             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingomonas sp.
            PP-F2F-G114-C0414].
ACCESSION   WP_121885264
VERSION     WP_121885264.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. PP-F2F-G114-C0414
  ORGANISM  Sphingomonas sp. PP-F2F-G114-C0414
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sphingomonas sp. PP-F2F-G114-C0414"
                     /db_xref="taxon:2135662"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34124
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtthttrmli lgsgpaglsa aiygaragma pivvqgiqpg gqlttttdve nypgfkdviq
       61 gpwlmeqmta qaehvgtrmm wdtvtqvdlt srpfrligds gdvyegdtlv iatgaqakwl
      121 gidseepmkg kgvsacatcd gffyrgkkva vigggntave ealyltnhsp dvtlihrrds
      181 lrsekilqer lfahkgvtvl wnkevrefvd gggnaglval eledtvtger srlavdggfv
      241 aighhpatel frghidldsd gyisveigst rtsvegvfac gdvadkvyrq avtaagtgcm
      301 aaldaerfla aaefaelaea ae
//
LOCUS       WP_121889484             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces shenzhenensis].
ACCESSION   WP_121889484
VERSION     WP_121889484.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces shenzhenensis
  ORGANISM  Streptomyces shenzhenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces shenzhenensis"
                     /db_xref="taxon:943815"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34257
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfrdgim
       61 gpelmdnmra qaerfgaelv pddvvsvdlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedtlsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfv wdsevaeiqg dpklsglklr nlktgelsdl pvtglfiaig
      241 hdprtelfkg qldldgegyl kvdapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala deekaaepek tsv
//
LOCUS       WP_121898590             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodophyticola porphyridii].
ACCESSION   WP_121898590
VERSION     WP_121898590.1
KEYWORDS    RefSeq.
SOURCE      Rhodophyticola porphyridii
  ORGANISM  Rhodophyticola porphyridii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Rhodophyticola.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Rhodophyticola porphyridii"
                     /db_xref="taxon:1852017"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55850
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkevg qgesrvamtp dsalqlqklg ydcaietgag laagfsdaly eeagveiikt
       61 paglwkavdi iakvrpptet eakrlkhgql lisffypgqn ealmelarsk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvflefee sgqdssstgg yaapsspefr
      241 ekqlekfrel apemdivitt alipgrdapv lwtkdmvemm kpgsvivdla aerggncelt
      301 ekdekivsdn gvtiigytdf psrmaaqsst lystnirhmm tdltpekdgq vkhdmeddvi
      361 rgatavhdge itfpppppkv aaiaaaprkq aakdltpeek raqelaafks qtksqvtlla
      421 vgaalvlgvg lipgmpasfm qhfivfvlsv figfqviwnv ahslhtplma vtnaissiii
      481 lgaliqigss svlitilgal gifmasvnif ggflvtrrml amfqks
//
LOCUS       WP_121899171             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhodophyticola porphyridii].
ACCESSION   WP_121899171
VERSION     WP_121899171.1
KEYWORDS    RefSeq.
SOURCE      Rhodophyticola porphyridii
  ORGANISM  Rhodophyticola porphyridii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Rhodophyticola.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Rhodophyticola porphyridii"
                     /db_xref="taxon:1852017"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35148
     Region          9..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetrhspvl iigsgpagyt aavyasraml kpvlvqgiqp ggqltittdv enwpgdssvm
       61 gpdlmvrmen hakemgteii sdhimsldls arpftaigds gttytadavi latgaqakwl
      121 glpsedhfkg fgvsacatcd gffyrgqeiv vigggntave ealfltnfas kvtlihrrds
      181 lraekimqnr lfknskievl wnhtveeivg tdeprgvegv rakhvesgei tevpckgffv
      241 aighspstel vkdqlemhng gyvkvepgst rtsipgvfaa gdltdhiyrq avtsagmgcm
      301 aaldaekfla eqdgetvada gvyavatdaa e
//
LOCUS       WP_121900039             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tessaracoccus antarcticus].
ACCESSION   WP_121900039
VERSION     WP_121900039.1
KEYWORDS    RefSeq.
SOURCE      Tessaracoccus antarcticus
  ORGANISM  Tessaracoccus antarcticus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Tessaracoccus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Tessaracoccus antarcticus"
                     /db_xref="taxon:2479848"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33450
     Region          6..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msekihdvii vgsgpagyta aiyaaraale pvlfegslds ggalmnttev enypgfaegi
       61 mgpdlmlamr aqaerfgtqi itddatelkl tgavkevtds dgvvwrsrav ilamgsgyrk
      121 lgiddedrls grgvswcatc dgaffrnkdi avvgggdsam eeatfltrfa nkvtvihrrd
      181 elrasaimag rakrdpkief awnssvsgig gensvesitl tdtvtgqhre vpmqglfiav
      241 ghdprselvt dqveldedgy vltqpdstgt nlvgvfacgd lvdhtyrqai taagsgcaaa
      301 ldaekylaal ddmaata
//
LOCUS       WP_121902257             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tessaracoccus antarcticus].
ACCESSION   WP_121902257
VERSION     WP_121902257.1
KEYWORDS    RefSeq.
SOURCE      Tessaracoccus antarcticus
  ORGANISM  Tessaracoccus antarcticus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Tessaracoccus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Tessaracoccus antarcticus"
                     /db_xref="taxon:2479848"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53072
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigiplevt pgenrvaatp ktvrqlialg ydvvvqegag sraafddagy aeagasvadv
       61 naawhsdvvl avnpptddqi aalrvgatli tflaprqdae ltaklsaqgv talsmdmvpr
      121 tsraqaldal samanisgyr avveaahafg rfftgqvtaa gkvppakvlv agtgvaglaa
      181 igaanamgai vratdvrpet aeqvesmgat flhvrsedqg vssdgyakev gadyadrarq
      241 lyaeqaadvd iiittaaipg rpspklitad mvasmhngsv ivdlaaqggg nceltkpges
      301 wvtdngvtii gwtdlasrlp gqssqlygtn lvnaltlmtp akdgqlvldf dddvvrtmtt
      361 vrngeitfpp ppievsaaap avvvraapap ppkpkkpgpw wlpvvwvgla gmaliallti
      421 spsnfvtlfg ifvlagvvgy yvvwnvtyal htplmsvtna isgiiivgam tqladenpvv
      481 kgisfvaivl aainvfggft vthrmltmfr kg
//
LOCUS       WP_121907187             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Ulvibacter antarcticus].
ACCESSION   WP_121907187
VERSION     WP_121907187.1
KEYWORDS    RefSeq.
SOURCE      Ulvibacter antarcticus
  ORGANISM  Ulvibacter antarcticus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Ulvibacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Ulvibacter antarcticus"
                     /db_xref="taxon:442714"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34214
     Region          9..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtierikc liigsgpagy taaiyaarad lkpimytgme pggqltttte vdnfpgypeg
       61 idgptmmvql qqqaerfgtq vrigmvtave fsevhggihk itvdnttqle aetviistga
      121 takylglpse qklrgggvsa cavcdgffyk gqdvaivgag dtaaeeatyl anicknvtml
      181 vrkdqmrask amqhrvtatk ninvryntev devlgdmvve glrmknnqtg ekeeiaitgl
      241 fiaighkpnt difkgqlkmd ntgylitegk stktnkpgvf asgdvqdkey rqavtaagtg
      301 cmaaldaery lvsiesevta
//
LOCUS       WP_121912782             314 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Bifidobacterium].
ACCESSION   WP_121912782
VERSION     WP_121912782.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium
  ORGANISM  Bifidobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Bifidobacterium"
                     /db_xref="taxon:1678"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33260
     Region          6..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkqtvhdaiv igsgpagyta aiylgragya plviagaltp ggqlmnttev enfpgfpkav
       61 lgpdlmdqmr dqaehfgaqi eyddvvsvdl sgdvkrittd ggeeyqarvv vittgsqyrk
      121 leipgerefs grgvsycatc dgfffkdkpi vvvgggdsam gdadfltrfg ssvtlihrrq
      181 gfraskimvd rakandkinf lldsvvtrin gddsgvtsld vrntatdqqs tipangvfva
      241 igftpqtafl ngqvdldqdg yilveggstk tsapgvfaag dvtdkiyrqa isaagmgcra
      301 aldaqeylts ldnr
//
LOCUS       WP_121911777             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corynebacterium macginleyi].
ACCESSION   WP_121911777
VERSION     WP_121911777.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium macginleyi
  ORGANISM  Corynebacterium macginleyi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Corynebacterium macginleyi"
                     /db_xref="taxon:38290"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33091
     Region          4..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtvhdvaivg sgpagytaal yaaraelspi vfegfeygge lmntteveny pgfqkgimgp
       61 elmeemraqs irfgadlrme vvdsvelege ikklhvgdev feartvilat gaaprhlgvp
      121 geeelsgrgv stcatcdgff fkghniavig ggdsameeat fltkfaesvt ivnrsekfra
      181 skimlerare neqikwetnk vvervledng kvgglqlkdv etgetstldv tamfvaighd
      241 prssflngqv kldengyvkv dqpstktslp gvfacgdlvd dhyqqaitaa gsgcraaida
      301 eqflaanr
//
LOCUS       WP_121915985             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Dokdonia sinensis].
ACCESSION   WP_121915985
VERSION     WP_121915985.1
KEYWORDS    RefSeq.
SOURCE      Dokdonia sinensis
  ORGANISM  Dokdonia sinensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Dokdonia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Dokdonia sinensis"
                     /db_xref="taxon:2479847"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35210
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msvehvkcli igsgpagyta aiyaaranmk pvlyqgtqpg gqltttneve nfpgyvdgvt
       61 gpemmiqlqk qaerfdtdvr dgwitkvdft gpvhkawvng dkeihantvi istgasamyl
      121 gleseqkylk lgggvsacav cdgffyrnqe vvivgagdsa ceeahylskl ckkvtmlvrr
      181 defraskime arvrntenie ilfnteteev lgdgqvvtgv rvvnnktket heipatgffv
      241 aighkpntdi fkdyldldat gyiknipgta ktnvdgvfvs gdaadhvyrq aitaagtgcm
      301 aaldaeryla asevfprdka gvnsty
//
LOCUS       WP_121925954             315 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Flavobacterium].
ACCESSION   WP_121925954
VERSION     WP_121925954.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium
  ORGANISM  Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Flavobacterium"
                     /db_xref="taxon:237"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33933
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtieklkc liigsgpagy taaiyaaran mfpvlyqgmq pggqltttne venwpgnpeg
       61 itgpemmvgl qaqaerfgtd vrdgwatkvd fsgdifkvwi ngekelhces viistgasak
      121 ylglpseqhy lkmgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rsekfraski mearvrkten itilmnhdti evlgdeqvvt gvkalnkttn etfeipatgf
      241 fvaighkpnt difkeyisld etgyiintpg ssktnvegvf vagdaadhvy rqaitaagtg
      301 cmaaldaery laake
//
LOCUS       WP_121930527             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter sp. 2JN-4].
ACCESSION   WP_121930527
VERSION     WP_121930527.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. 2JN-4
  ORGANISM  Acinetobacter sp. 2JN-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter sp. 2JN-4"
                     /db_xref="taxon:2479844"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39597
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgesrvaatp etvkklinag hsvviergag vkaayidsay eqvgaaitdd
       61 aytgsqiilk vrapsgneiq klaantavia mfdpyrnsel dqfaaqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgaiv eatdlrptak eqveslggkw ldvpmsdeek qkaadaakng ygwmpgeqyi
      241 qdqaaivdka vsnadivitt allpgrnapr likaetvakm kpgsvildma vetggnvegs
      301 kegetvttdn gvkilgipni pgtvateasa lyarnvfnfl etlfdkdkaf ainqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_121930714             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter sp. 2JN-4].
ACCESSION   WP_121930714
VERSION     WP_121930714.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. 2JN-4
  ORGANISM  Acinetobacter sp. 2JN-4
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acinetobacter sp. 2JN-4"
                     /db_xref="taxon:2479844"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33579
     Region          8..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnarhsrlii lgsgpagysa avyaaranlk ptliagiqlg gqlttttevd nwpgdpeglt
       61 gpvlmdrmqa haerfgtelv ydhinevdlk trpfvlkgdm aeytcdalii atgataqylg
      121 leseaafmgq gvsacatcdg ffyknqnvmv vgggntavee alylsniaah vtlvhrrdsl
      181 rsekilqdhl fakekegkis iiwnhqvdev lgdktgvtsv rikstqdsst qdvqvqglfv
      241 aighkpntsm fdgqlnlrdg yiqvqsgtsg nataasiegv faagdvadsi yrqaitsags
      301 gcmaaldaek yldnsn
//
LOCUS       WP_121934913             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Faecalibacter macacae].
ACCESSION   WP_121934913
VERSION     WP_121934913.1
KEYWORDS    RefSeq.
SOURCE      Faecalibacter macacae
  ORGANISM  Faecalibacter macacae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Faecalibacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Faecalibacter macacae"
                     /db_xref="taxon:1859289"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33482
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mssnildtii igsgpagyta aiyaaranmn plvltgmepg gqlttttevd nfpgypngit
       61 gpelmadlqk qaerfgtkiq yeyvtevifg enngdvhtvk tntaeyqtks viistgasak
      121 ylglddekky agsgvsacat cdgffyrgkd vavvgggdta aeeatylakl cnkvyllvrk
      181 demraskamq drvantpnle vlynhellgl dgnqvvekak iinnvtneen elivdgvfia
      241 ighkpntdlf kgkldmdetg ylitqgrsya tnipgvfaag dvqdsvyrqa isaagsgcaa
      301 aldaeryvae ffeg
//
LOCUS       WP_121937497             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Eilatimonas milleporae].
ACCESSION   WP_121937497
VERSION     WP_121937497.1
KEYWORDS    RefSeq.
SOURCE      Eilatimonas milleporae
  ORGANISM  Eilatimonas milleporae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Kordiimonadales; Kordiimonadaceae; Eilatimonas.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Eilatimonas milleporae"
                     /db_xref="taxon:911205"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33823
     Region          7..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msttkhtkll iigsgpagyt aaiyaarasl dpmivtgmqa ggqltittdv enypgfatav
       61 qgpdlmeamr qqaenvgtdi iydtitevdl katpkraigd sgtiytadtv vistgaqakw
      121 lgleseqafn gygvsacatc dgffyrgkdv vvvgggntav eealylsnla ksvtllhrrd
      181 slraekilqn rlfktenvtv rwdsvldevv gtdnpksvtg vrikntktga vedlavdgvf
      241 iaightpstq ifkgqlpmdd egyilktads tatdipgvya agdvtdkvyr qavtaagmgc
      301 maaleaekyl aaledateea a
//
LOCUS       WP_121941273             532 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. 100].
ACCESSION   WP_121941273
VERSION     WP_121941273.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. 100
  ORGANISM  Acidovorax sp. 100
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Acidovorax sp. 100"
                     /db_xref="taxon:2135635"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55471
     Region          11..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtspvpqpq rigvpretlp gekrvatvpd vvekliklgf svtvesgagd ganfsddayr
       61 aagaeivgda aslwaasdiv fkvrppssde valmregttl idfiwpaqnp elmqqlaark
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rkmyaeqakd adiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg qavvrhgvti vgytdlasrl akqsstlyat nllrlteelc kakdgvavvn
      361 meddairglt vvkegsitwp applkqapap apkaaapvae kksshgtgap msaktltivf
      421 avlavlfwai gayapvaflg hftvfvlacf igymvvwnvt palhtplmsv tnaissiiai
      481 galvqiappd agingrpdgl ilwlafaalv ltainmfggf avtrrmlamf rk
//
LOCUS       WP_121943513             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acidovorax sp. 100].
ACCESSION   WP_121943513
VERSION     WP_121943513.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. 100
  ORGANISM  Acidovorax sp. 100
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acidovorax sp. 100"
                     /db_xref="taxon:2135635"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33856
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msttqhakvl ilgsgpagyt aavyaaranl npvlitgmaq ggqlmtttev dnwpadvhgv
       61 qgpelmqrfl ehaerfktqi ifdhinkvdf skrpftlagd sgtytcdali latgasakyl
      121 glpseeafmg kgvsgcatcd gffyreqdvc vvgggntave ealylsniar kvtlvhrrdk
      181 fkaepilvdk lnekvaagki elklfhtlde vlgdntgvtg irikstkdgs tediklqgcf
      241 iaighapnte ifqgqlemen gyiitqgglk gfatqtsvpg vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq rfleqes
//
LOCUS       WP_121954964             512 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudoalteromonas].
ACCESSION   WP_121954964
VERSION     WP_121954964.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53926
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkeih tgerrvattp dvvskltklg fdvvietgag maanyadday geagckivns
       61 aqdvwaqsdi ilkvqapegd entllksgqt licflwpaqn pvmlkdltqr gitaiaidsi
      121 prisraqkmd arssmanisg yraiveaaqh fgrfftgqit aagrvapakv lvigagvagl
      181 aaigaaksmg aivrsfdtra evkeqiesmd aeflmldfkd edgsgeggya kvmsdefiea
      241 emalfaaqak dvdiivttal ipgkpapkli tsemvasmks gsvivdlaae qggnceltvp
      301 gkvavchgvs iigytdlpsr laaqssqlys nnlhnllaem tpekdgklfv dmtndvvlga
      361 tictegkttw pppaptlsap pkkvaatpkp kptivekkks vfgpiigaai galallglgg
      421 vapadfmshf tvfvlacfvg ymviwsvspa lhtplmsvtn aissiiviga liqisstddt
      481 ikwfavftvl iasinivggf avthrmlkmf rk
//
LOCUS       WP_121957836             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Petrotoga sp. 9PWA.NaAc.5.4].
ACCESSION   WP_121957836
VERSION     WP_121957836.1
KEYWORDS    RefSeq.
SOURCE      Petrotoga sp. 9PWA.NaAc.5.4
  ORGANISM  Petrotoga sp. 9PWA.NaAc.5.4
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Petrotogales;
            Petrotogaceae; Petrotoga.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Petrotoga sp. 9PWA.NaAc.5.4"
                     /db_xref="taxon:1434328"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36249
     Region          18..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mffnvenvgk kfqlkeeyev vivgggpagi aasiyalqgg asalvvekav eggqmnitdi
       61 ienypgfksi rgeelstlmk ehashfgvef ypaqvnsief kdnlkltkld ngelvkskvv
      121 iiasgskpkk levkgekefs skgvsycasc dghffkdkki avvgggntav eeavylsnia
      181 kevyiihrrd elradklyqe rafnkpnikf kwnsvveeik gkekveslki kdlktgeiye
      241 ekfdgififi gllpetsfld itkfetdeyg fivtdenmet kiegvyaigd vrhknvrqiv
      301 tavsdgaiaa shavreridq sqsklki
//
LOCUS       WP_121959709             333 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Petrotoga].
ACCESSION   WP_121959709
VERSION     WP_121959709.1
KEYWORDS    RefSeq.
SOURCE      unclassified Petrotoga
  ORGANISM  unclassified Petrotoga
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Petrotogales;
            Petrotogaceae; Petrotoga.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="unclassified Petrotoga"
                     /db_xref="taxon:2620614"
     gene            1..333
                     /gene="trxB"
     Protein         1..333
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36845
     Region          18..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mffnvegank kseikqqydv viigggpagi saaiyalqgg astlviekai eggqmnltdi
       61 ienypgfkti kgeelsslmk ehaeqfgadf ydgkvielkd edshktvvme ngktikskai
      121 iiasgsyprk lgvkgeeefs srgvsycasc dghffknkki avvgggntav eeavylsnia
      181 kevyiihrre klradklyqd rafsrnnikf kwnsvieeik gkdkveslvi knlkndevye
      241 epfdgvfvfv glvpetsfln kdlfdfdeyg flitdenmet kvkgiyavgd vrkkelrqiv
      301 tavsdgaiaa shaireyvne dqisstqsin ltk
//
LOCUS       WP_121967387             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Myroides sp. N17-2].
ACCESSION   WP_121967387
VERSION     WP_121967387.1
KEYWORDS    RefSeq.
SOURCE      Myroides sp. N17-2
  ORGANISM  Myroides sp. N17-2
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Myroides.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Myroides sp. N17-2"
                     /db_xref="taxon:2030799"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33598
     Region          8..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstiervkcl iigsgpagyt aaiyaaranm apvmyqgmqp ggqltttnev enfpgypegv
       61 tgpemmmqlq aqaqrfgtdi rdgwvtkael tgevkkvwvn ettevhadtv iistgataky
      121 lglpseqhyl slgggvsaca vcdgffyrnq evvivgagds aceeahylsq lckkvtmlvr
      181 tdkfrasrim eervrkteni eillntstde vlgdgnvvtg irvknnvtge ltdipatgff
      241 vaighkpntd ifkgelemde tgylqthgkt sktnvagvfa cgdvqdkdyr qaitaagsgc
      301 iaaldaeryl aak
//
LOCUS       WP_121979219             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lentilactobacillus raoultii].
ACCESSION   WP_121979219
VERSION     WP_121979219.1
KEYWORDS    RefSeq.
SOURCE      Lentilactobacillus raoultii
  ORGANISM  Lentilactobacillus raoultii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lentilactobacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Lentilactobacillus raoultii"
                     /db_xref="taxon:1987503"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33843
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maksydvvvi gagpggmtaa lyasranlsv amvdrgiygg qmnntaaien ypgfksimgp
       61 dlaqqmydss vnfgaeyvyg svesvedkge vklvktdsde leakvviiat gseykklgip
      121 geheyggkgv sycavcdgaf frhknvvvvg ggdsaieeas ylagivdhvt vihrrdqlra
      181 qkvlqdrafe ndkidfvwns nvtevlgdgk kvtavkvvnn qtnetselet sgvfiyvgll
      241 pmtepfanlk itnedgwikt ndqmetavpg iyaigdvrqk elrqittavg dggiagqqaf
      301 kyvealsskg qteaar
//
LOCUS       WP_121980281             320 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Acinetobacter].
ACCESSION   WP_121980281
VERSION     WP_121980281.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34030
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttdvd nwpgdpeglt
       61 gpalmermqa haerfgteiv ydhinevdls qrpfvlkgdm eeftcdalii ctgataqylg
      121 leseaaymgq gvsacatcdg ffyknqkvmv vgggntavee alylsniash vtlvhrrdsl
      181 rsekilqdhl fakekegkis iiwnhqvdev lgdaqsgvts vrlkstqdds tqnvdvtgmf
      241 vaighkpnsa mfegqlelrd gyiqvqsgta gnatqtsvpg vfaagdiads iyrqaitsag
      301 sgcmaaldae kyldamgkld
//
LOCUS       WP_121985865             434 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Brucella/Ochrobactrum group].
ACCESSION   WP_121985865
VERSION     WP_121985865.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..434
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44959
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke sdpnesrvaa saetvkkfia lgfdvvvekg ageksripda efiaagarig
       61 taadaktadv vlkvrrpsda elkgyksgaa lfamldpygh edavaalaka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vskemvasmr pgsvlvdlav erggnvegai
      301 agqiaevngv kivghlnvpg riaasasqly arnliafvet lvdketkllk idpedelvka
      361 tllthqgkil hpafakaeta paeaaekavk pkaapkpkae kpaakaaakp akktpakapk
      421 tpsspkspvd ggea
//
LOCUS       WP_121985992             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase
            [Brucella/Ochrobactrum group].
ACCESSION   WP_121985992
VERSION     WP_121985992.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34382
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqrhapviv igsgpagyta aiyaaramlk piviaglqqg gqlmittdve nypgyadpvq
       61 gpwmmdqmat qaqnvgaeiv hdiitevett vrpfrlkgds gtvytcdali iatgaqakwl
      121 gldseqtfmg ggvsacatcd gffyrgkdvv vvgggntave ealylshiak svtvvhrrdg
      181 fraekimqdr llsrqnvsvi wnsvideilg teakppmgat vtgvrlknvv tcetqeldth
      241 gvfvaighap avslfegklk qkpngylwta pdstatdvpg ifaagdvtdd iyrqavtaag
      301 mgcmaaleae rwlaaqeplh eaae
//
LOCUS       WP_121987837             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nitrospira lenta].
ACCESSION   WP_121987837
VERSION     WP_121987837.1
KEYWORDS    RefSeq.
SOURCE      Nitrospira lenta
  ORGANISM  Nitrospira lenta
            Bacteria; Pseudomonadati; Nitrospirota; Nitrospiria; Nitrospirales;
            Nitrospiraceae; Nitrospira.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Nitrospira lenta"
                     /db_xref="taxon:1436998"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32355
     Region          3..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrdvviigsg pagltaaiya aranlaplli egwqsggqli tttevenypg fakgimgpel
       61 mkdmrtqagr fgtefltadv tavnfaqrpf tltvdgeqti ytqtviiatg asaipiglkn
      121 esrltghgvs tcatcdgffs kgkellvvgg gdsaleeaif ltkfatkvsl vhrrdtlras
      181 kimqdralhn ekisfiwntv vedilgsevv tgarlknvvt gkisevpcag ifvaighrpn
      241 tslfagqvdm dekgyirtyr gtttnvpgvf aagdvqdsty rqavtaagsg cmaaidaerf
      301 lesqh
//
LOCUS       WP_122013887             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Biomaibacter acetigenes].
ACCESSION   WP_122013887
VERSION     WP_122013887.1
KEYWORDS    RefSeq.
SOURCE      Biomaibacter acetigenes
  ORGANISM  Biomaibacter acetigenes
            Bacteria; Bacillati; Bacillota; Clostridia;
            Thermosediminibacterales; Tepidanaerobacteraceae; Biomaibacter.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Biomaibacter acetigenes"
                     /db_xref="taxon:2316383"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32434
     Region          3..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkdvaiigag paglsagiya araklstviv ekmypggqaa itdrienypg fnegiggsel
       61 tdnmkaqaek fgaellngdv igikkenekf iiqltgetle aktvilamga esrklgvkge
      121 keytgrgvsy catcdgafyt dkpimmvggg dtaieealyl trfaesikvv hrrdqlratk
      181 ilqerafkne kikfiwnsvv deikgqdmve evivknvktg ektsvlvngv fvaiglvpnt
      241 sfvkdlvkln eqgyiitden mgtgvpglya agdvrqkslr qvvtavadga iaaveagkyl
      301 esl
//
LOCUS       WP_122017978             308 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Lactobacillus].
ACCESSION   WP_122017978
VERSION     WP_122017978.1
KEYWORDS    RefSeq.
SOURCE      unclassified Lactobacillus
  ORGANISM  unclassified Lactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="unclassified Lactobacillus"
                     /db_xref="taxon:2620435"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33384
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqkydviii gagpggltaa lyasranlsv lildrgpygg qmnntdaidn ypgfseikgp
       61 elgekmynsv mkfgakfeyg dvqtvtvern tklvktdtge ysapvliiat gadhrhldvp
      121 gedeysgkgv sycavcdaaf fkdedlavig ggdsaieegi ylaqnaksvt vvhrrdqlra
      181 qptlqkrafa nekmhfiwda etasiegdgn rvtgitykdk ktaelkhlsv hgvfiyvgvi
      241 pqttafknld ildqngwipt dehmktkhdg vfaigdvrak dlrqianavg dgsiagqeay
      301 nylqalnd
//
LOCUS       WP_122019823             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            campbellii].
ACCESSION   WP_122019823
VERSION     WP_122019823.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53007
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmsap iavatlfasq lflvgaplaa edkglvdprn dvfeqnhpdq yhswkatses
       61 ehiedalged pnmvilwagy gfakdynkar ghfyalddvr qtlrtgapsd eksgpmpmac
      121 wsckspdvar vidergedgy fegkwarlgs eivnpigcsd chdtrseefk kgepalavtr
      181 pyverafdti gknfdeqsrl dkqasvcaqc hveyyftgpt kavkfpwdmg ttvndmekyy
      241 dalnfkdwth avskapmlka qhpgyetwrd gihgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfed tcaqchtqtk eqlqgivstr kaqvlnmklt aekqivaahf eagaawkaga
      361 teaemepilq dirhaqwrwd yaiashgvhm hapevalevl gtavdraada rtklvrllat
      421 kgitdpvqip distkakaqq algmdmdkmn adkkhfletv vpdwdkaaae reaty
//
LOCUS       WP_122020603             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            campbellii].
ACCESSION   WP_122020603
VERSION     WP_122020603.1
KEYWORDS    RefSeq.
SOURCE      Vibrio campbellii
  ORGANISM  Vibrio campbellii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio campbellii"
                     /db_xref="taxon:680"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54536
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agesrvaasp ksveqliklg fdvaiesqag vlasfddaay eaagakivss
       61 eevwtsglil kvnaplvdee kgideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgkpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqvitta ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg nididfedvv
      361 lrgvtvvkeg evtwpappiq vsaqpqakpq epvkpqpkde eptspvkkfg alavglgafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_122021476             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lactobacillus sp. ESL0230].
ACCESSION   WP_122021476
VERSION     WP_122021476.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus sp. ESL0230
  ORGANISM  Lactobacillus sp. ESL0230
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Lactobacillus sp. ESL0230"
                     /db_xref="taxon:2069353"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33261
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqnydviii gagpggltaa lyasranlsv llldrglygg qmnntdaidn ypgfseikgs
       61 elgekmynsi mkfgakfeyg dvqqvslegn ykvvttdtge yrapaliiat gadhrhlnip
      121 gedeyagkgv sycavcdaaf fknediavig ggdsaieegi ylaqnaksvt vihrrdqlra
      181 qptlqkrafa nekmnfiwna etesidgdgn rvtsvtykdk ekgitkkltt rgvfiyvgvi
      241 pqtaplkdig ivneqgwipt dehmktkvag ifavgdvrak dlrqianavg dgsiagqeay
      301 nylqalnd
//
LOCUS       WP_122022797             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lactobacillus sp. ESL0228].
ACCESSION   WP_122022797
VERSION     WP_122022797.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus sp. ESL0228
  ORGANISM  Lactobacillus sp. ESL0228
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Lactobacillus sp. ESL0228"
                     /db_xref="taxon:2069352"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33472
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqkydviii gagpggltaa lyasranlsv lildrgpygg qmnntdaidn ypgfseikgp
       61 elgekmynsv mkfgakfeyg dvqtvtvern tklvktdtge ysapvliiat gadhrhldvp
      121 gedeysgkgv sycavcdaaf fkdedlavig ggdsaieegi yltqnaksvt vvhrrdqlra
      181 qptlqkrafa nekmhfiwda etesiegdgn rvtgitykdk ktaelkhlsv hgvfiyvgvi
      241 pqttafknld ildqngwipt dehmktkhdg vfaigdvrak dlrqianavg dgsiagqeay
      301 nylqalnd
//
LOCUS       WP_122024535             308 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Lactobacillus].
ACCESSION   WP_122024535
VERSION     WP_122024535.1
KEYWORDS    RefSeq.
SOURCE      unclassified Lactobacillus
  ORGANISM  unclassified Lactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="unclassified Lactobacillus"
                     /db_xref="taxon:2620435"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33233
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqnydviii gagpggltaa lyasranlsv llldrglygg qmnntdaidn ypgfseikgs
       61 elgekmynsi mkfgakfeyg dvqqvslegn ykvvttdtge yrapaliiat gadhrhlnip
      121 gedeyagkgv sycavcdaaf fknediavig ggdsaieegi ylaqnaksvt vihrrdqlra
      181 qptlqkrafa nekmnfiwna etesidgdgn rvtsvtykdk etgitkkltt rgvfiyvgvi
      241 pqtaplkdig ivneqgwipt dehmktkvag ifavgdvrak dlrqianavg dgsiagqeay
      301 nylqalnd
//
LOCUS       WP_122025853             311 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Lactobacillus].
ACCESSION   WP_122025853
VERSION     WP_122025853.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus
  ORGANISM  Lactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Lactobacillus"
                     /db_xref="taxon:1578"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33569
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtekydviii gagpggltaa lyasranlsv lmldrglygg qmnntdaidn ypgfseikgp
       61 elgekmynsv mkfgakfeyg dvqsvttdgd lkivktdtge ysapaliiat gadhrhlgvp
      121 gedeysgkgv sycavcdaaf fkdediavig ggdsaieegi ylaqsaksvt vihrrdqlra
      181 qptlqkrafa npkmhfiwng ltqsidgdgn kvtgvtykdk etgeekhlkt rgvfiyvgvi
      241 pqtapfkdlg vtdengwipt dehmrtkvdg ifalgdvrak dlrqianavg dgsiagqqay
      301 nylqdlndrk i
//
LOCUS       WP_122027734             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium sp. 6424].
ACCESSION   WP_122027734
VERSION     WP_122027734.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. 6424
  ORGANISM  Chryseobacterium sp. 6424
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium sp. 6424"
                     /db_xref="taxon:2039166"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33443
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypegvt
       61 gpqmmidlqk qaerfdtkvh yemitkvafa qeeggihrlw agnkeilakt viistgatak
      121 ylgledekky agggvsacat cdgffykgkd vivvgagdta aeeatylakl tnkvtmlvrk
      181 dtfraskamv hrvnntpnie vrfnheligi egenglvera vvinnqtqet akitvegifi
      241 aighkpntdv fagqvdlden gyiktipgta ktnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 aamdaekyla ela
//
LOCUS       WP_122033051             479 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aliivibrio sp. EL58].
ACCESSION   WP_122033051
VERSION     WP_122033051.1
KEYWORDS    RefSeq.
SOURCE      Aliivibrio sp. EL58
  ORGANISM  Aliivibrio sp. EL58
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Aliivibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Aliivibrio sp. EL58"
                     /db_xref="taxon:2107582"
     gene            1..479
                     /gene="nrfA"
     Protein         1..479
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53387
     Region          1..476
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkkqwtrrsa aaiamvttll lsshsfaase nservdprne ayakehadqy eswrstsdsv
       61 qiedalaedp nmvimwagyg fakdynkarg hfyaiddvrq tlrtagptde nsgpmpmacw
      121 sckspdvgrv ieekgedgyf sgkwarlgse iqnpigcadc hdtrsegfkn gepalaitkp
      181 hveramdaig kpfgdqsrld qqaavcgqch veyyftgktk avkfpwdkgt tvdemeeyyd
      241 eigfkdwthk vskapmlkaq hpgyetwrdg ihgknnvtcv dchmpkvkke dgtvytdhkv
      301 gnpfdrfedt canchtqske mlqgvvasrk aqvlkmklta erqivaahfe agaawdagat
      361 ekemepilqd irhaqwrwdy aiashgvhmh apevalevlg tavdkaadar tklirllakk
      421 gitdpiaipd istkaaaqka lgmdmkgmea ekkhfletvv pqwenqaker estdyapik
//
LOCUS       WP_122034719             309 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Lactobacillus].
ACCESSION   WP_122034719
VERSION     WP_122034719.1
KEYWORDS    RefSeq.
SOURCE      unclassified Lactobacillus
  ORGANISM  unclassified Lactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="unclassified Lactobacillus"
                     /db_xref="taxon:2620435"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33278
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtkkydvivi gagpggltaa lyasranlsv lildrglygg qmnntdaidn ypgfteikgp
       61 elgekmynsv mkfgsefeyg dvqsvtidge nkvvktdtge ysapaliiat gadhrhlnvp
      121 geeeysgkgv sycavcdaaf fkdediavig ggdsaieegi ylaqsaksvt vihrrdqlra
      181 qptlqkrafa ndkinfiwng itesidgdgq rvtgvtykdk etgeekqlat rgvfiyvgvi
      241 pqtapfkelg itdeqgwipt ddhmrtkadg ifalgdvrak dlrqianavg dgsiagqaay
      301 nylqdlndk
//
LOCUS       WP_122039227             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Asaia bogorensis].
ACCESSION   WP_122039227
VERSION     WP_122039227.1
KEYWORDS    RefSeq.
SOURCE      Asaia bogorensis
  ORGANISM  Asaia bogorensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Asaia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Asaia bogorensis"
                     /db_xref="taxon:91915"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33853
     Region          7..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqsfrtdll vigagpagyt aaiyaaranl kpilvaglqp ggqltittdv enypgfaepv
       61 qgpwlveqmr lqaehvgtem hydlitecaf nektddgyfr lkadsgadyl artvviatga
      121 qakwlglpse arlqsggvsa catcdgffyr gkkvaviggg ntaveealyl thhadhvtlv
      181 hrrdslraer ilqdrlfanp kitvlwnnav eeilgagkpe tvcgvrlrnt qdgseqtldv
      241 dgvfvaighs pntgpfretl ecdtegyivt vpgstktsve gvfaagdvqd kkfrqaitaa
      301 gtgcmaalea ehllagls
//
LOCUS       WP_122041766             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas sp. LTJR-52].
ACCESSION   WP_122041766
VERSION     WP_122041766.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. LTJR-52
  ORGANISM  Pseudomonas sp. LTJR-52
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas sp. LTJR-52"
                     /db_xref="taxon:2479392"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34049
     Region          1..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrharvi ilgsgpagyt aavyaaranl kpllitgmqm ggqlttttev dnwpgdphdl
       61 tgpalmermr ehaqrfetei vfdhingvdl ankpftlkgd sgtytcdali iatgasaryl
      121 gltseesfmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlihrrdt
      181 fraekilqdk lksrvaegki elklnaavde vlgdnmgvtg vrlknndgsm deiqvaglfv
      241 aightpnssl fegqlelkdg yvvvkggres natatsiegv faagdiadht yrqaitsaga
      301 gcmaaldver yldglgdnlw
//
LOCUS       WP_122042853             242 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Klebsiella pneumoniae].
ACCESSION   WP_122042853
VERSION     WP_122042853.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..>242
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..>226
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpqerl aqetraaatp ktveqllklg fsvavesgag klasfddeaf aeagaeivtg
       61 devwqsdvil kvnapnddei allnpgttli sfiwpaqnpq lmeklaarni nvmamdsvpr
      121 israqsldal ssmaniagyr aiveaahefg rfftgqitaa gkvppakvmv igagvaglaa
      181 igaanslgai vrafdtrpev keqvqsmgae fleldfkeea gsgdgfraay fprpvagcaq
      241 ln
//
LOCUS       WP_122049417             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Asaia bogorensis].
ACCESSION   WP_122049417
VERSION     WP_122049417.1
KEYWORDS    RefSeq.
SOURCE      Asaia bogorensis
  ORGANISM  Asaia bogorensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Asaia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Asaia bogorensis"
                     /db_xref="taxon:91915"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33794
     Region          7..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqsfrtdll vigagpagyt aaiyaaranl kpilvaglqp ggqltittdv enypgfaepv
       61 qgpwlveqmr lqaehvgtem hydlitecaf nektddgyfr lkadsgaeyl artvviatga
      121 qakwlglpse arlqsggvsa catcdgffyr gkkvaviggg ntaveealyl thhadhvtlv
      181 hrrdslraer ilqdrlfanp kitvlwnnav eeilgagkpe tvcgvrlrnt vdgseqtlgv
      241 dgvfvaighs pntapfretl ecdsegyiit vpgstktsve gvfaagdvqd kkfrqaitaa
      301 gtgcmaalea ehllagls
//
LOCUS       WP_122059905             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium autoethanogenum].
ACCESSION   WP_122059905
VERSION     WP_122059905.1
KEYWORDS    RefSeq.
SOURCE      Clostridium autoethanogenum
  ORGANISM  Clostridium autoethanogenum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Clostridium autoethanogenum"
                     /db_xref="taxon:84023"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34340
     Region          5..293
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnniydviii gsgpaglsaa iysararlkt lilerskvgg qivitdevan ypgsikdatg
       61 psligrmeeq vesfgaerkk dnikqvdftg kikklkgeke eyyaksiiia tganprkigc
      121 pgeneligkg vsycatcdae ffedlevfvv gggdsaieea iyltkfakkv tivhrrdelr
      181 aaksiqekaf knpkieikwn svitqikgdg ivqsavfkdt ktgelseyfa deedgtfgif
      241 vfvgylptnq lvkelvdide agyiitndkm etniegvfaa gdirekplrq vvtaaadgai
      301 aavqaekyie nnfee
//
LOCUS       WP_122067320             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            owensii].
ACCESSION   WP_122067320
VERSION     WP_122067320.1
KEYWORDS    RefSeq.
SOURCE      Vibrio owensii
  ORGANISM  Vibrio owensii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio owensii"
                     /db_xref="taxon:696485"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53051
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 msikhwmsap iavatlfasq lflvgtplaa eekglidprn dafeqnhpdq yhswkatses
       61 ehiedalsed pnmvilwagy gfakdynkar ghfyalddvr qtlrtgaptd eksgpmpmac
      121 wsckspdvar vidergedgy fegkwarlgs eivnpigcsd chetrseefk kgepalaitr
      181 pyvdrafdai gknfdeqsrl dkqasvcaqc hveyyftgpt kavkfpwdmg ttvndmekyy
      241 dalnfkdwth avskapmlka qhpgyetwrd gihgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfed tcaqchtqtk eqlqgivstr kaqvlnmklt aekqivaahf eagaawkaga
      361 teaemepilq dirhaqwrwd yaiashgvhm hapevalevl gtavdraada rtklvrllat
      421 kgitdpvqip distkakaqq algmdmdkmn adkkhfletv apewdkaaae reaty
//
LOCUS       WP_122070404             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            owensii].
ACCESSION   WP_122070404
VERSION     WP_122070404.1
KEYWORDS    RefSeq.
SOURCE      Vibrio owensii
  ORGANISM  Vibrio owensii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio owensii"
                     /db_xref="taxon:696485"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54575
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreil agesrvaasp ksveqliklg fdvaiesqag vlasfddaay eaagakivss
       61 eevwtsglil kvnaplvdee kgideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivrsf dvrpevkeqv esmgaefltv dfkedsgsgd gyakemsdef
      241 nkkaaelyae qakdvdiiit talipgrpap tlitkemvds mkagsvivdl aaanggncey
      301 tvkdqvitta ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 lrgvtvvkeg evtwpappiq vsaqpqakpq epvkpqpkve eptspvkkfg alavglgafa
      421 wvasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_122074033             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudophaeobacter sp. EL27].
ACCESSION   WP_122074033
VERSION     WP_122074033.1
KEYWORDS    RefSeq.
SOURCE      Pseudophaeobacter sp. EL27
  ORGANISM  Pseudophaeobacter sp. EL27
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudophaeobacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Pseudophaeobacter sp. EL27"
                     /db_xref="taxon:2107580"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33502
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtrhtkvl iigsgpagyt agvyaaraml epvlvqgiep ggqlttttev enypgftevq
       61 gpdlmikmqe hasamgcdiv gdiitsldts krpfvakgds gttytadavi latgarakwl
      121 gleseekfkg fgvsacatcd gffyrgqeiv vigggntave ealfltnfas kvtlvhrrde
      181 lrsekilqdr lfknpkietl wfheleevyg tdsplgvegi kvkhvktgei tdipakgvfv
      241 aighapanel vkdtlelhng gyvsvkpgtt etsipgvfaa gdltdhkyrq avtsagmgcm
      301 aaldaerfla eqdd
//
LOCUS       WP_122075500             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudophaeobacter].
ACCESSION   WP_122075500
VERSION     WP_122075500.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudophaeobacter
  ORGANISM  unclassified Pseudophaeobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudophaeobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="unclassified Pseudophaeobacter"
                     /db_xref="taxon:2637024"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55159
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevi ngearvamtp dsarqlqklg yecaiesgag laagfsdaty eeagveiikt
       61 aaalwkasdi iakvrqpnea elkrlnskkt lisffnpggn eeglelaksk gasvvamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtsaslg aitlafdvrp evaeqvesmg aefvyldfee eqadgaasgg yasvsspefr
      241 daqlakflel apevdivitt alipnreape lwteemvaam kpgsvivdla aekggncklt
      301 vmdekivten gvtiigytdf psrmaaqssm lyatnirhmm adltpekdgq vnhdmeddvi
      361 rgatvthgge itfpppppkv aaiaakpkev vpeltpeekr aeevaafkaq tknqvtllav
      421 ggalllavgl vapasfmqhf ivfvlsvfig fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_122099010             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas songnenensis].
ACCESSION   WP_122099010
VERSION     WP_122099010.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas songnenensis
  ORGANISM  Pseudomonas songnenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas songnenensis"
                     /db_xref="taxon:1176259"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38803
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkligqg hrvtlqsgag llssvpdsay eavgatigda
       61 aaafaaelvl kvnapdeael aqmqsgsvll gmlnpfdndc iarmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vlvgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhera lqsdivitta lipgrkaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvaadasaly arnlldflkl aidkdgqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_122099863             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas songnenensis].
ACCESSION   WP_122099863
VERSION     WP_122099863.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas songnenensis
  ORGANISM  Pseudomonas songnenensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas songnenensis"
                     /db_xref="taxon:1176259"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33631
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kplmitgiqp ggqlttttev dnwpgdvegl
       61 tgpdlmvrmq khaerfdtei vfdhihtael qqrpftlrgd sgvytcdali iatgasaqyl
      121 glpseeafag rgvsacatcd gffyrnqvva vigggntave ealylsniak evhlihrrdk
      181 lrsekilqdk imdkatngni rlhwnhtlee vlgdasgvtg vrlkstltge enqldlagvf
      241 iaighkpntd lfqgqlemkd gylkirggge gdatctsipg vfaagdvadh vyrqaitsag
      301 agcmaaldae kyldn
//
LOCUS       WP_122113380             330 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paracoccus alkanivorans].
ACCESSION   WP_122113380
VERSION     WP_122113380.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus alkanivorans
  ORGANISM  Paracoccus alkanivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Paracoccus alkanivorans"
                     /db_xref="taxon:2116655"
     gene            1..330
                     /gene="trxB"
     Protein         1..330
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35248
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtdsthtkll ivgsgpagyt aavygaraml epmliqglqp ggqltittev enwpgeteiq
       61 gpelmvkmee haramgadiv tdmvtrldlg qrpfvaecds grrvtadavi latgaqarwl
      121 glpseekfkg fgisacatcd gffyrnrevl vigggntave ealfltrfas kvtlvhrrds
      181 lraekilqnr lfknpkveii wdhelievkg addplgvtga vlrstkdggt relpadgifv
      241 aighapasel vkdqlelhhg gyvkvepgst rtsvpgvfaa gdltdhfyrq avtsagmgcm
      301 aaldaehwla aqeeagaspv kaepektpae
//
LOCUS       WP_122113794             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            alkanivorans].
ACCESSION   WP_122113794
VERSION     WP_122113794.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus alkanivorans
  ORGANISM  Paracoccus alkanivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus alkanivorans"
                     /db_xref="taxon:2116655"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55571
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkesy egearvaitp ssaahlqklg hevfvesgag aragfmdsdy ekagvtvekt
       61 aadliravdv vakvrqpsda eigqmregqt lisffypaqn aellekakeq gitaiamdmv
      121 prisraqkmd alssmaniag yrsvieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aqvfafdvrp evaeqiesmg aefvfldfee qaqdgaatgg yaapsspefr
      241 ekqlekfrel apdmdvvitt alipgrdapv lwtrdmveam kqgsvivdla aekggncelt
      301 vaderivten gvtiigytdf asrmgaqase lygnnirhfm gdltpkkdgv ivhdmeddvi
      361 rgatvahdhd vtfpppppkv aaiaaqkpke kpkeltpeek raqevaafka etrsqvalla
      421 gggillllvg lvapasfmsh fivfvlacfv gfkviwnvah slhtplmavt naissiiilg
      481 almqigsgsa wvlilaalav lmagvnivgg flvtrrmlam fqks
//
LOCUS       WP_122123328             265 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Commensalibacter melissae].
ACCESSION   WP_122123328
VERSION     WP_122123328.1
KEYWORDS    RefSeq.
SOURCE      Commensalibacter melissae
  ORGANISM  Commensalibacter melissae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Commensalibacter melissae"
                     /db_xref="taxon:2070537"
     Protein         1..265
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=30728
     Region          <7..117
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mdskqlwvlt yeavsrewgn kfldsnslnf idrfesyivs ndnyehvldl iecvigiris
       61 ilskvdpnyk fnndeiligl ieelnkrfly agvgyqyeng eiiridhqyv hkeivkpale
      121 iihnkafekv neeysnahkh yrnqyikdci vgcnrafesl lksicnecew eydpnnrasd
      181 likiihkngl fpvgmektid syimtlktgv pelrnhfggh gsssqspsps iymaeyvlhl
      241 tatnivflyn afrdyqskqn qglff
//
LOCUS       WP_122123938             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Commensalibacter melissae].
ACCESSION   WP_122123938
VERSION     WP_122123938.1
KEYWORDS    RefSeq.
SOURCE      Commensalibacter melissae
  ORGANISM  Commensalibacter melissae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Commensalibacter melissae"
                     /db_xref="taxon:2070537"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34346
     Region          7..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mgetfltdll iigagpagyt aaiygaranl sptlltglqp ggqltitnei enfpgfadpi
       61 qgpwlmeqma qqainvgaki indsvtrcsl qqkqkennyf ilqtdmgnty kaktviiatg
      121 aqarwlglea eeklqgfgvs acatcdgffy rgkqvavigg gntaveealy lthhaahvfl
      181 ihrrnslrae kiqqtrlmkn pkvtiiwnsv vedilaesnp psvtgltlkn tltkeisqlp
      241 idgvfiaigh tpntelfknq idldeegyiq ttpgttktsv pgifaagdvq dkiyrqaita
      301 agsgcmaale aerflsaseg
//
LOCUS       WP_122125046             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Bacteroides].
ACCESSION   WP_122125046
VERSION     WP_122125046.1
KEYWORDS    RefSeq.
SOURCE      unclassified Bacteroides
  ORGANISM  unclassified Bacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="unclassified Bacteroides"
                     /db_xref="taxon:2646097"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33931
     Region          6..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mekettkcli igsgpagyta aiyagranlc pvlyeglqpg gqlttttdve nfpgypegis
       61 gtalmedlra qatrfgtdir ygiataadls krpyqitidd ekvietetli iatgatakyl
      121 glpdeqkyag mgvsacatcd gffyrkkvva vvgggdtace ealylaglas kvylivrksy
      181 lraskimqqr vmenenivil fnhnavglyg engvegvhll envagvekry dlpidgffla
      241 ighkpnsdif kpyietdevg yiitepdspr tcvpgvfaag dvadphyrqa itaagsgcka
      301 aieaerylse lgllksv
//
LOCUS       WP_122139379             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bacteroides caccae].
ACCESSION   WP_122139379
VERSION     WP_122139379.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides caccae
  ORGANISM  Bacteroides caccae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Bacteroides caccae"
                     /db_xref="taxon:47678"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33771
     Region          8..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeiekvkcl iigsgpagyt aaiyagranl cpvlyeglqp ggqlttttdv enfpgypegi
       61 sgpqlmedlr aqasrfgtdv rfgiataadl skapykitid gekeieaetl iistgataky
      121 lgledekkya gmgvsacatc dgffyrkkvv avvgggdtac eeavylsgla skvylivrkp
      181 flraskimqe rvmnhekiev lfehnavgly gdngvegvnl vkrwgepdee ryslpidgff
      241 laighqpnsd ifkdyldtde vgyiitdgas prtkvpgvfa agdvadphyr qaitaagsgc
      301 kaaieaeryl sakgli
//
LOCUS       WP_122147491             353 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Cellulomonas triticagri].
ACCESSION   WP_122147491
VERSION     WP_122147491.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas triticagri
  ORGANISM  Cellulomonas triticagri
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Cellulomonas triticagri"
                     /db_xref="taxon:2483352"
     gene            1..353
                     /gene="trxB"
     Protein         1..353
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36465
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtetpvrdiv ivgsgpagyt aaiyaaragl apyvvagsvt aggalmnttd venfpgfpdg
       61 ilgpdlmdnl qkqaerfgae vvwddateld ltgpvktvvt aggetvrara vilatgsayr
      121 elglddekrl sgrgvswcat cdgfffkdqd ilvvgggdsa veeatfltrf gksvtivhrr
      181 delraskima draladpkiq fawnsevvgi qgqdkvtgvt lrdtvtgetr ehgatglfva
      241 ighiprtdll hgqvdldeng yivvegrstr tnlpgvfaag davdhtyrqa itaagsgcsa
      301 aldaqhylaa lgdvdpasps dippalddad vdaadavaar gadtaaaaaa agh
//
LOCUS       WP_122150930             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cellulomonas triticagri].
ACCESSION   WP_122150930
VERSION     WP_122150930.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas triticagri
  ORGANISM  Cellulomonas triticagri
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Cellulomonas triticagri"
                     /db_xref="taxon:2483352"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52842
     Region          1..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkegr pgerlvaatp atvarlaklg yevvvehgag aaasfpdeay adagaalada
       61 aevwasdvvt avnapadaqv aamtpgatlv amlapaqhpe rvaalhargv talaldavpr
      121 israqaldvl stmsnvagyr avieaaeefg gmftgqvtaa gktppatvfv igagvaglaa
      181 igaagslgaq vrafdvrpev geqiesmgat fvqaevaqqe vsadgyasal taeqerltaq
      241 myaaesaqad ivittalvrg taprtitaem vaamrpgsvv vdlaasgggn celtvpgekv
      301 vspngvtvlg ytdltsrmar htsqlfgtnv vnllalltpg kdgaltldlg dpvqrgmavt
      361 rdgevlwppp pvqvsaapap eatpavapvd paekaraare aahrkgqrqm vglalgavll
      421 alaitfspaa flghitvfvl avfvgyyvis nvshslhtpl maqtnaisgi ilvgallqig
      481 sdswlvstla vvaaavasin ifggflvafr migmfrkeea
//
LOCUS       WP_122152506             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia sp.].
ACCESSION   WP_122152506
VERSION     WP_122152506.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp.
  ORGANISM  Paraburkholderia sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia sp."
                     /db_xref="taxon:1926495"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39416
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvsqg hrvtiqsgag tgasfpdeaf savgaeivda
       61 atafgadlvl kvqspteael phlkrgavlv gmldpfnadn aaklasagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaadlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaakgvggy arpmppswla
      241 rqgalvhera kqadivitta lipgrpaptl isvetvqamk pgsvlidlaa grgpeyegqr
      301 ggncpltvad kivtkngvqi vgftnlasmv aadasslyar nlldflklii nkegalnidl
      361 addivaatll ardgevtrka
//
LOCUS       WP_122160951             409 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium brachiatum].
ACCESSION   WP_122160951
VERSION     WP_122160951.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium brachiatum
  ORGANISM  Methylobacterium brachiatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Methylobacterium brachiatum"
                     /db_xref="taxon:269660"
     Protein         1..409
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42009
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd saesrvaavp etvkkfkalg aditvqagag lkagildsey eaagaeivgn
       61 aadaardadl vlkvrrpage elsllkrgat viaimdpygn eaalkamaea gvsgfamelm
      121 pritraqvmd vlssqanlag yravvdgaae ygrampmmmt aagtvpaarv fimgvgvagl
      181 qaiatarrlg avvtatdvrp atkeqveslg akfvavedde fkqaetaggy akemsagyqa
      241 kqaelvkghi akqdivitta lipgrpapkl vseemvasmk pgsvlvdlav erggnvagak
      301 pgevvvtdrg vkivghtnvp grlaatassl yarnlyafve tlidketkal ainwddelvk
      361 atnltrdgsv vhasfqsktd gpaseaaavg laksetgkae aapapsgah
//
LOCUS       WP_122163982             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Stutzerimonas zhaodongensis].
ACCESSION   WP_122163982
VERSION     WP_122163982.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas zhaodongensis
  ORGANISM  Stutzerimonas zhaodongensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Stutzerimonas zhaodongensis"
                     /db_xref="taxon:1176257"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33687
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mnevkrsrli ilgsgpagyt aavyaaranl kplmitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmermq khaerfdtev vfdhihtael qqrpfilkgd satyscdali iatgasaqyl
      121 glpseeafag rgvsacatcd gffyrnqvva vigggntave ealylsniak evhlihrrdk
      181 lrsekilqdk imekaangni rlhwnhtlee vlgdasgvtg vrlkstlsge eqklelsgvf
      241 iaighkpntd lfhgqlemrd gylmikggse gdatsttipg vfaagdvadh vyrqaitsag
      301 agcmaaldae kfldq
//
LOCUS       WP_122168031             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas zhaodongensis].
ACCESSION   WP_122168031
VERSION     WP_122168031.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas zhaodongensis
  ORGANISM  Stutzerimonas zhaodongensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas zhaodongensis"
                     /db_xref="taxon:1176257"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39136
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletr pgetrvaatp etikkligqg hrvtvqsgag lqasvpdsay eaagatiada
       61 aaafaaeill kvnapsetel aqmqpgtvlv gmlnpfdnen isrmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmvaanqypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaegvggy arpmpaswmt
      241 rqaqavhera kqadiiitta lipgrkaptl lqeetvqqmk pgsvvidlaa sqggncplte
      301 adqvvvkhgv tlvgytnlat lvpadasaly arnlldflkl vidgearfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_122183419             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces triticirhizae].
ACCESSION   WP_122183419
VERSION     WP_122183419.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces triticirhizae
  ORGANISM  Streptomyces triticirhizae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces triticirhizae"
                     /db_xref="taxon:2483353"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33977
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslnp lvfegavtag galmntteve nfpgfqegim
       61 gpdlmdnmra qaerfgaelv pddivsvdls gevktvtdts gavhraraii vatgsqhrkl
      121 glpnedqlsg rgvsycatcd gfffreqdia vvgggdtame eatflsrfar kvtvihrrdt
      181 lraskamqer afadpkiefl wdsevaeiqg aegkvsglvv rntstdekse lpvtglfvai
      241 ghdprvelfk gvlelddegy iavdapstrt nvpgvfaagd vvdhtyrqai taagtgcsaa
      301 ldaerylaal adaasvtsea qv
//
LOCUS       WP_122187013             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nocardia stercoris].
ACCESSION   WP_122187013
VERSION     WP_122187013.1
KEYWORDS    RefSeq.
SOURCE      Nocardia stercoris
  ORGANISM  Nocardia stercoris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Nocardia.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Nocardia stercoris"
                     /db_xref="taxon:2483361"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34578
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpvrdlii vgsgpagyta aiyaaraele pllfegtqfg galmttteve nfpgfrsgim
       61 gpdlmdemre qakrfgadir tedvdaidls gevksvtvgg evyraksiil amgsaaryln
      121 vpgeqellgr gvsacatcdg fffkgqdivv vgggdsamee atfltkfass vtvvhrreef
      181 rasrimlera kandkirfrl dsevvavhge nsvtsltlrn trtgetsela atglfvaigh
      241 dprselvrgq valdgegyvl vdgsstatdv pgvfaagdlv dhtyrqaita agtgcraaid
      301 aerwlaeqgd itantvgnag spvdvtvn
//
LOCUS       WP_122203597             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Parabacteroides merdae].
ACCESSION   WP_122203597
VERSION     WP_122203597.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides merdae
  ORGANISM  Parabacteroides merdae
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Parabacteroides merdae"
                     /db_xref="taxon:46503"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33783
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnttqnekvr cliigsgpag ytaaiyasra nlspvlyegi qpggqltttt evenfpgype
       61 gvtgtelmed lrkqaarfga dirvgiatet dlsaapykvt idgekviete tliistgata
      121 kylglpdeqk yagmgvsaca tcdgffyrkk vvavvgggdt aceealylss lakqvylivr
      181 kpylraskvm qervlntlni tvlfehntig lfgeggvega hlvkrmgeld eekvdiaidg
      241 fflaightpn skifkpwvet devgyiktvp gtpktrvpgv faagdvadph yrqaitaags
      301 gcaaaieaer ylseigk
//
LOCUS       WP_122210376             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122210376
VERSION     WP_122210376.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39013
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay eaagatvrga
       61 ddtfaselil kvvapnenel aliksgtvvi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpvswmq
      241 rqavavhera klsdivitta lipgrkapvl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adhvtlehgv tlvghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqiir kng
//
LOCUS       WP_122215175             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. ZS0098].
ACCESSION   WP_122215175
VERSION     WP_122215175.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. ZS0098
  ORGANISM  Streptomyces sp. ZS0098
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces sp. ZS0098"
                     /db_xref="taxon:1904044"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34271
     Region          8..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msgtvirdvi vigsgpagyt atlytgrael kplvfggaif vggaltttte venfpgfpeg
       61 idgpdlmtnm raqaekfgae mvdddivavd ltgdiktvtd tagtvhrakt vivatgsgyr
      121 klglpkedel sgrgvswcat cdgfffrnrd ivvvgggdta meeatfltrf arsvtvvhrr
      181 stlrasqvmq nrafaddkis fafdteiaei kesngmlagl vlrdvfsnat rdldatglfi
      241 aighdprtel fkgqldldgn gyiqvaspst rtnipgvfaa gdvvdhtyrq aitaaasgca
      301 aaldaeryla aladdsaarl taavpa
//
LOCUS       WP_122222475             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae group genomosp. 3].
ACCESSION   WP_122222475
VERSION     WP_122222475.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 3
  ORGANISM  Pseudomonas syringae group genomosp. 3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae group genomosp. 3"
                     /db_xref="taxon:251701"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38945
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tretrvaatp etikklisqg hrvtvqsgag vhasvpdsay eaagatigca
       61 deafagelil kvvapnddel aliksgsvii gmlnpfnsel igkmaehgvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera rlsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tlcgptnlpa qvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdghvvr kng
//
LOCUS       WP_122217740             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lactiplantibacillus pentosus].
ACCESSION   WP_122217740
VERSION     WP_122217740.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus pentosus
  ORGANISM  Lactiplantibacillus pentosus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Lactiplantibacillus pentosus"
                     /db_xref="taxon:1589"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33330
     Region          5..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maksydviii gagpagmtaa lyasranlsv llldrgiygg qmnntaaien ypgfksilgp
       61 dlakdmyesa tqfgaeyayg svesvedrgd vkivttdsdt fetkalvigt gseyrklgvp
      121 gedtyggrgv sycavcdgaf frnkhvvvvg ggdsaieegt yltqladkvt vihrrdqlra
      181 qqilqdrafa npkiefvwns nvteivgddk kvtavtvnnn ktgedseiav dgvfiyvgin
      241 pitkpfsnlg itdengwiet ndhmetkvpg ifaigdvrkk dlrqvatavg eggtagqgvy
      301 nyitalgdkv kn
//
LOCUS       WP_122222702             145 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas syringae group
            genomosp. 3].
ACCESSION   WP_122222702
VERSION     WP_122222702.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 3
  ORGANISM  Pseudomonas syringae group genomosp. 3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Pseudomonas syringae group genomosp. 3"
                     /db_xref="taxon:251701"
     Protein         1..145
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=16332
     Region          <6..42
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mdecieelna rfkehgvgya fvsdelirvd sqvmhsevvk pvihylsapg fegpqeefff
       61 ahghyrhgvd keaiteanka fvstmkvicd qkgweykkrd takkliivci englfpsyyq
      121 sqlaslsnll esgvpnirnn eggrh
//
LOCUS       WP_122223078             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_122223078
VERSION     WP_122223078.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38803
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqrgag iqasvpdsaf eaagavigea
       61 seafagelil kvvapndnel alinsgsvvi gmlnpfnnel igkmadrgvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv egsdvrpavk eqieslgakf idvpyetdee hecaegvggy arpmpaswmq
      241 rqaaavhera rladiiitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adevvvahgv tlightnlpa lvaadasaly arnlldfikl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122226208             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Corticibacter populi].
ACCESSION   WP_122226208
VERSION     WP_122226208.1
KEYWORDS    RefSeq.
SOURCE      Corticibacter populi
  ORGANISM  Corticibacter populi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Corticibacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Corticibacter populi"
                     /db_xref="taxon:1550736"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38424
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvaaeta agerrvaatp etvkklvaqg havlvqagag egasvtdaay qaagaeitds
       61 agalgaelvl tvrspdaqal almkpgsvlv gmldpfdrdg larlaaaglt afaleaaprt
      121 traqsldvls sqaniagyka viiaaniyqr ffpmlmtaag tvkaarvvvl gvgvaglqai
      181 atakrlgati easdvrpsvk eqvaslgakf idvpyetqee kdaaegvggy arpmpaswlq
      241 rqqaevakrv aqadvviata lipgraaptl iteemvrsmk pgsvivdiaa gkgeggvggn
      301 cplteagatv vkhgvhivge tnlpalvaad asalyarnvl dflklilpkd eglkidlqdd
      361 ivaaclvard rqvtra
//
LOCUS       WP_122226537             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corticibacter populi].
ACCESSION   WP_122226537
VERSION     WP_122226537.1
KEYWORDS    RefSeq.
SOURCE      Corticibacter populi
  ORGANISM  Corticibacter populi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Corticibacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Corticibacter populi"
                     /db_xref="taxon:1550736"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34178
     Region          10..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstsntlhak vlilgsgpag ytaaiyaara nlepvlitgm aqggqltttt evdnwpadpl
       61 gvqgpelmer flkhaerfqt riifdhvnqv dlskrpftlt gdsgtytads lilatgasar
      121 ylglaseesf mgrgvsacat cdgffyrgqe vavvgggnta veealylsni askvtlihrr
      181 dkfraepimi dklmekvqag kivlklhsvl devlgddsgv tgvrirhvqd gstediplqg
      241 tfiaightpn teifqgqldm kdgyiltrgg hhgfatqtsv pgvfaagdvq dnvyrqaits
      301 agtgcmaald aqrfleqned
//
LOCUS       WP_122227244             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudoxanthomonas spadix].
ACCESSION   WP_122227244
VERSION     WP_122227244.1
KEYWORDS    RefSeq.
SOURCE      Pseudoxanthomonas spadix
  ORGANISM  Pseudoxanthomonas spadix
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Pseudoxanthomonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudoxanthomonas spadix"
                     /db_xref="taxon:415229"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33950
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mstskhsrll ilgsgpagwt aavyaaranl kpvvitglqq ggqlmtttev dnwpgdahgl
       61 mgpdlmarmq ahaerfetev ifdhihtadl sqrpfrligd saeytcdali iatgataryl
      121 gleseeafkg rgvsacatcd gffyrdqdva vvgggntave ealylsnian rvylihrrdt
      181 lraekimqdk lqakidtgki vpvwhhtvee vlgdeagvig lrvrsvldgs trdlvvhgff
      241 vaightpnts lfdgqlamnn gyliiksgld gnatqttvpg vfaagdvadq hyrqaitsag
      301 fgcmaaldae rfldkgt
//
LOCUS       WP_122232243             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas syringae].
ACCESSION   WP_122232243
VERSION     WP_122232243.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33652
     Region          1..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgpalmermr ehaerfetei vfdhinsvdl agkplslqgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlvhrret
      181 fraekilidk lharvaegki elklnatlde vlgdnmgvtg arlknndgss selkvdgvfi
      241 aightpntsl fdgqlalkdg ymvvqggreg natatsvegv faagdvadhv yrqaitsaga
      301 gcmaaldver yldgladvsf
//
LOCUS       WP_122232426             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae].
ACCESSION   WP_122232426
VERSION     WP_122232426.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38841
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag ihasvpdsty eaagavigdt
       61 netyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaahgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122237413             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Allofranklinella
            schreckenbergeri].
ACCESSION   WP_122237413
VERSION     WP_122237413.1
KEYWORDS    RefSeq.
SOURCE      Allofranklinella schreckenbergeri
  ORGANISM  Allofranklinella schreckenbergeri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Allofranklinella.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Allofranklinella schreckenbergeri"
                     /db_xref="taxon:1076744"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34071
     Region          10..315
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mstsntlhak vlilgsgpag ytaavyaara nlqpvlitgm aqggqltttt evdnwpadfa
       61 gvqgpelmer flkhaqrfnt hivfdhiqqv dlsqrpftlk gdsgtytadt liiatgasak
      121 ylglpseaaf mgrgisacat cdgffyrdqd vavvgggnta veealylsgi arkvtlihrr
      181 dkfraepimi dklmekvqqg kielkllhvl devlgndsgv tgvrikhves gatedvavhg
      241 afiaighspn teifqgqlam engyivtqgg hagfatqtsv pgvfaagdvq dhvyrqaits
      301 agtgcmaald aqrfleqsce t
//
LOCUS       WP_122238246             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Allofranklinella schreckenbergeri].
ACCESSION   WP_122238246
VERSION     WP_122238246.1
KEYWORDS    RefSeq.
SOURCE      Allofranklinella schreckenbergeri
  ORGANISM  Allofranklinella schreckenbergeri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Allofranklinella.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Allofranklinella schreckenbergeri"
                     /db_xref="taxon:1076744"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38828
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletf agetrvaltp etakklvaqg htigvqsgag vaasvtnday vaagaqivda
       61 aaalgadlvl kvrapspeel ahckrgatlv gmldpfdaeg lqrladaglt afaleaaprt
      121 traqsmdvls sqaniagyka vvlaasvyqr ffpmlmtaag tikaarvvvl gvgvaglqai
      181 atakrlgati easdvrpsvk eqveslgakf idvpyetdee reaaegvggy arpmpaswle
      241 rqkqevakrv aaadvvista lipgrpaptl iteemvramr pgsvivdlaa grgangggnc
      301 pltvadqtvq hdgvtllgpt nlpaqmaada salyarnvld flklilpkde glkidleddi
      361 vaaclvardg qvlrgr
//
LOCUS       WP_122244821             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Vandammella animalimorsus].
ACCESSION   WP_122244821
VERSION     WP_122244821.1
KEYWORDS    RefSeq.
SOURCE      Vandammella animalimorsus
  ORGANISM  Vandammella animalimorsus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Vandammella.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Vandammella animalimorsus"
                     /db_xref="taxon:2029117"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38758
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvplett agetrvaatp etvkklvaqg hevlvqseag laaaatdeay raagaqivda
       61 avalgaelvl kvrapsaqel palqpgavlv gmlnpfdaqg lqaladarlt afaleaaprt
      121 traqsmdvls sqaniagyka vimaadaypr ffpmlmtaag tvkaakvvvl gvgvaglqai
      181 atakrlgati easdvrpsvk eqveslgakf idvpyetdee reaaegvggy arpmpaswle
      241 rqkaevakrv aaadvvitta lipgraaptl vtedmvramk pgavivdiaa grgeggvggn
      301 cpltqadatv vrhgvtiigq tnlpalvaad asqlyarnvl dflklilpkd eglkidtedd
      361 ivaaclmard gqllrs
//
LOCUS       WP_122241183             307 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas syringae].
ACCESSION   WP_122241183
VERSION     WP_122241183.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     gene            1..>307
                     /gene="trxB"
     Protein         1..>307
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..307
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgpalmermr ehaerfetei vfdhinsvdl agkpfslqgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlvhrret
      181 fraekilidk lharvaegki elklnatlde vlgdnmgvtg arlknndgss selkvdgvfi
      241 aightpntsl fdgqlalkdg ymvvqggreg natatsvegv faagdvadhv yrqaitsaga
      301 gcmaald
//
LOCUS       WP_122245051             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vandammella animalimorsus].
ACCESSION   WP_122245051
VERSION     WP_122245051.1
KEYWORDS    RefSeq.
SOURCE      Vandammella animalimorsus
  ORGANISM  Vandammella animalimorsus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Vandammella.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Vandammella animalimorsus"
                     /db_xref="taxon:2029117"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33843
     Region          10..315
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msttntlhak vlilgsgpag ytaaiyaara nlqpvlitgm aqggqltttt evdnwpadaa
       61 gvqgpelmer flkhaerfnt qivfdhiqsv dlsqrpfklh gdsgsysads liiatgasak
      121 ylglpseqaf mgrgvsacat cdgffyrdqp vavvgggnta veealylsni askvtlihrr
      181 dkfraeaimi dklmekvqag kvelklhsvl devlgdasgv tgvrirnvqd dstedlplqg
      241 afiaighapn teifqgqlem kngyiltqgg hdgfatqtsv pgvfaagdvq dhvyrqaits
      301 agtgcmaald aqrfleqqa
//
LOCUS       WP_122247969             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Allofranklinella
            schreckenbergeri].
ACCESSION   WP_122247969
VERSION     WP_122247969.1
KEYWORDS    RefSeq.
SOURCE      Allofranklinella schreckenbergeri
  ORGANISM  Allofranklinella schreckenbergeri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Allofranklinella.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Allofranklinella schreckenbergeri"
                     /db_xref="taxon:1076744"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34057
     Region          10..315
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mstsntlhak vlilgsgpag ytaavyaara nlqpvlitgm aqggqltttt evdnwpadfa
       61 gvqgpelmer flkhaqrfnt hivfdhiqqv dlsqrpftlk gdsgtytadt liiatgasak
      121 ylglpsetaf mgrgisacat cdgffyrdqd vavvgggnta veealylsgi arkvtlihrr
      181 dkfraepimi dklmekvqqg kielkllhvl devlgndsgv tgvrikhves gatedvavhg
      241 afiaighspn tgifqgqlam engyivtrgg hagfatqtsv pgvfaagdvq dhvyrqaits
      301 agtgcmaald aqrfleqsce t
//
LOCUS       WP_122248750             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Allofranklinella schreckenbergeri].
ACCESSION   WP_122248750
VERSION     WP_122248750.1
KEYWORDS    RefSeq.
SOURCE      Allofranklinella schreckenbergeri
  ORGANISM  Allofranklinella schreckenbergeri
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Allofranklinella.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Allofranklinella schreckenbergeri"
                     /db_xref="taxon:1076744"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38814
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,295,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletf agetrvaltp etakklvaqg htigvqsgag vaasvtnday vaagaqivda
       61 aaalgadlvl kvrapspeel ahckrgatlv gmldpfdadg lqrladaglt afaleaaprt
      121 traqsmdvls sqaniagyka vvlaasvyqr ffpmlmtaag tikaarvvvl gvgvaglqai
      181 atakrlgati easdvrpsvk eqveslgakf idvpyetdee reaaegvggy arpmpaswle
      241 rqkqevakrv aaadvvista lipgrpaptl iteemvramr pgsvivdlaa grgangggnc
      301 pltvadqtvq hdgvtllgpt nlpaqmaada salyarnvld flklilpkde glkidleddi
      361 vaaclvardg qvlrgr
//
LOCUS       WP_122261712             340 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Ornithinimicrobium cerasi].
ACCESSION   WP_122261712
VERSION     WP_122261712.1
KEYWORDS    RefSeq.
SOURCE      Ornithinimicrobium cerasi
  ORGANISM  Ornithinimicrobium cerasi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Ornithinimicrobiaceae; Ornithinimicrobium.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Ornithinimicrobium cerasi"
                     /db_xref="taxon:2248773"
     gene            1..340
                     /gene="trxB"
     Protein         1..340
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35763
     Region          21..326
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtiqlpsqtg spspdaegav heiivvgsgp agytaavyaa ranlaplvfe gsvtaggalm
       61 nttevenfpg faegimgpel mmnmreqaer fgatlvrddv vamdlagtvk tvtdaegtth
      121 raravilamg sayrelglpe ekelsghgvs wcatcdgaff rdqdivvvgg gdsameeatf
      181 lsrfgssvtv ihrrgelras kimaeramnd pkirfvwnte vtalngrpkl asitlrdtlt
      241 getrehpttg lfiaighdpr nelvqgqval dpegyvlvqg rstatdvpgv facgdlvdht
      301 yrqaitaags gcaaaldaer ylsalddelp tevavalsah
//
LOCUS       WP_122256591             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            jordanis].
ACCESSION   WP_122256591
VERSION     WP_122256591.1
KEYWORDS    RefSeq.
SOURCE      Legionella jordanis
  ORGANISM  Legionella jordanis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Legionella jordanis"
                     /db_xref="taxon:456"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40468
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miistlnesd kdtrvaispa avkqyikmgf evtvetqagn asgfsdadyq qagatvvner
       61 tvllkttniv llvnepnpse ldglqahslv iahidnepqa elitwacken islismnlip
      121 risraqsmds lssqanlagy ravleatayf kraipmmmta agmihpakvl vlgagvaglq
      181 aiatakrlga vvyafdvrra akeqveslga efvevgveqd aetkggyase tseeykrqqa
      241 elidkfarqs divistalip grkapilltk qtvegmkpgs iivdlatsrg gnceyserdk
      301 vvriggvtlv gysnlagfvp ataselyatn llnlmrllap kaeqldfnae deiikqallc
      361 hagkylpfqa nkeaqha
//
LOCUS       WP_122267575             233 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Pseudomonas savastanoi].
ACCESSION   WP_122267575
VERSION     WP_122267575.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..>233
                     /product="STM4504/CBY_0614 family protein"
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiidlyskr qgrernglnd vytydefssk friqlsmmie ellggiedvy rggkprdaye
       61 glakilrkey glshlvstar sfapdyfsei hdflsvevdv ekvldavela yqlgnrfarh
      121 ssyrlaqidd sddhvdacie elngrfkeag ygyafvedni lrvdseflhs evvkpaihfl
      181 nfegfeaarn eflggydhyr hkrykealad agksfestmk iicglngwet vrn
//
LOCUS       WP_122267012             308 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas syringae].
ACCESSION   WP_122267012
VERSION     WP_122267012.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..308
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35055
     Region          5..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 malvdifskr qkrlrgefsd vysydaipes lrvqivhiml dslgrsdera egepwrfice
       61 tlsreygffr lcdspptrsr nyhqelvdff ltvrevdral dvvemafqil hrvgrefsfr
      121 ylrdadanvt aaidelngrf rehsvgypfe ageiirvdsq ylhaevvkpa lqllnspgfa
      181 gpqdeflrah ehyrhgnske slneclksfe smmkaicskr gwpltgketa sslikvcler
      241 nlipafwqtq fnslkslles avptgrnnla ghgqgveatt vpdhlvayml hmtgaclvfl
      301 aesehrlq
//
LOCUS       WP_122270096             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas savastanoi].
ACCESSION   WP_122270096
VERSION     WP_122270096.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35857
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maindlyskr lkrkrgetpe iytydsipqe livqmfhifd dgignviytg rndiltvwes
       61 ivstlnreyg sftlarfshs kysthydefy hfmfsehnvd rlidgielal gamnttarea
      121 yyggrnnnde kidelieean qrlkehgvgy rfaenvivri dsefihaevt kpalsllqge
      181 wcagaeeefy rahehyrhgn fketlneylk sfesilksvc rkrgweisdk atassliqtr
      241 ldnglipsfw qshfsslksl lesgiptgrn kmsghgqgat ptevpryivs ymlnmtaacl
      301 lficeaeaef eql
//
LOCUS       WP_122267711             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas savastanoi].
ACCESSION   WP_122267711
VERSION     WP_122267711.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38773
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hritvqsgag iqasvpdsay eaagavigsa
       61 neafagelil kvvapddnel sliksgsvvi gmlnpfnnel igkmaaqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera rladivitta lipgrkapvl lgaktvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122277875             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Parabacteroides sp. AM08-6].
ACCESSION   WP_122277875
VERSION     WP_122277875.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides sp. AM08-6
  ORGANISM  Parabacteroides sp. AM08-6
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Parabacteroides sp. AM08-6"
                     /db_xref="taxon:2292053"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33731
     Region          11..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtnsinekvr cliigsgpag ytaaiyasra nlspvlyegi qpggqltttt dvenfpgype
       61 gvtgpelmed lkqqaarfga dmrigiatkt dlsaapykvt idgekviete tliiatgata
      121 kylglpdenk yagmgvsaca tcdgffyrkk tvavvgggdt aceealylas lakqvylivr
      181 kpylraskvm qervmkasni tvlfehntvg lfgedgvega hlvkrmgepd eekvdiaidg
      241 fflaighkpn sdifkpwiet devgyiktip gtpktkvpgv faagdvadph yrqaitaags
      301 gcaaaieaer ylsemgk
//
LOCUS       WP_122279855             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae group genomosp. 3].
ACCESSION   WP_122279855
VERSION     WP_122279855.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 3
  ORGANISM  Pseudomonas syringae group genomosp. 3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae group genomosp. 3"
                     /db_xref="taxon:251701"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38796
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqrgag iqasvpdsaf eaagavigea
       61 sdafagelil kvvapndnel alinsgsavi gmlnpfnnel igkmadrgvi afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv egsdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera rladiiitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adevvvahgv tlvghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122280161             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas syringae group].
ACCESSION   WP_122280161
VERSION     WP_122280161.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38789
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqsgag iqasvpdsay eaagavigsa
       61 teafagelil kvvapddnel sliksgsvvi gmlnpfnnel igkmaaqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyeteee recaegvggy arpmpaswmq
      241 rqaaavhera rladivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122283028             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae group genomosp. 3].
ACCESSION   WP_122283028
VERSION     WP_122283028.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 3
  ORGANISM  Pseudomonas syringae group genomosp. 3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae group genomosp. 3"
                     /db_xref="taxon:251701"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38844
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqrgag iqasvpdsaf eaagavigea
       61 sdafagelil kvvapndnel aminsgsavi gmlnpfnnel igkmadrgvi afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv egsdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqtaavhera rladiiitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adevvvahgv tlvghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122298921             367 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas savastanoi].
ACCESSION   WP_122298921
VERSION     WP_122298921.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..367
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38093
     Region          1..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,275..276,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,225,236,
                     253..255,262,264)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqsgag ihasvpdsay eaagavigsa
       61 neafagelil kvvapddnel sliksgsvvi gmlnpfnnel igkmaaqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdeg vggyarpmpa swmqrqaaav
      241 herarladii ittalipgrk apvllsaetv aqmkpgsvvi dlaaaqggnc pltvadqvvv
      301 ehgvtivght nlpalvaada salyarnlld fmkllfdkdg tfsinleddi vaaclmcrdg
      361 qvvrkng
//
LOCUS       WP_122299462             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_122299462
VERSION     WP_122299462.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38749
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaerdit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_122302298             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas amygdali].
ACCESSION   WP_122302298
VERSION     WP_122302298.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas amygdali
  ORGANISM  Pseudomonas amygdali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas amygdali"
                     /db_xref="taxon:47877"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38880
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqsgag ihasvpdnay eaagavigsa
       61 neafagelil kvvapddnel sliksgsvvi gmlnpfnnel igkmaaqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqalavhera rladiiitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122307516             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas cyclaminis].
ACCESSION   WP_122307516
VERSION     WP_122307516.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas cyclaminis
  ORGANISM  Pseudomonas cyclaminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas cyclaminis"
                     /db_xref="taxon:2781239"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33835
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermk ehaerfetei vfdhinqvdf skkpysltgd ngvytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlvhrret
      181 fraekilidk lharvaegki ilklnatlde vlgdtmgvtg arlknndgsf deltvdgvfi
      241 aightpntsl fegvleakdg ylvvqggreg natatniegi faagdvadhv yrqaitsaga
      301 gcmaaldaer yldglqnasf
//
LOCUS       WP_122315086             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas cichorii].
ACCESSION   WP_122315086
VERSION     WP_122315086.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas cichorii
  ORGANISM  Pseudomonas cichorii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas cichorii"
                     /db_xref="taxon:36746"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38935
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth tgetrvaatp etikklisqg hrvtvqsgag irasvpdsay eaagatiggt
       61 seafaaelil kvtapndsel aliksgtivi gmlnpfsnet iaqlaergit afaleaaprt
      121 sraqsldvls sqaniagyks vllaahhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera rlsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tlvghtnlpa lvaadasaly arnlldfikl lfdkdgqlqi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122316393             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas cichorii].
ACCESSION   WP_122316393
VERSION     WP_122316393.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas cichorii
  ORGANISM  Pseudomonas cichorii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas cichorii"
                     /db_xref="taxon:36746"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33697
     Region          1..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgpalmermr ehaerfetei vfdhinavdl ankpfsltgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlvhrret
      181 fraekilidk lharvaegki elklnatlde vlgdnmgvtg arlknndgss aelkvdgvfi
      241 aightpntsl fegqlalkdg ymvvqggreg natatsvegv faagdvadhv yrqaitsaga
      301 gcmaaldver yldglanvsf
//
LOCUS       WP_122321688             323 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas amygdali].
ACCESSION   WP_122321688
VERSION     WP_122321688.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas amygdali
  ORGANISM  Pseudomonas amygdali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Pseudomonas amygdali"
                     /db_xref="taxon:47877"
     Protein         1..323
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36296
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiidlyskr qgrerngvnd vytydefssk friqlsmmie ellggiedvy rggkprdaye
       61 glvkilrkey glshlvsaar sftpdyfsei hdflsvevdv ekvldavela yqlgnrfarh
      121 ssyrlaymdd sddhvdacie elngrfkeag ygyafvedni lrvdseflhs evvkpaihfl
      181 nfegfeaarn eflggydhyr hkrykealad agksfestmk iicglngwtf kptdgankli
      241 qvlvdkeflp sihqahlsgi htvlsagipt lrnkwgshgd gdtisevhpd vvayglhlta
      301 saivllgslq enhpnaiedk tki
//
LOCUS       WP_122322353             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas amygdali].
ACCESSION   WP_122322353
VERSION     WP_122322353.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas amygdali
  ORGANISM  Pseudomonas amygdali
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas amygdali"
                     /db_xref="taxon:47877"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38746
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqsgag iqasvpdsay eaagavigsa
       61 neafagelil kvvapddnel sliksgsvvi gmlnpfnnel igkmaaqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaaralil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera rladivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tvvghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122321701             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas cichorii].
ACCESSION   WP_122321701
VERSION     WP_122321701.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas cichorii
  ORGANISM  Pseudomonas cichorii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas cichorii"
                     /db_xref="taxon:36746"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33743
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgpalmermr ehaerfetei vfdhinsvdl agkpfsltgd savytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlvhrret
      181 fraekilidk lharvaegki elklnatlde vlgdnmgvtg arlknndgth delkvdgvfi
      241 aightpntsl fegqlalkdg ymvvhggreg natatsvegv faagdvadhv yrqaitsaga
      301 gcmaaldver yldglanasf
//
LOCUS       WP_122325512             300 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas coronafaciens].
ACCESSION   WP_122325512
VERSION     WP_122325512.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas coronafaciens
  ORGANISM  Pseudomonas coronafaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudomonas coronafaciens"
                     /db_xref="taxon:53409"
     Protein         1..300
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34626
     Region          5..162
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mavtdlfskr qkrlrgggpd vyvydklpmp lriqmlymln eligdehefy ktfstcnqiv
       61 hyvvktlrle ygkhhiatdp enddyhelil flrkeedier vmdaveliin qtreypdyde
      121 qcrdfindln irfrehgvgy elingeiiri dsrfhhavvv kpaiqflkqp gfegaqqefi
      181 layehyrhgr hkealnealk tvestmraic sargwaykss dnakrlivil qneqlfpayy
      241 qshlsalvsl megvvslrnn esahgqgpev rhvrddvvay alhmtasvvv mlaglhadkp
//
LOCUS       WP_122327185             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Parabacteroides].
ACCESSION   WP_122327185
VERSION     WP_122327185.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33885
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdsinekvr cliigsgpag ytaaiyasra nlspvlyegi qpggqltttt evenfpgype
       61 gitgpelmed lkqqalrfga dirfgiatet dlsaapykit idgekvieae tviiatgata
      121 kylgipdenk yagmgvsaca tcdgffyrkk vvavvgggdt aceeaiylag lakqvylivr
      181 kpflraskvm qervfnmpni mvlfehntig lfgengvega hlvkrmgesd eekvdiaidg
      241 fflaighkpn sdifkpwidt devgyiktvp gtprtkvpgv faagdvadph yrqaitaagt
      301 gcqaaieaer ylseigk
//
LOCUS       WP_122332793             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Parabacteroides sp. AF48-14].
ACCESSION   WP_122332793
VERSION     WP_122332793.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides sp. AF48-14
  ORGANISM  Parabacteroides sp. AF48-14
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Parabacteroides sp. AF48-14"
                     /db_xref="taxon:2292052"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33709
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntnqnekvr cliigsgpag ytaaiyasra nlspvlyegi qpggqltttt evenfpgype
       61 gvtgtelmed lkqqaarfga dirigiatat dlsaapykvt idgekviete tliiatgata
      121 kylglpdeqk yagmgvsaca tcdgffyrkk vvavvgggdt aceealylas lakqvylivr
      181 kpylraskvm qervlnapni tvlfehntvg lfgedgvega hlvkrmgepd eekvdiaidg
      241 fflaighkpn aeifkpwiet devgyiktip gtpktkvpgv faagdvadph yrqaitaags
      301 gcaaaieaer ylsehgk
//
LOCUS       WP_122341927             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas caricapapayae].
ACCESSION   WP_122341927
VERSION     WP_122341927.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas caricapapayae
  ORGANISM  Pseudomonas caricapapayae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas caricapapayae"
                     /db_xref="taxon:46678"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38892
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag ihasvpdsay eaagaiigna
       61 devyagdlil kvvapddnel nliksgsvvi gmlnpfnnel igkmaargvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera rqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddiaaac
      361 lmcrdghvvr kng
//
LOCUS       WP_122336042             328 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Pseudomonas coronafaciens].
ACCESSION   WP_122336042
VERSION     WP_122336042.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas coronafaciens
  ORGANISM  Pseudomonas coronafaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Pseudomonas coronafaciens"
                     /db_xref="taxon:53409"
     Protein         1..>328
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..328
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hrvtvqsgag lhasvpdsay eaagavigdt
       61 netyaaelil kvvapddeal sliksgsvvv gmlnpfnnel igkmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqveslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera klsdivitta lipgrkapvl lgaetvaqmk pgsvvidlaa aqggncpltv
      301 adrvvvehgv tivghtnlpa lvaadasa
//
LOCUS       WP_122344689             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Parabacteroides sp. AF17-28].
ACCESSION   WP_122344689
VERSION     WP_122344689.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides sp. AF17-28
  ORGANISM  Parabacteroides sp. AF17-28
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Parabacteroides.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Parabacteroides sp. AF17-28"
                     /db_xref="taxon:2292241"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33742
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntnqnekvr cliigsgpag ytaaiyasra nlspvlyegi qpggqltttt evenfpgype
       61 gvtgtelmed lkqqaarfga dirigiatat dlsaapykvt idgekviete tliiatgata
      121 kylglpdeqk yagmgvsaca tcdgffyrkk vvavvgggdt aceealylas lakqvylivr
      181 kpylraskvm qervlnapni tvlfehntvg lfgedgvega hlmkrmgepd eekvdiaidg
      241 fflaighkpn aeifkpwiet devgyiktip gtpktkvpgv faagdvadph yrqaitaags
      301 gcaaaieaer ylsehgk
//
LOCUS       WP_122349415             323 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Pseudomonas syringae
            group].
ACCESSION   WP_122349415
VERSION     WP_122349415.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group
  ORGANISM  Pseudomonas syringae group
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Pseudomonas syringae group"
                     /db_xref="taxon:136849"
     Protein         1..323
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36277
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiidlyskr qdrernglnd vytydefssk friqlsmmie ellggiedvy rggkprdaye
       61 glvkilrkey glshlvstar sftpdyfsei hdflsvevdv gkvldaveva yklgnrfarh
      121 ssyrlaqrdd sddhvdacie elngrfkeag ygyafvedni lrvdseflhs evvkpaihfl
      181 nfegfkaarn eflggyghyr hqrykealad agksfestmk iicglngwtf kptdgankli
      241 qvlvdkeflp sihqahlsgi htvlsagipt lrnkwgshgd gdtisevhpd vvayglhlta
      301 saivflgslq enhpnaiedk tki
//
LOCUS       WP_122354007             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Parabacteroides].
ACCESSION   WP_122354007
VERSION     WP_122354007.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33953
     Region          11..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdsinekvr cliigsgpag ytaaiyasra nlspvlyegi qpggqltttt evenfpgype
       61 gitgpelmed lkqqalrfga dirfgiatat dlsaapykit idgekviete tliiatgata
      121 kylgipdehk yagmgvsaca tcdgffyrkk vvavvgggdt aceeaiylag lakqvylivr
      181 kpylraskvm qdrvfntpni mvlfehntig lfgengvega hlvkrmgepd eekvdiaidg
      241 fflaighkpn sdifkpwlet deigyiktip dtprttvpgv faagdvadph yrqaitaags
      301 gckaaieaer ylsemgk
//
LOCUS       WP_122360794             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Parabacteroides].
ACCESSION   WP_122360794
VERSION     WP_122360794.1
KEYWORDS    RefSeq.
SOURCE      Parabacteroides
  ORGANISM  Parabacteroides
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Parabacteroides"
                     /db_xref="taxon:375288"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33952
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdsinekvr cliigsgpag ytaaiyasra nlspvlyegi qpggqltttt evenfpgype
       61 gitgpelmed lkqqalrfga dirfgiatat dlsaapykit idgekviete tliiatgata
      121 kylgipdehk yagmgvsaca tcdgffyrkk vvavvgggdt aceeaiylag lakqvylivr
      181 ksylraskvm qervfntpni mvlfehntig lfgengvega hlvkrmgepd eekvdiaidg
      241 fflaighkpn sdifkpwlet deigyiktip dtprtkvpgv faagdvadph yrqaitaags
      301 gckaaieaer ylsevgk
//
LOCUS       WP_122388131             300 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas savastanoi].
ACCESSION   WP_122388131
VERSION     WP_122388131.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     gene            1..>300
                     /gene="trxB"
     Protein         1..>300
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..299
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgpalmermr ehaerfetei vfdhinsvdl agkpfslqgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlvhrret
      181 fraekilidk lharvaegki elklnatlde vlgdnmgvtg arlknndgts delkvdgvfi
      241 aightpntsl fegqlalkdg ymvvhggreg natatsvegv faagdvadhv yrqaitsaga
//
LOCUS       WP_122390248             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas savastanoi].
ACCESSION   WP_122390248
VERSION     WP_122390248.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38839
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqsgag ihasvpdsay eaagavigsa
       61 neafagelil kvvapddnel sliksgsvvi gmlnpfnnel igkmaaqgit afvleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recvegvggy arpmpaswmq
      241 rqaaavhera rladiiitta lipgrkapal lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122389360             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas syringae group genomosp. 3].
ACCESSION   WP_122389360
VERSION     WP_122389360.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae group genomosp. 3
  ORGANISM  Pseudomonas syringae group genomosp. 3
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas syringae group genomosp. 3"
                     /db_xref="taxon:251701"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38808
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqrgag iqasvpdsaf eaagavigea
       61 seafagelil kvvalndnel alinsgsvvi gmlnpfnnel igkmadrgvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv egsdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera rladiiitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adevvvahgv tlvghtnlpa lvaadasaly arnlldfmkl lfdkdgtlsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122393632             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas savastanoi].
ACCESSION   WP_122393632
VERSION     WP_122393632.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas savastanoi
  ORGANISM  Pseudomonas savastanoi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas savastanoi"
                     /db_xref="taxon:29438"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38857
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq agetrvaatp etikklisqg hritvqsgag ihasvpdsay eaagavigsa
       61 neafagelil kvvapddnel sliksgsvvi gmlnpfnnel igkmaaqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqaaavhera rladiiitta lipgrkapvl lsaetvaqmk pcsvvidlaa aqggncpltv
      301 adqvvvehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgtfsi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_122401407             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium vignae].
ACCESSION   WP_122401407
VERSION     WP_122401407.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium vignae
  ORGANISM  Bradyrhizobium vignae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium vignae"
                     /db_xref="taxon:1549949"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39271
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfralg aeiavepgag lksglpdsef tavgatvsad
       61 alkdadivik vkrpeasela qykrgalvia imdpygneaa lktmadagva afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake msreyqakqa
      241 altaehikkq divittalip grpapklvsa dmvrsmkpgs vlvdlaverg gnvegakage
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekqlavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_122411931             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122411931
VERSION     WP_122411931.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38957
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay eaagatirga
       61 ddifaselil kvvapnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggngpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldftkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122405608             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium vignae].
ACCESSION   WP_122405608
VERSION     WP_122405608.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium vignae
  ORGANISM  Bradyrhizobium vignae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium vignae"
                     /db_xref="taxon:1549949"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39255
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pleprvaasp dtvkkfkalg aevavepgag iksglpdsef taagatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneaa lramadagva afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake msreyqakqa
      241 altaehikkq divittalip grpapklvsa dmvrsmkpgs vlvdlaverg gnvegakage
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekqlavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_122425189             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122425189
VERSION     WP_122425189.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39021
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqtgag ihasvpdsay eaagatirga
       61 ddtfaselil kvvapnesel tliksgtivi gmlnpfnnen iarmaergvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122433214             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122433214
VERSION     WP_122433214.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38930
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay eaagaaisga
       61 ddtfaselil kvvapnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswiq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tlvgytnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122434128             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas viridiflava].
ACCESSION   WP_122434128
VERSION     WP_122434128.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33695
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgpvlmermr ehaerfetei vfdhinsvdl agkpfslqgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlvhrret
      181 fraekilidk lharvaegki elklnatlde vlgdnigvtg arlknndgss delkvdgvfi
      241 aightpntsl fdgqlalkdg ymvvqggreg natatsvegv faagdvadhv yrqaitsaga
      301 gcmaaldver yldglanasf
//
LOCUS       WP_122436826             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122436826
VERSION     WP_122436826.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39012
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay etagatisga
       61 ddtfaselil kvvtpnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122439454             310 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas viridiflava].
ACCESSION   WP_122439454
VERSION     WP_122439454.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..310
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35235
     Region          4..170
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mihdlfskrq rrqrgefpdv fqyhtlpadl rkqlcmliqq tlgnsetdns glarqvydri
       61 lhalaeewar pellperfnf hperllldaf vqesdneral dvielafqwa nrqaasaeyy
      121 kgvdgrayvd kcieelnarf kehgvgyafv sdelirvdsq vmhtevvkpv ihylsvpgfe
      181 gpqeefftah dhyrhgfyke aiteankafe stmkvicdqk gweykksdta kklimvcien
      241 glfpsyyqsh laslsnlles gvptirnneg ghgqgsavkt vephivsytl hmaasailll
      301 vnsangmear
//
LOCUS       WP_122438544             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas viridiflava].
ACCESSION   WP_122438544
VERSION     WP_122438544.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33712
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgpvlmermr ehaerfetei vfdhinsvdl agkpfslqgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlvhrret
      181 fraekilidk lharvaegki elklnatlde vlgdnmgvtg arlknndgss delkvdgvfi
      241 aightpntsl fdgqlalkdg ymvvqggreg natatsvkgv faagdvadhv yrqaitsaga
      301 gcmaaldver yldglanasf
//
LOCUS       WP_122440344             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122440344
VERSION     WP_122440344.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38892
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay eaagaaisga
       61 ddtfaselil kvvapnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldftkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122440606             369 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium attenuatum].
ACCESSION   WP_122440606
VERSION     WP_122440606.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium attenuatum
  ORGANISM  Mycobacterium attenuatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Mycobacterium attenuatum"
                     /db_xref="taxon:2341086"
     Protein         1..369
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38109
     Region          9..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdaqthtir vgvvaesrpd errvalvpka vaalvnsgva vvvesgaghr allpdelytd
       61 agatvgdawa advvvkvapp taeevgrlhs gqtligflap rnadncigal eqagvqafal
      121 eaiprisraq vmdalssqan vagykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwlevg vtasgeggya reltdeeraq
      241 qqkaleeais gfdvvittal vpgrpaprlv taaaveamkp gsvvvdlage tggnceltep
      301 gktvvkhgvt iasplnlpat mpehaselys knitallell vkdgklapdf ddeviaescv
      361 traqdreds
//
LOCUS       WP_122446490             329 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas viridiflava].
ACCESSION   WP_122446490
VERSION     WP_122446490.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..329
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=37016
     Region          25..191
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mdddthglwh hraitqmelt vpihdiyskr krrlsgdapd vytydalpta lrnqivfvlk
       61 dllgnvfkgi hredictyaa tsiarewgka yvvdhadlys wegqllevir rdpetdhsld
      121 vieflfgfae naasnnteyc pykaieklap cieelnhrfk engvgyeysd gqiirvdsml
      181 lhgevvkpal qllgvagfeg pqeefldahe hyrhkrykea lvsglksfes tmkviserkv
      241 fpfkrtdtak klilvcmeng lfpsyyqshl salanllegg vpsirnneag hgqgaavkei
      301 aphvvaytlh mtaaaivlla nsyleledk
//
LOCUS       WP_122462751             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_122462751
VERSION     WP_122462751.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38599
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipletl tgetrvaatp etikkligqg hkvtvqsgag itasivdgay etagatigsa
       61 seafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqair kna
//
LOCUS       WP_122464539             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brevundimonas lutea].
ACCESSION   WP_122464539
VERSION     WP_122464539.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas lutea
  ORGANISM  Brevundimonas lutea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Brevundimonas lutea"
                     /db_xref="taxon:2293980"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37663
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtvavavtre rregearaal tpdtvktlia sgatvtveag tgqgssipds ayveagaava
       61 pdlqtvlaga dillkvrcpt aqeisalkpg avvvgmldpt retatiealt aarvtafame
      121 rvprisraqv mdalssqanl agyravieaa safgrgfpmm mtaagtvapa kvfimgvgva
      181 glqaiatarr lgavvtatdv rpatkeqves lgakflavdd eefrnaqtag gyakemsaey
      241 qakqaalvge hlkkqdivit talipgrpap rlvtadqvat mkpgsvlidl avetggnveg
      301 aqadqavtta ngatilgfsn lpariaadat alyarnlaaf vgllikdgal apdledeilk
      361 aalvtgegsa
//
LOCUS       WP_122480118             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_122480118
VERSION     WP_122480118.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38837
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq qgetrvaatp etikklvaqg havtvergag vlasvtdday qaagatigsa
       61 aqafatqlvl kvnapsdael qqmaagtvll gmlnpfnnev iakmaargis afaleaaprt
      121 sraqsldvls sqaniagyks vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee recavgtggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lgaetvaqmk pgsvvidlaa lqggncpltv
      301 adqivvhngv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgqfti nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_122477967             530 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_122477967
VERSION     WP_122477967.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54784
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taheerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ataadlwgrs divlkvrpps seevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfiagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvve elckgkdgti nvdfnddair
      361 gltvvkegnv twppppiqqp aaapkpatpp vaaaaskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgdaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_122494338             369 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium attenuatum].
ACCESSION   WP_122494338
VERSION     WP_122494338.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium attenuatum
  ORGANISM  Mycobacterium attenuatum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Mycobacterium attenuatum"
                     /db_xref="taxon:2341086"
     Protein         1..369
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38137
     Region          9..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdaqthtir vgvvaesrpd errvalvpka vaalvnsgva vvvesgaghr allpdelytd
       61 agatvgdawa advvvkvapp taeeigrlhs gqtligflap rnadncigal eqagvqafal
      121 eaiprisraq vmdalssqan vagykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwlevg vtasgeggya reltdeeraq
      241 qqkaleeais gfdvvittal vpgrpaprlv taaaveamkp gsvvvdlage tggnceltep
      301 gktvvkhgvt iasplnlpat mpehaselys knitallell vkdaklapdf ddeviaescv
      361 traqdreds
//
LOCUS       WP_122501832             369 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycobacterium pseudokansasii].
ACCESSION   WP_122501832
VERSION     WP_122501832.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium pseudokansasii
  ORGANISM  Mycobacterium pseudokansasii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Mycobacterium pseudokansasii"
                     /db_xref="taxon:2341080"
     Protein         1..369
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38121
     Region          9..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,78,97,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(52,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdaqthtir vgvvaesrpd errvalvpka vaslvnsgva vvvesgagqr allpdehytd
       61 agatigdawa advvvkvapp taeevgrlhs gqtligflap rnadnsigal kqagvqafal
      121 eavprisraq vmdalssqan vagykavlla asestrffpm lttaagtvkp atvlvlgvgv
      181 aglqalatak rlgarttgyd vrpevadqvr svgaqwlevg vtasgeggya reladeervq
      241 qqkaleeais gfdvvittal vpgrpaprlv taaaveamkp gsvvvdlage tggnceltep
      301 gktvvkhgvt iasplnlpat mpehaselys knitallell vkdgklapdf ddeviaescv
      361 traqdreds
//
LOCUS       WP_122506366             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas atacamensis].
ACCESSION   WP_122506366
VERSION     WP_122506366.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas atacamensis
  ORGANISM  Pseudomonas atacamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas atacamensis"
                     /db_xref="taxon:2565368"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38831
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag vkasvvdsay eaagasigts
       61 ndafgaelil kviapsdael plikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_122522514             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122522514
VERSION     WP_122522514.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38950
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvavtp etikklisqg hsvtvqsgag ihasvpdsay eaagaaisga
       61 ddtfaselil kvvapnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122571219             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122571219
VERSION     WP_122571219.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38992
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay eaagatirga
       61 ddtfaselil kvvapnesel triksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv egsdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrggqvir kng
//
LOCUS       WP_122584393             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122584393
VERSION     WP_122584393.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38937
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay eaagaaisga
       61 ddtfaselil kvvapnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa qvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122585172             300 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas viridiflava].
ACCESSION   WP_122585172
VERSION     WP_122585172.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..300
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34670
     Region          5..162
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mavtdlfskr qkrlrgggpd vyvydklpmp lriqmlymln eligdehefy ktfstcnqiv
       61 hyvvktlrle ygkhhiatdp enddyhelil flrkeedier vmdaieliin qtdeypdyde
      121 kcrdfindln irfrehgvgy efingeiiri dsrfhhavvv kpaiqflkqp gfegaqqefi
      181 layehyrhgr hkealnealk tvestmraic sargwaykss dnakrlivil qnehlfpayy
      241 qshlsalvsl megvvslrnn esahgqgpev rhvrddvvay alhmtasvvv mlaglhvdkp
//
LOCUS       WP_122626705             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Allolucifera butyrica].
ACCESSION   WP_122626705
VERSION     WP_122626705.1
KEYWORDS    RefSeq.
SOURCE      Allolucifera butyrica
  ORGANISM  Allolucifera butyrica
            Bacteria; Bacillati; Bacillota; Negativicutes; Veillonellales;
            Veillonellaceae; Allolucifera.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Allolucifera butyrica"
                     /db_xref="taxon:1351585"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53332
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl agetrvaatp ntvgqlkklg fevvietgag eaasftdaay taagagiaag
       61 dvvwqsdiiy kvnapndaem aavkegatlv sflwpaqnpd lvtklaakki nvlamdmvpr
      121 israqsldal ssmaniggyr avveaahafg rffngqitaa gkvppakvlv igagvaglaa
      181 igtarslgai vrafdtrlev aeqiesmgge flkldfgted gssadgyakv msdefiqaem
      241 alfaeqakev diiittalip gkpapklvtk amvdsmkags vivdmaaatg gnceytvqdt
      301 mvvtdsgvkv igytdlpgrl paqssqlyat nlvnltklls kakdgsihld fedavlrnlc
      361 vvhngevtfp pppirvsaap qkntaavapa tekkpkpssl kywlgiagla lfgwvgyvsp
      421 peflshftvf vlacvvgyyv vwnvthslht plmsvtnais giivvgallq igstampvkv
      481 lafiavmiat vniiggftvt qrmlkmftkg
//
LOCUS       WP_122651707             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia pseudomallei].
ACCESSION   WP_122651707
VERSION     WP_122651707.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39102
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvrkyaaag hrvtvergag agasfpdday aaagaelada
       61 aaafgadivl kvqaptdaec gqlkrgsvli gmlepfnaeq aarlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaarypr ffpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetqde rdaaqgvggy arpmpaswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qvivhhgvti aghtnlaamv padasslyar nlfdflkliv tkegalnidl
      361 sddivaatll crdgevvrk
//
LOCUS       WP_122663325             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122663325
VERSION     WP_122663325.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38963
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth pqetrvsatp etvrkliaqg hqvvvqagag llssitddgy qaagasigta
       61 ddafgaqvil kvvapnetel slvkagtvli gmlnpfdlms itrmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfdtdee recalgvggy arpmppswmq
      241 rqaqvvhera kksdivitta lipgrkapil lsaetvaqmk pgsvvidlaa lqggncpltv
      301 adqvlvhngv tivgptnlpa qvgadasaly arnlldftkl lfdkegtlti nleddivaac
      361 lmcrdgsvir kng
//
LOCUS       WP_122664640             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122664640
VERSION     WP_122664640.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38865
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgekrvaatp etikkliaqg hrvtvqsgag itasvtdsay eaagatigaa
       61 aealaaelvl kvcapndsel tqiksgtivv gmlnpfnnet iikmaeqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllgahhypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recavgvggy arpmpaswmq
      241 rqavavhera kqsdivitta lipgrkapvl lsaetvaemk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tlvgytnlpa lvaadasaly arnlldfmkl lfdkdgqlhi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122671873             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122671873
VERSION     WP_122671873.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38966
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay etagaaisga
       61 ddtfaselil kvvapnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqiir kng
//
LOCUS       WP_122679535             307 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas viridiflava].
ACCESSION   WP_122679535
VERSION     WP_122679535.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..307
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34792
     Region          5..169
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mpifdifskr qkklrgetpd iyqydrlpda lrvqivhamc dalggpndrp nqncwkfise
       61 mlcreyglfa lptarqhgqr dfadevinff lqtedleqal dvvelcfrav drisretqyl
      121 wrnnsneiad asidelnkrf qehgvgyqfv ngeilridsq llhaevvkpa lrllesksya
      181 gpqqeflkah ehyrhgnske alneclksfe slmkaicakr kwtvtgketa sslikvcmdn
      241 glipafwqtq ftslksllea avptgrnnla ghgqgaeptv vpdylvayml hmtgaclvfl
      301 ataeqhl
//
LOCUS       WP_122705363             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas atacamensis].
ACCESSION   WP_122705363
VERSION     WP_122705363.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas atacamensis
  ORGANISM  Pseudomonas atacamensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas atacamensis"
                     /db_xref="taxon:2565368"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38805
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag vkasvvdsay eaagasigsa
       61 ndafgaelil kviapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_122710579             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122710579
VERSION     WP_122710579.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38938
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay easgaaisga
       61 ddtfaselil kvvapnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122743114             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas coleopterorum].
ACCESSION   WP_122743114
VERSION     WP_122743114.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas coleopterorum
  ORGANISM  Pseudomonas coleopterorum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas coleopterorum"
                     /db_xref="taxon:1605838"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39024
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq qgetrvaatp etikklvaqg hvvtvesgag vrasvtdgay eaagaiigsa
       61 aqvfatqlvl kvnppndael lqmssgtvll gmlnpfnnel iakmaergis afaleaaprt
      121 sraqsldvls sqaniagyks vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee recaegtggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa lqggncpltv
      301 adqvvvhngv tivgptnlpa qvgadasaly arnlldfmkl lfdkegqfti nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_122769708             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia pseudomallei].
ACCESSION   WP_122769708
VERSION     WP_122769708.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39058
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvrkyaaag hrvtvergag agasfpdday aaagaelada
       61 aaafgadivl kvqaptdaec gqlkrgsvli gmlepfnaeq aarlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr ffpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetqde rdaaqgvggy arpmpaswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvan qvivhhgvti aghtnlaamv padasslyar nlfdflkliv tkegalnidl
      361 sddivaatll crdgevvrk
//
LOCUS       WP_122788034             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cutibacterium modestum].
ACCESSION   WP_122788034
VERSION     WP_122788034.1
KEYWORDS    RefSeq.
SOURCE      Cutibacterium modestum
  ORGANISM  Cutibacterium modestum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Cutibacterium.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Cutibacterium modestum"
                     /db_xref="taxon:2559073"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53774
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgenrvaatp ttvptllklg yevvvesgag ehaalpdray eeagarivep
       61 geaweadlvl avneptddqi almragavlv tflhprqdla lteklaaagv tglsmdmvpr
      121 israqsmdal ssmanisgyr aaieaafayg rtfggqvtaa gkvppakvfv igtgvaglaa
      181 lgaansmgae vyatdvrpet aeqvqsmgat flhvrtgdsd qgvssdgyak etsddynara
      241 aelymeqagk ddviittaai pgkpspqlit aemvaamkpg svivdlaalg ggnceltrpg
      301 esyvtdngvt iigytdlpsr lpgqasqlyg tnlvnllkla tpekngelvl nfddevvrtm
      361 tvchegqvaf ppppvqvaaa pkpvakadta svpatpekka rpwpqtfgiv avlsialial
      421 ltfspmefva lfgtfaiavv vgyyvvwnvt halhtplmsv tnaisgiiiv gaitqlgses
      481 wgirivaalt vliasinifg gftvtqrmlk mfrka
//
LOCUS       WP_122794738             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia pseudomallei].
ACCESSION   WP_122794738
VERSION     WP_122794738.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomallei
  ORGANISM  Burkholderia pseudomallei
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei
            group.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia pseudomallei"
                     /db_xref="taxon:28450"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39087
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvrkyaaag hrvtvergag agasfpdday vaagaelada
       61 aaafgadivl kvqaptdaec gqlkrgsvli gmlepfnaeq aarlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr ffpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetqde rdaaqgvggy arpmpaswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qvivhhgvti aghtnlaamv padasslyar nlfdflkliv tkegalnidl
      361 sddivaatll crdgevvrk
//
LOCUS       WP_122819694             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Varibaculum vaginae].
ACCESSION   WP_122819694
VERSION     WP_122819694.1
KEYWORDS    RefSeq.
SOURCE      Varibaculum vaginae
  ORGANISM  Varibaculum vaginae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Varibaculum.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Varibaculum vaginae"
                     /db_xref="taxon:2364797"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54376
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkept pdqtlvaatp dtvkklsklg yevlvehgag ekaayldeqy laagaqivdt
       61 eaawqadivt vldtpptnyl dlirpgalli armaparhpe tvdtlvergi tgfamdtvpr
      121 israqsmdvl ssmsnvsgyr avieaaesfg rlftgqvtaa gkippakvyv igvgvaglaa
      181 igtansmgaq vsatdvrset aeqaesvgat fvpipiaqek sddgyakems adqadaatkl
      241 yteqaachdi vittanipgr rspllitkea vagmapgsvi vdmaaagggn celtrpgekv
      301 vtengvtiig ytdlagrlpg qssqlygqni vnlfklitpe kdgkyvldme devvrgitia
      361 kdgenmfppp pikvhaapap ektesvadaa emarkkaeaa asnkrkrllw aavgivlgla
      421 liaatpkpli pyyfilmlai vvgfyvitsv thslhtplms etnaisgiil vgailqvgsa
      481 npvvstlsfl ailvasinif ggfsvthrml amfrgeek
//
LOCUS       WP_122858989             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122858989
VERSION     WP_122858989.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38922
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay eaagaaisga
       61 ddtfaselil kvvapnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdlvitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122864434             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas viridiflava].
ACCESSION   WP_122864434
VERSION     WP_122864434.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas viridiflava
  ORGANISM  Pseudomonas viridiflava
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas viridiflava"
                     /db_xref="taxon:33069"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38888
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq sgetrvaatp etikklisqg hsvtvqsgag ihasvpdsay eaagaaisga
       61 ddtlaselil kvvapnesel tliksgtivi gmlnpfnnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera klsdivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvtiehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkdgafsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_122899476             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter sp. B51(2017)].
ACCESSION   WP_122899476
VERSION     WP_122899476.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. B51(2017)
  ORGANISM  Acinetobacter sp. B51(2017)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter sp. B51(2017)"
                     /db_xref="taxon:2060938"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39802
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv agehrvaatp etvkklvnag hqvviergag iraayidssy eqvgaklted
       61 aysgseiilk vrapkaeeiq klpqgshvva mfdpyrnpel elfakqnvta falellprtl
      121 sraqnmdvls sqanlagyka vllasneyqr mfpmlmtaag tvkparvvvm gvgvaglqai
      181 atakrlgavv eatdlrptak dqveslggkw ldvpmseeek nraaeaakng ygwmpgeqyi
      241 kdqaaivdka vanadivitt allpgrdapr liqadtvakm kpgsvildma vetggnvags
      301 kcgetvvtan gvkilgvpni patvateasa lyarnvynfv etlfdadkkl alnqedeiqk
      361 almvahggqv llkrg
//
LOCUS       WP_122937241             410 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Agromyces tardus].
ACCESSION   WP_122937241
VERSION     WP_122937241.1
KEYWORDS    RefSeq.
SOURCE      Agromyces tardus
  ORGANISM  Agromyces tardus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Agromyces.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Agromyces tardus"
                     /db_xref="taxon:2583849"
     Protein         1..>410
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvgiaqerr egerrvaatp etvrqlaslg levqvergag vasgfadgay aeagaelvdr
       61 ldpavvdvla hvrplepeqp grlrpgtitv glaspaselg tvvalaeagv tafalelvpr
      121 israqsmdal tsqalvagyr cvleaamrlp rffplfmtaa gtippatvvv lgagvaglqa
      181 igtakrlgar vsandvraas adevasmggt fidldldaaa daaggyakel gedraalqrr
      241 llaphiaaad vlittaaipg rpapllvtad mvaamkpgsv vvdlaaesgg nvegsvaged
      301 vavatadglg tvtivgmkda asrmpsdasr lyaknvanli almtvdgava pdfddevvag
      361 aclthggevr haptaaaiad alaeaadema pptdvappap pappappapp
//
LOCUS       WP_122944498             379 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_122944498
VERSION     WP_122944498.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39042
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etakkfaaag hrvsiakgag iaasypdaay aaagaeltgq
       61 saafdvdivl kvqaptdael pllkrgavlv gmldpfngeq aaklaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qvivhdgvti agytnlasml aadasalyar nlldfmkliv tkegtlnidl
      361 tddivaatll crdgevark
//
LOCUS       WP_122949919             530 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia cepacia complex].
ACCESSION   WP_122949919
VERSION     WP_122949919.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54832
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigvple taheerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ptaadlwgrs divfkvrpps seevslmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfiagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akevdiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvae elckakdgti nvdfnddair
      361 gltvikegnv twppppipqp vaaakpaaap vaaaaskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgdaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_122954204             371 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Polaromonas].
ACCESSION   WP_122954204
VERSION     WP_122954204.1
KEYWORDS    RefSeq.
SOURCE      unclassified Polaromonas
  ORGANISM  unclassified Polaromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Polaromonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="unclassified Polaromonas"
                     /db_xref="taxon:2638319"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38253
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeit agetrvaitp etakklkaqg htvrvqsgag vaasvpdeay tavgaeitda
       61 agaygadivl kvrcpldsem glaksggvlv gmlnpfdaag lqrlaaaqlt sfaleaaprt
      121 sraqsmdvls sqaniagyka vmmaaaeyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslggkf idvpyetdee reaavgvggy akpmppswle
      241 rqkaevakrv aqadvvitta lipgrpapvl vtedmvkamk pgsvivdlaa pqggncplte
      301 pgktvvkhgv tligqtnvpa lvaadasaly arnlldflkl iitkegtlnv dleddivaac
      361 lmtqggevkk k
//
LOCUS       WP_122976472             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinoplanes teichomyceticus].
ACCESSION   WP_122976472
VERSION     WP_122976472.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes teichomyceticus
  ORGANISM  Actinoplanes teichomyceticus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Actinoplanes teichomyceticus"
                     /db_xref="taxon:1867"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52286
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigvlgesd pgerrvaatp atveqlrklg yevvvepgag rrasfadeay adagatigdp
       61 yradvvftin apeparldrl ragatligvf nprlnaelvq efarrpitvl smdavprisr
      121 aqsldvlssm aniagyravv eaahafgrff tgqvtaagkv ppakvlvagv gvaglaaiga
      181 agslgavvra tdprpevadq vkslggeyla vraadvevsa tgyakemsdd yneraarlya
      241 eqatevdiii ttalipgrpa prlitapmva smkpgsvivd maaanggnve gtvpgesitt
      301 pngvtiigyt dlagrlpaqa sqlygtnlvn liklmtpgrd gtlvldfddv vqraitvvre
      361 geltwppppv avsaapaqaa paatapkava qppaagrnrg lalvgagala lfllaalapa
      421 alrghltvfa laivigyyvi ghvhhalhtp lmsvtnaisg iivvgallql ghgglavtvl
      481 sliaillasi nvfggfavtr rmlamftrs
//
LOCUS       WP_123013930             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_123013930
VERSION     WP_123013930.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53889
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 deiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqdsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_123026673             364 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium stellerae].
ACCESSION   WP_123026673
VERSION     WP_123026673.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium stellerae (Mycobacterium stellerae)
  ORGANISM  Mycolicibacterium stellerae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Mycolicibacterium stellerae"
                     /db_xref="taxon:2358193"
     Protein         1..364
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37667
     Region          4..354
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,71,90,283,309,311)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,273..274,316..317,321,
                     324..325)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,223,234,
                     251..253,260,262)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtligvpret apgerrvalv pkiverlcga glsviieaga gagalipdah yeeagatvgd
       61 pwpadvvvkv npptddeitf mkpgsivagf laprtrpdva drlriagvtg fameavpris
      121 raqtmdalss qanvagykav lcaaecstrf fpmlttaagt vkpsavlvlg vgvaglqala
      181 takrlgartt gfdvrpevae qvrslgaqwl elgvqaagdg gyartlttee qaeqqlrlte
      241 aisgfdvvit talvpgrpap rlvtaeavhr mrpgsvvvdl ageaggncel tvagetvvrh
      301 avtiasplnl patmpehase lyarnvaall ehmladgeiv pdlsdeilsa ccvtatsdql
      361 tear
//
LOCUS       WP_123028696             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium stellerae].
ACCESSION   WP_123028696
VERSION     WP_123028696.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium stellerae (Mycobacterium stellerae)
  ORGANISM  Mycolicibacterium stellerae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Mycolicibacterium stellerae"
                     /db_xref="taxon:2358193"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52459
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl pgetrvaatp qtvgqliklg yevvvetgag aassfsdaaf teagadvgsa
       61 eqvwaadvvl kvnapddaei aamrdgatli slispalkpe lveqlasrpi talamdavpr
      121 israqsldvl ssmaniagyr aviesankfg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaagslgai vratdprpev adqvkslgge ylsiespeaq vsatgyakem gddykareaa
      241 lyadqagdvd iiittalipg kpapriitad mvasmkpgsv ivdmaaangg nvegtvkdqa
      301 iltdngvtii gytdlagrlp atasqlygtn lvnllklltp ekdgqltldw ddvvqrsvtv
      361 vrdgevtwpp ppvqvsaapv aaaapaeakp akqpmttarr lgltftaaav lfalialspa
      421 alqvhltvfa laivigyyvi gnvhhalhtp lmsvtnaisg iivvgallqi ghgiqsggav
      481 itavatlail lasinvfggf avtrrmlamf srs
//
LOCUS       WP_123030765             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus paracasei].
ACCESSION   WP_123030765
VERSION     WP_123030765.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34037
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 makkydvivi gagpggmtaa lyasranlsv lmldrgvygg qmnntaeven ypgfksilgp
       61 dlgqkmydga tqfgaeyayg nvvsvqnrga vklvktdede yeakaiviat gaehkklgvp
      121 geeaysgrgv sycavcdgaf fkdrelavig ggdsaieegl yltqmakkvt vihrrdqlra
      181 qqiiqkrafa nakmhfvwna qvqeiqgddm kvtgvkyrdk etgeehvlpv agvfiyvgim
      241 pmteafqdlg vldehgwipt dehmrtkvpg vfaigdvrak dlrqittavg eggtagqgvf
      301 nyiqslndtn ieika
//
LOCUS       WP_123032696             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Haliea
            alexandrii].
ACCESSION   WP_123032696
VERSION     WP_123032696.1
KEYWORDS    RefSeq.
SOURCE      Haliea alexandrii
  ORGANISM  Haliea alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Haliea.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Haliea alexandrii"
                     /db_xref="taxon:2448162"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40792
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriaipreth pgenrvpvtp etakklcrlg aelviengmg lgsgftdeey aaagatlttd
       61 reglfrdadm llrlrkpeka dialmkkgci hisyldpfne hdlvrnlqqh gvtaismemi
      121 prttrsqkmd alssqanlag yvmvlqaath lprifpmmmt pagtlkpakv fiigagvagl
      181 qavatakrlg arvtafdtrp vvaeqvrslg atfldidlgq tgetaggyat eltpeqiqkq
      241 rdaqketiad sdvvittaqv fgrkppvivt kdmvegmkpg svivdmaaet ggnvegsvpn
      301 evvtvngvti igkgnlpnev crdashmyas nlfnlvddaw dkesntfkid fehdilpgci
      361 ithggevtne tiknileggn
//
LOCUS       WP_123036314             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia gladioli].
ACCESSION   WP_123036314
VERSION     WP_123036314.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia gladioli
  ORGANISM  Burkholderia gladioli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia gladioli"
                     /db_xref="taxon:28095"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38998
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,300,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetr ayearvaatp etvkkyvaag hsvcvergag aaasfpdeay aaagatlger
       61 aaayaaeivl kvqapdsdel pqmkrgavlv gmldpfnaeq aarlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee reaaqgtggy arpmppswla
      241 rqaalvhera kqadivista lipgrpaptl iqadtvaamk pgavivdlaa grgpenadgr
      301 rggncpltva dqvvkvhgvs iaghtnlaaq vgadasalya rnladflkli vtkegalnid
      361 mnddivaatl lcrdgevvrk
//
LOCUS       WP_123034404             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Haliea alexandrii].
ACCESSION   WP_123034404
VERSION     WP_123034404.1
KEYWORDS    RefSeq.
SOURCE      Haliea alexandrii
  ORGANISM  Haliea alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Halieaceae; Haliea.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Haliea alexandrii"
                     /db_xref="taxon:2448162"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33559
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvqhhpli ilgsgpagyt aavyaaranl kpvvitgmqq ggqlttttev enwpgghael
       61 qgpelmqqmq ahverfetav vfdhiekvdl ssrpfqlegs sryscdalii atgasaqylg
      121 lpseaafmgk gvsacatcdg ffyrnqkvav igggntavee alylaniase vvlvhrrdsl
      181 raekvlqdrl fkraeegkvr llwnhtldev lgdssgvtgm rvrstgdgat sdhdlagvfi
      241 aighkpntdi fqgqldmkdg yinlrsgteg natatsvpgv faagdvgdhi yrqaitsagf
      301 gcmaaldaek yldnlg
//
LOCUS       WP_123048694             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corynebacterium alimapuense].
ACCESSION   WP_123048694
VERSION     WP_123048694.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium alimapuense
  ORGANISM  Corynebacterium alimapuense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Corynebacterium alimapuense"
                     /db_xref="taxon:1576874"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33084
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtapdtvhdv aiigsgpagy taalyaarae lkpivfegye yggslmttte venypgfkag
       61 imgpelmeem rsqaerfgad lrmelvdhve ldgeikkihv gdgiyharav ilatgaaprl
      121 lgvpgedtlm grgvstcatc dgfffrgkdi aiigggdsam eeamfltrfa nkvsivhrre
      181 efrasaimld rarandkief itnktvdhvi eadgkvgals lrdtvtgels elavaamfva
      241 ighdprssfl ggqvtlkedg yvnvdepstn tnlsgvfacg dlvddhyqqa itaagsgcra
      301 aidaehylas l
//
LOCUS       WP_123052755             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium sp. JN-1].
ACCESSION   WP_123052755
VERSION     WP_123052755.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. JN-1
  ORGANISM  Clostridium sp. JN-1
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Clostridium sp. JN-1"
                     /db_xref="taxon:2483110"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33708
     Region          5..286
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mshlydcvii gggpaglsag iyasrsrmnt llierakygg qatttdelen ypgsiedctg
       61 tslsqrmksq amnfgtkfvk deiidvdldg evkvikgknd kyeartviia tganprlsgf
      121 knekelrgrg isycatcdad fftdldvavv gggdsaitea iyltkfaehv tvihrrdelr
      181 avkslqekaf andkisfiwn stveeavgde ileelviknk itgeksklkv ngcfvfvgyn
      241 piselfkgkv smdgreyiit dedmrtnvpg vfaagdirkk slrqvitaaa dgaiaattae
      301 kyieenkilg
//
LOCUS       WP_123071735             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Massilia
            aurea].
ACCESSION   WP_123071735
VERSION     WP_123071735.1
KEYWORDS    RefSeq.
SOURCE      Massilia aurea (Telluria aurea)
  ORGANISM  Massilia aurea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Massilia aurea"
                     /db_xref="taxon:373040"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38799
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaakh qvlvqsgagl haaapdsaye aagasivdas
       61 aafgadmvlk vrspdaaerg lmrreavlvg mldpfdadnl salaasgvta faleaaprit
      121 raqsldvlss qaniagykai llaantygrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpyvtdeer eiaqgsggya rpmpadwmrr
      241 qgelvherak ladivvttal ipgrkapili geetvramkp gsvivdmaia qggncpltel
      301 gktvirhgvh iigepnlaal vpadasalya rnvldflklv idkddrffid redeivtatl
      361 vcvggevlrk
//
LOCUS       WP_123059375             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Virgibacillus dokdonensis].
ACCESSION   WP_123059375
VERSION     WP_123059375.1
KEYWORDS    RefSeq.
SOURCE      Virgibacillus dokdonensis
  ORGANISM  Virgibacillus dokdonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Virgibacillus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Virgibacillus dokdonensis"
                     /db_xref="taxon:302167"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35922
     Region          19..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maelfirkea ntmsdikmyd viiagagpag mtaavyasra nletlmierg ipggqmante
       61 dvenypgydh ilgpdlsnkm fehakkfgaa yaygdikevi dhgayktiva gqkeyhtral
      121 iittgaqykk lgipgeeels grgvsycavc dgaffkdknl vvigggdsav eegiyltrfa
      181 nkvtiihrrd elraqrilqd rafdndkidf iwdtivekin egagkvgsvt lknnntgety
      241 dheidgvfvy igmvplsepf tslgitneeg yiptnenmet kipgifaagd irektlrqiv
      301 tatgdgsiaa eqaikyvedl meelkaths
//
LOCUS       WP_123073194             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus aureus].
ACCESSION   WP_123073194
VERSION     WP_123073194.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33517
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteidfdiai igagpagmta avyasranlk tvmiergipg gqmanteeve nfpgfemitg
       61 pdlstkmfeh akkfgavyqy gdiksvedkg eykminfgnk eltakaviia tgaeykkigv
      121 pgeqelggrg vsycavcdga ffknkrlfvi gggdsaveeg tfltkfadkv tivhrrdelr
      181 aqrilqdraf kndkidfiws htlksinekd gkvgsvtlts tkdgseethe adgvfiyigm
      241 kpltapfkdl gitndvgyiv tkddmttsvp gifaagdvrd kglrqivtat gdgsiaaqsa
      301 aeyiehlndq a
//
LOCUS       WP_123073545             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus aureus].
ACCESSION   WP_123073545
VERSION     WP_123073545.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33484
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteidfdiai igagpagmta avyasranlk tvmiergipg gqmanteeve nfpgfemitg
       61 pdlstkmfeh akkfgavyqy gdiksvedkg eykvinfgnk eltakaviia tgaeykkigv
      121 pgeqelggrg vsycavcdga ffknkrlfvi gggdsavkeg tfltkfadkv tivhrrdelr
      181 aqrilqdraf kndkidfiws htlksinekd gkvgsvtlts tkdgseethe adgvfiyigm
      241 kpltapfkdl gitndvgyiv tkddmttsvp gifaagdvrd kglrqivtat gdgsiaaqsa
      301 aeyiehlndq a
//
LOCUS       WP_123079563             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. ADI95-16].
ACCESSION   WP_123079563
VERSION     WP_123079563.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. ADI95-16
  ORGANISM  Streptomyces sp. ADI95-16
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces sp. ADI95-16"
                     /db_xref="taxon:1522758"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33613
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgim
       61 gpdlmdnmrg qaerfgaeli pddivsadlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtivhrrds
      181 lraskamqdr afadpkikfa wdsevaeihg dpklsgltlr ntktgetsel pvtglfiavg
      241 hdprtelftg qldldeegyl kveapstrtn itgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala daehatatv
//
LOCUS       WP_123088482             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Montanilutibacter
            psychrotolerans].
ACCESSION   WP_123088482
VERSION     WP_123088482.1
KEYWORDS    RefSeq.
SOURCE      Montanilutibacter psychrotolerans
  ORGANISM  Montanilutibacter psychrotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Montanilutibacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Montanilutibacter psychrotolerans"
                     /db_xref="taxon:1327343"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34098
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mtptkhsrlv ilgsgpagwt aavyaaranl rplvitglqm ggqlmtttev dnwpgdahgl
       61 mgpdlmarmq ahaerfdtet vfdhihtadv sqrpfrlrgd ngdytcdali iatgatakyl
      121 glpseetfkg rgvsacatcd gffykeqdva vigggntave ealylsnicr kvylvhrrdt
      181 lraekimqdk lqakiqagki eaiwhhqvde vlgndagvtg vrlksvqdgs trevdihglf
      241 vaightpntt lfegqlemkn gyltiqtglh gnatqtsvqg vfaagdvadq vyrqaitsag
      301 fgcmaaldae kyldkeg
//
LOCUS       WP_123091437             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Janibacter
            melonis].
ACCESSION   WP_123091437
VERSION     WP_123091437.1
KEYWORDS    RefSeq.
SOURCE      Janibacter melonis
  ORGANISM  Janibacter melonis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Janibacter.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Janibacter melonis"
                     /db_xref="taxon:262209"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52314
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqvgvpaesr pgetrvaatp ktvgqvvalg ydvvvesgag arssypdeay aeagaqigta
       61 aqawaadvvv rvnapteael ammrpgatla sllapaidpa avdrvtragi talamdavpr
      121 israqsldvl ssmaniagyr avieaageyg glftgqvtaa gkmppakvlv cgagvaglaa
      181 igtagslgai vrafdvrpev aeqvesmgad fltvdvvter ssdgyakeag edfdraaaal
      241 yleqardvdi iittalipgr paprlitaam ldamrpgsvv vdmaasnggn vegsvpdemv
      301 vtdhgvkiig ytdlagrlpt qasqlygtnv vnllklltpg kdgqlvldld dvvvrgmtva
      361 rdgetlwppp pvqvsaapap ppsaevappp ppkepmsptt rlalggagal lflfvaavsp
      421 apflghfmvf mlavvvgfyv ighvhhalht plmsvtnais giivvgallq vghdggvavs
      481 alafvailla sinvfggftv tarmlqmfrk gda
//
LOCUS       WP_123094663             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Marinomonas hwangdonensis].
ACCESSION   WP_123094663
VERSION     WP_123094663.1
KEYWORDS    RefSeq.
SOURCE      Marinomonas hwangdonensis
  ORGANISM  Marinomonas hwangdonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Marinomonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Marinomonas hwangdonensis"
                     /db_xref="taxon:1053647"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34152
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvkhaklm ilgsgpagyt aavyaaranl npvmitgmqm ggqlttttev dnwpgddqgv
       61 qgpelmermr khaerfetei ifdhvnkvdl qnrpfrlegd sgvytcdali istgasaqyl
      121 gleseskfmg qgvsacatcd gffyrnqdva vvgggntave ealylaniak tvtvihrrdk
      181 frsekiladk lmekaktgnv kiewyselde vlgddagvtg vriknnetge kkdiavsglf
      241 iaighkpntd ifkgqlemkd gyltvqsgtq gnatqtsieg vfaagdvsdh iyrqaitsag
      301 tgcmaaldae ryldsle
//
LOCUS       WP_123103038             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acidithiobacillus sulfuriphilus].
ACCESSION   WP_123103038
VERSION     WP_123103038.1
KEYWORDS    RefSeq.
SOURCE      Acidithiobacillus sulfuriphilus
  ORGANISM  Acidithiobacillus sulfuriphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Acidithiobacillia;
            Acidithiobacillales; Acidithiobacillaceae; Acidithiobacillus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Acidithiobacillus sulfuriphilus"
                     /db_xref="taxon:1867749"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34749
     Region          16..321
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnaeegklin skhsrllilg sgpggytaai yaaranlhpv lvqgmepggq lmtttevdnw
       61 pgaadgimgp elmeqlekqa rrfdteilfd hihqaelgqr pfrlsgdqhc ytcdaliitt
      121 gasakylglp seekfrgkgv sacatcdgff yrgqsvavig ggntaveeal ylsnivshvt
      181 lvhrrdrlra ekilqdkllg kenitvlwnh gveevlgdvs gvtglrvrhl pddkiqdlav
      241 tgvfvaighr pntdifkgql nmdaggylit rggrdgmata tsipgvfaag dvqdyiyrqa
      301 vtsagsgcma aldaerwleq qar
//
LOCUS       WP_123120471             358 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Hanamia
            caeni].
ACCESSION   WP_123120471
VERSION     WP_123120471.1
KEYWORDS    RefSeq.
SOURCE      Hanamia caeni
  ORGANISM  Hanamia caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hanamia.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Hanamia caeni"
                     /db_xref="taxon:2294116"
     Protein         1..358
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38768
     Region          1..357
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,91,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigvlkepq hetrvsllpe hiallkklns tvlveknage nafasdekyt eagasvlsre
       61 dvltrseiil sihlpseiei pslqskiilg iyqplydqem vekfitkevk vfsidmlprt
      121 traqsmdvls sqaniagyka vlvaankysr yfpmfmtaag sihpakilil gagvaglqai
      181 atarrlgavv evfdtrpavk eevmslgakf vevegaadas kaggyavdqt eefkerqkqk
      241 iaehvsradi vittaqifgk kapilitkem ieamkngsvi idiaaatggn tevtendkei
      301 nykgvtiign snlsatmpsd asklygknic nfleliidke gklnlnlede lvkgclis
//
LOCUS       WP_123108024             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces botrytidirepellens].
ACCESSION   WP_123108024
VERSION     WP_123108024.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces botrytidirepellens
  ORGANISM  Streptomyces botrytidirepellens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Streptomyces botrytidirepellens"
                     /db_xref="taxon:2486417"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54836
     Region          12..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 maapepevqr rrigipaest pgetrvaatp atvgrlaelg yhvivepgag easrfsdaay
       61 eeagaglgdp wsapvvlkvn gpsgeeigrl rdgatliali gpalhpelve elarrpitvl
      121 amdavprisr aqsldvlssm aniagyravv eaahafgrff tgqvtaagkv pparvlvaga
      181 gvaglaaiga arslgavvra tdprpevaeq vrslggefle vrpeesapse qsaqqvssdg
      241 yakatsddyn rlaarlyaeq aadvdiiitt alvpgrpapk litaedvarm kpgsvivdma
      301 aaqggnvegt vagkavvtgn dvtiigytdl pgrlpaqasq lygtnlvnlm klltpgkdgr
      361 lvldfddvvq rsmtvvrdge ktwppppvqv saaptpatpt pagapepatp pgpaagstrs
      421 arsdyalvga galalflvta fsphqlighf lvfvlsivvg fyvigkvhha lhtplmsvtn
      481 aisgivvvga llqighahta vtvlsfaail lasinifggf avtrrmlgmf skg
//
LOCUS       WP_123120894             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Hanamia caeni].
ACCESSION   WP_123120894
VERSION     WP_123120894.1
KEYWORDS    RefSeq.
SOURCE      Hanamia caeni
  ORGANISM  Hanamia caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hanamia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Hanamia caeni"
                     /db_xref="taxon:2294116"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35629
     Region          5..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mptfdlfskr qkrlrgevpe iftfddisqp lriqivhiik dvigedryst dhhahdifef
       61 fkqtlcreyg vfhlgesyka ssqaqvlnfl lqttetekal dvielsfkyi ddvlrknfhq
      121 ysyhsnskin pdeaiielne rfkehgigys fdggeiirid styihtqitk pviallwndk
      181 fkganeeylk ahehyrhgrn keclaeclka festmkvick eknwlfnstd tskkliqicf
      241 qnglvpiftq nqftslqnll esgiptirnk lgghgqgqtp qkvddemtry alnlagtnii
      301 flveqsglt
//
LOCUS       WP_123116317             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Shewanella algae].
ACCESSION   WP_123116317
VERSION     WP_123116317.1
KEYWORDS    RefSeq.
SOURCE      Shewanella algae
  ORGANISM  Shewanella algae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Shewanella algae"
                     /db_xref="taxon:38313"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33764
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msqakhcnll ilgsgpagyt aavyaaranl kpvmitgiqq ggqlttttev enwpgdaegl
       61 tgpalmermq khaekfdtei ifdhinevdl qqrpftlkgd ngeytcdali iatgasakyl
      121 glpseeafkg rgvsacatcd gffyrnqkva vigggntave ealylsniaa evhlihrrdt
      181 frsekilidr lmdkvengni vlhldktlde vtgdamgvtg lkmkstkdgs isdlevagvf
      241 vaighspntg ifegqlemng gyikvesgln gnatqtsvkg ifaagdvmdq hyrqaitsag
      301 tgcmaaldae rfldaqk
//
LOCUS       WP_123121279             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hanamia caeni].
ACCESSION   WP_123121279
VERSION     WP_123121279.1
KEYWORDS    RefSeq.
SOURCE      Hanamia caeni
  ORGANISM  Hanamia caeni
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Hanamia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Hanamia caeni"
                     /db_xref="taxon:2294116"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35554
     Region          10..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdigtehvqc liigsgpagy taaiyaaran lkpvlyqgiq pggqltitte venypgypng
       61 vqgpdmmidf enqakrmgad iryglatkvd fgscpcrvli ddekwisada iilatgasak
      121 wlgleseirl ngygvsacav cdgfffkgke vcivgggdta aeealylski cskvhmfvrk
      181 dqmraskimq mrvletkniq vywnteveei lgegkteavr iknsltgeis eipvsayfva
      241 ighqpnseif kgwlemdesg yiktvpgstk tnidgifaag dlqdkifrqa itaagsgcma
      301 aieaerylsv lehpvpsdhf qaasnnger
//
LOCUS       WP_123125941             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rufibacter latericius].
ACCESSION   WP_123125941
VERSION     WP_123125941.1
KEYWORDS    RefSeq.
SOURCE      Rufibacter latericius
  ORGANISM  Rufibacter latericius
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Rufibacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rufibacter latericius"
                     /db_xref="taxon:2487040"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33919
     Region          9..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdnqkervkc liigsgpagy taaiyasrag lkpvmyqglq pggqltitnd venypgypag
       61 ingpqmmedf rqqaarfgad irygiatsvd fsgkphkvti deqkeieadt viiatgasak
      121 wlglesearl ngsgvsacav cdgffyrgqe vaivgagdta ceeahylsnl cskvymivrr
      181 eemrasiimq nrvkhtpnie ilwnsvtdei lgehgvegvr lkntvtgetr eiavkgffva
      241 ighepnskif qpylqhdesg ylktipgtsk tnvdgvfacg dvqdnvyrqa vtaagtgcma
      301 aldaerylas ledy
//
LOCUS       WP_123134152             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rufibacter immobilis].
ACCESSION   WP_123134152
VERSION     WP_123134152.1
KEYWORDS    RefSeq.
SOURCE      Rufibacter immobilis
  ORGANISM  Rufibacter immobilis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Rufibacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rufibacter immobilis"
                     /db_xref="taxon:1348778"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34018
     Region          9..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 menqkervkc liigsgpagy taaiyasrag lkpvmyqglq pggqltitnd venypgyptg
       61 vngpqmmedf rqqaerfgtd irygiatsvd fsgkphkvti deqkeieadt viiatgasak
      121 wlglesearl ngsgvsacav cdgffyrgqe vaivgagdta ceeahylsnl cskvymivrr
      181 demkaslimq qrvqntpnie ilwnsvteei lgefgvegar ikdtrsgetr diavkgffva
      241 ighepnskif qpylehdang ylktipgtsk tnvdgvfacg dvqdnvyrqa itaagtgcma
      301 aldaerylas leyh
//
LOCUS       WP_123140715             364 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Marichromatium].
ACCESSION   WP_123140715
VERSION     WP_123140715.1
KEYWORDS    RefSeq.
SOURCE      Marichromatium
  ORGANISM  Marichromatium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Marichromatium"
                     /db_xref="taxon:85076"
     Protein         1..364
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38611
     Region          1..360
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipmerr pgearvastp evvrklvakg levwveegag aragypdady aeagaslgar
       61 etvydadlvl kvrrpepdev almrrgaryl gflescgedd llaamqarel lvfplermpr
      121 tsraqsmdal ssqssiagyr atleaasryg rffpmmmtsa gsakparlvv lgagvaglqa
      181 iatarrlgad vhaydvrpet heqirslgar pieldlgesg ageggyarel sdeakarqqa
      241 aladelaraq viittaqipc rqapmlipet vvermrpgsv ivdlaaasgg ncpltvadev
      301 verhgvtlvg ltnypallaa dasafyarnl anllelmiet gasgpqlrdp addeitaamv
      361 arad
//
LOCUS       WP_123141301             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Marichromatium sp. AB31].
ACCESSION   WP_123141301
VERSION     WP_123141301.1
KEYWORDS    RefSeq.
SOURCE      Marichromatium sp. AB31
  ORGANISM  Marichromatium sp. AB31
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Marichromatium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Marichromatium sp. AB31"
                     /db_xref="taxon:2483362"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34527
     Region          1..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtkhcrll ilgsgpagyt aavyaaranl dpvlvtgleq ggqlmtttev dnwagdpdgv
       61 qgpelmermr rhaerfetei ifdhihsadl gnrpftlegd satytcdali iatgasamyl
      121 glpseqtfrg rgvsacatcd gffyrnqeva vigggntave ealylsniaa kvtlihrrds
      181 lraekilqrq lfekaehgni eilwdhtlde vlgdasgvtg irvkstkdar trelaltgvf
      241 vaighkpnte lftgqlemdn gyirvasglq gnataasvpg vfaagdvmdq iyrqaitsag
      301 tgcmaaldae kyldalaleq aqs
//
LOCUS       WP_123142734             323 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Marichromatium].
ACCESSION   WP_123142734
VERSION     WP_123142734.1
KEYWORDS    RefSeq.
SOURCE      Marichromatium
  ORGANISM  Marichromatium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Marichromatium"
                     /db_xref="taxon:85076"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34513
     Region          1..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtkhcrll ilgsgpagyt aavyaaranl dpvlvtgleq ggqlmtttev dnwagdpdgv
       61 qgpelmermr rhaerfetei ifdhihsadl gnrpftlegd satytcdali iatgasamyl
      121 glpseqsfrg rgvsacatcd gffyrnqeva vigggntave ealylsniaa kvtlihrrds
      181 lraekilqrq lfekaehgni eilwdhtlde vlgdasgvtg irvkstkdar trelaltgvf
      241 vaighkpnte lftgqlemdn gyirvasglq gnataasvpg vfaagdvmdq iyrqaitsag
      301 tgcmaaldae kyldalaleq aqs
//
LOCUS       WP_123144151             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus debuckii].
ACCESSION   WP_123144151
VERSION     WP_123144151.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus debuckii
  ORGANISM  Staphylococcus debuckii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Staphylococcus debuckii"
                     /db_xref="taxon:2044912"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34088
     Region          9..306
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 manqqpdydv viigagpagm taavyasrad lktlmiergv pggqmanted venfpgfesi
       61 sgpdlstkmf dhaqkfgavy qygdikried kgdikeifyg dksvtayavi ittgaeykki
      121 gvpgeeelgg rgvsycavcd gaffkgkklf vigggdsave egafltkfad svtvvhrrdk
      181 lraqkilqdr afknekmdfi wnhtlasine engkvgsvtl qstvdgkeet lsadgvfvyi
      241 gmkpltapfk dlgitndagy ivtndemetk lpgiyaagdv rekglrqivt atgdgsiaaq
      301 nsqayieevk dkletea
//
LOCUS       WP_123146346             418 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium delmotii].
ACCESSION   WP_123146346
VERSION     WP_123146346.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium delmotii
  ORGANISM  Mesorhizobium delmotii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Mesorhizobium delmotii"
                     /db_xref="taxon:1631247"
     Protein         1..418
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42953
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre vdvseprvaa spdtvkrlag lgfdvivesg agtasripde efakagavig
       61 kagdvakadv vlkvrrpdea elkayrpgta viaimdpygn daavdalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvttang vkivghlnvp grvaasasll yarnlfafle tlvdktaktl ainrdddlvk
      361 atmltdggqv vhpafagkpa vmiasaepak paaakkpaap kkaaalkrpa aakpkria
//
LOCUS       WP_123148546             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Mesorhizobium].
ACCESSION   WP_123148546
VERSION     WP_123148546.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34481
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mitkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlvittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdvi ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilser lfkkdnirvi wdtvvdeitg qsgktplpps veglklrnvv tgqemhltvd
      241 gvfvaighap avelfagklk qkpngylwta pdstctdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_123157965             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Ruthenibacterium lactatiformans].
ACCESSION   WP_123157965
VERSION     WP_123157965.1
KEYWORDS    RefSeq.
SOURCE      Ruthenibacterium lactatiformans
  ORGANISM  Ruthenibacterium lactatiformans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Oscillospiraceae; Ruthenibacterium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Ruthenibacterium lactatiformans"
                     /db_xref="taxon:1550024"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32142
     Region          5..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqiydvavl gggpggytaa lycaraglst vvleklspgg qmattsnven ypgfaegvdg
       61 fdlamqmkdg aerfgvetlf adatavaleg gvktittssg errartvila tgadprplgv
      121 phedelrgrg vaycatcdgm lyrgktvvvv gggnsaaeda lflsrvckkv ylvhrgavlt
      181 asksywtalq kaenvefiwn srvvellygs vvtgvvlegv esgnrselac dgvfiavgri
      241 pntglfhgvl emdaagylia dettrtalpg vfavgdvrtk plrqiitaaa dgavaskyae
      301 aylaeqeg
//
LOCUS       WP_123159651             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sp. AM43-2AT].
ACCESSION   WP_123159651
VERSION     WP_123159651.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. AM43-2AT
  ORGANISM  Streptococcus sp. AM43-2AT
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sp. AM43-2AT"
                     /db_xref="taxon:2293247"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32618
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigag pagmtaalya arsnlkvall eagipggqmn ntsdienypg yanisgpela
       61 ekmfeplevl gvehlfgrae nivdqgsyke ittddgllqa ktviiatgsn hrllgvpgee
      121 elnsrgvsyc avcdgaffrd edlmvvgggd saveeaiflt qfaksvtivh rrdalraqkv
      181 lqdrafanek ihlawntvve eikgdnrvts lvlkdvqtgq vreqaaggaf iyvgldpvsd
      241 fakdlgildd qgwvitddhm ktsvpgvfav gdvrqkdlrq vttavgdgav agqeaykyit
      301 ehee
//
LOCUS       WP_123160917             304 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptococcus].
ACCESSION   WP_123160917
VERSION     WP_123160917.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32668
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigag pagmtaalya arsnlkvall eagipggqmn ntsdienypg yanisgpela
       61 ekmfepleal gvehlfgrae nivdqgcyke ittddgllqa ktviiatgsn hrllgvpgee
      121 elnsrgvsyc avcdgaffrd edlmvvgggd saveeaiflt qfaksvtivh rrdalraqkv
      181 lqdrafanek ihfawntvve eikgdnrvts lvlkdvktgq vreqaaggvf iyvgldpvsd
      241 fakdlgildd qgwvitddhm ktsvpgvfav gdvrqkdlrq vttavgdgav agqeaykyit
      301 ehee
//
LOCUS       WP_123161787             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_123161787
VERSION     WP_123161787.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53859
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvti
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vglfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_123162234             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            cholerae].
ACCESSION   WP_123162234
VERSION     WP_123162234.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53891
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreql agetrvaasp ssveqliklg fevcieskag alasfddaay taagatigsr
       61 eeiwacplil kvnapsddei allkegatlv sfiwpaqnpa lmeklsskni nvlamdavpr
      121 israqaldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvfv agagvaglaa
      181 igaagslgai vrafdvrpev keqvqsmgae flevnfqeta gsgdgyakem sdefnrkaae
      241 lyaaqakdvd iiittalipg kpapklitke mvdsmkagsv ivdlaaangg nceytvkdqv
      301 ittdngvkvi gytdmvgrlp tqssqlyatn lvnllkllck ekdgnidinf edvvlrgvtv
      361 vkageitwpa ppiqvsaqpq qkakvqptka qkkepeptsp vkklvglavg vclfawvasv
      421 apaaflghft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqigqgsgiv
      481 tflafiavli asinifggft vtkrmlemfr kn
//
LOCUS       WP_123168722             429 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Mesorhizobium].
ACCESSION   WP_123168722
VERSION     WP_123168722.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     Protein         1..429
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44156
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivetg agtrsripde efakagavig
       61 kaadvgkadv vlkvrrptea elksyksgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaaki fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegaq
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafle tlvdkttktl aikrddelvk
      361 atmltdggkv vhpafakadq qphvepaaip attmvadasa apkkpaprkt aaskssspks
      421 sspkskgta
//
LOCUS       WP_123165437             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Planococcus salinus].
ACCESSION   WP_123165437
VERSION     WP_123165437.1
KEYWORDS    RefSeq.
SOURCE      Planococcus salinus
  ORGANISM  Planococcus salinus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Planococcus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Planococcus salinus"
                     /db_xref="taxon:1848460"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34423
     Region          9..306
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mtenttiydv iiigagpagm taavytsran lstlmlergi pggqmantee ienypgfdhi
       61 lgpdlstkmf dhakkfgaey aygdvkeiid geeyktikag skeykaraii ittgaeykkm
      121 gipgeselgg rgvsycavcd gaffkqkelv vvgggdsave egvyltrfad kvtivhrrde
      181 lraqkilqdr afandkidfi wshtvkeihe engkvgsvtl vsakdgeere fkadgvfiyi
      241 gmlpltkpfa dlgilndegy ivtnekmeta vpgiyaagdv rekklrqvvt atgdgslaad
      301 taqhyieela eklsika
//
LOCUS       WP_123175026             171 aa            linear   BCT 07-JUL-2024
DEFINITION  aromatic/alkene monooxygenase hydroxylase subunit gamma
            [Methylocystis hirsuta].
ACCESSION   WP_123175026
VERSION     WP_123175026.1
KEYWORDS    RefSeq.
SOURCE      Methylocystis hirsuta
  ORGANISM  Methylocystis hirsuta
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae; Methylocystis.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Rosenzweig,A.C., Frederick,C.A., Lippard,S.J. and Nordlund,P.
  TITLE     Crystal structure of a bacterial non-haem iron hydroxylase that
            catalyses the biological oxidation of methane
  JOURNAL   Nature 366 (6455), 537-543 (1993)
   PUBMED   8255292
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Cardy,D.L., Laidler,V., Salmond,G.P. and Murrell,J.C.
  TITLE     Molecular analysis of the methane monooxygenase (MMO) gene cluster
            of Methylosinus trichosporium OB3b
  JOURNAL   Mol Microbiol 5 (2), 335-342 (1991)
   PUBMED   1904125
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Fox,B.G., Liu,Y., Dege,J.E. and Lipscomb,J.D.
  TITLE     Complex formation between the protein components of methane
            monooxygenase from Methylosinus trichosporium OB3b. Identification
            of sites of component interaction
  JOURNAL   J Biol Chem 266 (1), 540-550 (1991)
   PUBMED   1845980
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Stainthorpe,A.C., Murrell,J.C., Salmond,G.P., Dalton,H. and Lees,V.
  TITLE     Molecular analysis of methane monooxygenase from Methylococcus
            capsulatus (Bath)
  JOURNAL   Arch Microbiol 152 (2), 154-159 (1989)
   PUBMED   2505721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF045805.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Methylocystis hirsuta"
                     /db_xref="taxon:369798"
     gene            1..171
                     /gene="mmoZ"
     Protein         1..171
                     /product="aromatic/alkene monooxygenase hydroxylase
                     subunit gamma"
                     /EC_number="1.14.13.25"
                     /GO_function="GO:0015049 - methane monooxygenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=19300
     Region          7..167
                     /region_name="MeMO_Hyd_G"
                     /note="Methane monooxygenase, hydrolase gamma chain;
                     pfam02964"
                     /db_xref="CDD:427082"
ORIGIN      
        1 mgkkepihdn atratwedki skltsvdaat kfiqdfrlay sspwrksyal dtdyqyierk
       61 ieeklsqlkv ghlpvsalmt ktsagedaaa veatwigkmk aaknkydaer ihvefrqlyk
      121 ppvmpvnvfl rtdaalgall memrntdyya tplaglrker gvkvlylqka s
//
LOCUS       WP_123175477             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Methylocystis hirsuta].
ACCESSION   WP_123175477
VERSION     WP_123175477.1
KEYWORDS    RefSeq.
SOURCE      Methylocystis hirsuta
  ORGANISM  Methylocystis hirsuta
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae; Methylocystis.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Methylocystis hirsuta"
                     /db_xref="taxon:369798"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34175
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpqharviii gsgpagytaa iyaarallep mliagfdqgg qlmitteven ypgfaepiqg
       61 pwlmeqmrlq aehvgtklvs dhiveahlde rpfrltgdsg ksytcdsliv atgakakwlg
      121 lpseekfkgf gvsacatcdg fffrgkrvlv vgggnsavee alylsnlash vtiihrrdef
      181 rservlikrl laqenvsilf nhvideivgd enplsvtgar vknvttgaih tleadgvfva
      241 ighspaself rgqltikpsg yiavepgstr tsmpgvyaag dvadevyrqa vtaaglgcma
      301 alevekflld apkpaikeia
//
LOCUS       WP_123176928             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylocystis hirsuta].
ACCESSION   WP_123176928
VERSION     WP_123176928.1
KEYWORDS    RefSeq.
SOURCE      Methylocystis hirsuta
  ORGANISM  Methylocystis hirsuta
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae; Methylocystis.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Methylocystis hirsuta"
                     /db_xref="taxon:369798"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38877
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlaetd kseprvaatp etvkkfiglg advvvearag aaagfadsdy aaagatiadn
       61 aaaaltgadv alrvrrpsaa elpgarsnla viaimdpfga gaqladlaks gaiafamelm
      121 pritraqtmd vlssqanlag yravidamae ygrsfpmmmt aagtvpaarv fimgvgvagl
      181 qaiatarrmg aivtatdvrp atkeqveslg akflavenee fqqaqtaggy akemspeyqk
      241 aqaelvashi akqdivitta lipgrpapkl isaemvrsmr pgsvivdlaa erggnceltq
      301 pgetvvvdgv kilgalnlag rmastassly aknllafvet lvskdtkqla inwedelvka
      361 taltrdgavv derfk
//
LOCUS       WP_123181275             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Zhongshania marina].
ACCESSION   WP_123181275
VERSION     WP_123181275.1
KEYWORDS    RefSeq.
SOURCE      Zhongshania marina
  ORGANISM  Zhongshania marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Zhongshania.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Zhongshania marina"
                     /db_xref="taxon:2304603"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33689
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdsqhhrli ilgsgpagyt aavyaaranl kpvvitgiqq ggqlttttdv dnwpgdqngv
       61 qgpelmvrmq ehaerfdtdi ifdhiesvdl knkpftlkgs ktytcdglii atgasaqylg
      121 lpseeafmgk gvsacatcdg ffyrgkkvav igggntavee alylsniase vtlvhrrdsl
      181 rsekilqdkl leraangnvn ilwnntldev lgddsgvtgl rlksttdgst qeidvagvfi
      241 aighkpntdi fegqlemkdg ylkihsgteg natrtsvegv faagdvadhi yrqavtsagf
      301 gcmaaldaer ylddla
//
LOCUS       WP_123184167             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_123184167
VERSION     WP_123184167.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53614
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vtpaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_123188526             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. I6].
ACCESSION   WP_123188526
VERSION     WP_123188526.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. I6
  ORGANISM  Streptomyces sp. I6
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces sp. I6"
                     /db_xref="taxon:2483113"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33756
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslnp lvfegavtag galmnttdve nfpgfrdgim
       61 gpdlmdsmra qaerfgaelv pddviavnlt deiktvtdta gtvhsakavi vatgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfar svtvvhrrds
      181 lraskamqer afadpkitfs wdsevaeihg dqkltgltlr ntktcessel pvtglfiavg
      241 hdprtelfkg qleldeegyl kvdapstrts ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala deektaaasv
//
LOCUS       WP_123194952             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pannonibacter phragmitetus].
ACCESSION   WP_123194952
VERSION     WP_123194952.1
KEYWORDS    RefSeq.
SOURCE      Pannonibacter phragmitetus
  ORGANISM  Pannonibacter phragmitetus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Stappiaceae; Pannonibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pannonibacter phragmitetus"
                     /db_xref="taxon:121719"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55253
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspreii dgearvamtp dsaaqlqklg yscviesgag kaagfsdeay rkagvdvaas
       61 aadlfaaadi iakvrpplds evallgegkt lisffypaqn kellekakat ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv liigagvagl
      181 aaigtatslg avtyafdvrp evaeqiesmg aefvyldfad qvqdgaatgg yaapsspefr
      241 ekqlekfrel apdmdivitt alipgrdapk lwladmvaam kpgsviidla aerggncdlt
      301 vadqrvvsdn gvivigytdf psrmaaqsst lyatnirhmm tdltpakdgq vvhnmeddvi
      361 rgatvtfkgd itfpppppkv qaiaaqkpke kareltpeek raqevaafka qtrnqvalla
      421 gsgalillag lfapasfmsh fivfvlscfv gfqviwnvsh slhtplmait naissiiilg
      481 almqvgsgsf lvillgalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_123192261             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paraeggerthella hongkongensis].
ACCESSION   WP_123192261
VERSION     WP_123192261.1
KEYWORDS    RefSeq.
SOURCE      Paraeggerthella hongkongensis
  ORGANISM  Paraeggerthella hongkongensis
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Paraeggerthella.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Paraeggerthella hongkongensis"
                     /db_xref="taxon:230658"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34696
     Region          23..322
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mneerplnet sqeckgshle amdvavigag pagltaglya aragldvvvf erispggqla
       61 qtehmenypg fpegadgfel afsmkqqadr fgvrhvgeev vsvdfaqepk vlttafgeyr
      121 aksvivatga rprklglele delqgrgvsy catcdgnffr dkevmvvggg ntavgdaiyl
      181 srickkvylv hrrdklrata iyhkrledle nlefvwsaap rklmadegal agvrvemlkt
      241 geirdipvsg lfvavgtepn teflkgalql detgyvvade sgatdvpgvy vagdvrtkfl
      301 rqvvtavadg avcaeeasey lai
//
LOCUS       WP_123196544             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria meningitidis].
ACCESSION   WP_123196544
VERSION     WP_123196544.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33438
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msqhrkliil gsgpagytaa vyaaranlnp viitgiaqgg qlmtttevdn gpadadgvqg
       61 pelmarflah aerfgteiif dqinavdlqk rpftlkgdmg eytcdaliva tgasakylgl
      121 pseeafagkg vsacatcdgf fyknqdvavv gggntaveea lylaniaktv tlihrrsefr
      181 aekimidklm krveegkiil klesnlqevl gddrgvngal lknndgseqq iavsgifiai
      241 ghkpntdifk gqlemdeagy lktkggtadn vgatniegvw aagdvkdhty rqaitsaasg
      301 cqaaldaerw lgsqni
//
LOCUS       WP_123197415             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Slackia faecicanis].
ACCESSION   WP_123197415
VERSION     WP_123197415.1
KEYWORDS    RefSeq.
SOURCE      Slackia faecicanis
  ORGANISM  Slackia faecicanis
            Bacteria; Bacillati; Actinomycetota; Coriobacteriia;
            Eggerthellales; Eggerthellaceae; Slackia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Slackia faecicanis"
                     /db_xref="taxon:255723"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32308
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstqekhfdv avigqgpagm taslytarsg lstasfermg pggqmtdteq ldnypgfadg
       61 vsafelafam sgqaarfgaq tvgeevvelq ldaspkkivt asgaaytada vilamgaepr
      121 plgveregel agrgvsycat cdggffrdka vavvgggnta vgdvlylari csevhlihrr
      181 dalradavyt eplrelsnlt mhldsvvdal hdeegklsgl tlrnvktdea seidvagmfv
      241 avgtapknal lagagleldr ggyvvsdetg ktnipgvfva gdlrtkplrq vstavgdgan
      301 aaqsafefls ls
//
LOCUS       WP_123199095             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_123199095
VERSION     WP_123199095.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53454
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lgkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_123203977             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pedobacter jejuensis].
ACCESSION   WP_123203977
VERSION     WP_123203977.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter jejuensis
  ORGANISM  Pedobacter jejuensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pedobacter jejuensis"
                     /db_xref="taxon:1268550"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34126
     Region          10..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqenehvqc liigsgpagy taaiyaarad lkpimytgmq aggqltqttd venfpgypqg
       61 imgpemmedf rkqaerfgtd irfgyissvd fsstphkvvv deiktitadt viiatgatak
      121 wlglpseqqy ngfgvsacav cdgfffkgqd vaivgagdta aeeatylakl cktvhllvrr
      181 defrasktmv arvlatpnii vhyntetqei lgngknvtav kvlnnktgee tdiavegffv
      241 aighkpntdi fkgqldmdet gylltkpgst ltnaegvfac gdvqdmyyrq avtaagsgcm
      301 aaldaeryla akehpvev
//
LOCUS       WP_123202391             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Halostreptopolyspora alba].
ACCESSION   WP_123202391
VERSION     WP_123202391.1
KEYWORDS    RefSeq.
SOURCE      Halostreptopolyspora alba
  ORGANISM  Halostreptopolyspora alba
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Nocardiopsidaceae; Halostreptopolyspora.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Halostreptopolyspora alba"
                     /db_xref="taxon:2487137"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33491
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa iysaraelrp lvfegaitag galmnttdve nfpgfpdgim
       61 gpdlmdhfrk qserfgaelv pddvtevdlt adpkivkvgd dtyrartvii atgsgyrklg
      121 vpgeeefsgr gtswcatcdg fffrdkdiav vgggdtamee atfltrfars vtvihrrdel
      181 raskimqera fdnekikfiw ntevtevlgd skvtgiqlrn tqsgeeskld isglfiaigh
      241 dprvelfedq ldldedgylv vdapttktkl pgvfacgdvv dhvyrqavta agtgcsasld
      301 aerylaelga
//
LOCUS       WP_123204051             313 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pedobacter jejuensis].
ACCESSION   WP_123204051
VERSION     WP_123204051.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter jejuensis
  ORGANISM  Pedobacter jejuensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pedobacter jejuensis"
                     /db_xref="taxon:1268550"
     Protein         1..313
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35544
     Region          4..178
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mtydlfskrq krergevpev lsfdilptal rvqikmiidd afgvrksgsg esnrpqlays
       61 mihkilcrey gvfeigvngs gyaqseleqv kshllyspnv dqvldiiels fryisrvink
      121 dlneyeitvn ismtpeeamn elnlrfrehg vgyqfesdki irvdstymhs evtkptlsll
      181 wderftgane eylkahehyr hgrnkecltd clkafesaik ticnengwty nptdtaskli
      241 sicftnnlip sftqnqfssl qnllttgipt irnkvgghgq gqvpqkvdde ltryglnltg
      301 aniiflieqs glk
//
LOCUS       WP_123211929             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Stagnimonas aquatica].
ACCESSION   WP_123211929
VERSION     WP_123211929.1
KEYWORDS    RefSeq.
SOURCE      Stagnimonas aquatica
  ORGANISM  Stagnimonas aquatica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Nevskiales; Nevskiaceae; Stagnimonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Stagnimonas aquatica"
                     /db_xref="taxon:2689987"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33735
     Region          9..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mstpvhhpli ilgsgpagyt aavyaaranl kpvmitglev ggqlmtttev dnwpgdvhgl
       61 mgpdlmarlq qhaerfetqf vydhihtvdl knkpytlvgd qgsyscdali iatgasakyl
      121 glpseqefrg kgvsacatcd gffykgqeva vigggntave ealylanias kvtivhrrdk
      181 fkgekilhdk lfkkavegkv eiiwnstlde vlgdasgvtg mrvknlqtge lreiglkgvf
      241 vaighspnta ifegqlameg gylkvksgsa gdatatsvpg vfaagdvqdh vyrqaitsag
      301 tgcqaaldae ryldqlggh
//
LOCUS       WP_123214497             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinomicrobium pectinilyticum].
ACCESSION   WP_123214497
VERSION     WP_123214497.1
KEYWORDS    RefSeq.
SOURCE      Sinomicrobium pectinilyticum
  ORGANISM  Sinomicrobium pectinilyticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Sinomicrobium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sinomicrobium pectinilyticum"
                     /db_xref="taxon:1084421"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34218
     Region          8..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtneritcli igsgpagyta aiyaaranmn pvlyqgtqpg gqltttndve nfpgfpggit
       61 gpelmvqlqq qaerfgtdir ngwvtrvdft gplhkvwiee etelhcdtvi iatgasakyl
      121 glpseqkyle sgggvsacav cdgffyrnqe vvivgagdsa ceeahylskl ckkvtmlvrr
      181 nefrasiime arvrntknie ilfnteteev lgdgqlvtgv rvknndtget reipatgffv
      241 aighkpntdi fkghirlnet gyiintpgta qtgvegvfvc gdaadhvyrq aitaagtgcm
      301 aaleaeryls svevhamg
//
LOCUS       WP_123220486             303 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Salmonella enterica].
ACCESSION   WP_123220486
VERSION     WP_123220486.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35928
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqiill iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lndifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlmlndf acvvkechav frsvllrihe rkgivyheqd slntlmtnlm argvisaeya
      241 hkfhflsnvl eseiflpiap ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vap
//
LOCUS       WP_123224191             437 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides pocheonensis].
ACCESSION   WP_123224191
VERSION     WP_123224191.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides pocheonensis
  ORGANISM  Nocardioides pocheonensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Nocardioides pocheonensis"
                     /db_xref="taxon:661485"
     Protein         1..437
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45003
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,275..276,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,225,236,
                     253..255,262,264)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavvretr egearvamvp elvgkltglg ydvlvepgag aqaefadeey teagasisds
       61 alseadlvva vqpldtskvg rlregaavis flpvnseqdl vvrlrdagvt sfamelvpri
      121 sraqsmdals sqalvagyrc aivaagllrr ffplnmtaag tvqpaqvvvl gagvaglqai
      181 atakrlgavv qaydvraaaa eeirsmgaka idlkletleg aggyaremte eraqrqmeal
      241 apyiaqadal ittaavpgrr apllvtsamv eamkpgsvvv dlaaetggnv egsvagkvvk
      301 ighaqvwgga nvasqmpgpa srlyaqnvvn lltlmtaage kqedgsvspg sfapdfddei
      361 vagsavthag rivheptrea iegpapepae qpxaaevepa aevepaetpa atatqvlepv
      421 dpaepqldlp ydqeadq
//
LOCUS       WP_123214967             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinomicrobium pectinilyticum].
ACCESSION   WP_123214967
VERSION     WP_123214967.1
KEYWORDS    RefSeq.
SOURCE      Sinomicrobium pectinilyticum
  ORGANISM  Sinomicrobium pectinilyticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Sinomicrobium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Sinomicrobium pectinilyticum"
                     /db_xref="taxon:1084421"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34219
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtverikc liigsgpagy taaiyaarad lkpvlytgle pggqltttte vdnfpgypdg
       61 vdgptmmlql qkqaerfgte vrigmatsve fsserggihk vtidnskkle aesviiatga
      121 sakylglpse qrlrgggvsa cavcdgffyk gqdvaivggg dtaaeeatyl anicskvtml
      181 vrkgemrask amqhrvantp nlevryftei devlgdqvve girmvnnqtg ekedikvtgl
      241 fiaighkpnt difkgqlemd etgyvltygk stktskpgvf asgdvqdkey rqaitaagtg
      301 cmaaldaery latvkspeev v
//
LOCUS       WP_123225033             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides pocheonensis].
ACCESSION   WP_123225033
VERSION     WP_123225033.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides pocheonensis
  ORGANISM  Nocardioides pocheonensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Nocardioides pocheonensis"
                     /db_xref="taxon:661485"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53469
     Region          1..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvlnear pgekrvaatp atvsqllklg ydvevepgag agssfsdday saagatlgdl
       61 raadvvlgvn aptstqldgl rpgatviail spaldaalvd elaerpltal amdavprisr
      121 aqsldvlssm aniagyravi eaanvfgrff tgqvtaagkv pparvlvvga gvaglaaiga
      181 agslgaivra tdprpevgdq vkslggeyls iespdvevst tgyakemged ykkreaelya
      241 eqcrdvdiii ttalipgrpa priisaemva smkpgsvivd maaqnggnve gtvtdevivt
      301 rngvtiigyt dlagrlpaqa sqlygtnlvn llklmtpqqd gelvldfddv vqrcvtvvrh
      361 vggrseltwp pppvqvsaah aaaaegstga aadesppsaa yapispgrrl avvfagaall
      421 fglvaispap lqvhltvfal aivigfyvig qvhhalhtpl msvtnaisgv vvvaallqfg
      481 yadqhggggv avlsfvaill asinifggfa vtrrmlamfs rs
//
LOCUS       WP_123229454             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides marmoriginsengisoli].
ACCESSION   WP_123229454
VERSION     WP_123229454.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides marmoriginsengisoli
  ORGANISM  Nocardioides marmoriginsengisoli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Nocardioides marmoriginsengisoli"
                     /db_xref="taxon:661483"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52048
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresk agetlvaats ttagqlqklg ydvvveagag vhssqpdsaf tdaevtvgta
       61 edvwssdivi kvnaptteei srlrsgaviv simapgrspe lvdalaaqgv talamdavpr
      121 israqsmdvl ssmanvagyr aviegahafg rqftgqvtaa gkvpparvfv vgagvaglaa
      181 vgaagsmgai vrsfdvrpev aeqvesmgae fvtvdmesev stdgyakemt eaqvaatavm
      241 ydeesraadi vittalipgr papklitaes iagmrtgsvi vdmaaanggn teltvtddvv
      301 vtengvtiig ytdlagrlaa qtsqlygtni vnllklmtpe kdgvmtldle dvivrgitva
      361 dqgasmwppp pvqvsaapaa paaaaaepea pkaqlsagak vglvlgaiaa fwlvnatapd
      421 pipkhfttlm lsivigyyvi gkvahalhtp lmsvtnaisg vvvvgallqi ssddaavral
      481 stiaillasi nifggfavtr rmlgmfskga
//
LOCUS       WP_123231737             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_123231737
VERSION     WP_123231737.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53555
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 asllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_123231842             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_123231842
VERSION     WP_123231842.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53718
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglag
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_123231902             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_123231902
VERSION     WP_123231902.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53945
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwvcpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeipfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_123235371             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides marmorisolisilvae].
ACCESSION   WP_123235371
VERSION     WP_123235371.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides marmorisolisilvae
  ORGANISM  Nocardioides marmorisolisilvae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Nocardioides marmorisolisilvae"
                     /db_xref="taxon:1542737"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52747
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipresk sgetlvaata atagqlqklg ydvvvesgag eaadqpdsaf tdaevtvgta
       61 edvwssdivv kvnaptdeel arvrpgttli slmapmrspe lvealvasgv talamdavpr
      121 israqsmdvl ssmanvagyr aviegahafg rqftgqvtaa gkvppakvfv vgagvaglaa
      181 lgaagsmgav vrafdvrpev aeqvesmgaq fvtvdmesev ssdgyakemt aeqeaatavm
      241 ydeearnadi vittalipgr papklitaet iagmrtgsvi idmaaanggn teltrtdqvi
      301 ttqngvtiig ytdlagrlpa qtsqlygtni vnllklmtpe kdgqlvldld dvivrgitva
      361 tggesmwppp avqvsaapkv eaaaavepke pkpqltarak talvlgaial fglinaaapt
      421 delrthftvl mlsivigyyv igkvahalht plmsvtnais gvvvvgallq vnsdetkiqv
      481 latiaillas inifggfavt rrmlgmfnkg a
//
LOCUS       WP_123238592             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_123238592
VERSION     WP_123238592.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53555
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtqrmlnmf kkg
//
LOCUS       WP_123235947             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomethylobacillus aquaticus].
ACCESSION   WP_123235947
VERSION     WP_123235947.1
KEYWORDS    RefSeq.
SOURCE      Pseudomethylobacillus aquaticus
  ORGANISM  Pseudomethylobacillus aquaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Methylophilaceae; Pseudomethylobacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomethylobacillus aquaticus"
                     /db_xref="taxon:2676064"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33675
     Region          2..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msakharlli lgsgpagysa avyaaranlk pvlitgiaqg gqlmtttevd nwpadaegvm
       61 gpelmarfqr haerfntemi fdhihtthln ekpirlvgds geytcdalii atgasakylg
      121 lpseelfagk gvsacatcdg ffyrnqevav igggntavee alylsniask vtlvhrrdkf
      181 kaeailidkv mervnegkiv lelystldev lgddtgvtgm rvknvqsges rdialkgvfi
      241 aighkpntdi fegqldmegg yivtqagreg nftatsvpgv faagdvqdhi yrqavtsagt
      301 gcmaaldaer ylaqls
//
LOCUS       WP_123246048             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas dhakensis].
ACCESSION   WP_123246048
VERSION     WP_123246048.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53396
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tclgtsgwaq aadeaqpkgk vearselfak dhadqfsswk
       61 atgesrertd alaedpnmvv lwagyafakd ynkprghfya ltdvretlrt gapksaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy ftgptkavkf pwdkgttveq
      241 meqyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg vvkqrkdaih dlklrvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtsld kaadartkla
      421 rllaakglsq eiaipdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_123255407             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arthrobacter oryzae].
ACCESSION   WP_123255407
VERSION     WP_123255407.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter oryzae
  ORGANISM  Arthrobacter oryzae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Arthrobacter oryzae"
                     /db_xref="taxon:409290"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39231
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,287,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvgvgreqc dgerrvaatp etvhelaalg leifvergag aqagypdeaf keagaaitae
       61 lvlesvdvll hvrpftpdaa aslrpgtiti gfaspgselp tvralaeagv tsfamelipr
      121 israqsmdal ssqslvsgyr avleaavryp rffplymtaa gtipparvlv lgagvaglqa
      181 igtakrlgar vsandvraas adevasmggt finldldaaa egpggyarel gedraqrqrg
      241 llaphvaatd vlittaaipg raapllvttd mvagmragsv vvdlaaesgg nvegiiagqd
      301 vqlpvvggfv tlvgmkdaas ampsdasrly arnvsnllal mtadgratpd fddevisgac
      361 ltcdgtvrhp ataaalaaev megea
//
LOCUS       WP_123270801             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Flexivirga
            caeni].
ACCESSION   WP_123270801
VERSION     WP_123270801.1
KEYWORDS    RefSeq.
SOURCE      Flexivirga caeni
  ORGANISM  Flexivirga caeni
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermacoccaceae; Flexivirga.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Flexivirga caeni"
                     /db_xref="taxon:2294115"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52146
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrvgvvkesq vgetrvaatp gtvgqlrslg yevvvepgag eragfadeay aeagtalgdp
       61 leaevvlgvn alapaqldrl qpgatiigil gprtnpdlvm dlarrpital aldaaprisr
      121 aqsldvlssm aniagyravv eaahvfgrff tgqvtaagkv ppatvlvcga gvaglaaigt
      181 agslgavvra tdprpevadq vkslggeyls iedpevevsa tgyakemgqd yqareaqlya
      241 qqaadvdiii ttalipgrpa prlitadmva smrpgsvivd maaasggnve gsmpgevvrt
      301 pggvtiigyt dlagrlpaqa sqlygtnlvn llklltpgkd gqlvldeddv vqrsilvcre
      361 gesrwppppv qvsaapaqta aapaverqvk apltagrrlt mvlvaaavvf vllaispaal
      421 tvhltvfala ivigyyvirs vhhalhtplm svtnaisgii vvgallqigq hntaitilsa
      481 vailvasinv fggfavtrrm lgmfsrs
//
LOCUS       WP_123287718             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brevundimonas halotolerans].
ACCESSION   WP_123287718
VERSION     WP_123287718.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas halotolerans
  ORGANISM  Brevundimonas halotolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Brevundimonas halotolerans"
                     /db_xref="taxon:69670"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38502
     Region          3..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavtiavtre rrdgetrtal tpdmvrkltg mgvtvvvetg tglgssipdt ayaeagatva
       61 rdlktaltga dilmkvrgpt aseisalrpg tvvvalldaw rdkdtvqals gagvtsfame
      121 fvprisraqv mdalssqanl agyravieaa aaygrgfpmm mtaagtvaaa kvfimgagva
      181 glqaiatarr lgavvtatdv rpaakeqves lgakfvaved eefkaaetag gyakamsdey
      241 qakqaaltas hivkqdvvit talipgrpap rlvtaahvss mkpgsvivdl avdnggnveg
      301 ikagelatta ngvtlvgwtn mpgriasdas slyarnlvaf valmlkdgil avdlddeilk
      361 aaavthggai vhegvkg
//
LOCUS       WP_123328109             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas morbosilactucae].
ACCESSION   WP_123328109
VERSION     WP_123328109.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas morbosilactucae
  ORGANISM  Pseudomonas morbosilactucae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas morbosilactucae"
                     /db_xref="taxon:2938197"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38673
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 tdafgaelvl kvvapndsel tliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123342748             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas brassicacearum].
ACCESSION   WP_123342748
VERSION     WP_123342748.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33768
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmermk ehaerfetei vfdhinavdf aakpytlkgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlvhrret
      181 fraekilidk lnarvaegki ilklnatlde vlgdnmgvtg arlknndgsf delkvdgvfi
      241 aightpntsl fegqlelkdg ylvvkggrdg natatsvegv faagdvadhv yrqaitsaga
      301 gcmaaldter yldglqnasf
//
LOCUS       WP_123344991             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_123344991
VERSION     WP_123344991.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38706
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvidsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfnnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123348132             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [unclassified Enterobacter].
ACCESSION   WP_123348132
VERSION     WP_123348132.1
KEYWORDS    RefSeq.
SOURCE      unclassified Enterobacter
  ORGANISM  unclassified Enterobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Enterobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="unclassified Enterobacter"
                     /db_xref="taxon:2608935"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53484
     Region          5..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 martksrvrr ffslilpflf issvhaeqts lpakpvtvea knetfspqhp dqylswkats
       61 eqsaredala edprlvilwa gyafsrdynk prghayavtd vretlrtgap ktaedgpmpm
      121 acwsckspdv arliqkegee gyfhgkwasg gpevvnnlgc adchntased fakgkpaltl
      181 srpyaarame aigkpfdkag rfdqqsmvcg qchveyyfeg kdkavkfpwd egmkvenmek
      241 yydaiafsdw tnslskapml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf pqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gateaemkpi lqdirhaqwr wdlaiashgi hmhapeeglr mlgsamdkta dartrlvrll
      421 atkgitdevp lpdistkeka qkaiglnmqq inaekqdfik ttipqwedqa rkngllsq
//
LOCUS       WP_123358427             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Gammaproteobacteria].
ACCESSION   WP_123358427
VERSION     WP_123358427.1
KEYWORDS    RefSeq.
SOURCE      Gammaproteobacteria (g-proteobacteria)
  ORGANISM  Gammaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Gammaproteobacteria"
                     /db_xref="taxon:1236"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38621
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag avaadasaly arnlldflkl vfnkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123362676             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_123362676
VERSION     WP_123362676.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33506
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mteakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtael qqrpfilkgd sgtyscdali iatgasaqyl
      121 glpseetfag kgvsacatcd gffyrnqvva vigggntave ealylsniak evhlvhrrdk
      181 lraekilqdk lfdkaakgni rlhwnqnlde vlgdtsgvtg arlrdsltge tqelalagvf
      241 iaighkpntd lfkgqlemrd gyllvkggse gdatatgipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kflddn
//
LOCUS       WP_123363567             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas chlororaphis].
ACCESSION   WP_123363567
VERSION     WP_123363567.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38686
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel vliksgtvlv gmlnpfsnet iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123366310             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas brassicacearum].
ACCESSION   WP_123366310
VERSION     WP_123366310.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33951
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseakhsrli ilgsgpagys aavyaaranl npvvitgiqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfhtei vydhihtakl qqrpfeligd sgtytcdali iatgasaqyl
      121 glpseetfag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlihrrdk
      181 lrsekilqdk lfekaakgni rlhwnqnlde vlgdasgvtg arlrdshtde tselalagvf
      241 iaighkpntd lfegqlkmrd gyllvkggse gdatsteipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddipvv
//
LOCUS       WP_123369328             352 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Pseudomonas brassicacearum].
ACCESSION   WP_123369328
VERSION     WP_123369328.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     Protein         <1..352
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..345
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(23,103..104,113..114,117..118,121..122,124..125,
                     127..132,134,136..138,141,164..165,260..261,303..304,308,
                     311..312)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(52,71,270,296,298)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(98..99,103,106,109,150..153,173..175,210,221,
                     238..240,247,249)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(100..101,103,113,156..157,164,180..181,183..186)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(133..137,140,143,166,168)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 tikkligqgh kvtvqrgagi nasvvdsaye aagaiigsan dafgaelilk vvapsdsela
       61 liksgtvvvg mlnpfsneti aklaecgita faleaaprts raqsldvlss qaniagykav
      121 llaahhyprf mpmlmtaagt vkaarvlilg agvaglqaia takrlgavie asdvrpavke
      181 qieslgakfv dvpyetdeer ecavgvggya rpmpaswmqr qalavherak qadivittal
      241 ipgrkapmll saetvaqmkp gsvvidlaaa qggncpltva dqvvvengvi icgptnlaga
      301 vaadasalya rnlldflklv fnkegqfein leddivaacl mcrdgqvirk na
//
LOCUS       WP_123370009             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Cellulomonas sp. PhB150].
ACCESSION   WP_123370009
VERSION     WP_123370009.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas sp. PhB150
  ORGANISM  Cellulomonas sp. PhB150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Cellulomonas sp. PhB150"
                     /db_xref="taxon:2485188"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33391
     Region          6..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msmqrdlviv gsgpagytaa iyaaraglap livagsvtag galmntteve nfpgfpdgiq
       61 gpelmenlqk qaerfgaevl wddatsleld gpvkkivvsg getylarsvi lstgsayrel
      121 glddekrlsg rgvswcatcd gfffkdqeii vvgggdsave eatfltrfgk rvtmvhrrdq
      181 lraskimadr aandpkiefa wnseivaiag dakvtgvtlr dtvtgetreh patgvfvaig
      241 hvprsellvg qielddagyv kvvgrttatn lpgvfacgdl vdhtyrqait aagsgcsaal
      301 daqhflaald drsevap
//
LOCUS       WP_123371848             333 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Cellulomonas sp. PhB150].
ACCESSION   WP_123371848
VERSION     WP_123371848.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas sp. PhB150
  ORGANISM  Cellulomonas sp. PhB150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Cellulomonas sp. PhB150"
                     /db_xref="taxon:2485188"
     gene            1..333
                     /gene="trxB"
     Protein         1..333
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34934
     Region          9..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqdstvrdl vivgsgpagy taaiyaarag laplivagsv taggalmntt evenfpgfpd
       61 giqgpelmen lqkqaerfga evlwddatsl eldgpvkkiv vsggetylar svilstgsay
      121 relglddekr lsgrgvswca tcdgfffkdq eiivvgggds aveeatfltr fgkrvtmvhr
      181 rnqlraskim adraandpki efawnseivg iagdakvtgv tlrdtvtget rehpatgvfv
      241 aighvprsel lvgqieldda gyvkvvgrtt atnlpgvfac gdlvdhtyrq aitaagsgcs
      301 aaldaqhfla aledgladpv pdlgpapvle ear
//
LOCUS       WP_123372465             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cellulomonas sp. PhB150].
ACCESSION   WP_123372465
VERSION     WP_123372465.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas sp. PhB150
  ORGANISM  Cellulomonas sp. PhB150
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Cellulomonas sp. PhB150"
                     /db_xref="taxon:2485188"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51803
     Region          4..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mttigipret rpgerlvaas ptsvgrlvgl gydvvveaga gtaatyadea yaeagative
       61 nawgadvvta vnapsdeqva alragavlva mlapaahpel aerlraqgvt alaldavpri
      121 sraqsldvls tlsnvagyra vieaaeqygg mfggqvtaag ktaparvfvi gagvaglaai
      181 gaadslgaqv rafdvrpeva eqiesmgaaf vraqsaqqqv stdgyasalt deqeaataav
      241 yahesaeadv vittalvrgt apttitadmv aamrpgsviv dlaasgggnc eltvpgqrvv
      301 tpngvtivgw tdlagrlprh tsqlfgtnvv hllqlltpgk dgvlvldled pvqrgmtvah
      361 ggdllwpppp vavsaapapv pppeppapad prpaarrrlv gfalaavlvt laisfappvf
      421 lshatvfvla vfvgyyvisn vshalhtplm aqtnaisgii lvgallqigs ddwlvttlac
      481 vaaalasinv fggflvanrm irmfrrda
//
LOCUS       WP_123375989             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas fluorescens].
ACCESSION   WP_123375989
VERSION     WP_123375989.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38843
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vftkecqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123378940             376 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudokineococcus lusitanus].
ACCESSION   WP_123378940
VERSION     WP_123378940.1
KEYWORDS    RefSeq.
SOURCE      Pseudokineococcus lusitanus
  ORGANISM  Pseudokineococcus lusitanus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kineosporiales;
            Kineosporiaceae; Pseudokineococcus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Pseudokineococcus lusitanus"
                     /db_xref="taxon:763993"
     gene            1..376
                     /gene="trxB"
     Protein         1..376
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=39341
     Region          58..362
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mipttgfitl aptadqtpdg sqaqhpaqdp aqdpaqdrpt ggqgdagaqh dsggevrdvv
       61 ivgsgpsgyt aavyaaraal rpvviagsvt aggalvqtte venypgfadg imgpdlmsam
      121 qaqaerfgae lvlddatevd ltepikvvrd gsgrtyrara vilatgsgyr rldvpgeerl
      181 tghgvswcat cdgfffrdkd vvvvgggdsa veeatfltrf assvtlvhrr dalraskima
      241 eraqadpkir fawnsevvev lgqdtveavt ladtrtgqqr rletagvfia ighdprsell
      301 rrqvrtdseg yvlvssptth tnlpgvfacg dlvdsryrqa itaagtgcsa aldaehylag
      361 lddaartgda vqaavv
//
LOCUS       WP_123403038             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas frederiksbergensis].
ACCESSION   WP_123403038
VERSION     WP_123403038.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas frederiksbergensis
  ORGANISM  Pseudomonas frederiksbergensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas frederiksbergensis"
                     /db_xref="taxon:104087"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33822
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseskhsrli ilgsgpagys aavyaaranl kpvvitgiqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfatei vydhihtakl qqrpfeligd sgtytcdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlvhrrdk
      181 lrsekilqdk lfekaangnv rlhwnqnlde vlgdasgvtg arlrdshtge trelplagvf
      241 iaighkpntd lfqgqlamrd gyllikggse gdatateipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddiptv
//
LOCUS       WP_123405339             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas frederiksbergensis].
ACCESSION   WP_123405339
VERSION     WP_123405339.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas frederiksbergensis
  ORGANISM  Pseudomonas frederiksbergensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas frederiksbergensis"
                     /db_xref="taxon:104087"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33903
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmermk ehaerfetei vfdhinavdf aakpytltgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlihrret
      181 fraekilidk lnarvaegki ilklnsnlde vlgdnmgvtg arlknndgsf delkvdgvfi
      241 aightpntsl fegqltlkdg ylvvhggreg natatnlegi faagdvadhv yrqaitsaga
      301 gcmaaldaer ylddlqnakf
//
LOCUS       WP_123405827             314 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Bacteroidales].
ACCESSION   WP_123405827
VERSION     WP_123405827.1
KEYWORDS    RefSeq.
SOURCE      Bacteroidales
  ORGANISM  Bacteroidales
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Bacteroidales"
                     /db_xref="taxon:171549"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34063
     Region          6..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteertkvli igsgpagyta giyasranls pviyegnqpg gqltqtteie nfpgypngvq
       61 gmemmqhlrd qaerfgarvv srlidsvdfs qrpfrcvddr gdvvvadtvi istgasakyl
      121 gipdeekyng lgvsacatcd gffyrkktva vvgggdtace ealylstlak kvymivrkdy
      181 lrasdimkkr vnerenieil fncntvglfg edgvegarlv rhlgtpeqte fdieidgffl
      241 gighrpntgi fkgqidmdee gyikvnapyt stnvagvfaa gdcadpiyrq avsaagtgcr
      301 aaidaeryil endl
//
LOCUS       WP_123408446             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas frederiksbergensis].
ACCESSION   WP_123408446
VERSION     WP_123408446.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas frederiksbergensis
  ORGANISM  Pseudomonas frederiksbergensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas frederiksbergensis"
                     /db_xref="taxon:104087"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38622
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag vkasvvdsay eaagatigsa
       61 sdafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vfnkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123411088             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_123411088
VERSION     WP_123411088.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33534
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmermr ehaerfetei vfdhinavdf aakpytltgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias kvtlihrrdt
      181 fraekilidk lnarvaegki elklnanlde vlgdnmgvtg arlksndgsf deikvdgvfi
      241 aightpntsl fegqlelkdg ylvvqggreg natatsiagi faagdvadhv yrqaitsaga
      301 gcmaaldter yldglqna
//
LOCUS       WP_123411693             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas chlororaphis].
ACCESSION   WP_123411693
VERSION     WP_123411693.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38684
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdiel aliksgtvlv gmlnpfsnet iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123415418             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas brassicacearum].
ACCESSION   WP_123415418
VERSION     WP_123415418.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33820
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmermk ehaerfetei vfdhinavdf aakpytlkgd satytcdali iatgasaryi
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlvhrrei
      181 fraekilvdk lnarvaegki ilklnatlde vlgdnmgvtg arlknndgsf eelkvdgvfi
      241 aightpntll fdgqldlkdg ylvvkggrdg natatsvegi faagdvadhv yrqaitsaga
      301 gcmaaldaer ylddlqnasf
//
LOCUS       WP_123417592             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas moraviensis].
ACCESSION   WP_123417592
VERSION     WP_123417592.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas moraviensis
  ORGANISM  Pseudomonas moraviensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas moraviensis"
                     /db_xref="taxon:321662"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38861
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag ikasvvdsay eaagasigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet ivkmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera rqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123421817             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Gallaecimonas pentaromativorans].
ACCESSION   WP_123421817
VERSION     WP_123421817.1
KEYWORDS    RefSeq.
SOURCE      Gallaecimonas pentaromativorans
  ORGANISM  Gallaecimonas pentaromativorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Gallaecimonadaceae; Gallaecimonas.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Gallaecimonas pentaromativorans"
                     /db_xref="taxon:584787"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53179
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipaesv sgenrvaasp ksvaelkklg fevliapgag qgasfddsay ldagaeltdp
       61 wecdlifkvn apsdeeiarl kagttlvsfi qpaqnpelld klkaqqvnvl amdmvprisr
      121 aqsldalssm aniagyravv eaanafgrff tgqitaagkv ppakvmviga gvaglaaiga
      181 agslgavvra fdtrpevkeq iqsmgaefle vhleeeggss dgyakemsqa fidaemalfl
      241 eqakevdiii ttalipgkpa pklitremvk amkpgsvivd laapnggnce ltkpgkrfks
      301 dngviilgyt dlasrlagqs stlyatnlvn lakllckekd gninidfddv vlrnmtvvke
      361 geltfppppi avsaapkpka apkevpkeat epakpsrkky vlggigllaf awvanaappa
      421 flshftvfvl acvvgyyvvw nvthalhtpl msvtnaisgi ivvgallqag sggltgflaf
      481 vavlvasini fggftvtrrm lkmfqkg
//
LOCUS       WP_123422884             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vibrio crassostreae].
ACCESSION   WP_123422884
VERSION     WP_123422884.1
KEYWORDS    RefSeq.
SOURCE      Vibrio crassostreae
  ORGANISM  Vibrio crassostreae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Vibrio crassostreae"
                     /db_xref="taxon:246167"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34398
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvkhcnll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttev enwpgdaegl
       61 tgpalmdrmk ehaerfetei lfdhinevdl snrpfrlkgd sgeytcdali istgasakyl
      121 gldseeafkg rgvsacatcd gffyrnqkva vvgggntave ealylsnias evhlvhrrdt
      181 fraekilvkr lmdkvengni vlhtdrtlde vlgddmgvtg vrikdtqsdk tedievmgvf
      241 iaighqpnte ifkgqvdmkd dyiivqsgle gnatqtsipg vfaagdvmdh nyrqaitsag
      301 tgcmaaldae rfldglndk
//
LOCUS       WP_123424300             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas brassicacearum].
ACCESSION   WP_123424300
VERSION     WP_123424300.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33925
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmermk ehaerfetei vfdhinavdf aakpytltgd satytcdali iatgasaryl
      121 glpseetfmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlihrret
      181 fraekilidk lharvaegki vlklnstlde vlgdnmgvtg arlknndgsf delkvdgvfi
      241 aightpntsl fegqltlkdg ylvvqggrdg natatslegi faagdvadhv yrqaitsaga
      301 gcmaaldaer ylddlqnatf
//
LOCUS       WP_123425893             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas brassicacearum].
ACCESSION   WP_123425893
VERSION     WP_123425893.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33851
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtael qqrpfrltgd sgtytcdali iatgasaqyl
      121 glpseetfag kgvsacatcd gffyrnqvva vigggntave ealylgniak evhlihrrdk
      181 lrsekilqdk lferakngni rlhwnqnlde vlgdasgvtg arlrdsltge mkdleltgvf
      241 iaighkpntd lfqgqlemhn gylrvrggse gnatateieg vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddn
//
LOCUS       WP_123427838             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas brassicacearum].
ACCESSION   WP_123427838
VERSION     WP_123427838.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38626
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagamigsa
       61 ndafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklaecgit afsleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvivahgv tiagptnlaa qvgadasaly arnlldflkl vftpegqfqi nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123432245             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas brassicacearum].
ACCESSION   WP_123432245
VERSION     WP_123432245.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33976
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseakhsrli ilgsgpagys aavyaaranl kpvvitgiqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtakl qqrpfeligd ggtytcdali iatgasaqyl
      121 glpseetfag rgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlihrrdk
      181 lrsekilqdk lfekaangni rlhwnqnlde vlgdasgvtg arlrdsltge trelalagvf
      241 iaighkpntd lfidqlpmhd gylrvksgne gdatatiipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddiptv
//
LOCUS       WP_123433328             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_123433328
VERSION     WP_123433328.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38648
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvvv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag avaadasaly arnlldflkl vfnkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123435331             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas brassicacearum].
ACCESSION   WP_123435331
VERSION     WP_123435331.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34010
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermk ehaerfetei vfdhinavdf askpytligd sakytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias kvtlihrret
      181 fraekilidk lnarvaegki elklnsnlde vlgdnmgvtg arlknndgsf delkvdgvfi
      241 aightpntsl fegqltlkdg ylvvqggreg natatsvegi faagdvadhv yrqaitsaga
      301 gcmaaldter ylddlqnakf
//
LOCUS       WP_123437345             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. PanSC9].
ACCESSION   WP_123437345
VERSION     WP_123437345.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. PanSC9
  ORGANISM  Streptomyces sp. PanSC9
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces sp. PanSC9"
                     /db_xref="taxon:1520461"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34269
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfregim
       61 gpdlmdnmra qaerfgaeli pddivsvdlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfv wdseiaevqg dqklsglklr nvktgelsdl pvtglfiaig
      241 hdprtelfkg qlnldeegyl kvaspstrtn lagvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala dedkaepekt aav
//
LOCUS       WP_123441957             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_123441957
VERSION     WP_123441957.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38789
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag vkasivdsay eaagasigsa
       61 ndafgaelil kviapsdael tlikrgavlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123447268             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Rathayibacter].
ACCESSION   WP_123447268
VERSION     WP_123447268.1
KEYWORDS    RefSeq.
SOURCE      unclassified Rathayibacter
  ORGANISM  unclassified Rathayibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Rathayibacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Rathayibacter"
                     /db_xref="taxon:2609250"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34090
     Region          3..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrdiviigsg pagwtaaiya aradlhpvvv assveiggdl mnttdvenfp gfpdgvlgpe
       61 lmtamqkqae kfgadtfydd vvsldleget ktihlgsges ieaktvvvat gsayrklglh
      121 dedrlsghgv swcatcdgff fkgktiavvg ggdsameeat fltkfaekvy vihrkdslra
      181 skvmqkrard nekiefvwnt evtgitgenh vngvklrdtv dgteskleld glfiaigndp
      241 rthivhgkld lttdgtiavt grssqtsvag vfaagdvidp tyrqavtaaa sgtvaaldae
      301 hylaaltdgi astegtpaae lltl
//
LOCUS       WP_123451732             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas fluorescens].
ACCESSION   WP_123451732
VERSION     WP_123451732.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33881
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermr ehaerfetei vfdhinavdf askpysltgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlihrret
      181 fraekilidk lnarvaegki ilklnanlde vlgdnmgvtg arlknndgsf deikvdgvfi
      241 aightpntsl fegqlelkdg ylvvqggreg natatnvegi faagdvadhv yrqaitsaga
      301 gcmaaldter yldglqnasf
//
LOCUS       WP_123456350             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. PanSC19].
ACCESSION   WP_123456350
VERSION     WP_123456350.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. PanSC19
  ORGANISM  Streptomyces sp. PanSC19
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces sp. PanSC19"
                     /db_xref="taxon:1520455"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52399
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgvlkear agehrvsatp atiepirklg ydvvvdsgag aaagftdsay eaagatigda
       61 taadvvlgvn apspaqldgv rpeatvialf apafdpamve elgrrpftal smdavprisr
      121 aqsmdvlssm aniagyravv eaahtfgrff tgqvtaagkv ppakvlvaga gvaglaaiga
      181 agslgaivra tdprpevadq vrslggeyls iespevevsk tgyakemgdd ykarevelya
      241 aqcrevdivi ttalipgrpa pklitaemva smkpgsvivd maaanggnve gtvkgektvt
      301 engvtiigyt dlagrlpaqa sqlygtnlvn llklmtpdkd grlvldwddp vqrsitvvre
      361 gesawppppv qvsaapapap aatetkppkp krepmtparr fggvavaala lflaagfapa
      421 allphvtvfv laivigyyvi ghvhhalhtp lmsvtnaisg iivvgallqi ghsstavtvl
      481 ssvaillasi nvfggfavtr rmlamfnrs
//
LOCUS       WP_123455102             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas fluorescens].
ACCESSION   WP_123455102
VERSION     WP_123455102.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38795
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vnasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123460445             320 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Streptomyces].
ACCESSION   WP_123460445
VERSION     WP_123460445.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33661
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfqdgim
       61 gpelmdnmra qaerfgaeli pddvvsvdlt gdiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtivhrrds
      181 lraskamqdr afadpkikfa wdsevagvhg eqklsgltlr ntktgetsel pvtglfiavg
      241 hdprtelfkg qldlddegyl kveapstrtn vtgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala ddekaaaatv
//
LOCUS       WP_123462484             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Pseudomonas].
ACCESSION   WP_123462484
VERSION     WP_123462484.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33704
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mnaakhsrli ilgsgpagys aavyaaranl kpvvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfatei vydhihtakl qqrpfeligd sgtytcdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlihrrdk
      181 lrsekilqdk lfdkaasgnv rlhwnqnlde vlgdasgvtg arlrdshtge trelslagvf
      241 iaighkpntd lfqgqlpmrd gylvikggse gdatataipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddipvi
//
LOCUS       WP_123470291             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_123470291
VERSION     WP_123470291.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38775
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagaiigsa
       61 ndafgaelil kvvapsdael alikrgavlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123476226             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Muribaculum intestinale].
ACCESSION   WP_123476226
VERSION     WP_123476226.1
KEYWORDS    RefSeq.
SOURCE      Muribaculum intestinale
  ORGANISM  Muribaculum intestinale
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae; Muribaculum.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Muribaculum intestinale"
                     /db_xref="taxon:1796646"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33564
     Region          5..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdttkclii gsgpagytaa iyaaranmap iiyeglqpgg qltttseven fpgypdgvmg
       61 aqlmedlrkq aarfeadirt gviskvdfss rpfhataddg teiqadtvii atgasarylg
      121 ledevrysgl gvsacatcdg ffyrgrtvav vgggdtacee ayylsglakk vylivrkdyl
      181 raskvmqkrv ldkenitilf ntqtlglfgk efvegahlie yagtdreqkf dididgffla
      241 ighkpntdif ktqialdeqg yikiegntqa tsvpgvfaag dvadpnyqqa ivaaasgcka
      301 aldaehflme qpq
//
LOCUS       WP_123472749             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas protegens].
ACCESSION   WP_123472749
VERSION     WP_123472749.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33508
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mndakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqlttttev dnwpgdvegl
       61 tgpvlmermq rhaerfdtei vydhihtaql qqrpfiligd sgtyscdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vvgggntave ealylsniaq evhlvhrrdk
      181 lraekilqdk lfdkaangni rlhwnqhlee vlgdasgvtg arlkdshsge tkdlalagvf
      241 iaighkpntd lfqgqlemrd gyllvrggse gnatatgiqg vfaagdvadh vyrqaitsag
      301 agcmaaldae kflddn
//
LOCUS       WP_123478334             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas canadensis].
ACCESSION   WP_123478334
VERSION     WP_123478334.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas canadensis
  ORGANISM  Pseudomonas canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas canadensis"
                     /db_xref="taxon:915099"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38733
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasvvdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaigvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123480237             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas rhodesiae].
ACCESSION   WP_123480237
VERSION     WP_123480237.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas rhodesiae
  ORGANISM  Pseudomonas rhodesiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas rhodesiae"
                     /db_xref="taxon:76760"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33819
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msatrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermk ehaerfetei vfdhinkvdf skkpysltgd sgvytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlvhrret
      181 fraekilidk lharvaegki ilklnatlde vlgdnmgvtg arlknndgsf delkvdgvfi
      241 aightpntsl fegvleakdg ylvvqggreg natatniegi faagdvadhv yrqaitsaga
      301 gcmaaldaer yldglkdatf
//
LOCUS       WP_123483969             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lepagella muris].
ACCESSION   WP_123483969
VERSION     WP_123483969.1
KEYWORDS    RefSeq.
SOURCE      Lepagella muris
  ORGANISM  Lepagella muris
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae; Lepagella.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Lepagella muris"
                     /db_xref="taxon:3032870"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34251
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseektrvli igsgpagyta alyasranlq pllfegdqpg gqltqtteie nfpgypdgiq
       61 gqemmeqfrq qalrfgadvr srmvvkvdfs qrpfrceder gdvvyadsvi vctgasakyl
      121 glpdeekyrg lgvsacatcd gffyrkknva vvgggdtace ealylstlak kvylivrrgv
      181 lrasdvmqrr vkerenieil yhcntlglfg edgvegahiv rhkgtpeeet fdiaidgffl
      241 aighrpntei fkgqldmdee gyikvegatt htnvegvfaa gdcadpryrq avaaagtgcr
      301 aaldaekflm eqd
//
LOCUS       WP_123506642             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Frondihabitans sp. PhB188].
ACCESSION   WP_123506642
VERSION     WP_123506642.1
KEYWORDS    RefSeq.
SOURCE      Frondihabitans sp. PhB188
  ORGANISM  Frondihabitans sp. PhB188
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frondihabitans.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Frondihabitans sp. PhB188"
                     /db_xref="taxon:2485200"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34332
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqviiigsg pagytaaiya graglaplvv assveaggel mktteienfp gfpeglqgpe
       61 lmfkmqeqae kfgaevlldd vveldlsgdi kkvtlgsgav eealtvifat gsayrklgve
      121 geerlsgrgv swcatcdgff fkqkeiavvg ggdsameeat fltrfatkvy vihrgdtlra
      181 skimqdrafd nekieflwnk kvtavtgdek aagvtltdtv dgteshldle glfiaigndp
      241 rvhlvhnqld ltsdgtiave grssktnlkg vfaagdvidi tyrqaitaag sgtvaaldae
      301 hylagldkav ldqaqgaapa epvtasa
//
LOCUS       WP_123513381             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas frederiksbergensis].
ACCESSION   WP_123513381
VERSION     WP_123513381.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas frederiksbergensis
  ORGANISM  Pseudomonas frederiksbergensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas frederiksbergensis"
                     /db_xref="taxon:104087"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38579
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv ticgptnlag avaadasaly arnlldflkl vfnkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123508927             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas frederiksbergensis].
ACCESSION   WP_123508927
VERSION     WP_123508927.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas frederiksbergensis
  ORGANISM  Pseudomonas frederiksbergensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas frederiksbergensis"
                     /db_xref="taxon:104087"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33889
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseakhsrli ilgsgpagys aavyaaranl kpvvitgiqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtakl qqrpfeligd sgtytcdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlvhrrdk
      181 lrsekilqdk lfekaangni rlhwnqnlde vlgdasgvtg arlrdshtge trelplagvf
      241 iaighkpntd lfqgqlamrd gyllikggne gdatateipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddipvv
//
LOCUS       WP_123515260             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas frederiksbergensis].
ACCESSION   WP_123515260
VERSION     WP_123515260.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas frederiksbergensis
  ORGANISM  Pseudomonas frederiksbergensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas frederiksbergensis"
                     /db_xref="taxon:104087"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33862
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmdrmk ehaerfetei vfdhinavdf aakpytltgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlihrret
      181 fraekilidk lnarvaegki ilklnsnlde vlgdnmgvtg arlknndgsf deltvdgvfi
      241 aightpntsl fegqltlkdg ylvvhggreg natatnlegi faagdvadhv yrqaitsaga
      301 gcmaaldaer ylddlqnakf
//
LOCUS       WP_123522227             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudofulvimonas gallinarii].
ACCESSION   WP_123522227
VERSION     WP_123522227.1
KEYWORDS    RefSeq.
SOURCE      Pseudofulvimonas gallinarii
  ORGANISM  Pseudofulvimonas gallinarii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Pseudofulvimonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudofulvimonas gallinarii"
                     /db_xref="taxon:634155"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33587
     Region          8..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtvkhsrlli lgsgpagysa avyaaranlk pllitglqqg gqlmtttevd nwpgdveglv
       61 gpdlmdrmlr haqrfdteiv ldhiieadls qrpfrlkgds geytcdalii atgatakylg
      121 lpseqafmgr gvsacatcdg ffyrnqdvav igggntavee alylanicrk vtlvhrrdkl
      181 raekilqdkl fareregkve iiwdhaveev lgddsgvtgv riapvkggas rdlvvqgffv
      241 aighspntgl fdgqldmrag gylvvktgld glatqtsvpg vfaagdvads vyrqaitsag
      301 sgcmaaldae rfldqg
//
LOCUS       WP_123524863             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. 840.1].
ACCESSION   WP_123524863
VERSION     WP_123524863.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. 840.1
  ORGANISM  Streptomyces sp. 840.1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces sp. 840.1"
                     /db_xref="taxon:2485152"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33647
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfqdgim
       61 gpelmdnmra qaerfgaelv pddvvsvdlt gdiktvtdta gtvhrakaii vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtivhrrds
      181 lraskamqdr afadpkikfa wdsevagvhg eqklsgltlr ntktgetsel pvtglfiavg
      241 hdprtelfkg qldlddegyl tvqapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala ddekaaaatv
//
LOCUS       WP_123534149             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas fluorescens].
ACCESSION   WP_123534149
VERSION     WP_123534149.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33794
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitglqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermr ehaerfetei vfdhinavdf askpysltgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlihrret
      181 fraekilidk lnarvaegki ilklnanlde vlgdnmgvtg arlknndgsf deikvdgvfi
      241 aightpntsl fegqltlkdg ylvvqggrdg natatsvegi faagdvadhv yrqaitsaga
      301 gcmaaldter yldglqnasf
//
LOCUS       WP_123547389             335 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Frigoribacterium].
ACCESSION   WP_123547389
VERSION     WP_123547389.1
KEYWORDS    RefSeq.
SOURCE      unclassified Frigoribacterium
  ORGANISM  unclassified Frigoribacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Frigoribacterium.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="unclassified Frigoribacterium"
                     /db_xref="taxon:2627005"
     gene            1..335
                     /gene="trxB"
     Protein         1..335
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35112
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqiiiigsg pagytagiya araglepliv assveaggel mkttevenfp gfpdgiqgpe
       61 lmfklqeqae kfgaevlldd vtsvdltgdv kkvtlgsgtv eealtvifat gsayrklglp
      121 deerlsgrgv swcatcdgff fkqkeiavvg ggdsameeat fltrfaskvy vihrsetlra
      181 skimqdraqg ndkieflfnk qvtailgdek atgvqltdtv dgstsdldld glfiaigndp
      241 rvhlvhgqvd ltssgtiave grssktnlrg vfaagdvvdd tyrqaataag sgvvaaldae
      301 hflasldqtf laehtegaae gidtaesvap epvsa
//
LOCUS       WP_123537016             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas fluorescens].
ACCESSION   WP_123537016
VERSION     WP_123537016.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38823
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael slikrgtvlv gmlnpfnnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123549698             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paramuribaculum intestinale].
ACCESSION   WP_123549698
VERSION     WP_123549698.1
KEYWORDS    RefSeq.
SOURCE      Paramuribaculum intestinale
  ORGANISM  Paramuribaculum intestinale
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae; Paramuribaculum.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Paramuribaculum intestinale"
                     /db_xref="taxon:2094151"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33875
     Region          6..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnqihtkcli igsgpagfta aiytsranmk plvyaghqpg gqltitteve nfpgyhegvt
       61 gtqlmadlek qaarfgadir qgiitsvdfs qhplraiadd nteitadtvi istgataryl
      121 glpdeerykg mgvsacatcd gffyrrkrva vvgggdtace ealylsnias evflivrkdy
      181 lraskvmqrr veekanitvl fntntlglyg ddylegaqlv efastdkerv ynlpvdgffl
      241 aighkpatdi frpwieldea gyiktegqst rtnvagvfaa gdvadpnyrq aitaagsgck
      301 aaldaerylt eqgg
//
LOCUS       WP_123553873             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora sp. HM5-17].
ACCESSION   WP_123553873
VERSION     WP_123553873.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. HM5-17
  ORGANISM  Micromonospora sp. HM5-17
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Micromonospora sp. HM5-17"
                     /db_xref="taxon:2487710"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33632
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa iyaaranlap lviegvesgg almttteven fpgfadgimg
       61 pelmdamrkq aerfgaefvt ddvtrvelvd tgvpgsgalh tvyvgetayr akavilstgs
      121 awrplgvpge qeylghgvss catcdgfffr gqeivvvggg dsameeavfl tkfaskvtiv
      181 hrrdefrask imadralane kiqvewnsvv eeilgadgkv sgvrlrnvht getktlevag
      241 vfvaighdpr stlfrgqvdl dengyvkvqs pstrtnipgv faagdlvdht yrqaitaags
      301 gcaaaldaer flatlted
//
LOCUS       WP_123554008             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Kitasatospora cineracea].
ACCESSION   WP_123554008
VERSION     WP_123554008.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora cineracea
  ORGANISM  Kitasatospora cineracea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Kitasatospora cineracea"
                     /db_xref="taxon:88074"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34200
     Region          8..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvvrnviv igsgpsgyta glytaraslq plvfegavta ggalmnttev enfpgyrdgi
       61 mgpelmdnmr aqaerfgael vpddvvavdl tgeiktvtds egtvhrarav ivatgsqhrk
      121 lglpnedkls grgvswcatc dgfffrdqdi avvgggdtal eeatflsrfa rsvtvihrrn
      181 slraskamqe rafadpkitf awdsaveeih gdpklsgltl rdtntgdlre lpvtglfiai
      241 ghdprtelfk gqleldaegy lkvdapstrt nlpgvfaagd vvdhtyrqai taagtgcsaa
      301 ldaerylaal adadeapatv lav
//
LOCUS       WP_123572382             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas chlororaphis].
ACCESSION   WP_123572382
VERSION     WP_123572382.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38716
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafdaelil kvvapsdsel aliksgtvlv gmlnpfsnet iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123571099             330 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Frigoribacterium].
ACCESSION   WP_123571099
VERSION     WP_123571099.1
KEYWORDS    RefSeq.
SOURCE      Frigoribacterium
  ORGANISM  Frigoribacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Frigoribacterium"
                     /db_xref="taxon:96492"
     gene            1..330
                     /gene="trxB"
     Protein         1..330
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34498
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqviiigsg pagytagiya araglrpliv assveaggel mkttevenfp gfpdgiqgpe
       61 lmfkmqeqae kfgaevlldd vtavdltgdv kkvtlgngtv eesltvifat gsayrklgla
      121 deerlsgrgv swcatcdgff fkekaiavvg ggdsameeat fltrfaskvy vihrssslra
      181 skimqdraha ndkieflfdk qvtailggek atgvtltdtv dgsttdldld glfiaigndp
      241 rvhlvhgqvd ltsdgtiavq grssktnltg vfaagdvida tyrqaataaa sgtvaaldve
      301 hylasldqtf laeqtvgsae gvetsesvva
//
LOCUS       WP_123562298             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Kitasatospora cineracea].
ACCESSION   WP_123562298
VERSION     WP_123562298.1
KEYWORDS    RefSeq.
SOURCE      Kitasatospora cineracea
  ORGANISM  Kitasatospora cineracea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Kitasatospora.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Kitasatospora cineracea"
                     /db_xref="taxon:88074"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51943
     Region          13..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msgydssvrp pqqvgvvaes vpgetrvaat patvrgllal gygvvvesga gaasgfddaa
       61 yeaagaavgd awaaevvlkv napstaevgr lregaalvgl lapaqhpell aalagrgvta
      121 lsldavpris raqsmdvlss maniagyrav ieaahafgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvrslggeyl avevaqeast dgyakatsad
      241 ydraaaalyr aqaadvdivv ttalipgrpa pklltaedva amkpgsvvvd maaaqggnva
      301 gtvagrtvvt dngvtligyt dlasrlpaqa sqlfgtnlvn llklltpgkd grltidfedv
      361 vqravtvvrd gattwppppv avsaapaapp aapaaapape parltpavrt glvgagmlal
      421 flliafapaq laenftvfal avvigyyvig kvhhalhtpl msvtnaisgi vvigallqig
      481 hggvlvtvls fvailltsvn ifggfavtrr mlsmfskg
//
LOCUS       WP_123578770             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas brassicacearum].
ACCESSION   WP_123578770
VERSION     WP_123578770.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33989
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mnevkhsrli ilgsgpagys aavyaaranl kpvvitgmqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq rhaerfdtqi vydhihtakl qqrpfeligd sgtytcdali iatgasaqyl
      121 glpseesfag kgvsacatcd gffyrnqvva vvgggntave ealylsniar evhlihrrdk
      181 lrsekilqdk lfekaangnv klhwnqnlde vlgdasgvtg arlrhsetge tstlslagvf
      241 iaighkpnte lfqgqlnmrd gyllvrggse gnatatdieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddiptv
//
LOCUS       WP_123579330             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas brassicacearum].
ACCESSION   WP_123579330
VERSION     WP_123579330.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38790
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq pgetrvaatp etikkligqg hkvtvqsgag ikasvidsay eaagatigsa
       61 seafgaelil kvvapndsel tlikrgavlv gmlnpfnnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123581761             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas brassicacearum].
ACCESSION   WP_123581761
VERSION     WP_123581761.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38677
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagamigsa
       61 ndafgaelil kvvapsdsel alikrgtvlv gmlnpfsnet iaklaecgit afsleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvahgv tiagptnlaa qvgadasaly arnlldflkl vftpegqfqi nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123582645             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas brassicacearum].
ACCESSION   WP_123582645
VERSION     WP_123582645.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33915
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmermk ehaerfetei vfdhinavdf aakpytltgd satytcdali iatgasaryl
      121 glpseetfmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlihrret
      181 fraekilidk lharvaegki vlklnstlde vlgdnmgvtg arlknndgsf delkvdgvfi
      241 aightpntsl fegqltlkdg ylvvqggreg natatslegi faagdvadhv yrqaitsaga
      301 gcmaaldaer ylddlqnash
//
LOCUS       WP_123583603             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas brassicacearum].
ACCESSION   WP_123583603
VERSION     WP_123583603.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas brassicacearum
  ORGANISM  Pseudomonas brassicacearum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas brassicacearum"
                     /db_xref="taxon:930166"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33883
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqltttiev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtael qqrpfrltgd sgtytcdali iatgasaqyl
      121 glsseetfag kgvsacatcd gffyrnqvva vigggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lferakngni rlhwnqnlee vlgdasgvtg arlrdsltge mkdleltgvf
      241 iaighkpntd lfqgqlemhn gylrvrggse gnatateieg vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddn
//
LOCUS       WP_123588290             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas fluorescens].
ACCESSION   WP_123588290
VERSION     WP_123588290.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33869
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mnaakhsrli ilgsgpagys aavyaaranl kpvvitglqa ggqltttfev dnwpgdvegl
       61 tgpalmermq khaerfatei vydhihtakl qqrpfeligd sgtytcdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlihrrdk
      181 lrsekilqdk lfekaasgnv rlhwnqnlde vlgdasgvtg arlrdshseq treltlagvf
      241 iaighkpntd lfqgqlpmrd gyllvkggsd gdatsteipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddipvi
//
LOCUS       WP_123587236             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas fluorescens].
ACCESSION   WP_123587236
VERSION     WP_123587236.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33794
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmermr ehaerfetei vfdhinavdf aakpytltgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlihrret
      181 fraekilidk lnarvaegki ilklnanlde vlgdnmgvtg arlknndgsf deikvdgvfi
      241 aightpntsl fegqlilkdg ylvvqggrdg natatsvegi faagdvadhv yrqaitsaga
      301 gcmaaldter yldglqnasf
//
LOCUS       WP_123596829             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas frederiksbergensis].
ACCESSION   WP_123596829
VERSION     WP_123596829.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas frederiksbergensis
  ORGANISM  Pseudomonas frederiksbergensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas frederiksbergensis"
                     /db_xref="taxon:104087"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33861
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseakhsrli ilgsgpagys aavyaaranl kpvvitgiqa ggqltttvev dnwpgdvegl
       61 tgpalmermq khaerfdtei vydhihtakl qqrpfeligd sgtytcdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlvhrrdk
      181 lrsekilqdk lfekaangni rlhwnqnlde vlgdasgvtg arlrdshtge trelplagvf
      241 iaighkpntd lfqgqlamrd gyllikggne gdatateipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddipvv
//
LOCUS       WP_123606655             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora sp. Llam0].
ACCESSION   WP_123606655
VERSION     WP_123606655.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora sp. Llam0
  ORGANISM  Micromonospora sp. Llam0
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Micromonospora sp. Llam0"
                     /db_xref="taxon:2485143"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33753
     Region          7..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlrp vviegvqsgg almttteven fpgfpdgimg
       61 pelmdsirkq aerfgaefvt ddvtrvelad tgtpgtteas tvyvgetgyr akavilatgs
      121 awrplnvpge qeflghgvss catcdgfffr gqhvvvvggg dsameeatfl trfaesvtiv
      181 hrrdefrasq imaaralgne kirvewnsvv eeilgadgkv sgirlrntht gesrtldvtg
      241 vfvaighdpr semfrgqvel dengyvlvds pstrtsvpgv faagdlvdht yqqaitaags
      301 gcaaaldaer ylatleev
//
LOCUS       WP_123610973             307 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mobilisporobacter senegalensis].
ACCESSION   WP_123610973
VERSION     WP_123610973.1
KEYWORDS    RefSeq.
SOURCE      Mobilisporobacter senegalensis
  ORGANISM  Mobilisporobacter senegalensis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Mobilisporobacter.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Mobilisporobacter senegalensis"
                     /db_xref="taxon:1329262"
     gene            1..307
                     /gene="trxB"
     Protein         1..307
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33018
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mekiydliiv gsgpaglaag iyasradlnf iiieknpisg gqiintyevd nypgvpgisg
       61 feladrfrkh cdnqgvnfvt gdvqsfdveg avktitldng dtyksktiiv stgavykklg
      121 aegeekfsgm gvsycatcdg affrnkdvav vgggdvaved aiflarlchk vyvihrrdef
      181 raakslqlkl ksmenveiiw dsvveeirgt eavesitirn lkteekraln iegafiaign
      241 mpssdvykef vatdssgyii agedcetnvk gvfaagdirt kglrqiitaa adganaitav
      301 ekylnen
//
LOCUS       WP_123614440             314 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Duncaniella].
ACCESSION   WP_123614440
VERSION     WP_123614440.1
KEYWORDS    RefSeq.
SOURCE      Duncaniella
  ORGANISM  Duncaniella
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Duncaniella"
                     /db_xref="taxon:2518495"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33507
     Region          6..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeiktrcli igsgpagyta aiyasranis plviegmqpg gqltitteve nfpgqpngit
       61 gpqlmedirt qalkfgadir tglvtevdfs trpfkaktnn gleieantvi istgasaryl
      121 glpdeqkysg lgvsacatcd gffyrkkrva vvgggdtace ealylsnlas dvflivrkph
      181 lraskvmqer vlnksnikvl fntnttglyg eeylegahlv envgtsneqh ydlaldgffl
      241 aighnpntev frqyidcdaa gyikvkgsgt qtnvpgvfaa gdvadptyrq aicaagmgck
      301 aaldaerfln eegl
//
LOCUS       WP_123630641             390 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Salinisphaera orenii].
ACCESSION   WP_123630641
VERSION     WP_123630641.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera orenii
  ORGANISM  Salinisphaera orenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Salinisphaera orenii"
                     /db_xref="taxon:856731"
     Protein         1..390
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40737
     Region          3..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msvkiavpke tadgetrvam vpkvaaklak mnvdirvakg agegsripdd ayddpvqisd
       61 qaadifgadi vlgvnapepk qigemkkgsv lisfvqahnn petvkalnda gvtcfamelv
      121 pritraqsmd alssqasaag ykaalmaana lerflpmltt aagtirpakv lvigagvagl
      181 qaiatakrlg akvfaydvrt dtkeqveslg adflmaegvk aeaeggyare ltdeekkkqq
      241 dmleknmada davittaavp gkpapkiise amvdsmkpgs vlidlgasgg gnceltkpde
      301 vvthgsvtih gpsnvpalla ehasemyaqn lfnflqlivv peagqedakp adkthkleid
      361 wddevlaksa lthdgqivnd aakqalegsa
//
LOCUS       WP_123630396             338 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Salinisphaera orenii].
ACCESSION   WP_123630396
VERSION     WP_123630396.1
KEYWORDS    RefSeq.
SOURCE      Salinisphaera orenii
  ORGANISM  Salinisphaera orenii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Salinisphaerales; Salinisphaeraceae; Salinisphaera.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Salinisphaera orenii"
                     /db_xref="taxon:856731"
     gene            1..338
                     /gene="trxB"
     Protein         1..338
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36203
     Region          7..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mskdeirhqk liilgsgpag ytaavyaara nlkpvlitgm eqggqlmttt dvdnwpgdve
       61 glqgpglmqr meehakrfdt eilfdhihtt dlskppyrle gdrgvytcda liiatgatar
      121 ylglesettf mgkgisacat cdgffykgkn vavigggnta leealylsnl aahvtvvhrr
      181 dkfrgekila dklfdkqang nvsiiwdhel devlgdemgv tggrikhtrs getqaldvdg
      241 ifiaighkpn tdifagqldm eggyikvqsg tqgnatatsk pgvfaagdvm dhvyrqaits
      301 agsgcmaald aekyldalta ddsareahve aqeahrev
//
LOCUS       WP_123633490             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Marinobacter sp. R17].
ACCESSION   WP_123633490
VERSION     WP_123633490.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. R17
  ORGANISM  Marinobacter sp. R17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Marinobacter sp. R17"
                     /db_xref="taxon:2484250"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34319
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvkhsrli ilgsgpagyt aavyaaranl nptlitgiev ggqlttttdv dnwpgdndgv
       61 qgpelmqrml khaerfetsv vydtineadl nqrpfrlkgd sgeytcdali iatgasamyl
      121 gldseekfkg qgvsacatcd gffyrkqkva vigggntave ealylsniad evtlvhrrdk
      181 lraekilqdk lfekekngnv rivwdhtlde vlgdatgvtg mrirntktgd tqemelagvf
      241 iaighkpntd lfqgqldmen gylrirsgle gmatqtsvpg vfaagdvadh vyrqavtsag
      301 fgcmaaldae rfldqlgd
//
LOCUS       WP_123635387             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter sp. R17].
ACCESSION   WP_123635387
VERSION     WP_123635387.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. R17
  ORGANISM  Marinobacter sp. R17
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Marinobacter sp. R17"
                     /db_xref="taxon:2484250"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55372
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkech pgenrvaatp asvgkliklg htvvvetgag daakyhdday reagaeiaen
       61 ardlwsaaef ilkvrgpgyn keadldetsl ikddsyllsf lwpaqnpeml etlasknvta
      121 fsidalpris raqkmdalsa mgniagyrav veasnrfgrf ftgqvtaagk vppakvmvig
      181 agvaglaaig aarsmgaivr afdtrlevke qvesmgadfl eldfeedgsg sggyakqmsk
      241 efieaemalf meqakevdii ittalipgkp aprlitadmv ramkpggvvv dlaaeqggnc
      301 eltqpgevav engvsivgyt dlpsrmasvs sdlyatnlwh llgeltpekd geinvnmedt
      361 virgvtvthe gkvtwpapqp ekpapkpaqp kpaaqpasde aedgksgaka fwkgallvat
      421 vaalygigay aptsflshft vfvlacfvgw qviwnvtasl htplmsvtna isgiivigav
      481 lhlaqaqnlv igilaffavl iacinigggf rvtyrmlkmf hr
//
LOCUS       WP_123637604             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Marinimicrobium koreense].
ACCESSION   WP_123637604
VERSION     WP_123637604.1
KEYWORDS    RefSeq.
SOURCE      Marinimicrobium koreense
  ORGANISM  Marinimicrobium koreense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Marinimicrobium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Marinimicrobium koreense"
                     /db_xref="taxon:306545"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33731
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseaqhhrli ilgsgpagyt aaiyaaranl npvlitgmqq ggqlttttdv enwpggvsdl
       61 qgpdlmvemq qhaerfdtqi ifdhihetdl serpyklign etytcdalii atgasaqyig
      121 lpseeafmgk gvsacatcdg ffyrdqkvav vgggntavee alylsniase vtlihrrdkl
      181 raekilqdkl fakaengnvk ivwdhtldev lgddngvtga rlrsmlnest heidvqgvfi
      241 aighkpntdi fagqldmkdg yikiksglng natatsvpgv faagdvsdhv yrqaitsaga
      301 gcmaaldaek ylddl
//
LOCUS       WP_123639215             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinimicrobium koreense].
ACCESSION   WP_123639215
VERSION     WP_123639215.1
KEYWORDS    RefSeq.
SOURCE      Marinimicrobium koreense
  ORGANISM  Marinimicrobium koreense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Cellvibrionaceae; Marinimicrobium.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Marinimicrobium koreense"
                     /db_xref="taxon:306545"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40502
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,323,325)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,330..331,335,
                     338..339)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipkerr eherrvaatp etvkklialg aevaveagag lssritdeay eaagatlvsd
       61 lnsllgdadv vlkvqrpllg ggdqpdelsp mkkgalliag lspyaepdai kryaeagvta
      121 iamefvprit raqsmdilss qsnlagyrav leaayvydra mpmmmtaagt iaparvmvlg
      181 agvaglqaia takrlgaivs atdvrpaake qveslggkfv mvesdetkea etaggyakem
      241 sedykrkqae lvaetlkkqd iaictalipg rkaptlinde mvhsmrpgsv ivdlaaeqgg
      301 nctlskpgev vdvngvsiig hynipsrlsa dasslfaknl lnyltplvda eskalkvdwe
      361 deivaasvlt rdgqvvhsaf qseq
//
LOCUS       WP_123643199             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Histidinibacterium lentulum].
ACCESSION   WP_123643199
VERSION     WP_123643199.1
KEYWORDS    RefSeq.
SOURCE      Histidinibacterium lentulum
  ORGANISM  Histidinibacterium lentulum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Histidinibacterium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Histidinibacterium lentulum"
                     /db_xref="taxon:2480588"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35695
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 magtrhtkll iigsgpagyt agvyasraml epllvqglep ggqlttttev enwpgdtevq
       61 gpdlmvrmea haramgteiv sdiitsldls hrpftarsds gtvytadavi latgarakwl
      121 glpsedaykg fgvsacatcd gffyrgqeiv vigggntave ealfltnfas kvtlvhrrde
      181 lraekilqdr lfknpkietl whheldevlg etdprgvtgv rvrhvrtget reipakgvfv
      241 aighapasel vkdqlethmg gyvktvpgst ettipgvfaa gditdwkyrq avtsagmgcm
      301 aaleaerfla eqgetegkdq tpplgyglpv daae
//
LOCUS       WP_123644412             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bifidobacterium mongoliense].
ACCESSION   WP_123644412
VERSION     WP_123644412.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium mongoliense
  ORGANISM  Bifidobacterium mongoliense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Bifidobacterium mongoliense"
                     /db_xref="taxon:518643"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53767
     Region          3..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mviigipket legerlvagt pktvvqlkkl gydvavesga ghaasfsdev yvaagayivn
       61 adrawgadvv atvdpptdrq idalkpgall vsrlaphsht eligtlahhq vtalaldavp
      121 risraqsldv lstmsnvagy ravieaaeef ggmftgqvta agktpparvf vigggvagls
      181 aigaaaslga evrafdvrpe aaeqieslga tfvrapqaqq qrsstgyasa lsdeqqqatl
      241 alytqeasqa divittalvr gvavptitke avaamkpgsv ivdvaatggg ncaltvpgrs
      301 ivtdndvtii gytdlagrmp qhtsqlfgtn vvnlmklitp kgdgvptldl ddpvqrgmtv
      361 srggdilwpp pavavsaapv asasntasaa akapdpavka reeaerkaaa arrngvltvv
      421 agvalavala ftnyaflltf sifvlaivvg yyvvsnvshs lhtplmsqtn aisgiilvgs
      481 llqigsdntl vtvlavlsaa iasinvfggf lvtyrmlgmf rkda
//
LOCUS       WP_123647991             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lysobacter enzymogenes].
ACCESSION   WP_123647991
VERSION     WP_123647991.1
KEYWORDS    RefSeq.
SOURCE      Lysobacter enzymogenes
  ORGANISM  Lysobacter enzymogenes
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Lysobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Lysobacter enzymogenes"
                     /db_xref="taxon:69"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33836
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msptkhsrvv ilgsgpagwt aavyaaranl kplvitglqq ggqlmtttev dnwpgdahgl
       61 mgpdlmarmq ahaerfdtev qfdhihtadl skrpfrligd sgeytadali iatgatakyl
      121 glpseeeykg rgvsacatcd gffykdqdva vvgggntave ealylsniar kvylvhrrdt
      181 lraekimqdk lqakiqagki epvwhhtvde vvgndagvtg lklksvldgs srelaihglf
      241 vaightpnts lfdgqlemkn gyltirtgld gnatqtsveg vfaagdvadq vyrqaitsag
      301 fgcmaaldae kfldkda
//
LOCUS       WP_123655010             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Curtobacterium sp. ZW137].
ACCESSION   WP_123655010
VERSION     WP_123655010.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. ZW137
  ORGANISM  Curtobacterium sp. ZW137
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Curtobacterium sp. ZW137"
                     /db_xref="taxon:2485104"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34292
     Region          4..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqliiigsg pagftagiya araqlkpliv assvetggel tkttevenfp gfaegiqgpd
       61 lmikmqeqae kfgaevlydd avsveltgdv kkvtvgsget yealaviyat gsayrqlgla
      121 deerlsghgv swcatcdgff frqkniavvg ggdsameeat fltrfadkvt vihrkdtlra
      181 skimqdrain dpkiefawnk evvgitgasa vegvtlkdtv tgetselald glfiaigndp
      241 rvhlvhkqlq lapegtiave grtskavgvp gvfvagdvld htyrqaitaa gsgavaalda
      301 ekfladlddt ltsaaegetp agpvtisa
//
LOCUS       WP_123660490             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pusillimonas sp. NJUB218].
ACCESSION   WP_123660490
VERSION     WP_123660490.1
KEYWORDS    RefSeq.
SOURCE      Pusillimonas sp. NJUB218
  ORGANISM  Pusillimonas sp. NJUB218
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pusillimonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pusillimonas sp. NJUB218"
                     /db_xref="taxon:2023230"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33974
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mttakhakvm ilgsgpagyt aavyaaranl npvlitgleq ggqlmtttdv dnwpadaqgv
       61 qgpdlmqrfq ehaarfdtef vydhissvdl skrpftlngd sgevytcdal iiatgasaqy
      121 lglpseqafm grgvsgcatc dgffykkqnv vvvgggntav eealylsnic ntvtvihrrd
      181 kfraepilid kmmdkvnngn mrlklfyelq evlgddsgvt gvrilnnqtg qtedlavtga
      241 fiaighkpnt gifegqlkme ngyivtqsgl sgmatqtsvp gvfaagdvqd hvyrqaitsa
      301 gtgcmaalda qrwlenggq
//
LOCUS       WP_123642799             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Histidinibacterium lentulum].
ACCESSION   WP_123642799
VERSION     WP_123642799.1
KEYWORDS    RefSeq.
SOURCE      Histidinibacterium lentulum
  ORGANISM  Histidinibacterium lentulum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Histidinibacterium.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Histidinibacterium lentulum"
                     /db_xref="taxon:2480588"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55302
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeil pgearvamtp asagmlqklg yqcvieagag lasgftdaay aeagvevvad
       61 aealwaaaei vakvrpptee eaarlregql lisffypasn ealmetaraq gasviamdmv
      121 prisraqkmd alssmaniag yravieagne fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvflefee selpdgsatg gyappsspef
      241 qakqlekfre iapdmdivit talipnrpap vlwtkdmvea mkpgsvivdl aaerggncel
      301 tvkdekvvtd ngvtilgytd lnsrmatqss tlyatnirhm mtdltpekdg tvvhnmeddv
      361 irgativhag eitypppppk vaaiaaqpkk dkpkeltaee kraqevaafr aqtrsqvall
      421 svlavlllav glvapasfma qfiifilavf vgfqviwgva hslhtplmav tnaissiiil
      481 galiqvgaes vlitilaaag ilmaavnifg gflvtrrmla mfqks
//
LOCUS       WP_123666698             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinocorallia herbida].
ACCESSION   WP_123666698
VERSION     WP_123666698.1
KEYWORDS    RefSeq.
SOURCE      Actinocorallia herbida
  ORGANISM  Actinocorallia herbida
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinocorallia.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Actinocorallia herbida"
                     /db_xref="taxon:58109"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52619
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvtreqt getrvaatpa tvrqlvglgy dvvveagaga lsaftdaayi eagagigtae
       61 dgwgadvvlr vngpavgeag rlkegallis tlapalnpdl vdelaardvt alamdavpri
      121 sraqsldvls smaniagyra vveaahefgr fftgqvtaag kvppakvlva gagvaglaai
      181 gaasslgaiv ratdprpeva eqvkslggef lpvlvdeeaq qssdgyakat selydeaaak
      241 lyadqaadvd ivittalipg rpaprlitaa dvaamkpgsv ivdmaaamgg nvegsvpgek
      301 ivteggvtil aytdlagrlp tqasqlygtn ivnllklltp dkdgevvldl ddvvqrgmtv
      361 vratgwgrse tlwppppvqi saapaaapaq aeapvgrekk plsaaaklam vftatglfgl
      421 vtafapapip qhftvltlav vigyyvigkv hhalhtplms vtnavsgviv vgalvqvgld
      481 vpliqvlagv aillasinif ggfavtrrml tmfskgn
//
LOCUS       WP_123669638             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinocorallia herbida].
ACCESSION   WP_123669638
VERSION     WP_123669638.1
KEYWORDS    RefSeq.
SOURCE      Actinocorallia herbida
  ORGANISM  Actinocorallia herbida
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinocorallia.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Actinocorallia herbida"
                     /db_xref="taxon:58109"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33168
     Region          7..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttdirdvii igsgpagyta aiyaaradlk plvfegsisa ggalmnttdv enfpgfpdgi
       61 mgpdlmdnlr kqaerfgael vtddvtevdl tgnpkvvkvg eeyhyakavi iatgsgyrel
      121 glpnekrlsg rgvswcatcd gfffrdqnia vvgggdtale eaifltkfan vtvihrrdtl
      181 raskimqera lanekitflw dsevidvlge dkvksvrvrn tkngeegsld vtglfiaigh
      241 dprselfkgq ldlddegylq vehpttktkl agvfacgdvv dhvyrqaita aasgcsaaid
      301 aerylqeg
//
LOCUS       WP_123671305             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Curtobacterium sp. PhB172].
ACCESSION   WP_123671305
VERSION     WP_123671305.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. PhB172
  ORGANISM  Curtobacterium sp. PhB172
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Curtobacterium sp. PhB172"
                     /db_xref="taxon:2485196"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34453
     Region          4..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqliiigsg pagftagiya araelkpliv assvetggel tkttevenfp gfpegiqgpd
       61 lmikmqeqae kfgaevlydd aisvdltgdv kkvtvgsget yealaviyat gsayrhlgia
      121 deerlsghgv swcatcdgff frqkniavvg ggdsameeat fltrfadkvt vihrkdtlra
      181 skimqdrahn dpkiefawnk evigiqgdsa vtgvtlkdtv dgteselald glfiaigndp
      241 rvhlvhgqle lapegtiave grtskavgvp gvfvagdvld htyrqaitaa gsgavaalda
      301 ekyladledt ltdaaagetp vepvtisa
//
LOCUS       WP_123663208             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Candidatus Cardinium hertigii].
ACCESSION   WP_123663208
VERSION     WP_123663208.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Cardinium hertigii
  ORGANISM  Candidatus Cardinium hertigii
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Amoebophilaceae; Candidatus Cardinium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Candidatus Cardinium hertigii"
                     /db_xref="taxon:247481"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33693
     Region          8..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msnqpvqlvi igggpagyta alyaaraglh pilyqgpqpg gqltitgdve nypgyrngvm
       61 gavmmedfqa qaerfgtiik egsitkvdfs iyprllivds gehvlarsvi iatgasakwl
      121 glpsekrfyg kgvsacavcd gfffknetvv vvgggdtaaq eslylaklck tvhllvrkgq
      181 mraskimqer vfkrsnieiw fhtevkevlg qtvveaievi htlskkitti patgffvaig
      241 hqpnslpffp ymavdsqgyi qiqpgttktn isgifaagdv qdahyrqavt aagtgcmaal
      301 daehflqnye dii
//
LOCUS       WP_123680392             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Curtobacterium sp. PhB115].
ACCESSION   WP_123680392
VERSION     WP_123680392.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium sp. PhB115
  ORGANISM  Curtobacterium sp. PhB115
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Curtobacterium sp. PhB115"
                     /db_xref="taxon:2485173"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34915
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqliiigsg pagftagiya araelkpliv assvetggel tkttevenfp gfpegiqgpd
       61 lmikmqeqae kfgaevlydd avsvdltgdv kkvtvgsget yealaviyat gsayrhlgla
      121 deerlsghgv swcatcdgff frqkniavvg ggdsameeat fltrfadkvt vihrkdslra
      181 skimqdramn dpkiefawnk evtgitgdsa vtgvtlrdtv dgseselald glfiaigndp
      241 rthlihgqid iapegtiavq grssktnlpg vfaagdvidp tyrqaitaag sgtvaaldae
      301 kyladledtl tdqaegvtpv epvtvdvtsr v
//
LOCUS       WP_123682919             506 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis thermoflava].
ACCESSION   WP_123682919
VERSION     WP_123682919.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis thermoflava
  ORGANISM  Amycolatopsis thermoflava
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis; Amycolatopsis
            methanolica group.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Amycolatopsis thermoflava"
                     /db_xref="taxon:84480"
     Protein         1..506
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51218
     Region          1..505
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligilreta pretrvaatp rtigqlrglg ydvvveagag mrsgfpdday eeagarigda
       61 caadvvlavn appaerlsal rpgatliglv dprgdrarva dlakrhltvl amdavprisr
      121 aqsmdvlssm anlagyravi eaahefgrpf tgqvtaagki pparvfvvga gvaglaaiga
      181 asalgavvra fdvrpevaeq vrsmgaefvt vgltgastad gyaaemtaaq erataamyde
      241 earnadivit talvpgrpap kligartvaa margsvivdl aaanggncgl tvpgerttte
      301 sgvtvlgytd laarlpaqas qlygtnvvnl vrlmtpgadg rlvvdfddvv irsmtvvrdg
      361 eltwppppvp vsaaspaaap gtvqaaepra pltpaarlgi vaaaavvvfg liaiaperlq
      421 qhlvvfalav vvgfavignv ahalhtplms vtnaisgiiv vgallqaggg savttalsav
      481 avlvagldia ggfavtrrml amftrg
//
LOCUS       WP_123694207             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Allostella
            humosa].
ACCESSION   WP_123694207
VERSION     WP_123694207.1
KEYWORDS    RefSeq.
SOURCE      Allostella humosa
  ORGANISM  Allostella humosa
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Allostellaceae; Allostella.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Allostella humosa"
                     /db_xref="taxon:94"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39946
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklailkerr pgearvaasp dsvkrlvalg ftvaveadag rsaampdday atagativad
       61 ratlladadv vlkvqrpthg tdgtvdelsa mrrgtvlvgm lapyaepdll rlyaergida
      121 famellprit raqtmdvlss qanlagyrav leaahvygka fpmmmtaagt vaaarvfvmg
      181 agvaglqaia tarrlgaivt atdvrpaake qveslgakfv avedeefkqa etaagyakem
      241 saayrakqae lvaqhiakqd ivittalipg rpapklitae mvaamkpgav vvdlaveqgg
      301 ncagsrpdei avtdggvsiv gwtntasria vdasqlyarn lvafltplvd kasgtlkidt
      361 adeivkatll trggaivhpa fagqgg
//
LOCUS       WP_123694217             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Allostella humosa].
ACCESSION   WP_123694217
VERSION     WP_123694217.1
KEYWORDS    RefSeq.
SOURCE      Allostella humosa
  ORGANISM  Allostella humosa
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Allostellaceae; Allostella.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Allostella humosa"
                     /db_xref="taxon:94"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34710
     Region          8..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maqrhhskvl iigggpagyt aaiyaaranl qpmlvegmqp ggqlmittdv enypgfadvi
       61 qgpwlmeqmr rqaehvgtrl vgdlivscdl sqrpfraigd sgdeytadsi viatgaqarw
      121 lglpseeryr gagvsacatc dgfffrgrkv avvgggntav eealyltnha sevvlihrrd
      181 rlraekilqd rlfrhpkvrv iwnavvdeil gegtppgvtg vrlnhvdsge qstleldgvf
      241 vaightpvte lfqgqlalds egyiltrads tatdipgvfa agdvrdkiyr qavtaaglgc
      301 maaleaerwl aeaedelskq aad
//
LOCUS       WP_123696685             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Agrococcus jenensis].
ACCESSION   WP_123696685
VERSION     WP_123696685.1
KEYWORDS    RefSeq.
SOURCE      Agrococcus jenensis
  ORGANISM  Agrococcus jenensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Agrococcus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Agrococcus jenensis"
                     /db_xref="taxon:46353"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33846
     Region          2..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhdliiigsg pagftaaiya aranlkpivl assvemggdl mtttdvenfp gfpegiqgpd
       61 lmfamqqqae rfgadvrmqd vtdleldgev krvhvgdevl earavifatg sayrklgidg
      121 eerlsghgvs wcatcdgfff kqkqlivvgg gdsameeanf ltkfadkvti vhrsetfras
      181 evmldrsran ekiefvtnaf vesiegeaqv savtlrdrit getsrmpidg vfvaigsdpr
      241 thlvhgklel taegtiavgg rssrtsvegv faagdvidpt yrqavtaaas gtvaaldaeh
      301 ylaahavpvl vtspeeaal
//
LOCUS       WP_123700999             328 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Curtobacterium].
ACCESSION   WP_123700999
VERSION     WP_123700999.1
KEYWORDS    RefSeq.
SOURCE      unclassified Curtobacterium
  ORGANISM  unclassified Curtobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="unclassified Curtobacterium"
                     /db_xref="taxon:257496"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34390
     Region          4..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqliiigsg pagftagiya araqlkpliv assvetggel tkttevenfp gfpegiqgpd
       61 lmikmqeqae kfgaevlydd avsveltgdv kkvtvgsget yealaviyat gsayrqlgla
      121 deerlsghgv swcatcdgff frqkniavvg ggdsameeat fltrfadkvt vihrkdtlra
      181 skimqdrain dpkiefawnk evvgitgasa vegvtlkdtv tgetselald glfiaigndp
      241 rvhlvhkqlq lapegtiave grtskavgvp gvfvagdvld htyrqaitaa gsgavaalda
      301 ekfladlddt ltsaaegetp aepvtisa
//
LOCUS       WP_123706120             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rathayibacter sp. PhB127].
ACCESSION   WP_123706120
VERSION     WP_123706120.1
KEYWORDS    RefSeq.
SOURCE      Rathayibacter sp. PhB127
  ORGANISM  Rathayibacter sp. PhB127
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Rathayibacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rathayibacter sp. PhB127"
                     /db_xref="taxon:2485176"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34104
     Region          3..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrdiviigsg pagwtaaiya aradlhpvvv assveiggdl mnttdvenfp gfpdgvlgpe
       61 lmtamqkqae kfgaetfydd vvsldleget ktihlgsges ieaktvvvat gsayrklglh
      121 dedrlsghgv swcatcdgff fkgktiavvg ggdsameeat fltkfaekvy vihrkdslra
      181 skvmqkrard nekiefvwnt evtgitgenh vngvklrdtv dgteskleld glfiaigndp
      241 rthivhgkld lttdgtiavt grssqtsvag vfaagdvidp tyrqavtaaa sgtvaaldae
      301 hylaaltdgi astegtpaae lltl
//
LOCUS       WP_123710552             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinobacterium caligoides].
ACCESSION   WP_123710552
VERSION     WP_123710552.1
KEYWORDS    RefSeq.
SOURCE      Sinobacterium caligoides
  ORGANISM  Sinobacterium caligoides
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Sinobacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Sinobacterium caligoides"
                     /db_xref="taxon:933926"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33629
     Region          9..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetihhpli ilgsgpagyt aavyaaranl npvvitgmqq ggqlttttev dnwpggqegl
       61 qgpelmmkmq ehaerfdtqi vfdhiestdl asapftlvgn nntytcdsli iatgasaqyl
      121 glpseeafmg kgvsacatcd gffyrgkkva vigggntave ealylsniaa evtlvhrrds
      181 lrsekilqdk ikdraengni nilwnntlne vlgddtgvtg leltstldgs kqkidvdgvf
      241 iaighkpntd ifkgqlemkd gylkinsgte gnatqcsveg vfaagdvadh iyrqaitsag
      301 fgcmaaldae ryldnq
//
LOCUS       WP_123710867             378 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinobacterium caligoides].
ACCESSION   WP_123710867
VERSION     WP_123710867.1
KEYWORDS    RefSeq.
SOURCE      Sinobacterium caligoides
  ORGANISM  Sinobacterium caligoides
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Cellvibrionales; Spongiibacteraceae; Sinobacterium.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Sinobacterium caligoides"
                     /db_xref="taxon:933926"
     Protein         1..378
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40506
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigipketl sdetrtslip ssvkrltdqg aevvfeaglg lrlgiedsey idagakvstd
       61 rdqllasadm vlrlrkpald eiaklkkgsi hisfldpfne helvdafaah qitaismemi
      121 prttraqkmd alssqaslag yamvilaaer ldkilpmmmt pagtispsrv fiigagvagl
      181 qavatakrlg arvdafdtrp vvkeqveslg gkfveidlgd tgqteggyak altpeqielq
      241 rlgqkkvmaq adivittaql fgrkapivvt tdmveamkpg svivdlaves ggnvegsvag
      301 eevihngvki igltnmpghv amnasqmysa nlhnlvleyw dkeqasfdlk ldddilkgci
      361 ithdgelvnd miknsrak
//
LOCUS       WP_123716754             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_123716754
VERSION     WP_123716754.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38721
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag vkasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avsadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123722030             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase
            [Gammaproteobacteria].
ACCESSION   WP_123722030
VERSION     WP_123722030.1
KEYWORDS    RefSeq.
SOURCE      Gammaproteobacteria (g-proteobacteria)
  ORGANISM  Gammaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Gammaproteobacteria"
                     /db_xref="taxon:1236"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33928
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mteakhsrli ilgsgpagys aavyaaranl kpvvitgiqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtakl qqhpfeligd sgtytcdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlihrrdk
      181 lrsekilqdk lfekaangni rlhwnqnlde vlgdasgvtg arlrhshtge tnelplagvf
      241 iaighkpntd lfqgqlkmrd gyllvkggse gdatatdieg vfaagdvadh iyrqavtsag
      301 agcmaaldae kylddiptv
//
LOCUS       WP_123723802             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas protegens].
ACCESSION   WP_123723802
VERSION     WP_123723802.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas protegens
  ORGANISM  Pseudomonas protegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas protegens"
                     /db_xref="taxon:380021"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38683
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigna
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_123729242             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Stenotrophomonas rhizophila].
ACCESSION   WP_123729242
VERSION     WP_123729242.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas rhizophila
  ORGANISM  Stenotrophomonas rhizophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Stenotrophomonas rhizophila"
                     /db_xref="taxon:216778"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34204
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msnskhsrll ilgsgpagwt aavyaaranl kpvvitglqq ggqlmtttev dnwpgdahgl
       61 mgpdlmtrmq ahaerfetev ifdhihtadv sqrpfkligd saeytcdali iatgatakyl
      121 gipseeafkg rgvsacatcd gffyrdqdvv vvgggntave ealylsniar kvylvhrrdt
      181 lkaekimqdk lfakveagki etvwhhqvde vlgneagvtg vrvkstldgs trdieahgff
      241 vaighhpnts lfdgqltmnn gyldirsglg gnatqtsveg vfaagdvadq hyrqaitsag
      301 fgcmaaldae ryldakgqas
//
LOCUS       WP_123731439             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rathayibacter sp. PhB152].
ACCESSION   WP_123731439
VERSION     WP_123731439.1
KEYWORDS    RefSeq.
SOURCE      Rathayibacter sp. PhB152
  ORGANISM  Rathayibacter sp. PhB152
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Rathayibacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rathayibacter sp. PhB152"
                     /db_xref="taxon:2485190"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34103
     Region          3..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrdiviigsg pagwtaaiya aradlhpvvv assveiggdl mnttdvenfp gfpdgvlgpe
       61 lmtamqkqae kfgaetfydd vvsldleget ktihlgsges ieaktvvvat gsayrklglh
      121 dedrlsghgv swcatcdgff fkgktiavvg ggdsameeat fltkfaekvy vihrkdslra
      181 skvmqkrard nekiefvwnt evtgitgenh vngvklrntv dgteskleld glfiaigndp
      241 rthivhgkld lttdgtiavt grssqtsvag vfaagdvidp tyrqavtaaa sgtvaaldae
      301 hylaaltdgi astegtpaae lltl
//
LOCUS       WP_123736143             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Rathayibacter].
ACCESSION   WP_123736143
VERSION     WP_123736143.1
KEYWORDS    RefSeq.
SOURCE      Rathayibacter
  ORGANISM  Rathayibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rathayibacter"
                     /db_xref="taxon:33886"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34089
     Region          3..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrdiviigsg pagwtaaiya aradlhpvvv assveiggdl mnttdvenfp gfpdgvlgpe
       61 lmtamqkqae kfgadtfydd vvsldleget ktihlgsges ieaktvvvat gsayrklglh
      121 dedrlsghgv swcatcdgff fkgktiavvg ggdsameeat fltkfaekvy vihrkdslra
      181 skvmqkrard nekiefvwnt evtgitgenh vngvklrntv dgteskleld glfiaigndp
      241 rthivhgkld lttdgtiavt grssqtsvag vfaagdvidp tyrqavtaaa sgtvaaldae
      301 hylaaltdgi astegtpaae lltl
//
LOCUS       WP_123738807             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Salana multivorans].
ACCESSION   WP_123738807
VERSION     WP_123738807.1
KEYWORDS    RefSeq.
SOURCE      Salana multivorans
  ORGANISM  Salana multivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Beutenbergiaceae; Salana.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Salana multivorans"
                     /db_xref="taxon:120377"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35136
     Region          8..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeptvqdvv ivgsgpsgyt aaiyaaragl apvvfagsit aggalmntte venfpgfptg
       61 vmgpdlmehm aeqagrfgad iryedvesve lhgpvktitt aegetvqars vilatgsayk
      121 elglpdekrl sgrgvswcat cdgfffrdqd ivvvgggdsa meeatfltrf arsvtvvhrr
      181 gelraskimv dratadpkis fawysevaai hgedkvtgvt lrdvrtgeer elpatglfva
      241 ighlprtell kgqidlddag yvivehptta tnlpgvfaag dvvdhlyrqa itaagtgcaa
      301 aldaerylaa lddaatqghp eaaaeevrev eavl
//
LOCUS       WP_123740191             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Salana
            multivorans].
ACCESSION   WP_123740191
VERSION     WP_123740191.1
KEYWORDS    RefSeq.
SOURCE      Salana multivorans
  ORGANISM  Salana multivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Beutenbergiaceae; Salana.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Salana multivorans"
                     /db_xref="taxon:120377"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52785
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mnlgvpratl tgastvaatp ptvralrklg ydvlveagag araslpdaly etegamltda
       61 agawgadvvl lvqpltvddv nrlspgaavi apmapaanpq lvtalaargv talaldavpr
      121 israqaldil stnsniagyr avieaaeays gmfggqvtaa gktapatvfv igagvaglaa
      181 igaasslgaq vrafdvrpea geqiasmggt pvvapqaqqe iaadgyakpl tpeqqaaamd
      241 vyaaetatad vvittalvrg sapttitsam veamrpgsvi vdlaasgggn ceetepgeri
      301 vtrggvtiig drdltaampr htsqllgtni vnlltlmtpg kdgqlvldld dvvvrgmtvt
      361 agdevlwppp pvqvsaapaa ttapaptaee laaraaaaee aargrarrrm lwyalgavll
      421 alglsfspga flghfwifal avvigfyvis qvshslhtpl maqtnaisgi ilvgallqlg
      481 sdnpwvtgla fvaaavasin ifggflvtyr mlgmfrtgda k
//
LOCUS       WP_123743520             365 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Saccharothrix texasensis].
ACCESSION   WP_123743520
VERSION     WP_123743520.1
KEYWORDS    RefSeq.
SOURCE      Saccharothrix texasensis
  ORGANISM  Saccharothrix texasensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharothrix.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Saccharothrix texasensis"
                     /db_xref="taxon:103734"
     Protein         1..365
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38087
     Region          1..358
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,284,310,312)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,274..275,317..318,322,
                     325..326)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,224,235,
                     252..254,261,263)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrvgipvear paerrvaglp etvttligag ltvdvqagag rhahasdaay raaganviad
       61 hpagqsdviv svqpptpeqa aalregdvti sflqpnaepe lievlkarkv tafsldllpr
      121 vtraqaadal ssqalvagyr avleaanrlp rflpmfttaa gtippakvlv lgagvaglqa
      181 iatarrlgav veaydvraaa kdevkslgar fleldletqq gvyaeaqset flerqrelia
      241 ervaasdvvi staaipgrka pvlvtndmlk amapgsvvvd laaesggnvt asspgeetwv
      301 gevlvygaln mpsgmpvhas rlyarnvanl lmmmtedgqv vpdltdevls gcclthagel
      361 rrelr
//
LOCUS       WP_123744839             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Saccharothrix texasensis].
ACCESSION   WP_123744839
VERSION     WP_123744839.1
KEYWORDS    RefSeq.
SOURCE      Saccharothrix texasensis
  ORGANISM  Saccharothrix texasensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharothrix.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Saccharothrix texasensis"
                     /db_xref="taxon:103734"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35427
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnlivv gsgpagytaa vyaaraqlep lvfegsqygg almttteven ypgfrdgimg
       61 pdlmeqmreq akrfgaelra edvegleldg pvkyvtangk ryaarsvila mgaaarylhv
      121 pgeqellgrg vsscatcdgf ffrdqdiavi gggdsameea tfltkfartv tiihrreefr
      181 askimlerar snekikwlln aevvevlgqd agtvsgvktr dtrtgevseh pftgffvaig
      241 hdprselvkg qveldgegyv qvvgrtthtn vdgvfgagdl vdhtyrqait aagsgcaaai
      301 daerwlaehg tteaavtaeh vgggygepvs ts
//
LOCUS       WP_123766531             336 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mycobacterium avium].
ACCESSION   WP_123766531
VERSION     WP_123766531.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium avium
  ORGANISM  Mycobacterium avium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            avium complex (MAC).
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Mycobacterium avium"
                     /db_xref="taxon:1764"
     gene            1..336
                     /gene="trxB"
     Protein         1..336
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35145
     Region          7..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtadtvhdvi iigsgpagyt aalytaraql apvvfegtsf ggalmtttav enypgfrdgi
       61 tgpelmdqmr eqalrfgadl rmedvesvsl agpvksvtta egetvrarav ilamgaaary
      121 lgvpgeqdll grgvsscatc dgfffkdqdi avigggdsam eeatfltrfa rsvtlvhrre
      181 efrasrimle rarandkiti vtnkaveave gsetvtglrl rdtvtgetst lavtgvfvai
      241 ghdprselvr dvldtdpdgy vlvqgrttat sipgvfaagd lvdrtyrqav taagsgcaaa
      301 idaerwlaeh aessaaaqgd atefpgstdt ligapq
//
LOCUS       WP_123769177             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vulcaniibacterium tengchongense].
ACCESSION   WP_123769177
VERSION     WP_123769177.1
KEYWORDS    RefSeq.
SOURCE      Vulcaniibacterium tengchongense
  ORGANISM  Vulcaniibacterium tengchongense
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Vulcaniibacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Vulcaniibacterium tengchongense"
                     /db_xref="taxon:1273429"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33820
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtpskhsrvi ilgsgpagwt aavyaaranl kpvvitglqm ggqlmtttev dnwpgdahgl
       61 mgpdlmarmq ahaerfdtev vfdhihtadl srrpfrlvgd sgeytcdali vatgatakyl
      121 glpseelykg rgvsacatcd gffykeqdva vigggntave ealylsniar kvylvhrrdt
      181 lraekimqdk lfakvqagki epvwhhvvde vlgndagvtg vrvksvqdgg treipihglf
      241 vaightpnts lfegqlemkn gyivirtgld gnatatsvpg vfaagdvadq vyrqaitsag
      301 fgcmaaldae kfldkge
//
LOCUS       WP_123777392             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Shewanella frigidimarina].
ACCESSION   WP_123777392
VERSION     WP_123777392.1
KEYWORDS    RefSeq.
SOURCE      Shewanella frigidimarina
  ORGANISM  Shewanella frigidimarina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Shewanella frigidimarina"
                     /db_xref="taxon:56812"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33950
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msearhvnll ilgsgpagyt aavyaaranl npvmitgmqq ggqlttttev enwpgdaedl
       61 tgpalmermq khaekfdtei ifdhinevtl terpfrlkgd ngeftcdali iatgasakyl
      121 glpseeafmg rgvsacatcd gffyrnqkva vigggntave ealylsnias evhlihrrds
      181 frsekilinr lmdkvangni ilhldqtlee vtgndmgvtg lkkkstkdgs vtdlevagvf
      241 vaighspntg ifagqlemnh gylqvnsglq gnatqtsieg vyacgdvmdq hyrqaitsag
      301 tgcmaaldae ryldakk
//
LOCUS       WP_123780873             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            ponticus].
ACCESSION   WP_123780873
VERSION     WP_123780873.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ponticus
  ORGANISM  Vibrio ponticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio ponticus"
                     /db_xref="taxon:265668"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52665
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnklhwiqks vaalvivass visaastaas enkalidprn dayqqqhpdq yhswkatses
       61 eaiddaladd pnmvilwagy gfakdynkar ghfyalddvr qtlrtggptd ensgpmpmac
      121 wsckspdvgr videqgedgy fsgkwakggn qianpigcad chdtrsdgfk ngepalalak
      181 pyverafvai dkpfdkqsrl dqqasvcgqc hveyyftgxt kavkfpwdmg ttvedmekyy
      241 dalgfkdwth kvskapmlka qhpgyetwrd gihgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfed tcanchtqsk eqmleivntr kgqvhnmklt aekqivaahf eagaawdaga
      361 teaemadilq dirhaqwrwd yaiashgvhm hapevalevl gtavdkaada rtklvrllak
      421 kgitdpielp distkekaqq algmdmeamn aekkhfletv vpewdkqake resqy
//
LOCUS       WP_123781747             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            gonorrhoeae].
ACCESSION   WP_123781747
VERSION     WP_123781747.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53544
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwvcpliy kvnapsegel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldflqes ggggdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaatgg nceltrpgel
      301 svtgngvkii gytdmanrla gqssqlyatn lvnltkllsp nkdgeitldf edviirnmtv
      361 trdgeitfpp ppiqvsarpq qtpsekaapa akpepkpvpl wkklapaaia avlvlwvgav
      421 apaaflnhfi vfvlacvigy hvvwnvshsl htplmsvtna isgiivvgal lqigqgngfv
      481 sllsfvaili aginifggfa vtrrmlnmfk kg
//
LOCUS       WP_123782964             475 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            ponticus].
ACCESSION   WP_123782964
VERSION     WP_123782964.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ponticus
  ORGANISM  Vibrio ponticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Vibrio ponticus"
                     /db_xref="taxon:265668"
     gene            1..475
                     /gene="nrfA"
     Protein         1..475
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52763
     Region          1..475
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnklhwiqks vaalvivass visaastaas enkalidprn dayqqqhpdq yhswkatses
       61 eaiddaladd pnmvilwagy gfakdynkar ghfyalddvr qtlrtggptd ensgpmpmac
      121 wsckspdvgr videqgedgy fsgkwakggn qianpigcad chdtrsdgfk ngepalalak
      181 pyverafvai dkpfdkqsrl dqqasvcgqc hveyyftgpt kavkfpwdmg ttvedmekyy
      241 dalgfkdwth kvskapmlka qhpgyetwrd gihgknkvvc vdchmpkvtk edgtvytdhk
      301 vgnpfdrfed tcanchtqsk eqmleivntr kgqvhnmklt aekqivaahf eagaawdaga
      361 teaemadilq dirhaqwrwd yaiashgvhm hapevalevl gtavdkaada rtklvrllak
      421 kgitdpielp distkekaqq algmdmeamn aekkhfletv vpewdkqake resqy
//
LOCUS       WP_123783159             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vibrio ponticus].
ACCESSION   WP_123783159
VERSION     WP_123783159.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ponticus
  ORGANISM  Vibrio ponticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Vibrio ponticus"
                     /db_xref="taxon:265668"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34519
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msnvkhcnll ilgsgpagyt aavyaaranl kpvlvtgmqq ggqlttttev enwpgdpegl
       61 tgpalmdrmk ehaerfetem lfdhinqvdf sqrpfrlfgd sgeytcdali istgasakyl
      121 gleseeafkg rgvsacatcd gffyrnqkva vvgggntave ealylsnias evhlvhrrds
      181 fraekilvkr lmdkvengni ilhtdrtlee vvgddmgvtg vrlkhtqsda ieelevmgaf
      241 iaighqpntt ifdgqlemkd gyiivksgld gnatqtsveg ifaagdvmdh nyrqaitsag
      301 tgcmaaldae ryldsladka
//
LOCUS       WP_123790160             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia multivorans].
ACCESSION   WP_123790160
VERSION     WP_123790160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38968
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsvakgag taasypdeay aaagaeltdq
       61 saafgadivl kvlaptdael pslkrgavlv gmlepfnaeq aaklaatgvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmppswla
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqamk pgsvlvdlaa grgpevdgrk
      301 ggncpltvad qvivhngvti aghtnlasmv asdasalyar nlldfmkliv tkegvlnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_123783256             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            ponticus].
ACCESSION   WP_123783256
VERSION     WP_123783256.1
KEYWORDS    RefSeq.
SOURCE      Vibrio ponticus
  ORGANISM  Vibrio ponticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio ponticus"
                     /db_xref="taxon:265668"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54666
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp ksveqliklg fdvvvesqag elasfdnasf easgakvvsk
       61 deawnsdiif kvnapivdne ngvdeiaqln dgatlvsfiw paqnpelmeq lsskninvma
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv qsmgaeflev dfqensgsgd gyakemsdef
      241 nkkaaelyae qakdvdiivt talipgrpap klitkemvds mkagsvivdl aaanggncey
      301 tvadqvitta ngvkvvgytd mvgrlptqss qlyatnlvnl mkllckekdg nididfedvv
      361 lrgvtvvkeg evtwpappiq vsaqpeqkpq sapapekkvd epvspvkkli glgvavtafg
      421 wvasvapaaf lahftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvtflsf iavliasini fggftvtkrm lemfrkdr
//
LOCUS       WP_123791323             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pacificibacter maritimus].
ACCESSION   WP_123791323
VERSION     WP_123791323.1
KEYWORDS    RefSeq.
SOURCE      Pacificibacter maritimus
  ORGANISM  Pacificibacter maritimus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Pacificibacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Pacificibacter maritimus"
                     /db_xref="taxon:762213"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55409
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkelf egearvaltp dsakqlqklg ydclietgag alagfadkdy ndagvevvkt
       61 aaalwkaadi vakvrqpnea elkrltkgkt lisffnpaan dagmeaaksk ganviamemv
      121 prisraqkmd alssmaniag yravieasnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqvesmg aefvyldfee eqadgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvsam kpgsvivdla aekggncklt
      301 vmdekivten gvtiigytdf psrmaaqast lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgatvtyage itfpppppki aaiaakpkea vkeltpeekr aeevaafkkq tknqvtllav
      421 ggalllavgl vapasfmqhf ivfvlsvfig fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_123793154             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pacificibacter maritimus].
ACCESSION   WP_123793154
VERSION     WP_123793154.1
KEYWORDS    RefSeq.
SOURCE      Pacificibacter maritimus
  ORGANISM  Pacificibacter maritimus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Pacificibacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pacificibacter maritimus"
                     /db_xref="taxon:762213"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33640
     Region          7..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetkhtkvl iigsgpagyt agvyasraml epllvqgiep ggqlttttev enwpgekeiq
       61 gpelmvnmqe haaamgceik qdiitsldtt vrpfvamgds gttytadavi latgarakwl
      121 glpseeafkg fgvsacatcd gffyrgmeiv vigggntave ealfltnfas kvtlihrrds
      181 lrcekilenr lfknekievl wdhelvevyg deapmkgvng vrakhvktge ikdipakgvf
      241 vaighapase lvsdvlethn ggyvkvtpgt smtsipgifa agdltdhtyr qavtsagmgc
      301 maaldaerfl aeqdda
//
LOCUS       WP_123795864             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria animalis].
ACCESSION   WP_123795864
VERSION     WP_123795864.1
KEYWORDS    RefSeq.
SOURCE      Neisseria animalis
  ORGANISM  Neisseria animalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Neisseria animalis"
                     /db_xref="taxon:492"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33711
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msqhhkliil gsgpagytaa vyaaranlnp viitgiqqgg qlmtttevdn wpadaegvqg
       61 pelmarflah aerfgtemif dqihtaqlqq rpfkligdmg eytcdaliia tgasakylgl
      121 pseetfagkg vsacatcdgf fyrnqpvavv gggntaveea lylaniaetv tlihrrdsfr
      181 aekimveklm krveegkiil klnanldeil gddkgvngar lkyndgssed isvqgvfiai
      241 ghkpntdifk gqldmdetgy lktkggtgdn vgltniegiw aagdvkdhty rqaitsaasg
      301 cqaaldaerw ldsqa
//
LOCUS       WP_123799706             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Limosilactobacillus fermentum].
ACCESSION   WP_123799706
VERSION     WP_123799706.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus fermentum
  ORGANISM  Limosilactobacillus fermentum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Limosilactobacillus fermentum"
                     /db_xref="taxon:1613"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33413
     Region          9..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeekqmnyd vvvigagpgg mtaamyasra nlsvllldrg iyggnlnnta tienytgfkt
       61 vqgpelaqnm ydgatqfgat ygygtvtalt vnedgtksvt tdmgdtfiak avviatgsdq
      121 rklgapgeqe ysgrgvsyca vcdgaffrnk hlivvgggds aveegmyltq fadkvivlvr
      181 hdhlkaqmva qerakkngqm efifntevte ikgddnkvtg vkthnnqtne dgyidadgvf
      241 vyvgvvpmts afkdlgilde rgwvktdekm atsvpgvyav gdvrntvlrq iatavgdgai
      301 agqqifnyis end
//
LOCUS       WP_123803677             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria weixii].
ACCESSION   WP_123803677
VERSION     WP_123803677.1
KEYWORDS    RefSeq.
SOURCE      Neisseria weixii
  ORGANISM  Neisseria weixii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Neisseria weixii"
                     /db_xref="taxon:1853276"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33785
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msnhhkliil gsgpagytaa vyaaranlnp viitgveqgg qlmtttevdn wpadaegvqg
       61 pelmarfqah aerfgtkmif dqihtvnlqn rpftlkgdmg eytcdaliia tgasakylgl
      121 pseetfagkg vsacatcdgf fyheqdvavv gggntaveea lylaniaktv tlihrretfr
      181 aekimvdklm krveegkiil klntnldevl gddmgvtgar lkhndgnien idvkgvfiai
      241 ghkpntdifk gqldmdatgy lktkggtadn vgatniegvw aagdvkdhty rqaitsaasg
      301 cqaaldaerw ldsptl
//
LOCUS       WP_123804684             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            weixii].
ACCESSION   WP_123804684
VERSION     WP_123804684.1
KEYWORDS    RefSeq.
SOURCE      Neisseria weixii
  ORGANISM  Neisseria weixii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria weixii"
                     /db_xref="taxon:1853276"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53888
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl agetrvactp atvaqlqklg fevvvehdag laasldnaay eaagavvada
       61 htvwqspliy kvnapaesei gllnagqtlv sflwpaqnse lvqkladkkv dvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvli igagvaglaa
      181 igtanslgav vkafdtrlev aeqiesmggq flkldfpqea gdngdgyakv mseefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkags vivdlaaatg gnceltkpge
      301 lfitdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeiald fedviirnmt
      361 vtregeitfp ppaiqvsaap qqtpsekaap aakpepkpvp awkklapavi gavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwdvshs lhtplmsvtn aisgiivvga llqigqghgf
      481 vsllafiavl iasinifggf yvtrrmlnmf rkg
//
LOCUS       WP_123805995             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria chenwenguii].
ACCESSION   WP_123805995
VERSION     WP_123805995.1
KEYWORDS    RefSeq.
SOURCE      Neisseria chenwenguii
  ORGANISM  Neisseria chenwenguii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Neisseria chenwenguii"
                     /db_xref="taxon:1853278"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33547
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mskhhkliil gsgpagytaa vyaaranlnp viitgieqgg qlmtttevdn wpadaegvqg
       61 pelmarflah aerfgtemvf dqihtvdlqn rpftlkgdmg eytcdaliva tgasakylgl
      121 pseetfagkg vsacatcdgf fykkqdvavv gggntaveea lylaniantv tlihrrdtfr
      181 aekimveklm krveegkivl klnaaleevl gddsgvtgvr lkfndgtsed iavkgvfiai
      241 ghkpntdifk gqldmdetgy lktkggtgdn vgatniegvw aagdvkdhty rqaitsaasg
      301 cqaaldaerw ldsln
//
LOCUS       WP_123807131             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Abyssicoccus albus].
ACCESSION   WP_123807131
VERSION     WP_123807131.1
KEYWORDS    RefSeq.
SOURCE      Abyssicoccus albus
  ORGANISM  Abyssicoccus albus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Abyssicoccaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Abyssicoccus albus"
                     /db_xref="taxon:1817405"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33727
     Region          6..303
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mtvdydvaii gagpagmtaa vyasranlkt vmlergmpgg qmanteeven fpgfdyisgp
       61 elsnkmfeha kkfgatyqya nieaiedrgd ykvlktsdke itattiiiat gaeykkmgip
      121 geeefggrgv sycavcdgaf fkgrelvvvg ggdsaveegi fltkfadkvt ivhrrdelra
      181 qkilqdrafk nekidfiydt tvekilgedn kvsgvilkdk nnqetrefka dgvfvyigmk
      241 plsqvvegln itnelgyiet ddkmhtaipg iyavgdvrnk tlrqivtatg dgsvaaieaq
      301 hyietlndk
//
LOCUS       WP_123808816             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Abyssicoccus albus].
ACCESSION   WP_123808816
VERSION     WP_123808816.1
KEYWORDS    RefSeq.
SOURCE      Abyssicoccus albus
  ORGANISM  Abyssicoccus albus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Abyssicoccaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Abyssicoccus albus"
                     /db_xref="taxon:1817405"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33525
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myktvilgtg pagltsaiyl aranmeplil egpepggqlt lttavenypg fsdpvmgpel
       61 ietmraqakr fgaqfktalv knvdfssrpf rlevdglgei qaesvivstg arakmleilg
      121 eaenfgrgvs tcatcdgfff rdkkvvvvgg gdsameealf ltkfakevhv ihrrdqlras
      181 kimqdramnn ekiswifnst pveilsqdsq vtgvrlknke tqeeqlietd gvflaighip
      241 nthflkgaid iypngyikve pgttktnipg vfaagdvqdq ryrqaitaag tgcmaamdve
      301 tfietnplt
//
LOCUS       WP_123811611             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lactobacillus crispatus].
ACCESSION   WP_123811611
VERSION     WP_123811611.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus crispatus
  ORGANISM  Lactobacillus crispatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Lactobacillus crispatus"
                     /db_xref="taxon:47770"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34183
     Region          5..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 madkydviii gagpggmtag lyaaranlki lvldrgpygg qmnntdaidn ypgfseikgp
       61 elsqkmydtm mkfkpdykyg nvqsveldge dklvktddgn eyrapiviia tgsdhkhlnv
      121 pgeeeysgkg vsycavcdaa ffkdedvavi gggdsaieeg iylsqlaksv tvihrrdqlr
      181 aqptlqkraf ankkmhfiwn aqteeilgdd mkvtgvkyrd ketgaekeip vagvfiyvgv
      241 lpqtepfkdl gilddhgwiv tddhmetkvp gifalgdvrq kdlrqianav gegsvagqaa
      301 ynyyqdlqdk kn
//
LOCUS       WP_123812771             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Myceligenerans xiligouense].
ACCESSION   WP_123812771
VERSION     WP_123812771.1
KEYWORDS    RefSeq.
SOURCE      Myceligenerans xiligouense
  ORGANISM  Myceligenerans xiligouense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Myceligenerans.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Myceligenerans xiligouense"
                     /db_xref="taxon:253184"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33946
     Region          8..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteeqtihdv viigsgpagy taavyaarag ltpvvlagsv taggalmntt evenfpgfpe
       61 avmgpdlmdn mraqaerfga qvvwddveqa elsgdvkvlt tglgdvyrar avilatgsay
      121 relglpdekr lsgrgvswca tcdgfffrdq hivvvgggds ameeatfltr faskvtvvhr
      181 rdelraskim adralndpki efawnsevtg iigedkvesv mlrdtvsgeq reldatglfv
      241 aigheprtdl vkgqvelden gyivvegrst rtnlpgvfas gdavdhtyrq aitaagsgca
      301 aaldaqayid tlndittpaa
//
LOCUS       WP_123813690             549 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Myceligenerans xiligouense].
ACCESSION   WP_123813690
VERSION     WP_123813690.1
KEYWORDS    RefSeq.
SOURCE      Myceligenerans xiligouense
  ORGANISM  Myceligenerans xiligouense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Myceligenerans.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Myceligenerans xiligouense"
                     /db_xref="taxon:253184"
     Protein         1..549
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54667
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipddag plvaatpsav grlcalgydv vvtegagaaa glpdddyrda galvvsdpav
       61 awesdvvvat vvpddvterm rpgstlvarl apaahpervr alaergital aldavprisr
      121 aqsldvlsvl snvagyravv eaaaeysgmf ggqvtaagst rpatvfviga gvaglaalga
      181 atalgarvra fdvrpevaeq iesmgaefvs epeaqqqisa dgyaapltee qlaaalrlyt
      241 reaaaadivi ttalvrgtap ttltaeavaa mrpgsvvvdl aapgggncel tvpgervlsg
      301 ngvvvlgytd lparmprhts elygtavanl ltlltpakdg earldlddvv qrgitvargg
      361 evlwpppavq vsaapaapat pptdtapgat gkaparprpa wldgalavaa avlgglavaa
      421 spaetvghit vlalaivvgf yvirsvthal htplmsqtna vsgiilvgal lqigsssllv
      481 tvlatiaaav asinvfggfl vtrrmlrmfr kaddgggavg agatgsngaa gaarstgatg
      541 vagttegsv
//
LOCUS       WP_123816787             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria gonorrhoeae].
ACCESSION   WP_123816787
VERSION     WP_123816787.1
KEYWORDS    RefSeq.
SOURCE      Neisseria gonorrhoeae
  ORGANISM  Neisseria gonorrhoeae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Neisseria gonorrhoeae"
                     /db_xref="taxon:485"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33505
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msqhrkliil gsgpagytaa vyaaranlnp viitgiaqgg qlmtttevdn wpadadgvqg
       61 pelmarflah aerfgteiif dqinavdlqk rpfalkgdmg eytcdaliva tgasakylgl
      121 pseeafagkg vsacatcdgf fyknqdvavv gggntaveea lylaniaktv tlihrrsefr
      181 aekimidklm krveegkiil klesnlqevl gddrgvngal lknndgsdqq iavsgifiai
      241 ghkpntdifk gqleideagy lktkggtadn vgatniegvw aagdvkdhty rqaitsaasg
      301 cqaaldaerw lgsqni
//
LOCUS       WP_123821449             330 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Petrotoga sp.
            HWH.PT.55.6.1].
ACCESSION   WP_123821449
VERSION     WP_123821449.1
KEYWORDS    RefSeq.
SOURCE      Petrotoga sp. HWH.PT.55.6.1
  ORGANISM  Petrotoga sp. HWH.PT.55.6.1
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Petrotogales;
            Petrotogaceae; Petrotoga.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Petrotoga sp. HWH.PT.55.6.1"
                     /db_xref="taxon:1307425"
     gene            1..>330
                     /gene="trxB"
     Protein         1..>330
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          18..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mffnvegank kseikqqydv viigggpagi saaiyalqgg astlviekai eggqmnltdi
       61 ienypgfkti kgeelsslmk ehaeqfgadf ydgkvielkd edshktvvme ngktikskai
      121 iiasgsyprk lgvkgeeefs srgvsycasc dghffknkki avvgggntav eeavylsnia
      181 kevyiihrre klradklyqd rafsrnnikf kwnsvieeik gkdkveslvi knlkndevye
      241 epfdgvfvfv glvpetsfln kdlfdfdeyg flitdenmet kvkgiyavgd vrkkelrqiv
      301 tavsdgaiaa shaireyvne dqisstqsin
//
LOCUS       WP_123823911             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_123823911
VERSION     WP_123823911.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53864
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwvcpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_123824331             363 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Kocuria soli].
ACCESSION   WP_123824331
VERSION     WP_123824331.1
KEYWORDS    RefSeq.
SOURCE      Kocuria soli
  ORGANISM  Kocuria soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Kocuria.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Kocuria soli"
                     /db_xref="taxon:2485125"
     gene            1..363
                     /gene="trxB"
     Protein         1..363
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=38268
     Region          36..340
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mspdftpalk ldlgatppgt aesdqqqvad gdstvhdvvi vgsgpagyta aiytgranlk
       61 pvviagsvta ggdlmqttev enypgftdgi mgpelmatmq aqaerfgadv ryedavklel
      121 dgevkkitve ggevlhaktv ilatgsayre lgledekrls ghgvswcatc dgfffkgqni
      181 avvgggdsai eeatfltkfa dkvtlihrrd efraseimqk rafddpkiei lwnkqvigis
      241 geskvqelsl edtvtgdvsa lpvtglfvai gsdprtdlfk dqveltpegt vavqgrsskt
      301 tlpgvfaagd vldptyrqav taagsgcvaa idvehylaeh saraqdqdql tapsaaqrsp
      361 lph
//
LOCUS       WP_123839507             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Enterococcus faecium].
ACCESSION   WP_123839507
VERSION     WP_123839507.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33349
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydvivigag pagmtaalya srsnlsvlmi eqgapggqmn ntaeienypg fdsimgpdla
       61 ykmyesvsrf gtenaygivq dikdhgshke vicedksyeg ktviiatgci hrklgvpgee
      121 efagrgvsyc avcdgaffrn krlvvigggd saveeaiylt qfasevvivh rrdelraqki
      181 iqdrafanek isfmwdtvvd eivgnemvvt gvkarnvktg nefdlaadgv fiyvgldplt
      241 apfreagltn eagwiptdne mktnmpsvfa igdvrekdlr qittavgdgg iagqqvykyl
      301 esleetta
//
LOCUS       WP_123840330             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Enterococcus faecium].
ACCESSION   WP_123840330
VERSION     WP_123840330.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33333
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydvivigag pagmtaalya srsnlsvlmi eqgapggqmn ntaeienypg fdsimgpdla
       61 ykmyesvsrf gtenaygivq dikdhgshke vicedksyeg ktviiatgci hrklgvpgee
      121 efagrgvsyc avcdgaffrn krlivigggd saveeaiylt qfasevvivh rrdelraqki
      181 iqdrafanek isfmwdtvvd eivgnemvvt gvkarnvktg nefdlaadgv fiyvgldplt
      241 apfreagltn eagwiptdne mktnmpgvfa igdvrekdlr qittavgdgg iagqqvykyl
      301 esleetta
//
LOCUS       WP_123848095             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chitinophaga lutea].
ACCESSION   WP_123848095
VERSION     WP_123848095.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga lutea
  ORGANISM  Chitinophaga lutea
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Chitinophaga lutea"
                     /db_xref="taxon:2488634"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33814
     Region          12..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mennttpehv hvliigsgpa gytaaiyaar anlkpvlyqg iqpggqltit tevenypgyp
       61 egiqgpemmv dfekqasrmg adirygmatk vdfssqpytv eideektita daiiiatgas
      121 akwlglpseq rlngsgvsac avcdgfffrg keaaivgagd taaeealyls kicsnvhmlv
      181 rrhemraskv mqdrvlktsn imvywntetl evtgenkvdg vrilntqtke ekvipvsaff
      241 vaighqpnsg ifagqldmde qgyiktipgt tktsvegvfa cgdvqdknyr qavtaagsgc
      301 maaldaeryl sakgh
//
LOCUS       WP_123848355             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga lutea].
ACCESSION   WP_123848355
VERSION     WP_123848355.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga lutea
  ORGANISM  Chitinophaga lutea
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Chitinophaga lutea"
                     /db_xref="taxon:2488634"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40337
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milavlkeka genrvslvpe vvkqivqqqv nvwveegagm qafypdeayr qagaeirpra
       61 ellqqadill sirhpaaedw knaspgkiwm gvyqplynat lmqewadkqf tvfsldtipr
      121 ttraqsmdvl ssqaniagyk avllaaytys ryfpmlmtaa gsippakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgak fvevegaada skaggyaveq saeykqkqeq
      241 kiaestakad ivittaqipg kpapilisra mvenmktgsv iidlaaatgg ntevtknget
      301 ilhngvtvig nsdlagtapa dasklyarnv lnflkliigk egaldlnfad dlvkgtcith
      361 hgeivndrvk qlqtatv
//
LOCUS       WP_123851976             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium shandongense].
ACCESSION   WP_123851976
VERSION     WP_123851976.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium shandongense
  ORGANISM  Chryseobacterium shandongense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium shandongense"
                     /db_xref="taxon:1493872"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33696
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypagit
       61 gpemmmdlqk qaerfdtkvh yemitkvefs kevggvhkly agnkeifart viistgatak
      121 ylglddekky agggvsacat cdgffykgkd vvvvgagdta aeeatylakl ckkvtmlvrk
      181 dvfraskami hrventpnie vkfhheliai egennlvera vvinnqtket stidvdgifi
      241 aighkpntdi flgqinlden gyivtekgsa rtnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 aamdaekyla elh
//
LOCUS       WP_123853841             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium shandongense].
ACCESSION   WP_123853841
VERSION     WP_123853841.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium shandongense
  ORGANISM  Chryseobacterium shandongense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium shandongense"
                     /db_xref="taxon:1493872"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33654
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypagit
       61 gpemmmdlqk qaerfdtkvh yemitkvefs kevggvhkly agnkeifakt viistgatak
      121 ylglddekky agggvsacat cdgffykgkd vvvvgagdta aeeatylakl ckkvtmlvrk
      181 dvfraskami hrventpnie vkfhheliai egennlvera vvinnqtket stidvdgifi
      241 aighkpntdi fvgqinlden gyivtekgsa rtnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 aamdaekyla elh
//
LOCUS       WP_123860257             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium nakagawai].
ACCESSION   WP_123860257
VERSION     WP_123860257.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium nakagawai
  ORGANISM  Chryseobacterium nakagawai
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium nakagawai"
                     /db_xref="taxon:1241982"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33645
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypagit
       61 gpemmmdlqk qaerfetkvh yemitkaefs kevggvhkly agnkeilakt viistgatak
      121 ylgledekky agggvsacat cdgffyrgkd vvvvgagdta aeeatylakl crkvtllvrk
      181 dvfraskamv hrventpnie vkfhheligi egenslvera viinnqtqek atvdvegifi
      241 aighkpntdi fvgqvdlden gyivtekgst rtnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 aamdaekyla elh
//
LOCUS       WP_123870765             313 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Chryseobacterium].
ACCESSION   WP_123870765
VERSION     WP_123870765.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium
  ORGANISM  Chryseobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium"
                     /db_xref="taxon:59732"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33619
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypagit
       61 gpemmmdlqk qaerfetkvh yemitkaefs kevggvhkly agnkeilakt viistgatak
      121 ylgledekky agggvsacat cdgffyrgkd vvvvgagdta aeeatylakl crkvtllvrk
      181 dvfraskamv hrvqntpnie vkfhheligi egenslvera viinnqtqet stvdvegifi
      241 aighkpntdi fvgqvdlden gyivtekgss rtnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 aamdaekyla elh
//
LOCUS       WP_123879336             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aurantiacibacter spongiae].
ACCESSION   WP_123879336
VERSION     WP_123879336.1
KEYWORDS    RefSeq.
SOURCE      Aurantiacibacter spongiae
  ORGANISM  Aurantiacibacter spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Aurantiacibacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Aurantiacibacter spongiae"
                     /db_xref="taxon:2488860"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34659
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtthttrmli igsgpaglsa aiyaaragme pivvqglqpg gqltittdve nypgfadviq
       61 gpwlmeqmqk qaehvgtrmi wdtitdvdia ggspfratgd sgdayvgdvl vistgaqakw
      121 lgvpgeqelg gkgvsacatc dgffyrgkkv vvigggntav eealyltnhs ddvtlihrrd
      181 elrsekilqd rlfasekitp vwnkvverfv agedgkldhl elvdtqtqek stiradgafv
      241 aighapatel frgklpmddg gyllvepgtp ktsvpgvfac gdvmdhtyrq avtaagtgcm
      301 aaldaerfla tlefaerear taeaae
//
LOCUS       WP_123881824             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aurantiacibacter spongiae].
ACCESSION   WP_123881824
VERSION     WP_123881824.1
KEYWORDS    RefSeq.
SOURCE      Aurantiacibacter spongiae
  ORGANISM  Aurantiacibacter spongiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Aurantiacibacter.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Aurantiacibacter spongiae"
                     /db_xref="taxon:2488860"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39349
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlkera egetrvaatp etvkklsalg atlaieegag rhaaisdeay rdaggevasa
       61 saavknadmv lgvnaprpdl legakqgawv iamfnpfgqr drieayaaag lealsmefmp
      121 ritraqsmdv lssqsnlagy kavlaaadty grafpmmmta agtvnaarvf vmgvgvaglq
      181 aiatakrlgs qvsatdvrsa tkeqiqslga kpvfvdeveg iegegsggya temseeyrka
      241 qaelvsahia rqdivittal ipgkpaprlv sdaqiatmkp gsvifdlavs qggnvegsva
      301 drivdrhgvr imgysntpgh lpadasalys rnlfnflnaf wdnetgrpvl deeigeavrl
      361 trdgrivndr ltgaa
//
LOCUS       WP_123885285             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium indoltheticum].
ACCESSION   WP_123885285
VERSION     WP_123885285.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium indoltheticum
  ORGANISM  Chryseobacterium indoltheticum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium indoltheticum"
                     /db_xref="taxon:254"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33756
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meenildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypagit
       61 gpemmmdlqk qaerfdtkvh yemiikaefs kevggihkly agnkeilaks viistgatak
      121 ylglddekky ngggvsacat cdgffyrgkd vvvvgagdta aeeatylskl vnkvtmlvrk
      181 defraskami hrventpnie vkfhheligi egennlvera vvinnqtqek stvdvhgifi
      241 aighkpntdi figqidlden gyivtekgss rtnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 aamdaekyla elh
//
LOCUS       WP_123888476             315 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Pseudomonas].
ACCESSION   WP_123888476
VERSION     WP_123888476.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33629
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrli ilgsgpagys aavyaaranl kpllitgmqm ggqlttttev dnwpgdvegl
       61 qgpdlmermr khaerfetei qfdhinkvdl skrpftlwgd sgeyqcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnqeva vvgggntave ealylaniak kvtvvhrrev
      181 fraekilvdk llarvaegki elklnatlde vlgdetgvtg mrialnsggt edialagvfi
      241 aightpntsl fegqldmhdg ylkiksgteg natqtniagv faagdvadhv yrqaitsaga
      301 gcmsaldaer fldel
//
LOCUS       WP_123896245             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aureibaculum marinum].
ACCESSION   WP_123896245
VERSION     WP_123896245.1
KEYWORDS    RefSeq.
SOURCE      Aureibaculum marinum
  ORGANISM  Aureibaculum marinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aureibaculum.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Aureibaculum marinum"
                     /db_xref="taxon:2487930"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33741
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseniekikc liigsgpagy aaaiyaarad lkpviytgle pggqltttte vdnypgypeg
       61 vdgtmmmedf kkqaerfdtd vrygmvtkvd fsdkvggihk vivdgakeie aqtviistga
      121 takylglpse erlkgggvsa catcdgffyk gqdvivvggg dtaaeeatyl aklckkvtll
      181 vrrgemrask amqhrvntte nlevmyftel devlgdqvve gvrvvnnqtg ekqeievtgv
      241 fiaighkpnt dlfkgildmd esgylitkgk stktklpgif aagdvqdkey rqaitaagsg
      301 cmaaldaery laale
//
LOCUS       WP_123908136             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium sp. G0162].
ACCESSION   WP_123908136
VERSION     WP_123908136.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. G0162
  ORGANISM  Chryseobacterium sp. G0162
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium sp. G0162"
                     /db_xref="taxon:2487063"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33661
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypagit
       61 gpemmmdlqk qaerfetkvh yemitkaefs kevggvhkly agnkeilakt viistgatak
      121 ylgledekky agggvsacat cdgffyrgkd vvvvgagdta aeeatylakl crkvtllvrk
      181 dvfraskamv hrventpnie vkfhheligi egenslvera viinnqtqek stvdvegifi
      241 aighkpntdi fvgqvdlden gyivtekgst rtnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 aamdaekyla elh
//
LOCUS       WP_123915811             358 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Georgenia muralis].
ACCESSION   WP_123915811
VERSION     WP_123915811.1
KEYWORDS    RefSeq.
SOURCE      Georgenia muralis
  ORGANISM  Georgenia muralis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Allobogoriellales; Allobogoriellaceae; Georgenia.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Georgenia muralis"
                     /db_xref="taxon:154117"
     gene            1..358
                     /gene="trxB"
     Protein         1..358
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=37179
     Region          35..336
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtsnafssal galsglvtga eaaaenghra aevrdviivg sgpagytaav ygaranlrpl
       61 vfagsvtagg almntteven fpgfpegilg pqlmenmqaq aerfgaevry edvvsvdltg
      121 etktvttddg dtfaartvil angseykeig lpaektlsgk gvsycatcdg fffrdqhivv
      181 vgggdsamee atfltrfask vtvvhrrdel raskimaera lgndkiefaw nsvvsaihge
      241 dkvtgvtltd tvtgqtreld atgvfvaigh vprtgiltgq vdlddsgyik vdspttltni
      301 pgvfacgdav dhtyrqaita agtgcsaald aerylavlde agepatdasq tpqgdvlv
//
LOCUS       WP_123919390             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bacillus sp. FJAT-42376].
ACCESSION   WP_123919390
VERSION     WP_123919390.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. FJAT-42376
  ORGANISM  Bacillus sp. FJAT-42376
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Bacillus sp. FJAT-42376"
                     /db_xref="taxon:2014076"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34391
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeekiydvi iagagpaglt aavytsranl stlmiergip ggqmantedv enypgfdhil
       61 gpelstkmfd hakkfgaeya ygdikgiedg eefkivrags keykaravii gtgaeykkln
      121 vpgekelggr gvsycavcdg affknkelvv vgggdsavee gvyltrfask vtivhrrdql
      181 raqkilqkra fdndkiefiw nhtvseihee ggkvgsvtlv ntqtgeeqpf kadgafiyig
      241 mvplsqpfen lritnengyi etnelmetrv pgifaagdir ektlrqivta tgdgsiaaqs
      301 aqnyveelhe klkask
//
LOCUS       WP_123921141             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_123921141
VERSION     WP_123921141.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33378
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnkktelvv pglfifvgyd
      241 vnnavlkqed nsmlceydey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_123926919             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gordonia oryzae].
ACCESSION   WP_123926919
VERSION     WP_123926919.1
KEYWORDS    RefSeq.
SOURCE      Gordonia oryzae
  ORGANISM  Gordonia oryzae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Gordonia oryzae"
                     /db_xref="taxon:2487349"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35398
     Region          10..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqsdnqqih eliivgsgpa gytaavyaar aelaplvfeg tqfggalmtt tevenfpgfq
       61 ngiqgpalmd emreqairfg adlrmedvde lrlngvikev vasgethrar avilamgaaa
      121 rylgidgeqe llgrgvsaca tcdgfffkdq diavigggds ameeatfltk farsvtlihr
      181 reefrasrim ldrarnndki rfvtnaavrs vigdgsvtgl elidtrsgdt rtvdvtgmfv
      241 aighdprsel vrgqvdldsd gyvqvqgrtt ytslpgvfaa gdlvdhtyrq aitaagsgca
      301 aaidaerwla eqgdidttqv eadlmvvdah s
//
LOCUS       WP_123930461             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corynebacterium choanae].
ACCESSION   WP_123930461
VERSION     WP_123930461.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium choanae
  ORGANISM  Corynebacterium choanae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Corynebacterium choanae"
                     /db_xref="taxon:1862358"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33103
     Region          5..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 madihdliii gsgpagytaa iyaaraqmnl vmfegieygg slmttteven ypgfaegimg
       61 palmeemrnq alrfgadlrq elvdevalsg dvktvhagge vfhaktvilg mgaaprylgv
      121 pgeqellgrg isacatcdgf ffrdhdiavi gggdsameea lfltrvaksv tivhrrdefr
      181 asaimlqraq dnekirfltn tvvtqvngqd kvenlhvknt vtgeestldv tamfvaighd
      241 prsqivagqv dldpagyvqv qhpstatnip gvfavgdlvd shyqqaitaa gsgcraaida
      301 eqylmaqeaa q
//
LOCUS       WP_123934647             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tetragenococcus osmophilus].
ACCESSION   WP_123934647
VERSION     WP_123934647.1
KEYWORDS    RefSeq.
SOURCE      Tetragenococcus osmophilus
  ORGANISM  Tetragenococcus osmophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Tetragenococcus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Tetragenococcus osmophilus"
                     /db_xref="taxon:526944"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34045
     Region          5..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 makkydvvii gagpagmtaa lyasranlsv mlldrgiygg qmnntaeien ypgfksilgp
       61 dlsqemydsa iqfgadfgyg tvksvtdhgd yktietdadn yetkaiviat gsnykdlgvp
      121 geeeyrgrgv sncavcdgaf frnqhvvvvg ggdsaveege yltrlvdkvt iihrrdelra
      181 qqiiqdrafk nskidfiwds nvqeitgdgn kvtgvkginn ktgepfavda ggtfiyvgie
      241 pmsdpfrsln itddegwfvt nedmetpvpg ifavgdirkk nlrqvvtatn dggiagqkay
      301 qyiteleakt taanv
//
LOCUS       WP_123935765             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corynebacterium gerontici].
ACCESSION   WP_123935765
VERSION     WP_123935765.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium gerontici
  ORGANISM  Corynebacterium gerontici
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Corynebacterium gerontici"
                     /db_xref="taxon:2079234"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33348
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdapihdva iigsgpagyt aalyaarael kpivfegiey ggslmtttev enfpgfkdgi
       61 mgpelmeemr sqaerfgadl rmelvtrvel egeikkiwvd delfqaravi latgsapryl
      121 gvegeqrllg rgvsacatcd gfffrdhdia vigggdsame eatfltkfak svtivhrree
      181 frasaimler akennkirfa tnkqvagvlg entveglelk dtvtgeastl dvtamfvaig
      241 hdprsemfre qvncdengyv lvehpstrtn ipgvfavgdl vdatyqqait aagagcrgai
      301 daehylaar
//
LOCUS       WP_123939672             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium sp. G0186].
ACCESSION   WP_123939672
VERSION     WP_123939672.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. G0186
  ORGANISM  Chryseobacterium sp. G0186
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium sp. G0186"
                     /db_xref="taxon:2487064"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33588
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypagit
       61 gpemmmdlqk qaerfetkvh yelitkaefs kevggvhkly agnkeilakt viistgatak
      121 ylglddekky agggvsacat cdgffyrgkd vvvvgagdta aeeatylakl crkvtllvrk
      181 dvfraskamv hrvestpnie vkfhheligi egenslvera vvinnqtqet skvdvegifi
      241 aighkpntdi fvgqvdlden gyivtekgst rtnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 aamdaekyla elh
//
LOCUS       WP_123946434             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_123946434
VERSION     WP_123946434.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33361
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkhtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_123948004             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sp. FDAARGOS_522].
ACCESSION   WP_123948004
VERSION     WP_123948004.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. FDAARGOS_522
  ORGANISM  Streptococcus sp. FDAARGOS_522
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sp. FDAARGOS_522"
                     /db_xref="taxon:2420310"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32992
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigsg pggmtaalya arsnlkvgli eqgapggqmn ntaeienypg ydhisgpels
       61 mkmyeplekf evehiygivq rvendgdvkr vitedesyea ktvilatgak nsllgvpgee
      121 eytsrgvsyc avcdgaffrd qdllvvgggd saveeavflt qfaksvtiih rrdqlraqkv
      181 lqdrafanek lkfvwdsvvk eikgneikvs gvtvenlktg eisemtfggv fiyvglkphs
      241 smvselgitd etgwvltdtn mktsipglya igdvrqkdlr qiatavgega iagqgvynyi
      301 tehf
//
LOCUS       WP_123955799             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Frederiksenia canicola].
ACCESSION   WP_123955799
VERSION     WP_123955799.1
KEYWORDS    RefSeq.
SOURCE      Frederiksenia canicola
  ORGANISM  Frederiksenia canicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Frederiksenia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Frederiksenia canicola"
                     /db_xref="taxon:123824"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33735
     Region          2..313
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mttkhaklli lgsgpagyta avyaaranls pvlvtgmqqg gqltttseie nwpgefgdit
       61 gselmskmqk haekfnteii fdhihsvdls krpftlngdf ntftcdalii atgasakylg
      121 lpseeafkgr gvsacatcdg ffyrnkpvav igggntavee alylsnvasq vhlihrrdtf
      181 rsekilidrl mkkveegkiv lhlnavldev lgdnsgvtgv rikctkteqp etltldgvfv
      241 aighapntem fkdqlelnng yivvrsgleg natatsvegv faagdvmdhn yrqaitsagt
      301 gcmaaldaer fldsq
//
LOCUS       WP_123961157             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corynebacterium pseudopelargi].
ACCESSION   WP_123961157
VERSION     WP_123961157.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudopelargi
  ORGANISM  Corynebacterium pseudopelargi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Corynebacterium pseudopelargi"
                     /db_xref="taxon:2080757"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33471
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdatihdva iigsgpagyt aalyaarael rpivfegiey ggslmtttev enfpgfkdgi
       61 lgpelmeemr aqaerfgadl rmelvtrvel egeikkiwvd deefqaravi latgsapryl
      121 gvdgeqqllg rgvsacatcd gfffrdhdia vigggdsame eaifltkfak svtivhrree
      181 frasaimler akenekiril tnkqvsrvlg entveglelv dslsgetstl dvtamfvaig
      241 hdprselfrd evecddagyv rvqhpstrtn ipgvfaigdl vdatyqqait aagsgcrgai
      301 daehylaei
//
LOCUS       WP_123961912             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vibrio crassostreae].
ACCESSION   WP_123961912
VERSION     WP_123961912.1
KEYWORDS    RefSeq.
SOURCE      Vibrio crassostreae
  ORGANISM  Vibrio crassostreae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Vibrio crassostreae"
                     /db_xref="taxon:246167"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34369
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvkhcnll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttev enwpgdaegl
       61 tgpalmdrmk ehaerfetei lfdhinevdl snrpfrlkgd sgeytcdali istgasakyl
      121 gldseeafkg rgvsacatcd gffyrnqkva vvgggntave ealylsnias evhlvhrrdt
      181 fraekilvkr lmdkvqngni vlhtdrtlde vlgddmgvtg vrikdtqsdk tedievmgaf
      241 iaighqpnte ifkgqvdmkd dyiivqsgle gnatqtsipg vfaagdvmdh nyrqaitsag
      301 tgcmaaldae rfldglndk
//
LOCUS       WP_123966233             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. TLI_185].
ACCESSION   WP_123966233
VERSION     WP_123966233.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. TLI_185
  ORGANISM  Streptomyces sp. TLI_185
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces sp. TLI_185"
                     /db_xref="taxon:2485151"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34145
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfrdgim
       61 gpelmdnmra qaerfgaelv pddvvsvdlt geiktvtdta gtvhkakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfv wdsevaeieg dpklsglklr nlktgeisdl avtglfiaig
      241 hdprtelfkg qldldeegyl kvaapstrtn ltgvfaagdv vdhtyrqait aagtgcsaal
      301 daerflaala deeqaepekt sv
//
LOCUS       WP_123975727             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_123975727
VERSION     WP_123975727.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34203
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmra qaerfgaelv pddivsvdlt geiktvtdta gtvhkakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfa wdseiaevqg eqklaglklr nvktgelsdl pvtglfiaig
      241 hdprtelfkg qldldeegyl kvaspstrtn ltgvfaagdv vdhtyrqait aagtgcsaal
      301 daerflsala deekaepekt sv
//
LOCUS       WP_123984014             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium sp. G0201].
ACCESSION   WP_123984014
VERSION     WP_123984014.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. G0201
  ORGANISM  Chryseobacterium sp. G0201
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Chryseobacterium sp. G0201"
                     /db_xref="taxon:2487065"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33673
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgfta aiyaaradlk pelytglepg gqlttttevd nfpgypagit
       61 gpemmmdlqk qaerfdtkvh yemitkvefs kevggvhkly agtkeifakt viistgatak
      121 ylglddekky ngggvsacat cdgffykgkd vvvvgagdta aeeatylakl vnkvtmlvrk
      181 gefraskami hrvqntpnie vkffheligi egennlvera vainnqtqek stidvhgifi
      241 aighkpntdi fagqidlden gyivtekgst rtnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 samdaekyla elh
//
LOCUS       WP_123990376             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Streptomyces].
ACCESSION   WP_123990376
VERSION     WP_123990376.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34156
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgim
       61 gpelmdnmra qaerfgaeli pddivsvdlt geiktvtdts gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfv wdsevaeiqg dpklsglklr nlktgeisdl avtglfiaig
      241 hdprtelfkg qleldgegyl kveapstrtn ltgvfgagdv vdhtyrqait aagtgcaaal
      301 daerflaala deekaepekt av
//
LOCUS       WP_124006593             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tetragenococcus koreensis].
ACCESSION   WP_124006593
VERSION     WP_124006593.1
KEYWORDS    RefSeq.
SOURCE      Tetragenococcus koreensis
  ORGANISM  Tetragenococcus koreensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Tetragenococcus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Tetragenococcus koreensis"
                     /db_xref="taxon:290335"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34242
     Region          5..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mekkydvvii gagpagmtaa lyasranlsv mlldrgiygg qmnntaeien ypgfksilgp
       61 dlsqemygsa iqfgadfgyg tvksvtdhgd yktietdadd yetkaiviat gsnyrdlgvp
      121 geeeyrgrgv sncavcdgaf frnqhvvvvg ggdsaveege yltrlvdkvt iihrrdelra
      181 qqiiqdrafk ndkidfiwds nvqeivgdgn kvtgvkginn ktgepfevea ggtfiyvgie
      241 pmsepfrpln itdedgwfit nenmettipg ifavgdirkk elrqvvtatn dggiagqkay
      301 qyiteleakt eaana
//
LOCUS       WP_124007935             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            diabolicus].
ACCESSION   WP_124007935
VERSION     WP_124007935.1
KEYWORDS    RefSeq.
SOURCE      Vibrio diabolicus
  ORGANISM  Vibrio diabolicus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio; Vibrio diabolicus subgroup.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Vibrio diabolicus"
                     /db_xref="taxon:50719"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54618
     Region          1..516
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agesrvaasp ksveqliklg fdiaiesqag vlasfddaay eaagakivss
       61 eevwasglil kvnapivdee qgideiallq dgatlvsfiw paqnaelmeq lsskninvla
      121 mdsvprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv esmgaefltv dfqedsgsgd gyakemsddf
      241 nrkaaelyae qakdvdiiit talipgkpap klitnemvds mkagsvivdl aaanggncey
      301 tvkdqvimtd ngvkivgytd mvgrlptqss qlyatnlvnl lkllckekdg ninidfedvv
      361 irgvtvvkeg eitwpappiq vsaqpqvkqe qpakpepkve eptsptkkii gvaaavgafa
      421 wiasvapaaf lshftvfvla cvvgyyvvwn vthalhtplm svtnaisgii vvgallqigq
      481 gngvvsflsf iavliasini fggftvtkrm lemfrkdk
//
LOCUS       WP_124015425             509 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Shewanella].
ACCESSION   WP_124015425
VERSION     WP_124015425.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53398
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresi egetrvaatp atviqliklg fsvaieaqag vkssfdnaaf eaagadvvds
       61 vyqadfifkv napsdeeiaq mkpgttlvsf iwpaqnpelv eklsshnitv mamdmvpris
      121 raqsldalss maniggyrav ieaahefgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggsfl klefenkegg ssdgyakvms eefiaaemal
      241 faeqakdvdi iittalipgr papklitkdm vdtmkpgsvi vdlaaatggn ceytvtgerf
      301 itdngvkvlg ytdlpgrlpa qssqlygtnl vnlmklmcka kdgnavldfd dvvmrnmtvt
      361 rggeitfppp aisvsaapqk paasiepkaa kvdkapsklk yilgvlglag faavasvapa
      421 eflshftvfi lacvvgyyvv wnvshslhtp lmsvtnaisg iivvgallqi gqgsalvtal
      481 afvavliasi nifggftvtq rmlkmfrkd
//
LOCUS       WP_124008750             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Vibrio].
ACCESSION   WP_124008750
VERSION     WP_124008750.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34245
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvkhckll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttev enwpgdaegl
       61 tgpalmdrmk ehaerfetei vfdhinevel sqrpfrlkgd sgeytcdali istgasakyl
      121 gleseetfkg rgvsacatcd gffyrnqkva vvgggntave ealylsnias evhlihrrds
      181 fraekilvkr lmdkvesgni vlhtdrtlde vlgddmgvtg vrikdvntga tedlevmgaf
      241 iaighqpntq ifegqvdmkd gyiivksgle gnatqtsieg vfaagdvmdh nyrqaitsag
      301 tgcmaaldae rfldslgdk
//
LOCUS       WP_124009529             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus aureus].
ACCESSION   WP_124009529
VERSION     WP_124009529.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33457
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteidfdiai igagpagmta avyasranlk tvmiergipg gqmanteeve nfpgfemitg
       61 pdlstkmfeh akkfgavyqy gdiksvedkg eykvinfgnk eltakaviia tgaeykkigv
      121 pgeqelggrg vsycavcdga ffknkrlfvi gggdsaveeg tfltkfadkv tivhrrdelr
      181 aqrilqdraf kndkidfiws htlksinekd gkvgsvtlts tkdgseethe adgvfiyigm
      241 kpltapfkdl gitndvgyiv tkddmttsap gifaagdvrd kglrqivtat gdgsiaaqsa
      301 aeyiehlndk a
//
LOCUS       WP_124014941             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Shewanella].
ACCESSION   WP_124014941
VERSION     WP_124014941.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34009
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msearhvnll ilgsgpagyt aavyaaranl npvmitgmqq ggqlttttev enwpgdaedl
       61 tgpalmermq khaekfdtei ifdhinevtl terpfrlkgd ngeftcdali iatgasakyl
      121 glpseeafmg rgvsacatcd gffyrnqkva vigggntave ealylsnias evhlihrrds
      181 frsekilinr lmdkvangni ilhldqtlee vtgndmgvtg lkkkstkdgs vtdlevagvf
      241 vaighspntg ifadqlemnh gylkvnsglq gnatqtsieg vyacgdvmdq hyrqaitsag
      301 tgcmaaldae ryldakk
//
LOCUS       WP_124013505             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            psychromarinicola].
ACCESSION   WP_124013505
VERSION     WP_124013505.1
KEYWORDS    RefSeq.
SOURCE      Shewanella psychromarinicola
  ORGANISM  Shewanella psychromarinicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Shewanella psychromarinicola"
                     /db_xref="taxon:2487742"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53571
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresi egetrvaatp atviqlkklg fsvaieaqag vkssfdnaaf eaagadivdn
       61 vyqadfifkv napsddeiaq mkpgttlvsf iwpaqnpelv eklstnnitv mamdmvpris
      121 raqsldalss maniggyrav ieaahefgrf ftgqitaagk vppakvliig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggsfl klefenkegg ssdgyaktms eefiaaemal
      241 faeqakevdi iittalipgr papklitkdm vdnmkpgsvi vdlaaatggn ceytvkgerf
      301 itdngvkvlg ytdlpgrlpa qssqlygtnl vnlmklmcke kdgnavldfd dvvmrnmtvt
      361 rggeitfppp aisvsaapqk saastepkaa kvekapsklk yilgalgiag faavasvapa
      421 eflshftvfi lacvvgyyvv wnvshslhtp lmsvtnaisg iivvgallqi gqgsalvtal
      481 affavliasi nifggftvtq rmlkmfrkd
//
LOCUS       WP_124026740             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Alteromonas sediminis].
ACCESSION   WP_124026740
VERSION     WP_124026740.1
KEYWORDS    RefSeq.
SOURCE      Alteromonas sediminis
  ORGANISM  Alteromonas sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Alteromonadaceae; Alteromonas/Salinimonas group;
            Alteromonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Alteromonas sediminis"
                     /db_xref="taxon:2259342"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33809
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msearhvrll ilgsgpagys aavyaaranl npvlltgiqq ggqlttttev enwpgdpegl
       61 tgpdlmvrmq khaekfdtei ifdhinktdl skrpftlygd sgtytcdali iatgasakyl
      121 gleseqafmg rgvsacatcd gffyrnqkva vigggntave ealylsnias evhvvhrrdt
      181 frsekilsqr lldkaengnv vlhlnktlde vvgdemgvtg ikikdtqtgd vsdldimglf
      241 vaighqpntg ifdgqlemkd gylkvnsgle gnatqtsvpg vfaagdvsdh vyrqaitsag
      301 tgcmaaldae kfldsqd
//
LOCUS       WP_124021068             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Citrobacter youngae].
ACCESSION   WP_124021068
VERSION     WP_124021068.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter youngae
  ORGANISM  Citrobacter youngae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter youngae"
                     /db_xref="taxon:133448"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53558
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mariksrvrr ffsllvpllf isavyaeqtp vpaktvtvea knevfapqhp dqylswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc gdchntaspd fakgkpeltl
      181 srpyaerame tigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmek
      241 yydtiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegkiytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gateaemkpi ledirhaqwr wdlsiashgi hmhapeeglr mlgsamdkaa dartklvrll
      421 atkgitheip lpdistkeka qaaiglnmqq inaekqdfik tvipqwedqa rkngllsq
//
LOCUS       WP_124020206             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_124020206
VERSION     WP_124020206.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33391
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_124023182             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Buttiauxella warmboldiae].
ACCESSION   WP_124023182
VERSION     WP_124023182.1
KEYWORDS    RefSeq.
SOURCE      Buttiauxella warmboldiae
  ORGANISM  Buttiauxella warmboldiae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Buttiauxella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Buttiauxella warmboldiae"
                     /db_xref="taxon:82993"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53330
     Region          20..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mariilsapr slglmllllf issvyaqqtp spakaaaiea rnetfapqhp dqylswqats
       61 eqsaredala ddprlvilwa gypfsrdynk prghawaltd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkegee ayfhgkwarg gplivntlgc adchntasdd fakgkpaltl
      181 srpyaqrame tignpfekas rfdqqamvcg qchveyyfdg knkavkfpwd egmkvenmek
      241 yydaiafsdw tnalsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaagklyts
      301 hkignpfdnf aqtcagchtq dkaflqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gateaemqpv lenirhaqwr wdlaiashgi hmhapeeglr mlgsaldkaa esrtrlirll
      421 atkditdeip lpdistkeka qraigldmqq inaekqdflk tvvpqwdeqa rhngllsq
//
LOCUS       WP_124033343             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Olavius algarvensis spirochete
            endosymbiont].
ACCESSION   WP_124033343
VERSION     WP_124033343.1
KEYWORDS    RefSeq.
SOURCE      Olavius algarvensis spirochete endosymbiont
  ORGANISM  Olavius algarvensis spirochete endosymbiont
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Spirochaetales.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Olavius algarvensis spirochete endosymbiont"
                     /db_xref="taxon:260710"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34228
     Region          6..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mqpewdlivv gggpaglsaa qygsranlrt lvieelapgg tallinemen ypgfpkaing
       61 yefselmrqq teqfgamiks atvtaikktq dvftvetfde sfsswtvvls tgakhkhlgi
      121 pgeetfsgrg vsycatcdgp ffknkkilvv gggdaacdea aylanlsdki tlihrrdrfr
      181 aqksladrvl knpnievrfn hvlekilged kvrrvrlrrt ienkvyeenf davfifvgai
      241 pqtalvpklk kdeagyivtn qnmettqpgl ytigdvrstp frqvvvacge gaisahmaaa
      301 yidaikgeiy ggaa
//
LOCUS       WP_124040547             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium perfringens].
ACCESSION   WP_124040547
VERSION     WP_124040547.1
KEYWORDS    RefSeq.
SOURCE      Clostridium perfringens
  ORGANISM  Clostridium perfringens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Clostridium perfringens"
                     /db_xref="taxon:1502"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34162
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdkeikeldl iiigagpagl tsaiyasrak lstlvlednl vggqvrstyt venypgftei
       61 tgndladriq aqaeacgaii defdfienvs lkddekiiet gdyiykpkav iiatgatpkk
      121 lpipseskyl gkgvhycavc dgavyqdevv avvgggnaal eealylsniv kkvivirryd
      181 yfhaeaktle aasnkeniei mynwdlvdvl ggefveaari kntktgeeke iaingvfgyi
      241 gtepktsmfr eyinvkengy iegdenmrtn vkgvyvagdv rekmfrqitt avsdgtiaal
      301 haekyiseik er
//
LOCUS       WP_124053790             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arcanobacterium ihumii].
ACCESSION   WP_124053790
VERSION     WP_124053790.1
KEYWORDS    RefSeq.
SOURCE      Arcanobacterium ihumii
  ORGANISM  Arcanobacterium ihumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Arcanobacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Arcanobacterium ihumii"
                     /db_xref="taxon:2138162"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53427
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpreph asqslvaatp dtvgkliklg yelvveqgag drasfpdhly eeagaaivnt
       61 devwdsdivf aldtppteyl dkmrqgatli armapgrnsd tlqalaqrgi tglamdmvpr
      121 israqsmdvl ssmaniagyr avveaaaqfg rlftgqvtaa gkmppatvyv igagvaglaa
      181 igtansmgav vnatdvrdet aeqvesmgaq fvaipapaqe ssdgyakemt adqaaaaakl
      241 yaeqasisdv vittanipgr kspilldaea vanmkpgsvv vdmaaanggn celtvpgevi
      301 ttengvkiig ytdlagrlpa qasqlygqnl vnffklttpe kdgilhldld dvvvrqmtvt
      361 lnndvlfppp pvqvsaapaa kkpvanvapa epepekswfa knwwmlvvgv lfasliisap
      421 pgmtshfivf alavvvgfyv itsvthslht plmsvtnais giivvgallq vpadsiavkv
      481 ltffaivvas invfggftvt hrmlkmfqrs
//
LOCUS       WP_124054471             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arcanobacterium ihumii].
ACCESSION   WP_124054471
VERSION     WP_124054471.1
KEYWORDS    RefSeq.
SOURCE      Arcanobacterium ihumii
  ORGANISM  Arcanobacterium ihumii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Arcanobacterium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Arcanobacterium ihumii"
                     /db_xref="taxon:2138162"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32840
     Region          5..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstqydviiv gsgpagwtaa iytaraglnp lvlagtldag galmttteve nfpgwpdaim
       61 gpelmekmqa qaerfgaqve yedaiefdla gdtkiiktds qtyeaksvil algsaykklg
      121 legetvfsgk gvsfcatcdg fffkgqeiav vgggdsavte alflarfask vhiihrreel
      181 raskvmadrl lanekvemhw nsrvtdiqge nklealtled tvtgekselp vgglfvaigh
      241 eprsavvssq ikvddggyii vdspssrtni pgvfacgdvv dheyrqaita agsgcvaald
      301 aqdylskfe
//
LOCUS       WP_124058229             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vaginisenegalia massiliensis].
ACCESSION   WP_124058229
VERSION     WP_124058229.1
KEYWORDS    RefSeq.
SOURCE      Vaginisenegalia massiliensis
  ORGANISM  Vaginisenegalia massiliensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Aerococcaceae; Vaginisenegalia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Vaginisenegalia massiliensis"
                     /db_xref="taxon:2058294"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34168
     Region          12..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 menntlekev vdvvvigagp ggltaalyas ranlktvile kgmpggeinn tadvenytgf
       61 sliagpelaq qmydsamrfg aqhiytevtg ieldgqdrlv ytrdkvyqtk vviiatgaqh
      121 rkldvegeer lngrgvsyca vcdgfffrdk elvvvgggds aveegvyltq fakkvtiihr
      181 rdqlraqqvl qdrakanpki efvwdsvvea iegqdkvesl qvrhvktnqv stlkadgvfv
      241 yvglipnsel fnqlgitdae gwiitnekme tavdgifavg dvrqthlrqi atavgdgsha
      301 ghmayqyits lnd
//
LOCUS       WP_124069746             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Filibacter tadaridae].
ACCESSION   WP_124069746
VERSION     WP_124069746.1
KEYWORDS    RefSeq.
SOURCE      Filibacter tadaridae
  ORGANISM  Filibacter tadaridae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Filibacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Filibacter tadaridae"
                     /db_xref="taxon:2483811"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34115
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 minekiydvi iigagpagmt aavytsrgnl stlmlergvp ggqmanteei enypgfesil
       61 gpdlstkmfd hakrfgaeya ygdvteiidg rsyktivagg keykaraiii ttgaeykkmg
      121 ipgeteltgr gvsycavcdg affkgkdvvv igggdsavee gsyltrfadk vtivhrreel
      181 raqkiiqdra fandkidfiw nttvkqvnae ngkvgsvtlv stvdgtekef etdgmfvyig
      241 mdplttpfek lgildengyv ktndimetsv pgiyaagdvr ekllrqvvta tgdgsiaaqa
      301 vqkyieelme siatea
//
LOCUS       WP_124081788             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pigmentiphaga humi].
ACCESSION   WP_124081788
VERSION     WP_124081788.1
KEYWORDS    RefSeq.
SOURCE      Pigmentiphaga humi
  ORGANISM  Pigmentiphaga humi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pigmentiphaga.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Pigmentiphaga humi"
                     /db_xref="taxon:2478468"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38801
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigipaetr pgetrvaatp etvkkmsagg nqvlvqagag qrasytdeay aaagatvvsd
       61 aaqvygqael ilkvqapdag elpqlrpgqi llgmlnpfda dgleklaatg vtgfaleaap
      121 ritraqsldv lssqaniagy kavivaadhy grfmpmlmta agtvkaarvv vlgagvaglq
      181 aiatakrlga vveasdvrpa akeqieslga kfidvpfetd eereiaqgtg gyarpmpaaw
      241 marqaalvae rckqadivit talipgrpap vlvseetvag mkpgsvivdl averggncpl
      301 srpdevvdan gvkivgytnl aarvatdasa lyarnlldfm klvvakdgal diqredeiva
      361 acmvcdaqrv lrsr
//
LOCUS       WP_124088012             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudogemmobacter humi].
ACCESSION   WP_124088012
VERSION     WP_124088012.1
KEYWORDS    RefSeq.
SOURCE      Pseudogemmobacter humi
  ORGANISM  Pseudogemmobacter humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudogemmobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Pseudogemmobacter humi"
                     /db_xref="taxon:2483812"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55202
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalteva sgecrvaltp esalqlqklg hdcvieagag lragftdaay qaagvsvlps
       61 aqavadaadv vvkvrgpepa eldllhegqt lisffwpaqn pelleqarak gvtavamdmv
      121 prisraqkmd alssmanlag yravieaann fprfftgqvt aagkvppakv lvvgagvagl
      181 aaigasvslg aityafdvrp evaeqigsmg aefvyldfae saqdgaatgg yaapsspefr
      241 eaqlkkfrel apdmdivitt alipgrpapk lwtadmvalm krgsvivdla aerggncdlt
      301 vpdekivtdn gvtvigytdf psrmaaqass lyannirhmm tdltpkkdgv idhnmeddvi
      361 rgatvtkage ttwpppppki qaiaaqkpke kpkeltpaer raqevaafka qtrnqiglla
      421 igggllllag wfapasfmsh fivfvlscfv gfqviwnvsh slhtplmait naissiiilg
      481 allqigsgnw lvivlaalsv lmagvnifgg flvtrrmlam fqks
//
LOCUS       WP_124081187             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pigmentiphaga humi].
ACCESSION   WP_124081187
VERSION     WP_124081187.1
KEYWORDS    RefSeq.
SOURCE      Pigmentiphaga humi
  ORGANISM  Pigmentiphaga humi
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pigmentiphaga.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pigmentiphaga humi"
                     /db_xref="taxon:2478468"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33906
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msqdkhakvl ilgsgpagyt aavyasranl spmlvtgveq ggqlmtttev dnwpadangv
       61 qgpelmqrfq qhaerfntdi vfdhihtahl gqrpfklegd sgtytcdali iatgasakyl
      121 glpseeafkg rgvsgcatcd gffyknqdva vvgggntave ealylanicr tvtlihrrdk
      181 fraepimvdk lhekvaegri vlklfsqlqe vlgddsgvvg arlldnqtga tediavtgvf
      241 iaighqpntg ifkgqvemkd dyiitrsgln glatmtsvpg vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq rwldgemv
//
LOCUS       WP_124088165             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudogemmobacter humi].
ACCESSION   WP_124088165
VERSION     WP_124088165.1
KEYWORDS    RefSeq.
SOURCE      Pseudogemmobacter humi
  ORGANISM  Pseudogemmobacter humi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudogemmobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudogemmobacter humi"
                     /db_xref="taxon:2483812"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33084
     Region          9..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mgetrhsrvl iigsgpagyt aavyaaraml dpvliqglqp ggqltittev enwpglsvvq
       61 gpdlmvqmee haremgaaiv adyitaldls arpftatads gttytadavi latgaqakwl
      121 glpseekfkg fgvsacatcd gffyrgkevv vtgggntave ealfltnfas kvtlvhrrds
      181 lraekilqdr lfknpkikvv wnsavievkg aesplgveav rihnvstgee rdipcagffv
      241 aighapasel vrdqlelhng gyvkvepgst rtsipgvfaa gdltdhiyrq avtsagmgcm
      301 aaldaerwla eh
//
LOCUS       WP_124089546             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arthrobacter ulcerisalmonis].
ACCESSION   WP_124089546
VERSION     WP_124089546.1
KEYWORDS    RefSeq.
SOURCE      Arthrobacter ulcerisalmonis
  ORGANISM  Arthrobacter ulcerisalmonis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Arthrobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Arthrobacter ulcerisalmonis"
                     /db_xref="taxon:2483813"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33285
     Region          13..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mssaentapg vrdviivgsg pagytaavyt aranlqplll agsvtaggel mnttdvenyp
       61 gfpegimgpd lmenfekqaa rfgteiqfed vteldlegpi ktvtiatgek fqakaiilst
      121 gsayrelglp nekrlsghgv swcatcdgff fkgqdiavig ggdsameeal fltkfansvt
      181 vihrrdtlka skimadrala hekinfvwnt avedvlgdpk vtgltlknlv dgtvselavt
      241 gvfvaigndp rtdlvkgild ltpegtiave grtsktsiag vfaagdvidp tyrqaitasg
      301 sgcvaaldve hyladlpa
//
LOCUS       WP_124089466             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124089466
VERSION     WP_124089466.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33446
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekixqdk lxdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124093720             380 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_124093720
VERSION     WP_124093720.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39012
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,300,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetr ayearvaatp etvkkyvaag hsvcvergag aaasfpdeay aaagatlger
       61 aaayaaeivl kvqapdsdel pqmkrgavlv gmldpfnaeq aarlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr flpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee reaaqgtggy arpmppswla
      241 rqaalvhera kqadivista lipgrpaptl iqadtvaamk pgavivdlaa grgpenadgr
      301 rggncpltva dqvvkvhgvt iaghtnlaaq vgadasalya rnladflkli vtkegalnid
      361 mnddivaatl lcrdgevvrk
//
LOCUS       WP_124100478             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_124100478
VERSION     WP_124100478.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38479
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp xtvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael tqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_124101859             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_124101859
VERSION     WP_124101859.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38612
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpfeth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_124102883             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124102883
VERSION     WP_124102883.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33632
     Region          1..313
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkntidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcgragcrk ylddh
//
LOCUS       WP_124103019             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124103019
VERSION     WP_124103019.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33322
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlahrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_124112047             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Palleronia sp. THAF1].
ACCESSION   WP_124112047
VERSION     WP_124112047.1
KEYWORDS    RefSeq.
SOURCE      Palleronia sp. THAF1
  ORGANISM  Palleronia sp. THAF1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Palleronia.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Palleronia sp. THAF1"
                     /db_xref="taxon:2587842"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35308
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msthrhvkll ivgsgpagyt aavyaaraml epvlvqgiqp ggqltittdv enwpgdtsim
       61 gpdlmvrmea hanamgaeiv sdhinsvdls krpftavads gttytadami latgaqakwl
      121 glpseeafkg fgvsacatcd gffyrgqeva vigggntave ealfltnfas kvtlvhrrde
      181 lraekilqkr llehpkvevi wnhqldsvyg adspkgvegi nikntetgdv rkvqvsgvfi
      241 aighapasdl vkdqlethmg gyvvtkpgtt etsvpgvfaa gdltdhvyrq avtsagmgcm
      301 aaleaerwla engetegkdv seplgygakv epaq
//
LOCUS       WP_124112261             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Palleronia
            sp. THAF1].
ACCESSION   WP_124112261
VERSION     WP_124112261.1
KEYWORDS    RefSeq.
SOURCE      Palleronia sp. THAF1
  ORGANISM  Palleronia sp. THAF1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Palleronia.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Palleronia sp. THAF1"
                     /db_xref="taxon:2587842"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55750
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkfgvvkesq etearvaltp qsaeaiqklg hscvieagag sradisddly rgadvevlds
       61 akavfdacdv iakvrpptea evemmregqt lisffypaen ealmkkaadk gatliamdmv
      121 prisraqkmd alssmaniag yravieaani fgrfltgqvt aagkvppaki lvvgagvagl
      181 aalgtatslg aivrafdvrp etaeqiesmg aeflfldfed tegvgeggya apsspefrek
      241 qlalfleqap eidivittal ipnreapelw tkemveamkp gsvivdlaae kggnckmtvk
      301 derivtdngv iiigytdfps rmakqsstly stnirhmltd ltpekdgtvn qnmedqvird
      361 stiahggevt wpppkrenps pakpkaekpk ektaeekrae evatfkkqtq sqvgllvvga
      421 vimllvgsva pesfmshfiv falacfvgfq viwgvahslh tplmavtnai sgiiilgall
      481 qigsgswlvv flsfiavlia sinivggflv trrmlsmfvk s
//
LOCUS       WP_124118319             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Paenibacillus].
ACCESSION   WP_124118319
VERSION     WP_124118319.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34251
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mskyrtivig tgpagltaai ylaranlkpl vieglqpggq lttttevenf pgfpqgimgp
       61 elmdnmrkqa erfgaefkng wveevdfskp pfkvkvggig eleaesiiis tgasarylgi
      121 pgeqenvgrg vstcatcdgf ffrgkkivvv gggdsameea sfltrfatdv tlvhrrdelr
      181 askimqdrar snekvkwaln rtplevvpea mgvkglkvrn netgqeelle adgvfvaigh
      241 tpntgflgna itldehgyvv vkpgttetni pgvfacgdvq dtkyrqaita agsgcmaamd
      301 cekflegsiv hdwsetldk
//
LOCUS       WP_124119889             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124119889
VERSION     WP_124119889.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33722
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdksengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124118130             313 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Paenibacillus].
ACCESSION   WP_124118130
VERSION     WP_124118130.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33273
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksiiigtg pagltaaiyl aranlsplvi egpqpggqlt tttevenfpg fpdgimgpel
       61 mdnmrkqaer fgaefrtgwv nnidmserpf kiqvegmgel vsetlilstg asakylgipg
      121 eetnvgrgvs tcatcdgfff rnkeiivigg gdsaleeasf lsrfgskvtl vhrreelrgs
      181 kimqdrarsn ekvemalnrt plevlagdng vtglkvlnne tgeeevipas gvfvaightp
      241 ntgflggqit tdehgyiltt pgtsetnipg vfacgdvqdt rykqaitaag sgcmaamdte
      301 kyieslehsa vvl
//
LOCUS       WP_124126289             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124126289
VERSION     WP_124126289.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33397
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iifgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlknrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_124123364             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124123364
VERSION     WP_124123364.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33649
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlxe vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqdqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124125924             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_124125924
VERSION     WP_124125924.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38606
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleavprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_124121516             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124121516
VERSION     WP_124121516.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33705
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave kalylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124127401             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_124127401
VERSION     WP_124127401.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38606
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 vdqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_124128857             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124128857
VERSION     WP_124128857.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33635
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali ixtgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124129988             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_124129988
VERSION     WP_124129988.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38491
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvlx sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_124131079             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124131079
VERSION     WP_124131079.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33396
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lackpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_124134197             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter hepaticus].
ACCESSION   WP_124134197
VERSION     WP_124134197.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter hepaticus
  ORGANISM  Campylobacter hepaticus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter hepaticus"
                     /db_xref="taxon:1813019"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33265
     Region          3..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldlaiiggg paglsaglya trgglknvvm fekgmpggqi tlsseienyp gvaqvmdgis
       61 fmapwneqcm rfglkhemve vqqilqnndg sftinigggk sqlakavivc tgsspkkagf
      121 kgeeeffgkg vstcatcdgf fyknkevavl gggdtaleea lylanicskv ylihrrdefr
      181 aipstvekak knekielitn asidevygdk tgvlgvkvkl kngdiknlnv pgiftfvgln
      241 vrneilkqdn gkflcnmeen gqvsvdlkmq tnipglfvag dlrkdapkqv icaagdgaia
      301 alsaisyies lh
//
LOCUS       WP_124137717             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124137717
VERSION     WP_124137717.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33221
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqlttttx vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_124138767             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124138767
VERSION     WP_124138767.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33697
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydqihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124139519             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Prevotella intermedia].
ACCESSION   WP_124139519
VERSION     WP_124139519.1
KEYWORDS    RefSeq.
SOURCE      Prevotella intermedia
  ORGANISM  Prevotella intermedia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Prevotella intermedia"
                     /db_xref="taxon:28131"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33658
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mekvktliig sgpagytaai yasrsnlqpv lyaglqpggq lttttiienf pgfkdgidan
       61 qlmlemkaqa invgadvrdg sivkadlskr pfivedergn vieantliia tgasakylgl
      121 sdeekyrgqg vsacatcdgf fyrkrtvavv gggdtaceea mylsslakrv ymivrkpylr
      181 aaeimrkrve ekenieilyn tntlglygen gvegahlvrf kgeeneekyd iqidgfflai
      241 ghlpntdlfk gqleldpqgf ivtkgtstat svegvyaagd vadptyrqgv vaagsgakaa
      301 ieaerflqdk gek
//
LOCUS       WP_124145706             449 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Okeania].
ACCESSION   WP_124145706
VERSION     WP_124145706.1
KEYWORDS    RefSeq.
SOURCE      Okeania
  ORGANISM  Okeania
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Okeania"
                     /db_xref="taxon:1458928"
     gene            1..449
                     /gene="trxB"
     Protein         1..449
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=49633
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
     Region          350..446
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
ORIGIN      
        1 mtkqrienlv iigsgpagyt aaiyagranl kpvvfegyqi ggvpggqlmt ttevenfpgf
       61 pegitgpqlm ermknqavrw gtelytedvt fvdlaqypft ikseereiqt ysiiiatgat
      121 akklklpsee kfwnsgisac avcdganpaf kgvelavigg gdtaaeesiy ltkygshihl
      181 lvrrdqmras ktmqqrvlen pkitvhwqte vidvygngvl egvklrnnqt gtqqdlpvgg
      241 lfyaightpn tqifqgqlel dekgyvvtrd mvktsvegvy avgdvqdsef rqaitaagsg
      301 cmgamlverw lsergltqef aqekatkksd keivvdtves fdhnathhlg gyalrklyhq
      361 sdrliivkys apscapchtl kpifekviqe fegkihyvei dieqdpeiaq nagvmstpti
      421 qffknkglve qlkgvkrkse yrqviqnni
//
LOCUS       WP_124147108             380 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Okeania].
ACCESSION   WP_124147108
VERSION     WP_124147108.1
KEYWORDS    RefSeq.
SOURCE      Okeania
  ORGANISM  Okeania
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Oscillatoriales; Microcoleaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Okeania"
                     /db_xref="taxon:1458928"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40217
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavaketl vnesrvalvp dviarlvkqg leiqveasag eksfffdgay eqagakiisd
       61 sdalwretev llkigvlqes eidklpegtv lisfldplgn paivqrlaer kitafsmeli
      121 prtsraqvmd alssqanigg ykavllasaa lpkffpmltt aagtikpakv lvmgagvagl
      181 qaiatarrlg avveafdirp evkeqvqslg akfvdvtlqe dtvaeggyak elseqakqht
      241 revltqhvaa sdivittaqv pgkkapllvt kemvdqmkpg avivdmaasq ggncecteag
      301 knvqwngvti igpvnlpatm pvhaselyak nisallklmi kdgelnldfe ddiiagacva
      361 hggeirnqrv kdalgvavgs
//
LOCUS       WP_124149211             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paraburkholderia dinghuensis].
ACCESSION   WP_124149211
VERSION     WP_124149211.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia dinghuensis
  ORGANISM  Paraburkholderia dinghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Paraburkholderia dinghuensis"
                     /db_xref="taxon:2305225"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35481
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msvtkhakvl ilgsgpagyt aavyaaranl spllitglaq ggqlmtttdv enwpadangv
       61 qgpelmqrfl ehaerfntei vfdhihtakl dekpirligd sgeytcdsli iatgasaqyl
      121 glpseelymg rgvsacatcd gffyrnqhva vvgggntave ealylagiak kvtvihrrdk
      181 fraepilidr llekekegvv eirwnhvlde vkgddggvng lriknaqtge ttdldlqglf
      241 vaighkpntd ifegqlemkn gyiitnggmn gnatatsvag vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq rylesiheit qphvmsaeae r
//
LOCUS       WP_124152692             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia dinghuensis].
ACCESSION   WP_124152692
VERSION     WP_124152692.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia dinghuensis
  ORGANISM  Paraburkholderia dinghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia dinghuensis"
                     /db_xref="taxon:2305225"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39281
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anesrvaatp etvkkyvaqg htvtvqsgag gpasfpdeay aavgaqiada
       61 aaafgadlvl kvqspsvsel afmkrgavvv gmldpfnaen aaqlagagvt afaleaaprt
      121 traqsldvls sqaniagyka vlvaanlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atarrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgvggy arpmppswla
      241 rqsalvhera kqadivista lipgrdaptl lpaetvqamk pgsvvidlaa grgpvadpat
      301 grrggncplt vadqvvtqhg vqvcgytnla smvaadasal yarnlldflk livtkegtln
      361 idladdivaa tllardgavt kkt
//
LOCUS       WP_124150697             521 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia dinghuensis].
ACCESSION   WP_124150697
VERSION     WP_124150697.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia dinghuensis
  ORGANISM  Paraburkholderia dinghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Paraburkholderia dinghuensis"
                     /db_xref="taxon:2305225"
     Protein         1..521
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53790
     Region          3..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mvmtlavpre thpgerrvaa tpqsiaelik lgytvnveag agalasfsde aytlagaqiv
       61 adaatlwata dvvtkvrpps idearqlkpg atlisfvwpa qnatlldvla trsasvlamd
      121 cvprisraqk ldalssmanm agyravieaa qhfgrvftgq itaagkmppa kvlvigagva
      181 glaaigaarg lgaivrafdt rpdvaqqves mgaeflgidi deegggtggy akqmsakfie
      241 aemalfeaqa revdiiitta lipgktapll inaqtvacmr agsvivdmaa eqggnceltq
      301 pgevvsvngv tvigytdlps rmanqssqly atnvrhlltd itpgkngelq ldmddvvqrg
      361 ttvmqsgtlc wpspvvapsp aptpmsptak gvasatpdaa dahaarrhgv wslvalmata
      421 llllalgava pgafvahftv fvlavfvgyq vvwnvtpalh tplmsvtnai sgiivigall
      481 hpggtgtivs vlsgialvva tiniaggflv tqrmlkmfqr t
//
LOCUS       WP_124160445             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bradyrhizobium sp. RP6].
ACCESSION   WP_124160445
VERSION     WP_124160445.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. RP6
  ORGANISM  Bradyrhizobium sp. RP6
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bradyrhizobium sp. RP6"
                     /db_xref="taxon:2489596"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34142
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msapvhakvv iigsgpagyt aaiyaaraml epiliqgiqp ggqltittdv enypgfadvi
       61 qgpwlmeqme kqavhvgtri vtdlvtrlet aqrpfrltcd sgdvyladtv ilatgaqarw
      121 lglaseakfq gggvsacatc dgffyrgkdv ivvgggntav eealyltnha sqvtivhrrd
      181 hfraerilqe rlfkhpkikv iwdsavdeic gtetpnkvth vrlknvktga ltdvktdgvf
      241 iaighapate lvkdqvklkp sgyvevapns tatsvpglfa agdvadetyr qavtaaglgc
      301 maaleaerfl alraseraaa e
//
LOCUS       WP_124170012             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124170012
VERSION     WP_124170012.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33380
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiaedgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_124171861             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124171861
VERSION     WP_124171861.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33237
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylanxa srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_124172412             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124172412
VERSION     WP_124172412.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33649
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqhpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv hlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemhd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124172265             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_124172265
VERSION     WP_124172265.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38542
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vsasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanqypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_124181393             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_124181393
VERSION     WP_124181393.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38637
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael tqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 vdqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_124182525             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124182525
VERSION     WP_124182525.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33701
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdiegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv hlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124185829             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_124185829
VERSION     WP_124185829.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38551
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavck ng
//
LOCUS       WP_124188883             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124188883
VERSION     WP_124188883.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33323
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gsatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_124189466             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_124189466
VERSION     WP_124189466.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53626
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkivipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_124199590             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_124199590
VERSION     WP_124199590.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38562
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdgay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqalrk ng
//
LOCUS       WP_124206163             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124206163
VERSION     WP_124206163.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33207
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfxaekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlknrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_124207226             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124207226
VERSION     WP_124207226.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33736
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdtli iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124200026             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124200026
VERSION     WP_124200026.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33678
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkssvdgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124208477             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_124208477
VERSION     WP_124208477.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53784
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwvcpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakdv diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggg fvtrrmlnmf rkg
//
LOCUS       WP_124209265             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_124209265
VERSION     WP_124209265.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53541
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav grafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_124207925             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_124207925
VERSION     WP_124207925.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38676
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eavgatvgga
       61 aeafgaelvl kvvapsatel aqmksgamlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera rqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_124209295             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria meningitidis].
ACCESSION   WP_124209295
VERSION     WP_124209295.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33551
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msqhrkliil gsgpagytaa vyaaranlnp viitgiaqgg qlmtttevdn wpadadgvqg
       61 pelmarflah aerfgteiif dqinavdlqk rpftlkgdmg eytcdaliva tgaaakylgl
      121 pseeafagkg vsacatcdgf fyknqdvavv gggntaveea lylaniaktv tlihrrsefr
      181 aekimidklm krveegkiil klesnlqevl gddrgvngal lknndgseqq iavsgifiai
      241 ghkpntdifk gqlemdeagy lktkggtadn vgatniegvw aagdvkdhty rqaitsaasg
      301 cqaaldaerw lgsqni
//
LOCUS       WP_124209669             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_124209669
VERSION     WP_124209669.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53704
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapaai aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_124209910             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_124209910
VERSION     WP_124209910.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53642
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglea
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_124211272             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vespertiliibacter pulmonis].
ACCESSION   WP_124211272
VERSION     WP_124211272.1
KEYWORDS    RefSeq.
SOURCE      Vespertiliibacter pulmonis
  ORGANISM  Vespertiliibacter pulmonis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Vespertiliibacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Vespertiliibacter pulmonis"
                     /db_xref="taxon:1443036"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33907
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mmatkhaqll ilgsgpagyt aavyaaranl npvlvtgiqq ggqltttsei enwpgefgei
       61 tgselmnkmq khaekfntei ifdhihsvdl sqrpftlqgd fntftcdali iatgasakyl
      121 glpseesykg rgvsacatcd gffyrnkpva vigggntave ealylsnias qvhlihrrdt
      181 frsekilier lmkkveegki ilhlncelde vlgndagvtg iriksikenn vtsltldgvf
      241 vaighmpntd mfagqlelnn gyivvksgle gnatatsveg vfaagdvmdh tyrqaitsag
      301 tgcmaaldae rfldnq
//
LOCUS       WP_124209937             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria meningitidis].
ACCESSION   WP_124209937
VERSION     WP_124209937.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33527
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msqprkliil gsgpagytaa vyaaranlnp viitgiaqgg qlmtttevdn wpadadgvqg
       61 pelmarflah aerfgteiif dqinavdlqk rpftlkgdmg eytcdaliva tgasakylgl
      121 pseeafagkg vsacatcdgf fyknqdvavv gggntaveea lylaniaktv tlihrrsefr
      181 aekimidklm krveegkiil klesnlqevl gddrgvngal lknndgseqq iavsgifiai
      241 ghkpntdifk gqlemdeagy lktkggtadn vgatniegvw aagdvkdhty rqaitsaasg
      301 cqaaldaerw lgsqni
//
LOCUS       WP_124211434             488 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Vespertiliibacter pulmonis].
ACCESSION   WP_124211434
VERSION     WP_124211434.1
KEYWORDS    RefSeq.
SOURCE      Vespertiliibacter pulmonis
  ORGANISM  Vespertiliibacter pulmonis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Vespertiliibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Vespertiliibacter pulmonis"
                     /db_xref="taxon:1443036"
     gene            1..488
                     /gene="nrfA"
     Protein         1..488
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=54746
     Region          4..484
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mryvsknfkn nltvvtatfl gclssawalv pdkyegpnpn lviesvnqkf aekyplqyds
       61 waatkestev idalnedprl vvlwggysfs haynkprghy yaitdvrsil rtgapkdens
      121 gpqpmacwtc kgpdiprlia ekgedgyfda kwakygseiv nqigcadchd ttsqdfkegk
      181 palrvarphv lralesigwk fdqldkhgkr vaicanchve yyfagktkav tfpwdkgvdv
      241 dsiekyydei efkdwthsls kapmlkaqhp dfeiwsmgth gkngvtcidc hmpkveakdg
      301 kiytdhkign pfdafdstck tcheqskesl qarvkshkke ikdvmvrled qlvkahfeak
      361 aawdagatet emkealedir haqwrwdysa ashggymhap dvilhvistg ldkaaeartk
      421 iarvlaahgv tkaieipdis tkekaqavig vdyakivrek eeflrtvvpq wekeakkkgl
      481 lpadaqtp
//
LOCUS       WP_124211890             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124211890
VERSION     WP_124211890.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33745
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvedl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv hlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124212678             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_124212678
VERSION     WP_124212678.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53705
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgsgf
      481 vtllafiail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_124215748             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria meningitidis].
ACCESSION   WP_124215748
VERSION     WP_124215748.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33611
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msqhrkliil gsgpagytaa vyaaranlnp viitgiaqgg qlmtttevdn wpadadgvqg
       61 pelmarflah aerfgteiif dqinavdlqk rpftlkgdmg eytcdaliva tgasakylgl
      121 pseeafagkg vsafatcdgf fyknqdvavv gggntaveea lylaniaktv tlihrrsefr
      181 aekimidklm krveegkiil klesnlqevl gddrgvngal lknndgseqq iavsgifiai
      241 ghkpntdifk gqlemdeagy lktkggtadn vgatniegvw aagdvkdhty rqaitsaasg
      301 cqaaldaerw lgsqni
//
LOCUS       WP_124215089             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_124215089
VERSION     WP_124215089.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53666
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthageipsp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflkhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_124217807             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rummeliibacillus sp. TYF005].
ACCESSION   WP_124217807
VERSION     WP_124217807.1
KEYWORDS    RefSeq.
SOURCE      Rummeliibacillus sp. TYF005
  ORGANISM  Rummeliibacillus sp. TYF005
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Caryophanaceae; Rummeliibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rummeliibacillus sp. TYF005"
                     /db_xref="taxon:2058214"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34192
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseekiydvv iigagpagmt aavytsrgnl stlmlergip ggqmanteev enypgfesil
       61 gpelstkmfe hakkfgaeya ygdvteivdg eeyktikagt keyktraiii stgaeykkmg
      121 vpgekelggr gvsycavcdg affknknliv vgggdsavee gmyltrfadk vtivhrrdkl
      181 raqkiiqdra fanekinfiw nntvkeihek dgkvgsvtlv stvdgteqev qadgvfiyig
      241 llpltkpfen lgilsetgyi ktnaemetsv pgiyaagdvr dktlrqivta tgdgsiaaqa
      301 vqhyveelke kfavk
//
LOCUS       WP_124216430             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Limosilactobacillus reuteri].
ACCESSION   WP_124216430
VERSION     WP_124216430.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus reuteri
  ORGANISM  Limosilactobacillus reuteri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Limosilactobacillus reuteri"
                     /db_xref="taxon:1598"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33203
     Region          7..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeskqydvv iigagpggmt aamyasranl svlmldrgiy ggnlnntaei enytgfksvr
       61 gpelaqqmye gatqfgaeya ygtvtkveld gdlkkittdm detytakavv iatgsdqrhl
      121 nvpgeeefgg rgvsycavcd gaffkgkhli vvgggdaave egvyltqlas kvtvlvrrde
      181 lraepiiqae amnndkiefv yntsvteivg ddikvtgvkt hnnktgedge maadgvfiyv
      241 gnfpmtaafk nldilddqgw vktdermrta vpgifaigdv retplrqvat avgdgaiagq
      301 qvyqyiksma
//
LOCUS       WP_124218763             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria meningitidis].
ACCESSION   WP_124218763
VERSION     WP_124218763.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33524
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msqhrkliil gsgpagytaa vyaalanlnp viitgiaqgg qlmtttevdn wpadadgvqg
       61 pelmarflah aerfgteiif dqinavdlqk rpftlkgdmg eytcdaliva tgasakylgl
      121 pseeafagkg vsacatcdgf fyknqdvavv gggntaveea lylaniaktv tlihrrsefr
      181 aekimidklm krveegkiil klesnlqevl gddrgvngal lknndgseqq iavsgifiai
      241 ghkpntdifk gqlemdeagy lktkggtadn vgatniegvw aagdvkdhty rqaitsaasg
      301 cqaaldaerw lgsqni
//
LOCUS       WP_124224184             538 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Tibeticola
            sediminis].
ACCESSION   WP_124224184
VERSION     WP_124224184.1
KEYWORDS    RefSeq.
SOURCE      Tibeticola sediminis
  ORGANISM  Tibeticola sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Tibeticola.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Tibeticola sediminis"
                     /db_xref="taxon:1917811"
     Protein         1..538
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56514
     Region          17..538
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msseatppaa apaaqcigvp revypgekrv atvpeiverl rklgfsvcve sgagaaasfs
       61 deayravgae iapdaaalwq radivfkvrp psaeevarmh agqtligfiw paqhpelmqq
      121 laaqkvtvla mdclprtlsr aqkmdaltsm agvsgyravi eaayvfgrff ngqitaagkv
      181 ppakvfvaga gvaglaaigt avglgaivra ndtrsevadq vvslggefvk vdyeeegsgg
      241 ggyakvmseg fqqaqremya kqarevdiii ttalipgkpa pklitaemvq tmkpgsvivd
      301 maaeqggnce ltvpgeavvr hgvtivgytd lpsrlakqss tlyatnllrl teelcktkdg
      361 vihinmedda irgltvikdg eitwpapppk lppaaakpav apaaaakkaa ahgevsgplp
      421 atrlavlaav aavlfwligr yappeflshf tvfvlacfvg ymvvwnvkpa lhtplmsvtn
      481 aissiiviga lvqisptgap erpddwirwl aaaavvltai nmfggfavtq rmlamfrk
//
LOCUS       WP_124221348             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aquisalibacillus elongatus].
ACCESSION   WP_124221348
VERSION     WP_124221348.1
KEYWORDS    RefSeq.
SOURCE      Aquisalibacillus elongatus
  ORGANISM  Aquisalibacillus elongatus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Aquisalibacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Aquisalibacillus elongatus"
                     /db_xref="taxon:485577"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34936
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mmeeriydvi iagagpaglt aavytsradl dtlmlergvp ggqmvntedv enypgynhil
       61 gpdlsnkmfe haqkfgaeyg fgdikeiidg keyktvkagn kefktraiil atgaeykklg
      121 ipgeeeyggr gvsycavcdg affrdkslfv vgggdsavee gvyltrfank vtiihrrdel
      181 raqkilqqra fdnekidfkw ntemkeikek dgkvgsavly nnetdetyee eiegvfiyig
      241 miplnqaftd lgitndegyv etnenmatni pgifaagdir dkelrqivta tgdgsiaaqs
      301 aqhyienlme elkvqq
//
LOCUS       WP_124221140             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tibeticola sediminis].
ACCESSION   WP_124221140
VERSION     WP_124221140.1
KEYWORDS    RefSeq.
SOURCE      Tibeticola sediminis
  ORGANISM  Tibeticola sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Tibeticola.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Tibeticola sediminis"
                     /db_xref="taxon:1917811"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34352
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 meqtlhskvl ilgsgpagyt aaiyaaranl qptlitgmaq ggqlmtttev dnwpgdvhgv
       61 qgpdlmqrll qhaerfrtqi ifdqihqvdl sqrpfrlkgd sghytcdali iatgasakyl
      121 glpseqafmg rgvsacatcd gffyrdevcc vvgggntave ealylsniak kvylihrrdk
      181 fraepimvdk lmekvqagki elktfrtvee vlgdasgvtg vrlrnvldgs lediavkgcf
      241 iaighspnta ifegqleldn gyivtqggrh gmatmtsvpg vfaagdvqdy vyrqaitsag
      301 tgcmaaldaq ryleqaggql
//
LOCUS       WP_124224399             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Coxiella burnetii].
ACCESSION   WP_124224399
VERSION     WP_124224399.1
KEYWORDS    RefSeq.
SOURCE      Coxiella burnetii
  ORGANISM  Coxiella burnetii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Coxiella.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Coxiella burnetii"
                     /db_xref="taxon:777"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34475
     Region          9..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnkpqhhsli ilgsgpagyt aaiyaaranl kpimitgmeq ggqlmtttdv dnwpgeapgl
       61 qgpqlmermq khaerldtqf vfdhineadl nqrpfllkgd natyscdali iatgasaryl
      121 glpsekaymg kgvsacatcd gffyrgkkva vvgggntave ealylshias hvtlihrrdk
      181 lraekmlsaq likkveegkv aivwshviee vlgddqgvtg vhlkhvkekk tqdltidglf
      241 iaighdpntk ifkeqlemde agylraksgl qgnatatnip gvfaagdvtd hvyrqaitaa
      301 gmgcmaalda eryldslnqa
//
LOCUS       WP_124229781             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium butyricum].
ACCESSION   WP_124229781
VERSION     WP_124229781.1
KEYWORDS    RefSeq.
SOURCE      Clostridium butyricum
  ORGANISM  Clostridium butyricum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Clostridium butyricum"
                     /db_xref="taxon:1492"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34241
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvkeikeldl iiigggpagl taaiyagrak lntlllenki lggqvrnsft ienypgfksi
       61 qggkladlfq eqaaefgavi defdliekid lseeekviet etfiykpkav iiatgavprk
      121 lpikgeknfa gkgihycavc dgamyegkni avvgggnaal eealfltkfa ekvylirryn
      181 yfkgeqsvid evfnhpkiev llnedvieak gqdflnsvvl kntldgivse lkvdavfgyi
      241 gtepkteevk kylnlneqgy iitnedmetn ikgvyaagdv rekkyrqitt avsdgtiall
      301 naekyilerk k
//
LOCUS       WP_124236019             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aeromicrobium camelliae].
ACCESSION   WP_124236019
VERSION     WP_124236019.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium camelliae
  ORGANISM  Aeromicrobium camelliae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Aeromicrobium camelliae"
                     /db_xref="taxon:1538144"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52623
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigivtesa agetrvsatp atvaqllklg ydvvvesgag arasftdday aeagavvvgt
       61 deawasdvvl kvnapndaei arvregatli sllspalnpd lvdklaarpi talamdavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksigge ylaveveeqm essdgyakat seaydrraae
      241 iyseqakdvd iiittalipg raaprlitaa dvasmkpgsv ivdmaaaqgg nvegsvpgek
      301 vvtangvtil gytdlagrlp tqasqlygtn lvnllklltp gkdgqlvldf ddvvqravtv
      361 ardgeklwpp ppvqvsaapa aapaaavpae pkpekpaltq qgkyalvalg vaalflvnaf
      421 apaplpqhft vltlavvigy yvigkvhhal htplmsvtna isgiivvgam lqlsvddpvi
      481 rtlafiavlv asinvfggfa vtrrmlsmfs kd
//
LOCUS       WP_124237680             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aeromicrobium camelliae].
ACCESSION   WP_124237680
VERSION     WP_124237680.1
KEYWORDS    RefSeq.
SOURCE      Aeromicrobium camelliae
  ORGANISM  Aeromicrobium camelliae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Aeromicrobium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Aeromicrobium camelliae"
                     /db_xref="taxon:1538144"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33939
     Region          7..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msevrnviii gsgpsgytaa vyaaranlep lvfegsvtag galmnttdve nfpgfpdgim
       61 gpelmdkfra qaerfgaeli addvtnvdla gpiktvslad grtfsaravi lamgsgyrkl
      121 glpgedrlsg hgvswcatcd gfffrgkeia vvgggdsave eatfltrfad kvtlihrrde
      181 lraskimaqr alanpkiefa wnsevaeihg dgtleavtlr dtrtgdtrql pvsglfiaig
      241 hdprsellig qvdlddegyv ltqpgstatn ipgvfaagdl vdhtyrqait aagtgcsaal
      301 daerylasfe eagepapaaa lte
//
LOCUS       WP_124240435             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas enteropelogenes].
ACCESSION   WP_124240435
VERSION     WP_124240435.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas enteropelogenes (Aeromonas trota)
  ORGANISM  Aeromonas enteropelogenes
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Aeromonas enteropelogenes"
                     /db_xref="taxon:29489"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52895
     Region          25..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivgshnkqt klglaalllt gllgsswaqa eestkgkiea rnelfakdha dqfsswkats
       61 dskersdala edpnmvvlwa gyafakdynk prghfyaltd vretlrtgap ktaedgplpm
      121 acwsckspdv arvideqged gyfkgmwakg gpeivntigc adchdtaske fkegkpalhl
      181 srpyadramt aigkpfkeqg rfdqqsqvcg qchveyyftg ptkavkfpwd dgtsveqmea
      241 yydelgfsdw thavsktpml kaqhpeyetw ragihgqnnv acvdchmpkv qneqgkvytd
      301 hkignpfdrf eqtcrnchtq skemlqgivk qrkdavvetk lkvekqlvra hfeakaawda
      361 gatdaemkdi lqdirhaqwr wdyaiashgv qmhapevalk vlggaldkaa dartklarll
      421 aakgisqeia ipdistkeka qaalgmdmkq fnsdkaqflk ttvpawdaea kaagrlaq
//
LOCUS       WP_124242867             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas jandaei].
ACCESSION   WP_124242867
VERSION     WP_124242867.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas jandaei
  ORGANISM  Aeromonas jandaei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas jandaei"
                     /db_xref="taxon:650"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53368
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mmvsshnrqs rlglaalllt tclgtsgwaq aadeaqskgk iearselfak dhadqftswk
       61 gtsesrertd alaedpqmvv lwagypfakd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta sqefkegkpa
      181 lhlsrpyadr amsaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgtsveq
      241 meayydelgf adwthalska pmlkaqhpey etwragihgq nnvacvdchm pkvqndqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg ivkqrkdavh elklkvekql vhthfeakav
      361 wdagateaem keilqdirha qwrwdyaias hgvqmhapev alkvlgsald kaadartkla
      421 rllaskgish eiaipdistk ekaqaalgmd mkqfnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_124246138             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gordonia sp. X0973].
ACCESSION   WP_124246138
VERSION     WP_124246138.1
KEYWORDS    RefSeq.
SOURCE      Gordonia sp. X0973
  ORGANISM  Gordonia sp. X0973
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Gordonia sp. X0973"
                     /db_xref="taxon:2742602"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34671
     Region          11..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstssddtia dviivgsgpa gytaaiyaar aelspivfeg tqfggelmtt tevenfpgfr
       61 agiqgpdlmd emreqalrfg adlrmedvdt irldgeikev evggevyrsk aiilamgaaa
      121 rylglddeqr llgrgvsaca tcdgfffkdn eiavigggds ameeatfltk fatkvylihr
      181 rdefrasrim ldrarnnpki efitntavdk ivgddsvtgl vlsdtrtget rdlpvtgmfv
      241 aighdprsel vagqvdrdea gyvltegrss ytsvpgvfaa gdlvdhtyrq aitaagsgca
      301 aaidaerwla draaeptkqa aaaqs
//
LOCUS       WP_124244202             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas caviae].
ACCESSION   WP_124244202
VERSION     WP_124244202.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53090
     Region          29..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsydklf rpglaalllt vllgagslaq addsapkgki earselfakd hadqftswkg
       61 tseskertda laedpqmvvl wagypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eeyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfdqtcrnch tqskemlqgv vkqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaemk gilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llaakgishe iaipdisske kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_124247552             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Gordonia
            sp. X0973].
ACCESSION   WP_124247552
VERSION     WP_124247552.1
KEYWORDS    RefSeq.
SOURCE      Gordonia sp. X0973
  ORGANISM  Gordonia sp. X0973
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Gordonia sp. X0973"
                     /db_xref="taxon:2742602"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52251
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpresk sgetlvaata ktvaqlqqlg ydvvveagag qraeqadtaf seagarigsa
       61 devwgadvvv kvnaptdaei arlrrgatvi smmapgrspe lleklqqagv tglamdavpr
      121 israqsmdvl ssqanvagyr avveaahefg rmftgqvtaa gkipparvfv vgagvaglaa
      181 igaasamgai vrafdvrpev aeqvesmgae fvnvdfeaek sadgyakemt aeqeaatasm
      241 ydeearaadi vittalipgr papklitaet vaamhngsvv vdmaaanggn vagtvadekv
      301 vtdngvtilg ytdlagrlaa qtsqlygtni vnllklitpg kdgeltldmd dvvqrgitvt
      361 rdgegmwppp pvqvsaapqa aaaapapvae pkapmapakk vaislagill fgaliafapk
      421 plpahftvlm laivigyyvi gnvahalhtp lmsvtnaisg vvvvgallql atdnltiril
      481 atiailvasi nvfggfavtr rmlamfskga
//
LOCUS       WP_124250052             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas dhakensis].
ACCESSION   WP_124250052
VERSION     WP_124250052.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53452
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tvlgtsgwaq aadeaqpkgk iearselfak dhadqfsswk
       61 atgesrertd alaedpnmvv lwagyafakd ynkprghfya ltdvretlrt gapksaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy ftgptkavkf pwdkgttveq
      241 meqyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg mvkqrkdaih dlklrvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakglsq eiaipdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeaktagrla
      481 q
//
LOCUS       WP_124249852             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aeromonas dhakensis].
ACCESSION   WP_124249852
VERSION     WP_124249852.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34111
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msqvthskll ilgsgpagyt aavyaaranl npllitgmqq ggqlttttev enwpgdpegl
       61 tgpalmermk ehaekfdtri lfdhinevel tqrpfrlkgd ngeytcdali iatgasakyl
      121 glpseeafkg rgvsacatcd gffyrnqeva vvgggntave ealylaniak kvhlihrrde
      181 fraekilikr lhdkvasgni vlhthqtlde vlgddmgvtg vrlrntqndt ttdlplmgvf
      241 iaighqpntq ifdgqlemqn gylkvrggld gfatqtsieg vfaagdvadh tyrqaitsag
      301 tgcmaaldte ryldaq
//
LOCUS       WP_124265737             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. ADI98-10].
ACCESSION   WP_124265737
VERSION     WP_124265737.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. ADI98-10
  ORGANISM  Streptomyces sp. ADI98-10
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Streptomyces sp. ADI98-10"
                     /db_xref="taxon:1522763"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34634
     Region          10..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msagtdirnv ivigsgpagy taalytarad lkplvfegsv taggalmntt evenfpgfpe
       61 givgpdlmdn mraqatrfga elipddivav eltgdiktvt dssggihrar avivttgsqh
      121 rklnlerede lsgrgvsyca tcdgfffrdr divvvgggdt ameeatfltr farsvtvvhr
      181 rsalrasqvm qsrafaddki sfaldseiae ikeedgalsg lvlrdtvsgr trdldatglf
      241 vaighdprte lfagqldldg egylkveapt trtnvpgvfg agdvvdhtyr qaitaagsgc
      301 aaaldaeryl aaltdteava epektpaav
//
LOCUS       WP_124269103             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. ADI96-02].
ACCESSION   WP_124269103
VERSION     WP_124269103.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. ADI96-02
  ORGANISM  Streptomyces sp. ADI96-02
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces sp. ADI96-02"
                     /db_xref="taxon:1522760"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34143
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslnp lvfegavtag galmnttdve nfpgfqdgim
       61 gpelmdnmra qaerfgaeli pddvvavdlt geiktvtdtv gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdhdia vvgggdtame eatflsrfak svtivhrrdt
      181 lraskamqdr afadpkisfa wdsevaevkg eqklssltlr ntktgetsel avtglfiavg
      241 hdprtelfkg qlelddegyl kveapstrtn qtgvfgagdv vdhtyrqait aagtgcsaal
      301 daerylaala daqpaepekt pav
//
LOCUS       WP_124277463             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. ADI93-02].
ACCESSION   WP_124277463
VERSION     WP_124277463.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. ADI93-02
  ORGANISM  Streptomyces sp. ADI93-02
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Streptomyces sp. ADI93-02"
                     /db_xref="taxon:1522757"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34153
     Region          6..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msvisdvvii gsgpagytaa lytaraqlrp vlfgssifvg gsltttteve nfpgfpegvd
       61 gpdlmakmra qaekfgaemi ddditdvdlt gpvklltdsn gtvhqartvi vatgsgyrkl
      121 gvpgeeelsg rgvswcatcd gfffrdrdiv vvgggdtame eatfltrfak svtvvhrrsa
      181 lraskvmqnr afaddkisfa fdtevaelrq egtmlggivl rdvlsgatre vaatglfiai
      241 ghdprtelfr gqldldeegy lkvsspttrt nlpgvfgagd vvdhtyrqav taagsgasaa
      301 ldaerylagl psgdladasi tsvava
//
LOCUS       WP_124281865             323 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_124281865
VERSION     WP_124281865.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34151
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfqdgim
       61 gpelmdnmra qaerfgaeli pddvisvdlt gdiktvtdta gtvhhakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrds
      181 lraskamqdr afadpkikfa wdsevaaihg dqklasltlr ntkngetsel aatglfiavg
      241 hdprtelfkg qldlddegyl kveapstrtn lkgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaals deklaepekt pav
//
LOCUS       WP_124291992             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium sp. ABRD28].
ACCESSION   WP_124291992
VERSION     WP_124291992.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. ABRD28
  ORGANISM  Microbacterium sp. ABRD28
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Microbacterium sp. ABRD28"
                     /db_xref="taxon:2268461"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34565
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrhviiigsg pagytaaiya aranleplvi assveaggel mnttevenfp gfpegiqgpe
       61 lmakmqeqae kfgaevvydd vvsleldgdv krvtlgsgas heaesivfat gsaprkigie
      121 gesrlsgrgv sycatcdgff frerviavvg ggdsameeat fltkfaskvy vihrrdelra
      181 skimqdrafk ndkiefvwns evvdilgeea vtglvlestl dgsrrelald gifvaigydp
      241 rvhlvhgkld ltdagtvwvd grssrtsvpg vfaagdvidp tyrqavtaag sgtvaaldve
      301 hylaalgeag epapdvaeid nlpsvna
//
LOCUS       WP_124297112             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acetobacter pasteurianus].
ACCESSION   WP_124297112
VERSION     WP_124297112.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter pasteurianus
  ORGANISM  Acetobacter pasteurianus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Acetobacter pasteurianus"
                     /db_xref="taxon:438"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33028
     Region          8..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 maetittdll vigagpagyt aaiyaaranl spvlvaglqp ggqltittev enypgfatai
       61 qgpwlmeqma eqaqnvgtri eydiitsvdf kagspflltg dsgtiykara vvvatgaqar
      121 wlglpsekhl qgagvsacat cdgffyrgkn vvvvgggnta veealylthh aahvtlvhrr
      181 dslrsekilq drlfanpkvs viwnsvvedi ladgtpetvc gvqlkntqdg skqtiptdgv
      241 fiaighapnt aifrdqltld segyiettpg ttrtsvpgvf aagdvqdkty rqavtaagtg
      301 cmaaldaery lagla
//
LOCUS       WP_124300993             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas chlororaphis].
ACCESSION   WP_124300993
VERSION     WP_124300993.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38635
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllathyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvdngv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124301148             320 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Pseudomonas].
ACCESSION   WP_124301148
VERSION     WP_124301148.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33865
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmermr ehaerfetei vfdhinavdf aakpytltgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias kvtlihrrdi
      181 fraekilidk lnarvaegki elklnanlde vlgdnmgvtg arlknndgsf deikvdgvfi
      241 aightpntsl fegqlelkdg ylvvqggreg natatsiegi faagdvadhv yrqaitsaga
      301 gcmaaldter yldglqnasf
//
LOCUS       WP_124309027             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_124309027
VERSION     WP_124309027.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33447
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mteakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq thaerfdtei vydhihtael qqrpfvlkgd sgvyscdali iatgasaqyl
      121 glpseetfag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlvhrrdk
      181 lraekilqdk lfdkaakgni rlhwnqnlde vlgdasgvtg arlrdslsge iqelaltgvf
      241 iaighkpntd lfkgqlemrd gyllvkggse gdatatgipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kflddn
//
LOCUS       WP_124311615             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_124311615
VERSION     WP_124311615.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33459
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mteakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtael qqrpfvlkgd sgvyscdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vigggntave ealylsniak evhlvhrrdk
      181 lraekilqdk lfdkaakgni rlhwnqnlde vlgdasgvtg arlrdslsge tqelaltgvf
      241 iaighkpntd lfkgqlemrn gyllvkggse gdatatgipg vfaagdvadh vyrqaitsag
      301 agcmaaldae kflddn
//
LOCUS       WP_124314992             300 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas chlororaphis].
ACCESSION   WP_124314992
VERSION     WP_124314992.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..300
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34059
     Region          5..162
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mavtdlfskr qqrlrgevsd vyvydkipip lriqllymvd ellgpaleyy kpfsvcnqif
       61 kavvktlrle ygkrrissae endeyhelvs fikneenvdr lldaieliva nvsgysgyde
      121 slvefvgdln irfrehavgy eiingevvrv dsrfmhsqvv kpsiqflnqp gfegaqqefi
      181 rayehyrhar hkeaineavk svestmraic tarnwrfkts dsakrlivvc qennlfpsyy
      241 qshlaalasl megvvsirnn esahgqgpkv revdadivay glhmaaaavl mlaslhtnqp
//
LOCUS       WP_124315260             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_124315260
VERSION     WP_124315260.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33575
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mteakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtael qqrpfvlkgd sgvyscdali iatgasaqyl
      121 glpseetfag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlvhrrdk
      181 lraekilqdk lfdkaakgni rlhwnqnlde vlgdasgvtg arlrdrlsge trelaltgvf
      241 iaighkpntd lfkgqlemrd gyllvkggse gdatatgipg vfaagdvadh vyrqavtsag
      301 agcmsaldae kflddn
//
LOCUS       WP_124319193             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_124319193
VERSION     WP_124319193.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33911
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmermr ehaerfetei vfdhinavdf aakpytltgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias kvtlihrrdt
      181 fraekilidk lnarvaegki elklnanlde vlgdnmgvtg arlknndgsf deikvdgvfi
      241 aightpntsl fedqlelkdg ylvvqggreg natatsiegi faagdvadhv yrqaitsaga
      301 gcmaaldter yldglqnasf
//
LOCUS       WP_124321357             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_124321357
VERSION     WP_124321357.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33462
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mteakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtael qqrpfvlkgd sgvyscdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vigggntave ealylsniak evhlvhrrdk
      181 lraekilqdk lfdkaakgni rlhwnqnlde vlgdasgvtg arlrdsltge tqelalagvf
      241 iaighkpntd lfkgqlemrd gyllvkggse gdatatgieg vfaagdvadh vyrqavtsag
      301 agcmaaldae kflddn
//
LOCUS       WP_124327192             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Desulfonema ishimotonii].
ACCESSION   WP_124327192
VERSION     WP_124327192.1
KEYWORDS    RefSeq.
SOURCE      Desulfonema ishimotonii
  ORGANISM  Desulfonema ishimotonii
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfococcaceae; Desulfonema.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Desulfonema ishimotonii"
                     /db_xref="taxon:45657"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33401
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkknadydlv iigggpaglt aglyaararl ktvlvekvvp ggqvlitdwv enypgfpegi
       61 tgtdlvkhmt gqaqrfglei eadevisvdh gpgpvrtirl tgktitahav ivatgatpkk
      121 lgvpgedmff gkgisscatc dgpfyknrvv aavgggdtav qesvfltkfa ekvylihrrd
      181 rfraekilqe ralandriev lwdtvvtgvs glthvenlhi rnvrtgesrs lradaffiwi
      241 gikpnaafld drverdefgf irandrmets vpgifaagdv rstplrqiat avgdaaiaas
      301 saehyienle
//
LOCUS       WP_124329880             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Desulfonema ishimotonii].
ACCESSION   WP_124329880
VERSION     WP_124329880.1
KEYWORDS    RefSeq.
SOURCE      Desulfonema ishimotonii
  ORGANISM  Desulfonema ishimotonii
            Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
            Desulfobacterales; Desulfococcaceae; Desulfonema.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Desulfonema ishimotonii"
                     /db_xref="taxon:45657"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34676
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetrnydlv iigggpggls agiyamraal ktvlvekgap ggqvtmsdev enypgfahis
       61 ggelsmkfse hadsygleti sdevaavepg leyhsvrleg gdvlkthsvi latggsprkl
      121 gipgedeyyg kgvsycavcd gfffrnktvv vigggdsaae ealylskiak kvylvhrrda
      181 lragmllqqr vkaeckieil wntvptdika desgvcgigl qdtlsgekre matdgvfifi
      241 gfnpanalvp agtkmnadgy vvtdekcetq mpgifvigdl rekyarqivi saadgctaal
      301 aaahyvetkk seedfceape glleen
//
LOCUS       WP_124338675             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_124338675
VERSION     WP_124338675.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33442
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mteakhsrli ilgsgpagys aavyaaranl kptviaglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtael qqrpfvlkgd sgvyscdali iatgasaqyl
      121 glpseetfag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlvhrrdk
      181 lraekilqdk lfdkaakgni rlhwnqnlde vlgdasgvtg arlrdsltge pkelaltgvf
      241 iaighkpntd lfkgqlemrd gyllvkggse gdatatgipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kflddn
//
LOCUS       WP_124338820             312 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas chlororaphis].
ACCESSION   WP_124338820
VERSION     WP_124338820.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..312
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34870
     Region          5..170
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifdlyskr qrrsrgevsd vytydifpsa frmqlsymvq dllgdgsmyn riyqareayt
       61 eivrilrkey gkqtlskihq tdpfselhnf llqepdverc ldaielcyal gddmvrsvsy
      121 agrtdgdthv decltelner fkeaglgyel idgrivrids qllhseivkp aigflnaegf
      181 egardeffga yehyrhgyhe ealvdalkaf estmkvilva nektygagdt asklilacrd
      241 aglmpaynes qlsslvnvlt sgiptlrnkn gghgqgeavr tvepeivayg lhltasaivm
      301 lagleskrrt al
//
LOCUS       WP_124340452             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_124340452
VERSION     WP_124340452.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33487
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mteakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtael qqrpfilkgd sgvyscdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vigggntave ealylsnlak evhlvhrrdk
      181 lraekilqdk lfdkaakgni rlhwnqnlde vlgdasgvtg arlrnslsge trelaltgvf
      241 iaighkpntd lfkgqlemrd gyllvkggse gdatatgipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kflddn
//
LOCUS       WP_124341018             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Cellulomonas algicola].
ACCESSION   WP_124341018
VERSION     WP_124341018.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas algicola
  ORGANISM  Cellulomonas algicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Cellulomonas algicola"
                     /db_xref="taxon:2071633"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52921
     Region          4..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mttigvprea rpgerlvaat pktvaqlral gydvlvehga gagatfddaa yeaagattvd
       61 aaqawgadvv tavgapdveq vaglrpdavl vamlnpggra dlvdaltarg vtalsldavp
      121 risraqsldv lstlsnvagy ravveaaqey ggmfagqvta agktppakvf vigagvagla
      181 aigaadslga qvrafdvrpe vgeqiesmga tfvraesaqq qvsadgyasa ltqdqeaata
      241 avyaaetaga dvvittalvr gtaprtitaa mvagmrpgsv ivdlaasggg nceltvpger
      301 vvtengvvil gwtdlagrlp qhtsqlfgtn vvhllqlltp gkdgelvldl ddpvqrgmtv
      361 tragevlwpp ppvavsaamp ppadtapsle eiaaaeaaah alaerrtqrr tvtfalaavl
      421 valavsfapa aflghftvfv lavfvgyyvi snvshslhtp lmaqtnaisg iilvgallqi
      481 gsddwvvtvl acvaaavasv nifggflvan rmirmfrkda
//
LOCUS       WP_124341051             336 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Cellulomonas algicola].
ACCESSION   WP_124341051
VERSION     WP_124341051.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas algicola
  ORGANISM  Cellulomonas algicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Cellulomonas algicola"
                     /db_xref="taxon:2071633"
     gene            1..336
                     /gene="trxB"
     Protein         1..336
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35101
     Region          10..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdqpstvrd lvivgsgpag ytaaiyaara glaplvvags vtaggalmnt tevenfpgfp
       61 dgiqgpelmd alqkqaekfg aevlwddava lslegdvktv tvsggetyaa ravilstgsa
      121 yrelglddek rlsgrgvswc atcdgfffrd qeiivvgggd saveeatflt rfgkrvtlvh
      181 rrdqlraski madraasdpk iefawnsevv aihgedkvtg vtlrdtvtge trehsatgvf
      241 vaighvprtd llvgqveldd ngyvsvvgrs trtnlpgvfa agdvvdhtyr qaitaagsgc
      301 aaaldaqhyl aalgdtahdv vdpvpttvap vlvqev
//
LOCUS       WP_124345424             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_124345424
VERSION     WP_124345424.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38681
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvpdsay eaagatigna
       61 ndafgaelil kvvapndsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswmq
      241 rqalavhera kqadvvitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124348958             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas chlororaphis].
ACCESSION   WP_124348958
VERSION     WP_124348958.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38604
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvvdsay eaagatigsa
       61 ndafgaelil kvaapsdnel aliksgtvlv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvvdlaa aqggncpltv
      301 adqvvvengv tivgptnlag avaadasaly arnlldflkl vftkegqfev nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124351657             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_124351657
VERSION     WP_124351657.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33518
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mteakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtael qqrpfilkgd sgvyscdali iatgasaqyl
      121 glpseetfag kgvsacatcd gffyrnqiva vigggntave ealylsniak evhlvhrrdk
      181 lraekilqdk lfdkaakgni rlhwnqnlde vlgdasgvtg arlrdsltge tqelaltgvf
      241 iaighkpntd lfkgqlemrd gyllvkggse gdatatgipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kflddn
//
LOCUS       WP_124355216             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas chlororaphis].
ACCESSION   WP_124355216
VERSION     WP_124355216.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33476
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mteakhsrli ilgsgpagys aavyaaranl kptvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfdtei vydhihtael qqrpfvlkgd sgvyscdali iatgasaqyl
      121 glpseetfag kgvsacatcd gffyrnqvva vigggntave ealylsniak evhlvhrrdk
      181 lraekilqdk lfdkaakgni rlhwnqnlde vlgdasgvtg arlrdslsge tqelaltgvf
      241 iaighkpntd lfkgqlemrd gyllvkggse gdatatgipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kflddn
//
LOCUS       WP_124356473             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas orientalis].
ACCESSION   WP_124356473
VERSION     WP_124356473.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas orientalis
  ORGANISM  Pseudomonas orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas orientalis"
                     /db_xref="taxon:76758"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38690
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasivdsay etagatlgsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kladivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftqegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124359783             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas orientalis].
ACCESSION   WP_124359783
VERSION     WP_124359783.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas orientalis
  ORGANISM  Pseudomonas orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas orientalis"
                     /db_xref="taxon:76758"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33864
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermk ehaerfetei vfdhinkvdf srkpysltgd sgvytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlvhrret
      181 fraekilidk lharvaegki ilklnatlde vlgdnmgvtg arlknndgsf deltvdgvfi
      241 aightpntsl fegvleakdg ylvvqggreg natatniegi faagdvadhv yrqaitsaga
      301 gcmaaldaer yldglkdatf
//
LOCUS       WP_124360670             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. R3-52-08].
ACCESSION   WP_124360670
VERSION     WP_124360670.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. R3-52-08
  ORGANISM  Pseudomonas sp. R3-52-08
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. R3-52-08"
                     /db_xref="taxon:1173284"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38745
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkapil lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124364362             320 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Pseudomonas].
ACCESSION   WP_124364362
VERSION     WP_124364362.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33835
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermk ehaerfetei vfdhinkvdf skkpysltgd sgvytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlvhrret
      181 fraekilidk lharvaegki ilklnatlde vlgdnmgvtg arlknndgsf delkvdgvfi
      241 aightpntsl fegvleakdg ylvvqggreg natatnidgi faagdvadhv yrqaitsaga
      301 gcmaaldaer yldglkdasf
//
LOCUS       WP_124365312             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_124365312
VERSION     WP_124365312.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38680
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124375760             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas synxantha].
ACCESSION   WP_124375760
VERSION     WP_124375760.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas synxantha
  ORGANISM  Pseudomonas synxantha
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas synxantha"
                     /db_xref="taxon:47883"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38752
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqsgag vnasivdsay etagatigsa
       61 sdafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklaersit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera rqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124372761             309 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas chlororaphis].
ACCESSION   WP_124372761
VERSION     WP_124372761.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas chlororaphis
  ORGANISM  Pseudomonas chlororaphis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Pseudomonas chlororaphis"
                     /db_xref="taxon:587753"
     Protein         1..309
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34774
     Region          5..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mgihdlfskr qkrargevpd vyiydelpgs lriqivhiir dafgtdhygh nlseglydyv
       61 nkvlckeygv fhlttkrpyy tsesifeffl qekqaerald vielcfnivs gyiasnqdny
      121 syftdrgvea edavselner frehgvgyqf esgeiirvds eflhaeavkp tlrvlrgekf
      181 eganeeflsa hehyrhgrhk eclvdalksf estmkaicel rgwtvqpgdt aknlittcln
      241 ngllpsylss qvgtlrslle sgiptvrnkn gghgqgaapi avpeffarya lnltattilf
      301 lveahaann
//
LOCUS       WP_124381927             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Ralstonia sp. SET104].
ACCESSION   WP_124381927
VERSION     WP_124381927.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia sp. SET104
  ORGANISM  Ralstonia sp. SET104
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Ralstonia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Ralstonia sp. SET104"
                     /db_xref="taxon:2448774"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34110
     Region          2..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 makhakvlil gsgpagytaa iyaaranlnp vlvtglaqgg qlmtttdven wpadkehlqg
       61 pelmqrfleh aerfktevlf dhihtahlne kpirlvgdsg eytcdalivs tgasaqylgl
      121 pseetfagrg vsacatcdgf fykgqevavv gggntaveea lylaniaskv tlihrrdkfr
      181 aepilidrlh dqekkgkiei ktnmvldeil gddsgvtgar lkgthenegk veevklagvf
      241 iaighkpntd ifrgqldmnd tgyirtksgl dgmatatnip gvfaagdvqd hiyrqaitsa
      301 gtgcmaalda qrylesle
//
LOCUS       WP_124383925             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ralstonia
            sp. SET104].
ACCESSION   WP_124383925
VERSION     WP_124383925.1
KEYWORDS    RefSeq.
SOURCE      Ralstonia sp. SET104
  ORGANISM  Ralstonia sp. SET104
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Ralstonia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Ralstonia sp. SET104"
                     /db_xref="taxon:2448774"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39259
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipqetr adetrvaatp etvkkyvalg hqvtvqsgag vaaaqpdeay vaagakigta
       61 aealgaqivl kvrspeaael aqmqagavli gmlnpfdden tarlaaanvt afaleaaprt
      121 traqsmdvls sqaniagyka vmvaanhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfltdee reiaqgvggy arpmppdwmr
      241 rqaelvhtra sqadivitta lipgrraptl lseatvqamk pgsvvvdlaa aqggncplte
      301 adrvvvkhgv tlvgytnlas mvaadasaly arnvldflkl ivdkdgglvi nreddivaac
      361 llsqagqvvr apaatsaak
//
LOCUS       WP_124384526             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. R5-89-07].
ACCESSION   WP_124384526
VERSION     WP_124384526.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. R5-89-07
  ORGANISM  Pseudomonas sp. R5-89-07
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. R5-89-07"
                     /db_xref="taxon:658644"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38747
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigga
       61 ndafgaelil kvvapsdsel alinsgtvlv gmlnpfsnet iaklaerdit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124392365             327 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Rhodococcus].
ACCESSION   WP_124392365
VERSION     WP_124392365.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34540
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpstvhel iivgsgpagy taavyaarae leplqfegtq fggalmttte venfpgfreg
       61 imgpdlmdqm reqakrfgtd irtedveeld ltgpikkvvv ngetyqahav vlamgaaary
      121 lgipgeekll grgvsacatc dgfffkdqdi vvvgggdsam eeatfltrfa rsvtvvhrre
      181 efrasrimle rakanakirf vtnaapvevl gensvtglvi rdtvtgetst ldvtgmfvai
      241 ghdprselvk gqvdldeagy vivqnpstat svdgvfaagd lvdhiyqqai taagtgcsaa
      301 mdaerwlaer gditantvaa agspvda
//
LOCUS       WP_124393521             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus wratislaviensis].
ACCESSION   WP_124393521
VERSION     WP_124393521.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus wratislaviensis
  ORGANISM  Rhodococcus wratislaviensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus wratislaviensis"
                     /db_xref="taxon:44752"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37964
     Region          13..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqsasta rptigvvres ndgerrvalv pkivasliak gidvvvesga glgalipdel
       61 ytgagakiad pwsadvivkv appsdeevgr lhagqtligf laprnqdnqv aalkaagvqa
      121 faveaipris raqvmdalss qanvsgyksv llaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrat gydvrpevad qvrsvgaqwl dlgidaageg gyareltede
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvvvdl agetggncel
      301 tepgqtvvkh gvticsplnl pasmpehase lysknisall elmlvdgala pdfsdevlaa
      361 scvtreegvs
//
LOCUS       WP_124397987             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thermaurantimonas aggregans].
ACCESSION   WP_124397987
VERSION     WP_124397987.1
KEYWORDS    RefSeq.
SOURCE      Thermaurantimonas aggregans
  ORGANISM  Thermaurantimonas aggregans
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Schleiferiaceae; Thermaurantimonas.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Thermaurantimonas aggregans"
                     /db_xref="taxon:2173829"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33986
     Region          4..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqhkcviig sgpagytaai yaaranlkpi mytglevggq lttttevenf pgypdgvmgp
       61 qmmedlkrqa erfhtdvrfg mvtkvefste kggwhtltid dekqiqartv iiatgasaky
      121 lglesekrlm ghgvsacavc dgffykgkev vlvgggdaac eeaiylsklc pkvtmlvrsd
      181 kmraskimqe rvfktpniev lfntetidli gdhavegvkv lskkenreyv ipaygffvai
      241 ghkpntdifk gqidmdetgy iktipgtskt nlpgvfavgd vqdkvyrqav taagsgcmga
      301 ldaerylaei eea
//
LOCUS       WP_124402615             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. R3-18-08].
ACCESSION   WP_124402615
VERSION     WP_124402615.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. R3-18-08
  ORGANISM  Pseudomonas sp. R3-18-08
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. R3-18-08"
                     /db_xref="taxon:1173283"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38742
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaehgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera rqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124405931             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_124405931
VERSION     WP_124405931.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38708
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera rqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124408737             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. R4-34-07].
ACCESSION   WP_124408737
VERSION     WP_124408737.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. R4-34-07
  ORGANISM  Pseudomonas sp. R4-34-07
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. R4-34-07"
                     /db_xref="taxon:658642"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38734
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrppvk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera rqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124413459             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_124413459
VERSION     WP_124413459.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38773
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel vliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkapil lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124421871             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas orientalis].
ACCESSION   WP_124421871
VERSION     WP_124421871.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas orientalis
  ORGANISM  Pseudomonas orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas orientalis"
                     /db_xref="taxon:76758"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38649
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg htvtvqsgag vnasivdsay etagatlgsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kladivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftqegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124424957             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas orientalis].
ACCESSION   WP_124424957
VERSION     WP_124424957.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas orientalis
  ORGANISM  Pseudomonas orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas orientalis"
                     /db_xref="taxon:76758"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33821
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermk ehaerfetei vfdhinkvdf skkpysltgd sgvytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlvhrret
      181 fraekilidk lharvaegki ilklnatlde vlgnnmgvtg arlknndgsf deltvdgvfi
      241 aightpntsl fegvleakdg ylvvqggreg natatniegi faagdvadhv yrqaitsaga
      301 gcmaaldaer yldglkdasf
//
LOCUS       WP_124427503             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas orientalis].
ACCESSION   WP_124427503
VERSION     WP_124427503.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas orientalis
  ORGANISM  Pseudomonas orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas orientalis"
                     /db_xref="taxon:76758"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33891
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermk ehaerfetei vfdhinkvdf srkpysltgd sgvytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlvhrret
      181 fraekilidk lharvaegki ilklnatlde vlgdnmgvtg arlknndgsf delkvdgvfi
      241 aightpntsl fegvleakdg ylvvqggreg natatniegi faagdvadhv yrqaitsaga
      301 gcmaaldaer yldglkdatf
//
LOCUS       WP_124425712             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas orientalis].
ACCESSION   WP_124425712
VERSION     WP_124425712.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas orientalis
  ORGANISM  Pseudomonas orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas orientalis"
                     /db_xref="taxon:76758"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38660
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasivdsay etagatlgga
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kladivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftqegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124431000             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas orientalis].
ACCESSION   WP_124431000
VERSION     WP_124431000.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas orientalis
  ORGANISM  Pseudomonas orientalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas orientalis"
                     /db_xref="taxon:76758"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38720
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasivdsay etagatlgsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet itklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpsswmq
      241 rqalavhera kladivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124434780             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_124434780
VERSION     WP_124434780.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38733
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 ndafgaelil kvvapsdsel aliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124440741             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. NL15-2K].
ACCESSION   WP_124440741
VERSION     WP_124440741.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NL15-2K
  ORGANISM  Streptomyces sp. NL15-2K
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces sp. NL15-2K"
                     /db_xref="taxon:376149"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34216
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfqdgim
       61 gpelmdnmra qaerfgaeli pddivnvdlt geiktvidtt gtvhkakavi vatgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtvvhrrdt
      181 lraskamqdr afadpkikfv wdsevaevqg dqkltglklr nvktgelsdl avtglfiaig
      241 hdprtelfkg qleldeegyl kvdapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala deekaepekt sv
//
LOCUS       WP_124444654             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. NL15-2K].
ACCESSION   WP_124444654
VERSION     WP_124444654.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. NL15-2K
  ORGANISM  Streptomyces sp. NL15-2K
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces sp. NL15-2K"
                     /db_xref="taxon:376149"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33452
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrnvivigsg pagytaalyt araslkplvf egavtaggal vqttevenfp gfrdgimgpd
       61 lmdnmraqae rfgaelvpdd iveadltgtv ktvtdsagtv hraqavivat gsqhrqlglp
      121 gedalsgrgv sycatcdgff frehdivvvg ggdtaleeat flsrfaksvt ivhrrdalra
      181 skamqdrafa dpkisfawnr evaavhedgg klagltlrdt atgetselaa tglfvaighd
      241 prtdlvtgql dlddegylqv aspstrtniv gvfgagdvvd htyrqaitaa gsgcaaalda
      301 erylaaladn eknpepaava v
//
LOCUS       WP_124447754             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paucibacter sp. KBW04].
ACCESSION   WP_124447754
VERSION     WP_124447754.1
KEYWORDS    RefSeq.
SOURCE      Paucibacter sp. KBW04
  ORGANISM  Paucibacter sp. KBW04
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paucibacter sp. KBW04"
                     /db_xref="taxon:2153361"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34105
     Region          10..314
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mtsapqhhsl lilgsgpagy taaiyaaran lkptlltgma qggqlmttte vdnwpadvmg
       61 vqgpelmqrf qehaerfqtq ivfdhihtvd fskrpftlig dsatytcdal iiatgasaky
      121 lglpseetfa grgvsacatc dgffyrgqev cvvgggntav eealylsnia skvhvihrrd
      181 kfraepilid klsekaksgn vvlhlwntld evlgdqsgvt gvrikstqdg stqdlalqgc
      241 fiaighqpnt difkgqlemk dgyivtksgl ngfatmtsvp gifaagdvqd hiyrqaitsa
      301 gtgcmaalda qryleqeqg
//
LOCUS       WP_124448955             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paucibacter sp. KBW04].
ACCESSION   WP_124448955
VERSION     WP_124448955.1
KEYWORDS    RefSeq.
SOURCE      Paucibacter sp. KBW04
  ORGANISM  Paucibacter sp. KBW04
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Roseateles.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Paucibacter sp. KBW04"
                     /db_xref="taxon:2153361"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38485
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpresa agetrvaatp etikklkaqg hvlrvergag laasvtdeaf aaagaelvdr
       61 geafaadlll kvrspdadel slvkpgtalv gmlnpfdrag lqalataqlt sfaleaaprt
      121 sraqsmdvls sqaniagyka vmmaaeryqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf ievsydtpee keaaegvggy akpmpqswld
      241 rqkievakrv aqadvvitta lipgraapvl vteemvrsmk agsvivdlaa aaggncplte
      301 agrtvvkhgv tlvgetnlpa lvaadasaly arnvldflkl vltkegtlqv pmdddivaac
      361 lvtqsgsvlr s
//
LOCUS       WP_124449006             320 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Burkholderia].
ACCESSION   WP_124449006
VERSION     WP_124449006.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34131
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlitgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfq ehaerfntei vfdhihtakl heqpirligd sgeytcdsli iatgasaqyl
      121 glpseelfmg kgvsacatcd gffyrgqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegvv dikwdhvlde vtgeesgvtg lriknvktga tedlavqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglh gnatstsvag vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_124457905             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Variovorax sp. KBW07].
ACCESSION   WP_124457905
VERSION     WP_124457905.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. KBW07
  ORGANISM  Variovorax sp. KBW07
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Variovorax sp. KBW07"
                     /db_xref="taxon:2153358"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34115
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msapqhakvl ilgsgpagyt aavyaaranl kpllitgiaq ggqlmtttev dnwpadvhgv
       61 qgpelmqrfl ehaerfktqi vfdhinkvdl skrpftltgd sgtytcdsli iatgasakyl
      121 gldseekfmg rgvsacatcd gffyreqevc vigggntave ealylsnian kvtlvhrrdk
      181 fraepilidk vmekvaegki vlklhnqlde vlgdgtgvtg irikntqtga teqidlkgcf
      241 iaighhpntd ifqgqlemkd nyiltrsglq gfatmtsipg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq rfleqdd
//
LOCUS       WP_124455708             532 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Burkholderia].
ACCESSION   WP_124455708
VERSION     WP_124455708.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55010
     Region          3..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple iatgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagatva
       61 ataaelwsgs divfkvrppt sdevalmreg gtligfvwpa qnpelmeqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq ardadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvve elckakdgti nvdfdddair
      361 gltvikegni twppppikqa vvapkppaap vaaapakskg hghsgepmsa kalaivfavg
      421 alafllvgqf apasflshft vfvlacfvgy mviwnvtpsl htplmsvtna issiiaigal
      481 vqvapplgel anagdrpsgl ilglavgalt ltavnmfggf avtrrmlamf rk
//
LOCUS       WP_124458492             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. KBW07].
ACCESSION   WP_124458492
VERSION     WP_124458492.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. KBW07
  ORGANISM  Variovorax sp. KBW07
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Variovorax sp. KBW07"
                     /db_xref="taxon:2153358"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38762
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etvkklvasg htvgvqsgag vaasvtdaay qaagaqitdq
       61 agalsadmvl kvrtptdaea allkpgavvi gmlnpfdatg lqrlasagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmppswla
      241 rqqvevakrv aladivista lipgraaptl itedmvkamk pgsvivdiaa gkgpvnpdgg
      301 vggncplsea dktvvkhgvt ivgetnlaal vaadasalya rnvldflkli vtkegalkid
      361 leddivaacr vtqdgqvtrk
//
LOCUS       WP_124467599             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_124467599
VERSION     WP_124467599.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54787
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrkagaevv
       61 ataadlwgrs divlkvrpps seevalmrdg stlvgfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfl
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgti nvdfnddair
      361 gltvikegnv twppppiqqp aaapkpaapp vaaaaskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_124472454             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia contaminans].
ACCESSION   WP_124472454
VERSION     WP_124472454.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34165
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlitgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfl ehaerfntei vfdhihtakl heqpirligd sgeytcdsli vatgasaqyl
      121 glpseeafmg kgvsacatcd gffyrnqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegav vikwdhvlde vtgeesgvtg lriknvktga tedlhvqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglh gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_124476224             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia cenocepacia].
ACCESSION   WP_124476224
VERSION     WP_124476224.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34231
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlitgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfq ehaerfntei vfdhihtakl herpirligd sgeytcdsli iatgasaqyl
      121 glpseeafmg kgvsacatcd gffyrnqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekqkegvv dikwdhvlde vtgeesgvtg lriknvktga tedllvqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglq gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhnkk
//
LOCUS       WP_124481570             379 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia cepacia complex].
ACCESSION   WP_124481570
VERSION     WP_124481570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39079
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiakgag saasypdeay vaagaeltdq
       61 saafaadlvl kvqaptdael pllkrgavlv gmlepfngeq aaqlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvdtaqsmk pgsvlvdlaa grgpeidgrr
      301 ggncpltvad qvivhngvti agytnlasmv asdasalyar nlldflkliv tkegtlnidl
      361 tddivaatll crdgevtrk
//
LOCUS       WP_124476108             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cenocepacia].
ACCESSION   WP_124476108
VERSION     WP_124476108.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39035
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiakgag saasypdeay vaagaeltdq
       61 saafaadlvl kvqapadael pllkrgavlv gmlepfngeq aaqlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvdtaqsmk pgsvlvdlaa grgpeidgrk
      301 ggncpltvad qvivhngvti agytnlasmv asdasalyar nlldflkliv tkegtlnidl
      361 tddivaatll crdgeltrk
//
LOCUS       WP_124483785             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia stagnalis].
ACCESSION   WP_124483785
VERSION     WP_124483785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55042
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlrigiple tttgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagatvv
       61 ataaelwsgs divfkvrpps seevallrdg gtligfvwpa qnpelmqqla arratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq ardadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvve elckgkdgti nvdfdddair
      361 gltvikegnv twppppikqa avapkpqaap aaaapakskg hghsgepmsa kalaivfaig
      421 alafllvgqy apssflshft vfvlacfvgy mviwnvtpsl htplmsvtna issiiaigal
      481 vqvapplgel aggagdrpsg lilglavgal altavnmfgg favtrrmlam frk
//
LOCUS       WP_124483875             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cenocepacia].
ACCESSION   WP_124483875
VERSION     WP_124483875.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54910
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigvple taheerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ptaadlwgrs divlkvrpps sdevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfiagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akeadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvve elcktkdgti nvdfnddair
      361 gltvikegnv twppppiqlp vvaakpvaap vaaaaskghg hgsgapmsak slaivfavga
      421 lafllvgqfa patflthftv fvlacfigym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_124489171             534 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Burkholderia].
ACCESSION   WP_124489171
VERSION     WP_124489171.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..534
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55005
     Region          3..534
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigvple tatgerrvat vpevveklik lgfsvavqsg agaganfddd tyraagasia
       61 ataaelwsgs divlkvrpps adevalmreg galigfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvie elckakdgti nvdfdddair
      361 gltvikegnv twppppikqa avapkppaaa paaaaapaks kghghsgepm sakalaivfa
      421 igalafllvg qfapasflsh ftvfvlacfv gymviwnvtp slhtplmsvt naissiiaig
      481 alvqvapplg elanagdrps glilglavga ltltavnmfg gfavtrrmla mfrk
//
LOCUS       WP_124496822             320 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Burkholderia].
ACCESSION   WP_124496822
VERSION     WP_124496822.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34341
     Region          8..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mptpkhakvl ilgsgpagyt aavyaaranl spvlitgiaq ggqlmtttdv enwpadargv
       61 qgpelmtrfq ehaerfntei vfdhihtakl heqpirligd sgeytcdsli iatgasaqyl
      121 glaseeafmg kgvsacatcd gffyrnqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegvv dikwdhvlde vtgeesgvtg lriknvktge kqdlnvqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglh gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_124491639             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia stagnalis].
ACCESSION   WP_124491639
VERSION     WP_124491639.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34147
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlvtgiaq ggqlmtttdv enwpadakgv
       61 qgpdlmqrfl ehaerfntei lfdhihtakl hekpirligd ageytcdsli iatgasaqyl
      121 glpseeafmg kgvsacatcd gffyrgqnva vvgggntave ealyltgias kvtvihrrdk
      181 fraepilvdr llekekegkv eikwnhvlde vtgedsgvtg lrlknvqtga tediqvqgvf
      241 vaighkpntd ifqgqlemkd gyiltksglq gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdrk
//
LOCUS       WP_124501253             531 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp9140].
ACCESSION   WP_124501253
VERSION     WP_124501253.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9140
  ORGANISM  Burkholderia sp. Bp9140
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia sp. Bp9140"
                     /db_xref="taxon:2184572"
     Protein         1..531
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55223
     Region          5..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mattiavpre vhagerrvaa tpqsvgqlik lgyavnveag agaaasfddd ayraagaqiv
       61 adsralwaga dvvikvrppe fhpalavdea tlvkpgatli gfiwpaqnpa lleqlaargt
      121 nvlaidcvpr israqkldal ssmanmagyr avieaanhfg rlftgqitaa gkmppakvmv
      181 igagvaglaa igaarglgai vrafdtrpdv eeqvksmgae fltvdfeeeg sgsggyakqm
      241 saryieaeml lfaeqakeid iivttalipg kpapklitae mvasmrsgsv ivdmaseqgg
      301 nceltrpgev vsaggvtiig ytdlpsrmat qssqlyatni rhlltdltpg kdgvlqinid
      361 ddvmrgvtvv nrgaitwppp apkqpaiaah vpqpskqaan qekargreds nrgpgvgkfa
      421 lvvvaaiall algavapppf vahltvfvla vfvgyqvvwn vtpalhtplm svtnaisgii
      481 vigallqlgi skplvttlgg valfmasini aggflvtqrm lkmfqrdqsg e
//
LOCUS       WP_124499061             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp9140].
ACCESSION   WP_124499061
VERSION     WP_124499061.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9140
  ORGANISM  Burkholderia sp. Bp9140
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia sp. Bp9140"
                     /db_xref="taxon:2184572"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55134
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagasia
       61 ataaelwsgs dimfkvrpps adevalmreg gtligfvwpa qnpelmqqla arratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvrsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl ygtnllrvve elcktkdgki nvdfdddair
      361 gltvikegtv twpappikqa avapkppaaa pavaapaksk ghghsgepms akslaivfai
      421 galafllvgq fapssflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqiapplge lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_124512525             532 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Acidovorax
            sp. FJL06].
ACCESSION   WP_124512525
VERSION     WP_124512525.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. FJL06
  ORGANISM  Acidovorax sp. FJL06
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Acidovorax sp. FJL06"
                     /db_xref="taxon:2153365"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55429
     Region          11..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqtspvpqpq rigvpretfp gekrvatvpe vvekliklgf tvavesgagd aanfsddayr
       61 aagaevigga aalwaasdiv fkvrppssde valmregstl idfiwpaqnp elmqqlmark
      121 atvlaidclp rtlsraqkmd altstagvsg yravieaana fgrffngqit aagkvppakv
      181 fiagagvagl aaigtaanlg aivrandtra evadqvkslg gefvkvdyee egsggggyak
      241 vmsegfqaaq rqmyasqakd vdiiittali pgkpapklit aemvqsmkpg svivdmaaeq
      301 ggnceltvpg eavvrhgvti vgytdlasrl akqsstlyan nllrlteelc kakdgvavvn
      361 ieddairglt vvkdgaitwp applkqapap apkaaapvae kksshgpgap msaktltivf
      421 avmavlfwai gayapvaflg hftvfvlacf igymvvwnvt palhtplmsv tnaissiiai
      481 galvqiappd atlngrpagl ilwlafaatv ltavnmfggf avtrrmlamf rk
//
LOCUS       WP_124515307             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acidovorax sp. FJL06].
ACCESSION   WP_124515307
VERSION     WP_124515307.1
KEYWORDS    RefSeq.
SOURCE      Acidovorax sp. FJL06
  ORGANISM  Acidovorax sp. FJL06
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Acidovorax.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acidovorax sp. FJL06"
                     /db_xref="taxon:2153365"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33832
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msttqhakvl ilgsgpagyt aavyaaranl npvlitgmaq ggqlmtttev dnwpadvhgv
       61 qgpdlmqrfl ehaerfktqi ifdhinkvdf sqrpftltgd sgtytcdali latgasakyl
      121 glpseeafmg kgvsgcatcd gffyreqdvc vvgggntave ealylsniar kvtlvhrrdk
      181 fkaepilvdk lnekvaagki elklfntlde vlgdntgvtg irikstkdgs tediklqgcf
      241 iaighapnte ifqgqlemen gyiitqgglk gfatqtsvpg vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq rfleqea
//
LOCUS       WP_124523943             534 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Burkholderia].
ACCESSION   WP_124523943
VERSION     WP_124523943.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..534
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55035
     Region          3..534
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigvple tatgerrvat vpevveklik lgfsvavqsg agaganfddd tyraagasia
       61 ataaelwsgs divlkvrpps adevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvie elckakdgti nvdfdddair
      361 gltvikegnv twppppikqa avapkppaaa paaaaapaks kghghsgepm sakalaivfa
      421 igalafllvg qfapasflsh ftvfvlacfv gymviwnvtp slhtplmsvt naissiiaig
      481 alvqvapplg elanagdrps glilglavga ltltavnmfg gfavtrrmla mfrk
//
LOCUS       WP_124526458             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas sp. KBW05].
ACCESSION   WP_124526458
VERSION     WP_124526458.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. KBW05
  ORGANISM  Pseudomonas sp. KBW05
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Pseudomonas sp. KBW05"
                     /db_xref="taxon:2153360"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33277
     Region          1..313
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermk ehaerfetei vfdhinqvdf skkpysltgd sgvytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlvhrret
      181 fraekilidk lharvaegki ilklnatlde vlgdnmgvtg arlknndgsf deltvdgvfi
      241 aightpntsl fegqlelkdg ylivqggreg natatsiegi faagdvadhv yrqaitsaga
      301 gcmaaldaer yldd
//
LOCUS       WP_124527111             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. KBW05].
ACCESSION   WP_124527111
VERSION     WP_124527111.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. KBW05
  ORGANISM  Pseudomonas sp. KBW05
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. KBW05"
                     /db_xref="taxon:2153360"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38737
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasitdsay etagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vftkegqfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_124533901             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_124533901
VERSION     WP_124533901.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39084
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiargag laasypdaay aaagaeltgq
       61 saafdvdivl kvqaptdael pslkrgavlv gmldpfngeq aaklaaagvt gfaleaaprt
      121 traqgldvls sqaniagyka vlvaaalypr ffpmlmtaag tvkaarvlil gagvaglqat
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee rdaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qviahhgvti agytnlasmv asdasalyar nlldfmkliv tkegtlnidl
      361 tddivaatll crdgevtrr
//
LOCUS       WP_124535317             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_124535317
VERSION     WP_124535317.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54899
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ataadlwgrs divlkvrpps seevallreg stlvgfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgti nvdfnddair
      361 gltvikegnv twppppiqqp vaapkpatpp vaataskghg hgsgepmsak slaivfavga
      421 lafllvgqfa patflahftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_124541055             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Piscinibacter terrae].
ACCESSION   WP_124541055
VERSION     WP_124541055.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter terrae
  ORGANISM  Piscinibacter terrae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Piscinibacter terrae"
                     /db_xref="taxon:2496871"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38785
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpleta agetrvavtp etakklkaqg htlriqsgag lkasvtdeay aaagaeitdq
       61 agafacelvl kvrspldsel qlmntgaalv gmlnpfdrdn lhrlagagvt sfaleaaprt
      121 traqsmdvls sqaniagyka vmmaadryqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvsydtpee keaaegvggy akpmpqswle
      241 rqkvevakrv amadvvitta lipgrpapvl vteemvksmk pgsvivdlaa aqggncplte
      301 anrtvtkhgv tligetnlpa lvaadasaly arnvldflkl vitkegtfnv pmdddivaac
      361 lmtqggevkr k
//
LOCUS       WP_124544471             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_124544471
VERSION     WP_124544471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54815
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ataadlwgrs divlkvrpps seevallreg stlvgfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgti nvdfnddair
      361 gltvikegnv twppppiqqp aaapkpaaap vaataskghg hgsgepmsak slaivfavga
      421 lafllvgqfa patflahftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_124545180             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_124545180
VERSION     WP_124545180.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39138
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiargag laasypdaay aaagaeltgq
       61 saafdvdivl kvqaptdael pllkrgavlv gmldpfngeq aaklaaagvt gfaleaaprt
      121 traqgldvls sqaniagyka vlvaatlypr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee rdaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qviahhgvti agytnlasmv asdasalyar nlldfmkliv tkegtlnidl
      361 tddivsatll crdgevarr
//
LOCUS       WP_124558521             318 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Pedobacter].
ACCESSION   WP_124558521
VERSION     WP_124558521.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pedobacter
  ORGANISM  unclassified Pedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="unclassified Pedobacter"
                     /db_xref="taxon:2628915"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34056
     Region          10..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqenehvqc liigsgpagy taaiyaarad lkpimytgmq aggqltqttd venfpgypqg
       61 imgpemmedf rkqaerfgtd irfgyvssvd fsstphkvvv deiktitadt viiatgatak
      121 wlglpseqqy ngfgvsacav cdgfffkgqd vaivgagdta aeeatylakl cktvhllvrr
      181 defraskamv srvlatpniv vhyntetqei lgngknvtav kvinnktgie sdiavegffv
      241 aighkpntdi fkgqldmdet gylttkpgst ltniegvfac gdvqdmyyrq avtaagsgcm
      301 aaldaeryla akehpvea
//
LOCUS       WP_124564498             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Ectobacillus antri].
ACCESSION   WP_124564498
VERSION     WP_124564498.1
KEYWORDS    RefSeq.
SOURCE      Ectobacillus antri
  ORGANISM  Ectobacillus antri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Ectobacillus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Ectobacillus antri"
                     /db_xref="taxon:2486280"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34888
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseekiydvm iigagpagmt aalytsranl stlmlergip ggqmanteev enypgydhil
       61 gpelstkmfe hakkfgaeya ygdvkeiidg kefktviagk keykaraiii asgaeykkig
      121 vpgekelggr gvsycavcdg affkgkelvv vgggdsavee gvyltrfakk vtivhrrdkl
      181 raqkilqdra fnnekisfiw nstvkeinea ngkvgsvtlt dvntgeeqef ktdgvfiyig
      241 mlplskpfea lgitnengyi etndrmetkv pgifaagdvr ekalrqivta tgdgsiaaqt
      301 aqhyieelle elsretvtee
//
LOCUS       WP_124566989             335 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhodococcus sp. KBW08].
ACCESSION   WP_124566989
VERSION     WP_124566989.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. KBW08
  ORGANISM  Rhodococcus sp. KBW08
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rhodococcus sp. KBW08"
                     /db_xref="taxon:2144188"
     gene            1..335
                     /gene="trxB"
     Protein         1..335
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35533
     Region          12..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttqlentpa vhdviivgsg pagytagvyt araelqpllf egtqfggalm tttevenfpg
       61 fregimgpdl meqmreqalr fdtdirtedv eeidlsgpik tvvangetya ahaiilamga
      121 aarylgipge erllgrgvsa catcdgfffr dqdivvvggg dsameeatfl trfarsvtlv
      181 hrreefrasr imlerakane kirfltnaep vevlgencvt glvvrdtvtg etstleitgm
      241 fvaighdprs elvkgqvdld dagyvrvapg statsvdgvf aagdlvdhty rqaitaagtg
      301 csaaidaerw ladrgditan tldaaghtvd vvgap
//
LOCUS       WP_124573630             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Herminiimonas sp. KBW02].
ACCESSION   WP_124573630
VERSION     WP_124573630.1
KEYWORDS    RefSeq.
SOURCE      Herminiimonas sp. KBW02
  ORGANISM  Herminiimonas sp. KBW02
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herminiimonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Herminiimonas sp. KBW02"
                     /db_xref="taxon:2153363"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33680
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mssakhahvl ilgsgpagys aavyaaranl kpvlitgveq ggqlmtttdv enwpgdplgv
       61 qgpelmqrll qhaerfntei ifdhihttkl dekpirligd ageytcdali iatgasaqyl
      121 glpseqafmg kgvsacatcd gffyrnqeva vigggntave ealylsnian kvtvvhrrdk
      181 fraeailidr lmakvaegki evkwnstleq vcgddsgvtg mtikstvdgs ttdidlhgvf
      241 vaighkpnts ifegqlemnn gyiktktgle gmatstsvpg vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq rylesqe
//
LOCUS       WP_124575603             532 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Herminiimonas sp. KBW02].
ACCESSION   WP_124575603
VERSION     WP_124575603.1
KEYWORDS    RefSeq.
SOURCE      Herminiimonas sp. KBW02
  ORGANISM  Herminiimonas sp. KBW02
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Herminiimonas.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Herminiimonas sp. KBW02"
                     /db_xref="taxon:2153363"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55613
     Region          5..531
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mslvigvpre sfpgekrvat vpevveklik lgfsvnvesg agdeanfsdd tyraagaqiv
       61 qgaanlwsts divfkvraps aeevglireg stligfiwpa qnpelmqqla akrvtvlamd
      121 slprtlsraq kmdaltstag vsgyraviea anafgrffng qitaagkvap akvfvagagv
      181 aglaaigtaa slgaivrand traevadqvv slggefvkvd ydeegsgggg yakvmsegfq
      241 aaqremyaqq akecdiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 epgkvvvkhg vtivgytdlp srlpkqastl ystnllrlte elckdaegkk ttdgiinvnm
      361 edeairgltv ikegnitwpp pppkpvvapp akpapvaapa hghgpsttvs spkrvvtmfv
      421 fatllfalig mgaptaflgh ltvfvlgcfi gymvvwnvtp alhtplmsvt nsissiivig
      481 alvqvappla dgmarpelli kclaaagial tainmfggfa vtrrmldmfr kn
//
LOCUS       WP_124576706             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia contaminans].
ACCESSION   WP_124576706
VERSION     WP_124576706.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34084
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlitgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfl ehaerfntei vfdhihtakl heqpirligd sgeytcdsli iatgasaqyl
      121 glpseelfmg kgvsacatcd gffyrgqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegav vikwdhvlde vtgedsgvtg lriknvktga tedlavqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglh gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_124581093             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia contaminans].
ACCESSION   WP_124581093
VERSION     WP_124581093.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54799
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taheerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagadvv
       61 ataadlwgrs divlkvrpps sdevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvrvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akeadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvve elckgkdgti nvdfsddair
      361 gltvvkegnv twppppiqqp aaapkpatpp vaataskghg hgsgapmsak slaitfavga
      421 lvfllvgqfa patflahftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgdaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_124583528             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pedobacter sp. KBW06].
ACCESSION   WP_124583528
VERSION     WP_124583528.1
KEYWORDS    RefSeq.
SOURCE      Pedobacter sp. KBW06
  ORGANISM  Pedobacter sp. KBW06
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pedobacter sp. KBW06"
                     /db_xref="taxon:2153359"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34483
     Region          10..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseeiehvqc liigsgpagy taaiyaarad lkpvmytgme pggqltqttd vdnfpgypgg
       61 vmgpemmedf rkqaerfgtd irfgyvssvd fssmphkvvv ddiktitadt viistgatak
      121 wlglpseqky ngfgvsacav cdgfffkgqd vaivgagdta aeeatylakl ckkvymlvrr
      181 defraskamv hrvlntpnie vvyhtetqei igngknvtav kvlnnqtgve seipvegffv
      241 aighkpntdi fkgwldmdet gylqtipgst ktnvegvfaa gdvqdhyyrq avtaagsgcm
      301 aaldaeryla akehevkals
//
LOCUS       WP_124596641             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia stagnalis].
ACCESSION   WP_124596641
VERSION     WP_124596641.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54777
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlrigvple taheerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ptaadlwgrs divlkvrpps sdevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllhvve elckgkdgti nvdfnddair
      361 gltvikegnv twppppiqqp aaapkpatpp vastaskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflahftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgdaa aggrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_124600332             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia sp. Bp8963].
ACCESSION   WP_124600332
VERSION     WP_124600332.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp8963
  ORGANISM  Burkholderia sp. Bp8963
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia sp. Bp8963"
                     /db_xref="taxon:2184547"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34191
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlvtgiaq ggqlmtttdv enwpadakgv
       61 qgpelmqrfl ehaerfntei lfdhihtakl hekpirligd aseytcdali iatgasaqyl
      121 glpseeafmg kgvsacatcd gffyrgqnva vigggntave ealyltgian kvtvihrrdk
      181 fraepilvdr llekekegkv eikwnhvlde vtgedsgvtg lrikhvqtga tedlavqglf
      241 vaighkpntd ifqgqlemkd gyiltksglq gnatstsvpg vfaagdvqdn iyrqaitsag
      301 tgcmaaldaq ryleslhdhk
//
LOCUS       WP_124602010             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp8963].
ACCESSION   WP_124602010
VERSION     WP_124602010.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp8963
  ORGANISM  Burkholderia sp. Bp8963
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia sp. Bp8963"
                     /db_xref="taxon:2184547"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54937
     Region          5..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlvigvple taiqerrvat vpdvveklik lgfavavqsg agaganfsdd dyraagaevv
       61 asatdlwgrs divfkvrpps seevalmrhg gtligfvwpa qnpelmqqla akqatvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea anafgryfng qitaagkvpp akifiagagv
      181 aglaaigtaa gmgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtiigytdla srlarqssnl yatnllrvae elcktkdgti nvdfdddair
      361 gltvikegnv twppppikqp aaapkaqtpp ptvaapkghg hgssepmsak tlaivfgvga
      421 lafllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplggaa vgdrpsglil gmavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_124607419             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp9142].
ACCESSION   WP_124607419
VERSION     WP_124607419.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9142
  ORGANISM  Burkholderia sp. Bp9142
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia sp. Bp9142"
                     /db_xref="taxon:2184573"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55115
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagasia
       61 ataaelwsgs divfkvrpps adevalmreg gtligfvwpa qnpelmqqla arratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvrsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl ygtnllrvve elcktkdgki nvdfdddair
      361 gltvikegnv twpappikqa avapkppaaa pavaapaksk ghghsgepms akslaivfai
      421 galafllvgq fapssflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqiapplge lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_124605714             531 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp9142].
ACCESSION   WP_124605714
VERSION     WP_124605714.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9142
  ORGANISM  Burkholderia sp. Bp9142
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia sp. Bp9142"
                     /db_xref="taxon:2184573"
     Protein         1..531
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55299
     Region          5..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mattiavpre vhagerrvaa tpqsvgqlik lgyavnveag agaaasfddd ayraagaqiv
       61 adsralwaga dvvikvrppe fhpalavdea tlvkpgatli gfiwpaqnpa lleqlaargt
      121 nvlaidcvpr israqkldal ssmanmagyr avieaanhfg rlftgqitaa gkmppakvmv
      181 igagvaglaa igtarglgai vrafdtrpdv eeqvksmgae fltvdieeeg sgsggyakqm
      241 saryieaeml lfaeqakeid iivttalipg kpapklitae mvasmrsgsv ivdmaseqgg
      301 nceltrpgev vsaggvtiig ytdlpsrmat qssqlyatni rhlltdltpg kdgvlqinid
      361 ddvmrgvtvv nrgaitwppp apkqpaiaah vpqpskqaan qekargreds nrrpgvgkfa
      421 lvvvaaiall algavapppf vahltvfvla vfvgyqvvwn vtpalhtplm svtnaisgii
      481 vigallqlgi skplvttlgg valfmasini aggflvtqrm lkmfqhdqsg e
//
LOCUS       WP_124611721             531 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp9143].
ACCESSION   WP_124611721
VERSION     WP_124611721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9143
  ORGANISM  Burkholderia sp. Bp9143
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia sp. Bp9143"
                     /db_xref="taxon:2184574"
     Protein         1..531
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55150
     Region          5..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mattiavpre vhagerrvaa tpqsvgelik lgyavnveag agaaasfddd ayraagaqiv
       61 adsralwaga dvvikvrppe chpalavdea tlvkpgatli gfiwpaqnpa llqqfaargt
      121 nvlamdcvpr israqkldal ssmanmagyr avieaanhfg rlftgqitaa gkmppakvmv
      181 igagvaglaa igtarglgai vrafdtrpdv eeqvqsmgae fltvdieeeg sgsggyakqm
      241 saryieaeml lfaeqakeid vivttalipg kpapklitae mvasmrsgsv ivdmaseqgg
      301 nceltrpgev vsvggvtiig ytdlpsrmat qssqlyatni rhlltdltpg kdgvlqinid
      361 ddvmrgvtvv nrgaitwppp apkqpaiaah apkpskqaan qekargreds srgpgvgkfa
      421 lvvvaaiall algavappsf vahltvfvla vfvgyqvvwn vtpalhtplm svtnaisgii
      481 vigallqlgs skplvttlgg valfmasini aggflvtqrm lkmfqrdqsg e
//
LOCUS       WP_124611886             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp9143].
ACCESSION   WP_124611886
VERSION     WP_124611886.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9143
  ORGANISM  Burkholderia sp. Bp9143
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia sp. Bp9143"
                     /db_xref="taxon:2184574"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55000
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatgerrvat vpevveklik lgfsvavqsg agaganfddd tyraagasia
       61 ataaelwsgs divfkvrpps adevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk lisaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl ygtnllrvie elckakdgti nvdfdddair
      361 gltvikegnv twppppikqa avapkppaaa paaaapaksk ghghsgepms akalaivfai
      421 galafllvgq fapssflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapplge lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_124612962             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp9143].
ACCESSION   WP_124612962
VERSION     WP_124612962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9143
  ORGANISM  Burkholderia sp. Bp9143
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia sp. Bp9143"
                     /db_xref="taxon:2184574"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39654
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaeiv agewrvaatp etvkklvaqg havrvqhaag dranfsdaay aaagatlvda
       61 svaldaevvl kvqaptdael drlkkgtvlv gmldpfnter iarlanagit gfaleaiprt
      121 traqsmdvls sqaniagyka vlvaaglyqr ffptlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgarf ldvpfetdee rdaangsggy arpmpaswla
      241 rqgvlvrerv raadivista lipgrtaptl lpedmvremk pgavivdlaa grgaetnghr
      301 ggncpltead cvvtrygvqi agytnlpsmv aadasalyar nvldflkliv deggqlridt
      361 tddivaatll ghdasrqksa
//
LOCUS       WP_124613298             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia sp. Bp9143].
ACCESSION   WP_124613298
VERSION     WP_124613298.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9143
  ORGANISM  Burkholderia sp. Bp9143
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia sp. Bp9143"
                     /db_xref="taxon:2184574"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34238
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlitgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfl ehaerfntei vfdhihtakl hekpirligd sgeytcdsli istgasaqyl
      121 glaseeafmg kgvsacatcd gffyrnqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegvv dikwdhvlde vtgedsgvtg lriknvktge kqdltvqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglq gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_124617978             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp9143].
ACCESSION   WP_124617978
VERSION     WP_124617978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9143
  ORGANISM  Burkholderia sp. Bp9143
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia sp. Bp9143"
                     /db_xref="taxon:2184574"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39974
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpvett pgetrvavtp etakklkdqg htvrvtsgag laasytdeay ravgaeivdq
       61 aaalaselvl kvrppleset sslgkgallv gmlnpfdvag lqrlaqagit afaleaaprt
      121 traqsmdvls sqaniagyka vmiaadryqr ifpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvggy arpmptswlq
      241 rqqaevakrv aaadivitta lipgrpapvl vteamvqsmk pgsvivdlaa aqggncplte
      301 pgatvlrsgv tivgetnlpa lvatdssnly arnvldflkl ilpkdggvti dleddivagc
      361 lvtrdgmvmr dqpapvrpta easttn
//
LOCUS       WP_124621719             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cenocepacia].
ACCESSION   WP_124621719
VERSION     WP_124621719.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39079
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiakgag saasypdday vaagaeltdq
       61 saafaadlvl kvqaptdael pllkrgavlv gmlepfngeq aaqlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvdtaqsmk pgsvlvdlaa grgpeidgrr
      301 ggncpltvad qvivhngvti agytnlasmv asdasalyar nlldflkliv tkegtlnidl
      361 tddivaatll crdgeltrk
//
LOCUS       WP_124627336             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp9012].
ACCESSION   WP_124627336
VERSION     WP_124627336.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9012
  ORGANISM  Burkholderia sp. Bp9012
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia sp. Bp9012"
                     /db_xref="taxon:2184562"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55025
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatqerrvas vpevveklik lgftvavqsg agaganfgdd ayraagasia
       61 ataaelwsgs divfkvrpps adevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmas isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvie elckakdgti nvdfdddair
      361 gltvikegnv twppppikqa avapkppaaa paaaapaksk ghghsgepms akalaivfai
      421 galafllvgq fapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapplge lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_124627482             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_124627482
VERSION     WP_124627482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54830
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrkagaevv
       61 ataadlwgrs divlkvrpps seevalmrdg stlvgfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgti nvdfnddair
      361 gltvikegnv twppppiqqp vaapkpaapp vaaaaskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_124634285             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Taibaiella sp. KBW10].
ACCESSION   WP_124634285
VERSION     WP_124634285.1
KEYWORDS    RefSeq.
SOURCE      Taibaiella sp. KBW10
  ORGANISM  Taibaiella sp. KBW10
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Taibaiella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Taibaiella sp. KBW10"
                     /db_xref="taxon:2153357"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34478
     Region          11..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstentteli dcliigsgpa gytaaiyasr anlkpvlysg lqpggqltit tdvenypgyp
       61 dgimgpqmmk dfehqakrmg adlrwgmisk vdlsvrpfkv evdesswiea nsiiiatgas
      121 akwlgleseq rlngygvsac avcdgfffke kevaivgagd taceealyls kicskvhmfi
      181 rkeemraskv mqdrvlktan iqvywntetd evlgekkvea vrilnnktne kteipvsaff
      241 vaighqpnsd lfkgtidmde qgyiltvpgt sktniqgvfa cgdvqdkmyr qavtaagsgc
      301 maaldseryl gehvhn
//
LOCUS       WP_124642997             313 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Amniculibacterium].
ACCESSION   WP_124642997
VERSION     WP_124642997.1
KEYWORDS    RefSeq.
SOURCE      Amniculibacterium
  ORGANISM  Amniculibacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Amniculibacterium"
                     /db_xref="taxon:2715289"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33784
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqnildcvi vgsgpsgyta aiyaaradlk pelytglepg gqlttttevd nfpgypqgit
       61 gpemmmdlqk qaerfdtkvh yemitkaefs kevggihklw agnkeihakt vivstgatar
      121 ylglddekky sgggvsacat cdgffyrgke vivvgagdta aeeatylanl cskvtmlvrk
      181 dhfraskamv hrventpnie vkfnheligi egenslvera vvinnqtqet skidvhgifi
      241 aighkpntev fqgqinlden gyiitegkss ktnlpgvfaa gdvqdhiyrq aitaagsgcm
      301 aaidaerylg elk
//
LOCUS       WP_124643469             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Aquitalea].
ACCESSION   WP_124643469
VERSION     WP_124643469.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea
  ORGANISM  Aquitalea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Aquitalea"
                     /db_xref="taxon:407217"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33694
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtrhspll ilgsgpagyt aavyaaranl kpvlitglaq ggqlmtttev dnwpadasgv
       61 mgpelmqrfq qhaerfgtem ifdhihtthl hekpirlvgd ageytcdali iatgasakyl
      121 glpseeafag kgvsacatcd gffyrnqdva vvgggntave ealylaniak hvtlihrrds
      181 fraekimidk lmsrvaegki tlklnaslde vlgddsgvtg arlkftdgst ediklmgvfi
      241 aighqpntdi fkgqlemdat gylitrggre gnatltsvdg vfaagdvqdh iyrqavtsaa
      301 sgcqaaldae ryldslk
//
LOCUS       WP_124645318             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Aquitalea].
ACCESSION   WP_124645318
VERSION     WP_124645318.1
KEYWORDS    RefSeq.
SOURCE      Aquitalea
  ORGANISM  Aquitalea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chromobacteriaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Aquitalea"
                     /db_xref="taxon:407217"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39071
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqiaipaerl agekrvaatp etvkkliamg htvvveqgag qfaaapdaay aelgasiaan
       61 raealaqadi vlsvraldea giaelkpgav ligqlapyqn ttfpqlaark vsafamellp
      121 rttraqsmdv lssqnniagy kavllathyy prfmpmlmta agtvkpakvl imgvgvaglq
      181 aiatakrlga vveatdvrps tkeqveslgg kfievpmtde ekaasdgvya remsddykrr
      241 qaelvskhar aadiiittal ipgkkaptli sadivaamkp gsviidiaae aggncertqp
      301 gevvvtdnhv tvvgqfnlpg elaadassly aknlltflsl mlskegftln leddllaatl
      361 vthdgqvrfp aan
//
LOCUS       WP_124646094             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp8990].
ACCESSION   WP_124646094
VERSION     WP_124646094.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp8990
  ORGANISM  Burkholderia sp. Bp8990
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia sp. Bp8990"
                     /db_xref="taxon:2184552"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39820
     Region          1..373
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaesv agearvaatp etvrklaarg hevlvqrsag eranftdday assgatlvda
       61 qralaadvvl kvqaptdtef allrkgaali gmldpfnaer aarlttagit afaleaiprt
      121 traqsmdvls sqaniagyka vliaaglyqr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrmgavi easdvrpavr eqieslgakf vdvpfetnee reaaegtggy arpmpaswla
      241 rqsalvrera rsadiviata lipgrtaptl lpedilrdmk pgsvivdlaa grgaetngrr
      301 ggncpltead rvvthhgvhi agftnlpamv asdasslyar nvldflklii dddgrlridt
      361 tddivaatll ghdashqqsa
//
LOCUS       WP_124646100             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp8990].
ACCESSION   WP_124646100
VERSION     WP_124646100.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp8990
  ORGANISM  Burkholderia sp. Bp8990
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia sp. Bp8990"
                     /db_xref="taxon:2184552"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40082
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpvett pgearvavtp etakklrdqg htvrtasgag lgasytdday ravgaeivdq
       61 aaalgcelvl kvrpplesel aafgsgamlv gmlnpfdaig lerlakagit afaleaaprt
      121 traqsmdvls sqaniagyka vmiaadryqr ifpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee eeaaegfggy arpmpaswlq
      241 rqqvevakrv aaadivitta lipgrpapvl vteamvqsmk pgsvivdlaa aqggncpltk
      301 pggttvwngv tivgetnlpa lvatdssnly arnvldflkl ilpkeggvmi dleddiiagc
      361 lvtrdgivlr dqpararpta evsttn
//
LOCUS       WP_124647158             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia contaminans].
ACCESSION   WP_124647158
VERSION     WP_124647158.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34165
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlitgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfl ehaerfntei vfdhihtakl heqpirligd sgeytcdsli iatgasaqyl
      121 glpseeafmg kgvsacatcd gffyrnqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegav vikwdhvlde vtgedsgvtg lriknvktga tedlhvqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglh gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_124657644             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia anthina].
ACCESSION   WP_124657644
VERSION     WP_124657644.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34256
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlitgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfq ehaerfntei vfdhihtakl hekpirligd sgeytcdsli iatgasaqyl
      121 glpseeafmg kgvsacatcd gffyrnqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekqkegvv dikwdhvlde vtgeesgvtg lriknvktgv tedlhvqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglq gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_124661204             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia sp. Bp8998].
ACCESSION   WP_124661204
VERSION     WP_124661204.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp8998
  ORGANISM  Burkholderia sp. Bp8998
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia sp. Bp8998"
                     /db_xref="taxon:2184557"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34178
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlvtgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfl ehaerfntei vfdhihtakl hekpirligd sgeytcdsli iatgasaqyl
      121 glaseeafmg kgvsacatcd gffyrnqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegvv dikwdhvlde vtgedsgvtg lriknvktge kqdlavqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglq gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_124665683             530 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_124665683
VERSION     WP_124665683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54920
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlrigvple tatqerriat vpevveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ataadlwgrs divlkvrpps sdevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfiagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akeadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgqavvrhg vtivgytdla srlarqsstl yatnllrvie elcktkdgti nvdfdddair
      361 gltvikegnv twppppiqqp vaaakpatpp vvaaaskghg hgsgapmsak slaitfavga
      421 lafllvgqfa patflshftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgdaa aegrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_124665716             430 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Burkholderia sp. Bp8998].
ACCESSION   WP_124665716
VERSION     WP_124665716.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp8998
  ORGANISM  Burkholderia sp. Bp8998
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia sp. Bp8998"
                     /db_xref="taxon:2184557"
     Protein         <1..430
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..430
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 elmqqlaakr atvlaidslp rtlsraqkmd altsmagisg yravieaaha fgrflngqvt
       61 aagkippakv fiagagvagl aaigtaaslg aivrandtra evadqvkslg gefvkvdyee
      121 egsggggyak vmsegfqqaq ramyaqqakd adiiittali pgkpapklit vemvqsmrpg
      181 svivdmaaeq ggnceltvpg eavvrhgvti vgytdlasrl srqsstlygt nllrvieelc
      241 kgkdgtinvd fdddairslt vikegnvtwp pppikqaava pkppaaapaa aapakskghg
      301 hsgepmsaka laivfaigal afllvgqfap ssflshftvf vlacfvgymv iwnvtpslht
      361 plmsvtnais siiaigalvq vapplgelan agdrpsglil glavgaltlt avnmfggfav
      421 trrmlamfrk
//
LOCUS       WP_124666954             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia sp. Bp8986].
ACCESSION   WP_124666954
VERSION     WP_124666954.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp8986
  ORGANISM  Burkholderia sp. Bp8986
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia sp. Bp8986"
                     /db_xref="taxon:2184550"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34218
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlitgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfl ehaerfntei vfdhihtakl hekpirligd sgeytcdsli iatgasaqyl
      121 glpseglfmg kgvsacatcd gffyrnqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegvv dikwdhvlde vtgedsgvtg lriknvktge kqdltvqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglq gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_124668284             534 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp8986].
ACCESSION   WP_124668284
VERSION     WP_124668284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp8986
  ORGANISM  Burkholderia sp. Bp8986
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Burkholderia sp. Bp8986"
                     /db_xref="taxon:2184550"
     Protein         1..534
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55037
     Region          3..534
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigvple tatgerrvat vpevveklik lgfsvavqsg agaganfddd tyraagasia
       61 ataaelwsgs divlkvrpps adevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvie elckakdgti nvdfdddair
      361 gltvikegnv twppppikqa avapkpaaaa paavaapaks kghghsgepm sakalaivfa
      421 igalafllvg qfapasflsh ftvfvlacfv gymviwnvtp slhtplmsvt naissiiaig
      481 alvqvapplg elanagdrps glilglavga ltltavnmfg gfavtrrmla mfrk
//
LOCUS       WP_124670565             532 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_124670565
VERSION     WP_124670565.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54854
     Region          3..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple iatgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagasia
       61 ataaelwsgs divfkvrppt sdevalmreg gtligfvwpa qnpelmaqla arratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akgadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvve elckakdgti nvdfdddair
      361 gltvikdgni twppppikqa vvapkppaap aaaapakskg hghsgepmsa kalaivfavg
      421 alaflvvgqy apasflshft vfvlacfvgy mviwnvtpsl htplmsvtna issiiaigal
      481 vqvapplgel anagdrpsgl ilglavgalt ltavnmfggf avtrrmlamf rk
//
LOCUS       WP_124672390             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_124672390
VERSION     WP_124672390.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54802
     Region          3..530
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlligvple taneerrvat vpdvveklik lgfsvavqsg agtganfsdd dyrtagaevv
       61 ataadlwgrs divlkvrpps seevallreg stlvgfvwpa qnpelmqqla arratvlaid
      121 slprtlsraq kmdaltsmag vsgyraviea ahafgryfng qitaagkvpp akvfvagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvie elckakdgti nvdfnddair
      361 gltvikegsv twppppiqqp aaapkpaaap vaataskghg hgsgepmsak slaivfavga
      421 lafllvgqfa patflahftv fvlacfvgym viwnvtpslh tplmsvtnai ssiiaigalv
      481 qvapplgeaa agdrpsglil glavgaltlt avnmfggfav trrmlamfrk
//
LOCUS       WP_124673261             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_124673261
VERSION     WP_124673261.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54796
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlrigvple tatgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagasva
       61 ataaelwsgs divfkvrpps adevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa glgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litagmvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlarqsstl yatnllrvve elckgkdgti nvdfdddair
      361 gltvikegnv twppppikqa vvapkpaaaa paaaapaksk ghghsgepms akslaivfai
      421 gavafllvgq fapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapplge lanagdrpsg lilglavgal altavnmfgg favtrrmlam frk
//
LOCUS       WP_124683292             374 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Cupriavidus].
ACCESSION   WP_124683292
VERSION     WP_124683292.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus
  ORGANISM  Cupriavidus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Cupriavidus"
                     /db_xref="taxon:106589"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39285
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipletr agetrvaatp etvkkyvaqg hqvtvqagag vrasipdaaf eaagariggp
       61 adalgaelvl kvrapddaer aqfrpgavlv gmlnpfdien narmasaait afaleaaprt
      121 traqsmdvls sqaniagyka vlvaahhyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfvtdee reiaqgvggy arpmppdwmr
      241 rqaelvhqra iqadivitta lipgrrapvl laedtvkqmk pgsvvvdlaa aqggncpltv
      301 adevverhgv tlightnlas mvaadasaly arnvldflkl ivdkdgrytl nleddivaac
      361 lmckdgqvvr qqaa
//
LOCUS       WP_124682222             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Cupriavidus pauculus].
ACCESSION   WP_124682222
VERSION     WP_124682222.1
KEYWORDS    RefSeq.
SOURCE      Cupriavidus pauculus
  ORGANISM  Cupriavidus pauculus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Cupriavidus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Cupriavidus pauculus"
                     /db_xref="taxon:82633"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33848
     Region          2..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msakhakvli lgsgpagyta avyaaranln pvlitglaqg gqlmtttdve nwpadpngvq
       61 gpdlmqrfla haerfnteii fdhihtaklt ekpirlvgda geytcdalii atgasaqylg
      121 lpseesfmgr gvsacatcdg ffyknqevav igggntavee alylshiask vtvihrrdkf
      181 raepilvdrl lqrvkegrve lrydhtldev lgdqsgvtgl rirstkdtaq tedlkvsglf
      241 vaighkpntd lfvgqlemnn gyivtksglt gdatatnipg vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq ryvealq
//
LOCUS       WP_124688256             374 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pigmentiphaga].
ACCESSION   WP_124688256
VERSION     WP_124688256.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pigmentiphaga
  ORGANISM  unclassified Pigmentiphaga
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pigmentiphaga.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="unclassified Pigmentiphaga"
                     /db_xref="taxon:2626614"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38820
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvpteir pgetrvaatp etvkklsagg nqvlvqagag rqasfpdeay aaagatlvpd
       61 aaqvyaqael vlkvqapqes elallragqi llgmlnpfda egleklaatg vtgfsleaap
      121 ritraqsldv lssqaniagy kavivaadhy grfmpmlmta agtvkaarvv vlgagvaglq
      181 aiatakrlga vveasdvrpa akeqieslga kfidvpyetd eereiaqgvg gyarpmppaw
      241 marqaalvae rckqadivit talipgrpap vlvseetvag mkpgsvivdl averggncpl
      301 srpdqvvdah gvkivgytnl aaqvatdasa lyarnlldfl klvvakdgap aiqredeiva
      361 acmvcdanrv lrnk
//
LOCUS       WP_124688503             318 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Pigmentiphaga].
ACCESSION   WP_124688503
VERSION     WP_124688503.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pigmentiphaga
  ORGANISM  unclassified Pigmentiphaga
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pigmentiphaga.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="unclassified Pigmentiphaga"
                     /db_xref="taxon:2626614"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34126
     Region          1..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msqdkhakvl vlgsgpagyt aavyaaranl spmlitgveq ggqlmtttev dnwpadvngv
       61 qgpelmqrfq qhaerfntdi vfdhihtahl dqrpfklegd sgtytcdalv iatgasakyl
      121 glpseenykg rgvsgcatcd gffyknqdva vvgggntave ealylanicr tvtlihrrdk
      181 fraepimvdk lnekvqegrv ilklfnelqe vlgddsgvtg arlrdnqtgq tediavtgvf
      241 iaighqpntg ifkgqvemkd dyiitrsgln glatmtsvpg vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq rwldgeav
//
LOCUS       WP_124691386             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pigmentiphaga sp. H8].
ACCESSION   WP_124691386
VERSION     WP_124691386.1
KEYWORDS    RefSeq.
SOURCE      Pigmentiphaga sp. H8
  ORGANISM  Pigmentiphaga sp. H8
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pigmentiphaga.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Pigmentiphaga sp. H8"
                     /db_xref="taxon:2488560"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34427
     Region          8..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mekrhapvii lgagpagyta avyaaranlr pmvitgmspg gqlmtttdvd nwpadhagvq
       61 gpelmqrflt haerfgttma ydhihgvelg srpftlhgdn gaytcdalil atgasakylg
      121 lpseqafagr gvsacatcdg ffykgedvcv vgggnaavee alylsgiart vtlihrrdkf
      181 raepilvdkl lekaasgkir lqlfqtvdei lgdesgvtgv rikstvngki qelalkgcfi
      241 aighhpntdi vrgqletrng yvvtgtsrhg fatmtsiagv faagdvqddi yrqaitsags
      301 gcmaaldaqr flelegpggv sepatmaa
//
LOCUS       WP_124696096             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus rhizophilus].
ACCESSION   WP_124696096
VERSION     WP_124696096.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus rhizophilus
  ORGANISM  Paenibacillus rhizophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paenibacillus rhizophilus"
                     /db_xref="taxon:1850366"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33831
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksivigtg pagltaaiyl aranlsplvi eglqpggqlt tttevenfpg fpegilgpdl
       61 mdnmrkqaer fgaefkngwv esvdfsqrpf kvnvdglgql eaetviistg asarylgipg
      121 eqenvgrgvs tcatcdgfff rgkkiivvgg gdsameeasf ltrfasnvtl vhrreelras
      181 kimqdraken akiswalgrt pvevvknetg vkgllvrnne tgaeelievd gvfvaightp
      241 ntsflggqit tdangyivvr pgttetnipg vfacgdvqdt ryrqaisaag sgcmaamdae
      301 kylegamvhd wsetldk
//
LOCUS       WP_124697058             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus rhizophilus].
ACCESSION   WP_124697058
VERSION     WP_124697058.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus rhizophilus
  ORGANISM  Paenibacillus rhizophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenibacillus rhizophilus"
                     /db_xref="taxon:1850366"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33176
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksiivgtg pagltaaiyl aranlnplvi egpqpggqlt ttteienfpg fpegilgtel
       61 mdnmraqaer fgakfvtgwv nsvelgerpf klnvedmgtl etdtliistg atakylgipg
      121 eqdnvgrgvs tcatcdgfff rgkeiivvgg gdsaleeagf ltrfaskvtl vhrreelras
      181 kimqdrvrdn akvewalsrt plevvagdng vtglkvlnne tgeeqiieas gvfvaighhp
      241 ntaflggqit tdangyivtn pgtsetnipg vfacgdvqdt ryrqaitaag sgckaamdae
      301 kyieslehsa vml
//
LOCUS       WP_124708936             360 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Gordonia
            insulae].
ACCESSION   WP_124708936
VERSION     WP_124708936.1
KEYWORDS    RefSeq.
SOURCE      Gordonia insulae
  ORGANISM  Gordonia insulae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Gordonia insulae"
                     /db_xref="taxon:2420509"
     Protein         1..360
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37058
     Region          1..356
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,70,89,282,308,310)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,122..123,132..133,136..137,140..141,143..144,
                     146..151,153,155..157,160,183..184,272..273,315..316,320,
                     323..324)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(117..118,122,125,128,169..172,192..194,222,233,
                     250..252,259,261)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,122,132,175..176,183,199..200,202..205)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(152..156,159,162,185,187)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 msvgvvresa agerrvalvp kvvgslvgkg vpvivesgag lgalipdehy veagatigdp
       61 ysadvvvrva ppsdeeigrl rsgqkligfl aprnadnqig alksagveay aveaiprisr
      121 aqvmdalssq anvsgykavv vaadlstryf pmmttaagtv kpatvlvlgv gvaglqalat
      181 akrlggrttg ydvrpevaeq vrsvgaqwld lgidaagegg yareltdder akqqqaleda
      241 iksfdvvitt alvpgrpapr lvtaaavegm kagsvvvdla getggncelt epgetvvkhd
      301 vtitsplnlp atmpehasel ysknllalie lmlddngaia pdfddevlaa scvtreeava
//
LOCUS       WP_124705971             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sulfuriferula multivorans].
ACCESSION   WP_124705971
VERSION     WP_124705971.1
KEYWORDS    RefSeq.
SOURCE      Sulfuriferula multivorans
  ORGANISM  Sulfuriferula multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sulfuricellaceae; Sulfuriferula.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sulfuriferula multivorans"
                     /db_xref="taxon:1559896"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33827
     Region          7..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtttqhhrli ilgsgpagys aavyaaranl npvvitgmaq ggqlmtttdv dnwpadpdgv
       61 qgpelmarfe kharrfntei ifdhihtakl sdkpisligd qgtytcdali iatgasamyl
      121 gleseqafmg kgvsgcatcd gffyrnqdva vigggntave ealylsnitr hvtvvhrrdk
      181 fksekiladh lmekvkegkv svewnsqlde vlgdktgvtg mrikstvdgs trdialtgvf
      241 iaighkpntd iftgqvemeg gyivtkggnk gnatatnipg vfaagdvqdh iyrqavtsag
      301 tgcmaaldad ryleslgk
//
LOCUS       WP_124709446             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gordonia insulae].
ACCESSION   WP_124709446
VERSION     WP_124709446.1
KEYWORDS    RefSeq.
SOURCE      Gordonia insulae
  ORGANISM  Gordonia insulae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Gordonia insulae"
                     /db_xref="taxon:2420509"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35527
     Region          10..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqhdsqqih dliiigsgpa gytaaiyaar aelapivfeg tqfggalmtt tevenfpgfq
       61 sgiqgpalmd emreqairfg adlrmedvdt vrlagavkev evggevyrsr avilamgaaa
      121 rylgieneqt llgrgvsaca tcdgfffkdq diavigggds ameeatfltk farsvtlvhr
      181 reefraskim lerarandki rfvtnsavts vlgdtsvtgl qlsdtitges stidvtgmfv
      241 aighdprsel irgqvdldpe gyvqvdgrtt ytslpgvfac gdlvdhtyrq aitaagsgcs
      301 aaidaerwla eqadvlpdrs vdgeyvvvda papa
//
LOCUS       WP_124714029             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium nivoides].
ACCESSION   WP_124714029
VERSION     WP_124714029.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium nivoides (Mycobacterium nivoides)
  ORGANISM  Mycolicibacterium nivoides
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Mycolicibacterium nivoides"
                     /db_xref="taxon:2487344"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52388
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipresl tgetrvaatp qtvgqiiklg yevvvetgag aassfsdaay ldagaeigqa
       61 wdadvvlkvn apddaeigkl rdgatlvsli spglkpelve klstrpitvl amdavprisr
      121 aqsldvlssm aniagyravv eaahsfgrff tgqvtaagkv ppakvlvvga gvaglaaiga
      181 agslgaivra tdprpevadq vaslggeyls vanenaevsa tgyakemddd ykareaqlya
      241 eqckdvdiiv ttalipgrpa priitaemva smkagsvivd maaanggnve gtvkdqaiit
      301 dngvtiigyt dlagrlpaqa sqlygtnlvn llklltpekd gkvvldwddv vqrsmtvvrd
      361 gettwppppv qvsaapaaqp aaaapvvkee kkpmstgrrl gvtfaaaaai faliamspaa
      421 lqvhltvfal aivigyyvig nvhhalhtpl msvtnaisgi ivvgallqig hgdiaitsla
      481 fvaillasin vfggfavtrr mlamfsrs
//
LOCUS       WP_124715491             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia stagnalis].
ACCESSION   WP_124715491
VERSION     WP_124715491.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39161
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anetrvaatp etvkkyaaag hrvsvakgag vaasypdeay aaagaeltdq
       61 sgafdadivl kvqaptdiei pslkrgsvli gmldpfdgeq aarlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvgaalypr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee cdaaqgvggy arpmpaswlg
      241 rqaalvhera kqadiiitta lipgrpaptl isvetvqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad evivhdgvti agytnlasmv asdasalyar nlldfmkliv tkegtlnidl
      361 tddivaatll crdgevark
//
LOCUS       WP_124719879             320 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Streptomyces].
ACCESSION   WP_124719879
VERSION     WP_124719879.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33679
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfqdgim
       61 gpelmdnmra qaerfgaelv pddvvsvdlt gdiktvtdta gtvhraksvi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfa wdsevagvhg eqklsgltlr ntktgetsel avtglfiavg
      241 hdprtelfkg qldldeegyl kvdapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala ddekaaaatv
//
LOCUS       WP_124722811             329 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Streptomyces].
ACCESSION   WP_124722811
VERSION     WP_124722811.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34665
     Region          11..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msgvtdsgir evviigsgpa gytaalytar aqlkpllfgs sisvggsltt ttevenfpgf
       61 pdgidgpalm enmraqaekf gaemidddiv evdltgdikl ltdssgtvhr aktvivatgs
      121 gyrklgldke dtlsgrgvsw catcdgfffr drdivvvggg dtameeatfl trfaksvtiv
      181 hrrstlrasq vmqnrafadd kisfafdsei aelreengml agltlrdtft gktreldatg
      241 lfiaighdpr talftsqldl ddegyiqvaa pstrtslagv faagdvvdht yrqaitaagt
      301 gaaaaldaer yiaastadpa ngrrptvav
//
LOCUS       WP_124727386             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylospora marina].
ACCESSION   WP_124727386
VERSION     WP_124727386.1
KEYWORDS    RefSeq.
SOURCE      Staphylospora marina
  ORGANISM  Staphylospora marina
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Thermoactinomycetaceae; Staphylospora.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Staphylospora marina"
                     /db_xref="taxon:2490858"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34526
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhrvivlgsg pagltaaiyl aranmqplvv egpepggqlt tttdvenfpg fpegilgpdl
       61 menmrkqaer fgarfrrawv qkvdlssrpf klwigeketl eadaliistg asakllgipg
      121 eresigmgvs tcatcdgfff rgkriivvgg gdsameeatf ltrfasevtv vhrrdqlras
      181 kimqerarqn dkikwcmnrt plevvrteqg tvaglkvrnn etgqeelmet egifvaighk
      241 pntdflkgql emdelgyirv kpgstltsvp gvfacgdvqd rvyrqaitaa gsgcmaaldc
      301 erwlegsmth dwsqtl
//
LOCUS       WP_124729779             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            livingstonensis].
ACCESSION   WP_124729779
VERSION     WP_124729779.1
KEYWORDS    RefSeq.
SOURCE      Shewanella livingstonensis
  ORGANISM  Shewanella livingstonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Shewanella livingstonensis"
                     /db_xref="taxon:150120"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53358
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresi egetrvaatp atviqlkklg fsvaieaqag vkssfdnaaf eaagadvvds
       61 vyqadfifkv naptddeiak mkpgttlvsf iwpaqnpelv eklsshnitv mamdmvpris
      121 raqsldalss maniggyrav ieaahefgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgaivr afdtrlevae qiesmggsfl klefenkegg ssdgyakvms eefieaemal
      241 faeqakdvdi iittalipgr papklitkdm vdtmkpgsvi vdlaaatggn ceytvtgerf
      301 itdngvkvlg ytdlpgrlpa qssqlygtnl vnlmklmcka kdgnavldfd dvvmrnmtvt
      361 rggeitfppp aisvsaapqk paasiapkak vdkapsklky ilgvlglagf aavasvapae
      421 flshftvfil scvvgyyvvw nvshslhtpl msvtnaisgi ivvgallqig qgsalvtala
      481 fvavliasin ifggftvtqr mlkmfrkd
//
LOCUS       WP_124730957             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Shewanella livingstonensis].
ACCESSION   WP_124730957
VERSION     WP_124730957.1
KEYWORDS    RefSeq.
SOURCE      Shewanella livingstonensis
  ORGANISM  Shewanella livingstonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Shewanella livingstonensis"
                     /db_xref="taxon:150120"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33967
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msearhvnll ilgsgpagyt aavyaaranl npvmitgmqq ggqlttttev enwpgdaedl
       61 tgpalmdrmq khaekfdtei ifdhinevtl terpfrlkgd ngeftcdali iatgasakyl
      121 glpseeafmg rgvsacatcd gffyrnqkva vigggntave ealylsnias evhlihrrds
      181 frsekilisr lmdkvangni ilhldqtlee vtgndmgvtg lkkkstkdgs vtdlevagvf
      241 vaighspntg ifadqlemnh gylkvnsglq gnatqtsieg vyacgdvmdq hyrqaitsag
      301 tgcmaaldae ryldakk
//
LOCUS       WP_124733101             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_124733101
VERSION     WP_124733101.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33339
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvvlaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_124736160             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Craterilacuibacter sinensis].
ACCESSION   WP_124736160
VERSION     WP_124736160.1
KEYWORDS    RefSeq.
SOURCE      Craterilacuibacter sinensis
  ORGANISM  Craterilacuibacter sinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Craterilacuibacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Craterilacuibacter sinensis"
                     /db_xref="taxon:2686017"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33531
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msatrhspll ilgsgpagyt aavyaaranl kpvlitgmaq ggqlmtttdv dnwpadaegv
       61 mgpdlmqrfq qhaerfgtem ifdqihttyv qekpirlvgd ageytcdali iatgasaqyl
      121 glpseeafsg kgvsacatcd gffyrnqdva vigggntave ealylaniar hvtlvhrrdt
      181 fraekilvdk lmarvaegki tlklnanlde vlgdasgvtg arlrgndgsl ediklmgvfi
      241 aighkpntdi fkgqlemdat gylvtqggrd gnatatsvag vfaagdvqdh iyrqavtsaa
      301 sgcqaaldae ryldqlk
//
LOCUS       WP_124737812             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Methylocystis rosea].
ACCESSION   WP_124737812
VERSION     WP_124737812.1
KEYWORDS    RefSeq.
SOURCE      Methylocystis rosea
  ORGANISM  Methylocystis rosea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae; Methylocystis.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Methylocystis rosea"
                     /db_xref="taxon:173366"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34027
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mphharviii gsgpagytaa iyaarallep vliagfeqgg qlmitteven ypgfaepiqg
       61 pwlmeqmrlq aehvgtklis dhiveahlde rpfrltgdsg ksytcdslii atgakakwlg
      121 lpseekfkgf gvsacatcdg fffrgkkvlv vgggnsavee alylsnlash vtiihrrdef
      181 rservlvkrl laqenvsilf nhvideivgd enplsvtgar vknvatgaih tlaadgvfva
      241 ighspaself rgqltikpsg yiavepgttr tsmpgvyaag dvadevyrqa vtaaglgcma
      301 alevekflld aptsavkeia
//
LOCUS       WP_124739228             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylocystis rosea].
ACCESSION   WP_124739228
VERSION     WP_124739228.1
KEYWORDS    RefSeq.
SOURCE      Methylocystis rosea
  ORGANISM  Methylocystis rosea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylocystaceae; Methylocystis.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Methylocystis rosea"
                     /db_xref="taxon:173366"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38642
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlaetd kseprvaatp etvkkfiglg advvvaagag adagfadsdy aaagatiads
       61 aaaaltgadv alrvrrpsaa elagaksnla viaimdpfga gaqladlaks gaiafamelm
      121 pritraqtmd vlssqanlag yravidamae ygrsfpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrmg aivtatdvrp atkeqveslg akfiavenee fkqaetsggy akemspeyqk
      241 aqaelvaahi akqdivitta lipgrpapkl isaemvrsmr pgsvivdlaa erggnceltk
      301 pgetvvvdgv kilgalnlag rmastassly aknllafvet lvskdtkqla inwddelvka
      361 taltrdgavv derfk
//
LOCUS       WP_124751625             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tannerella forsythia].
ACCESSION   WP_124751625
VERSION     WP_124751625.1
KEYWORDS    RefSeq.
SOURCE      Tannerella forsythia
  ORGANISM  Tannerella forsythia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Tannerella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Tannerella forsythia"
                     /db_xref="taxon:28112"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33249
     Region          8..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtnekvrcli igsgpagyta aiyasranla pvlyegiqpg gqltttteve nfpgypdgvt
       61 gtemmedmkk qaarfgadir qgiataadls aapyqitidd dkvieaetli iatgasakyl
      121 glpdeqkysg mgvsacatcd gffyrkkkva vvgggdtace ealylsglas qvylivrkpf
      181 lraskvmqdr vmntpniqvl fehntvglfg engvegahlv krkgepdeem vdividgffl
      241 aighnpnski fkpwlatdet gyiqteagtp rttvpgvfaa gdvadphyrq avtaaasgck
      301 aaieaerylm sr
//
LOCUS       WP_124759060             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus agalactiae].
ACCESSION   WP_124759060
VERSION     WP_124759060.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus agalactiae
  ORGANISM  Streptococcus agalactiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus agalactiae"
                     /db_xref="taxon:1311"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32993
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigsg pggmtaalya arsnlkvgli eqgapggqmn ntaeienypg ydhisgpels
       61 mkmyeplekf evehiygivq rvendgdvkr vitedesyea ktvilatgak nsllgvpgee
      121 eytsrgvsyc avcdgaffrd qdllvvgggd saveeavflt qfaksvtiih rrdqlraqkv
      181 lqdrafanee ikfvwdsvvk eikgneikvs gvtvenlktg eisemtfggv fiyvglkphs
      241 smvselgitd etgwvltdtn mktsipglya igdvrqkdlr qiatavgega iagqgvynyi
      301 tehf
//
LOCUS       WP_124756852             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Kaistella daneshvariae].
ACCESSION   WP_124756852
VERSION     WP_124756852.1
KEYWORDS    RefSeq.
SOURCE      Kaistella daneshvariae
  ORGANISM  Kaistella daneshvariae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group; Kaistella.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Kaistella daneshvariae"
                     /db_xref="taxon:2487074"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33418
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meenildcvi vgsgpsgfta aiyaaradlk pqlytglepg gqlttttevd nfpgyadgvt
       61 gpqmmmdlqk qaerfdtkvi yemitkaefs tevggvhklw agnkeilart viistgatak
      121 ylglddekky sgggvsacat cdgffykgkd vivvgagdta aeeatylakl tnkvtllvrk
      181 dhfraskami hrvsntpnie vkfnheligi qgennlverg vvinnltqek stidvhgifi
      241 aighkpntei fagqinlden gyintipgtt ltnlpgvfaa gdvqdshyrq aitaagsgcm
      301 aamdaekyla gle
//
LOCUS       WP_124764361             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lysinibacillus composti].
ACCESSION   WP_124764361
VERSION     WP_124764361.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus composti
  ORGANISM  Lysinibacillus composti
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Lysinibacillus composti"
                     /db_xref="taxon:720633"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34193
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseekiydvv iigagpagmt aavyasranl stimiergip ggqmanteev enypgfdtil
       61 gpelstkmfe hakkfgaeya ygdvseiing edykiikags keyktrsiii tsgaeykkmg
      121 ipgekelggr gvsycavcdg affkqknliv vgggdsavee gvyltrfadk vtivhrrdql
      181 raqkilqdra fanekvdfiw nntvkeinek dgkvgsvtlv ntvdgteqev qadgvfiyig
      241 mipltapfqn lgilneqgyi vtndkmetsv kgifaagdvr dkmlrqivta tgdgsiaaqs
      301 aqhyveelke kisqs
//
LOCUS       WP_124765584             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_124765584
VERSION     WP_124765584.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33006
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedrggfke iitederfet ktviiasgan hrhlgvpgee
      121 dynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdrafanek irfvwdsvve sihgnerkvt gvtfknvktg etsqadfggi fiyvgldpvs
      241 efaadlgitd eagwiltdhq mktsvagiya vgdvrqkdlr qittavgdga tasqeaykyl
      301 teqa
//
LOCUS       WP_124774235             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora inaquosa].
ACCESSION   WP_124774235
VERSION     WP_124774235.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora inaquosa
  ORGANISM  Micromonospora inaquosa
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Micromonospora inaquosa"
                     /db_xref="taxon:2203716"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33608
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlkp liiegvqsgg almttteven fpgfadgilg
       61 pelmdnmrkq aerfgaeflt ddvtrvelvd tgdagsgavs tvwvgetayr arsiilstgs
      121 awrplgvpge qeylghgvsa catcdgfffr nqhivvvggg dsameeatfl trfadsvtii
      181 hrrdsfrask imadralsne kikvewnstv eeilgddgkv tgvrvrnvht getkvmdvtg
      241 vfvaighdpr selfqgqiel ddegyvkvea pstrtnvpgv faagdvvdht yrqaitaagt
      301 gcaaaldaer fiatls
//
LOCUS       WP_124776038             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus minor].
ACCESSION   WP_124776038
VERSION     WP_124776038.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus minor
  ORGANISM  Streptococcus minor
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptococcus minor"
                     /db_xref="taxon:229549"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33197
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigsg pagmtaalya srsnlkvgll ergiyggqmn ntadienypg yelisgpela
       61 ekmyeplekf gvehlfgqvv evqvegsvkk viteddtfea ktvilamgaq hrplgapgea
      121 efnsrgvsyc avcdgaffrn qdllvvgggd saveeaiflt qfansvtivh rrdelraqki
      181 iqdrafanek itflwdsvve eikgderkvq svnirnlktg evtehafggv fiyvgldpms
      241 eavanlgitd ehgwvvtnel metnqpgifa igdlrqkqlr qittavgdga taaqqayhyi
      301 teleg
//
LOCUS       WP_124782804             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia albertii].
ACCESSION   WP_124782804
VERSION     WP_124782804.1
KEYWORDS    RefSeq.
SOURCE      Escherichia albertii
  ORGANISM  Escherichia albertii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia albertii"
                     /db_xref="taxon:208962"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53622
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtriktnarr ffsllipfff ftsvhaeqta spakpvtvea knetfapqhp dqylswkats
       61 elservdala edprlvilwa gypfsrdynk prghayaitd vretlrtgap knaedgtmpm
      121 acwsckspdv arliqkeged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaeramn aigkpfekgg rfdqqsmvcg qchveyyfdg kdkavkfpwd ngmkvenmeq
      241 yydkiafsdw tnalsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkatlqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gataaemksi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_124784486             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium taklimakanense].
ACCESSION   WP_124784486
VERSION     WP_124784486.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium taklimakanense
  ORGANISM  Chryseobacterium taklimakanense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Chryseobacterium taklimakanense"
                     /db_xref="taxon:536441"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33668
     Region          5..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 menihdcvii gsgpsgftaa iyaaradlkp qlytglepgg qlttttevdn fpgypdgitg
       61 pqmmmdlqkq aerfdtkvhy emitkvefat evggihklwa gnkelfaktv iistgataky
      121 lgledekkya gggvsacatc dgffykgkdv ivvgagdtaa eeatylaklt nkvtmlvrrd
      181 efraskamih rvkntpniev kfhheligie genglverav vinnqtqets kidvhgifia
      241 ighkpnteif kdqintdeng yivtvpgstk tnlpgvfaag dvqdhvyrqa itaagtgcma
      301 amdaekylae lq
//
LOCUS       WP_124788180             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sp. OH4692_COT-348].
ACCESSION   WP_124788180
VERSION     WP_124788180.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. OH4692_COT-348
  ORGANISM  Streptococcus sp. OH4692_COT-348
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus sp. OH4692_COT-348"
                     /db_xref="taxon:2491052"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32969
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehiygyvk nvedhgdfkk vitddqtyet rtvivatgsk hrplgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdrafanek isfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldplsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrlkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_124789348             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tannerella forsythia].
ACCESSION   WP_124789348
VERSION     WP_124789348.1
KEYWORDS    RefSeq.
SOURCE      Tannerella forsythia
  ORGANISM  Tannerella forsythia
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Tannerellaceae; Tannerella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Tannerella forsythia"
                     /db_xref="taxon:28112"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33221
     Region          8..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtnekvrcli igsgpagyta aiyasranla pvlyegiqpg gqltttteve nfpgypdgvt
       61 gtemmedmkk qaarfgadir qgiataadls aapyqitidd dkvieaetli iatgasakyl
      121 glpdeqkysg mgvsacatcd gffyrkkkva vvgggdtace ealylsglas qvylivrkpf
      181 lraskvmqdr vmntpniqvl fehntvglfg engvegahlv krkgepdeem vdiaidgffl
      241 aighnpnski fkpwlatdet gyiqteagtp rttvpgvfaa gdvadphyrq avtaaasgck
      301 aaieaerylm sr
//
LOCUS       WP_124792836             308 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Desulfovibrio].
ACCESSION   WP_124792836
VERSION     WP_124792836.1
KEYWORDS    RefSeq.
SOURCE      unclassified Desulfovibrio
  ORGANISM  unclassified Desulfovibrio
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfovibrio.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="unclassified Desulfovibrio"
                     /db_xref="taxon:2593640"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32516
     Region          4..286
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkgydavvig ggpagitaam ylarsgcsvl ltehmatggq ilqtealeny pgfpqgikgy
       61 eladlftahl eglgvdrsav tvesvsgdag qfsvraggee haakvvlvct garhrqlgle
      121 gedrlrgrgv sycalcdgnf frnqtvavvg ggnsaleesl ylaklvdkly lihrrdefrg
      181 hkiyldkimh lsgkielvrs svitglhgdn qltglsvknl ktndervlav dglfvyvgse
      241 patgflpdgi acdaqgflvt dtemrtsipg ifaagdirsk lcrqvitaag dgataaqaaf
      301 vfleqlha
//
LOCUS       WP_124794341             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Conchiformibius steedae].
ACCESSION   WP_124794341
VERSION     WP_124794341.1
KEYWORDS    RefSeq.
SOURCE      Conchiformibius steedae
  ORGANISM  Conchiformibius steedae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Conchiformibius.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Conchiformibius steedae"
                     /db_xref="taxon:153493"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33397
     Region          5..310
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mshhkliilg sgpagytaav yaaranlqpa litgmaqggq lmtttevdnw padaqgvqgp
       61 elmarfqaha erfgtemifd qiqrvdlqnr pftlvgdage ytcdalivat gasakylgla
      121 geeqfagrgv sacatcdgff yknqnvavvg ggntaveeal ylaniaakvt lihrrdsfra
      181 ekimvdklmr rveegkielk lnaevaeilg ddmgvnalrl kladgsseel avqglfvaig
      241 hkpntdifqg qldmdetgyl ktrggsgdnv gatniegvwa agdvkdhtyr qaitsaasgc
      301 qaaldaerwl dgqr
//
LOCUS       WP_124803008             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Epilithonimonas vandammei].
ACCESSION   WP_124803008
VERSION     WP_124803008.1
KEYWORDS    RefSeq.
SOURCE      Epilithonimonas vandammei
  ORGANISM  Epilithonimonas vandammei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Epilithonimonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Epilithonimonas vandammei"
                     /db_xref="taxon:2487072"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34566
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mennildcvi igsgpagfta aiyaaraslk pelftglepg gqltttteve nfpgypdgit
       61 gpemmlqlqk qaerfetkvh yemiskvefs kvrggihkls tgsreilaks viistgatak
      121 ylgladekky agggvsacat cdgffyrgkd vivvgagdta aeeatylski cnkvtllvrk
      181 dhfraskvmv drvlstsnie vkynheligi egenalvera kvvnnltdev stidvhgifi
      241 aighkpntdl fkgqvdlden gyiitegksa rtnlpgvfaa gdvqdhhyrq aitaagsgcm
      301 aamdaekylg elagekhtwv eq
//
LOCUS       WP_124803490             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Halomonas sp. YLB-10].
ACCESSION   WP_124803490
VERSION     WP_124803490.1
KEYWORDS    RefSeq.
SOURCE      Halomonas sp. YLB-10
  ORGANISM  Halomonas sp. YLB-10
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Halomonas sp. YLB-10"
                     /db_xref="taxon:2483111"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33948
     Region          9..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msevrherli ilgsgpagys aavyaaranl kpllitgmqt ggqlttttdv dnwpgddagv
       61 qgpelmermr rhaerfdtev lfdhihevel rerpftlkgd ngtytcdali iatgasaryl
      121 glpseqhfmg qgvsacatcd gffyrnqevi vvgggntave ealylsnias kvtlvhrrds
      181 lraekilqdk lfekaengnv eliwnhtlde vlgdntgvtg arlkavedgs treitapgvf
      241 iaighspntg ifegqlemag gyikvksgle gnatatsvpg vfaagdvmdh vyrqaitsag
      301 sgcmaaldve ryldsld
//
LOCUS       WP_124807958             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Novosphingobium sp. LASN5T].
ACCESSION   WP_124807958
VERSION     WP_124807958.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. LASN5T
  ORGANISM  Novosphingobium sp. LASN5T
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Novosphingobium sp. LASN5T"
                     /db_xref="taxon:2491021"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34153
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 matthktrml iigsgpaglt aaiygaragm epivvqglqp ggqltittdv enypgfreav
       61 qgpwlvqemq aqaehvgtrm lwdtitevsl egppfravgd sgdmyegdtl viatgaqakw
      121 lgvpgevefg gkgvsacatc dgffyrgkkv vvigggntav eealyltnhs qdvtiihrrd
      181 sfraekilqd rlfahphvkv lwnkkvdrfv gepgkgltgv avidtetgeq svvetdgafv
      241 aighapatel fkgkleldes gyifvqpgtp ktaipgvfaa gdvmdhtyrq avtaagtgcm
      301 aaldaerfva eldfaatkte avg
//
LOCUS       WP_124813953             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas caviae].
ACCESSION   WP_124813953
VERSION     WP_124813953.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53444
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tclgtsgwaq aadeaqskgk iearselfak dhadqftswk
       61 gtsesrertd alaedpqmvv lwagypfskd ynkprghfya ltdvretlrt gapktaedgp
      121 lpmacwsckg pdvarvider gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meeyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg vvkqrkdavt eiklkvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakgish eiaipdissk ekaqaalgmd mqqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_124818206             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cepacia].
ACCESSION   WP_124818206
VERSION     WP_124818206.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39138
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiargag laasypdaay aaagaeltgq
       61 saafdvdivl kvqaptdael pllkrgavlv gmldpfngeq aaklaaagvt gfaleaaprt
      121 traqgldvls sqaniagyka vlvaaalypr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee rdaaqgvggy arlmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetvqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qviahhgvti agytnlasmv asdasalyar nlldfmkliv tkegtlnidl
      361 tddivaatll crdgevtrr
//
LOCUS       WP_124819930             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micromonospora ureilytica].
ACCESSION   WP_124819930
VERSION     WP_124819930.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora ureilytica
  ORGANISM  Micromonospora ureilytica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Micromonospora.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Micromonospora ureilytica"
                     /db_xref="taxon:709868"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33533
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlkp liiegvqsgg almttteven fpgfadgilg
       61 pelmdnmrkq aerfgaeflt ddvtrvelvd tgdagsgavs tvwvgetayr arsiilstgs
      121 awrplgvpge qeflghgvss catcdgfffr nqhivvvggg dsameeasfl trfaesvtii
      181 hrrdsfrask imadralsne kikvewnsav eeilgddgkv tgvrvrnvht gdtkvldvtg
      241 vfvaighdpr selfqgqvem ddegyvkvqa pgtrtnvpgv faagdlvdht yrqaitaagt
      301 gcaaaldaer fiatls
//
LOCUS       WP_124825559             381 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Burkholderia].
ACCESSION   WP_124825559
VERSION     WP_124825559.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39241
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnigvpveta agetrvavtp etakkltaqg hvvriasgag alsnapdday raagaemtdq
       61 agalgcdlvl kvrapddael ggfrhgavlv gmldpfdagr aqrlavagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaahayqr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgsggy arpmppswla
      241 rqaalvhera kqadivista lipgrtaptl ipaetvrsmr pgsvivdlaa grgvqhgtht
      301 ggncpltepd rivvhhgvti ightnlpama aadasalyar nvldflkliv gqdgrlnidt
      361 dddivaatll thdgavmrha a
//
LOCUS       WP_124836788             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia glumae].
ACCESSION   WP_124836788
VERSION     WP_124836788.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia glumae
  ORGANISM  Burkholderia glumae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia glumae"
                     /db_xref="taxon:337"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34002
     Region          7..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstkhakvli lgsgpagyta avyaaranls pllitgiaqg gqlmtttdve nwpadpngvq
       61 gpelmqrfle haerfnteiv fdhihtarld ekpirligds geytcdalii stgasaqylg
      121 laseeafmgk gvsacatcdg ffyrnqdvav igggntavee alyltgiakk vtvihrrdkf
      181 raepilidrl lekekegkve ikwnhvldev tgddsgvtgv rikhtgtgea eqialqgvfv
      241 aighkpntdi fqgqlemkdg yivtksglag natatsipgv faagdvqdhi yrqaitsagt
      301 gcmaaldaqr yleslhdan
//
LOCUS       WP_124844863             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arachnia propionica].
ACCESSION   WP_124844863
VERSION     WP_124844863.1
KEYWORDS    RefSeq.
SOURCE      Arachnia propionica
  ORGANISM  Arachnia propionica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Arachnia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Arachnia propionica"
                     /db_xref="taxon:1750"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32541
     Region          4..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msihdliiig sgpagytaai yaaraalspv vfegafsggg almnttdven fpgfpegvmg
       61 pdlmenmraq akrfgaelvt ddvtavdltg evkqvtdstg nlwqaravil amgsgyrklg
      121 vpgedrlsgf gvswcatcdg affrdkpiiv vgggdsavee atfltrfgss vllvhrrdel
      181 raskvmvara ekdpklsfaw nsvvesmnge stvesvtlrd vvtgatrdve aagvfvaigh
      241 dprselvkgq vdlddagyvl vregsqatnl dgvfacgdlv dhtyrqaita agsgcraald
      301 aerwlaalqs
//
LOCUS       WP_124845503             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Arachnia
            propionica].
ACCESSION   WP_124845503
VERSION     WP_124845503.1
KEYWORDS    RefSeq.
SOURCE      Arachnia propionica
  ORGANISM  Arachnia propionica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Arachnia.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Arachnia propionica"
                     /db_xref="taxon:1750"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52886
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigviremg dtrvaatprt vqqlirlgye vvvesgaglk asfrdedyea agagivpsaw
       61 esdvvlgigs phetqiagmr pgatlitfla prqhpelttr laaqgitals mdmvprtsra
      121 qaldalssla nisgyravve aahafgrfft gqvtaagkvp patvlvigag vaglaaigaa
      181 nslgavvrat dvrpetaeqv esmgatfvhv dgmdqevssd gyakevgadf aaraaelyaa
      241 qarevdiiit taaipgrpsp rlitaemvas mkpgsvivdl aasgggncel trpgeshvtd
      301 ggvtiigytd lasrlpgqss qlygtnlvna lslmtpgkdg qlvvdfddev vrtmtvvrdg
      361 rvtfppppiq vsatparapv rqgpevvtpp psprpwwhqv alvgvgaigf iaaltvapss
      421 fvtlmgvfvv aivvgyyvvw nvthalhtpl msvtnavsgi ivvgamtqla hddwvvkala
      481 fiavliasin vfggftvthr mldmfrkg
//
LOCUS       WP_124847524             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acidipila sp. EB88].
ACCESSION   WP_124847524
VERSION     WP_124847524.1
KEYWORDS    RefSeq.
SOURCE      Acidipila sp. EB88
  ORGANISM  Acidipila sp. EB88
            Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia;
            Terriglobales; Acidobacteriaceae; Acidipila.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Acidipila sp. EB88"
                     /db_xref="taxon:2305226"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33712
     Region          9..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpdtsirnvv ilgsgcsglt aaiytgrsnl rplvieghep ggqlsittlv enfpgwpegi
       61 qgpdlienmk tqagrfgaef qmghlvsadl sqrpfalnfg ketiythtlv iasgasarwl
      121 nlpseqslig hgvsscatcd gfffsgreia vvgggdsame ealfltrfas kvtllhrsdn
      181 frasaimler akahekiefr tnvaieevlg veerevkgvr lrdrrtdelt dlpiaglflg
      241 ighepnakaf agqieldedg yikthdnvft rvpgvfacgd vqdrryrqai taagsgcmaa
      301 levekflede gl
//
LOCUS       WP_124852109             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Buchananella hordeovulneris].
ACCESSION   WP_124852109
VERSION     WP_124852109.1
KEYWORDS    RefSeq.
SOURCE      Buchananella hordeovulneris
  ORGANISM  Buchananella hordeovulneris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Buchananella.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Buchananella hordeovulneris"
                     /db_xref="taxon:52770"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52485
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvprehp dqplvaatpt svkalrqlgy evtvesgage rasfpdahyq dagaelgdaa
       61 avwsadivis ldaptaaqla smrtgatlla rlaparhpel vaelsaaelt alavdavpri
      121 sraqsmdvls sqanivgyra vieaaahfgr vftgqitaag klpparvyvi gagvaglaai
      181 gtasslgaev sasdvrpeva eqvqslgakf vplptatsqs tdgyaqalad eqaavaaaly
      241 aaqaaahdiv ittanipgrr apvlldeaav aamapgsviv dlaaanggnc tltvpdevvt
      301 tpsgvqivgy rdlaarlpaq ashlygsnlv nllrlltpgr dgqlqldltd eivrgitvtd
      361 rgqvlwpppp vtvsatpapa gpptptaatd stapdranqa rarrgrlcgl faaglalaal
      421 ifvspaqvtg hyvtlllsvt lgfyvisnvt palhtplmsv tnaisgivll ggiaqighph
      481 pavaalsfaa itlasvnifg gfavthrmla mfrkd
//
LOCUS       WP_124872386             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Deinococcus psychrotolerans].
ACCESSION   WP_124872386
VERSION     WP_124872386.1
KEYWORDS    RefSeq.
SOURCE      Deinococcus psychrotolerans
  ORGANISM  Deinococcus psychrotolerans
            Bacteria; Thermotogati; Deinococcota; Deinococci; Deinococcales;
            Deinococcaceae; Deinococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Deinococcus psychrotolerans"
                     /db_xref="taxon:2489213"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34749
     Region          14..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtnaqpsqpq psehdvviig ggpagltaai ytgraslnti ilekglpggq iaqteeveny
       61 pgfpepisgp elaqrmteqa erfgakieme evqgvehhph ggflvrgysg tyhakavila
      121 tganpkrlyv pgeeqfwgkg vstcatcdgf fyrgkkvvvv gggdaaveeg lfltkfadev
      181 tlihrrdtlr ankvaqaral anpkmkfvwd taveaiiged svsavqlknl ktgeesrfdt
      241 dgvfifighv pnteflkgvv klredgyvdv rddiftsvpg mfaagdisdy vyrqlatsvg
      301 agtraamsve rmlaalelee saad
//
LOCUS       WP_124870789             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Larkinella rosea].
ACCESSION   WP_124870789
VERSION     WP_124870789.1
KEYWORDS    RefSeq.
SOURCE      Larkinella rosea
  ORGANISM  Larkinella rosea
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Larkinella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Larkinella rosea"
                     /db_xref="taxon:2025312"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34055
     Region          8..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttehvncli igsgpagyta aiyasragmk pvlyqgmqpg gqltitnevd nfpgypegvh
       61 gqqlmvdleq qarrfgtdir ygvvtavdfs gsihkatvde qqeisanvvi istgasakwl
      121 glpsemrlng lgvsacavcd gfffrgkdva ivgagdtaae easylanlcr kvymivrrge
      181 mraskfmqnr vkslpnieil wnseteevlg edevtgalik ntvtgekrvi dvsgffvaig
      241 hepntaifkp yvemdetgyi itekgssrtn vpgvfacgda qdniyrqait aagtgcmaal
      301 daerylamke vemhaea
//
LOCUS       WP_124868751             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Schaalia
            canis].
ACCESSION   WP_124868751
VERSION     WP_124868751.1
KEYWORDS    RefSeq.
SOURCE      Schaalia canis
  ORGANISM  Schaalia canis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Schaalia canis"
                     /db_xref="taxon:100469"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52636
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligvpkegv nqplvgatpd tvkklislgy dvrvqsgaga yahltdqaya nagaeltdda
       61 dawgadlvia ldaptdehla lmrsgatlit rlaparnpel leklraagvt amamdtvpri
      121 sraqamdvls sqanvagyra vveaaaafgr lftgqvtaag kmppakvyvi gagvaglaai
      181 gtansmgaev satdvrpeva eqvesmgarf vaipaqqevs sdgyakemsa dqemvaraly
      241 akvaaesdiv ittanipgrt apilldedav namrpgsviv dmaaanggnt altvagetiv
      301 tpggvtiigh sdlagrlpgq ssqlygqnvv nllklmtpgk dgelvvdled eivrgitvtq
      361 sgeilwpppp vkvsaapaaa aaepspqera aaaaraaeea alakrrtffg llaaalvgaa
      421 lvlatpalaa gnyivlmlav vvgfyvitgv thslhtplms vtnaisgiil lgailqigss
      481 npivsalsfv aivvssinif ggflvthrml amfqkg
//
LOCUS       WP_124869929             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Schaalia canis].
ACCESSION   WP_124869929
VERSION     WP_124869929.1
KEYWORDS    RefSeq.
SOURCE      Schaalia canis
  ORGANISM  Schaalia canis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Schaalia canis"
                     /db_xref="taxon:100469"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32777
     Region          6..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msekvhdvvi vgsgpagyta aiytaragla pvvvagaisa ggalmtttdv enfpgfpegi
       61 mgpdlmenmr aqaerfgadi rfedasavdl tgeiktvtid detlqaravi latgsahrql
      121 hvrgeellmg hgvsycatcd gfffrdkvla vigggdsame eatfltrfas kvyvvhrrdq
      181 lraskvmadr amndpkiefv wnsavsevlg gaqveglrle stvdgsestl pvdgvfvaig
      241 hlprseivag qvelddagyv rveepttrtn lpgvfacgdl vdhsyrqait aagsgcraal
      301 dverwladqg
//
LOCUS       WP_124886185             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Leucobacter sp. OH1287].
ACCESSION   WP_124886185
VERSION     WP_124886185.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter sp. OH1287
  ORGANISM  Leucobacter sp. OH1287
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Leucobacter sp. OH1287"
                     /db_xref="taxon:2491049"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32638
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhhvaiigsg paaltaaiyt araglkpvlf assvtpggel mnttevenfp gfpegiqgpd
       61 lmakiqeqae kfgtevryed veelrldgde kvivtadgte hsahaiifat gsayrklgia
      121 dedrlsghgv swcatcdgff frdkviavvg ggdsameeat fltrfaskvy vihrrdslra
      181 skimqqrald nekiefvwns evsalhgdda ltgvtltdtv tgdtrqldld glfiaigndp
      241 rthlvhdkle ltsggtiavd grssrtsvag vfaagdvidp tyrqaitaaa sgtvaaldae
      301 hyladlag
//
LOCUS       WP_124887462             396 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Fretibacterium sp.
            OH1220_COT-178].
ACCESSION   WP_124887462
VERSION     WP_124887462.1
KEYWORDS    RefSeq.
SOURCE      Fretibacterium sp. OH1220_COT-178
  ORGANISM  Fretibacterium sp. OH1220_COT-178
            Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
            Aminobacteriaceae; Fretibacterium.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Fretibacterium sp. OH1220_COT-178"
                     /db_xref="taxon:2491047"
     gene            1..396
                     /gene="trxB"
     Protein         1..396
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=42458
     Region          5..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mekrelviig agpagmtaai ygrrsgldvl llekaatggq initdeienw pgvqhstgpd
       61 lgnmfrehal kfnteiriad vkkvelrdgk kivvtdkgev eaeavivatg ahfrrlgceg
      121 eaehigqgvs fcavcdgafy edeevavvgg gntaveegvy ltkfaskvyi ihrrdefrad
      181 raaiehamsn pkivpvwnsv veriegdgvv enlvlknvkt gelsdlkvag vfmfvgqtpd
      241 ddcvrglvka ekggwilvne hmetsvegif aagdvcskhl rqvitaasdg aiaamgasay
      301 ineqlhlrtt llepesvtaf fyssidekqv klsstveaaa kakgvkvpli dgyrnarmte
      361 kleltakmpa lvelhkgvva kvttvgsdad vqkala
//
LOCUS       WP_124894637             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Microbacterium].
ACCESSION   WP_124894637
VERSION     WP_124894637.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium
  ORGANISM  Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Microbacterium"
                     /db_xref="taxon:33882"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33844
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msiqevelvi igsgpagyta avyaaragla pvvlagsvta ggalmtttev enfpgfvdgv
       61 qgpelmesmr aqaerfgari llddavavdl agpvktvrtg sgdtylarav ilamgsayrk
      121 igladeerlt ghgvswcatc dgfffrdqei vvvgggdsam eealfltrfa skvtvvhrrd
      181 tfrasqimaq rvlehpkidv awnsevagil gtdkveavtl rdtvsgaere lsvtgvfvai
      241 ghdprselva gsvdtdadgy vrvvhpstrt tldgvfaagd lvdhiyrqai taagtgcaaa
      301 qdaqhylaal tdtapafdaq evla
//
LOCUS       WP_124897429             532 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_124897429
VERSION     WP_124897429.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..532
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55003
     Region          3..532
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagasiv
       61 ataaelwsgs divfkvrpps teevasmreg gtligfvwpa qnpelmeqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq ardadiiitt alipgkpapk litadmvrsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvve elckgkdgti dvdfdddair
      361 gltvikegnv twppppikqa avapkppaaa paaapakskg hghsgepmsa kalaivfavg
      421 avafllvgqf apasflshft vfvlacfvgy mviwnvtpsl htplmsvtna issiiaigal
      481 vqvappldel anagdrpsgl ilglavgalt ltavnmfggf avtrrmlamf rk
//
LOCUS       WP_124899916             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenimyroides viscosum].
ACCESSION   WP_124899916
VERSION     WP_124899916.1
KEYWORDS    RefSeq.
SOURCE      Paenimyroides viscosum
  ORGANISM  Paenimyroides viscosum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Paenimyroides.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenimyroides viscosum"
                     /db_xref="taxon:2488729"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33684
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msttietikc liigsgpagy taaiyaaran mnpvlyqgmq pggqltttne venfpgypdg
       61 vtgpemmmql qaqakrfgtd vrdgfatkvd lsgeikkvwi ndtieihakt viistgatak
      121 ylglpseqhy lqmgggvsac avcdgffyrn qeviivgagd saceeahyls hlckkvtmlv
      181 rsekfraski medrvkntpn ieilmsteid evlgdgqivn gvrvvnnvtg ekkevavtgv
      241 fvaighkpnt difagqltmd etgylitegk tsktnmpgvf acgdvqdkdy rqaitaagsg
      301 ciaaldaery lasls
//
LOCUS       WP_124902592             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia sp. Bp9004].
ACCESSION   WP_124902592
VERSION     WP_124902592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9004
  ORGANISM  Burkholderia sp. Bp9004
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia sp. Bp9004"
                     /db_xref="taxon:2184559"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55083
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatqerrvas vpevveklik lgftvavqsg agaganfddd ayraagasia
       61 ataaelwsgs divfkvrpps adevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmas isgyraviea ahafgrflng qvtaagkipp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvie elckakdgti nvdfdddair
      361 gltvikegnv twppppikqa avapkppaaa paaaapaksk ghghsgepms akalaivfai
      421 galafllvgq fapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapplge lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_124904354             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Larkinella knui].
ACCESSION   WP_124904354
VERSION     WP_124904354.1
KEYWORDS    RefSeq.
SOURCE      Larkinella knui
  ORGANISM  Larkinella knui
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Larkinella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Larkinella knui"
                     /db_xref="taxon:2025310"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33926
     Region          8..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttehvncli igsgpagyta aiyasragmk pvlyqgmqpg gqltitnevd nfpgypdgvn
       61 gpqlmadleq qarrfgsdir ygvvtsvdfs gpihkavidd qqeisanvvi istgasakwl
      121 glpsemrlng lgvsacavcd gfffrgkdva ivgagdtaae easylanlcr kvymivrrge
      181 mraskfmqnr vkslpnieil wnseteevlg eeevtgalik navtgekrvi disgffvaig
      241 hvpntaifkp yieldetgyi itekgstrts mpgvfacgda qdntyrqavt aagtgcmaal
      301 daerylamke vemhaea
//
LOCUS       WP_124905843             386 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Burkholderia].
ACCESSION   WP_124905843
VERSION     WP_124905843.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39720
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpvett pgearvavtp etagklqdqg htvrvasgag lgasytdday raagaeivdq
       61 atalgcevvl kvrspldsel aafgmgaalv gmlnpfdaag lerlakagit afaleaaprt
      121 traqsldvls sqaniagyka vmiaadryrr ifpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvggy arpmpaswlq
      241 rqqvevarrv aaadivitta lipgrpapvl vteamvesmk pgsvivdlaa aqggncplte
      301 pgstavrhgv tivgetnlpa lvatdasnly arnvldflkl ilpkgggvti dleddivtac
      361 lvardgmvmr dqpapvrsta easttn
//
LOCUS       WP_124912355             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Buchananella hordeovulneris].
ACCESSION   WP_124912355
VERSION     WP_124912355.1
KEYWORDS    RefSeq.
SOURCE      Buchananella hordeovulneris
  ORGANISM  Buchananella hordeovulneris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Buchananella.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Buchananella hordeovulneris"
                     /db_xref="taxon:52770"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52500
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvprehp dqplvaatpt svkalrqlgy evtvesgage rasfpdahyq dagaelgdaa
       61 tvwsadivis ldaptaaqlv smrtgatlla rlaparhpel vaelsaaelt alavdavpri
      121 sraqsmdvls sqanivgyra vieaaahfgr vftgqitaag klpparvyvi gagvaglaai
      181 gtasslgaev sasdvrpeva eqvqslgakf vplptatsqs tdgyaralad eqaaaaaaly
      241 aaqaaahdiv ittanipgrr apvlldeaav aamapgsviv dlaaanggnc tltvpdevvt
      301 tpggvqivgy rdlaarlpaq ashlygsnlv nllrlltpgr dgqlqldltd eivrgitvtd
      361 rgqvlwpppp vtvsatpvpa gpptptaatd stapdrasqa rarrgrlcgl faaglalaal
      421 ifvspaqvtg hyvtlllsvt lgfyvisnvt palhtplmsv tnaisgivlv ggiaqighph
      481 pavaalsfaa itlasvnifg gfavthrmla mfrkd
//
LOCUS       WP_124921384             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia sp. Bp9099].
ACCESSION   WP_124921384
VERSION     WP_124921384.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9099
  ORGANISM  Burkholderia sp. Bp9099
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia sp. Bp9099"
                     /db_xref="taxon:2184568"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34318
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlitgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfl ehaerfntei vfdhihtakl hekpirligd sgeytcdsli iatgasaqyl
      121 glpseelfmg kgvsacatcd gffyrnqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegvv dikwdhvlde vtgedsgvtg lriknvktge kqdltvqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglq gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldvq ryleslhdkk
//
LOCUS       WP_124921962             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia stagnalis].
ACCESSION   WP_124921962
VERSION     WP_124921962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34142
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlvtgiaq ggqlmtttdv enwpadakgv
       61 qgpdlmqrfl ehaerfntei lfdhihtakl hekpirligd ageytcdsli iatgasaqyl
      121 glpseeafmg kgvsacatcd gffyrgqnva vvgggntave ealyltgias kvtvihrrdk
      181 fraepilvdr llekekegkv eikwnhllde vtgedsgvtg lrlknvqtga tediqvqgvf
      241 vaighkpntd ifqgqlemkd gyiltksglq gnatstsvpg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdhk
//
LOCUS       WP_124932171             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Alloprevotella sp.
            OH1205_COT-284].
ACCESSION   WP_124932171
VERSION     WP_124932171.1
KEYWORDS    RefSeq.
SOURCE      Alloprevotella sp. OH1205_COT-284
  ORGANISM  Alloprevotella sp. OH1205_COT-284
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Alloprevotella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Alloprevotella sp. OH1205_COT-284"
                     /db_xref="taxon:2491043"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33496
     Region          7..291
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mellktvilg sgpagytaai yagrsgitpv iyeglqpggq ltqttdvdnf pgypqgvdgn
       61 vlmddlrsqa irfgaeirtt lctaadlsqr pftltfddgs qvktetliia tgatakylgl
      121 pdeekyrgig vsacatcdgf fyrkkkvavv gggdtaceea tylaglaekv ylivrkpylr
      181 asqamqdrvf snekieilfe tntvglfgkd gvegahlvrr kgepdeekfd iaidgfflai
      241 ghnpnseifr kwinvdetgy iktegqtprt nipgvfaagd vadplyrqav taaaagckaa
      301 ievkafldeh ns
//
LOCUS       WP_124917436             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bifidobacterium adolescentis].
ACCESSION   WP_124917436
VERSION     WP_124917436.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium adolescentis
  ORGANISM  Bifidobacterium adolescentis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Bifidobacterium adolescentis"
                     /db_xref="taxon:1680"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32915
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdmrdvvii gsgpagytaa iylgragfep lvvagaltpg gqlvntteve nfpgfpdgim
       61 gpdlmdnmrk qaerfgthiv wddvvsvasn adsgiktvtl dggdvydara lviatgsnyr
      121 klgvpgeaey agkgvsycat cdgfffrnkp ivvvgggdsa feeadflsrf gssvtlihrr
      181 stfrasrimv eraqrnpkid fmldavvqei rgdengvqev evrntstekt svipangvfv
      241 aightpataf lnglvdvdsa gyitvdgast rtsepgvfaa gdcvdsvyrq aisaagmgcr
      301 aaldaqayld slk
//
LOCUS       WP_124927006             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Amphritea balenae].
ACCESSION   WP_124927006
VERSION     WP_124927006.1
KEYWORDS    RefSeq.
SOURCE      Amphritea balenae
  ORGANISM  Amphritea balenae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Amphritea.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Amphritea balenae"
                     /db_xref="taxon:452629"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34149
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msetqhhkli ilgsgpagyt aavyaaranl npvvitgmqa ggqlttttev dnwpgdvdgv
       61 qgpelmqrmq ahaerfdtqv lfdhinetdl qnrpfrlkgd mgeytcdali ictgasaqyi
      121 glpseeafmg kgvsacatcd gffyrgqkva vigggntave ealylsniaa evtlihrrds
      181 lrsekilqdk lleraengni nilwnhqlde vlgddmgvtg irvkstqdes tqqldlqgvf
      241 vaighkpntd ifagqlemkd gyltiqsgte gnatqttveg vfaagdvadh iyrqaitsag
      301 fgcmaaldae ryldnqe
//
LOCUS       WP_124932623             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces bowdenii].
ACCESSION   WP_124932623
VERSION     WP_124932623.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces bowdenii
  ORGANISM  Actinomyces bowdenii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Actinomyces bowdenii"
                     /db_xref="taxon:131109"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53216
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpcerp drplvsatpq taerlsrlgh evlvergagl rasapdeaya eagarladra
       61 evwgcdivls tgapgaedld lmrrgamilg rldparrpel leslrerglt gvaldavpri
      121 sraqamdvls sqanlagyra vieaaahfgr lfsgqvtaag kfppaqayvi gagvaglsai
      181 gtahslgaiv rgsdvrpeva dqvrsmgaqf valpgaqevs sdgyakelgt dqeaaaraly
      241 aqqaaqadiv ittasipgrq apllldraai eamrpgsviv dmaaanggnt eltvpgevvr
      301 tpggvtivgh ldlagrlpaq asqlygqniv nllalmtpek dgalaldldd eilrsvtvah
      361 dgavlwpppp isvsaapsap agpspeelrq srereaaqra rsrrrrtagl alvaalaaal
      421 vlvtpaaaas hyvvltlavi lgfhvisnvt palhtplmsv tnaisgiilv gaisqvgsan
      481 plisavsfva ivlatinvfg gfavthrmlt mfrkd
//
LOCUS       WP_124933159             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinomyces bowdenii].
ACCESSION   WP_124933159
VERSION     WP_124933159.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces bowdenii
  ORGANISM  Actinomyces bowdenii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Actinomyces bowdenii"
                     /db_xref="taxon:131109"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32895
     Region          3..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mihdvvivgs gpagytaaiy aaraqlsplv lagsvtagga lmntteveny pgfiegimgp
       61 almnqmqeqa erfgaeirye dvtalelqge ikrltteegt yeartviist gseyrhlgle
      121 geerlaghgv sycatcdgff fkdqnivvvg ggdsameeat fltrfgksvt vvhrrdelra
      181 savmaqrakd dpkisfawns rvvelhgeds ltgvtledtv tgerrlleat glfvaigqip
      241 rselvadald ldeagyirve apsqrtripg vfacgdvadp tyqqaitaag sgcraaldae
      301 hyladlqa
//
LOCUS       WP_124936852             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vibrio viridaestus].
ACCESSION   WP_124936852
VERSION     WP_124936852.1
KEYWORDS    RefSeq.
SOURCE      Vibrio viridaestus
  ORGANISM  Vibrio viridaestus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Vibrio viridaestus"
                     /db_xref="taxon:2487322"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34128
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdakhskll ilgsgpagyt aavyaaranl dpvlitgmqq ggqlttttev enwpgdaegl
       61 tgpglmdrmk ehaerfntqi ifdhinevdl kqrpftlkgd sevytcdali ittgasakyl
      121 gldseeafkg rgvsacatcd gffyrnqkva vvgggntave ealylsnias evhlihrrdt
      181 frsekilidr mmdkvangni ilhtdrtlee vvgddmgvtg vrlkdtksgd veqldvmgvf
      241 iaighqpnts ifadqlelkd gyivvqsgln gnatqtsveg vfaagdvmdh nyrqaitsag
      301 tgcmaaldae ryldslak
//
LOCUS       WP_124943660             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Weissella viridescens].
ACCESSION   WP_124943660
VERSION     WP_124943660.1
KEYWORDS    RefSeq.
SOURCE      Weissella viridescens
  ORGANISM  Weissella viridescens
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Weissella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Weissella viridescens"
                     /db_xref="taxon:1629"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33239
     Region          5..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtekfdvvii gagpggmtaa tyasranlsv vmldrgiygg qmnntaeven ypgynsimga
       61 dlsekmyass tqfgaeyqfg tvqhietnad ntwhvvtdmn dyqansviva tgseykklgv
      121 pgeldyagrg vsycavcdga ffkgqgvvvv gggdsaieea tylagivdhv tvvhrgdtlk
      181 aqpilqkraf dadnidfiwn tevqsingdg tkvtsvtlkn nvtnetedfa tsatfiyigl
      241 lpvsdsvdgl gitdeqgwil tndqmettqp gifaigdvrq kqlrqittav gdaaiagqna
      301 yaynetlkdg ve
//
LOCUS       WP_124947915             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sulfurirhabdus autotrophica].
ACCESSION   WP_124947915
VERSION     WP_124947915.1
KEYWORDS    RefSeq.
SOURCE      Sulfurirhabdus autotrophica
  ORGANISM  Sulfurirhabdus autotrophica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sulfuricellaceae; Sulfurirhabdus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sulfurirhabdus autotrophica"
                     /db_xref="taxon:1706046"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33695
     Region          2..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msvkhsrlli lgsgpagyta avyaaranla pvmitgmqqg gqlttttevd nwpadvdgvq
       61 gpalmerfqk haerfnteii fdqihtaklt ekpytligda gtytcdalii atgasakylg
      121 lpseqafmgr gvsgcatcdg ffyknqdvav igggnsaiee alylsniakh vtlvhrrdtf
      181 kaekimvdkl veksktgnit leyfneldev lgdktgvtgi rikntkdgst kdialqgvfi
      241 aighspntgi fegqlemkng ylttqggsag natltsipgi faagdvqdhi yrqavtsagt
      301 gcmaaldaer ylddlgka
//
LOCUS       WP_124949255             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sulfuriferula thiophila].
ACCESSION   WP_124949255
VERSION     WP_124949255.1
KEYWORDS    RefSeq.
SOURCE      Sulfuriferula thiophila
  ORGANISM  Sulfuriferula thiophila
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sulfuricellaceae; Sulfuriferula.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Sulfuriferula thiophila"
                     /db_xref="taxon:1781211"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33929
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msetkhsrll ilgsgpagya aavyaaranl npvlitgmaq ggqlmtttev dnwpadvdgv
       61 qgpelmerfe kharrfntei ifdhihtakl tekpmtligd qgtytcdali iatgasamyl
      121 gleseqefmg kgvsgcatcd gffyrnqdva vigggntave ealylsniar hvtvvhrrdk
      181 fksekiladr lmekvaegki slelncelne vlgdktgvtg mrvksvvdgs tkdialtgvf
      241 iaighkpntd lftgqidmeg gyivthgghk gnatatnipg vfaagdvqdh iyrqaitsag
      301 tgcmaaldad ryleslvk
//
LOCUS       WP_124957310             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Variovorax beijingensis].
ACCESSION   WP_124957310
VERSION     WP_124957310.1
KEYWORDS    RefSeq.
SOURCE      Variovorax beijingensis
  ORGANISM  Variovorax beijingensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Variovorax beijingensis"
                     /db_xref="taxon:2496117"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34268
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msapqhakvl ilgsgpagyt aavyaaranl qpllitgiaq ggqlmtttev dnwpadvhgv
       61 qgpdlmqrfl ehaerfktqi vfdhinkvdl gkrpftltgd sgtytcdsli iatgasakyl
      121 gldseqkfmg rgvsacatcd gffyreqevc vigggntave ealylanian kvtlvhrrdk
      181 fraepilidk lmekvaegki vlklhneldq vlgddtgvtg irvkntqtga teqidlkgcf
      241 iaighhpntd ifqgqlemkd nyiltrsglq gfatmtsipg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq rfleqdgtl
//
LOCUS       WP_124958474             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            beijingensis].
ACCESSION   WP_124958474
VERSION     WP_124958474.1
KEYWORDS    RefSeq.
SOURCE      Variovorax beijingensis
  ORGANISM  Variovorax beijingensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax beijingensis"
                     /db_xref="taxon:2496117"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38524
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetm agetrvavtp etvkklaasg htvrvqsgag iaasvtdaay qaagaeitda
       61 tgafgadmvl kvrtptdaet almkpgtvvi gmlnpfdaag lqrlataglt afaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy arpmpaswla
      241 rqqvevakrv aladivista lipgraaptl itedmvkamk pgsvivdiaa gkgadgiggn
      301 cplseadktv vkhgvtivge tnlpalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvaqd gqvtkq
//
LOCUS       WP_124964528             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Falsigemmobacter faecalis].
ACCESSION   WP_124964528
VERSION     WP_124964528.1
KEYWORDS    RefSeq.
SOURCE      Falsigemmobacter faecalis
  ORGANISM  Falsigemmobacter faecalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Falsigemmobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Falsigemmobacter faecalis"
                     /db_xref="taxon:2488730"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55568
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkeif egenrvamtp dsalqlvklg htcviesgag akagfsdaty ekagvtvlpt
       61 aqavseaadv lvkvrgpeas evallrqgqt lisffwpaqn adlleavnar gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvyldfse tqidgaatgg yaapsspefr
      241 eaqlkkfrel apeidivitt alipgrpapk lwtedmvqmm kpgsvivdla aerggncdlt
      301 ipdekivten gvtivgytdf psrmaaqast lystnirhml tdltpkkdgv idhnmeddvi
      361 rgatvthega itfpppppki qaiaaqkpke kvkeltpeek rakeaaefka qtrtqftvlg
      421 vsaalllavg lvapasfmqh fivfvlacfv gfqiiwnvah slhtplmait naissiiilg
      481 almqigsgsw lvivlaglsv fmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_124965026             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Falsigemmobacter faecalis].
ACCESSION   WP_124965026
VERSION     WP_124965026.1
KEYWORDS    RefSeq.
SOURCE      Falsigemmobacter faecalis
  ORGANISM  Falsigemmobacter faecalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Falsigemmobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Falsigemmobacter faecalis"
                     /db_xref="taxon:2488730"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33284
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetrhtkvl iigsgpagyt aavyasraml spilvqgiqp ggqltittev enwpgdktvq
       61 gpdlmvrmee haqemgaeil fdtitelklg srpftalgds gttytadavi latgaqarwl
      121 glpteekfkg fgvsacatcd gffyrdkpva vigggntave ealfltnfas kvtlihrrds
      181 lraekilqer lfnhpkvevl wnhevdevlg teaplgvtgl rvkhaqtget seiacdgffv
      241 aighspasel vkdqlelhng gyvkvepgtt rtsipgvfaa gdltdhvyrq aitsagmgcm
      301 aaldaerfla gh
//
LOCUS       WP_124966835             305 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Falsigemmobacter faecalis].
ACCESSION   WP_124966835
VERSION     WP_124966835.1
KEYWORDS    RefSeq.
SOURCE      Falsigemmobacter faecalis
  ORGANISM  Falsigemmobacter faecalis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Falsigemmobacter.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Falsigemmobacter faecalis"
                     /db_xref="taxon:2488730"
     Protein         1..305
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34575
     Region          5..168
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
     Region          <225..304
                     /region_name="FlbT"
                     /note="Flagellar protein FlbT; cl11455"
                     /db_xref="CDD:472187"
ORIGIN      
        1 maivdifskr kmarersnnd vyiydempkt lrsqlkqmft egvnnysrss aayhsfriea
       61 dqiseivsil rreygvdhlc rvhynsnlie llnfinecsa dhfldcaemy grllsintet
      121 ndeilkahma elnhrfkeas vgyeyingel iridslvlhs evlkptltil ssnkiykgae
      181 deivqafqkf khndnkgavs dalkafestm kaildkrqwt yspndtaskl iaacfdnnli
      241 paymqthfsg lrtilesgvp tirnktsghg qgssvkpldd hfasyvlyta lanmkllidc
      301 ekvlp
//
LOCUS       WP_124972201             359 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gulosibacter macacae].
ACCESSION   WP_124972201
VERSION     WP_124972201.1
KEYWORDS    RefSeq.
SOURCE      Gulosibacter macacae
  ORGANISM  Gulosibacter macacae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Gulosibacter.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Gulosibacter macacae"
                     /db_xref="taxon:2488791"
     gene            1..359
                     /gene="trxB"
     Protein         1..359
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=37995
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrnvaiigsg pagytaaiyv araglkpvmf tsavtvggel mnttdvenfp gfpdgvmgpd
       61 lmqkmqeqae rfgtelvydd vesvdlsgei krirtsysge yealaviiat gsayrrlgle
      121 sedrlagrgi swcatcdgaf fkeqhiavvg ggdsameeat fltrfadrvt vihrsdnfra
      181 skimlerara npkidwvtnv tveeilgdqq vsgvrlrdtv tgderkldlt gifvaignvp
      241 rtelvagqid ltesgviave grssrtslpg vfacgdvvdd hyrqaitaag sgctaaldae
      301 aylaglpael lakvdeesap setpaespie vaaapelggi tlnpidfgnl glaglkken
//
LOCUS       WP_124975443             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aphanothece sacrum].
ACCESSION   WP_124975443
VERSION     WP_124975443.1
KEYWORDS    RefSeq.
SOURCE      Aphanothece sacrum
  ORGANISM  Aphanothece sacrum
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Aphanothecaceae; Aphanothece.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Aphanothece sacrum"
                     /db_xref="taxon:1122"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40860
     Region          2..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,76,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mikiavpkes elgelrvalv pdtvsrfvkl gfevlvqtga glgahftdad yelagatiis
       61 spsrlwgead lllkvgppgi qhgqpemnwl kagsvlisfl dplanperiq elaqrkital
      121 smeliprssr aqsmdalssq aniagykaal iaaaslprlf pmmttaagti ppakvlviga
      181 gvaglqaiat arrlgavvea fdvrpavkee vqsvgakfie ipieedtatn ggyakevgqs
      241 tqerirqvlt ehvkkadvvi ttaqvqgkra plivteemvg emklgsvivd maagqggnca
      301 ctepgkdvyy ngvtiigpln lpssvpidas qvyaknlltl vkylvkdgef nfnfeddiid
      361 stcvtyegei rhakvkqals tlvea
//
LOCUS       WP_124977673             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Ligilactobacillus salitolerans].
ACCESSION   WP_124977673
VERSION     WP_124977673.1
KEYWORDS    RefSeq.
SOURCE      Ligilactobacillus salitolerans
  ORGANISM  Ligilactobacillus salitolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Ligilactobacillus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Ligilactobacillus salitolerans"
                     /db_xref="taxon:1808352"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33683
     Region          5..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 makhydvivi gagpggmtaa lyasranlsv lmldrgiygg qlnntaaven ypgfksimgp
       61 dlaekmyqgs tqfdaeyayg svesvtvadd glktittdsd vyetqalvia tgseyrklgv
      121 pgedkyggrg vsycavcdga ffknkpvvvv gggdsaveeg gylsqltsqv niihrrdqlr
      181 aqkilqdraf andkigftwd tivteilgdd qkvtgvmthn kktgkdqevp vdgvfiyvgn
      241 qpmteaftdl gitdeagwiv tdekmqtnvp gifavgdvrq kdlrqittav gdggiagqea
      301 fnylqtlqdk vqtk
//
LOCUS       WP_124979972             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nonlabens xiamenensis].
ACCESSION   WP_124979972
VERSION     WP_124979972.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens xiamenensis
  ORGANISM  Nonlabens xiamenensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Nonlabens xiamenensis"
                     /db_xref="taxon:2341043"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35021
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msenierikc liigsgpagy taaiyaarad mkpvvytgme pggqltttte vdnfpgypeg
       61 idgpammvdl qkqaerfgtq vrigmvtevq faqekggiht aiidgktkve ahtviistga
      121 sakylglpse qrlrgggvsa cavcdgffyk nqdvaivgag dtaaeeatyl anicksvtml
      181 vrkdymrask amqhrvhgke nikvlfnsev devlgdtvve glrivnnetq ekheieitgl
      241 fiaighkpnt difkgqldmg gdgylktvpg ttktnlpgvf asgdvqdkiy rqavtaagtg
      301 cmaaldaery laelgvveem tagdyhve
//
LOCUS       WP_124986048             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Epilithonimonas vandammei].
ACCESSION   WP_124986048
VERSION     WP_124986048.1
KEYWORDS    RefSeq.
SOURCE      Epilithonimonas vandammei
  ORGANISM  Epilithonimonas vandammei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Epilithonimonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Epilithonimonas vandammei"
                     /db_xref="taxon:2487072"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34775
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mennildcvi igsgpagfta aiyaaraslk pelftglepg gqltttteve nfpgypdgit
       61 gpemmlqlqk qaerfetkvh yemiskvefs kerggihkls tgsreilaks viistgatak
      121 ylgladekky agggvsacat cdgffyrgkd vivvgagdta aeeatylski cnkvtllvrk
      181 dhfraskvmv drvlstsnie vkynheligi egenflvera kvvnnltdev stidvhgifi
      241 aighkpntei fkgqidlden eyiitegkss rtnlpgvfaa gdvqdhhyrq aitaagsgcm
      301 aamdaekylg elagenhtwv eq
//
LOCUS       WP_124988099             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_124988099
VERSION     WP_124988099.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33725
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evrlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_124991385             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Labilibaculum euxinicum].
ACCESSION   WP_124991385
VERSION     WP_124991385.1
KEYWORDS    RefSeq.
SOURCE      Labilibaculum euxinicum
  ORGANISM  Labilibaculum euxinicum
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Labilibaculum.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Labilibaculum euxinicum"
                     /db_xref="taxon:2686357"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34059
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknkenierv kcliigsgpa gytagiyasr anlnpvvyeg lqpggqlttt teidnfpgyp
       61 egvtgnvmmg elkkqaerfg cdcrwgivte vnlnerpfkl kvdgnkdiea dsviiatgat
      121 akylglesee kyrgsgvsac atcdgffyrg kdvavvgggd taceeasyla glcnkvyliv
      181 rkdflraska mqervfktan ieilfehttk eltgengveg ctliknagts speevkiaid
      241 gfflaighhp nsdvfsdyvd tdeqgyiltq agtpmtnikg vfacgdvqdp nyrqaitsaa
      301 sgcqaaieae rylaemn
//
LOCUS       WP_124999630             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium tamadayense].
ACCESSION   WP_124999630
VERSION     WP_124999630.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium tamadayense
  ORGANISM  Mesorhizobium tamadayense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mesorhizobium tamadayense"
                     /db_xref="taxon:425306"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43032
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlvg lgfevivekg aglgsripdl dfasaggaig
       61 aaadarkadv vlkvrrptda elkgyksgaa viaimdpygn daavaamaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaara fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 tqaaltaehi akqdivitta lipgrpapkl vsaamvasmr pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkaakel aikrddelvk
      361 atmltdggkv vhpnfanaae aprtepaaip atflvadaad kkptpkkksa akpkgtv
//
LOCUS       WP_124999663             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium tagluense].
ACCESSION   WP_124999663
VERSION     WP_124999663.1
KEYWORDS    RefSeq.
SOURCE      Clostridium tagluense
  ORGANISM  Clostridium tagluense
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Clostridium tagluense"
                     /db_xref="taxon:360422"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33685
     Region          5..285
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mehiydtiii gggpaglsag lyasrsrmdt liierakfgg qatttdeldn ypgsieectg
       61 ttlskrmkqq aeefgtqfvk eevveveleg dikvikckke tykaktiiia tgayprlggf
      121 kneielrgkg vsycatcdad fftdldiavl gggdsalsea iylakfgesv tvihrrdelr
      181 gakslqekaf knpkikfiwd tvvqeakgee ileglvlknv ktgelsdlkv dgcfvfvgyl
      241 piselfkgmi nmtergdvit deemrtnipg vyaagdirek llrqvitaaa dgaiaathae
      301 hyieekfn
//
LOCUS       WP_125001759             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_125001759
VERSION     WP_125001759.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33334
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd kpqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_125003656             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium tamadayense].
ACCESSION   WP_125003656
VERSION     WP_125003656.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium tamadayense
  ORGANISM  Mesorhizobium tamadayense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium tamadayense"
                     /db_xref="taxon:425306"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34502
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdvv ndiitevdin vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylanlak svtvihrrsd
      181 fraerilrer lfkkenvrvi wdtvvdeitg qpgkaplpps veglklrnvv tgdvsrlkvd
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_125012295             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium macacae].
ACCESSION   WP_125012295
VERSION     WP_125012295.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium macacae
  ORGANISM  Flavobacterium macacae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Flavobacterium macacae"
                     /db_xref="taxon:2488993"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33456
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekvkc liigsgpagy saaiyaarad mkpllytgme pggqltttte vdnfpgypeg
       61 idgptmmvql qqqaerfgte vrigmatsve fskekggihk vivdgkkqih aetviistga
      121 takylglpse qklrgggvsa cavcdgffyk nqdvaivgag dtaaeeatyl anicksvtml
      181 vrkdamrask amqhrventp nlkviyntev devlgdqvve glrmvnnvtg ekaeiaitgl
      241 fiaighkpnt difkgqldmd etgylitpgk stktnlpgvf aagdvqdkey rqaitaagtg
      301 cmaaldaery laale
//
LOCUS       WP_125012935             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium macacae].
ACCESSION   WP_125012935
VERSION     WP_125012935.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium macacae
  ORGANISM  Flavobacterium macacae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Flavobacterium macacae"
                     /db_xref="taxon:2488993"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33668
     Region          12..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqgsehvkc miigsgpagy taaiyaarad lepvlytglt tggqltqtte vdnypgypdg
       61 imgidmmenf rrqaerfgtd irngiitavd fsappykvtt dgqvtilcds viistgatak
      121 wlgleseqmy ngkgvsacat cdgfffkgqd vaivgagdta aeeathlakl crkvymlvrk
      181 gelkaskama hkieitpnie vlyhtettei lgngravtgv tiynnstnas glldvtglfv
      241 aighnpntgv fkdwiemdnn gyiltapkss rtnipgifcc gdaqdptyrq avtaagsgcm
      301 aaldcerfls giehgsk
//
LOCUS       WP_125015219             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aestuariirhabdus litorea].
ACCESSION   WP_125015219
VERSION     WP_125015219.1
KEYWORDS    RefSeq.
SOURCE      Aestuariirhabdus litorea
  ORGANISM  Aestuariirhabdus litorea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Aestuariirhabdaceae; Aestuariirhabdus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Aestuariirhabdus litorea"
                     /db_xref="taxon:2528527"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33762
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtkharli ilgagpagyt aavyaaranl npvlitgiqp ggqlttttei dnwpsgaegl
       61 qgpelmermr ehaerfdtei vydhinqadl serpfklkgd sgeyscdali iatgatalyl
      121 glpseeafmg kgvsacatcd gffyknqkva vvgggntave ealylanias evtlihrrdk
      181 lrcekilqdk lfekaengnv rlqwnhtlee vlgdasgvtg arikhtesge tkdldvagif
      241 iaighkpntd lfagqlemkd gflkvisgte gnatqtnipg ifaagdvadh iyrqaitsag
      301 tgcmaaldae rfldee
//
LOCUS       WP_125016852             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenimyroides tangerinum].
ACCESSION   WP_125016852
VERSION     WP_125016852.1
KEYWORDS    RefSeq.
SOURCE      Paenimyroides tangerinum
  ORGANISM  Paenimyroides tangerinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Paenimyroides.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Paenimyroides tangerinum"
                     /db_xref="taxon:2488728"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33683
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqnienikc liigsgpagy taaiyaaran mnpvmyqgmq pggqltttne venfpgypeg
       61 vtgpemmnql qaqakrfgtd vrdgwatkvd lsgdvkkvwi ndtieihaqt viistgatak
      121 ylglpseqhy lqmgggvsac avcdgffyrk qdviivgagd saceeahyls hlcnkvtmlv
      181 rsekfraski meervrntan ieilmsseid evlgdgqlvs gvrvvnrvtg ekheiaatgv
      241 fvaighkpnt difagqlnmd etgylitegk tsktnipgvf acgdvqdkdy rqaitaagsg
      301 ciaaldaery lask
//
LOCUS       WP_125015601             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aestuariirhabdus litorea].
ACCESSION   WP_125015601
VERSION     WP_125015601.1
KEYWORDS    RefSeq.
SOURCE      Aestuariirhabdus litorea
  ORGANISM  Aestuariirhabdus litorea
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Aestuariirhabdaceae; Aestuariirhabdus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Aestuariirhabdus litorea"
                     /db_xref="taxon:2528527"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39998
     Region          3..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavsvavpke ikegerrvai vpevalrlqq lgaelvletd vgvsaghada lysdakfykq
       61 rkkvfeaaev llkvlpptpe evalmkpgti cvgfmapyan degilamker gitafsmeli
      121 prisraqsmd altsqaslag ykavlmaasi sgkffpmltt aagtirpskv lvvgagvagl
      181 qaiatarrlg aiveaydvrs aareqveslg arfvdtgvsa dglggyarel tdeekkrqqe
      241 vlaarvaasd vvittaaipg rpspriiste mvesmhacsv ivdmaaeggg nceltrageq
      301 vehngvtvyg plnvpsmlai hasemfaknl lnfckllire gelsidwedq vladsclthd
      361 geirfaaare rleggks
//
LOCUS       WP_125021927             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Kaistella carnis].
ACCESSION   WP_125021927
VERSION     WP_125021927.1
KEYWORDS    RefSeq.
SOURCE      Kaistella carnis
  ORGANISM  Kaistella carnis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group; Kaistella.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Kaistella carnis"
                     /db_xref="taxon:1241979"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33652
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meenildcvi igsgpagfta aiyaaradlk pelftglepg gqlttttevd nfpgypsgit
       61 gpemmmdlqk qaerfetkvh yemitkaefs tevggvhklw agnreilart viistgatak
      121 ylglddekky mgggvsacat cdgffykgkd vivvgagdta aeeatylakl vnkvtmlvrk
      181 dymraskaml hrvsntpnie vkfnheligi egennlverg vvinnltqek stidvhgifi
      241 aighkpntei fkgqidlden gyintipgts ktnlpgvfav gdvqdshyrq aitaagsgcm
      301 gamdaekylg elv
//
LOCUS       WP_125024088             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas sp. SCT].
ACCESSION   WP_125024088
VERSION     WP_125024088.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. SCT
  ORGANISM  Pseudomonas sp. SCT
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas sp. SCT"
                     /db_xref="taxon:412955"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33659
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kplmitgiqp ggqlttttev dnwpgdvegl
       61 tgpdlmvrmq khaerfdtei vfdhihtael qqrpftlrgd savytcdali iatgasaqyl
      121 glpseeafag rgvsacatcd gffyrnqvva vigggntave ealylsniak evhlihrrdk
      181 lrsekilqdk lmdkatngni rlhwnhtlee vlgdasgvtg vrlkstltge enrldlagvf
      241 iaighkpntd lfqgqldmkd gylkirggge gdatctsipg vfaagdvadh vyrqaitsag
      301 agcmaaldae kyldn
//
LOCUS       WP_125023860             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. SCT].
ACCESSION   WP_125023860
VERSION     WP_125023860.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. SCT
  ORGANISM  Pseudomonas sp. SCT
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. SCT"
                     /db_xref="taxon:412955"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38773
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkligqg hrvtlqsgag llssvpdsay eavgatigda
       61 aaafaaelvl kvnapddael aqmqsgsvll gmlnpfdnac iarmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vlvgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhera lqsdivitta lipgrnaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvpadasaly arnlldflkl vtdkdgqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_125032121             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ancylomarina euxina].
ACCESSION   WP_125032121
VERSION     WP_125032121.1
KEYWORDS    RefSeq.
SOURCE      Ancylomarina euxina
  ORGANISM  Ancylomarina euxina
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Ancylomarina.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Ancylomarina euxina"
                     /db_xref="taxon:2283627"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40481
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milgllkeqg aeqrvallpe ivsklvqakv evyvekgagt kafqtdeayr nagakifsrd
       61 ellkkadlfv qigepsieii qslsdkqvwl sqynplwntd lvksflanni tsfsmdsipr
      121 ttraqamdvl ssmatvagyk avlqaanelp nffpmfmtaa gtirpatvli lgagvaglqs
      181 iaiarklgaq veafdvraav keevnslgak fvevegaidd saaggyaveq teefkkkqqe
      241 vindhaakad vvictaqipg rkapllipte avermrpgsv iidlaassgg nceltknset
      301 viynevkiig qseypslmpi daskmfgknv fnflqlliae dgslnlnfed divkgtcith
      361 sgeiynervk svves
//
LOCUS       WP_125030803             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Ancylomarina euxina].
ACCESSION   WP_125030803
VERSION     WP_125030803.1
KEYWORDS    RefSeq.
SOURCE      Ancylomarina euxina
  ORGANISM  Ancylomarina euxina
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia;
            Marinilabiliales; Marinifilaceae; Ancylomarina.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Ancylomarina euxina"
                     /db_xref="taxon:2283627"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35526
     Region          25..331
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdlfkpmnle ekkstapegd iervkclivg sgpagytaai yaaranlspv lieglqpggq
       61 ltttteidnf pgyadgvtgt emmadlkkqa qrfgtdcrwg vvtsvdfssy phkvvvdgnk
      121 tieaesvilg tgatakylgi esetkyagsg vsacatcdgf fyrgmdvavv gggdtaaeea
      181 tylaglcnkv ylivrkpflr askamqdrve rtdnievlye hntkeitgdg vvqgatlikr
      241 lgeeneeevk ikidgfflai ghtpnsdffk qyiktdehgy vitepdstrt nvpgvfacgd
      301 lkdsvyrqav tsagsgcmaa mdaekflaeh e
//
LOCUS       WP_125035202             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides sp. LS1].
ACCESSION   WP_125035202
VERSION     WP_125035202.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. LS1
  ORGANISM  Nocardioides sp. LS1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Nocardioides sp. LS1"
                     /db_xref="taxon:1027620"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52674
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipresk pgetlvaata ktatqltklg ydvivesgag daadqsdamf ldagvrvgtv
       61 mevwaadvvv kvnapseeev rrlrqgativ smmaparspq llerlqaqgv ialamdavpr
      121 israqsmdvl ssmanvagyr avveaahefg rmftgqvtaa gkvpparvfv vgagvaglaa
      181 igaasamgav vrgfdvrpev aeqvesmgah fvkvdfeaev stdgyaremt aeqeaataam
      241 ydeearqadi vittalvpgr aapqlitaet iagmgkgsvi vdmaaanggn aamtqpderi
      301 vtdngvtilg ytdlasrlaa qtsqlygtnv vnllklmtpe qdgqltidvd dvvqrsitvv
      361 regeltwppp avnvsaapaa ttaakngsvk eekppisagr rlglvalaaa alfglialsp
      421 qglqghlvvf alaivigyyv ignvhhalht plmsvtnais giivvgaliq igegstpitv
      481 laaiatllas inifggfavt rrmlgmfsrs
//
LOCUS       WP_125037092             336 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nocardioides sp. LS1].
ACCESSION   WP_125037092
VERSION     WP_125037092.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. LS1
  ORGANISM  Nocardioides sp. LS1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Nocardioides sp. LS1"
                     /db_xref="taxon:1027620"
     gene            1..336
                     /gene="trxB"
     Protein         1..336
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35673
     Region          11..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpesqsdtrn viiigsgpsg ytaavyaara nlhplvfegs vtaggalmnt tevenfpgfr
       61 dgimgpalmd emraqaerfg aelvaddvve vdltgdvkvv ktatdtytar avvlatgsgy
      121 rklglpreee lsgrgvswca tcdgfffreq hiavvgggds aveeatflsr fgskvslivr
      181 rdelraskim qerafadpki dilwnsavdq ingedrlesl tlkdtvtget reldatglfi
      241 avghdprsel lvgqvdlddn gyvlvdqpst rtnlagvfaa gdlvdhhyrq aitaagtgca
      301 aaldaeryla dldhaastrd agtaevltet vqtagl
//
LOCUS       WP_125036883             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides sp. LS1].
ACCESSION   WP_125036883
VERSION     WP_125036883.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. LS1
  ORGANISM  Nocardioides sp. LS1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Nocardioides sp. LS1"
                     /db_xref="taxon:1027620"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39643
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,275..276,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,225,236,
                     253..255,262,264)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavaretr dgesrvamvp elvgkltalg ydvavepgag qpaliadddy eqagatveeg
       61 alhgadlvvs vqplstatir tlpagtatis flptnqepdt vrdlrdcgvt afamelvpri
      121 sraqsmdals sqalvagyrc aivaagmlrr ffplnmtaag tvppaeivvl gagvaglqai
      181 atakrlgavv saydvraaaa eeirsmgaka ieleletleg aggyaremte draarqrell
      241 tpyianadal ittaavpgrq apmlvtaemv eqmkpgsvvv dlaaetggnv egsvpgevvr
      301 ignaqvwggr nvpsqmpgpa srlyaqnvvn lvtlmtrtas eeqdaafapd fedeivagsc
      361 vthdgtirhe ptrlniegap e
//
LOCUS       WP_125038032             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides sp. LS1].
ACCESSION   WP_125038032
VERSION     WP_125038032.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides sp. LS1
  ORGANISM  Nocardioides sp. LS1
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Nocardioides sp. LS1"
                     /db_xref="taxon:1027620"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52133
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipqesk agemlvaatg atvgllrklg yevvveagag aasdqpdevy aaaearvgga
       61 eevwssdvvv kvnaptpeei grlrrgavvv smmaparspe lvealvaagv talamdavpr
      121 israqsmdvl ssmanvagyr avvegayafg rqftgqvtaa gkvpparvfv vgagvaglaa
      181 lgaagsmgai vrafdvrpev aeqvesmgaq fvtvdmesev ssdgyakemt aeqvaataam
      241 ydeeargadi vittalipgr papklitagt iaamrtgsvi idmaaanggn teltrtdevv
      301 vtdngvtiig ytdlagrlpa qtsqlygtni vnllklmtpe kdgvlaldld dvvvrgitva
      361 hegasmwppp avkvsaapap vaaaepvvpk pppdprrtvy aagiaavlfi lvatfsppef
      421 lghftvfvla vfvgyyvisn vahalhtplm setnaisgii lvggilqvgs tnpaiaimat
      481 lavlvasini fggflvtlrm lqmfrkd
//
LOCUS       WP_125046035             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces chrestomyceticus].
ACCESSION   WP_125046035
VERSION     WP_125046035.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces chrestomyceticus
  ORGANISM  Streptomyces chrestomyceticus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces chrestomyceticus"
                     /db_xref="taxon:68185"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34407
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmra qaerfgaelv pddvvavdlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpredelsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtiihrrdt
      181 lraskamqer afadpkisfv wdsevaelhg enklsgltlr nlktgetses pvtglfiaig
      241 hdprtelfkg qlelddegyl qveapstrtn itgvfaagdv vdhtyrqait aagtgcsaal
      301 daerhlaals dsedvpepek tasa
//
LOCUS       WP_125040490             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bacteroides faecalis].
ACCESSION   WP_125040490
VERSION     WP_125040490.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides faecalis
  ORGANISM  Bacteroides faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Bacteroides faecalis"
                     /db_xref="taxon:2447885"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33827
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 metekvkcli igsgpagyta aiyagranlc pvlyeglqpg gqlttttdve nfpgypegis
       61 gpqlmedlrn qasrfgtdvr fgiataadls kapykitidg ekvietesli istgatakyl
      121 glddekkyag mgvsacatcd gffyrkkvva vvgggdtace eaiylaglas kvylivrkpy
      181 lraskimqer vmkhekievl yehnavglfg dngvegvnlv krwgepdeeh yslpidgffl
      241 aighkpnsdi fkdyidtdev gyiitegnsp rtkvpgvfaa gdvadphyrq aitaagsgck
      301 aaieaeryls ekgii
//
LOCUS       WP_125055285             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_125055285
VERSION     WP_125055285.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34434
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmra qaerfgaelv pddvvavdlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpredelsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtiihrrdt
      181 lraskamqer afadpkinfv wdsevaelhg enklsgltlr nlktgetses pvtglfiaig
      241 hdprtelfkg qlelddegyl qveapstrtn itgvfaagdv vdhtyrqait aagtgcsaal
      301 daerhlaals dsedvpepek tasa
//
LOCUS       WP_125060116             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia albertii].
ACCESSION   WP_125060116
VERSION     WP_125060116.1
KEYWORDS    RefSeq.
SOURCE      Escherichia albertii
  ORGANISM  Escherichia albertii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia albertii"
                     /db_xref="taxon:208962"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53606
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtriktnarr ffsllipfff ftsvhaeqta spakpvtvea knetfapqhp dqylswkats
       61 elservdala edprlvilwa gypfsrdynk prghayaitd vretlrtgap knaedgtmpm
      121 acwsckspdv arliqkeged gyfhgkwarg gpesvnnlgc adchntaspe fakgkpeltl
      181 srpyaeramn aigkpfekgg rfdqqsmvcg qchveyyfdg kdkavkfpwd ngmkvenmeq
      241 yydkiafsdw tnalsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkatlqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gataaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_125070467             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lactiplantibacillus garii].
ACCESSION   WP_125070467
VERSION     WP_125070467.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus garii
  ORGANISM  Lactiplantibacillus garii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Lactiplantibacillus garii"
                     /db_xref="taxon:2306423"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33172
     Region          5..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maksydviii gagpagmtaa lyasranlsv llldrgiygg qmnntaaien ypgfksvlgp
       61 dlakdmydsa tqfgaeyayg svesvedqga vkvvktdsdt fetkaivigt gseyrklgvp
      121 gedtyggrgv sycavcdgaf fknkhvvvig ggdsaieegs yltqlaskvt vihrrdqlra
      181 qqilqdrafa npkmefvwns nvteivgddk kvtavkvnnn ktgedseiav dgvfiyvgin
      241 pitkpfgnlg itdengwiit ndhmetkvpg ifavgdvrkk dlrqvatavg eggtagqgvy
      301 nyitalgdqv kn
//
LOCUS       WP_125066900             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tenacibaculum singaporense].
ACCESSION   WP_125066900
VERSION     WP_125066900.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum singaporense
  ORGANISM  Tenacibaculum singaporense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Tenacibaculum singaporense"
                     /db_xref="taxon:2358479"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33214
     Region          6..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maekikclii gsgpagytaa iyaaradmkp vmytgmqmgg qlttttevdn fpgypkgtdg
       61 tammedlksq aerfgtdvrf gmvtkvelsk eeggihkvtv desteieaqt iiistgatak
      121 ylgleseqrl igggvsacat cdgffykgqd vvvvgagdta aeeatylani cskvtmlvrk
      181 dymraskamq hrvnktenit vmynteidev lgenvvegvr avnnqtgekt eipvtgvfia
      241 ighkpnsdlf kgvldmddtg ylitkgkstk tnlpgvfaag diqdkeyrqa vtaagtgcma
      301 aldaerylga le
//
LOCUS       WP_125073678             307 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus canis].
ACCESSION   WP_125073678
VERSION     WP_125073678.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus canis
  ORGANISM  Streptococcus canis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Streptococcus canis"
                     /db_xref="taxon:1329"
     gene            1..307
                     /gene="trxB"
     Protein         1..307
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33526
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigsg pagmtaalya arsnlrvgii eqgapggqmn ntsdienypg ydhisgpels
       61 lkmyeplekf kveniygivq kiedfgsykr vstedesyda ktiilatgak yrvlgvpgee
      121 eytsrgvsyc avcdgaffrn qdllvvgggd saveeaiylt qfakkvtvvh rrdqlraqki
      181 lqdrafandk vdfiwdsvvk eiqgndikvs nvlvenvktg tvtdhafggv fiyvgmipvt
      241 smvselgitd qegwiitddy mrtsipgifa igdvrqkdlr qittavgdga iagqgvyhyi
      301 enmpses
//
LOCUS       WP_125077904             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_125077904
VERSION     WP_125077904.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53531
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knnavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_125081562             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus lentus].
ACCESSION   WP_125081562
VERSION     WP_125081562.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus lentus
  ORGANISM  Paenibacillus lentus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Paenibacillus lentus"
                     /db_xref="taxon:1338368"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34101
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mykaivigtg pagltaaiyl aranlnplvi egmepggqlt tttevenfpg fpqgimgpel
       61 mdqmrkqaer fgakfrsgwv qevdfgtrpf kltleggeal esetviistg asakylgipg
      121 ekenvgrgvs tcatcdgfff rgkkiivigg gdsameeasf ltrfaasvtv vhrrdelras
      181 kimqdrargn ekvewalnrt pievstdeqg avtglkvrnn atqeeelipa dgifiaight
      241 pntkflggqi vtdehgyiiv qpgttmtnve gvfacgdvqd tryrqaitaa gsgcmaaldc
      301 ekllegamvr dwsetlnp
//
LOCUS       WP_125082216             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus lentus].
ACCESSION   WP_125082216
VERSION     WP_125082216.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus lentus
  ORGANISM  Paenibacillus lentus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paenibacillus lentus"
                     /db_xref="taxon:1338368"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33756
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksiiigtg pagltaaiyl aranlnplvi egpqpggqlt tttdvenfpg fpdgilgpel
       61 mdnmrkqaer fgaefrtgwv nsvdlsnrpf klqveglgel vsetlvistg atakylgipg
      121 eqdnvgrgvs tcatcdgfff rgkeiivigg gdsaleeagf ltrfaskvtl vhrrdelrgs
      181 kimqdrvran ekvewalnrt plevltnemg vtglkvrnna tgeeeiieas gvfvaighhp
      241 ntaflggqid tdengyivvk pgttetnvpg vfacgdvqdt ryrqavtaag sgcmaaldce
      301 kfiesiehea etttvk
//
LOCUS       WP_125092561             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Saccharopolyspora rhizosphaerae].
ACCESSION   WP_125092561
VERSION     WP_125092561.1
KEYWORDS    RefSeq.
SOURCE      Saccharopolyspora rhizosphaerae
  ORGANISM  Saccharopolyspora rhizosphaerae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Saccharopolyspora.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Saccharopolyspora rhizosphaerae"
                     /db_xref="taxon:2492662"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34673
     Region          8..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtsdvrnvii vgsgpagyta avyaaraele pvifegtqfg galmtttdve nypgfkdgim
       61 gpdlmeqmrs qaerfgaelr tedveridls gdvktvvang vehkaravil amgaaaryld
      121 vpgeeallgr gvsacatcdg fffrdqdiav vgggdsamee atfltrfaks vtiihrreef
      181 raskimlera randkikwlt nktvaevqge gkvsglklrd tvtgetsdla vtgmfvaigh
      241 dprsqlvrdq vtlddegyvq vqhptthtgv pgvfacgdlv dhiyrqavta agsgcsaaid
      301 aerwlaehet pqaevaselv gggygg
//
LOCUS       WP_125085824             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesohalobacter salilacus].
ACCESSION   WP_125085824
VERSION     WP_125085824.1
KEYWORDS    RefSeq.
SOURCE      Mesohalobacter salilacus
  ORGANISM  Mesohalobacter salilacus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Mesohalobacter.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Mesohalobacter salilacus"
                     /db_xref="taxon:2491711"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35200
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdnqverikc liigsgpagy taaiyaarad lkpvlytgme pggqlttttd vdnfpgypdg
       61 idgptmmeql kaqaerfdtd vrigmatkte lskekggihk vqidnnkwie aesiiistga
      121 sakylnipse qrlrgggvsa cavcdgffyk nqdvaivggg dtaaeeatyl akicksvtml
      181 vrrdvlrask amqhrvfntk nidvrfntev devlgeqvve glrmvnnetq ekedikitgl
      241 fiaighkpnt difkgqlnmd dvgyiitesk stktnypgvf asgdaqdkey rqavtaagtg
      301 cmaaldaery lasvesvdel veeak
//
LOCUS       WP_125094261             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Lautropia
            dentalis].
ACCESSION   WP_125094261
VERSION     WP_125094261.1
KEYWORDS    RefSeq.
SOURCE      Lautropia dentalis
  ORGANISM  Lautropia dentalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Lautropia.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Lautropia dentalis"
                     /db_xref="taxon:2490857"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39379
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipkerr pgetrvaatp etvrklvkag hevvvereag vasdipdtaw eeagaqlvdt
       61 agafgaelva kvrspmeeel khlkagtall gmlnpfhaeg leklaatgvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaanlyqr ffpmmmtaag takaarvvil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyetdee reaaagvggy arpmpaswlq
      241 rqaaavaeri rqadvvitta lipgrkapvl vtramvesmk pgsvivdmav eqggncelsq
      301 adkvvrhhgv siagvgnlpa lvpadasafy arnildflkl ivddekklki nleddivkac
      361 lvtqdgkvlr eqk
//
LOCUS       WP_125094840             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lautropia dentalis].
ACCESSION   WP_125094840
VERSION     WP_125094840.1
KEYWORDS    RefSeq.
SOURCE      Lautropia dentalis
  ORGANISM  Lautropia dentalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Lautropia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Lautropia dentalis"
                     /db_xref="taxon:2490857"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33963
     Region          9..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mstprhtrll ilgsgpagyt aaiyaaranl kpllvtgliq ggqlttttev dnwpadvngv
       61 qgpelmerfr ahaerfqtni vfdhinavdl sqrpfrltgd sgtytcdali iatgasaryl
      121 glpseeafag kgvsacatcd gffyrnqdva vigggntave ealylsniar kvtvvhrrdk
      181 lraepimidh lmekvqegkv emrwnselde vlgdqsgvtg mrvrnretge kqdvklsgvf
      241 iaightpnte lftgqvdmng gyirtqgggn gnatatsipg vfaagdvqdh iyrqaitsaa
      301 sgcmaaldaq rylenqa
//
LOCUS       WP_125100140             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Leucobacter chromiireducens].
ACCESSION   WP_125100140
VERSION     WP_125100140.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter chromiireducens
  ORGANISM  Leucobacter chromiireducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Leucobacter chromiireducens"
                     /db_xref="taxon:283877"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33781
     Region          4..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mqqiiiigsg pagftaaiya araglkpllf asaigiggel mnttevenfp gfpegiqgpe
       61 lmqrmqeqae kfgtevvydd itevdfsgdv krvtagdgsv healtviyat gsayrkigla
      121 deerlsghgv swcatcdgff frektiavvg ggdsameeat fltrfaekvy vihrrnelka
      181 skimqqrafd nekiefiwds evtaihgeae vegvtlrstv dgserelplq glfvaigndp
      241 rthlvhgkld lteegtiave grssrtsapg vfaagdvtdp hyrqaitaaa sgtiaaldae
      301 aflalheqkn aelaav
//
LOCUS       WP_125100229             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Leucobacter chromiireducens].
ACCESSION   WP_125100229
VERSION     WP_125100229.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter chromiireducens
  ORGANISM  Leucobacter chromiireducens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Leucobacter chromiireducens"
                     /db_xref="taxon:283877"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33955
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msnqevelvi vgsgpagyta avyaaragla pvviagsvta ggalmtttev enfpgfvdgv
       61 qgpelmesmr vqaerfgaei vyddatrldl dgdvktietg agvtyrarav iltmgsayrn
      121 lglpeeerls ghgvswcatc dgfffreqgi vvvgggdsam eealfltrfa skvtvvhrrd
      181 efrasrimaq rvlddpkiev awnsevaail ggeqvtgltl rdtitgaert ldatgvfvai
      241 ghdprselvt gqvdtdadgy vrvahpstrt nlagvfaagd lvdhtyrqai taagtgcaaa
      301 qdaqhylsnl apttvsapvl evsa
//
LOCUS       WP_125106551             325 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Gulosibacter].
ACCESSION   WP_125106551
VERSION     WP_125106551.1
KEYWORDS    RefSeq.
SOURCE      Gulosibacter
  ORGANISM  Gulosibacter
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Gulosibacter"
                     /db_xref="taxon:256818"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34805
     Region          6..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstrnvaiig sgpagytaai yvaraglkpi mftsavevgg elmnttdven fpgfpegimg
       61 pdlmtklqqq aerfgtelvy ddvtevdldg dikhiktays gdfealtvif stgsayrrlg
      121 lesedrlagr giswcatcdg affkeqhiav igggdsamee atfltrfadr vtiihrsdnf
      181 rasnimlera rqnekidwlp fktveefvge qtvsglklrd tqtgeeslfd vtgvfvaign
      241 dprtdlvkgk leltdkgvia vdgrssrtsv pgvfaagdvi ddhyrqaita agsgctaald
      301 aeayiaglpa ellarveaep aeatn
//
LOCUS       WP_125120657             301 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Intestinibaculum porci].
ACCESSION   WP_125120657
VERSION     WP_125120657.1
KEYWORDS    RefSeq.
SOURCE      Intestinibaculum porci
  ORGANISM  Intestinibaculum porci
            Bacteria; Bacillati; Bacillota; Erysipelotrichia;
            Erysipelotrichales; Erysipelotrichaceae; Intestinibaculum.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Intestinibaculum porci"
                     /db_xref="taxon:2487118"
     gene            1..301
                     /gene="trxB"
     Protein         1..301
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=31635
     Region          3..301
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldlaiigag pagltaalya sragasvtvi eagapggkln ltadienypg iksmqgpqla
       61 yqmyehglsf gaslemrevt gledhgdykv vktstgdiea knviiasgtk erkmnvpgee
      121 eltghgvsyc avcdgpffkg kevavvgggn saieeavyls tiastvhvvm rrdvfradki
      181 isdkalaadn ivfhfkkkph avlsedgkvs glevsdsddg slsvinvsav fpfvgndpvt
      241 gfakdlgild ergyvltdeh metkvkgifa igdvrqkdlr qvvtatndga iagqyiansl
      301 r
//
LOCUS       WP_125130911             306 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Schaedlerella arabinosiphila].
ACCESSION   WP_125130911
VERSION     WP_125130911.1
KEYWORDS    RefSeq.
SOURCE      Schaedlerella arabinosiphila
  ORGANISM  Schaedlerella arabinosiphila
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Lachnospiraceae; Schaedlerella.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Schaedlerella arabinosiphila"
                     /db_xref="taxon:2044587"
     gene            1..306
                     /gene="trxB"
     Protein         1..306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32312
     Region          12..283
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydigiiggg tagmtaaiyg qragkrtvii eamnyggqit vspkvenypg iasvsgaefs
       61 mnlldqamkl gaeteleqvt gireedgikv ietegkeypc rtviiatgvt hrhlgldree
      121 allgagvsyc atcdgaffkg kdvavigggn talqdaefls nycnkvylvh rrdefrgeag
      181 lveplkrken vefvlsatvk elvgetvveg lilnnkktge dfqisvsgvf aaigqvpenh
      241 afaglvrlde sgfvaasedc vtscpgifaa gdcrtkevrq lttaaadgav aalaackyis
      301 rqeiae
//
LOCUS       WP_125135382             485 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Bibersteinia trehalosi].
ACCESSION   WP_125135382
VERSION     WP_125135382.1
KEYWORDS    RefSeq.
SOURCE      Bibersteinia trehalosi
  ORGANISM  Bibersteinia trehalosi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Bibersteinia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Bibersteinia trehalosi"
                     /db_xref="taxon:47735"
     gene            1..485
                     /gene="nrfA"
     Protein         1..485
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=54259
     Region          4..483
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mervnkvlks glafaamlsf wqtsiaapqp telegakpdl kiesanhkfa ekyplqynsw
       61 katsestard smleedprlv vlwggyafsk dynkprghfy aiadvreilr tgapknendg
      121 pmpmacwtck gpdvarmiae kgedgyfnek wakygaemvn aigcadchdt sskefeegka
      181 alniarphvl raleaigwkf edldkhgqra svcanchvey yfrgdkkvvt fpwdkgidvd
      241 smekyydeiq ftdwthslsk apmlkaqhpd fetwamdthg qngvtcidch mpkvetkdgk
      301 vytdhkignp fdnfehtckt cheqsketlq arvkdskkqi kdamlkledq lvkahfeaka
      361 awdagaaede mkqaltairh aqwrwdmsaa ghgghmhapk vvlhmiatgm draadaraal
      421 agvlvkhgve tpvqvpdist kekaqkvmgi dfdgekaakd eflrtvvpqw eaeakkkgll
      481 padnq
//
LOCUS       WP_125133237             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium sp. 10M-3C3].
ACCESSION   WP_125133237
VERSION     WP_125133237.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. 10M-3C3
  ORGANISM  Microbacterium sp. 10M-3C3
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Microbacterium sp. 10M-3C3"
                     /db_xref="taxon:2483401"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34754
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrhviiigsg pagytaaiya aranleplvi assveaggel mnttevenfp gfpegiqgpe
       61 lmdkmqqqae kfgaevlydd vvgleldgpv kkvtlgsgat heaesivfat gsaprkigie
      121 gesrlsgrgv sycatcdgff frertiavvg ggdsameeat fltkfaskvy vihrreelra
      181 skimqerafk ndkiefvwns evvdilgdea vtgvrlrntv dgseselald gifvaigydp
      241 rthlvhgald ltsegtvwvd grtsrtsvpg vfaagdvidp tyrqavtaag sgtvaaldve
      301 hylaalgdag apapdaaeid glpdatsvsv a
//
LOCUS       WP_125136744             306 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Petrocella atlantisensis].
ACCESSION   WP_125136744
VERSION     WP_125136744.1
KEYWORDS    RefSeq.
SOURCE      Petrocella atlantisensis
  ORGANISM  Petrocella atlantisensis
            Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
            Vallitaleaceae; Petrocella.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Petrocella atlantisensis"
                     /db_xref="taxon:2173034"
     gene            1..306
                     /gene="trxB"
     Protein         1..306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33165
     Region          22..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 menvldliiv gagpagiaaa iyasraklsf vilekaftgg qivntyeien ypgikatsgf
       61 elsnmfreha etldveflse evseiitdgp ikkvitndgt yeartiilat gaswkklgak
      121 gedkfsgmgv sycatcdgaf yrdkvtavvg ggdvavedai ylsrlckkvy lihrrdelra
      181 vkvlqehlfk ienieiiwds evaeiigdqm vekihvknrl tdeeqmievs gvfiavgsdp
      241 nsglvldqve tdlkgwiktn edcatsvpgv faagdlrvks lrqvitaasd gaisvyaaer
      301 ylvtns
//
LOCUS       WP_125143785             306 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium transplantifaecale].
ACCESSION   WP_125143785
VERSION     WP_125143785.1
KEYWORDS    RefSeq.
SOURCE      Clostridium transplantifaecale
  ORGANISM  Clostridium transplantifaecale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Clostridium transplantifaecale"
                     /db_xref="taxon:2479838"
     gene            1..306
                     /gene="trxB"
     Protein         1..306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32635
     Region          5..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdkihdliii gsgpaglsaa vyaqraeldt vviernmmsg gqilntyevd nypglpgisg
       61 fdlgmklreh adklgaefke dtvmaaelgg dvkkivcend tylaktviia tgahhrklga
      121 kgeeiltgag vsycatcdga ffknkvtavi gggdvaleda iflarmcskv ylihrrdelr
      181 garslqnrll sldnveviwd tvvdeieged kveslmlink ktgeksglkv dgvfiavgie
      241 pdseqysgqv emdqhgyiva gedgktsvdg vyaagdvrtk alrqvitaaa dgancitsaq
      301 syltmi
//
LOCUS       WP_125144534             302 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium transplantifaecale].
ACCESSION   WP_125144534
VERSION     WP_125144534.1
KEYWORDS    RefSeq.
SOURCE      Clostridium transplantifaecale
  ORGANISM  Clostridium transplantifaecale
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Clostridium transplantifaecale"
                     /db_xref="taxon:2479838"
     gene            1..302
                     /gene="trxB"
     Protein         1..302
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32066
     Region          5..301
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkqsydvavi gggpggytaa lycarsgysv ivleklspgg qmattgqvdn ypgfdegidg
       61 felgekmqkg aerfgvetaf vnvtevkldg dvkkittskg eiearavvla tgasprelgl
      121 aeekmlrgrg vaycatcdgm mykgktvvvv gggnsaaada lylskickkv ylvhrrdslr
      181 askiyleplk nsgiefvwns rvteilhdkk vsgvivtnnd gtvkeiacdg vfaaigrvpd
      241 tslfkgqvem dkqgylaade ttrtnlpgvf avgdartkpl rqivtaaadg avashyieey
      301 lv
//
LOCUS       WP_125149592             311 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Clostridium].
ACCESSION   WP_125149592
VERSION     WP_125149592.1
KEYWORDS    RefSeq.
SOURCE      Clostridium
  ORGANISM  Clostridium
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Clostridium"
                     /db_xref="taxon:1485"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34038
     Region          9..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdkeikeldl iiigggpagl taaiyagrak lntllledkv lggqvrnsyt ienypgfksi
       61 qgselsdilq sqaeesgaii defdliedii lsddekivet esfiykpkai iiatgaspkk
      121 lpipqeskfs gngvhycavc dgalyegkki avvgggnsal eeaifltrfa ekvylirrhd
      181 yfkgektkie aifnhpkiev mlnegiiglq gdgklegiel kntktnqitn iamdavfayi
      241 gtepktdlik kyinlneygy vitdenmqtn ikgvyaagdv rekefrqitt avadgtiall
      301 saekyivdke k
//
LOCUS       WP_125155647             335 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Caulobacter sp. 602-1].
ACCESSION   WP_125155647
VERSION     WP_125155647.1
KEYWORDS    RefSeq.
SOURCE      Caulobacter sp. 602-1
  ORGANISM  Caulobacter sp. 602-1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Caulobacter.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Caulobacter sp. 602-1"
                     /db_xref="taxon:2492472"
     gene            1..335
                     /gene="trxB"
     Protein         1..335
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35515
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msttaprqtr cliigsgpag ytaaiyaara llkpvliagi qpggqltitt dvenypgfad
       61 viqgpwlmdq mraqaehvgt efvsdivtgv dlskrpftvk tdsgqdwiae tiiiatgaqa
      121 kwlglesesk fqgfgvsaca tcdgffyrnk evivvgggnt aveealflts faskvtlvhr
      181 kdelraekil qerllahpki eviwdsvide vtgqtdpmgv tgarlknikt gettevaadg
      241 vfiaighaps selfagqlev gpggylkvkp gtastaiegv yaagdvtddv yrqavtaagm
      301 gcmaaleavr flaeedhkva hhpishqean kigvw
//
LOCUS       WP_125170537             507 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tessaracoccus sp. OH4464_COT-324].
ACCESSION   WP_125170537
VERSION     WP_125170537.1
KEYWORDS    RefSeq.
SOURCE      Tessaracoccus sp. OH4464_COT-324
  ORGANISM  Tessaracoccus sp. OH4464_COT-324
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Tessaracoccus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Tessaracoccus sp. OH4464_COT-324"
                     /db_xref="taxon:2491059"
     Protein         1..507
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52694
     Region          1..506
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 meigvpkeig darvaatpks vaglnklgye vtiesgagla asfaddayee agarivadpw
       61 ladivlavna psqeqlqrmr agatlitfla prqnpelver laaqgitals mdmvprtsra
      121 qaldalssla nisgyravie aahafgrfft gqvtaagkvp pakvlvagtg vaglaaigaa
      181 nslgaivrat dvrpetaeqv esmgatflhv aadqgvssdg yakeasadya akaaelyaqq
      241 akevdiiitt aaipgrpspk litadmvatm rpgsvivdla avgggncelt rpgeayetgn
      301 gvtiigytdm vsrlpgqasq lygtnlvnal qlmtpgkdge lvvdfddevv rnmtitrdge
      361 vtfppppiqv saapastvpa kvvepvvesr pprpwwqeva vvgigsilmi alltvapssf
      421 vtlfgvfala cvvgyyvvwn vthalhtplm svtnaisgii vvgamtqlas enlmvkiiaf
      481 vavliasinv fggftvthrm lnmfrkg
//
LOCUS       WP_125171710             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tessaracoccus sp. OH4464_COT-324].
ACCESSION   WP_125171710
VERSION     WP_125171710.1
KEYWORDS    RefSeq.
SOURCE      Tessaracoccus sp. OH4464_COT-324
  ORGANISM  Tessaracoccus sp. OH4464_COT-324
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Tessaracoccus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Tessaracoccus sp. OH4464_COT-324"
                     /db_xref="taxon:2491059"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32928
     Region          6..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstvreiiii gsgpagytaa iyaaranlkp lvfegaldsg galmnttdve nfpgfpegim
       61 gpdlmqnmra qaerfgaeli tddvsavdlt gevkvvrdse gteyrahsvv lamgsgyrrl
      121 glagedrlsg rgvswcatcd gaffrdkhia vvgggdsave eatfltrfas kvtlihrrde
      181 lraskimvar aqadpkiefa wnsrvtaing enavesvtle dtvtgetrql elsgvfiaig
      241 hdprsnlvad qvtvdpagyv vvephstetn lpgvfacgdl vdnryrqait aagsgckaal
      301 daekyiaala d
//
LOCUS       WP_125176782             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_125176782
VERSION     WP_125176782.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>304
                     /gene="trxB"
     Protein         1..>304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..304
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vqgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcm
//
LOCUS       WP_125176802             104 aa            linear   BCT 07-JUL-2024
DEFINITION  SSU0592/SSU0593 family protein [Streptococcus suis].
ACCESSION   WP_125176802
VERSION     WP_125176802.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Haas,B. and Grenier,D.
  TITLE     Isolation, Characterization and Biological Properties of Membrane
            Vesicles Produced by the Swine Pathogen Streptococcus suis
  JOURNAL   PLoS One 10 (6), e0130528 (2015)
   PUBMED   26110524
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046094.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     Protein         1..104
                     /product="SSU0592/SSU0593 family protein"
                     /calculated_mol_wt=11123
ORIGIN      
        1 mkqlvtkrsy kiglsaialv llmttaggat ahastgtysv etrgdaevyr lletpagsft
       61 qggivlkpvn nsttkpsetk swfdsfwssv ktfweaicrg vgwc
//
LOCUS       WP_125181407             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Thiohalobacter thiocyanaticus].
ACCESSION   WP_125181407
VERSION     WP_125181407.1
KEYWORDS    RefSeq.
SOURCE      Thiohalobacter thiocyanaticus
  ORGANISM  Thiohalobacter thiocyanaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiohalobacterales; Thiohalobacteraceae; Thiohalobacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Thiohalobacter thiocyanaticus"
                     /db_xref="taxon:585455"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40622
     Region          3..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mpirvavpke tlegecrval dpvvakrfaa lgcevrmehd agagahyvdd dyedvsfvtd
       61 kaellgnaev ilkvqppded einqiaegsi vvgfmsphry pervklmrdr ritsfameli
      121 prisraqgmd alssqaavag ykaaimaadr sgrffpmltt aagtirpakv liigagvagl
      181 qaiatakrlg avveaydvrs atreqvqslg akyidtgvaa egeggyarel teeekrkqle
      241 vlakhitqsd avittaaipg rpspkiiske mvdnmkvgsv iidlaaeggg ncevtkpged
      301 yvygcvrvyg pfnvpsmlpv hasdmyaknl lnfltpmike gelkldwedq vikdsalthd
      361 geirheptra lvegdas
//
LOCUS       WP_125182542             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thiohalobacter thiocyanaticus].
ACCESSION   WP_125182542
VERSION     WP_125182542.1
KEYWORDS    RefSeq.
SOURCE      Thiohalobacter thiocyanaticus
  ORGANISM  Thiohalobacter thiocyanaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiohalobacterales; Thiohalobacteraceae; Thiohalobacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Thiohalobacter thiocyanaticus"
                     /db_xref="taxon:585455"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34821
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseskhcrll ilgsgpagyt aaiyaaranl npvlvtgleq ggqlmtttev enwpggaadl
       61 qgpqlmeemr qhterfdaei vfdhinnvdl kqrpfqlqgd sgsytcdali iatgasamyl
      121 gldseeafkg rgvsacatcd gffyrdkava vigggntave ealylanias hvtlvhrrda
      181 lraekilqdr lfakekegkv siewnhvlde vlgddagvtg mrlkntqdds treidvhgvf
      241 iaighkpntd mfedqldmeh gyikvksgte gnatatsveg vfaagdvmdh vyrqaitsag
      301 tgcmaaldae kyldnldqsa shy
//
LOCUS       WP_125184076             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus suis].
ACCESSION   WP_125184076
VERSION     WP_125184076.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus suis
  ORGANISM  Streptococcus suis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptococcus suis"
                     /db_xref="taxon:1307"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33078
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtvvigag pagmtaalya grsnlkvall ergiyggqmn ntaeienypg ydhisgpala
       61 ekmfeplekf gvdhifgtlv rieeegqikk vitedgvlet ktvvlamgak hrllgvpged
      121 tynsrgvsyc avcdgaffrg qkllvvgggd saveealflt qfaesvtivh rrdqlraqkv
      181 iqdrafanek infiwdsvve eikgddlrvq svviknvkte evsevdfggv fiyvgldpmt
      241 dtvadlgitd eagwvitnek mettqsgiya igdirqnqlr qiatavgnga vagqevynyi
      301 telae
//
LOCUS       WP_125189607             518 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. RP5T].
ACCESSION   WP_125189607
VERSION     WP_125189607.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. RP5T
  ORGANISM  Streptomyces sp. RP5T
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Streptomyces sp. RP5T"
                     /db_xref="taxon:2490848"
     Protein         1..518
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53456
     Region          13..517
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msaeesahhp pcrvgvvaes vsgetrvaat patarqligl gyevvvesga geasgfddqa
       61 yadvgagiae aweadvvlkv napteaeirr lrrgavvval lapaqnpell raladagvta
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvkslggeyl pvnvtqeast dgyaratsdd
      241 ydraaaelyh eqardvdivi ttalipgrpa prlltaedva vmkpgsvivd maaamggnve
      301 gtvpgrivvt dngvtligyt dlasrlpaqa sqlfgtnlvn llklltpgkd gqltidfddv
      361 vqravtvvrd gevtwppppv avsaapaarp aarseapapk qprltparrf gliglgmlam
      421 fllvafapaq lagnftvfal avvigyyvig kvhhalhtpl msvtnaisgi vvigallqig
      481 hesrlvtvls fvailltsvn ifggfavtrr mlsmfskg
//
LOCUS       WP_125188587             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. RP5T].
ACCESSION   WP_125188587
VERSION     WP_125188587.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. RP5T
  ORGANISM  Streptomyces sp. RP5T
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces sp. RP5T"
                     /db_xref="taxon:2490848"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34230
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgim
       61 gpelmdnmra qaerfgaelv pddivsvelt geiktvtdts gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfv wdsevaeiqg dpklsglklr nlktgelsdl avtglfiaig
      241 hdprtelfkg qlelddegyl kveapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala deekaepekt av
//
LOCUS       WP_125199355             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Guyparkeria sp. SCN-R1].
ACCESSION   WP_125199355
VERSION     WP_125199355.1
KEYWORDS    RefSeq.
SOURCE      Guyparkeria sp. SCN-R1
  ORGANISM  Guyparkeria sp. SCN-R1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Thioalkalibacteraceae; Guyparkeria.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Guyparkeria sp. SCN-R1"
                     /db_xref="taxon:2341113"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34004
     Region          6..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 madsntrhsk llilgsgpag ysaavyaara nldpvlitgm emggqltttt evenwpgdpd
       61 dltgpalmdr mkahaekfdt eiifdhihtt klderpftlt gdqgtytcda liiatgasar
      121 ylgieseqaf rgkgvsacat cdgffyknqt vavvgggnta veealylski aakvhvvhrr
      181 drfraedili drlmkkaedg nveihwnhev devlgdqmgv nglrikdkeg etsdlelsgv
      241 fiaighspnt gifegqldmp ggyisvksgt ngnatatsvd gvfaagdvmd hvyrqaitsa
      301 gtgcmaalda kaflekldd
//
LOCUS       WP_125202678             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium sp. SC28].
ACCESSION   WP_125202678
VERSION     WP_125202678.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium sp. SC28
  ORGANISM  Chryseobacterium sp. SC28
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Chryseobacterium sp. SC28"
                     /db_xref="taxon:2268028"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34768
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mesnildcvi vgsgpagfta aiyaaranlk pelftglepg gqlttttdve nfpgfpdgis
       61 gpemmlllqk qaerfdtkvh yemitkvefs qkrggihkls tgsreilaks viistgatak
      121 ylglpdekky sgggvsacat cdgffyrgqd vvvvgagdta aeeatylani ckkvtllvrk
      181 dhfraskvmv ervlntpnie vkynheligi egenalvera ivinnltkev ftidvhgifi
      241 aighkpntai fkgqvdldey eyiitegksa rtnvpgifaa gdvqdrhyrq aitaagsgcm
      301 aamdaekylg elagenhtwv er
//
LOCUS       WP_125215449             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rickettsiales endosymbiont of
            Stachyamoeba lipophora].
ACCESSION   WP_125215449
VERSION     WP_125215449.1
KEYWORDS    RefSeq.
SOURCE      Rickettsiales endosymbiont of Stachyamoeba lipophora
  ORGANISM  Rickettsiales endosymbiont of Stachyamoeba lipophora
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Rickettsiales endosymbiont of Stachyamoeba
                     lipophora"
                     /db_xref="taxon:2486578"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34308
     Region          10..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtkqihsk vliigsgpag ytaaiyaara nlqptlvrgm qpggqltitt evenypgfae
       61 tiqgpwlmeq mekqaehvgt qlitdhiksv dllkrpfsal gesgttytgd tviiatgaqa
      121 kwlglesesk fqgfgvsgca tcdgffyknk kcivvgggns aveealylth hasevvlihr
      181 rdslraekia qdrlfnhpki kviwnsaiee ivgveqpfks vtgvkikntq tgeiteittd
      241 gvfvaighkp ntdmfkgqle mdnegylitn pgttytsiag iyaagdvqdk iyrqavtaag
      301 tgcmaaldae kylsnkeva
//
LOCUS       WP_125222801             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Maribacter algicola].
ACCESSION   WP_125222801
VERSION     WP_125222801.1
KEYWORDS    RefSeq.
SOURCE      Maribacter algicola
  ORGANISM  Maribacter algicola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Maribacter.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Maribacter algicola"
                     /db_xref="taxon:2498892"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35139
     Region          11..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseviervkt liigsgpagy taaiyaarad lkpvlytgle pggqltttte vdnfpgypeg
       61 idgptmmvql qqqaerfgtd vrigmvtkae fgkkegdihk itvdhekqie aetviistga
      121 sakylnipse qrlrgggvsa cavcdgffyk gqdvaivgag dtaaeeasyl anicnkvtml
      181 vrkdhmrask amqhrvqslk nieikyntev devlgdqvve glrmvnnqtg ekeeiaitgl
      241 fiaighkpnt difkgqldmd etgyiitkgk stktnipgvf asgdaqdkey rqavtaagtg
      301 cmaaldaery latigsiket iadnyni
//
LOCUS       WP_125227624             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Arachnia
            propionica].
ACCESSION   WP_125227624
VERSION     WP_125227624.1
KEYWORDS    RefSeq.
SOURCE      Arachnia propionica
  ORGANISM  Arachnia propionica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Arachnia.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Arachnia propionica"
                     /db_xref="taxon:1750"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52610
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvirerd darvaatptt verlirlgye vdvesgagam aslpddayva agarivesaw
       61 gadvvvavnp peeeqiaamr pgatligfla prqrpeltdr laaqgitals mdmvprtsra
      121 qaldalssla nisgyravve aahafgrfft gqvtaagkvp patvfvigag vaglaaigaa
      181 nslgavvrat dvrpetaeqv esmgatfvhv dsadqgissd gyakevgedy arraaelyaa
      241 qarevdiiit taaipgkpsp klitadmvas mkpgsvivdl gavgggncel trpgeshvtd
      301 ngvtiigwtd laarlpgqss qlygtnivna lalmtpgkdg elvidvddev vrtmtvvlrg
      361 eitfppppiq vsaapspspa aatevvappp rpprpwwhev alvglgaavf iaaltvapas
      421 fvglmavfvv avvvgyyvvw nvthalhtpl msvtnavsgi ivvgamtqla hpewavkila
      481 fvavliasin vfggftvthr mlgmfrkg
//
LOCUS       WP_125228079             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arachnia propionica].
ACCESSION   WP_125228079
VERSION     WP_125228079.1
KEYWORDS    RefSeq.
SOURCE      Arachnia propionica
  ORGANISM  Arachnia propionica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Arachnia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Arachnia propionica"
                     /db_xref="taxon:1750"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32671
     Region          4..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msvheliiig sgpagytaai yaaraalnpv vfegafssgg almnttdven fpgfpegvmg
       61 ptlmtnmraq aerfgaqlit ddveqveltg pvkkvtdsag kvweartvil amgsgyrelg
      121 vpgeatlsgr gvswcatcdg affrdkpivv vgggdsavee atfltrfgss vllvhrrdel
      181 raskvmadra ekdpklsfaw nsvvesingd skvesvtlrd vntgetrdve aagvfvaigh
      241 dprnelvkgq vdldeggyvl vregsqatnl dgvfacgdlv dhtyrqaita agsgcraald
      301 aerwlaahes
//
LOCUS       WP_125230750             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingorhabdus wooponensis].
ACCESSION   WP_125230750
VERSION     WP_125230750.1
KEYWORDS    RefSeq.
SOURCE      Sphingorhabdus wooponensis
  ORGANISM  Sphingorhabdus wooponensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingorhabdaceae; Sphingorhabdus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Sphingorhabdus wooponensis"
                     /db_xref="taxon:940136"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33611
     Region          9..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtenrhapvi iigsgpagyt aavyaaranl tpmmitgvev ggqlmtttev dnwpgddagv
       61 mgpelmermr khaerfgtri endyiekvdf skrpfvltgg agdytadsvi iatgasaqyl
      121 glpsetafmg kgvsacatcd gffyrnkpva vigggntave ealylanias hvtlvhrrdk
      181 lkaekilqdr lfareaegki tikwnhrlde vlgdamgvtg mriaatdgsg tedielhgvf
      241 iaighkpntg ifeghldmag gyikvrggfe gqatetsvpg vfacgdvmdh iyrqactsag
      301 tgcmaaldae rfidava
//
LOCUS       WP_125232031             301 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Leptospira adleri].
ACCESSION   WP_125232031
VERSION     WP_125232031.1
KEYWORDS    RefSeq.
SOURCE      Leptospira adleri
  ORGANISM  Leptospira adleri
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Leptospira adleri"
                     /db_xref="taxon:2023186"
     Protein         1..301
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34483
     Region          3..162
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mynifskrqk qmrgevpdiy rydvlpetlr vqfihiindv lksiggeeer yqvrelledv
       61 hrillkeygv fflisshqsp iddylnfilr eknvervldg ielfgkalsl vkdnlyypgk
      121 itsseaikev nsrfreagig fkiedgiivk idsellhket vqdtlklihg keylninney
      181 lsahehfrhg ryseaiadsl kafesslkla cekrkisydk kdtskrlidl lfqntffpsy
      241 mqtyigslra ilesgiptir nrtsghgkgv gtdpealate slsnfilnit gsvikfiiks
      301 i
//
LOCUS       WP_125236677             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Leptotrichia sp. OH3620_COT-345].
ACCESSION   WP_125236677
VERSION     WP_125236677.1
KEYWORDS    RefSeq.
SOURCE      Leptotrichia sp. OH3620_COT-345
  ORGANISM  Leptotrichia sp. OH3620_COT-345
            Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia;
            Fusobacteriales; Leptotrichiaceae; Leptotrichia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Leptotrichia sp. OH3620_COT-345"
                     /db_xref="taxon:2491048"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34016
     Region          5..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maehfdliii gsgpaglssa lyasrgrlkt lvlekgqngg qaaithlien ypgsienptg
       61 pnltarmleq cksfgtevrk eevvevdfss kekivkckdt vytakavvia tgatprklda
      121 pgikelsgkg isycatcdad ffkelevyvv gggnsaieea iflskfarqv hivhmldhfq
      181 cegitlekak ntpnidittr tvvqevkgdg ilesivfknl dteevyevea deedgtmglf
      241 vfigytpqte lfkgkieldq ygyivagent etnvpgvfva gdcrikevrq vvtaaadgav
      301 saimaekyis ehfe
//
LOCUS       WP_125233686             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Prevotella sp. OH937_COT-195].
ACCESSION   WP_125233686
VERSION     WP_125233686.1
KEYWORDS    RefSeq.
SOURCE      Prevotella sp. OH937_COT-195
  ORGANISM  Prevotella sp. OH937_COT-195
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Prevotella sp. OH937_COT-195"
                     /db_xref="taxon:2491051"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33244
     Region          4..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkhtkclivg sgpagytaai yagranlspv lvcgmqmggq ltqttivenf pgypdgvdan
       61 qmmmemqqqa erfgaelvqg tvtdvdfgnk paivtlddge kieadtviva tgasakylgl
      121 sdeekyngrg vsacatcdgf fyrkkvtavv gggdtaceda lylsqlcskv ylvvrkpflr
      181 askimqervm aaenieilfe hnatglygen gvegmhvvkr kgetdeqhyd vaidgfflai
      241 ghkpnsevfg kwvdtdeigy iktigttqqt rtpglfaagd vcdptyrqav vaagtgckaa
      301 leaerylqtl
//
LOCUS       WP_125238913             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Prevotella heparinolytica].
ACCESSION   WP_125238913
VERSION     WP_125238913.1
KEYWORDS    RefSeq.
SOURCE      Prevotella heparinolytica (Bacteroides heparinolyticus)
  ORGANISM  Prevotella heparinolytica
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Prevotella heparinolytica"
                     /db_xref="taxon:28113"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33619
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meiekvkcli igsgpagyta aiyagranls pvlyaglqpg gqlttttdve nfpgypegig
       61 gpelmedlrk qaerfgadlr ygvataadls kapykitidg ektieaetli istgaaakyl
      121 gledekkyag mgvsacatcd gffyrkktva vvgggdtace eavylaglaa kvylivrkpy
      181 lraskimqer vmqhekievl fehnavglyg esgvegvhlv qrmgesdekr ydlaidgffl
      241 aighkpnsdi fkpyldtdev gyivtepgtp rtkipgvfaa gdvadphyrq aitaagtgcq
      301 aaieaeryls akgll
//
LOCUS       WP_125242458             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aquabacterium soli].
ACCESSION   WP_125242458
VERSION     WP_125242458.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium soli
  ORGANISM  Aquabacterium soli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Aquabacterium soli"
                     /db_xref="taxon:2493092"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33980
     Region          9..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msdtthsnvl ilgsgpagyt aaiyaaranl kptlvtgmaq ggqlmtttev dnwpadvhgv
       61 qgpelmqrfl ehaerfqtqm vfdhvnevdl skrpftlkgd sgtyttdtli iatgasakyl
      121 glpseeafmg rgvsgcatcd gffyrdqvvc vvgggntave ealylsnias kvhlihrrdk
      181 fraeailidk vaekvkagkm elhlfqtlde vlgdqtgvtg vrlksttdgs tkelelkgcf
      241 iaighqpntd ifkgqlemkd gyiltksgse gfatmtsvpg vfaagdvqdh iyrqaitsag
      301 tgcmaaldaq rfleqngg
//
LOCUS       WP_125245061             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Aquabacterium soli].
ACCESSION   WP_125245061
VERSION     WP_125245061.1
KEYWORDS    RefSeq.
SOURCE      Aquabacterium soli
  ORGANISM  Aquabacterium soli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Aquabacterium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Aquabacterium soli"
                     /db_xref="taxon:2493092"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38667
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligipletv agesrvaitp etvkklkaqg htlrvqsgag iaasvideay vaagaeitda
       61 agalgadmvl kvrspqasel plmkpgavlv gmlnpfdkdg lqaltgaqlt afaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr lfpmlmtaag tikaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetpee keaaegvggy arpmpqswld
      241 rqkvevakrv aqadivitta lipgraapvl vtedmvksmk pgsvivdlaa paggncplte
      301 pgqivvkhgv tlvgetnlpa lvaadsssly arnvldflkl vfnkegqfhv dleddivkac
      361 lmcrdgqllr a
//
LOCUS       WP_125251468             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudoalteromonas sp. J010].
ACCESSION   WP_125251468
VERSION     WP_125251468.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. J010
  ORGANISM  Pseudoalteromonas sp. J010
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudoalteromonas sp. J010"
                     /db_xref="taxon:998465"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33836
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdakhckll ilgsgpagyt aavyaaranl npvlitgmqq ggqlttttev enwpgdahgl
       61 tgpalmdrmk ehaerfetei ifdhinkvdv tkrpftltgd qgtytcdali iatgasakyl
      121 glesetafqg rgvsacatcd gffyrgqkva vvgggntave ealylsniae evhvihrrds
      181 frsekiladr lmdkaangnv vlhlnrtlde vlgdemgvtg irikdtdsda teqldlagvf
      241 iaighkpntd mfegqlemkd gylvvqsgln gnatqtsieg vfaagdvsdh iyrqaitsag
      301 tgcmaaldae rfldsqk
//
LOCUS       WP_125256413             336 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Brevundimonas fluminis].
ACCESSION   WP_125256413
VERSION     WP_125256413.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas fluminis
  ORGANISM  Brevundimonas fluminis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Brevundimonas fluminis"
                     /db_xref="taxon:2487274"
     gene            1..336
                     /gene="trxB"
     Protein         1..336
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35585
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstprtvrca iigsgpagwt aaiyaarasl npvviagiqp ggqltittdv enypgfadvi
       61 qgpwlmeqmr aqaehvgtev iedivtradl ssrpfrltld sgqemlaetv iistgaqakw
      121 lgleseatyq gfgvsacatc dgffyrgkqv vvvgggntav eealfltnfa ekvtvvhrrd
      181 efraekilqe rlfahpkvev iwnhkvdeiv gvvdgmaknv tgvrlsstvd gsarevacdg
      241 vfvaighaps selfagqlet kaggylvvkp gttataiegv yaagdvtddv yrqavtaagm
      301 gcmaaleavr flaeedhkaa grpishkeae kigawd
//
LOCUS       WP_125272221             316 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Acinetobacter].
ACCESSION   WP_125272221
VERSION     WP_125272221.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33694
     Region          8..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdpeglt
       61 gpvlmermqa haerfgteiv ydhinevdlk trpfvlkgdm eeytcdalii stgataqylg
      121 leseaafmgq gvsacatcdg ffyknqnvmv vgggntavee alylsniaah vtlvhrrdsl
      181 rsekilqdhl fakekegkis iiwnhqvdev lgdntgvtsv rikstqdsst qdvqvqglfv
      241 aighkpntdm fegqlnlrdg yiqvqsgtsg nataasiegv faagdvadsi yrqaitsags
      301 gcmaaldaek yldnln
//
LOCUS       WP_125257744             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brevundimonas fluminis].
ACCESSION   WP_125257744
VERSION     WP_125257744.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas fluminis
  ORGANISM  Brevundimonas fluminis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Brevundimonas fluminis"
                     /db_xref="taxon:2487274"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38383
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtvalavtre rrdgetrcav tpdavkklta lgctvtveag aglgssipda eftaagatva
       61 adtkavlsha dvllkvrgpt aqeisalkpg avvvallday rekdgvaala kanatafame
      121 fvpritraqv mdalssqanl agyravieaa hsygrgfpmm mtaagtvaaa kvfvmgagva
      181 glqaiatarr lgavvtatdv rpaakeqves lgakfvaved eefkaaetaa gyakpmsaey
      241 qakqaeltas hivkqdvvit talipgrpap rlitaahvas mkpgsvivdl avdnggnveg
      301 akpgevvttp ngvqivgwsn lpgriasdas alyarnltaf lgllvkdgel avdledeilk
      361 aavvthggav vhegvrg
//
LOCUS       WP_125273873             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter johnsonii].
ACCESSION   WP_125273873
VERSION     WP_125273873.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33633
     Region          8..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msvrhsrlii lgsgpagysa avyaaranlk ptliagiqlg gqlttttevd nwpgdpeglt
       61 gpalmermqa haerfgteii ydhinevdls vrpfllkgdm deftcdalii atgataqylg
      121 leseaafmgq gvsacatcdg ffyknqkvmv vgggntavee alylsniash vtlvhrrdsl
      181 rsekilqdhl fekekegkis iiwnhqvdev lgdntgvtav rlkstqdest qdidvqglfv
      241 aighkpnsam fdgqlnlrdg yiqvqsgtsg nataasvagv faagdiadsv yrqaitsags
      301 gcmaaldaek yldalge
//
LOCUS       WP_125281215             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter johnsonii].
ACCESSION   WP_125281215
VERSION     WP_125281215.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter johnsonii
  ORGANISM  Acinetobacter johnsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Acinetobacter johnsonii"
                     /db_xref="taxon:40214"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33561
     Region          8..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliagiqlg gqlttttevd nwpgdpeglt
       61 gpalmermqa haerfgteii ydhinevdls vrpfvlkgdm deftcdalii atgataqylg
      121 leseaafmgq gvsacatcdg ffyknqkvmv vgggntavee alylsniash vtlvhrrdsl
      181 rsekilqdhl fekekegkis iiwnhqvdvv lgdntgvtav rlkstqdest qdidvqglfv
      241 aighkpnsam fdgqlnlrdg yiqvqsgtsg nataasvagv faagdiadsv yrqaitsags
      301 gcmaaldaek yldalge
//
LOCUS       WP_125282843             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Achromobacter denitrificans].
ACCESSION   WP_125282843
VERSION     WP_125282843.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter denitrificans
  ORGANISM  Achromobacter denitrificans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Achromobacter denitrificans"
                     /db_xref="taxon:32002"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33955
     Region          12..316
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msaaetprha rvlilgsgpa gyaaavyaar anlspvliag maqggqlmtt tdvdnwpada
       61 agvqgpelmq rfqdhalrfg tdviadhvqs vdlsrrpfvl rgeraaytcd alivatgava
      121 rylglaseqa ymgrgvsgca tcdgffhrgr dvcvvgggnt aveealylsn iartvtlvhr
      181 rdtfraepim ldklaakveq gqirlrlrsv ledvlgddsg vtgvrirnla ddaradlevs
      241 gcfvaighrp stelfqgqle ledgyivtra grrglatmts vsgvfaagdv qdhvyrqait
      301 sagsgcmaal daqrfleqas a
//
LOCUS       WP_125292863             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Atlantibacter subterraneus].
ACCESSION   WP_125292863
VERSION     WP_125292863.1
KEYWORDS    RefSeq.
SOURCE      Atlantibacter subterraneus
  ORGANISM  Atlantibacter subterraneus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Atlantibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Atlantibacter subterraneus"
                     /db_xref="taxon:255519"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53311
     Region          10..476
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mariskflpy fwslfaglll lspahaeqap aatapakiea hnevfankhp dqfnswkats
       61 eqseredala edpnmvilwa gypfsrdynk prghayaltd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkegea gyfhgkwarg gpeivndlgc adchntased fakgkpaltl
      181 srpyaarame tigkpfdkas rldqqamvcg qchveyyfdg kdkavkfpwd ngpnvdgmek
      241 yyddiafsdw vnplsktpml kaqhpeyetw sagihgknnv tcidchmpkm qnaegkmfts
      301 hkignpfdtf dqtcknchtq tkealqsvva erkaaiqdlk rkvevqlvha hfeakaalda
      361 gatdeemkpi qtdirhaqwr wdlaiashgv hmhapdealr mlgtalnkaa daraklirll
      421 atkgiteevk lpdistkaka qaaigldmqk inaekqdflk tvvpqwddqa rkngllgteg
      481 k
//
LOCUS       WP_125296960             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aliarcobacter skirrowii].
ACCESSION   WP_125296960
VERSION     WP_125296960.1
KEYWORDS    RefSeq.
SOURCE      Aliarcobacter skirrowii (Arcobacter skirrowii)
  ORGANISM  Aliarcobacter skirrowii
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Aliarcobacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Aliarcobacter skirrowii"
                     /db_xref="taxon:28200"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32855
     Region          3..292
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldlaiiggg pagltaglya trgglkdvvm femgmpggqi tgsseienyp gqgsvmsgmd
       61 lmatwpeqcq kfglkhemae vsnvtkvgdi fkittsdkke fearavlfat gsvprragfk
      121 gedeffgrgv stcatcdgff ykgkevavig ggdsaleeay ylskmckkvy lvhrrdtyra
      181 apstiahvkn tenieevtnv sveevygdms gvlglkvksn vtgeirdlpt pgvfvfvgrn
      241 vlnaplkqad gsflcemsqn gevvvdlkmr tnvkglwaag diridaakqv vcaaadgata
      301 avdiieylg
//
LOCUS       WP_125299990             440 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Brucella].
ACCESSION   WP_125299990
VERSION     WP_125299990.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..440
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45493
     Region          4..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlfipke sdpsetrvaa saetvkkfia lgfdvvvekg ageksripda eftaagarig
       61 tvadaktadv vlkvrrptda elkgyksgaa lfamldpygh edavaalaka gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedee fkaaetsggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vsremvasmr pgsvlvdlav erggnvegav
      301 agqiadvngv rivghlnvsg riaasasqly arnliafvet lvdkeakvlk idpeeelvka
      361 tllthqskil hpafakaeta paqavaekaa kpkaapkpka ekpaakaaap kaaakpakna
      421 pakapkttss pkspvdggea
//
LOCUS       WP_125300069             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Brucella].
ACCESSION   WP_125300069
VERSION     WP_125300069.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Brucella"
                     /db_xref="taxon:234"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34330
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqrhapviv igsgpagyta aiyaaramlk pliiaglqqg gqlmittdve nypgyadpvq
       61 gpwmmeqmak qaenvgseiv hdiiteveta vrpfrlkgds gtiytcdali iatgaqakwl
      121 gldseqtfmg ggvsacatcd gffyrgkdvv vvgggntave ealylshiak svtvvhrrdg
      181 fraekimqdr llsrqnvsvv wnsvideilg teakppmgat vtgvrlknvv tgeaqeldth
      241 gvfvaighap avslfegklk qkpngylwta pdstatdvpg ifaagdvtdd iyrqavtaag
      301 lgcmaaleae rwlaaqeplh eaae
//
LOCUS       WP_125306200             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis eburnea].
ACCESSION   WP_125306200
VERSION     WP_125306200.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis eburnea
  ORGANISM  Amycolatopsis eburnea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Amycolatopsis eburnea"
                     /db_xref="taxon:2267691"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38392
     Region          10..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(24,79,98,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(53,131..132,141..142,145..146,149..150,152..153,
                     155..160,162,164..166,169,192..193,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,131,134,137,178..181,201..203,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,131,141,184..185,192,208..209,211..214)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(161..165,168,171,194,196)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mtdseqsqql tvgvvtesrp gerrvavvpk lvgrlaqrgl rvvvepgaga gahlsddayt
       61 qagaelgdaw garivvkvnp ptpdevakls rgavlvgfld prgnpdglak leeaglrafa
      121 meaiprisra qamdalssqa siggyravll aaqklprffp mlttaagtvp pakvlvlgag
      181 vaglqalata krlgaqttgy dvrpevaeqv kslgaqfldl gieavgeggy areltadere
      241 eqqrrlteai tkfdvvitta lvpgrkaptl vtadavkgmp agsvvvdlag etggnceltk
      301 pgedvvehdv tissplnlpa empshasely arnvvellel lvtkegalel nfedeivaga
      361 cvagregsps
//
LOCUS       WP_125309331             330 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Amycolatopsis eburnea].
ACCESSION   WP_125309331
VERSION     WP_125309331.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis eburnea
  ORGANISM  Amycolatopsis eburnea
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Amycolatopsis eburnea"
                     /db_xref="taxon:2267691"
     gene            1..330
                     /gene="trxB"
     Protein         1..330
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35344
     Region          9..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maaeeirnli ivgsgpagyt aavyaaraql eplvfegtqf ggalmtttev enfpgfrdgi
       61 mgpdlmeemr kqaerfgael raedveslel tgdvkyvhan gkryaaravi lamgaaaryl
      121 nvpgeqellg rgvsacatcd gfffrdhdiv vagggdsame eatfltkfak svtvvhrrde
      181 fraskimler aranekikwr lnsqitevlg dgkveglrlk dtkdgsestl dvsgffvaig
      241 hdprselvrg qvdldedgyv itqgrtsytn vdgvfaagdl vdrtyrqait asgsgcsaai
      301 daerwlaehg esdaheaael vgggygagtn
//
LOCUS       WP_125321986             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vibrio pectenicida].
ACCESSION   WP_125321986
VERSION     WP_125321986.1
KEYWORDS    RefSeq.
SOURCE      Vibrio pectenicida
  ORGANISM  Vibrio pectenicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Vibrio pectenicida"
                     /db_xref="taxon:62763"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34371
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mseikhskll ilgsgpagyt aavyaaranl hpvlvtgmqq ggqlttttdv enwpgdpegl
       61 tgpalmermk ehaerfetqi ifdhinhvdf skrpfilkgd sneyscdali istgasakyl
      121 gleseetfkg rgvsacatcd gffyrsqkva vigggntave ealylsnias evhlihrrds
      181 fraekilvrr lmekvesgni tlhtdkvlee ivgddmgvtg vrikdtktnk vdgldvmgaf
      241 iaighqpntg ifegqldmkd gyiivqsgln gnatqtsipg ifaagdvmdh tyrqaitsag
      301 tgcmaaldae ryldalangk
//
LOCUS       WP_125323141             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            pectenicida].
ACCESSION   WP_125323141
VERSION     WP_125323141.1
KEYWORDS    RefSeq.
SOURCE      Vibrio pectenicida
  ORGANISM  Vibrio pectenicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Vibrio pectenicida"
                     /db_xref="taxon:62763"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54492
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpkeil agetrvaasp ksveqllklg fsvhvesnag alasfddaaf tslgativtk
       61 devwlsdiil kvneptdkei qlfkegatli sfiwpaqnte lleklsakki nvlamdsvpr
      121 israqsldal ssmaniagyr avveaahefg rfftgqitaa gkvppakvlv agagvaglaa
      181 igaagslgav vrsfdvrpev keqvqsmgae flevnfkees gsgdgyakem seafnkkaee
      241 lyteqakdvd iiittalipg kpapklitkk mvdsmkagsv ivdlaaangg nceytktdkv
      301 vttkngvkiv gytdmvgrlp tqssqlyatn ivnllkllck ekngnihidf ddvvlrgvtv
      361 ikegevtwpa ppiqvsaqpq qkpidknikt ddkkdkpvsq tkkltalgvg lcsfawvasv
      421 apasflshft vfvlacvvgy yvvwnvthal htplmsvtna isgiivvgal lqighgngav
      481 sflafiaili asinifggft vtkrmlqmfr kd
//
LOCUS       WP_125326001             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tabrizicola piscis].
ACCESSION   WP_125326001
VERSION     WP_125326001.1
KEYWORDS    RefSeq.
SOURCE      Tabrizicola piscis
  ORGANISM  Tabrizicola piscis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tabrizicola.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Tabrizicola piscis"
                     /db_xref="taxon:2494374"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33118
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maetrhtrvl iigsgpagyt aavysaraml npilvqglqp ggqltittev enwpgdshvq
       61 gpdlmvrmqd haaamgaeii sdyitsldls krpftatads gttytadavi latgaqakwl
      121 glpseekfkg fgvsacatcd gffyrgkevv vigggntave ealfltnfat kvtlihrrdf
      181 lraekimqdr lfknpkievl wnhevtevlg detplgvtav rarnvqtgat qdipcagffv
      241 aighapasel vkdqlplhng gyvvvepgtt rtaipgvfaa gdltdhvyrq avtsagmgcm
      301 aaldaekfls gh
//
LOCUS       WP_125327753             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tabrizicola piscis].
ACCESSION   WP_125327753
VERSION     WP_125327753.1
KEYWORDS    RefSeq.
SOURCE      Tabrizicola piscis
  ORGANISM  Tabrizicola piscis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tabrizicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Tabrizicola piscis"
                     /db_xref="taxon:2494374"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54944
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaltevf pgenrvamtp esaaqlvklg htcciqagag akagfsdaly saagvtvlps
       61 aaaviadsdv ivkvrgpeaa eletlaegqt lisffwpaqn pelleaaakk nltvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtsvslg aivhafdvrp evaeqiesmg asfvflefed aqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrpapkl wtedmvqmmk pgsvivdlaa erggncdltv
      301 pdqkivtdng vtivgytdfp srmaaqastl ystnirhmlt dltpkkdgvi lhnmeddvir
      361 gatvahvgav typppppkia aiaaakpkpk aveltpaerr aqevaafktq trnqvgllvv
      421 agglmllagl yapasfmshf ivfvlsvfvg fqviwnvshs lhtplmaitn aissiiilga
      481 lmqigsgnwl vvilaalsvf maginifggf mvtrrmlamf qks
//
LOCUS       WP_125330292             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125330292
VERSION     WP_125330292.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33161
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedrgdfke iitederfet ktviiasgan hrhlgvpgee
      121 dynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdraftnek irfvwdsvve sihgderkvt gvtfknvktg elsqaefggi fiyvgldpvs
      241 efaadlgitd eagwiltdhq mktsvagiya vgdvrqkdlr qittavgdga iasqevykyl
      301 teqa
//
LOCUS       WP_125336191             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sp. A12].
ACCESSION   WP_125336191
VERSION     WP_125336191.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. A12
  ORGANISM  Streptococcus sp. A12
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sp. A12"
                     /db_xref="taxon:1759399"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32625
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigag pagmtaalya arsnlkvall eagipggqmn ntsdienypg yanisgpela
       61 ekmfepletl gvehlfgrae nivdqgsyke ittddgllqa ktviiatgsn hrllgvpgee
      121 elnsrgvsyc avcdgaffrd edlmvvgggd saveeaiflt qfaksvtivh rrdalraqkv
      181 lqdrafanek ihfawntvve eikgdnrvts lvlkdvqtge vreqaaggvf iyvgldpvsd
      241 faqdlgildg qgwvitddhm ktsvpgvfav gdvrqkdlrq vttavgdgav agqeaykyit
      301 ehee
//
LOCUS       WP_125337775             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125337775
VERSION     WP_125337775.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33014
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedqgdfke iitederfea ktviiasgan hrhlgvpgee
      121 dynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdrafanek irfvwdsvve sihgderkvt gvtfknvktg klgqaefggi fiyvgldpvs
      241 efaadlgitd eagwiltdhq mktsvagiya vgdvrqkdlr qittavgdga iasqeaykyl
      301 teqa
//
LOCUS       WP_125338099             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125338099
VERSION     WP_125338099.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33045
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedqgdfke iitederfea ktviiasgan hrhlgvpgee
      121 dynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdrafanek irfvwdsvve sihgderkvt gvtfknvktg eisqaefggi fiyvgldpvs
      241 efaadlgitd eagwiltdhq mktsvagiya vgdvrqkdlr qittavgdga iasqeaykyl
      301 teqa
//
LOCUS       WP_125344675             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tenacibaculum singaporense].
ACCESSION   WP_125344675
VERSION     WP_125344675.1
KEYWORDS    RefSeq.
SOURCE      Tenacibaculum singaporense
  ORGANISM  Tenacibaculum singaporense
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Tenacibaculum.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Tenacibaculum singaporense"
                     /db_xref="taxon:2358479"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33244
     Region          6..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maekikclii gsgpagytaa iyaaradmkp vmytgmqmgg qlttttevdn fpgypkgtdg
       61 tammedlksq aerfgtdvrf gmvtkvelsk eeggihkvtv desteieaqt iiistgatak
      121 ylgleseqrl igggvsacat cdgffykgqd vvvvgagdta aeeatylani cskvtmlvrk
      181 dymraskamq hrvnktenit vmynteidev lgenvvegvr avnnqtgekm eipvtgvfia
      241 ighkpnsdlf kgvldmddtg ylitkgkstk tnlpgvfaag diqdkeyrqa vtaagtgcma
      301 aldaerylga le
//
LOCUS       WP_125346904             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125346904
VERSION     WP_125346904.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33061
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedrgdfke iitederfea ktviiasgan hrhlgvpgee
      121 dynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdrafanek irfvwdsvve sihgderkvt gvtfknvktg etsqaefggi fiyvgldpvs
      241 efaadlgitd eagwiltdhq mktsvagiya vgdvrqkdlr qittavgdga iasqeaykyl
      301 teqa
//
LOCUS       WP_125348581             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125348581
VERSION     WP_125348581.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33103
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedrgdfke iitederfet ktviiasgan hrhlgvpgee
      121 dynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdrafanek irfvwdsvve sihgderkvt gvtfknvktg eisqaefggi fiyvgldpvs
      241 efaadlgitd eagwiltdhq mktsvagiya vgdvrqkdlr qittavgdga iasqeaykyl
      301 teqa
//
LOCUS       WP_125350129             314 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Empedobacter].
ACCESSION   WP_125350129
VERSION     WP_125350129.1
KEYWORDS    RefSeq.
SOURCE      Empedobacter
  ORGANISM  Empedobacter
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Empedobacter"
                     /db_xref="taxon:59734"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33852
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mennvrdvii igsgpagyta giyaaranmn pliltgmepg gqlttttdve nfpgypeavt
       61 gpelmadlqk qaerfgteik yeyvtevtfg ekegdvhtvk snngtyqars iiistgatak
      121 ylglddetky agsgvsacat cdgffyrgkd vavvgggdta aeeatylskl cnkvyllvrk
      181 eemraskamq drvtnthnle vlynheligl egnnvvekak iinnitneek eliidgvfia
      241 ighkpntelf qgkldmdetg ylitqdrsyk tnvpgvfaag dvqdsvyrqa itaagsgcaa
      301 aldaeryvae ffea
//
LOCUS       WP_125353348             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125353348
VERSION     WP_125353348.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33089
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedrgdfke vitederfea ktviiasgan hrhlgvpgee
      121 dynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdrafanek irfvwdsvve sihgderkvt gvtfknvktg eisqadfggi fiyvgldpvs
      241 efaadlsitd eagwiltdhq mktsvagiya igdvrqkdlr qittavgdga iasqeaykyl
      301 teqa
//
LOCUS       WP_125357070             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125357070
VERSION     WP_125357070.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33114
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedrgdfke iitederfea ktviiasgan hrhlgvpgee
      121 dfnsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdrafanek irfvwdsvve sihgderkvt gvtfknvktg elsqaefggi fiyvgldpvs
      241 efakdlgitd eagwiltdhq mktsvagiya vgdvrqkdlr qittavgdga iasqeaykyl
      301 teqa
//
LOCUS       WP_125359062             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Stenotrophomonas sp. 278].
ACCESSION   WP_125359062
VERSION     WP_125359062.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. 278
  ORGANISM  Stenotrophomonas sp. 278
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Stenotrophomonas sp. 278"
                     /db_xref="taxon:2479851"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34441
     Region          11..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msnskpsrhq klvilgsgpa gwtaavyaar anlkpvvitg lqqggqlmtt tevdnwpgda
       61 hglmgpdlmt rmqahaerfe tevifdhiht adlsqrpfrl igdsaeytcd alivatgata
      121 kylgipteet fkgrgvsaca tcdgffyrdq dvvvvgggnt aveealylsn iarkvylvhr
      181 rdtlkaekim qdklfakvaa gkietvwhht veevlgddag vtgvrvkstq dgstrdisah
      241 gffvaighhp ntalfdgqla mnngyleirs glggnatqts vegvfaagdv adqhyrqait
      301 sagfgcmaal daeryldakg ala
//
LOCUS       WP_125365812             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus gordonii].
ACCESSION   WP_125365812
VERSION     WP_125365812.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus gordonii
  ORGANISM  Streptococcus gordonii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus gordonii"
                     /db_xref="taxon:1302"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32927
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall eagipggqmn ntadvenypg yalisgpela
       61 ekmfeplenl gvehvfghvq riedqgdfkk vitedevyes ktviiatgaf hrqlnvpgea
      121 efnsrgvsyc avcdgaffrd edllvvgggd saveeaiflt qfaksvtivh rrdqlraqkv
      181 lqdrafanek isfvwdsvve aihgnerkvt gvtfkniktg etsqadfggi fiyvgldpvs
      241 efvadlgird esgwivtddh mktsvagiya igdvrqkdlr qittavgdga iagqeaykfi
      301 aehe
//
LOCUS       WP_125372108             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus cristatus].
ACCESSION   WP_125372108
VERSION     WP_125372108.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus cristatus
  ORGANISM  Streptococcus cristatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus cristatus"
                     /db_xref="taxon:45634"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33242
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtmiigag pagmtaalya arsnlkvall ergiyggqmn ntaeienypg yarisgpela
       61 ekmfeplenl gvehlfgqve kiedhgdykk iitedeafet ktvilasgan hrhlgvpgee
      121 eynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdqlraqql
      181 lqerafanek isfiwdsvvk eikgddrrvt svvfenvktg qisesdfggv fvyvgldpvs
      241 dfvkdlgicd eagwivtdqh mktaidgiya igdvrqkdlr qittavgdga vagqevykyi
      301 teh
//
LOCUS       WP_125372519             306 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus cristatus].
ACCESSION   WP_125372519
VERSION     WP_125372519.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus cristatus
  ORGANISM  Streptococcus cristatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Streptococcus cristatus"
                     /db_xref="taxon:45634"
     gene            1..306
                     /gene="trxB"
     Protein         1..306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32677
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydaiivgsg pagytagiyl sraglknrli tgyseggqlt tttlvenypg fengidgnkl
       61 vqtmrrqaeq fgtemtfgfv qkiegekspf evhldngeii dtkaviiatg ssakylgieg
      121 eeeavgkgvs acatcdaffy kerevlvvgg gdvameealy ltrfaskvtv vhrrnklras
      181 dimakraqan dkihwmlnyt pikvasnlmg mtgldvrnne tgdiehiqad glfvaighqp
      241 ntdfldgkla lddkgyiqtq agtaktsvag ifaagdvqdp kyqqaitaag sgaiaaldtl
      301 ayidnl
//
LOCUS       WP_125375193             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus australis].
ACCESSION   WP_125375193
VERSION     WP_125375193.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus australis
  ORGANISM  Streptococcus australis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus australis"
                     /db_xref="taxon:113107"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32708
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigag pagmtaalya arsnlkvall eagipggqmn ntsdienypg yanisgpela
       61 ekmfeplevl gvehlfgrae nivdqgsyke ittddgllqa ktviiatgsn hrllgvpgee
      121 elnsrgvsyc avcdgaffrd edlmvvgggd saveeaiflt qfaksvtivh rrdalraqkv
      181 lqdrafanek ihfawntvve eikgdnrvts lvlkdvqtgq vreqaaggvf iyvgldpvsd
      241 fakelgilde ngwvitddhm ktsvpgifav gdvrqkdlrq vttavgdgav agqeaykyit
      301 ehee
//
LOCUS       WP_125372657             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus cristatus].
ACCESSION   WP_125372657
VERSION     WP_125372657.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus cristatus
  ORGANISM  Streptococcus cristatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus cristatus"
                     /db_xref="taxon:45634"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33206
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtmiigag pagmtaalya arsnlkvall ergiyggqmn ntaeienypg yarisgpela
       61 ekmfeplenl gvehlfgqve kiedhgdykk iitedevfet kavilapgan hrhlgvpgee
      121 eynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdqlraqkl
      181 lqerafanek isfiwdsvvk eikgddrrvt svvfenvktg qisesdfggv fvyvgldpvs
      241 dfvkdlgicd eagwivtdqh mktaiagiya igdvrqkdlr qittavgdga vagqevykyi
      301 teh
//
LOCUS       WP_125378611             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125378611
VERSION     WP_125378611.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33087
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedrgdfke iitederfea ktviiasgan hrhlgvpgee
      121 dynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdrafanek irfvwdsvve sihgderkvt gvtfknvktg elsqaefggi fiyvgldpvs
      241 efaadlgitd eagwiltdhq mktsiagiya vgdvrqkdlr qittavgdga iasqeaykyl
      301 teqa
//
LOCUS       WP_125379882             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus cristatus].
ACCESSION   WP_125379882
VERSION     WP_125379882.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus cristatus
  ORGANISM  Streptococcus cristatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus cristatus"
                     /db_xref="taxon:45634"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33280
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtmiigag pagmtaalya arsnlkvall ergiyggqmn ntaeienypg yarisgpela
       61 ekmfeplenl gvehlfgqve kiedhgdykk iitedevfet ktvilapgan hrhlgvpgee
      121 eynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdqlraqkl
      181 lqerafanek isfiwdsvvk eikgddrrvt svvfenvktg qisesdfggv fvyvgldpvs
      241 dfvkdlgicd eagwivtdqh mktaidgiya igdvrqkdlr qittavgdga vagqevykyi
      301 teh
//
LOCUS       WP_125384111             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus intermedius].
ACCESSION   WP_125384111
VERSION     WP_125384111.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus intermedius
  ORGANISM  Streptococcus intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus anginosus group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus intermedius"
                     /db_xref="taxon:1338"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33083
     Region          2..301
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagvtaalya arsnlkvali ergipggqmn ntsdienypg ytnisgpela
       61 ekmfeplenl gvehlfgave kieqqgtikk vytednvfes ktliiatgaf hrhlgvpgee
      121 elnsrgvsyc avcdgaffrd edllvvgggd saveeavflt rfaktvtiih rrkelraqkl
      181 lqdrafanek ihfiwdsvvq eikgdnrvqs vvvenvktge vsehefggvf iyvglnpvse
      241 fvkdlgitne sgwivtdhhm ktaisgiyai gdvrekdlrq vttavgdgai agqevykyit
      301 enc
//
LOCUS       WP_125383394             303 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptococcus].
ACCESSION   WP_125383394
VERSION     WP_125383394.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33264
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtmiigag pagmtaalya arsnlkvall ergiyggqmn ntaeienypg yarisgpela
       61 ekmfeplenl gvehlfgqve kiedhgdfkk iitedevfet ktvilapgan hrhlgvpgee
      121 eynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdqlraqkl
      181 lqerafanek isfiwdsvvk eikgddrrvt svvfenvktg qisesdfggv fvyvgldpvs
      241 dfvkdlgicd eagwivtdqh mktaidgiya igdvrqkdlr qittavgdga vagqevykyi
      301 teh
//
LOCUS       WP_125388216             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus cristatus].
ACCESSION   WP_125388216
VERSION     WP_125388216.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus cristatus
  ORGANISM  Streptococcus cristatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus cristatus"
                     /db_xref="taxon:45634"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33207
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtmiigag pagmtaalya arsnlkvall ergiyggqmn ntaeienypg yarisgpela
       61 ekmfeplenl gvehlfgqve kiedhgdfkk iitedeafet ktvilapgan hrhlgvpgee
      121 eynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdqlraqkl
      181 lqerafanek isfiwdsvvk eikgddrrvt nvvfenvktg qssesdfggv fiyvgldpvs
      241 dfvkdlgicd eagwivtdqh mktaiagiya igdvrqkdlr qittavgdga vagqevykyi
      301 teh
//
LOCUS       WP_125384653             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125384653
VERSION     WP_125384653.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33006
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiivgag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygyve niedqgdykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdelraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vifenvktgq vteqafggvf iyvgldpvsd
      241 fvkelniqdq agwivtdnhm ktgvdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125388791             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125388791
VERSION     WP_125388791.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33050
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiivgag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygyve niedqgdykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdelraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vvfenvktdq vteqafggvf iyvgldpvsd
      241 fvkdlniqdq agwivtdnhm ktavdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125390323             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus cristatus].
ACCESSION   WP_125390323
VERSION     WP_125390323.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus cristatus
  ORGANISM  Streptococcus cristatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus cristatus"
                     /db_xref="taxon:45634"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33242
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtmiigag pagmtaalya arsnlkvall ergiyggqmn ntaeienypg yarisgpela
       61 ekmfeplenl gvehlfgqve kiedhgdykk iitedevfet ktvilasgan hrhlgvpgee
      121 eynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdqlraqkl
      181 lqerafanek isfiwdsvvk eikgddrrvt svvfenvktg qisesdfggv fvyvgldpvs
      241 dfvkdlgicd eagwivtdqh mktsiagiya igdvrqkdlr qittavgdga vagqevykyi
      301 teh
//
LOCUS       WP_125390928             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125390928
VERSION     WP_125390928.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33006
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygyve niedqgdykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaksvtivh rrdelraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldpvsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125392453             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus gordonii].
ACCESSION   WP_125392453
VERSION     WP_125392453.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus gordonii
  ORGANISM  Streptococcus gordonii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus gordonii"
                     /db_xref="taxon:1302"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32944
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall eagipggqmn ntadvenypg yalisgpela
       61 ekmfeplenl gvehifghvq riedqgdskk vitedevyes ktviiatgaf hrqlnvpgea
      121 efnsrgvsyc avcdgaffrd edllvvgggd saveeaiflt qfaksvtivh rrdqlraqkv
      181 lqdrtfanek isfvwdsvve aihgddrkvt gvtfkniktg etsqadfggi fiyvgldpvs
      241 efvadlgird esgwivtddh mktsvagiya igdvrqkdlr qittavgdga iagqeaykyi
      301 tehe
//
LOCUS       WP_125395390             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125395390
VERSION     WP_125395390.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33037
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiivgag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygfve kiedcadykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdelraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vifenvktgq vteqafggvf iyvgldpvsd
      241 fvkelniqdq agwivtdnhm kttvdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125396922             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus gordonii].
ACCESSION   WP_125396922
VERSION     WP_125396922.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus gordonii
  ORGANISM  Streptococcus gordonii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus gordonii"
                     /db_xref="taxon:1302"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32999
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall eagipggqmn ntadvenypg yalisgpela
       61 ekmfeplenl gvehvfghvq riedqgdfkk vitedevyes ktviiatgaf hrqlnvpgea
      121 efnsrgvsyc avcdgaffrd edllvvgggd saveeaiflt qfaksvtivh rrdqlraqkv
      181 lqdrafanek isfvwdsvve aihgnerkvt gvtfkniktg etsqadfggi fiyvgldpvi
      241 efvadlgird esgwivtddh mktsvagiya igdvrqkdlr qittavgdga iagqeaykyi
      301 tehe
//
LOCUS       WP_125398828             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125398828
VERSION     WP_125398828.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32990
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiivgag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygyve niedqgdykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaksvtivh rrdqlraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldpvsd
      241 fvkelniqdq agwivtdnhm ktavngifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125406736             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus cristatus].
ACCESSION   WP_125406736
VERSION     WP_125406736.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus cristatus
  ORGANISM  Streptococcus cristatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus cristatus"
                     /db_xref="taxon:45634"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33196
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergiyggqmn ntaeienypg yarisgpela
       61 ekmfeplenl gvehlfgqve kiedhgdykk iitedevfet ktvilasgan hrhlgvpgee
      121 eynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdqlraqql
      181 lqerafanek isfiwdsvvk eikgddrrvt svvfgnvktg qssesdfggv fvyvgldpvs
      241 dfvkdlgicn edgwivtdqh mktaidgiya igdvrqkdlr qittavgdga vagqevykyi
      301 teh
//
LOCUS       WP_125408137             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125408137
VERSION     WP_125408137.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33071
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedrgnfke iitederfea ktviiasgan hrhlgvpgee
      121 gynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdrafanek irfvwdsvve sihgderkvt gvtfknvktg elsqaefggi fiyvgldpvs
      241 efakdlgitd eagwiltdhq mktsvagiya vgdvrqkdlr qittavgdga iasqeaykyl
      301 teqa
//
LOCUS       WP_125409246             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125409246
VERSION     WP_125409246.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33089
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedrgdfke iitederfea ktviiasgan hrhlgvpgee
      121 dynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdraftnek irfvwdsvve sihgderkvt gvtfknvktg evsqaefggi fiyvgldpvs
      241 efaadlgitd eagwiltdhq mktsvagiya vgdvrqkdlr qittavgdga iasqeaykyl
      301 teqa
//
LOCUS       WP_125410905             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus mitis].
ACCESSION   WP_125410905
VERSION     WP_125410905.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mitis
  ORGANISM  Streptococcus mitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus mitis"
                     /db_xref="taxon:28037"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32958
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehiygyve nvedhgdfkk vttddqtyet rtvivatgsk hrplgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdrafanek isfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldplsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrlkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125413558             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125413558
VERSION     WP_125413558.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32992
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygyve niedqgdykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdelraqkv
      181 lqdrafanek vnfiwdsvvk eikgdnrves vvfenvktgq vteqafggvf iyvgldpvsd
      241 fvkdlniqdq agwivtdnhm ktavdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125412040             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus intermedius].
ACCESSION   WP_125412040
VERSION     WP_125412040.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus intermedius
  ORGANISM  Streptococcus intermedius
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus anginosus group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus intermedius"
                     /db_xref="taxon:1338"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33073
     Region          2..301
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagvtaalya arsnlkvali ergipggqmn ntsdienypg ytnisgpela
       61 ekmfeplenl gvehlfgave kieqqgtikk vytednvfes ktliiatgaf hrhlgvpgee
      121 elnsrgvsyc avcdgaffrd edllvvgggd saveeavflt rfaktvtiih rrnelraqkl
      181 lqdrafanek irfiwdsvvq eikgdnrvqs vvvenvktge vsehefggvf iyvgldpvse
      241 fvkdlgitne agwivtdhhm ktaisgiyai gdvrekdlrq vttavgdgai agqevykyit
      301 enc
//
LOCUS       WP_125415057             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125415057
VERSION     WP_125415057.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33019
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygyve niedqgdykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vvfenvktgk vteqafggvf iyvgldpvsd
      241 fvkelnikdq agwivtdnhm ktavdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125421107             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125421107
VERSION     WP_125421107.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32990
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygyve niedqgdfkk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaksvtivh rrdelraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldpvsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125421147             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus mitis].
ACCESSION   WP_125421147
VERSION     WP_125421147.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mitis
  ORGANISM  Streptococcus mitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus mitis"
                     /db_xref="taxon:28037"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32972
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehiygyve niqdhgdfkt vmtddqayet rtvivatgsk hrplgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdrafanek isfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldplsd
      241 fvkelnirdq agwivtdnhm ktavdgifav gdvrlkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125423688             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hymenobacter rigui].
ACCESSION   WP_125423688
VERSION     WP_125423688.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter rigui
  ORGANISM  Hymenobacter rigui
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Hymenobacter rigui"
                     /db_xref="taxon:334424"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33740
     Region          10..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 matstpehik cliigsgpag ytaaiyaara nlkpvmyqgl qpggqltitn dvenfpgypd
       61 gimgpemmed lkkqaarfgt dirygiatsv dfsghphrvt idenleltad tiiiatgasa
      121 kwlglpseqr lngsgvsaca vcdgffyrgk dvaivgagdt aaeeatylan lcnkvymivr
      181 kgemraskim qkrvmdnpki evlwntvtde ilgehavdga rvknvldgtt rdlaiegffv
      241 aighepnski fqpylhhdeq gylktipgta ktnvdgvfac gdvqdytyrq avtaagsgcm
      301 aaldaeryla algdh
//
LOCUS       WP_125425225             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus mitis].
ACCESSION   WP_125425225
VERSION     WP_125425225.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mitis
  ORGANISM  Streptococcus mitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus mitis"
                     /db_xref="taxon:28037"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32993
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiivgag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygfve kiedcadykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdelraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vvfenvktgk vteqafggvf iyvgldpvsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125432981             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hymenobacter metallilatus].
ACCESSION   WP_125432981
VERSION     WP_125432981.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter metallilatus
  ORGANISM  Hymenobacter metallilatus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Hymenobacter metallilatus"
                     /db_xref="taxon:2493666"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33755
     Region          10..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpspehik cliigsgpag ytaaiyaara nlkpvmyqgl qpggqltitn dvenfpgypd
       61 gimgpemmed lkkqaarfgt dirygiatav dfsghphrvt idehleltad tiiiatgasa
      121 kwlglpseqr lngsgvsaca vcdgffyrgk dvaivgagdt aaeeatylan lcnkvymivr
      181 kgemraskim qkrvldnpki evlwntvtde ilgehavdga rvknvldgtt rdlaiegffv
      241 aighepnski fqpylhhdeq gylktipgta ktnvdgvfac gdvqdytyrq avtaagsgcm
      301 aaldaeryla algdh
//
LOCUS       WP_125434991             302 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sanguinis].
ACCESSION   WP_125434991
VERSION     WP_125434991.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sanguinis
  ORGANISM  Streptococcus sanguinis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Streptococcus sanguinis"
                     /db_xref="taxon:1305"
     gene            1..302
                     /gene="trxB"
     Protein         1..302
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32833
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedrgdfke iitederfea ktvivasgan hrhlgvpgee
      121 dynsrgvsyc avcdgaffrn edllvvgggd saveeaiflt rfaksvtivh rrdelraqkv
      181 lqdrafanek irfvwdsvve sihgderkvt gvtfknvktg etsqadfggi fiyvgldpvs
      241 efaadlgitd eagwiltdhq mktsvagiya vgdvrqkdlr qittavgdga iasqeaykyl
      301 te
//
LOCUS       WP_125440280             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hymenobacter perfusus].
ACCESSION   WP_125440280
VERSION     WP_125440280.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter perfusus
  ORGANISM  Hymenobacter perfusus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Hymenobacter perfusus"
                     /db_xref="taxon:1236770"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33678
     Region          10..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 matttpehik cliigsgpag ytaaiyaara nlnpvmyqgl qpggqltitn dvenfpgypd
       61 gimgpemmed lkkqaarfgt dirygiatsv dfsghphrvi vdekveltad tiiiatgasa
      121 kwlglpseqr lngsgvsaca vcdgffyrgk dvaivgagdt aaeeatylan lcnkvymivr
      181 kgemraskim qkrvtdnpki evlwntvtde ilgehavdga rvknvldgtt rdlaiegffv
      241 aighdpnski fqpylhhdeq gylktipgta ktnvdgvfac gdvqdftyrq avtaagsgcm
      301 aaldaeryla algdh
//
LOCUS       WP_125441316             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125441316
VERSION     WP_125441316.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32978
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiivgag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygyve niedqgdfkk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaksvtivh rrdelraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldpvsd
      241 fvkelnvqdq agwivtdnhm ktsvdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125443059             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus mitis].
ACCESSION   WP_125443059
VERSION     WP_125443059.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mitis
  ORGANISM  Streptococcus mitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus mitis"
                     /db_xref="taxon:28037"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32916
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehiyghve nvedhgsfkk vitddqtyet rtvivatgsk hrplgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdrafanek isfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldplsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrlkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125447307             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus cristatus].
ACCESSION   WP_125447307
VERSION     WP_125447307.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus cristatus
  ORGANISM  Streptococcus cristatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus cristatus"
                     /db_xref="taxon:45634"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33168
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtmiigag pagmtaalya arsnlkvall ergiyggqmn ntaeienypg yarisgpela
       61 dkmfeplenl gvehlfgqve kiedhgnykk iitedgafet ktvilasgan hrhlgvpgee
      121 eynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrdqlraqql
      181 lqerafanek isfiwdsvvk eikgddrrvt svvfenvktg qisesdfggv fvyvgldpvs
      241 dfvkdlgicd eagwiitdqh mktaidgiya igdvrqkdlr qittavgdga vagqevykyi
      301 teh
//
LOCUS       WP_125449728             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125449728
VERSION     WP_125449728.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33037
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygyve niedqgdykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vvfenvktgq iteqafggvf iyvgldpvsd
      241 fvkelniqdq agwivtdnhm ktcadgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125453263             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus mitis].
ACCESSION   WP_125453263
VERSION     WP_125453263.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mitis
  ORGANISM  Streptococcus mitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus mitis"
                     /db_xref="taxon:28037"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32968
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehiygyvk nvedhgdfkk vmtddqtyet htvivatgsk hrplgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdrafanek isfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldplsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrlkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125455372             303 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptococcus].
ACCESSION   WP_125455372
VERSION     WP_125455372.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33050
     Region          2..301
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagitaalya arsnlkvali ergipggqmn ntsdienypg ytnisgpela
       61 ekmfeplenl gvehlfgave kieqqgtikk vytednvfes ktliiatgaf hrhlgvpgee
      121 elnsrgvsyc avcdgaffrd edllvvgggd saveeavflt rfaktvtiih rrnelraqkl
      181 lqdrafanek ihliwdsvvq eikgdnrvqs vvvenvktge vsehefggvf iyvgldpvse
      241 fvkdlgitne sgwivtdhhm ktaisgiyai gdvrekdlrq vttavgdgai agqevykyit
      301 enc
//
LOCUS       WP_125456144             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus mitis].
ACCESSION   WP_125456144
VERSION     WP_125456144.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mitis
  ORGANISM  Streptococcus mitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus mitis"
                     /db_xref="taxon:28037"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32946
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehiyghve nvedhgsfkk vitddqtyet rtvivatgsk hrplgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdraftnek isfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldplsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrlkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125461372             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Rhodococcus
            erythropolis].
ACCESSION   WP_125461372
VERSION     WP_125461372.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus erythropolis
  ORGANISM  Rhodococcus erythropolis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus; Rhodococcus
            erythropolis group.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rhodococcus erythropolis"
                     /db_xref="taxon:1833"
     gene            1..>324
                     /gene="trxB"
     Protein         1..>324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtipstvhdv iivgsgpagy tagvytarae lapllfegtq fggalmttte venfpgfreg
       61 imgpdlmeqm reqalrfdtd irtedveeid lsgpiktvva ngetyaahai ilamgaaary
      121 lgipgeerll grgvsacatc dgfffrdqdi vvvgggdsam eeatfltrfa rsvtlvhrre
      181 efrasrimle rakanekirf ltnaepvevl gensvtglvv rdtvtgetst leitgmfvai
      241 ghdprselvk gqvdlddagy vrvapgstat sidgvfaagd lvdhtyrqai taagtgcsaa
      301 idaerwladr gditantlda aght
//
LOCUS       WP_125462105             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_125462105
VERSION     WP_125462105.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38819
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklvsqg hqvtvqrgag lnasipdsay eavgatlgea
       61 tdafgaqlvl kvvapndqel alinsgsvla gmlnpfnnel igkmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee recaegvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvqangv tivgptnlpa qvgadasaly arnlldfmkl lfdkdgalvi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_125465494             318 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Pseudomonas].
ACCESSION   WP_125465494
VERSION     WP_125465494.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33569
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgpalmqrmq ehaerfetei vfdhinavdl ankpftlrgd sgtytcdali vatgasaryl
      121 glpseetfmg kgvsacatcd gffyrnkpva vvgggntave ealylanias kvtlvhrrdt
      181 fraekilidk lharvaegki elklnatlde vlgdnmgvtg arlknndgsf deikvdgvfi
      241 aightpntsl fegqltlkdg ylvvhggreg natatnvegv faagdvadhv yrqaitsaga
      301 gcmaaldver yldglana
//
LOCUS       WP_125468089             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mangrovimonas spongiae].
ACCESSION   WP_125468089
VERSION     WP_125468089.1
KEYWORDS    RefSeq.
SOURCE      Mangrovimonas spongiae
  ORGANISM  Mangrovimonas spongiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Mangrovimonas.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Mangrovimonas spongiae"
                     /db_xref="taxon:2494697"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35376
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtienvkc liigsgpagy taaiyaaran mnpvlyqgtq pggqltttne venfpgypeg
       61 itgpemmiel qkqaqrfgtd vrdgwitkvd fsgdthkvwv neekeihcet viistgasak
      121 ylgldseqky lklgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rrdefraski mearvrnten ieilmntete evigdgqvvt gvkvknnqtn evteipatgf
      241 fvaighkpnt difkeyleld etgyiinkpg taktnvngvf vsgdaadhvy rqaitaagtg
      301 cmaaldaery laakdsefev ststyn
//
LOCUS       WP_125470867             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter aegrifaciens].
ACCESSION   WP_125470867
VERSION     WP_125470867.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter aegrifaciens
  ORGANISM  Achromobacter aegrifaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter aegrifaciens"
                     /db_xref="taxon:1287736"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38452
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkyvggk htvivergag taaryldeay eaagatlgsa
       61 qdalgaelvm kvrapsaael pqmksgavvv gmldpfdaeg iqqiaaaglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravvl gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgtggy arpmppawma
      241 rqaalvserc kqadivitpa lipgrpaptl vsaetvaamk pgsvlvdlav erggncplse
      301 kglvvekhgv tiigltnlpg lvatdasaly arniqdflkl iinadgalai qrddeivaac
      361 lvceggnvar rn
//
LOCUS       WP_125471023             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Achromobacter aegrifaciens].
ACCESSION   WP_125471023
VERSION     WP_125471023.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter aegrifaciens
  ORGANISM  Achromobacter aegrifaciens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Achromobacter aegrifaciens"
                     /db_xref="taxon:1287736"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34013
     Region          12..316
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mnaghsprha rvlilgsgpa gyaaavyaar anlrpvliag maqggqlmtt tdvdnwpadv
       61 hgvqgpdlmq rfqdhalrfg tdviadhvqs vdlsrrpftl rgeratytcd alivatgava
      121 rylgleseqa ymgrgvsgca tcdgffhrgr dvcvvgggnt aveealylsn iarsvtlvhr
      181 rntfraepim ldklhakveq glirlkldsv ldevlgdagg vtgvrirrls nascielevs
      241 gcfvaighrp stelfegqla ledgyivtqa grkglatmts vsgvfaagdv qdhvyrqait
      301 sagsgcmaal daqrfleqsa a
//
LOCUS       WP_125486091             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Edaphobacter aggregans].
ACCESSION   WP_125486091
VERSION     WP_125486091.1
KEYWORDS    RefSeq.
SOURCE      Edaphobacter aggregans
  ORGANISM  Edaphobacter aggregans
            Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia;
            Terriglobales; Acidobacteriaceae; Edaphobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Edaphobacter aggregans"
                     /db_xref="taxon:570835"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34326
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msenttrdtv ilgsgcsglt aaiyaarsnl kplvleghep ggqlsittlv enfpgwpegi
       61 qgpelienmk kqatrfgael rmahlnsidl tkhpfelnig ketihtrtli iasgasarwl
      121 nlpseqalig hgvsscatcd gfffsgkeia vigggdsame ealfltrfat kvtlinrter
      181 fraspimler amahpqiqfm tnttveevlg veekdvrglk lknrlseees vlpvsamflg
      241 ighipnakaf kglldldddg yiltknnvlt tlngeiipgv facgdiqdrr yrqaitaags
      301 gcmaalevek yleehgr
//
LOCUS       WP_125490268             522 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. WAC 04229].
ACCESSION   WP_125490268
VERSION     WP_125490268.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC 04229
  ORGANISM  Streptomyces sp. WAC 04229
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Streptomyces sp. WAC 04229"
                     /db_xref="taxon:2203206"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53014
     Region          13..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtghhathhp pqrvgvvaes ipgetrvaat patvrpllgl gyevvvesga gtasgfadda
       61 yaeagasige awaadvvlkv napsgeeiae lregaalval iapaqhpell ealaardvtv
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgavvr atdprpevad qvrslggeyl avdasqeast dgyaratsad
      241 ydraaaelyh rqagdvdivi ttalipgrpa prlltaadva amrpgsvvvd maaaqggnve
      301 gtvagrtvvt dngvtligyt dlasrlpaqa sqlfgtnlvn llalatpgrd grlvvdfddv
      361 vqravtvvra gavtwppppv avsaaptaae paapapapvp agksrltpag rfgliglgma
      421 itflliafap arlaenltvf alaviigyyv igkvhhalht plmsvtnais givvigallq
      481 vghestlvtv lsfvaillts vnifggfavt rrmlsmfsrg es
//
LOCUS       WP_125496692             323 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_125496692
VERSION     WP_125496692.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34345
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpelmdnmra qaerfgaelv pddivsvdlt geiktvtdts gtvhkakavi vatgsqyrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtiihrrdt
      181 lraskamqer afadpkikfi wdsevaeiqg dqklsglklr nvktgeltdl avtglfiaig
      241 hdprtelfqg qldldeegyl kvaspstrtn iagvfaagdv vdhtyrqait aagtgcsaal
      301 daerylaala dteqqaepek ttv
//
LOCUS       WP_125481375             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesobacillus subterraneus].
ACCESSION   WP_125481375
VERSION     WP_125481375.1
KEYWORDS    RefSeq.
SOURCE      Mesobacillus subterraneus
  ORGANISM  Mesobacillus subterraneus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Mesobacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Mesobacillus subterraneus"
                     /db_xref="taxon:285983"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34149
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseekiydvi iigagpagmt aavytsranl stlmlergvp ggqmanteev enypgfdhil
       61 gpelstkmfd hakkfgaeya ygdvkevidg keyktikagn keykarsiii sagaeykklg
      121 vpgeqelggr gvsycavcdg affkgkelvv vgggdsavee gvyltrfask vtivhrrdel
      181 raqkilqdra fandkidfiw nhtvkqindk dgkvgsvtlv stqdgaeqef aadgvfiyig
      241 mvpltkpfeg lgitnsngyi etneqmetkv pgifaagdir ektlrqivta tgdgsiaaqn
      301 aqhyveelie elkana
//
LOCUS       WP_125501504             522 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Streptomyces].
ACCESSION   WP_125501504
VERSION     WP_125501504.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..522
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53586
     Region          14..521
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msaqhpahph pprrigvvte stpgetrvaa tpatvrglrg lgyatvvepg agaaagygde
       61 ayaqagadig dawdaevvlk vnapsteeia rlrsgatlva lispaqrpdl leqlaargvt
      121 vlaldavpri sraqsmdvls smaniagyra vieaahvfgr fftgqvtaag kvppakvlva
      181 gagvaglaai gaasslgavv ratdprpeva dqvkslggey lavddtphea stdgyarqts
      241 adydraaaal yheqaqdvdi vittalipgr paprlltaad vaamkpgsvv vdmaaaqggn
      301 vegtiagrtv vtdngvtiig ytdlasrlpd qasqmfgtnv vnllalitpg kdgrpvldfd
      361 dvvqravtvv rsgqvtwppp pvavsaapqd tapeepaaap adperprftp aarygliglg
      421 mlatfllvay apaqlaenft vfalavvigf yvigkvhhal htplmsvtna isgivvigal
      481 vqighgnrlv tvlsfvaill tsvnvfggfa vtrrmlsmfs kg
//
LOCUS       WP_125501784             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter haemolyticus].
ACCESSION   WP_125501784
VERSION     WP_125501784.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter haemolyticus
  ORGANISM  Acinetobacter haemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acinetobacter haemolyticus"
                     /db_xref="taxon:29430"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33569
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdpeglt
       61 gpvlmermqa haerfgteiv ydhinevdlk trpfvlkgdm eeytcdalii atgataqylg
      121 leseaafmgq gvsacatcdg ffyknqnvmv vgggntavee alylsniaah vtlvhrrdsl
      181 rsekilqdhl fakekegkis iiwnhqvdev lgdktgvtsv rikstqdsst qdipvqglfv
      241 aighkpntgm fegqlnlrdg yiqvhsgtag nataasvegv faagdvadsi yrqaitsags
      301 gcmaaldaek yldnls
//
LOCUS       WP_125505347             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Streptomyces].
ACCESSION   WP_125505347
VERSION     WP_125505347.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34099
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfqdgim
       61 gpelmdnmra qaerfgaelv pddvvsvdlt geiktvtdta gtvhkakavi vatgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfi wdsevaeaqg dqklsglklr nvktgelsdl pvtglfiaig
      241 hdprtelfkg qleldeegyl kvdapstrtn vtgvfgagdv vdhtyrqait aagtgcaaal
      301 daerylaalt dgekpepekt av
//
LOCUS       WP_125524329             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. WAC 05379].
ACCESSION   WP_125524329
VERSION     WP_125524329.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC 05379
  ORGANISM  Streptomyces sp. WAC 05379
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces sp. WAC 05379"
                     /db_xref="taxon:2203207"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34244
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfqdgim
       61 gpelmdnmrs qaerfgaelv pddivnvdls geiktvtdta gtvhrakaii vatgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfv wdsevaevqg eqklsglklr niktgelsdl avtglfiaig
      241 hdprtelfkg qleldeegyl kvsapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflsala deekaepekt pv
//
LOCUS       WP_125535816             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter baumannii].
ACCESSION   WP_125535816
VERSION     WP_125535816.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33706
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdpeglt
       61 gpvlmdrmqa haerfgtelv ydhinevdln vrpfvlkgdm deytcdalii atgataqylg
      121 leseqkfmgq gvsacatcdg ffyknqnvmv vgggntavee alylsniaeh vtlvhrrdsl
      181 rsekilqdhl fakekegkis ivwnheveev lgdntgvtgv rlkstkddsk qevqvqglfi
      241 aighkpntsm fegqlnlrdg yiqvqsgtsg natatsvagv faagdvadsi yrqaitsass
      301 gcmaaldaek yldnl
//
LOCUS       WP_125537264             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_125537264
VERSION     WP_125537264.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34022
     Region          6..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseirevvii gsgpagytaa lytaraqlkp llfgssifvg gsltttteve nfpgfpdgvd
       61 gpvlmenmra qaekfgaemi dddivevdlt gnvklltdsa gtvhraktvi iatgsgyrkl
      121 glpkedelsg rgvswcatcd gfffrdrdiv vvgggdtame eatfltrfah svtvvhrrst
      181 lraskvmqdr afaddkisfa fdseiaeike kggmlggvvl rdvftgatrd ldvtglfiai
      241 ghdprtelfk gqlaldtdgy itvaspttrt slpgvfaagd vvdhtyrqai taagtgaaaa
      301 ldaerylaag saaksegape avpa
//
LOCUS       WP_125541511             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_125541511
VERSION     WP_125541511.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53636
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gylhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydaiafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_125542047             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_125542047
VERSION     WP_125542047.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33730
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmrg qaerfgaeli addivsvdlt geiktvtdta gtvhrakavi vatgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtaie eatflsrfak svtvvhrrda
      181 lraskamqdr afadpkirfa wdsevavihg eqklsgltlr ntktgetsel pvtglfiavg
      241 hdprtelfkd qlelddegyl kvdapstrtn vtgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaals haekahatv
//
LOCUS       WP_125552009             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Loigolactobacillus jiayinensis].
ACCESSION   WP_125552009
VERSION     WP_125552009.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus jiayinensis
  ORGANISM  Loigolactobacillus jiayinensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Loigolactobacillus jiayinensis"
                     /db_xref="taxon:2486016"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34293
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtkqadvvvi gagpggltaa lyasrsnlsv iivdrgiygg qmnntaeien ypgfssvlgp
       61 dlaqkmydsa trfgaeyvyg nvtdvedqgq yklihtddgd ykakavviat gadhrklgvp
      121 geqeysgrgv sycavcdgaf fknrevavig ggdsaveegl ylaqlaskvt iihrrdqlra
      181 qkiiqqrafd nekvefvwna nteeikgddq kvtgvrytdk vtgeehvlpa sgafiyvgid
      241 altdafknln ildekgwvvt dehmrtatpg ifaigdvrqk dlrqittavg dggvagqqtf
      301 nyiqelddql knevpak
//
LOCUS       WP_125550699             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Loigolactobacillus zhaoyuanensis].
ACCESSION   WP_125550699
VERSION     WP_125550699.1
KEYWORDS    RefSeq.
SOURCE      Loigolactobacillus zhaoyuanensis
  ORGANISM  Loigolactobacillus zhaoyuanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Loigolactobacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Loigolactobacillus zhaoyuanensis"
                     /db_xref="taxon:2486017"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34144
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtkqadvvvi gagpggltaa lyasrsnlsv iivdrgiygg qmnntaeien ypgfssvlgp
       61 dlaqkmydga trfgaeyvyg nvtdvedqge fklvhtddgd yqakavviat gadhrklgvp
      121 geqdysgrgv sycavcdgaf fknrevavig ggdsaveegl ylaqlaskvt iihrrdqlra
      181 qkiiqqrafd npkidfvwna nteeilgdeq kvtgvrytdk vtgvehtlpa sgtfiyvgid
      241 altdafknln ildekgwvvt ddhmqtatpg vfaigdvrqk dlrqittavg dggmagqqvf
      301 nyiqelddka khevpak
//
LOCUS       WP_125553323             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Salibacterium salarium].
ACCESSION   WP_125553323
VERSION     WP_125553323.1
KEYWORDS    RefSeq.
SOURCE      Salibacterium salarium
  ORGANISM  Salibacterium salarium
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Salibacterium salarium"
                     /db_xref="taxon:284579"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34177
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseekiydvi iagagpagmt aavytsraem stlmlergip ggqvantedv enypgfdhil
       61 gpdlsnkmft hakkfgaeya ygdvkeiedg keykivragn keyktrsiiv stgavykqig
      121 vpgeqelggr gvsycavcdg affrdkeivv vgggdsavee avyltrfask vtvihrrdel
      181 raqkilqqra fenekiefkw shvvkeingk dgkvgsvtlt dlksgedyef etqgafiyig
      241 mlplndavkg lgiineegyi etneemetki pgifaagdlr ekslrqivta tgdgsvaaqt
      301 aqqyveelnn tvna
//
LOCUS       WP_125559965             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Salibacterium salarium].
ACCESSION   WP_125559965
VERSION     WP_125559965.1
KEYWORDS    RefSeq.
SOURCE      Salibacterium salarium
  ORGANISM  Salibacterium salarium
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Salibacterium salarium"
                     /db_xref="taxon:284579"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34306
     Region          8..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseqekiydv iiagagpagm taavytsrae mstlmlergi pggqvanted venypgfdhi
       61 lgpdlsnkmf thaqkfgaey aygdvkeied gkeyktvkag nkeyktrsii vstgavykqi
      121 gvpgeqelgg rgvsycavcd gaffrnkeiv vvgggdsaie eavyltrfas kvtvihrrde
      181 lraqkilqqr afvndkiefk wshivkeing kdgkvgsvtl tdlnsgedye fetegafiyi
      241 gmlplndavk gldiineegy vetneemetk ipgifaagdl rekslrqivt atgdgsvaaq
      301 taqqyveeln nkvna
//
LOCUS       WP_125561236             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Salibacterium salarium].
ACCESSION   WP_125561236
VERSION     WP_125561236.1
KEYWORDS    RefSeq.
SOURCE      Salibacterium salarium
  ORGANISM  Salibacterium salarium
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salibacterium salarium"
                     /db_xref="taxon:284579"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33166
     Region          1..290
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtaavytsra kmktllieks vaggqvakte eienypgfks ilgpdlsnem fehskifgak
       61 yvnedvigie esypfksvlt nhgnhqtksv iiasgaehrp lgvpgekels gagvsycavc
      121 dgafftdqei vvvgggdsav eeaifltrfa skvtiihrrd qlraqkilqk raqdnekinf
      181 iwnhivtevc gkgmvegvki knvlnnetdf ypsqgvfiyi gmdpftepfk nldvtnesgy
      241 viadenmktt vpgifsagdv nekmlrqvit atgdgsiaai ssqqyvenld eevkekkevl
      301 ard
//
LOCUS       WP_125561331             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudoalteromonas rubra].
ACCESSION   WP_125561331
VERSION     WP_125561331.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas rubra
  ORGANISM  Pseudoalteromonas rubra
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudoalteromonas rubra"
                     /db_xref="taxon:43658"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33836
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdakhckll ilgsgpagyt aavyaaranl npvlitgmqq ggqlttttev enwpgdahgl
       61 tgpalmdrmk ehaerfetei ifdhinkvdv tkrpftltgd qgtytcdali iatgasakyl
      121 glesetnfqg rgvsacatcd gffyrgqkva vvgggntave ealylsniae evhvihrrdt
      181 frsekilsdr lmekanngnv vlhlnktlde vlgddmgvtg irikdtgsda teqldlagvf
      241 iaighkpntd mfagqlemkd gylvvqsgln gnatqtsieg vfaagdvsdh iyrqaitsag
      301 tgcmaaldae ryldnlk
//
LOCUS       WP_125565500             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Companilactobacillus insicii].
ACCESSION   WP_125565500
VERSION     WP_125565500.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus insicii
  ORGANISM  Companilactobacillus insicii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Companilactobacillus insicii"
                     /db_xref="taxon:1732567"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33385
     Region          4..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mktydvvvig agpggltaal yasranlsvm ildrgiyggq mnntaeieny pgfesilgpd
       61 lsekmynssi rfgadfgygt vesvedkgtt kivhtddgdy eakvviiatg sqykkigvpg
      121 eeelsgrgvs ycavcdgaff kgkdvavigg gdsaveegvy ltqlaksvti ihrrdqlraq
      181 kilqdrafkn dkikfvwnad vkeivekdgk vggvryidke tgdehivpas gafiyvgiqp
      241 mtdsfkslgi ldedgwintt ehmetkvpgv yaigdvrkkd lrqiatavge ggiagqeafn
      301 yiqtlgdkvt a
//
LOCUS       WP_125568432             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides baekrokdamisoli].
ACCESSION   WP_125568432
VERSION     WP_125568432.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides baekrokdamisoli
  ORGANISM  Nocardioides baekrokdamisoli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Nocardioides baekrokdamisoli"
                     /db_xref="taxon:1804624"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52221
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresk pgetrvaatp atvaqliglg ydviveagag slasfldday aaagatvgsn
       61 adawnsdvvf rvngptldev asipdgvtiv ctlapalnpe lvdalagrpv tvlamdavpr
      121 israqsldvl ssmaniagyr avveaahqfg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdpraev adqvkslgge yllvdveqeq stdgyakats eaydrraaei
      241 yseqaadcdi iittalipgr paprlltaad vasmksgsvi vdmaasnggn vegtvagevv
      301 ttangvtiig ytdlvgrlpq qssqlygqnl vnltklvtpg kdgqftldle dvvqrgiavv
      361 vrgekmwppp qvqvsaapaa apaavvekap ekatmtprgk lilalagiav fgllnaiapt
      421 telrthftvl mlsivigyyv igkvahalht plmsvtnais gvvvvgalls vaqgnttvti
      481 lsavaillas invfggfavt rrmlvmfskg h
//
LOCUS       WP_125572136             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus
            songhuajiangensis].
ACCESSION   WP_125572136
VERSION     WP_125572136.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus songhuajiangensis
  ORGANISM  Lacticaseibacillus songhuajiangensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Lacticaseibacillus songhuajiangensis"
                     /db_xref="taxon:1296539"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33244
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mskevdvvvi gagpggmtaa lyasrsnlsv vmldrgiygg qmnntatien ypgfpsvmgp
       61 dlgekmfaga tqfgaeyeyg nvtgietdgd nkivhtddgd yiakavilat gseykklgip
      121 geqeyagrgv sycavcdgaf fkgqdlivig ggdsaieegl yltqlansvt vihrrdqlra
      181 qpimqkrafa ndkmkfiwna qveeilggdd gvtgvrykdk vtgeekvvdg kgtfiyvgik
      241 pmtdafanlg vldeqgwviv ddhmqtkvpg vfaigdvrqk elrqittaig dgglagqgvf
      301 nyiqglkdsa lk
//
LOCUS       WP_125568522             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nocardioides baekrokdamisoli].
ACCESSION   WP_125568522
VERSION     WP_125568522.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides baekrokdamisoli
  ORGANISM  Nocardioides baekrokdamisoli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Nocardioides baekrokdamisoli"
                     /db_xref="taxon:1804624"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34339
     Region          7..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseprnviii gsgpsgytaa vyaaraalnp lvfegsvtag galmntteve nfpgfrdgim
       61 gpelmenmra qaerfgaeli addvievdlt gdikivktae atyeatavil amgsgykklg
      121 lpdedrlsgr gvswcatcdg fffrnqhiav vgggdsalee atflsrfgsk vsllvrrdel
      181 rgskimqdra iadekieivw nsavdslnge ngldsvtlvd tvtgekreld atglfiaigh
      241 eprseliggq vdlddegyvl tqpgstatnl egvfaagdlv dhtyrqavta agsgcaaald
      301 aerwlavreh hasqnrasag nvpata
//
LOCUS       WP_125575675             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Levilactobacillus angrenensis].
ACCESSION   WP_125575675
VERSION     WP_125575675.1
KEYWORDS    RefSeq.
SOURCE      Levilactobacillus angrenensis
  ORGANISM  Levilactobacillus angrenensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Levilactobacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Levilactobacillus angrenensis"
                     /db_xref="taxon:2486020"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32885
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknydvivig agpggmtgal yasranlsvl mldrgiyggq mnntaaieny pgfksvlgpd
       61 lakdmyegst qfgaefaygs veaiedhgdh kvvktddgdy aakaviigtg seykklgvpg
      121 edkfggrgvs ycavcdgaff knrevavvgg gdsaveesly laglaskvtv fvrrdqlraq
      181 kilqdrafan dkiefvwntn vteilgddmk vtgvaiknnq tgetgekavs gvfiyvgnlp
      241 mtdafkdlgi tddagwiktd ehmqtavagi faigdvrqkd lrqittavgd ggiagqqafs
      301 yiedlkaaaa k
//
LOCUS       WP_125573290             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Levilactobacillus huananensis].
ACCESSION   WP_125573290
VERSION     WP_125573290.1
KEYWORDS    RefSeq.
SOURCE      Levilactobacillus huananensis
  ORGANISM  Levilactobacillus huananensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Levilactobacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Levilactobacillus huananensis"
                     /db_xref="taxon:2486019"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33091
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknydvivig agpggmtgal yasranlsvl mldrgiyggq mnntaaieny pgfksvlgpd
       61 lskdmyegst qfgaefaygs vediedhgdy kivktddgdy kagaviiatg seykklgvpg
      121 edkfggrgvs ycavcdgaff knrevvvigg gdsaieegly laglaskvti ihrrdqlraq
      181 kilqdrafan dkiefvwntn vteilgddmk vtgvatknnl tgetgeiaas gvfiyvgtlp
      241 mtssfttmgi tddagwiktd ndmatavpgv faigdvrqkt lrqittavgd ggiagqeafs
      301 yletlkdkta saq
//
LOCUS       WP_125577237             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lapidilactobacillus mulanensis].
ACCESSION   WP_125577237
VERSION     WP_125577237.1
KEYWORDS    RefSeq.
SOURCE      Lapidilactobacillus mulanensis
  ORGANISM  Lapidilactobacillus mulanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lapidilactobacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Lapidilactobacillus mulanensis"
                     /db_xref="taxon:2485999"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34055
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mskqydvvii gagpggmtaa lyasrsnlsv lmldrgiygg qmnntaeien ypgfksilgp
       61 elgekmyass tqfgaeytyg tvsdvidhga yktvktdegd yeakavviat gaehrhlgvp
      121 gedqysgmgv sycavcdgaf fkdrevavig ggdsaveegi ylanlaskvt vvhrrdqlra
      181 qkilqhrafa ndkmefvwna qveeivgdgk kiesvkyrdk etgeekslpa egvfiyvgie
      241 pmtepfknlg ilneagwiet ddttrtkvpg vfavgdvrdk hlrqianavg egglagqavf
      301 dylqelgdse iaatek
//
LOCUS       WP_125580966             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus suibinensis].
ACCESSION   WP_125580966
VERSION     WP_125580966.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus suibinensis
  ORGANISM  Lacticaseibacillus suibinensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Lacticaseibacillus suibinensis"
                     /db_xref="taxon:2486011"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33556
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 makqydvivi gagpggmtaa lyasranlsv lmldrgiygg qmnntaaven ypgfssilgp
       61 dlsqkmydga tqfgaeyayg nvtdlrdega mkrvvtdege feakaviiat gaehrklgip
      121 geeefggrgv sycavcdgaf fknqevavig ggdsaveegl ylaglaskvt vihrrdqlra
      181 qqiiqqrafa ndkmhfvwna dvqeilgddq kvtgvqykdk vtsethvipa agafiyvgik
      241 pltdsfknvg vldeagwipt ndlmetrvpg ifaigdvrak glrqiatavg eggqagqsaf
      301 nyiqslqdat ltaatk
//
LOCUS       WP_125584789             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus jixianensis].
ACCESSION   WP_125584789
VERSION     WP_125584789.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus jixianensis
  ORGANISM  Lacticaseibacillus jixianensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Lacticaseibacillus jixianensis"
                     /db_xref="taxon:2486012"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33968
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 makqydvivi gagpggmtaa lyasranlsv lmldrgiygg qmnntaaven ypgfksilgp
       61 dlgqqmydga tqfgaeyayg nvtdltddgp lktvvtdege fqakaviiat gaehrklgvp
      121 geeeyggrgv sycavcdgaf fkgqevavig ggdsaveegl ylaglaskvt vihrrdqlra
      181 qkiiqqrafa ndkmhfvwna qteeilgddn kvtgvryrdk vtgeehvlpa agafiyvgik
      241 pltdsfkhag vldedgwipt delmatrvpg ifaigdvrak nlrqiatavg eggqagqsaf
      301 nyiqslqdeq lkagavpeak
//
LOCUS       WP_125583266             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Levilactobacillus cerevisiae].
ACCESSION   WP_125583266
VERSION     WP_125583266.1
KEYWORDS    RefSeq.
SOURCE      Levilactobacillus cerevisiae
  ORGANISM  Levilactobacillus cerevisiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Levilactobacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Levilactobacillus cerevisiae"
                     /db_xref="taxon:1704076"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33040
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknydvivig agpggmtgal yasranlsvl mldrgiyggq mnntaaieny pgfksvlgpd
       61 lakdmydgst qfgaefaygs vetiedhgdh kvvktddgdy sakaviigtg seykklgvpg
      121 edkfggrgvs ycavcdgaff knrevavigg gdsaveegly laglaskvti fvrrdqlraq
      181 kilqdrafan ekiefvwnts vteilgddmk vtgvatknnq tgetgekavs gvfiyvgtlp
      241 mtdaftglgi tddagwiktd ehmrtavpgl faigdvrqkd lrqittavgd ggiagqgtfn
      301 yieslkstat ssn
//
LOCUS       WP_125587699             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Companilactobacillus jidongensis].
ACCESSION   WP_125587699
VERSION     WP_125587699.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus jidongensis
  ORGANISM  Companilactobacillus jidongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Companilactobacillus jidongensis"
                     /db_xref="taxon:2486006"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33270
     Region          4..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mktydvvvig agpggltaal yasranlsvm ildrgiyggq mnntaeieny pgfdsilgpd
       61 lsekmynsst rfgadfgyga vesvedkgtt kivhtddgdy eakvviiatg sqykkigvpg
      121 eeqlsgrgvs ycavcdgaff kgkdvavigg gdsaveegiy ltqlassvti ihrrdqlraq
      181 kilqdrafkn dkikfvwnad vkeivekdgk vggvryidke tgdehvvpas gafiyvgiep
      241 mtepfkslgv ldengwidtt thmetkvpgv yaigdvrkkd lrqiatavge ggiagqeafn
      301 yiqtlgdkvt a
//
LOCUS       WP_125592827             414 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Companilactobacillus
            baiquanensis].
ACCESSION   WP_125592827
VERSION     WP_125592827.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus baiquanensis
  ORGANISM  Companilactobacillus baiquanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Companilactobacillus baiquanensis"
                     /db_xref="taxon:2486005"
     gene            1..414
                     /gene="trxB"
     Protein         1..414
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=44469
     Region          21..291
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
     Region          311..410
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 msevydlliv gagpgglaag iygsraklks aildknaepg gqasttdeme nypgfykgtt
       61 gpgimkefad hakafgtefl rgtvdevdfs gpikkvhtqq gdtyeskvvi lspgatprki
      121 nvkgeaelrg kgvsycatcd adffvdldvv vvgngdaaie eamyltkfae tvtiivihee
      181 gnldcnkasa ekamknpklk wvwnstveei agdelvekvv lknintgels dletngvfvf
      241 igtephtdfl kgkvelddrg ylvandmmet nvpgvyavgd arakylrqvv taaadgaiaa
      301 saaekylsel etlqndvldv skekpvilaf wapqveesid siaivdkvve ekdgavglvk
      361 ldtyrakkta tqykvseipt ivlfkdgkdv griegaknit pdavenilke svev
//
LOCUS       WP_125595662             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_125595662
VERSION     WP_125595662.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33676
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslnp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmrd qaerfgaelv pddvvavdlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtivhrrds
      181 lrasktmqdr afadpkikfa wdsevaeihg eqklsgltlr ntktgetsel pvtglfiavg
      241 hdprtelftg qldlddegyl kvdapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala dtepaaatv
//
LOCUS       WP_125600706             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lapidilactobacillus achengensis].
ACCESSION   WP_125600706
VERSION     WP_125600706.1
KEYWORDS    RefSeq.
SOURCE      Lapidilactobacillus achengensis
  ORGANISM  Lapidilactobacillus achengensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lapidilactobacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Lapidilactobacillus achengensis"
                     /db_xref="taxon:2486000"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33964
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtkqydvivi gagpggmtaa lyasrsnlsv lmldrgiygg qmnntaeien ypgftsilgp
       61 elgekmyasa tqfgaeytyg tvktvedhhd yktvitdege yqakaviiat gaehrhlgvp
      121 geedysgkgv sycavcdgaf fkgrevavig ggdsaveegi ylaqlaskvt ivhrrdqlra
      181 qkilqqrafa ndkiefvwna qveaiegdgq kitsvryrdk vsglekqlpa sgvfiyvgie
      241 pmtepfralg vldeagwipt deqtrtkvpg vfavgdvrak hlrqianavg eggqagqaaf
      301 dfiqelqdeq sgrtv
//
LOCUS       WP_125599998             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas salmonicida].
ACCESSION   WP_125599998
VERSION     WP_125599998.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53238
     Region          22..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrlt rlglaalllt tcfgasglaq adeanskgki earselfakd hvdqfsswke
       61 tsesatrtda laedpqmvvl wggypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggseivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eqyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqskemlqgi vqqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaqmk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llatkgishe ialpdistke kaqaalgmdm kqmnsdkaqf lkttapawda eakaagrlaq
//
LOCUS       WP_125606873             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas salmonicida].
ACCESSION   WP_125606873
VERSION     WP_125606873.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53347
     Region          22..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrlt rlglaalllt tcfgasglaq adeanskgki earselfakd hvdqfsswkd
       61 tseskertda laedpqmvvl wggypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eqyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqskemlqgi vqqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaqmk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llatkgishe ialpdistke kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_125608267             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lapidilactobacillus bayanensis].
ACCESSION   WP_125608267
VERSION     WP_125608267.1
KEYWORDS    RefSeq.
SOURCE      Lapidilactobacillus bayanensis
  ORGANISM  Lapidilactobacillus bayanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lapidilactobacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Lapidilactobacillus bayanensis"
                     /db_xref="taxon:2485998"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34126
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtkkydvivi gagpggmtaa lyasrsnlsv lmldrgiygg qmnntaeien ypgfksilgp
       61 elseqmyass iqfgaefayg tvsdvedhgd yktvktddgd ydakaiviat gaehkhlnvp
      121 gedtysgmgv sycavcdgaf fkhrevavig ggdsaveegl ylaqlaskvt ivhrrdqlra
      181 qqilqrrafa ndkiefvwna qveeivgdgr kienvkyrdk vtgtekllpa sgvfiyvgve
      241 pmtsafknlg ilndagwiet neethtkvpg ifavgdvrek hlrqianavg egglagqavf
      301 eylqglgdqa eiaattk
//
LOCUS       WP_125613073             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Specibacter cremeus].
ACCESSION   WP_125613073
VERSION     WP_125613073.1
KEYWORDS    RefSeq.
SOURCE      Specibacter cremeus
  ORGANISM  Specibacter cremeus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Specibacter.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Specibacter cremeus"
                     /db_xref="taxon:1629051"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34478
     Region          21..325
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkkeehppvs tevttasdvr dviivgsgpa gytaaiytar anlkplmiag svtaggelmn
       61 ttdvenfpgf pdgimgpdlm enfgkqaerf gtevmyddvd svaldgdvkt vvladgqefk
      121 artviistgs ayrelglade krlsghgvsw catcdgfffk dqdiaviggg dsameeatfl
      181 tkfartvtvv hrretlrask imadralanp kinfvwnsev igidgdakvs nlrlnnlvtg
      241 eksdlpvtgv fvaigndpri elvrdqldlt negtiavegr ssktsipgvf aagdvvdpty
      301 rqaitasgsg cvaaldvehy laahe
//
LOCUS       WP_125623978             328 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Streptomyces].
ACCESSION   WP_125623978
VERSION     WP_125623978.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34669
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfrdgim
       61 gpdlmdnmra qserfgaeli pddvtavdlt gdiktvtdsa gtvhkaravi iatgsqhrkl
      121 glpredelsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtvihrrdt
      181 lrasramqer afadpkitfa ydsevaeihg dpkltgvtlr stktgetrel pvtglfiavg
      241 hdprtelftg qlnlddegyl tvdapsthtn lpgvfaagdv vdhtyrqait aagtgcsaal
      301 daerylaals dtsaehtpep ektaaatv
//
LOCUS       WP_125625824             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. WAC 00631].
ACCESSION   WP_125625824
VERSION     WP_125625824.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC 00631
  ORGANISM  Streptomyces sp. WAC 00631
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Streptomyces sp. WAC 00631"
                     /db_xref="taxon:2203201"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54024
     Region          4..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mvqrlgvvae satgetrvaa tpdtvrrlms lgfdvlvesg agqrsdfade lyaeagakig
       61 sredawrsdv vlkvdpptae eigrlrddat ligmigpalr pelvetltqr sitvlamdav
      121 prisraqsld vlssmaniag yravieaahr fgrfftgqvt aagkvppakv lvagagvagl
      181 aaigaakglg aivratdprp evadqvrsmg geflaveveq easadgyaka tsedydrraa
      241 eiyteqaaev divittalip grpaprlita ehvanmrpgs vivdmaaaqg gnvagsvage
      301 vvvtdngvti igytdlpgrl paqasqlygt nlvnllkllt pgkdgqivld fddvvqrsmt
      361 vvragektwp pppvqvsavp aprqpdaaar pagegsaaga rgkqpmprnr klaigglsaf
      421 glflltafsp sqlagnftvf vlaivigyyv igsvhhalht plmsvtnais giivvgallq
      481 ighgntvvtv lsfaavllas inifggfavt rrmlgmfskd
//
LOCUS       WP_125630055             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_125630055
VERSION     WP_125630055.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34156
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgim
       61 gpelmdnmra qaerfgaeli pddvvavdls geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkitfv wdsevaevqg dqklaglklr nvktgelsdl pvtglfiaig
      241 hdprtelfkg qldldpegyl kveapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaals dedkaepekt tv
//
LOCUS       WP_125634574             523 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Streptomyces].
ACCESSION   WP_125634574
VERSION     WP_125634574.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53404
     Region          13..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtghqpahqp pqrvgvvaes lpgetrvaat pstvrlllgl gyevvvesga gtasgfgdea
       61 yaeagarvge awtadvvlkv naptdeeisa lragttlval iapaqrpell ealaaravtv
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgaivr atdprpevad qvrslggeyl avnvtqeest dgyaratsad
      241 ydraaaelyh eqardvdvvv ttalipgrpa prlltaadva amkpgsvvvd maaaqggnve
      301 gtvagrsvvt dngvtligyt dlasrlpaqa sqlfgtnlvn llrlltpggd grlvvdfddv
      361 vqravtvvra gavtwppppv svsaappata paaataapvg akpsrltpag rfsliglgml
      421 atflmvafap aqlaenftvf alavvigyyv igkvhhslht plmsvtnais givvigallq
      481 ighesalvtv lsfvaillts vnifggfavt rrmlsmfsrg esr
//
LOCUS       WP_125640433             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Levilactobacillus tangyuanensis].
ACCESSION   WP_125640433
VERSION     WP_125640433.1
KEYWORDS    RefSeq.
SOURCE      Levilactobacillus tangyuanensis
  ORGANISM  Levilactobacillus tangyuanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Levilactobacillus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Levilactobacillus tangyuanensis"
                     /db_xref="taxon:2486021"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32802
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknydvivig agpggmtgal yasranlsvl mldrgiyggq mnntaaveny pgfksvlgpd
       61 lakdmydgst qfgaefaygs veaiedhgdh kvvktddgdy takavivatg seykklgvpg
      121 enefggrgvs ycavcdgaff knrdvvvvgg gdsaieegiy laglaskvti vvrrdqlraq
      181 kilqdrafan ekiefvwdtn vteilgdemk vtgvatlnnk tgekgeiaan gvfiyvgtlp
      241 mteaftgmgi tddagwiktd idmktavpgi faigdvrqkt lrqittavgd ggiagqeafg
      301 yieslksaaa ak
//
LOCUS       WP_125638641             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. WAC06614].
ACCESSION   WP_125638641
VERSION     WP_125638641.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC06614
  ORGANISM  Streptomyces sp. WAC06614
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces sp. WAC06614"
                     /db_xref="taxon:2487416"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33632
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmra qaerfgaelv pddvvsvdlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtivhrrds
      181 lraskamqdr afadpkitfa wdsevaeihg eqkltgltlr ntktgetsel pvtglfiavg
      241 hdprtelfkg qleldeegyl tvdapstrts vsgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaalt daehaaatv
//
LOCUS       WP_125640675             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nonomuraea sp. WAC 01424].
ACCESSION   WP_125640675
VERSION     WP_125640675.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea sp. WAC 01424
  ORGANISM  Nonomuraea sp. WAC 01424
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Nonomuraea sp. WAC 01424"
                     /db_xref="taxon:2203200"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33421
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa vysaraelkp lvfegsvtag galmnttdve nfpgfpdgim
       61 gpdlmdnlrk qaerfggelv addvvevdle anpkvvrtht dtyyaksvil tmgsgyrelg
      121 lenekrlsgh gvswcatcdg fffrnkdivv vgggdtamee atfltrfgrm vtvvhrrgel
      181 raskimqera fandkirfvw dsevvdvlgd gkveavklrn vetgeecela tdalflaigh
      241 dprtdlvkgq ieldengyik vaspstatni dgvfaagdvv dhtyrqaita agtgcaasld
      301 serwlannek
//
LOCUS       WP_125651158             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lapidilactobacillus gannanensis].
ACCESSION   WP_125651158
VERSION     WP_125651158.1
KEYWORDS    RefSeq.
SOURCE      Lapidilactobacillus gannanensis
  ORGANISM  Lapidilactobacillus gannanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lapidilactobacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Lapidilactobacillus gannanensis"
                     /db_xref="taxon:2486002"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33944
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvkkydviii gagpggmtaa lyasranlsv lmldrgiygg qmnntaaien ypgfasilgp
       61 elgekmyasa tqfgaeytyg tvksvvdhqd hktiitddge yeakaviiat gaehrhlgvp
      121 geeqysgrgv sycavcdgaf fknkevavig ggdsaveegi ylaqlaskvt ivhrrdslra
      181 qkilqrrafa nekiefvwna dvqeivgddq kitavhyrdk vtneehdlpa tgvfiyvgve
      241 pmtapfkdlg ildeagwikt detthtavpg ifavgdvrqk hlrqianavg egglagqaaf
      301 dylqelqdet qsvea
//
LOCUS       WP_125655658             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingomonas sp. 2R-10].
ACCESSION   WP_125655658
VERSION     WP_125655658.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. 2R-10
  ORGANISM  Sphingomonas sp. 2R-10
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Sphingomonas sp. 2R-10"
                     /db_xref="taxon:3045148"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33567
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mlvlgsgpag lsaaiygara gmepivvqgi qpggqlmttt dvenypgfrd vvqgpwlmge
       61 mqaqaehvgt rmmwdtivdv dvtrrpfrlt gdsgdvyege vlviatgaqa rwlgldseel
      121 lkgkgvsaca tcdgffyrgk kvavigggnt aveealyltn hsddvtiihr rdsfraeril
      181 qqrlfasdki gvlwnkqver fvgggdphgl vgielkdtvt gelsmldvdg gfvaighhpa
      241 telfrghial dddgyiavet gstrtsvpgv facgdvmdkv yrqavtaagt gcmaaldaer
      301 flqavefddi aqaae
//
LOCUS       WP_125618940             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinomadura sp. WAC 06369].
ACCESSION   WP_125618940
VERSION     WP_125618940.1
KEYWORDS    RefSeq.
SOURCE      Actinomadura sp. WAC 06369
  ORGANISM  Actinomadura sp. WAC 06369
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Thermomonosporaceae; Actinomadura.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Actinomadura sp. WAC 06369"
                     /db_xref="taxon:2203193"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34047
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa vyaargdlkp lvfegsvtag galmnttdve nfpgfpdgim
       61 gpdlmdnlrk qaerfgaeli addvtevdln adpkivkvgd dvyraraviv atgsgyrelg
      121 lpdeqrlsgr gvswcatcdg fffreqdiav vgggdtamee aifltkfart vtvvhrrdel
      181 raskimqdra fandkikfrw dsevtaihgd drvqgvtlrn vktgeedrld itglfiaigh
      241 dprselfagq letdpdgyll vdapttrtkv pgvfacgdvv dhiyrqavta agsgcsaaid
      301 aerwlqdrda eaaqqs
//
LOCUS       WP_125661252             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus baekrokdamisoli].
ACCESSION   WP_125661252
VERSION     WP_125661252.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus baekrokdamisoli
  ORGANISM  Paenibacillus baekrokdamisoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Paenibacillus baekrokdamisoli"
                     /db_xref="taxon:1712516"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34152
     Region          4..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqivivgtg pagltaaiyl aragysplvl egaqpggqlt tttevenypg fpdgilgsel
       61 msnmrkqaqr fgarfqtgwv qstdlserpf kltmetgsei iaqamiistg asarymgipg
      121 erenvgrgvs tcatcdgfff rgkkiivvgg gdsameeavf ltrfasevtl vhrrdelras
      181 kimqdraran ekikwrlnvt plevaateqg lsglrvrdnl tgeevllead gifvaightp
      241 nttflggqit tdeqgyivvd pgtsqtnlpg vyacgdvqdr hyrqaitaag sgcmaaldce
      301 hdlgalgmep aaneavsgri n
//
LOCUS       WP_125661380             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces sp. WAC08241].
ACCESSION   WP_125661380
VERSION     WP_125661380.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC08241
  ORGANISM  Streptomyces sp. WAC08241
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Streptomyces sp. WAC08241"
                     /db_xref="taxon:2487421"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52203
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgvlkear agesrvsatp atveqirklg ygvvvdpgag vaagftdgay eaagatvgda
       61 vaadvvlgvn apapsqldrv rpeatvialf spafdpamve elsrrpftal smdavprisr
      121 aqsmdvlssm aniagyravi eaahefgrff tgqvtaagkv ppakvlvaga gvaglaaiga
      181 agslgaivra tdprpevadq vrslggeyls iespetevsk tgyakemgdd ykareaelya
      241 aqcrevdivv ttalipgrpa ptlitaemva gmrpgsvivd maaanggnve gtvkgektvt
      301 engvtiigyt dlagrlpaqa sqlygtnlvn llklmtpdkd arlvldwddp vqrsitvvrk
      361 getawppppv qvsaapapap aaaagepapk kapmtvrqrf ggvalgalal fllaafapaa
      421 llphvtvfvl aivigyyvig hvhhalhtpl msvtnaisgi ivvgallqig htstavtvls
      481 svaillasin vfggfavtrr mlamfnrs
//
LOCUS       WP_125655955             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingomonas sp. 2R-10].
ACCESSION   WP_125655955
VERSION     WP_125655955.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. 2R-10
  ORGANISM  Sphingomonas sp. 2R-10
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Sphingomonas sp. 2R-10"
                     /db_xref="taxon:3045148"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38324
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mklallaeqa agerrvaatp etvkkliglg agvaveagag tgasiddeay aaagasvgpr
       61 aqtiagadil lgvagpapds lagvkpgawl vaglnpfger aridayaalg vealamewmp
      121 ritraqsmdi lssqanlagy kavldaaaey grafpmmmta agtisaarvf vmgvgvaglq
      181 aiatarrlga qvsatdvrsa tkeqiqslga kpifvetvag iegegaggya gemsaeyrea
      241 qaelvsahia kqdivittal ipgkpaprlv serqvasmrp gsvlvdlave qggnvegava
      301 gevvvrhgvk ivghrnvpsr laadasalfa rnlfnflsay wdkdagrpvl pdedevtqai
      361 rltqngqvvn prltg
//
LOCUS       WP_125666529             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus baekrokdamisoli].
ACCESSION   WP_125666529
VERSION     WP_125666529.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus baekrokdamisoli
  ORGANISM  Paenibacillus baekrokdamisoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus baekrokdamisoli"
                     /db_xref="taxon:1712516"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33850
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myktiiigtg pagltaaiyl aranmnplvi egpepggqlt tttevenfpg fpegimgpdl
       61 manmrkqaer fgaefrtgwv nsvdtskrpf tlqvegqgel qaesliistg asakylgidn
      121 erenigrgvs tcatcdgfff rgkkiivvgg gdsameeasf ltrfasevvl vhrrdemras
      181 kimqdraren skiswalgrt plevvagplg vtglkvrnne tgleevietn gifvaightp
      241 ntkflggqle tdetgylivk pgtsetnieg ifacgdvqdh kyrqaitaag sgcmaaldce
      301 kfieghpthd wsqtl
//
LOCUS       WP_125677837             414 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Companilactobacillus keshanensis].
ACCESSION   WP_125677837
VERSION     WP_125677837.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus keshanensis
  ORGANISM  Companilactobacillus keshanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Companilactobacillus keshanensis"
                     /db_xref="taxon:2486003"
     gene            1..414
                     /gene="trxB"
     Protein         1..414
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=44544
     Region          21..291
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
     Region          311..410
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mskiydllii gagpgglaag iygsraklst avldknaepg gqasttdeme nypgfyngtt
       61 gpgimkefad haksfgtefl rgtvdevdft gpvkkvhtqq gdtyeskvvv lspgatprki
      121 nvkgeaelrg kgvsycatcd adffvdldvv vvgngdaaie eamyltkfae tvtiivihee
      181 gnldcnkasa ekamknpklk wvwnstveei agdelvekvv lknintgelt dletngvfvf
      241 igtephtdfl kgkvelddrg ylvandmmet nvpgvyavgd arvkylrqvv taaadgaiaa
      301 saaekylsel etlqndvldv snkkpvilaf wapqveesid siaavdkive ekngavelvk
      361 ldtyrakkta tqykvtqipt iilfkdgkdv ariegvknit ssavenllke svev
//
LOCUS       WP_125683488             313 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Levilactobacillus].
ACCESSION   WP_125683488
VERSION     WP_125683488.1
KEYWORDS    RefSeq.
SOURCE      Levilactobacillus
  ORGANISM  Levilactobacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Levilactobacillus"
                     /db_xref="taxon:2767886"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32939
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknydvivig agpggmtgal yasranlsvl mldrgiyggq mnntaaieny pgfksvlgpd
       61 lakdmydgst qfgaefaygs vesiedhgdh kvvktddgdy sakavivatg seykklgvpg
      121 edefggrgvs ycavcdgaff knrevivvgg gdsaieegiy laglaskvti vvrrdqlraq
      181 kiiqdrafan ekiefvwntn vtailgdemk vtgvatknnq tgetgelaas gvfiyvgtlp
      241 mtdafkglgi ldeagwiktd dhmatavpgi faigdvrqkd lrqittavgd ggiagqeafs
      301 yletlkskaa saq
//
LOCUS       WP_125688002             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Levilactobacillus fujinensis].
ACCESSION   WP_125688002
VERSION     WP_125688002.1
KEYWORDS    RefSeq.
SOURCE      Levilactobacillus fujinensis
  ORGANISM  Levilactobacillus fujinensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Levilactobacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Levilactobacillus fujinensis"
                     /db_xref="taxon:2486024"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32945
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknydvivig agpggmtgal yasranlsvl mldrgiyggq mnntaaieny pgfksvlgpd
       61 lakdmydgst qfgaefaygs vesiedqgdh kvvktddgdy sakavivatg seykklgvpg
      121 edqfggrgvs ycavcdgaff knrevavigg gdsaveesiy laglaskvtv fvrrdklraq
      181 kviqdrafan ekiefvwnts vtevlgddmk vtgvatknnq tgetgekavs gvfiyvgnlp
      241 mtaafkglgi tndagwittn elmqtavpgi faigdvrekt lrqittavgd ggiagqeafs
      301 yletlksqaa atk
//
LOCUS       WP_125692356             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis sp. WAC 04169].
ACCESSION   WP_125692356
VERSION     WP_125692356.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis sp. WAC 04169
  ORGANISM  Amycolatopsis sp. WAC 04169
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Amycolatopsis sp. WAC 04169"
                     /db_xref="taxon:2203197"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37931
     Region          8..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maaeneqltv gvvretgqge rrialvpkli ervsgrglrv vvepgdgaga lladetfeqa
       61 gavigdpwda divvkvapps aaevaklkqg tiligflnpr gdpdgiaale aagvrafave
      121 aiprisraqa mdalssqssv agyravllaa ekltrffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgaqttgydv rpevgeqvks lgakfldlgi eavgeggyar eltdeekaeq
      241 qrrlteaitk fdavittalv pgrkapvlvt adavkgmpag gvvvdlages ggnceltkpg
      301 eevvehdvti csplnlaaem pahsselyar nvtellellv dkegklaldf sdeivagacv
      361 agkeegge
//
LOCUS       WP_125697054             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus yichunensis].
ACCESSION   WP_125697054
VERSION     WP_125697054.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus yichunensis
  ORGANISM  Lacticaseibacillus yichunensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Lacticaseibacillus yichunensis"
                     /db_xref="taxon:2486015"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33471
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 makeydvivi gagpggmtaa lyasrsnlsv lmldrgiygg qmnntaaien ypgfksilgp
       61 elgqkmydga tqfgaeyayg nvtsitldgt tkvvttdedt yrakavviat gaehrklgip
      121 geedyggrgv sycavcdgaf fknrevavig ggdsaieegt ylaqlaskvt iihrrdqlra
      181 qkilqqrafa ndkidfvwna qveavegden kvtgvrykdk vtgeekvvpa sgafiyvgit
      241 pltegfdglg ildengwipt degmhtsvpg ifaigdvrqk tlrqittavg egglagqgvf
      301 dyiqslqdds lsvna
//
LOCUS       WP_125701968             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Levilactobacillus fuyuanensis].
ACCESSION   WP_125701968
VERSION     WP_125701968.1
KEYWORDS    RefSeq.
SOURCE      Levilactobacillus fuyuanensis
  ORGANISM  Levilactobacillus fuyuanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Levilactobacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Levilactobacillus fuyuanensis"
                     /db_xref="taxon:2486022"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32988
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknydvivig agpggmtgal yasranlsvl mldrgiyggq mnntaaieny pgfksvlgpd
       61 lakdmydgst qfgaefaygn vesiedhgdh kvvktddgdy sagavliasg seykklgvpg
      121 enefggrgvs ycavcdgaff knrevvvvgg gdsaveesly lagivskvtv vvrrdqlraq
      181 kviqdrafan dkiefvwntn vtevlgdemk vtgvatknnq tgetgeiaas gvfiyvgnlp
      241 mtdaftdlgi tddkgwiktd drmatavpgi faigdvrqkt lrqittavgd ggiagqeafs
      301 fledlkakaa saq
//
LOCUS       WP_125703860             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Companilactobacillus mishanensis].
ACCESSION   WP_125703860
VERSION     WP_125703860.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus mishanensis
  ORGANISM  Companilactobacillus mishanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Companilactobacillus mishanensis"
                     /db_xref="taxon:2486008"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33732
     Region          4..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mktfdvvvig agpggltaal yasranlsvm ildrgiyggq mnntaeieny pgfdsvlgpd
       61 lsekmfnsst qfgaefgyga vesiedngak kivhtddgdy etsvviiatg seykkigipg
      121 enelsgrgvs ycavcdgaff kgqdvavigg gdsaveegvy ltqlaksvti ihrrdqlraq
      181 kilqdrafkn dkikfvwnad vkeivdeddk vagvryvdke tgeehvvpak gafiyvgiqp
      241 mtesfkglgi lddagwidtd dhmktkvagi yaigdvrkkd lrqittavgd ggiagqeafn
      301 yiqtlsdadt kvtsk
//
LOCUS       WP_125704782             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus daqingensis].
ACCESSION   WP_125704782
VERSION     WP_125704782.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus daqingensis
  ORGANISM  Lacticaseibacillus daqingensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Lacticaseibacillus daqingensis"
                     /db_xref="taxon:2486014"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33883
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mskqydvivi gagpggmtag lyasranlsv lmldrgiygg qmnntaaien ypgfssilgp
       61 elgqkmydga tqfgaeyayg nvvdvrlegq skivvtdege ytakaviiat gaehrklgip
      121 geeeyggrgv sycavcdgaf fknrdvavig ggdsaveegl yltglaakvt vlhrrdqlra
      181 qkiiqqrafa ndkmdfvwna gveaiegdgs kvtgvrykdk vtgetqvlpv sgvfiyvgit
      241 pltkgfehlg vldeagwipt denmatrvpg ifaigdvrak hlrqittavg eggqagqsvf
      301 dyiqslqdet lktgavpsan
//
LOCUS       WP_125708899             409 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Companilactobacillus
            zhongbaensis].
ACCESSION   WP_125708899
VERSION     WP_125708899.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus zhongbaensis
  ORGANISM  Companilactobacillus zhongbaensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Companilactobacillus zhongbaensis"
                     /db_xref="taxon:2486009"
     gene            1..409
                     /gene="trxB"
     Protein         1..409
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=43950
     Region          21..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
     Region          311..409
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 msevydllvv gagpgglaag iygsrskmkt aildknaepg gqaattaele nypgfwegtt
       61 gpgimekfad hakafgtefl rgtvdevdfs gpiktvhtqq gdtyqakaiv lspgatprki
      121 nvkgeadlrg qgvsycatcd adffvdldvc vvgngdaaie eamyltkfae tvtiivihee
      181 gnldcnkasa ekamknpklk wiwnstveei agdglvekvv lknidtgelt dyptngvfvf
      241 igtephtefv kdkielddrg yivtndmmet nvpgvygvgd arekylrqvi taasdgaiaa
      301 saaekylsel etlqndvlde skdkpvllaf wapqiqesid sisavdkvve nnsdpvglvk
      361 ldtyrakkta tqynvneipt vvlfkdgkdv arvegaknit aesvadllk
//
LOCUS       WP_125710225             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus porcinae].
ACCESSION   WP_125710225
VERSION     WP_125710225.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus porcinae
  ORGANISM  Lacticaseibacillus porcinae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Lacticaseibacillus porcinae"
                     /db_xref="taxon:1123687"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33501
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maksydvivi gagpggmtag lyasranlsv lmldrgiygg qmnntaaien ypgfksvlgp
       61 dlgqqmydga tqfgaeyayg nvtslktdgd tkivetddgt ytakaviiat gaehrklgip
      121 geeefsgrgv sycavcdgaf fknrevvvig ggdsaieegt ylaglashvt ivhrrdslra
      181 qkilqdrafa ndkisfvwna nteeilgddn kvtgvrytdk vtgeshvipa sgvfiyvgim
      241 pltdsfkdvd ildengwipt detmatrvpg ifaigdvrak klrqittavg dggqagqsvf
      301 dyiqtlqdad lkvqa
//
LOCUS       WP_125713838             414 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Companilactobacillus kedongensis].
ACCESSION   WP_125713838
VERSION     WP_125713838.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus kedongensis
  ORGANISM  Companilactobacillus kedongensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Companilactobacillus kedongensis"
                     /db_xref="taxon:2486004"
     gene            1..414
                     /gene="trxB"
     Protein         1..414
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=44532
     Region          21..291
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
     Region          311..410
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 msklydllii gagpgglaag iygsraklst avldknaepg gqasttdeme nypgfyngtt
       61 gpgimkefad haksfgtefl rgtvdevdft gpvkkvhtqq gdtyeskvvv lspgatprki
      121 nvkgeaelrg kgvsycatcd adffvdldvv vvgngdaaie eamyltkfae tvtiivihee
      181 gnldcnkasa ekamknpklk wvwnstveei agdelvekvv lknintgelt dletngvfvf
      241 igtephtdfl kgkvelddrg ylvandmmet nvpgvyavgd arvkylrqvv taaadgaiaa
      301 saaekylsel etlqndvldv snkkpvilaf wapqveesid siaavdkive ekngavelvk
      361 ldtyrakkta tqykvteipt ivlfkdgkdv ariegaknit sdavedllke svev
//
LOCUS       WP_125729481             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas salmonicida].
ACCESSION   WP_125729481
VERSION     WP_125729481.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas salmonicida
  ORGANISM  Aeromonas salmonicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas salmonicida"
                     /db_xref="taxon:645"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53259
     Region          22..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrlt rlglaalllt tcfgasglaq adeatpkgki earselfakd hvdqfsswkd
       61 tsesatrtda laedpqmvvl wggypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eqyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfeqtcrnch tqskemlqgi vqqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaqmk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llatkgishe ialpdistke kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_125722640             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium ustbae].
ACCESSION   WP_125722640
VERSION     WP_125722640.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium ustbae
  ORGANISM  Flavobacterium ustbae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Flavobacterium ustbae"
                     /db_xref="taxon:2488790"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34058
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msntiekikc liigsgpagy taaiyaaran mnpvlyqgmq pggqltttne venfpgyvdg
       61 vtgpemmiql qeqakrfgad irdgwatkvd fsgdihkvwi ndsielhcet viistgasak
      121 ylglpseqhy lnmgggvsac avcdgffyrn qdvvivgagd saceeahyls klcrkvtmlv
      181 rsekfraski meervrkten ieilmnhdtv evlgdnnvvh aikalnkttg evieipatgf
      241 fvaighkpnt difkeyitld etgyivntpg tsktnvegvf vagdaadhvy rqaitaagtg
      301 cmaaldaery laske
//
LOCUS       WP_125730937             452 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Microcystis].
ACCESSION   WP_125730937
VERSION     WP_125730937.1
KEYWORDS    RefSeq.
SOURCE      Microcystis
  ORGANISM  Microcystis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Microcystis"
                     /db_xref="taxon:1125"
     gene            1..452
                     /gene="trxB"
     Protein         1..452
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=49374
     Region          6..310
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
     Region          353..449
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
ORIGIN      
        1 mtvenlviig sgpagytaai yaaranlkpl mfegfqaggi pggqlmttte venfpgfpeg
       61 itgpklmerm keqaerwgtq cytedvisvd lsqrpfairs tdrevkansi iiatgatakr
      121 lglpseaqfw sngisacaic dgatpifree nlavigggds aaeeavyltk ygshvhllir
      181 geamraskam qdrvlnnpkv tvhfhtqavd vfgtgskmag lriknsqtge iselavrglf
      241 yavghtpnts lfqgqlelde vgyvkvkpgt vatsvegvfa agdvqdheyr qaitaagtgc
      301 maallaerwl sehnliqeyr qsatsehyet ktvsetpadt eetfdihktr hvggyalrkl
      361 fhdgdrllmv kyvsptcgpc ktlkpildkv vdeydgkiyf veidieadpe iakmgqvtgt
      421 ptvqffkdre lvkemrgvkq ksdfrqvies yq
//
LOCUS       WP_125731203             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Microcystis viridis].
ACCESSION   WP_125731203
VERSION     WP_125731203.1
KEYWORDS    RefSeq.
SOURCE      Microcystis viridis
  ORGANISM  Microcystis viridis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Oscillatoriophycideae; Chroococcales; Microcystaceae; Microcystis.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Microcystis viridis"
                     /db_xref="taxon:44822"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40202
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikesd qgearvalvp dtvarlvkag fevivqngag iganfadsay savgaalsen
       61 seyiyetadi ilkvvppsds eidrlknggi ligfldplrq prriaklaer gitalsmeli
      121 prssraqsmd alssqanlag ykavllaavq lpkmfpmmtt aagtiapakv lvlgagvagl
      181 qacatarrlg avveafdirp qvkeevqsvg akfiemplee dtvadngyak evslstqeri
      241 cqaltepikr advvittaqv pgkqapllvt kemiatmkag svivdlaaeq ggncaytqpg
      301 reiivngvki vgavnlpatv atnasqmyak nlqmllqllv skegslnldf addiidsacv
      361 thageirnqr iksalseqls af
//
LOCUS       WP_125737941             368 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Amycolatopsis].
ACCESSION   WP_125737941
VERSION     WP_125737941.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis
  ORGANISM  Amycolatopsis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Amycolatopsis"
                     /db_xref="taxon:1813"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37874
     Region          8..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maaeneqltv gvvretgqge rrialvpkli ervsgrglrv vvepgagaga lladetfeqa
       61 gavigdpwda divvkvapps aaevaklkqg tiligflnpr gdpdgiaale aagvrafave
      121 aiprisraqa mdalssqssv agyravllaa ekltrffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgaqttgydv rpevgeqvks lgakfldlgi eavgeggyar eltdeekaeq
      241 qrrlteaitk fdvvittalv pgrkapvlvt adavkgmpag gvvvdlages ggnceltkpg
      301 eevvehdvti csplnlaaem pahsselyar nvtellellv dsegklaldf sdeivagacv
      361 agkeegge
//
LOCUS       WP_125731363             331 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Amycolatopsis].
ACCESSION   WP_125731363
VERSION     WP_125731363.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis
  ORGANISM  Amycolatopsis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Amycolatopsis"
                     /db_xref="taxon:1813"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35457
     Region          9..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maaeeirnli ivgsgpagyt aavyaaraql eplvfegtqf ggalmtttev enfpgfregi
       61 qgpdlmeemr eqakrfgadl rqedvesvel tgdvkyvvan gkryaaravv lsmgaaaryl
      121 nvpgeqellg rgvsacatcd gfffrdhdiv vagggdsame eatfltkfak svtivhrree
      181 fraskimler arenekikwa lnkqitaveg egkvegltlk dtvtgeeskl dvtgffvaig
      241 hdprselvrg qvdldedgyv ltqgrtsytn lpgvfaagdl vdrtyrqait aagsgcaaai
      301 daerwlaeha gvetaqetpe lvgggygast n
//
LOCUS       WP_125739357             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Acinetobacter lactucae].
ACCESSION   WP_125739357
VERSION     WP_125739357.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lactucae
  ORGANISM  Acinetobacter lactucae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Acinetobacter lactucae"
                     /db_xref="taxon:1785128"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39770
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,124,127,130,171..174,194..196,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigiptetv vgenrvaatp etvkklisag hsvviergag vkaayidsay eqvgatitdd
       61 aytgsqiilk vrapqggeiq klaantavva mfdpyrntel eqfanqqvsa falellprtl
      121 sraqnmdvls sqanlagyks vllaaaeyqr mfpmlmtaag tvkparvvim gvgvaglqai
      181 atakrlgaiv eatdlrptak dqveslggkw ldvpmseeeq qraadaakng ygwmpgeqyi
      241 kdqaaivdka vsnadivitt allpgrdapr likaetvakm kpgsvildma vetggnvegs
      301 kvgetvften gvkilgvpni patvateasa lyarnvfnfv etlfdkeknf ainqedeiqk
      361 allvthggqv llkrg
//
LOCUS       WP_125739729             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter lactucae].
ACCESSION   WP_125739729
VERSION     WP_125739729.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter lactucae
  ORGANISM  Acinetobacter lactucae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Acinetobacter lactucae"
                     /db_xref="taxon:1785128"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33643
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdpeglt
       61 gpalmdrmqa haerfgtelv ydhinevdln vrpfvlkgdm eeytcdalii atgataqylg
      121 leseqkfmgq gvsacatcdg ffyknqkvmv vgggntavee alylsniash vtlvhrrntl
      181 rsekilqdhl fakekegkis iiwnheveev lgdntgvtsi rlkstqddsk qdvevhglfv
      241 aighkpntgm fdgqlnlrdg yiqvqsgtsg natatsvagv faagdvadsi yrqaitsags
      301 gcmaaldaek yldnl
//
LOCUS       WP_125743903             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. WAC01280].
ACCESSION   WP_125743903
VERSION     WP_125743903.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC01280
  ORGANISM  Streptomyces sp. WAC01280
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Streptomyces sp. WAC01280"
                     /db_xref="taxon:2487424"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35011
     Region          14..318
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtdsnaatgg dvrevivigs gpagytaaly taraqlkpll fgssifvggs lttttevenf
       61 pgfptgidgp almdnmraqa erfgaemidd difsvdltgd ikevtdsegt vhrakaviia
      121 tgsgyrklgl pnedelsgrg vswcatcdgf ffrdrdivvv gggdtameea tfltrfarsv
      181 tvvhrrstlr asktmqnraf addkisfafd seiaeikaen gmlagvvlrd tftgktrdld
      241 atglfiavgh dlrtelftgq idlddegyik veapstrtnl pgvfaagdvv dhtyrqaita
      301 agsgcqaald aerhlaalad mskaaasvav ta
//
LOCUS       WP_125746185             315 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Vreelandella venusta].
ACCESSION   WP_125746185
VERSION     WP_125746185.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella venusta
  ORGANISM  Vreelandella venusta
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Vreelandella venusta"
                     /db_xref="taxon:44935"
     Protein         1..315
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36315
     Region          5..171
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maifelfskr qkkqrgempd vyvyeeipqs frvqiihiir dtfgedryss dasssayefi
       61 hkalckeygv ftlneyarsd seaileyfln csdyencldv ieisfslien yvgenyynyk
      121 qrttssqdpe daveelnkrf keagigyefs sgeliridsq lihsevvkpv lallktnrly
      181 nganqeflka henyrhkryk eclveclksi eslmkgvckq hswefkesdp akklinicle
      241 nklvpeylqn qfsslrille sgvptirnre gghgqgpels tvpehfasyt lhltasnllf
      301 lmqcneqltn kgsgr
//
LOCUS       WP_125749498             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus baoqingensis].
ACCESSION   WP_125749498
VERSION     WP_125749498.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus baoqingensis
  ORGANISM  Lacticaseibacillus baoqingensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Lacticaseibacillus baoqingensis"
                     /db_xref="taxon:2486013"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33523
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpksydvivi gagpggmtaa lyasrsnlsv lmldrgiygg qmnntaeien ypgfnsilgp
       61 dlgqkmydga tqfgaeyayg nvtairvngd lrevdtdegn yvakaviiat gaehrklgip
      121 geedysgrgv sycavcdgaf fkdrevvvig ggdsaieegt ylaqlaskvt ivhrrdslra
      181 qqilqkrafa npkinfvwna dtkailgden kvtgvqytdk etgethvipa sgvfiyvgim
      241 pltegfesvg ildeagwipt detmatkvpg ifaigdvrak tlrqittavg dggqagqsvf
      301 dyiqslqdad lkvna
//
LOCUS       WP_125751631             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vreelandella venusta].
ACCESSION   WP_125751631
VERSION     WP_125751631.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella venusta
  ORGANISM  Vreelandella venusta
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Vreelandella venusta"
                     /db_xref="taxon:44935"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33660
     Region          3..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 metrherlii lgsgpagyta avyaaranlk pllitglqag gqlttttdvd nwpgdaqgvq
       61 gpelmermkq haerfntevl fdhinevslg ekpytlkgds giytcdalii atgasarylg
      121 lpteqqfmgq gvsacatcdg ffyrnqeviv vgggntavee alylsniask vtlvhrrdtl
      181 raekilqdkl fekveagkia lewfyevdev lgdnsgvtgv rvkstkdgst keiqapglfi
      241 aighspntgi fegqldmngg yikvqsgleg natatsvpgv facgdvmdhi yrqaitsags
      301 gcmaaldaer yldgia
//
LOCUS       WP_125755011             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus hegangensis].
ACCESSION   WP_125755011
VERSION     WP_125755011.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus hegangensis
  ORGANISM  Lacticaseibacillus hegangensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Lacticaseibacillus hegangensis"
                     /db_xref="taxon:2486010"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34214
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 makqydvivi gagpggmtaa lyasranlsv lmldrgiygg qmnntaaven ypgfksilgp
       61 elgqqmydga tqfgaeyayg nvtdltddgk iktvvtdege yqakaviiat gaehrklgvp
      121 geeayggrgv sycavcdgaf fkgqevavig ggdsaveegl ylaglaskvt vihrrdqlra
      181 qkiiqqrafa npkmhfvwna qteeilgddn kvtgvryhdk etgedkvlpv sgvfiyvgik
      241 pltdsfkhvd vlddagwipt nelmetqvpg ifaigdvrak nlrqiatavg eggqagqsaf
      301 nyiqslqdaq lqagavpsae qn
//
LOCUS       WP_125752170             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Vreelandella venusta].
ACCESSION   WP_125752170
VERSION     WP_125752170.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella venusta
  ORGANISM  Vreelandella venusta
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Vreelandella venusta"
                     /db_xref="taxon:44935"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55423
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapketa qgearvaltp esakqlqklg heclveagag aaagfnddty rdagvsvves
       61 aealwrdadv vikvrepset eahylregqt liaffwpaqn ealletckaq gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 saigtaaslg avvrafdvrp evseqiesmg aeflfldfed sqdgsesggy aspsspefre
      241 kqlecfreqa pdvdivitta lipgrpapkl wledmvaamk pgsvivdlaa ekggncdltk
      301 pdervvsdng vvvvgytdfp srmatqasll yatnirhmla dltpekdgvi hhnmeddvir
      361 gatvthqgei tfpppppkvk aiaaakpkkk eqeptpeekk atehaafkaq tkrqagllav
      421 ggalmlllgq iapasfmqhf ivfvlacfig fqviwkvshs lhtplmavtn aisgiiilga
      481 ilqigsgsgv vivlaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_125765541             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Levilactobacillus mulengensis].
ACCESSION   WP_125765541
VERSION     WP_125765541.1
KEYWORDS    RefSeq.
SOURCE      Levilactobacillus mulengensis
  ORGANISM  Levilactobacillus mulengensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Levilactobacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Levilactobacillus mulengensis"
                     /db_xref="taxon:2486025"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32872
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknydvivig agpggmtgal yasranlsvl mldrgiyggq mnntaaieny pgfksvlgpd
       61 lakdmyegst qfgaefaygs veaiedhgdh kvvktddgdy aakaviigsg seykklgvpg
      121 edkfggrgvs ycavcdgaff knrevavigg gdsaveesiy lsglaskvtv yvrrdqlraq
      181 kviqdrafan dkiefvwnts vtevlgddmk vtgvatknnv tgetgekavs gvfiyvgnlp
      241 mtapfkdlgi tddagwiktd ehmrtavpgi faigdvrqkd lrqittavgd ggiagqeafs
      301 fiedlkaaat k
//
LOCUS       WP_125766920             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lapidilactobacillus wuchangensis].
ACCESSION   WP_125766920
VERSION     WP_125766920.1
KEYWORDS    RefSeq.
SOURCE      Lapidilactobacillus wuchangensis
  ORGANISM  Lapidilactobacillus wuchangensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lapidilactobacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Lapidilactobacillus wuchangensis"
                     /db_xref="taxon:2486001"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34013
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvkkydvivi gagpggmtaa lyasrsnlsv lmldrgiygg qmnntaaien ypgfksilgp
       61 elgekmyasa tqfgaeytyg tvksvvdhhd yktivtddge yeakaviiat gaehrhlgvp
      121 geekysgrgv sycavcdgaf fkgkevavig ggdsaveegi ylaqlaskvt ivhrrdslra
      181 qkilqrrafa nekiefvwna dvqeivgddq kitavryrdk vtneehdlpa tgvfiyvgie
      241 pmtepfkdlg ildeagwikt detshtavpg ifavgdvrqk hlrqianavg egglagqaaf
      301 dylqdlqdet qavka
//
LOCUS       WP_125775631             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Antribacter gilvus].
ACCESSION   WP_125775631
VERSION     WP_125775631.1
KEYWORDS    RefSeq.
SOURCE      Antribacter gilvus
  ORGANISM  Antribacter gilvus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Antribacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Antribacter gilvus"
                     /db_xref="taxon:2304675"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33317
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteqqtattv hdvvivgsgp agytaaiyaa raglepvvva gsvtaggalm nttevenfpg
       61 fpagiqgpdl mdamreqaek fgarvvwdda eqvdlggdvk tvvtgggetf harsvilatg
      121 sayrelglpe ekrlsgrgis wcatcdgfff rdqhiavvgg gdsameeatf ltrfaskvti
      181 vhrrdtlras kimadratnd pkiefawnse vagvsgenkv eavtlrdtat getrelpvtg
      241 vfvaighepr tdlvkgqidl dpngyvlveg rttrtnlpgv facgdavdht yrqaitaags
      301 gcaaaldaqa yldeiah
//
LOCUS       WP_125776971             504 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Antribacter gilvus].
ACCESSION   WP_125776971
VERSION     WP_125776971.1
KEYWORDS    RefSeq.
SOURCE      Antribacter gilvus
  ORGANISM  Antribacter gilvus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Promicromonosporaceae; Antribacter.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Antribacter gilvus"
                     /db_xref="taxon:2304675"
     Protein         1..504
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49914
     Region          1..500
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpreqg rlvaatpssv srlvalgydv vveagagaga sladagyaaa gaavgsaddv
       61 waadvvtavg pvdreppags flvaqlgpat npgrvqalaa ggvtalalda vprisraqal
      121 dvlsalsnva gyrgvveaaa eyggmfggqi taagttkpat vfvigagvag laaigaavsl
      181 garvrafdvr pevaeqiesm gatfvradaa tqqvsadgya saltsdqeaa aarvyaaeta
      241 aadvvvttal vrgvaprtlt aemvagmrpg svivdlaasg ggnceltvpg ervvtpggvv
      301 vlgytdlpar mprhtselvg tavanllalv tpgkdghlvl dladpvvrgm tvahagevlw
      361 ppppvavtas aaapppppve dkdaarrrtl asrvalalgv vaagllvsvs ppslaghftv
      421 lalavvvgfy vishvshslh tplmaqtnav sgiilvgall qigssswvvt llavvaaava
      481 sinifggflv thrmlgmfrr ggga
//
LOCUS       WP_125771419             409 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Companilactobacillus furfuricola].
ACCESSION   WP_125771419
VERSION     WP_125771419.1
KEYWORDS    RefSeq.
SOURCE      Companilactobacillus furfuricola
  ORGANISM  Companilactobacillus furfuricola
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Companilactobacillus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Companilactobacillus furfuricola"
                     /db_xref="taxon:1462575"
     gene            1..409
                     /gene="trxB"
     Protein         1..409
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=43733
     Region          21..291
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
     Region          311..409
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 msevydllvv gagpgglaag iygsrskmkt avldknaepg gqaattaele nypgfwegtt
       61 gpgimekfad hakafgtefl rgtvdevdfs gpiktvhtqq gdtyqakavv lspgatprki
      121 nvkgeaelrg qgvsycatcd adffvdldvc vvgngdaaie eamyltkfaa tvtiivihee
      181 gnldcnkasa ekamknpklk wvwnstveei agdglvekvv lknidtgelt dyptngvfvf
      241 igtephtafv kdkielddrg yivtndmmet nvpgvygvgd arekylrqvi taaadgaiaa
      301 saaekylsel etlqndvlde skdkpvllaf wapqiqesid sisavdkvve gnsdpvglvk
      361 ldtyrakkta tqynvneipt vvlfkdgkdv arvegaknit aesvadllk
//
LOCUS       WP_125780323             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudoalteromonas rubra].
ACCESSION   WP_125780323
VERSION     WP_125780323.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas rubra
  ORGANISM  Pseudoalteromonas rubra
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudoalteromonas rubra"
                     /db_xref="taxon:43658"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33894
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdakhckll ilgsgpagyt aavyaaranl npvlitgmqq ggqlttttev enwpgdahgl
       61 tgpalmdrmk ehaerfetei ifdhinkvdv tkrpftltgd qgtytcdali iatgasakyl
      121 glesetnfqg rgvsacatcd gffyrgqkva vvgggntave ealylsniae evhvihrrdt
      181 frsekilsdr lmekanngnv vlhlnktlde vlgddmgvtg irikdtdsea teqldlagvf
      241 iaighkpntd mfagqlemkd gylvvqsgln gnatqtsveg vfaagdvsdh iyrqaitsag
      301 tgcmaaldae ryldnlk
//
LOCUS       WP_125781527             331 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Amycolatopsis].
ACCESSION   WP_125781527
VERSION     WP_125781527.1
KEYWORDS    RefSeq.
SOURCE      unclassified Amycolatopsis
  ORGANISM  unclassified Amycolatopsis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="unclassified Amycolatopsis"
                     /db_xref="taxon:2618356"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35532
     Region          9..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maaeeirnli vigsgpagyt aavyaaraql eplvfegtqf ggalmtttev enfpgfregi
       61 qgpdlmeemr eqakrfgadl rqedvesvel tgdvkyvfan gkryaaravv lsmgaaaryl
      121 nvpgeqellg rgvsacatcd gfffrdhdiv vagggdsame eatfltkfak svtivhrree
      181 fraskimler arenekikwa lnkqitgveg egkveglklk dtvtgeeskl dvtgffvaig
      241 hdprselvrg qvdldedgyv ltqgrtsytn lpgvfaagdl vdrtyrqait aagsgcaaai
      301 daerwlaeha gvetaqetpe lvgggygatt n
//
LOCUS       WP_125786423             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis sp. WAC 01375].
ACCESSION   WP_125786423
VERSION     WP_125786423.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis sp. WAC 01375
  ORGANISM  Amycolatopsis sp. WAC 01375
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Amycolatopsis sp. WAC 01375"
                     /db_xref="taxon:2203194"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37904
     Region          8..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maaeneqltv gvvretgqge rrialvpkli ervsgrglrv vvepgagaga lladetfeqa
       61 gavigdpwda divvkvapps aaevaklkqg tiligflnpr gdpdgiaale sagvrafave
      121 aiprisraqa mdalssqssv agyravllaa ekltrffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgaqttgydv rpevgeqvks lgakfldlgi eavgeggyar eltdeekaeq
      241 qrrlteaitr fdvvittalv pgrkapvlvt adavkgmpag gvvvdlages ggnceltkpg
      301 eevvehdvti csplnlaaem pahsselyar nvtellellv dsdgklaldf sdeivagacv
      361 agkeegge
//
LOCUS       WP_125790689             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Amycolatopsis sp. WAC 01376].
ACCESSION   WP_125790689
VERSION     WP_125790689.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis sp. WAC 01376
  ORGANISM  Amycolatopsis sp. WAC 01376
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Amycolatopsis sp. WAC 01376"
                     /db_xref="taxon:2203195"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35541
     Region          9..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maaeeirnli vvgsgpagyt aavyaaraql eplvfegtqf ggalmtttev enfpgfregi
       61 qgpdlmeemr eqakrfgadl rqedvesvel tgdvkyvvan gkryaarsvv lamgaaaryl
      121 nvpgeqellg rgvsacatcd gfffrdhdiv vagggdsame eatfltkfak svtivhrree
      181 fraskimler arenekikwa lnkqitqveg egkveglklk dtvtgeeskl dvtgffvaig
      241 hdprselvrg qvdldedgyv ltqgrtsytn lpgvfaagdl vdrtyrqait aagsgcaaai
      301 daerwlaeha gvetaqetpe lvgggygatt n
//
LOCUS       WP_125799231             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Amycolatopsis sp. WAC 01416].
ACCESSION   WP_125799231
VERSION     WP_125799231.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis sp. WAC 01416
  ORGANISM  Amycolatopsis sp. WAC 01416
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Amycolatopsis sp. WAC 01416"
                     /db_xref="taxon:2203196"
     Protein         1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37890
     Region          8..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,77,96,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(51,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maaeneqltv gvvretgqge rrialvpkli ervsgrglrv vvepgagaga lladetfeqa
       61 gavigdpwda divvkvapps aaevaklkqg tiligflnpr gdpdgiaale sagvrafave
      121 aiprisraqa mdalssqssv agyravllaa ekltrffpml ttaagtvppa kvlvlgagva
      181 glqalatakr lgaqttgydv rpevgeqvks lgakfldlgi eavgeggyar eltdeekaeq
      241 qrrlteaitr fdvvittalv pgrkapvlvt adavkgmpag gvvvdlages ggnceltkpg
      301 eevvehdvti csplnlaaem pahsselyar nvtellellv dsdgklaldf sdeivagacv
      361 agneegge
//
LOCUS       WP_125810394             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinoplanes sp. ATCC 53533].
ACCESSION   WP_125810394
VERSION     WP_125810394.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes sp. ATCC 53533
  ORGANISM  Actinoplanes sp. ATCC 53533
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Actinoplanes sp. ATCC 53533"
                     /db_xref="taxon:1288362"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34269
     Region          7..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpsgytaa lyaaranlkp lviegvqsgg almttteven fpghpdgimg
       61 pelmdnmrkq aerfgaefit ddvtrvelgd kpteagtegl ktvwvgetqy faralilstg
      121 sawrplgvpg eqellghgvs scatcdgfff rnqhiivvgg gdsameeatf ltrfaetvti
      181 vhrrddfras kvmalraksn pkikiewnsv veeilgddgk vvgarlrnlq tgetkvldvt
      241 gvfvaighdp rselfkgqie mdddgyvkvd apstrtnvqg vfaagdlvdh tyrqaitasg
      301 tgcaaaldae rfiasfiel
//
LOCUS       WP_125813375             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_125813375
VERSION     WP_125813375.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33662
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslnp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmrd qaerfgaelv pddvvavdlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtivhrrds
      181 lrasktmqdr afadpkikfa wdsevaeihg eqklsgltlr ntktgetsel pvtglfiavg
      241 hdprtelftg qldlddegyl kvdapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaals daepaaatv
//
LOCUS       WP_125826973             303 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptococcus].
ACCESSION   WP_125826973
VERSION     WP_125826973.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32797
     Region          2..301
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mfdtviigag pagmtaalya arsnlkvali ergipggqmn ntsdienypg yanisgpdla
       61 ekmfeplenl gvehlfgqve riedlgatkk ivtddgefea ktvviatgsn hrplnvpgee
      121 elnsrgvsyc avcdgaffrd enllvvgggd saveeavflt qfaktvtiah rrdqlraqkv
      181 lqdrafandk ihfawntvve eikgeqkvts vllkdvktgv vreqafggvf iyvgldpvsd
      241 fatelgilde ngwvvtddhm rtkvpgifav gdvrqkdlrq vttavgdgai agqevykyit
      301 enf
//
LOCUS       WP_125829459             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. v388].
ACCESSION   WP_125829459
VERSION     WP_125829459.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. v388
  ORGANISM  Pseudomonas sp. v388
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. v388"
                     /db_xref="taxon:2479849"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38652
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hritvqsgag vqasvpdsay aaagatigsl
       61 qeafaadlil kvaapndael allksgtivv gmlnpfsnet igklaaqgvt afaleaaprt
      121 sraqsldvls sqaniagyka vllgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf idvpyetdee recaegvggy arpmpaswmq
      241 rqavavhera rqadivitta lipgrkapvl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvivehgv tivghtnlpa lvaadasaly arnlldfmkl lfdkegtlsi nleddivaac
      361 lmcrdgqvir kng
//
LOCUS       WP_125830610             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas sp. v388].
ACCESSION   WP_125830610
VERSION     WP_125830610.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. v388
  ORGANISM  Pseudomonas sp. v388
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas sp. v388"
                     /db_xref="taxon:2479849"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33672
     Region          1..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgpalmermr ehaerfetei vfdhissvdl agkpfsltgd sgvytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlvhrret
      181 fraekilidk lharvaegki elklnatlde vlgdnmgvtg arlknndgss delkvdgvfi
      241 aightpntsl fegqlalkdg ymvvqggreg natatsvegv faagdvadhv yrqaitsaga
      301 gcmaaldver yldglaevsf
//
LOCUS       WP_125828054             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus mitis].
ACCESSION   WP_125828054
VERSION     WP_125828054.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mitis
  ORGANISM  Streptococcus mitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus mitis"
                     /db_xref="taxon:28037"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32979
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygfve kiedhadykk vitddqvyet rtvivatgsk hrllgvsgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdelraqkv
      181 lqdrafanek vsfiwdsvvk eikgesrves vvfenvktgq vteqafggvf iyvgldpvsd
      241 fvkdlniqdq sgwivtdnhm ktavdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125835931             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas sp. o96-267].
ACCESSION   WP_125835931
VERSION     WP_125835931.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. o96-267
  ORGANISM  Pseudomonas sp. o96-267
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Pseudomonas sp. o96-267"
                     /db_xref="taxon:2479853"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33011
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msavrharvi ilgsgpagys aavyaaranl kpllitgiqa ggqlttttev dnwpgdphgl
       61 tgpalmqrmq ehaerfetei vfdhinavdl agkpftlvgd sgtyscdali iatgasaryl
      121 glpseeafmg rgvsacatcd gffyrgreva vvgggntave ealylanias kvtlvhrret
      181 fraekilqdk lrsriaegki elqlnaevde vlgdasgvtg vrlkqyggay relsveglfv
      241 aightpntsl fegqlalkdg ylvvnggreg natatsipgv faagdvadsv yrqaitsaga
      301 gcmaaldver yldgl
//
LOCUS       WP_125838618             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas saudiphocaensis].
ACCESSION   WP_125838618
VERSION     WP_125838618.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas saudiphocaensis
  ORGANISM  Pseudomonas saudiphocaensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas saudiphocaensis"
                     /db_xref="taxon:1499686"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38982
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpletr pgetrvaatp etvkkliaqg hqvivqsgag mqssvpdgay eaagativea
       61 aatfaanivl kvnapnetel aqmqlgsvli gmlnpfdsan iarmaergit sfaleaaprt
      121 sraqsldvls sqaniagyka vmiaanqypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpceteee recaegvggy arpmpqswme
      241 rqakavhera kqadiiitta lipgrkapvl lqeatvaemk pgsvivdlaa aqggncpltv
      301 adqvvishgv tlvgysnlat lvpadasaly arnlldflkl vidkdgqfql nleddivaac
      361 lmcrdgqivr tng
//
LOCUS       WP_125841114             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus mitis].
ACCESSION   WP_125841114
VERSION     WP_125841114.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mitis
  ORGANISM  Streptococcus mitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus mitis"
                     /db_xref="taxon:28037"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33018
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlygyve niedkgdykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldpvsd
      241 fvkelniqnq agwivtdnhm ktavdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125842408             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Stutzerimonas stutzeri].
ACCESSION   WP_125842408
VERSION     WP_125842408.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33590
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kplmitgiqp ggqlttttev dnwpgdvegl
       61 tgpdlmvrmq khaerfdtei vfdhihtael qqrpftlrgd sgvyscdali iatgasaqyl
      121 glpseeafag rgvsacatcd gffyrnqvva vigggntave ealylsniak evhlihrrdk
      181 lrsekilqdk imdkatngni rlhwnhtlee vlgdasgvtg vrlkstltge entldlagvf
      241 iaighkpntd lfqgqlemkd gylkirggge gdatctsipg vfaagdvadh vyrqaitsag
      301 agcmaaldae kyldn
//
LOCUS       WP_125843452             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Rhizobium].
ACCESSION   WP_125843452
VERSION     WP_125843452.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34793
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mparhtkvli igsgpagyta avyaaramlk pvliagleqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlq qakhvgaeiv ndlvtevdmn qrpfvartds gqvwtadtli iatgakakwl
      121 gieseqhfqg fgvsacatcd gffyrnkdvi vvgggnsave ealylsniak svtlvhrrdf
      181 fraekilqer lfskenvkvl wntevaeitg tpakppmpqs vsgarlrdtr tgaitemaid
      241 gvfvaighap atelfkdrlk lkdngylwta pdstatsleg vyaagdvtdd tfrqaitaag
      301 mgcmaaleae ryltghmpva vaae
//
LOCUS       WP_125843428             368 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Stutzerimonas stutzeri].
ACCESSION   WP_125843428
VERSION     WP_125843428.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     Protein         <1..368
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(10,68,87,286,312,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(39,119..120,129..130,133..134,137..138,140..141,
                     143..148,150,152..154,157,180..181,276..277,319..320,324,
                     327..328)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(114..115,119,122,125,166..169,189..191,226,237,
                     254..256,263,265)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(116..117,119,129,172..173,180,196..197,199..202)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(149..153,156,159,182,184)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 plethsgetr vaatpetvkk ligqghrvtl qsgagllssv pdsayeavga tigdaaaafa
       61 aelvlkvnap ddaelaqmqs gsvllgmlnp fdndciarma argitafale aaprtsraqs
      121 ldvlssqani agykavlvga hhyprfmpml mtaagtvkaa rvlilgagva glqaiatakr
      181 lgavveasdv rpavkeqies lgakfvdvpl etdeerecae gvggyarpmp aswmarqaqa
      241 vheralqsdi vittalipgr kaptllqeat veqmkpgsvi vdlaaghggn cplteidqvv
      301 vrhgvtivgh anlatlvpad asalyarnll dflklvidkd gqfqlnledd ivaaclmcrd
      361 gqvvrtng
//
LOCUS       WP_125847130             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus oralis].
ACCESSION   WP_125847130
VERSION     WP_125847130.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus oralis
  ORGANISM  Streptococcus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus oralis"
                     /db_xref="taxon:1303"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33067
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gveylygfve kiedhadykk vitddqvyet rtvivatgsk hrllgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdelraqkv
      181 lqdrafanek vnfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldpvsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125852038             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus mitis].
ACCESSION   WP_125852038
VERSION     WP_125852038.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mitis
  ORGANISM  Streptococcus mitis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus mitis group.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus mitis"
                     /db_xref="taxon:28037"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32927
     Region          2..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlrvali egglpggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehiygyvg nvedhgdfkk vitddqtyet rtvivatgsk hrplgvpgee
      121 elnsrgvsyc avcdgaffrd qdllvvgggd saveealflt rfaktvtivh rrdqlraqkv
      181 lqdrafanek vsfiwdsvvk eikgenrves vvfenvktgq vteqafggvf iyvgldplsd
      241 fvkelniqdq agwivtdnhm ktavdgifav gdvrqkdlrq vttavgdgai agqeaykfit
      301 ehs
//
LOCUS       WP_125860844             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Stutzerimonas].
ACCESSION   WP_125860844
VERSION     WP_125860844.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas
  ORGANISM  Stutzerimonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas"
                     /db_xref="taxon:2901164"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38789
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkligqg hrvtlqsgag llssvpdsay eavgatigda
       61 aaafaaelvl kvnapddtel aqmqsgsvll gmlnpfdnac iarmaargvt afaleaaprt
      121 sraqsldvls sqaniagyka vlvgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhera lqsdivitta lipgrkaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvaadasaly arnlldflkl vidkdgqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_125863918             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Stutzerimonas nitrititolerans].
ACCESSION   WP_125863918
VERSION     WP_125863918.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas nitrititolerans
  ORGANISM  Stutzerimonas nitrititolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Stutzerimonas nitrititolerans"
                     /db_xref="taxon:2482751"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33577
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kplmitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmermq khaerfdtev vfdhihtael qqrpfilkgd satyscdali iatgasaqyl
      121 glpsedafag rgvsacatcd gffyrnqsva vigggntave ealylsniak evhlvhrrdk
      181 lrsekilqdk imdkatngni rlhwnhtlee vlgdasgvtg vrlkdalsge eqklelsgvf
      241 iaighkpntd lfqgqlemkd gylkikggse gdatstsipg vfaagdvadh vyrqaitsag
      301 agcmaaldae kyldq
//
LOCUS       WP_125874196             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Ectopseudomonas oleovorans].
ACCESSION   WP_125874196
VERSION     WP_125874196.1
KEYWORDS    RefSeq.
SOURCE      Ectopseudomonas oleovorans
  ORGANISM  Ectopseudomonas oleovorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Ectopseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Ectopseudomonas oleovorans"
                     /db_xref="taxon:301"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38837
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etikklvgqg hqvtvqagag isasipdsay eaagatignd
       61 aaafgadlvl kvvaptdael shmragavlv gmlnpfcnet iarmnargvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarilil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpqswme
      241 rqakavheka kqadivitta lipgrkaptl lheatvqqmk pgsvvidlaa aqggncplte
      301 adkvvvkhgv tlvghtnlaa lvpadasaly arnlldflkl vidkegqfrl nleddivaac
      361 lmcnagevvr kng
//
LOCUS       WP_125880645             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas sp. o96-267].
ACCESSION   WP_125880645
VERSION     WP_125880645.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas sp. o96-267
  ORGANISM  Pseudomonas sp. o96-267
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas sp. o96-267"
                     /db_xref="taxon:2479853"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38866
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth agetrvaatp etirklvgqg hqvtvqagag isasipdsay eaagatignd
       61 saafgadlvl kvvaptdael ahmragavlv gmlnpfcnet iarmnargvt afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarilil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpfetdee recaqgvggy arpmpqswme
      241 rqakavhera kqadivitta lipgrkaptl lheatvqemk pgsvvidlaa aqggncplte
      301 adkvvvkhgv tlvghtnlaa lvpadasaly arnlldflkl vidkegqfql nleddivaac
      361 lmcnagevvr kng
//
LOCUS       WP_125885095             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_125885095
VERSION     WP_125885095.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33350
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaarat lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlknrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_125885478             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_125885478
VERSION     WP_125885478.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38574
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkappl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_125887428             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas luteola].
ACCESSION   WP_125887428
VERSION     WP_125887428.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas luteola
  ORGANISM  Pseudomonas luteola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas luteola"
                     /db_xref="taxon:47886"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34050
     Region          1..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrharvi ilgsgpagyt aavyaaranl kpllitgmqm ggqlttttev dnwpgdphdl
       61 tgpalmermr ehaqrfetei vfdhingvdl ankpftltgd sgtytcdali iatgasaryl
      121 gltseesfmg kgvsacatcd gffyrnreva vvgggntave ealylanias kvtlihrrdt
      181 fraekilqdk lksrvvegki elklnaavde vlgdnmgvtg vrlknndgsm deiqvaglfv
      241 aightpnssl fegqlelkdg yvvvkggres natatsiegv faagdiadht yrqaitsaga
      301 gcmaaldver yldglgdnlw
//
LOCUS       WP_125885849             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Stutzerimonas stutzeri].
ACCESSION   WP_125885849
VERSION     WP_125885849.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Stutzerimonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38841
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpleth sgetrvaatp etvkkmigqg hrvtlqsgag llssvpdsay eavgatigda
       61 aaalaaelvl kvnapdeael aqmqsgsvll gmlnpfdndc iarmaargit afaleaaprt
      121 sraqsldvls sqaniagyka vlvgahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavv easdvrpavk eqieslgakf vdvpletdee recaegvggy arpmpaswma
      241 rqaqavhera lqsdivitta lipgrkaptl lqeatveqmk pgsvivdlaa ghggncplte
      301 idqvvvrhgv tivghanlat lvpadasaly arnlldflkl vidkdgqfql nleddivaac
      361 lmcrdgqvvr tng
//
LOCUS       WP_125891476             477 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Providencia].
ACCESSION   WP_125891476
VERSION     WP_125891476.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Providencia"
                     /db_xref="taxon:586"
     gene            1..477
                     /gene="nrfA"
     Protein         1..477
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53367
     Region          11..477
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 manlrnnalc llslvagifl ftsvhaqtpt kdststinar netfeaahpd qyhswratse
       61 qsnredalae dprlvvlwag ypfsrdynkp rghayaiidv retlrtgapk daqdgplpma
      121 cwsckspdva rliqehgedg yfegkwakgg pevvnvlgca dchktdsadf akgkpeltls
      181 rpyaeramet igkpfdkasr fdqqsmvcgq chveyyfsgd kksvkfpwdn gtkveemevy
      241 ydnigfsdwt nslskapmlk aqhpeyetws agihgknnvt cidchmpklq nekgelytsh
      301 kignpfdnfe qtcstchtqs kqqlqdvvae rkvaiqemki kaedqlvrah feakaawdag
      361 atedemkpil tdirhaqwrw dlaiashgih mhapdeglrm lggsmdkaad artklarllg
      421 skgitheiai pdistkekaq qaigldmqki naekqeflkt vvpqwddqar kndllak
//
LOCUS       WP_125893222             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Providencia].
ACCESSION   WP_125893222
VERSION     WP_125893222.1
KEYWORDS    RefSeq.
SOURCE      Providencia
  ORGANISM  Providencia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Providencia"
                     /db_xref="taxon:586"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34071
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msttthrkli ilgsgpagyt aavyaaranl npalitgvek ggqlttttdv enwpgdpegl
       61 tgpglmermh ehaakfetei isdhiqkvdl kqrpfrligd eneytcdali iatgasaryi
      121 glpseeafkg rgvsacatcd gffyrnqkva vvgggntave ealylsnias evhlihrrds
      181 fraekilinr lmdkvengni ilhtdrtlne vlgddmgvtg vrlectktht tedipvmgaf
      241 iaighspntg ifagqldldn gyikvqsgtq gnatqtsveg vfaagdvmdh iyrqaitsag
      301 tgcmaaldae ryldglask
//
LOCUS       WP_125900546             339 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Brevundimonas sp. 357].
ACCESSION   WP_125900546
VERSION     WP_125900546.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas sp. 357
  ORGANISM  Brevundimonas sp. 357
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Brevundimonas sp. 357"
                     /db_xref="taxon:2555782"
     gene            1..339
                     /gene="trxB"
     Protein         1..339
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35997
     Region          13..318
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqakapart vrvaiigsgp agwtaaiyaa raslnpviia glqpggqlti ttdvenypgy
       61 aetiqgpwlm qqmqaqaehv gtevihdivt qadlsqrpfr ltldsgteil aetviistga
      121 qakwlgldse aeyqgfgvsa catcdgffyr gkqvvvvggg ntaveealfl tnfaetvtvv
      181 hrrdefraek ilqdrlfahp kikviwdvsv eevvgvvdgv arnvtgvrlk nvktgeisei
      241 padgvfiaig hapsselfkg qletnsggyl rvkpgtaata iegvwaagdv tddvyrqavt
      301 aagmgcmaal eaarflaeed hkaaqhpish keaekigaw
//
LOCUS       WP_125905087             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bacillus
            salinus].
ACCESSION   WP_125905087
VERSION     WP_125905087.1
KEYWORDS    RefSeq.
SOURCE      Bacillus salinus
  ORGANISM  Bacillus salinus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Bacillus salinus"
                     /db_xref="taxon:2495421"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55008
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl tgetrvaaip ktveqlkklg fevavesgag erasftdeqy tnagasclna
       61 ekvwqsdviy kinppneeev armkkgttlv sliepaqnkk lmerlnekni nvlamdmvpr
      121 israqsvdvl ssmaniggyr avmeathafg rflngqitaa gkvppakilv igagvaglaa
      181 igagkslgai vrafdtrsev aeqiesmgge flkldldedg stasgyakem seafvraeme
      241 lfaaqakevd iiittalirg rpapklitke mvdsmkpgsv ivdlaastgg nceytvpgel
      301 vvtasgvkii gytdlpgrmp aqasdmyatn lvnltkllck ekdgnihidf ddvilrnmtv
      361 trngqitfpp peisvsaapv kkevqhpkte tkeprnlsgl kygfgiaail lfgwmgqvsp
      421 peflshftvf alaivvgyyv iwkvthalht plmsvtnavs giivvgallq inssilavki
      481 lafigilias inifggftvt hrmlkmfrkd qgv
//
LOCUS       WP_125907567             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bacillus salinus].
ACCESSION   WP_125907567
VERSION     WP_125907567.1
KEYWORDS    RefSeq.
SOURCE      Bacillus salinus
  ORGANISM  Bacillus salinus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Bacillus salinus"
                     /db_xref="taxon:2495421"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34202
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteetiydva iigagpagmt aavyasranl ttvmiergvp ggqmantedv enypgyesil
       61 gpdlsnkmfe hakkfgaeya ygdvkeivdg edhkilkagn kdikaraiii asgaeykklg
      121 vpgekelggr gvsycavcdg affkgkelvv igggdsavee gvyltrfask vtivhrrdel
      181 raqkilqqra fdnekvdfiw dtvvtsinek egkvgsvtlk nvnteeesef aadgvfiyig
      241 lvplskpyes lsitnengyi etndqmetrv pgifaagdir ektlrqivta tgdgsiaaqa
      301 aqhyveelke kqkqqa
//
LOCUS       WP_125927288             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas moraviensis].
ACCESSION   WP_125927288
VERSION     WP_125927288.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas moraviensis
  ORGANISM  Pseudomonas moraviensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas moraviensis"
                     /db_xref="taxon:321662"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38771
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqsgag vkasivdsay eaagasigsa
       61 ndafgaelil kviapsdael tlikrgavlv gmlnpfnnet iakiaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_125922006             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas fulva].
ACCESSION   WP_125922006
VERSION     WP_125922006.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fulva
  ORGANISM  Pseudomonas fulva
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas fulva"
                     /db_xref="taxon:47880"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33552
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msearhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdphgl
       61 tgptlmqrmq ehaerfetei vfdhinavdl ankpftltgd sgtytcdali vatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias kvtlvhrrdt
      181 fraekilidk lharvaegki elklnatlde vlgdnmgvtg arlknndgss deikvdgvfi
      241 aightpntsl fegqltlkdg ylvvsggreg natatnvagv faagdvadhv yrqaitsaga
      301 gcmaaldver yldglanasf
//
LOCUS       WP_125927882             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bacillus canaveralius].
ACCESSION   WP_125927882
VERSION     WP_125927882.1
KEYWORDS    RefSeq.
SOURCE      Bacillus canaveralius
  ORGANISM  Bacillus canaveralius
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Bacillus canaveralius"
                     /db_xref="taxon:1403243"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34025
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseekiydvi iagagpagmt aavytsranl stlmiergvp ggqmanteev enypgfdhil
       61 gpdlstkmfd hakkfgaeya ygdikeiidg eeyktvvags krykahavii ttgaeykkig
      121 vpgekelggr gvsycavcdg affkgkelvv vgggdsavee gvyltrfatk vtivhrrdql
      181 raqailqqra fandkidfiw nhtikeingk dgkvgsvtlv stetgeeqdf padgvfiyig
      241 mvplskpfan lgitnangyi etnelmetkv pgifaagdir ektlrqivta tgdgsiaaqs
      301 aqhfieevke aqkaaka
//
LOCUS       WP_125940873             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_125940873
VERSION     WP_125940873.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33749
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaardae kylddh
//
LOCUS       WP_125942823             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vagococcus humatus].
ACCESSION   WP_125942823
VERSION     WP_125942823.1
KEYWORDS    RefSeq.
SOURCE      Vagococcus humatus
  ORGANISM  Vagococcus humatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Vagococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vagococcus humatus"
                     /db_xref="taxon:1889241"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32806
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhdvivigag pggmtaalya sradldvlvl ergipggqmn ntadvenypg agivtgpdla
       61 rkiyedstnf gathaygnvt giedhgdykv vltddkqyet kaviiasgcd hrqlgvpgee
      121 dysgrgvsyc avcdgaffrn khlavigggd saveegsylt qmaskvtivh rrdqlraqkv
      181 lqdrafknek idlvwnktve eiagddmkvt kvvlkdtqtg elselavdgv fiyvgldplt
      241 epfktlgitn eqgwiptnek metsipgiya igdvretvlr qittavgdgs iagqevfkyi
      301 etltd
//
LOCUS       WP_125947660             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Variovorax].
ACCESSION   WP_125947660
VERSION     WP_125947660.1
KEYWORDS    RefSeq.
SOURCE      unclassified Variovorax
  ORGANISM  unclassified Variovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="unclassified Variovorax"
                     /db_xref="taxon:663243"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34268
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msapqhakvl ilgsgpagyt aavyaaranl qpllitgiaq ggqlmtttev dnwpadvhgv
       61 qgpdlmqrfl ehaerfktqi vfdhinkvdl skrpftltgd sgtytcdsli iatgasakyl
      121 gldseqkfmg rgvsacatcd gffyreqevc vigggntave ealylanian kvtlvhrrdk
      181 fraepilidk vkekvaegki vlklhseldq vlgddsgvtg irikntqtga teqidlkgcf
      241 iaighhpntd ifqgqlemkd nyiltrsglq gfatmtsipg vfaagdvqdn iyrqaitsag
      301 tgcmaaldaq rfleqdgtl
//
LOCUS       WP_125948943             376 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Variovorax].
ACCESSION   WP_125948943
VERSION     WP_125948943.1
KEYWORDS    RefSeq.
SOURCE      unclassified Variovorax
  ORGANISM  unclassified Variovorax
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="unclassified Variovorax"
                     /db_xref="taxon:663243"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38510
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etvkklvasg htvrvqsgag iaasatdgay qaagaeitdq
       61 tgafsadmvl kvrtptesea allksgavvi gmlnpfdaag lqrlaaagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf idvpyetqee kdaaegvggy arpmpaswlt
      241 rqqaevakrv aladvvista lipgraaptl itedmvksmk pgsvivdiaa gkgadgiggn
      301 cplseadktv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvtqd gqvtkk
//
LOCUS       WP_125955039             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Novosphingobium sp. MD-1].
ACCESSION   WP_125955039
VERSION     WP_125955039.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium sp. MD-1
  ORGANISM  Novosphingobium sp. MD-1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Novosphingobium sp. MD-1"
                     /db_xref="taxon:1630648"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34071
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 matthktrml iigsgpaglt aaiygaragm epivvqglqp ggqltittdv enypgfreav
       61 qgpwlvqemq aqaehvgtrm lwdtitevsl egppfravgd sgdiyegdtl viatgaqakw
      121 lgvpgevefg gkgvsacatc dgffyrgkkv vvigggntav eealyltnhs qdvtiihrrd
      181 sfraekilqd rlfahphvrv lwnkkvdrfv gepgkgltgv avidtetgeq svvetdgafv
      241 aighapatel fkgkleldes gyivvqpgtp ktaipgvfaa gdvmdhtyrq avtaagtgcm
      301 aaldaerfva eldfaaskae avg
//
LOCUS       WP_125957941             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vagococcus bubulae].
ACCESSION   WP_125957941
VERSION     WP_125957941.1
KEYWORDS    RefSeq.
SOURCE      Vagococcus bubulae
  ORGANISM  Vagococcus bubulae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Vagococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vagococcus bubulae"
                     /db_xref="taxon:1977868"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33195
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydviiigag pggmtsalya srsglsvlvi ergapggqlm ntdevenypg fnlisgpdla
       61 lkmyenssnf gakhvygnvv niedhgttkk vvcddetyeg ktviiasgse hrkinipgee
      121 eyagrgvsyc avcdgaffrd rhlvvigggd saieegmylt qfaskvtiih rrdelraqki
      181 lqdrafknek iefmwnkvpi eingndmsvq siklkdtktg diedlladgv fiyigldplt
      241 dfvkdlgitn ehgwietdah mstkipgiya igdvretvlr qiatavgdgs iagqevynyl
      301 ssldd
//
LOCUS       WP_125960396             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Sphingomonas].
ACCESSION   WP_125960396
VERSION     WP_125960396.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34329
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtthttrmli lgsgpaglsa aiygaragln pivvqgiqpg gqlttttdve nypgfaeviq
       61 gpwlmeqmqa qaehvgtrmm ydtivevdvs qrpfrligdg gdvyegdvlv iatgaqarwl
      121 gleteealkg kgvsacatcd gffyrgkkva vigggntave ealyltnhsp dvtiihrrds
      181 fraekilqer lfahdavsvl wnkkverfid gggnvglvgi elkdtvtgel sqievdggfv
      241 aighhpatel frghvelded gyivvekgst rtnvpgvfac gdvtdkvyrq avtaagtgcm
      301 aaldaerfla eadfekiaea ae
//
LOCUS       WP_125962139             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingomonas sp. ABOLF].
ACCESSION   WP_125962139
VERSION     WP_125962139.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. ABOLF
  ORGANISM  Sphingomonas sp. ABOLF
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Sphingomonas sp. ABOLF"
                     /db_xref="taxon:1985879"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38948
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlseaa pderrvsata etvkkfvqlg arvaveagag rsasvadady aaagatlgsr
       61 aevladadvv lavqgpapes ltgikpgawl vaglnpfger arvdgyaalg iealamewmp
      121 ritraqsmdi lssqsnlagy kavidaaaay grafpmmmta agtvsaarvf vmgvgvaglq
      181 aiatarrlga qvsatdvrsa tkeqiqslga kpifvenvag iegegsggya temspdyqka
      241 qaelvsshla kqdvvittal ipgrpaprli sdaqlqtmrp gsivvdlave qggnvegava
      301 gevverhgvr ilghrnvpsr laadtsalfa rnlynflsay wekdagrpvl pdedevtqgi
      361 rltrggavvh prllqa
//
LOCUS       WP_125963972             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bifidobacterium dolichotidis].
ACCESSION   WP_125963972
VERSION     WP_125963972.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium dolichotidis
  ORGANISM  Bifidobacterium dolichotidis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Bifidobacterium dolichotidis"
                     /db_xref="taxon:2306976"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33680
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtekqelrdv iiigsgpagy taaiylgrag lkplviagal tpggqlintt evenfpgfpd
       61 gimgpdlmen mqrqaerfga elvfddvidt slegeekvvr vsggdefrsr avivatgsny
      121 rhldvpgede ysgrgvsyca tcdgfffrnk pivvvgggds afeeaqflsr fgssvtlihr
      181 rnefraskim vdraianpkl dmvldsvves ingdgtsaes vtvrnlktde ittipangvf
      241 vavghipqtg flgdqvrldd rgyvltegas trtnlpgvfa agdcadpvym qaisaagmgc
      301 raaldvqsfl edaplgq
//
LOCUS       WP_125965459             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            beijingensis].
ACCESSION   WP_125965459
VERSION     WP_125965459.1
KEYWORDS    RefSeq.
SOURCE      Variovorax beijingensis
  ORGANISM  Variovorax beijingensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax beijingensis"
                     /db_xref="taxon:2496117"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38536
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetm agetrvavtp etvkklaasg htvrvqsgag iaasvtdaay qaagaeitda
       61 tgafgadmvl kvrtptdaet almkpgtvvi gmlnpfdaag lqrlataglt afaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy arpmpaswla
      241 rqqvevakrv aladivista lipgraaptl itedmvkamk pgsvivdiaa gkgpdgvggn
      301 cplseadktv vkhgvtivge tnlpalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvaqd gqvtkq
//
LOCUS       WP_125969238             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter baumannii].
ACCESSION   WP_125969238
VERSION     WP_125969238.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter baumannii
  ORGANISM  Acinetobacter baumannii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Acinetobacter baumannii"
                     /db_xref="taxon:470"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33694
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdpeglt
       61 gpvlmdrmqa haerfgtelv ydhinevdln vrpfvlkgdm deytcdalii atgataqylg
      121 leseqkfmgq gvsacatcdg ffyknqnvmv vgggntavee alylsniaeh vtlvhrrdsl
      181 rsekilqdhl fakekegkis mvwnheveev lgdntgvtgv rlkstkddsk qevqvqglfi
      241 aighkpntsm fegqlnlrdg yiqvqsgtsg natatsvagv faagdvadsi yrqaitsags
      301 gcmaaldaek yldnl
//
LOCUS       WP_125971680             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Iodobacter
            ciconiae].
ACCESSION   WP_125971680
VERSION     WP_125971680.1
KEYWORDS    RefSeq.
SOURCE      Iodobacter ciconiae
  ORGANISM  Iodobacter ciconiae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chitinibacteraceae; Iodobacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Iodobacter ciconiae"
                     /db_xref="taxon:2496266"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40854
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,292,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,282..283,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mliaipaeay pgefrvaatp etikklikag htvrvestag lhaaisdaay teagaeialh
       61 pealyqgaql ilkvrapqah elpllpdhaa lvalfdihry thldtlnskn isayalelvp
      121 ritraqsmdv lssqaniagy raillatqyy prfmpmlmta agtvkparvl ilgagvaglq
      181 aiatakrlga ivevfdvrpa treqveslgg kfievalsed ekaatetsgg yaremsdnyk
      241 lrqtllidqq arladiiist aqipgktapi lipektvkam kagsviidla vdsggncpls
      301 radevvhsen gvvivghgnl asllaadasa lyarnmlafi sllqdssgty aphfddeiik
      361 atlishqgvl skvsepapvp ilaqpa
//
LOCUS       WP_125976120             323 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Sphingomonas].
ACCESSION   WP_125976120
VERSION     WP_125976120.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas
  ORGANISM  Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Sphingomonas"
                     /db_xref="taxon:13687"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34392
     Region          7..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtathstrml ilgsgpagls aaiygaragl apivvqgiqp ggqlmtttdv enypgfrevi
       61 qgpwlmqemq aqaehvgaqm mwdtiveidv sqrpfrlvgd ggtvytgdtl viatgaqarw
      121 lgldseellk gkgvsacatc dgfffrgkkv avigggntav eealyltnhs hdvtlihrrd
      181 slraekilqq rlfaneritm awnkevvrfi gggqpeglva ielkdtvtge lsmlevdggf
      241 vaighhpate lfrghialdd dgyiqvekgt tntsvpgvfa cgdvmdkhyr qaitaagtgc
      301 maaldaerfl aaadfetvaq aae
//
LOCUS       WP_125978688             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lactobacillus acidophilus].
ACCESSION   WP_125978688
VERSION     WP_125978688.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus acidophilus
  ORGANISM  Lactobacillus acidophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Lactobacillus acidophilus"
                     /db_xref="taxon:1579"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33694
     Region          5..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 madkydvivi gagpggmtaa lyatranlnv lvldrgpygg qmnntdaidn ypgftevkgp
       61 elsqkmydtl mkfepdykyg nvqsveldgd ekviktddee yrapvlivat gadhrhlnvp
      121 geeeysgrgv sycavcdaaf fkdedvvvvg ggdsaieegi ylsqmaksvt vihrrdqlra
      181 qptlqkrafa nekmkfiwna qteeilgdgn rvtgvkyldk engetkevsa agvfiyvgvl
      241 pqtepfkklg ilneqgwipt nehmetkvsg ifalgdvrdk dlrqianavg egsvagqaay
      301 nyfqdlkn
//
LOCUS       WP_125972498             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Iodobacter ciconiae].
ACCESSION   WP_125972498
VERSION     WP_125972498.1
KEYWORDS    RefSeq.
SOURCE      Iodobacter ciconiae
  ORGANISM  Iodobacter ciconiae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Chitinibacteraceae; Iodobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Iodobacter ciconiae"
                     /db_xref="taxon:2496266"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33215
     Region          8..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 matqharlli lgsgpagyta avyaaranln pvmvtglaqg gqlmtttdvd nwpadadgvq
       61 gpelmarfqk haerfgtemi fdhihtthln ekpirlvgds geytcdalii atgasaqyig
      121 lpseeafagr gvsacatcdg ffyrnqqvav vgggntavee alylsniaah vtlvhrrdtf
      181 rsekilidhl mekvatgkit lainstldev lgdatgvtga rlkstidgtt rdieltgvfi
      241 aighkpntdi fkgqlemdas gyiitkggrd ggstgtnipg vfaagdvqdh iyrqavtsaa
      301 sgcqaaldad kylgasv
//
LOCUS       WP_125978935             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lactobacillus acidophilus].
ACCESSION   WP_125978935
VERSION     WP_125978935.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus acidophilus
  ORGANISM  Lactobacillus acidophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Lactobacillus acidophilus"
                     /db_xref="taxon:1579"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33698
     Region          26..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkkydvaiig agpggmaaal yaaranltva midrgvygrq mnntaeveny pgfpsilgpe
       61 lgekmyqntv kqgvnfvygd vqgievkddk rivklgseds dietkaviig tgssnrklgv
      121 pgedeysgkg vsycavcdga ffknenvvvv gggdsavseg lylanvtdnv nvihrrdqlr
      181 aeqvlqkraf knpkmdftwd sevkeiigde nkmtgvkvhn kktgkdetid angafiyign
      241 ipnsepfrdl nitdkdgwil tndqmetevp gifaigdvrk kklrqiitav ndggiagqna
      301 yeyiqklten
//
LOCUS       WP_125987285             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Halocella sp. SP3-1].
ACCESSION   WP_125987285
VERSION     WP_125987285.1
KEYWORDS    RefSeq.
SOURCE      Halocella sp. SP3-1
  ORGANISM  Halocella sp. SP3-1
            Bacteria; Bacillati; Bacillota; Clostridia; Halanaerobiales;
            Halanaerobiaceae; Halocella.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Halocella sp. SP3-1"
                     /db_xref="taxon:2382161"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33339
     Region          14..291
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdkikkekl iiigggpagl taaiyglrag ldplvlmgpe pggqittspe ienfpgfpgg
       61 ingfelmqkv iqqvesfegr layemvdeln lkqkpytikt gnqvyqtdti iiatgasprk
      121 lglvregell gqgvsycatc dgaffkgqav avvgggdval eeasylsgfa skvylihrrn
      181 qfrgtkllad rlisnpklei lwnsevrdll gdeklsgivv ennktnekkv lndvrglfia
      241 igynpnvslf egiieldesg fiktndrymt niegvfaagd vqdplyqqvv tsagsgaaaa
      301 ieagqyidsl l
//
LOCUS       WP_125982766             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vagococcus vulneris].
ACCESSION   WP_125982766
VERSION     WP_125982766.1
KEYWORDS    RefSeq.
SOURCE      Vagococcus vulneris
  ORGANISM  Vagococcus vulneris
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Vagococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Vagococcus vulneris"
                     /db_xref="taxon:1977869"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32992
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydviiigsg pagmtaalya srsglsvlvi ergapggqmm ntsevenypg fdmiqgpdla
       61 ikmydnaikf gtenaygnvq riedkgdykv vvcedasyea ktviiatgse hrkigipgee
      121 gfsgrgvsyc avcdgaffrd khlvvvgggd saveeglylt qfaskvtivh rrdqlraqni
      181 lqdrafkner vdfiwnhvpi eikgddtkvt sirlenvvtk eqadfeadgv fiyigldplt
      241 epfknmgitd segwiltner metaipgvfa vgdvrktvlr qiatavgdgs iagqevynyl
      301 qnl
//
LOCUS       WP_125989317             400 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Halocella sp. SP3-1].
ACCESSION   WP_125989317
VERSION     WP_125989317.1
KEYWORDS    RefSeq.
SOURCE      Halocella sp. SP3-1
  ORGANISM  Halocella sp. SP3-1
            Bacteria; Bacillati; Bacillota; Clostridia; Halanaerobiales;
            Halanaerobiaceae; Halocella.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Halocella sp. SP3-1"
                     /db_xref="taxon:2382161"
     gene            1..400
                     /gene="trxB"
     Protein         1..400
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=44270
     Region          20..288
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
     Region          305..389
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mdkydlviig ggpagmaaal ygsrsrlntm vleakrktgg qpstyhdmen ypgvpettas
       61 elmdnfrtha ekfgtefkrg evvnvavdgl ekiiktkegq eytaksiiia tgakprrlgi
      121 kgeeefkgkg vsycatcdad ifedldivvv gngnsavees iyltkfvnkl tmivihdegv
      181 mdaekilqek amnnekinfv wnsvveeikg eglvekavvk niktnelsei dcngvfffvg
      241 rvpstdfled tveltengyi ktnnevetnv pgvfaagdvr dkvirqvita agdgataavl
      301 aqgyieeedy wqnnvlksdn pvivafwsvt dknsmdtisk leemnledkd yrfvkidtyk
      361 nrlissryni keipaviklv ngkveerlvn pstekieksi
//
LOCUS       WP_125995524             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingomonas sp. S-NIH.Pt15_0812].
ACCESSION   WP_125995524
VERSION     WP_125995524.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. S-NIH.Pt15_0812
  ORGANISM  Sphingomonas sp. S-NIH.Pt15_0812
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sphingomonas sp. S-NIH.Pt15_0812"
                     /db_xref="taxon:1920129"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34194
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mathstrmli lgsgpaglsa aiygaragmk pivvqgiqpg gqltttteve nypgfadviq
       61 gpwlmeqmqk qaehvgttlm wdtivsvdls rrpfrligdg gdvyegevlv iatgaqakwl
      121 gldseeamkg kgvsacatcd gffyrgkkva vigggntave ealyltnhsd dvtlihrrds
      181 lraerilqer lfahpnitvl wnkevrtfvd gggtaglval dledtvtgeh srldvaggfv
      241 aighhpatel frghlalded gyivvetgst rtsvagvfac gdvadkvyrq avtaagtgcm
      301 aaldaerflq aeefaelqqa ae
//
LOCUS       WP_126002425             337 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingomonas sp. ABOLE].
ACCESSION   WP_126002425
VERSION     WP_126002425.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. ABOLE
  ORGANISM  Sphingomonas sp. ABOLE
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Sphingomonas sp. ABOLE"
                     /db_xref="taxon:1985878"
     gene            1..337
                     /gene="trxB"
     Protein         1..337
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35193
     Region          19..321
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maveieisea avpsarhskv liigsgpagy taavyaaraa laptlikgpq pggqltitte
       61 venwpgdasv lgpdlmarmg eqvrtagvdv vsdmivevdl artpfravgd ggthytadti
      121 viatgassrw leldseaeyr grgvsacatc dgffyrgrvc avvgggntav eealyltnfa
      181 ekvylihrrd tlradrtnqt rlhanpkiem vwnaevadvl gdgggvtgva lrdtrdgtfs
      241 qlavhglfva ighdpattlf kgqlhmddeg yilvthgsta tsvpgvfaag dvqdklfrqa
      301 vtsagmgcma aleaerylag hnaraiaadg adtgmtv
//
LOCUS       WP_126009229             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Georhizobium profundi].
ACCESSION   WP_126009229
VERSION     WP_126009229.1
KEYWORDS    RefSeq.
SOURCE      Georhizobium profundi
  ORGANISM  Georhizobium profundi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Georhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Georhizobium profundi"
                     /db_xref="taxon:2341112"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34553
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mserhtpvli igsgpagyta aiyaaramlk piviagmeqg gqlmittdve nypgyadpvq
       61 gpwmmeqmln qainvgaeiv ndlvvevetd rrpfrvrtdg gqvftadali iatgakakwl
      121 gieseqnfmg fgvsacatcd gffyrgkdva vvgggntave ealylsnlak svtlihrreg
      181 lraerilqdr lfakdnvsvv wnavideitg tpakppmpps vtgvrlkdtq tgeikdlavd
      241 gvfvaighap avdlfkdklr mkpngylwsa pdstatdvpg ifaagdvtdd vyrqavtaag
      301 mgcmaaleve rylagyvhia eaae
//
LOCUS       WP_126011925             399 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Georhizobium profundi].
ACCESSION   WP_126011925
VERSION     WP_126011925.1
KEYWORDS    RefSeq.
SOURCE      Georhizobium profundi
  ORGANISM  Georhizobium profundi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Georhizobium.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Georhizobium profundi"
                     /db_xref="taxon:2341112"
     Protein         1..399
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40842
     Region          7..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 makllfiake kapgesrvag spdtvkklva aglevvvead agsqsripda efekagatig
       61 taadaaradv vlkvrrpdae eaagyksgai viaimdpygh ndliadlgsk glttfamelm
      121 pritraqsmd vlssqanlag yqavidaaaa fdrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatakrlg aavsatdvrp askeqvaslg gkfiavedee fkaaetaggy akemskeyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vtadmiasmr pgsilvdlav erggnvegav
      301 agevvdkngv riigynnvpg riaasaslly aknlltflqt mikdgdiain fddelvkata
      361 lthggkvihp nfgggtpapt papppqatea vaatnkgda
//
LOCUS       WP_126013290             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus albus].
ACCESSION   WP_126013290
VERSION     WP_126013290.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus albus
  ORGANISM  Paenibacillus albus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus albus"
                     /db_xref="taxon:2495582"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33671
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mykaiiigtg pagltaaiyl aranmnplvi egpepggqlt tttevenfpg fpdgimgpdl
       61 manmrkqaer fgaefrtgwv nsvdtskrpf tlqvegqgel qaesliistg asakylgian
      121 erenvgkgvs tcatcdgfff rgkkiivvgg gdsameeanf ltrfasevvl vhrrpemras
      181 kimqdraren skiswaldrt plevvatgmg vtglkvrnna tgeeevietn gifvaightp
      241 ntkflggqln tdetgyllvk pgtsetnipg ifacgdvqdn kyrqaitaag sgcmaaldce
      301 kyleghavhd wsqtv
//
LOCUS       WP_126014057             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus albus].
ACCESSION   WP_126014057
VERSION     WP_126014057.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus albus
  ORGANISM  Paenibacillus albus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paenibacillus albus"
                     /db_xref="taxon:2495582"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33872
     Region          3..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 medivivgtg pagltaaiyl aragysplvl egpqpggqlt tttevenfpg fpegvlgtdl
       61 manmrqqaek fgarfqtgwv qstdlskrpf kltfengsem ftqsmiistg asakymgipg
      121 erdnigrgvs tcatcdgfff rgkkiivvgg gdsameeagf ltrfasevrl vhrreelras
      181 kimqdraran dkikwslgvt pleveageqg lrglrvhdna tgeetllead gvfvaightp
      241 ntgflggqvt tdelgyiavq pgtsltnipg vyacgdvqdh ryrqaitaag sgcmaaldce
      301 helevfkagr lkeevnv
//
LOCUS       WP_126022261             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            guangxiensis].
ACCESSION   WP_126022261
VERSION     WP_126022261.1
KEYWORDS    RefSeq.
SOURCE      Variovorax guangxiensis
  ORGANISM  Variovorax guangxiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax guangxiensis"
                     /db_xref="taxon:1775474"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38523
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeil agetrvavtp etvkklvasg htvrvqsgag vaasatdaay qaagaeitdq
       61 agafsadmvl kvrtpteaet allkpgavvi gmlnpfdaag lqrlaaagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf idvpyetqee kdaaegvggy arpmpaswls
      241 rqqaevakrv aladvvista lipgraaptl itedmvksmk pgsvivdiaa gkgpdgvggn
      301 cplseadktv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvthd gqvtkk
//
LOCUS       WP_126030648             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bifidobacterium callimiconis].
ACCESSION   WP_126030648
VERSION     WP_126030648.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium callimiconis
  ORGANISM  Bifidobacterium callimiconis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Bifidobacterium callimiconis"
                     /db_xref="taxon:2306973"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33409
     Region          6..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdirdaiii gsgpagytaa iylaragyqp lviagvlnpg gqlintteve nfpgfpegvl
       61 gpdlmdrmre qaekfgamie yddvtsvdfs dttpgairtv rtdggneyra rtvivatgse
      121 prklgvpgeq efsgrgvsyc atcdgfffrd kpivvvgggd sameeadfls rfgssvtlvh
      181 rrdefrasri mieraqqnpk iefvmntvvd eihgdnanga tsvtlrdvtt getrdidang
      241 vfvaightpq tafldgalel agdgtvivdg gstrtsvpgv faagdnadsv yrqaisaagm
      301 gcraaldaqm ylvete
//
LOCUS       WP_126031546             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bifidobacterium castoris].
ACCESSION   WP_126031546
VERSION     WP_126031546.1
KEYWORDS    RefSeq.
SOURCE      Bifidobacterium castoris
  ORGANISM  Bifidobacterium castoris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Bifidobacterium castoris"
                     /db_xref="taxon:2306972"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33148
     Region          6..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseirdviii gsgpagytaa iylgraglrp lviagaltpg gqlvntteve nfpgfpdgvl
       61 gpdlmesmqr qaerfdaelv yddvesveld etvktvrcsg gdvyrtravi vatgsyyrhl
      121 dvpgeeeyag rgvsycatcd gfffrgkpiv vvgggdsame eagflsrfgs svtllhrrdq
      181 frasrimvdr tlanpaidvm tntvvtging dgkavtsvsv rdvstgeere ldangvfiaa
      241 gqipqtaflg galalddhgy iivdgagtrt nvpgvfaagd cadpvyqqai saagtgcraa
      301 idvqmylesl ieeaga
//
LOCUS       WP_126034323             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Mesorhizobium].
ACCESSION   WP_126034323
VERSION     WP_126034323.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34557
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gtiytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilser lfkkdnvrvi wdtvvdeitg qsgkmplpps veglklrnlv tgqemhltvd
      241 gvfvaighap avelfagklk qkpngylwta pdstctdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_126037165             429 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M9A.F.Ca.ET.002.03.1.2].
ACCESSION   WP_126037165
VERSION     WP_126037165.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M9A.F.Ca.ET.002.03.1.2
  ORGANISM  Mesorhizobium sp. M9A.F.Ca.ET.002.03.1.2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Mesorhizobium sp. M9A.F.Ca.ET.002.03.1.2"
                     /db_xref="taxon:2493668"
     Protein         1..429
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44005
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvvvetg agtrsripde efakagaaig
       61 kagdvakadv vlkvrrpdea elkayrpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemsreyqa
      241 kqatltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafle tlvdkttktl avnrdddlvk
      361 atmltdggqv vhpafagkpa vmiasaepvk paaaktpaaa kkpaapkkla apkkpaapks
      421 aapkskgva
//
LOCUS       WP_126039635             506 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Flaviflexus salsibiostraticola].
ACCESSION   WP_126039635
VERSION     WP_126039635.1
KEYWORDS    RefSeq.
SOURCE      Flaviflexus salsibiostraticola
  ORGANISM  Flaviflexus salsibiostraticola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Flaviflexus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Flaviflexus salsibiostraticola"
                     /db_xref="taxon:1282737"
     Protein         1..506
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52014
     Region          1..505
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpaeqg qtlvaatpdt vaqliklgyd vavetgagae aqfpdeqyis agariveaee
       61 awssdivtsi rppaelerir rggiliskls pganpalvea laeqgvtama mdaiprisra
      121 qsmdvlssqa nvagyravve aahafgrlft gqvtaagkvp paniyvigag vaglaaigta
      181 gsmgavvrat dirsevgeqv esmgaefvai papaqessdg yakemtdaqa eaaatlyaeq
      241 taradivist asipgrrspi litadmvdam kpgsvivdma aagggncelt epgrtivten
      301 gvtiigiedl aarlpaqssq lyaqnivnyl klltpekdgr aainfddvii rtvtvadagq
      361 vmwppppiqv saapapkvvd papvaeeapa agglkkstiw lalaavlgaa lvlvspvgmt
      421 ghyivlalav ivgfyvitnv thalhtplms vtnaisgiii vgaiiligsg swvvtifsfi
      481 aivissinif ggfavthrml gmfrra
//
LOCUS       WP_126040904             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flaviflexus salsibiostraticola].
ACCESSION   WP_126040904
VERSION     WP_126040904.1
KEYWORDS    RefSeq.
SOURCE      Flaviflexus salsibiostraticola
  ORGANISM  Flaviflexus salsibiostraticola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Flaviflexus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Flaviflexus salsibiostraticola"
                     /db_xref="taxon:1282737"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32845
     Region          5..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteihdiiiv gsgpagytaa iytaraglnp ivlagaidag galmttteve nfpgfpegiq
       61 gpelmenmre qaerfgadvr fedavelkle gdikeiktdt adhrakavil algseyrklg
      121 legestysgk gvswcatcdg fffkgqeiav vgggdsavte alfltkfask vtvihrrdel
      181 raskvmadrl ladekvemaw nsavtkingt pdgrlqsvtl tdtktgeqre lpvgglfiai
      241 ghdprtaivk deinldangy itvdqpttat sipgvfacgd vvdhryrqai taagtgcsaa
      301 ldaesyldal
//
LOCUS       WP_126045031             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Candidatus Aquarickettsia
            rohweri].
ACCESSION   WP_126045031
VERSION     WP_126045031.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Aquarickettsia rohweri
  ORGANISM  Candidatus Aquarickettsia rohweri
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Candidatus Midichloriaceae; Candidatus
            Aquarickettsia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Candidatus Aquarickettsia rohweri"
                     /db_xref="taxon:2602574"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33987
     Region          8..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtfkkfktev liigsgpagy saaiyaarsa lnpilvsgsq pggqltittd venypgfaet
       61 iqgpwlmeqm kqqsekagte findtiknve ltknpfiasg dsgnvyeaks iiiatgaqak
      121 wlglesekky mgfgvsgcat cdgffyknke vivvgggnta veeslyltnh askvtlihrr
      181 dslraekilq erlfnhpkih ilwdtvllev lgtdkplsve gakiknlktg redkikidgi
      241 fiaighkpnt elfkgsidmd degyiithpd stktstpgif asgdvqdkiy rqavtaagtg
      301 cmaalevskf lete
//
LOCUS       WP_126047696             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Siminovitchia acidinfaciens].
ACCESSION   WP_126047696
VERSION     WP_126047696.1
KEYWORDS    RefSeq.
SOURCE      Siminovitchia acidinfaciens
  ORGANISM  Siminovitchia acidinfaciens
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Siminovitchia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Siminovitchia acidinfaciens"
                     /db_xref="taxon:2321395"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34634
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msedkiydvi iagagpagmt aavytsranl stlmiergvp ggqmadtadv enypgfdhil
       61 gpdlstkmfe hakkfgaeya ygdikeivdg deykvvkagn keykayaviv ttgaeyrkig
      121 vpgeaeltgr gvsycavcdg affkdkelvv igggdsavee gayltrfask vtiihrrdel
      181 raqkilqdra fandkidfiw shtvkqvnee dgkvgsltlv stkdgsekef ktdgmfvyig
      241 mdpltqsvah lgitneegyi etnenmatrv pgifaagdvr dkllrqivta tgdgsiaaqs
      301 aqiyierlkd eqlakkqaea
//
LOCUS       WP_126057004             424 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_126057004
VERSION     WP_126057004.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..424
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43719
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneqrvaa spdtvkrlag lgfevvvekg agtgsripde efakagaaig
       61 kaadaskadv vlkvrrptdt elkgykqgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvaamk pgsvivdlav erggnvegae
      301 agkvvttang vkivghlnvp grvaasasll yaknlfafle tlvdkesktl aikrddelvk
      361 atmltdagqv vhpnfakadq qprvepaaip attmaadaap kaapkkaadk kstskpaaks
      421 kgia
//
LOCUS       WP_126059818             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_126059818
VERSION     WP_126059818.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34340
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmsqmla qaehvgtdii ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrsd
      181 fraerilrer llakdnvrvi wdtvvdeitg rpgkaplpps vegltlrnvv tgqesklpvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_126058744             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_126058744
VERSION     WP_126058744.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34547
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdiv ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrgd
      181 fraerilrer lfkkenvrvi wdtvvdeitg qpgkaplpps vegltlrnvv tgevtrlkvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_126063115             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M2A.F.Ca.ET.043.05.1.1].
ACCESSION   WP_126063115
VERSION     WP_126063115.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M2A.F.Ca.ET.043.05.1.1
  ORGANISM  Mesorhizobium sp. M2A.F.Ca.ET.043.05.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mesorhizobium sp. M2A.F.Ca.ET.043.05.1.1"
                     /db_xref="taxon:2493671"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43054
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqivfipre ldpneprvaa spetvkrlag lgfdvivekg aglgsripdq dfaavgavig
       61 kasdagradv vlkvrrptda elkgykpgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkttktl aikrddelvk
      361 atmltdggrv vhpafakaae eprtepaaip attmvaeaad akpaakkkaa akpkgta
//
LOCUS       WP_126067379             427 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M7D.F.Ca.US.005.01.1.1].
ACCESSION   WP_126067379
VERSION     WP_126067379.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7D.F.Ca.US.005.01.1.1
  ORGANISM  Mesorhizobium sp. M7D.F.Ca.US.005.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Mesorhizobium sp. M7D.F.Ca.US.005.01.1.1"
                     /db_xref="taxon:2493678"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43858
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglnsriida dyasagaaig
       61 kasdvakadv vlkvrrpgda elksykpgta viaimdpygn daavtalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafakadq qprvepaaip attmvadasv kpatakkaap kkaaapksps
      421 skpkgia
//
LOCUS       WP_126071427             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Candidatus Annandia adelgestsuga].
ACCESSION   WP_126071427
VERSION     WP_126071427.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Annandia adelgestsuga
  ORGANISM  Candidatus Annandia adelgestsuga
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Candidatus Annandia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Candidatus Annandia adelgestsuga"
                     /db_xref="taxon:1302411"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35540
     Region          4..313
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 miktkliilg sgpagytaai yasranlypi litglekggq ltktlkienw pgdyknitgn
       61 dlmnrmyiha kkfntniifd niykvdlkny pfrligdyne yysdsliist gsspkyleik
      121 seekfkgkgl stcatcdgyf yrnktvaivg ggnkaieeal ylsnivkkih iihrnnifka
      181 ekillnqlkn kiidnkviih tdfflkeiig ndkniksini cynknkkiik kikvsgvfis
      241 ighkpntylf knqlklknny iyikknkiys tqtsipgvfa agdvidknyk qaitaagsgc
      301 msaidaikyi nsikkk
//
LOCUS       WP_126073865             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Massilia
            atriviolacea].
ACCESSION   WP_126073865
VERSION     WP_126073865.1
KEYWORDS    RefSeq.
SOURCE      Massilia atriviolacea (Mokoshia atriviolacea)
  ORGANISM  Massilia atriviolacea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Massilia atriviolacea"
                     /db_xref="taxon:2495579"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38947
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr sgetrvaatp etvkklaakh qvvvqagagv masvtdeaya aagatigsaa
       61 dafgcdvvlk vrapnaeerp lmkadavlig mlnpfdsenl aamagarlra faleavprit
      121 raqsmdvlss qaniagykav mmaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfi dvpyltdeek eiaqgsggya rpmpadwmrr
      241 qgelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlavs qggncplsel
      301 nktvtrhgvh iigepdlatl vaadasalya rnvldflkli idkdeqltid redeilkatl
      361 vcadgtvlrk
//
LOCUS       WP_126076445             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Massilia atriviolacea].
ACCESSION   WP_126076445
VERSION     WP_126076445.1
KEYWORDS    RefSeq.
SOURCE      Massilia atriviolacea (Mokoshia atriviolacea)
  ORGANISM  Massilia atriviolacea
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Telluria group; Massilia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Massilia atriviolacea"
                     /db_xref="taxon:2495579"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33980
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mtttkhakvl ilgsgpagys aavyaaranl qpmlvtgveq ggqlmtttdv enwpgdpmgv
       61 qgpdlmqrll qhaerfntei vfdhihttkl nekpmrligd sheytcdali iatgasaqyl
      121 glesetafmg kgvsacatcd gffyrnqeva vvgggntave ealylsnian kvtiihrrdk
      181 fraepilidr lnakaaegki vikynhtlee vlgndsgvtg vnikstvdga itplsvhglf
      241 vaighkpnts ifegqldmhn gyiktrtgle gmatatnipg vfaagdvqdh iyrqaitssg
      301 tgcmaaldaq ryleslnd
//
LOCUS       WP_126079587             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M2A.F.Ca.ET.046.03.2.1].
ACCESSION   WP_126079587
VERSION     WP_126079587.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M2A.F.Ca.ET.046.03.2.1
  ORGANISM  Mesorhizobium sp. M2A.F.Ca.ET.046.03.2.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mesorhizobium sp. M2A.F.Ca.ET.046.03.2.1"
                     /db_xref="taxon:2493674"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43041
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maraifipre ldpneprvaa spetvkrlvg lgfdvivekg aglgsrildq dfaavgaaig
       61 kaadaskadv vlkvrrptda elkgyksgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvttdng vkivghlnvp grvaasasll yaknlyafle tmvdkttktl aikrddelvk
      361 atmltdggrv vhpnfaraae eprtepaavp attmvaeaad akpaakkkaa akpkgta
//
LOCUS       WP_126079867             417 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_126079867
VERSION     WP_126079867.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43008
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqivfipre ldpneprvaa spetvkrlvg lgfdvivekg aglgsripdq dfaavgavig
       61 kasdagradv vlkvrrptda elkgyksgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdktaktl aikrddelvk
      361 atmltdggrv vhpafakaae eprtepaaip attmvaeaad akpaarkkaa akpkgta
//
LOCUS       WP_126081713             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_126081713
VERSION     WP_126081713.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34375
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmsqmla qaehvgtdiv ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrnd
      181 fraerilrer llakdnvrvi wdtvvheitg rpgkaplpps vegltlrnvv tgqesklpvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_126086303             426 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_126086303
VERSION     WP_126086303.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43709
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlvg lgfgvivekg aglgsritdq dfaaagaaig
       61 kaadaskadv vlkvrrptda elkgykpgaa viaimdpygn daalaamaka gvtafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgraapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatkel aikrddelvk
      361 atmltdggqv vhpnfskaae aprtepaaip atiivadast kpvakktaak kpaaaksass
      421 kskgta
//
LOCUS       WP_126087309             428 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M1D.F.Ca.ET.043.01.1.1].
ACCESSION   WP_126087309
VERSION     WP_126087309.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M1D.F.Ca.ET.043.01.1.1
  ORGANISM  Mesorhizobium sp. M1D.F.Ca.ET.043.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Mesorhizobium sp. M1D.F.Ca.ET.043.01.1.1"
                     /db_xref="taxon:2493669"
     Protein         1..428
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43993
     Region          6..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(19,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maatqtifip reldaneprv aaspetvkrl vglgfevive kgaglgsrii dqdfaaagaa
       61 igkaadaska dvvlkvrrpt daelkgykpg aaviaimdpy gndaavaama kagitafsme
      121 fmpritraqv mdvlssqanl agyqavvdaa aeydralpmm mtaagtvpaa ktfimgvgva
      181 glqaiatarr lgavvtatdv rpavkeqvqs lgakflaved eefkaaetag gyakemskey
      241 qakqaaltae hiakqdivit talipgraap klvsaamvas mkpgsvivdl averggnveg
      301 avpgkvvtte ngvkivghln vpgrvaasas llyaknlyaf letmvdkatk elaikrddel
      361 vkatmltdgg qvvhpnfska aeaprtepaa ipatiivada stkpvakkta akkpaaaksa
      421 sskskgta
//
LOCUS       WP_126088099             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_126088099
VERSION     WP_126088099.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34486
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntrhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdiv ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylanlak svtvihrrgd
      181 fraerilrer lfkkdnvrvi wdtvvdeitg qpgkaplpps veglklrnva tgdvsrlkvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_126090602             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M1E.F.Ca.ET.045.02.1.1].
ACCESSION   WP_126090602
VERSION     WP_126090602.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M1E.F.Ca.ET.045.02.1.1
  ORGANISM  Mesorhizobium sp. M1E.F.Ca.ET.045.02.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. M1E.F.Ca.ET.045.02.1.1"
                     /db_xref="taxon:2493672"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43388
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqsvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsritdq dfaaaggtig
       61 tagdakkadv vlkvrrptda elkgyksgaa viaimdpygn daalaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaace ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedde fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatktl aikrddelvk
      361 atmltdagqv vhpnfakaag eprtepaaip aktmvadaap kkvaakkpaa aksasskskg
      421 ta
//
LOCUS       WP_126092434             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_126092434
VERSION     WP_126092434.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34414
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgteiv ndiitevdln vrpfraagds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylanlak svtvihrrgd
      181 fraerilrer lfkkdnvrvi wdtvvdeitg qpgkaplpps veglklrnva tgdvsrlkvd
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_126098832             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_126098832
VERSION     WP_126098832.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34420
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmak qaehvgtdiv ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylanlak svtvihrrgd
      181 fraerilrer lfkkdnvrvi wdtvvdeitg qpgkaplpps veglkmrnva tgevsrlkvd
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_126103919             417 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_126103919
VERSION     WP_126103919.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42841
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripde efakagavig
       61 kagdiakadv vlkvrrpsea elkayrrgta viaimdpygn daavdalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fraaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsviidlav erggnvegav
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafie tlvdkttkal ainrdddlvk
      361 atmltdggqv vhpafagkpa vmiasaepak paaakkpaaa kkpaapkspa nkpkgia
//
LOCUS       WP_126109392             321 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Allobosea].
ACCESSION   WP_126109392
VERSION     WP_126109392.1
KEYWORDS    RefSeq.
SOURCE      unclassified Allobosea
  ORGANISM  unclassified Allobosea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="unclassified Allobosea"
                     /db_xref="taxon:2653178"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34382
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mahihakvmi igsgpagyta aiyaaramle pvmisglqag gqlmittdve nypgfadviq
       61 gpwlmeqmra qaehmgtkmv sdhiarvdls qrpfrlwgdg getyscdsli iatgaqakwl
      121 glpseqsfqg fgvsacatcd gfffrnkqvv vvgggntave ealylanlas kvtlvhrrds
      181 lraekvmqdr lfkhpkievi wnaevaeilg gaqppsvthi rlrdaktgal rdiatdgifi
      241 aighkpatel fagqlamrds gylevtpgtt qtnvpgvfaa gdvtdehyrq avtaaglgcm
      301 aaldaerwlq aqelgireaa e
//
LOCUS       WP_126110179             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Jeotgalibaca ciconiae].
ACCESSION   WP_126110179
VERSION     WP_126110179.1
KEYWORDS    RefSeq.
SOURCE      Jeotgalibaca ciconiae
  ORGANISM  Jeotgalibaca ciconiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae; Jeotgalibaca.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Jeotgalibaca ciconiae"
                     /db_xref="taxon:2496265"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34346
     Region          8..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 melqeklydv iiigagpggm taalyasran letliiergv pggelintae venypgfdsi
       61 tgpdladkiy essmrfgaeh vygdvkgika dgayhiieag kkayrtksvi iatgshhrkl
      121 nipgeeqyng rgvsycavcd gaffrdkdlv vvgggdsave egtyltqfad vnivhrrdel
      181 raqkilqdra fkndkvsftw dtvveeikgd dnkvtavavk nvntgevtek svdgvfvyvg
      241 ilpqtdafrd lgitdeegwi itndlmettv pgifavgdvr kktlrqitta vgdggeagnr
      301 ayhyveewne rneak
//
LOCUS       WP_126115928             379 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Allobosea].
ACCESSION   WP_126115928
VERSION     WP_126115928.1
KEYWORDS    RefSeq.
SOURCE      unclassified Allobosea
  ORGANISM  unclassified Allobosea
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Alloboseaceae; Allobosea.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="unclassified Allobosea"
                     /db_xref="taxon:2653178"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39383
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavpaetq gaetrvavtp etvrkfiglg aeiavekgag lasgitdsdy eaagatiaks
       61 akdalkgadi vlkvrrpged eiaglpagal vvgimdpygs eaqvealaka nvaafamefm
      121 pritraqvmd vlssqanlag yravidgaae ygralpmmmt aagtvpaari fimgvgvagl
      181 qaiatarrmg aivtatdvrp atkeqveslg akflavedee fkqaqtaggy akemskeyqa
      241 kqaeltashi akqdivitta lipgrpapkl isaamvesmk pgsviidlav erggncelar
      301 pgevvttpng vkivghlnvp grlpatsssl yaknlfafve tlidkaekkl avnwddelvk
      361 atcltkdgav vhpnfvaka
//
LOCUS       WP_126116906             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus cohnii].
ACCESSION   WP_126116906
VERSION     WP_126116906.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus cohnii
  ORGANISM  Staphylococcus cohnii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus; Staphylococcus cohnii species
            complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Staphylococcus cohnii"
                     /db_xref="taxon:29382"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33629
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeqvdfdva ivgagpagmt aavyasranl stvmiergmp ggqmanteev enfpgfemit
       61 gpdlstkmfe hakkfgakyq ygdiksiedk grykvinlgn seitaravii stgaeykkig
      121 vpgeqglggr gvsycavcdg affknqklfv igggdsavee gtfltkfads vtivhrrdel
      181 raqkilqdra fkndkidfiw shtlktinek dgkvgsvtle stkdgaeqtf dadgvfvyig
      241 mkpltapfen lgitnevgyi vtnedmstki pgvyaagdvr akglrqivta tgdgsiaaqs
      301 aisyieelkd tiea
//
LOCUS       WP_126121329             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corynebacterium hylobatis].
ACCESSION   WP_126121329
VERSION     WP_126121329.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium hylobatis
  ORGANISM  Corynebacterium hylobatis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Corynebacterium hylobatis"
                     /db_xref="taxon:1859290"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33241
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtaqdtihdv iiigsgpaay taavyaarae lkplvfegye yggalmnttd venfpgfkdg
       61 imgpdlmmem raqaerfgsd mrmelvdsve legdvkkvhv gdevhlarti ilatgaaarl
      121 lgvpgedklm grgvstcatc dgfffkgaei avvgggdsam eeatfltkfa dkvtlihrre
      181 gfsasaimle raranekidf alnkvvdhvi egtgdnqnkv agvmlrdtvt gelselpvaa
      241 mfvaighdpr sgflggqiel keggyvkvde pstatsvpgv facgdlvddh yqqaitaags
      301 gcraatdaeh ylaal
//
LOCUS       WP_126122302             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus epidermidis].
ACCESSION   WP_126122302
VERSION     WP_126122302.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus epidermidis
  ORGANISM  Staphylococcus epidermidis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Staphylococcus epidermidis"
                     /db_xref="taxon:1282"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33978
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeqvdfdva iigagpagmt aavyvsranl stvmiergmp ggqmanteev enfpgfemvt
       61 gpdlstkmfe hakkfgaqyq ygdiksiedk ggykvinlgn keitaravii stgaeykkig
      121 vpgeqdlggr gvsycavcdg affkgkklfv igggdsavee gtfltkfads vtivhrrdel
      181 raqkilqdra fkndkidfiw shtlktindk dgkvgsvtle stkdgseqtl dadgvfiyig
      241 mkplttpfld lgitndvgyi etnedmstkv pgiyaagdvr dkglrqivta tgdgsiaaqs
      301 aiayiehlnd nseilsi
//
LOCUS       WP_126123663             294 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Staphylococcus
            epidermidis].
ACCESSION   WP_126123663
VERSION     WP_126123663.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus epidermidis
  ORGANISM  Staphylococcus epidermidis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Staphylococcus epidermidis"
                     /db_xref="taxon:1282"
     gene            1..>294
                     /gene="trxB"
     Protein         1..>294
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          8..294
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 maeqvdfdva iigagpagmt aavyvsranl stvmiergmp ggqmanteev enfpgfemvt
       61 gpdlstkmfe hakkfgaqyq ygdiksiedk ggykvinlgn keitaravii stgaeykkig
      121 vpgeqdlggr gvsycavcdg affkgkklfv igggdsavee gtfltkfads vtivhrrdel
      181 raqkilqdra fkndkidfiw shtlktindk dgkvgsvtle stkdgseqtl dadgvfiyig
      241 mkplttpfld lgitndvgyi etnedmstkv pgiyaagdvr dkglrqivta tgdg
//
LOCUS       WP_126128209             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Neoundibacterium parvum].
ACCESSION   WP_126128209
VERSION     WP_126128209.1
KEYWORDS    RefSeq.
SOURCE      Neoundibacterium parvum
  ORGANISM  Neoundibacterium parvum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Neoundibacterium.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Neoundibacterium parvum"
                     /db_xref="taxon:401471"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38602
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaesr pgetrvaatp etikkyvaak hsvivqagag iaasitdeay qaagaqigta
       61 aeafaaelil kvrapsaeer aliksgtvlv gmlnpfdaen iaamaahgis afaleaapri
      121 traqsldvls sqaniagyka vlmaantyqr fmpmlmtaag tvkaarvlim gvgvaglqai
      181 atakrlgavi easdvrppvk eqveslgakf idvpyetdee reiakgaggy arsmpaawma
      241 rqaalvhera kqadiiitta lipgrkapil iseetvkamk pgsvivdmav eqggncplse
      301 lgktvtkygv hiigepnlat llaadasaly arnvldflkl iidkdaalvi nkedeiiaat
      361 lvcaggevlk k
//
LOCUS       WP_126129153             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neoundibacterium parvum].
ACCESSION   WP_126129153
VERSION     WP_126129153.1
KEYWORDS    RefSeq.
SOURCE      Neoundibacterium parvum
  ORGANISM  Neoundibacterium parvum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Neoundibacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Neoundibacterium parvum"
                     /db_xref="taxon:401471"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33638
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mstpkhahvl ilgsgpagys aavyaaranl kpvlitgveq ggqlmtttdv enwpadplgv
       61 qgpelmqrfl qhaerfntei ifdyihtakl nekpirligd qaeytcdsli iatgasaqyl
      121 glpseqafmg kgvsacatcd gffyrgkeva vvgggntave ealylsnias kvtvihrrdk
      181 fraeailidr lmakvaegkv eikwnhtlde vigddsgvtg iriksmsnae tsaiplhgvf
      241 iaighkpnts ifdgqlemhn gyiktktgte gmatatnvpg vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq rflee
//
LOCUS       WP_126131241             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_126131241
VERSION     WP_126131241.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33309
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsiavdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_126133191             306 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Latilactobacillus curvatus].
ACCESSION   WP_126133191
VERSION     WP_126133191.1
KEYWORDS    RefSeq.
SOURCE      Latilactobacillus curvatus
  ORGANISM  Latilactobacillus curvatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Latilactobacillus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Latilactobacillus curvatus"
                     /db_xref="taxon:28038"
     gene            1..306
                     /gene="trxB"
     Protein         1..306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32688
     Region          5..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maksydvivi gagpggmtaa lyasranlsv lmldrgiygg qmnntaeven ypgfksilgp
       61 elgekmyasa tqfgaeygyg tvnsielqge mkimhtdegd fearsiiiat gsehkkigip
      121 gedefggrgv sycavcdgaf fknkevvvig ggdsaieegl yltqlaskvt vihrrdelra
      181 qkilqdrafa ndkmdfiwna qvttiegddk kvtgvtyidk atgetkevaa sgvfiyvgie
      241 pmtsafgdlg iltdagwikt ddhmatsvpg iyaigdvrek dlrqittavg dggiagqevf
      301 kylqsi
//
LOCUS       WP_126137353             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tritonibacter mobilis].
ACCESSION   WP_126137353
VERSION     WP_126137353.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55569
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeia egesrvamtp lsaldlqklg fecciesgag eaagftdaay aeagvevikt
       61 aaglwkaadi iakvrapnet elkrlnkskt lisffnpggn eeglelaksk gatviamemv
      121 prisraqkmd alssmaniag yravieagnn fdrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg avtyafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreapk lwladmvaam krgsvivdla aerggnvegt
      301 vkdekvvtdn gvtiigytdf psrmasqsss lyatnirhmm tdltpekdgq vvhdmeddvi
      361 rgatvthage itfpppppkv qaiaaqkkpe ppkeltaeek raaevaafkq qtknqvtlla
      421 vgaallltvg lvapasfmqh fivfvlsvfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsw lviflaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_126136243             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tritonibacter mobilis].
ACCESSION   WP_126136243
VERSION     WP_126136243.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55597
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtprela tgesrvamtp lsaldlqklg fecciesgag eaagftdaay aeagvevikt
       61 aaglwkaadi iakvrapnet elkrlnkskt lisffnpggn eeglelaksk gatviamemv
      121 prisraqkmd alssmaniag yravieagnn fdrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg avtyafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreapk lwladmvaam krgsvivdla aerggnvegt
      301 vkdekvvtdn gvtiigytdf psrmasqsss lyatnirhmm tdltpekdgq vvhdmeddvi
      361 rgatvthage itfpppppkv qaiaaqkkpe ppkeltaeek raaevaafkq qtknqvtlla
      421 vgaallltvg lvapasfmqh fivfvlsvfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsw lviflaalsv fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_126142470             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus whitsoniae].
ACCESSION   WP_126142470
VERSION     WP_126142470.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus whitsoniae
  ORGANISM  Paenibacillus whitsoniae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Paenibacillus whitsoniae"
                     /db_xref="taxon:2496558"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32948
     Region          4..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkkhdvvivg tgpagltaai ylsraglapl viegvqpggq lttttevdnf pgfpegitgp
       61 elmenmrkqa lrfgavilag rvasvdtsrr pfaltlesge qlsaeaviis tgasskmlgi
      121 pgekdyigrg vstcatcdgf ffrgkkiivi gggdtameea nfltrfasev rivhrraelk
      181 askimqdhar anskiawsln rtpleviggp lgvtglrvrd eatgeeevle adgifvaigh
      241 tpntgflggq latdelgylq vtpgasmtsv qgifacgdvq driyrqaits agsgamaald
      301 aerflteqhi avtv
//
LOCUS       WP_126134524             508 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Actinotignum].
ACCESSION   WP_126134524
VERSION     WP_126134524.1
KEYWORDS    RefSeq.
SOURCE      Actinotignum
  ORGANISM  Actinotignum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Actinotignum"
                     /db_xref="taxon:1653174"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52075
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mlvgipqstr pgdplvagtp dtvaklialg yevvvetgag eassypdsqy esagarlvsa
       61 qeawaadivl atdapdvsyl drmsrgatli armnpagspd lieelsrrel talaldaipr
      121 israqsmdvr ssmanisgyr avieaashfg rlftgqvtaa gkvppatvyv igagvaglaa
      181 vgtansmgai vkatdvradv aeqvqsmgae fveipvrqes adgyaremta dqanaagvvy
      241 areaaaadiv ittalipgkp apllldsaav aamkpgsviv dlaaanggnv agtrpgevvh
      301 tengvtiigy edlalrlpgq asqlfgqnlv nflklttpqk dgqlvldted divrgilvtl
      361 ggavawpppp ikvsaapaap pappappaap eaarpsalry lwaglaaava lwilftappg
      421 mtshfivfml acvvgfyvit svthalhtpl msvtnaisgi ivvgailqls sghlavtila
      481 aialtlasin ifggflvtar mlsmfkrs
//
LOCUS       WP_126137424             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tritonibacter mobilis].
ACCESSION   WP_126137424
VERSION     WP_126137424.1
KEYWORDS    RefSeq.
SOURCE      Tritonibacter mobilis
  ORGANISM  Tritonibacter mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tritonibacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Tritonibacter mobilis"
                     /db_xref="taxon:379347"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33397
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetrhtkvl iigsgpagyt aavyasraml qpilvqgiep ggqlttttev enwpghteiq
       61 gpdlmvnmes haramgteii gdmitsldts srpfvakgds gttytadavi latgarakwl
      121 glpseekfkg fgvsacatcd gffyrgqeiv vigggntave ealfltnfas kvtlihrrde
      181 lraekilidr lmknpkiepl wfheldevvg tdaplgveav rvkhtktgei teipakgvfv
      241 aighapatel vkdvlethng gyvkvkpgtt etsipgifaa gdltdhkyrq avtsagmgcm
      301 aaldaerfla eqe
//
LOCUS       WP_126146832             459 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Synechococcus elongatus].
ACCESSION   WP_126146832
VERSION     WP_126146832.1
KEYWORDS    RefSeq.
SOURCE      Synechococcus elongatus
  ORGANISM  Synechococcus elongatus
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Synechococcales; Synechococcaceae; Synechococcus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Synechococcus elongatus"
                     /db_xref="taxon:32046"
     gene            1..459
                     /gene="trxB"
     Protein         1..459
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=49811
     Region          7..310
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
     Region          355..451
                     /region_name="TRX_NTR"
                     /note="TRX domain, novel NADPH thioredoxin reductase (NTR)
                     family; composed of fusion proteins found only in oxygenic
                     photosynthetic organisms containing both TRX and NTR
                     domains. The TRX domain functions as a protein disulfide
                     reductase via the reversible...; cd02949"
                     /db_xref="CDD:239247"
     Site            order(379,382)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239247"
ORIGIN      
        1 mtgvenvvii gsgpagltaa iyaaranlkp lmfegyqlgg lpggqlmttt evenfpgfpe
       61 gitgpelmer mraqavrwga elytedvisa dlsqrpfrir sqerevlahs viiatgatar
      121 rlslpgedrl wnngisacai cdgaapifrd gelvvigggd taaeeavylt kyakhvhllv
      181 rsdrmraska mqdrvlahpn vtvhwhteai eavgdtllea vrvrnnqtge ekaiaaqglf
      241 yaightpntk lfegqieldg tgyirtkpds vetslegvfa agdvqdheyr qaitaagtgc
      301 aaallaeryl sahnllqeyk qeaaaaepet kaaatpaasq peasefdpts vyhegsyalr
      361 klyhesdrll avlytaptcg pcrtlkpilr kvaeefsdrl hyvlididad peiaqsagvv
      421 gtptlqlfkd kakvdeirgv kmksdyrarf eqhlqpvsr
//
LOCUS       WP_126149950             492 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Devosia
            equisanguinis].
ACCESSION   WP_126149950
VERSION     WP_126149950.1
KEYWORDS    RefSeq.
SOURCE      Devosia equisanguinis
  ORGANISM  Devosia equisanguinis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Devosia equisanguinis"
                     /db_xref="taxon:2490941"
     Protein         1..492
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49816
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
     Region          443..>492
                     /region_name="DUF6465"
                     /note="Family of unknown function (DUF6465); pfam20069"
                     /db_xref="CDD:466279"
ORIGIN      
        1 mkiavlrert egesrvaatp etvakliglg agvtvekgag sgsriadeqf sasgatigad
       61 arttlagadi vlvvrrpaaa dlagvnpgal ligaldpygn dgdvaalaka gvtamvmefm
      121 pritraqvmd ilssqanlag yqavieaasv fdrampmmmt aagtvrpaka fvmgagvagl
      181 qaiatakrlg avvsatdvra aageqveslg akfimtealk dasgtggyar eltkdeqaaq
      241 aelvaghisk qdivittali pgrpapklvt ramvesmapg svivdlaaer ggnveltqpg
      301 kvidhngvvi igytnlagri pttasqlyar nllsfidtlv dkkekklain wddelvkatv
      361 ltrdgavvhp nfvaaaktgd ivtapsgavs gdvvsakpkp apkkpaakae pkdapvktga
      421 akkpaaikka apkaeaapap eavvtpapav pvvakkapar kpatpkadav akepaakkpa
      481 skkpaakpee gk
//
LOCUS       WP_126155145             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Paracoccus
            haematequi].
ACCESSION   WP_126155145
VERSION     WP_126155145.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus haematequi
  ORGANISM  Paracoccus haematequi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Paracoccus haematequi"
                     /db_xref="taxon:2491866"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55467
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkegf egearvaitp ssaghlmklg hevfvesgag aragfsddsy raagitvvpt
       61 aaeligavdv vakvrqpsda eirqmregqt lisffypaqn pellalakeq gvtaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtavslg aqvyafdvrp evaeqiesmg aefvfldfee aqdgaatggy aapsspefre
      241 kqlakfrela pqmdvvitta lipgrdapkl wtrdmveamk pgsvivdlaa erggncelti
      301 pderhvteng vtiigytdfp srmgaqasel ygnnvrhfla dltpkkdgvi qhnmeddvir
      361 gatvtrdhdv twpppppkia aiaaqkpkek pkaltveerr aaevaafkae tksqvtllgv
      421 gaivllliga vapasfmahf ivfvlacfig frviwnvahs lhtplmaitn aissiiilga
      481 lmqigsgsww vvalgalavl magvnifggf mvtrrmlamf qks
//
LOCUS       WP_126150330             316 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Devosia].
ACCESSION   WP_126150330
VERSION     WP_126150330.1
KEYWORDS    RefSeq.
SOURCE      Devosia
  ORGANISM  Devosia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Devosia"
                     /db_xref="taxon:46913"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33858
     Region          4..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhakvviigs gpagytaaiy aaramleplm iqglqpggql tittdvenyp gfadviqgpw
       61 lmdqmkaqae hvgtrivndi ithvdfdrrp fvltgdsgdt ytadsviiat gaqakwlglp
      121 seqkfqgfgv sacatcdgff yrgkqvlvvg ggntaveeal fltnfaekvi vvhrrdefra
      181 erilqdrlfk npkievrwnt evvevggapm ppsvntvtlk nrlsgevyeq pidgvfvaig
      241 hapatsvfsg kldmkpggyl qvkpgtthtn ipgvfaagdv tddvyrqavt aagmgcmaal
      301 daerylaehe laeaae
//
LOCUS       WP_126156923             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Amphritea opalescens].
ACCESSION   WP_126156923
VERSION     WP_126156923.1
KEYWORDS    RefSeq.
SOURCE      Amphritea opalescens
  ORGANISM  Amphritea opalescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Amphritea.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Amphritea opalescens"
                     /db_xref="taxon:2490544"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34136
     Region          1..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msetqhhkli ilgsgpagyt aavyaaranl npivitgmqa ggqlttttdv dnwpgdvdgv
       61 qgpelmqrmq ahaerfdtkv ifdhisetdl qnrpfrlkgd maeytcdali ictgasaqyi
      121 glpseeafmg kgvsacatcd gffyrgqkva vigggntave ealylsniaa evtlihrrds
      181 lrsekilqdk lferakngni niiwnhqlde vlgddmgvtg irikstedda mqtlelqgvf
      241 iaighkpnte ifgdqlamen gylsiqtgth gnatqtsieg vfaagdvadh iyrqaitsag
      301 fgcmaaldae rylddqa
//
LOCUS       WP_126157063             394 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Amphritea
            opalescens].
ACCESSION   WP_126157063
VERSION     WP_126157063.1
KEYWORDS    RefSeq.
SOURCE      Amphritea opalescens
  ORGANISM  Amphritea opalescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Amphritea.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Amphritea opalescens"
                     /db_xref="taxon:2490544"
     Protein         1..394
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41745
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,97,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,130..131,140..141,144..145,148..149,151..152,
                     154..159,161,163..165,168,191..192,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,130,133,136,177..180,200..202,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,130,140,183..184,191,207..208,210..213)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(160..164,167,170,193,195)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiglakepl anesrvaltp eniirlsatg atfvvetgag laagfsdqdy rdvgaqinss
       61 aravyqqadi llrvnlsgam lnqaaawlen splligmmdp ftkperftdl aeqgissiam
      121 eliprisraq smdvltsmat lagykavlla anaasriypm mmtaagnlsp arvfimgagv
      181 aglqaaatak rmgavvkayd vrpaareqii svgakpvela leadstegqg gyakqqgedf
      241 lqrqrelmta vlseqdivit taaipgarsp vlitaemvgq mkpgavivdl aserggncel
      301 tqhgevvveq gvtiigpdni vatvayhasq mygnnienll hhllneqgdc dldfddeiiq
      361 qavvtyggei innglrerld lpplasmprl eeva
//
LOCUS       WP_126158679             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Amphritea opalescens].
ACCESSION   WP_126158679
VERSION     WP_126158679.1
KEYWORDS    RefSeq.
SOURCE      Amphritea opalescens
  ORGANISM  Amphritea opalescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae; Amphritea.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Amphritea opalescens"
                     /db_xref="taxon:2490544"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33344
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msevkhspli ilgsgpagyt aavyaaragl tpviitgaav ggqltgttev dnwpgdvdgv
       61 qgpelmarmq qhaerfdtei lydhitkael ssrpfaltgd sgqrysadal iiatgasaqy
      121 lglpsetdym nkgvsgcatc dgffykggkv avvgggntav eealylsnia sevtlihrrg
      181 elraekilqe klftkaatgn ikilwhhqve evlgdgkkve glrltdalsg nakelsvdav
      241 fiaighkpnt elfqnqldmq agylivhsgl egnvtqtsie gvfaagdvad hayrqaitsa
      301 gmgcmaaldt erflsr
//
LOCUS       WP_126161425             366 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arenibacter aquaticus].
ACCESSION   WP_126161425
VERSION     WP_126161425.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter aquaticus
  ORGANISM  Arenibacter aquaticus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Arenibacter aquaticus"
                     /db_xref="taxon:2489054"
     Protein         1..366
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39921
     Region          1..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigilketf dgerrvaitp niakqliaag feilveegag ehssfkdsdy revdavvekr
       61 gvvfhegqvl lkinpfdeed lklvdkrqil isklyhksnp qliqtiankg atafsmdaip
      121 risraqdmdv lssqnnlagy kavilgafem tkifplmmts agtiapsrvl iygigvaglq
      181 aiatakrlga vveatdirse tkeqaeslga kfisvdnege qseggyakea saeyakkqke
      241 avnkslfqad lvittanipg rkapvlitre qlmqmkngav iidlaaaqgg nceisennkt
      301 ivengvkvig tsidprsvst nasdlyakni ynyimhltke ttfewdleee itdetlivhd
      361 geirkn
//
LOCUS       WP_126164159             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arenibacter aquaticus].
ACCESSION   WP_126164159
VERSION     WP_126164159.1
KEYWORDS    RefSeq.
SOURCE      Arenibacter aquaticus
  ORGANISM  Arenibacter aquaticus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Arenibacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Arenibacter aquaticus"
                     /db_xref="taxon:2489054"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34502
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maekverlkt liigsgpagy taaiyaarad lkpvlytgme pggqltttte vdnfpgypeg
       61 vdgptmmvql qkqaerfgte vrigmvtkvd fsdevggihk ltiddnkiie aetviistga
      121 takylglpse qklrgggvsa cavcdgffyk gqdvaivgag dtaaeeasyl anickkvtml
      181 vrkdymrask amqhrvnsle nieiryntev dtvlgdqvve glrmvnnvtg ekediaitgl
      241 fiaighkpnt eifkdqlemd dtgyiitkgk stktskpgvf asgdvqdkey rqavtaagtg
      301 cmaaldaery latiespeev ss
//
LOCUS       WP_126165526             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Thermus
            scotoductus].
ACCESSION   WP_126165526
VERSION     WP_126165526.1
KEYWORDS    RefSeq.
SOURCE      Thermus scotoductus
  ORGANISM  Thermus scotoductus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Thermus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Thermus scotoductus"
                     /db_xref="taxon:37636"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39701
     Region          2..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvtiavpker apgerrvalv pevvarlvkq garvrvekga gegayypdta yqevgaevve
       61 rgellkdanl lftvqppped ligalepgai vvgfvqahkn ldlvkalaak katviameli
      121 pritraqsmd alssqatvag ylaaihaarl sprffpmltt aagtirpakv mvmgvgvagl
      181 maiatakrlg aqvfaydvrk aaveqalslg akpielpisa egeggyarel teeekriqhe
      241 alrehvagmd aiittaqvpg rrapillted mverlkpgtv vvdlaaesgg ncvltqpgev
      301 vevkgvrifg plnlpsklsv hasemyaknl lnlssllmek gefapkwede iiqgallmke
      361 geilhgptka lvgga
//
LOCUS       WP_126165810             467 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella khirikhana].
ACCESSION   WP_126165810
VERSION     WP_126165810.1
KEYWORDS    RefSeq.
SOURCE      Shewanella khirikhana
  ORGANISM  Shewanella khirikhana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Shewanella khirikhana"
                     /db_xref="taxon:1965282"
     gene            1..467
                     /gene="nrfA"
     Protein         1..467
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=51502
     Region          1..467
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvkklngksf alsalvaasf vaagamasek teprsevykd kfskqynswh ataesealtd
       61 algqdpalvi lwagygfakd ynaprghmya lsdvrntlrt ggptsaedgp mpmacwscks
      121 pdvprlieeq gedgyftgkw akggaevant igcsdchekg spklrlsrpf aerameaigt
      181 pfdkaskqdk esmvcaqchv eyyfekvdgr kgfvkfpwdg gttvenmeay ydaiqfvdwt
      241 havsktpmlk aqhpgyetwk lgthgqnnvs cvdchmpkvt neqgkkftdh kvgnpfdrfe
      301 etcgtchsqd kehmltvykd nkskvmelkg kaetqlvaah feagaawkag ateeemkpil
      361 tnirhaqwrw dyaiashgvs ahapaealrv lgtavdkaan arvqlaqlla tkgvkqpiel
      421 pdistkakaq aalgmdmdkm kaekekfkke llpkweeeak areatyk
//
LOCUS       WP_126166930             318 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Shewanella].
ACCESSION   WP_126166930
VERSION     WP_126166930.1
KEYWORDS    RefSeq.
SOURCE      Shewanella
  ORGANISM  Shewanella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Shewanella"
                     /db_xref="taxon:22"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33966
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msqakhsqll ilgsgpagyt aavyaaranl npvmitglqq ggqlttttev enwpgdpegl
       61 tgpglmarmq ehaekfntei lfdhinevtl terpfrlkgd ngeytcdali iatgasakyl
      121 glpseeafkg rgvsacatcd gffyrnqkva vigggntave ealylsnias evhlihrrds
      181 frsekilidr lmdkvangni ilhldktlde vvgdnmgvtg vklkstkdds veefdvagvf
      241 vaighspntg ifegqlemnh gylkvqsgln gnatqtsieg vfaagdvmdq hyrqaitsag
      301 tgcmaaldae ryldakhg
//
LOCUS       WP_126168024             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            khirikhana].
ACCESSION   WP_126168024
VERSION     WP_126168024.1
KEYWORDS    RefSeq.
SOURCE      Shewanella khirikhana
  ORGANISM  Shewanella khirikhana
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Shewanella khirikhana"
                     /db_xref="taxon:1965282"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53297
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipresl agetrvaatp atveqlkklg fevaiesgag tlasfsdaaf eaagasvvps
       61 vwqadlifkv naptedeike ikdgatlvsf iwpaqnpelv eklskrninv mamdmvpris
      121 raqsldalss maniggyrav veaahefgrf ftgqitaagk vppakvlvig agvaglaaig
      181 tagslgavvr afdtrlevae qiesmggqfl kldfggedga ssdgyakvms eefikaemal
      241 faeqakevdi ivttalipgk paprlitkem vdsmksgsvi vdmaaatggn ceytvpgelf
      301 vtangvkvig ytdlpgrlpv qssqlygtnl vnlmklmcke kdgnavidfd dvvmrnmtvv
      361 kagevtfppp qisvsaapak aapkvelkka epkepsklky ilgalgligf gavasvappe
      421 flshftvfll scvvgyyvvw nvthalhtpl msvtnaisgi ivvgallqig ggstlvtala
      481 fvavliasin ifggftvthr mlkmfrkd
//
LOCUS       WP_126172489             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Altericroceibacterium
            xinjiangense].
ACCESSION   WP_126172489
VERSION     WP_126172489.1
KEYWORDS    RefSeq.
SOURCE      Altericroceibacterium xinjiangense
  ORGANISM  Altericroceibacterium xinjiangense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Altericroceibacterium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Altericroceibacterium xinjiangense"
                     /db_xref="taxon:762261"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34743
     Region          6..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtrhttrmli igsgpaglsa aiyaaragme pivvqglqpg gqltittdve nypgfrdviq
       61 gpwlmeqmqa qaehvgtrmm wdtivevdve sgppfvargd sgdeyvgdtl viatgaqakw
      121 lgvpgeeals gkgvsacatc dgffyrgkkv avigggntav eealyltnhs edvtlihrre
      181 dlraekilqd rlfahprisv lwnkrverfl gdplqggltg lqladtvtge msefgcegaf
      241 vaighapste lfkgkleida ngyivvapgt pktnrpgvfa cgdvmdhtyr qavtaagtgc
      301 maaldaerfl atleyvrneq qaaaae
//
LOCUS       WP_126175196             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tsuneonella rigui].
ACCESSION   WP_126175196
VERSION     WP_126175196.1
KEYWORDS    RefSeq.
SOURCE      Tsuneonella rigui
  ORGANISM  Tsuneonella rigui
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Tsuneonella.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Tsuneonella rigui"
                     /db_xref="taxon:1708790"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34616
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mathktrmli igsgpaglsa aiygaramme pivvqglqpg gqltittdve nypgfrdviq
       61 gpwlmqemqa qaehvgtrmm wdtivrvdla ngspfraygd sgdvyegdtl viatgaqakw
      121 lgvpgemdlg gkgvsacatc dgffyrgkkv avigggntav eealyltnhs ddvtlihrrg
      181 dlraekilqd rlfkhpkikv lwnqvverfe gdpaagglth lvlkdaqtga lsdfhcdgaf
      241 vaighapste lfkgqletda sgylivepgt pktaipgvfa cgdvmdhtyr qavtaagtgc
      301 maaldaerfv aglsidlagh aekaeaaa
//
LOCUS       WP_126178231             325 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Thermus].
ACCESSION   WP_126178231
VERSION     WP_126178231.1
KEYWORDS    RefSeq.
SOURCE      Thermus
  ORGANISM  Thermus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Thermus"
                     /db_xref="taxon:270"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35001
     Region          18..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meftltglag sgekeerydv viigggpagl tagiyagraq lktvilekgl pggqiaqtde
       61 venypgfpeg isgpelasrm vqqaekfgar ivmdevlgle aqdggflvrg fersyfgrav
      121 iiatganprk lgvpgeekfy grgvstcatc dgffyrdkev vvvgggdaav eeglfltkfa
      181 rkvtlihrrd elrankvaqa rafqnpkmhf lfshvvtevl geeqvtgvrl knlktgeeyv
      241 yptdgvfvfi ghepntgflk gvvelrpdgy vavrdevfts vpgifaagdv adpiyrqltt
      301 svgagtraam maerylaeah ekvkp
//
LOCUS       WP_126200886             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thermus scotoductus].
ACCESSION   WP_126200886
VERSION     WP_126200886.1
KEYWORDS    RefSeq.
SOURCE      Thermus scotoductus
  ORGANISM  Thermus scotoductus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Thermus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Thermus scotoductus"
                     /db_xref="taxon:37636"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35043
     Region          18..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meftltglag sgekeerydv viigggpagl tagiyagraq lktvilekgl pggqiaqtde
       61 venypgfpeg isgpelasrm vqqaekfgar ivmdevlgle aqdggflvrg fersyfgrav
      121 iiatganprk lgvpgeerfy grgvstcatc dgffyrdkev vvvgggdaav eeglfltkfa
      181 rkvtlihrrd elrankvaqa rafqnpkmhf lfshivtevl geeqvtgvrl knlktgeeyv
      241 yptdgvfvfi ghepntgflk gvvelrpdgy vavrdevfts vpgifaagdv adpiyrqltt
      301 svgagtraam maerylaeah ekvkp
//
LOCUS       WP_126204932             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thermus scotoductus].
ACCESSION   WP_126204932
VERSION     WP_126204932.1
KEYWORDS    RefSeq.
SOURCE      Thermus scotoductus
  ORGANISM  Thermus scotoductus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Thermus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Thermus scotoductus"
                     /db_xref="taxon:37636"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35100
     Region          18..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meftltglag sgekeerydv viigggpagl tagiyagraq lktvilekgl pggqiaqtde
       61 venypgfpeg isgpelasrm vqqaekfgar ivmdevlgle aqdggflvrg fersyfgrav
      121 iiatganprk lrvpgeekfy grgvstcatc dgffyrdkev vvvgggdaav eeglfltkfa
      181 rkvtlihrrd elrankvaqa rafqnpkmhf lfshvvtevl geeqvtgvrl knlktgeeyv
      241 yptdgvfvfi ghepntgflk gvvelrpdgy vavrdevfts vpgifaagdv adpiyrqltt
      301 svgagtraam maerylaeah ekvkp
//
LOCUS       WP_126203460             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thermus scotoductus].
ACCESSION   WP_126203460
VERSION     WP_126203460.1
KEYWORDS    RefSeq.
SOURCE      Thermus scotoductus
  ORGANISM  Thermus scotoductus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Thermus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Thermus scotoductus"
                     /db_xref="taxon:37636"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34863
     Region          18..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meftltglag sgekeerydv viigggpagl tagiyagraq lktvilekgl pggqiaqtde
       61 venypgfpeg isgpelasrm vqqaekfgar ivmdevlgle aqdggflvrg fersyfgrav
      121 iiatganprk lgvpgeekfy grgvstcatc dgffyrdkev vvvgggdaav eeglfltkfa
      181 rkvtlihrrd elrankvaqa rafqnpkmhf lfshvvtevl geeqvtgvrl knlktgeeyv
      241 yptdgvfvfi ghepntgflk gvvelrpdgy vavrdevfts vpgifaagdv adpiyrqltt
      301 svgagtraam maerylaeah ekvs
//
LOCUS       WP_126206927             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thermus scotoductus].
ACCESSION   WP_126206927
VERSION     WP_126206927.1
KEYWORDS    RefSeq.
SOURCE      Thermus scotoductus
  ORGANISM  Thermus scotoductus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Thermus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Thermus scotoductus"
                     /db_xref="taxon:37636"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34919
     Region          18..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meftltglag sgekeerydv viigggpagl tagiyagraq lktvilekgl pggqiaqtde
       61 venypgfpeg isgpelasrm vqqaekfgar ivmdevlgle vqdggflvrg fersyfgrav
      121 iiatganprk lgvpgeerfy grgvstcatc dgffyrdkev vvvgggdaav eeglfltkfa
      181 rkvtlihrrd elrankvaqa rafqnpkmhf lfshvvtevl geeqvtgvrl knlktgeeyv
      241 yptdgvfvfi ghepntgflk gvvelrpdgy vavrdevfts vpgifaagdv adpiyrqltt
      301 svgagtraam maerylaeah ekvs
//
LOCUS       WP_126208807             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thermus scotoductus].
ACCESSION   WP_126208807
VERSION     WP_126208807.1
KEYWORDS    RefSeq.
SOURCE      Thermus scotoductus
  ORGANISM  Thermus scotoductus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Thermus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Thermus scotoductus"
                     /db_xref="taxon:37636"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34863
     Region          18..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meftltglag sgekeerydv viigggpagl tagiyagraq lktvilekgl pggqiaqtde
       61 venypgfpeg isgpelasrm vqqaekfgar ivmdevlgle aqdggflvrg fersyfgrav
      121 ilatganprk lgvpgeekfy grgvstcatc dgffyrdkev vvvgggdaav eeglfltkfa
      181 rkvtlihrrd elrankvaqa rafqnpkmhf lfshvvtevl geeqvtgvrl knlktgeeyv
      241 yptdgvfvfi ghepntgflk gvvelrpdgy vavrdevfts vpgifaagdv adpiyrqltt
      301 svgagtraam maerylaeah ekvs
//
LOCUS       WP_126210732             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Thermus
            scotoductus].
ACCESSION   WP_126210732
VERSION     WP_126210732.1
KEYWORDS    RefSeq.
SOURCE      Thermus scotoductus
  ORGANISM  Thermus scotoductus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales;
            Thermaceae; Thermus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Thermus scotoductus"
                     /db_xref="taxon:37636"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39691
     Region          2..361
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,75,94,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvtiavpker apgerrvalv pevvarlvkq garvrvekga gegayypdta yqevgaevve
       61 rgellkdanl lftvqppped ligalepgai vvgfvqahkn ldlvkalaak katviameli
      121 pritraqsmd alssqatvag ylaaihaarl ssrffpmltt aagtirpakv mvmgvgvagl
      181 maiatakrlg aqvfaydvrk aaveqalslg akpielpisa egeggyarel teeekriqhe
      241 alrehvagmd aiittaqvpg rrapillted mverlkpgtv vvdlaaesgg ncvltqpgev
      301 vevkgvrifg plnlpsklsv hasemyaknl lnlssllmek gefapkwede iiqgallmke
      361 geilhgptka lvgga
//
LOCUS       WP_126211261             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter jejuni].
ACCESSION   WP_126211261
VERSION     WP_126211261.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33072
     Region          3..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldvaiiggg paglsaglya trgglknvvm fekgmpggqi tssseienyp giaqvmdgis
       61 fmapwneqcm rfglkhemvg veqilknsdg sftikleggk teltkavivc tgsapkragf
      121 kgedeffgkg vstcatcdgf fyknkevavl gggdtaleea lylanicskv ylihrrdefr
      181 aapstvekvk knekielits asvdevygdk mgvtgvkvkl kdgsirdlnv pgiftfvgln
      241 vrneilkqdd gkflcnmeeg gqvsvdlkmq tsvaglfaag dlrkdapkqv icaagdgava
      301 alsamayies lh
//
LOCUS       WP_126217992             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter jejuni].
ACCESSION   WP_126217992
VERSION     WP_126217992.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33027
     Region          3..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldvaiiggg paglsaglya trgglknvvm fekgmpggqi tssseienyp gvaqvmdgis
       61 fmapwneqcm rfglkhemvg veqilknsdg sftikleggk telakavivc tgsapkragf
      121 kgedeffgkg vstcatcdgf fyknkevavl gggdtaleea lylanicskv ylihrrdefr
      181 aapstvekvk knekielits asvdevygdk mgvtgvkvkl kdgsirdlnv pgiftfvgln
      241 vrnkilkqdd gkflcnmeeg gqvsvdlkmq tsvaglfaag dlrkdapkqv icaagdgava
      301 alsamayies lh
//
LOCUS       WP_126223858             533 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia ambifaria].
ACCESSION   WP_126223858
VERSION     WP_126223858.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..533
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54947
     Region          3..533
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlqigiple tatgerrvat vpevveklvk lgfsvavqsg agaganfddd ayraagasia
       61 asaaelwsgs divfkvrpps adevalmreg gtligfvwpa qnpelmqqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq akdadiiitt alipgkpapk litaemvhsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqastl ygtnllrvie elckgkdgti nvdfdddair
      361 gltvikegni twppppikqa vvapkppaaa paaaapaksk ghghsgepms akalaivfai
      421 galafllvgq fapasflshf tvfvlacfvg ymviwnvtps lhtplmsvtn aissiiaiga
      481 lvqvapplge lanagdrpsg lilglavgal tltavnmfgg favtrrmlam frk
//
LOCUS       WP_126213872             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter jejuni].
ACCESSION   WP_126213872
VERSION     WP_126213872.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33058
     Region          3..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldvaiiggg paglsaglya trgglknvvm fekgmpggqi tssseienyp gvaqvmdgis
       61 fmapwneqcm rfglkhemvg veqilknsdg sftikleggk telaktvivc tgsapkragf
      121 kgedeffgkg vstcatcdgf fyknkevavl gggdtaleea lylanicskv ylihrrdefr
      181 aapstvekvk knekielits asvdevygdk mgvtgvkvkl kdgsirdlnv pgiftfvgln
      241 vrneilkqdd gkflcnmeeg gqvsvdlkmq tsvaglfaag dlrkdapkqv icaagdgava
      301 alsamayies lh
//
LOCUS       WP_126227691             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia ambifaria].
ACCESSION   WP_126227691
VERSION     WP_126227691.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39367
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkisipketr tgekrvaatp etakklcaqg hlvlvqsgag feasyqddaf vaagakvvda
       61 asafdadivl kvqaptdtel pslkrgavlv gmlepfnaeq aaklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrptvk eqieslgakf ldvpfetdee reaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetaqsmk pgsvlvdlaa grgpefdgrr
      301 sgncpltvad qvivhngvti agytnlasmv asdasalyar nlldfvkliv tkegalnidl
      361 tddivaatll crdgevtrk
//
LOCUS       WP_126231222             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter jejuni].
ACCESSION   WP_126231222
VERSION     WP_126231222.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33144
     Region          3..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldvaiiggg paglsaglya trgglknvvm fekgmpggqi tssseienyp gvaqvmdgis
       61 fmapwneqcm rfglkhemvg veqilknsdg sftiklegdk telakavivc tgsapkragf
      121 kgedeffgkg vstcatcdgf fyknkevavl gggdtaleea lylanicskv ylihrrdefr
      181 aapstvekvk knekielits asvdevygdk mgvtgvkvkl kdgsirdlnv pgiftfvgln
      241 vrneilkqdd dkflcnmeeg gqvsvdlkmq tsvaglfaag dlrkdapkqv icaagdgava
      301 alsamayies lh
//
LOCUS       WP_126242041             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia gladioli].
ACCESSION   WP_126242041
VERSION     WP_126242041.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia gladioli
  ORGANISM  Burkholderia gladioli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia gladioli"
                     /db_xref="taxon:28095"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34204
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spllitglaq ggqlmtttdv enwpadpngv
       61 qgpelmqrfl ehaerfntei vfdhihtakl eekpirligd sgeytcdsli istgasaqyl
      121 gltseeafmg kgvsacatcd gffyrnqeva vvgggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegkv eikwnhvlde vtgddsgvtg vkikhtgtge teqltlqgvf
      241 vaighkpntd lfqgqlemkd gyivtksgla gnatatnipg vfaagdvqdh iyrqaitsag
      301 tgcmaaldaq ryleslhdak
//
LOCUS       WP_126233332             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter jejuni].
ACCESSION   WP_126233332
VERSION     WP_126233332.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32986
     Region          3..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldvaiiggg paglsaglya trgglknvvm fekgmpggqi tssseienyp gvaqvmdgis
       61 fmapwneqcm rfglkhemvg veqilknsdg sftikleggk teltkavivc tgsapkragf
      121 kgedeffgkg vstcatcdgf fyknkevavl gggdtaleea lylanicskv ylihrrdefr
      181 aapstvekvk kngkielits asvdevygdk mgvtgvkvkl kdgsirdlnv pgiftfvgln
      241 vrneilkqdd gkflcnmeeg gqvsvdlkmq tsvaglfaag dlrkdapkqv icaagdgava
      301 alsamayies lh
//
LOCUS       WP_126247032             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Chitinophaga rhizosphaerae].
ACCESSION   WP_126247032
VERSION     WP_126247032.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga rhizosphaerae
  ORGANISM  Chitinophaga rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Chitinophaga rhizosphaerae"
                     /db_xref="taxon:1864947"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39726
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,73,92,287,313,315)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,277..278,320..321,325,
                     328..329)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,227,238,
                     255..257,264,266)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milavlkens genrvslvpe vvkqlvqqqv evwveegaga aafypdsgyr eagaalksre
       61 dilkgadvll tirppeaadf ekvppgktwa gvfqplfnpa lmqqlagrqf tifsldsipr
      121 ttraqsmdvl ssqaniagyk avllaaftys ryfpmfmtaa gsippakvli lgagvaglqa
      181 iatarrlgav vevfdtrpav keevmslgar fvevegaada skaggyaveq sedfkerqaa
      241 riaesaakad vvittaqipg kpapillpta avegmrpgsv iidlaaatgg ntgltknget
      301 ivhkdvtiig nsdlagtapa dasklyaknm hnflklligk egqwqpdfad divqgaciar
      361 dgqvvnervk qlqpaav
//
LOCUS       WP_126248913             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chitinophaga rhizosphaerae].
ACCESSION   WP_126248913
VERSION     WP_126248913.1
KEYWORDS    RefSeq.
SOURCE      Chitinophaga rhizosphaerae
  ORGANISM  Chitinophaga rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Chitinophaga.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Chitinophaga rhizosphaerae"
                     /db_xref="taxon:1864947"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33842
     Region          12..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mekntnqeha hvliigsgpa gytaaiyaar anlkpvlyqg iqpggqltit tevenypgyp
       61 egiqgpemmv dfekqaarmg adirygmats vdfssqpykv videektita daiiiatgas
      121 akwlglpseq rlngsgvsac avcdgfffrg keaaivgagd taaeealyls kicsnvhmlv
      181 rrhemraskv mqdrvlktsn imvywnsetl evvgenkveg vrilntqtke ektipvsaff
      241 vaighqpnsg ifngqlemde qgyiktipgt tktsvegvfa cgdvqdknyr qavtaagsgc
      301 maaldaeryl sakgh
//
LOCUS       WP_126253211             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter jejuni].
ACCESSION   WP_126253211
VERSION     WP_126253211.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33042
     Region          3..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldvaiiggg paglsaglya trgglknvvm fekgmpggqi tssseienyp gvaqvmdgis
       61 fmapwneqcm rfglkhemvg veqilknsdg sftikleggk telakavivc tgsapkragf
      121 kgedeffgkg vstcatcdgf fyknkevavl gggdtaleea lylanicskv ylihrrdefr
      181 aapstvekvk knekielits asvdevygdk mgvtgikvkl kdgsirdlnv pgiftfvgln
      241 vrneilkqdd gkflcnmeeg gqvsvdlkmq tsvaglfaag dlrkdapkqv icaagdgava
      301 alsamayies lh
//
LOCUS       WP_126254445             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter jejuni].
ACCESSION   WP_126254445
VERSION     WP_126254445.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter jejuni
  ORGANISM  Campylobacter jejuni
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter jejuni"
                     /db_xref="taxon:197"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33086
     Region          3..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldvviiggg paglsaglya trgglknvvm fekgmpggqi tssseienyp gvaqvmdgis
       61 fmapwneqcm rfglkhemvg veqilknsdg sftikleggk teltkavivc tgsapkragf
      121 kgedeffgkg vstcatcdgf fyknkevavl gggdtaleea lylanicskv ylihrrdefr
      181 aapstvekvk knekielits asvdevygdk mgvtgvkvkl kdgsirdlnv pgiftfvgln
      241 vrneilkqdd gkflcnmeeg gqvsvdlkmq tsvaglfaag dlrkdapkqv icaagdgava
      301 alsamayies lh
//
LOCUS       WP_126258797             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium sp. LVM 105].
ACCESSION   WP_126258797
VERSION     WP_126258797.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium sp. LVM 105
  ORGANISM  Bradyrhizobium sp. LVM 105
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Bradyrhizobium sp. LVM 105"
                     /db_xref="taxon:2341115"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39344
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag iksglpdsef taagatvstd
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneaa lktiadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa emvrsmkpgs vlvdlaverg gnvegakpge
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpksa
//
LOCUS       WP_126259127             321 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Bradyrhizobium].
ACCESSION   WP_126259127
VERSION     WP_126259127.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34219
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msapvhakvv iigsgpagyt aaiyaaraml epiliqgiqp ggqltittdv enypgfadvi
       61 qgpwlmeqme kqavhvgtri vtdlvtklet ahrpfrltcd sgdvyladsv ilatgaqarw
      121 lglpseakfq gggvsacatc dgffyrnkdv vvvgggntav eealyltnha sqvtivhrrd
      181 hfraerilqe rlfkhpkikv iwdsavdeic gtenpnkvth vrlknvktga ltdvktdgif
      241 iaighapate lvkdqiklkp sgyvevapns tatsvpglfa agdvadetyr qavtaaglgc
      301 maaleaerfl alraseraaa e
//
LOCUS       WP_126282379             535 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia stagnalis].
ACCESSION   WP_126282379
VERSION     WP_126282379.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     Protein         1..535
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55165
     Region          3..535
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtlrigiple tttgerrvat vpevveklik lgfsvavqsg agaganfddd ayraagatva
       61 ataaelwsgs divfkvrpps sdevalmrdg gtligfvwpa qnpelmaqla akratvlaid
      121 slprtlsraq kmdaltsmag isgyraviea ahafgrflng qvtaagkvpp akvfiagagv
      181 aglaaigtaa slgaivrand traevadqvk slggefvkvd yeeegsgggg yakvmsegfq
      241 qaqramyaqq ardadiiitt alipgkpapk litaemvqsm kpgsvivdma aeqggncelt
      301 vpgeavvrhg vtivgytdla srlsrqsstl yatnllrvie elcktkdgti nvdfdddair
      361 gltvikegnv twppppikqa avapkpqaaa pavaaaaksk ghghgsgepm sakalaivfa
      421 igalafllvg qyapasflsh ftvfvlacfv gymviwnvtp slhtplmsvt naissiiaig
      481 alvqvapplg elagsagdrp sglilglavg altltavnmf ggfavtrrml amfrk
//
LOCUS       WP_126285214             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia stagnalis].
ACCESSION   WP_126285214
VERSION     WP_126285214.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39146
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyasag hrvsvakgag taasypdeay aaagaeltdq
       61 taafdadivl kvqapteaei pslkrgsvli gmldpfngeq aaqlagagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvgaalypr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee rdaaqgvggy arpmpaswlg
      241 rqaalvhera kqadiiitta lipgrpaptl isvetvqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad evivhngvti aghtnlaamv asdasalyar nlldfmkliv tkegtlnidl
      361 tddivaatll crdgevtrk
//
LOCUS       WP_126295147             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lysinibacillus telephonicus].
ACCESSION   WP_126295147
VERSION     WP_126295147.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus telephonicus
  ORGANISM  Lysinibacillus telephonicus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Lysinibacillus telephonicus"
                     /db_xref="taxon:1714840"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34137
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mmsekiydvv iigagpagmt aavyasranl stimiergip ggqmanteev enypgfetil
       61 gpelstkmfe hakkfgaeya ygdvseiidg eeykiikaga keyktrsiii ttgaeykkmg
      121 vpgekelggr gvsycavcdg affkqknlvv vgggdsavee gvyltrfadk vtivhrrdkl
      181 raqkilqdra fanekidfiw nhtvkqinek dgkvgsvtlv stvdgseqef aadgvfvyig
      241 mvpltqpfkd lgivnehgyi vtndkmetsv kgifaagdvr ekmlrqivta tgdgsiaaqs
      301 vqsyveelke kinq
//
LOCUS       WP_126297653             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Cellulomonas fimi].
ACCESSION   WP_126297653
VERSION     WP_126297653.1
KEYWORDS    RefSeq.
SOURCE      Cellulomonas fimi
  ORGANISM  Cellulomonas fimi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Cellulomonadaceae; Cellulomonas.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Cellulomonas fimi"
                     /db_xref="taxon:1708"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34331
     Region          6..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstvrdlviv gsgpagytaa iyaaraglap lvvagsvtag galmntteve nfpgfpdgiq
       61 gpelmdalqk qaekfgaevl wddavslsle gpvktvtvsg getyaaravi lstgsayrel
      121 glddekrlsg rgvswcatcd gfffrdqeii vvgggdsave eatfltrfgk rvtlvhrrdq
      181 lraskimadr aaadpkiefa wnsevvaihg tekvtgvtlr dtvtgetreh patgvfvaig
      241 hvprtdllvg qvdlddngyv svqgrstltn lpgvfaagdv vdhtyrqait aagsgcaaal
      301 daqhylagla dtahdvvdpv pttdlegar
//
LOCUS       WP_126298981             306 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corynebacterium matruchotii].
ACCESSION   WP_126298981
VERSION     WP_126298981.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium matruchotii
  ORGANISM  Corynebacterium matruchotii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Corynebacterium matruchotii"
                     /db_xref="taxon:43768"
     gene            1..306
                     /gene="trxB"
     Protein         1..306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32745
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtvhdviiig sgpagytaal ysaradlkpl vfegyeygga lmtttevenf pgfpdgimgp
       61 dlmeamrnqa erfganlrpe lvtkvdltgd tkkvwvddee fqarvvilat gsaarylgvp
      121 geqellghgv sacatcdgff frdhdiavvg ggdsameeai fltkfaksvt ivhrregfra
      181 saimleraqa ndkirfatnk vvekvlgesa vtglelrdtq tgetsvldvt amfvaighdp
      241 rtqlfrdvid tdeagyvtvq hpttktnipg vfavgdlvdn hyqqaitaag sgargaidae
      301 hylaal
//
LOCUS       WP_126302476             500 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Mannheimia haemolytica].
ACCESSION   WP_126302476
VERSION     WP_126302476.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     gene            1..500
                     /gene="nrfA"
     Protein         1..500
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56056
     Region          1..486
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkflikslav atisilgclq talaeeakte sltdkavkhe klgvkiesan hlfaekyplq
       61 ydswkstaqs tdrgsalead pryvilwagy afakdynkpr ghfyavtdvr dilrtgapkd
      121 endgpqpmac wtckgpdvpr lieekgergy fdpkwakyga eivnsigcad chdttseefk
      181 qgkpalrvar phvlralntv gwkfedldkh gkrpavcanc hveyyfknkt dvtfpwdkgv
      241 dvdsiekyyd einftdwtha lskapmlktq hpdfevwsqg thgkngvtci dchmpkvkdk
      301 ddkvytdhki gnpfdqfeat cktcheqske tlekrvkeyk hevkeamirl edqlvkahfe
      361 akaaweagat qeemkeilma irhaqwrwdy saaghgnhfh apdvmlrtia tgidraadar
      421 aklgvvlakh gvttpvaipd istkekaqla igldipkeqa akdeflktvv pqwekearak
      481 gllpaeeadk pvaapkaeak
//
LOCUS       WP_126302588             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mannheimia haemolytica].
ACCESSION   WP_126302588
VERSION     WP_126302588.1
KEYWORDS    RefSeq.
SOURCE      Mannheimia haemolytica
  ORGANISM  Mannheimia haemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Mannheimia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Mannheimia haemolytica"
                     /db_xref="taxon:75985"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34208
     Region          2..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mttkhtklli lgsgpagyta avyaaranln pvlvtgmqqg gqltttdeie nwpgefeqit
       61 gtelmnkmlk haekfeteiv fdhihsvdls krpftlkgdl htftcdalii atgasakylg
      121 lpseehfkgk gvsacttcdg ffyrnkpvav vgggntavee alylanlase vhlihrrdsf
      181 raekillgrl qkrieegkii lhtdrtvdev lgdnmgvtgl rltstkeels eeikvdgffv
      241 aighapntam fegqleleng yikvksgleg natatsvegv faagdvmdhn yrqaitsagt
      301 gcmaaldaer fldaqea
//
LOCUS       WP_126304097             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            animaloris].
ACCESSION   WP_126304097
VERSION     WP_126304097.1
KEYWORDS    RefSeq.
SOURCE      Neisseria animaloris
  ORGANISM  Neisseria animaloris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Neisseria animaloris"
                     /db_xref="taxon:326522"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53722
     Region          1..510
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipkesl pgetrvactp stvtqlqklg fevvvergag laaslddaay eaagalvade
       61 aevwacpliy kvnapsesea grlkagqtlv sflwpaqnpe lvqkltdqkv nvlamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vkafdtrlev aeqiesmggq flkldfpqea ggsgdgyakv mseefiaaem
      241 klfaeqaqqv diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnlsklls pnkggeiald fedviirnmt
      361 vtrdgeitfp ppaiqvsaap qqqaqaapvs kpepkpvptw kklapaviga vlvlwmgava
      421 paeflnhfiv fvlacvigyy vvwnvshslh tplmsvtnai sgiivvgall qigqgngvvs
      481 flafiavlia sinifggfyv trrmlnmfrk g
//
LOCUS       WP_126311654             374 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Delftia].
ACCESSION   WP_126311654
VERSION     WP_126311654.1
KEYWORDS    RefSeq.
SOURCE      Delftia
  ORGANISM  Delftia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Delftia"
                     /db_xref="taxon:80865"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38736
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetm agetrvaatp etvkklraqg hvlrvqsgag vaasvpdalf eaagaeivda
       61 agalgadlvl kvripsedel plvrkgatlv gmldpfqpag lqrladagvt ayaleaaprt
      121 traqsmdvls sqaniagyka vmiaanqyqr ffpmlmtaag tvkaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvr eqveslgakf idvpyetaee keaaegvggy arpmpqswld
      241 rqkaevakrv aqadvvitta lipgrpapvl vtaemvqamk pgavivdlaa erggncpltq
      301 agmtvvthgv tivgltnlaa lvaadasaly arnvldflkl iinkdgalhv dmeddivaac
      361 lmahegqlaa qrrk
//
LOCUS       WP_126319513             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Citrobacter portucalensis].
ACCESSION   WP_126319513
VERSION     WP_126319513.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter portucalensis
  ORGANISM  Citrobacter portucalensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter
            freundii complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter portucalensis"
                     /db_xref="taxon:1639133"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53606
     Region          21..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mariksrvrr ffslllpllf isavhaeqts vpaktvtvea knetfapqhp dqylswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspd fakgkpeltl
      181 srpyaerame tigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmek
      241 yydniafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegkiytd
      301 hkignpfdnf pqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvra hfeakaawda
      361 gateaemkpi ledirhaqwr wdlsiashgi hmhapeeglr mlgsaldkaa dartklvrll
      421 atkgitheip lpdistkeka qaaiglnmqq inaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_126322324             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Candidatus Rickettsiella viridis].
ACCESSION   WP_126322324
VERSION     WP_126322324.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Rickettsiella viridis
  ORGANISM  Candidatus Rickettsiella viridis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Coxiellaceae; Rickettsiella.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Candidatus Rickettsiella viridis"
                     /db_xref="taxon:676208"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33726
     Region          7..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnkaqkhrli ilgsgpagyt aaiyaaranl nplvitgmqq ggqlmtttdv dnwpgdvegl
       61 qgpalmerml khaerfksqm vfdqintvdl skkpfilkgd qatyhcdali iatgasaryl
      121 gldseteftg kgvsacatcd gffykgqkva vvgggntave ealymaniae hvmlihrrds
      181 frsekilidk lmakvkagki tlvldsvvea ivgdeqgvng vkiknvktqa lsqlavhgvf
      241 iaightpnta lfqdqlkmek gyilvkggsq gaatatnihg vfaagdvads vyrqavtsag
      301 tgcmaaldae kyldecan
//
LOCUS       WP_126323723             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Morganella morganii].
ACCESSION   WP_126323723
VERSION     WP_126323723.1
KEYWORDS    RefSeq.
SOURCE      Morganella morganii (Proteus morganii)
  ORGANISM  Morganella morganii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Morganellaceae; Morganella.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Morganella morganii"
                     /db_xref="taxon:582"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34159
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mnatrhskli ilgsgpagyt aavyaaranl npvlitgvev ggqlttttev enwpgdpegl
       61 tgpvlmermq ahaekfetei indyitdvdf skrpftltge ntytcdalii atgasaryig
      121 lpseeafkgr gvsacatcdg ffyrnqkvav vgggntavee alylsniase vhlihrrdsf
      181 raekilinrl mdkvqngniv lhtdrtldev lgdqmgvtav rlrdtksdat eelpvmgcfi
      241 aighspntgi feghldleng yirvqsgthg natqtsvpgv faagdvmdhi yrqaitsagt
      301 gcmaaldaer yldsladsk
//
LOCUS       WP_126330219             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Moraxella cuniculi].
ACCESSION   WP_126330219
VERSION     WP_126330219.1
KEYWORDS    RefSeq.
SOURCE      Moraxella cuniculi
  ORGANISM  Moraxella cuniculi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Moraxella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Moraxella cuniculi"
                     /db_xref="taxon:34061"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33327
     Region          5..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maahhqliil gsgpagysaa vyaaranlkp viitglqvgg qlttttevdn wpgdaygltg
       61 nglmdrmkeh aerfgttliy dnithadlqt rpfvltgdsg tytcdaliia tgataqylgl
      121 dseqkfmgqg vsacatcdgf fyknqkvavi gggntaveea lylsniashv tlvhrrdglr
      181 aekilqeqlf ekvkqgnisi ewnhevkevl gdemgvtgik iastidnsek tlevmgmfva
      241 ighkpntalf dsqltmkdgy ivvnsgldgn atatniagvf aagdvadhvy rqaitsagtg
      301 cmaaldaeky ldals
//
LOCUS       WP_126331792             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Enterococcus faecium].
ACCESSION   WP_126331792
VERSION     WP_126331792.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33299
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydvivigag pagmtaalya srsnlsvlmi eqgapggqmn ntaeienypg fdsimgpdla
       61 ykmyegvsrf gtenaygivq dikdhgshke vicedktyeg ktviiatgci hrklgvpgee
      121 efagrgvsyc avcdgaffrn krlvvigggd saveeaiylt qfasevvivh rrdelraqki
      181 iqdrafanek isfmwdtvvd eivgnemvvt gvkarnvktg nefdlaadgv fiyigldplt
      241 apfreagltn eagwiptdne mktnipgvfa igdvrekdlr qittavgdgg iagqqvykyl
      301 esleetta
//
LOCUS       WP_126337652             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            spiritensis].
ACCESSION   WP_126337652
VERSION     WP_126337652.1
KEYWORDS    RefSeq.
SOURCE      Legionella spiritensis
  ORGANISM  Legionella spiritensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Legionella spiritensis"
                     /db_xref="taxon:452"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41046
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miiavlnesa ndtrvamtpn vvkhylklgl kvqceknagi asgftdksye eagaaiikdr
       61 kqllqqadil acvqapdpkd ldelksqall iapldnepds plikwcmkqs isafsmnlvp
      121 ritraqgmds lssqanlagy ravleavchf kraipmmmta agmihpakil ilgagvaglq
      181 aiatakrlgg viyafdvrra akeqveslga efievemeed setsggyake msedykrqqs
      241 eliakyvaqs divvttalip grqapllitk tmvetmkpgs vivdlatsrg gncelsqcdk
      301 vtlhneitii gysnmagfip ataselyann ilnlvktlat spealdfked deimkqallc
      361 hqnkylpfqs ipsketvha
//
LOCUS       WP_126341125             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter lari].
ACCESSION   WP_126341125
VERSION     WP_126341125.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter lari
  ORGANISM  Campylobacter lari
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Campylobacter lari"
                     /db_xref="taxon:201"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33091
     Region          3..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldlaiiggg paglsaglya trgglknvvm fekgmpggqi tssseienyp gvaqvldgis
       61 fmapwneqcm rfglkhemvg veqiskntdg sfnikleggk seqakavivc tgstprragf
      121 kgedeffgkg vstcatcdgf fyknkevavl gggdtaleea lylanicskv ylvhrrnefr
      181 aapstvekvk nnekielitn avvdevcgdn mgvnkvkiaf ndgskreldv pgiftfvgln
      241 vrneilkqdn geflcameeg gqvsvdlkmq tniaglfaag dlrkdapkqv icaagdgava
      301 alsalayies lh
//
LOCUS       WP_126343507             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Enterococcus hirae].
ACCESSION   WP_126343507
VERSION     WP_126343507.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus hirae
  ORGANISM  Enterococcus hirae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Enterococcus hirae"
                     /db_xref="taxon:1354"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33403
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydvivigag pagmtaalya srsnlsvami eqgapggqmn ntaevenypg fdsimgpdla
       61 ykmyegvtkf gtenvygivq dikdhgnyke vicedqsyea ktviiatgci hrklgvpgee
      121 eyagrgvsyc avcdgaffrn krlvvigggd saveeaiylt qfasevvivh rrdelraqki
      181 iqdrafanek isfvwdtvtd eivgndmvvt gvkahnvktn etidlaadgv fiyvgldplt
      241 epfkkagltn vagwiptdqd mrttmpgvfa igdvrekdlr qittavgdgg iagqqvykyl
      301 ealeettqa
//
LOCUS       WP_126351588             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Deinococcus radiophilus].
ACCESSION   WP_126351588
VERSION     WP_126351588.1
KEYWORDS    RefSeq.
SOURCE      Deinococcus radiophilus
  ORGANISM  Deinococcus radiophilus
            Bacteria; Thermotogati; Deinococcota; Deinococci; Deinococcales;
            Deinococcaceae; Deinococcus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Deinococcus radiophilus"
                     /db_xref="taxon:32062"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35975
     Region          8..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseqaqmydv iivgggpagl taaiytgrge lstlvlergl pggqisqtee venypgfpea
       61 isgmelsqrm vqqaekfgav iemdevlsid htteavqypf tvqghagnyq aksvilttga
      121 eprrlgvpge ekfwgkgvst catcdgffyr gkkvvvvggg daaveeglfl tkfadevtli
      181 hrreelrank saqarvfane kmkfiwnttv eeilgneqvs gvrlkdvntg eervmetdgv
      241 fifighipnt gfvkdtvklr ddgyvdvred iytsvpmlfa agdvsdwvyr qlatsvgtgt
      301 raamsaeral aeleaaftge gsqaaqahaa vand
//
LOCUS       WP_126358131             424 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Brucella
            abortus].
ACCESSION   WP_126358131
VERSION     WP_126358131.1
KEYWORDS    RefSeq.
SOURCE      Brucella abortus (Brucella melitensis biovar Abortus)
  ORGANISM  Brucella abortus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Brucella abortus"
                     /db_xref="taxon:235"
     Protein         1..424
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44049
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maqtlyipke sdpnetrvag saetvkkfia lgfdvvvekg ageksripda efaaagarig
       61 tavdaktadv ilkvrrpgda elkayksgaa lfamldpygh edavaalara gisaftmefm
      121 pritraqvmd vlssqanlag yqavidaaev ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskdyqa
      241 kqaalvadhi akqdivitta lipgrpaprl vskemvasmr pgsvlvdlav erggnvegav
      301 pgeiadvngv kivgylnvpg riaasasqly arnliafvet lvdkeskvlk idpeeglvka
      361 tllthqgril hpafakaeta paavtekaek pkaapkappq gcckaceksp gksgeetivp
      421 qvsg
//
LOCUS       WP_126358906             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas fluorescens].
ACCESSION   WP_126358906
VERSION     WP_126358906.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas fluorescens
  ORGANISM  Pseudomonas fluorescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas fluorescens"
                     /db_xref="taxon:294"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38767
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikklisqg hkvtvqtgag vkasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdael tlikrgtvlv gmlnpfnnda iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv ticgptnlag evaadasaly arnlldflkl vftkegqfdv nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_126359798             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia cenocepacia].
ACCESSION   WP_126359798
VERSION     WP_126359798.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39051
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrvsiakgag saasypdeay vaagaaltdq
       61 saafdadlvl kvqaptdtel pllkrgtvlv gmldpfngeq aaqlaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaslypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetaqamk pgsvlvdlaa grgpdidgrk
      301 ggncpltvad qvivhngvti agytnlasmv asdasalyar nlldflkliv tkegtpnidl
      361 tddivaatll crdgevtrk
//
LOCUS       WP_126371687             497 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Avibacterium volantium].
ACCESSION   WP_126371687
VERSION     WP_126371687.1
KEYWORDS    RefSeq.
SOURCE      Avibacterium volantium
  ORGANISM  Avibacterium volantium
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Avibacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Avibacterium volantium"
                     /db_xref="taxon:762"
     gene            1..497
                     /gene="nrfA"
     Protein         1..497
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=55253
     Region          1..493
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnifrktlas laiagltlvs aqplmaadns vaekraptre elakpnpdlk iqaiseqfae
       61 kypkqynswa ataesteivp aievdprmiv mwggyafske ynkprghfyt vtdvrnilrt
      121 gapfdansgp qpmacwtckg pdvprliaew geeeyfngkw akggaevans igcadchdtt
      181 skdfaegkpa lriarphvlr aldaigkdfa hldktdkrga icanchveyy fdkkvvnnvv
      241 fpwmkgvdvd smeqyydnie fydwihsisk tpmlkaqhpd yetwlqgthg kngvtcvdch
      301 mpkvqgadgk vytdhkignp ldsfentcan chdqsketlt kvvaghkkdi kdvmikledq
      361 ivkahfeaka awdagateee mkpalqairh aqwrwdysaa ghgghihapd iilktiatgl
      421 driadartkl aiiltkhgvk qpinypdist adkawkamgi diekeraaka kflkevvpqw
      481 nkealekglm ekappak
//
LOCUS       WP_126375912             385 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Desulfovibrio ferrophilus].
ACCESSION   WP_126375912
VERSION     WP_126375912.1
KEYWORDS    RefSeq.
SOURCE      Desulfovibrio ferrophilus
  ORGANISM  Desulfovibrio ferrophilus
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae;
            Desulfovibrio.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Desulfovibrio ferrophilus"
                     /db_xref="taxon:241368"
     Protein         1..385
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40484
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 milavpkety pgerrvalvp savpplikag ftvlveqdag taascldtdf kdkgaeivps
       61 rsdlfaradv ilqvrspgan peagaadiam lregqivigl tepftdpais kavaetgavl
      121 fsmeliprit raqsmdalss matlagyqav llaagnlpkm fpmmmtaagt iapakvfivg
      181 vgvaglmaia qarklgavve aydvrpavke qvqslgakfv emeleaddae dkggyakamd
      241 edfyrkqrel mtrvvaandv vittaaipgr aapilvteem vkgmapgsvi vdlaavgggn
      301 celtrpdevv eahgvkifgp tdlpsqmcid asrmyaknis alllnmaedg rvdidkddev
      361 vagtmvtrdg kvvhpmilek leeta
//
LOCUS       WP_126374369             506 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Actinobacillus lignieresii].
ACCESSION   WP_126374369
VERSION     WP_126374369.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus lignieresii
  ORGANISM  Actinobacillus lignieresii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Actinobacillus lignieresii"
                     /db_xref="taxon:720"
     gene            1..506
                     /gene="nrfA"
     Protein         1..506
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=56365
     Region          1..492
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mkrltknlam atiamlgcls saawaeekpa qtpsltdkal kheklgvvve sanhkfaeky
       61 plqynswkat sestdrgsal aadpryvvlw agyafakdyn kprghyyait dvreilrtga
      121 pkdendgpqp macwtckgpd varlieekge rgyfdpkwak ygaeivnsig cadchdttsk
      181 efeegkpalr varphvlral etvgwkfedl dkhgkraavc anchveyyfk dkkdvtfpwt
      241 kgidvdsiek yydeiqfadw thalskapml ktqhpdfeiw sqgvhgkngv tcidchmpkt
      301 vdsktgkvyt dhkianplea gqfertcktc heqseetlka rvkehkkqvk eamirledql
      361 vkahfeakaa wdagatqeem kdiltairha qwrwdysaag hgshmhapdv mlhviasgid
      421 raadaraqlg vvlakhgvtt pvaipdistk ekaqkaigld ipkdqaakde flrtvvpqwd
      481 aearkkgllp aeeepkavva pkaeak
//
LOCUS       WP_126380262             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arachnia propionica].
ACCESSION   WP_126380262
VERSION     WP_126380262.1
KEYWORDS    RefSeq.
SOURCE      Arachnia propionica
  ORGANISM  Arachnia propionica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Arachnia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Arachnia propionica"
                     /db_xref="taxon:1750"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32513
     Region          4..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtvheliiig sgpagytaai yaaraalnpi vfegaldsgg almntteven fpgfpdgvmg
       61 pdlmgqmrsq aerfgaqlvt ddaeavdltg evkkvtdsag kvweakavil amgsgyrklg
      121 vdgedrlsgr gvswcatcdg affrdkpiav igggdsavee atfltrfasr vtlvhrrdel
      181 raskamasra ekdpkldfaw nsvvesvngd arvesvtlrd tvtgetrrle vsgvfvaigh
      241 dprsalvkgq veldeagyvk vaagsqatnl pgvfacgdlv dhtyrqaita agsgcqaald
      301 aerwlaanea
//
LOCUS       WP_126379087             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Arachnia
            propionica].
ACCESSION   WP_126379087
VERSION     WP_126379087.1
KEYWORDS    RefSeq.
SOURCE      Arachnia propionica
  ORGANISM  Arachnia propionica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Propionibacteriaceae; Arachnia.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Arachnia propionica"
                     /db_xref="taxon:1750"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52829
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mdvgvpreig dtrvaatpkt vaqlrklgyh vfvesgaglg asfsddayre vggvivdnaw
       61 drdivlavga psdtqlldmh pgatlisfla prqdpsltrr iaaqgvnals mdmvprtsra
      121 qaldalssla nisgyravve aahafgrfft gqvtaagkvp patvfvigtg vaglaaigaa
      181 sslgavvrat dvrpetaeqv tsmgatflhv gqadqgvssd gyakevgady aaraaelyaa
      241 qarevdiiit taaipgkpsp rlitaemves mkpgsvivdm aaigggncel trpgesyvte
      301 ngvtiigytd lssrlpgqss qlygtnlvna lklmtpgkdg nlvidfddev vrnmtivrdg
      361 evtfpppeik vsaapapaaa arpstpatpa kpprpwwhqv awvgagsval ialltlapsp
      421 lvglmavfvl aivvgyyvvw nvthalhtpl msvtnavsgi ivvgamtqlp sdnwvvkiia
      481 fvavliasin vfggftvthr mlnmfrkg
//
LOCUS       WP_126382228             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces howellii].
ACCESSION   WP_126382228
VERSION     WP_126382228.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces howellii
  ORGANISM  Actinomyces howellii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Actinomyces howellii"
                     /db_xref="taxon:52771"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52638
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgvpcegp dqpvvaatpq tvekmirlgy evlvergage rarfpdsaye ragarlvgpt
       61 gawtcevvls asapdeeslg mlgpgttvvs rldparhpel ieslratgat alaldavpri
      121 sraqamdvls sqanlagyra vieaathfgr llggqvtaag kfppasvyvi gagvaglaai
      181 gtatslgavv rgtdvrpeva dqvrsmgaqf vpvptaqets sdgyatqmsq dqaalaarly
      241 aqqaaqadiv ittaaipgra apilldreai eamapgsvii dmaaatggnt eltvagevvt
      301 teggvtivgh tdlagrlpsq asqlygqnlv nlltlmtpek dgtlvldled evvraitvch
      361 egqtlwpppp vtvsaapaaq gpsaeelara eaqeaaarar srrlravgla aaalvgaalv
      421 lvtpeaatsh yvvlvlsvil gfhvisnvtp alhtplmsvt naisgiillg aisqvghsdp
      481 lisaaafval vlatvnvfgg favthrmlam frkd
//
LOCUS       WP_126385160             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudanabaena sp. ABRG5-3].
ACCESSION   WP_126385160
VERSION     WP_126385160.1
KEYWORDS    RefSeq.
SOURCE      Pseudanabaena sp. ABRG5-3
  ORGANISM  Pseudanabaena sp. ABRG5-3
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Pseudanabaenales; Pseudanabaenaceae; Pseudanabaena.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Pseudanabaena sp. ABRG5-3"
                     /db_xref="taxon:685565"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40354
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvikeie fgerrvalip evvsrltkng levlveshag elsffadsay teagakiitd
       61 kstlinesdi llkvgapree evsmfkqgqi tigflnplgr pelirrlahq gvtalsmemi
      121 prssraqsmd alssqasiag ykavllaaaa lpkylpmltt aagtippakv vvlgagvagl
      181 qaiatarrlg aqveaydirp avreevqslg akfidvilqe dttaaggyak eiseaakhha
      241 qvvlakhike adivittaqv pgrkapvmvt eamisqmrrg siivdlageq ggncegtvag
      301 kdvishgvti ispinlpatm pihasqkyak nllnllnhli kkgelnldfa ddiisstcit
      361 hageilnqrv kdalsqlavt a
//
LOCUS       WP_126382753             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinomyces howellii].
ACCESSION   WP_126382753
VERSION     WP_126382753.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces howellii
  ORGANISM  Actinomyces howellii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Actinomyces howellii"
                     /db_xref="taxon:52771"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32768
     Region          3..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mihdvvivgs gpagytaaiy aaraqlkpvl lagsvtagga lmntteveny pgftdgilgp
       61 elmtqmqeqa erfgtdirye dvvalelege vkrvrteeav yetrtviist gseyrtlglp
      121 dearlsghgv sycatcdgff fkdkpivvvg ggdsameeal fltrfgssvt vvhrrdelra
      181 savmakramd hpsidfawns vvvglngqda lesvvledtv tgerreleaa glfvaigqip
      241 rtelvsdvlt ldeagyivvd spsqrtgvpg vfacgdvadp lyqqaitaag sgcraaldae
      301 hyletlra
//
LOCUS       WP_126387102             329 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudanabaena sp. ABRG5-3].
ACCESSION   WP_126387102
VERSION     WP_126387102.1
KEYWORDS    RefSeq.
SOURCE      Pseudanabaena sp. ABRG5-3
  ORGANISM  Pseudanabaena sp. ABRG5-3
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Pseudanabaenales; Pseudanabaenaceae; Pseudanabaena.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Pseudanabaena sp. ABRG5-3"
                     /db_xref="taxon:685565"
     Protein         1..329
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=37389
     Region          5..184
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiidiyskr kkavergnqt eiyqytslpi efrrqviyiw kdaigayrir nlfdspsnll
       61 aslkspdtlv epivnrvwks iykllarelg lsessnpfeq cqsfllddnt nidnlldiie
      121 ltfsyiedki pdlleeyeyd gikldqtatg ainelnyrfh ehgigyqyik gqivrvdslf
      181 ihaeavipal tliseedfig aeqefrsahe hyrnqeykaa ivealkafes tmkticdkfn
      241 wdygkkpnas nlikvvlkee liplylqdhl tsltnvlqgg vptvrnktsg hgqgseikev
      301 peylaayvlh ltasnivllv eaykakssg
//
LOCUS       WP_126385777             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudanabaena sp. ABRG5-3].
ACCESSION   WP_126385777
VERSION     WP_126385777.1
KEYWORDS    RefSeq.
SOURCE      Pseudanabaena sp. ABRG5-3
  ORGANISM  Pseudanabaena sp. ABRG5-3
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae;
            Pseudanabaenales; Pseudanabaenaceae; Pseudanabaena.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudanabaena sp. ABRG5-3"
                     /db_xref="taxon:685565"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33950
     Region          12..316
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msdtiapssv rdvviigsgp agytaaiyag ranlhplvfe gfqkggiagg qlmttteven
       61 fpgfptgvmg pqlmmqmkeq asncgaelvm edvvavdfsd rpftvksssl svqahsviia
      121 tgatakrlhl psetkywnrg isacavcdga apifrgvela vvgggdtave eaifltkygs
      181 kvhllvrsdr lraskvmqer ifnhpkitvh whslpvdvyg eeivqgvkic daitneerdl
      241 avgglfyaig htpntelftg qieldptgyi itrgkstatn iegvyacgdv qdheyrqait
      301 aagtgcmaal everwlsk
//
LOCUS       WP_126393494             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces cyaneochromogenes].
ACCESSION   WP_126393494
VERSION     WP_126393494.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces cyaneochromogenes
  ORGANISM  Streptomyces cyaneochromogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces cyaneochromogenes"
                     /db_xref="taxon:2496836"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34218
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgim
       61 gpelmdnmra qserfgaelv pddivnvdlt geiktvtdta gtvhrakavi vatgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqdr afadpkikfv wdsevaevqg dqklsalklr nvktgelsdl avtglfiaig
      241 hdprtelfkg qleldeegyl kvdapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala deenaepekt sv
//
LOCUS       WP_126402642             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus lutetiensis].
ACCESSION   WP_126402642
VERSION     WP_126402642.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus lutetiensis
  ORGANISM  Streptococcus lutetiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus lutetiensis"
                     /db_xref="taxon:150055"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32673
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigsg pagmtaglya aranlkvgii eqgapggqmn ntseienypg ydhisgpels
       61 mkmhaplekf gveniygivk siedagdvkr vitedatyea ktiilatgak nralgvagee
      121 eytsrgvsyc avcdgaffrn kdllvigggd saveeagylt qfaksvtiih rrdelraqki
      181 lqdrafanek infiwdsvvk eikgndikvs gvvvenvktg eisehefggi fiyvgvdpvs
      241 kmieglgitd eagwvitddh mktaipgifa igdvrkkelr qittavgdga iagqgvyqyi
      301 enmk
//
LOCUS       WP_126401081             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Blastochloris tepida].
ACCESSION   WP_126401081
VERSION     WP_126401081.1
KEYWORDS    RefSeq.
SOURCE      Blastochloris tepida
  ORGANISM  Blastochloris tepida
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Blastochloridaceae; Blastochloris.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Blastochloris tepida"
                     /db_xref="taxon:2233851"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33804
     Region          6..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtthaklvii gsgpagytaa iyaarallqp vliqglqpgg qltvtteven ypgfaepiqg
       61 pelmeqmrlq aervgtrivt dlvesvdlsa rpfrlvcesg evwlaeslii atgaqakwlg
      121 lpsetafrgf gvsacatcdg fffrgrnvmv vgggnsavee alflthfaak vtvvhrrdaf
      181 raekilqerl fanpkvevvw nhavedilge aspsrvtavr lknvltgevs eravdglfva
      241 ighapatalf egqlkmkpng ylwvapysta tsvpgvfaag dvaddvyrqa vtaagmgcma
      301 aleaerflaa eaapasaaae
//
LOCUS       WP_126398822             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Blastochloris tepida].
ACCESSION   WP_126398822
VERSION     WP_126398822.1
KEYWORDS    RefSeq.
SOURCE      Blastochloris tepida
  ORGANISM  Blastochloris tepida
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Blastochloridaceae; Blastochloris.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Blastochloris tepida"
                     /db_xref="taxon:2233851"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39771
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaipvetd eaeprvaatp etvkrlvglg adivvqagag lasgirdney eaagaklalt
       61 akdavanadi vlkvrrptpd efadyksgal viaimdpygn eaalkamaea rlvsfamelm
      121 pritraqvmd vlssqanlag yravidgaae ygralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfiavedde fkqaetaggy akemskeyqa
      241 kqaelvashi akqdivitta lipgrpapkl vskemvesmk qgsvvvdlav erggncalae
      301 pgavvvhegv kivgylnvpg rlaatassly aknlfafvet lvdkntksla vnwddelvka
      361 tcltkdgavi hpsfspkhaa e
//
LOCUS       WP_126403840             304 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptococcus].
ACCESSION   WP_126403840
VERSION     WP_126403840.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32733
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigag pagmtaalya arsnlkvall eagipggqmn ntsdienypg yanisgpela
       61 ekmfepleal gvehlfgrae nivdqgsyke ittddghlqa ktviiatgsn hrllgvpgee
      121 elnsrgvsyc avcdgaffrd edlmvvgggd saveeaiflt qfaksvtivh rrdalraqkv
      181 lqdrafanek ihfawntvve eikgdnrvts lllkdvqtgq vreqlaggvf iyvgldpvsd
      241 fatelgilde ngwvvtddhm rtsvpgvfav gdvrqkdlrq vttavgdgav agqeaykyit
      301 ehee
//
LOCUS       WP_126406460             303 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptococcus].
ACCESSION   WP_126406460
VERSION     WP_126406460.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33043
     Region          2..301
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlfgsve kiehqgaikk vftedeifet ktliiatgav hrhlgvpgee
      121 elnsrgvsyc avcdgaffrd edllvvgggd saveeavflt rfaktvtiih rrdelraqkl
      181 lqerafanek ihfiwdsvvk eikgdkrvss vmvenvktge isehefggvf iyvgldpvse
      241 fakdlgitne agwivtnnhm ktaisgiyai gdvrekdlrq vttavgdgav agqevykyit
      301 enf
//
LOCUS       WP_126414672             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinomyces viscosus].
ACCESSION   WP_126414672
VERSION     WP_126414672.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces viscosus
  ORGANISM  Actinomyces viscosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Actinomyces viscosus"
                     /db_xref="taxon:1656"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33033
     Region          3..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mihdvvivgs gpagytaaiy aaraqlnpvi lagsvtagga lmntteveny pgfidgimgp
       61 elmnqmqeqa erfgaeirye dvtalelegd ikrittsdat yeartviist gseyrhlgid
      121 geerlsghgv sycatcdgff fkdqdivvvg ggdsameeat fltrfarsvt vvhrrdelra
      181 savmakraqe dskisfawns rvvelhgeds ltgvtledtv tgerrrleat glfvaigqvp
      241 rselvadvle ldeagyikve vpsqrtripg vfacgdvadp tyqqaitaag sgcraaldae
      301 hylttvqa
//
LOCUS       WP_126415204             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces viscosus].
ACCESSION   WP_126415204
VERSION     WP_126415204.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces viscosus
  ORGANISM  Actinomyces viscosus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Actinomyces viscosus"
                     /db_xref="taxon:1656"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53567
     Region          1..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvprepa dqprtaaspq tvermtrlgy evlvergage raqfpddaye aagaelagga
       61 rvwgcevvvs asapseehla lmsrgavlic rldparrpel lealrergit claldvvprv
      121 sraqsldvls sqanlagyra vieaashlgr lfsgqvtaag kfppatvyvi gagvaglsai
      181 gtacslgaqv rgsdvrpeva dqvrsmgaqf vplpraqevs sdgyakemda dqaaaanaly
      241 arqaaesdvv ittasipgrr apvlldrgai eamrpgsvvi dmaaatggnt eltvpgevvt
      301 taggvtivgh tdlagmlpsq asqlygrniv nllglltpak dgvltldled evvraitvth
      361 dgevmwpppp iqvsaavapg hsaeaaadda asqeaareaa raaqarsrsr qwlglaaasl
      421 vgaalvlvtp paatshyivl mlsvilgfhv isnvtpalht plmsvtnais giilvgaisq
      481 vgnphplisa isliavvlat inivggfavt hrmlamftkd
//
LOCUS       WP_126417133             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Trueperella bialowiezensis].
ACCESSION   WP_126417133
VERSION     WP_126417133.1
KEYWORDS    RefSeq.
SOURCE      Trueperella bialowiezensis
  ORGANISM  Trueperella bialowiezensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Trueperella.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Trueperella bialowiezensis"
                     /db_xref="taxon:312285"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53001
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvprepa gqalvaaspd tvgklvklgy dvavesgagv aasfpdshya dagalitnke
       61 evwaadivta idapgqteld lmrrgatlia rmsprsneal lgelssrgit glamdmvpri
      121 sraqsmdvls slanvggyra vieaanqfgr vfsgqvtaag kvppatvyvi gagvaglaai
      181 gtaksmgaiv katdvraeta eqvesmgaqf veipvaaqes adgyakemge eqaraaekly
      241 aqqaaeadiv ittaaipgkr spilltadav anmkpgsvvv dmgagnggnv vgsqpdevvv
      301 tdngvtiigy telacrlpsq asqlfgqnvv nffklttpgk dgnlhldldd eivrqmlvtl
      361 edqimfpppp vqvsaapasp ppaqpqpeav ppqqekswla khwwklaava ifawlilsap
      421 pgmdgsfmvf ilavvvgfyv itavthslht plmsvtnais giivvggllq igsdnvavqi
      481 laflavavgs inifggftvt ermlkmfhrs
//
LOCUS       WP_126416459             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Trueperella bialowiezensis].
ACCESSION   WP_126416459
VERSION     WP_126416459.1
KEYWORDS    RefSeq.
SOURCE      Trueperella bialowiezensis
  ORGANISM  Trueperella bialowiezensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Trueperella.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Trueperella bialowiezensis"
                     /db_xref="taxon:312285"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32610
     Region          3..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mihdvvivgs gpagwtaaiy taraglkpil lagtmdagga lmtttevenf pgwpegimgp
       61 elmqkfeeqa vrfgtdmrye davelkldgd ikeirtdqdt yrtravilav gseykklgle
      121 geelftgkgv sycatcdgff fkdreiavig ggdsavteal fltrfgstvh vihrrdelra
      181 sqimadrlla ndkvtmhwns vvekingegk lesltlrdtq tgetrdlpvs gmfvaighep
      241 rtkildgale lddagyivvs epstatsipg vfacgdvvds yyqqaitaag sgakaaldve
      301 aylg
//
LOCUS       WP_126417651             492 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Pasteurella multocida].
ACCESSION   WP_126417651
VERSION     WP_126417651.1
KEYWORDS    RefSeq.
SOURCE      Pasteurella multocida
  ORGANISM  Pasteurella multocida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Pasteurella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Pasteurella multocida"
                     /db_xref="taxon:747"
     gene            1..492
                     /gene="nrfA"
     Protein         1..492
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=54919
     Region          14..491
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mngviivntl kkrlfvattm iwglsvtlpv laeykpieqp vepanpslki esrndlfkek
       61 ypkqyqtwad tsksmdldsv nyedprvivl wagyafakdy kkprghfyav tdvreilrta
      121 apmtsdagpm pmacwscksp dvprliaerg eagyfgatwa sggsevvnpi gcadchdtts
      181 kdfaegkpal riarpyvlra lekidhkfdt sdrtdqraal canchveyyf agdlkqvtfp
      241 wdngitvdam ekyyddigfv dwthavskap mlkaqhpdye twmlgvhgkn gvtcidchmp
      301 kvqgadgkvy tdhqignpfn afehtcanch dqskeklqam vksrkteikd vmlrledqlv
      361 aahfeakaaw eagaskeemk ealqdirhaq wrwdyaaagh gghihapdvl lkvigtgldk
      421 ssdartklvr vlakhgitdp vqlpdistae nawkatgvdi ekerkakaef lktvvpqwdk
      481 earekgllpa ek
//
LOCUS       WP_126420746             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Asticcacaulis excentricus].
ACCESSION   WP_126420746
VERSION     WP_126420746.1
KEYWORDS    RefSeq.
SOURCE      Asticcacaulis excentricus
  ORGANISM  Asticcacaulis excentricus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Asticcacaulis.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Asticcacaulis excentricus"
                     /db_xref="taxon:78587"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38643
     Region          3..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,76,95,292,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,128..129,138..139,142..143,146..147,149..150,
                     152..157,159,161..163,166,189..190,282..283,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,128,131,134,175..178,198..200,232,243,
                     260..262,269,271)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(125..126,128,138,181..182,189,205..206,208..211)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(158..162,165,168,191,193)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mvlvigipke sltgetrvaa tpdtvkkwva sgqrvvvetg aglsaaftde aftaagaeia
       61 dtkavwssad illkvrgpst teaktlkqga tvvalldayr ekdalkalae agatayamef
      121 vpritraqvm dalssqanla gyraviegah lygkafpmmm taagtvapak vfvmgvgvag
      181 lqaiatarrl gavvsatdvr patkeqvesl gakfiavede efknaqtagg yakemsddyk
      241 akqaelisgh igkqdivitt alipgrpapr lvtaaqvasm kagsvlvdia apqggnvegc
      301 vpdsvaethg vkiygptniv aaiandasal yaknlqaflg llikdgalsp dfedeilkaa
      361 lvtqngavvh pnlqn
//
LOCUS       WP_126428651             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Brevibacillus marinus].
ACCESSION   WP_126428651
VERSION     WP_126428651.1
KEYWORDS    RefSeq.
SOURCE      Brevibacillus marinus
  ORGANISM  Brevibacillus marinus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Brevibacillus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Brevibacillus marinus"
                     /db_xref="taxon:2496837"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34648
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseqkvydvi iagagpagmt aavytsranm stlmiergvp ggqmanteei enypgfatil
       61 gpdlstkmye halkfgaeya ygeiseiqdg dpykkvitsd gkeylaksvi vatgaehrll
      121 gvpgekelsg rgvsycavcd gaffrgkelv vvgggdsave eavfltrfat kvtivhrrde
      181 fraqkilqkr afenekidvi wdtvvkeirg dgvvqsvlle nrktgeqref ptngvfiyvg
      241 mdpltscvan lgitnqagyi etdeamrtkv pgifaagdvr ektlrqvvta tgdgsiaaqs
      301 aqhyveslne rlqeknvtis
//
LOCUS       WP_126422763             328 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Asticcacaulis].
ACCESSION   WP_126422763
VERSION     WP_126422763.1
KEYWORDS    RefSeq.
SOURCE      Asticcacaulis
  ORGANISM  Asticcacaulis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Asticcacaulis"
                     /db_xref="taxon:76890"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35072
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttprtvrca iigsgpagwt aaiyaargll hpvvftgpqt ggqltittdv enypgfaevi
       61 qgpwlmdqmk aqaehmgtev itdivvkadl sqrpfrletd agnvylaetv iistgaqakw
      121 lglesektyq gfgvsacatc dgffyrnktv avvgggntav eealfltkfa skvylihrrd
      181 svrsekilae rmyaepkiqp vwnsaideil getnefggas vtgvrlknvh tgdthelpld
      241 gvfiaighap ssqlfqgqle tnaggylkve pgtpktaikg vfaagdvtdd vyrqavtaag
      301 mgcmaaleai rllaeedhhr qdakigaw
//
LOCUS       WP_126433711             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_126433711
VERSION     WP_126433711.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33712
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lhsekilqdk lfdkaengnv rlhwnttlde vlddasgvtg vrlkntidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vcrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_126442938             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_126442938
VERSION     WP_126442938.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33334
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksvivat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_126438987             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Peptoniphilus harei].
ACCESSION   WP_126438987
VERSION     WP_126438987.1
KEYWORDS    RefSeq.
SOURCE      Peptoniphilus harei
  ORGANISM  Peptoniphilus harei
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Peptoniphilus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Peptoniphilus harei"
                     /db_xref="taxon:54005"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34626
     Region          11..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydiiiiggg pagltaglya arskkktlii ekgieggqia ettqvenypg idsidgvelg
       61 kkmadqakkf gaeivmdqve dmeldgevkk ikgyvdsyea ksviiatgas preigapgek
      121 eykgrgvsyc stcdaafyed evvyvvgggd savqealfit nfakkvyiih rrdelraskv
      181 lqeqafnndk idfiwnttvk eikgdkivne milhntktge drsiksddpf gifvfigyip
      241 stemfegkve ltddryiktd eemrtnvpgv faagdirkkt vrqvvnaagd gavaamnaqk
      301 yvdemegnly egfken
//
LOCUS       WP_126444133             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sulfuricystis multivorans].
ACCESSION   WP_126444133
VERSION     WP_126444133.1
KEYWORDS    RefSeq.
SOURCE      Sulfuricystis multivorans
  ORGANISM  Sulfuricystis multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Sulfuricystis.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Sulfuricystis multivorans"
                     /db_xref="taxon:2211108"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33576
     Region          2..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mttrhsklli lgsgpagyta avyaaranlq pvlitgmaqg gqlmtttevd nwpadadgvm
       61 gpdlmarfek harrfgteii fdhihtarlt ekpfrligda geytcdalii atgasaqylg
      121 lpseqafmgk gvsacatcdg ffyrdqpvav igggntavee alylaniash vtlvhrrdkl
      181 raekimqdkl fekekagkvt ikwdsvldev lgdksgvtgm riknvksgat eeiqlmgifi
      241 aighkpntai fagqlemqng yivtragrdg natatsvpgv faagdvqdmi ykqavtsaas
      301 gcqaaldaek yldaia
//
LOCUS       WP_126439958             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus equinus].
ACCESSION   WP_126439958
VERSION     WP_126439958.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus equinus (Streptococcus bovis)
  ORGANISM  Streptococcus equinus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus equinus"
                     /db_xref="taxon:1335"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32730
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtliigsg pagmtaglya aranlkvgii eqgapggqmn ntseienypg ydhisgpels
       61 mkmhaplekf gveniygivk siedagkikr vitedatyea ktiilatgak nralgvagee
      121 eftsrgvsyc avcdgaffrn qdllvvgggd saveeagylt qfaksvtiih rrdelraqki
      181 lqdrafanek ikfiwdsvvk eikgndikvs gvtvenvktg eiskhefggi fiyvgvdpvs
      241 kmvenlgitd eagwvitddh mktsipgifa vgdvrkkelr qittavgdga iagqgvyqyi
      301 enmk
//
LOCUS       WP_126441192             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus milleri].
ACCESSION   WP_126441192
VERSION     WP_126441192.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus milleri
  ORGANISM  Streptococcus milleri
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus milleri"
                     /db_xref="taxon:33040"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33205
     Region          2..301
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigsg pagmtaalya arsnlkvall ergipggqmn ntsdienypg yanisgpela
       61 ekmfeplekl gvehlfgyvk kiedhgnmkk vftedevfet ktviiasgaf hrhlgvlgee
      121 elnsrgvsyc avcdgaffrd edllvvgggd saveeavflt rfaktvtiih rrdelraqkv
      181 lqdrafanek irfiwgsvvk eikgdkrvss vivenvktge isehefggvf iyvglepvse
      241 fvkdlgitne agwivtdnhm kttisgiyav gdvreknlrq vttavgdgai agqevykyit
      301 enf
//
LOCUS       WP_126442770             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_126442770
VERSION     WP_126442770.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33380
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealyltnia srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_126446325             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sulfuricystis multivorans].
ACCESSION   WP_126446325
VERSION     WP_126446325.1
KEYWORDS    RefSeq.
SOURCE      Sulfuricystis multivorans
  ORGANISM  Sulfuricystis multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Sterolibacteriaceae; Sulfuricystis.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Sulfuricystis multivorans"
                     /db_xref="taxon:2211108"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54490
     Region          3..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mpltigvpre ttpgekrvat vpevveklik lgfavaiehd agaaanfsda ayqaagaqvl
       61 pdaaslwaaa divfkvrpps laeiasmkeg atligfiwpa qnpqlmetla akkatvlald
      121 clprqlsraq kmdaltsmas iagyraviea anafgrffag qvtaagkipp akvfiagagv
      181 aglaaigtaa nlgaivrand trsevadqvk slggefvkvd yeeegagagg yakemsegfk
      241 aaqramyare vkdadivitt alipgkpapk litaemvqtm rpgsvivdma aeqggncelt
      301 vpgeavvrhg vtiigytdlp srlsrqastl yatnllrlae elcknkdgti dvnfdddair
      361 gltvikngei twpapppklp aaapkpapas apkpaaaghg aggpmagktl ailfaigavl
      421 fgligafapa sflshftvfv lacfvgymvi wnvtpslhtp lmsvtnaiss iiaigaliqi
      481 appesgladr pdalirglaf vavllvainm fggfavtrrm lamfrk
//
LOCUS       WP_126446993             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nonlabens ponticola].
ACCESSION   WP_126446993
VERSION     WP_126446993.1
KEYWORDS    RefSeq.
SOURCE      Nonlabens ponticola
  ORGANISM  Nonlabens ponticola
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Nonlabens.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Nonlabens ponticola"
                     /db_xref="taxon:2496866"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34991
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 madtierikc liigsgpagy taaiyaarad mkpvmytgme pggqltttte vdnfpgypdg
       61 idgpammedl kkqaerfgte vrfgmatevd faseeggihk vvidgkttve antviistga
      121 sakylglpse qrlrgggvsa cavcdgffyk gqdvaivgag dtaaeeasyl akicksvtml
      181 vrkdymkask amqhrvnsld nitvmyntev devlgdqvve glrmvnnqtn ekteieitgi
      241 fiaighkpnt difkgqldmg edgylktipg stktnlpgvf asgdvqdkiy rqaitaagtg
      301 cmaaldaery laeigvveem tagdyyve
//
LOCUS       WP_126455211             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sulfuriflexus mobilis].
ACCESSION   WP_126455211
VERSION     WP_126455211.1
KEYWORDS    RefSeq.
SOURCE      Sulfuriflexus mobilis
  ORGANISM  Sulfuriflexus mobilis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Granulosicoccaceae; Sulfuriflexus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Sulfuriflexus mobilis"
                     /db_xref="taxon:1811807"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34313
     Region          1..320
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mndvkhcrll ilgsgpagyt aavyaaranl spvmvtglqq ggqlmtttdv dnwpgdqagv
       61 qgpqlmermr ehaerfntei lfdhinkvdl nsrpfqlsgd sgqytcdalv iatgasamyl
      121 gldseeafkg rgvsacatcd gffykgrkva vigggntave ealylaniae hvtvvhrrds
      181 frsekiladq lieksktgnv siewnhqlde vlgddsgvtg lrlkntqdds tkdidvhgvf
      241 iaighkpnta lfdgqldmeh gylsvkggsq gnatqtsieg vfaagdvadh iyrqaitsag
      301 sgcmaaldae ryldnlergg k
//
LOCUS       WP_126466506             303 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus periodonticum].
ACCESSION   WP_126466506
VERSION     WP_126466506.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus periodonticum
  ORGANISM  Streptococcus periodonticum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Streptococcus periodonticum"
                     /db_xref="taxon:2490633"
     gene            1..303
                     /gene="trxB"
     Protein         1..303
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33044
     Region          2..301
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigag pagmtaalya arsnlkvall ergipggqmn ntsdienypg yanisgpela
       61 ekmfeplenl gvehlfgsve kiehqgaikk vftedevlet ktliiatgaf hrhlgvpgee
      121 elnsrgvsyc avcdgaffrd edllvvgggd saveeavflt rfaktvtiih rrdelraqkl
      181 lqerafanek ihfiwdsvvk eikgdkrvss vmvenvktge isehefggvf iyvgldpvse
      241 fakdlgitne agwivtdnhm ktaisgiyai gdvrekdlrq vttavgdgav agqevykyit
      301 enf
//
LOCUS       WP_126456237             314 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Flavobacterium].
ACCESSION   WP_126456237
VERSION     WP_126456237.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium
  ORGANISM  Flavobacterium
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Flavobacterium"
                     /db_xref="taxon:237"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33847
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaaran mnpilyqgmq pggqltttne venwpgnpeg
       61 itgpemmvgl qaqaqrfgtd vrdgwatkvd fsgdihkvwi ndtielhcet viistgatak
      121 ylgmpseqhy lkmgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rsekfraski meervrkten itilmnhdtv evlgdeqvvt gvkalnkttn evfdipatgf
      241 fvaighkpnt difkdfisld etgyiintpg tsktnvegvf vagdaadhvy rqaitaagtg
      301 cmaaldaery laak
//
LOCUS       WP_126461425             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium sp. LS1R10].
ACCESSION   WP_126461425
VERSION     WP_126461425.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. LS1R10
  ORGANISM  Flavobacterium sp. LS1R10
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Flavobacterium sp. LS1R10"
                     /db_xref="taxon:2497482"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33789
     Region          9..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaaran mnpilyqgmq pggqltttne venwpgnpeg
       61 itgpemmvgl qaqaqrfgtd vrdgwatkvd fsgdihkvwi ndtielhcet viistgatak
      121 ylgmpseqhy lkmgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rsekfraski meervrkten itilmnhdtv evlgdeqvvt gvkalnkttn evfdipatgf
      241 fvaighkpnt difkdfisld etgyiintpg tsktnvagvf vagdaadhvy rqaitaagtg
      301 cmaaldaery laak
//
LOCUS       WP_126461727             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sulfuritortus calidifontis].
ACCESSION   WP_126461727
VERSION     WP_126461727.1
KEYWORDS    RefSeq.
SOURCE      Sulfuritortus calidifontis
  ORGANISM  Sulfuritortus calidifontis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Nitrosomonadales; Thiobacillaceae; Sulfuritortus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Sulfuritortus calidifontis"
                     /db_xref="taxon:1914471"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33619
     Region          8..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mstkhaqlli lgsgpagyta aiyaaranlk pvvvtglqqg gqlmtttevd nwpadvngvq
       61 gpelmqrfqa haerfnteiv fdhihtaklt ekpftligds gtytcdalii atgasamylg
      121 leseqaymgr gvsgcatcdg ffyknqevav igggntavee aiylaniask vtlvhrrdvf
      181 kaekimvehl mekvkegkia lelnsvldev lgdkngvtgm rlknvqtnat keialagifi
      241 aighkpntdl ftgqlemdhg yivtqggrlg fatqtsipgv faagdvqdmi ykqaitsaas
      301 gcqaaldaer flegka
//
LOCUS       WP_126465759             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aedoeadaptatus ivorii].
ACCESSION   WP_126465759
VERSION     WP_126465759.1
KEYWORDS    RefSeq.
SOURCE      Aedoeadaptatus ivorii (Peptoniphilus ivorii)
  ORGANISM  Aedoeadaptatus ivorii
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Aedoeadaptatus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Aedoeadaptatus ivorii"
                     /db_xref="taxon:54006"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32966
     Region          2..300
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydviivggg pagltaaiyc granlktlvl epeleggqma mtmeianypg aneddtgmdl
       61 amrmgkqart fgaefarasv esltldgedk vlattdgeyr araviaatgs rphtlgipge
      121 ekfvsrgisy catcdgafyq tgdvyviggg nsaveealyl sglgakvhiv hrrdqlraea
      181 yladlalkde nieilwntel kevigdvtad glvlynnked ksytvkkddk plgifiyvga
      241 rprtefladv leldngyvpv daeqrtavpg lfaagdivak kfrqvinacg egctaamava
      301 ldhvreqk
//
LOCUS       WP_126473430             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            gossypii].
ACCESSION   WP_126473430
VERSION     WP_126473430.1
KEYWORDS    RefSeq.
SOURCE      Variovorax gossypii
  ORGANISM  Variovorax gossypii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax gossypii"
                     /db_xref="taxon:1679495"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38620
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaetl agetrvavtp etvkklvasg htvrvqsgag vaasvtdsay qaagaeitdq
       61 pgafsadmvl kvrtpteset sllksgavvi gmlnpfdaag lqrlaaagvt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf idvpyetqee kdaaegvggy arpmpaswlt
      241 rqqaevakrv aladvvista lipgraaptl itedmvkamk pgsvivdiaa gkgpdgvggn
      301 cplseadrtv vkhgvtivge tnlaalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvtqd gqvtkk
//
LOCUS       WP_126474462             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_126474462
VERSION     WP_126474462.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33371
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh ffilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_126483898             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Halomonas nitroreducens].
ACCESSION   WP_126483898
VERSION     WP_126483898.1
KEYWORDS    RefSeq.
SOURCE      Halomonas nitroreducens
  ORGANISM  Halomonas nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Halomonas nitroreducens"
                     /db_xref="taxon:447425"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33771
     Region          9..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msearherli ilgsgpagyt aavyaaranl kpllitgmqa ggqlttttdv dnwpgddigv
       61 qgpelmermk rhaerfdtev lfdhihevel rdkpftlkgd ngtytcdali iatgasaryl
      121 gleseqkfmg qgvsacatcd gffyrnqevv vvgggntave ealylsniaa kvtlvhrrds
      181 lraekilqdk lfekaqngnv eliwnhtlde vlgdstgvtg arlkstqdgs treldapgvf
      241 iaighspntg ifegqldmag gyirvksgle gnatatsvpg vfaagdvmdh vyrqavtsag
      301 sgcmaaldae ryldel
//
LOCUS       WP_126474945             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_126474945
VERSION     WP_126474945.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33734
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt vavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_126485150             387 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            nitroreducens].
ACCESSION   WP_126485150
VERSION     WP_126485150.1
KEYWORDS    RefSeq.
SOURCE      Halomonas nitroreducens
  ORGANISM  Halomonas nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Halomonas nitroreducens"
                     /db_xref="taxon:447425"
     Protein         1..387
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40814
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlsvmrerh pgearvavtp tnvsaltgrg cqvfvetgag daagfpnasy reagaeilet
       61 raqlldkgei ilcvdashee gladlreghv ciglmdplsh sdrfsdlarr gittlalelv
      121 prisraqsmd alssiatlag ykavllaaaq aprifpmmmt aagtlnpsrv fimgagvagl
      181 qaaatakrlg avveaydvrp aareqilsvg akpveldldt saaegqggya seqddafldr
      241 qraqmgavla qqdvvittaa ipgaeapvli teemvkgmka gavivdlaae rggncaltqp
      301 gevisvygvt iigprnlvat lphhasqmyg rnlenllrhl lddqgglhld fedeildetv
      361 vthagqvrat rirkrlsfpv kaseeva
//
LOCUS       WP_126486928             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Halomonas
            nitroreducens].
ACCESSION   WP_126486928
VERSION     WP_126486928.1
KEYWORDS    RefSeq.
SOURCE      Halomonas nitroreducens
  ORGANISM  Halomonas nitroreducens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Halomonas.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Halomonas nitroreducens"
                     /db_xref="taxon:447425"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55225
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkera sgearvaltp esaqqiqklg heclveagag kaagfddaay rdagvtvidg
       61 aealwqaadv vikvrepsee etgylrkgqt lisffwpaqn etlleqcrdk gasviamdmv
      121 prisraqkmd alsstaniag yravieagnq fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg avvrafdvrp evaeqiesmg aeflfldfed sqdgsesggy aapsspefre
      241 kqlalfreqa pdvdivitta lipgrpapkl wledmvkamk pgsvivdlaa ekggncdltv
      301 pdqrivtdng vvvvgytdfp srmatqasll yatnirhmlt dltpekdgtl dhnmdddvir
      361 gatvahegei tfpppppkvq aiaaakpkpk ekeptpeekk aaehtafvaq tkrqatllgv
      421 ggalmlllgq vapasfmqhf ivfalacfvg fqviwgvshs lhtplmavtn aisgiivlga
      481 vlqigsgsal vgllaaisvl iatinivggf qvtrrmlamf qks
//
LOCUS       WP_126500799             348 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Rothia].
ACCESSION   WP_126500799
VERSION     WP_126500799.1
KEYWORDS    RefSeq.
SOURCE      Rothia
  ORGANISM  Rothia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Rothia"
                     /db_xref="taxon:32207"
     gene            1..348
                     /gene="trxB"
     Protein         1..348
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36689
     Region          44..347
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntntttggl fgnaalggvr lgaastkpeg astsaaeqge qtvhnviivg agpagytaai
       61 yaaranlspv lfassvspgg almntteven fpgfiegiqg pelmtnigaq aerfgtdiry
      121 qdvekldltg evkkviladg svhlaktvil stgseyrklg vegedrlsgy gvswcatcdg
      181 fffkekdiav vgggdsalee alflttfark vyiihrrdsf rasdimqkra fenpkievlw
      241 dsevsaidgd snlekvtlkn tkdgserelp lnglfiaigs dprvdmvkdq ltlseqgtie
      301 vqgrssktsv pgvfaagdvi dptyrqaiia agsgavaald aqhyienm
//
LOCUS       WP_126503094             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            atlantica].
ACCESSION   WP_126503094
VERSION     WP_126503094.1
KEYWORDS    RefSeq.
SOURCE      Shewanella atlantica
  ORGANISM  Shewanella atlantica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Shewanella atlantica"
                     /db_xref="taxon:271099"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54221
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipreil aqesrvaatp atviqlkklg fsvvvqsgag eaanfkdeay qeagaevvsl
       61 eqafqadlvl kvnapginad tgvdetdlmk agstvasfvw paqnpellek fkakginlla
      121 mdmvprisra qsldarssla nvdgyravie aanhfgrfft gqitaagkvp pakvliigag
      181 vaglsalgaa gslgaivraf dtrpevkeqi nsmgaeflel dfeeesgsgd gyakvmskef
      241 idaemalfre qakdvdiiit talipgkpap kliledmvgl mkpgsvivdl aaanggncel
      301 tvpgevavvn dvtiigytel srrlptqasq lygtnlvnll klmvpekdgn yeinfddevi
      361 rgvaavkdge itfpppaiqv saqpqakaee apvevvekkk npwikpaiat vaaglfglva
      421 ssapadflqh fsifvlscvv gyyvvwnvsh slhtplmsvt naisgiivvg alvqmnsdst
      481 avlvlsgiai liasiniagg ftvtqrmlkm frkd
//
LOCUS       WP_126504510             466 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella atlantica].
ACCESSION   WP_126504510
VERSION     WP_126504510.1
KEYWORDS    RefSeq.
SOURCE      Shewanella atlantica
  ORGANISM  Shewanella atlantica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Shewanella atlantica"
                     /db_xref="taxon:271099"
     gene            1..466
                     /gene="nrfA"
     Protein         1..466
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52162
     Region          1..466
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvrnltkksf alsalvaasl masgvmasdk teprneeykd kfskqynswh dtaeskevvd
       61 mleevpslvv lwagygfakd ynaprghmya vtdvrntlrt gapkaatdgp mpmacwscks
      121 pdvprvieeq gedgyftgkw ykggaeivnt igcgdchekg ksklrvsrpf aerafetldt
      181 pfakaskkdk qsmvcaqchv eyyfektkdk kgfvkfpwdq gvtveamety ydnlefkdwt
      241 hkvsktpmlk aqhpgyetwk lgvhgknnvs ctdchmpkvk nekgrkytdh kvgnpfdrfe
      301 etcgtcheqs kefmvnlthe rkvkvadlka rvesqlvkah feakaawdag ateaemkpil
      361 tdirhsqwrw dyatashgva ahapdealrv lgtsvdkaad arvklaqlla akgvkqpiay
      421 pdtstkakaq aalgmdmkkl nsdkadfkkn tlpkwdaeak kreaty
//
LOCUS       WP_126505166             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Shewanella atlantica].
ACCESSION   WP_126505166
VERSION     WP_126505166.1
KEYWORDS    RefSeq.
SOURCE      Shewanella atlantica
  ORGANISM  Shewanella atlantica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Shewanella atlantica"
                     /db_xref="taxon:271099"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34019
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msqarhcell ilgsgpagyt aavyaaranl kpvlvtglqq ggqlttttev enwpgdaddl
       61 tgpalmermq khaekfetei ifdhinevdl kvrpfklkgd ngdftcdsli istgasamyl
      121 gleseeafkg kgvsacatcd gffyrnqkva vigggntave ealylsnias evhlihrrda
      181 frsekiltkr lmdkvengni ilhldntlde vvgdqmgvtg lkmkstkdgs itdlevmgvf
      241 vaighkpntq mfegqlemnn gyikvqsgld gnatqasieg vfaagdvmdq hyrqaitsag
      301 tgcmaaldae ryldsk
//
LOCUS       WP_126510496             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus warneri].
ACCESSION   WP_126510496
VERSION     WP_126510496.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus warneri
  ORGANISM  Staphylococcus warneri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Staphylococcus warneri"
                     /db_xref="taxon:1292"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33530
     Region          6..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtevdfdvai igagpagmta avyasranln tvmiergmpg gqmanteeve nfpgfemitg
       61 pdlstkmfeh akkfgatyqy gdiksiedkg dykvvnvgnk eitahaviis tgaeykkigv
      121 pgeqelggrg vsycavcdga ffknkrlfvi gggdsaveeg tfltkfadkv tivhrrdqlr
      181 aqsilqdraf kndkidfiws htlktindkd gkvgsvtles tkdgsevtyd adgvfiyigm
      241 kpltapftdl gitnengyiv teadmstnvp giyaagdvrd kglrqivtat gdgsiaaqsa
      301 adyieaikdk lea
//
LOCUS       WP_126512481             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gemella haemolysans].
ACCESSION   WP_126512481
VERSION     WP_126512481.1
KEYWORDS    RefSeq.
SOURCE      Gemella haemolysans
  ORGANISM  Gemella haemolysans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Gemellaceae;
            Gemella.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Gemella haemolysans"
                     /db_xref="taxon:1379"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33829
     Region          5..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msrnydviii gsgpaglsaa lyasraklnv lvlekskngg qaaithmien ypgaiedptg
       61 prltarmaeq aknfgtefkq eevlnveleg dekvvtctsg dytakavvia tgasprkldi
      121 pgvreleskg isycatcdgd ffdglevfvv gggnsaveea lfltkfarkv tiihfeedih
      181 ceritaekar nhpqieirte tvvleaigdg ileaiklknv atgeeyvvea deedgtmglf
      241 ffigyvpqtk lfegkvelte ggyikagedt ktnvegvfva gdcrqkeirq vvtavcdgav
      301 aaitaekyia ekfe
//
LOCUS       WP_126513677             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Haemophilus influenzae].
ACCESSION   WP_126513677
VERSION     WP_126513677.1
KEYWORDS    RefSeq.
SOURCE      Haemophilus influenzae
  ORGANISM  Haemophilus influenzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Haemophilus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Haemophilus influenzae"
                     /db_xref="taxon:727"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34325
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtkhakll ilgsgpagyt aaiyaaranl kpvlvtglqq ggqltttdei enwpgdfemt
       61 tgsglmqrml qhaekfetei vfdhinrvdl ssrpfklfgd vqnftcdali iatgasaryi
      121 glpseenykg rgvsacatcd gffyrnkpvg vigggntave evlylanias tvhlihrrds
      181 fraekilidr lykkveegki vlhtdrtlde vlgdnmgvtg lrltdtktge keelkldglf
      241 vaighspnte ifqgqlelnn gyivvksgle gnatatsveg vfaagdvmdh nyrqaitsag
      301 tgcmaaldae ryldaqea
//
LOCUS       WP_126518386             466 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Shewanella canadensis].
ACCESSION   WP_126518386
VERSION     WP_126518386.1
KEYWORDS    RefSeq.
SOURCE      Shewanella canadensis
  ORGANISM  Shewanella canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Shewanella canadensis"
                     /db_xref="taxon:271096"
     gene            1..466
                     /gene="nrfA"
     Protein         1..466
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52169
     Region          1..466
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mvrnltkksf alsalvaasl masgvmasdk teprneeykd kfskqynswh dtaeskevvd
       61 mleevpslvv lwagygfakd ynaprghmya vtdvrntlrt gapkaatdgp mpmacwscks
      121 pdvprvieeq gedgyftgkw ykggaeivnt igcgdchekg ksklrvsrpf aerafetldt
      181 pfakaskkdk qsmvcaqchv eyyfektkdk kgfvkfpwdq gvtveamesy ydnlefkdwt
      241 hkvsktpmlk aqhpgyetwk lgvhgknnvs ctdchmpkvk nekgrkytdh kvgnpfdrfe
      301 etcgtcheqs kefmvnltke rkvkvadlka raesqlvkah feakaawdag ateaemkpil
      361 tdirhsqwrw dyatashgva ahapdealrv lgtsvdkaad ariklaqlla vkgvkqpiay
      421 pdtstkakaq aalgmdmkkm nadkadfkkn tlpkweaeak kreaty
//
LOCUS       WP_126521337             514 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shewanella
            canadensis].
ACCESSION   WP_126521337
VERSION     WP_126521337.1
KEYWORDS    RefSeq.
SOURCE      Shewanella canadensis
  ORGANISM  Shewanella canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Shewanella canadensis"
                     /db_xref="taxon:271096"
     Protein         1..514
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54223
     Region          1..513
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipreil aqesrvaatp atviqlkklg fsvvvqsgag eaanfkdeay qeagaevvsl
       61 eqafqadlil kvnapginad tgvdeadlmk agstvasfvw paqnpellek fkakginlla
      121 mdmvprisra qsldarssla nvdgyravie aanhfgrfft gqitaagkvp pakvliigag
      181 vaglsalgaa gslgaivraf dtrpevkeqi nsmgaeflel dfeeesgsgd gyakvmskef
      241 idaemalfre qakdvdiiit talipgkpap kliledmvgl mkpgsvivdl aaanggncel
      301 tvpgevavvn nvtiigytel srrlptqasq lygtnlvnll klmvpekdgn yeinfddevi
      361 rgvaavkdge itfpppaiqv saqpqakaae aavevvekkk npwvkpfiat vaaglfglia
      421 nsapadflqh fsifvlscvv gyyvvwnvsh slhtplmsvt naisgiivvg alvqmnsdst
      481 avlvlsgiai liasiniagg ftvtqrmlkm frkd
//
LOCUS       WP_126521522             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Shewanella canadensis].
ACCESSION   WP_126521522
VERSION     WP_126521522.1
KEYWORDS    RefSeq.
SOURCE      Shewanella canadensis
  ORGANISM  Shewanella canadensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Shewanella canadensis"
                     /db_xref="taxon:271096"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33960
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msqarhcell ilgsgpagyt aavyaaranl kpvlvtglqq ggqlttttev enwpgdaddl
       61 tgpalmermq khaekfetei lfdhinevdl kvrpfklkgd ngeftcdali istgasamyl
      121 gleseeafkg kgvsacatcd gffyrnqkva vigggntave ealylsnias evhlihrrda
      181 frsekiltkr lmdkvengni ilhldntlde vvgdamgvtg lkmkstkdgs itdlevmgvf
      241 vaighkpntq mfegqlemnn gyikvqsgld gnatqasieg vfaagdvmdq hyrqaitsag
      301 tgcmaaldae ryldsk
//
LOCUS       WP_126524319             303 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [Salmonella].
ACCESSION   WP_126524319
VERSION     WP_126524319.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..303
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35987
     Region          5..167
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mhtfrpyslr hsdllyedip leireqilll iintlgncss fydmtlycyh nshsdevyrr
       61 icktlrkeyg lftlyahsts yldemsnlll ktddkrkhid tielafnyid tylrtyevtl
      121 glepdkaise lnnifhehsl kyryengriv rlrrikrlkn icyylyspge ygfveydlme
      181 aynrlilndf acvvrechaa frsvilrihe rkgivyheqd slntlmtnlm argvisaeyv
      241 hkfhflsdvl eseiflpmaq ekshhhyamm lriseelacs iyyltersif fltqraeeds
      301 vap
//
LOCUS       WP_126529181             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_126529181
VERSION     WP_126529181.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33687
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmthmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_126538966             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Oharaeibacter diazotrophicus].
ACCESSION   WP_126538966
VERSION     WP_126538966.1
KEYWORDS    RefSeq.
SOURCE      Oharaeibacter diazotrophicus
  ORGANISM  Oharaeibacter diazotrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Oharaeibacter.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Oharaeibacter diazotrophicus"
                     /db_xref="taxon:1920512"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34157
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mahhrskvli vgsgpagyta aiyaaramle pilvsglqqg gqltittdve nypgfaepiq
       61 gpwlmdqmra qaehmgtrlv adhvvkaeia gggpfrlvgd sgdtyagdal ivatgaqarw
      121 lglpseetfk gfgvsacatc dgffyrgkhv lvvgggntav eealylthha akvtlihrrd
      181 hfraervmqq rlfdnpkiev iwntaldevl gtrgfppsvn garlrnvatg atseiavdgi
      241 fvaighapav elfkdqlrlk psgylwtepg strtsvpgvf aagdvadevf rqavtaagmg
      301 cmaaleaerw laetafreaa e
//
LOCUS       WP_126538098             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aerosticca soli].
ACCESSION   WP_126538098
VERSION     WP_126538098.1
KEYWORDS    RefSeq.
SOURCE      Aerosticca soli
  ORGANISM  Aerosticca soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Aerosticca.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Aerosticca soli"
                     /db_xref="taxon:2010829"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34214
     Region          9..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpnakhsrll ilgsgpagyt aaiyaaranl aptlitglqq ggqlttttev dnwpgdvegv
       61 qgpalmqrma ehaerfhtkm vfdhihrvdl tqrpfhlkgd ageytcdali vatgatakyl
      121 giaseekfkg rgvsacatcd gfffreqdvv vvgggntave ealylsniar kvylvhrrdk
      181 lraekimqdk lfekaaagki elvwnhtvee vlgddsgvtg vrvksvddgv lrdidatgff
      241 vaightpntg ifegqldmre gyikvrsgqn gmatmtsvpg vfaagdvadh vyrqaitsag
      301 fgcmaaldae rwleqagal
//
LOCUS       WP_126548911             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Dictyobacter kobayashii].
ACCESSION   WP_126548911
VERSION     WP_126548911.1
KEYWORDS    RefSeq.
SOURCE      Dictyobacter kobayashii
  ORGANISM  Dictyobacter kobayashii
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Dictyobacteraceae; Dictyobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Dictyobacter kobayashii"
                     /db_xref="taxon:2014872"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34134
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 makiygviii gsgpagytaa iyaarsnlsv lmlqgyaagg qlmltseven fpgfeagilg
       61 peimekfegq arrfgaemlp edvtavdfsk rpftvttdmg eyqarsivia tgasakwlgl
      121 psekllqgrg vtacatcdgf ffknrdvivi gggdtameea tfltryashv tivhrrdsfr
      181 askimqdrat knpkisfmmd sevievlged avtgvrirnt ktgeeskfdt qgvflaighq
      241 pntalfkgii dldeagyiip seytmtnipg vfaagdvtdh ryrqaitaag dgcraaidle
      301 rwlaeqgedv gvenwn
//
LOCUS       WP_126565121             313 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Staphylococcus].
ACCESSION   WP_126565121
VERSION     WP_126565121.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus
  ORGANISM  Staphylococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Staphylococcus"
                     /db_xref="taxon:1279"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33624
     Region          6..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtevnydvai igagpagmta avyasranls tvmiergmpg gqmanteeve nfpgfemitg
       61 pdlstkmfeh akkfgaeyqy gdiksiedkg dykvinlgnk eitahaviis tgaeykkigv
      121 pgeqelggrg vsycavcdga ffknknlfvi gggdsaveeg afltkfadkv tivhrrdelr
      181 aqkilqdraf kndkidfiws htlksinekd gkvgsvtlvs tkdaseqtld adgvfiyigm
      241 kplttpfnnl gitndmgyiv tkddmttsvp gifaagdvrd kglrqivtat gdgsiaaqsa
      301 idyieelkdk aea
//
LOCUS       WP_126540941             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Oharaeibacter diazotrophicus].
ACCESSION   WP_126540941
VERSION     WP_126540941.1
KEYWORDS    RefSeq.
SOURCE      Oharaeibacter diazotrophicus
  ORGANISM  Oharaeibacter diazotrophicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Pleomorphomonadaceae; Oharaeibacter.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Oharaeibacter diazotrophicus"
                     /db_xref="taxon:1920512"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38993
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlresa adegrvaatp dtvkrliglg aavsvetgag tlsripdady aaagatvapt
       61 aaeaateadv vllvrrpead rlalvkrgal vvatmdpygh qdavkamada gvtavamefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydrampmmmt aagtvpaarv fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedee fkqaetaagy akpmsaeyqa
      241 kqaalvaehi kkqdivitta lipgraaprl vtaamvasmk pgsvlvdlav erggnvegsv
      301 pgeivtvgdg vrivghrnvp griaatasql yaknlfafve tlidkkekkl avnwddelvk
      361 atvltrdgav vhpafqs
//
LOCUS       WP_126566076             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_126566076
VERSION     WP_126566076.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33318
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafv gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_126573535             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vibrio aquaticus].
ACCESSION   WP_126573535
VERSION     WP_126573535.1
KEYWORDS    RefSeq.
SOURCE      Vibrio aquaticus
  ORGANISM  Vibrio aquaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Vibrio aquaticus"
                     /db_xref="taxon:2496559"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34518
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdvkhsnll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttev enwpgdaegl
       61 tgpalmermk ehaerfetei lfdhinevdf sqrpfrlkgd sseytcdali istgasakyl
      121 gleseeafkg rgvsacatcd gffyrnqkva vvgggntave ealylsnias evhlihrrdt
      181 fraekilvkr lmdkvengni vlhtdrtlee vvgddmgvtg vrikdtqsds ieqidvmgaf
      241 iaighqpnta mfegqlemkd gyiivrsgle gnatqtsipg ifaagdvmdh nyrqaitsag
      301 tgcmaaldae ryldaladnk
//
LOCUS       WP_126574754             476 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Vibrio
            aquaticus].
ACCESSION   WP_126574754
VERSION     WP_126574754.1
KEYWORDS    RefSeq.
SOURCE      Vibrio aquaticus
  ORGANISM  Vibrio aquaticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Vibrio aquaticus"
                     /db_xref="taxon:2496559"
     gene            1..476
                     /gene="nrfA"
     Protein         1..476
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53249
     Region          3..476
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mnklrwipks aaalaivass llsftsvaas enkalidprn dayeqqhpdq yhswkatses
       61 ehledalaed pnmvilwagy gfakdynkar ghfyavddvr qtlrtgapqd etsgpmpmac
      121 wsckspdvgr iidergedgy fegkwarlge qvvnpigcad chdtrsegfk ngepalalak
      181 pyverafeai dkpfeqqsrl dqqasvcgqc hveyyfvkse knavkfpwdr gttvddmeey
      241 ydalgfkdwt hkvskapmlk aqhpgyetwr dgihgknkva cvdchmpkvt kedgtvytdh
      301 kvgnpfdrfe dtcaschtqs keqmqeivst rkaqvlnmkl taekqivaah feagaawdag
      361 atetemkdil qdirhaqwrw dyaiashgvh mhapevalev lgtavdraad artklvrlla
      421 kkgitdpvel pdistkaaaq qalgmdmekm nadkenflkt vvpdwdkaae eresqy
//
LOCUS       WP_126579574             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tengunoibacter tsumagoiensis].
ACCESSION   WP_126579574
VERSION     WP_126579574.1
KEYWORDS    RefSeq.
SOURCE      Tengunoibacter tsumagoiensis
  ORGANISM  Tengunoibacter tsumagoiensis
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Dictyobacteraceae; Tengunoibacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Tengunoibacter tsumagoiensis"
                     /db_xref="taxon:2014871"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34495
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mekvygviii gsgpagytaa iyagrsnlsv lvlqgyetgg qlmqtseven fpgfeegimg
       61 pemmekfekq alrfgaelip edvtsvdftq rpfvvrtdsa eyrsqaviia tgasaqwlgl
      121 pnetrlkgrg vtacatcdgf ffkgkdvvvi gggdtameea tfltryvnhv tlihrrdtfr
      181 askimqdral nnpkidalme sevvdvvgda aitavrvrnt rtgeestlet qglflaighr
      241 pntelfkgii dmdetgyiip kehtmtnipg vfvagdvsdh ryrqaitaag egcraaidle
      301 rwlesqgeev gienwn
//
LOCUS       WP_126585928             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_126585928
VERSION     WP_126585928.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38707
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag ikasivdsay etagatigsa
       61 sdafgaelil kvvapsdsel tliksgtvlv gmlnpfsnet iaklaeqgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmptswmq
      241 rqalavhera kqadivitta lipgrkaptl lsadtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv iicgptnlag avaadasaly arnlldflkl vfnkegkfei nleddivaac
      361 lmcrdgqvir kna
//
LOCUS       WP_126588002             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_126588002
VERSION     WP_126588002.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38604
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivgysnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_126588146             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas veronii].
ACCESSION   WP_126588146
VERSION     WP_126588146.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas veronii
  ORGANISM  Pseudomonas veronii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas veronii"
                     /db_xref="taxon:76761"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38620
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhiavpletq tgetrvaatp etikklisqg hkvtvqsgag vnasvvdsay eaagatigsa
       61 ndafgaelil kvvapsdsel tliksgtvvv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahyypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlaa avgadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_126594826             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Dictyobacter aurantiacus].
ACCESSION   WP_126594826
VERSION     WP_126594826.1
KEYWORDS    RefSeq.
SOURCE      Dictyobacter aurantiacus
  ORGANISM  Dictyobacter aurantiacus
            Bacteria; Bacillati; Chloroflexota; Ktedonobacteria;
            Ktedonobacterales; Dictyobacteraceae; Dictyobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Dictyobacter aurantiacus"
                     /db_xref="taxon:1936993"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34144
     Region          7..303
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 makiygviii gsgpagytaa iyaarsnlsv lmlqgysagg qlmltseven fpgfetgilg
       61 pemmekfeaq asrfgaellp edvtsvdfsk rpftvttdmg qyqarsivia tgasakwlgl
      121 psekrlqgrg vtacatcdgf ffknrdvivi gggdtameea tfltryvnhv tivhrrdsfr
      181 askimqdraa knpkisflmd sevtevlged avtgvrirnt ktgaettlet qglflaighq
      241 pntelfkgii dldeagyiip seftmtnipg vfaagdvtdh ryrqaitaag dgcraaidle
      301 rwlaeqgedv gvenwd
//
LOCUS       WP_126598169             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinobacillus delphinicola].
ACCESSION   WP_126598169
VERSION     WP_126598169.1
KEYWORDS    RefSeq.
SOURCE      Actinobacillus delphinicola
  ORGANISM  Actinobacillus delphinicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pasteurellales; Pasteurellaceae; Actinobacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Actinobacillus delphinicola"
                     /db_xref="taxon:51161"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34190
     Region          3..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mntkhcqlli lgsgpagyta aiyaaranlh pvmvtgmqqg gqltttdeie nwpgdfektt
       61 gqglmermlk haekfdteii fdqiksvdfs srpfklfgem qnftcdalii atgasarylg
      121 leseekykgr gvsacatcdg ffyrnkpvav igggnsavee alylaniasv vhlvhrrhef
      181 rsekillsrl dqkvsegkiv ihtpytlqev lgddmgvtgi riqnmendtq eeinidglfv
      241 aightpntai fdgqlelnng yivvksglng datatsvegi faagdvmdhi yrqaitsagt
      301 gcmaaldaer fldkl
//
LOCUS       WP_126603609             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bartonella vinsonii].
ACCESSION   WP_126603609
VERSION     WP_126603609.1
KEYWORDS    RefSeq.
SOURCE      Bartonella vinsonii
  ORGANISM  Bartonella vinsonii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Bartonella vinsonii"
                     /db_xref="taxon:33047"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34022
     Region          8..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvqshirlli igsgpagyta aiyaaramlk pvlvtgmqqg gqltittdve nypgfadsiq
       61 gpwlmeqmak qaenmgtkiv ydtitkaell kypfilhgdl gtqyccdali iatgakarwl
      121 gleseqtfmg ggvsacatcd gffyrdkdvi vvgggntave ealylshlak svsvvhrrdy
      181 fraekilqdr llardnvrvl wdhvveeivg lpaqdsrgai vtgarlknvk tgqemkvnae
      241 gifiaighdp avslfegqlk qktggylwta pdstatsisg vfaagdvade vfrqavtaag
      301 rgcmaaleae rfldlqa
//
LOCUS       WP_126609042             516 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Vibrio
            penaeicida].
ACCESSION   WP_126609042
VERSION     WP_126609042.1
KEYWORDS    RefSeq.
SOURCE      Vibrio penaeicida
  ORGANISM  Vibrio penaeicida
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Vibrio penaeicida"
                     /db_xref="taxon:104609"
     Protein         1..516
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54417
     Region          1..515
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigvpketl agerrvaatp ktveqllklg fdvsvesqag vlasfddtaf esagatvvsr
       61 dnvwksdlil kvnapqvdpe sgvdefdlik egaslisfiw paqnealmek lsskninvma
      121 mdavprisra qaldalssma niagyravve aahefgrfft gqitaagkvp pakvlvagag
      181 vaglaaigaa gslgaivraf dvrpevkeqv qsmgaeflev dfqensgsgd gyakemsdef
      241 nkkaeelyaa qakdvdiiit talipgrpap klitkamvds mkagsvivdl aaanggncey
      301 tvadevittp ngvkivgytd mvgrlptqss qlygtnlvnl lkllckekdg nidinfedvv
      361 lrgvtvvkeg eitwpappiq vsaqpevkpk aqpvetakee paspfkkvaa laigvgafaw
      421 vasvapasfl ahftvfvlac vvgyyvvwnv shslhtplms vtnaisgiiv vgallqigqg
      481 sgvvtflsfi avliasinif ggftvtkrml emfrkd
//
LOCUS       WP_126614863             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flammeovirga pectinis].
ACCESSION   WP_126614863
VERSION     WP_126614863.1
KEYWORDS    RefSeq.
SOURCE      Flammeovirga pectinis
  ORGANISM  Flammeovirga pectinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Flammeovirga.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Flammeovirga pectinis"
                     /db_xref="taxon:2494373"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33540
     Region          9..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 marehvktli igsgpagyta aiyasranls pvlyqgpqpg gqltitndve nfpgyakgvm
       61 gpqmmmelqe qagrfgtdir tgfvtgvqfn engphiatvn deieieadsv iistgasakw
      121 lglesetrln gsgvsacavc dgffyrgqev vvvgagdsaa eeahylsnlc skvhllvrrd
      181 emraskimqd rvikkdniei hwntdtlevl gesevegvkv lnnktneesv invtgffvai
      241 ghkpntdifk gqldmdkagy litkpdstkt nikgvfaagd vqdtiyrqav taagtgcmaa
      301 leaerylvel ed
//
LOCUS       WP_126619229             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum griseum].
ACCESSION   WP_126619229
VERSION     WP_126619229.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum griseum
  ORGANISM  Azospirillum griseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Azospirillum griseum"
                     /db_xref="taxon:2496639"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39652
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,102,299,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,135..136,145..146,149..150,153..154,156..157,
                     159..164,166,168..170,173,196..197,289..290,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,135,138,141,182..185,205..207,239,250,
                     267..269,276,278)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(132..133,135,145,188..189,196,212..213,215..218)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(165..169,172,175,198,200)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkvaipkerr agelrvaasp etvkklkglg ldvvvesgag lgsslpdaaf eaagatiaad
       61 aasalagadi vlkvqrplls gegsdgvdel allkkgallf ailnphnsrd hvkayaaagv
      121 nafamefmpr itraqvmdvl ssqanlagyk avvdaateyg rafpmmmtaa gtvpparafi
      181 mgvgvaglqa iatakrlgai vsatdvrpav keqvqslggs fvavendefk qaetaggyak
      241 emsddykrqq aalvaehikk qdivittali pgrkapilvt aehvasmkpg sviidlaveq
      301 ggnvegsklg etvvtangvk ivghanypsr iaesasllya knllalltal ndkekgitvn
      361 wddeivkaia ltrdgavihp afag
//
LOCUS       WP_126618127             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Flammeovirga pectinis].
ACCESSION   WP_126618127
VERSION     WP_126618127.1
KEYWORDS    RefSeq.
SOURCE      Flammeovirga pectinis
  ORGANISM  Flammeovirga pectinis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flammeovirgaceae; Flammeovirga.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Flammeovirga pectinis"
                     /db_xref="taxon:2494373"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41423
     Region          1..359
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(12,71,90,285,311,313)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(41,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,275..276,318..319,323,
                     326..327)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,225,236,
                     253..255,262,264)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mlfgilreed hrvsvtpela kkfiseghev yfekgagssa yfedslynei gaveksreei
       61 isssnvlitl aplskeevak laentflfss fqpfqdasic etfatkgisa fsfdmiprss
      121 iaqsmdilss masisgykav lkatdylpry mpmlstaagt vppskvlimg agvaglqaia
      181 takrlgaqve afdtraaske evqslgakfv evegasddtn aggyaveqse eykkkqaeli
      241 alkiekadvv ittaqlrgrp apkliteeav ktmkpgsviv dlasstggnc vltedekvvk
      301 khgvtiigss nlaaeiseqa svlfsknvqn ylklmltkeg lnfnfndeii lqscivykge
      361 viygneakqk alvpapkaee kadaqa
//
LOCUS       WP_126620621             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Azospirillum griseum].
ACCESSION   WP_126620621
VERSION     WP_126620621.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum griseum
  ORGANISM  Azospirillum griseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Azospirillum griseum"
                     /db_xref="taxon:2496639"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39694
     Region          1..375
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,102,299,326,328)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,135..136,145..146,149..150,153..154,156..157,
                     159..164,166,168..170,173,196..197,289..290,333..334,338,
                     341..342)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,135,138,141,182..185,205..207,239,250,
                     267..269,276,278)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(132..133,135,145,188..189,196,212..213,215..218)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(165..169,172,175,198,200)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiaiprerr agelrvaasp etvkklkglg ldvvvesgag lgsslpdaaf eaagatiaad
       61 aasalagadi vlkvqrplls gegsdgvdel allkkgallf ailnphnsrd hvkayaaagv
      121 nafamefmpr itraqvmdvl ssqanlagyk avvdaateyg rafpmmmtaa gtvpparafi
      181 mgvgvaglqa iatakrlgai vsatdvrpav keqvqslggs fvavendefk qaetaggyak
      241 emsddykrqq aalvaehikk qdivittali pgrkapilvt aehvasmkpg sviidlaveq
      301 ggnvegsklg etvvtangvk ivghanypsr iaesasllya knllalltal ndkekgitvn
      361 wddeivkaia ltrdgavihp afag
//
LOCUS       WP_126618176             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Azospirillum griseum].
ACCESSION   WP_126618176
VERSION     WP_126618176.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum griseum
  ORGANISM  Azospirillum griseum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Azospirillum griseum"
                     /db_xref="taxon:2496639"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34105
     Region          8..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpsthhskvl iigagpagyt aaiyaaranl eplmvqgmqp ggqlmittdv enfpgfadpi
       61 qgpwlmeqmq kqaehvgtkm vfdlitdvdf tqrpyvckgd sgdtytadsv iiatgaqarw
      121 lgisseeiyr gfgvsacatc dgfffrgkev avigggnsav eealyltnha tkvtiihrrd
      181 sfraerimqd rlfrhpkiev vwdsaveeiv gegdgslgnp rgvtgvrvkn vktgdsrvip
      241 vagvfvaigh epatsvfkgk vamdesgyil tapdstatdi pgvfaagdvk dkvyrqavta
      301 agmgcmaale aerwlahhe
//
LOCUS       WP_126633735             229 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein, partial [Pseudomonas aeruginosa].
ACCESSION   WP_126633735
VERSION     WP_126633735.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         <1..229
                     /product="STM4504/CBY_0614 family protein"
     Region          <9..89
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 wnphlvdifv depdversld vielvfrsan rqaenaeyyp gfdgrghvdd cieelntrfr
       61 ehgvgyayvn deiirvdsem mhtevvkpvv hflnvpgfeg aqeefftays hyrqglykea
      121 itaankafes tmkviceqkg weykkrdtas klimiciekg lfpgyyqshl sslfnllegg
      181 vpairnnegg hgqgvevktv ephivsytlh maasailllv nsatsmdsr
//
LOCUS       WP_126633340             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Shigella
            sonnei].
ACCESSION   WP_126633340
VERSION     WP_126633340.1
KEYWORDS    RefSeq.
SOURCE      Shigella sonnei
  ORGANISM  Shigella sonnei
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Shigella sonnei"
                     /db_xref="taxon:624"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53570
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdisikeka qqaiglnmeq inaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_126640265             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Embleya hyalina].
ACCESSION   WP_126640265
VERSION     WP_126640265.1
KEYWORDS    RefSeq.
SOURCE      Embleya hyalina
  ORGANISM  Embleya hyalina
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Embleya.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Embleya hyalina"
                     /db_xref="taxon:516124"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33135
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgptgytaa vyaaradlkp lvfegavtag galmntteve nfpgwpdgim
       61 gpdlmdnmrk qaerfgaelv pddivavdla gdvktvtdsa gtvhkaravi latgsayrkl
      121 slpnedalsg rgvswcatcd gfffrdqdia vvgggdsaie eatflsrfar svtvihrrde
      181 lraskamqhr afanekisfa wnsevaeirg dgklsgvglr dtvtgelrdl avtglfiavg
      241 hdprtelvrg qidlddegyi kvdapttrtn ltgvfaagdv vdhtyrqait aagtgcaaal
      301 daehylasla dgasa
//
LOCUS       WP_126669023             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Colwellia sp. Arc7-635].
ACCESSION   WP_126669023
VERSION     WP_126669023.1
KEYWORDS    RefSeq.
SOURCE      Colwellia sp. Arc7-635
  ORGANISM  Colwellia sp. Arc7-635
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Colwellia sp. Arc7-635"
                     /db_xref="taxon:2497879"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34201
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msearhcpll ilgsgpagyt aavyaaranl kpvmitgmqq ggqlttttev enwpgdaddl
       61 tgpalmdrmq khaekfdtei ifdhinevdf sekpyklkgd sgvytcdali ictgasaqyl
      121 glpseeafmg kgvsacatcd gffyknqkva vvgggntave ealylsnias evhlihrrdt
      181 frsekiltkr lmdkvangni vlhldrtlde vlgdnmgvtg vrikdmnsda teefdvmgvf
      241 iaighkpntd ifkdqlamkd gyltiqsgtn gnatqtsveg iyaagdvadh iyrqaitsag
      301 agcmaaldae ryldakgsh
//
LOCUS       WP_126660620             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lysinibacillus antri].
ACCESSION   WP_126660620
VERSION     WP_126660620.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus antri
  ORGANISM  Lysinibacillus antri
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Lysinibacillus antri"
                     /db_xref="taxon:2498145"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34078
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeekiydvv iigagpagmt aavyasranl stlmiergip ggqmanteev enypgfdsil
       61 gpelstkmfe hakkfgaeyv ygdvaevidg eeyktikags keyktrtiii ttgaeykkmg
      121 vpgekelggr gvsycavcdg affkqknlvv vgggdsavee gvyltrfadk vtivhrrdkl
      181 raqkilqdra fanekvdfiw nhtvkeinek dgkvgsvtlv stvdgseqef tadgvfvyig
      241 ldpltkpfsn lgilnehgyi vtndkmetsv kgifaagdvr ekmlrqivta tgdgsiaaqs
      301 aqhyveelmd kisq
//
LOCUS       WP_126669252             512 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Colwellia
            sp. Arc7-635].
ACCESSION   WP_126669252
VERSION     WP_126669252.1
KEYWORDS    RefSeq.
SOURCE      Colwellia sp. Arc7-635
  ORGANISM  Colwellia sp. Arc7-635
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Colwellia sp. Arc7-635"
                     /db_xref="taxon:2497879"
     Protein         1..512
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54157
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigipketl sgenrvasap tavaallklg fevqvqkgcg tkasftdnef vdagasvvtk
       61 knvwqsdiif kvnpptieei aamkdgayli gfiapaqned vltalkdkni ttlamemvpr
      121 mtrsqsmdal ssmgniagyr avieathhfg rfltgqitaa gkmppakvmi igagvaglaa
      181 igtagslgai vrafdtrpev keqiesmgae fleldyeepe dtgsgdgyak emskafidae
      241 malfaeqakd vdiiittami pgkpapklit tamvqsmktg siivdlaaag ggnceltqag
      301 kvvnvngvki igytdlvsrl pnqssqlyan nlvslakllc kekdgtlvid fddvvirnmt
      361 vvkdntitfp pppiqvsaap sqpkvepika idvksnepvs qrkkhifmaa gallfawvas
      421 vapadflshf tvfvlacvig ynvvwnvshs lhtplmsvtn aisgiivvga vlqvgnsnpl
      481 iqllagvail iatinivggf vvtkrmlkmf rk
//
LOCUS       WP_126669077             511 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Colwellia
            sp. Arc7-635].
ACCESSION   WP_126669077
VERSION     WP_126669077.1
KEYWORDS    RefSeq.
SOURCE      Colwellia sp. Arc7-635
  ORGANISM  Colwellia sp. Arc7-635
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Colwelliaceae; Colwellia.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Colwellia sp. Arc7-635"
                     /db_xref="taxon:2497879"
     Protein         1..511
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53899
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpkeii kgerrvattp dtvkkltklg fsvaieagag daanypddvy aqagceivss
       61 akalwqqsdi vlkvqapeae erallksgqt lvsflwpaqn pdmlkelter gvtaiaidsi
      121 prisraqkmd arssmanisg yraiveaaqh fdrfftgqit aagkvdpakv lvigagvagl
      181 aaigaaksmg aivrsfdtra evkeqiesmn aeflmldfkd edgsgeggya kvmsdefiqa
      241 emalfaaqak dvdiivttal ipgkpapkli tsdmvasmkk gsvivdlaae qggnceltvp
      301 gevalvdgvs iigytdlpsr laaqssqlys nnlhnllaem tpekdgnllv dmtndvvlga
      361 ticlagkttw pppapklsaa pkkpkaqkaa aipvekkqsi vgpligatll alallglggf
      421 apanfmshft vfvlacfvgy mviwsvspal htplmsvtna issiivigal iqisstddti
      481 kwfavftvli asinivggfa vthrilkmfr k
//
LOCUS       WP_126672706             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Dyella dinghuensis].
ACCESSION   WP_126672706
VERSION     WP_126672706.1
KEYWORDS    RefSeq.
SOURCE      Dyella dinghuensis
  ORGANISM  Dyella dinghuensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Dyella dinghuensis"
                     /db_xref="taxon:1920169"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34370
     Region          9..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpkhsrll ilgsgpagyt aavyaaranl kptmvtglqq ggqlmtttev dnwpgdvkgv
       61 qgpelmqrma ehaerfetem vfdhihsadl kqrpfrlkgd sgeytcdali iatgatakyl
      121 giaseehfkg kgvsacatcd gfffrdqdvv vvgggntave ealylanigr kvylvhrrdk
      181 lraekimqdk lfekaaagki elvwnhtide ilgdssgvtg vrvkdinsgv trdieatgff
      241 vaightpntg ifegqldmhd gyikirsgle gmatmtsvpg vfaagdvadh vyrqavtsag
      301 fgcmaaldae rwldqgkpta
//
LOCUS       WP_126676051             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_126676051
VERSION     WP_126676051.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33350
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpbtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_126676628             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_126676628
VERSION     WP_126676628.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38498
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vsasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iacmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_126677562             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Prevotella koreensis].
ACCESSION   WP_126677562
VERSION     WP_126677562.1
KEYWORDS    RefSeq.
SOURCE      Prevotella koreensis
  ORGANISM  Prevotella koreensis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Prevotellaceae; Prevotella.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Prevotella koreensis"
                     /db_xref="taxon:2490854"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33372
     Region          4..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkhtkclivg sgpagytaav yagranlnpv vvcgmqmggq ltqttivenf pgypdgvdan
       61 qmmmemqqqa erfgaemvag tvtdvdfsnk pavvtlddge kieadtviia tgasakylgm
      121 pdedkyngrg vsacatcdgf fyrkkvtavv gggdtaceda lylsqlcskv ylvvrkpflr
      181 askimqervm aaenieilfe hnatglygen gvegmhvvkr kgeadeqhyd vaidgfflai
      241 ghkpnsdvfr kwvdtdeigy irtigntqqt rtpglfvagd vcdptyrqav vaagtgckaa
      301 leaerylqti
//
LOCUS       WP_126678057             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_126678057
VERSION     WP_126678057.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53571
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgkniv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_126682699             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Dyella choica].
ACCESSION   WP_126682699
VERSION     WP_126682699.1
KEYWORDS    RefSeq.
SOURCE      Dyella choica
  ORGANISM  Dyella choica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Dyella choica"
                     /db_xref="taxon:1927959"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34428
     Region          9..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpkhsrll ilgsgpagyt aavyaaranl kptmvtglqq ggqlmtttdv dnwpgdvkgv
       61 qgpelmqrma ehaerfetqm efdhihsvdl kqrpfrlkgd sgeyscdali iatgatakyl
      121 gipseehykg kgvsacatcd gfffreqdvv vvgggntave ealylanigr kvylvhrrdk
      181 lraekimqdk lfekaahgki elvwnhtide vlgdntgvtg vrvkdvdsgv trdiaatgff
      241 vaightpntg ifegqldmhd gyikirsgle gmatmasvpg vfaagdvadh vyrqavtsag
      301 fgcmaaldae rwldqhakv
//
LOCUS       WP_126695623             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hymenobacter gummosus].
ACCESSION   WP_126695623
VERSION     WP_126695623.1
KEYWORDS    RefSeq.
SOURCE      Hymenobacter gummosus
  ORGANISM  Hymenobacter gummosus
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Hymenobacteraceae; Hymenobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Hymenobacter gummosus"
                     /db_xref="taxon:1776032"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33815
     Region          10..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mentaaehvk cliigsgpag ytaaiyaara nmapvmyqgl qpggqltitn dvenfpgype
       61 gimgpemmed lkkqaarfgt dirygiatsv dfsghphrvt idekhtltad sviiatgasa
      121 kwlglesear lngsgvsaca vcdgffyrgk dvaivgagdt aaeeatylan lcnkvymlvr
      181 kgemraskim qkrvldnpki evlfdtatde ilgehaveav rvknllthet reipihgffv
      241 aighepnsai freylhhdeq gylktipgts ktnvdgvfac gdvqdfvyrq avtaagtgcm
      301 aaldaeryla algvh
//
LOCUS       WP_126697916             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aquibium carbonis].
ACCESSION   WP_126697916
VERSION     WP_126697916.1
KEYWORDS    RefSeq.
SOURCE      Aquibium carbonis
  ORGANISM  Aquibium carbonis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Aquibium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Aquibium carbonis"
                     /db_xref="taxon:2495581"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34933
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 matkhapvii igsgpagyta aiyaaramlk pmliagmqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmmk qaehvgtdmv sdiiveadia rrpfrlkgds gteytcdali iatgaqakwl
      121 giaseetykg fgvsacatcd gffyrgkdvv vigggnsave ealylsnlak svtvihrrde
      181 fraerilqer lfrkenvkil wdtevheivg dpgkvpmpps vngirlrnrk sgevsdlpid
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 mgcmaaleae kylaeiethr eaae
//
LOCUS       WP_126704331             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flaviflexus ciconiae].
ACCESSION   WP_126704331
VERSION     WP_126704331.1
KEYWORDS    RefSeq.
SOURCE      Flaviflexus ciconiae
  ORGANISM  Flaviflexus ciconiae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Flaviflexus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Flaviflexus ciconiae"
                     /db_xref="taxon:2496867"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32920
     Region          6..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtdirdvviv gsgpagytaa iytaraglkp lilagvldag galmttteve nfpgfpegiq
       61 gpelmenmre qaerfgaqve yedavelkle gdikeiktds etyyaksvil algseyrklg
      121 legesvysgk gvswcatcdg fffkgqeiav vgggdsavte alfltkfask vtvihrrdel
      181 raskvmadrl lanekiemaw nsavtkings adgrlesitv tdtntgdqrd mpvgglfiai
      241 ghdprtsivd gqvdldvngy itvdspttat sipgvfacgd vvdhryrqai taagtgcaaa
      301 ldaehylndm
//
LOCUS       WP_126700512             427 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aquibium
            carbonis].
ACCESSION   WP_126700512
VERSION     WP_126700512.1
KEYWORDS    RefSeq.
SOURCE      Aquibium carbonis
  ORGANISM  Aquibium carbonis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Aquibium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Aquibium carbonis"
                     /db_xref="taxon:2495581"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43367
     Region          4..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,289,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipne vsvgeprvaa spdtvkrika lgldviveag agrasriada dyvkmgatlg
       61 taadvgradi vlrvrrpses eltayksgaa viatmdpygn easvaamara gvaafamefm
      121 pritraqvmd ilssqanlag yqavidaaaa ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrmg avvtatdvra aageqvaslg akfimtdalk dasgsggyar eltedekkaq
      241 salvaehiak qdlvittali pgrpapmlvs aemvasmrpg svivdlaver ggnvegavag
      301 evvttandvk ilghlnvpgr iaasasllya rnlqafletl vdkstgtlti npedelvkat
      361 mltyggaivh psfaaviaap aksdgvvaaa phsdimaapa svapnkkaqa kapakraeak
      421 gkpeggv
//
LOCUS       WP_126708467             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Candidimonas sp. SYP-B2681].
ACCESSION   WP_126708467
VERSION     WP_126708467.1
KEYWORDS    RefSeq.
SOURCE      Candidimonas sp. SYP-B2681
  ORGANISM  Candidimonas sp. SYP-B2681
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Candidimonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Candidimonas sp. SYP-B2681"
                     /db_xref="taxon:2497686"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38716
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligipresl agearvaatp etvrkylagk htvvvergag agshypdday aeagaqlvds
       61 tealgadivl kvrspnhler qhmkagavlv gmldpfdpag isdlagaglt afaleaapri
      121 traqsldvls sqanlagyka vllaadhygr mipmmmtaag tlkaarvvil gagvaglqai
      181 atakrlgavv easdvrpaak eqieslgakf idvpfetdee reiaqgvggy arpmpaswma
      241 rqatlvaerc rqadivista lipgrpapvl isaetvqamk pgsvivdlav erggncplse
      301 kdvivekhgv tliglsnlpa liatdasaly arnvldfmkl itdadgqlai kqddeiitac
      361 lmctdgkvlr sa
//
LOCUS       WP_126707406             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Candidimonas sp. SYP-B2681].
ACCESSION   WP_126707406
VERSION     WP_126707406.1
KEYWORDS    RefSeq.
SOURCE      Candidimonas sp. SYP-B2681
  ORGANISM  Candidimonas sp. SYP-B2681
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Candidimonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Candidimonas sp. SYP-B2681"
                     /db_xref="taxon:2497686"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34051
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mttpkhakvl ilgsgpagys aavyaaranl npvlvtgleq ggqlmtttdv dnwpadaegv
       61 qgpdlmqrfq ahaerfntem vfdhiasvdl srrpftltgd tgaqytcdsl iiatgasaqy
      121 lglpseesfm grgvsgcatc dgffyknqdv ivvgggntav eealylsnic rtvtlvhrrd
      181 kfrsepiild rlmdkvangn iklklfyelq evlgdqsgvt garlrnnqtd vtedlsvtgv
      241 fiaighkpnt aifesqldma ngyiitkggl ngmatmtsip gvfaagdvqd hvyrqaitsa
      301 gtgcmaalda qrwlenaae
//
LOCUS       WP_126714335             307 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Trueperella pyogenes].
ACCESSION   WP_126714335
VERSION     WP_126714335.1
KEYWORDS    RefSeq.
SOURCE      Trueperella pyogenes
  ORGANISM  Trueperella pyogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Trueperella.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Trueperella pyogenes"
                     /db_xref="taxon:1661"
     gene            1..307
                     /gene="trxB"
     Protein         1..307
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32735
     Region          6..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvteihdvvi vgsgpagwta aiytaraglk pvvlagavsa ggalmqttev enfpgwpegi
       61 lgpelmqkfe qqairfgadl ryedatsmkl dgavkeivts edtyhartvi lalgseykkl
      121 glpgeeefsg kgisycatcd gfffrdheia vvgggdsavt eaqflsrfak tvhvihrrde
      181 lrasqimsdr llanekvqmh wnsvvdsing dsrlqsltlr dtvtgetsel pvtglfvaig
      241 heprtafleg vtlddkgyik vaepstatnv pgvfacgdvv dstyqqaita agmgckaald
      301 aeaylar
//
LOCUS       WP_126714872             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Trueperella pyogenes].
ACCESSION   WP_126714872
VERSION     WP_126714872.1
KEYWORDS    RefSeq.
SOURCE      Trueperella pyogenes
  ORGANISM  Trueperella pyogenes
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Trueperella.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Trueperella pyogenes"
                     /db_xref="taxon:1661"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52888
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpresg gqtlvaatpd tvgklsklgy evvvehdags aasfpdslye sagarivske
       61 eawaadivta ldapaladld lmrsgatlis rmapgrnpdi lqalssrsit glamdmvpri
      121 sraqsmdvls sqanvagyra vieaahhfgr lfsgqvtaag kvapanvyvi gagvaglaai
      181 gtansmgtvv katdvrpeta eqvesmgagf vaipvaaees adgyakemgq eqaaaaekly
      241 teqaawadiv ittaaipgrr spvlltaeav agmkpgsviv dmgaanggnv vgsrpdevvv
      301 tdngviiigy selaarlpgq asqlygqnvf nffklatpdk dgvlhldldd eivrsmlvtl
      361 dervmypppp vkvsaapapv passeeptsa eakekswiak hwwkiaagav ftwliltapa
      421 gstthflvfa lavvigfyvi tsvthalhtp lmsvtnaisg iivvgalmqv sassvvvqil
      481 sfiaiavasi nifggflvte rmlkmfhrs
//
LOCUS       WP_126718543             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingomonas ginkgonis].
ACCESSION   WP_126718543
VERSION     WP_126718543.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas ginkgonis
  ORGANISM  Sphingomonas ginkgonis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sphingomonas ginkgonis"
                     /db_xref="taxon:2315330"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34365
     Region          7..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msntvstrml ilgsgpaglt aaiyaaragl spivvqgiqp ggqlttttdv enypgfrevi
       61 qgpwlveemq aqaehvgtkm vwdhisavdl kqrpfrltgd sgttyvadtl viatgaqakw
      121 lglpseehmk gkgasacatc dgffyrgkkv avigggntav eealyltnhs hdvtlihrrd
      181 slraekilqd rlfahpgikv iwnhkvtefl aggtpealvg lelqdtrtga trtldvegaf
      241 vaighhpate lftgqlevdd dgylkvetgs trtsipgvfa cgdvmdkiyr qavtaagtgc
      301 maaldaerwl aeqefealqa ae
//
LOCUS       WP_126722216             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_126722216
VERSION     WP_126722216.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53646
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fskgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tadihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_126723308             344 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tautonia sociabilis].
ACCESSION   WP_126723308
VERSION     WP_126723308.1
KEYWORDS    RefSeq.
SOURCE      Tautonia sociabilis
  ORGANISM  Tautonia sociabilis
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Isosphaerales; Isosphaeraceae; Tautonia.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Tautonia sociabilis"
                     /db_xref="taxon:2080755"
     gene            1..344
                     /gene="trxB"
     Protein         1..344
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36507
     Region          7..338
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqhaavivi gsgsagltaa iyaaranlap lvfegrepgg qltlttdven fpgfpeging
       61 pdlmnrmreq aqrfgadtrw etaiavdlsk rpfvvsttdd psgdpesgtr teytadsliv
      121 atgaaarwlg negpfkgagv stcatcdghf ykgkeiavvg ggdsaaeeat fltrfaskvt
      181 lihrrdrlra skimqeklfa npkidyawna vvdevygetd prpklqgirl rstqtgeivk
      241 dlkvsglfla ighvpntqif rgqlamtpeg ylltraalaw ddveapaglr ermanfatat
      301 dvagvfacgd vvdthyrqai taagsgcaaa ldcekwleqg gagh
//
LOCUS       WP_126734749             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Amycolatopsis roodepoortensis].
ACCESSION   WP_126734749
VERSION     WP_126734749.1
KEYWORDS    RefSeq.
SOURCE      Amycolatopsis roodepoortensis
  ORGANISM  Amycolatopsis roodepoortensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Pseudonocardiales; Pseudonocardiaceae; Amycolatopsis.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Amycolatopsis roodepoortensis"
                     /db_xref="taxon:700274"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35574
     Region          9..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maaeeirnli vigsgpagyt aavyaaraql eplvfegtqf ggalmtttev enfpgfregi
       61 qgpdlmeemr eqakrfgadl rqedvesvel tgdvkyvfan gkryaaravv lsmgaaaryl
      121 nvpgeqellg rgvsacatcd gfffrdhdiv vagggdsame eatfltkfak svtivhrree
      181 fraskimler arenekikwa lnkqiteveg egkveglklk dtvtgeeskl dvtgffvaig
      241 hdprselvrg qvdldedgyv ltkgrtsytn lpgvfaagdl vdrtyrqait aagsgcaaai
      301 daerwlaeha gveaaqetpe lvgggygatt n
//
LOCUS       WP_126727704             391 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Tautonia
            sociabilis].
ACCESSION   WP_126727704
VERSION     WP_126727704.1
KEYWORDS    RefSeq.
SOURCE      Tautonia sociabilis
  ORGANISM  Tautonia sociabilis
            Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia;
            Isosphaerales; Isosphaeraceae; Tautonia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Tautonia sociabilis"
                     /db_xref="taxon:2080755"
     Protein         1..391
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41028
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 miigivresf pgerrvalip asvpaltkag fevlvepgag apagypdesy qqkgaslags
       61 rdevfsradv lfhvlgfgan peagrddlpr yrpeqvvfgf lrplgapeav aelartgvta
      121 fsiellprit raqrmdalss mstvagykav lmaadalprm fpmlmtaagt isparvlvvg
      181 vgvaglqaia takrlgavvs aydirpavke qvqslgarfv elplettqae dvggyaraqg
      241 eefyrkqrel maravaesdv vittanvpgr kapvlitgem vagmnpgsvi vdmaaerggn
      301 caltragqtv svhgvtilga vnlaslvpfh asqmyssnlt tlllhmardg rlnidtddei
      361 tretlvargg evvhprvlea lgaaagesrs s
//
LOCUS       WP_126729708             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseobacterium lacus].
ACCESSION   WP_126729708
VERSION     WP_126729708.1
KEYWORDS    RefSeq.
SOURCE      Chryseobacterium lacus
  ORGANISM  Chryseobacterium lacus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Chryseobacterium group;
            Chryseobacterium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Chryseobacterium lacus"
                     /db_xref="taxon:2058346"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33565
     Region          5..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 menihdcviv gsgpsgftaa iyaaradlkp qlytglepgg qlttttevdn fpgypngvtg
       61 pemmmdlqkq aerfdtkvhy elitkaifsk erggihqlwa gekeilaktv iistgataky
      121 lglddekkya gggvsacatc dgffykgkev ivvgggdtaa eeatylaklc skvtmlvrkn
      181 efraskamih rventpniev kfhheligie gennlverav vinnqtkats kisvhgifia
      241 ighqpntdif kdqittdqng yivtekgstr tnfpgvfaag dvqdaiyrqa vtaagsgcma
      301 amdaekylge le
//
LOCUS       WP_126743585             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium sp. GT3R68].
ACCESSION   WP_126743585
VERSION     WP_126743585.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. GT3R68
  ORGANISM  Flavobacterium sp. GT3R68
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Flavobacterium sp. GT3R68"
                     /db_xref="taxon:2594437"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33812
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaaran mhpvlyqgiq pggqltttne venfpgypdg
       61 vtgpemmvql qgqaerfgta vregwatkvd fsgevlkvwi ndvkelhcet viistgaaak
      121 ylglqseqhy lltgggvsac aicdgffyrn qevvivgagd saceeahyls kmcskvtmlv
      181 rsehfraski medrvrkten itilmnhdtv evlgdgqvvt svqaknkttg eiidipatgf
      241 fvaighkpnt difkdyitld etgyiinkpg taqtnvpgvf vagdaadhvy rqavtaagtg
      301 cmaaldaery lstle
//
LOCUS       WP_126745647             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Variovorax sp. DXTD-1].
ACCESSION   WP_126745647
VERSION     WP_126745647.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. DXTD-1
  ORGANISM  Variovorax sp. DXTD-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Variovorax sp. DXTD-1"
                     /db_xref="taxon:2495592"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34347
     Region          8..313
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mpapqhakvl ilgsgpagyt aavyaaranl qpllitgiaq ggqlmtttev dnwpadvhgv
       61 qgpelmqrfl ehaerfktqi vfdhinkvdl srrpftlagd sgtytcdsli iatgasakyl
      121 gldseqkfmg rgvsacatcd gffyreqevc vigggntave ealylanian kvtlvhrrdk
      181 fraepilidk vkekvaegki vlklhneldq vlgddtgvtg iqikntqtge teqidlkgcf
      241 iaighhpntd ifqgqlemkd nyiltrsglq gfatmtsipg vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq rfleqdgtl
//
LOCUS       WP_126748828             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. DXTD-1].
ACCESSION   WP_126748828
VERSION     WP_126748828.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. DXTD-1
  ORGANISM  Variovorax sp. DXTD-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax sp. DXTD-1"
                     /db_xref="taxon:2495592"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38555
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaett asetrvavtp etvkklvtag htirvqsgag vaasvtdaay iaagaeitdv
       61 agafgadmvl kvrspndaea almkpgtvvi gmlnpfdaag lqrlataglt afaleaaprt
      121 traqsmdvls sqaniagyka vimaadkyqr ffpmlmtaag tvkaarvvil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqieslggkf ievsydtdee keaavgvggy akpmpaswla
      241 rqqvevakrv aladivista lipgraaptl itedmvksmk pgsvivdiaa gkgpdgvggn
      301 cplseadrtv vkhgvtivge tnlpalvaad asalyarnvl dflklivtke galkidledd
      361 ivaacrvahd gqvtkk
//
LOCUS       WP_126754665             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudidiomarina insulisalsae].
ACCESSION   WP_126754665
VERSION     WP_126754665.1
KEYWORDS    RefSeq.
SOURCE      Pseudidiomarina insulisalsae
  ORGANISM  Pseudidiomarina insulisalsae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Pseudidiomarina.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudidiomarina insulisalsae"
                     /db_xref="taxon:575789"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33907
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 maeakhcrll ilgsgpagyt aavyaaranl npvmvtgmqq ggqlttttdv enwpgdaegl
       61 tgpdlmvrmq qhaekfntei vfdhinavdf skrpfrltgd tneytadavi istgasakyl
      121 gldseeafmg kgvsacatcd gffyrnqkvc vvgggntave ealylanias evhvihrree
      181 fraekilvdr lmdkaangnv tlhlnktlde vlgddsgvtg vrikdtetgg lselevmgcf
      241 iaighqpntg ifegqvemqd gyilvrsglq gnatatsvpg vfaagdvmdh tyrqaitsag
      301 tgcmaaldae ryldaltka
//
LOCUS       WP_126751245             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Idiomarina piscisalsi].
ACCESSION   WP_126751245
VERSION     WP_126751245.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina piscisalsi
  ORGANISM  Idiomarina piscisalsi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Idiomarina piscisalsi"
                     /db_xref="taxon:1096243"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33950
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 madakhckll ilgsgpagyt aavyaaranl dpvmvtgmqq ggqlttttdv enwpgdaegl
       61 tgpdlmvrmq qhaerfntei vfdhinsvdf skrpfqlkgd vgeytadsvi istgasakyl
      121 gldseeafmg kgvsacatcd gffykkqkvc vvgggntave ealylsnias evhvihrrdt
      181 fraekilvdr lhekekngni tfhlnktlde vlgddagvtg vrikdtqtgg teeldvagcf
      241 iaighqpntg ifdgqlemqn gyitvqsgle gnatatsvpg vfaagdvmdh vyrqaitsag
      301 tgcmaaldae ryldvltks
//
LOCUS       WP_126756485             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aliidiomarina taiwanensis].
ACCESSION   WP_126756485
VERSION     WP_126756485.1
KEYWORDS    RefSeq.
SOURCE      Aliidiomarina taiwanensis
  ORGANISM  Aliidiomarina taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Aliidiomarina.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Aliidiomarina taiwanensis"
                     /db_xref="taxon:946228"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33790
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 madvkhckll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttdv enwpgdpegl
       61 tgpdlmvrmq khaerfdtei ifdhineadl tqrpfrlkgd sgeytcdali iatgasakyl
      121 glpsetafqg rgvsacatcd gffyrgqqvc vvgggntave ealylsniae evhvihrrdt
      181 frsekilidr lmekaengni tlhlnktlde vvgddagvtg vrirdtqsde vsdlavhgvf
      241 iaighqpntq lfegqldmen gylkvqsgaq anatqtsipg vfaagdvsdf tyrqaitsag
      301 tgcmaaldae rfldsl
//
LOCUS       WP_126758779             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudidiomarina marina].
ACCESSION   WP_126758779
VERSION     WP_126758779.1
KEYWORDS    RefSeq.
SOURCE      Pseudidiomarina marina
  ORGANISM  Pseudidiomarina marina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Pseudidiomarina.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudidiomarina marina"
                     /db_xref="taxon:502366"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33815
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 maeakhcrll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttdv enwpgdpegl
       61 tgpdlmvrmq qhaekfntem ifdhinrvdf sskplklfgd sgeytadavi iatgasakyl
      121 gldseeafmg rgvsacatcd gffyrnqkva vvgggntave ealylanias evhvihrrdt
      181 fraekilvdr lmdkasngnv tlhlnktlde vlgddagvtg vrikdtqdga lseldvmgcf
      241 iaighqpntg ifadqlemhd gyivvksglh gnatatsvpg vfaagdvmdh iyrqaitsag
      301 tgcmaaldae ryldgltka
//
LOCUS       WP_126761403             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vagococcus lutrae].
ACCESSION   WP_126761403
VERSION     WP_126761403.1
KEYWORDS    RefSeq.
SOURCE      Vagococcus lutrae
  ORGANISM  Vagococcus lutrae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Vagococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vagococcus lutrae"
                     /db_xref="taxon:81947"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32932
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydvivigag pggmtaalya sradlsvlvl ekgiyggqlq ntadvenypg vglvtgpela
       61 ekiykdstaf gaehaygsvt kvedhgthkt vhtedeqyda kvviiatgsd hrrlgapgee
      121 efsgrgvsyc avcdgpffrn khvavigggd saveegsylt qvadkvsvih rrdelraqkv
      181 lqdrafknek mtfvwnhvve eiqgddikvn nlrikdtqtg evsdypvdav fiyvgldpit
      241 epfkslgvtn eegwiptnek metsvpgvya igdvretvlr qittavgdgs iagqeafkyi
      301 eslad
//
LOCUS       WP_126766010             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aliidiomarina iranensis].
ACCESSION   WP_126766010
VERSION     WP_126766010.1
KEYWORDS    RefSeq.
SOURCE      Aliidiomarina iranensis
  ORGANISM  Aliidiomarina iranensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Aliidiomarina.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Aliidiomarina iranensis"
                     /db_xref="taxon:1434071"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34351
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 maevkhckll ilgsgpagyt aavyaaranl npvlvtgiqq ggqlttttev enwpgdaegl
       61 tgpdlmvrmq qhaerfdtei vfdhinsvef tqrpfrlkgd saeytadavi iatgasakyl
      121 glpsedafkg rgvsacatcd gffyrgqkvc vvgggntave ealylsniae evhvihrrds
      181 fraekilidr lmakaeqgnv vlhlhqtlde vlgdnmgvtg irmkdfrdgs tselevqgvf
      241 iaighqpntq mfvdqldman gylkvqsglh gnatqtsipg vfaagdvsdh iyrqaitsag
      301 tgcmaaldae rfldaldnek
//
LOCUS       WP_126770240             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Pseudidiomarina].
ACCESSION   WP_126770240
VERSION     WP_126770240.1
KEYWORDS    RefSeq.
SOURCE      Pseudidiomarina
  ORGANISM  Pseudidiomarina
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudidiomarina"
                     /db_xref="taxon:2800384"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34036
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 maeakhcrll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttdv enwpgdaegl
       61 tgpdlmvrmq qhaekfdtei vfdhinkvdf sqrpfrlfgd sqeftadavi istgasakyl
      121 gldseeafmg kgvsacatcd gffyrnqkvc vvgggntave ealylanias evhvihrreq
      181 fraekilvdr lmdkaengnv tlhlnktlde vlgddsgvtg vrvkdtqdgs lselevmgcf
      241 iaighqpntg ifdgelemqd gyiivqsglq gnatatsvpg vfaagdvmdh tyrqaitsag
      301 tgcmaaldae ryldaltka
//
LOCUS       WP_126775757             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aliidiomarina sanyensis].
ACCESSION   WP_126775757
VERSION     WP_126775757.1
KEYWORDS    RefSeq.
SOURCE      Aliidiomarina sanyensis
  ORGANISM  Aliidiomarina sanyensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Aliidiomarina.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Aliidiomarina sanyensis"
                     /db_xref="taxon:1249555"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34153
     Region          1..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 maevkhckll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttdv enwpgdpegl
       61 tgpdlmvrmq qhaerfntei lfdhihsvdl qqrpfrlkgd keytcdalii atgasakylg
      121 lpsedafkgk gvsacatcdg ffyrgqkvcv vgggntavee alylsniaee vhvihrrdtf
      181 raekilidrm mekaktgnit lhlhktldev lgdnmgvtgi rikdardest evlelqgvfi
      241 aighqpntsm fegqlameng yikvqsglhg natqtsipgv faagdvsdhv yrqaitsagt
      301 gcmaaldaer fldavkk
//
LOCUS       WP_126761946             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudidiomarina halophila].
ACCESSION   WP_126761946
VERSION     WP_126761946.1
KEYWORDS    RefSeq.
SOURCE      Pseudidiomarina halophila
  ORGANISM  Pseudidiomarina halophila
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Pseudidiomarina.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudidiomarina halophila"
                     /db_xref="taxon:1449799"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33932
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 madakhcrll ilgsgpagyt aavyaaranl dpvmvtgmqq ggqlttttdv enwpgdaegl
       61 tgpdlmvrmq qhaekfntei vfdhinkvdf sskpfrlygd sheftadavv istgasakyl
      121 gldseeafmg kgvsacatcd gffyrnqkvc vvgggntave ealylanias evhvihrreq
      181 fraekilvdr lmdkaangnv tlhlnktlde vlgddsgvtg vriqdtedgs lselevmgcf
      241 iaighqpntg ifdgqlemhd gyivvrsglt gnatatsvpg vfaagdvmdh vyrqaitsag
      301 tgcmaaldae ryldaltka
//
LOCUS       WP_126778420             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_126778420
VERSION     WP_126778420.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53600
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklvrll
      421 atkgitheiq ipdistkeka qkaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_126779155             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Idiomarina ramblicola].
ACCESSION   WP_126779155
VERSION     WP_126779155.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina ramblicola
  ORGANISM  Idiomarina ramblicola
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Idiomarina ramblicola"
                     /db_xref="taxon:263724"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33986
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 maeakhckll ilgsgpagyt aavyaaranl npvmvtgmqq ggqlttttdv enwpgdaegl
       61 tgpdlmvrmq khaerfdtei vfdhissvdf skrpfrlkgd vgeytadsvi istgasakyl
      121 gldseeafmg kgvsacatcd gffykkqkvc vvgggntave ealylsnias evhvihrrdt
      181 fraekilvdr lnekeqngni tfhlnktlde vlgddagvtg vrikdtqdgs teelevagcf
      241 iaighqpntg ifdgelemqd gyiqvqsglq gnatatsvpg vfaagdvmdh vyrqavtsag
      301 tgcmaaldae ryldaltks
//
LOCUS       WP_126783746             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Idiomarina seosinensis].
ACCESSION   WP_126783746
VERSION     WP_126783746.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina seosinensis
  ORGANISM  Idiomarina seosinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Idiomarina seosinensis"
                     /db_xref="taxon:281739"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34040
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 madakhckll ilgsgpagyt aavyaaranl dpvmvtgmqq ggqlttttdv enwpgdaegl
       61 tgpdlmvrmq qhaerfntei vfdhinsvdf serpfrlkgd vgeytadsvi istgasakyl
      121 gldseeafmg kgvsacatcd gffykkqkvc vvgggntave ealylsnias evhvihrrdt
      181 fraekilvdr lhekeqngnv vfhlnktlde vlgdemgvtg vrikdtnegs ykeldvagcf
      241 iaighqpntg ifdgqlemnn gyiqvqsgle gnatatsipg vfaagdvmdh vyrqaitsag
      301 sgcmaaldae ryldaltk
//
LOCUS       WP_126780147             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vagococcus salmoninarum].
ACCESSION   WP_126780147
VERSION     WP_126780147.1
KEYWORDS    RefSeq.
SOURCE      Vagococcus salmoninarum
  ORGANISM  Vagococcus salmoninarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Vagococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vagococcus salmoninarum"
                     /db_xref="taxon:2739"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32636
     Region          3..302
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrdviiigag pggmtaalya sradlsvlvl egglpggqln ntaevenypg vgimqgpelg
       61 ekmladssnf gaehaygfvt giedhgtfkk vitedetfet kvviiaagse hrklgvvgee
      121 eysgrgvsyc avcdgpffrn khlvvigggd saveegsylt qvaekvtiih rrdalraqki
      181 lqdrafknek idfiwnstae eilgndmqvk glrlkdtqtg etseitadgv fiyvgldplt
      241 apfkglgitd eegwiptnek metripgiya vgdvratvlr qvatavgdgs iagqeaykyi
      301 eamnd
//
LOCUS       WP_126787648             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aliidiomarina sedimenti].
ACCESSION   WP_126787648
VERSION     WP_126787648.1
KEYWORDS    RefSeq.
SOURCE      Aliidiomarina sedimenti
  ORGANISM  Aliidiomarina sedimenti
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Aliidiomarina.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Aliidiomarina sedimenti"
                     /db_xref="taxon:1933879"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34536
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 madvkhckll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttdv enwpgdpegl
       61 tgpdlmvrmq qhaerfntei ifdhinevtl nerpfrlrgd naeytcdgli iatgasakyl
      121 glpseeafkg kgvsacatcd gffyrnqkvc vvgggntaie ealylsnias evhlihrrdt
      181 fraekilidr lmdkaengnv tlhlhknlde vlgddmgvtg vrikdsrdgs teelavqgaf
      241 iaighspntd mfqgqldmen gyikvqtgsh gnatqtsieg vfaagdvsdh vyrqaitsag
      301 tgcmaaldae rfldqldqak k
//
LOCUS       WP_126790594             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aliidiomarina haloalkalitolerans].
ACCESSION   WP_126790594
VERSION     WP_126790594.1
KEYWORDS    RefSeq.
SOURCE      Aliidiomarina haloalkalitolerans
  ORGANISM  Aliidiomarina haloalkalitolerans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Aliidiomarina.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Aliidiomarina haloalkalitolerans"
                     /db_xref="taxon:859059"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34139
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 madarhckll ilgsgpagyt aavyaaranl npvlvtglqq ggqlttttdv enwpgdpegl
       61 tgpdlmvrmq qhaerfntei ifdhinavel tekpfrlkgd sgeytcdali iatgasakyl
      121 glpseeafkg kgvsacatcd gffyrgqkvc vvgggntave ealylsniae evhvihrrds
      181 fraekilvdr lmakaesgnv klhlyktlde vlgdnmgvtg irirdtrnde lselelagvf
      241 iaighqpntq mfagqldmen gylkvhsgtn gnatqtsipg vfaagdvsdh iyrqaitsag
      301 tgcmaaldae ryldalaek
//
LOCUS       WP_126794841             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vagococcus carniphilus].
ACCESSION   WP_126794841
VERSION     WP_126794841.1
KEYWORDS    RefSeq.
SOURCE      Vagococcus carniphilus
  ORGANISM  Vagococcus carniphilus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Vagococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vagococcus carniphilus"
                     /db_xref="taxon:218144"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33200
     Region          2..300
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydvivigag pggmtaalya srsdlsvlvi ergapggqlm ntaevenypg fntilgpdla
       61 mkmyenssnf gathtygnvt rienegtikk vycdeevyea kavviasgsd hrkigikgee
      121 eyagrgvsyc avcdgaffkd rhlyvigggd saveegmylt qfaskvtivh rrdelraqki
      181 lqdrafknek vdflwnkvpv eftgddkkit gitlkdtktd evsqveadgv fvyvgldplt
      241 epfkdlgitt eegwittnnr metaipgiya igdvrdtvlr qiatavgdgs iagqevykyi
      301 talqd
//
LOCUS       WP_126802698             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aliidiomarina minuta].
ACCESSION   WP_126802698
VERSION     WP_126802698.1
KEYWORDS    RefSeq.
SOURCE      Aliidiomarina minuta
  ORGANISM  Aliidiomarina minuta
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Aliidiomarina.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Aliidiomarina minuta"
                     /db_xref="taxon:880057"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34491
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 madakhckll ilgsgpagyt aavyaaranl dpvlltgieq ggqlttttdv enwpgdaegl
       61 tgpdlmvrmq khaerfdtei ifdhinevql kqrpfvlkgd sgeytcdali iatgasakyl
      121 glpseeafkg kgvsacatcd gffyrnqkvc vvgggntaie ealylsnias evhlihrrdt
      181 frgekilidr mmdkakngni tlhlhktlde vlgdnmgvtg vrikdtrsde lnelevqgaf
      241 iaighqpntd mfagqldmen gyikvqtgsh gnatqtsieg vyaagdvsdh vyrqaitsag
      301 tgcmaaldae rfldqlehnk
//
LOCUS       WP_126799012             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aliidiomarina soli].
ACCESSION   WP_126799012
VERSION     WP_126799012.1
KEYWORDS    RefSeq.
SOURCE      Aliidiomarina soli
  ORGANISM  Aliidiomarina soli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Aliidiomarina.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Aliidiomarina soli"
                     /db_xref="taxon:1928574"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34522
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 madvkhckll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttdv enwpgdpegl
       61 tgpdlmvrmq qhaerfntei ifdhindvtl nerpfrlrgd naeytcdgli iatgasakyl
      121 glpseeafkg kgvsacatcd gffyrnqkvc vvgggntaie ealylsnias evhlihrrdt
      181 fraekilidr lmdkaengnv tlhlhknlde vlgddmgvtg vrikdsrdgs teelavqgaf
      241 iaighspntd mfqgqldmen gyikvqtgsh gnatqtsieg vfaagdvsdh vyrqaitsag
      301 tgcmaaldae rfldqldqak k
//
LOCUS       WP_126809648             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vagococcus elongatus].
ACCESSION   WP_126809648
VERSION     WP_126809648.1
KEYWORDS    RefSeq.
SOURCE      Vagococcus elongatus
  ORGANISM  Vagococcus elongatus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Vagococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vagococcus elongatus"
                     /db_xref="taxon:180344"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32971
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydvivigag pggmtaalya sradlkvlvl ergiyggqmq ntaevenfpg aglitgpels
       61 ekmyqdstnf gaehgygyvt nvedhgdykt vitedtsydt kvviiatgae hrkldipgee
      121 eyagrgvsyc avcdgaffrn qplvvvgggd saveegiyls qlaesvtiih rrdelrcqkv
      181 vagrafnnek inflwnkvve eiegddqkvr tlklkdtktg eistletggv fiyigvipit
      241 eafssldild gegwvvtnek metsvpgiya vgdvrqtvlr qittavgdgs iagleaykyi
      301 eslkd
//
LOCUS       WP_126805515             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aliidiomarina shirensis].
ACCESSION   WP_126805515
VERSION     WP_126805515.1
KEYWORDS    RefSeq.
SOURCE      Aliidiomarina shirensis
  ORGANISM  Aliidiomarina shirensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Aliidiomarina.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Aliidiomarina shirensis"
                     /db_xref="taxon:1048642"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34408
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 maevkhckll ilgsgpagyt aavyaaranl npvlvtgiqq ggqlttttev enwpgdpegl
       61 tgpdlmvrmq qhaerfdtei vfdhinsvnf tqrpfrlqgd saeytadavi iatgasakyl
      121 glpsedafkg rgvsacatcd gffyrgqkvc vvgggntave ealylsniae evhvihrrds
      181 fraekilidr lmakaengnv vlhlhqtlde vlgdqmgvtg irmkdfrdgs tseldvqgvf
      241 iaighqpntq mfteqldmen gylkvqsglh gnatqtsipg vfaagdvsdh iyrqaitsag
      301 tgcmaaldae rfldaldndk
//
LOCUS       WP_126822189             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vagococcus entomophilus].
ACCESSION   WP_126822189
VERSION     WP_126822189.1
KEYWORDS    RefSeq.
SOURCE      Vagococcus entomophilus
  ORGANISM  Vagococcus entomophilus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Vagococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vagococcus entomophilus"
                     /db_xref="taxon:1160095"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33197
     Region          2..300
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydviiigag pggmtaalya sradlsvlvi ergapggqmn ntaevenypg fdrilgpdla
       61 mkmyegseqf gakheygivq kiedhgnykt vqceeesydt ktviiasgce hrklgvlgee
      121 efsgrgvsyc avcdgaffkg khlvvvgggd saveegtylt qfaekvtiih rrdtlraqki
      181 lqdrafkndk isfiwnktvq eiigddtkvt elklkdtvtk eeetlqadgv fiyvgldpls
      241 epfadlgitn kegwietnas metavpgiya igdvretvlr qittavgdgs iagqevyqyi
      301 valed
//
LOCUS       WP_126825030             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudidiomarina taiwanensis].
ACCESSION   WP_126825030
VERSION     WP_126825030.1
KEYWORDS    RefSeq.
SOURCE      Pseudidiomarina taiwanensis
  ORGANISM  Pseudidiomarina taiwanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Pseudidiomarina.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudidiomarina taiwanensis"
                     /db_xref="taxon:337250"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33882
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 madakhcgll ilgsgpagyt aavyaaranl kpvlvtgmqq ggqlttttev enwpgdpegl
       61 tgpdlmvrmq qhaekfntei ifdhinrvdf sakplrlfgd sgeytadavi iatgasakyl
      121 glpseqafmg kgvsacatcd gffyrnqkvc vvgggntave ealylanias evhvihrrdt
      181 fraekilvdr lmdkaengnv tlhlnktlde vlgddmgvtg vrvrdtqdds lseievmgcf
      241 iaighqpntg ifqdqlemkd gyiivqsgln gnatatsvpg vfaagdvmdh tyrqaitsag
      301 tgcmaaldae kyldalqk
//
LOCUS       WP_126827242             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            fabae].
ACCESSION   WP_126827242
VERSION     WP_126827242.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium fabae
  ORGANISM  Rhizobium fabae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium fabae"
                     /db_xref="taxon:573179"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39172
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare ltdgetrvaa spetvkkmks fgfdvvveag agvlsripda efeaagarig
       61 sfadaisadv vlkvrrpsas eisgyksgav viavmdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaagv ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgraaprl vsramlasmk pgavavdlav erggniegvv
      301 ageiadvdgv rvigfanmpg rvaasasaly aknlvtflet mvnkesrsvv vnlddelvka
      361 tmltyagdvv hpafggakkg dn
//
LOCUS       WP_126829763             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vagococcus fessus].
ACCESSION   WP_126829763
VERSION     WP_126829763.1
KEYWORDS    RefSeq.
SOURCE      Vagococcus fessus
  ORGANISM  Vagococcus fessus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Vagococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Vagococcus fessus"
                     /db_xref="taxon:120370"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32647
     Region          3..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrdviiigag pggmtaalya sraelsvmvl eggipggqmn ntaevenypg vgvvqgpela
       61 skmledssnf gaehaygfvt giedhgdykt vvtddarydt ktviiatgse hrklgvpgee
      121 efggrgvsyc avcdgpffrn khlivigggd saveegsylt qvaskvtvih rrdklraqkl
      181 lqerafnnek mefiwnttve eivgndrqvt glrlknvetg dvtemdadgv fiyvgldpls
      241 epfkslgitn eegwietdat matsvpgiya igdvratvlr qiatavgdgs iagqevykyi
      301 ealnd
//
LOCUS       WP_126832436             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudidiomarina aquimaris].
ACCESSION   WP_126832436
VERSION     WP_126832436.1
KEYWORDS    RefSeq.
SOURCE      Pseudidiomarina aquimaris
  ORGANISM  Pseudidiomarina aquimaris
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Pseudidiomarina.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudidiomarina aquimaris"
                     /db_xref="taxon:641841"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34094
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 maeakhcrll ilgsgpagyt aavyaaranl npvlvtgmqq ggqlttttdv enwpgdaegl
       61 tgpdlmvrmq qhaekfdtei vfdhinkvdf sqrpfrlfgd sqeftadavi istgasakyl
      121 gldseeafmg kgvsacatcd gffyrnqkvc vvgggntave ealylanias evhvihrreq
      181 fraekilvdr lmdkaengnv tlhlnktlde vlgddmgvna vrikdtndgs lselevmgcf
      241 iaighqpntg ifdgeldmqd gyiivqsglq gnatatsvpg vfaagdvmdh tyrqaitsag
      301 tgcmaaldae ryldaltka
//
LOCUS       WP_126835840             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Variovorax
            sp. MHTC-1].
ACCESSION   WP_126835840
VERSION     WP_126835840.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. MHTC-1
  ORGANISM  Variovorax sp. MHTC-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Variovorax sp. MHTC-1"
                     /db_xref="taxon:2495593"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38658
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpaeta pgetrvavta etakklvaqg htvriqsgag vaasvtdaay qaagaeitda
       61 pgslgadivl kvrapsdaea tlmkpgtvvi gmlnpfdaag lqrlataglt gfaleaaprt
      121 traqsmdvls sqaniagyka vmiaadkyqr ffpmlmtaag tvkaarivil gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf ievsydteee keaaqgvggy arpmpqswld
      241 rqkievakrv aaadvvista lipgraaptl itedmvksmk pgsvivdiaa gkgpdgvggn
      301 cplseadktv vkhnvtivge tnlaalvaad asslyarnvl dflklivnke galnidledd
      361 ivaaclmsrd gqvtrk
//
LOCUS       WP_126837442             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus aureus].
ACCESSION   WP_126837442
VERSION     WP_126837442.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33554
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteidfdiai igagpagmta avyasranlk tvmiergipg gqmanteeve nfpgfemitg
       61 pdlstkmfeh akkfgavyqy gdiksvedkg eykvinfgnk eltakaviia tgaeykkigv
      121 pgeqelggrg vsycavcdga ffknkrlfvi gggdsaveeg tfltkfadkv tivhrrdelr
      181 aqrilqdraf kndkidfiws htlkrinekd gkvgsvtlts tkdgseethe adgvfiyigm
      241 kpltapfkdl gitndvgyiv tkddmttsvp gifaagdvrd kglrqivtat gdgsiaaqsa
      301 aeyiehlndq a
//
LOCUS       WP_126839635             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Variovorax sp. MHTC-1].
ACCESSION   WP_126839635
VERSION     WP_126839635.1
KEYWORDS    RefSeq.
SOURCE      Variovorax sp. MHTC-1
  ORGANISM  Variovorax sp. MHTC-1
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Variovorax.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Variovorax sp. MHTC-1"
                     /db_xref="taxon:2495593"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34348
     Region          4..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msssprhakv lilgsgpagy taavyaaran lqpmlitgia qggqlmtttd vdnwpadvhg
       61 vqgpdlmqrf lehaerfkte ivfdhinkvd lskrpftltg dsgtytcdal viatgasaky
      121 lgldseqhfm grgvsgcatc dgffyrdqev cvvgggntav eealylsnia kkvtlvhrrd
      181 kfraepilid klhekaaegk ielkvhntld evlgddtgvt girlkntqtg ateridlkgc
      241 fiaighhpnt difqgqvemk dgyiltrsgl qgfatmtsvp gvfaagdvqd hvyrqaitsa
      301 gtgcmaalda qrfleqdgtl
//
LOCUS       WP_126840476             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus aureus].
ACCESSION   WP_126840476
VERSION     WP_126840476.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33425
     Region          7..304
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mteidfdiai igagpagmta avyasranlk tvmiergipg gqmanteeve nfpgfemitg
       61 pdlstkmfeh akkfgavyqy gdiksvedkg eykvinfgnk eltakaviia tgaeykkigv
      121 pgeqelggrg vsccavcdga ffknkrlfvi gggdsaveeg tfltkfadkv tivhrrdelr
      181 aqrilqdraf kndkidfiws htlksinekd gkvgsvtlts tkdgseethe adgvfiyigm
      241 kpltapfkdl gitndvgyiv tkddmttsvp gifaagdvrd kglrqivtat gdgsiaaqsa
      301 aeyiehlndq a
//
LOCUS       WP_126840592             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Idiomarina tyrosinivorans].
ACCESSION   WP_126840592
VERSION     WP_126840592.1
KEYWORDS    RefSeq.
SOURCE      Idiomarina tyrosinivorans
  ORGANISM  Idiomarina tyrosinivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Idiomarina.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Idiomarina tyrosinivorans"
                     /db_xref="taxon:1445662"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33841
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhckll ilgsgpagyt aavyaaranl npvmvtgmqq ggqlttttdv enwpgdaegl
       61 tgpdlmvrmq qhaerfntei vfdhinevdf ssrpfklkgd tgsyiadsvi istgasakyl
      121 gldseqkfmg kgvsacatcd gffyknqkvc vvgggntave ealylanias evhvihrret
      181 fraekilvdr lrdraengnv tlhlnktlde vlgdemgvtg vrvkdtqdgs lsefdvagcf
      241 iaighqpntg ifdgqlamqd gyivvesgls gnatatsvpg vfaagdvmdh vyrqaitsag
      301 tgcmaaldae rfldsltk
//
LOCUS       WP_126846216             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Sphingomonas].
ACCESSION   WP_126846216
VERSION     WP_126846216.1
KEYWORDS    RefSeq.
SOURCE      unclassified Sphingomonas
  ORGANISM  unclassified Sphingomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="unclassified Sphingomonas"
                     /db_xref="taxon:196159"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34485
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtthktrmli lgsgpaglsa aiygaragmk pilvqgiqpg gqlmtttdve nypgfadviq
       61 gpwlmeqmqk qaehvgttlm ydtvvevdfs qrpfrlvgds gdiyegdvli iatgaqakwl
      121 gldsedalkg kgvsacatcd gffyrgkkva vigggntave ealyltnhsp dvtlihrrds
      181 fraekilqer lfahkgitvl wnkevaefvd gggtaglval elidtvtger srleteggfv
      241 aighhpatel frghlkldad hyiwvetgst rtsvpgvfac gdvmdkvyrq avtaagtgcm
      301 aaldaerfla eaefemvaea ae
//
LOCUS       WP_126847972             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Dermabacter sp. HSID17554].
ACCESSION   WP_126847972
VERSION     WP_126847972.1
KEYWORDS    RefSeq.
SOURCE      Dermabacter sp. HSID17554
  ORGANISM  Dermabacter sp. HSID17554
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Dermabacter.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Dermabacter sp. HSID17554"
                     /db_xref="taxon:2419511"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53567
     Region          1..511
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipretl edqplvaatp dtvrkllklg yevvvergag erasyldaay aeagaeivge
       61 evwqsdivtt ldtppretre kmlpgavlis rmapgrnpel idelkehrlt alamdavpri
      121 sraqsmdvls smaniagyra vieaasnfgr lftgqvtaag kvppanvyvi gagvaglaai
      181 gtansmgaiv katdlrpeaa eqvesmgaef vaipakteks edgyakemta dqakaaaely
      241 sqqsaeadiv ittanipgrk apvlltaadv qnmkpgsviv dmaaanggnc eltkpsevyq
      301 tdngvtivgh tdlagrlpgq asqlygqniv nlmklvtpqk dgvmmldfed tivrgitvtf
      361 ahdgqadvlw ppppvkvsaa papapeaapa paeapeakks hagtiaaiig gilgvalvla
      421 spfqvaeqym vlmlaivvgy yvitsvthsl htplmsetna isgiilvgai lqvgsaniav
      481 ailsfiaivi asinifggft vthrmlsmfs reg
//
LOCUS       WP_126846715             349 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Dermabacter sp. HSID17554].
ACCESSION   WP_126846715
VERSION     WP_126846715.1
KEYWORDS    RefSeq.
SOURCE      Dermabacter sp. HSID17554
  ORGANISM  Dermabacter sp. HSID17554
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae; Dermabacter.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Dermabacter sp. HSID17554"
                     /db_xref="taxon:2419511"
     gene            1..349
                     /gene="trxB"
     Protein         1..349
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36586
     Region          45..349
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttsepqtpi lntlgggfgi slsgsqtdta etaapsdaad apvrdivivg sgpagytaav
       61 yaaraglkpv viagsldagg almttteven fpgfpegvmg pdlmgnmqeq aerfgaeilf
      121 edatevelag dvktiraegg evfrakavil atgsayrklg vdgeerlsgk gvswcatcdg
      181 fffkdkdifv vgggdsavee atfltrfgks vtllhrrdal raskimakra eddpklairw
      241 ntqvvgiege nelshlvled tvtgeretvp adglfeaigh lprsglfkgq ididdegyii
      301 cegrtthtsl egvfacgdvv dhryrqaita agsgcsaald aekylatle
//
LOCUS       WP_126849988             307 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corynebacterium
            pseudodiphtheriticum].
ACCESSION   WP_126849988
VERSION     WP_126849988.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pseudodiphtheriticum
  ORGANISM  Corynebacterium pseudodiphtheriticum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Corynebacterium pseudodiphtheriticum"
                     /db_xref="taxon:37637"
     gene            1..307
                     /gene="trxB"
     Protein         1..307
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32765
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mivhdvaiig sgpagysaal yaaraelnpi vfegyeygge lmntteveny pgfqkgimgp
       61 elmeemraqa qrfgadlrme lvdrveldge ikkiyvgdee faartvilat gsaprhlgve
      121 gekaltgrgv stcatcdgff fkdhdiavvg ggdsameeat fltkfarsvt ivhrregfsa
      181 spimldrakn nekiswalnk tvaaiqesag kvsgltlqdt qtgetseldv talfvaigsd
      241 prtdlvqgqv dleetgyvkv nhphthtnld gvfacgdlvd dhyqqaitaa gsgcraaida
      301 geylaah
//
LOCUS       WP_126851774             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_126851774
VERSION     WP_126851774.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53581
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dhylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_126858856             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_126858856
VERSION     WP_126858856.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33724
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnm rlhwnttlde vlgdasgvtg vrlkstvdgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_126862704             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_126862704
VERSION     WP_126862704.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38587
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivhsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_126863291             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Peribacillus cavernae].
ACCESSION   WP_126863291
VERSION     WP_126863291.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus cavernae
  ORGANISM  Peribacillus cavernae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Peribacillus cavernae"
                     /db_xref="taxon:1674310"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35220
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mteekiydvi iigagpagmt aavytsranl stlmlergvp ggqmanteev enypgfgsil
       61 gpelstkmfd hakkfgaeya ygdvkevidg eeyktiiags keykaraiiv sagaeykkig
      121 vpgenelggr gvsycavcdg affkqkelvv vgggdsavee gvyltrfask vtivhrrdel
      181 raqkilqdra fdnekidfiw nhtikqindk dgkvggvtli ntvngeeqef kadgvfiyig
      241 mlpltkpfqs lgitnvngyi etnermetki pgiyaagdir ektlrqivta tgdgsiaaqa
      301 aqhyieelke qmklklniga digr
//
LOCUS       WP_126867933             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_126867933
VERSION     WP_126867933.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33720
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg lrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_126868328             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_126868328
VERSION     WP_126868328.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33253
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkxllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_126869932             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_126869932
VERSION     WP_126869932.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33705
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvkgl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_126878078             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia kururiensis].
ACCESSION   WP_126878078
VERSION     WP_126878078.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia kururiensis
  ORGANISM  Paraburkholderia kururiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia kururiensis"
                     /db_xref="taxon:984307"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39616
     Region          1..377
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,302,328,330)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,335..336,340,
                     343..344)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anetrvaatp etvkkyvsqg hrvtvqagag taasftdeay tavgaeitda
       61 atafaadlvl kvqspsvsel pfmkrgavlc gmldpfnadn aaqlaeaglt afaleaaprt
      121 traqsldvls sqaniagyka vlvaasfypr fmpmlmtaag tvkaarvlvl gagvaglqai
      181 atarrlgavi easdvrpavk eqieslgakf ldvpyetqee reaaegvggy arpmppswla
      241 rqsalvhera rqadivista lipgrdaptl lpaqtveamk pgsvvvdlaa grgpvadeat
      301 grrggncplt vadqavtkhg vtivgytnla amvaadassl yarnlldflk livtkegtln
      361 idladdivaa tllardgavt rka
//
LOCUS       WP_126881958             481 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas dhakensis].
ACCESSION   WP_126881958
VERSION     WP_126881958.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas dhakensis
  ORGANISM  Aeromonas dhakensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Aeromonas dhakensis"
                     /db_xref="taxon:196024"
     gene            1..481
                     /gene="nrfA"
     Protein         1..481
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53366
     Region          26..481
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mivsshnrqt rlglaalllt tclgtsgwaq aadeaqpkgk vearselfak dhadqfsswk
       61 atgesrertd alaedpqmvv lwggyafakd ynkprghfya ltdvretlrt gapksaedgp
      121 lpmacwsckg pdvarvidek gedgyfkgmw akggpeivnt igcadchdta skefkegkpa
      181 lhlsrpyadr amtaigkpfk eqgrfdqqsq vcgqchveyy fsgptkavkf pwdkgttveq
      241 meqyydeigf adwthalskt pmlkaqhpey etwragihgq nnvacvdchm pkvqneqgkv
      301 ytdhkvgnpf drfdqtcrnc htqskemlqg vvkqrkdaih dlkirvekql vhahfeakaa
      361 wdagateaem kdilqdirha qwrwdfsias hgvqmhapev alrmlgtald kaadartkla
      421 rllaakglsq eiaipdissk ekaqaalgmd mkqmnsdkaq flkttvpawd aeakaagrla
      481 q
//
LOCUS       WP_126884166             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces sp. WAC05374].
ACCESSION   WP_126884166
VERSION     WP_126884166.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces sp. WAC05374
  ORGANISM  Streptomyces sp. WAC05374
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces sp. WAC05374"
                     /db_xref="taxon:2487420"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34097
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfrdgim
       61 gpdlmdnmra qaerfgaelv pddvvsvdlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfa wdsevaaihg eqkltgvtlr ntktgetsel pvtglfiavg
      241 hdprtelfkg qlelddegyl kvaapstrtn lagvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala dgekaaepek taav
//
LOCUS       WP_126889963             332 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Curtobacterium].
ACCESSION   WP_126889963
VERSION     WP_126889963.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium
  ORGANISM  Curtobacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Curtobacterium"
                     /db_xref="taxon:2034"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34993
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqliiigsg pagftagiya araelkpliv assvetggel tkttevenfp gfpegiqgpd
       61 lmikmqeqae kfgaevlydd avsvdltgev kkvtvgsget yealaviyat gsayrhlgla
      121 deerlsghgv swcatcdgff frqkniavvg ggdsameeat fltrfadkvt vihrkdslra
      181 skimqdramn dpkiefawnk evtgitgdsa vegvtlrdtv tgeesslqld glfiaigndp
      241 rthlihgqid lapegtiavq grssrtnlpg vfaagdvidp tyrqaitaag sgtvaaldae
      301 kyladlddal vdqaegvtpe gpaiidveaa ra
//
LOCUS       WP_126904353             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Staphylococcus aureus].
ACCESSION   WP_126904353
VERSION     WP_126904353.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33499
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteidfdiai igagpagmta avyasranlk tvmiergipg gqmanteeve nfpgfemitg
       61 pdlstkmfeh akkfgavyqy gdiksvedkg eykvinfgnk eltakaviia tgaeykkigv
      121 pgeqelggrg vsycavcdga ffknkrlfvi gggdsaveeg tfltkfadkv tivhrrdelr
      181 aqrilqdraf kndkidfiws htlktinekd gkvgsvtlts tkdgseethe adgvfiyigm
      241 kpltapfkdl gitndvgyiv tkddmttsvp gifaagdvrd kglrqivtat gdgsiaaqsa
      301 aeyiehlndq a
//
LOCUS       WP_126907549             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            chutanense].
ACCESSION   WP_126907549
VERSION     WP_126907549.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium chutanense
  ORGANISM  Rhizobium chutanense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium chutanense"
                     /db_xref="taxon:2035448"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39071
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare iageetrvaa saetvkkmkg fgfdvvveag agaasripda efeaagarig
       61 sfadaaaadv vlkvrrpsps eisgyksgav viaimdpygn deaiaalasa gvsafamelm
      121 pritraqsmd vlssqanlag yqavieaagv ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vsramlssmk pgavavdlav erggniegvv
      301 ageiadvegv rvigfanmpg rvaasasaly aknlvtflet mvnketktvv vnlddelvka
      361 tmltyagdvv hpafggakkg dm
//
LOCUS       WP_126908103             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            chutanense].
ACCESSION   WP_126908103
VERSION     WP_126908103.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium chutanense
  ORGANISM  Rhizobium chutanense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium chutanense"
                     /db_xref="taxon:2035448"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55456
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtlrerl ddearvaltp dsasqlrklg hdavvetgag iragisdday raagvsvves
       61 aealvaaadv ivkvrppsey evsllsarkt lisffypaan kellegaras ganviamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqit aagkvpparv liigagvagl
      181 aaigtsvslg aityafdvrp evaeqiesmg aqfvyldfde qqadgavagg yaapsspefr
      241 qkqlakfrel apdidivitt alipghdapk lwsadmvaam kpgsvivdla aerggncelt
      301 vphqrvvsdn gvaiigytdf psrmaaqsas lystnirhmi adltprkdgv ivhdmeddii
      361 rgatvtfrgn itfpppppkv qaiavqkpke kakeltreet raaemasfrs atrtqiglll
      421 vggflmalvg ayappafmah fivfvlacfv gfqviwgvsh alhtplmait naisgiivlg
      481 allqigspgw lvpllgsvsv liatinivgg fmvtrrmlmm fqks
//
LOCUS       WP_126912278             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            chutanense].
ACCESSION   WP_126912278
VERSION     WP_126912278.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium chutanense
  ORGANISM  Rhizobium chutanense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium chutanense"
                     /db_xref="taxon:2035448"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55630
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeiy vgerrvaltp esavhlrklg yqclveagag ltsglsdday rtagvevvat
       61 aqdlwqgadv ivkvrppqqe elalltsgkt ilsfvhpaqn adlletarmr qvnliamdmv
      121 prisraqkmd alssmaniag yravieagns fgrfftgqvt aagkvapakv lvigagvagl
      181 aaigtstalg aityafdvrp evaeqiesmg aefvsldfae qqqdgaasgg yatpsspqfr
      241 naqlnkfrel apqidivist alipgrdapk lwladmvaam kpgsvvvdla aerggnceft
      301 iadqkvvtpn gvtivgytdf psrmaeqast lysnnirhli adltpnrdgr lvhdmeddvi
      361 rgatvahegi ityppppprv qaiatqkpre rakepspeer raqelaafrr qartqgllla
      421 sgtalllvvg amapasfmqh fvvfvlacfi gfqviwnvsh alhtplmavt navsgivivg
      481 allqigssng ivvtlaaisv lvatinivgg flvtrrmlsm fqks
//
LOCUS       WP_126922104             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            vallis].
ACCESSION   WP_126922104
VERSION     WP_126922104.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium vallis
  ORGANISM  Rhizobium vallis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rhizobium vallis"
                     /db_xref="taxon:634290"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55286
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigslkett erearvaltp dsarqliklg heclvesgag aksgfsdeay rsagivvved
       61 avalsaasdv lvkvrppqpd eldrlfagqt lisffypsqn erllqqaver gvntiamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aitlafdvrp evaeqiesmg aefvyldfag qqdgsasggy aapsspefre
      241 kqlskfrela pevdivitta lipgrdapkl wladmvaamk pgsvvvdlaa erggncdltr
      301 ldekvisdng vtiigytdfp srmaaqsssl yamnirhmla dltpgkdgkl vhnmdddvir
      361 gatvafdgsl tfpppppkvq aiaaqkprek aeeptaeerr aketaafkvq tknqgllllg
      421 gtalllvlga fapasfmahf vvfalacfvg fqviwnvshs lhtplmavtn avsgivilga
      481 llqvgssdwl vatlaaisia iatinivggf lvtrrmlamf qrs
//
LOCUS       WP_126923013             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            vallis].
ACCESSION   WP_126923013
VERSION     WP_126923013.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium vallis
  ORGANISM  Rhizobium vallis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium vallis"
                     /db_xref="taxon:634290"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39163
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare itdgetrvaa saetvkkmks fgfdvvveag agvasripda efeaagarig
       61 sfadaasadv vlkvrrpsas eisgyksgav viaimdpygn deaiaalasa glsafamelm
      121 pritraqsmd vlssqanlag yqavieaagi ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgraaprl vsrsmlasmk pgavavdlav erggniegvv
      301 adeiadiegv rvigfanmpg rvaasasaly aknlvtflet mvnkesrsav vnlddelvka
      361 tmltyagdvv hpafggakkg di
//
LOCUS       WP_126923542             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            vallis].
ACCESSION   WP_126923542
VERSION     WP_126923542.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium vallis
  ORGANISM  Rhizobium vallis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium vallis"
                     /db_xref="taxon:634290"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55544
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtprely tgesrvamtp dsalqlqklg yecvveagag kaagftdday rsagvavved
       61 aaalyaradv vakvrppeas evehlrpgqt llsffypaqn ndlleqakgr ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfkd qqedgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvamm kpgsvivdla aerggncdlt
      301 iadqkvvsan gvivigytdf psrmaaqasm lystnirhmm tdltpakdgk ivhnmeddvi
      361 rgatvafese itfpppppkv raiaaqkpke kikeltpeek raseaaafaa qtrsqglmlv
      421 igtallllvg avapasfmsh fvvfvlacfv gfqiiwnvsh slhtplmavt navsgivilg
      481 allqigsgnw lvvtlaalsv liatvnivgg flvtrrmlam fqks
//
LOCUS       WP_126924228             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhizobium vallis].
ACCESSION   WP_126924228
VERSION     WP_126924228.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium vallis
  ORGANISM  Rhizobium vallis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rhizobium vallis"
                     /db_xref="taxon:634290"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34620
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mparhtkvli igsgpagyta avyaaramlk pvliagleqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlq qakhvgaeiv ndlvtevdmn qrpfvartds gqvwtadtli iatgakakwl
      121 gieseqhfqg fgvsacatcd gffyrkkdvi vvgggnsave ealylsniak svtlvhrrds
      181 fraekilqer lfakenvkvl wntevaeitg apakppmpps vsgarlrdvr tgtitempid
      241 gvfvaighap atelfkgklk lkdngylwta pdstatsleg vyaagdvtdd tfrqaitaag
      301 lgcmaaleae ryltghmpva vaae
//
LOCUS       WP_126926860             348 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Rothia].
ACCESSION   WP_126926860
VERSION     WP_126926860.1
KEYWORDS    RefSeq.
SOURCE      Rothia
  ORGANISM  Rothia
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Rothia"
                     /db_xref="taxon:32207"
     gene            1..348
                     /gene="trxB"
     Protein         1..348
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36678
     Region          44..347
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstntttggl fgnaalggvr lgaastkpeg astsaaeqge qtvhnviivg agpagytaai
       61 yaaranlspv lfassvspgg almntteven fpgfiegiqg pelmtnigaq aerfgtdiry
      121 qdvekldltg evkkvilsdg svhlaktvil stgseyrklg vegedrlsgy gvswcatcdg
      181 fffkekdiav vgggdsalee alflttfark vyiihrrdsf rasdimqkra fenpkievlw
      241 dsevsaidgd snlekvtlkn tkdgserelp lnglfiaigs dprvdmvkdq ltlseqgtie
      301 vqgrssktsv pgvfaagdvi dptyrqaiia agsgavaald aqhyienm
//
LOCUS       WP_126946085             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Vreelandella andesensis].
ACCESSION   WP_126946085
VERSION     WP_126946085.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella andesensis
  ORGANISM  Vreelandella andesensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Vreelandella andesensis"
                     /db_xref="taxon:447567"
     Protein         <1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..519
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 gapketaqge arvaltpesa tqlqklghec lveagagvaa gfnddtyrda gvsvvesaea
       61 lwrdadvvik vrepsekeah ylregqtlia ffwpaqndal letckaqgas viamdmvpri
      121 sraqkmdals smaniagyra vieagnnfgr fftgqvtaag kvppakvlvi gagvaglaai
      181 gtatslgavv rafdvrpevs eqiesmgaef lfldfedsqd gsesggyasp sspefrekql
      241 acfreqapdv divittalip grpapklwle dmvaamkpgs viidlaaekg gncdltkpde
      301 rvvsdngvvv vgytdfpsrm atqasllyat nirhmltdlt pekdgvihhn meddvirgat
      361 vthqgeitfp ppppkvkaia aakpkkkeka ptpeekkaae latfkaqtkr qagllavggv
      421 lmlllgqiap asfmqhfivf vlacfigfqv iwkvshslht plmavtnais giiilgailq
      481 igsgssvviv laaisvlias inivggflvt rrmlamfqks
//
LOCUS       WP_126948071             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Vreelandella andesensis].
ACCESSION   WP_126948071
VERSION     WP_126948071.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella andesensis
  ORGANISM  Vreelandella andesensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Vreelandella andesensis"
                     /db_xref="taxon:447567"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55413
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapketa qgearvaltp esatqlqklg heclveagag vaagfnddty rdagvsvves
       61 aealwrdadv vikvrepsek eahylregqt liaffwpaqn dalletckaq gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfed sqdgsesggy aspsspefre
      241 kqlacfreqa pdvdivitta lipgrpapkl wledmvaamk pgsviidlaa ekggncdltk
      301 pdervvsdng vvvvgytdfp srmatqasll yatnirhmlt dltpekdgvi hhnmeddvir
      361 gatvthqgei tfpppppkvk aiaaakpkkk ekaptpeekk aaelatfkaq tkrqagllav
      421 ggvlmlllgq iapasfmqhf ivfvlacfig fqviwkvshs lhtplmavtn aisgiiilga
      481 ilqigsgssv vivlaaisvl iasinivggf lvtrrmlamf qks
//
LOCUS       WP_126949208             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vreelandella andesensis].
ACCESSION   WP_126949208
VERSION     WP_126949208.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella andesensis
  ORGANISM  Vreelandella andesensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Vreelandella andesensis"
                     /db_xref="taxon:447567"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33683
     Region          3..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 metrherlii lgsgpagyta avyaaranlk pllitglqag gqlttttdvd nwpgdaqgvq
       61 gpelmermkq haerfntevl fdhinevslg ekpytlkgds giytcdalii atgasarylg
      121 lpteqqfmgq gvsacatcdg ffyrnqeviv vgggntavee alylsniask vtlvhrrdtl
      181 raekilqdkl fekveagkia lewfyevdev lgdntgvtgv rvkstkdgss keihapglfi
      241 aighspntgi fegqlemngg yikvksgleg natatsvpgv facgdvmdhi yrqaitsags
      301 gcmaaldaer yldgia
//
LOCUS       WP_126949255             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Xanthomonas vesicatoria].
ACCESSION   WP_126949255
VERSION     WP_126949255.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas vesicatoria
  ORGANISM  Xanthomonas vesicatoria
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Xanthomonas vesicatoria"
                     /db_xref="taxon:56460"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34324
     Region          14..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msassaspak hsrllilgsg pagwtaavya aranlkpvvi tglqqggqlm tttevdnwpg
       61 dphglmgpdl mnrmqahaer fetevifdhi htsdlsqrpf rligdsaeyt cdaliiatga
      121 takylgipte eafkgrgvsa catcdgffyk dqdvvvvggg ntaveealyl sniarkvylv
      181 hrrdtlraek imqdklfakv aagkietvwh haieevlgnd agvtgvrvks tldgstrdid
      241 ahgffvaigh hpntqlfdgq lvmnngylei rsglngaate tsvagvfaag dvadqhyrqa
      301 itsagfgcma aldaeryldk sa
//
LOCUS       WP_126950182             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vreelandella populi].
ACCESSION   WP_126950182
VERSION     WP_126950182.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella populi
  ORGANISM  Vreelandella populi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Vreelandella populi"
                     /db_xref="taxon:2498858"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34472
     Region          8..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 metrherlii lgsgpagyta avyaaranlk pllitgmqag gqlttttdvd nwpgdaegvq
       61 gpelmermka haerfntevl fdhinevslr ekpftlkgds atytcdaliv atgasarylg
      121 lpteqqfmgq gvsacatcdg ffyrnqevvv vgggntavee alylsniask vtlvhrrdsl
      181 raekilqdrl fekvaagtma lewfqeidev lgdntgvtgv rlkstldgst kelhapglfi
      241 aighspntgi fegqlamndg yikvnsgleg natatsvpgv facgdvmdhi yrqaitsags
      301 gcmaaldaer yldgiawped ste
//
LOCUS       WP_126952207             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Vreelandella populi].
ACCESSION   WP_126952207
VERSION     WP_126952207.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella populi
  ORGANISM  Vreelandella populi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Vreelandella populi"
                     /db_xref="taxon:2498858"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55507
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigapkets rgearvaltp esakqiqklg heclietgag laagfnddty rdagvtvvdd
       61 admlwqdaev vikvrepsdt eaarlrqgqt liaffwpaqn eallekcraq gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfed sqdgsesggy aspsspefre
      241 kqlecfreqa pdvdivitta lipgrpapkl wledmvaamk pgsvivdlaa ekggncdltq
      301 pderivsdng vivvgytdfp srmatqssll yatnirhmlt dltpgkdgvi nhnmdddvir
      361 gatvahqgev tfpppppkvk aiaaakpkkk ekeptpeekk aaeatafkaq tkrqvgilai
      421 ggalmlllgq vapasfmqhf ivfvlacfig fqviwkvshs lhtplmavtn aisgiiilga
      481 ilqigsgsav vsvlaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_126953032             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Legionella septentrionalis].
ACCESSION   WP_126953032
VERSION     WP_126953032.1
KEYWORDS    RefSeq.
SOURCE      Legionella septentrionalis
  ORGANISM  Legionella septentrionalis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Legionella septentrionalis"
                     /db_xref="taxon:2498109"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34108
     Region          7..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msatnhhrli ilgsgpagyt aavyaaranl qpvlltgmqp ggqlttttdv dnwpgdvegl
       61 qgpalmermq qhaerfqtei ifdhitradl lsrpftlegd tqtytcdali iatgasaryi
      121 glesekayqg rgvsacatcd gffyrnkhvc vvgggntave ealylsnlaa svtlihrrds
      181 lraekilqnk lfekartgni kllwnhtlqe vlgdgmkvtg arvcnvftda ctdlpvdgif
      241 iaightpnts lftdqldmkd gyliirsgle gmatatnipg vfacgdvadh vyrqaitsag
      301 fgcmaaldae kyldtvr
//
LOCUS       WP_126960352             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Cohnella sp. AR92].
ACCESSION   WP_126960352
VERSION     WP_126960352.1
KEYWORDS    RefSeq.
SOURCE      Cohnella sp. AR92
  ORGANISM  Cohnella sp. AR92
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Cohnella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Cohnella sp. AR92"
                     /db_xref="taxon:648716"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33691
     Region          5..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mfksivigtg pagltaaiyl aranlnplvi egpepggqlt tttevenfpg fpegimgpdl
       61 manmrkqaer fgaefrtgwi nsvdlskrpf tldleggekl qaetliistg asakylgipg
      121 ekdnvgrgvs tcatcdgfff rnkkivvvgg gdsameeanf ltrfasdltl vhrrdelras
      181 kimqdrvken pkvslglnrt plevvandqg vtglkvfnna tgqeevieah gvfvaightp
      241 ntkflggqve tdehgyivtk pgssetsieg vfacgdvqdt kyrqaitaag sgcmaaldce
      301 rflessavhd wsqtlg
//
LOCUS       WP_126964449             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium perfringens].
ACCESSION   WP_126964449
VERSION     WP_126964449.1
KEYWORDS    RefSeq.
SOURCE      Clostridium perfringens
  ORGANISM  Clostridium perfringens
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Clostridium perfringens"
                     /db_xref="taxon:1502"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34209
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdkeikeldl iiigagpagl tsaiyasrak lstlvlednl vggqvrstyt venypgftei
       61 tgndladriq aqaeacgaii defdfienvs lkddekiiet gdyiykpkav iiatgatpkk
      121 lpipseskyl gkgvhycavc dgavyqdevv avvgggnaal eealylsniv kkvivirryd
      181 yfraeaktle vasnkeniei mynwdlvdvl ggefveaari kntktgeeke iaingvfgyi
      241 gtepktsmfr eyinvkengy iegdenmrtn vkgvyvagdv rekmfrqitt avsdgtiaal
      301 haekyiseik er
//
LOCUS       WP_126971874             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gynurincola endophyticus].
ACCESSION   WP_126971874
VERSION     WP_126971874.1
KEYWORDS    RefSeq.
SOURCE      Gynurincola endophyticus
  ORGANISM  Gynurincola endophyticus
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Gynurincola.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Gynurincola endophyticus"
                     /db_xref="taxon:2479004"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34050
     Region          8..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meserihcli igsgpagyta aiyaaranmk pvlyqglqpg gqltitteve nypgypdgvq
       61 gpdmmqdlek qakrmgadir wglatkvdfs qkpykvwide dhlieadavi istgasakwl
      121 gleseqrlng fgvsacavcd gfffkgkeva ivgagdtaae ealylsklct nvhmfvrkdh
      181 mraskvmqdr vlatpnikvy wntetdevlg ekrtegvrir niltgekqei pisgffvaig
      241 hqpnsdifkp winmdeagyi ltqpgtsktn megifaagdv qdkiyrqait aagsgcmaal
      301 daerylsvnn iv
//
LOCUS       WP_126975793             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Frigidibacter oleivorans].
ACCESSION   WP_126975793
VERSION     WP_126975793.1
KEYWORDS    RefSeq.
SOURCE      Frigidibacter oleivorans
  ORGANISM  Frigidibacter oleivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Frigidibacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Frigidibacter oleivorans"
                     /db_xref="taxon:2487129"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54900
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigspresh egearvaltp dsaaqlkklg hdclveagag maagitdaay eaagvtvlpd
       61 aaalyaaadv vakvrpptea evdllrpgqt lisffypaqn tellerakar gatvvamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqvt aagkvpparv lvvgagvagl
      181 aaigtatslg aitlafdvrp evaeqiesmg aefvyldfae qqtdgaatgg yaapsspefr
      241 eaqlkkfrel apsvdivitt alipgrpapk lwtedmvamm kpgsvivdla aerggncdlt
      301 vpdqkivspn gvtvvgytdf psrmaaqast lyatnirhmm tdltpgkdgv ivhnmeddvi
      361 rgatvttage itfpppppkv aaiaaqkpke kvkeptpeer raaevaafka qtrnqvglla
      421 vgavlmlglg mvapasfmqh fivfvlavfv gfqviwnvsh slhtplmavt naissiiilg
      481 almqigsgsf lvillaalsi fmaginifgg flvtrrmlam fqks
//
LOCUS       WP_126976150             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Frigidibacter oleivorans].
ACCESSION   WP_126976150
VERSION     WP_126976150.1
KEYWORDS    RefSeq.
SOURCE      Frigidibacter oleivorans
  ORGANISM  Frigidibacter oleivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Frigidibacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Frigidibacter oleivorans"
                     /db_xref="taxon:2487129"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33434
     Region          8..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mgetrhskvl iigsgpagyt aavyaaraml kpvlvqgiqp ggqltittdv enwpgeaqim
       61 gpdlmvkmed haramgtevv gdiiltldls rrpfvavgds gttytadavi latgaqakwl
      121 glpseekfkg fgvsacatcd gffyrgkevv vigggntave ealfltnfas kvtlvhrrdt
      181 lraerimqer lfahpkvell wnhevtevlg tetplgvtgv rardvrtgat tdvpcagffv
      241 aighhpasel vkdqlelhsg gyvkvepgst atsvpgvfaa gdltdhvyrq avtsagmgcm
      301 aaldaerwla aqglaeg
//
LOCUS       WP_126980723             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Saezia sanguinis].
ACCESSION   WP_126980723
VERSION     WP_126980723.1
KEYWORDS    RefSeq.
SOURCE      Saezia sanguinis
  ORGANISM  Saezia sanguinis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Saeziaceae; Saezia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Saezia sanguinis"
                     /db_xref="taxon:1965230"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34156
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maqhakilil gsgpagytaa iyaaranlsp vlvtglaqgg qlmtttevdn wpadvmgvqg
       61 pdlmqrfleh aerfktqiif dhihtvdlqh rpftlkgdgd tytcdtliia tgasarylgl
      121 pseeafkgkg vsacatcdgf fyreqdvcvv gggnsaveea lylsniarlv tvihrrdkfr
      181 aeaimvdklm dkvkegkikl mlnaeldevl gdqtgvtgvr vrnkdsgqtq dlkvqgcfva
      241 ighhpnteif anqldmkngy ittrgggegh atmtsvpgvf aagdvqdqvy rqaitsaatg
      301 cmaaldaqry leengldn
//
LOCUS       WP_126985988             357 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Brachybacterium].
ACCESSION   WP_126985988
VERSION     WP_126985988.1
KEYWORDS    RefSeq.
SOURCE      Brachybacterium
  ORGANISM  Brachybacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Dermabacteraceae.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Brachybacterium"
                     /db_xref="taxon:43668"
     gene            1..357
                     /gene="trxB"
     Protein         1..357
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=37648
     Region          33..334
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqpiqalni lggpapaaqp lvqpvanddg tvhevvivgs gpagytaaiy taraemkpiv
       61 iagaldagga lmtttdvenf pgfpegvqgp elmasfqeqa erfgaevvye davdlqldgd
      121 vkkvtledgt vyraksliit tgsayrklgi dgeadlsgkg vswcatcdgf ffkdqdivvv
      181 gggdsaveea tfltrfgksv tlvhrrdalr askimarrae adpkltfawn seivringrd
      241 kvesvtlrdt vtgeerdlvt savfeaighl prtdlvrgkl elddegyivc qgrstftsvp
      301 gvfaagdvvd htyrqaitaa gtgcqaalda erwladraag idaaadaeqp vveavsq
//
LOCUS       WP_126992724             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thermosipho globiformans].
ACCESSION   WP_126992724
VERSION     WP_126992724.1
KEYWORDS    RefSeq.
SOURCE      Thermosipho globiformans
  ORGANISM  Thermosipho globiformans
            Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
            Fervidobacteriaceae; Thermosipho.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Thermosipho globiformans"
                     /db_xref="taxon:380685"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33895
     Region          17..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvhfdlgnis tgpkdyydil iigggpaglt aaiyagragl saavfekale ggavtqthvv
       61 enwpgfirie ggelgekfae hakafgaeii taevlkisyd neykyveldn gkkvkgkvli
      121 yatgavprkl gvpgeeefrg kgvtycaacd gylfsgkdvv vvgggdsacd eahflakmvk
      181 sitmvqnlpy ltaakvlqdr llenknvkvi lnslvkeirg kdkveevvvv nnetgeetvi
      241 kaegvfiyvg lvpksdllkg ivdineygyi ktdenmetnv pgiyavgdvr eknlrqivta
      301 aadgaiaveh aakkyf
//
LOCUS       WP_126994326             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Azospirillum doebereinerae].
ACCESSION   WP_126994326
VERSION     WP_126994326.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum doebereinerae
  ORGANISM  Azospirillum doebereinerae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Azospirillum doebereinerae"
                     /db_xref="taxon:92933"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35443
     Region          7..319
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpsthhtkvl iigagpagyt aaiyaaranl eplmvqgmqp ggqlmittdv enypgfadpi
       61 qgpwlmeqmq kqaehvgtkm vfdlitevdf tqrpfvckgd sgdtytadsv iiatgaqarw
      121 lgisseeiyr gagvsacatc dgfffrgkev avigggnsav eealyltnha tkvtvihrrd
      181 sfraerimqd rlfrhpkiev vwdsaveeiv gegdgslgnp rgvtgvrvkn vktgeprvip
      241 aagvfvaigh epatavfkgk vamdeagyiv ttpdstatdv vgvfaagdvk dkvyrqavta
      301 agmgcmaale aerwlahhep aagahgdrsp agtw
//
LOCUS       WP_126994593             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus lutimineralis].
ACCESSION   WP_126994593
VERSION     WP_126994593.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus lutimineralis
  ORGANISM  Paenibacillus lutimineralis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paenibacillus lutimineralis"
                     /db_xref="taxon:2707005"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33918
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksivigtg psgltaaiyl aranlnplvi egvqpggqlt tttevenfpg fpegilgpel
       61 mdrmrkqaer fgaefkngwv kkvdfsdkpl rltleggeel tsetvivstg asarylgipg
      121 eqdnvgrgvs tcatcdgfff rgkgiivvgg gdsameeagf ltrfatsvtv vhrrdelras
      181 kimqervrkn ekvkwalnri plevatddgg aviglkvrnn angqeeliea egvfvaight
      241 pntkflegvv ktdehgyivv apgttrtsip gvfacgdvqd thyrqaitaa gsgcmaamdc
      301 ekylegdmvh dwskml
//
LOCUS       WP_127021204             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flagellimonas beolgyonensis].
ACCESSION   WP_127021204
VERSION     WP_127021204.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas beolgyonensis
  ORGANISM  Flagellimonas beolgyonensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Flagellimonas beolgyonensis"
                     /db_xref="taxon:864064"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34477
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseqvervkt liigsgpagy taaiyasrad lkpvlytgme pggqltttte vdnfpgypeg
       61 idgptmmiql qqqaerfgtd vrigmvtaat fsdevggihk vtiddskqie aetviistga
      121 takylnipse qrlrgggvsa cavcdgffyk gqevaivgag dtaaeeasyl anickkvtml
      181 vrkdhmrask amqhrvnsie nieilyntev devlgdqvve glrivnnqtn ekseisvtgl
      241 fiaighkpnt difkgqldmd etgyiitqpk stktnkpgvf asgdaqdkiy rqavtaagtg
      301 cmaaldaery laaveskeml ts
//
LOCUS       WP_127016218             403 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Anoxybacter fermentans].
ACCESSION   WP_127016218
VERSION     WP_127016218.1
KEYWORDS    RefSeq.
SOURCE      Anoxybacter fermentans
  ORGANISM  Anoxybacter fermentans
            Bacteria; Bacillati; Bacillota; Clostridia; Halanaerobiales;
            Anoxybacter.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Anoxybacter fermentans"
                     /db_xref="taxon:1323375"
     gene            1..403
                     /gene="trxB"
     Protein         1..403
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=44177
     Region          21..290
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
     Region          309..402
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mnkeydllii gggpaglaag iygsraklkt aiiekkrkpg gqaatteeme nypgfaqgtt
       61 gpeltkrmae hakafgaefi rtealeikce gdkrivktrd gdlvtktvii atgaeprvlg
      121 vkgegefrgr gvsycatcda dfytdldvvv vgngdaavee aiyltrfark vtiivvhdeg
      181 imdatkviqe rayanpkidf vwnsvleevv gdevvtgvki knlktgeite mpcdgvfffv
      241 gtvpktdfvk dliemddfgy iitndkmetn vpgifaagdv rqkylrqvvt aaadgaiaat
      301 aaekyiaeee gfktdvlnad kpvlvifwsp tvestfdtin mlenlgleek nvklvkidty
      361 knrliadrye ikniptllyf vdgelknrle dvtkenvlki ieg
//
LOCUS       WP_127002674             316 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Paenibacillus].
ACCESSION   WP_127002674
VERSION     WP_127002674.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33901
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myktiiigtg pagltaaiyl aranmkplvi egpqpggqlt tttdvenfpg fpdgimgpvl
       61 menmrkqaer fgaefrtgwv nsvdmsrrpf kldvdglgel eaetlvlstg asakylgipg
      121 eqdnvgrgvs tcatcdgfff rnreiivigg gdsaleeagf ltrfaskvtv vhrrdelras
      181 kimqdrvrsn ekvewaldrt plevvtndmg vtglkvrnna tgeeevisat gvfvaightp
      241 ntgflggqid tdengyiivk pgtsetnvpg vfacgdvqdt ryrqaitaag sgcmaaldce
      301 kyiealeheq kelatk
//
LOCUS       WP_127022041             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rheinheimera mangrovi].
ACCESSION   WP_127022041
VERSION     WP_127022041.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera mangrovi
  ORGANISM  Rheinheimera mangrovi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Rheinheimera mangrovi"
                     /db_xref="taxon:2498451"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33727
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mstikhsrll ilgsgpagyt aavyaaranl npvlltgmqa ggqlttttev enwpgdphgl
       61 tgpalmdrmk ahaetfntei lfdhihtvdf qqrpfiltgd ngqyscdali iatgasakyl
      121 glpseqtyng rgvsacatcd gffyrnqkva vvgggntave ealylanias evhlvhrrdt
      181 fkaekilvdr lmakvasgni ilhthrelee ilgddmgvng mrlkstngqp tedvavagvf
      241 iaighkpntd ifagqlemng gylkvqsgte gnatqtsieg vfaagdvsdh iyrqaitsag
      301 tgcmaaldae ryldalak
//
LOCUS       WP_127024400             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rheinheimera mangrovi].
ACCESSION   WP_127024400
VERSION     WP_127024400.1
KEYWORDS    RefSeq.
SOURCE      Rheinheimera mangrovi
  ORGANISM  Rheinheimera mangrovi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Chromatiales; Chromatiaceae; Rheinheimera.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Rheinheimera mangrovi"
                     /db_xref="taxon:2498451"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53477
     Region          1..507
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mfiaipkekl qdetrvaatp atteqlqklg fsvllesgag aaagfsdeay iqagasvads
       61 aklwaseliy kvnaptdqei sllqkgstlv sfiwpaqnpd lvarlaaqgi nvlamdmvpr
      121 israqsldal ssmsniagyr avieaahsfg rflsgqitaa gkvqpakvlv igagvaglaa
      181 igaarslgsi vrafdtrlev aeqieslgge flklefaedg ssssgyakvm seefiaaema
      241 lfadqakevd iiittalipg rpapklitka mvdsmkpgsv ivdlaaatgg nceytvtgqi
      301 tetasgvkvi gytdlpgrla aqssqlygtn lvnlakllck tkdgqmvldm qdviirnmsv
      361 vhqgevtfpp paisvtaaak pvaapekpaa ktpkksintn wfigvaalll lwigysapsd
      421 flahftvfll scvvgyylvw nvthalhtpl msvtnaisgi ivlgallqis sdsllvqvla
      481 fvavmiasin ivggftvtqr mlkmftkgge
//
LOCUS       WP_127027484             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Candidatus
            Methylobacter oryzae].
ACCESSION   WP_127027484
VERSION     WP_127027484.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Methylobacter oryzae
  ORGANISM  Candidatus Methylobacter oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylobacter.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Candidatus Methylobacter oryzae"
                     /db_xref="taxon:2497749"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55429
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipkeih pgekrvattp eaaeqiiklg fsvllesgag leanisdeay qevgveives
       61 aktlwksadi vmkvrapeqh pelaldeidl lpeggrlisf iwpaqneelm qklaaknatv
      121 lamdsvprms raqkldalss maniagyrav ieaaqhfgrf ftgqitaagk ippakvlvig
      181 agvaglaaig aakgmgaivr afdtrpevke qiesmdaefl mldfkeegsg tggyakvmsk
      241 efieaemalf arqamevdii ittalipgkp apklitegmv esmkpgsviv dlaseqggnc
      301 altekdkvvv khgvtiigyt dlpsrlanqa sqlygtnlrh lltdlcpdkn geinvnmdde
      361 virgatvike gkitwppppp klsaapapqt eapaykteqe pkksiipcwl kqliplaigg
      421 aalfgigava pasfmthftv fvlacfvgyq viwnvtpalh tplmsvtnai sgiivigali
      481 qvsapdqniq ilaglailia siniaggflv trrmlemfrk
//
LOCUS       WP_127026793             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Candidatus Methylobacter oryzae].
ACCESSION   WP_127026793
VERSION     WP_127026793.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Methylobacter oryzae
  ORGANISM  Candidatus Methylobacter oryzae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Methylococcales; Methylococcaceae; Methylobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Candidatus Methylobacter oryzae"
                     /db_xref="taxon:2497749"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33803
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msnpkhcrll ilgsgpagyt aaiyaaranm npviitgmqq ggqlttttev dnwpgdiegl
       61 qgpalmerml khaerfntei ifdhihtadl sarpftltgd sgtytcdali iatgasaryl
      121 gmeseeafkg kgvsacatcd gffyrnkpva vigggntave ealylanias kvivvhrrdk
      181 frsekilsdk lieksqngnv siewnsqlde vlgddmgvtg lriknvqdgs tkeldvhgvf
      241 iaightpntg ifegqlemeh gyikvksgih gnatatsveg vfaagdvmds vykqaitsag
      301 agcmaaldae kfldelvg
//
LOCUS       WP_127032451             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Legionella].
ACCESSION   WP_127032451
VERSION     WP_127032451.1
KEYWORDS    RefSeq.
SOURCE      Legionella
  ORGANISM  Legionella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Legionella"
                     /db_xref="taxon:445"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34109
     Region          7..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msatnhhrli ilgsgpagyt aavyaaranl qpvlltgmqp ggqlttttdv dnwpgdvegl
       61 qgpalmermq qhaerfqtei ifdhitradl lsrpftlegd tqtytcdali iatgasaryi
      121 glesekayqg rgvsacatcd gffyrnkhvc vvgggntave ealylsnlaa svtlihrrds
      181 lraekilqdk lfekartgni kllwnhtlqe vlgdgmkvtg arvcnvftda ctdlpvdgif
      241 iaightpnts lftdqldmkd gyliirsgle gmatatnipg vfacgdvadh vyrqaitsag
      301 fgcmaaldae kyldtvr
//
LOCUS       WP_127039289             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vreelandella populi].
ACCESSION   WP_127039289
VERSION     WP_127039289.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella populi
  ORGANISM  Vreelandella populi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Vreelandella populi"
                     /db_xref="taxon:2498858"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34485
     Region          8..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 metrherlii lgsgpagyta avyaaranlk pllitgmqag gqlttttdvd nwpgdaegvq
       61 gpelmermka haerfntevl fdhinevslr ekpftlkgds atytcdaliv atgasarylg
      121 lpteqqfmgq gvsacatcdg ffyrnqevvv vgggntavee alylsnmask vtlvhrrdsl
      181 raekilqdrl fekvaagnma iewfqeidev lgdntgvtgv rlkstldgst kelhapglfi
      241 aighspntgi fegqlamndg yikvnsgleg natatsvpgv facgdvidhi yrqaitsags
      301 gcmaaldaer yldgiawped ste
//
LOCUS       WP_127047552             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudorhodobacter sp. E13].
ACCESSION   WP_127047552
VERSION     WP_127047552.1
KEYWORDS    RefSeq.
SOURCE      Pseudorhodobacter sp. E13
  ORGANISM  Pseudorhodobacter sp. E13
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudorhodobacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pseudorhodobacter sp. E13"
                     /db_xref="taxon:2487931"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33388
     Region          8..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maetrhskil iigsgpagyt aavyaaramt npilvqglqp ggqltittev enwpgdthvq
       61 gpdlmvrmee hakamgaevi sdyissldls krpftakads gttftadavi latgaqakwl
      121 glpseekfkg fgvsacatcd gffyrgkevv vigggntave ealfltnfat kvtlihrrds
      181 lraekimqdr lfkhpkvevl wnhsveevlg detprgvtav rakhvetget tdipcagffv
      241 aighapasel vkdqlelhng ayvkvkpgst qtsipgvfaa gdltdhvyrq avtsagmgcm
      301 aaldaerfla eqe
//
LOCUS       WP_127048770             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudorhodobacter sp. E13].
ACCESSION   WP_127048770
VERSION     WP_127048770.1
KEYWORDS    RefSeq.
SOURCE      Pseudorhodobacter sp. E13
  ORGANISM  Pseudorhodobacter sp. E13
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pseudorhodobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Pseudorhodobacter sp. E13"
                     /db_xref="taxon:2487931"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55673
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egearvamtp dsakllqklg hscvietgag ekagfsdkay edagvevvkt
       61 aaalfkaadi ivkvrgpepk eakmlgegqt lisffwpaqn eklleqmkkq gttaiamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aqfvylefda selpdgaatg gyaapstpef
      241 qakqlakfre lapdidivit talipgrpap klwtkdmvem mkpgsvivdl aaerggncdl
      301 tvmdqkvvtd ngvtivgytd fpsrmaaqas tlysnnirhm ladltpgkdg vinhnmeddv
      361 irgatvahqg eitfpppppk vaaiavqkpk ekakeltpee krakevaafk aqtrnqvgll
      421 avggglllla gmftpasfma hfivfvlacy vgfqviwnvs hslhtplmav tnaissiiil
      481 gallqigsgs wlvivlasls vfmaginifg gfmvtrrmla mfqks
//
LOCUS       WP_127050945             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Labedella endophytica].
ACCESSION   WP_127050945
VERSION     WP_127050945.1
KEYWORDS    RefSeq.
SOURCE      Labedella endophytica
  ORGANISM  Labedella endophytica
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Labedella.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Labedella endophytica"
                     /db_xref="taxon:1523160"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34649
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrnviiigsg pagytaaiya araglepvll assveaggdl mntteienfp gfpdavmgpe
       61 lmakfqeqae kfgtevildd vteldlrget ktiktgysgd fegrtvifat gsayrklgig
      121 dedrlsgrgv swcatcdgff fkgkeiavvg ggdsameeat fltrfaskvy vihrrdslka
      181 skimqdraft nekiefvwns evagivgdna vegvvlrdtv dgterqlaig glfvaigndp
      241 rthlihgqld ltdegtiavd grssrtnlpg vfaagdvidp hyrqaitaag sgtvaaldae
      301 hylsalddaa kldeegetae adaliasa
//
LOCUS       WP_127052145             452 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Trichormus variabilis].
ACCESSION   WP_127052145
VERSION     WP_127052145.1
KEYWORDS    RefSeq.
SOURCE      Trichormus variabilis
  ORGANISM  Trichormus variabilis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Trichormus.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Trichormus variabilis"
                     /db_xref="taxon:264691"
     gene            1..452
                     /gene="trxB"
     Protein         1..452
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=49096
     Region          9..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
     Region          353..449
                     /region_name="TRX_NTR"
                     /note="TRX domain, novel NADPH thioredoxin reductase (NTR)
                     family; composed of fusion proteins found only in oxygenic
                     photosynthetic organisms containing both TRX and NTR
                     domains. The TRX domain functions as a protein disulfide
                     reductase via the reversible...; cd02949"
                     /db_xref="CDD:239247"
     Site            order(377,380)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239247"
ORIGIN      
        1 mansmvenlv iigsgpagyt aaiyagranl kpvvfegfqa gglpggqlmt ttevenfpgf
       61 pqgitgpelm dnmkaqaerw gaqlytedvi svdlsqrpfi irsqerevka hslviatgat
      121 akrlglpseh efwsrgisac aicdgatpif rgaelaviga gdsaaeeaiy ltkygskvnl
      181 lvrsekmras kamqdrvlsn pkiqvhwhte avdvfgnglm agvkvrnnqt gevselsakg
      241 lfyavghkpn tslfqgqlel devgyittkh ggvetsidgv faagdvqdhe frqaitaagt
      301 gcmaamlaer wlsakgliqe fhqiqseele aqpeetktet aaefdlqatr heggyalrkl
      361 fhesdrlmlv kyvspgcgpc htlkpilnkv vdefdgkihf veididkdrd iaenagvtgt
      421 ptvqlfknqe lvkeikgvkq kseyrqlies nl
//
LOCUS       WP_127054627             384 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Trichormus
            variabilis].
ACCESSION   WP_127054627
VERSION     WP_127054627.1
KEYWORDS    RefSeq.
SOURCE      Trichormus variabilis
  ORGANISM  Trichormus variabilis
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Nostocaceae; Trichormus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Trichormus variabilis"
                     /db_xref="taxon:264691"
     Protein         1..384
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40666
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeie vcerrvalip dtvarlvkqg levfveagag ekaffsdsdy eaagakiisd
       61 taqlwreadv llkvsppqer edgrseidll ksgsvlisfl nplgnpvvaq klanrqital
      121 smeliprttr aqsmdalssq aslagykavl iaaaalpkyf pmlttaagti apakvfimga
      181 gvaglqaiat arrlgavvea fdirpavkee vqslgakfve vkleeetvaa ggyakeised
      241 skkrtqelva ehvknsdvvi ttaqvpgrka pqlvtqemva qmkpgsvivd laaeqggnca
      301 cteagkdiiw ngvtiigpin lpssmpvhas qlyaknvtsl mqllikdkal einfgddivd
      361 aacvthggei rnqrvkdalq avav
//
LOCUS       WP_127060498             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Vreelandella nanhaiensis].
ACCESSION   WP_127060498
VERSION     WP_127060498.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella nanhaiensis
  ORGANISM  Vreelandella nanhaiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Vreelandella nanhaiensis"
                     /db_xref="taxon:1258546"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33685
     Region          3..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 metrherlii lgsgpagyta avyaaranlk pllitgmqag gqlttttdvd nwpgdaegvq
       61 gpelmermka haerfntevl fdhinevslr ekpftlkgds gtytcdaliv atgasarylg
      121 lpteqqfmgq gvsacatcdg ffyrnqeviv vgggntavee alylsniask vtlvhrrdsl
      181 raekilqdrl fekvaagtma lewfqeidev lgdntgvtgv rlrstldgst kelhapglfi
      241 aighspntgi fegqltmndg yikvnsgleg natatsvpgv facgdvmdhi yrqaitsags
      301 gcmaaldaer yldgia
//
LOCUS       WP_127060704             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Vreelandella nanhaiensis].
ACCESSION   WP_127060704
VERSION     WP_127060704.1
KEYWORDS    RefSeq.
SOURCE      Vreelandella nanhaiensis
  ORGANISM  Vreelandella nanhaiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Halomonadaceae; Vreelandella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Vreelandella nanhaiensis"
                     /db_xref="taxon:1258546"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55523
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigapkets rgearvaltp esakqiqklg heclietgag laagfndday rdagvtvvds
       61 adtlwqdaev vikvrepsdt eaarlrqgqt liaffwpaqn eallekckaq gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg avvrafdvrp evseqiesmg aeflfldfed sqdgsesggy aspsspefre
      241 kqlecfreqa pdvdivitta lipgrpapkl wledmvaamk pgsvivdlaa ekggncdltq
      301 pderivsdng vivigytdfp srmatqssll yatnirhmlt dltpekdgvi nhnmdddvir
      361 gatvthqgev tfpppppkvk aiaaakpkkk ekeptpeekk ateasafkaq tkrqvgilai
      421 ggalmlllgq vapasfmqhf ivfvlacfig fqviwkvshs lhtplmavtn aisgiiilga
      481 ilqigsgsav vsvlaaisvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_127072884             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pelagibacterium lentulum].
ACCESSION   WP_127072884
VERSION     WP_127072884.1
KEYWORDS    RefSeq.
SOURCE      Pelagibacterium lentulum
  ORGANISM  Pelagibacterium lentulum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Pelagibacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pelagibacterium lentulum"
                     /db_xref="taxon:2029865"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33788
     Region          4..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhakviiigs gpagytaaiy aaramleplm laglqpggql tittdvenyp gfadpiqgpw
       61 lveqmraqae nmgtkiknem ivdvdfntrp frltgdsgtv ytadsvviat gaqakwlglp
      121 teekfkgfgv sacatcdgff yrdktvlvvg ggntaveeal fltnfaskvi lihrrdqfta
      181 ekvmqqrlfk npkievrwnt vldevkgdnm ppsvrgavlr dvatgqtsel evdgifvaig
      241 hspateifag kldmkqggyi itepdstqts vpgvfaagdv tddvyrqavt aagmgcmaal
      301 eaerylaahe laeaae
//
LOCUS       WP_127073771             489 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pelagibacterium lentulum].
ACCESSION   WP_127073771
VERSION     WP_127073771.1
KEYWORDS    RefSeq.
SOURCE      Pelagibacterium lentulum
  ORGANISM  Pelagibacterium lentulum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Pelagibacterium.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Pelagibacterium lentulum"
                     /db_xref="taxon:2029865"
     Protein         1..489
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48708
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiailrerl ggetrvaatp dsvtklvglg aevsvekgag easripdaly aaagakveag
       61 aaatlkganv vlavrrpeak slggiakgal vlavmdpfgn eadlaalakt gisafgmefm
      121 pritraqvmd vlssqanlag yqsvidaaaa fdralpmmmt aagtvraakv fvmgagvagl
      181 qaiatarrlg aavsatdvra aageqveslg akfimtealk dasgtggyar eltkkeqaaq
      241 aelvaghiak qdivittali pgrpapklvt kamvesmapg svivdlaaer ggnvevtkpg
      301 avsvhkdvtv igtlnmagki aatasqlyak nllafletmi dkekkalavn wedelvaatl
      361 ltrdgaivhp alaavpkpaa askpaakkap akkapakaes asaaakvepk apaktgaaak
      421 apaaksataa kptakapakt gapaktsaak paaakssaak agtaksgtak paarkpaakk
      481 paakkdgdq
//
LOCUS       WP_127075633             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Butyricimonas faecalis].
ACCESSION   WP_127075633
VERSION     WP_127075633.1
KEYWORDS    RefSeq.
SOURCE      Butyricimonas faecalis
  ORGANISM  Butyricimonas faecalis
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Odoribacteraceae; Butyricimonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Butyricimonas faecalis"
                     /db_xref="taxon:2093856"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34195
     Region          11..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstenaiekv kcliigsgpa gytaaiyasr anlnpvlytg mqmggqlttt tevenfpgyp
       61 egvtgpvmme dmrkqaerfg tdirfgiatd vdfsghphkv tidgekviea daviiatgat
      121 akylglpsee afrgagvsac atcdgffyrg kdvavvgggd taceeatyla glcrkvyliv
      181 rknylraska mqervfrten ievlfehntl ellgsdmgve garlvykkgt peeatkeiki
      241 dgfflaight pntevfkkyi nvdeqgyiit egkscktnvp gvfaagdvmd ptyrqgiaaa
      301 gtgcraaida eryigelqa
//
LOCUS       WP_127076556             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhodomicrobium lacus].
ACCESSION   WP_127076556
VERSION     WP_127076556.1
KEYWORDS    RefSeq.
SOURCE      Rhodomicrobium lacus
  ORGANISM  Rhodomicrobium lacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Hyphomicrobiaceae; Rhodomicrobium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Rhodomicrobium lacus"
                     /db_xref="taxon:2498452"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33899
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maarhhrvii vgsgpagyta aiyaaramlk plliegmqpg gqltttteve nypgfaepiq
       61 gpwlmeqmra qalhvgaeiv qdlitsvdfs rlplvlngds gatyraesvi istgaqarwl
      121 gipseqdfrg ygvsacatcd gffyrgkdvl vigggntave ealfltkfak svtvahrrds
      181 fraekilqtr lfsnpkvkvl wntvldkvvg ndnpkavtga rlrdtvtdev tllpvdgifi
      241 aighapatei fkgqldttsg gylvtaakst atniagvfaa gdvtddtyrq avtaagmgcm
      301 aaldaeryla sletlaqaae
//
LOCUS       WP_127080076             454 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Dulcicalothrix desertica].
ACCESSION   WP_127080076
VERSION     WP_127080076.1
KEYWORDS    RefSeq.
SOURCE      Dulcicalothrix desertica
  ORGANISM  Dulcicalothrix desertica
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Calotrichaceae; Dulcicalothrix.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Dulcicalothrix desertica"
                     /db_xref="taxon:32056"
     gene            1..454
                     /gene="trxB"
     Protein         1..454
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=49284
     Region          9..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
     Region          355..451
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
ORIGIN      
        1 mtnptvenvv iigsgpagyt aaiyagranl kpvvfegfqa gglpggqlmt ttevenfpgf
       61 pagitgpelm dkmkaqaerw gaelytedvi svdlsqrpft vrseerefkt hsiiiatgat
      121 akrlglpseh tfwsrgisac aicdgatpif hgaelaviga gdsaaeeaiy ltkygskvnl
      181 lvrtekmras kamqdrvltn pkitvhwnte avdiygnghm egvkvrntkt geesllhakg
      241 lfyaighkpn tslfegqiql devgyivtkp gspetsvegv yaagdvqdhe yrqaitaags
      301 gcaaamlaer wlsvndlvqe ykqaphtpdn eleheesakt vapvefslsa trhegglalr
      361 klfhdsdrli vvkyvspgcg pchtlkpiln kvvdefdgki hfveididkd rdiaenagvt
      421 gtptvqffkd kellqevkgv kqksqyrqli etni
//
LOCUS       WP_127080680             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Dulcicalothrix desertica].
ACCESSION   WP_127080680
VERSION     WP_127080680.1
KEYWORDS    RefSeq.
SOURCE      Dulcicalothrix desertica
  ORGANISM  Dulcicalothrix desertica
            Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
            Calotrichaceae; Dulcicalothrix.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Dulcicalothrix desertica"
                     /db_xref="taxon:32056"
     Protein         1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40503
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,294,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,284..285,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,234,245,
                     262..264,271,273)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeie vcerrvalip divarlvkqg levlvetgag draffsdaay eaagatiiad
       61 tarvwgeadv vlkvsppqer sdgssevell regsvlisfl nplgnpavaq klaerkvsal
      121 smemiprstr aqsmdalssq asisgykavl igaaalpkyf pmlttaagti apakvfvmga
      181 gvaglqaiat arrlgaivea fdirpavkee vlslgakfve vkldeetata ggyareised
      241 srrrtqelva ahiktadvvi ttaqvpgkka pllvteemvm gmktgsvivd iaaeqggnca
      301 ctepgkdiik hgvtiigpin lpssvpvhas qlysknltsl lqliiknnai qidfgddiin
      361 dacithagei rnsrvkealq tvvgag
//
LOCUS       WP_127089279             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aquabacter cavernae].
ACCESSION   WP_127089279
VERSION     WP_127089279.1
KEYWORDS    RefSeq.
SOURCE      Aquabacter cavernae
  ORGANISM  Aquabacter cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Xanthobacteraceae; Aquabacter.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Aquabacter cavernae"
                     /db_xref="taxon:2496029"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34063
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msthhakvvi igsgpagyta aiyaaramle pilfegiqpg gqltittdve nypgfadviq
       61 gpwlmeqmra qaehvgtrii sdhvsslemt grpfrlvtds gdtylaetvi latgaqarwl
      121 gipseetyrg fgvsacatcd gffyrgktvv vvgggntave ealfltnfaa kvilvhrrdk
      181 lraerilqdr lfahpkveii wnaeieeivg aeepsrvtgv rlrdvdggge rlvaadgffv
      241 aighapstsl vegkvrlkpn gyvwtapdst atsvaglfaa gdvaddvyrq avtaagrgcm
      301 aaleaerfla reetplaae
//
LOCUS       WP_127097089             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium lemovicicum].
ACCESSION   WP_127097089
VERSION     WP_127097089.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium lemovicicum
  ORGANISM  Microbacterium lemovicicum
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Microbacterium lemovicicum"
                     /db_xref="taxon:1072463"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34337
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqviiigsg pagytaavya aranlsplvi assveaggel mnttevenfp gfpdgiqgpe
       61 lmekmqaqae kfgaevvydd vvgldidgpv ktitlgsgav hetsaliyat gsayrklgld
      121 gedrlsghgv swcatcdgff frertiavvg ggdsameeat fltrfaskvy iihrkdslra
      181 skimqerafa nekiefvwns qvvdvlgdga ltgvvledtv dgsrrelald glfiaigndp
      241 rthlvhdkld ltpdgtiwvd grssrtsvpg vfaagdvidp tyrqaataag sgtvaaldae
      301 hflaalgeag aperfddqie rlpva
//
LOCUS       WP_127098122             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            sp. km772].
ACCESSION   WP_127098122
VERSION     WP_127098122.1
KEYWORDS    RefSeq.
SOURCE      Legionella sp. km772
  ORGANISM  Legionella sp. km772
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Legionella sp. km772"
                     /db_xref="taxon:2498111"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40481
     Region          1..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mmiatiheqg netrvaitpq sakqylklgf tvaiekdagl aagftnaeye qvgvqiqdnk
       61 knllaqtkvl lclnepdsel igelprncli iahvdnntds kliqaalaqg itilsmnfip
      121 risraqsmds lssqanlagy ravlegvntf hraipmmmta agmiqpakil ilgagvaglq
      181 aiatakrlgg ivyafdvrra akeqveslga efievaqdqd setkggyase mseeykklqa
      241 elidqyakia dlvistalip grpapiliqk stveqmkpgs vivdlatsrg gncelsqkdk
      301 tikhgeitii gisnmaglvp ttaselyann lvhlinllts ktaelsfnpd deiiqqavlc
      361 hegaqlpfqk akekqna
//
LOCUS       WP_127098251             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Legionella sp. km772].
ACCESSION   WP_127098251
VERSION     WP_127098251.1
KEYWORDS    RefSeq.
SOURCE      Legionella sp. km772
  ORGANISM  Legionella sp. km772
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Legionella sp. km772"
                     /db_xref="taxon:2498111"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33984
     Region          7..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msnsnhhrli ilgsgpagyt aavyaaranl kpvlitgmqp ggqlttttev dnwpgdiegl
       61 qgpalmermq khaerfdtei ifdhivkadl kqspfslqgd satytcdali iatgasaryl
      121 gldsetayqg kgvsacatcd gffyrnksvc vvgggntave ealylsniaa svtlihrrds
      181 lraekmlqdk lfskvekgni kliwnstlde vmgdgrkvtg vslrnlqdgs kqelnfdgvf
      241 iaightpntq lfqdqlamrd gyltiksgld gmatstsipg vfacgdvadh vyrqaitsag
      301 fgcmaaldae kyldllk
//
LOCUS       WP_127090466             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Aquabacter
            cavernae].
ACCESSION   WP_127090466
VERSION     WP_127090466.1
KEYWORDS    RefSeq.
SOURCE      Aquabacter cavernae
  ORGANISM  Aquabacter cavernae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Xanthobacteraceae; Aquabacter.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Aquabacter cavernae"
                     /db_xref="taxon:2496029"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39514
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavpaevd lgeprvaatp dtvkrlvtlg atvavetgag lksgiidady eaagatiaas
       61 ahdalagadv vlkvrrptta elpdykagal vlaimdpygn edalkalada glatfamemm
      121 pritraqvmd vlssqanlag yravidasse fgralpmmmt aagtvpaarc fimgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedee fkqaetaagy akpmsaeyqa
      241 kqaalvaehi kkqdmvitta lipgrpapkl vtaamvasmk pgsviidlav erggnvegav
      301 pgevaqvngv kivghlntag riaasasqly aknlyaflet midkqakala vkwddelvka
      361 tlltrdsavv hpnfapkveg avq
//
LOCUS       WP_127104880             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pararhodobacter zhoushanensis].
ACCESSION   WP_127104880
VERSION     WP_127104880.1
KEYWORDS    RefSeq.
SOURCE      Pararhodobacter zhoushanensis
  ORGANISM  Pararhodobacter zhoushanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pararhodobacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Pararhodobacter zhoushanensis"
                     /db_xref="taxon:2479545"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33333
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetkhtrll iigsgpagyt aavyasraml epvlvqgmqp ggqltittdv enwpgdasvm
       61 gpdlmvrmen haremgaeii tdiilsldls krpftavgds gtvytadavv latgaqakwl
      121 glesedkfkg fgvsacatcd gffyrgkeiv vvgggntave ealfltnfas kvtlvhrrds
      181 lraekimqdr lfkhpkievv wdseiveveg tsmplgvsgv kirnlktgae svlpaegffv
      241 aighapasel vkdqlklhsg nyvwvepgst rtsvpgvfaa gdltddkyrq avtsagmgcm
      301 aaldaehwla aqd
//
LOCUS       WP_127109814             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pararhodobacter zhoushanensis].
ACCESSION   WP_127109814
VERSION     WP_127109814.1
KEYWORDS    RefSeq.
SOURCE      Pararhodobacter zhoushanensis
  ORGANISM  Pararhodobacter zhoushanensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Pararhodobacter.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Pararhodobacter zhoushanensis"
                     /db_xref="taxon:2479545"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55217
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreiy pgenrvamtp dsalllqklg hscaietgag aasgfedaay taagveivpt
       61 aealfetadv vvkvreatie elgrlradqt liaffwpaqn pemlelakqr gttvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg aitmafdvrp evaeqiesmg asfvyldfee aqdgaatggy aapsspefre
      241 kqlakfrela pdvdivitta lipgrpapkl wtedmvalmk rgsvvvdlaa erggncdltv
      301 pdekivsang vtiigytdfp srmgtqastl ysnnirhmla dltpgkdgvi vhnmeddvir
      361 gatvahggei tfpppppkvk aiaaakpkek akeltveerr aaevaafkaq tksqftllgv
      421 gggllllagf fapasfmshf ivfvlacfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgswl vvilaalavf maginifggf mvtrrmlamf qks
//
LOCUS       WP_127110660             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Legionella
            sp. km535].
ACCESSION   WP_127110660
VERSION     WP_127110660.1
KEYWORDS    RefSeq.
SOURCE      Legionella sp. km535
  ORGANISM  Legionella sp. km535
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Legionellales; Legionellaceae; Legionella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Legionella sp. km535"
                     /db_xref="taxon:2498107"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41109
     Region          12..363
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mnittllesg retrvaitpn sakqlikigf nvaieknagi asdfsneeyq rigveliehr
       61 etllqqtdvl lcinepnped lkglaknsli ighidndpqs kliqwcqkqh inlfsmnlip
      121 risraqsmds lssqanlagy ravleavtqf hrvipmmmta agmiqpskil ilgagvaglq
      181 aiatakrlga vvyafdvrra akeqveslga efievsqeld sesksgyase tsdeykklqa
      241 elidqyakis divistalip grkapvllyk stieqmkpgs iiidlatsrg gncelsvpdq
      301 iikhgtitii gisnmaglvp atasdlyann lvhlinliap tppeikfnpd deiiqqavlc
      361 yegnylpyqa trekqna
//
LOCUS       WP_127112468             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Shimia
            sediminis].
ACCESSION   WP_127112468
VERSION     WP_127112468.1
KEYWORDS    RefSeq.
SOURCE      Shimia sediminis
  ORGANISM  Shimia sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Shimia sediminis"
                     /db_xref="taxon:2497945"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55279
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkevf dgenrvamtp dsaiqlqklg ydcaiesgag anagfsdavy eeagveiikt
       61 aaalwkacdi vakvrqpnet elkrltkgkt lisffnpagn edgmeaakak ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aaigtstslg aitlafdvrp evaeqvesmg aefvyldfee eqqdgaatgg yasvsspefr
      241 eaqlakfrel apevdivitt alipnreape lwtedmvaam kpgsvivdla aekggncklt
      301 vmdekivten gvtiigytdf psrmgaqass lyatnirhmm tdltpekdgq inhdmeddvi
      361 rgatvtfegd itfpppppkv qaiaakpkev vpeltpeekr aaevaafkaq tksqvtllav
      421 ggalllgvgl vapasfmqhf ivfvlavfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsvf maginifggf lvtrrmlamf qks
//
LOCUS       WP_127115397             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Shimia sediminis].
ACCESSION   WP_127115397
VERSION     WP_127115397.1
KEYWORDS    RefSeq.
SOURCE      Shimia sediminis
  ORGANISM  Shimia sediminis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Shimia sediminis"
                     /db_xref="taxon:2497945"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33330
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 madtkhtkvl iigsgpagyt agvyasraml epilvqgiep ggqlttttev enypgftevq
       61 gpdlmvkmqe haaamgceii gdiitnldms erpfkatgds gtiytadavi latgarakwl
      121 gleseekfkg fgvsacatcd gffyrgqeiv vigggntave ealfltnfas kvtlihrrde
      181 lraekilqdr lmknekiepl wfhtleevvg ddnplgvtgv kvrnvktdev seipcagvfv
      241 aighspanel vkdtlemhng gyvqvkpgst etsvpgvfaa gdltdhvyrq avtsagmgcm
      301 aaldaerfla gqd
//
LOCUS       WP_127119978             318 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase
            [Piscirickettsiaceae].
ACCESSION   WP_127119978
VERSION     WP_127119978.1
KEYWORDS    RefSeq.
SOURCE      Piscirickettsiaceae
  ORGANISM  Piscirickettsiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Piscirickettsiaceae"
                     /db_xref="taxon:135616"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33819
     Region          2..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mskhckllil gsgpagytaa vyaaranlep vmvtgmqqgg qlttttevdn wpgdvegltg
       61 pdlmvrmqkh aerfgteiif dhihtaelqq rpfkligdsg eytcdaliia tgasakylgl
      121 eseeafkgkg vsacatcdgf fyrnqkvavi gggntaveea lylsniaaev tivhrrdsfs
      181 sekiladqlk ekaengniki eynstleevl gdnmgvtglr lkntqsgdtk eidvagvfia
      241 ightpntgif dgqldmdhgy lkvqsglqgn atqtsipgif aagdvmdqvy kqaitsagag
      301 cmaaldaeky ldhlesqs
//
LOCUS       WP_127141518             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flagellimonas marinaquae].
ACCESSION   WP_127141518
VERSION     WP_127141518.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas marinaquae
  ORGANISM  Flagellimonas marinaquae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Flagellimonas marinaquae"
                     /db_xref="taxon:254955"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34622
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseqverikt liigsgpagy taaiyaarad lkpvlytgme pggqltttte vdnfpgypeg
       61 vdgptmmmql qqqaerfgtd vrigmvtave lseevggihk itvddstqle aetviistga
      121 sakylnlpse qrlrgggvsa cavcdgffyk gqevaivgag dtaaeeasyl anictkvtml
      181 vrkdymrask amqhrvnsid nieiryntev eevlgeqvve gvrvvnnetg ekedipvtgl
      241 fiaighkpnt dvfkgqldmd etgyiitqpk stktnrpgvf asgdaqdkiy rqavtaagtg
      301 cmaaldaery laaveskelq vse
//
LOCUS       WP_127126376             336 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Georgenia sp. SYP-B2076].
ACCESSION   WP_127126376
VERSION     WP_127126376.1
KEYWORDS    RefSeq.
SOURCE      Georgenia sp. SYP-B2076
  ORGANISM  Georgenia sp. SYP-B2076
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Allobogoriellales; Allobogoriellaceae; Georgenia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Georgenia sp. SYP-B2076"
                     /db_xref="taxon:2495881"
     gene            1..336
                     /gene="trxB"
     Protein         1..336
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35368
     Region          12..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqetstptt ihdviivgsg pagytaavya aranlrpivf agsvtaggal mnttevenfp
       61 gfpegvlgpq lmenmqkqae rfgadvryed vvavdlggei ktvttdddet ysaravilan
      121 gsaykeigvp eekrlsgrgv swcatcdgff frnqhiivvg ggdsameeat fltrfadkvt
      181 vvhrrgelra skimaarala nekiefawns evaaingetk vtsvtlrdtv tgetreldat
      241 gvfvaighrp rteilagqve ldeagyvvvg hpttatnvpg vfacgdavdh iyrqaitaag
      301 tgcaaaldae rylaeldeag epapdasqtp egavlv
//
LOCUS       WP_127137714             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flagellimonas oceanensis].
ACCESSION   WP_127137714
VERSION     WP_127137714.1
KEYWORDS    RefSeq.
SOURCE      Flagellimonas oceanensis
  ORGANISM  Flagellimonas oceanensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flagellimonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Flagellimonas oceanensis"
                     /db_xref="taxon:2499163"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34425
     Region          11..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseqverikt liigsgpagy taaiyaarad lkpvlytgme pggqltttte vdnfpgypeg
       61 idgpammmql qqqaerfgte vrigmvtave lsdevggkhk vtvdetiele aetviistga
      121 sakylnipse qrlrgggvsa cavcdgffyk gqdvaivgag dtaaeeasyl anicnkvtml
      181 vrkdymrask amqhrvnsid nieikyntev eevlgdqvve giravnnqtg ekedipvtgl
      241 fiaighkpnt dvfkgqldmd etgyiitqpk stktnkpgvf asgdaqdkiy rqavtaagtg
      301 cmaaldaery lasveseeml as
//
LOCUS       WP_127124450             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudoflavitalea rhizosphaerae].
ACCESSION   WP_127124450
VERSION     WP_127124450.1
KEYWORDS    RefSeq.
SOURCE      Pseudoflavitalea rhizosphaerae
  ORGANISM  Pseudoflavitalea rhizosphaerae
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Pseudoflavitalea.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Pseudoflavitalea rhizosphaerae"
                     /db_xref="taxon:1884793"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33633
     Region          8..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mesekvhcli igsgpagyta aiyaaranmk pvlyqgiqpg gqltitteve nypgypegiq
       61 gpemmvdfek qatrmgadir yglatkvdfs qqpfkvwide eklveadavi iatgasakwl
      121 glpseerlng fgvsacavcd gfffrgkdva ivgagdtaae ealylskltn kvsmlvrkdq
      181 mraskvmqdr vlatpnikvy wetetdeilg enkvdsvrvr nvktgateti pvqgffvaig
      241 htpnseifkd yldmdeagyi ktipgtsktn vegvfaagdv qdkiyrqavt aagsgcmaal
      301 daerylsakg lv
//
LOCUS       WP_127142536             395 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pelagibacterium montanilacus].
ACCESSION   WP_127142536
VERSION     WP_127142536.1
KEYWORDS    RefSeq.
SOURCE      Pelagibacterium montanilacus
  ORGANISM  Pelagibacterium montanilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Pelagibacterium.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Pelagibacterium montanilacus"
                     /db_xref="taxon:2185280"
     Protein         1..395
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40231
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiailrerv gdeprvaatp etvakllglg aevsveagag ehsrisdaay aeagatmags
       61 aaealkgaev iftvrrpraa dldgagtgal vigmmdpfgh eddiaalaga glstfamefm
      121 pritraqvmd vlssqanlag yqavidaaaq yeralpmmmt aagtvraakv fvmgagvagl
      181 qaiatarrlg aavsatdvra vageqveslg akfimtealk dasgtggyar eltdaekasq
      241 aelvaghiak qdivittali pgrpapqlvt ramvesmapg svivdlaaer ggnveltapg
      301 evivhndvti igtlnlpgki aatasqlyak nllaffetmv dkenkalavn wedqlvtatl
      361 ltrdgavvhp nlvdaapaaa kapaapeaas kdgda
//
LOCUS       WP_127123770             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Chryseotalea sanaruensis].
ACCESSION   WP_127123770
VERSION     WP_127123770.1
KEYWORDS    RefSeq.
SOURCE      Chryseotalea sanaruensis
  ORGANISM  Chryseotalea sanaruensis
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Chryseotaleaceae; Chryseotalea.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Chryseotalea sanaruensis"
                     /db_xref="taxon:2482724"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33652
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 merehiqvli igsgpagyta aiyaaraglk pvlytggqpg gqltttndve nfpgypegin
       61 gpqmmmdlqk qaerfgtqvr yglvtavdfa gyphkltide ntevvadtvi istgatakyl
      121 gipseetyan kgvsacavcd gyfyrgkeva vvgagdsaae eatylaklct kvhlivrrde
      181 mraskimqqr vintpnieih wnseteeilg ddtgvtgari vnsktgekkn lsvqgfflai
      241 ghkpntdifk gfidmdetgy ikvkpgstkt nvegvfavgd aadkiyrqai taagtgcmga
      301 ldaekflqak eavha
//
LOCUS       WP_127142603             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pelagibacterium montanilacus].
ACCESSION   WP_127142603
VERSION     WP_127142603.1
KEYWORDS    RefSeq.
SOURCE      Pelagibacterium montanilacus
  ORGANISM  Pelagibacterium montanilacus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Pelagibacterium.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pelagibacterium montanilacus"
                     /db_xref="taxon:2185280"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33873
     Region          4..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhakviivgs gpagytaaiy aaramlepvm vsgmqpggql tittdvenyp gfadpiqgpw
       61 lveqmrtqae hmgtrmendv ivdvdldvrp frltgdsgtv ytadsviiat gaqakwlglp
      121 seekfmgfgv sacatcdgff yrdktvlvvg ggntaveeal fltnfaskvi vvhrrdefra
      181 ekilqqrlfk hpkievrwnt aldevkgdnm ppsvrgavlr dmasgqttei evdgifvaig
      241 hapatevfkg klemkhggyi vtapdstatn ipgvfaagdv tddvyrqavt aagmgcmaal
      301 eaerylaehe laeaae
//
LOCUS       WP_127152042             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces lydicus].
ACCESSION   WP_127152042
VERSION     WP_127152042.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces lydicus
  ORGANISM  Streptomyces lydicus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces lydicus"
                     /db_xref="taxon:47763"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34445
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfrdgim
       61 gpdlmdnmra qaerfgaelv pddivavdls eeiktvtdta gnvhraktvi vstgsqhrkl
      121 glpredelsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtvvhrrdt
      181 lraskamqer afadpkikfv wdsevaeihg esklsgltlr nlktgettel pvtglfiaig
      241 hdprtelfkg qlkldddgyl kvdapstrtn lsgvfaagdv vdhtyrqait aagtgcsaal
      301 daerflasls dgeataepek tpsa
//
LOCUS       WP_127162628             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Entomomonas moraniae].
ACCESSION   WP_127162628
VERSION     WP_127162628.1
KEYWORDS    RefSeq.
SOURCE      Entomomonas moraniae
  ORGANISM  Entomomonas moraniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Entomomonas.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Entomomonas moraniae"
                     /db_xref="taxon:2213226"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33320
     Region          8..312
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msdikhskvi ilgagpagyt aavyaaranl spllitgmqp ggqlttttev dnwpgdvegv
       61 qgpdlmarmq khaerfatei vydhinqadl skkpfilvgd sgtytcdsli vatgasaqyl
      121 glpsetqfmg kgvsacatcd gffyknqvva vvgggntave ealylsniak evhvihrrdk
      181 lrcekimqdk lfekaktgnv vihwntelde vlgdktgvtg vslksvatge kttlnlmgvf
      241 iaighkpntd ifqnqlaldn gyikicggkl gvtatsiegv faagdvadqv yrqaitsaga
      301 gcmaaldver yldgl
//
LOCUS       WP_127179006             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_127179006
VERSION     WP_127179006.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34167
     Region          7..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfrdgim
       61 gpdlmdnmrg qaerfgaeli pddivsvdls gdiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfv wdsevaeieg dpklsglklr nlktgelsdl avtglfiaig
      241 hdprtelfkg qldldeegyl kvaapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerylsfla dgenaepekt tv
//
LOCUS       WP_127187121             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arsenicitalea aurantiaca].
ACCESSION   WP_127187121
VERSION     WP_127187121.1
KEYWORDS    RefSeq.
SOURCE      Arsenicitalea aurantiaca
  ORGANISM  Arsenicitalea aurantiaca
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Arsenicitalea.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Arsenicitalea aurantiaca"
                     /db_xref="taxon:1783274"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33648
     Region          4..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhakvmiigs gpagytaaiy aaramlepvm isgmqpggql tittdvenyp gfadviqgpw
       61 lmeqmkaqae hvgtrmvsdl ivsvdldkrp ftltgdtgai ytcdsliiat gaqarwlglp
      121 aeekfqgfgv sacatcdgff yrdrqvlvvg ggntaveeal fltnfaskvi vihrrdefra
      181 erilqdrlfr npkievrwnt eladitgaam ppsvqgvvlr ntrtgelsel avdgvfvaig
      241 hspstaifsg kldmkpggyl ktvpgstatn vpgvfaagdv tddvfrqavt aagmgcmaal
      301 eaerflaehq laeaae
//
LOCUS       WP_127193184             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus anaericanus].
ACCESSION   WP_127193184
VERSION     WP_127193184.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus anaericanus
  ORGANISM  Paenibacillus anaericanus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus anaericanus"
                     /db_xref="taxon:170367"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34013
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksivigtg pagltaaiyl aradlnpivi egiqpggqlt tttevenfpg fpqgimgpel
       61 mdnmrkqaer fgaefrsgwv eevdftkqpf kvkveggdel eaetvilstg alakyldipg
      121 eqdnigrgvs tcatcdgfff rgkklivvgg gdsameeasf ltrfassvtv vhrreelras
      181 kimqeraknn ekvhwalgrt plevatdekg aviglkvrnn vsnqeelvea dgvfvaight
      241 pntkflgtqi eidkhgyivv mpgtsetnip gvfacgdvqd tryrqaitaa gsgcmaamdc
      301 ekflegsmvh dwskn
//
LOCUS       WP_127193552             315 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Paenibacillus].
ACCESSION   WP_127193552
VERSION     WP_127193552.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33777
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksiiigtg pagltaaiyl aranlsplvi egpqpggqlt tttevenfpg fpegimgpel
       61 mdnmrkqaer fgaefrtgwv nsvdmsqrpf klqvegigel itdtlvlstg atakylgipg
      121 eqdnigrgvs tcatcdgfff rnkeiivvgg gdsaleeagf ltrfaskvtl vhrrdemras
      181 kimqdrvrgn ekvewalnrt plevitdekg vtglkvrnnd tgeeeiinas gvfvaighhp
      241 ntaflggaid tdengyiivk pgtsetnipg vfacgdvqdt ryrqaitaag sgcmaaidce
      301 kyienlehet vpssv
//
LOCUS       WP_127196922             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Pseudomonas].
ACCESSION   WP_127196922
VERSION     WP_127196922.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38744
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq pgetrvaatp etikkligqg hkvtvqsgag vnasvidsay eaagatigsa
       61 tdafsaelil kvvapsdsel alissgtvli gmlnpfsnet iaklaergit afsleaaprt
      121 sraqsldvls sqaniagyka vlvaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqalavhera kqadivitta lipgrkapvl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvehgv tivgytnlpa mvaadasaly arnlldflkl vftpegqfqi nleddivaac
      361 lmcrdgqvvr kng
//
LOCUS       WP_127200307             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus zeisoli].
ACCESSION   WP_127200307
VERSION     WP_127200307.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus zeisoli
  ORGANISM  Paenibacillus zeisoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenibacillus zeisoli"
                     /db_xref="taxon:2496267"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33375
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksiivgtg pagltaaiyl aranlsplii egpqpggqlt tttevenfpg fpegimgpel
       61 mdnmrkqaer fgaefrtgwv nsvdtssrpf klqveglgel vtetlilstg atakylgipg
      121 eqdnvgrgvs tcatcdgfff rgkeiivvgg gdsaleeagf ltrfaskvtl vhrreelras
      181 kimqdrvrsn ekvewalnrt pieviagerg vtglkvlnnv tgeeeiieas gvfvaighhp
      241 ntgflggqit tdengyivvn pgtsetnvkg vfacgdvqdt ryrqaitaag sgcmaamdae
      301 kyieslehea avr
//
LOCUS       WP_127201901             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127201901
VERSION     WP_127201901.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53907
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdseitfp pppiqvsaqp qqtpsekavp aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_127204980             427 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127204980
VERSION     WP_127204980.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44045
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripde efakagaaig
       61 kagdvakadv vlkvrrpsea elkayrrgta viaimdpygn daavdalara svtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fraaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggqv vhpafvrveq apcveppaip aktmvadasa kpaaakkaap kkpvapkspp
      421 skskgta
//
LOCUS       WP_127206374             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.
            M6A.T.Ce.TU.002.03.1.1].
ACCESSION   WP_127206374
VERSION     WP_127206374.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M6A.T.Ce.TU.002.03.1.1
  ORGANISM  Mesorhizobium sp. M6A.T.Ce.TU.002.03.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. M6A.T.Ce.TU.002.03.1.1"
                     /db_xref="taxon:2496782"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34547
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfgdpiq
       61 gpwlmeqmlk qaehvgtdvi ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilser lfkkdnvrii wdtvvdeitg qsgkmplpps veglklrnvv tsqemhltvd
      241 gvfvaighap avelfagklk qkpngylwta pdstctdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127207164             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127207164
VERSION     WP_127207164.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53790
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrlge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflkhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_127199321             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus zeisoli].
ACCESSION   WP_127199321
VERSION     WP_127199321.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus zeisoli
  ORGANISM  Paenibacillus zeisoli
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Paenibacillus zeisoli"
                     /db_xref="taxon:2496267"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34452
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksivigtg psgltaaiyl aranlsplvi egmepggqlt tttevenfpg fpqgilgpel
       61 mdnmrkqaer fgaefrngwv eevdfskrpf kvkitgqaet leaetviist gasarylgip
      121 geqenvgrgv stcatcdgff frgkkiivvg ggdsameeas fltrfasevt lvhrrdelra
      181 skimqdrard nekvkwalnr tplevvtdek gvkglkvrnn eadqeeivea dgvfvaight
      241 pntkflggqi etdehgyivv kpgttetnip gvfacgdvqd tkyrqaitaa gsgcmaamdc
      301 ekflegamvh dwsetldm
//
LOCUS       WP_127209836             423 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127209836
VERSION     WP_127209836.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43429
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtifipre ldaneprvaa spdtvkrlag lgfnvivesg agtasripde efgkagavig
       61 kaadvakadv vlkvrrpdea elkayrpgta viaimdpygn daavdalara gatafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttasg vkiighlnvp grvaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggqv vhpafigkpa vmiasaepak paagekpaap kkaatsrkla apkslankpk
      421 gia
//
LOCUS       WP_127213702             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127213702
VERSION     WP_127213702.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53790
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaattg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_127214914             422 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127214914
VERSION     WP_127214914.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43541
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsritdq efaaaggtig
       61 tagdaknadv vlkvrrptda elkgyksgaa viaimdpygn daalaamasa giiafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatktl aikrddelvk
      361 atmltdagqi vhpsfakaag qprtepaaip atvlvadaad kkpaprrraa akspspkpeg
      421 ta
//
LOCUS       WP_127219833             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127219833
VERSION     WP_127219833.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53916
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsddgyakv msdefiaaem
      241 klfaeqakev diiitpaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_127225968             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_127225968
VERSION     WP_127225968.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34469
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrsd
      181 fraerilrer llkkdnvrii wdtvvdeitg rpgkaplpps vegltlrnvv tgqesklpvd
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127219912             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127219912
VERSION     WP_127219912.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53822
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvagvaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_127229732             426 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127229732
VERSION     WP_127229732.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43979
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqvvfipre idpneprvaa spetvkrlag lgfdvivekg aglgsripdq dfaavgamig
       61 tasdakkadv vlkvrrptda elkgyksgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvmtteng vkivghlnvp grvaasasll yaknvyafle tmvdkatkql aikrddelvk
      361 atmltdggnv vhpafakaaq eprtepaaip attmvadasv kpaakkaatr kpatakspss
      421 kpegta
//
LOCUS       WP_127230037             315 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: STM4504/CBY_0614 family protein [unclassified
            Mesorhizobium].
ACCESSION   WP_127230037
VERSION     WP_127230037.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..315
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35746
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mtifdifskr qkrqrgempd vyqydtipmp lrvqivhilr dtigelnndt yyyhtdiqec
       61 yeaavqillr eygvfrlgsa pahadrdypn qllnfilqaq dteqvidaie isfkivngfv
      121 rrdgylgrsd adrvaseait elnarlkehg vgyqfldgei vrvdseliha eavkpalrll
      181 ntksykgahe eflkaydhyr hgrtkealne clkafestmk sicdkrhwty nsndtaknli
      241 gvlydnglvp sfwqgqltsl rsllessipt grnrmgghgq gttptnvpsy iaaymlhmta
      301 stlvflttae eampk
//
LOCUS       WP_127233463             400 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M2C.T.Ca.TU.002.02.1.1].
ACCESSION   WP_127233463
VERSION     WP_127233463.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M2C.T.Ca.TU.002.02.1.1
  ORGANISM  Mesorhizobium sp. M2C.T.Ca.TU.002.02.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Mesorhizobium sp. M2C.T.Ca.TU.002.02.1.1"
                     /db_xref="taxon:2496788"
     Protein         1..400
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41351
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqivfipre vdpneprvaa spetvkrlag lgfdvivekg aglgsripdq dftaaggaig
       61 taadakkadv vlkvrrptda elkgyksgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaage ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg aivtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatktl aikrddelvk
      361 atmltdagqv vhpafakaaq eprtepaakk ksaakpkgta
//
LOCUS       WP_127234011             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.
            M2C.T.Ca.TU.002.02.1.1].
ACCESSION   WP_127234011
VERSION     WP_127234011.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M2C.T.Ca.TU.002.02.1.1
  ORGANISM  Mesorhizobium sp. M2C.T.Ca.TU.002.02.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. M2C.T.Ca.TU.002.02.1.1"
                     /db_xref="taxon:2496788"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34365
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmsqmla qaehvgtdiv ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrrd
      181 fraerilrer llakdnvrvi wdtvvdeitg rpgkaplpps veglalrnvv tgqesklpvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127235041             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127235041
VERSION     WP_127235041.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53763
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 tavwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakdv diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtssekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf avtrrmlnmf kkg
//
LOCUS       WP_127240541             422 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127240541
VERSION     WP_127240541.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43634
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrmag lgfevivekg aglgsritdq efvtaggtig
       61 tagdaknadv vlkvrrptda elkgyksgaa viaimdpygn daalaamasa gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkvtktl aikrddelvk
      361 atmltdagqi vhpsfakaag qprtepaaip atvlvadaad kkpaprrraa akspspkpeg
      421 ta
//
LOCUS       WP_127244554             402 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Mesorhizobium sp. M7A.F.Ca.CA.001.05.1.1].
ACCESSION   WP_127244554
VERSION     WP_127244554.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.CA.001.05.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.CA.001.05.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Mesorhizobium sp. M7A.F.Ca.CA.001.05.1.1"
                     /db_xref="taxon:2496721"
     Protein         <1..402
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..344
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(22,103..104,113..114,117..118,121..122,124..125,
                     127..132,134,136..138,141,164..165,257..258,301..302,306,
                     309..310)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(51,70,267,294,296)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(98..99,103,106,109,150..153,173..175,207,218,
                     235..237,244,246)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(100..101,103,113,156..157,164,180..181,183..186)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(133..137,140,143,166,168)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 vkrlaalgfd vvveagaglk sriidadyas agaaigkasd vakadvvlkv rrpgdaelks
       61 ykpgaaviai mdpygndaav aalakagvta fsmefmprit raqsmdvlss qanlagyqav
      121 idgaseydra lpmmmtaagt vpaakvfimg vgvaglqaia tarrlgavvt atdvrpaake
      181 qvaslgakfl avedeefkaa etaggyakem skeyqakqaa ltsehiakqd ivittalipg
      241 rpapklvsaa mvasmkpgsv ivdlavergg nvegaeagkv vttannvkiv ghlnvpgria
      301 asasllyarn lfafletlvd kttktlainr dddlvkatml tdggkvvhpa fvkadqqpak
      361 gqyvepaaip aktmvadasp kkaapkkaaa pkspsskpkg ia
//
LOCUS       WP_127244760             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria meningitidis].
ACCESSION   WP_127244760
VERSION     WP_127244760.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33625
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msqhrkliil gsgpagytaa vyaaranlnp viitgiaqgg qlmtttevdn wpadadgvqg
       61 pelmarflah aerfgteiif dqinavdlqk rpftlkgdmg eytcdaliva tgasakyldl
      121 pseeafagkg vsacatcdgf fyknqdvavv gggntaveea lylaniaktv tlihrrsefr
      181 aekimidklm krveegkiil klesnlqevl gddrgvngal lknndgseqq iavsgifiai
      241 ghkpntdifk gqlemdeagy lktkggtadn vgatniegvw aagdvkdhty rqaitsaasg
      301 cqaaldaerw lgsqni
//
LOCUS       WP_127249710             417 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127249710
VERSION     WP_127249710.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43086
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqivfipre ldpneprvaa spetvkrlag lgfdviveqg aglgsripdq dfaavgatig
       61 kaadaskadv vlkvrrptda elkgyksgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtaidvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatkql aikrddelvk
      361 atmltdggrv vhpnfakaae eprtepaaip attmvadaad akpaakkksa akpkgta
//
LOCUS       WP_127254472             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127254472
VERSION     WP_127254472.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53916
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltkpge
      301 lfvtdngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrngeitfp pppiqvsaqp qqtpsekvvp aakpepkpvp lwqklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf fvtrrmlnmf kkg
//
LOCUS       WP_127254626             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127254626
VERSION     WP_127254626.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53746
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvagvaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_127256120             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M2A.F.Ca.ET.037.01.1.1].
ACCESSION   WP_127256120
VERSION     WP_127256120.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M2A.F.Ca.ET.037.01.1.1
  ORGANISM  Mesorhizobium sp. M2A.F.Ca.ET.037.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mesorhizobium sp. M2A.F.Ca.ET.037.01.1.1"
                     /db_xref="taxon:2496748"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42969
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maraifipre ldpneprvaa spetvkrlvg lgfdvivekg aglgsripdq dfvavgaatg
       61 tagdakkadv vlkvrrptda elkgyksgaa vvaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlfafle tmvdkatktl aikrddelvk
      361 atmltdggrv vhpnfakaae eprtepaaip atttvaeaad akpaakkkaa akpkgta
//
LOCUS       WP_127259565             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M7A.F.Ca.US.008.03.1.1].
ACCESSION   WP_127259565
VERSION     WP_127259565.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.US.008.03.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.US.008.03.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mesorhizobium sp. M7A.F.Ca.US.008.03.1.1"
                     /db_xref="taxon:2496742"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43900
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvieag aglksriida dyasagaaig
       61 kvsdvakadv vlkvrrpsda elksykpgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlidkttktl ainrdddlvk
      361 atmltdggkv vhpafvkadq qppkgqyvep aaipaktmva daspkkaapk kaaapkspss
      421 kpkgia
//
LOCUS       WP_127262056             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127262056
VERSION     WP_127262056.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53667
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwvcpliy kvnapseqel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkkpapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_127260950             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_127260950
VERSION     WP_127260950.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34650
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipteqdfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlar svtvihrrsd
      181 fraerilrer llkkdnvrvi wdtivdeitg rpgktplpps veglklkhav tgemshlkid
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127264174             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127264174
VERSION     WP_127264174.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53725
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qaagatvadk
       61 aavwaypliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmkpgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vtrdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvp lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_127264156             427 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M7D.F.Ca.US.004.01.2.1].
ACCESSION   WP_127264156
VERSION     WP_127264156.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7D.F.Ca.US.004.01.2.1
  ORGANISM  Mesorhizobium sp. M7D.F.Ca.US.004.01.2.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Mesorhizobium sp. M7D.F.Ca.US.004.01.2.1"
                     /db_xref="taxon:2496738"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43813
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdviveag agldsriida dyasagaaig
       61 kasdvakadv vlkvrrpsda elksykpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkatktl ainrdddlvk
      361 atmltdggkv vhpafakadq qprvepaaip aatmvadasv kpatakkaap kkaaapksps
      421 skpkgia
//
LOCUS       WP_127267395             422 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Mesorhizobium].
ACCESSION   WP_127267395
VERSION     WP_127267395.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43621
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag agtrsripde efskagatig
       61 kasdvvkadv vlkvrrpgda elksykpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltnggki vhpsfakpdq qpyvepaaip attmvadasp kkaapkkpaa skspsskpkg
      421 ia
//
LOCUS       WP_127267436             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Mesorhizobium].
ACCESSION   WP_127267436
VERSION     WP_127267436.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34604
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipteqdfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlar svtvihrrsd
      181 fraerilrer llkkdnvrvi wdtivdeitg rpgktplpps veglklkhav tgevshlkid
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127273124             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.
            M7A.F.Ca.CA.004.04.1.1].
ACCESSION   WP_127273124
VERSION     WP_127273124.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.CA.004.04.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.CA.004.04.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Mesorhizobium sp. M7A.F.Ca.CA.004.04.1.1"
                     /db_xref="taxon:2496733"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33336
     Region          6..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstrgiiigs gpagytaaiy aaralcnpvl icgpqpggql tvttdvenyp gfpdivqgpw
       61 lmeqmqkqae hcgativtdh vetadlserp frvitssgkr yetealiiat gaqarwlglp
      121 seerfrgfgv sacatcdgif firkhvvvvg ggntaaeeal flskyaskvt lvhrgaslra
      181 ekilqqrlfn dtkievvweh vvdevlgnee palsvegirl rhartgavqn lpadglfvai
      241 ghspsvrvfg dqlrqkpggy iwvepgstrt svpgvfaagd vsddvyrqav taaglgcmaa
      301 ieaerflahp hs
//
LOCUS       WP_127274351             362 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Mesorhizobium sp. M7A.F.Ca.AU.002.02.1.1].
ACCESSION   WP_127274351
VERSION     WP_127274351.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.AU.002.02.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.AU.002.02.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Mesorhizobium sp. M7A.F.Ca.AU.002.02.1.1"
                     /db_xref="taxon:2496671"
     Protein         1..>362
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          4..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvvaag aglksriida dyasagaaig
       61 kasdvakadv vlkvrrpgda elksykpgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdktaktl ainrdddlvk
      361 at
//
LOCUS       WP_127277794             425 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127277794
VERSION     WP_127277794.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..425
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43783
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdviveag agtrsripde efaktgavig
       61 kasdvakadv vlkvrrptda elksykagaa viaimdpygn daavaalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 pgkivttann vkivghlnvp grvaasasll yaknlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafakadq qpyvepaaip attlvadast papkkaaakk paapkspask
      421 pkgta
//
LOCUS       WP_127278289             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.
            M8A.F.Ca.ET.021.01.1.1].
ACCESSION   WP_127278289
VERSION     WP_127278289.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M8A.F.Ca.ET.021.01.1.1
  ORGANISM  Mesorhizobium sp. M8A.F.Ca.ET.021.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. M8A.F.Ca.ET.021.01.1.1"
                     /db_xref="taxon:2496757"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34502
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipteqdfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrsd
      181 fraerilrer llkkdnvrvi wdtivdeitg rpgkaplpps veglklrhav tgaeshlkvd
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvadd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127282906             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M4B.F.Ca.ET.017.02.2.1].
ACCESSION   WP_127282906
VERSION     WP_127282906.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M4B.F.Ca.ET.017.02.2.1
  ORGANISM  Mesorhizobium sp. M4B.F.Ca.ET.017.02.2.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mesorhizobium sp. M4B.F.Ca.ET.017.02.2.1"
                     /db_xref="taxon:2496649"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44105
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneqrvaa spdtvkrlag lgfevvvekg agtgsripdq dfaangakig
       61 tagdakkadv vlkvrrptda elkgykqgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 agkvvttang vkivghlnvp grvaasasll yaknlfafle tlvdkesktl aikrddelvk
      361 atmltdagrv vhpnfakadq qprlepaavp attlvaease kktapkktad kktatsksaa
      421 kpkgia
//
LOCUS       WP_127286932             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.
            M4B.F.Ca.ET.017.02.2.1].
ACCESSION   WP_127286932
VERSION     WP_127286932.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M4B.F.Ca.ET.017.02.2.1
  ORGANISM  Mesorhizobium sp. M4B.F.Ca.ET.017.02.2.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. M4B.F.Ca.ET.017.02.2.1"
                     /db_xref="taxon:2496649"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34455
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdiv ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrgd
      181 fraerilrer llkkenvrii wdtvvdeitg qpgkaplpps veglalrnva tgevtrlkvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127288218             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127288218
VERSION     WP_127288218.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53862
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn visgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_127289776             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M7A.F.Ca.US.011.01.1.1].
ACCESSION   WP_127289776
VERSION     WP_127289776.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.US.011.01.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.US.011.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mesorhizobium sp. M7A.F.Ca.US.011.01.1.1"
                     /db_xref="taxon:2496741"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44062
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvvetg agtrsripde efakagaaig
       61 kvsdvakadv vlkvrrpgdv elksykrgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsadmvasmk pgsvlvdlav erggnvegav
      301 pgqvvttang vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggki vhpafvkadq qppkghyvep aaipaktmva daspkkaapk kaaapkspss
      421 kpkgia
//
LOCUS       WP_127289951             417 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127289951
VERSION     WP_127289951.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42877
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripde efakigavig
       61 kagdvakadv vlkvrrpsea elkayrrgta viaimdpygn daavdalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsvamvasmk pgsvivdlav erggnvegav
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafie tlvdkttktl ainrdddlvk
      361 atmltdggqv vhpafagkpa vmiasaepak paaakkpaat kkpaapkspa nkskgia
//
LOCUS       WP_127304218             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127304218
VERSION     WP_127304218.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53864
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaattg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf kkg
//
LOCUS       WP_127291525             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127291525
VERSION     WP_127291525.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53656
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqigqgngf
      481 vsllsfvail iaginifggf avtrrmlnmf kkg
//
LOCUS       WP_127312579             332 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Mesorhizobium sp. M7A.F.Ca.CA.002.12.1.1].
ACCESSION   WP_127312579
VERSION     WP_127312579.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.CA.002.12.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.CA.002.12.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Mesorhizobium sp. M7A.F.Ca.CA.002.12.1.1"
                     /db_xref="taxon:2496735"
     Protein         1..>332
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          4..332
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglksriida dyasagaaig
       61 kasdvakadv vlkvrrpgda elksykpgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll ya
//
LOCUS       WP_127311946             285 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Mesorhizobium sp.
            M4B.F.Ca.ET.049.02.1.2].
ACCESSION   WP_127311946
VERSION     WP_127311946.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M4B.F.Ca.ET.049.02.1.2
  ORGANISM  Mesorhizobium sp. M4B.F.Ca.ET.049.02.1.2
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Mesorhizobium sp. M4B.F.Ca.ET.049.02.1.2"
                     /db_xref="taxon:2496752"
     gene            1..>285
                     /gene="trxB"
     Protein         1..>285
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          8..285
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdiv ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrgd
      181 fraerilrer llkkenvrvi wdtvvdeitg qpgkaplpps vegltlrnva tgevtrlkvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaag
//
LOCUS       WP_127310636             426 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127310636
VERSION     WP_127310636.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44049
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneqrvaa spdtvkrlag lgfevvvekg agtgsripdq dfaangakig
       61 tagdakkadv vlkvrrptdt elkgykqgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 agkvvttang vkivghlnvp grvaasasll yaknlfafle tlvdkesktl aikrddelvk
      361 atmltdagqv vhpnfakadq qprvepaavp attlvadase kktapkktad kkaatsksaa
      421 kpkgia
//
LOCUS       WP_127315827             423 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127315827
VERSION     WP_127315827.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43321
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripdd efgkagavig
       61 kaadvakadv vlkvrrpdea elkayrpgta viaimdphgn daavdalara gatafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fraaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttang vkivghlnva grvaasasll yarnlfafve tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafigkpa vmiasaepgk aaaaekpaap kkaaasrkla apkslankpk
      421 gia
//
LOCUS       WP_127318697             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_127318697
VERSION     WP_127318697.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34513
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaarallk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdvi ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilser lfkkdnirvi wdtvvdeitg qsgnmplpps veglklrnlv tgqemhltvd
      241 gvfvaighap avelfagklk qkpngylwta pdstctdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127325000             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M1A.F.Ca.IN.022.07.1.1].
ACCESSION   WP_127325000
VERSION     WP_127325000.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M1A.F.Ca.IN.022.07.1.1
  ORGANISM  Mesorhizobium sp. M1A.F.Ca.IN.022.07.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. M1A.F.Ca.IN.022.07.1.1"
                     /db_xref="taxon:2496767"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43565
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrmag lgfevivekg aglgsritdq efvtaggtig
       61 tagdaknadv vlkvrrptda elkgyksgaa viaimdpygn daalaamasa gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtagrtsv avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkvtktl aikrddelvk
      361 atmltdagqi vhpsfakaag qprtepaaip atvlvadaad kkpaprrraa akspspkpeg
      421 ta
//
LOCUS       WP_127331416             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M7A.F.Ca.MR.245.00.0.0].
ACCESSION   WP_127331416
VERSION     WP_127331416.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.MR.245.00.0.0
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.MR.245.00.0.0
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. M7A.F.Ca.MR.245.00.0.0"
                     /db_xref="taxon:2496778"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43530
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag agtrsripde efskagatig
       61 kasdvakadv vlkvrrpgda elksykpgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedde fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl afnrdddlvk
      361 atmltdggkv vhpafvkadq qphvepaaip aktmvadasp kkaapkkaaa skspsskpkg
      421 ia
//
LOCUS       WP_127332445             520 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter sp. NP-4(2019)].
ACCESSION   WP_127332445
VERSION     WP_127332445.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. NP-4(2019)
  ORGANISM  Marinobacter sp. NP-4(2019)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Marinobacter sp. NP-4(2019)"
                     /db_xref="taxon:2488665"
     Protein         1..520
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55587
     Region          1..520
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpkeid egekrvaltp dvarqlkelg ftlaietnag keasfdddqy reagveiied
       61 pkelwhssdi vmkvrppsqh pelgfygvel lgkgqtlisf lypaqnpell qdlsnhgvta
      121 lamdsvpris raqkmdalss maniagyrav veasqhfgrf ftgqitaagk ippakvlvig
      181 agvaglaaig aaksmgavvr afdtrpevke qvesmdaefl mldfegedgs gqggyaktms
      241 pefieaemal faeqakdvdi iittalipgk papelitedm vasmkpgsvi vdlaaetggn
      301 cklteadqvv vrhgvtligy tnlpsrlasq asqlyatnlr hllsdlcpek ngeivvnmed
      361 evirgatvvk egevtwpppa prlsaapktd mgdkarveve kaepkpkhpl aflvpvalag
      421 lgllglgsva ppefmghltv fvlscfvgym viwgvshslh tplmsvtnai ssiivigalm
      481 qisseqplvl ilavlavfit sinivggfav tqrmlrmfrk
//
LOCUS       WP_127332796             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Marinobacter sp. NP-4(2019)].
ACCESSION   WP_127332796
VERSION     WP_127332796.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. NP-4(2019)
  ORGANISM  Marinobacter sp. NP-4(2019)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Marinobacter sp. NP-4(2019)"
                     /db_xref="taxon:2488665"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34038
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msetkhsrli ilgsgpagyt aavyaaranl kptlitgiev ggqlttttdv dnwpgdndgv
       61 qgpelmqrml khaerfetsi vydtineadl rnrpfrlkgd sgeytcdali iatgasamyl
      121 gleseekfkg qgvsacatcd gffykkqkva vigggntave ealylsniad evtlvhrrds
      181 lraekilqdk lfekaengni nivwdhtlde vlgdgtgvtg mrikstkdds tqeldlagvf
      241 iaighkpntd lfagqldmen gyikirsgle gmatqssipg vfaagdvadh vyrqavtsag
      301 fgcmaaldae kfldqqd
//
LOCUS       WP_127334180             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Marinobacter sp. NP-4(2019)].
ACCESSION   WP_127334180
VERSION     WP_127334180.1
KEYWORDS    RefSeq.
SOURCE      Marinobacter sp. NP-4(2019)
  ORGANISM  Marinobacter sp. NP-4(2019)
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Marinobacteraceae; Marinobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Marinobacter sp. NP-4(2019)"
                     /db_xref="taxon:2488665"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56002
     Region          1..525
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipreif enerrvaatp psvhkliglg yevvveagag eaahysdaay ekvgaaiaad
       61 taslwqeadf ilkvrapmeh pvlnrhevdl mkegaflvsy iwpaqnpell drlaarkits
      121 faidslpris raqkmdalsa maniagyrav ieaanhfgrf ftgqvtaagk vppakimvig
      181 agvaglaaig aansmgaivr afdtrlevke qvesmgaefl qldfgdedgs gtggyakqms
      241 defikaemal faeqakevdi iittalipgk papklitadm vksmkpgsvi vdlaserggn
      301 celtepgtvs rqhgvtligy tdlpsrmakv asdlyatnlv hllteltpek dgqpqvnmed
      361 dvirgltvvr enditwpppq peapvspapp pgteepsaad maaakrhadr rsligrgvll
      421 ivtvlalygv gahapesflq hftvfvlacf igwqviwnvt pslhtplmsv tnaisgiivi
      481 gailhlaqaa niavaimafv avliasinvg ggfrvthrml kmfrk
//
LOCUS       WP_127339884             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium cupreum].
ACCESSION   WP_127339884
VERSION     WP_127339884.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium cupreum
  ORGANISM  Flavobacterium cupreum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Flavobacterium cupreum"
                     /db_xref="taxon:2133766"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33965
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaaran mnpvlyqgmq pggqltttne venfpgyvdg
       61 vtgpemmvql qeqakrfgsd irdgwatkvd fsgdihkvwi ndsielhcet viistgasak
      121 ylglpseqhy lqmgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rsekfrasri meervrkten ieillnhdtv evlgdgnvvh aikalnktta evveipatgf
      241 fvaighkpnt difkdylnld etgyiintpg tsntnvpgvf vagdaadhvy rqaitaagtg
      301 cmaaldaery laake
//
LOCUS       WP_127335435             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.
            M1A.F.Ca.IN.022.05.2.1].
ACCESSION   WP_127335435
VERSION     WP_127335435.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M1A.F.Ca.IN.022.05.2.1
  ORGANISM  Mesorhizobium sp. M1A.F.Ca.IN.022.05.2.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. M1A.F.Ca.IN.022.05.2.1"
                     /db_xref="taxon:2496760"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34609
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgteiv ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacapcd gffyrgkdva vvgggnsave ealylanlar svtvihrrnd
      181 fraerilrer lfkkdnvrii wdtvvdeitg qpgkaplpps vdglklrnvv tgevsrlqvd
      241 gvfvaighap avelfigklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127348026             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudidiomarina mangrovi].
ACCESSION   WP_127348026
VERSION     WP_127348026.1
KEYWORDS    RefSeq.
SOURCE      Pseudidiomarina mangrovi
  ORGANISM  Pseudidiomarina mangrovi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Pseudidiomarina.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudidiomarina mangrovi"
                     /db_xref="taxon:2487133"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33718
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 maeakhcrll ilgsgpagyt aavyaaranl kpvlvtgmqq ggqlttttev enwpgdpegl
       61 tgpdlmvrmq qhaekfntem vfdhinrvdf sskplrlfgd sgeytadavi iatgasakyl
      121 glpsetafmg kgvsacatcd gffyrqqkvc vvgggntave ealylanias evhvihrrds
      181 fraekilvdr lmdkaangnv tlhlnktlde vlgdnmgvsa vrikdmhsgd tselevmgcf
      241 iaighqpnts ifagqldmhd gyikvqsglh gnatatsvag vfaagdvmdh iyrqaitsag
      301 tgcmaaldae ryldalk
//
LOCUS       WP_127349543             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Campylobacter fetus].
ACCESSION   WP_127349543
VERSION     WP_127349543.1
KEYWORDS    RefSeq.
SOURCE      Campylobacter fetus
  ORGANISM  Campylobacter fetus
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Campylobacteraceae; Campylobacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Campylobacter fetus"
                     /db_xref="taxon:196"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33418
     Region          3..309
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mldvaiiggg paglsaglya trgglknvvm fekgmpggqi tsssemenyp gvatvmdgls
       61 fmapwteqct rfglkheman vqrvsknsdg sfsiflegnk vetakavivc tgstpkragf
      121 kgedeffgkg istcatcdgf fyknkevavl gggdtaleea eylanicskv ylihrrdsfr
      181 aapitvekvk knpkielitn arvdevygdr vagvkgvkvk lqdgsvrdla vpgiftfvgl
      241 dvrndvlkde ngnficdtls tgqvrvnlkm qtnipglfaa gdlredapkq vvcaaadgat
      301 aalsamsyie slhy
//
LOCUS       WP_127350467             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium botulinum].
ACCESSION   WP_127350467
VERSION     WP_127350467.1
KEYWORDS    RefSeq.
SOURCE      Clostridium botulinum
  ORGANISM  Clostridium botulinum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium; Clostridium botulinum group.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Clostridium botulinum"
                     /db_xref="taxon:1491"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34570
     Region          9..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnkknknldl miigagpagl saaiyaarak lnmiliengi iggqvrssyt venypgfkki
       61 egnrladlmq eqatdlgati defdmvekiq lnnnekivet seyiykptvl iistgaaark
      121 lpipsegkfs gkgihycaic dgamyegktv gvigggnaal eealfltkfa skvymirryd
      181 yfkgekatle evennskiei lynwdlvdvy gsnfidkali knvktkeeke lkldgifgfi
      241 gsepktelfk eyisltpkgy iktnenmetn ikgvyaagdv rekqfrqitt avadgtiaal
      301 aaekyimekt rek
//
LOCUS       WP_127354726             331 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces soli].
ACCESSION   WP_127354726
VERSION     WP_127354726.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces soli
  ORGANISM  Streptomyces soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Streptomyces soli"
                     /db_xref="taxon:2487275"
     gene            1..331
                     /gene="trxB"
     Protein         1..331
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35029
     Region          7..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfregim
       61 gpdlmdnmra qaerfgaeli pddvvevdlt gdiktvtdsa gtvhqaktvi vttgsqhrkl
      121 glpredelsg rgvswcatcd gfffkehnia vigggdtale eatflsrfat svtvvhrrdt
      181 lraskamqer afadpkisfv wdsevaeihg enklsgltlr ntktgetsel pvtglfiaig
      241 hdprtdlfkg vldldhdgyl kvetpstrtn ipgvfaagdv vdhtyrqait aagtgcsaal
      301 daerylaalg dadadadaeq tlepekaaaa v
//
LOCUS       WP_127355085             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces soli].
ACCESSION   WP_127355085
VERSION     WP_127355085.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces soli
  ORGANISM  Streptomyces soli
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Streptomyces soli"
                     /db_xref="taxon:2487275"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52545
     Region          8..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msesppqqig vvtestaget rvaatpasvr qllglgyevv vaseagaasg fsddayaeag
       61 arigdawqad vvlkvnapsh eeigklrdga tlvgliapgl npdlldelar rpvtvlsmda
      121 vprisraqsm dvlssmania gyravieaah afgrffagqv taagkvppak vlvagagvag
      181 laaigaagsl gavvratdpr aevadqvrsl ggeflaveve qesstdgyak atseaydrra
      241 aeiyseqaad vdiivttali pgrpaprlit aadvasmkpg svivdmaaaq ggnvegtvsg
      301 kaivtdndvt iigytdlvgr lpaqasqlyg tnlvnllkll tpgedgqltl dfddivqrsv
      361 tvvrdgektw ppppaqvsaa paqpaaapaa apqakeprls paarygligl gmimmfllia
      421 isptqlaanf tvfalavvig yyvigkvhha lhtplmsvtn aisgivvvga llqighdgaa
      481 vtvlsfvaim lttvnifggf avtrrmlgmf skg
//
LOCUS       WP_127365203             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Brevibacterium linens].
ACCESSION   WP_127365203
VERSION     WP_127365203.1
KEYWORDS    RefSeq.
SOURCE      Brevibacterium linens
  ORGANISM  Brevibacterium linens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Brevibacteriaceae; Brevibacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Brevibacterium linens"
                     /db_xref="taxon:1703"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34302
     Region          4..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtdtqlviig sgpagytaav yaaranlspv viagsvtagg elmnttdven fpgfpagvqg
       61 pelmesmreq aekfgadviy ddvetlklnp gaheietalg srytakavil atgsayrelg
      121 lpnekklsgh gvswcatcdg fffrdqhiav igggdsalee atfltrfask vtlvhrrqel
      181 rasqamqdra nadeklefll dsevaevhge dsltgltirn tvtgetselp vtgmfvaigs
      241 dprtslfadq lemradgyls vdgrtsktsv egvfaagdvi dsvyrqaita agsgcsaald
      301 aehylgdlea askpavaeaa paetvvas
//
LOCUS       WP_127368040             426 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127368040
VERSION     WP_127368040.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43794
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglksriida dyasagaaig
       61 kasdvakadv vlkvrrpgda elksykpgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vssamvasmk pgsvivdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafvkadq qpakgqyvep aaipaktmva daspkkaask kaaapkspss
      421 kpkgia
//
LOCUS       WP_127368155             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_127368155
VERSION     WP_127368155.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34560
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipteqdfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilrer llkkdnvrvi wdtivdeitg rpgktplpps vvglklkhav tgevshlkid
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127371108             397 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Mesorhizobium sp. M7A.F.Ca.US.003.02.1.1].
ACCESSION   WP_127371108
VERSION     WP_127371108.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.US.003.02.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.US.003.02.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Mesorhizobium sp. M7A.F.Ca.US.003.02.1.1"
                     /db_xref="taxon:2496710"
     Protein         1..>397
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglksriida dyasagaaig
       61 kasdvakadv vlkvrrpgda elksykpgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdktaktl ainrdddlvk
      361 atmltdggkv vhpafvkadq qpakgqyvep aaipakt
//
LOCUS       WP_127373495             349 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Mesorhizobium sp. M7D.F.Ca.US.004.03.1.1].
ACCESSION   WP_127373495
VERSION     WP_127373495.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7D.F.Ca.US.004.03.1.1
  ORGANISM  Mesorhizobium sp. M7D.F.Ca.US.004.03.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Mesorhizobium sp. M7D.F.Ca.US.004.03.1.1"
                     /db_xref="taxon:2496702"
     Protein         1..>349
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          4..346
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdviveag aglnsriida dyasagaaig
       61 kasdvakadv vlkvrrpsda elksykpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegav
      301 pgqvvttann vkivghlnvp grvaasasll ygrnlfafve tlvdkttkt
//
LOCUS       WP_127381470             422 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127381470
VERSION     WP_127381470.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43431
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglnsrivda dyasagaaig
       61 kasdvakadv vlkvrrpgda elksyrpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl afnrdddlvk
      361 atmltdggkv vhpafvkadq qphvepaaip aktmvadasp kkaapkkaaa skspsskpkg
      421 ia
//
LOCUS       WP_127389045             293 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Mesorhizobium sp.
            M7A.F.Ca.CA.001.08.2.1].
ACCESSION   WP_127389045
VERSION     WP_127389045.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.CA.001.08.2.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.CA.001.08.2.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Mesorhizobium sp. M7A.F.Ca.CA.001.08.2.1"
                     /db_xref="taxon:2496692"
     gene            1..>293
                     /gene="trxB"
     Protein         1..>293
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          8..293
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipteqdfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilrer llkkdnvrvi wdtivdeitg rpgktplpps veglklkhav tgevshlkid
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyr
//
LOCUS       WP_127393408             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M4B.F.Ca.ET.019.03.1.1].
ACCESSION   WP_127393408
VERSION     WP_127393408.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M4B.F.Ca.ET.019.03.1.1
  ORGANISM  Mesorhizobium sp. M4B.F.Ca.ET.019.03.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mesorhizobium sp. M4B.F.Ca.ET.019.03.1.1"
                     /db_xref="taxon:2496651"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44131
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maraifipre ldpneprvaa spetvkrlvg lgfdvivekg aglgsripdq dftaaggttg
       61 taadarkaei vlkvrrptda elkgymsgaa vlaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 agkvvttang vkivghlnvp grvaasasll yaknlfafle tlvdkenktl aikrddelvk
      361 atmltdagqv vhpnfakadq qprvepaavp attlvaease kktapkktad kktatsksaa
      421 kpkgia
//
LOCUS       WP_127395766             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.
            M7A.F.Ca.ET.027.03.2.1].
ACCESSION   WP_127395766
VERSION     WP_127395766.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.ET.027.03.2.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.ET.027.03.2.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. M7A.F.Ca.ET.027.03.2.1"
                     /db_xref="taxon:2496656"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34576
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipteqdfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlar svtvihrrsd
      181 fraerilrer llkkdnvrvi wdtivdeitg rpgktplpps veglklkhaa tgevshlkid
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127396064             427 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127396064
VERSION     WP_127396064.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43911
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglnsrivda dyasagaaig
       61 kasdvakadv vlkvrrpgda elksyrpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltnggki vhpafikadq qphlepaaip aktmvadasd kpaaakkaas kkpaasksps
      421 skpkgia
//
LOCUS       WP_127402556             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127402556
VERSION     WP_127402556.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53920
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 atvwacpliy kvnapsedel pllkegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlev aeqiesmggk flkldfpqes ggsddgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrpge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflnhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_127405362             424 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127405362
VERSION     WP_127405362.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..424
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43688
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvav spdtvkrlag lgfevvvekg agtgsripde efakagaaig
       61 kaadaskadv vlkvrrptda elkgykqgaa viaimdpygn daavaamaea gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 agkvvttang vkivghlnvp grvaasasll yaknlfafle tlvdkesksl aikrddelvk
      361 atmltdagqv vhpnfakadq qprvepaaip attmaadaap kaapkkaadk kstskpaaks
      421 kgia
//
LOCUS       WP_127408187             513 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Neisseria
            meningitidis].
ACCESSION   WP_127408187
VERSION     WP_127408187.1
KEYWORDS    RefSeq.
SOURCE      Neisseria meningitidis
  ORGANISM  Neisseria meningitidis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Neisseria meningitidis"
                     /db_xref="taxon:487"
     Protein         1..513
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53822
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigipresl sgetrvactp atvallgklg fetvvesgag laaslddaay qtagatvadk
       61 aavwacpliy kvnapsegel pllnegqtiv sflwprqnea lvealrakkv nalamdmvpr
      121 israqaldal ssmanisgyr avieaanafg rfftgqitaa gkvppaqvlv igagvaglaa
      181 igtanslgav vrafdtrlem aeqiesmggk flkldfpqes ggsgdgyakv msdefiaaem
      241 klfaeqakev diiittaaip gkpapklitk emvesmksgs vivdlaaatg gnceltrlge
      301 lsvtgngvki igytdmanrl agqssqlyat nlvnltklls pnkdgeitld fedviirnmt
      361 vthdgeitfp pppiqvsaqp qqtpsekaap aakpepkpvs lwkklapavi aavlvlwvga
      421 vapaaflkhf ivfvlacvig yyvvwnvshs lhtplmsvtn aisgiivvga llqisqgngf
      481 vtllafiail iasinifggf fvtrrmlnmf rkg
//
LOCUS       WP_127408371             422 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127408371
VERSION     WP_127408371.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43585
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag agtrsripde efskagatig
       61 kasdvakadv vlkvrrpgda elksykpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedde fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsvamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkmtktl ainrdddlvk
      361 atmltdggkv vhpafvkadq qphvepaaip aktmvadasp kkaapkkaaa skspsskpkg
      421 ia
//
LOCUS       WP_127412895             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1].
ACCESSION   WP_127412895
VERSION     WP_127412895.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1"
                     /db_xref="taxon:2496707"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43915
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglksriida dyasagaaig
       61 kvsdvakadv vlkvrrpdna elksykpgaa viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaettggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp grvaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafvkadq qppkgqyvep aaipaktmva daspkkaapk kaaapkspss
      421 kpkgia
//
LOCUS       WP_127415013             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.
            M7A.F.Ca.US.006.01.1.1].
ACCESSION   WP_127415013
VERSION     WP_127415013.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1"
                     /db_xref="taxon:2496707"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34537
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipteqdfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilrer llkkdnvrvi wdtivdeitg rpgktplpps veglklkhav tgevshlkid
      241 gvfvaighap avelfagklk qkpngylwta pdstctdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127409518             428 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M2A.F.Ca.ET.039.01.1.1].
ACCESSION   WP_127409518
VERSION     WP_127409518.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M2A.F.Ca.ET.039.01.1.1
  ORGANISM  Mesorhizobium sp. M2A.F.Ca.ET.039.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Mesorhizobium sp. M2A.F.Ca.ET.039.01.1.1"
                     /db_xref="taxon:2496746"
     Protein         1..428
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44219
     Region          6..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(19,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(48,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maatqtifip reldaneprv aaspetvkrl aglgfevive kgaglgsrip dqdfvtaggt
       61 lgtaadakka dvvlkvrrpt daelkgykpg aaviaimdpy gndaalaama kagitafsme
      121 fmpritraqv mdvlssqanl agyqavidaa aeydralpmm mtaagtvpaa ktfimgvgva
      181 glqaiatarr lgavvtatdv rpavkeqvqs lgakflaved eefkaaetag gyakemskey
      241 qakqaaltae hiakqdivit talipgrpap klvsaamvas mkpgsvivdl averggnveg
      301 aqpgkvvtte ngvkivghln vpgrvaasas llyaknlyaf letmvdkaek elaikrddel
      361 vkatmltdgg kivhpnfaka teaprtepaa iaatimvada sdkpaakktv akkpaaaksp
      421 sskpegta
//
LOCUS       WP_127409693             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M2A.F.Ca.ET.039.01.1.1].
ACCESSION   WP_127409693
VERSION     WP_127409693.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M2A.F.Ca.ET.039.01.1.1
  ORGANISM  Mesorhizobium sp. M2A.F.Ca.ET.039.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mesorhizobium sp. M2A.F.Ca.ET.039.01.1.1"
                     /db_xref="taxon:2496746"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43042
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maraifipre ldpneprvaa spetvkrlag lgfdvivekg aglgsrildq dfaavgaaig
       61 kaadaskadv vlkvrrptda elkgykpgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlfafle tmvdkatktl aikrddelvm
      361 atmltdggrv vhpnfakaae eprtepaaip attmvaeaad akpaakkkaa aqpkgta
//
LOCUS       WP_127416079             457 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1].
ACCESSION   WP_127416079
VERSION     WP_127416079.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Mesorhizobium sp. M7A.F.Ca.US.006.01.1.1"
                     /db_xref="taxon:2496707"
     Protein         <1..457
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..456
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 adiiakvrpp eaaeiarlrp gktlisffyp sqnkdlleqa mgtgadiiam dmvprisraq
       61 kmdalssman iagyraviea sanfgrfftg qvtaagkvpp akvlvvgagv aglaaigaat
      121 slgaityafd vrpevaeqie smgaefvyld fpeaqvdgaa tggyaapssp efrdaqlmkf
      181 relapqvdiv ittalipgrd apmlwtkdmv damkpgsvii dlaaerggnc eltkadrkiv
      241 tangvtivgy tdfpslmaaq sstlystnir hmltdltpak dgkvvhnmed dvirgatvay
      301 rgaitfpppp pkiqaiaaqk pkekakgltl eerrakeaad fktatnvqvt llgigtilml
      361 lvgnyapqsf mghfvvfmls cfvgfqviwn vshslhtplm avtnavsgii ilgalaqigs
      421 sswlvaivaa lsvliatini vggffvtrrm lamfhks
//
LOCUS       WP_127419979             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Mesorhizobium sp.
            M7A.F.Ca.CA.001.15.1.1].
ACCESSION   WP_127419979
VERSION     WP_127419979.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.CA.001.15.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.CA.001.15.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Mesorhizobium sp. M7A.F.Ca.CA.001.15.1.1"
                     /db_xref="taxon:2496713"
     gene            1..>308
                     /gene="trxB"
     Protein         1..>308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          3..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstrviiigs gpagytaaiy aaralcnpvl icgpqpggql tvttdvenyp gfpdivqgpw
       61 lmeqmqkqae hcgativtdh vetadlserp frvitssgkr yetealiiat gaqarwlglp
      121 seerfrgfgv sacatcdgif firkhvvvvg ggntaaeeal flskyaskvt lvhrgaslra
      181 ekilqqrlfn dtkievvweh vvdevlgnee palsvegirl rhartgavqn lpadglfvai
      241 ghspsvrvfg dqlrqkpggy iwvepgstrt svpgvfaagd vsddvyrqav taaglgcmaa
      301 ieaerfla
//
LOCUS       WP_127424656             426 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127424656
VERSION     WP_127424656.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43777
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvsa spetvkrlvg lgfgvivekg aglgsritdq dfaaagaaig
       61 kaadaskadv vlkvrrptda elkgykpgaa viaimdpygn daalaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatkel aikrddelvk
      361 atmltdggqv vhpsfakaae qlrtepaaip atiivaevsa kpaaktpaak kpaaaksass
      421 kskgta
//
LOCUS       WP_127426953             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127426953
VERSION     WP_127426953.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54873
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeiv agearvamtp qsalqlaklg hvclieagag aragfsdedy rnagvtvldt
       61 akalysaadv itkvrppera eigqltsgkt lisffypaqn aellamaaat sanviamdmv
      121 prisraqkmd alssmaniag yravieagsn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatalg aityafdvrp evaeqiesig aefvfldfdg anqdgaatgg yaapsspefr
      241 qkqlakfrel apeidivitt alipgreapk lwladmvaam krgsvvidla aerggncdlt
      301 vpdarivsdn gvvivgytdf psrmsaqast lyatnirhmi adltpgkagk ivhnmeddvv
      361 rgatvafege vaypppppkv qaiaaqkpke kdkqlspeek raselavfra qtrsqvglla
      421 vgtalvlvlg iyapasfmnh fivfvlacfi gfqviwkvsh slhtplmavt naisgivilg
      481 allqigsgnl lvvilaavsv liatvnvvgg flvtrrmlam fqks
//
LOCUS       WP_127428018             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_127428018
VERSION     WP_127428018.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34472
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdiv ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylanlak svtvihrrgd
      181 fraerilrer lfqkdnvrvi wdtvvdeitg qpgkaplpps veglklrnva tgevsrlkvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127431895             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            anhuiense].
ACCESSION   WP_127431895
VERSION     WP_127431895.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium anhuiense
  ORGANISM  Rhizobium anhuiense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium anhuiense"
                     /db_xref="taxon:1184720"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55490
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mfigsprerf egearvamtp dsatqlqklg yhcaietgag klagfsdday ravgvtvvds
       61 idalyasvdv iaqvrppean dlarlsaskt lisffypaqn kelleqaktt ganvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkippakv lvigagvagl
      181 aavgtsislg aityafdvrp evaeqiesmg aefvfldfke qqqdgaatgg yaspsspefr
      241 eaqlkkfrei apdidivvst alipgrdapk lwladmvaam kpgsvvvdla aerggncdlt
      301 vpdqkivsen gvtvigytdf psrmaaqast lystnirhmm tdltpkkdgv lvhnmeddvi
      361 rgatvafqge itypppppki qaiaaqkrqe kpkeltpeer raaeasafks atrqqvgllv
      421 vggvlmalig ayapsafmgh fivfalscfv gfqviwgvsh slhtplmavt naisgiiiig
      481 allqvtaggw lvtalaavsv aiatinivgg fmvtrrmlnm fqks
//
LOCUS       WP_127439047             323 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_127439047
VERSION     WP_127439047.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34229
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgim
       61 gpelmdnmra qaerfgaelv pddvvavdlt gevktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkitfv wdsevaevqg dqklsglklr nvktgelsdl pvtglfiaig
      241 hdprtelfkg qldldpegyl kvdspstrtn ltgvfaagdv vdhtyrqait aagtgcsaal
      301 daerflaalt dedkaepekt aav
//
LOCUS       WP_127446889             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_127446889
VERSION     WP_127446889.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53618
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafsvtd vretlrtgtp knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_127458365             315 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Paenibacillus].
ACCESSION   WP_127458365
VERSION     WP_127458365.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33711
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksvvvgtg psgltaaiyl aranlsplvi egpepggqlt tttevenfpg fpegimgpel
       61 menmrkqaer fgaefktgwv nsvelttrpf klqveglgei etetliistg asakllgign
      121 ekenigrgvs tcatcdgfff rgkkiivvgg gdsameeanf ltrfasevrl vhrrdelras
      181 kimqdrargn ekvkwalnnt plevvsgekg vtglkvknnt tgeeeiietd gifvaightp
      241 ntkflggqid tdelgyiivk pgttetnipg vfacgdvqdt kyrqaitaag sgcaaaleae
      301 kfleghivhd wsqsl
//
LOCUS       WP_127457069             314 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Paenibacillus].
ACCESSION   WP_127457069
VERSION     WP_127457069.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33307
     Region          4..304
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mhhkaiiigt gpagltaaiy larasmeplv iegiqpggql ttttevdnfp gfpdgimgpe
       61 lmdnmrkqal rfgakiqsgr vtevdmskrp ftlflegggq ltadsiiist gasakklgip
      121 gesenigkgv stcatcdgff frnkkiivig ggdtameeaq fltrfasevr vvhrrddlka
      181 skimqdharg nekvvwslnr tpleveagpl gvkglrvrnn etgeeellea dgiflaight
      241 pntgflggql ptdelgylqv ipgtsktaip gvfacgdvqd hiyrqaitsa gsgamaalda
      301 eryisehaal vtsr
//
LOCUS       WP_127459160             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus elgii].
ACCESSION   WP_127459160
VERSION     WP_127459160.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus elgii
  ORGANISM  Paenibacillus elgii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenibacillus elgii"
                     /db_xref="taxon:189691"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33657
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mynsviigtg pggltaaiyl araglkplvi egpepggqlt tttevenfpg fpegimgpel
       61 mdnmrkqaer fgaefrtgwv nkadlskrpf tlsvegmgdi qaetvivstg asakylgipg
      121 ekenvgrgvs tcatcdgfff rgkkiivigg gdsameeanf ltrfasevvl vnrrtelras
      181 kimqeraran ekiswqlnrt pleviagerg vtglkvrnnd tgeeeiievd gifvaightp
      241 ntkflddqlt tddhgyllvk pgttetnipg vfacgdvqds ryrqaisaag tgcmaaldce
      301 rflesaelke lar
//
LOCUS       WP_127470323             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Thiomicrorhabdus aquaedulcis].
ACCESSION   WP_127470323
VERSION     WP_127470323.1
KEYWORDS    RefSeq.
SOURCE      Thiomicrorhabdus aquaedulcis
  ORGANISM  Thiomicrorhabdus aquaedulcis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiotrichales; Piscirickettsiaceae; Thiomicrorhabdus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Thiomicrorhabdus aquaedulcis"
                     /db_xref="taxon:2211106"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33894
     Region          3..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mvtkhcklli lgsgpagyta avyaaranle pviitgmqqg gqlttttevd nwpgdpeglt
       61 gpdlmqrmqq haerfgteil fdhihtanlk krpfkligda geytcdalii atgasakylg
      121 lpseeafkgk gvsacatcdg ffyrnqkvav igggntavee alylsniaae vtivhrrdqf
      181 scekilakhl lekaqngnik iefnstleev lgdkmgvtgv rlnnlptgis kdvdvagvfi
      241 aightpntgi fadqlkmeng ylhvksgrkg nttqtsrkgi faagdvmdqh ykqaitssat
      301 gcmaaldaek yldnlak
//
LOCUS       WP_127473603             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium
            sulfonylureivorans].
ACCESSION   WP_127473603
VERSION     WP_127473603.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sulfonylureivorans
  ORGANISM  Microbacterium sulfonylureivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Microbacterium sulfonylureivorans"
                     /db_xref="taxon:2486854"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35261
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrhviiigsg pagytaaiya aranleplvv assveaggdl mtttdvenfp gfpegiqgpd
       61 lmtkmqeqae rfgaevlfdd vvsldldgav kkivlgsgke ydarsivyat gsahrkigie
      121 geerlsgrgv sycatcdgff frerviavvg ggdsameeat fltkfaskvy vihrrdelra
      181 skimqerafa nekiefvwns evvdvlgeda vtgvvlentv dgtrsdlald glfvaigndp
      241 rthlvhdkld ltpegtiwvd grssrtsvag vfaagdvidp tyrqavtaag sgtvaaldve
      301 hylaslgeag apdvvgdqie glpevtgese adaa
//
LOCUS       WP_127477363             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sulfurivermis fontis].
ACCESSION   WP_127477363
VERSION     WP_127477363.1
KEYWORDS    RefSeq.
SOURCE      Sulfurivermis fontis
  ORGANISM  Sulfurivermis fontis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Thiohalomonadales; Thiohalomonadaceae; Sulfurivermis.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Sulfurivermis fontis"
                     /db_xref="taxon:1972068"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33734
     Region          7..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqtkhcrll ilgsgpagyt aavyaaranl npvlitgmqq ggqlmtttei dnwpggehgl
       61 tgpglmqqme aharrfntei ifdtivkadl skrpftltgd satytcdali iatgasamyl
      121 gleseekfkg rgvsgcatcd gffyrnqnva vigggntave ealylsniak hvtvvhrrdk
      181 frcekilsdq lmekvkegkv tiewnhevde vlgdnsgvtg lrikstqdgs kkelaltgvf
      241 iaighkpntd lfagqltleh gyivtqggrn gnatatnieg vfaagdvadh nyrqaitsag
      301 tgcmaaldae afleskg
//
LOCUS       WP_127481816             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium oxydans].
ACCESSION   WP_127481816
VERSION     WP_127481816.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium oxydans
  ORGANISM  Microbacterium oxydans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Microbacterium oxydans"
                     /db_xref="taxon:82380"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34134
     Region          7..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msiqevelvi igsgpagyta avyaaragla pvvlagsvta ggalmtttev enfpgfvdgv
       61 qgpelmqsmr aqaerfgari llddavlvdl dgpvktvetg sgeafharav iltmgsayrk
      121 lgiadeerlt grgvswcatc dgfffreqei vvvgggdsam eealfltrfa skvtvvhrrg
      181 efraskimaq rvldhpkiev awnsevaglv gaekveavtl rdiitgtere lpatgvfiai
      241 ghdprselit giidtdadgy vlvehpstrt nlagvfaagd lvdhtyrqai taagtgcaaa
      301 qdaqhylaal devapvltat eevfa
//
LOCUS       WP_127481948             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium oxydans].
ACCESSION   WP_127481948
VERSION     WP_127481948.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium oxydans
  ORGANISM  Microbacterium oxydans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Microbacterium oxydans"
                     /db_xref="taxon:82380"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34333
     Region          7..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msiqqvelvi igsgpagyta avyaaragls pvvlagsvta ggalmtttev enfpgfvdgv
       61 qgpelmesmr aqaerfgari llddavlvdl dgplktvetg sgetflarav iltmgsayrk
      121 lgiadeerlt grgvswcatc dgfffreqei vvvgggdsam eealfltrfa skvtvvhrrg
      181 efraskimaq rvldhpkiei awnsevagli gaekveavtl rdtvtgaerk lpatgvfvai
      241 ghdprseiva rlvdtdadgy vlvehpstrt nvsgvfaagd lvdhtyrqai taagtgcaaa
      301 qdaqhylaal deaepviaek realla
//
LOCUS       WP_127484457             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus ehimensis].
ACCESSION   WP_127484457
VERSION     WP_127484457.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus ehimensis
  ORGANISM  Paenibacillus ehimensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenibacillus ehimensis"
                     /db_xref="taxon:79264"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33584
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mynsviigtg pggltaaiyl araglkplvi egpepggqlt tttevenfpg fpegimgpel
       61 mdnmrkqaer fgaefrtgwv nkadlskrpf tlsvegmgdi qaetvivstg asakylgipg
      121 ekenvgrgvs tcatcdgfff rgkkiivigg gdsameeanf ltrfasevvl vnrrtelras
      181 kimqeraran ekiswklnrt pleviagerg vtglkvrnnd tgeeeiievd gifvaightp
      241 ntkflegqlt tdehgyllvk pgttetnipg vfacgdvqds ryrqaisaag tgcmaaldce
      301 rflesaelke lal
//
LOCUS       WP_127491100             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus glycanilyticus].
ACCESSION   WP_127491100
VERSION     WP_127491100.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus glycanilyticus
  ORGANISM  Paenibacillus glycanilyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Paenibacillus glycanilyticus"
                     /db_xref="taxon:126569"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32717
     Region          6..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhqqtviigt gpagltaaiy laranltplv iegtqpggql ttttevenfp gfpdgitgpe
       61 lmdnmrkqae rfgtrfqsgf vtrvdaskrp ftlyleggte itadavilst gasakmvgip
      121 gevenigqgv stcatcdgff frnkkiivig ggdtameeal fltrfasevr vvhrreelra
      181 sqimqdrarg nakiswslna aplevlsgdk gvtglkvrnn atgeeevlet dgiflaighr
      241 pntgflggqi qtdeqgyvev vpgtsrtnvp gvfacgdvmd piyrqaitsa gsgakaaldc
      301 esflfeqh
//
LOCUS       WP_127493977             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acinetobacter calcoaceticus].
ACCESSION   WP_127493977
VERSION     WP_127493977.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter calcoaceticus
  ORGANISM  Acinetobacter calcoaceticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter; Acinetobacter
            calcoaceticus/baumannii complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Acinetobacter calcoaceticus"
                     /db_xref="taxon:471"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33713
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhsrlii lgsgpagysa avyaaranlk ptliaglqlg gqlttttevd nwpgdpeglt
       61 gpalmdrmqa haerfgtelv ydhinevdln vrpfvlkgdm eeytcdalii atgataqylg
      121 leseqkfmgq gvsacatcdg ffyknqkvmv vgggntavee alylsniaah vtlvhrrdsl
      181 rsekilqdhl fakekegkis iiwnheveev lgdntgvtsv rlkstqdetk qdvevhglfv
      241 aighkpntam fdaqlnlrdg yiqvqsgtsg natatsvagv faagdvadsi yrqaitsags
      301 gcmaaldaek yldnlg
//
LOCUS       WP_127498595             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus glycanilyticus].
ACCESSION   WP_127498595
VERSION     WP_127498595.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus glycanilyticus
  ORGANISM  Paenibacillus glycanilyticus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Paenibacillus glycanilyticus"
                     /db_xref="taxon:126569"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33294
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksiiigtg pagltaaiyl aranmkplvi egpepggqlt tttevenfpg fpegimgpdl
       61 manmrkqaer fgaefmtgwv nsvdmserpf klqvegkgef vgetiiistg asarwlgipg
      121 ekdnigrgvs tcatcdgfff rnkkivvigg gdsameeanf ltrfatnvel vnrrdelras
      181 kimqdraren ekiswslnrt pleveangmg vtglkvrnna tgedetiqtd gvfiaightp
      241 ntkflngqid tdehgyikvk pgssetnvpg vfacgdvqdn kyrqaitaag sgcmaaldce
      301 rflenigsh
//
LOCUS       WP_127509802             294 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Actinoplanes solisilvae].
ACCESSION   WP_127509802
VERSION     WP_127509802.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes solisilvae
  ORGANISM  Actinoplanes solisilvae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Actinoplanes solisilvae"
                     /db_xref="taxon:2486853"
     gene            <1..>294
                     /gene="trxB"
     Protein         <1..>294
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..272
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 aaranlkplv iegvqsggal mtttevenfp gfrdgimgpe lmdnmraqae rfgaefltdd
       61 vtrvelgdkp teagteglkt vwvgekeyfa ravilstgsa wrplgvpgeq ellghgvssc
      121 atcdgfffrn hnivvvgggd sameeatflt rfaetvtivh rrdsfraskv mqlralnnpk
      181 ikvewnsvve eiighdgkvs gariknvqtg eekvldvtgv fvaighdprs dlfkgqidld
      241 degyvkvdhp strtnlpgvf aagdlvdhty rqaitaagtg taaaldaerf iasf
//
LOCUS       WP_127517378             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127517378
VERSION     WP_127517378.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35198
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthharvli igagpagyta aicaalanlk pllvtgrqag gqlttmayve nfpgfaepvk
       61 gpllmehmrq qaenvgtkli ydiitsvdlw krpfrlqahs gdtyladali iatgaqprwl
      121 glpsekifag fgvsacatsd gffyrnkevv vvgggntave ealylsnlas kvtvvhrrnr
      181 fraepilqdr llarpnvdvi wnhvidevig kreprksvtg vrildvntgd akelpthglf
      241 ighdpatalf rgqldmdgag yikvgswstk tsvpgvlaag dvidpvfrra isaagmgsma
      301 aleaekflae pvetpaemre ieiigvyg
//
LOCUS       WP_127519328             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127519328
VERSION     WP_127519328.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35610
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaepvq
       61 gpwlmeqmre qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg irirevntdd vkeltthglf
      241 vaighdpata lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaeksl aehspdpavr pivphetemv ga
//
LOCUS       WP_127522203             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127522203
VERSION     WP_127522203.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35596
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtglqag gqltitadve nypgfaepvq
       61 glwlmeqmre qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg irirevntdd vkeltthglf
      241 vaighdpata lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaeksl aehspdpavr pivphetemv ga
//
LOCUS       WP_127522351             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp. Z1-4].
ACCESSION   WP_127522351
VERSION     WP_127522351.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. Z1-4
  ORGANISM  Mesorhizobium sp. Z1-4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. Z1-4"
                     /db_xref="taxon:2448478"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34413
     Region          8..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mssrhapvli igsgpagyta aiyaarallk pllvagleqg gqltittdve nypgfadpvq
       61 gpwlmeqmlk qaenvgaeia ndvivevdls vrpfrargds gteytgdali iatgakakwl
      121 glpseqkfmg fgvsacatcd gffyrdkdvv vvgggntave ealylsnlas hvtlvhrrde
      181 lraerilqer lfakknvtvv wdsvvdeikg eagkpplpas vngvvlknvk tgtttempvh
      241 gvfvaighap avelfkdklk hkpngylwtd pgstrtdvpg vfaagdvtdd ifrqavtaag
      301 lgcmaaleae rylaeqgahr eaae
//
LOCUS       WP_127522598             421 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. Z1-4].
ACCESSION   WP_127522598
VERSION     WP_127522598.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. Z1-4
  ORGANISM  Mesorhizobium sp. Z1-4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Mesorhizobium sp. Z1-4"
                     /db_xref="taxon:2448478"
     Protein         1..421
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43220
     Region          4..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,289,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,279..280,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtifvpre sdtteprvaa spetvkryag fgfdvvveag agaasritdd efvqagakig
       61 kaadagkadi vlkvrrpnaa elktykkgaa vfatmdpygn egevaamgka gisafamefm
      121 pritraqsmd vlssqanlag yqavidaaet ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvtatdvra aageqvaslg akfimtdalk dasgeggyar elteaekkaq
      241 aelvashiak qdivittali pgrpapklvs admvksmrpg svivdlaver ggnvegakag
      301 etvttangvk iighlnvagr vaasasllya knlyafletm vdkekksfai dpeeelakat
      361 llthggqvvh anfkaaakpa akpaarkaap kpaaaktdkd agakpvrkap arkpaakggk
      421 s
//
LOCUS       WP_127523011             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127523011
VERSION     WP_127523011.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35307
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthharvli igagpagyta aicaalanlk pllvtgrqag gqltittdve nypgfpkpvq
       61 gpwlmkqmrl qaenvgtkvm ydiitsvdlw krpfrlqahs gdtyladali iaagaqprwl
      121 glpsektfag fgvsacatsd gflyrdkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvdvi wnhvidevig ereprkgvta vrirdvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsvpgvlaag dvidpvfrra itaaamgsma
      301 aleaekflae pvetpaemre ieiigvyg
//
LOCUS       WP_127523417             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp. Z1-4].
ACCESSION   WP_127523417
VERSION     WP_127523417.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. Z1-4
  ORGANISM  Mesorhizobium sp. Z1-4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Mesorhizobium sp. Z1-4"
                     /db_xref="taxon:2448478"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33056
     Region          9..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtnlktcnvl iigsgpagyt aaiyaaranl qpvvveglqa ggqltsttdv enysgfadpi
       61 qgpwlmeqmr qqalnvgvel vgdivtgidt strpfkcttd sgltyaartv ivstgaqakw
      121 lgldseakfn grgvsacatc dgfffrnrrv avvgggntav eealylsaic nevvlvhrrd
      181 tlraekvlqd rlqakanisv ewnkrvdeil gddngvnala lrdtrtgaqs rievdgvfva
      241 ighspstqll tgkveidndg yvltepgttr tslpglfaag dvqdktyrqa itaagtgcma
      301 aldaerflag vah
//
LOCUS       WP_127523425             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. Z1-4].
ACCESSION   WP_127523425
VERSION     WP_127523425.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. Z1-4
  ORGANISM  Mesorhizobium sp. Z1-4
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Mesorhizobium sp. Z1-4"
                     /db_xref="taxon:2448478"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55743
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpketl kgenrvamtp dsalqlqklg hdcvieagag vaagfgdday ravgvevvkt
       61 atalwkaadi iakvrppsdt eigwltrdkt lisffwpaqn qallefcrtr gasaiamdmv
      121 prisraqkmd alssmaniag yravieagsn fgrfftaqvt aagkvppakv lvvgagvagl
      181 aaigaatslg aiayafdvrs evaeqiesmg aefvfldfed qaqdgaaacg yaapsspefr
      241 qkqlekfrel apqmdivitt alipgrdapk lwlkdmteam kpgsvvvdla aerggncdlt
      301 vpgekvvtkn gvtiigytdf psrmasqsst fysanirhml aeltpakdgv ivhnmeddvi
      361 rgatvihrge itfpppppkv qaiaaqkpre kakeltpeek rtheiaafka qtrqqftlla
      421 aggsaillag lfapasfmqh livfvlsvfv gfqviwnvsh alhtplmavt navssiiilg
      481 allqigsgsw lvlllaaasv lmaginifgg fmvtrrmlam fqks
//
LOCUS       WP_127525301             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127525301
VERSION     WP_127525301.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34580
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtarhtkvli igsgpagyta aiytaramls pvliagmeqg gqlmittdve nypgyadpvq
       61 gpwmmeqmln qaihvgteiv ndlvidvdls vrpfriktds gtdwtadali iatgakakwl
      121 gieteptfmg fgvsacatcd gffyrnkevi vvgggnsave ealylsnlak tvtvvhrrda
      181 fraekilqer lfakpnvkvi wdhevleylg tpakppmpas vngvklrntk tgetsdmaid
      241 gvfvaighap avelfkgklr qkpngylwta pdstatdvag vfaagdvtdd iyrqavtaag
      301 mgcmaaleae kylaghmpva iaae
//
LOCUS       WP_127533125             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus kobensis].
ACCESSION   WP_127533125
VERSION     WP_127533125.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kobensis
  ORGANISM  Paenibacillus kobensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenibacillus kobensis"
                     /db_xref="taxon:59841"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33204
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myktiiigtg pagltaaiyl aranmaplvi egpqpggqlt tttevenfpg fpegilgsel
       61 msnmrkqaqr fgatfmtgwv nsvdfsnrpf tvnveggqql qaesiiistg asakylgipg
      121 eqdnvgrgvs tcatcdgfff rgkkivvigg gdsameeahf ltrfasevkl vnrrselras
      181 kimqdrarsn ekiswalnnt pvevvagglg vtglkvrcne tgqeeiietd gvfvaightp
      241 ntgflggqie tddhgyivvk pgttetnipg vfacgdvqdt kyrqaitaag sgcmaaleae
      301 rfleeehsks vsv
//
LOCUS       WP_127525925             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127525925
VERSION     WP_127525925.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35386
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthharvli igagpagyta aiyaalanlk pllvtgrqag gqltittdve nypgfpkpvq
       61 gpwlmkqmrl qaenvgtsvv ydiitsvdlw krpfrlqahs gdtyladali iatgaqprwl
      121 glpsektfag fgvsacassd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrnr
      181 freesilrdr llakpnvdvi wnhvidevig ereprkgvta vrirdvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsipgvlaag dvidpvfrra isaagmgsma
      301 aleaekflae plvtpvetre ieiigvyg
//
LOCUS       WP_127533447             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus kobensis].
ACCESSION   WP_127533447
VERSION     WP_127533447.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus kobensis
  ORGANISM  Paenibacillus kobensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus kobensis"
                     /db_xref="taxon:59841"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33765
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksiiigtg psgltaaiyl aranmkplvi egpepggqlt tttevenfpg fpegimgpdl
       61 manmrkqaer fgaefrtgwv nsvdmsqrpf klqveghgel vaetliistg asarylgipg
      121 ekdnvgrgvs tcatcdgfff rgkkivvvgg gdsameeanf ltrfasevel vhrrdelras
      181 kimqdraren dkirwslnkt pvevvasgmg vtalkvrnne tgedellets gvfvaightp
      241 ntgflggqid tdehgyikvk pgttetnvpg vfacgdvqdn kyrqaitaag sgcmaaldae
      301 kfldghvtqd wsvsl
//
LOCUS       WP_127544332             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinoplanes sp. OR16].
ACCESSION   WP_127544332
VERSION     WP_127544332.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes sp. OR16
  ORGANISM  Actinoplanes sp. OR16
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Actinoplanes sp. OR16"
                     /db_xref="taxon:946334"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34285
     Region          7..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpsgytaa lyaaranlkp lviegvqsgg almttteven fpghrdgimg
       61 pelmdnmraq aekfgaefit ddvsrvelgd kptepgtegl ktvwvgdkqf faravilatg
      121 sawrpigvpg eqellgrgvs scatcdgfff rnqhivvvgg gdsameeatf ltrfaetvti
      181 vhrrdtfras kvmqkraldn ekikvewnsv veeilgedgk vsgarirnvq tgetrvldvt
      241 gvfvaighdp rselfkgqve lddegyvkvd spstrtnvpg vfaagdlvdh tyrqaitasg
      301 tgcaaaldae rfiasfvel
//
LOCUS       WP_127545345             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127545345
VERSION     WP_127545345.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34608
     Region          2..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 miigagpagy taaiyaaran lkpllvtglq aggqltittd venypgfaep vqgpwlmeqm
       61 reqaenvgte vvydiitsvd lsdrpfrleg dsgdayiada liiatgaqar wlglpsertf
      121 ngfgvsacat cdgffyrnke vvvggggnta vqealylsnl askvtvvhrr drfraepilq
      181 drllakpnve viwnhvidev igeqeprksv tgmrirevnt ddvkeltthg lfvaighdpa
      241 talfrgqldm ddagyikvgs wstkttvpgv laagdvidsv frqaitaagm gsmaaleaek
      301 slaehspdpa vrpivphete mvga
//
LOCUS       WP_127551390             506 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinoplanes sp. OR16].
ACCESSION   WP_127551390
VERSION     WP_127551390.1
KEYWORDS    RefSeq.
SOURCE      Actinoplanes sp. OR16
  ORGANISM  Actinoplanes sp. OR16
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae; Actinoplanes.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Actinoplanes sp. OR16"
                     /db_xref="taxon:946334"
     Protein         1..506
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51703
     Region          1..505
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 miigvprdph pgerrvaatp atvaqlvklg ydvvvqsgag egssfsdeay agsgatigdp
       61 laadvvfain pppaeqldkl apgttvigml nprldpdlva elarrpital smdavprisr
      121 aqsldvlssm aniagyravv eaahafgrff tgqvtaagkv apakvlvaga gvaglaaiga
      181 agslgaivra tdprpevadq vkslggeylp veapdvevss tgyakemsdd yneraarlya
      241 sqagdvdiii ttalipgrpa prlitapmva smkpgsvivd maaanggnve gtvpgevvvt
      301 andvtiigyt dlpgrlpaqa sqlygtnlvn lmklmtpekd grlvldfddv vqrsitvvrd
      361 geltwppppv avsaapapva aapapvagkp vekprnplpl igagaaalfv ltafapaalr
      421 ghltvfalai vigyyvighv hhalhtplms vtnaisgiiv vgallqighg davitalafv
      481 atllasinif ggfavtrrml amfsrs
//
LOCUS       WP_127556376             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Saccharospirillum alexandrii].
ACCESSION   WP_127556376
VERSION     WP_127556376.1
KEYWORDS    RefSeq.
SOURCE      Saccharospirillum alexandrii
  ORGANISM  Saccharospirillum alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Saccharospirillum.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Saccharospirillum alexandrii"
                     /db_xref="taxon:2448477"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34232
     Region          2..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mstqhhelii lgsgpagyta avyaaranlk pvlitgmqmg gqltttteve nwpgghaelq
       61 gpqlmeemka haerfnteii fdhihttdla kppftlvgdq gtytcdalii stgasarylg
      121 leseeafkgk gvsacatcdg ffyrnkevsv igggntavee alylsniask vhvihrrdsf
      181 rsekiladrl mdkvqegkvv lhwnrtldev lgdemgvtgi rikstqneet eelkldgvfv
      241 aightpntqi fegqldmagg yikvksgleg natatsvpgv fasgdvmdhv yrqaitsagt
      301 gcmaaldaek yldnlkhag
//
LOCUS       WP_127556442             530 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Saccharospirillum alexandrii].
ACCESSION   WP_127556442
VERSION     WP_127556442.1
KEYWORDS    RefSeq.
SOURCE      Saccharospirillum alexandrii
  ORGANISM  Saccharospirillum alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Saccharospirillaceae; Saccharospirillum.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Saccharospirillum alexandrii"
                     /db_xref="taxon:2448477"
     Protein         1..530
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55761
     Region          7..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msltlavpvd rapgetrvpv tpdttrklid lgftvliepg agaraqfada lyeqagaele
       61 adtaklyqra dvllkingpq aqaegltgse lealgstpek aktwisflap gqneplleqf
      121 ngqhatalsl daiprisraq kmdvlssman iagyraviea anqfgrfftg qitaagkipp
      181 akvlvigagv aglaaigaak slgaivrafd trkevkeqve smggefltve leedgagtgg
      241 yakemskafi daemalfmeq arevdiiitt alipgkpapk liteamvkam qpgsvvvdla
      301 apnggncect vkdevvkahd vtvigftnla araatqasql lannlwrlle hlcpnkdgql
      361 vidltdeitr sctvvhggdi twpppppkls atpkpaapsa qktteksppa prkarpialy
      421 wviagalilg lgavapadfv shftvfvlai figwqviwnv shslhtplms vtnaisgiii
      481 lgallqisgs gswlvsvlat isvlvasini aggfyvtrrm lnmfrkgdps
//
LOCUS       WP_127557572             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nioella ostreopsis].
ACCESSION   WP_127557572
VERSION     WP_127557572.1
KEYWORDS    RefSeq.
SOURCE      Nioella ostreopsis
  ORGANISM  Nioella ostreopsis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Nioella.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Nioella ostreopsis"
                     /db_xref="taxon:2448479"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33426
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtrhtrvl iigsgpagyt agvyasraml epilvqgiep ggqlttttev enwpgdtevq
       61 gpdlmirmea hakamgceii gdiitsldtt qrpfvaqgds gttytadavi lctgarakwl
      121 glpseeafkg fgvsacatcd gffyrgqeiv vigggntave ealfltnfas kvtlihrrde
      181 lraekilidr lmknpkiapl whhvleevvg tdnpkgveav rvkhvetgei teipckgvfv
      241 aighapanel vkdvlelhng gyvkveagst rtsipgifaa gdltdhkyrq avtsagmgcm
      301 aaldaehwla eqe
//
LOCUS       WP_127565591             374 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Glycocaulis alkaliphilus].
ACCESSION   WP_127565591
VERSION     WP_127565591.1
KEYWORDS    RefSeq.
SOURCE      Glycocaulis alkaliphilus
  ORGANISM  Glycocaulis alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Glycocaulis.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Glycocaulis alkaliphilus"
                     /db_xref="taxon:1434191"
     Protein         1..374
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38176
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavltety pgearvaatp dsvkalvkag asisiekgag lsasvtdgaf eaagakcvtr
       61 aaaikdgqlf ltvrrpdaat laklpkgavl vglldphgdk dfakacaeag vnalameytp
      121 ritraqsmda lssqsnlagy ravieaagly grafpmmmta agtvaaakaf vmgagvaglq
      181 aiatarrlga ivsandvrpa akeqvgslga kfiavedeef kaaetaggya kemsaeykak
      241 qaelvaahia kqdivvttal ipgrpaprli tkamvetmkp gsviidiaaa tggnceltka
      301 deivehggvk iagftnlpar laadasqlla knfvnlapll rgedgalspq wedeiikgmt
      361 ltrdgaavhp slgg
//
LOCUS       WP_127566056             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Glycocaulis alkaliphilus].
ACCESSION   WP_127566056
VERSION     WP_127566056.1
KEYWORDS    RefSeq.
SOURCE      Glycocaulis alkaliphilus
  ORGANISM  Glycocaulis alkaliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Maricaulales; Maricaulaceae; Glycocaulis.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Glycocaulis alkaliphilus"
                     /db_xref="taxon:1434191"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34633
     Region          8..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtetrhskvv iigsgsagyt aaiyaaraml epiviaglqp ggqltithev enypgfasvi
       61 egpwlmeqmk aqaenvgaei iadiiveadf skrpftmkgd ggtiytadsv iiatgasakw
      121 lgleseqslq gfgvsacatc dgffyrgkev vvvgggntav eealfltrfa skvtlihrrd
      181 slraekiaqa rlfdnekiev iwdsaveeil aegdvpgvtg vrvknlktge etklatdgvf
      241 iaighapats lfegqlemkd ggylvtkpgs tltsipgvfa agdvtddiyr qaitaagmgc
      301 maaleaerwl aemehhaase gkaaksdaa
//
LOCUS       WP_127573677             333 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Georgenia faecalis].
ACCESSION   WP_127573677
VERSION     WP_127573677.1
KEYWORDS    RefSeq.
SOURCE      Georgenia faecalis
  ORGANISM  Georgenia faecalis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Allobogoriellales; Allobogoriellaceae; Georgenia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Georgenia faecalis"
                     /db_xref="taxon:2483799"
     gene            1..333
                     /gene="trxB"
     Protein         1..333
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35165
     Region          9..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mthdaarlhe tviigsgpag ytaaiyaara nlepvvlags itaggalvnt tevenfpgfp
       61 esimgpelmd rmekqaekfk adiryedava vdlsgeiktv ttgegdvlrt rtvilatgsa
      121 yreldlpkek elggrgvsyc atcdgfffrd qhivvvgggd sameeatflt kfaskvtvvh
      181 rrdelraski maerafandk iefawnseva elhgterltg itlrdtvtge lreldatglf
      241 vaighvprtd llrghvelde sgyivvtsps tatsvpgvfa cgdavdhtyr qaitaagtgc
      301 aaaldaeryl aalgeaaepa adasqtpqga val
//
LOCUS       WP_127576212             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus barengoltzii].
ACCESSION   WP_127576212
VERSION     WP_127576212.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus barengoltzii
  ORGANISM  Paenibacillus barengoltzii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paenibacillus barengoltzii"
                     /db_xref="taxon:343517"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34147
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhkvlvigtg pagltaaiyl aranlspvvi eglepggqlt tttevenfpg fpegimgpel
       61 mdnmrkqaer fgaqfraswv ekvdfskrpf qvtleggevl esesviistg asakylgipg
      121 eqenvgrgvs tcatcdgfff rgkklivvgg gdsameeanf ltrfatevti vhrreelras
      181 kimqgrarsn ekirwalnrt plevvtdedg vkvkglkvrn nadgqeelle adgvfvaigh
      241 tpntkflgga vetddhgyiv vkpgttetnv pgvfacgdvq dtryrqaita agsgcmaamd
      301 cekflegsmv hdwsgptgs
//
LOCUS       WP_127582784             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127582784
VERSION     WP_127582784.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34510
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtarhtkvli igsgpagyta aiytaramls pvliagmeqg gqlmittdve nypgyadpvq
       61 gpwmmeqmln qaihvgteiv ndlvtdvdls vrpfriktds gtdwtadali iatgakakwl
      121 gieteptfmg fgvsacatcd gffyrnkevi vvgggnsave ealylsnlak tvtvvhrrda
      181 fraekilqer lfakpnvkvi wdhevleylg tpakppmpas vngvklrntk tgatsdmaid
      241 gvfvaighap avelfkgklr qkpngylwta pdstatdvag vfaagdvtdd iyrqavtaag
      301 mgcmaaleae kylaghmpva iaae
//
LOCUS       WP_127583170             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus koleovorans].
ACCESSION   WP_127583170
VERSION     WP_127583170.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus koleovorans
  ORGANISM  Paenibacillus koleovorans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Paenibacillus koleovorans"
                     /db_xref="taxon:121608"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34430
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mssttyhsiv vgtgpaglta aiylaranlk plviegpepg gqltttteve nfpgfpegim
       61 gpelmdnmrk qaerfgaefr tgwinevdls rrpftlkleg ghelkaetli istgasakll
      121 giegervnig rgvstcatcd gfffrgkkii vvgggdsame eanfltrfas evrlvhrrde
      181 lraskimqdr argnakvaws lnrtplevva gekgvtalkv rnnatgeeel letdgifvai
      241 ghtpntaflg gqletdengy lvvkpgtcet nipgvfacgd vqdhryrqav taagsgcmaa
      301 ldcekflegq avhdwsqsln k
//
LOCUS       WP_127586189             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium medicae].
ACCESSION   WP_127586189
VERSION     WP_127586189.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39503
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfiake sdpnegrvag sidsvkklks lgfdvvvesg agqgsripdq dyekagarig
       61 katdaktadv ilkvrrpsaq evagyrsgai viaimdpygn eesisamaga gltsfamelm
      121 pritraqsmd vlssqanlag yqavidaane ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsgeyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vtremldsmk pgsvavdlav erggniegae
      301 agkvtevggv kivghlnvpg riaasaslly aknlvtflet mvsketeala lnmedelvka
      361 talthggsvv hpafggamkg ek
//
LOCUS       WP_127588894             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127588894
VERSION     WP_127588894.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35571
     Region          8..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrsrvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaepvq
       61 gpwlmeqmrq qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vggggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg mrirevntdd vkeltthglf
      241 vaighdpata lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaeksl aehspdpavr pivphetemv ga
//
LOCUS       WP_127591409             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127591409
VERSION     WP_127591409.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34991
     Region          6..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthhtrvli igagpagyta aiyaaranlk pllvtgprag gqltiateve nypgfaepvq
       61 gpwlmeqmrl qaenvgtkvm ydiitsvdls krpfhlkgds gdtyiadali iatgaqarwl
      121 glpseekfng lgvfacascd gffyrnkevv vvgggniavq ealhlsslas kvtvvhrqdc
      181 fraepilrdr llarpnvevv wkhvldevvg eceprnwvtg vrirdvntgd vrelptnglf
      241 vaighdpata lfrgqldmdr agyikvgsws tktsvpgvla agdvidpvfr raisaagtgs
      301 maaleaakfl aepvetreie iigvyg
//
LOCUS       WP_127595005             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus lautus].
ACCESSION   WP_127595005
VERSION     WP_127595005.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus lautus
  ORGANISM  Paenibacillus lautus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paenibacillus lautus"
                     /db_xref="taxon:1401"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34135
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksivigtg pagltaaiyl aranlkplvi egmqpggqlt tttevenfpg fpqgimgpel
       61 mdnmrqqaer fgaefksawv esvdfserpf kvnvegmgel laesviistg asakylgipg
      121 eqenvgrgvs tcatcdgfff rgkkiivigg gdsameeasf ltrfassvtv vnrrtelras
      181 kimqdraren ekiqwaldrt pvevvtsetg vkglevrnne tgedelieae gvfvaightp
      241 ntgflgnqit tdptgyilvk pgttetnipg vfacgdvqdt ryrqaitaag tgcmaamdce
      301 kyleghmvhd wsetlnk
//
LOCUS       WP_127599172             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nitratireductor alexandrii].
ACCESSION   WP_127599172
VERSION     WP_127599172.1
KEYWORDS    RefSeq.
SOURCE      Nitratireductor alexandrii
  ORGANISM  Nitratireductor alexandrii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Nitratireductor.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Nitratireductor alexandrii"
                     /db_xref="taxon:2448161"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55315
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtprevl dgearvamtp dsarmlqklg fvcaietgag enagfsdaay eeagveivks
       61 aerlwadadl vakvrpptgt evallstgkv lisffhpaqn ealmrqaadt gatvvamdmv
      121 prisraqkld alssmaniag yravieagnn fgrfftgqvt aagkvpparv lvvgagvagl
      181 aaigtstalg aityafdvrp evaeqiesmg aefvyldfns dqqdgsasgg yaapsspefq
      241 akqlekfral apeidivitt alipnrdapv lwtkdmvaam kpgsvivdla aerggncelt
      301 vkedkivtdn kvtiigytdf psrmatqast lyannvrqfv celaptkdgt lvhdmhddvi
      361 rgstvahqga vtypppppkv raiaaaprkd kpkepspeek ralevaafra qtrrqagllv
      421 agavlialvg avapasfmqh fivfvlacfi gfqviwnvsh alhtplmavt naisgivvlg
      481 allqigsgdw lvvtlaaism liasinivgg flvtrrmlam fqks
//
LOCUS       WP_127596858             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127596858
VERSION     WP_127596858.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34720
     Region          2..302
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 miigagpagy taaiyaaran lkpllvtglq aggqltittd venypgfaap vqgpwlmeqm
       61 rqqaenvgte vvydiitsvd lsdrpfrleg dsgntyiada liiatgaqar wlglpsertf
      121 ngfgvsacat cdgffyrnke lvvvgggnta vqeahylsnl askvtvvhrr drfraepilq
      181 drllpkpnve viwnhvidev igeqeprksv tgvrirdvnt gdvkeltthg lfvaighdpa
      241 talfrgqldm deagyikvgs wstkttvpgv laagdvidpv frqaisaagm gcmaaleaek
      301 flaehsphpv vrpivpreae miga
//
LOCUS       WP_127604632             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus chibensis].
ACCESSION   WP_127604632
VERSION     WP_127604632.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus chibensis
  ORGANISM  Paenibacillus chibensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus chibensis"
                     /db_xref="taxon:59846"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33952
     Region          2..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksivigtg pagltaaiyl aranmkplvi egmqpggqlt ttteienfpg fpdgimgpel
       61 mdnmrkqaer fgaefktgwv dkvdfskrpf tltvegmgei qaesviistg asakylgipg
      121 eqenvgrgvs tcatcdgfff rgkkilvigg gdsameeagf ltrfgssvtl vhrreelras
      181 kimqdrargn ekiiwalnrv plevvagdng vkglkvfnne skqeeliead gvfvaightp
      241 ntqfldnqit tdevgyimvk pgttetnipg vfacgdvqdv ryrqaisaag tgcmaamdce
      301 kflegsmvhd wsetl
//
LOCUS       WP_127605028             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus chibensis].
ACCESSION   WP_127605028
VERSION     WP_127605028.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus chibensis
  ORGANISM  Paenibacillus chibensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenibacillus chibensis"
                     /db_xref="taxon:59846"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33497
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksviigtg pagltaaiyl aranlnplii egpqpggqlt tttevenfpg fpegimgpel
       61 mdnmrkqaer fgaefrtgwv nqvelngrpf kldvegmgqi etetliistg atakylgipg
      121 eqdnvgrgvs tcatcdgfff rgkeiivigg gdsaleeasf ltrfaskvtl vhrrtelrgs
      181 kimqdrvrsn dkvewalnrt pvevvaddrg vkglkvlnne tgeeelieas gvfvaighhp
      241 ntgflggqit tdangyivvq pgtsetnipg vfacgdvqdt ryrqaitaag sgcmaamdce
      301 kyieslehha avl
//
LOCUS       WP_127607907             315 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Paenibacillus].
ACCESSION   WP_127607907
VERSION     WP_127607907.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus
  ORGANISM  Paenibacillus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus"
                     /db_xref="taxon:44249"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33627
     Region          2..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhkaiiigtg pagltaaiyl aranlnplvi egpepggqlt tttevenfpg fpegimgpel
       61 manmrkqaer fgaefktgwv nsvdtsqrpf klnvegmgel vaesliistg asakllgitn
      121 ekesigrgvs tcatcdgfff rgkkiivvgg gdsameeanf ltrfasevtl vhrrselras
      181 kimqdraren skikwslnrt plevisgdkg vtglkvlnne tgveevietd gifvaighkp
      241 ntgflagqik tdevgyilvk pgttqtnveg ifacgdvqds kyrqaitaag sgcmaalece
      301 kfleghlvhd yslsl
//
LOCUS       WP_127609282             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127609282
VERSION     WP_127609282.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35627
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaepvq
       61 glwlmeqmre qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg irirevntdd vkeltthglf
      241 vaighdpata lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaeksl aehspdpavr pivphetemv ga
//
LOCUS       WP_127611197             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Croceicoccus ponticola].
ACCESSION   WP_127611197
VERSION     WP_127611197.1
KEYWORDS    RefSeq.
SOURCE      Croceicoccus ponticola
  ORGANISM  Croceicoccus ponticola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Croceicoccus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Croceicoccus ponticola"
                     /db_xref="taxon:2217664"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34624
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtthntrmli igsgpaglsa aiygaragme pivvqglqpg gqltittdve nypgfrdviq
       61 gpwlmqemqa qaehvgtrmm wdtivdidla ggssfvargd sgdeyigevl viatgaqakw
      121 lgvegeqaws gkgvsacatc dgffyrgkkv vvigggntav eealyltnhs ddvtlihrrd
      181 elraekilqe rlfnsdkist lwnksverfe gedgkglthl ilkdtvtgee srfdtegafv
      241 aighspatel fkgkldmddn gylivepgtp ktalpgvfac gdvmdhiyrq avtaagtgcm
      301 aaldaerfla tleftkekae aae
//
LOCUS       WP_127615128             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127615128
VERSION     WP_127615128.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35639
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthptrvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaapvq
       61 gpwlmeqmrq qaenvgtevv ydiitsvdls drpfrlegds gntyiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkelv vvgggntavq eahylsnlas kvtvvhrrdr
      181 fraepilqdr llpkpnvevi wnhvidevig eqeprksvtg vrirdvntgd vkeltthglf
      241 vaighdpata lfrgqldmde agyikvgsws tkttvpgvla agdvidpvfr qaisaagmgc
      301 maaleaekfl aehsphpvvr pivpreaemi ga
//
LOCUS       WP_127616584             312 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Sinorhizobium meliloti].
ACCESSION   WP_127616584
VERSION     WP_127616584.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..312
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=35679
     Region          5..172
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mgildifskr rdreaglpdv ytyddvpqkl riqcthilld rlkrpsdnhw shdpphetyq
       61 fivkglrkey gvfvlsdgik hdqgnyfsdy ytflgtapte rfldamelgm raietvasew
      121 nychendaak lseeaikein yrfrengfgy eyidgkiirv dsaflhaevt kpalallrgk
      181 iyagaqeeyl sahqhykesk ykeaivdclk sfestmkaic dkrrwayakn satakelini
      241 ciqnalipay wqnnvnslrs llessvptgr nkvaghgqgt dpkqveepiv ryimhmtgat
      301 ilflaeaere lp
//
LOCUS       WP_127624347             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127624347
VERSION     WP_127624347.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35271
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthharvli igagpagyta aicaalanlk pllvtgrqag gqlttmayve nfpgfaepvk
       61 gpllmeqmrq qaenvgtklm ydiitsvdlw krpfrlqahs gdtyladali iatgaqprwl
      121 glpsektfag fgvsacatsd gffyrnkevv vvgggntave ealylsnlas kvtvvhrrnr
      181 fraepilqdr llarpnvdvi wnhvidevig ereprksvtg vrildvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgpwstk tsvpgvlaag dvidpvfrra isaagmgsma
      301 aleaekilae pvetpaemre ieiigvyg
//
LOCUS       WP_127623436             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Sinorhizobium meliloti].
ACCESSION   WP_127623436
VERSION     WP_127623436.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..>322
                     /gene="trxB"
     Protein         1..>322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthharvli igagpagyta aicaalanlk pllvtgrqag gqltittdve nypgfpkpvq
       61 gpwlmkqmrl qaenvgtkvm ydiitsvdlw krpfrlqahs gdtyladali iaagaqprwl
      121 glpsektfag fgvsacatsd gflyrdkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvdvi wnhvidevig ereprkgvta vrirdvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsvpgvlaag dvidpvfrra itaaamgsma
      301 aleaekflae pvetpaemre ie
//
LOCUS       WP_127624853             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium meliloti].
ACCESSION   WP_127624853
VERSION     WP_127624853.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39522
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfiake sdpnegrvag svesvkklks lgfdvvveag aglgsripdq eyekagarvg
       61 taadaktadv ilkvrrpsaq eisgyrsgav viaimdpygn eeaisamaga glttfamelm
      121 pritraqsmd vlssqanlag yqavidaaye ydralpmmmt aagtvpaaki fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemsgeyqv
      241 kqaalvaehi akqdivitta lipgrpaprl vtremldsmk pgsvvvdlav erggniegae
      301 agkvtevggv rivghlnvag riaasaslly aknlvtflet mvsketkala lnmedelvka
      361 talthggavv ppafggamrg ek
//
LOCUS       WP_127626541             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127626541
VERSION     WP_127626541.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35726
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaepvq
       61 gpwlmeqmrq qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg irirevntdd vkeltthglf
      241 vaighdpeta lfrgqldmdd agyikvgsws tktivpgvla agdvidsvfr qaitaagmgs
      301 maaleaekfl aehspdpavr pvvphetemv ga
//
LOCUS       WP_127631472             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127631472
VERSION     WP_127631472.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35746
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaepvq
       61 gpwlmeqmrq qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg mrirevntdd vkeltthglf
      241 vaighdpeta lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaekfl aehspdpavr pivphetemv ga
//
LOCUS       WP_127632984             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127632984
VERSION     WP_127632984.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35638
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaepvq
       61 gpwlmeqmrq qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvag irirevntdd vkeltthglf
      241 vaighdpeta lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaeksl aehspdpavr pivphetemv ga
//
LOCUS       WP_127633671             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127633671
VERSION     WP_127633671.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34589
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtarhtkvli igsgpagyta aiytaramls pvliagmeqg gqlmittdve nypgyadpvq
       61 gpwmmeqmln qaihvgteiv ndlvtdvdls vhpfriktds gtdwtadali iatgakakwl
      121 gieteptfmg fgvsacatcd gffyrnkevi vvgggnsave ealylsnlak tvtvvhrrda
      181 fraekilqer lfakpnvkvi wdhevleylg tpakppmpas vnglklrntk tgetsdmaid
      241 gvfvaighap avelfkgklr qkpngylwta pdstatdvpg vfaagdvtdd iyrqavtaag
      301 mgcmaaleae kylaghmpva iaae
//
LOCUS       WP_127633849             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127633849
VERSION     WP_127633849.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35375
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthlarvli igagpagyta aicaalanlk pllvtgrqag gqlttmayve nfpgfaepvk
       61 gpllmeqmrq qaenvgtklm ydiitsvdlw krpfrlqahs gdtyladali iaagaqprwl
      121 glpsekifag fgvsacatsd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llarpnvdvi wnhvidevig kreprkwvtg vrildvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsvpgvlaag dvidpvfrra itaaamgsma
      301 aleaekflae pveppaemre ieiigvyg
//
LOCUS       WP_127640663             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127640663
VERSION     WP_127640663.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34608
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtarhtkvli igsgpagyta aiytaramls pvliagmeqg gqlmittdve nypgyadpvq
       61 gpwmmeqmln qaihvgteiv ndlvtdvdls vrpfriktds gtdwtadali iatgakakwl
      121 gieteptfmg fgvsacatcd gffyrnkevi vvgggnsave ealylsnlak tvtvvhrrda
      181 fraekilqer lfakpnvkvi wdhevleylg tpakppmpas vnglklrntk tgetsdmaid
      241 gvfvaighap avelfkgklr qkpngylwta pdstatdvpg vfaagdvtdd iyrqavtaag
      301 mgcmaaleae kylaghmpva iaae
//
LOCUS       WP_127641560             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127641560
VERSION     WP_127641560.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35620
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaepvq
       61 gpwlmeqmre qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vvgggntavq ealylsnlas kvtvvqrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg mrirevntdd vkeltthglf
      241 vaighdpata lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaeksl aehspdpavr pivphetemv ga
//
LOCUS       WP_127635750             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127635750
VERSION     WP_127635750.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35686
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaepvq
       61 gpwlmeqmre qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 rlpsertfng fgvsacatcd gffyrnkevv vggggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg mrirevntdd vkeltthglf
      241 vaighdpata lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaeksl aehspdpavr pivphetemv ga
//
LOCUS       WP_127641974             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127641974
VERSION     WP_127641974.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34598
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtarhtkvli igsgpagyta aiytaramls pvliagmeqg gqlmittdve nypgyadpvq
       61 gpwmmeqmln qaihvgteiv ndlvtdvdls vrpfriktds gtdwtadali iatgakakwl
      121 gieteptfmg fgvsacatcd gffyrnkevi vvgggnsave ealylsnlak tvtvvhrrdt
      181 fraekilqer lfakpnvkvi wdhevleylg tpakppmpas vngvklrntk tgetsdmaid
      241 gvfvaighap avelfkgklr qkpngylwta pdstatdvag vfaagdvtdd iyrqavtaag
      301 mgcmaaleae kylaghmpva iaae
//
LOCUS       WP_127643484             527 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium meliloti].
ACCESSION   WP_127643484
VERSION     WP_127643484.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55117
     Region          1..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtpkeas gearvaitpe salqlqqlgh acvveagaga gagvsddayr avgvavvega
       61 aelfdetdvi vkvrpptvde igrlsagqtl isffypgqng ellelarang vnviamdmvp
      121 risraqkmda lssmaniagy rsvieagnnf grfftgqita agkvppakvl vigagvagla
      181 aigvatslga qtyafdvrpe vaeqiesmga efvyldladg qgsnqqggaa tggyaapssp
      241 efrekqlakf relapemdiv ittalipgrd apklwladmv aamkpgsvvv dlaaerdgnc
      301 eltvadqkiv sdngvivigy tdfpsrmaaq astlyatnir hmlsdltpgk dgklvhnmed
      361 dvirgatvaf egqitypppp pkiaaiaaqr pkekvkeptp eekraaevaa fkaqtknqlt
      421 llaigtalll vvgafappaf mghfvvfvla cfvgfqviwn vshslhtplm avtnavsgiv
      481 ilgallqigs gnwlvvllaa lsvliatini vggflvtrrm lamfqks
//
LOCUS       WP_127647179             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127647179
VERSION     WP_127647179.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34706
     Region          2..302
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 miigagpagy taaiyaaran lkpllvtglq aggqltittd venypgfaap vqgpwlmeqm
       61 rqqaenvgte vvydiitsvd lsdrpfrleg dsgntyiada liiatgaqar wlglpsertf
      121 ngfgvsacat cdgffyrnke lvvvgggnta vqeahylsnl askvtvvhrr drfraepilq
      181 drllpkpnve viwnhvvdev igeqeprksv tgvrirdvnt gdvkeltthg lfvaighdpa
      241 talfrgqldm deagyikvgs wstkttvpgv laagdvidpv frqaisaagm gcmaaleaek
      301 flaehsphpv vrpivpreae miga
//
LOCUS       WP_127651018             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas koreensis].
ACCESSION   WP_127651018
VERSION     WP_127651018.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas koreensis
  ORGANISM  Pseudomonas koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudomonas koreensis"
                     /db_xref="taxon:198620"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33827
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mnaakhsrli ilgsgpagys aavyaaranl kpvvitglqa ggqltttvev dnwpgdvegl
       61 tgpvlmermq khaerfatei vydhihtakl qqrpfeligd sgtytcdali iatgasaqyl
      121 glpseeafag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlihrrdk
      181 lrsekilqdk lfekaangnv rlhwnqnlde vlgdasgvtg arlrdsrtge trdlalagvf
      241 iaighkpntd lfqgqlsmrd gylrvkggsd gdatsteipg vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddipvi
//
LOCUS       WP_127653849             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Alexandriicola marinus].
ACCESSION   WP_127653849
VERSION     WP_127653849.1
KEYWORDS    RefSeq.
SOURCE      Alexandriicola marinus
  ORGANISM  Alexandriicola marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Alexandriicola.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Alexandriicola marinus"
                     /db_xref="taxon:2081710"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55727
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeif egearvamtp asardiqklg hdclieagag eaagftdday reagvevvkt
       61 aaalwkeadi ivkvrppsdt eakrltkdkt lismfypaqn ealmelansk gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvyldfee qtqdgaatgg yaapsspefr
      241 ekqlekfrel apdvdivitt alipgrdapv lwtkdmveam kpgsvivdla aerggncelt
      301 eadkrivsdn gviivgytdf psrmaaqsst lystnirhml tdltpekdgv iehnmeddvi
      361 rgatathhge itfpppppkv kaiaaapkke apkeltpeek raqelaafka qtrqqvtlia
      421 igaalvlavg lvapasfmqh fivfvlsvfi gfqviwnvah slhtplmavt naissivilg
      481 aliqigsssi litllaavgi fmaavnifgg flvtrrmlam fqks
//
LOCUS       WP_127654927             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Alexandriicola marinus].
ACCESSION   WP_127654927
VERSION     WP_127654927.1
KEYWORDS    RefSeq.
SOURCE      Alexandriicola marinus
  ORGANISM  Alexandriicola marinus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Alexandriicola.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Alexandriicola marinus"
                     /db_xref="taxon:2081710"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34710
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maetrhtkll ivgsgpagyt agvyaaraml epvliqgiep ggqlttttev enwpgdtevq
       61 gpdlmvrmea haramgceii gdivteldls krpftaqtds gmvwtadavv latgarakwl
      121 gltseekfkg fgvsacatcd gffyrgqeiv vvgggntave ealfltnfas kvtlihrrne
      181 lraekilqer llnhpkiepm wfhtleevtg tdnplgvegv kvknvntgev teipakgvfi
      241 aighapasel vkdqlethmg gyvkvepgst rtsipgvfaa gdltdhiyrq avtsagmgcm
      301 aaldaekfla ehevpadahp tpsaae
//
LOCUS       WP_127661058             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium medicae].
ACCESSION   WP_127661058
VERSION     WP_127661058.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35349
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthharvli igagpagyta aiyaalanlk pllvtgrqag gqlttmayve nfpgfaepak
       61 gpllmeqmrq qaenvgtnlm ydivtsvdlw krpfrlqahs gdtyladali iatgaqprwl
      121 glpsekifag fgvsacatsd gffcrnkevv vvgggntave ealylsnlas kvtvvhrrnr
      181 fraepilqdr llarpnvdvi wnhvidevig kreprkwvtg vrildvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsvpgvlaag dvidpvfrra isaagmgsma
      301 aleaekflae pvetpaemre ieiigvyg
//
LOCUS       WP_127662998             337 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127662998
VERSION     WP_127662998.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..337
                     /gene="trxB"
     Protein         1..337
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=36382
     Region          8..310
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mnthhtrvli igagpagcta aiyaaranlk pllvtgrrag gqltttayve nfpgfaepvk
       61 gpllmeqmrr qaenvgtkvm ydiiafvdls mrpfrleghc gdtyladali vatgsearwh
      121 glpsektfkg fgvsanaifd gifyrnkevv vvgggdsavq aaldlsnlas kvtvvhrrdr
      181 fraeailkdr llskpnvdvi wnhvidevig ehepnkwvtg vrirdvktgd vrelpthglf
      241 vaighdpata lfrdqldmdr agyikvdpws tktsvpgvla agdvidpmfr qaisaaamgc
      301 iaalqaekfl iehppaptdp arsagpwwpv rplhggg
//
LOCUS       WP_127663039             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127663039
VERSION     WP_127663039.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34931
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthharvli igagpagyta aicaalanlk pllvtgrqag gqltittdve nypgfpkpvq
       61 gpwlmkqmrl qaenvgtsvv ydiitfvels trpfrlqths gdtyladali iatgaqprwl
      121 glpaektfag fgvsacatsd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 freesilqdl llskpnvdvi wnhvidevig efepskwvtg vrirdvnngd vrelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsvpgvlaag dvidpvfrra isaagmgsma
      301 aleaekflae paemreieii gvyg
//
LOCUS       WP_127663147             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127663147
VERSION     WP_127663147.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35685
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtrlqag gqltittdve nypgfaepvq
       61 gpwlmeqmrq qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vggggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg mrirevntdd vkeltthglf
      241 vaighdpata lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaeksl aehspdpavr pivphetemv ga
//
LOCUS       WP_127665275             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127665275
VERSION     WP_127665275.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35446
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntqharvli igagpagyta aiyaalanlt pllvtgrqag gqltittdve nypgfpkpvq
       61 gpwlmkqmrl qaenvgtkvm ydiitsvdlw krpfrlqahs gdtyladali iaagaqprwl
      121 glpsektfag fgvsacatsd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 freesilqdr llskpnvdvi wnhvidevig ereprkgvta vrirdvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsvpgvlaag dvidpvfrra itaaamgsma
      301 aleaekflae pvetpaemre iemigvyg
//
LOCUS       WP_127676001             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium medicae].
ACCESSION   WP_127676001
VERSION     WP_127676001.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium medicae (Ensifer medicae)
  ORGANISM  Sinorhizobium medicae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sinorhizobium medicae"
                     /db_xref="taxon:110321"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55159
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mnigipievs aterrvaltp dsalqlqklg ydclletgag aaagfsdaay haagvivves
       61 aaelyaqsdv vakvrppsea evtsmrsgqt lisffypaqn kelleaakak gvnvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qaadgaatgg yaapsspefr
      241 ekqlqkfrel apqidivitt alipgrdapk lwladmvamm kpgsvivdla aerggncdlt
      301 vadqrvvsdn gvivigytdf psrmatqast lystnirhmm adltpgkdgk lvhnmeddvi
      361 rgatvtfega itypppppki qaiaaqkpke kpkeptpeek raaetaafka qtksqglllv
      421 agtallllvg ayapasfmnh fvvfmlacfv gfqviwnvsh slhtplmavt navsgivvlg
      481 allqigssnw lvvvlaalsv liatvnivgg flvtrrmlam fqks
//
LOCUS       WP_127671250             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127671250
VERSION     WP_127671250.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35357
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthlarvli igagpagyta aicaalanlk pllvtgrqag gqlttmayve nfpgfaepvk
       61 gpllmeqmrq qaenvgtklm ydiitsvdlw krpfrlqahs gdtyladali iaagaqprwl
      121 glpsekifag fgvsacatsd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llarpnvdvi wnhvidevig ereprkgvta vrirdvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsvpgvfaag dvidpvfrra isaagmgsma
      301 areaekflae plvtptemrd ieiigvyg
//
LOCUS       WP_127677182             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127677182
VERSION     WP_127677182.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35746
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaepvq
       61 gpwlmeqmrq qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg irirevntdd vkeltthglf
      241 vaighdpeta lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaekfm aehspdpavr pivphetemv ga
//
LOCUS       WP_127677125             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127677125
VERSION     WP_127677125.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34715
     Region          30..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthhakvli igagpagsaa aiyaaraysk pllvtglqag gqltttayve nfpgfaepvk
       61 gpllmeqmrq qaenagtkvm ydiitfvdls mrpfrlqggs gdtytadali vatgsearwl
      121 glpsektfkg fgvsanaifd gvfyrnkevv vvgggdsavq aaldlsnlas kvtvvhrrdr
      181 fraesilkdr llskpnvkvi wnqaidevig ehepnkwvtg vrirdvktgd vrelpthglf
      241 vaighdpata lfrglldmdr agyikvgsws tktsvpgvla agdvidpvfr qaisaagmgs
      301 maaleaakfl aetvetreve iigvyg
//
LOCUS       WP_127678295             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium meliloti].
ACCESSION   WP_127678295
VERSION     WP_127678295.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39561
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfiake sdpnegrvag svesvkklks lgfdvvveag aglgsripdq eyekagarvg
       61 taadaktadv ilkvrrpsaq eisgyrsgav viaimdpygn eeaisamaga glttfamelm
      121 pritraqsmd vlssqanlag yqavidaaye ydralpmmmt aagtvpaaki fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavqdee fkaaetaggy akemsgeyqv
      241 kqaalvaehi akqdivitta lipgrpaprl vtremldsmk pgsvvvdlav erggniegae
      301 agkvtevggv rivghlnvag riaasaslly aknlvtflet mvsketkala lnmedelvka
      361 talthggavv hpafggamrg ek
//
LOCUS       WP_127681542             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nautilia sp. PV-1].
ACCESSION   WP_127681542
VERSION     WP_127681542.1
KEYWORDS    RefSeq.
SOURCE      Nautilia sp. PV-1
  ORGANISM  Nautilia sp. PV-1
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Nautiliales; Nautiliaceae; Nautilia.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Nautilia sp. PV-1"
                     /db_xref="taxon:2579250"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33453
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydviiigag pgglsaglya grmgldtlii ekltpggqit qsseienypg vcevksglel
       61 mqcwpeqtkr fgakiiseev vsisryeiqd dkygfiiktp kneyrslavi latgatpkra
      121 gfkgeeeyig kgvsycavcd gyfyknmdva vvgggdsale ealylsniak kvylihrrde
      181 fraapatvek vknkenieil ynttveevkg vpflntavin tdgeikelkv dgifvfvgmn
      241 vnsalvkdlc elneynevkv dlnmkttleg lyaigdvren svkqvvasag dgavaalnvv
      301 kyakslkd
//
LOCUS       WP_127683217             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Inhella
            crocodyli].
ACCESSION   WP_127683217
VERSION     WP_127683217.1
KEYWORDS    RefSeq.
SOURCE      Inhella crocodyli
  ORGANISM  Inhella crocodyli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Inhella.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Inhella crocodyli"
                     /db_xref="taxon:2499851"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38427
     Region          1..371
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mligvpresa agetrvavtp etakkfkaag htvrvergag laaactdaay eaagaeltda
       61 agalgaelvl kvqrpsaael aqmkpgsvlv gmlnpfdaeg lqamaqaglt afaleaaprt
      121 traqsldvls sqaniagyka vllaahhypk lfpmlmtaag tikaarvvvl gvgvaglqai
      181 atakrlgavi easdvrpsvk eqveslgakf idvpyetaee keaaegvggy arpmppswla
      241 rqaaevakrv aqadivista lipgrpaptl vseemvksmk agsvivdiaa grgpggvggn
      301 cpltvanqtv qvhgvtivge tnlpatvpad ssalyarnvl dflklivdkd aklslptddd
      361 ivtaclmaqg gevkrk
//
LOCUS       WP_127667243             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127667243
VERSION     WP_127667243.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35335
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthharvli igagpagyta aicaalanlk pllvtgrqag gqlttmayve nfpgfaepvk
       61 gpllteqmrq qaenvgtklm ydiitsvdlw krpfrlqahs gdtyladali iatgakprwl
      121 glpsekifag fgvsacatsd gffyrnkevv vvgggniave ealylsnlas kvtvvhrrnr
      181 fraepilqdr llarpnvhvi wnhvidevig kreprkwvtg vrildvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsvpgvlaag dvidpvfrra isaagmgsma
      301 aleaekflaa plvtpaemre ieiigvyg
//
LOCUS       WP_127680557             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Inhella crocodyli].
ACCESSION   WP_127680557
VERSION     WP_127680557.1
KEYWORDS    RefSeq.
SOURCE      Inhella crocodyli
  ORGANISM  Inhella crocodyli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Inhella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Inhella crocodyli"
                     /db_xref="taxon:2499851"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33609
     Region          2..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msqhhrliil gsgpagytaa iyaaranlnp vlitgmaqgg qlmtttevdn wpadvmgvqg
       61 pelmqrfqeh aerfktqivf dhinavdlgq rpfkltgdsg qyscdaliia tgasakylgl
      121 pseeafsgrg vsacatcdgf fyrdrdvcvv gggntaveea lylsniaskv hlihrrdkfk
      181 aepilvdkmm ekvaagkivl qtfhtldevl gdasgvtgvr ikhtqsgatt dialhgcfia
      241 ighspntaif qgqldmkdgy lrtrsgldgf atmtnvpgvf aagdvqdhvy rqaitsagtg
      301 cmaaldaqrf leqqa
//
LOCUS       WP_127690714             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingobium algorifonticola].
ACCESSION   WP_127690714
VERSION     WP_127690714.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium algorifonticola
  ORGANISM  Sphingobium algorifonticola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sphingobium algorifonticola"
                     /db_xref="taxon:2008318"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33832
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtathstrml ilgsgpagls aaiygaragl apivvqgmqp ggqltittdv enypgfrdvv
       61 qgpwlmeemq aqaehvgaqm mydqivsvdl tqrpfrligd ggtiysgdtl victgaqakw
      121 lgvegeahlg gkgvsacatc dgffyrgkkv vvigggntav eealyltnhs hdvtlihrrd
      181 slraekilqd rlfahprihv lwnkavarfv gggspeglvg vdlidtvtge ashmptdgaf
      241 vaighqpata lfegllpmde gyllvekgts rtniagvfaa gdvtdkvyrq avtaagmgcm
      301 aaldaekfla eadfeamava ae
//
LOCUS       WP_127691866             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sphingobium algorifonticola].
ACCESSION   WP_127691866
VERSION     WP_127691866.1
KEYWORDS    RefSeq.
SOURCE      Sphingobium algorifonticola
  ORGANISM  Sphingobium algorifonticola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingobiaceae; Sphingobium.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Sphingobium algorifonticola"
                     /db_xref="taxon:2008318"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54910
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapreva qgearvaltp dsalqlqklg hecvvesgag kaagfdddsy raadvrvvat
       61 aselwaaadv ivkvrppead eaaqlttgkt lisffypgqr seelaaisat ganvlamdmv
      121 prisraqkmd alssmaniag yravieagan fgrfftgqvt aagkvpparv lvigagvagl
      181 aaigaatslg aitlafdvrp evaeqiesmg aqfvyldfse eqqdgaatgg yaapsspefr
      241 eaqlkkfrel apsvdivist alipgrdapv lwtqdmveam rpgsvivdla aerggncelt
      301 vadqkivspn gvtiigytdf psrmaaqsss lyasnirhml fdltpgkdgv ivhnmeddvi
      361 rgatiafega vsfpppppki kaiaaqkpkp kaeeltpdqk rakdvtafka qtrsqvttli
      421 vaailliavg avapasfmgh ftvfvlacfv gfqviwnvsh slhtplmavt naisgivvvg
      481 amlqvgssst ivmvlatisi liasinivgg flvtrrmlam fqrs
//
LOCUS       WP_127693086             318 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Neptunomonas].
ACCESSION   WP_127693086
VERSION     WP_127693086.1
KEYWORDS    RefSeq.
SOURCE      Neptunomonas
  ORGANISM  Neptunomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Oceanospirillaceae.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Neptunomonas"
                     /db_xref="taxon:75687"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33814
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdiqhhkli ilgsgpagyt aavyaaranl kpvvitgmqa ggqlttttdv dnwpgdvdgv
       61 qgpelmqrmq ahaerfdtev ifdhindvsv aerpfvlkgd mgtyscdali ictgasaqyl
      121 glpseeafqg kgvsacatcd gffyrgqkva vvgggntave ealylsniae evtlihrrds
      181 lraekilqdk lldraengni nilwnhqlqe vlgddsgvtg lqlesttdgs tqqldvagvf
      241 iaighkpntd ifagkldmkd gyltiqsgle gnatqtsvpg ifaagdvcdh iyrqaitsag
      301 fgcmaaldae rylddlak
//
LOCUS       WP_127696736             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bacillus halotolerans].
ACCESSION   WP_127696736
VERSION     WP_127696736.1
KEYWORDS    RefSeq.
SOURCE      Bacillus halotolerans
  ORGANISM  Bacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Bacillus halotolerans"
                     /db_xref="taxon:260554"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33582
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meemeiydvi ivgagpagmt aavytsranl ntlliergip ggqmantqdv enypgfdhil
       61 gpdlsnkmfe hakkfgalye ygdikeiide grlkkvvttk kefyaksvii atgadhkklg
      121 vpgenelggl gvsycavcdg affkgrelvv vgggdsavee avyltrfask vtiihrrdql
      181 raqkilqera ysnekiefiw nkevtsinag ngtvntvtlk dtktgeqsqf pangvfiyvg
      241 tlplngafkn lditneegyv vtdeamatki pgiyaagdir dktlrqivta tgdgsiaaqs
      301 aqhyienlgn s
//
LOCUS       WP_127703157             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mucilaginibacter limnophilus].
ACCESSION   WP_127703157
VERSION     WP_127703157.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter limnophilus
  ORGANISM  Mucilaginibacter limnophilus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Mucilaginibacter limnophilus"
                     /db_xref="taxon:1932778"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34228
     Region          9..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msgelehvkc liigsgpagy taaiyasrad lkpvlytgml sggqltqtte venypgypdg
       61 ilgpemmqnf ekqasrlgtd irfgyvssvd fsslphkvvv desktiladt viistgasak
      121 wlgleseqky ngfgvsacav cdgfffrgqd vaivgagdta aeeatylakl crkvymlvrr
      181 defraskamv hrvlntpnie viyntetkei vgdgqvvtgv kvinnqtned ktldvtgffv
      241 aighhpntei frgwihmdet gyiitkpgss etniegvfac gdaqdhiyrq avtaagsgcm
      301 aaidaeryla akehvvta
//
LOCUS       WP_127709120             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Sinorhizobium meliloti].
ACCESSION   WP_127709120
VERSION     WP_127709120.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39662
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfiake sdpnegrvag svesvkklka lgfdvvveag aglssripdq eyekagarig
       61 taadaktadv vlkvrrptaq eisgyrsgav viaimdpygn eeaisamaga glttfamelm
      121 pritraqsmd vlssqanlag yqavidaaye ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedee fkaaetaggy akemseeyra
      241 kqaalvaehi akqdivitta lipgrpaprl lsremldsmk pgsivvdlav erggnvegae
      301 agkvtevggi rivghlnvag riaasaslly aknlvtflet mvsketkala lnmedelvka
      361 talthggavv hpafggamrg ek
//
LOCUS       WP_127710995             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Novosphingobium umbonatum].
ACCESSION   WP_127710995
VERSION     WP_127710995.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium umbonatum
  ORGANISM  Novosphingobium umbonatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Novosphingobium umbonatum"
                     /db_xref="taxon:1908524"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33633
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mathstrmli igsgpaglta aiygaraglq pivvqglqpg gqltittdve nypgfreaiq
       61 gpwlvqemqa qaehvgtrmm wdtivdidls gppfraigds gdvyegdtlv ictgaqakwl
      121 gakgeqelsg kgvsacatcd gffyrgkkvv vigggntave ealyltnhsd dvtlihrrds
      181 lrsekilqer lfahpnikvl wnkaveefvg dtaiggaglt gvalvdtvtg eksiepaqga
      241 fvaighapat elfkgkleld esgyivvqpg tpktaipgvf aagdvmdhty rqavtaagtg
      301 cmaaldaerf vaawdhakrg
//
LOCUS       WP_127711715             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Novosphingobium umbonatum].
ACCESSION   WP_127711715
VERSION     WP_127711715.1
KEYWORDS    RefSeq.
SOURCE      Novosphingobium umbonatum
  ORGANISM  Novosphingobium umbonatum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Novosphingobium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Novosphingobium umbonatum"
                     /db_xref="taxon:1908524"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33321
     Region          5..309
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mthskliilg sgpagytaav yaaranlapv litgevqggq lttttevdnw padaqgvqgp
       61 dlmarffdha drfgtqfefd qihtadlssr pfrlegdsgs ytcdaliist gasaqylglp
      121 seeaffgrgv sacatcdgyy fkgkpvavig ggntaveeal fltniashvt ivhrrdkfra
      181 ekilqdklfe keregkvtii wnhtldevlg edtvsamrlv stqtgqsree pvegifiaig
      241 hkpntdlfvg qlemdngyiv trggragqvt atsvagvfaa gdvqdqiyrq actsaasgcq
      301 aaldaekfle gla
//
LOCUS       WP_127711769             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127711769
VERSION     WP_127711769.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35652
     Region          8..310
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mnthrarvli igagpagyta aiyaaranlk pllvtglqag gqltittdve nypgfaepvl
       61 gpwlmeqmrq qaenvgtevv ydiitsvdls krpfhlkgds gdtyiadaii iatgaqarwl
      121 glpsektfsg fgvsacatcd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraesilqdr llskpnvdvi wnhvidevig ereprksvtg vrirnvktge vkelsthglf
      241 vaighdpata lfrgqldmda dgylkvgsws tkttvpgvqa agdvidpvfr qaisaagmgc
      301 maaleaekfl tehspdsvaw pivareaema ev
//
LOCUS       WP_127715969             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Halobacteriovorax sp. HLS].
ACCESSION   WP_127715969
VERSION     WP_127715969.1
KEYWORDS    RefSeq.
SOURCE      Halobacteriovorax sp. HLS
  ORGANISM  Halobacteriovorax sp. HLS
            Bacteria; Pseudomonadati; Bdellovibrionota; Bacteriovoracia;
            Bacteriovoracales; Halobacteriovoraceae; Halobacteriovorax.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Halobacteriovorax sp. HLS"
                     /db_xref="taxon:2234000"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33296
     Region          5..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqrklviig sgpagytaal yasranlnpl vieghepggq lttttdvdnf pgfpegimgp
       61 elmanmkkqt lrfgteylqt hvtavdlskr pfkvtcengt elhaetliis tgasakylgi
      121 pnekeligkg vsacatcdgf fyrdkivhvv gggdtameea tfltkfaskv yivhrrdtlr
      181 askpmqeraf anekiemvwd savteiihdq tgvtgikven lktgetterk tdglfmgigh
      241 tpntgflngq ikvddhgfii tgehpdtnva gvfacgdvqd syyrqaisaa gsgcqaaira
      301 erfledqe
//
LOCUS       WP_127718856             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127718856
VERSION     WP_127718856.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35254
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthharvli igagpagyta aicaalanlk pllvtgrqag gqlttmayve nfpgfaepvk
       61 gpllmeqmrq qaknvgtklm ydiitsvdlw krpfrlqahs gdtyladali iatgaqprwl
      121 glpsekifag fgvsacatsd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 freesilldr llarpnvdvi wnhvidevig kreprksvtg vrildvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsvpgvlaag dvidpvfhra isaagmgsma
      301 aleaekflae plvtpavmhe ieiigvyg
//
LOCUS       WP_127724634             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Anaerosphaera multitolerans].
ACCESSION   WP_127724634
VERSION     WP_127724634.1
KEYWORDS    RefSeq.
SOURCE      Anaerosphaera multitolerans
  ORGANISM  Anaerosphaera multitolerans
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Peptoniphilaceae; Anaerosphaera.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Anaerosphaera multitolerans"
                     /db_xref="taxon:2487351"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34913
     Region          3..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mlydlivlga gpagltagly garaklktlv iekgieggqi snttdvenyp gtpnisgfel
       61 shtvrkqaes fgaefvsdev ieadlkdkik kiktkekeye aktviiatga tprklgfpge
      121 difegrgisy catcdaafyq dfdvyviggg dsavdealfi skfakkvyiv hrrdelraak
      181 slqdrafsne kidfiwdsvv eeikgdkiae elvlrnlktg eltsikqadg pfgififvgf
      241 ipetqifegq iemekgyikt dedmntnieg vfaagdlrvk nlrqvvtata dgaiaavnae
      301 kyiaeqegtv ykafeekqi
//
LOCUS       WP_127729342             330 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Methylobacterium oryzihabitans].
ACCESSION   WP_127729342
VERSION     WP_127729342.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium oryzihabitans
  ORGANISM  Methylobacterium oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Methylobacterium oryzihabitans"
                     /db_xref="taxon:2499852"
     gene            1..330
                     /gene="trxB"
     Protein         1..330
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35150
     Region          13..315
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mpttsqapvh erliivgsgp agytaaiyaa ramvepllis gfqpggqlmi ttdvenypgf
       61 aeaiqgpwlm eqmrlqaehv gtrivseyia kvdlkqrpfr leadsgavwt cdaliiatga
      121 qakwlglpse aafqgfgvsa catcdgfffr gkevvvvggg ntaveealyl anlaskvtvv
      181 hrrdgfraer ilqerlfrhp nvevvwnhav eeicgtktpa psvthlrlrd vrtgaiterr
      241 tdgvfiaigh qpatgvfegq lplrsggyls vapgtaqtei pgvfaagdvt ddvyrqaita
      301 agmgcmaale aekylanlai gesprqaaae
//
LOCUS       WP_127734039             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium oryzihabitans].
ACCESSION   WP_127734039
VERSION     WP_127734039.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium oryzihabitans
  ORGANISM  Methylobacterium oryzihabitans
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Methylobacterium oryzihabitans"
                     /db_xref="taxon:2499852"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39125
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlsetd paeprvaavp etvkkykalg aevvvqagag lsagvpdgef eaagatvapd
       61 aaaaagnadi vlrvrrpgad elpalkrgai vvaimdpygh eaevkamaea gvsaiamelm
      121 pritraqvmd vlssqanlag yravidgaae ygralpmmmt aagtvsaari fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedde fkqaetaggy akemsaeykk
      241 kqaelvashi akqdivitta lipgrpapkl vsaamvaamr pgsvlvdlav erggnvegak
      301 pdevvktdng vkivgyanvp grlaatsssl yarnlyafve tlvdkaaktl avkwddelvk
      361 atcltrdgav vhpnfqpkaa
//
LOCUS       WP_127734706             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127734706
VERSION     WP_127734706.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35659
     Region          6..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthrtrvli igagpagyta aiyaaranlk pllvtglqag sqltittdve nypgfaepvq
       61 gpwlmeqmre qaenvgtevv ydiitsvdls drpfrlegds gdayiadali iatgaqarwl
      121 glpsertfng fgvsacatcd gffyrnkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvevi wnhvidevig eqeprksvtg mrirevntdd vkeltthglf
      241 vaighdpata lfrgqldmdd agyikvgsws tkttvpgvla agdvidsvfr qaitaagmgs
      301 maaleaeksl aehspdpavr pivphetemv ga
//
LOCUS       WP_127743284             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingomonas crocodyli].
ACCESSION   WP_127743284
VERSION     WP_127743284.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas crocodyli
  ORGANISM  Sphingomonas crocodyli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Sphingomonas crocodyli"
                     /db_xref="taxon:1979270"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33938
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maathstrml vlgsgpagls aaiygaragl apivvqgiqp ggqltittdv enypgfrdvi
       61 qgpwlmqemq aqaehvgatm vwdtivdvdl serpfrlkgd ggalyvcdtl viatgaqakw
      121 lgipgeqelg gkgvsacatc dgffyrgkkv avigggntav eealyltnhs qdvtlihrrd
      181 slraekilqd rlfkhpnvnv lwnketvrfi ggddpsqglv gielrdtqtg elsvlatdgg
      241 fvaighhpst elfrghlald sdgylivekg gtktnvpgvf gcgdvadkiy rqavtaagtg
      301 cmaaldaerf laetdfevep a
//
LOCUS       WP_127747491             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sinorhizobium meliloti].
ACCESSION   WP_127747491
VERSION     WP_127747491.1
KEYWORDS    RefSeq.
SOURCE      Sinorhizobium meliloti (Rhizobium meliloti)
  ORGANISM  Sinorhizobium meliloti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Sinorhizobium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Sinorhizobium meliloti"
                     /db_xref="taxon:382"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35325
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnthharvli igagpagyta aicaalanlk pllvtgrqag gqltittdve nypgfpkpvq
       61 gpwlmkqmrl qaenvgtkvm ydiitsvdlw krpfrlqahs gdtyladali iaagaqprwl
      121 glpsektfag fgvsacatsd gflyrdkevv vvgggntavq ealylsnlas kvtvvhrrdr
      181 fraepilqdr llakpnvdvi wnhvidevig ereprkgvta vrirdvntgd akelpthglf
      241 ighdpatalf rgqldmdrag yikvgswstk tsvpgvlaag dvidpvfrra itaaamgsma
      301 aleaekflae pvetpaemre iemigvyg
//
LOCUS       WP_127738148             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Niallia taxi].
ACCESSION   WP_127738148
VERSION     WP_127738148.1
KEYWORDS    RefSeq.
SOURCE      Niallia taxi
  ORGANISM  Niallia taxi
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Niallia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Niallia taxi"
                     /db_xref="taxon:2499688"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34285
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 maeekiydvi iigagpagmt aavytsranl stlmiergip ggqmanteev enfpgfesil
       61 gpdlsnkmfn hakkfgaeya ygdikeivdg nefktvkags keyktrsiii stgaeykkvg
      121 vpgekelggr gvsycavcdg affkekrlfv igggdsavee gvyltrfasq vtivhrrdel
      181 raqkilqdra fandkvdfiw nhtikainek dgkvgsvtlv stvddteqvl dadgvfiyig
      241 mlplskpfes lgitnengyi etndqmetkv pgifaagdir ektlrqivta tgdgsiaaqs
      301 aqhyveelve slkqka
//
LOCUS       WP_127748124             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Parasedimentitalea marina].
ACCESSION   WP_127748124
VERSION     WP_127748124.1
KEYWORDS    RefSeq.
SOURCE      Parasedimentitalea marina
  ORGANISM  Parasedimentitalea marina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Parasedimentitalea.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Parasedimentitalea marina"
                     /db_xref="taxon:2483033"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55216
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeif ngearvamtp esarhlqklg ydcaietgag aaagfsdaty veagveiikt
       61 paalwksvdi vakvrqpsev elkrmtsgkt lisffnpagn eagmelaksk ganviamemv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqit aagkvppakv lvvgagvagl
      181 aavgtstslg aitlafdvrp evaeqvesmg aefvyldfee dqadgaatgg yaavsspefr
      241 aaqlakflel apevdivitt alipnreape lwteemvaam kpgsvivdla aekggncklt
      301 vmdekivten gvtiigytdf psrmaaqast lyatnirhmv tdltpekdgq inhnmeddvi
      361 rgatvtfeke itfpppppkv qaiaakpkev vpeltaeekr aaeaaafkaa tkqqvtllgv
      421 gavlmllvgl vapasfmqhf ivfvlacfvg fqviwgvahs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaslsif maginifggf lvtrrmlamf qks
//
LOCUS       WP_127749798             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Parasedimentitalea marina].
ACCESSION   WP_127749798
VERSION     WP_127749798.1
KEYWORDS    RefSeq.
SOURCE      Parasedimentitalea marina
  ORGANISM  Parasedimentitalea marina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Parasedimentitalea.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Parasedimentitalea marina"
                     /db_xref="taxon:2483033"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33324
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtdtrhtkvl iigsgpagyt agvyasraml epilvqgiep ggqlttttdv enypgftevq
       61 gpdlmvkmqd haqamgceii gdiiteldts krpftakgds gtvysadavi latgarakwl
      121 gldseekfkg fgvsacatcd gffyrgqeiv vigggntave ealfltkfas kvtlihrrde
      181 lraekilidr lmkndkivpl wfntlkevvg tesplgvegv itenvqtgel teipckgvfv
      241 aighapasel vkdsldthag gyvvtkpgtt etsvpgvfaa gdltdhvyrq avtsagmgcm
      301 aaldaerfls eqdd
//
LOCUS       WP_127753684             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Devosia sp. 1566].
ACCESSION   WP_127753684
VERSION     WP_127753684.1
KEYWORDS    RefSeq.
SOURCE      Devosia sp. 1566
  ORGANISM  Devosia sp. 1566
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Devosiaceae; Devosia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Devosia sp. 1566"
                     /db_xref="taxon:2499144"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33999
     Region          4..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhakviiigs gpagytaaiy aaramlepvm iqgiqpggql tittdvenyp gfadviqgpw
       61 lmdqmrsqae hvgtrivndv itsvdfdrrp fvlhsdsgtt ytadsiiict gaqakwlglp
      121 seqkfqgfgv sacatcdgff yrnkevvvvg ggntaveeal fltnfaskvi lvhrrsefra
      181 erilqdrlfk npkievrwnt eidevhgsam ppsvnavtlr dlktgrtysq pidgvfvaig
      241 hspatsifag kldmkpggyl qvqpgttqtn ipgvfaagdv tddvyrqait aagmgcmaal
      301 daerflaehe laeaae
//
LOCUS       WP_127757678             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium/Agrobacterium group].
ACCESSION   WP_127757678
VERSION     WP_127757678.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium/Agrobacterium group
  ORGANISM  Rhizobium/Agrobacterium group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rhizobium/Agrobacterium group"
                     /db_xref="taxon:227290"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55754
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigtpkely egearvgmtp dsaqalqklg ydciletgag kaagfsdday raagvtivds
       61 adalyagsdi iakvrppets eidrlssdkt lisffypaqn kdlleqakek ganviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvyldfad qqqdgaatgg yaapsspefr
      241 ekqlekfrel apqidivitt alipgrdapk lwladmvamm kpgsviidla aerggncdlt
      301 vpdsrvvsdn gvivigytdf psrmatqast lystnirhmm tdltpakdgk pvhnmeddvi
      361 rgatvtyqge itypppppki qaiaaqkpke rakeltpeek hakehadfka qtksqvglla
      421 igtailllvg afapasfmsh fivfvlacfv gfqviwnvsh slhtplmavt naisgiviig
      481 allqigsgnw lvvilaslsv liatinivgg flvtrrmlam fqks
//
LOCUS       WP_127762038             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Peribacillus asahii].
ACCESSION   WP_127762038
VERSION     WP_127762038.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus asahii
  ORGANISM  Peribacillus asahii
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Peribacillus asahii"
                     /db_xref="taxon:228899"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34351
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mteekiydvv iigagpagmt aavytsranl stlmlergmp ggqmanteev enypgfetil
       61 gpelstkmfe hakkfgaeya ygdvkeiidg eeyktiiags keykarsiii ssgaeykkig
      121 vpgekelggr gvsycavcdg affkgkelfv igggdsavee gvyltrfask vtivhrrdel
      181 raqkilqdra fanekvdfiw nttlkqinek dgkvgsvtlv stvdgteteh padgvfvyig
      241 mlpltkpfen lgitnetgyi etnermetkv agifaagdvr ektlrqivta tgdgsiaaqs
      301 vqhyveelke klqika
//
LOCUS       WP_127763284             462 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hwanghaeella grinnelliae].
ACCESSION   WP_127763284
VERSION     WP_127763284.1
KEYWORDS    RefSeq.
SOURCE      Hwanghaeella grinnelliae
  ORGANISM  Hwanghaeella grinnelliae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Hwanghaeella.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Hwanghaeella grinnelliae"
                     /db_xref="taxon:2500179"
     Protein         1..462
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48144
     Region          1..372
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,99,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,132..133,142..143,146..147,150..151,153..154,
                     156..161,163,165..167,170,193..194,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(127..128,132,135,138,179..182,202..204,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(129..130,132,142,185..186,193,209..210,212..215)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(162..166,169,172,195,197)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavlkerr sgerrvaasp etvkkftdlg ctvtvekgag dgaalsdavf eeagakiaat
       61 peatvkdadv vlkvqrpmta adgedevalf skgqillcqm nalidgalvr acadggvqaf
      121 amelvpritr aqsmdilssq aniagykavl dgieqygrav pmmstaagrv tpanvfvmgv
      181 gvaglqaiat akrlgavvya tdvrpdtkeq veslggkfva vendeflqaq tsggyakems
      241 ddykrqqael vaktlpkidi vvttalipgr papvlvtedh vksmkpgsvi vdlaaeaggn
      301 cpltelgkvv vkhgvtlvgh gnwpsrvpet tsllfaknll nfltplidke tgklainyed
      361 diikgslvtr dgkiveerak anaeksggda pakttakkaa kksaakkssa kkssgkkssa
      421 kksaakkada tkqaaptdtp dgddpkpdat stetptdsge ek
//
LOCUS       WP_127763945             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hwanghaeella grinnelliae].
ACCESSION   WP_127763945
VERSION     WP_127763945.1
KEYWORDS    RefSeq.
SOURCE      Hwanghaeella grinnelliae
  ORGANISM  Hwanghaeella grinnelliae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Aestuariispiraceae; Hwanghaeella.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Hwanghaeella grinnelliae"
                     /db_xref="taxon:2500179"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34163
     Region          6..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maerhcktli igsgpagyta avyaaranle pvviaglqpg gqltittdve nypgfadpiq
       61 gpwlmeemrk qaenvgteii ydivtdvdfs atplravtdg gsvytadavi ittgaqarwl
      121 gldseqkfqg ygvsacatcd gfffrgkevi vvgggntave ealylinhas kvtlvhrrda
      181 lrsekilqdr lmenekievv wnaaideivg ddeplgvtgv klrdtqtgei terqvhgvfv
      241 aighdpatkv fkgkvemdge gyiltktgtt htnvpgvfaa gdvvdkhyrq avtaagmgcm
      301 aaldaekylg elsvtqraae
//
LOCUS       WP_127776293             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Peribacillus frigoritolerans].
ACCESSION   WP_127776293
VERSION     WP_127776293.1
KEYWORDS    RefSeq.
SOURCE      Peribacillus frigoritolerans
  ORGANISM  Peribacillus frigoritolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Peribacillus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Peribacillus frigoritolerans"
                     /db_xref="taxon:450367"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33429
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknqetydvi ivgagpagmt aavytsranl ntlliergip ggqmantqdv enypgfdhil
       61 gpdlsnkmfe hakkfgavye ygdikeivde grlkkvvttn kefyaksvii asgadhkklg
      121 vpgenelggl gvsycavcdg affkgrelvv lgggdsavee avyltrvask vtiihrrdql
      181 raqkilqera fsnekiefiw nkevtsineg ngkvnsvtlk dtktgeqsqf padgvfiyvg
      241 tlplngafkn lditneagyv vtdeamatki pgifaagdir dktlrqivta tgdgsiaaqs
      301 vqhyienles
//
LOCUS       WP_127789351             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodovarius crocodyli].
ACCESSION   WP_127789351
VERSION     WP_127789351.1
KEYWORDS    RefSeq.
SOURCE      Rhodovarius crocodyli
  ORGANISM  Rhodovarius crocodyli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Rhodovarius.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhodovarius crocodyli"
                     /db_xref="taxon:1979269"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39122
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,100,297,324,326)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,287..288,331..332,336,
                     339..340)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,237,248,
                     265..267,274,276)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrlavlkerr agetrvaatp etakklaalg csvaieagag aaagypdqly adagaeiapd
       61 aeaalfgagi vlkvraplgt gegeidelsl ihrgalligt leaianpera raiasvgvda
      121 csmellprtt raqsmdvlss qanlagyrav vegaaafdra fpmlmtaagt ipaanafimg
      181 agvaglqaia tarrlgarvs atdvrpaake eikslgasyv gyedeesraa qtsggyakam
      241 speflakqae vvaahiakqd ivvctalvqg rrapilvtea mvasmkpgsi ivdiasdagg
      301 ncaltrpgev tvtangvtil ghtnwpgria naasalyarn lltflttfwd keaqapklpe
      361 dddlvrgvti trngavvhpg la
//
LOCUS       WP_127794988             541 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Agromyces
            sp. LHK192].
ACCESSION   WP_127794988
VERSION     WP_127794988.1
KEYWORDS    RefSeq.
SOURCE      Agromyces sp. LHK192
  ORGANISM  Agromyces sp. LHK192
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Agromyces.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Agromyces sp. LHK192"
                     /db_xref="taxon:2498704"
     Protein         1..541
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54352
     Region          3..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msrigivteq apetrvaatp atvkqltalg yevvveagag aasafldday aasgavigta
       61 adalgadivl kvnaptdaev agmalgttfi gllapafkpe llqalaeqgv talamdavpr
      121 israqsmdvl ssmaniagyr avveaahefg rfftgqvtaa gkvppakvlv agagvaglaa
      181 igaasslgai vratdprpev adqvksigge ylkveveveq stdgyakats eaydrraaei
      241 yseqaadvdi ivttalipgr aapklitaad vasmksgsvi vdmaagqggn vegsvageri
      301 vtpngvtilg ytdlasrlpt qasqlygtni vnllklltpa kdgrleldfd dvvqravtvt
      361 rggdvtwppp pvqvsaapaa saapapaaaa pepkkpmsav kktalvavgi aalfavnaia
      421 paplpqhftv lvlavvvgfy vigkvahalh tplmsvtnai sgiiivgamv qitsdvlvvq
      481 ilaavavlla sinifggfav trrmlamfqa ghaqagnpqp aaaagagasd aasttaaraq
      541 r
//
LOCUS       WP_127789232             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhodovarius crocodyli].
ACCESSION   WP_127789232
VERSION     WP_127789232.1
KEYWORDS    RefSeq.
SOURCE      Rhodovarius crocodyli
  ORGANISM  Rhodovarius crocodyli
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Roseomonadaceae; Rhodovarius.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Rhodovarius crocodyli"
                     /db_xref="taxon:1979269"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34006
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstthhtpll vigagpagyt aaiyaaragl kpmlvaglqp ggqltittdv enypgfaeav
       61 qgpwlmeqmr aqaehmgtvm hydiitkvdf sqrpfrcesd sgdlfvaeti viatgaqarw
      121 lgipgeqqls gfgvsacatc dgfffrgrkv avvgggntat eealylanla ehvtlihrrd
      181 slrsekilqq rllalpnvsv kwntevaeal ptdaarpalr alklrdtvng tfselsvdgl
      241 fvaighdpat avfkgqiamd segyivteag strtsvpgvf aagdvqdkiy rqavtaagtg
      301 cmaaldaerf laaahsgerq aa
//
LOCUS       WP_127795027             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Agromyces sp. LHK192].
ACCESSION   WP_127795027
VERSION     WP_127795027.1
KEYWORDS    RefSeq.
SOURCE      Agromyces sp. LHK192
  ORGANISM  Agromyces sp. LHK192
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Agromyces.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Agromyces sp. LHK192"
                     /db_xref="taxon:2498704"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35227
     Region          3..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrdiiiigsg pagftaaiya araelqplli assveiggel mnttevenfp gfpegimgpd
       61 lmtqmqqqae rfgtevvydd vveleldgpv krvklgnggv eeaktviyat gsayrklglp
      121 eeehlsghgl swcatcdgff frqktiavvg ggdsameeat fltrfadkvy vihrreelka
      181 skimqqrafd nekiefvwna eiaeilgetq vsgvtlrdtv tgdlrpleld glfvaigndp
      241 rthlvhgkle ltgegtvwvd grssrtslpg vfaagdvidp hyrqavtaag sgtvaaldae
      301 hylaaladts spaeaeaeae averlasvn
//
LOCUS       WP_127802511             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sandaracinomonas limnophila].
ACCESSION   WP_127802511
VERSION     WP_127802511.1
KEYWORDS    RefSeq.
SOURCE      Sandaracinomonas limnophila
  ORGANISM  Sandaracinomonas limnophila
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Sandaracinomonas.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Sandaracinomonas limnophila"
                     /db_xref="taxon:1862386"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33283
     Region          6..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maekikclii gsgpagftaa iyasraglep ilyqgaqpgg qlttttevdn fpgyphgvdg
       61 ptmmvdlenq akrfgtdvrt gmatkvdfts spkkvwides yeieadavii atgasakwlg
      121 legektfngl gvsacavcdg ffyrnqtvav vgagdtaaee asylanlcek vhlivrrdem
      181 raslimqerv knnpkieihw nteteeilgd asgvtgirik nnksgetsel altgffvaig
      241 hqpntaifrg qlemdaqeyl itekgssktn vegvfacgdv qdtiyrqait aagsgcmaal
      301 daerwlaatg lh
//
LOCUS       WP_127805306             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hydrogenophaga sp. NH-16].
ACCESSION   WP_127805306
VERSION     WP_127805306.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga sp. NH-16
  ORGANISM  Hydrogenophaga sp. NH-16
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hydrogenophaga.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Hydrogenophaga sp. NH-16"
                     /db_xref="taxon:2184519"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33481
     Region          4..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkhtkvlilg sgpagytaav yaaranlspv litgiaqggq lmtttevdnw padvhgvqgp
       61 dlmqrfleha erfkteivfd hinavdlskr pfvltgdssq yscdtliiat gasarylglp
      121 seetfmgkgv sacatcdgff yrdqevavvg ggntaveeal ylsniaskvt lvhrrdsfra
      181 eaimidklmd kvkegkielk lhsvldevlg dasgvtgvrl knvqdgtted vtvkgcfiai
      241 ghspntgifk dqlamkdgyl itqsgnngma tmtsvpgvfa agdvqdhvyr qaitsagtgc
      301 maaldaqrfl eqnpa
//
LOCUS       WP_127806762             540 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hydrogenophaga sp. NH-16].
ACCESSION   WP_127806762
VERSION     WP_127806762.1
KEYWORDS    RefSeq.
SOURCE      Hydrogenophaga sp. NH-16
  ORGANISM  Hydrogenophaga sp. NH-16
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Comamonadaceae; Hydrogenophaga.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Hydrogenophaga sp. NH-16"
                     /db_xref="taxon:2184519"
     Protein         1..540
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55846
     Region          16..540
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mtsgaptdta aatpqrigip reifpgekrv atvpdvvtkl aklgfgvvve tgageladls
       61 deayreagas iagstaelwn tadivfkvrp ptadevalmh agqtligfvw paqnpdlmqq
      121 laakkvtvla idclprtlsr aqkmdaltsm agvsgyravv eaanafgrff ngqitaagkv
      181 ppakvfiaga gvaglaaiga aaslgaivra ndtraevadq vvslggefvk vdyeeegsgg
      241 ggyakvmseg fqaaqremya kqarevdiii ttalipgkpa pklitaemvr smkpgsvivd
      301 maaeqggnce ltepgksvvk hgvtivgytd lasrmarqss tlygtnlfrl teelcktkdg
      361 vinvnmadda irgltvikdg evtwpappia aapkppakpa vaapkapahg hgpgepmsak
      421 tlaivfgvga llfalvglya pasflshftv fvlacfvgym vvwnvtpslh tplmsvtnai
      481 ssiiaigali qvappldaag aadrpnalil gcavvalvlt ainmfggfav trrmlamfrk
//
LOCUS       WP_127808201             422 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127808201
VERSION     WP_127808201.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43429
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglnsrivda dyasagaaig
       61 kasdvakadv vlkvrrpgda elksyrpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafvksdq qphvepaaip aktmvadasp kkaapkkpaa skspsskskg
      421 ia
//
LOCUS       WP_127812362             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Bordetella
            avium].
ACCESSION   WP_127812362
VERSION     WP_127812362.1
KEYWORDS    RefSeq.
SOURCE      Bordetella avium
  ORGANISM  Bordetella avium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Bordetella.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Bordetella avium"
                     /db_xref="taxon:521"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38938
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipketr dgetrvaatp etvkkyvtvg havvveqgag eraryrdedy aaagasltdr
       61 aaalgselvl kvrapdadel rlmrrgavlv gmlapfdaag lariaaaglt afaleaapri
      121 traqnldvls sqanlagyka vllaadhstr ifpmmmtaag tlkaarvvvl gagvaglqai
      181 atakrlgaiv easdvrpaak eqieslgarf idvpfeteee rdiaqgsggy arpmpaawma
      241 rqaalvaqrc qqadvvitta lipgrpapql isadtvagmk agavlvdlai erggncplte
      301 kgsvvekhgv tligllnlpg mlatdasaly arnlmdflkl iigedaalnl rreddivaac
      361 lvcqdgqilr rf
//
LOCUS       WP_127813535             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bacillus thuringiensis].
ACCESSION   WP_127813535
VERSION     WP_127813535.1
KEYWORDS    RefSeq.
SOURCE      Bacillus thuringiensis
  ORGANISM  Bacillus thuringiensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Bacillus thuringiensis"
                     /db_xref="taxon:1428"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34480
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseekiydvi iigagpagmt aavytsranl stlmlergip ggqmantedv enypgyesil
       61 gpdlsnkmfe hakkfgaeya ygdvkevidg keyktiiagk keykaraiiv asgaeykkig
      121 vpgetelggr gvsycavcdg affkgkelvv igggdsavee gvfltrfask vtivhrrdtl
      181 raqkilqdra fqnekvdfiw nhtikeinea ngkvgsvtlv dvnsgeekev ktdgvfvyig
      241 mlplskpfve lgitnengyl etnermetkv pgifaagdvr ekmlrqivta tgdgsiaaqs
      301 aqhyveelle alktvsek
//
LOCUS       WP_127818776             322 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Microbacterium sp. CPCC 204701].
ACCESSION   WP_127818776
VERSION     WP_127818776.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. CPCC 204701
  ORGANISM  Microbacterium sp. CPCC 204701
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Microbacterium sp. CPCC 204701"
                     /db_xref="taxon:2493084"
     Protein         <1..322
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          <1..318
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 rpevadqvas iggvyleviv pdeakevsad gyakatseay drraaeiyse qaadvdiiit
       61 talipgrpap rlitaadvas mkpgsvivdm aaaqggnveg svagervvte ggvvilgytd
      121 lpgrlpqqas qlfatnlvnl vklltpakdg tlaldfddvv qrtvtvvreg eamwppppvq
      181 vsappaapka alpgagagvp aknpmsprar mwlvvagiaa lfaicafapp plpqhflvlt
      241 laivvgfyvi ghvahalhtp lmsvtnaisg iivvgamvqi tapdltvqil aaiavlvasi
      301 nifggfavtr rmlamfqkge ar
//
LOCUS       WP_127819743             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium sp. CPCC 204701].
ACCESSION   WP_127819743
VERSION     WP_127819743.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium sp. CPCC 204701
  ORGANISM  Microbacterium sp. CPCC 204701
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Microbacterium sp. CPCC 204701"
                     /db_xref="taxon:2493084"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34638
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqviiigsg pagytaaiya aranlnplvv assveaggel mnttdvenfp gfpegiqgpd
       61 lmakmqeqae rfgaevlfdd vvslevdgpv kkitlgsggt headsivfat gsaprkigid
      121 gearlsgrgv sycatcdgff frerviavvg ggdsameeat fltkfaskvy iihrreelra
      181 skimqerafk nekiefvwns evvdilgdda vtgvvlkdtv destrelpld gifvaigndp
      241 rthlvhdkle ltpegtiwvd grssrtsvpg vfaagdvidp tyrqavtaag sgtvaaldve
      301 hylaalgeag apdvhgdqle glpeadaa
//
LOCUS       WP_127822576             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_127822576
VERSION     WP_127822576.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53598
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qcyveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_127827535             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces antnestii].
ACCESSION   WP_127827535
VERSION     WP_127827535.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces antnestii
  ORGANISM  Streptomyces antnestii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces antnestii"
                     /db_xref="taxon:2494256"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33910
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgim
       61 gpelmdnmra qaerfgaeli pddvisvdlt geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afadpkikfv wdseiaevhg dqklshltlr nvktgetsel pvtglfiaig
      241 hdprtelfkg qlelddegyl kveapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala dsetaaatav
//
LOCUS       WP_127835923             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lactobacillus johnsonii].
ACCESSION   WP_127835923
VERSION     WP_127835923.1
KEYWORDS    RefSeq.
SOURCE      Lactobacillus johnsonii
  ORGANISM  Lactobacillus johnsonii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactobacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Lactobacillus johnsonii"
                     /db_xref="taxon:33959"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33534
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maekknydvi vigagpgglt aalyaaranl kvvildrgiy ggqmnntagi dnypgfvdiq
       61 gpelgekmyq tatnagaefa ygdvqsirqd gnkkivktds geyeagaivi atgavhkhlg
      121 vpgeeeyagk gvsycavcda affrdedvav igggdsaiqe glylaqsaks vtvihrrdql
      181 rakaklqkka fendkmkfiw naqteeivgd gnkvtdvkyk dketgeekei kvagvfiyvg
      241 iqpqtdafrd lgitdeqgwi ltddhmrtkv dgifalgdvr akelrqiata vgegsiagqe
      301 vynyyqglde d
//
LOCUS       WP_127836284             307 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium prolinivorans].
ACCESSION   WP_127836284
VERSION     WP_127836284.1
KEYWORDS    RefSeq.
SOURCE      Clostridium prolinivorans
  ORGANISM  Clostridium prolinivorans
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Clostridium prolinivorans"
                     /db_xref="taxon:2769420"
     gene            1..307
                     /gene="trxB"
     Protein         1..307
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33430
     Region          5..285
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhniydivii gggpaglsaa iyaarskmdt lvierskfgg qtattdeien ypgsienctg
       61 pqlvermrkq aedfgtkfek deilevdfts kikelkgnkd iykaksviia tgaspklagf
      121 kneielrgrg isycatcdad fftdlnvavv gggdsaltea iyltkfaesv tiihrrdkfr
      181 gvksiqekvf nnpkikviyd svveeaigdg ilegliiknv ktgeksnlkv dgcfvfvgye
      241 pisdlfkdki kmneagyiit deemktnipg vfaagdirvk slrqvitaaa dgaiaatnae
      301 hylenef
//
LOCUS       WP_127842537             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces wuliandei].
ACCESSION   WP_127842537
VERSION     WP_127842537.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces wuliandei
  ORGANISM  Actinomyces wuliandei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Actinomyces wuliandei"
                     /db_xref="taxon:2057743"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53305
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrtgipcerp gqalvaatpq tvsrlvrlgy evcvqrgagq aasfpdsaye evgaqvtdea
       61 qvwgcevvlg vdapdeehla lmspgaayvg rlaparspel vealrarglt glaldavpri
      121 sraqamdvls sqanlagyra vieaaahfgr vftgqvtaag klppasvyvi gagvaglaai
      181 gtasslgaqv rgtdvrpeve dqvrsmgatf vpvpsapghq eassdgyarq msaeqaelaa
      241 alyakeaaea divittasvp grqapvlltr aalegmrpgs vvvdmaaang gnteltapse
      301 vvvtdggvti vgytdlagrl ptqasqlygq nlvnlltlmt pakdgvltld ledqvvrgit
      361 vthagevlwp ppavtvsaap aagagtappg teapdtsaaa qeaaqrrars aararragla
      421 aaaltlaalv lvtpvaaash yivlmlavvl gfyvisnvtp alhtplmsvt naisgiillg
      481 aisqvgnddf lvsavsllai vlasvnvfgg favthrmlam frkd
//
LOCUS       WP_127843091             306 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinomyces wuliandei].
ACCESSION   WP_127843091
VERSION     WP_127843091.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces wuliandei
  ORGANISM  Actinomyces wuliandei
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Actinomyces wuliandei"
                     /db_xref="taxon:2057743"
     gene            1..306
                     /gene="trxB"
     Protein         1..306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32537
     Region          3..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mihdvvivgs gpagytaaiy aaraqlapiv lagsvtagga lmntteveny pgfvqgvmgp
       61 tlmtqmqeqa erfgaevrye dvtalelegt tkrvvteegt yeartviist gseyrhlgve
      121 gedrlsghgv sycatcdgff fkdqdvvvvg ggdsameeat fltrfarsvt vvhrrdelra
      181 savmaqraqd dpkitfawns tvaelrgqds ltgvtledtv tgerrqlevt glfvaigqvp
      241 rselvkdvld ldgagyiqve apsqrtrlpg vfacgdvadp syqqavtaag sgcraaldae
      301 hylatl
//
LOCUS       WP_127848916             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus hulanensis].
ACCESSION   WP_127848916
VERSION     WP_127848916.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus hulanensis
  ORGANISM  Lacticaseibacillus hulanensis
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Lacticaseibacillus hulanensis"
                     /db_xref="taxon:2493111"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33240
     Region          6..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtksvdvvvi gagpggmtaa lyasranlsv vmldrgiygg qmnntatien ypgytsilgp
       61 dlgekmyaga tqfgadyeyg nvtgvedkga tkivhtddgd yeakavilat gaehrkvgip
      121 geeeysgrgv sycavcdgaf frdrdlvvig ggdsaieegl yltqlaksvt vihrrdqlra
      181 qkiiqqrafa ndkmhfiwng lvqsvegdgk evtgvtykdk ftgeeatvpa agvfiyvgik
      241 pmtdafaglg vldehgwvit ndqmetsvpg iyaigdvrqk tlrqittavg dgglagqgvf
      301 nyiqslqdae ika
//
LOCUS       WP_127846283             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Psychroflexus aestuariivivens].
ACCESSION   WP_127846283
VERSION     WP_127846283.1
KEYWORDS    RefSeq.
SOURCE      Psychroflexus aestuariivivens
  ORGANISM  Psychroflexus aestuariivivens
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Psychroflexus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Psychroflexus aestuariivivens"
                     /db_xref="taxon:1795040"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35238
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msenierikc liigsgpagy taaiyaarad mkpvvytgme pggqltttte vdnfpgypeg
       61 idgprmmvdl qnqaerfgtd vrvgmvtkve lsdkiggihk aqidnknwve antviistga
      121 sakylglpse qklrgggvsa cavcdgffyk gqdvaivggg dtaceeatyl anictkvtml
      181 vrkgemkask amqhrventk nidlryhsev devlgdqvve glrivnnqtg ekeeisitgl
      241 fiaighkpnt difknylemd dvgyiitksk stktnypgvf acgdsqdkey rqaitaagtg
      301 cmasldaery lnsvedivep eteeasa
//
LOCUS       WP_127853496             416 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M00.F.Ca.ET.216.01.1.1].
ACCESSION   WP_127853496
VERSION     WP_127853496.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M00.F.Ca.ET.216.01.1.1
  ORGANISM  Mesorhizobium sp. M00.F.Ca.ET.216.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Mesorhizobium sp. M00.F.Ca.ET.216.01.1.1"
                     /db_xref="taxon:2500528"
     Protein         1..416
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42494
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvtveag agtasripde efakagaaig
       61 kagdvakadv vlkvrrpgea elkayrpgta viaimdpygn dagvaalasa gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflaiedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitaa lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaa
      301 sgqvvttang vkivghlnvp grvaasasll yarnlfafve tlvdkatktl ainrddelvk
      361 atmltdggqv vhpafagkpa mmiassehar paaakkpaap kkpaaarkpk tsggia
//
LOCUS       WP_127854737             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_127854737
VERSION     WP_127854737.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34588
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtvkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfgdpiq
       61 gpwlmgemlk qaehvgtdii sdiitevdln vrpfrakgds gttytadtli iatgaqakwl
      121 gipteqtfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilqer lfkrdnvrvi wdtvvdeitg rpgktplpps veglklrnav tgqeshlkve
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127861782             426 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127861782
VERSION     WP_127861782.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43840
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsripde efakagaaig
       61 kaadaskadv vlkvrrptda elkgyksgaa viaimdpygn daalsamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvs grvaasasll yaknlyafle tmvdkaakel aikrddelvk
      361 atmltdggkv vhpafakave aprtepaaip attmvadasa kpavkktaak kpvaakspss
      421 kskgta
//
LOCUS       WP_127858466             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_127858466
VERSION     WP_127858466.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34475
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdiv ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylanlak svtvihrrsd
      181 fraerilrer lfkkdnvrvi wdtvvdeitg qpgkaplpps veglklrnva tgevsrlkvd
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127864570             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_127864570
VERSION     WP_127864570.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34397
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnikhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilrer llakdnvrai wdtvvdeitg rpgkaplpps vegltlrsvv tgqesklpvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127871969             422 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127871969
VERSION     WP_127871969.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43484
     Region          3..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(16,74,93,290,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(45,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 maiifiprel haneprvaas pdtvkrlaal gldvivenga gtrsripdee fakagatigk
       61 agdaakadvv lkvrrpseae lkgykpgttv iaimdpygnd aavaalakag vtafsmefmp
      121 ritraqsmdv lssqanlagy qavidgasey dralpmmmta agtvpaakvf imgvgvaglq
      181 aiatarrlga vvtatdvrpa akeqvsslga kflavedeef kaaetaggya kemsreyqak
      241 qaaltaehia kqdivittal ipgrpapklv saamvasmkp gsvivdlave rggnvegava
      301 gqivttannv rivghlnvpg rvaasaslly arnlfaflet lvdkttktla inrdddlvka
      361 tmltdggkvv hpafakadqq phiepaaipa ktmvadagaa kkaaskkaaa pkspsskskg
      421 ia
//
LOCUS       WP_127866592             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M2E.F.Ca.ET.219.01.1.1].
ACCESSION   WP_127866592
VERSION     WP_127866592.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M2E.F.Ca.ET.219.01.1.1
  ORGANISM  Mesorhizobium sp. M2E.F.Ca.ET.219.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mesorhizobium sp. M2E.F.Ca.ET.219.01.1.1"
                     /db_xref="taxon:2500530"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43687
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqivfipre ldpseprvaa spetvkrlag lgfdvivekg aglgsripdq dftavgaaig
       61 ktadaskadv vlkvrrptda elkgyksgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmr pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatkql aikrddelvk
      361 atmltdggkv vhpnfakaae eprtepaaip attmvaeaaa pkpapkkraa aaksptsktk
      421 gta
//
LOCUS       WP_127872940             425 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127872940
VERSION     WP_127872940.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..425
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43811
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdviveag agtrsripde efaktgavig
       61 kasdvakadv vlkvrrptda elksykagaa viaimdpygn daavaalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 pgkivttann vkivghlnvp grvaasasll yaknlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafakadq qpyvepavip attlvadast papkkaaakk paapkspask
      421 pkgta
//
LOCUS       WP_127873462             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_127873462
VERSION     WP_127873462.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34546
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipteqdfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrsd
      181 fraerilrer llkkdnvrvi wdtivdeitg rpgkaplpps veglklrhav tgaeshlkid
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_127878456             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M2E.F.Ca.ET.209.01.1.1].
ACCESSION   WP_127878456
VERSION     WP_127878456.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M2E.F.Ca.ET.209.01.1.1
  ORGANISM  Mesorhizobium sp. M2E.F.Ca.ET.209.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mesorhizobium sp. M2E.F.Ca.ET.209.01.1.1"
                     /db_xref="taxon:2500526"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43671
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqivfipre ldpseprvaa spetvkrlag lgfdvivekg aglgsripdq dfaavgaaig
       61 ktadaskadv vlkvrrptda elkgyksgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmr pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatkql aikrddelvk
      361 atmltdggkv vhpnfakaae eprtepaaip attmvaeaad pkpapkkraa aaksptsktk
      421 gta
//
LOCUS       WP_127878766             423 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_127878766
VERSION     WP_127878766.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43713
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqivfipre ldpseprvaa spetvkrlag lgfdvivekg aglgsripdq dftavgaaig
       61 ktadaskadv vlkvrrptda elkgyrsgav viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmr pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatkql aikrddelvk
      361 atmltdggkv vhpnfakaae eprtepaaip attmvaeaaa pkpapkkraa aaksptsktk
      421 gta
//
LOCUS       WP_127881030             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas carnis].
ACCESSION   WP_127881030
VERSION     WP_127881030.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas carnis
  ORGANISM  Pseudomonas carnis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas carnis"
                     /db_xref="taxon:2487355"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33863
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdtrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpvlmermk ehaerfetei vfdhinqvdf skkpysltgd sgvytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlvhrret
      181 fraekilidk lharvaegki ilklnatlde vlgdnmgvtg arlknndgsf delkvdgvfi
      241 aightpntsl fegvleakdg ylvvqggreg natatniegi faagdvadhv yrqaitsaga
      301 gcmaaldaer yldalkdasf
//
LOCUS       WP_127889492             381 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Ensifer
            adhaerens].
ACCESSION   WP_127889492
VERSION     WP_127889492.1
KEYWORDS    RefSeq.
SOURCE      Ensifer adhaerens (Sinorhizobium morelense = Ensifer morelensis)
  ORGANISM  Ensifer adhaerens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group;
            Ensifer.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Ensifer adhaerens"
                     /db_xref="taxon:106592"
     Protein         1..381
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39525
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mseivfvake tdpnegrvaa spdtvkklkg lgfdvvveag agflsripda efekagarig
       61 ttadartadv vlkvrpptsv eiagyrsgai viaimdpygn eaviaemana gltafamelm
      121 pritraqsmd vlssqanlag yqavidaaye ydralpmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg avvsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemskdyqa
      241 kqaalvaehi akqdivitta lipgrpaprl vtremlksmk pgsiavdlav erggnvegae
      301 agkvaevegv kvighlnvpg riaasasgly aknlvtflet mvsketkala lnmedelvka
      361 talthggqvv hpnfgaskgd k
//
LOCUS       WP_127898450             524 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Paracoccus].
ACCESSION   WP_127898450
VERSION     WP_127898450.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55241
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigatresf egearvaitp staahlgklg hdvfvesgag aragfadddy rsagvtvcqt
       61 aaelidavdv vakvrqptta eigqmkagqt lisffypaqn aellaqakdq gitaiamdmv
      121 prisraqkmd alssmaniag yravieaann fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtsvslg aqvhafdvrp evaeqiesmg aefvyldfda paqdgaatgg yaapsspefr
      241 ekqlarfrel apqmdivitt alipgrdapk lwtadmvamm kqgsviidla aekggncdlt
      301 vpderivtdn gvvivgytdf psrmgaqase lygnnirhfv adltpkkdgv ivhnmeddvi
      361 rgatvvhdhd vtwpppppkv aaiaaqkpke kkkeltpder raadaaafka etasqiklll
      421 ggglvvllig liapasfmsh fivfvlacfv gfrviwnvah slhtplmait naissiiilg
      481 almqigsgsa wvvilgalav lmasvnifgg fmvtrrmlam fqks
//
LOCUS       WP_127899367             327 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Paracoccus].
ACCESSION   WP_127899367
VERSION     WP_127899367.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus
  ORGANISM  Paracoccus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Paracoccus"
                     /db_xref="taxon:265"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34712
     Region          8..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtershvkll ivgsgpagyt aavyasraml gpmliqgmqp ggqltittev enwpgdteiq
       61 gpdlmvkmet haramgaeiv tdlvtaldlq krpftatcds grvvtadavi latgaqarwl
      121 glpseekfkg fgvsacatcd gffyrnrevv vigggntave ealfltkfas kvtlvhrrds
      181 lraekilqnr lfahpkvevi wnselaevtg tetpvgvsga tlrnlvdgtt qtikadgvfv
      241 aighapasel vkdqlelhng gyvkveagst rtsipgvfaa gdltdhiyrq avtsagmgcm
      301 aaldaahfle aqgevelepe qrvaviy
//
LOCUS       WP_127901736             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Solirhodobacter olei].
ACCESSION   WP_127901736
VERSION     WP_127901736.1
KEYWORDS    RefSeq.
SOURCE      Solirhodobacter olei
  ORGANISM  Solirhodobacter olei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Solirhodobacter.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Solirhodobacter olei"
                     /db_xref="taxon:2493082"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33848
     Region          8..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mgetrhskvl iigsgpagyt aavyasraml epvlvqgiqp ggqltittev enwpgdtevq
       61 gpdlmvrmea haaamgaevv gdiitsldls hrpftakgds gttytadavi latgaqakwl
      121 glpseekfkg fgvsacatcd gffyrgkevv vigggntave ealfltnfas kvtlihrrdt
      181 lraekilqhr aennpklsfa wnktveeilg aedplgvtgv rvkdtltgev stipcdgffv
      241 aighapasel vkdqlelhhg gyvkvepgst rtsipgvfaa gdltdhvyrq avtsagmgcm
      301 aaldaerwla eqaavpeaaa ae
//
LOCUS       WP_127904582             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesobaculum littorinae].
ACCESSION   WP_127904582
VERSION     WP_127904582.1
KEYWORDS    RefSeq.
SOURCE      Mesobaculum littorinae
  ORGANISM  Mesobaculum littorinae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Mesobaculum.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Mesobaculum littorinae"
                     /db_xref="taxon:2486419"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35286
     Region          8..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maetkhskvl iigsgpagyt aavyasraml dpvliqgiqp ggqltittdv enwpgeasim
       61 gpdlmvkmea haremgteii gdiitsldls rrpftaqsds gtvytadali latgaqakwl
      121 glpseekfkg fgvsacatcd gffyrgqevv vigggntave ealfltnfas kvtlihrrdt
      181 lraekilqdr lfknpkveim wnhavdevvg aetplgvegv karhietgev tqvpcagffv
      241 aighapasel vadqldthhg gyvvtkpdst etsvpgvfaa gdltdhvyrq avtsagmgcm
      301 aaleaeryla glgevedkde seplgygapi eagh
//
LOCUS       WP_127906028             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesobaculum littorinae].
ACCESSION   WP_127906028
VERSION     WP_127906028.1
KEYWORDS    RefSeq.
SOURCE      Mesobaculum littorinae
  ORGANISM  Mesobaculum littorinae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Roseobacteraceae; Mesobaculum.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Mesobaculum littorinae"
                     /db_xref="taxon:2486419"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55636
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigtpkeim dgearvamtp dsakalqklg hdcvieagag mragftdaay aeagvevveg
       61 pdalwsasei vakvrppted etrrlyagqt lisffypasn aallelakdq gasviamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv livgagvagl
      181 aaigtatslg aityafdvrp evseqiesmg aefvfldfed tatdgaetgg yaapsspefq
      241 ekqlekfrel apdvdivitt alipnrdapv lwtrdmveam kpgsvivdla aerggncels
      301 rkdekivtdn gvtivgytdf psrmatqsst lyatnirhmm tdltpdkdgv vshdmeddvi
      361 rgatvthgge itypppppkv raiaaqpkrd kpkeltpeer raqetaafka qtrqqvtlla
      421 vgaalllavg lvapasfmqh fivfvlsvfv gfqviwgvah slhtplmavt naissiiilg
      481 almqigsgsf lvillgglsv lmaginifgg flvtrrmlam fqks
//
LOCUS       WP_127917418             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Prescottella agglutinans].
ACCESSION   WP_127917418
VERSION     WP_127917418.1
KEYWORDS    RefSeq.
SOURCE      Prescottella agglutinans
  ORGANISM  Prescottella agglutinans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Prescottella.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Prescottella agglutinans"
                     /db_xref="taxon:1644129"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37773
     Region          14..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsksaaqv rpsvgvvret sdgerrvalv pkvvaslaak gvdvvvepga glgalipdel
       61 ykeagatigd awtsdvvvkv appsdsevgk lrsgqtligf laprnaenqi galtaagvsa
      121 faveaipris raqvmdalss qanvagykav lvaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrtt gydvrpevad qvrsvgaqwl dlgidaageg gyareltdae
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvivdl agetggncel
      301 tepgqtavkh gvticsplnl patmpehase lysknvaali elmldengal apdfsdeila
      361 gacvtgsken s
//
LOCUS       WP_127917837             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Prescottella agglutinans].
ACCESSION   WP_127917837
VERSION     WP_127917837.1
KEYWORDS    RefSeq.
SOURCE      Prescottella agglutinans
  ORGANISM  Prescottella agglutinans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Prescottella.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Prescottella agglutinans"
                     /db_xref="taxon:1644129"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34966
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpttvrdl iivgsgpagy tagvyaarae lepllfegtq fggslmttte venfpgfreg
       61 imgpdlmdem reqakrfgad irtedveeie ldgpvkkvva ngetyyarav ilamgaaary
      121 lgipgeekll grgvsacatc dgfffrdqdi vvvgggdsam eeatfltkfa rsvtlvhrre
      181 efrasrimle rakanekirf vtnaepvevl gensvtglvi rdtvtgeqst levtgmfvai
      241 ghdprselvk gqvdldeagy vqvqspttat tapgvfaagd lvdhtyrqai taagtgcsaa
      301 idaerwlaeq gditentlaa agepvavda
//
LOCUS       WP_127908720             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces huasconensis].
ACCESSION   WP_127908720
VERSION     WP_127908720.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces huasconensis
  ORGANISM  Streptomyces huasconensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces huasconensis"
                     /db_xref="taxon:1854574"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33820
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgvm
       61 gpelmdnmra qaerfgaelv pddvvavdls geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrds
      181 lraskamqer afadpkikfi wdsevaeikg dqklsgltlr nlktgetsel pvtglfiaig
      241 hdprtelfkg qlelddegyl kveapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala dsenaatatv
//
LOCUS       WP_127920698             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127920698
VERSION     WP_127920698.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33377
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127922681             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127922681
VERSION     WP_127922681.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33363
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvvlaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127923284             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127923284
VERSION     WP_127923284.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33376
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkhtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdts gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127925105             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127925105
VERSION     WP_127925105.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33396
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdaf gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqgd nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127927540             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127927540
VERSION     WP_127927540.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33455
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdaf gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnveglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127937693             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127937693
VERSION     WP_127937693.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33350
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 tpitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127937859             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nonomuraea polychroma].
ACCESSION   WP_127937859
VERSION     WP_127937859.1
KEYWORDS    RefSeq.
SOURCE      Nonomuraea polychroma
  ORGANISM  Nonomuraea polychroma
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Streptosporangiales; Streptosporangiaceae; Nonomuraea.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Nonomuraea polychroma"
                     /db_xref="taxon:46176"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33390
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa vysaraelkp lvfegsvtag galmnttdve nfpgfpdgim
       61 gpdlmdnlrk qaerfgaelv addvvevdle anpkvvkths etyyaksvil amgsgyrelg
      121 ldnekrlsgh gvswcatcdg fffrnkdivv vgggdtamee atfltrfgrm vtvvhrrdtl
      181 raskimqdra fanekirfvw dsevvdvlgd gkveavklrn lksgeecela tdalfiaigh
      241 dprtdlvkgq idldengyik vaspttatni pgvfaagdvv dhtyrqaita agtgcaasld
      301 serwlaenee
//
LOCUS       WP_127944350             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus spongiicola].
ACCESSION   WP_127944350
VERSION     WP_127944350.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus spongiicola
  ORGANISM  Rhodococcus spongiicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus spongiicola"
                     /db_xref="taxon:2487352"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37968
     Region          14..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 metsksaeqv hpsvgvvret gtderrvalv pkvvaslsnk gvgviveaga glgalipdel
       61 ykeagatvgd awecdvvvkv appsdaevgk lragqtligf laprnadnqi galaaagvta
      121 faveaipris raqvmdalss qanvagykav lvaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrtt gydvrpevae qvrsvgaqwl dlgidaageg gyarelteae
      241 raeqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvivdl agetggncel
      301 tkpgqtiveh gvticsplnl patmpehase lysknvaali elmldengal epdftdeils
      361 gacvtrsken
//
LOCUS       WP_127947482             327 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhodococcus spongiicola].
ACCESSION   WP_127947482
VERSION     WP_127947482.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus spongiicola
  ORGANISM  Rhodococcus spongiicola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Rhodococcus spongiicola"
                     /db_xref="taxon:2487352"
     gene            1..327
                     /gene="trxB"
     Protein         1..327
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34783
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpttvrdl iivgsgpagy tagvyaarae lqpllfegtq fggalmttte venfpgfreg
       61 imgpdlmeem reqakrfgtd irtedveeie ldgpvkkvva ngetyyarai ilamgaaary
      121 lgipgeerll grgvsacatc dgfffrdqdi vvvgggdsam eeatfltkfa rsvtlvhrre
      181 efrasrimle rakanekirf vtnavpvevl gensvtglvi rdtvtgeqst ldvtgmfvai
      241 ghdprselvk gqvdldaagy vtvqsptttt svegvfaagd lvdhtyrqai taagtgcsas
      301 idaerwlaeq geitantlaa agkpvda
//
LOCUS       WP_127950161             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127950161
VERSION     WP_127950161.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33407
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gikevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt fesksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127952539             371 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus xishaensis].
ACCESSION   WP_127952539
VERSION     WP_127952539.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus xishaensis
  ORGANISM  Rhodococcus xishaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rhodococcus xishaensis"
                     /db_xref="taxon:2487364"
     Protein         1..371
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38023
     Region          14..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 metsksadqv hpsvgvvret gaderrvalv pkvvaslsnk gvgvvveaga glgalipdel
       61 yreagatvgd awacdvvvkv appsdaevak lragqmligf laprnadnqi galaaagvta
      121 faveaipris raqvmdalss qanvagykav lvaasestrf fpmlttaagt vkpasvlvlg
      181 vgvaglqala takrlggrtt gydvrpevae qvrsvgaqwl dlgidaageg gyareltdae
      241 raeqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvivdl agetggncel
      301 tepgqtiveh gvticsplnl patmpehase lysknvaall elmldengal epdfsdeils
      361 garvtrsken s
//
LOCUS       WP_127953644             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127953644
VERSION     WP_127953644.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33362
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt ainekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127956920             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit [Serratia
            microhaemolytica].
ACCESSION   WP_127956920
VERSION     WP_127956920.1
KEYWORDS    RefSeq.
SOURCE      Serratia microhaemolytica
  ORGANISM  Serratia microhaemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Serratia microhaemolytica"
                     /db_xref="taxon:2675110"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53017
     Region          27..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mlmlklhhip llltvtglgl lpssllaqan apqstatiet rserfatnlp dqyqswrata
       61 eqskqvdala edprlvilwa gyafakdynk prghafaltd vratlrtgap ktaedgplpm
      121 acwsckspdv arvinqqgee hyfrgqwarg gpeivnplgc adchntasaa fkqgkpeltl
      181 srpyadramq slgksfhseg rlsqqsmvcg qchveyyfsg knkavkfpwd qgtrvddmed
      241 yydklnfsdw vhplsktpml kaqhpefetw ragihgknnv tcidchmpkv qnsagkvytd
      301 hkignpfdnf dqscanchtq dkaslqavva qrkhdvneik lkvedqlvha hfeakaawsa
      361 gvssaemqpi lqdirhaqwr wdyaiashgv hmhapdvalr vlataldkaa sartklarvl
      421 atkgisheia lpdisskeka qlalgmdmqq lnaekqqfln tvvprwdeqa rnagllgk
//
LOCUS       WP_127954577             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhodococcus xishaensis].
ACCESSION   WP_127954577
VERSION     WP_127954577.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus xishaensis
  ORGANISM  Rhodococcus xishaensis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rhodococcus xishaensis"
                     /db_xref="taxon:2487364"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35097
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpttvrdl iivgsgpagy tagvyaarae lepllfegtq fggalmttte venfpgfreg
       61 imgpdlmeem reqakrfgtd irtedveeie ldgpvkkvva ngetyyarai ilamgaaary
      121 lgipgeerll grgvsacatc dgfffrdqdi vvvgggdsam eeatfltkfa rtvtlvhrre
      181 efrasrimle rakanekirf vtnavpvevl gdnsvtglvi rdtvtgeest ldvtgmfvai
      241 ghdprselvk gqvdldaagy vtvqlpttat svegvfaagd lvdhtyrqai taagtgcsas
      301 idaerwlaeq geitantlda agkpvdsrv
//
LOCUS       WP_127960047             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Serratia microhaemolytica].
ACCESSION   WP_127960047
VERSION     WP_127960047.1
KEYWORDS    RefSeq.
SOURCE      Serratia microhaemolytica
  ORGANISM  Serratia microhaemolytica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Serratia microhaemolytica"
                     /db_xref="taxon:2675110"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34654
     Region          1..321
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mstakhskll ilgsgpagyt aavyaaranl hpmlitgiqp ggqltttsei enwpgdggel
       61 tgtalmdrmr ehaekfdtei vfdhiqrvel qqrpfrlfgd nnqytcdali iatgasaryl
      121 gleseeafkg kgvsacatcd gffyrnqkva vvgggntave ealylaniaa evhlihrrds
      181 frsekilinr lmekvkngni vlhthrtlde vlgdemgvtg vrlrdvnatq hteelavagv
      241 fiaighspnt aifgdqlele ngyikvhsgi hgnatqtsip gvfaagdvmd hiyrqaitsa
      301 gtgcmaalda eryldslang gns
//
LOCUS       WP_127962040             335 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gordonia alkanivorans].
ACCESSION   WP_127962040
VERSION     WP_127962040.1
KEYWORDS    RefSeq.
SOURCE      Gordonia alkanivorans
  ORGANISM  Gordonia alkanivorans
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Gordoniaceae; Gordonia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Gordonia alkanivorans"
                     /db_xref="taxon:84096"
     gene            1..335
                     /gene="trxB"
     Protein         1..335
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35627
     Region          10..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqpetqqih dviiigsgpa gytaaiyaar aelapivfeg tqfggalmtt tevenfpgfq
       61 tgiqgpalmd emreqairfg adlrmedvdt vrlagdikev evggevfrar avilamgaaa
      121 rylgikgeqe llgrgvsaca tcdgfffkdq diavigggds ameeatfltk fartvtlvhr
      181 rdefraskim lerardndki rfvtnaavrs vigdgsvsgl eiedtrngev snldvtgmfv
      241 aighdprsel vrgqvdldde gyvlvqgrtt ytslpgvfac gdlvdhtyrq aitaagsgcs
      301 aaidaerwla eqgeapahtv daesvadvea vqapa
//
LOCUS       WP_127964100             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127964100
VERSION     WP_127964100.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33440
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdaf gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127969728             316 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Hahella].
ACCESSION   WP_127969728
VERSION     WP_127969728.1
KEYWORDS    RefSeq.
SOURCE      unclassified Hahella
  ORGANISM  unclassified Hahella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="unclassified Hahella"
                     /db_xref="taxon:2624107"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34067
     Region          5..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msketrhikl lilgsgpagy taavyaaran lnpviitgmq mggqlttttd vdnwpgddag
       61 vqgpelmqrm qkhaerfdte iifdhinetd lsqrpfrlkg dngeytcdal iiatgasaqy
      121 lgldseeafk gkgvsacatc dgffyrkqkv avigggntav eealylsnia aevtlvhrrd
      181 klraekilqd klfekeqngn ikivwdhtld evlgddsgvt glrlrstkdd stqelevtga
      241 fiaighkpnt difagqldmk dgyikirsgs egnatqtsvp gvfaagdvad hiyrqavtsa
      301 gfgcmaalda ekfldq
//
LOCUS       WP_127970925             508 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Hahella
            sp. KA22].
ACCESSION   WP_127970925
VERSION     WP_127970925.1
KEYWORDS    RefSeq.
SOURCE      Hahella sp. KA22
  ORGANISM  Hahella sp. KA22
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Oceanospirillales; Hahellaceae; Hahella.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Hahella sp. KA22"
                     /db_xref="taxon:1628392"
     Protein         1..508
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54116
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mqigipkesr phekrvaatp ksveeliklg fsvaveadag wlssfgdgmy eevgakvvsr
       61 eeawgadivl rvnepndeev ellksgatli gfiwpsqhee llqklaqrnv tvlamdsvpr
      121 israqsmdal ssmaniagyr avveashhfg rfftgqitaa gkvqpakilv igagvaglaa
      181 igtagslgai vrafdtrpev keqiqsmgae flevdmeees ssgdgyakvm skafieaemk
      241 lfleqakdvd iiittamipg kpapklitee mvkamrpgsv ivdlaapngg nceltqpgem
      301 aeihevkivg yvdlpsrlpt qasllysnnl vnlmkllckn kdgavdinfe devirgvtvv
      361 kdgeitwppp pikvsaapqq pkaaaapppp ksqpmsssfk hglqaagala liwlasaaps
      421 eflshftvfv lacivgyhvv wsvthalhtp lmsvtnaisg iivvgallqi ssdsllvtfl
      481 aaaatliati nivggfvvth rmlkmfrk
//
LOCUS       WP_127967506             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127967506
VERSION     WP_127967506.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33321
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127971172             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127971172
VERSION     WP_127971172.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33353
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdts gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127974978             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127974978
VERSION     WP_127974978.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33446
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslnikni atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127976111             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127976111
VERSION     WP_127976111.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33352
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelav pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127981672             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127981672
VERSION     WP_127981672.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33391
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt vtnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127983826             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127983826
VERSION     WP_127983826.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33276
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ngkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127984480             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127984480
VERSION     WP_127984480.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33354
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgtta
      301 alsvisyleh h
//
LOCUS       WP_127985091             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127985091
VERSION     WP_127985091.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33408
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgnas gvsslsirnt atnetrelvv pgffifvgyd
      241 vnnavlkqed dsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127990534             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_127990534
VERSION     WP_127990534.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33281
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkgsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveesi ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_127995978             526 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Piscinibacter defluvii].
ACCESSION   WP_127995978
VERSION     WP_127995978.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter defluvii
  ORGANISM  Piscinibacter defluvii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Piscinibacter defluvii"
                     /db_xref="taxon:1796922"
     Protein         1..526
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54196
     Region          1..526
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigvpreta agekrvatvp dvveklvklg fsvavqsgag eaanfaddty raagaeivgs
       61 aaelwagsdi vfkvrpptld evglmreggt ligfvwpaqn pqlmealaar katvlaidcl
      121 prqlsraqkm daltsmagvs gyravieaan afgryfngqi taagkippak vfiagagvag
      181 laaigtaagl gaivrandtr aevadqvvsl ggefvkvdye eegsggggya kvmsegfqaa
      241 qramyaqqar ecdiiittal ipgkpaprli taemvqsmrp gsvivdmaae qggnceltep
      301 gqavvkhgvt iigytdlasr lakqsstlys tnllrlteel ckakdgvavv nmdddairgl
      361 tvikdgsltw papplklpap ppkpkaaaaa papkghghga gepmsakala ivfavgalal
      421 lgvglfapas flshftvfvl acfvgymviw nvtpslhtpl msvtnaissi iaigaliqia
      481 pplagdaggr pnglilgmav lalvltainm fggfavtrrm lamfrk
//
LOCUS       WP_127999049             316 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Piscinibacter].
ACCESSION   WP_127999049
VERSION     WP_127999049.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter
  ORGANISM  Piscinibacter
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Piscinibacter"
                     /db_xref="taxon:1114981"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33896
     Region          7..315
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mstaplharv lilgsgpagy taavyaaran lkpvlitgia qggqlmtttd vdnwpadvdg
       61 vmgpdlmtrf qkhaerfntq ivfdhinevd fsrrpftlkg dsgsytcdal iiatgasaky
      121 lglpseqaym grgvsgcatc dgffyrnqev cvvgggntav eealylsnia skvhlihrrd
      181 kfraepilvd klmervtagk mqlhlwqtld evlgdargvs gvrlkgtqda ssrelkvsgc
      241 fiaighqpnt difkgqlemr dgyivtksgl ngmatmtsvp gifaagdvqd hvyrqaitsa
      301 gtgcmaalda qrfleq
//
LOCUS       WP_128003797             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128003797
VERSION     WP_128003797.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33391
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fergmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128009759             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128009759
VERSION     WP_128009759.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33293
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn nnkiefltpy vveeikgdas gvsslsirnt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128006848             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128006848
VERSION     WP_128006848.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33306
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 gesefwgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128011922             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128011922
VERSION     WP_128011922.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33331
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pglfifvgyd
      241 vnnavlkqed gsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128012459             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128012459
VERSION     WP_128012459.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33382
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdveglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128013208             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128013208
VERSION     WP_128013208.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33395
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnveglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128015332             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128015332
VERSION     WP_128015332.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33406
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlkhakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128014244             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128014244
VERSION     WP_128014244.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33361
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsikst atnekrelvv pglfifvgyd
      241 vnnavlkqed nsmlcecdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128019435             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128019435
VERSION     WP_128019435.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33414
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvifaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128018990             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128018990
VERSION     WP_128018990.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33309
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgvk
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn nnkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128021507             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128021507
VERSION     WP_128021507.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33334
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgna feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylvnickkvy lihrrdgfrc
      181 apitlehakn nnkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128022455             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128022455
VERSION     WP_128022455.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33350
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128023266             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128023266
VERSION     WP_128023266.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33335
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgki feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128024980             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128024980
VERSION     WP_128024980.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33351
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128029754             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128029754
VERSION     WP_128029754.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33359
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvvlaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt ttnekrelvv pglfifvgyd
      241 vnnavlkqed nsmlcecdky gsivvdfsmk tniqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128029145             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128029145
VERSION     WP_128029145.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33392
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn nnniefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128030741             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128030741
VERSION     WP_128030741.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33367
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksvivat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128033790             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128033790
VERSION     WP_128033790.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33324
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgnt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128036845             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128036845
VERSION     WP_128036845.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33263
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpc vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128038539             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128038539
VERSION     WP_128038539.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33321
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128041204             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128041204
VERSION     WP_128041204.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33395
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128043210             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128043210
VERSION     WP_128043210.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33350
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkgsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128044139             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128044139
VERSION     WP_128044139.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33409
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt fearsviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnetrelvv pgffifvgyd
      241 vnnavlkqed ssmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128044690             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128044690
VERSION     WP_128044690.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33287
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkgsh fvilaedgkt feaksviiat ggspkhtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128046294             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128046294
VERSION     WP_128046294.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33326
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehaks ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgtta
      301 alsvisyleh h
//
LOCUS       WP_128048091             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128048091
VERSION     WP_128048091.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33391
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128047050             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128047050
VERSION     WP_128047050.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33408
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskrdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128056989             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128056989
VERSION     WP_128056989.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33363
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt ainekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128058462             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128058462
VERSION     WP_128058462.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33436
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt atnekrelvv pgffifvgyd
      241 vnnavlkqed dsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128061556             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128061556
VERSION     WP_128061556.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33379
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgrt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnekrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128064034             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128064034
VERSION     WP_128064034.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33337
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fiilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed gsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128063220             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128063220
VERSION     WP_128063220.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33408
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta iqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128071586             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128071586
VERSION     WP_128071586.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33377
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslniknt aanetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128075319             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128075319
VERSION     WP_128075319.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33409
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv icaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128076613             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128076613
VERSION     WP_128076613.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33394
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsvknt atnekrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tdvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128093383             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Brucella pituitosa].
ACCESSION   WP_128093383
VERSION     WP_128093383.1
KEYWORDS    RefSeq.
SOURCE      Brucella pituitosa (Ochrobactrum pituitosum)
  ORGANISM  Brucella pituitosa
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Brucella pituitosa"
                     /db_xref="taxon:571256"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34522
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqrhapviv igsgpagyta aiyaaramlk piiitglqqg gqlmittdve nypgyaepvq
       61 gpwmmdqmat qaqnvgaeil ydiitevdtt srpfrligds gmvytcdali iatgaqakwl
      121 gleseqtfmg ggvsacatcd gffyrgkdvv vvgggntave ealylshiak svtvvhrreg
      181 fraekimqdr lmsrdnvkvi wnsvideivg teakppmgat vtgvrlkniv tgelseheth
      241 gvfvaighap avslfegklk qkpngylwta pdstatnvpg ifaagdvtdd iyrqavtaag
      301 mgcmaalese rwlaaqeplh eaae
//
LOCUS       WP_128097970             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Stenotrophomonas sp.
            HMWF003].
ACCESSION   WP_128097970
VERSION     WP_128097970.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. HMWF003
  ORGANISM  Stenotrophomonas sp. HMWF003
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Stenotrophomonas sp. HMWF003"
                     /db_xref="taxon:2056840"
     gene            <1..317
                     /gene="trxB"
     Protein         <1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          5..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 srhqklvilg sgpagwtaav yaaranlkpv vitglqqggq lmtttevdnw pgdahglmgp
       61 dlmarmqaha erfetevifd hihtadlaqr pfrligdsae ytcdaliiat gatakylgip
      121 teeefkgrgv sacatcdgff yrdqdvvvvg ggntaveeal ylsniarkvy lvhrrdtlka
      181 ekimqdklfa kvaagkietv whhqvdevlg neagvtgvrv kstldgstrd ieahgffvai
      241 ghhpntslfe gqltmnngyl dirsglggna tqtsvegvfa agdvadqhyr qaitsagfgc
      301 maaldaeryl dakgmas
//
LOCUS       WP_128099842             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus sp. DCT19].
ACCESSION   WP_128099842
VERSION     WP_128099842.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. DCT19
  ORGANISM  Paenibacillus sp. DCT19
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paenibacillus sp. DCT19"
                     /db_xref="taxon:2211212"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34193
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mskyrtivig tgpagltaai ylaranlnpl vieglqpggq lttttevenf pgfpqgimgp
       61 elmdnmrkqa erfgaeftng wveevdfskp pfkvkvggig dleadsiiis tgasarylgi
      121 pgeqenvgrg vstcatcdgf ffrgkkiivv gggdsameea sfltrfatdv tlvhrrdelr
      181 askimqdrar snekvkwaln rtplevvpea lgvkglkvrn nesgqeelle adgvfvaigh
      241 tpntgflgnq vtlddhgyvv vkpgttetni pgvfacgdvq dtkyrqaita agsgcmaamd
      301 cekflegsiv hdwsetldk
//
LOCUS       WP_128103586             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus sp. DCT19].
ACCESSION   WP_128103586
VERSION     WP_128103586.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. DCT19
  ORGANISM  Paenibacillus sp. DCT19
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenibacillus sp. DCT19"
                     /db_xref="taxon:2211212"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33231
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksiiigtg pagltaaiyl aranlsplvi egpqpggqlt tttevenfpg fpdgimgpel
       61 mdnmrkqaer fgaefrtgwv nnidmserpf kiqvegmgel vsetlilstg asakylgipg
      121 eetnvgrgvs tcatcdgfff rnkeiivigg gdsaleeasf lsrfgskvtl vhrreelrgs
      181 kimqdrarsn ekvemalnrt pievlageng vtglkvlnna tgeeevlpas gvfvaightp
      241 ntgflggqit tdehgyiltt pgtsetnipg vfacgdvqdt rykqaitaag sgcmaamdte
      301 kyieslehta vsl
//
LOCUS       WP_128105601             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Acetobacter oryzoeni].
ACCESSION   WP_128105601
VERSION     WP_128105601.1
KEYWORDS    RefSeq.
SOURCE      Acetobacter oryzoeni
  ORGANISM  Acetobacter oryzoeni
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Acetobacterales; Acetobacteraceae; Acetobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Acetobacter oryzoeni"
                     /db_xref="taxon:2500548"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33041
     Region          8..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 maetittdll vigagpagyt aaiyaaranl spvlvaglqp ggqltittev enypgfatai
       61 qgpwlmeqma eqaqnvgtri eydiitsvdf kagspflltg dsgtiykara vvvatgaqar
      121 wlglpsekhl qgagvsacat cdgffyrgkn vvvvgggnta veealylthh aahvtlvhrr
      181 dslraekilq drlfanpkvs viwnsvvedi ladgtpetvc gvrlkntqdg seqtiptdgv
      241 fiaighapnt aifrdqltld aegyiettpg ttrtsvpgvf aagdvqdkty rqavtaagtg
      301 cmaaldaery lagls
//
LOCUS       WP_128108524             510 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mycolicibacterium elephantis].
ACCESSION   WP_128108524
VERSION     WP_128108524.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium elephantis (Mycobacterium elephantis)
  ORGANISM  Mycolicibacterium elephantis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Mycolicibacterium elephantis"
                     /db_xref="taxon:81858"
     Protein         1..510
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52254
     Region          1..509
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mligipresh dgetrvaatp qtvgqllklg ysvvvesgag aassfadaay vdagaeiggt
       61 eqvlgadvil kvnaptdaei agvkdgatlv slispalhpe lleklsarri tvlamdavpr
      121 israqsldvl ssmaniagyr avveaahsfg rfftgqvtaa gkvppakvlv vgagvaglaa
      181 igaagslgav vkatdprpev adqvrslgge yvsiesaeae isatgyakem gedykareaa
      241 lyaelvpdvd iiittalipg kpapriitad mvaamkpgsv ivdmaaangg nvegtvkdqv
      301 vvtdnnvtii gytdlagrlp atasqlygtn lvnllklltp ekdgqltldf ddvvqrsmtv
      361 vrdgeitwpp ppvqvsaapa aapaaaveaq pakepmsnar rlgltfaaaa avfalialsp
      421 aalqvhltvf alaivigyyv ignvhhalht plmsvtnais giivvgallq ighgdvvitt
      481 lafvailias inifggfavt rrmlsmftrs
//
LOCUS       WP_128110325             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mycolicibacterium elephantis].
ACCESSION   WP_128110325
VERSION     WP_128110325.1
KEYWORDS    RefSeq.
SOURCE      Mycolicibacterium elephantis (Mycobacterium elephantis)
  ORGANISM  Mycolicibacterium elephantis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycolicibacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Mycolicibacterium elephantis"
                     /db_xref="taxon:81858"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34352
     Region          8..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtststvhdv iiigsgpagy taaiyaaraq lsplvfegtq fggalmttte venypgfrng
       61 itgpelmdem reqalrfgad lrmedveavs ldgpvktvtv gdethrarav ilamgaaarh
      121 lgvpgeeali gmgvstcatc dgfffrdedi ivvgggdsam eeaifltkfa rsvtlvhrrd
      181 efrasrimle raranekitf vtntevleie gspkvsgvrl rnkltgeesk lavtgvfvai
      241 ghdprselvr gqihldedgy vltegrttht slegvfaagd lvdrvyrqai taagsgcaaa
      301 idaerwlaei gsapsdeets tpa
//
LOCUS       WP_128112450             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Polynucleobacter necessarius].
ACCESSION   WP_128112450
VERSION     WP_128112450.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter necessarius
  ORGANISM  Polynucleobacter necessarius
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Polynucleobacter necessarius"
                     /db_xref="taxon:576610"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33751
     Region          5..317
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mttntpkhsk vlilgsgpag ytaavyaara nlnptlitgl aqggqlmttt dvenwpadad
       61 gvqgpelmdr flkhaerfnt eiifdhihta alkekpirlv gdsgtytcda liicigasaq
      121 yiglpseeaf mgrgvsgcat cdgffyrnqd vcvvgggnta veealyltgi akkvtvihrr
      181 dkfraepiln drlmakvaeg kvelklnstl devlgdetgv tgvrikkqdg stedlavtga
      241 fiaighkpnt elfvgqldms ngylkthsgl egnatatnip gvfaagdvqd hiyrqaitsa
      301 gtgcmaalda qryletle
//
LOCUS       WP_128112697             376 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Polynucleobacter necessarius].
ACCESSION   WP_128112697
VERSION     WP_128112697.1
KEYWORDS    RefSeq.
SOURCE      Polynucleobacter necessarius
  ORGANISM  Polynucleobacter necessarius
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Polynucleobacter.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Polynucleobacter necessarius"
                     /db_xref="taxon:576610"
     Protein         1..376
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39268
     Region          1..370
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,321,323)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,328..329,333,
                     336..337)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigvpletr pgearvaatp etvkkfigqg htvviqkdag lkasqpdsay eavgatigsa
       61 adafgaeivl kvrapepael kqiksgavll gmldpfdndm iaamaaqgvt afsleaaprt
      121 traqsmdvls sqaniagyka vmvaaneyqr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpaak eqieslgakf vdvpyetdee reiaqgvggy arpmpeawmk
      241 rqaalvaera qqadvvitta lipgrkppvl lhsdtvanmk pgsividlaa gkgdngsgnc
      301 pltqadkvvd vngvkivgyt nlasmvgada salysrnlld fmkliidkda klvipsdddi
      361 vtaclmcrdg qairkn
//
LOCUS       WP_128115078             339 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Brevundimonas diminuta].
ACCESSION   WP_128115078
VERSION     WP_128115078.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas diminuta
  ORGANISM  Brevundimonas diminuta
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Brevundimonas diminuta"
                     /db_xref="taxon:293"
     gene            1..339
                     /gene="trxB"
     Protein         1..339
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35935
     Region          13..318
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqakapart vrvaiigsgp agwtaaiyaa raslnpviia glqpggqlti ttdvenypgf
       61 aetiqgpwlm qqmqaqaehv gtevihdivt qadlsqrpfr ltldsgaeil aetviistga
      121 qakwlgldse aeyqgfgvsa catcdgffyr gkqvvvvggg ntaveealfl tnfaetvtvv
      181 hrrdefraek ilqdrlfahp kikviwdvav eevvgvvdgv arnvtgvrlk nvktgeisei
      241 padgvfiaig hapsselfkg qletnsggyl rvkpgtaata iegvwaagdv tddvyrqavt
      301 aagmgcmaal eaarflaeed hkaaqhpish keaekigaw
//
LOCUS       WP_128115927             377 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Brevundimonas diminuta].
ACCESSION   WP_128115927
VERSION     WP_128115927.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas diminuta
  ORGANISM  Brevundimonas diminuta
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Brevundimonas diminuta"
                     /db_xref="taxon:293"
     Protein         1..377
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38344
     Region          5..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,77,96,293,320,322)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,129..130,139..140,143..144,147..148,150..151,
                     153..158,160,162..164,167,190..191,283..284,327..328,332,
                     335..336)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,129,132,135,176..179,199..201,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(126..127,129,139,182..183,190,206..207,209..212)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(159..163,166,169,192,194)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mavaiavtre rregetrcav tpetvkklia lgatvsveag tglgsslpda dyaeagasvk
       61 pdlsaalaga dillkvrgpt aseisalkpg avvvclldaw rdkatlealr gagatafame
      121 fvpritraqv mdvlssqanl agyravieaa yaygkgfpmm mtaagtvaaa ktfvmgagva
      181 glqaiatarr lgavvtatdv rpaakeqves lgakfvaved eefkaaetag gyakamsaey
      241 qakqaeltaa hiikqdvvit talipgrpap klvtaahvas mkpgsviidl aveaggnveg
      301 skpnevvtta ngvkivgwsn mpgriaadas alyarnlvaf lglmikdgal avdleeeilk
      361 aavvthggav vhegvrg
//
LOCUS       WP_128124257             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Exiguobacterium sp. AM39-5BH].
ACCESSION   WP_128124257
VERSION     WP_128124257.1
KEYWORDS    RefSeq.
SOURCE      Exiguobacterium sp. AM39-5BH
  ORGANISM  Exiguobacterium sp. AM39-5BH
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillales
            Family XII. Incertae Sedis; Exiguobacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Exiguobacterium sp. AM39-5BH"
                     /db_xref="taxon:2292355"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34428
     Region          7..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteekiydvi iigagpagmt aalyasranl stlmiergip ggqmantedi enypgydsil
       61 gpdlsqkmfd hskafgaeya ygdvqsisde teykivhahn rdykaraiil asgaqykkig
      121 vpgeeelggr gvsycavcdg affkgknlfv igggdsavee gvfltrfadk vtivhrrdel
      181 raqkilqkra fdnpkidfiw nhtlkeikea dgkvggarlv stvdgtesdy eidgvfiyig
      241 mnpitgfvkd lgitneqgyi vtneametki pgifaagdvr dktlrqvvta tndgsiaaqn
      301 aqhyieglle tlheqna
//
LOCUS       WP_128136870             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Micromonospora].
ACCESSION   WP_128136870
VERSION     WP_128136870.1
KEYWORDS    RefSeq.
SOURCE      Micromonospora
  ORGANISM  Micromonospora
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Micromonosporales; Micromonosporaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Micromonospora"
                     /db_xref="taxon:1873"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33800
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdevrnliii gsgpagytaa vyaaranlkp lviegvqsgg almttteven fpgfadgilg
       61 pelmdnmrkq aerfgaeflt ddvtrvelkd tgeigsdavs tvwvgetayr aravilstgs
      121 awrplgvpge qeylghgvss catcdgfffr nqhivvvggg dsameeasfl trfaesvtil
      181 hrrdsfrask imadralsne kikvewntvv eeilgddgkv ngvrvrnvht geskvldvtg
      241 vfvaighdpr selfrgqvel ddegyvkvqa pstrtsvpgv faagdvvdht yrqaitaagt
      301 gcaaaldaer fiatiqg
//
LOCUS       WP_128141683             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium lividum].
ACCESSION   WP_128141683
VERSION     WP_128141683.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium lividum
  ORGANISM  Janthinobacterium lividum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Janthinobacterium lividum"
                     /db_xref="taxon:29581"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38731
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,290,316,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,123..124,133..134,137..138,141..142,144..145,
                     147..152,154,156..158,161,184..185,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(118..119,123,126,129,170..173,193..195,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,123,133,176..177,184,200..201,203..206)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(153..157,160,163,186,188)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mrigipaetr pgetrvaatp etvkklaskh qvvvqsgagl qasipddaya aagaqigtaq
       61 eaygcaivlk vrapdadera lmasgtvlig mlnpfdadni aamataglsa faleavprit
      121 raqsmdvlss qaniagykav lvaantyqrf mpmlmtaagt vkaarvlimg vgvaglqaia
      181 takrlgavie asdvrppvke qveslgakfl dvpfltdeek eiakgsggya rampadwmrr
      241 qaelvherak ladiiittal ipgraapvli seetvkamkp gsvivdlave qggncplsel
      301 gktvvkhgvy ivgepnlatl vaadasalya rnvldflkli idkddqllid redeiikasl
      361 vcagndilrk
//
LOCUS       WP_128150996             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paenirhodobacter ferrireducens].
ACCESSION   WP_128150996
VERSION     WP_128150996.1
KEYWORDS    RefSeq.
SOURCE      Paenirhodobacter ferrireducens
  ORGANISM  Paenirhodobacter ferrireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Paenirhodobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Paenirhodobacter ferrireducens"
                     /db_xref="taxon:1215032"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55845
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapretf egesrvamtp dsalqlqklg htcfieagag daagfsdeay rkagvtvipt
       61 vaelfaevdf ivkvrplvtd eehgwlrkgq tvisffypgq hpdrlelake tganfiamdm
      121 vprisraqkm dalssmania gyravmeaan nfgrfftgqv taagkvppak vlivgagvag
      181 laaigtttal gaityafdvr pevaeqiesm gaefvyldfe ektqdgaaag gyaapsspef
      241 reaqlkkfre lapdmdivit talipgrdap klwladmvaa mkrgsvvvdl aaerggncdl
      301 tvpgekivse ngvtiigynd fpsrmatqas qlyatnirhm itdltpgkdg vivhnmeddv
      361 irgatvafeg avtfpppppk ikaiaahkpk ekakeptpee rkaaekaafr katrqqvtll
      421 avgtallllv gtvapasfms hfvvfalscf vgfqviwnvs hslhtplmav tnaisgivil
      481 gallqvgsgs wlvvvlaals vliatvnivg gflvtrrmla mfqks
//
LOCUS       WP_128147481             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenirhodobacter ferrireducens].
ACCESSION   WP_128147481
VERSION     WP_128147481.1
KEYWORDS    RefSeq.
SOURCE      Paenirhodobacter ferrireducens
  ORGANISM  Paenirhodobacter ferrireducens
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Paenirhodobacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenirhodobacter ferrireducens"
                     /db_xref="taxon:1215032"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33523
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mgetkktrvl iigsgpagyt aavysaraml npvlvqgiqp ggqltittev enwpgrtave
       61 gpelmvqmee hartmgteii sdtitslnlg drpfvalgds gttyvadavi latgaqarwl
      121 glpseetfkg fgvsacatcd gffyrgkevv vigggntave ealfltnfat kvtvihrrds
      181 fraekimqdr lfrnpkievi wdsvpeeilg detplgvtgv rirnvkteae tvvpcdgffv
      241 aighapasel vkdqlrlhgg gyvwvqpgtt rtsiegvfaa gdltdhtyrq avtsagmgcm
      301 aaldaerwla eqe
//
LOCUS       WP_128152653             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Apibacter raozihei].
ACCESSION   WP_128152653
VERSION     WP_128152653.1
KEYWORDS    RefSeq.
SOURCE      Apibacter raozihei
  ORGANISM  Apibacter raozihei
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Apibacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Apibacter raozihei"
                     /db_xref="taxon:2500547"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34010
     Region          11..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseninilqt viigsgpagf taaiyaarae mnpvlisgme lggqltttte venfpgypeg
       61 itgpemmiql qnqaekfgtk vivdkvtevv fgsnskefht iktssgneyq thtiiistga
      121 sakylgkefe dtyrgggvsa catcdgffyr grnvvvvggg dtaaeeatyl akicktvymv
      181 vrkdylkask imqerveats nivlmynhev tnlkgennlv sqavvidnlt qeekildvdg
      241 lfiaighspn tdifkgkldm detgyltvkp fttetniagv faagdvadkr yrqaitaags
      301 gcmaaldaek yltsigh
//
LOCUS       WP_128154382             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenirhodobacter huangdaonensis].
ACCESSION   WP_128154382
VERSION     WP_128154382.1
KEYWORDS    RefSeq.
SOURCE      Paenirhodobacter huangdaonensis
  ORGANISM  Paenirhodobacter huangdaonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Paenirhodobacter.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paenirhodobacter huangdaonensis"
                     /db_xref="taxon:2501515"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33476
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mgetkktrvl iigsgpagyt aavysaraml npvlvqgiqp ggqltittev enwpgrtave
       61 gpelmvqmee haramgteii sdtitslnlg drpfvalgds gttyvadavi latgaqarwi
      121 glpseekfkg fgvsacatcd gffyrgkevv vigggntave ealfltnfat kvtvihrrds
      181 fraekimqdr lfrnpkievi wdsvpeeilg teaplgvtgv rirnvkteae tvvpcdgffv
      241 aighapasel vkdqlrlhgg gyvwvqpgtt rtsiegvfaa gdltdhtyrq avtsagmgcm
      301 aaldaerwla eqe
//
LOCUS       WP_128156392             525 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paenirhodobacter huangdaonensis].
ACCESSION   WP_128156392
VERSION     WP_128156392.1
KEYWORDS    RefSeq.
SOURCE      Paenirhodobacter huangdaonensis
  ORGANISM  Paenirhodobacter huangdaonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Paenirhodobacter.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Paenirhodobacter huangdaonensis"
                     /db_xref="taxon:2501515"
     Protein         1..525
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55884
     Region          1..524
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapretf egesrvamtp dsalqlqklg hscfieagag daagfsdeay rkagvtvipt
       61 vaelfaevdf ivkvrplvtd eehgwlrkgq tvisffypgq hpdrlelakk tganfiamdm
      121 vprisraqkm dalssmania gyravmeaan nfgrfftgqv taagkvppak vlivgagvag
      181 laaigtttal gaityafdvr pevaeqiesm gaefvyldfe ektqdgasag gyaapsspef
      241 reaqlkkfre lapemdivit talipgrdap klwladmvaa mkrgsvvvdl aaerggncel
      301 tvpgekivse ngvtiigynd fpsrmatqas qlyatnirhm itdltpgkdg vivhnmeddv
      361 irgatvafeg avtfpppppk ikaiaahkpk ekakeptpee rkaaekaafr katrqqvall
      421 avgtvllllv gtvapasfms hfvvfalscf vgfqviwnvs halhtplmav tnaisgivil
      481 gallqigsgs wlvvilaals vliatvnivg gflvtrrmla mfqks
//
LOCUS       WP_128162721             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp.].
ACCESSION   WP_128162721
VERSION     WP_128162721.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp.
  ORGANISM  Mesorhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mesorhizobium sp."
                     /db_xref="taxon:1871066"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43821
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsripde efakagaaig
       61 kaadaseadv vlkvrrptda elkgyksgaa viaimdpygn daalaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkaakel aikrddelvk
      361 atmltdggkv vhpafakave aprtepaaip attmvadasa kpavkktaak kpvaakspss
      421 kskgta
//
LOCUS       WP_128168377             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp.].
ACCESSION   WP_128168377
VERSION     WP_128168377.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp.
  ORGANISM  Mesorhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mesorhizobium sp."
                     /db_xref="taxon:1871066"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43369
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripde efakagaaig
       61 kagdvakadv vlkvrrpdea elkayrpgsa viaiidpygn daavdalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaara fvmgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafle tlvdktdktl ainrddelvk
      361 atmltdggqv vhpafagkpa vmiasaepak paaakdpalp kkaaasrkaa apkspanksk
      421 gia
//
LOCUS       WP_128165711             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.].
ACCESSION   WP_128165711
VERSION     WP_128165711.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp.
  ORGANISM  Mesorhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp."
                     /db_xref="taxon:1871066"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34441
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdiv ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylanlak svtvihrrsd
      181 fraerilrer llkkdnvrvi wdtvvdeitg qpgkaplpps veglklrnva tgevsrlkvd
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_128172910             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp.].
ACCESSION   WP_128172910
VERSION     WP_128172910.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp.
  ORGANISM  Mesorhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mesorhizobium sp."
                     /db_xref="taxon:1871066"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43296
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripdv efakagaaig
       61 kagdvakadv vlkvrrpdea elkayrpgsa viaiidpygn daavdalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fvmgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttvng vkivghinvp grvaasasll yarnlfafle tlvdkttktl ainrddelak
      361 atmltdggqv vhpafagkpa vmiasaepak paaaknpalp kkaaasrkaa apkspanksk
      421 gia
//
LOCUS       WP_128182386             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp.].
ACCESSION   WP_128182386
VERSION     WP_128182386.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp.
  ORGANISM  Mesorhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mesorhizobium sp."
                     /db_xref="taxon:1871066"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43375
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripde efakagavig
       61 kagdvakadv vlkvrrpdet elkayrpgta viaiidpygn daavdalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqaaidaaae ydralpmmmt aagtvpaaka fvmgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafve tlvdktektl ainrddelvk
      361 atmltdggqv vhpafagkpa vmiasaepae paaaknpals kkaaasrkaa apkspanksk
      421 gia
//
LOCUS       WP_128186461             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.].
ACCESSION   WP_128186461
VERSION     WP_128186461.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp.
  ORGANISM  Mesorhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp."
                     /db_xref="taxon:1871066"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34473
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtskhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdvi ndiitevdln vrpfrakgds gatytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilser lfkkdnvrvv wdtvvdeitg qsgkmplpps veglklrnlv tgqemhltvd
      241 gvfvaighap avelfagklk qkpngylwta pdstctdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_128183184             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenirhodobacter populi].
ACCESSION   WP_128183184
VERSION     WP_128183184.1
KEYWORDS    RefSeq.
SOURCE      Paenirhodobacter populi
  ORGANISM  Paenirhodobacter populi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Paenirhodobacter.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenirhodobacter populi"
                     /db_xref="taxon:2306993"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33755
     Region          7..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetkktrvl iigsgpagyt aavysaraml npvlvqgmqp ggqltittev enwpgrtevq
       61 gpelmvqmee haramgaevv fdtitdldls qrpfvahgds gteyvadavi latgaqarwl
      121 gleseetfkg fgvsacatcd gffyrgkevv vigggntave ealfltnfas kvtvihrreg
      181 fraekilqdr lfknpkvevl wnhtveeilg eetphlsvsg vrvrntvtga tsvvpchgff
      241 vaighapase lvkdqlelhh ggyvkvepgt thtsvpgvfa agdltdhtyr qaitsagmgc
      301 maaldaerwl aeqda
//
LOCUS       WP_128186907             529 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paenirhodobacter populi].
ACCESSION   WP_128186907
VERSION     WP_128186907.1
KEYWORDS    RefSeq.
SOURCE      Paenirhodobacter populi
  ORGANISM  Paenirhodobacter populi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Paenirhodobacter.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Paenirhodobacter populi"
                     /db_xref="taxon:2306993"
     Protein         1..529
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56066
     Region          1..528
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeiy egearvaltp dsavqlqklg htcfiqsgag mlagftdday qkagvtvieg
       61 aqalfeavdf vvkvrpptea evawlkkgqt lisffypaqn kelleeaqkt ganviamdmv
      121 prisraqkmd alssmanigg yravieaann fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigastslg aityafdvrp evaeqitsmg aefvyldfag eqqdgaatgg yatpsspefr
      241 eaqlkkfrel apdmdivist alipgrdapv lwtkdmvesm krgsvivdla aerggncelt
      301 vkdqkivtdn gvtiigytdl psrmatqasq lystnvrqmv gdltpakdgv inynmeddvi
      361 rtatvthegt itfpppplki qaiaaqkpke kpkeltpeek kaaekaayrk atvrqvsllv
      421 vgavvlfaig lfapasfmsh lvvfalacfv gfqviwgvsp slhtplmsvt navsgiiilg
      481 sllqigaggt gfggfviill svlailiasi nivggflvtr rmlamfqrs
//
LOCUS       WP_128190858             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Salmonella enterica].
ACCESSION   WP_128190858
VERSION     WP_128190858.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53659
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 marktlrarr ffslifpfff itsvyaeqtp esaktvtvea knemfapqhp dqyqswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqqeged gyfhgkwarg gpeivndlgc adchntasdd faqgkpaltl
      181 srpyaerame aigkpfdkag rfdqqsmvcg qchveyyfdg knkavkfpwd egmkvenmeq
      241 yydtiafsdw tsslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvha hfeakaawda
      361 gatdaemkpi lndirhaqwr wdlaiashgi hmhapeeglr mlgsamdkaa dartklarll
      421 atkgitheip lpdistkeka qkaiglnmqq inaekqdflk tvvpqwedqa rkngllsq
//
LOCUS       WP_128189646             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Agrococcus sediminis].
ACCESSION   WP_128189646
VERSION     WP_128189646.1
KEYWORDS    RefSeq.
SOURCE      Agrococcus sediminis
  ORGANISM  Agrococcus sediminis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Agrococcus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Agrococcus sediminis"
                     /db_xref="taxon:2599924"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34460
     Region          2..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhdviiigsg pagytaaiya aranlkpivl assvemggdl mtttevenfp gfpegiqgpd
       61 lmfamqqqae rfgadvrmqd ateleldgev krvhvgdevl etralifatg sayrklgveg
      121 eerlsghgvs wcatcdgfff kqkqlivvgg gdsameeanf ltkfadkvti vhrsehfras
      181 evmlersran ekidfimnav veeivgtesn gteqvssvtl rdttsghtws mpidgvfvai
      241 gsdprthlvh gkldlttegt iavdgrssrt svegvfaagd vidptyrqav taagsgtvaa
      301 ldaehylaah avpalvtspe eaal
//
LOCUS       WP_128194143             329 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium sufflavum].
ACCESSION   WP_128194143
VERSION     WP_128194143.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sufflavum
  ORGANISM  Flavobacterium sufflavum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Flavobacterium sufflavum"
                     /db_xref="taxon:1921138"
     gene            1..329
                     /gene="trxB"
     Protein         1..329
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35642
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaaran mhpilyqgmq pggqltttne venfpgyvdg
       61 vtgpemmvql qkqaerfgad irdgwatkvd fsgdvhkvwi ndtielhcet viistgasak
      121 ylglpseqhy lqmgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rsekfraski meervrrten ieillnhdtv evigdgqvve aikvlnkttn etydiqatgf
      241 fvaighkpnt difkdyltld etgyiintpg taktnvdgvf vagdaadhvy rqaitaagtg
      301 cmaaldaery lagkevvenv ftdvdssks
//
LOCUS       WP_128197912             527 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rubrivivax
            albus].
ACCESSION   WP_128197912
VERSION     WP_128197912.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax albus
  ORGANISM  Rubrivivax albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Rubrivivax albus"
                     /db_xref="taxon:2499835"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54641
     Region          3..527
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mplrigvple ttpgekrvat vpdvvaklik lgfsvsvqss agdaancddd syravgaevv
       61 dsaealwags divfkvrpps mdevalmreg glligfvwpa qnpelmqalq akkatvlaid
      121 alprqlsraq kmdaltsqag vsgyraviea anafgrffng qitaagkvpp akvfiagagv
      181 aglaaigtaa nlgaivrand traevadqvv slggefvkvd yeeegsgggg yakvmsegfq
      241 aaqrqmyaeq vkdadivitt alipgkpapk litaemvktm rpgsvivdma aeqggncelt
      301 vpgeaavrhg vtiigytdla srlakqsstl yatnllrlte dlckakdgtv dvnfddqair
      361 gltvikdgel twpappiqmp aappkpkaaa apaakahghg pgepmsaksl aivfgvgaal
      421 falvgafapa sflahftvfv lacfigymvi wnvtpslhtp lmsvtnaiss iiaigaliqv
      481 appligiegd rpsglilgls vlalvltain mfggfavtrr mlamfrk
//
LOCUS       WP_128199703             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rubrivivax albus].
ACCESSION   WP_128199703
VERSION     WP_128199703.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax albus
  ORGANISM  Rubrivivax albus
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rubrivivax albus"
                     /db_xref="taxon:2499835"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33329
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msttpharvl ilgsgpagwt aavyaaranl qptlitglat ggqlmtttev dnwpadvagv
       61 mgpdlmqrfq qhaerfntnv vydhinavdl skrpftltgd sgsytcdtlv iatgasakyl
      121 glpseeafmg kgvsgcatcd gffyrdqavc vvgggntave ealylsnias evhlihrrdk
      181 fraeaimvdk vmakveagki klhlfhtlde vlgdasgvtg vrikstqdgg tsdlavkgcf
      241 iaighqpntd ifkgqlemkd gyivtktgld gfatmtsvpg vfaagdvqdh vyrqaitsag
      301 tgcmaaldaq rfleqg
//
LOCUS       WP_128200758             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128200758
VERSION     WP_128200758.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33410
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvknavl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemta vqrvskkdsh fvilaedgkt feaksviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn ndkiefltpy vveeikgdas gvsslsiknt atnetrelvv pgffifvgyd
      241 vnnavlkqed nsmlckcdey gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgtta
      301 alsvisyleh h
//
LOCUS       WP_128211226             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium manihotivorum].
ACCESSION   WP_128211226
VERSION     WP_128211226.1
KEYWORDS    RefSeq.
SOURCE      Clostridium manihotivorum
  ORGANISM  Clostridium manihotivorum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Clostridium manihotivorum"
                     /db_xref="taxon:2320868"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34036
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maksekiidl miigggpagl taaiyasrak lnmvlledai vggqvrtsys ienypgfksi
       61 eggkladlmq eqalelgati defdlvervd fsdkekivet tsyiykpkav iiatgatpkk
      121 ipvpneekfs gkgihycavc dgamyegkvi gvvgggnsal eealfltkfa skvvmirryd
      181 yfkgeaatle evlhhpkiev mynwdlvdvs gekfmesaki kntntgeeke iqmdaifgyi
      241 gtepktghfk dyvnltpqgy iladestrtn ikgvyaagdv rekqfrqitt avadgtiaal
      301 daekyileak rg
//
LOCUS       WP_128217424             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Microbacterium enclense].
ACCESSION   WP_128217424
VERSION     WP_128217424.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium enclense
  ORGANISM  Microbacterium enclense
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Microbacterium.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Microbacterium enclense"
                     /db_xref="taxon:993073"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34640
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrhviiigsg pagytaaiya aranleplvv assveaggdl mtttdvenfp gfpdgilgpd
       61 lmakmqaqae rfgaevlydd vvsleldgpv ktvtlgsgkv heaasiiyat gsayrklgle
      121 geerlsgrgv swcatcdgff frertiavvg ggdsameeas fltkfaskvy iihrkdtlra
      181 skimqerafa npkiefvwns evadilgdea vngvrlrstv dgserdlpld glfvaigndp
      241 rthlvhdklq lteqgtiwvd grssrtsvdg vfaagdvidp tyrqaitaag sgtvaaldve
      301 hflaargeag epavaespid glpdpavv
//
LOCUS       WP_128220486             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Akkermansia muciniphila].
ACCESSION   WP_128220486
VERSION     WP_128220486.1
KEYWORDS    RefSeq.
SOURCE      Akkermansia muciniphila
  ORGANISM  Akkermansia muciniphila
            Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
            Verrucomicrobiales; Akkermansiaceae; Akkermansia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Akkermansia muciniphila"
                     /db_xref="taxon:239935"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33010
     Region          5..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseqviiiga gcagytaaiy taranlspll itgsqiggql ttttevenfp gfpdgvmgpd
       61 lmflmqqqae kfgtrfayed vksvvrdeat glftvktsgq nyetrsiiva tgasarylgi
      121 pgeeglvghg ltacatcdga fyrdvpvcvv gggdsaceea mfltrfasrv ylihrrdtlr
      181 askimaertl snekifpmwn stivsyktdd kgelgavmlk dvvegdetel pvkcvfmaig
      241 htpntsflgd lvdrddagyi irktgmmatr tpglfaagdv adphyrqais sagmgcsaai
      301 eaeryllgl
//
LOCUS       WP_128221941             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Nocardioides yefusunii].
ACCESSION   WP_128221941
VERSION     WP_128221941.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides yefusunii
  ORGANISM  Nocardioides yefusunii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Nocardioides yefusunii"
                     /db_xref="taxon:2500546"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52669
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigipretk pgeslvaata ktaeqlqklg ydvvvesgag aladqsdeaf taagitvatg
       61 devwasdvvv kvnapndeei grlrreatvv simaparspe liekfqaagv talamdavpr
      121 israqsmdvl ssmanvagyr avieaahefg rmftgqvtaa gktaparvfv vgagvaglaa
      181 igaassmgai vrafdvrpev aeqvesmgae fvrvemeqev stdgyakemt aeqeaataam
      241 ydeearnadi vittalipgr papklisaet iagmkpgsvi vdmaaanggn aaatvtdqrv
      301 vtdngvvvlg ytdlagrlaa qtsqlygtni vnlfklltpa kdgvltldhg dvvqrgitvt
      361 lsgesmwppp pvqvsaapka aeapapvvke ekkpvdpkvk lyaaaagavl fgaaamfmsy
      421 glltqltvlm lavfvgyyvi snvahalhtp lmaetnavsg iilvggilqv gsdniavtal
      481 svvailvasi nifggflvtv rmlemfrkd
//
LOCUS       WP_128222036             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Nocardioides yefusunii].
ACCESSION   WP_128222036
VERSION     WP_128222036.1
KEYWORDS    RefSeq.
SOURCE      Nocardioides yefusunii
  ORGANISM  Nocardioides yefusunii
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Propionibacteriales; Nocardioidaceae; Nocardioides.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Nocardioides yefusunii"
                     /db_xref="taxon:2500546"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33988
     Region          9..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdiqprnvi iigsgpsgyt aavyaaranl eplvfegsvt aggalmntte venfpgfrdg
       61 imgpalmdem raqaerfgae lvtddvvevd ltgdikvvkt adathyartv ilatgsayrk
      121 lglpredels grgvswcatc dgfffrdqti avvgggdsav eeatfltrfa kkvylihrrd
      181 elraskimvd raeadpklei iwnaevaeiq gedklsgvvl ndtvtgekrd laitglfiai
      241 ghdprselfk gqvelddegf vkvaspstat nltgvfasgd lvdhtyqqai taagtgctaa
      301 ldaerhiaml dqaaaeaaan
//
LOCUS       WP_128226817             534 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rubrivivax
            rivuli].
ACCESSION   WP_128226817
VERSION     WP_128226817.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax rivuli
  ORGANISM  Rubrivivax rivuli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Rubrivivax rivuli"
                     /db_xref="taxon:1862385"
     Protein         1..534
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55311
     Region          3..534
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 malligvpqe taagekrvat vpevveklik lgfqvavqsg agdaancsde ayrtagaevl
       61 pdaatlwara divfkvraps peevglmrpg gmligfvwpa qnpelmqqla akgatvlaid
      121 alprqlsraq kmdaltsqag vsgyraviea anafgrffng qitaagkvpp akvfiagagv
      181 aglaaigtaa nlgaivrand traevadqvv slggefvkvd yeeegsgggg yakvmsegfq
      241 aaqremyakq arevdiiitt alipgkpapk litaemvatm kpgsvivdma aeqggncelt
      301 vpgqavvrhg vtivgytdla srlakqsstl yatnllrlte elcktkdgqv nvnfeddair
      361 gltvikegav twpapppklp pappkakaea apaakagask gghghgsvep msaktlaivf
      421 avgavlfwfv gayapasflq hftvfvlacf vgymvvwnvt pslhtplmsv tnaissiiai
      481 galvqvappl daagaadrpn tlilvcavva lvltainmfg gfavtrrmla mfrk
//
LOCUS       WP_128233329             529 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paenirhodobacter populi].
ACCESSION   WP_128233329
VERSION     WP_128233329.1
KEYWORDS    RefSeq.
SOURCE      Paenirhodobacter populi
  ORGANISM  Paenirhodobacter populi
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Rhodobacter group; Paenirhodobacter.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Paenirhodobacter populi"
                     /db_xref="taxon:2306993"
     Protein         1..529
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55992
     Region          1..528
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigapkeiy egearvaltp dsavqlqklg htcfiqsgag mlagftdday qkagvtvieg
       61 aqalfeavdf vvkvrpptea evawlkkgqt lisffypaqn kelleeaqkt ganviamdmv
      121 prisraqkmd alssmanigg yravieaann fgrfftgqvt aagkvppakv lvigagvagl
      181 aaigastslg aityafdvrp evaeqitsmg aefvyldfag eqqdgaatgg yatpsspefr
      241 eaqlkkfrel apdmdivist alipgrdapv lwtkdmvaam krgsvivdla aerggncelt
      301 vkdqkivtdn gvtiigytdl psrmatqasq lystnvrqmv gdltpakdgv inynmeddvi
      361 rtatvthegt itfpppplki qaiaaqkpke kpkeltpeek kaaekaayrk atvrqvsllv
      421 vgavvlfaig lfapasfmsh lvvfalacfv gfqviwgvsp slhtplmsvt navsgiiilg
      481 sllqigaggt gfggfviill svlailiasi nivggflvtr rmlamfqrs
//
LOCUS       WP_128228777             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rubrivivax rivuli].
ACCESSION   WP_128228777
VERSION     WP_128228777.1
KEYWORDS    RefSeq.
SOURCE      Rubrivivax rivuli
  ORGANISM  Rubrivivax rivuli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Rubrivivax.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Rubrivivax rivuli"
                     /db_xref="taxon:1862385"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33666
     Region          10..318
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpstharv lilgsgpagy taalyaaran lepmlitgia qggqlmttte vdnwpadvag
       61 vqgpelmerf lkhaerfntk ivfdhinavd fsqrpfkltg dsgtytcdal viatgasaky
      121 lglesesafm gkgvsgcatc dgffyrgdtv cvvgggntav eealylsnia dkvhlihrrd
      181 kfraeaimvd kvmakvaagk ielhlwntld avlgddsgvt gvrlkstqdg stkevavkgc
      241 fiaighqpnt difkgqlemk dgyivtktgl dgmatmtsvp gvfaagdvqd hiyrqaitsa
      301 gtgcmaalda qrfleaqe
//
LOCUS       WP_128240643             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp.].
ACCESSION   WP_128240643
VERSION     WP_128240643.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp.
  ORGANISM  Mesorhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mesorhizobium sp."
                     /db_xref="taxon:1871066"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43820
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevilekg aglgsripdd efakagaaig
       61 kaadaskadv vlkvrrptda elkgyksgaa viaimdpygn daalaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkaakel aikrddelvk
      361 atmltdggkv vhpafakave aprtepaaip attmvadasa kpavkktaak kpvaakspss
      421 kskgta
//
LOCUS       WP_128242326             427 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_128242326
VERSION     WP_128242326.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44048
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripde efakagaaig
       61 kagdvakadv vlkvrrpsea elkayrrgta viaimdpygn daavdalara svtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fraaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttang vkivghlnvp grvaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggqv vhpafvrveq apcveppaip aktmvadasa kpaaakkaap kkpvapmspp
      421 skskgta
//
LOCUS       WP_128243264             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_128243264
VERSION     WP_128243264.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34533
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdvi ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 frserilser lfkkdnvrvi wdtvvdeitg qsgkmplpps veglklrnvv tgqemhltvd
      241 gvfvaighap avelfagklk qkpngylwta pdstctdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_128244516             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp.].
ACCESSION   WP_128244516
VERSION     WP_128244516.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp.
  ORGANISM  Mesorhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Mesorhizobium sp."
                     /db_xref="taxon:1871066"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43296
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlag lgfdvivesg agtasripdv efakagaaig
       61 kagdvakadv vlkvrrpdea elkayrpgsa viaiidpygn daavdalara gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fvmgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemsreyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttvng vkivghinvp grvaasasll yarnlfafle tlvdkttktl ainrddelak
      361 atmltdggqv vhpafagkpa vmiasaepaq paaaknpalp kkaaasrkaa apkspanksk
      421 gia
//
LOCUS       WP_128249200             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aequorivita ciconiae].
ACCESSION   WP_128249200
VERSION     WP_128249200.1
KEYWORDS    RefSeq.
SOURCE      Aequorivita ciconiae
  ORGANISM  Aequorivita ciconiae
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aequorivita.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Aequorivita ciconiae"
                     /db_xref="taxon:2494375"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34314
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msesierikc liigsgpagy taaiyaarad lkpvlytgme pggqltttte vdnfpgypeg
       61 idgptmmvql qqqaerfgtq vrigmvteve lsdkvggihk vtvdnttkle aetiiistga
      121 takylglpse qrlrgggvsa cavcdgffyk nqevaivgag dtaaeeatyl anlcskvtml
      181 vrkdymrask amqhrvnntk nlevhyntev devlgdqvve girmvnnqtg ekkeievtgl
      241 fiaighkpnt eifkgqldmd etgylitkgk stktnkpgvf asgdvqdsey rqavtaagtg
      301 cmaaldaery latieteee
//
LOCUS       WP_128254530             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Falsirhodobacter deserti].
ACCESSION   WP_128254530
VERSION     WP_128254530.1
KEYWORDS    RefSeq.
SOURCE      Falsirhodobacter deserti
  ORGANISM  Falsirhodobacter deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Falsirhodobacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Falsirhodobacter deserti"
                     /db_xref="taxon:1365611"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33770
     Region          8..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maetrhskvl iigsgpagyt aavysaraml kpilvqglqp ggqltittev enwpgdthvq
       61 gpdlmvrmee haramgaeiv tdyitsldls vrpfvahads gttftadavi latgaqarwl
      121 glpseekfkg fgvsacatcd gffyrgkevv vigggntave ealfltnfas kvtlihrrdt
      181 lraekilqdr lfahpkvema whsvveevlg tegplgvtgv rvkdmrdgse rvipcdgffv
      241 aightpasel vkdqlelhsd gygkveaggt rtsvpgvfaa gdltdhvyrq aitsagmgcm
      301 aaldaerwla gidsahf
//
LOCUS       WP_128255173             386 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Falsirhodobacter deserti].
ACCESSION   WP_128255173
VERSION     WP_128255173.1
KEYWORDS    RefSeq.
SOURCE      Falsirhodobacter deserti
  ORGANISM  Falsirhodobacter deserti
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Falsirhodobacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Falsirhodobacter deserti"
                     /db_xref="taxon:1365611"
     Protein         <1..386
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          <1..385
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 agyravieag nnfgrfftgq vtaagkvppa kvlvvgagva glaaigtsts lgaitlafdv
       61 rpevseqies mgaefvfldf eeqqvdgaat ggyaapsspe freaqlkkfr elapevdivi
      121 ttalipgrpa pklwtedmva amkpgsviid laaerggncd ltkpdekfvt dngvtivgyt
      181 dfpsrmatqs stlysnnirh mltdltpkkd gvidhnmedd virtatathe gaitfppppl
      241 kvqaiaaqkp rekvkepthe ekraaevakf kqqtktqvgl lvagtvllll vgsvapasfm
      301 ahfvvfalsc figfqviwav shslhtplma vtnavsgiii lgslvqvgag gflvvllsfi
      361 ailiatiniv ggflvtrrml gmfqks
//
LOCUS       WP_128256312             417 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp.].
ACCESSION   WP_128256312
VERSION     WP_128256312.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp.
  ORGANISM  Mesorhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Mesorhizobium sp."
                     /db_xref="taxon:1871066"
     Protein         1..417
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43004
     Region          3..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgmmvfvake qnnceprvaa spetvkrlag lgfdvivekg aglgsripdq dfaavgaaig
       61 katdaskadv vlkvrrptda elkgyksgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgkvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkttktl aikrddelvk
      361 atmltdggrv vhpnfakaae eprtepaaip attmvadaad akpaakkkaa akpkgta
//
LOCUS       WP_128258347             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.].
ACCESSION   WP_128258347
VERSION     WP_128258347.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp.
  ORGANISM  Mesorhizobium sp.
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp."
                     /db_xref="taxon:1871066"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34354
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmsqmla qaehvgtdii ndiitevdln vrpfratgds gtvytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrsd
      181 fraerilrer llakdnvrvi wdtvvdeitg rpgkaplpps vegltlrnvl tgqesklpvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_128264079             321 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Bradyrhizobium].
ACCESSION   WP_128264079
VERSION     WP_128264079.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34153
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msapvhakvv iigsgpagyt aaiyaaraml epiliqgiqp ggqltittdv enypgfadvi
       61 qgpwlmeqme kqavhvgtki vsdlvtklet aqrpfrltcd sgdvylaetv ilatgaqarw
      121 lglpseakfq gggvsacatc dgffyrgkev ivvgggntav eealyltnha sqvtivhrrd
      181 hfraerilqe rlfkhpkikv iwdaavdeic gtenpnkvth vrlknvktga ltdvkadgif
      241 iaighapate lvkdqvklkp sgyievapns tatsmpglfa agdvadetyr qavtaaglgc
      301 maaleaerfl alraseraaa e
//
LOCUS       WP_128264160             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium yuanmingense].
ACCESSION   WP_128264160
VERSION     WP_128264160.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium yuanmingense
  ORGANISM  Bradyrhizobium yuanmingense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium yuanmingense"
                     /db_xref="taxon:108015"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39184
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygndaa lktmadagia afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa dmvksmkpgs vlvdlaverg gnvegakpge
      301 vvnvdgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpka
//
LOCUS       WP_128272593             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas caviae].
ACCESSION   WP_128272593
VERSION     WP_128272593.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53092
     Region          29..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsydklf rpglaalllt allgagslaq addsapkgki earselfakd hadqftswkg
       61 tsesrertda laedpqmvvl wggyafakdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eeyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfdqtcrnch tqskemlqgv vkqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaemk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llaakgishe iaipdisske kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_128273365             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M4B.F.Ca.ET.089.01.1.1].
ACCESSION   WP_128273365
VERSION     WP_128273365.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M4B.F.Ca.ET.089.01.1.1
  ORGANISM  Mesorhizobium sp. M4B.F.Ca.ET.089.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mesorhizobium sp. M4B.F.Ca.ET.089.01.1.1"
                     /db_xref="taxon:2496662"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44062
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneqrvaa spdtvkrlag lgfevvvekg agtgsripde efakagaaig
       61 kaadaskadv vlkvrrptda elkgykqgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 agkvvttang vkivghlnvp grvaasasll yaknlfafle tlvdkenktl aikrddelvk
      361 atmltdagqv vhpnfakadq qprvepaavp attlvaease kktapkktad kktatsksaa
      421 kpkgia
//
LOCUS       WP_128273432             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Mesorhizobium].
ACCESSION   WP_128273432
VERSION     WP_128273432.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium
  ORGANISM  Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium"
                     /db_xref="taxon:68287"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34441
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdiv ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlak svtvihrrgd
      181 fraerilrer llkkenvrvi wdtvvdeitg qpgkaplpps veglalrnva tgevtrlkvd
      241 gvfvaighap avelfvgklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_128281854             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bacillus hominis].
ACCESSION   WP_128281854
VERSION     WP_128281854.1
KEYWORDS    RefSeq.
SOURCE      Bacillus hominis
  ORGANISM  Bacillus hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Bacillus hominis"
                     /db_xref="taxon:2817478"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34599
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseekiydvi iigagpagmt aavytsranl stlmlergip ggqmantedv enypgyesil
       61 gpdlsnkmfe hakkfgaeya ygdvkkiidg keyktiiagk keykaraiiv asgaeykkig
      121 vpgetelggr gvsycavcdg affkgkelvv igggdsavee gvfltrfask vtivhrrdtl
      181 raqkilqdra fqnekvdfiw nhtikeinda ngkvgsvtlv dvnsgeeqev ktdgvfiyig
      241 mlplskpfve lgitnengyf etnermetkv pgifaagdvr ekmlrqivta tgdgsiaaqs
      301 aqhyieelve elktvtek
//
LOCUS       WP_128288564             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M7A.F.Ca.MR.176.00.0.0].
ACCESSION   WP_128288564
VERSION     WP_128288564.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.MR.176.00.0.0
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.MR.176.00.0.0
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. M7A.F.Ca.MR.176.00.0.0"
                     /db_xref="taxon:2496776"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43443
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglnsrivda dyasagaaig
       61 kasdvakadv vlkvrrpgda elksyrpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlik
      361 atmltdggkv vhpafvksdq qphvepaaip aktmvadasp kkaapkkpaa skspsskskg
      421 ia
//
LOCUS       WP_128293819             322 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Afifella].
ACCESSION   WP_128293819
VERSION     WP_128293819.1
KEYWORDS    RefSeq.
SOURCE      Afifella
  ORGANISM  Afifella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Afifellaceae.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Afifella"
                     /db_xref="taxon:643217"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34240
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mptanhakll iigsgpagyt aavyaarall epvliagmep ggqltittev enypgfaepi
       61 qgpwlmeqmr sqaenvgtri vsdivvsael ttrpfrltld sgdvwtadav viatgaqarw
      121 lglpseerfk gfgvsacatc dgffykdkdv lvvgggntav eealylshla rhvtlvhrrd
      181 alraerilqd rlltrdnvsv mwdsaieevl gqggfppavt gakirnvrsg aisevavdgi
      241 fiaighapav slfkdqlrlk pngylwtapd statdipgvf aagdvtddvf rqavtaagqg
      301 cmaaleaeky lfalearqea ae
//
LOCUS       WP_128291052             383 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Afifella
            aestuarii].
ACCESSION   WP_128291052
VERSION     WP_128291052.1
KEYWORDS    RefSeq.
SOURCE      Afifella aestuarii
  ORGANISM  Afifella aestuarii
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Afifellaceae; Afifella.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Afifella aestuarii"
                     /db_xref="taxon:1909496"
     Protein         1..383
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39914
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,92,289,315,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,125..126,135..136,139..140,143..144,146..147,
                     149..154,156,158..160,163,186..187,279..280,322..323,327,
                     330..331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(120..121,125,128,131,172..175,195..197,229,240,
                     257..259,266,268)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,125,135,178..179,186,202..203,205..208)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(155..159,162,165,188,190)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavlkepr ddeprvaatp esikkfktlg advvvesgag agssladevf aeagadvaqt
       61 rqaalqgadi vltvrrpddf sgfpegaavv almdpyghee alkkmaaakl sgfalelipr
      121 itraqsmdvl ssqanlagyr avieaseayg ralpmmmtaa gtvpaarvfv mgagvaglqa
      181 iatakrlgav vtatdvrpaa keqveslggk fvavedeefk aaetaggyak emsaeyrakq
      241 aelvrehiak qdivittali pgrpapklvd aemvksmkdg svivdlaver ggnvegvead
      301 kqvvkdnvtl igivnmagqi aasasallar niyafvepmv dketkalsin redqivaatl
      361 lthggavvhp qfggepvnap nek
//
LOCUS       WP_128297222             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas caviae].
ACCESSION   WP_128297222
VERSION     WP_128297222.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53146
     Region          29..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsydklf rpglaalllt vllgagslaq addsapkgki earselfakd hadqftswkg
       61 tsesrertda laedpqmvvl wagypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnai gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eeyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfdqtcrnch tqskemlqgv vkqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaemk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llaakgishe iaipdisske kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_128302794             426 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M7A.F.Ca.US.010.02.1.1].
ACCESSION   WP_128302794
VERSION     WP_128302794.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.US.010.02.1.1
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.US.010.02.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Mesorhizobium sp. M7A.F.Ca.US.010.02.1.1"
                     /db_xref="taxon:2496743"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43703
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvveag aglnsrivda dyasagaaig
       61 kgsdaakadv vlkvrrpgda elksykpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegav
      301 pgqvvttang vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggkv vhpafvkadq qppkgqyvep aaipaktmva daspkkaapk kaaaskspss
      421 kpkgia
//
LOCUS       WP_128303811             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Mesorhizobium].
ACCESSION   WP_128303811
VERSION     WP_128303811.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34590
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipteqdfmg fgvsacatcd gffyrgkdva vigggnsave ealylsnlak svtvihrrsd
      181 fraerilrer llkkdnvrii wdtivdeitg rpgktplpps veglklkhav tgevshlkvd
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_128307220             427 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M7A.F.Ca.MR.362.00.0.0].
ACCESSION   WP_128307220
VERSION     WP_128307220.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.F.Ca.MR.362.00.0.0
  ORGANISM  Mesorhizobium sp. M7A.F.Ca.MR.362.00.0.0
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Mesorhizobium sp. M7A.F.Ca.MR.362.00.0.0"
                     /db_xref="taxon:2496779"
     Protein         1..427
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43899
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spdtvkrlaa lgfdvvvesg aglnsrivda dyasagaaig
       61 kasdvakadv vlkvrrpgda elksykpgta viaimdpygn daavaalaka gvtafsmefm
      121 pritraqsmd vlssqanlag yqavidgase ydralpmmmt aagtvpaakv fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltsehi akqdivitta lipgrpapkl vsaamvasmk pgsvlvdlav erggnvegae
      301 agkvvttann vkivghlnvp griaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltnggki vhpafikadq qphlepaaip aktmvadasd kpaaakkaas kkpaasksps
      421 skpkgia
//
LOCUS       WP_128316992             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Citrobacter].
ACCESSION   WP_128316992
VERSION     WP_128316992.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53570
     Region          21..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mariksrvrr ffslllpllf isavhaeqts vpaktvtvea knetfapqhp dqylswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspd fakgkpeltl
      181 srpyaerame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmek
      241 yydniafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegkiytd
      301 hkignpfdnf sqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvra hfeakaawda
      361 gateaemkpi ledirhaqwr wdlsiashgi hmhapeeglr mlgsamdkaa dartklvrll
      421 atkgitheip lpdistkeka qaaiglnmqq inaekqdfik tvipqwedqa rkngllsq
//
LOCUS       WP_128322123             373 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas alkylphenolica].
ACCESSION   WP_128322123
VERSION     WP_128322123.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas alkylphenolica
  ORGANISM  Pseudomonas alkylphenolica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Pseudomonas alkylphenolica"
                     /db_xref="taxon:237609"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38823
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hqvtvqsgag inasvpdsay eaagatigsa
       61 adafgaqlvl kvvapddsel tqiksgtvlv gmlnpfnndi iakmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf idvpyeteee recavgvggy arpmpaswmq
      241 rqaqavhera kqadivitta lipgrkaptl lsaetvaqmk pgsvvidlaa aqggncpltv
      301 adqvviengv tivgptnlpa qvgadasaly arnlldfmkl lfdkdsqlvi nleddivaac
      361 lmcrdgqiir kng
//
LOCUS       WP_128327755             306 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Pseudodesulfovibrio].
ACCESSION   WP_128327755
VERSION     WP_128327755.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudodesulfovibrio
  ORGANISM  unclassified Pseudodesulfovibrio
            Bacteria; Pseudomonadati; Thermodesulfobacteriota;
            Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="unclassified Pseudodesulfovibrio"
                     /db_xref="taxon:2661612"
     gene            1..306
                     /gene="trxB"
     Protein         1..306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33336
     Region          4..290
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrsydavvig ggpagmtaal yllragvktv mieklspggq vlmtseieny pgfpkglqgw
       61 eladkfanhl eeydldrind evraievgsp lhtirvgded vqaktiilat gsryrrlgip
      121 geerllgrgv sycalcdgnf frdqdvavig ggnsaleeal ylarlvkkvy iihrrqdfrg
      181 llcyqdkcft hekieiirnt vvdeiqgean vetlalrnta tgessqlkid gtfifvgfep
      241 imnfvpngve kekngivtdv emrtnvpgif aagdirakqc rqvasavgdg ataataafsy
      301 leqldv
//
LOCUS       WP_128322714             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas alkylphenolica].
ACCESSION   WP_128322714
VERSION     WP_128322714.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas alkylphenolica
  ORGANISM  Pseudomonas alkylphenolica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas alkylphenolica"
                     /db_xref="taxon:237609"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33692
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdahgl
       61 tgpalmqrmq ehaerfetev vfdhinavdl askpytlkgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias kvtlvhrrdt
      181 fraekilidk lnarvaegki elklnanlde vlgdnmgvtg arlknndgsf devkvdgvfi
      241 aightpntsl fegqltlkdg ylvvnggrdg natatnvegv faagdvadhv yrqaitsaga
      301 gcmaaldver yldglqnaah
//
LOCUS       WP_128331327             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Apibacter sp. HY039].
ACCESSION   WP_128331327
VERSION     WP_128331327.1
KEYWORDS    RefSeq.
SOURCE      Apibacter sp. HY039
  ORGANISM  Apibacter sp. HY039
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Weeksellaceae; Apibacter.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Apibacter sp. HY039"
                     /db_xref="taxon:2501476"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34029
     Region          11..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseninilqt viigsgpagf taaiyaarae mnpvlisgme lggqltttte venfpgypeg
       61 itgpemmiql qnqaekfgtk vivdkvtevv fgsnskefht iktssgneyq trtiiistga
      121 sakylgkefe dtyrgggvsa catcdgffyr grnvvvvggg dtaaeeatyl akicktvymv
      181 vrkdylkask imqerveats nivlmynhev tnlkgennlv sqavvidnlt qeekildvdg
      241 lfiaighspn tdifkgkldm detgyltvkp fttetniagv faagdvadkr yrqaitaags
      301 gcmaaldaek yltsigh
//
LOCUS       WP_128342364             480 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Aeromonas caviae].
ACCESSION   WP_128342364
VERSION     WP_128342364.1
KEYWORDS    RefSeq.
SOURCE      Aeromonas caviae
  ORGANISM  Aeromonas caviae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Aeromonadales; Aeromonadaceae; Aeromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Aeromonas caviae"
                     /db_xref="taxon:648"
     gene            1..480
                     /gene="nrfA"
     Protein         1..480
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53148
     Region          29..480
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtvgsydklf rpglaalllt allgagslaq addsapkgki earselfakd hadqftswkg
       61 tsesrertda laedpqmvvl wagypfskdy nkprghfyal tdvretlrtg apktaedgpl
      121 pmacwsckgp dvarvidekg edgyfkgmwa kggpeivnti gcadchdtas kefkegkpal
      181 hlsrpyadra mtaigkpfke qgrfdqqsqv cgqchveyyf sgptkavkfp wdkgttveqm
      241 eeyydeigfa dwthalsktp mlkaqhpeye twragihgqn nvacvdchmp kvqneqgkvy
      301 tdhkvgnpfd rfdqtcrnch tqskemlqgv vkqrkdavte iklkvekqlv hahfeakaaw
      361 dagateaemk dilqdirhaq wrwdfsiash gvqmhapeva lrmlgtaldk aadartklar
      421 llaakgishe iaipdisske kaqaalgmdm kqmnsdkaqf lkttvpawda eakaagrlaq
//
LOCUS       WP_128345042             423 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_128345042
VERSION     WP_128345042.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43444
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtifipre ldaneprvaa spdtvkrlag lgfnvivesg agtasripde efgkagavvg
       61 eaadvakadv vlkvrrpdea elkayrpgta viaimdpygn daavdalara gatafsmefm
      121 pritraqsmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgqvvttasg vkiighlnvp grvaasasll yarnlfafle tlvdkttktl ainrdddlvk
      361 atmltdggqv vhpafigkpa vmiasaepak paagekpaap kkaatsrkla aprslankpk
      421 gia
//
LOCUS       WP_128346265             426 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Mesorhizobium].
ACCESSION   WP_128346265
VERSION     WP_128346265.1
KEYWORDS    RefSeq.
SOURCE      unclassified Mesorhizobium
  ORGANISM  unclassified Mesorhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="unclassified Mesorhizobium"
                     /db_xref="taxon:325217"
     Protein         1..426
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44090
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneqrvaa spdtvkrlag lgfevvvekg agtgsripdq dfaangakig
       61 tagdakkadv vlkvrrptda elkgykqgaa viaimdpygn daavaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavidaaae ydralpmmmt aagtvpaaka fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegaq
      301 agkvvttang vkivghlnvp grvaasasll yaknlfafle tlvdkenktl aikrddelvk
      361 atmltdagqv vhpnfakadq qprvepaavp attlvaease kktapkktad kktatsksaa
      421 kpkgia
//
LOCUS       WP_128351491             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudidiomarina gelatinasegens].
ACCESSION   WP_128351491
VERSION     WP_128351491.1
KEYWORDS    RefSeq.
SOURCE      Pseudidiomarina gelatinasegens
  ORGANISM  Pseudidiomarina gelatinasegens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Idiomarinaceae; Pseudidiomarina.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pseudidiomarina gelatinasegens"
                     /db_xref="taxon:2487740"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33859
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 maeakhcrll ilgsgpagyt aavyaaranl npvmvtgmqq ggqlttttdv enwpgdpegl
       61 tgpdlmvrmq khaekfntem ifdhinrvdf sskplklfgd sgeytadsvi iatgasakyl
      121 gldseeafmg rgvsacatcd gffyrnqkva vvgggntave ealylanias evhvihrrdt
      181 fraekilvdr lhdkakngnv tlhlnktlde vlgddagvtg irikdtqnga lseldvmgcf
      241 iaighqpntg ifadqlemqd gyivvssglh gnatatsvpg vfaagdvmdh iyrqaitsag
      301 tgcmaaldae ryldgltka
//
LOCUS       WP_128353738             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pollutimonas thiosulfatoxidans].
ACCESSION   WP_128353738
VERSION     WP_128353738.1
KEYWORDS    RefSeq.
SOURCE      Pollutimonas thiosulfatoxidans
  ORGANISM  Pollutimonas thiosulfatoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pollutimonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Pollutimonas thiosulfatoxidans"
                     /db_xref="taxon:2028345"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34123
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpkhakvl ilgsgpagys aavyaaranl npvlitgleq ggqlmtttdv dnwpadaegv
       61 qgpdlmqrfq ahaerfntem ifdqivtvdl srkpftltgd tgaqytcdal iiatgasamy
      121 lglpseqefm grgvsgcatc dgffyknqdv ivvgggntav eealylsnic rsvtlvhrrd
      181 kfrsepiltd rlmdkvangn mklklfytld evlgdqsgvt gvrlrstktd etedlavtga
      241 fiaighkpnt difqgqlamk dgyiitrsgl dgmatmtsip gvfaagdvqd hiyrqaitsa
      301 gtgcmaalda qrwlenage
//
LOCUS       WP_128355174             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pollutimonas thiosulfatoxidans].
ACCESSION   WP_128355174
VERSION     WP_128355174.1
KEYWORDS    RefSeq.
SOURCE      Pollutimonas thiosulfatoxidans
  ORGANISM  Pollutimonas thiosulfatoxidans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Pollutimonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pollutimonas thiosulfatoxidans"
                     /db_xref="taxon:2028345"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38978
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipreta agetrvaatp etvkkfvaak hsvvvergag sqahfldeay eqagatlads
       61 sqalgadivl kvrspdsqer qhmkqgalli gmldpfnapg iaelasaglt afaleaapri
      121 traqsldvls sqanlagyka vllaanqygr lfpmmmtaag tlkaarvvvl gagvaglqai
      181 atakrlgavv easdvrpaak eqieslgakf idvpfetdee rdiaqgvggy arpmpaawma
      241 rqaalvaerc kqadivista lipgrpapel isaetvqgmk pgsvivdlav erggncplse
      301 kdqivqkhgv wlvgysnlpa lvahdasaly arnvldfmkl iannegelai qeedeiivac
      361 mvckdgkvlr sa
//
LOCUS       WP_128359995             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arcobacter venerupis].
ACCESSION   WP_128359995
VERSION     WP_128359995.1
KEYWORDS    RefSeq.
SOURCE      Arcobacter venerupis (Pseudarcobacter venerupis)
  ORGANISM  Arcobacter venerupis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Arcobacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Arcobacter venerupis"
                     /db_xref="taxon:1054033"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33146
     Region          3..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldlaiiggg pagltaglya trgglknvvm femgmpggqi tssseienyp gqsevvsgmd
       61 lmanwpeqcq rfglkhemaq idrvtkngdi ftlttndkke fqaktvliat gsvpkragfk
      121 geneffgkgv stcatcdgff yrgkevtvig ggdsaieeav ylskmcskvy lvhrrdtyra
      181 apstiehmkh aqnieevtnv tveevygdms gvqgikvkhr etgeirdlpt pgvfifvgrd
      241 vlnaplkqed gsflcnlnea gevivdlrmr tsvsglyaag diridapkqv vcaagdgata
      301 avniieylg
//
LOCUS       WP_128365435             517 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Phycicoccus flavus].
ACCESSION   WP_128365435
VERSION     WP_128365435.1
KEYWORDS    RefSeq.
SOURCE      Phycicoccus flavus
  ORGANISM  Phycicoccus flavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Intrasporangiaceae; Phycicoccus.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Phycicoccus flavus"
                     /db_xref="taxon:2502783"
     Protein         1..517
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53602
     Region          1..512
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrigvpretv pgetrvaatp ktveklvglg ytvfvesgag alaafddeay rtagadvidd
       61 avwnadvvlk vnaptetele rlrpgqllaa llspalrpel vealaargvt alamdavpri
      121 sraqsldvls smaniggyra vieaahefgs fftgqvtaag kvppakvlvv gagvaglaai
      181 gtanslgavv rafdarpeva eqvesmgaqf lrievedegp sadgyakets adfdakaadl
      241 yaaqardvdi vittalipgr paprlltedm vasmkpgsvv vdmaaanggn vagtvagekv
      301 vtdngvtllg ytdlpgrlpt qssqlygtnl vnllklltpe kdgevvldld dvvqrgmtvv
      361 rdgevmwppp pvqvsaapap gtdvitvdtt atkarrrplp agtklaaagv aallfllvaa
      421 fspapflghf mvfmlsvvig fyvignvhha lhtplmsvtn aisgiivvga llqvgrggwa
      481 vsvvafvgil vasinvfggf rvtarmlemf kreevar
//
LOCUS       WP_128369687             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.
            M7A.T.Ca.US.000.02.1.1].
ACCESSION   WP_128369687
VERSION     WP_128369687.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M7A.T.Ca.US.000.02.1.1
  ORGANISM  Mesorhizobium sp. M7A.T.Ca.US.000.02.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. M7A.T.Ca.US.000.02.1.1"
                     /db_xref="taxon:2496792"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34590
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli vgsgpagyta avyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgtdii ndiitevdln vrpfrakgds gttytadali iatgaqakwl
      121 gipteqdfmg fgvsacatcd gffyrgkdva vvgggnsave ealylsnlar svtvihrrsd
      181 fraerilrer llkkdnvrvi wdtivdeitg rpgktplpps veglklkhav tgevshlkid
      241 gvfvaighap avelfagklk qkpngylwta pdstrtdvpg vfaagdvtdd iyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_128370193             418 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha, partial
            [Mesorhizobium sp. M1A.F.Ca.IN.020.32.1.1].
ACCESSION   WP_128370193
VERSION     WP_128370193.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M1A.F.Ca.IN.020.32.1.1
  ORGANISM  Mesorhizobium sp. M1A.F.Ca.IN.020.32.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Mesorhizobium sp. M1A.F.Ca.IN.020.32.1.1"
                     /db_xref="taxon:2496763"
     Protein         1..>418
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsritdq efaaaggtig
       61 tagdaknadv vlkvrrptda elkgyksgaa viaimdpygn daalaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatktl aikrddelvk
      361 atmltdagqv vhpsfakaag qprtepaaip atvlvadaad kkpaprrraa akspspkp
//
LOCUS       WP_128371214             422 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Mesorhizobium sp. M1A.F.Ca.ET.072.01.1.1].
ACCESSION   WP_128371214
VERSION     WP_128371214.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M1A.F.Ca.ET.072.01.1.1
  ORGANISM  Mesorhizobium sp. M1A.F.Ca.ET.072.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Mesorhizobium sp. M1A.F.Ca.ET.072.01.1.1"
                     /db_xref="taxon:2496753"
     Protein         1..422
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43629
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre ldaneprvaa spetvkrlag lgfevivekg aglgsritdq efataggtig
       61 tagdaknadv vlkvrrptda elkgyksgaa viaimdpygn dpalaamaka gitafsmefm
      121 pritraqvmd vlssqanlag yqavvdaaae ydralpmmmt aagtvpaakt fimgvgvagl
      181 qaiatarrlg avvtatdvrp avkeqvqslg akflavedee fkaaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamvasmk pgsvivdlav erggnvegav
      301 pgrvvtteng vkivghlnvp grvaasasll yaknlyafle tmvdkatkgl aikrddelvk
      361 atmltdagqi vhpsfakaae tprtepaaip atvlvadtad kkpvprkraa akspspkpeg
      421 ta
//
LOCUS       WP_128371992             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mesorhizobium sp.
            M1A.F.Ca.ET.072.01.1.1].
ACCESSION   WP_128371992
VERSION     WP_128371992.1
KEYWORDS    RefSeq.
SOURCE      Mesorhizobium sp. M1A.F.Ca.ET.072.01.1.1
  ORGANISM  Mesorhizobium sp. M1A.F.Ca.ET.072.01.1.1
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Mesorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Mesorhizobium sp. M1A.F.Ca.ET.072.01.1.1"
                     /db_xref="taxon:2496753"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34555
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mntkhapvli igsgpagyta aiyaaramlk pmlvaglqqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qaehvgteiv ndiitevdln vrpfratgds gtvyaadali iatgaqakwl
      121 gipseqtfmg fgvsacatcd gffyrgkdva vvgggnsave ealylanlak svtvihrrnd
      181 fraerilrer lfkkdnvrii wdtvvdeitg qpgkaplpps vdglklrnvv tgevsrlqvd
      241 gvfvaighap avelfigklk qkpngylwta pdstrtdvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagievhr eaae
//
LOCUS       WP_128377520             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces cavernae].
ACCESSION   WP_128377520
VERSION     WP_128377520.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces cavernae
  ORGANISM  Streptomyces cavernae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces cavernae"
                     /db_xref="taxon:2259034"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34305
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpelmdnmra qaerfgaelv pddvvavdls geiktvtdts gtvhqakavi vttgsqhrkl
      121 glpnedklsg rgvswcatcd gfffreqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqdr afadpkikfi wdsevaeiqg dqklsglklr nvktgetsel pvtglfiaig
      241 hdprtelfkg qlelddegyl rveapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerylaala dteaaepekt tv
//
LOCUS       WP_128386216             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Leucobacter muris].
ACCESSION   WP_128386216
VERSION     WP_128386216.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter muris
  ORGANISM  Leucobacter muris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Leucobacter muris"
                     /db_xref="taxon:1935379"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34293
     Region          7..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msiqevelvi vgsgpagyta avyaaragla pvviagsvta ggalmtttev enfpgfvdgv
       61 qgpelmesmr araerfgaei ayddairldl dgdvktietg agltyrarav iltmgsayrk
      121 lglpeeerls ghgvswcatc dgfffreqei vvvgggdsam eealfltrfa skvtvvhrrd
      181 efraskimaq rvlddpkiev awnsevaail gdeqviglrl rdtvtgmert ldatgvfvai
      241 ghdprselvi wqvdtdadgy vrvahpstrt nlagvfaagd lvdhtyrqai taagtgcaaa
      301 qdaqhylsnl apatvsapvl evsa
//
LOCUS       WP_128387712             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Leucobacter muris].
ACCESSION   WP_128387712
VERSION     WP_128387712.1
KEYWORDS    RefSeq.
SOURCE      Leucobacter muris
  ORGANISM  Leucobacter muris
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leucobacter.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Leucobacter muris"
                     /db_xref="taxon:1935379"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32766
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhqiiiigsg pagftaavya araglkpvlf assvgiggel mnttdvenfp gfpegiqgpn
       61 lmqrmqeqae rfgtevvydd ivevdfsspv krvtagdgsv heartviyat gsayrklglp
      121 dedrlsghgv swcatcdgff frektiavvg ggdsameeat fltrfadkvy vihrreelka
      181 skimqqrafd nekiefiwns evaaihgade vtgvtlrstv dggerelplq glfiaigndp
      241 rthlvhgkld ltvdgtiave grssrtsvag vfaagdvvdp tyrqaitaag sgtvaaldae
      301 hylaaldg
//
LOCUS       WP_128388775             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium cerinum].
ACCESSION   WP_128388775
VERSION     WP_128388775.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium cerinum
  ORGANISM  Flavobacterium cerinum
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Flavobacterium cerinum"
                     /db_xref="taxon:2502784"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33657
     Region          9..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdtiekikc liigsgpagy taaiyaarad mkpilytgme pggqltttte vdnfpgypeg
       61 idgptmmiql qqqaerfgtq vrigmatave fstvaggwhk vtidgnkevh aqtviistga
      121 takylglpse qrlrgggvsa cavcdgffyr gqdvaivgag dtaaeeatyl anicknvtml
      181 vrkdamrask amqhrventp nltvlynsev devigdqvvd glrivnnvtg ekseiaitgl
      241 fiaighkpnt difkgqldmd dtgylitegk stktnlpgvf asgdvqdkey rqaitaagsg
      301 cmaaldaery latlesh
//
LOCUS       WP_128394918             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Advenella incenata].
ACCESSION   WP_128394918
VERSION     WP_128394918.1
KEYWORDS    RefSeq.
SOURCE      Advenella incenata
  ORGANISM  Advenella incenata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Advenella incenata"
                     /db_xref="taxon:267800"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33965
     Region          9..314
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 madktkhakv lilgagpagy taavyaaran lnpvlvtgme qggqlmtttd vdnwpadaqg
       61 vqgpdlmqrf lehatrfntd ivqehikead lsvrpfrlvs esgttftcda liiatgssak
      121 ylglpsetaf mgkgvsacat cdgffyrnqd vvvvgggnta veealylsni crhvtlvhrr
      181 dtfraepilv dklmdkvngg tmslklfntl eevlgdqsgv tgarlrhvdg hledlaatgv
      241 fiaighhpnt tlfegqlele ngyivtksgh gglatmtsvp gvfaagdvqd hvyrqaitsa
      301 gtgcmaaldv qrwlesqpe
//
LOCUS       WP_128402784             324 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Rhizobium].
ACCESSION   WP_128402784
VERSION     WP_128402784.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34775
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mparhtkvli igsgpagyta avyaaramlk pvliagleqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlq qakhvgaeiv ndlvtevdmn qrpfvartds gqvwtadtli iatgakakwl
      121 gieseqhfqg fgvsacatcd gffyrnkdvi vvgggnsave ealylsniak svtvvhrrdf
      181 fraekilqer lfskdnvkvl wntevaeitg tpakppmpqs vsgarlrdvr tgtitdmvid
      241 gvfvaighap atelfkdklk lkdngylwta pdstatsldg vyaagdvtdd tfrqaitaag
      301 lgcmaaleve ryltghmpva vaae
//
LOCUS       WP_128399451             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhizobium hidalgonense].
ACCESSION   WP_128399451
VERSION     WP_128399451.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium hidalgonense
  ORGANISM  Rhizobium hidalgonense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rhizobium hidalgonense"
                     /db_xref="taxon:1538159"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34721
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mparhtkvli igsgpagyta avyaaramlk pvliagleqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlq qakhvgaeiv ndlvtevdmn qrpfvartds gqvwtadtli iatgakakwl
      121 gieseqhfqg fgvsacatcd gffyrnkdvi vvgggnsave ealylsniak svtlvhrrdv
      181 fraekilqer lfakenvkvl wnseiaeitg tpakppmpqs vtgarlrdvr tgaitempid
      241 gvfvaighap atelfkdklk lkdngylwta pdstatsleg vyaagdvtdd tfrqaitaag
      301 lgcmaaleae ryltghmpva vaae
//
LOCUS       WP_128403347             382 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            leguminosarum].
ACCESSION   WP_128403347
VERSION     WP_128403347.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39165
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare itgeetrvaa saetvkkmks fgfdvvveag agaasripdg efeaagarig
       61 sfadaasadv vlkvrrpsgs eisgyksgav iisimdpygn deaiaalasa glstfamelm
      121 pritraqsmd vlssqanlag yqavievaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgraaprl vsramlasmk sgavavdlav erggniegvv
      301 pgeiadvegv rvigfanmpg rvaasasaly aknlvtflet mvnketrsvv vnlddelvka
      361 tmltyagdvv hpafggakkg di
//
LOCUS       WP_128424301             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_128424301
VERSION     WP_128424301.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53546
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsvlipffy ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglk mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_128412451             382 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Rhizobium].
ACCESSION   WP_128412451
VERSION     WP_128412451.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium
  ORGANISM  Rhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rhizobium"
                     /db_xref="taxon:379"
     Protein         1..382
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39149
     Region          4..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgnivfvare itgeetrvaa saetvkkmks fgfdvvveag agaasripdg efeaagarig
       61 sfadaasadv vlkvrrpsgs eisgyksgav iiaimdpygn deaiaalasa glstfamelm
      121 pritraqsmd vlssqanlag yqavievaav ydrampmmmt aagtvpaakv fvmgagvagl
      181 qaiatarrlg aavsatdvrp aakeqvaslg akfiavedde fkaaetaggy akemsadyqa
      241 kqaalvaehi akqdivitta lipgraaprl vsramlasmk sgavavdlav erggniegvv
      301 pgeiadvegv rvigfanmpg rvaasasaly aknlvtflet mvnketrsvv vnlddelvka
      361 tmltyagdvv hpafggakkg di
//
LOCUS       WP_128416502             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Xanthomonas populi].
ACCESSION   WP_128416502
VERSION     WP_128416502.1
KEYWORDS    RefSeq.
SOURCE      Xanthomonas populi
  ORGANISM  Xanthomonas populi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Xanthomonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Xanthomonas populi"
                     /db_xref="taxon:53414"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34237
     Region          14..320
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mspssaspak hsrllilgsg pagwtaavya aranlkpvvi tglqqggqlm tttevdnwpg
       61 dphglmgpdl msrmqahaer fetevifdhi htadlsqrpf rlvgdgaeyt cdalviatga
      121 takylgipse eafkgrgvsa catcdgffyk dqdvvvvggg ntaveealyl sniarkvylv
      181 hrrdtlraek imqdklfakv vagkietvwh haidevlgnd agvtgvrvkc tidgstrdiv
      241 ahgffvaigh hpntqlfdgq lamnngylei rsglngaate tsvsgvfaag dvadqhyrqa
      301 itsagfgcma aldaeryldk sa
//
LOCUS       WP_128426347             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gudongella oleilytica].
ACCESSION   WP_128426347
VERSION     WP_128426347.1
KEYWORDS    RefSeq.
SOURCE      Gudongella oleilytica
  ORGANISM  Gudongella oleilytica
            Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
            Tissierellaceae; Gudongella.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Gudongella oleilytica"
                     /db_xref="taxon:1582259"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33305
     Region          3..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvydvviiga gpaglsagly aararlktli vekeaaggqi attdevanyp gsiehatgps
       61 lvarmvqqae efgaekvsdt vvsvdlegdi ktvkcekney ktktiiiatg avpkhigcpg
      121 ekeltgrgis ycatcdgaff edlevfvvgg gdsaveeamy ltkfarkvti vhrrdalraa
      181 ksiqekafkn ekiafmwdsv itevkgdgil qsmvvknvkt geeteyfade ddgtfgifvf
      241 vgydpatklf egmvdmengy iktddnmktn ipgvfaagdn rvkplrqvvt atadgaiaat
      301 qaekyieehf
//
LOCUS       WP_128435541             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces cyaneus].
ACCESSION   WP_128435541
VERSION     WP_128435541.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces cyaneus
  ORGANISM  Streptomyces cyaneus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Streptomyces cyaneus"
                     /db_xref="taxon:1904"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34160
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgim
       61 gpelmdnmrg qaerfgaelv pddivnvdls geiktvtdta gtvhrakavi vatgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqdr afadpkikfv wdsevaevqg eqklsglklr nvktgelsdl avtglfiaig
      241 hdprtelfkg qleldeegyl kvdapstrtn lsgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala deenaepekt sv
//
LOCUS       WP_128438210             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhizobium leguminosarum].
ACCESSION   WP_128438210
VERSION     WP_128438210.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34743
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mparhtkvli igsgpagyta avyaaramlk pvliagleqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlq qakhvgaeiv ndlvtevdmn qrpfvartds gqvwtadtli iatgakakwl
      121 gieseqhfqg fgvsacatcd gffyrnkdvi vvgggnsave ealylsniak svtlvhrrdf
      181 fraekilqer lfskdnvkvl wntevaeitg tpakpplpqs vsgarlrdvr tgtitdmvid
      241 gvfvaighap atelfkdklk lkdngylwta pdstatsldg vyaagdvtdd tfrqaitaag
      301 lgcmaaleae ryltghmpva vaae
//
LOCUS       WP_128440445             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Enterococcus faecium].
ACCESSION   WP_128440445
VERSION     WP_128440445.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33299
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydvivigag pagmtaalya srsnlsvlmi eqgapggqmn ntaeienypg fdsimgpdla
       61 ykmyegvsrf gtenaygivq dikdhgshke vicedktyeg ktviiatgci hrklgvpgee
      121 efagrgvsyc avcdgaffrn krllvigggd saveeaiylt qfasevvivh rrdelraqki
      181 iqdrafanek isfmwdtvvd eivgnemvvt gvkarnvktg nefdlaadgv fiyvgldplt
      241 apfreagltn eagwiptdne mktnipgvfa igdvrekdlr qittavgdgg iagqqvykyl
      301 esleetta
//
LOCUS       WP_128442574             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neorhizobium lilium].
ACCESSION   WP_128442574
VERSION     WP_128442574.1
KEYWORDS    RefSeq.
SOURCE      Neorhizobium lilium
  ORGANISM  Neorhizobium lilium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Neorhizobium.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Neorhizobium lilium"
                     /db_xref="taxon:2503024"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34740
     Region          6..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msarhtevli igsgpagyta avyaaramlr pvliagmeqg gqlmittdve nypgfadpiq
       61 gpwlmeqmlk qamhvgteiv ndlvtevett rrpftirtds gavwtadtii iatgakakwl
      121 gieseqhfqg fgvsacatcd gffyrnrdvi vvgggnsave ealylsniak svtvvhrrde
      181 frsekilrer lfqrpnvhvm wntevaeitg kpakapmpps vegiklrntl tgtvterpvd
      241 gvfvaighap atdlfkgklk mkpggylwta pdstatdvpg ifaagdvtdd sfrqaitaag
      301 mgcmaaleae rylagiqpva vaae
//
LOCUS       WP_128446010             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_128446010
VERSION     WP_128446010.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38520
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn laddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_128447674             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_128447674
VERSION     WP_128447674.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>311
                     /gene="trxB"
     Protein         1..>311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..311
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv hlhwnttlde vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae k
//
LOCUS       WP_128453001             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Sphingomonas sp. UV9].
ACCESSION   WP_128453001
VERSION     WP_128453001.1
KEYWORDS    RefSeq.
SOURCE      Sphingomonas sp. UV9
  ORGANISM  Sphingomonas sp. UV9
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Sphingomonadaceae; Sphingomonas.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Sphingomonas sp. UV9"
                     /db_xref="taxon:1851410"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34227
     Region          6..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtthttrmli lgsgpaglsa aiygaragma pivvqgiqpg gqlttttdve nypgfkdviq
       61 gpwlmeqmta qaehvgtrmm wdtitqvdlt srpfrligds gdvyegdtlv iatgaqakwl
      121 gidseepmkg kgvsacatcd gffyrgkkva vigggntave ealyltnhsp dvtlihrrds
      181 lrsekilqer lfahkgvtvl wnkevrefvd gggnaglval eledtvtger srldvdggfv
      241 aighhpatel frghleldsd gyiavetgst rtnvegvfac gdvadkiyrq avtaagtgcm
      301 aaldaerfla aaefaemaea ae
//
LOCUS       WP_128461129             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Rhizobium
            leguminosarum].
ACCESSION   WP_128461129
VERSION     WP_128461129.1
KEYWORDS    RefSeq.
SOURCE      Rhizobium leguminosarum
  ORGANISM  Rhizobium leguminosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Rhizobium.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rhizobium leguminosarum"
                     /db_xref="taxon:384"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55219
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalreia gqearvaltp esalqlqklg yeciietgag eqagfsdqay gdagvvvved
       61 aaavcsssdv vikvrppepg eidklaagkt lisffypaqn aillekakht glnviamdmv
      121 prisraqkmd alssmanvag yravieagnn fgrfftgqvt aagkvppakv liigagvagl
      181 aaigtatslg aityafdvrp evaeqiesmg aefvfldfad qqdgaesggy aapsspkfre
      241 tqlakfrela peidivitta lipgrdapkl wladmvsamk pgsvivdlaa erggnceltv
      301 adqrivsdng viiigytdyp srmaaqastl ysnnirhmis dltphkngqi ihdmeddvir
      361 gatvsyqgev tfpppppkik aiaaqkpkdk ikeltpvekr akevaafkaq tksqgfllag
      421 gtaalllvga fapasfmshf vvfvlscfig fqviwnvshs lhtplmavtn avsgivilga
      481 llqigseswl vvtlsavsvl iatinivggf lvtrrmlamf qks
//
LOCUS       WP_128456258             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_128456258
VERSION     WP_128456258.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53556
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mpgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_128457601             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_128457601
VERSION     WP_128457601.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53545
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap qnaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_128457091             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_128457091
VERSION     WP_128457091.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53573
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apatpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf vqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_128452101             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_128452101
VERSION     WP_128452101.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53568
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkats
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qqaiglnmeq ikaekqdfik pvipqweeqa rkngllsq
//
LOCUS       WP_128462581             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces albidoflavus].
ACCESSION   WP_128462581
VERSION     WP_128462581.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34018
     Region          6..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mseirevvii gsgpagytaa lyaaraqlkp llfgssifvg gsltttteve nfpgfpdgvd
       61 gpvlmenmra qaekfgaemi dddivsvdlt geikeltdse gtvhrakavi iatgsgyrkl
      121 glpneeklsg rgvswcatcd gfffrdrdiv vvgggdtame eatfltrfar svtvvhrrst
      181 lrasqvmrnr afaddkisfm fdseiveike engmlggval rdtltgeire laatglfiai
      241 ghdprtelft gqldldddgy itveppstrt nlpgvfaagd vvdhiyrqai taagtgaaag
      301 ldverylaal adkapvlaas
//
LOCUS       WP_128463550             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces albidoflavus].
ACCESSION   WP_128463550
VERSION     WP_128463550.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces albidoflavus
  ORGANISM  Streptomyces albidoflavus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces; Streptomyces
            albidoflavus group.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces albidoflavus"
                     /db_xref="taxon:1886"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34126
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfqdgvm
       61 gpelmdnmra qaerfgaelv pddvvsvdls geiktvtdta gtvhrakavi vttgsqhrkl
      121 glpnedtlsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrds
      181 lraskamqer afadpkikfi wdsevaeihg dpkltgltlr nlksgdtell svtglfiaig
      241 hdprtelfkg qldldgegyl kvaapstrtn vtgvfaagdv vdhtyrqait aagtgcsaal
      301 daerylaava daeghektev vta
//
LOCUS       WP_128466299             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Geovibrio thiophilus].
ACCESSION   WP_128466299
VERSION     WP_128466299.1
KEYWORDS    RefSeq.
SOURCE      Geovibrio thiophilus
  ORGANISM  Geovibrio thiophilus
            Bacteria; Pseudomonadati; Deferribacterota; Deferribacteres;
            Deferribacterales; Geovibrionaceae; Geovibrio.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Geovibrio thiophilus"
                     /db_xref="taxon:139438"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34944
     Region          14..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mqdffnfqdi keeydvvilg agpagltaam yaardnlstl llekqfpggq vattefveny
       61 pgfpeglmga dlsekmyaha ekfgvviraa ecqnievkgd ykyltiknls fqikakalil
      121 clgahwkrld vtgenrffgr gvsfcatcdg sfykdkeiav igggdsavee glyltkfask
      181 vtiihrrdkl raakiyqdra lkhekmsfiw dtvvtavngd qkvssvslkn lktgeesele
      241 vagifvfigq tadtelvkdl ikldesgfiv adettetsvp gifaagdvrw kplrqittav
      301 adgsvaakaa gkyigevfeq
//
LOCUS       WP_128484243             478 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Escherichia coli].
ACCESSION   WP_128484243
VERSION     WP_128484243.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53582
     Region          4..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mtrikinarr ifsllipfff ftsvhaeqta apakpvtvea knetfapqhp dqylswkatp
       61 eqservdala edprlvilwa gypfsrdynk prghafavtd vretlrtgap knaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspe fakgkpeltl
      181 srpyaarame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmeq
      241 yydkiafsdw tnslsktpml kaqhpeyetw tagihgknnv tcidchmpkv qnaegklytd
      301 hkignpfdnf aqtcanchtq dkaalqkvva erkqsindlk ikvedqlvha hfeakaalda
      361 gateaemkpi qddirhaqwr wdlaiashgi hmhapeeglr mlgtamdkaa dartklarll
      421 atkgitheiq ipdistkeka qkaiglnmeq ikaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_128481240             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Helicobacter pylori].
ACCESSION   WP_128481240
VERSION     WP_128481240.1
KEYWORDS    RefSeq.
SOURCE      Helicobacter pylori
  ORGANISM  Helicobacter pylori
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Helicobacteraceae; Helicobacter.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Helicobacter pylori"
                     /db_xref="taxon:210"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33322
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 midcaiiggg paglsaglya trggvkntvl fekgmpggqi tgsseienyp gvkevvsgld
       61 fmqpwqeqcf rfglkhemsa iqrvskkdsh fvilaedgnt feansviiat ggspkrtgik
      121 geseywgkgv stcatcdgff yknkevavlg ggdtaveeai ylanickkvy lihrrdgfrc
      181 apitlehakn nnkiefltpy vveeikgdas gvsslsiknt atnetreliv pgffifvgyd
      241 vnnavlkqed gsmlckcdef gsivvdfsmk tnvqglfaag dirifapkqv vcaasdgata
      301 alsvisyleh h
//
LOCUS       WP_128486838             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Falsigemmobacter intermedius].
ACCESSION   WP_128486838
VERSION     WP_128486838.1
KEYWORDS    RefSeq.
SOURCE      Falsigemmobacter intermedius
  ORGANISM  Falsigemmobacter intermedius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Falsigemmobacter.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Falsigemmobacter intermedius"
                     /db_xref="taxon:1553448"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33235
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msetrhtkvl iigsgpagyt aavyasraml spilvqgiqp ggqltittev enwpgdktvq
       61 gpdlmvrmee haremgadiq fdtitelklg srpftavgds gttytadavi latgaqarwl
      121 glpseekfkg fgvsacatcd gffyrdkpva vigggntave ealfltnfas kvtlihrrds
      181 lraekilqer lfshpkvevl wnhevdevlg teaplgvtgl rvknvqsget seiacdgffv
      241 aighspasel vkdqlelhng gyvkvepgst rtsipgvfaa gdltdhvyrq aitsagmgcm
      301 aaldaerfla gh
//
LOCUS       WP_128490101             524 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Falsigemmobacter intermedius].
ACCESSION   WP_128490101
VERSION     WP_128490101.1
KEYWORDS    RefSeq.
SOURCE      Falsigemmobacter intermedius
  ORGANISM  Falsigemmobacter intermedius
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Falsigemmobacter.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Falsigemmobacter intermedius"
                     /db_xref="taxon:1553448"
     Protein         1..524
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55639
     Region          1..523
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigalkeif egenrvamtp dsalqlvklg htcviesgag akagfsdaay ekagvtvlpt
       61 aqavseaadv lvkvrgpeas evallrqgqt lisffwpaqn aelleaisar gatvvamdmv
      121 prisraqkmd alssmaniag yravieagnn fgrfftgqvt aagkvppakv lvvgagvagl
      181 aaigtstslg aityafdvrp evaeqiesmg aefvyldfad qvqdgaatgg yaapsspefr
      241 eaqlkkfrel apdmdivitt alipgrpapk lwtedmvqmm kpgsvivdla aerggncdlt
      301 ipderivten gvtivgytdf psrmaaqast lystnirhml tdltpkkdgv ifhnmeddvi
      361 rgatvthega itypppppki qaiaaqkpke kvkeltpeek rakeaaefka qtrnqftllg
      421 vsgallllvg lvapaefmqh fivfvlacfv gfqiiwnvah slhtplmait naissiiilg
      481 almqigsgsw lvivlaglsv fmaginifgg favtrrmlam fqks
//
LOCUS       WP_128493423             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Labedella phragmitis].
ACCESSION   WP_128493423
VERSION     WP_128493423.1
KEYWORDS    RefSeq.
SOURCE      Labedella phragmitis
  ORGANISM  Labedella phragmitis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Labedella.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Labedella phragmitis"
                     /db_xref="taxon:2498849"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34717
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrnviiigsg pagytaaiya araglepvll assveaggel mntteienfp gfpdgimgpd
       61 lmakfqeqae rfgtevildd vteldlrgei ktvktgysge fegrtvifat gsayrklglg
      121 dedrlsgrgv swcatcdgff fkgkeiavvg ggdsameeat fltrfaskvy vihrrdslka
      181 skimqdrafa nekiefvwns evtgitgega vdgvtlrdtv dgserhlaig glfvaigndp
      241 rthlihgqld lteegtiave grssrtnlpg vfaagdvidp hyrqaitaag sgtvaaldae
      301 hylsalddae kleaegette aealiasa
//
LOCUS       WP_128497101             328 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Labedella populi].
ACCESSION   WP_128497101
VERSION     WP_128497101.1
KEYWORDS    RefSeq.
SOURCE      Labedella populi
  ORGANISM  Labedella populi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Labedella.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Labedella populi"
                     /db_xref="taxon:2498850"
     gene            1..328
                     /gene="trxB"
     Protein         1..328
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34703
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrnviiigsg pagytaaiya araglepvll assveaggel mntteienfp gfpdgimgpd
       61 lmakfqeqae rfgtevildd vteldlrget ktvktgysgd fegrtvifat gsayrklglg
      121 dedrlsgrgv swcatcdgff fkgkeiavvg ggdsameeat fltrfaskvy vihrrdslka
      181 skimqdrafa nekiefvwns evvgitgega vdgltlrdti dgserhlaig glfvaigndp
      241 rthlvhgqld ltdegtiave grssrtnlpg vfaagdvidp hyrqaitaag sgtvaaldae
      301 hylsalddae kldeegetae aealiasa
//
LOCUS       WP_128499763             556 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium septicum].
ACCESSION   WP_128499763
VERSION     WP_128499763.1
KEYWORDS    RefSeq.
SOURCE      Clostridium septicum
  ORGANISM  Clostridium septicum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Clostridium septicum"
                     /db_xref="taxon:1504"
     gene            1..556
                     /gene="trxB"
     Protein         1..556
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=60898
     Region          3..556
                     /region_name="AhpF_homolog"
                     /note="putative alkyl hydroperoxide reductase F subunit;
                     TIGR03143"
                     /db_xref="CDD:132187"
ORIGIN      
        1 mndkifdlvi igagsaglsa giyatrakln tliieksspg gqitktseiv nypgirktsg
       61 helmeemrlq aedfgvkfqr aevndvdlsn evkilktdig eikgraviia tgatprklgf
      121 pgeeefagrg vaycatcdge ffkglevlvi gagfaaceea iyltrfakkv tiiarepdft
      181 caksigdkvk ahpkidikfn tevveaigdd llrsvklinn vtyekseyfp pkedgtfgif
      241 ifagyvpqts vfknhieldn fgyiitdenm qtnikgvyaa gdlrpkslrq vvtavadgai
      301 aatdaekyif eekerlgiad evtyeapvkk esnetttnne kksfngkshl lndtlrtqls
      361 silskienpi tlvtivdpnn gksielrdlv ldianlsdkl kaevyiknea ksieekinad
      421 kypvvalldk dnnysgvkfh gvpgghelns filaiynlag pgqpidpnnl ekiksinkat
      481 nikvcvslsc hlcpdvvvsa qriaienpnv etemldlanf deiktkyklm svpaiivnds
      541 evyfgakkld eilnii
//
LOCUS       WP_128511038             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces inhibens].
ACCESSION   WP_128511038
VERSION     WP_128511038.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces inhibens
  ORGANISM  Streptomyces inhibens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Streptomyces inhibens"
                     /db_xref="taxon:2293571"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34314
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfrdgim
       61 gpdlmdnmra qaerfgaelv pddvvavdls eeiktvtdta gnvhrakavi vstgsqhrkl
      121 glpredelsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtvvhrrdt
      181 lraskamqdr afadpkikfv wdsevaevhg dnklsgltlr nvktgetsel pvtglfiaig
      241 hdprtelfkg qlnlddegyl kvdapstrtn lagvfaagdv vdhtyrqait aagtgcsaal
      301 daerflaals dgeataepdk tvsa
//
LOCUS       WP_128513112             311 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Limosilactobacillus mucosae].
ACCESSION   WP_128513112
VERSION     WP_128513112.1
KEYWORDS    RefSeq.
SOURCE      Limosilactobacillus mucosae
  ORGANISM  Limosilactobacillus mucosae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Limosilactobacillus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Limosilactobacillus mucosae"
                     /db_xref="taxon:97478"
     gene            1..311
                     /gene="trxB"
     Protein         1..311
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33278
     Region          9..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maeekqtnyd vivvgagpag mtaalyasra nlsvlmldrg iyggnlnnta aienypgfkt
       61 vqgpelaqdm yqgatqfgal yaygtvekve lagdlkqltt dmgdvftakv lviatgtqqr
      121 hmgvpgeeey ggrgvsycav cdgaffknkh vvvvgggdsa veegmyltql akkvtvvvrr
      181 dqlraqpliq eqakqndkme fifntqvtev igddnkvvgv kthdsktgkd aeiqadgvfi
      241 yvgsvpmtap fkdlgilneq gyvktndlma tslpgvfaig dvretplrqi atavgdgaia
      301 gqqiyqylmn h
//
LOCUS       WP_128513998             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Tabrizicola thermarum].
ACCESSION   WP_128513998
VERSION     WP_128513998.1
KEYWORDS    RefSeq.
SOURCE      Tabrizicola thermarum
  ORGANISM  Tabrizicola thermarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tabrizicola.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Tabrizicola thermarum"
                     /db_xref="taxon:2670345"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33152
     Region          7..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mgdtrhtrvl iigsgpagyt aaiysaraml npiliqglqp ggqltittev enwpgdhsvq
       61 gpdlmvrmee hakamgaevi sdyitsldls erpftakads gttytadavi latgaqakwl
      121 glpseekfkg fgvsacatcd gffyrgkevv vigggntave ealfltnfas kvtvihrrds
      181 fraekimqdr lfrnpkievv wdtavieilg teaplgvtgv rvqnvktgae rvipcdgffv
      241 aighapasel vkdqlplhsg gyvvvepgst rtaipgvfaa gdltdhiyrq avtsagmgcm
      301 aaldaekfla eh
//
LOCUS       WP_128516941             523 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Tabrizicola thermarum].
ACCESSION   WP_128516941
VERSION     WP_128516941.1
KEYWORDS    RefSeq.
SOURCE      Tabrizicola thermarum
  ORGANISM  Tabrizicola thermarum
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Tabrizicola.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Tabrizicola thermarum"
                     /db_xref="taxon:2670345"
     Protein         1..523
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55056
     Region          1..522
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mkigaltevf pgenrvamtp dsamqlaklg htaciqagag akagftdaay aaagvevlpd
       61 aasviaaadv ivkvrgpdaq elaslqdgqt lisffwpaqn pelleaaakk nltivamdmv
      121 prisraqkmd alssmanlag yravieaann fgrfftgqvt aagkippakv lvvgagvagl
      181 aaigasvslg avthafdvrp evaeqiesmg anfvflefep tqdgaatggy aapsspefre
      241 kqlakfrela pemdivitta lipgrpapkl wtedmvramk pgsvivdlaa erggncdltv
      301 pdqkivtdng vtiigytdfp srmatqastl yannirhmlt dltpkkdgvi lhnmeddvir
      361 gatvahmgav typppppkvq aiaaakpkek pkeltpeerr aqevaafkaq trnqvgllti
      421 ggglmllagl yapasfmshf ivfvlavfvg fqviwnvshs lhtplmavtn aissiiilga
      481 lmqigsgsfl villaalsvf maginifggf mvtrrmlamf qks
//
LOCUS       WP_128528185             306 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase, partial [Pseudomonas aeruginosa].
ACCESSION   WP_128528185
VERSION     WP_128528185.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..>306
                     /gene="trxB"
     Protein         1..>306
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
     Region          1..306
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttlde vlgdasgvtg vtgvrlksti dgstselsla
      241 gvfiaighkp ntdlfqgqle mrdgylrihg gsegnatqts iegvfaagdv adhvyrqait
      301 sagagc
//
LOCUS       WP_128524907             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Halobacillus litoralis].
ACCESSION   WP_128524907
VERSION     WP_128524907.1
KEYWORDS    RefSeq.
SOURCE      Halobacillus litoralis
  ORGANISM  Halobacillus litoralis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halobacillus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Halobacillus litoralis"
                     /db_xref="taxon:45668"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34118
     Region          6..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkhksiilgt gpagltaavy laranmeplv iegpepggql tlttevenfp gfpdgimgpe
       61 lmdnmkkqae rfgatfkrgw vtdvevesrp fklqvdglge letetliist gasakllgip
      121 gekenmgkgv stcatcdgff frgkkvviig ggdsameeat fltkfanevq vihrrdelra
      181 skimqerakg ndkvtwalnk tpvemvsdgm kitgvkvkdn esgeeeliet dgifvaighn
      241 pnteflkgkl dmddkgyilv dpgttntnip gvfacgdvqd qkyrqaitaa gtgcmaamds
      301 erflegeatv dwsqnls
//
LOCUS       WP_128526026             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Halobacillus litoralis].
ACCESSION   WP_128526026
VERSION     WP_128526026.1
KEYWORDS    RefSeq.
SOURCE      Halobacillus litoralis
  ORGANISM  Halobacillus litoralis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Halobacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Halobacillus litoralis"
                     /db_xref="taxon:45668"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34699
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseeriydvi iagagpagmt aavytsranl dtlmiergvp ggqmantedv enypgfesil
       61 gpdlsnkmfe hakkfgaeya ygdikeiidg keyktvragn keykaravii ttgaqykelg
      121 vqgekelggr gvsycavcdg affrnkelvv vgggdsavee gvyltrfask vtivhrrdel
      181 raqkilqdra fdnekidfiw dtvvktinek dgkvgsvtlh nkktdeeydf dtngtfiyig
      241 mnplsepfvs lgitneqgyi etdenmetkv pgvfaagdir ekelrqivta tgdgsiaaqs
      301 sqhyienlle elkvvn
//
LOCUS       WP_128528825             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_128528825
VERSION     WP_128528825.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33296
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqn klqarvaegk ivlklnaevd evlgdtmgvt gvclktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_128534971             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mucilaginibacter gilvus].
ACCESSION   WP_128534971
VERSION     WP_128534971.1
KEYWORDS    RefSeq.
SOURCE      Mucilaginibacter gilvus
  ORGANISM  Mucilaginibacter gilvus
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Mucilaginibacter gilvus"
                     /db_xref="taxon:2305909"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34152
     Region          9..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqdtehvkc liigsgpagy taaiyasrad lkpvmytgml aggqltqttd venfpgypdg
       61 imgpemmedf rkqaerlgtd irfgyvssvd fsslphkvvv desrtiladt viistgasak
      121 wlgleseqky sgfgvsacav cdgfffkged vaivgagdta aeeatylakl arkvymivrr
      181 defraskamm hrvlntanie ilyntdttei lgdgqsvngv kvcnnvtnet tvldvtgffv
      241 aighkpntdi frgvihmdet gyiltrpgst etnvegvfcc gdaqdhiyrq avtaagtgcm
      301 aaidaeryla akehvvta
//
LOCUS       WP_128537642             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Lacticaseibacillus paracasei].
ACCESSION   WP_128537642
VERSION     WP_128537642.1
KEYWORDS    RefSeq.
SOURCE      Lacticaseibacillus paracasei
  ORGANISM  Lacticaseibacillus paracasei
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lacticaseibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Lacticaseibacillus paracasei"
                     /db_xref="taxon:1597"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34065
     Region          5..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 makkydvivi gagpggmtaa lyasranlsv lmldrgvygg qmnntaeven ypgfksilgp
       61 dlgqkmydga tqfgaeyayg nvvsvqnrga vklvktdede yeakaiviat gaehkklgvp
      121 geeaysgrgv sycavcdgaf fkdrelavig ggdsaieegl yltqmakkvt vihrrdqlra
      181 qqiiqkrafa ndkmhfvwna qvqeiqgddm kvtgvkyrdk etgeehilpv agvfiyvgim
      241 pmteafqdlg vldehgwipt dehmrtkvpg vfaigdvrak dlrqittavg eggtagqgvf
      301 nyiqslndan ieika
//
LOCUS       WP_128546729             325 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Larkinella soli].
ACCESSION   WP_128546729
VERSION     WP_128546729.1
KEYWORDS    RefSeq.
SOURCE      Larkinella soli
  ORGANISM  Larkinella soli
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Spirosomataceae; Larkinella.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Larkinella soli"
                     /db_xref="taxon:1770527"
     gene            1..325
                     /gene="trxB"
     Protein         1..325
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34737
     Region          8..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttekvncli igsgpagyta aiyasragln pvlyqgaqpg gqltitnevd nfpgypdgve
       61 gpqlmndler qaarfgteir ygvvtavdfs gyphkaivdd qheitanavi istgaaakwl
      121 glpsemrlng rgvsacavcd gfffrgqdva ivgagdtaae easylaklcr kvymlvrrse
      181 mraskfmqnr vktlpnieil wnteteevlg eeevtgvrvk nvvtgessvl evsgffvaig
      241 hkpnteifks svaldesgyi itekgstrtn ipgvfacgda qdniyrqavt aagtgcmaal
      301 daerflalke sehpavdrla evqtl
//
LOCUS       WP_128563288             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Methylobacterium crusticola].
ACCESSION   WP_128563288
VERSION     WP_128563288.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium crusticola
  ORGANISM  Methylobacterium crusticola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Methylobacterium crusticola"
                     /db_xref="taxon:1697972"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39234
     Region          1..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavltetd paeprvaavp etvkkykalg advtvqsgag rtagvpdaey eaagaaiapd
       61 araaadgadi vlkvrrpsae elpalkrgaa vvaimdpygh eaevramaea gvsafamelm
      121 pritraqvmd vlssqanlag yravvdgaat ygralpmmmt aagtvpaari fvmgagvagl
      181 qaiatarrlg avvtatdvrp aakeqveslg akfvavedde fkqaetaggy akemsaeykk
      241 kqaelvathi akqdivitta lipgrpaprl vsgdmvaamr pgsvlvdlav erggnvegvk
      301 adevvetgng vkivgyanvp grlaatassl yarnlyafve tlvdkaaktl avkwddelvk
      361 atcltrdgav vhpnfqpka
//
LOCUS       WP_128555985             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces triticagri].
ACCESSION   WP_128555985
VERSION     WP_128555985.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces triticagri
  ORGANISM  Streptomyces triticagri
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Streptomyces triticagri"
                     /db_xref="taxon:2293568"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33536
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmnttdve nfpgfqdgim
       61 gpelmdnmra qserfgaelv pddvvavdlt gdiktvtdta gtvhqakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vvgggdtame eatflsrfak svtivhrrds
      181 lraskamqdr afadpkikfa wdsevaaihg dpkltgltlr ntktgetsel avtglfiavg
      241 hdprtelfkg qldlddegyl kveapstrtn ltgvfaagdv vdhtyrqait aagtgcsaal
      301 daerylaala dsetaavtv
//
LOCUS       WP_128563779             334 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Methylobacterium crusticola].
ACCESSION   WP_128563779
VERSION     WP_128563779.1
KEYWORDS    RefSeq.
SOURCE      Methylobacterium crusticola
  ORGANISM  Methylobacterium crusticola
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Methylobacterium crusticola"
                     /db_xref="taxon:1697972"
     gene            1..334
                     /gene="trxB"
     Protein         1..334
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35613
     Region          17..319
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msttptplhr evtharlviv gsgpagytaa iyaaramvep llisgfqpgg qlmittdven
       61 ypgfaeaiqg pwlmeqmrlq aehvgtrivs eyiarvdlkq rpfrleadsg avytcdalvi
      121 atgaqakwlg lpseaafqgf gvsacatcdg fffrgkevvv vgggnsavee alylanlask
      181 vtvvhrrdaf raerilqerl fkhpnvevvw nhaveeicgr taptpsvthl rlrdtrtgal
      241 terrtdgvfv aighqpatgl fegqlpmrag gylevapgtt ttaipgvfaa gdvtddvyrq
      301 aitaagmgcm aaleaekyla nlaigetprq aaae
//
LOCUS       WP_128580751             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Neisseria flavescens].
ACCESSION   WP_128580751
VERSION     WP_128580751.1
KEYWORDS    RefSeq.
SOURCE      Neisseria flavescens
  ORGANISM  Neisseria flavescens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Neisseriales; Neisseriaceae; Neisseria.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Neisseria flavescens"
                     /db_xref="taxon:484"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33635
     Region          6..311
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 msnhhkliil gsgpagytaa vyaaranlnp viitgveqgg qlmtttevdn wpadaegvqg
       61 pelmarfqah aerfgtemif dqihtvdlqn rpftlkgdmg eytcdaliva tgasakylgl
      121 pseetfagkg vsacatcdgf fykkqdvavv gggntavgea lylaniantv tlihrrdsfr
      181 aekimvdklm qrveegkiil klnssvdeil gdesgvtgar lkhndsstee iavkgvfiai
      241 ghkpntdifk gqldmdetgy lktkggtgdn vgatniegvw aagdvkdhty rqaitsaasg
      301 cqaaldaerw ldrhgv
//
LOCUS       WP_128590067             333 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paraburkholderia
            kirstenboschensis].
ACCESSION   WP_128590067
VERSION     WP_128590067.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia kirstenboschensis
  ORGANISM  Paraburkholderia kirstenboschensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Paraburkholderia kirstenboschensis"
                     /db_xref="taxon:1245436"
     gene            1..333
                     /gene="trxB"
     Protein         1..333
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35447
     Region          5..320
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpatstkhak vlilgsgpag ytaavyaara nlapvlvtgl aqggqlmttt dvenwpadan
       61 gvqgpelmar flehaerfnt eiifdhihta klnekpirli gdsgeytcds liistgasaq
      121 ylglpseeaf mgkgvsacat cdgffykqqh vavigggnta veealylsgi akkvtvihrr
      181 dkfraepili drllakekeg vveikwnhtl devtgdqsgv tglrvkhtqt gettdialqg
      241 lfvaighkpn tdifegqlem kngyiitkgg lngfatatsv pgvfaagdvq dhvyrqaits
      301 agtgcmaald aqryletine magehamsqe aer
//
LOCUS       WP_128594291             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Paraburkholderia kirstenboschensis].
ACCESSION   WP_128594291
VERSION     WP_128594291.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia kirstenboschensis
  ORGANISM  Paraburkholderia kirstenboschensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia kirstenboschensis"
                     /db_xref="taxon:1245436"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39290
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,299,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr ahetrvaatp etvkkyvgqg hrvtiqsgag agasfpddaf taagaeivda
       61 asafgaelvl kvqspteael pllkrgavlv gmldpfnaen alklaaagvt afaleaaprt
      121 traqsldvls sqaniagyka vllaatlypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpyetdee reaaqgvggy arpmppswlq
      241 rqsalvhera kqadvvista lipgraaptl isvdtvqamk pgsvlvdlaa grgadyegqr
      301 ggncpltead kvvvkhgvti vgytnlasmv padasslyar nlldflkliv tkegalnidl
      361 addivaatll ardgevarka
//
LOCUS       WP_128604428             373 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Pseudomonas].
ACCESSION   WP_128604428
VERSION     WP_128604428.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     Protein         1..373
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38534
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpletq tgetrvaatp etikkligqg hkvtvqsgag inasvidsay eaagatigsa
       61 sdafgaelil kvvapsdsel aliksgtvvv gmlnpfsnet iakmaecgit afaleaaprt
      121 sraqsldvls sqaniagyka vllaahhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf vdvpyetdee recavgvggy arpmpaswmq
      241 rqavavhera kqadivitta lipgrkaptl lsaqtvaqmk pgsvvidlaa aqggncpltv
      301 adqvvvengv tivgptnlaa avaadasaly arnlldfmkl lfdkegqlvi nleddivaac
      361 lmcrdgqivr kng
//
LOCUS       WP_128611381             478 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: ammonia-forming nitrite reductase cytochrome c552
            subunit [Citrobacter].
ACCESSION   WP_128611381
VERSION     WP_128611381.1
KEYWORDS    RefSeq.
SOURCE      Citrobacter
  ORGANISM  Citrobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Citrobacter"
                     /db_xref="taxon:544"
     gene            1..478
                     /gene="nrfA"
     Protein         1..478
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53594
     Region          21..478
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mariksrvrr ffslllpllf isavhaeqts vpaktvtvea knetfapqhp dqylswkats
       61 eqsaredala edprlvilwa gypfsrdynk prghayavtd vretlrtgap ktaedgplpm
      121 acwsckspdv arliqkdged gyfhgkwarg gpeivnnlgc adchntaspd fakgkpeltl
      181 srpyaerame aigkpfekag rfdqqsmvcg qchveyyfdg knkavkfpwd dgmkvenmek
      241 yydniafsdw tnslsktpml kaqhpeyetw sagihgknnv tcidchmpkv qnaegkiytd
      301 hkignpfdnf pqtcanchtq dkaslqkvva erkqaihdlk ikvedqlvra hfeakaawda
      361 gateaemkpi ledirhaqwr wdlsiashgi hmhapeeglr mlgsamdkaa dartklvrll
      421 atkgitheip lpdistkeka qaaiglnmqq inaekqdfik tvipqweeqa rkngllsq
//
LOCUS       WP_128607948             319 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [unclassified
            Pseudomonas].
ACCESSION   WP_128607948
VERSION     WP_128607948.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudomonas
  ORGANISM  unclassified Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="unclassified Pseudomonas"
                     /db_xref="taxon:196821"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33840
     Region          1..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msaaqhhrli ilgsgpagys aavyaaranl kpvvitgiqa ggqltttvev dnwpgdvegl
       61 tgpilmermq khaerfatqi vydhihtakl qqrpfeltgd sgtytcdali iatgasaqyl
      121 glpseetfag kgvsacatcd gffyrnqvva vvgggntave ealylsniak evhlihrrdk
      181 lrsekilqdk lfekaangni rlhwnqnlde vlgdasgvtg arlrdshtde ikelaltgvf
      241 iaighkpntd lfvdqlkmhn gyllvkggse gnatataiag vfaagdvadh vyrqavtsag
      301 agcmaaldae kylddipav
//
LOCUS       WP_128627064             423 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Borborobacter arsenicus].
ACCESSION   WP_128627064
VERSION     WP_128627064.1
KEYWORDS    RefSeq.
SOURCE      Borborobacter arsenicus
  ORGANISM  Borborobacter arsenicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Borborobacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Borborobacter arsenicus"
                     /db_xref="taxon:1851146"
     Protein         1..423
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43247
     Region          4..368
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(17,75,94,291,318,320)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(46,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,325..326,330,
                     333..334)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mgqtvfipre idaneprvaa spdtvkrlvs lgldviveag agtlsripda dfakagasig
       61 kaadagkadv vlkvrrptea elkaykngaa viaimdpygn epavaalaka gvtafamefm
      121 pritraqvmd vlssqanlag yqavidgaae ydralpmmmt aagtvpaaki fimgvgvagl
      181 qaiatarrlg avvtatdvrp aakeqvaslg akfiavedee fkqaetaggy akemskeyqa
      241 kqaaltaehi akqdivitta lipgrpapkl vsaamlasmk pgsvivdlav erggnvegav
      301 agkvvttand vkivghlnma grvaasasll yaknlvafle tmidkdakai ainrddelvk
      361 atmltdagkv vhpnfansaa tpaakavkpe maaapkkaaa kkpaaakkpa arstagkask
      421 gda
//
LOCUS       WP_128627447             324 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Borborobacter arsenicus].
ACCESSION   WP_128627447
VERSION     WP_128627447.1
KEYWORDS    RefSeq.
SOURCE      Borborobacter arsenicus
  ORGANISM  Borborobacter arsenicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Borborobacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Borborobacter arsenicus"
                     /db_xref="taxon:1851146"
     gene            1..324
                     /gene="trxB"
     Protein         1..324
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34402
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttkhapvli igsgpagyta aiyaaramlk pvlmaglqqg gqlmittdve nypgfaepiq
       61 gpwlmeqmak qaehvgteiv ndlitevdld vrpfrlkgds gtqytcdalv iatgaqakwl
      121 gipseqtymg fgvsacatcd gffyrgkdva vvgggntave ealylanlar svtvihrrse
      181 fraerilrer lakaenvkvi wdtvvdeitg tpgkpplpps asglklrnvv tgaetllpvd
      241 gvfvaighap avelfvgklk qkpngylwte pdstrtsvpg vfaagdvtdd vyrqavtaag
      301 lgcmaaleae kylagvevhr eaae
//
LOCUS       WP_128627863             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Borborobacter arsenicus].
ACCESSION   WP_128627863
VERSION     WP_128627863.1
KEYWORDS    RefSeq.
SOURCE      Borborobacter arsenicus
  ORGANISM  Borborobacter arsenicus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Phyllobacteriaceae; Borborobacter.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Borborobacter arsenicus"
                     /db_xref="taxon:1851146"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39223
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(14,74,93,290,317)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(43,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,280..281,323..324,328,
                     331..332)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,230,241,
                     258..260,267,269)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhiavlsdkm tdarvaatpe tvrkyetlgg kvsiqggagg gagiadkdfe dagarlvpda
       61 isvvkdadiv lavnrpsgdv irackpgaiv iatmdphrpe agldimasag vsafamelmp
      121 ritraqamdv lssqanlsgy ravidasaef trslpmmmta agtvpaaqif vmgagvaglq
      181 aiatarrlga vvsatdvrpa akeqveslga rfvaieddef kaaeasggya kemskeyqak
      241 qaelvathig rqdivittal ipgrpapklv tqamietmra gsvlvdlave rggniegska
      301 geivttargv kiignstisk vaatasnlya rnlysfvstm vdqsksglav dwddelvkst
      361 nltrdgaivh pafakalps
//
LOCUS       WP_128629947             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus oralis].
ACCESSION   WP_128629947
VERSION     WP_128629947.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus oralis
  ORGANISM  Paenibacillus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paenibacillus oralis"
                     /db_xref="taxon:2490856"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33460
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksiiigtg pagltaaiyl aranlnplii egpqpggqlt tttevenfpg fpegimgpel
       61 mdnmrkqaer fgaefrtgwv nsvdmskrpf klqvegigel vtetlvlstg atakylgipg
      121 eqdnvgrgvs tcatcdgfff rgkeiivigg gdsaleeagf ltrfaakvtl vhrrdelrgs
      181 kimqdraran ekiemalnrt pleviageng vtglkvrnna tgeeevlnas gvfvaighqp
      241 ntaflggqid tdangyivvk pgtsetnvpg vfacgdvqds ryrqaitaag sgcmaaidce
      301 kyienlehet aaaaak
//
LOCUS       WP_128631011             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus oralis].
ACCESSION   WP_128631011
VERSION     WP_128631011.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus oralis
  ORGANISM  Paenibacillus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus oralis"
                     /db_xref="taxon:2490856"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33774
     Region          6..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrktmvigtg pagltaaiyl aranlspivi egtqpggqlt tttevenfpg fpegimgpel
       61 mdnmrkqaer fgaefrngwv eqvdfskrpf kvkleggeel eaeaviistg asakylgipg
      121 eqdnvgrgvs tcatcdgfff rgkkiivvgg gdsameeanf ltrfatevtv vhrreelras
      181 kimqdrargn gkirwalnrt plevatdetg vvkglkvrnn aygqeellea qgvfvaight
      241 pntkflggai atddhgyiav kpgttetnvp gvfacgdvqd mryrqaitaa gsgcmaamdc
      301 ekflegsmvh dwsgn
//
LOCUS       WP_128638751             310 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhodococcus opacus].
ACCESSION   WP_128638751
VERSION     WP_128638751.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     gene            1..310
                     /gene="trxB"
     Protein         1..310
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33203
     Region          6..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnsprdviii gggpagytaa iytaranlhp lvfegtqygg almqtteven fpgfvegiqg
       61 pelmdtlrkq aerygaelia rdvstvdlgd eikrvstddr qytaktvvla mgsayralam
      121 pnekrlsghg vswcatcdgf ffrdqhiavi gggdsaleea mfltrfaasv tvihrrdtlk
      181 askimqeraf anskilflwn svaedvigde qvaglvvrdt vtdqlstlrv tgvfiaighd
      241 prnelvhgqv alddagyvlt egrtsrtpvs gvfacgdlvd htyrqaitaa gsgcsaaldv
      301 erylaaagsh
//
LOCUS       WP_128632928             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus oralis].
ACCESSION   WP_128632928
VERSION     WP_128632928.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus oralis
  ORGANISM  Paenibacillus oralis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Paenibacillus oralis"
                     /db_xref="taxon:2490856"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33172
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksviigtg pagltaaiyl aranmnplvi egpepggqlt ttteienfpg fpegimgpql
       61 menmrqqakr fgaefytgwv nkvdlskrpf klhvegkgei itetliistg asakylgipn
      121 ekanigrgvs tcatcdgfff rnkelivvgg gdtaleeany ltrftskvil vhrrdelras
      181 kimqdraran gkiewalnrt pveviardhg vtglkvqnna tgedevipan gvfvaighhp
      241 ntdflegqik tdangyiitt pgttethipg vfacgdvqds ryrqaitaag sgamaaidse
      301 kfiesned
//
LOCUS       WP_128641668             335 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Rhodococcus].
ACCESSION   WP_128641668
VERSION     WP_128641668.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus
  ORGANISM  Rhodococcus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rhodococcus"
                     /db_xref="taxon:1827"
     gene            1..335
                     /gene="trxB"
     Protein         1..335
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35697
     Region          7..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdsprnviii gggpagytaa iytgradlnp lvvegtqygg almqtteven fpgfvegiqg
       61 pelmdtlrkq aarygadllt tdvsavdltg diktvtigdn tfeartvila mgsayrnlgl
      121 pneqrlsghg vswcatcdgf ffrdqhiaiv gggdsaleea mfltrfassv tvvhrrdtlr
      181 askimqeraf anpkirflwn svpedvvgdq evtgllvrdt gtgeqstvpv tgvfiaighd
      241 prhelvhgqi plddegyvlt egrssrttvs gvfacgdlvd htyrqaitaa gsgctaaldv
      301 eryladtaag gavadqqrpp npnqpipvrp hrqgn
//
LOCUS       WP_128641777             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus opacus].
ACCESSION   WP_128641777
VERSION     WP_128641777.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37980
     Region          13..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqsasta rptvgvvres ndgerrvalv pkivasliak gvdvvvesga glgalipdel
       61 yteagakiad pwsadvivkv appsdeevgr lhagqtligf laprnqdnqv aalksagvaa
      121 faveaipris raqvmdalss qanvsgyksv llaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrat gydvrpevad qvrsvgaqwl dlgidaageg gyarelteqe
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaaveg mkpgsvvvdl agetggncel
      301 tepgqtvvkh gvticsplnl pasmpehase lysknisall elmlvdgala pdfsdevlaa
      361 scvtreegvs
//
LOCUS       WP_128642263             370 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus opacus].
ACCESSION   WP_128642263
VERSION     WP_128642263.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     Protein         1..370
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37985
     Region          13..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(26,81,100,293,319,321)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(55,133..134,143..144,147..148,151..152,154..155,
                     157..162,164,166..168,171,194..195,283..284,326..327,331,
                     334..335)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(128..129,133,136,139,180..183,203..205,233,244,
                     261..263,270,272)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(130..131,133,143,186..187,194,210..211,213..216)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(163..167,170,173,196,198)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdisrsvalp pptvgvvres ndgerrvalv pkivasliak gvdvvvesga glgalipdel
       61 yteagakiad pwsadvivkv appsdeevgr lhagqtligf laprnqdnqv aalkaagvaa
      121 faveaipris raqvmdalss qanvsgyksv llaasestrf fpmlttaagt vkpatvlvlg
      181 vgvaglqala takrlggrat gydvrpevad qvrsvgaqwl dlgidaageg gyarelteqe
      241 raqqqqaled aikgfdvvit talvpgrpap rlvtaaavgg mkpgsvvvdl agetggncel
      301 tepgrtvvkh gvticsplnl pasmpehase lysknisall elmlvdgala pdfsdevlaa
      361 scvtrdpegh
//
LOCUS       WP_128643995             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Rhodococcus opacus].
ACCESSION   WP_128643995
VERSION     WP_128643995.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus opacus
  ORGANISM  Rhodococcus opacus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rhodococcus opacus"
                     /db_xref="taxon:37919"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34980
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtspttardl iivgsgpagy tagvyaarae lepllfegtq fggalmttte venfpgfrag
       61 imgpelmdem reqakrfgad irtedveaid ltgpikkvvv ngetyqahav ilamgaaary
      121 lgipgeerll grgvsacatc dgfffkdqdi vvvgggdsam eeatfltrfa nsvtvvhrre
      181 efrasrimle rakanakirf vtnaepvevl gegrvtglvi rdtvtgeqst ldvtgmfvai
      241 ghdprselvk gqvdlddagy vrvaspstat srggvfaagd lvdhiyqqai taagtgcsaa
      301 mdaerwlaer gditantvaa ehpadttvga ls
//
LOCUS       WP_128645158             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Rhodococcus sp. BS-15].
ACCESSION   WP_128645158
VERSION     WP_128645158.1
KEYWORDS    RefSeq.
SOURCE      Rhodococcus sp. BS-15
  ORGANISM  Rhodococcus sp. BS-15
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Nocardiaceae; Rhodococcus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Rhodococcus sp. BS-15"
                     /db_xref="taxon:1304954"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37975
     Region          16..369
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(29,84,103,296,322,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(58,136..137,146..147,150..151,154..155,157..158,
                     160..165,167,169..171,174,197..198,286..287,329..330,334,
                     337..338)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(131..132,136,139,142,183..186,206..208,236,247,
                     264..266,273,275)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(133..134,136,146,189..190,197,213..214,216..219)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(166..170,173,176,199,201)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mdtsqstekg sgsttvvgvv resgegerrv alvpkivasl tgkgvaivve sgaglgalip
       61 delyvaagat igdpwsadvv vkvappsdae iakltsgstl igflaprnae nsigalkaag
      121 vqafaveaip risraqvmda lssqanvagy kavllaases trffpmltta agtvkpatvl
      181 vlgvgvaglq alatakrlgg rptgydvrpe vadqvrsvga qwldlgidaa geggyarelt
      241 edervqqqka leeaikgfdv vittalvpgr paprlvtaaa vegmkpgsvv vdlagetggn
      301 celtepgetv vkhdvticsp lnlpasmpeh aselysknis allelmlvdg klapdfsdev
      361 lagacvtrek en
//
LOCUS       WP_128663336             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_128663336
VERSION     WP_128663336.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33692
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevkhsrli ilgsgpagyt aavyaaranl kpvvitgiqp ggqlttttev dnwpgdvegl
       61 tgpalmtrmq qhaerfdtei vydhihtael qqrpftlkgd sgtytcdali iatgasaqyl
      121 gmsseeafmg kgvsacatcd gffyrnqvvc vvgggntave ealylaniak evhlihrrdk
      181 lrsekilqdk lfdkaengnv rlhwnttldd vlgdasgvtg vrlkstidgs tselslagvf
      241 iaighkpntd lfqgqlemrd gylrihggse gnatqtsieg vfaagdvadh vyrqaitsag
      301 agcmaaldae kylddh
//
LOCUS       WP_128655399             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paenibacillus sp. 598K].
ACCESSION   WP_128655399
VERSION     WP_128655399.1
KEYWORDS    RefSeq.
SOURCE      Paenibacillus sp. 598K
  ORGANISM  Paenibacillus sp. 598K
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Paenibacillus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paenibacillus sp. 598K"
                     /db_xref="taxon:1117987"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33929
     Region          2..305
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myksiiigtg pagltaaiyl aranlnplii egpepggqlt tttevenfpg fpdgimgpel
       61 manmrkqaer fgaefktgwv nkvdtskrpf tlqveghgel qaetliistg asakylgipg
      121 erdnvgrgvs tcatcdgfff rgkkivvvgg gdsameeanf ltrfasevvl vhrrdemras
      181 kimqdraren pkitwqlnrt plevdagplg vtalkvrnne tgeeeaietn glfvaightp
      241 ntkflegqle tdetgylvvk pgttetnvpg ifacgdvqdh kyrqaitaag sgcmaaldce
      301 kflegsmvhd wsqsl
//
LOCUS       WP_128664305             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_128664305
VERSION     WP_128664305.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33263
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg xeeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_128667458             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Pseudomonas aeruginosa].
ACCESSION   WP_128667458
VERSION     WP_128667458.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38594
     Region          1..365
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mqigvpleth agetrvsatp etvkkligqg hqvivqsgag vnasqpdsay eaagatigsa
       61 aeafgadlvl kvvapsaael aqmksgavlv gmlnpfdnen iarmaergit afaleaaprt
      121 sraqsldvls sqaniagyka vmlaanhypr fmpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgsvi easdvrpavk eqieslgakf vdvpyetdee recaegvggy arpmpaswme
      241 rqakavhera kqsdivitta lipgrkaptl lheatvaemk pgsvvidlaa aqggncplte
      301 adqvvvrhgv tivghsnlaa lvpadasaly arnildflkl tlnaegfsvn leddivaacl
      361 mcrdgqavrk ng
//
LOCUS       WP_128668119             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_128668119
VERSION     WP_128668119.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33380
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq agsqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdtmgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvnggre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_128685866             307 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas aeruginosa].
ACCESSION   WP_128685866
VERSION     WP_128685866.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..307
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=34704
     Region          5..170
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 mgvfdlfskr qkrargevpd vyvyddlpqp lrvqivhiid dafgtdrygt snaeeaygfv
       61 kntlcrefgv feltrypksd qdsifnfflq eesieraldv velcfkvmhi hiaenatyrh
      121 qtvrkiepnd aiaelnerfk ehgvgyqfes geiirvdsqf lhseavkptl avlsdksfeg
      181 aneeflkahe hyrhgrykec lvdalkafes tmkticslrg wptqssdtak nliatcmskg
      241 lfppyfesqf asirsllesg vptvrnkngg hgqgaapvav peylarytln ltattilfmv
      301 eshqatk
//
LOCUS       WP_128687092             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Oenococcus sicerae].
ACCESSION   WP_128687092
VERSION     WP_128687092.1
KEYWORDS    RefSeq.
SOURCE      Oenococcus sicerae
  ORGANISM  Oenococcus sicerae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Oenococcus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Oenococcus sicerae"
                     /db_xref="taxon:2203724"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33448
     Region          5..285
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqkydvvii gagpagmtaa tyasranlsv lmidkgiygg qmndtaeven ypafdsilgp
       61 dlaekmyass trfgaeyvfg evqdvidhgn tktvvtddet yeakvivias gathrhigvl
      121 gedkysgrgv sycavcdgaf fknedvavig ggdsaieeai ylanlakhvt iihrrdtlra
      181 skiaqkrafs tknidfswnk qteaivgdde kvtavkvldt kenqesivpa sgifvyvgit
      241 pntqglnklg vlddqgwvet desmqtkvpg vfavgdvrkd sirqiaaavg dgavagkllf
      301 dyiqtlsdsq vea
//
LOCUS       WP_128699247             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Candidatus Velamenicoccus
            archaeovorus].
ACCESSION   WP_128699247
VERSION     WP_128699247.1
KEYWORDS    RefSeq.
SOURCE      Candidatus Velamenicoccus archaeovorus
  ORGANISM  Candidatus Velamenicoccus archaeovorus
            Bacteria; Pseudomonadati; Candidatus Omnitrophota; Candidatus
            Velamenicoccus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Candidatus Velamenicoccus archaeovorus"
                     /db_xref="taxon:1930593"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33779
     Region          3..297
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvydvvivga gpagltaaly agrsklktki lekeavggqi lltelienfp gvyrmnsfdw
       61 vevvkkqlad ldqvelqesa gvdklekngk efrlhvhsda aggpevleak siilatgarp
      121 rrlgvpgenk ltgrgvsyca tcdgplfrdk nvvvvggget aleealylsr fvktvtivhr
      181 rqglratali qervakdpki rlklefvple vvgasrveal kirnvadkhe eslacdgvfv
      241 figfnpetaf legmlettqe gyiltdermm asvegvfvcg dcrkrplnqv vtacsegaia
      301 ayaaarfleq at
//
LOCUS       WP_128704363             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Enterococcus faecium].
ACCESSION   WP_128704363
VERSION     WP_128704363.1
KEYWORDS    RefSeq.
SOURCE      Enterococcus faecium
  ORGANISM  Enterococcus faecium
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Enterococcaceae; Enterococcus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Enterococcus faecium"
                     /db_xref="taxon:1352"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33347
     Region          2..304
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydvivigag pagmtaalya srsnlsvlmi eqgapggqmn ntaeienypg fdsimgpdla
       61 ykmyesvsrf gtenaygivq dikdhgshke vicedksyeg ktviiatgci hrklgvpgee
      121 efagrgvsyc avcdgaffrn krlvvigggd saveeaiylt qfasevvivh rrdelraqki
      181 iqdrafanek isfmwdtvvd eivgnemvvt gvkarnvktg nefdlaadgv fiyvgldplt
      241 apfrevgltn eagwiptdne mktnmpgvfa igdvrekdlr qittavgdgg iagqqvykyl
      301 esleetta
//
LOCUS       WP_128702630             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Paramuribaculum intestinale].
ACCESSION   WP_128702630
VERSION     WP_128702630.1
KEYWORDS    RefSeq.
SOURCE      Paramuribaculum intestinale
  ORGANISM  Paramuribaculum intestinale
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Muribaculaceae; Paramuribaculum.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Paramuribaculum intestinale"
                     /db_xref="taxon:2094151"
     gene            1..314
                     /gene="trxB"
     Protein         1..314
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33845
     Region          6..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnqihtkcli igsgpagfta aiytsranmk plvyaghqpg gqltitteve nfpgyhegvt
       61 gtqlmadlek qaarfgadir qgiitsvdfs qhplraiadd nteitadtvi istgataryl
      121 glpdeerykg mgvsacatcd gffyrrkrva vvgggdtace ealylsnias evflivrkdy
      181 lraskvmqrr veekanitvl fnantlglyg ddylegaqlv efastdkerv ynlpvdgffl
      241 aighkpatdi frpwieldea gyiktegqst rtnvagvfaa gdvadpnyrq aitaagsgck
      301 aaldaerylt eqgg
//
LOCUS       WP_128718743             339 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Brevundimonas diminuta].
ACCESSION   WP_128718743
VERSION     WP_128718743.1
KEYWORDS    RefSeq.
SOURCE      Brevundimonas diminuta
  ORGANISM  Brevundimonas diminuta
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Caulobacterales; Caulobacteraceae; Brevundimonas.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Brevundimonas diminuta"
                     /db_xref="taxon:293"
     gene            1..339
                     /gene="trxB"
     Protein         1..339
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35891
     Region          13..318
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtqakapart vrvaiigsgp agwtaaiyaa raslnpviia glqpggqlti ttdvenypgf
       61 aetiqgpwlm qqmqaqaehv gtevihdivt qadlsqrpfr ltldsgaeil aetviistga
      121 qakwlglase aeyqgfgvsa catcdgffyr gkqvvvvggg ntaveealfl tnfaetvtvv
      181 hrrdefraek ilqdrlfahp kikviwdvav eevvgvvdgv arnvtgvrlk nvktgeisei
      241 padgvfiaig hapsselfkg qletnsggyl rvkpgtaata iegvwaagdv tddvyrqavt
      301 aagmgcmaal eaarflaeed hkaaqhpish keaekigaw
//
LOCUS       WP_128730270             317 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Pseudoalteromonas].
ACCESSION   WP_128730270
VERSION     WP_128730270.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33822
     Region          1..314
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msdakhckll ilgsgpagyt aavyaaranl npvlitgmqq ggqlttttev enwpgdahgl
       61 tgpalmdrmk ehaerfetei ifdhinkvdv tkrpftltgd qgtytcdali iatgasakyl
      121 glesetafqg rgvsacatcd gffyrgqkva vvgggntave ealylsniae evhvihrrds
      181 frsekiladr lmdkaangnv vlhlnrtlde vlgdemgvtg irikdtdsda teqldlagvf
      241 iaighkpntd mfegqlemkd gylvvqsgln gnatqtsveg vfaagdvsdh iyrqaitsag
      301 tgcmaaldae rfldsqk
//
LOCUS       WP_128734011             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Pseudomonas aeruginosa].
ACCESSION   WP_128734011
VERSION     WP_128734011.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33419
     Region          4..316
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mpdtlrharv iilgsgpagy saavyaaran lkpllitgmq aggqltttte vdnwpgdphg
       61 ltgpalmqrm qehaerfete ivfdhihavd lagkpftlrg dngtytcdal ivatgasary
      121 lglpseqafm gkgvsacatc dgffyrnrev avigggntav eealylania srvtlvhrre
      181 tfraekilqd klqarvaegk ivlklnaevd evlgdamgvt gvrlktrdgg seeiavdgmf
      241 vaightpnts lfegqlalkd gylvvngrre gnatatnvpg vfaagdvadh vyrqaitsag
      301 agcmaaldve ryldsl
//
LOCUS       WP_128748313             307 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium sp. JN-9].
ACCESSION   WP_128748313
VERSION     WP_128748313.1
KEYWORDS    RefSeq.
SOURCE      Clostridium sp. JN-9
  ORGANISM  Clostridium sp. JN-9
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Clostridium sp. JN-9"
                     /db_xref="taxon:2507159"
     gene            1..307
                     /gene="trxB"
     Protein         1..307
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33281
     Region          5..284
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mahiydtiii gggpaglsag lyasrsrmdt liiekakygg qvtttdeien ypgstedttg
       61 sslsermrkq aeefgtkfvk devqevqleg svkvikcrke tyeaktiiia tganprlsgf
      121 knenelrgkg isycatcdad fftdldvavi gggdsaitea iyltkfaetv tvihrrdslr
      181 aakslqekaf anpkikfiwd svvdeaigde ileglvvrnv ktgektnvkf dgcfvfvgyn
      241 pisqlfegki nmdkkgyiit dedmrvnipg vyaagdvrvk slrqiitaaa dgaiaattae
      301 ayistlh
//
LOCUS       WP_128756918             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Leeuwenhoekiella aequorea].
ACCESSION   WP_128756918
VERSION     WP_128756918.1
KEYWORDS    RefSeq.
SOURCE      Leeuwenhoekiella aequorea
  ORGANISM  Leeuwenhoekiella aequorea
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Leeuwenhoekiella.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Leeuwenhoekiella aequorea"
                     /db_xref="taxon:283736"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34203
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maverikcli igsgpagyta aiyasradlk pimytgmepg gqlttttevd nfpgypdgid
       61 gptmmmqlqk qaerfgtevr igmitkidla qeaggihkav vdntteieae tviistgata
      121 rylglpseqr lrgggvsaca vcdgffyknq rvaivgggdt aaeeatylan icehvtmlvr
      181 kdemraskam qhrvtsrkni tvlyntevee vlgeqvvegl kminnetkev teiditglfi
      241 aighkpntdi fkgqlemddt gyiitepkst ktgkpgvfas gdvqdkdyrq aitaagsgcm
      301 aaldaeryls eiekpvea
//
LOCUS       WP_128767757             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arcticibacter tournemirensis].
ACCESSION   WP_128767757
VERSION     WP_128767757.1
KEYWORDS    RefSeq.
SOURCE      Arcticibacter tournemirensis
  ORGANISM  Arcticibacter tournemirensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Arcticibacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Arcticibacter tournemirensis"
                     /db_xref="taxon:699437"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34446
     Region          10..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msqetehvqc liigsgpagy taaiyaarad lkpvlytgiv pggqltqttd venfpgypeg
       61 imgpemmedf rkqaerfgte irfgyvtsvd fsgpphtvvi dehktitadt viiatgasak
      121 wlgleseqky ngfgvsacav cdgfffkgee vaivgagdta aeeatylakl cskvhmlvrr
      181 defraskamq nrvlnthnie ihyntetkei vgngqnvtgi rvynnkttee svinvsgffv
      241 aighkpntdi fkgwldmdet gylitkpgta mtniegvfac gdaqdkiyrq avtaagtgcm
      301 aaleaeryla ekefaete
//
LOCUS       WP_128772460             515 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Actinomyces oricola].
ACCESSION   WP_128772460
VERSION     WP_128772460.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oricola
  ORGANISM  Actinomyces oricola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Actinomyces oricola"
                     /db_xref="taxon:206043"
     Protein         1..515
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53305
     Region          1..514
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mrlgvpcesp gqrlvaatpq sverlvrlgy evcvergagh rarfhdadye aagaslvdgd
       61 aawgcelvlg vqapatsdld rltegatfig rldpgrhpel vealrargvt alaldavpri
      121 sraqamdvls sqanlagyra vieaaahfgr llngqvtaag kfppatayvi gagvaglaai
      181 gtayslgavv rgtdvrpeva dqvrsmgaef iavptaqdvs sdgyaqemsa dqaaraally
      241 aeqaarsdiv ittanipgrr apilldraai damrpgsvvv dmaaanggnt eltvpgevvt
      301 tdggviivgy tdlagrlpsq asqlygqnlv nlltlmtpgk dgrftldldd qivrtitvch
      361 dsetlwpppp vtvsaapsat papsadevar teaqeaaara rsrrnriigl alaslagaal
      421 ilvtpaavts hyivlalsii lgfhiisnvt palhtplmsv tnaisgiill gaisqvghsn
      481 lfistaafva vvlstinvfg gfavthrmla mfkkd
//
LOCUS       WP_128770332             380 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Arcticibacter tournemirensis].
ACCESSION   WP_128770332
VERSION     WP_128770332.1
KEYWORDS    RefSeq.
SOURCE      Arcticibacter tournemirensis
  ORGANISM  Arcticibacter tournemirensis
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Arcticibacter.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Arcticibacter tournemirensis"
                     /db_xref="taxon:699437"
     Protein         1..380
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40742
     Region          1..362
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,74,93,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,126..127,136..137,140..141,144..145,147..148,
                     150..155,157,159..161,164,187..188,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,126,129,132,173..176,196..198,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(123..124,126,136,179..180,187,203..204,206..209)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(156..160,163,166,189,191)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkigvlkesk llenrvaltp divnqlvkkg fniliesgag ersffpdesy elagakiaas
       61 vkevydcdvl lkvdapsvee agqmkegtac ismlhaylrp elieifiark itafsmdavp
      121 risraqkmda lssqaniagy kavilaadal gkvfplmmta agtvkpakvl ifgagvaglq
      181 aiatakrlga vvevsdvrpe tkeqveslgg rfltvegagd vkiqggyare vsqeflqkqk
      241 eliqskikea divittalvm grkspilvte emvksmksgs vivdlavesg gncelsqynk
      301 tivkygvtii geadlpsrvp vnasqlyaan istlllhlat pegfnlhlee eitkgtlith
      361 qgelvheftk svleknsnlv
//
LOCUS       WP_128773303             308 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Actinomyces oricola].
ACCESSION   WP_128773303
VERSION     WP_128773303.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces oricola
  ORGANISM  Actinomyces oricola
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Actinomyces oricola"
                     /db_xref="taxon:206043"
     gene            1..308
                     /gene="trxB"
     Protein         1..308
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32829
     Region          3..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mvhdvvivgs gpagytaaiy aaraqlkplv lagsvtagga lmntteveny pgfidgvqgp
       61 dlmgqmqeqa erfgaevrye dvtameltgd vkrvttdsgv yqartvivst gseyrklgld
      121 geerlsghgv sycatcdgff fkdqdivvvg ggdaameeat fltrfarsvt vvhrrdelra
      181 savmakramn dpkivfawns rvvalngrds lesvtledtr tgerrdlaat glfvaigqvp
      241 rselvarvld ldeagyikvd spsqrtaipg vfacgdvadp hyqqavtaaa sgcraaldae
      301 hylttlrp
//
LOCUS       WP_128774749             323 aa            linear   BCT 07-JUL-2024
DEFINITION  STM4504/CBY_0614 family protein [Pseudomonas syringae].
ACCESSION   WP_128774749
VERSION     WP_128774749.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas syringae
  ORGANISM  Pseudomonas syringae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Sato,Y., Takaya,A. and Yamamoto,T.
  TITLE     Meta-analytic approach to the accurate prediction of secreted
            virulence effectors in gram-negative bacteria
  JOURNAL   BMC Bioinformatics 12, 442 (2011)
   PUBMED   22078363
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF046078.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Pseudomonas syringae"
                     /db_xref="taxon:317"
     Protein         1..323
                     /product="STM4504/CBY_0614 family protein"
                     /calculated_mol_wt=36324
     Region          5..175
                     /region_name="AbiJ_NTD4"
                     /note="AbiJ N-terminal domain 4; pfam18863"
                     /db_xref="CDD:465890"
ORIGIN      
        1 maiidlyskr qgrerngvnd vytydefssk friqlsmmie ellggiedvy rggkprdaye
       61 glvkilrkey glshlvsaar sftpdyfsei hdflsvevdv ekvldavela yqlgnrfarh
      121 ssyrlaymdd sddhvdacie elngrfkeag ygyafveeni lrvdseflhs evvkpaihfl
      181 nfegfeaarn eflggydhyr hkrykealad agksfestmk iicglngwtf kptdgankli
      241 qvlvdkeflp sihqahlsgi htvlsagipt lrnkwgshgd gdtisevhpd vvayglhlta
      301 saiillgslq enhpnaiedk tki
//
LOCUS       WP_128775530             395 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Hansschlegelia zhihuaiae].
ACCESSION   WP_128775530
VERSION     WP_128775530.1
KEYWORDS    RefSeq.
SOURCE      Hansschlegelia zhihuaiae
  ORGANISM  Hansschlegelia zhihuaiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylopilaceae; Hansschlegelia.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Hansschlegelia zhihuaiae"
                     /db_xref="taxon:405005"
     Protein         1..395
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40824
     Region          1..367
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,75,94,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,127..128,137..138,141..142,145..146,148..149,
                     151..156,158,160..162,165,188..189,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(122..123,127,130,133,174..177,197..199,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(124..125,127,137,180..181,188,204..205,207..210)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(157..161,164,167,190,192)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mriavakevd aaeprvaltp davkklaglg geivvetgag lragatdeay ketgativgs
       61 raealkdadv llavrrpqpg gldglksgav vlavmdpygk adeigalaks gaalfamelm
      121 pritraqvmd vlssqanlag yravidaaae fgrafpqmmt aagtvppaka fvmgagvagl
      181 qaiatarrlg aqvsatdvrp aakeqvaslg akfvavedde frqaetaggy akemsaeykk
      241 kqaelvashi skqdivitta lipgrpaprl vttemvksmk pgsvvvdlav erggnvegak
      301 pdevvevagv kivghvnwag rlaasssaly aknlsaflet midketkslk vnwddelvka
      361 taltrdgavi hpilkpadap aeapkpaddq pkess
//
LOCUS       WP_128782270             476 aa            linear   BCT 07-JUL-2024
DEFINITION  ammonia-forming nitrite reductase cytochrome c552 subunit
            [Photobacterium chitinilyticum].
ACCESSION   WP_128782270
VERSION     WP_128782270.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium chitinilyticum
  ORGANISM  Photobacterium chitinilyticum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR03152.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Photobacterium chitinilyticum"
                     /db_xref="taxon:2485123"
     gene            1..476
                     /gene="nrfA"
     Protein         1..476
                     /product="ammonia-forming nitrite reductase cytochrome
                     c552 subunit"
                     /EC_number="1.7.2.2"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0042279 - nitrite reductase (cytochrome,
                     ammonia-forming) activity [Evidence IEA]"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53563
     Region          23..476
                     /region_name="nrfA"
                     /note="ammonia-forming cytochrome c nitrite reductase;
                     PRK11125"
                     /db_xref="CDD:236854"
ORIGIN      
        1 mrikwtrnta avaallsalc lstnanaate dsgktriepr nsqfaqshie qyktweatke
       61 seeiddalag dpnmvimwag ygfskdynka rghfyaitdv rqtlrtggpk daksgpmpma
      121 cwsckspdva rvidergedg yfegkwarlg aeinnpigcs dchntasedf aqgkpaltlt
      181 rpyvdramet igmkfedqsr fdqqaqvcgq chveyyftgp kksvkfpwdk gttvdemevy
      241 ydeiefkdwt hkvskapmlk aqhpgyetwr egihgknnvt cidchmpkvq nedgkvftdh
      301 kignpfdrfe dtcaqchtqd ketlksvvds rkasvqemkl raekqivaah feakaawdag
      361 ateeemkpil mdirhaqwrw dyaiashgvh mhapevalrv lgtaldkatd artkvvrlla
      421 tkgimeeiqi pdistkekaq qalgmdmdkm nadkaeflkt vapewnkqae vreasy
//
LOCUS       WP_128783618             403 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Photobacterium chitinilyticum].
ACCESSION   WP_128783618
VERSION     WP_128783618.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium chitinilyticum
  ORGANISM  Photobacterium chitinilyticum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Photobacterium chitinilyticum"
                     /db_xref="taxon:2485123"
     gene            1..403
                     /gene="trxB"
     Protein         1..403
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=43765
     Region          17..292
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
     Region          311..400
                     /region_name="CnoX"
                     /note="Chaperedoxin CnoX, contains thioredoxin-like and
                     TPR-like domains, YbbN/TrxSC family [Posttranslational
                     modification, protein turnover, chaperones]; COG3118"
                     /db_xref="CDD:442352"
ORIGIN      
        1 mselydviii gggsggmsag vyaargkmkt liieekrntg gqaattseme nypgileatg
       61 pqlmdmfrah cnkfgvefak glvteislae dgfiktlktn kgeeyqtksv ivatgatpri
      121 lgikgesefr gkgvsycatc dadfyedldv vvvgsgntav eesvfltkfv nkvtmivlhe
      181 qgildadrta qeqafsndki efvwnsvvee itgddlvggv klknlktsei semsadgvfm
      241 fvgtvpktdf ikglvaltpq gyvltnekqe tnvpgifsvg dvtdkflrqv vtaagdgava
      301 avaadryiee eenwrksvae fggtamvafw nplskeslev inqleqnckd npdqrvvtid
      361 tyksqnianr fdvtevpvvi rfdagqeakr vdvkdiaele tly
//
LOCUS       WP_128776622             322 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Hansschlegelia zhihuaiae].
ACCESSION   WP_128776622
VERSION     WP_128776622.1
KEYWORDS    RefSeq.
SOURCE      Hansschlegelia zhihuaiae
  ORGANISM  Hansschlegelia zhihuaiae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Methylopilaceae; Hansschlegelia.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Hansschlegelia zhihuaiae"
                     /db_xref="taxon:405005"
     gene            1..322
                     /gene="trxB"
     Protein         1..322
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34398
     Region          11..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mteqpighvr laiigsgpag wtaalyaara mlepvvisgl qpggqltitt dvenypgfae
       61 avqgpwlmeq mqaqaermgt rtlhdhvskv dfsrrpfvie tessgritad avvvstgaqa
      121 rwlgleseei fkgygvsaca tcdgfffrnk evmvvgggnt aleealfltn faskvtlvhr
      181 resfrgeril qdrvfqnpki evvwnatvge ilgggtppkv tgvklvdtrt gqttvrpcdg
      241 vfvaighqpa telfrgqldm kpsgylkvtp gttftnvpgv faagdvadet yrqavtaagm
      301 gcmaaldaer flaaeeaert aa
//
LOCUS       WP_128782084             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Photobacterium chitinilyticum].
ACCESSION   WP_128782084
VERSION     WP_128782084.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium chitinilyticum
  ORGANISM  Photobacterium chitinilyticum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Photobacterium chitinilyticum"
                     /db_xref="taxon:2485123"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34499
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msnvrhckll ilgsgpagyt aavyaaranl spvmvtgmqq ggqlttttev enwpgdaegl
       61 tgpalmdrmk ehaekfdtei ifdhinetdf sqrpfrlkgd dgeytcdali iatgasakyl
      121 gleseenfkg rgvsacatcd gffyrnqkva vvgggntave ealylsnias evhlihrrds
      181 frsekilikr lmdkvkngni ilhtdrtlde vlgddmgvta vrikdtksda tetlevmgaf
      241 iaighqpntg ifegqldman gyikvqsgte gnatqtsveg vfaagdvmdh iyrqaitsag
      301 tgcmaaldae ryldaleeqq
//
LOCUS       WP_128780344             332 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Curtobacterium flaccumfaciens].
ACCESSION   WP_128780344
VERSION     WP_128780344.1
KEYWORDS    RefSeq.
SOURCE      Curtobacterium flaccumfaciens
  ORGANISM  Curtobacterium flaccumfaciens
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Curtobacterium.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Curtobacterium flaccumfaciens"
                     /db_xref="taxon:2035"
     gene            1..332
                     /gene="trxB"
     Protein         1..332
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34983
     Region          4..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mrqliiigsg pagftagiya araelkpliv assvetggel tkttevenfp gfpegiqgpd
       61 lmikmqeqae kfgaevlydd avsvdltgkv kkvtvgsget yealaviyat gsayrhlglp
      121 deerlsghgv swcatcdgff frqkniavvg ggdsameeat fltrfadkvt vihrkdslra
      181 skimqdramn dpkiefawnk evtgitgdsa vegvtlkdtv tgeeselald glfiaigndp
      241 rthlihgqid iapegtiavq grssktnlpg vfaagdvidp syrqaitaag sgtvaaldae
      301 kylaelddtl tdeaegvapt epamvdviaa ra
//
LOCUS       WP_128790862             323 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_128790862
VERSION     WP_128790862.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34316
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytsa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmra qaerfgaeli pddivsvdlt geiktvtdta gtvhkakavi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdqdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqer afgdpkikfv wdsevaeiqg eqklsglklr nlksgelsel pvtglfiaig
      241 hdprtelfkg qldldeegyl kvvspstrtn vtgvfaagdv vdhtyrqait aagtgcsaal
      301 daerflaala dedqaepekt aav
//
LOCUS       WP_128803845             519 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [unclassified Streptomyces].
ACCESSION   WP_128803845
VERSION     WP_128803845.1
KEYWORDS    RefSeq.
SOURCE      unclassified Streptomyces
  ORGANISM  unclassified Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="unclassified Streptomyces"
                     /db_xref="taxon:2593676"
     Protein         1..519
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53165
     Region          13..518
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 msadasshhp pqligvvaes asgetrvaat patvrlllkl gyeavvetga geasgfddqa
       61 yveagarigd awdadvvlkv naptgseitr lregatvagl lapaqnpell qelsragvta
      121 laldavpris raqsmdvlss maniagyrav ieaahvfgrf ftgqvtaagk vppakvlvag
      181 agvaglaaig aasslgavvr atdprpevad qvrslggeyl pvdvvqeast dgyakatsad
      241 ydraaaelyh eqaqdvdivv ttalipgrpa prlltaadva amkpgsvivd maaamggnve
      301 gtvagrtvvt gngvtiigyt dlasrlpaqa sqlfgtnlan lvklltpgkd grltvdfddv
      361 vqravtvvrg geitwppppv pvsaapaaqt aeaapvetep erprltpalr fgliglgmla
      421 mfllvafapa qlaenftvfa lavvigyyvi gkvhhalhtp lmsvtnaisg ivvigallqi
      481 ghennlvtal scvailltsv nvfggfavtr rmlsmfskg
//
LOCUS       WP_128809540             316 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bacteroides rodentium].
ACCESSION   WP_128809540
VERSION     WP_128809540.1
KEYWORDS    RefSeq.
SOURCE      Bacteroides rodentium
  ORGANISM  Bacteroides rodentium
            Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
            Bacteroidaceae; Bacteroides.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Bacteroides rodentium"
                     /db_xref="taxon:691816"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33769
     Region          8..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mmetekvkcl iigsgpagyt aaiyagranl spvlyaglqp ggqlttttdv enfpgypqgi
       61 ggpelmedlr kqaerfgvdl rygvataanl aeapykitid dekvieaetl iiatgaaaky
      121 lgledekkya gmgvsacatc dgffyrkktv avvgggdtac eeavylagla akvylivrkp
      181 ylraskimqe rvmkhdkiev lfehnavglf gengvegvhl vqrmgepdek rydvaidgff
      241 laighkpnsd ifkpyvdtde igyivtepgt prtkvpgvfa agdvadphyr qaitaagtgc
      301 qaaieaeryl sakgli
//
LOCUS       WP_128827580             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Achromobacter mucicolens].
ACCESSION   WP_128827580
VERSION     WP_128827580.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter mucicolens
  ORGANISM  Achromobacter mucicolens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Achromobacter mucicolens"
                     /db_xref="taxon:1389922"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33969
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpthakvl ilgsgpagyt aavyaaranl npvlvtglaq ggqlmtttdv dnwpadadgv
       61 qgpdlmqrfq khaerfntem lfdhiakvdl skrpftltgd tgkvytcdal iiatgasaky
      121 lglpseqsfm grgvsgcatc dgffyrnqdv vvvgggntav eealylsnic rkvtlihrrd
      181 kfraepilvd klmskvengn melklfhtld evlgddsgvt gvrvrhvdtg atedmavtga
      241 fiaighqpnt eifqgqlemk dgyivtksgl sgmatmtsvp gvfaagdvqd hvyrqaitsa
      301 gtgcmaalda qrwlenagq
//
LOCUS       WP_128834200             305 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus sp. DD11].
ACCESSION   WP_128834200
VERSION     WP_128834200.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. DD11
  ORGANISM  Streptococcus sp. DD11
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Streptococcus sp. DD11"
                     /db_xref="taxon:1777879"
     gene            1..305
                     /gene="trxB"
     Protein         1..305
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33036
     Region          2..303
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtviigag pagmtaalya arsnlkvall ergiyggqmn ntadienypg yanisgpela
       61 ekmfeplenl gvehlfglve kiedhgdfke iiteddrfet ktvviasgan hrqlgvpgea
      121 eynsrgvsyc avcdgaffrd edllvvgggd saveeaiflt rfaksvtivh rrgelraqkv
      181 lqyrafanek iqfvwdsvve eihgddrkvt gvtfknvktg qeskaafggi fiyvgldpvs
      241 afaadlgild qagwivtddh mktavdgiya vgdvrqkdlr qittavgdga vagqevykyi
      301 tehas
//
LOCUS       WP_128833707             304 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptococcus troglodytae].
ACCESSION   WP_128833707
VERSION     WP_128833707.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus troglodytae
  ORGANISM  Streptococcus troglodytae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Streptococcus troglodytae"
                     /db_xref="taxon:1111760"
     gene            1..304
                     /gene="trxB"
     Protein         1..304
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32924
     Region          2..300
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mydtiiigsg pagmtaalya arsnlkvali eqgapggqmn ntsdienypg ydlisgpels
       61 mkmheplekf gvenlygivt avedqgnfkk vltddnsyet ktviiatgak hrplavagee
      121 tynsrgvsyc avcdgaffrg qdllvvgggd saveealflt rfankvtivh rrdelraqkv
      181 lqerafandk vdfiwdsvvk eikgndlkvt nvdienvktg qvsnhafggv fiyvgldpvs
      241 smvkelditd eagwiptddh mktkvagvfa igdvrqkdlr qittavgdga vaaqeayqyi
      301 vnny
//
LOCUS       WP_128827805             372 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Achromobacter mucicolens].
ACCESSION   WP_128827805
VERSION     WP_128827805.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter mucicolens
  ORGANISM  Achromobacter mucicolens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Achromobacter mucicolens"
                     /db_xref="taxon:1389922"
     Protein         1..372
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38600
     Region          1..366
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,317,319)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,324..325,329,
                     332..333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigipketr dgetrvaatp etvkkyvggk htvvvergag aaarypdday vaagatlgsa
       61 qdalgadlvm kvrapapeel phmkpgtvvi gmldpfdaeg laqlaaaglt gfaleaapri
      121 traqsldvls sqanlagyka vllaahhygr lipmmmtaag tlkaaravil gtgvaglqai
      181 atakrlgavv easdvrpaar eqveslgakf idvpfetdee reiaqgkggy arpmppawma
      241 rqaalvserc kqadivitta lipgrpapml vsaetvaamk pgsvlvdlav erggncplse
      301 kgrivekhdv tiigltnlpg lvatdasaly arnildflkl iinadgalai qrddeivaac
      361 lvceggnvtr rt
//
LOCUS       WP_128843814             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Burkholderia catarinensis].
ACCESSION   WP_128843814
VERSION     WP_128843814.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia catarinensis
  ORGANISM  Burkholderia catarinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia catarinensis"
                     /db_xref="taxon:1108140"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34047
     Region          8..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstpkhakvl ilgsgpagyt aavyaaranl spvlvtgiaq ggqlmtttdv enwpadakgv
       61 qgpelmarfl ehaerfntei vfdhihtakl heqpirligd sgeytcdsli iatgasaqyl
      121 glpseeafmg kgvsacatcd gffyrgqeva vigggntave ealyltgiak kvtvihrrdk
      181 fraepilidr llekekegav eikwdhvlde vtgessgvtg lriknvktga tedlnvqgvf
      241 vaighkpntd lfqgqlemkd gyiltksglh gnatstsvag vfaagdvqdn vyrqaitsag
      301 tgcmaaldaq ryleslhdkk
//
LOCUS       WP_128845108             323 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Streptomyces].
ACCESSION   WP_128845108
VERSION     WP_128845108.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces
  ORGANISM  Streptomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Streptomyces"
                     /db_xref="taxon:1883"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34121
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslnp lvfegavtag galmnttdve nfpgfqdgim
       61 gpelmdnmra qaerfgaelv pddvvavdlt gaiktvtdta gtvhraksvi vttgsqhrkl
      121 glpnedalsg rgvswcatcd gfffkdhdia vigggdtame eatflsrfak svtivhrrdt
      181 lraskamqdr afadpkikfa wdsevaevkg eqklsgltlr ntktgelsel pvtglfiavg
      241 hdprtelfkg qlelddegyl kveapstrtn ltgvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaala dvepaepekt pav
//
LOCUS       WP_128847123             379 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Burkholderia catarinensis].
ACCESSION   WP_128847123
VERSION     WP_128847123.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia catarinensis
  ORGANISM  Burkholderia catarinensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia catarinensis"
                     /db_xref="taxon:1108140"
     Protein         1..379
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39123
     Region          1..374
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,73,92,291,325,327)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,281..282,332..333,337,
                     340..341)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,231,242,
                     259..261,268,270)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mhigvpaetr anearvaatp etvkkyaaag hrisiakgag saasypdeay aaagaeltdq
       61 saafdadvvl kvqaptdtel pslkrgsvlv gmlepfngeq aaklaaagvt gfaleaaprt
      121 traqsldvls sqaniagyka vlvaaalypr ffpmlmtaag tvkaarvlil gagvaglqai
      181 atakrlgavi easdvrpavk eqieslgakf ldvpfetdee reaaqgvggy arpmppswlg
      241 rqaalvhera kqadivitta lipgrpaptl isvetaqsmk pgsvlvdlaa grgpefdgrk
      301 sgncpltvad qvivhngvti agytnlasmv asdasalyar nlldfmkliv tkegalnidl
      361 addivaatll crdgevtrk
//
LOCUS       WP_128856311             318 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bacillus sp. CDB3].
ACCESSION   WP_128856311
VERSION     WP_128856311.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. CDB3
  ORGANISM  Bacillus sp. CDB3
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Bacillus sp. CDB3"
                     /db_xref="taxon:360310"
     gene            1..318
                     /gene="trxB"
     Protein         1..318
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34496
     Region          8..305
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mseekiydvi iigagpagmt aavytsranl stlmlergip ggqmantedv enypgyesil
       61 gpdlsnkmfe hakkfgaeya ygdvkeiidg keyktiiagk keyktraiiv asgaeykkig
      121 vpgeaelggr gvsycavcdg affkgkelvv igggdsavee gvfltrfask vtivhrrdtl
      181 raqkilqdra fqnekvdfiw nhtikeinda ngkvgsvtlv dvnsgeeqev ktdgvfvyig
      241 mlplskpfve lgitnengyv etnermetkv pgifaagdvr ekmlrqivta tgdgsiaaqs
      301 tqhyveelle glktvtek
//
LOCUS       WP_128872979             320 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Pseudomonas].
ACCESSION   WP_128872979
VERSION     WP_128872979.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33783
     Region          1..318
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 msevrhsrvi ilgsgpagys aavyaaranl kpllitgmqa ggqlttttev dnwpgdvhgl
       61 tgpalmermk ehaerfetei vfdhinavdf aakpytltgd satytcdali iatgasaryl
      121 glpseeafmg kgvsacatcd gffyrnkpva vvgggntave ealylanias tvtlihrret
      181 fraekilidk lnarvaegki vlklnatlde vlgdnmgvtg arlknndgsf deltvdgvfi
      241 aightpntsl fegqltlkdg ylvvqggrdg natatslegi faagdvadhv yrqaitsaga
      301 gcmaaldaer ylddlqnakf
//
LOCUS       WP_128883724             335 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mycobacterium tuberculosis].
ACCESSION   WP_128883724
VERSION     WP_128883724.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     gene            1..335
                     /gene="trxB"
     Protein         1..335
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35542
     Region          16..315
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mtappvhdra hhpvrdvivi gsgpagytaa lyaaraqlap lvfegtsfgg almtttdven
       61 ypgfrngitg pelmdemreq alrfgadlrm edvesvslhg plksvvtadg qthraravil
      121 tmgaaarylq vpgeqellgr gvsscatcdg fffrdqdiav igggdsamee atfltrfars
      181 vtlvhrrdef raskimldra rnndkirflt nhtvvavdgd ttvtglrvrd tntgaettlp
      241 vtgvfvaigh eprsglvrea idvdpdgyvl vqgrttstsl pgvfaagdlv drtyrqavta
      301 agsgcaaaid aerwlaehaa tgeadstdal igaqr
//
LOCUS       WP_128887813             335 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Mycobacterium tuberculosis].
ACCESSION   WP_128887813
VERSION     WP_128887813.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     gene            1..335
                     /gene="trxB"
     Protein         1..335
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35540
     Region          16..315
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mtappvhdra hhpvrdvivi gsgpagytaa lyaaraqlap lvfegtsfgg almtttdven
       61 ypgfrngitg pelmdemreq alrfgadlrm edvesvslhg plksvvtadg qthraravil
      121 amgvaarylq vpgeqellgr gvsscatcdg fffrdqdiav igggdsamee atfltrfars
      181 vtlvhrrdef raskimldra rnndkirflt nhtvvavdgd ttvtglrvrd tntgaettlp
      241 vtgvfvaigh eprsglvrea idvdpdgyvl vqgrttstsl pgvfaagdlv drtyrqavta
      301 agsgcaaaid aerwlaehaa tgeadstdal igaqr
//
LOCUS       WP_128890736             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Corynebacterium pelargi].
ACCESSION   WP_128890736
VERSION     WP_128890736.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium pelargi
  ORGANISM  Corynebacterium pelargi
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Corynebacterium pelargi"
                     /db_xref="taxon:1471400"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33443
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdatihdva iigsgpagyt aalyaarael rpivfegiey ggslmtttev enfpgfkdgi
       61 lgpelmeemr aqaerfgadl rmelvtrvel egeikkiwvd deefqaravi latgsapryl
      121 gvdgeqqllg rgvsacatcd gfffrdhdia vigggdsame eaifltkfak svtivhrree
      181 frasaimler akenekiril tnkqvsrvlg entveglelv dslsgetstl dvtamfvaig
      241 hdprselfrd evecddagyv qvqhpstrtn ipgvfaigdl vdatyqqait aagsgcrgai
      301 daehylaei
//
LOCUS       WP_128892359             323 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Erythrobacter sp. HKB08].
ACCESSION   WP_128892359
VERSION     WP_128892359.1
KEYWORDS    RefSeq.
SOURCE      Erythrobacter sp. HKB08
  ORGANISM  Erythrobacter sp. HKB08
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Sphingomonadales; Erythrobacteraceae; Erythrobacter/Porphyrobacter
            group; Erythrobacter.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Erythrobacter sp. HKB08"
                     /db_xref="taxon:2502843"
     gene            1..323
                     /gene="trxB"
     Protein         1..323
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34512
     Region          6..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mathrtkmli igsgpagysa aiygaramle pivvqglqpg gqltittdve nypgfrdviq
       61 gpwlmeemka qaehvgtrmm wdtivevdle sgppwraigd sgdeyigdtl viatgaqakw
      121 lgvpgeqelg gkgvsacatc dgffyrgkkv avigggntav eealyltnhs ddvtlihrrd
      181 elraekilqe rlfasdkist lwnktvvsfe agengtlshl vlkdtetget stlevdgafv
      241 aighapstel fkgklpmdet gyllvepgtp ktslpgvfaa gdvmdhtyrq avtaagvgcm
      301 aaldaerflq tmdfareeaq aae
//
LOCUS       WP_128896117             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Longirhabdus pacifica].
ACCESSION   WP_128896117
VERSION     WP_128896117.1
KEYWORDS    RefSeq.
SOURCE      Longirhabdus pacifica
  ORGANISM  Longirhabdus pacifica
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Paenibacillaceae; Longirhabdus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Longirhabdus pacifica"
                     /db_xref="taxon:2305227"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33829
     Region          2..307
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 myntvvigtg pagltaaiyl aranlkplvi egpepggqlt tttdvenfpg fpdgimgpel
       61 mdnmrkqatr fgaefktgwv neinfdqkpf kmtvegigei eansviistg asakllgipg
      121 ekenigrgvs tcatcdgfff rgkkivvvgg gdsameeanf ltkfasevti vhrrdtlras
      181 kimqdraken pkikwkldat plevmageha vsglkvknne tdqeeiletd gifiaighnp
      241 ntaflqgkvn tdeigyidvi pgttktnieg vfacgdvqdk hyrqaitaag sgcmaaldce
      301 kylegqpvhd wsqal
//
LOCUS       WP_128902227             319 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Janthinobacterium sp. 17J80-10].
ACCESSION   WP_128902227
VERSION     WP_128902227.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. 17J80-10
  ORGANISM  Janthinobacterium sp. 17J80-10
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Janthinobacterium sp. 17J80-10"
                     /db_xref="taxon:2497863"
     gene            1..319
                     /gene="trxB"
     Protein         1..319
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33948
     Region          1..319
                     /region_name="PRK10262"
                     /note="thioredoxin reductase; Provisional"
                     /db_xref="CDD:182343"
ORIGIN      
        1 mttskhakvl ilgsgpagys aavyaaranl kpvlvtgveq ggqlmtttdv enwpgdpmgv
       61 qgpelmqrll qhaerfqtei vfdhihttyl nekpfrlvgd agtytcdali iatgasaqyl
      121 glpseeafmg rgvsacatcd gffyrgrdva vigggntave ealylsnias kvtvihrrdk
      181 fraepilidr lmakvaegki evkwnhtlde vlgdasgvtg irikstadgs tgefnvhglf
      241 iaighkpnts ifegqidmhn gyiktktgle ggatgtnipg vfaagdvqdh iyrqaitsag
      301 tgcmaaldsq rylegledk
//
LOCUS       WP_128899523             320 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Dyella sp. M7H15-1].
ACCESSION   WP_128899523
VERSION     WP_128899523.1
KEYWORDS    RefSeq.
SOURCE      Dyella sp. M7H15-1
  ORGANISM  Dyella sp. M7H15-1
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Rhodanobacteraceae; Dyella.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Dyella sp. M7H15-1"
                     /db_xref="taxon:2501295"
     gene            1..320
                     /gene="trxB"
     Protein         1..320
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34463
     Region          9..317
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttpkhsrll ilgsgpagyt aavyaaranl kptmitglqq ggqlmittdv dnwpgdvkgv
       61 qgpelmqrma ehaerfetem vfdhihtanl kqrpfrlkgd sgeytcdali iatgatakyl
      121 gipseehykg kgvsacatcd gfffrdqdvv vvgggntave ealylanigr kvylvhrrdk
      181 lraekimqdk lfekaaagki elvwnhtige vlgdesgvtg vrvkdinsgt trdieatgff
      241 vaightpntg ifedqldmhd gyikirsgle gmatmtsvpg vfaagdvadh vyrqavtsag
      301 fgcmaaldae rwldqgkhag
//
LOCUS       WP_128903067             527 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Janthinobacterium sp. 17J80-10].
ACCESSION   WP_128903067
VERSION     WP_128903067.1
KEYWORDS    RefSeq.
SOURCE      Janthinobacterium sp. 17J80-10
  ORGANISM  Janthinobacterium sp. 17J80-10
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Oxalobacteraceae; Janthinobacterium.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Janthinobacterium sp. 17J80-10"
                     /db_xref="taxon:2497863"
     Protein         1..527
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54826
     Region          5..527
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 masvigipre typgekrvat vpevveklik lgftvtvesg agdaanfsdd ayraagaqvv
       61 dgaaalwaga divfkvrapd anelalvrag ttlvsfiwpa qnpdlmqqla arnvtvlaid
      121 alprqlsraq kmdaltsmag isgyraviea anafgrffng qitaagkipp akvfiagagv
      181 aglaaigtaa nlgaivrand trpevadqvk slggefvkve yeeegsgggg yakvmsegfq
      241 qaqremyakq areadiiitt alipgkpapk litaemvqsm kpgsvivdma geqggncelt
      301 epgeavvrhg vtiigytdlp srlakqsstl yasnllrlte elcktkdgki dvnmeddair
      361 gltvikngev twpapapklp aapaaaakpa ampppkahgh gaaapasats iavtfgiaaa
      421 lfwligafap aafighftvf vlacfigymv vwnvtpalht plmsvtnais siiaigalvq
      481 vappldggag rpddwirwla vigivltain mfggfavtrr mlamfrk
//
LOCUS       WP_128914302             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Granulicella sibirica].
ACCESSION   WP_128914302
VERSION     WP_128914302.1
KEYWORDS    RefSeq.
SOURCE      Granulicella sibirica
  ORGANISM  Granulicella sibirica
            Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia;
            Terriglobales; Acidobacteriaceae; Granulicella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Granulicella sibirica"
                     /db_xref="taxon:2479048"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33984
     Region          8..315
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mpdssvrdtv ilgsgcsglt aaiyagrsnl kplvleghep ggqlsittlv enfpgwpegi
       61 qgpelienmk kqaerfgael smahlvsadl tkypielnlg keivktrtli iasgasarwl
      121 nlpseqalig hgvsscatcd gffsrgkeia vigggdsame ealfltrfas kvtlinrtgk
      181 fraspimler amahpqiefl sntvveevlg veekdvkglr irntvtgves ilpisfmflg
      241 ighipnagmf sgqmdldedg yilahddvyt tlngevlkgv facgdikdrk yrqaitaags
      301 gcmaalevek fleehgr
//
LOCUS       WP_128918224             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium nanningense].
ACCESSION   WP_128918224
VERSION     WP_128918224.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium nanningense
  ORGANISM  Bradyrhizobium nanningense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium nanningense"
                     /db_xref="taxon:1325118"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39253
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag lksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasela qykrgalvia imdpygneaa lktiadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake msreyqakqa
      241 altaehikkq divittalip grpapklvsa emvksmkpgs vlvdlaverg gnvegakpge
      301 vvdldgikiv gytnvagrva asasslyarn lfsfvetmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_128921484             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bradyrhizobium nanningense].
ACCESSION   WP_128921484
VERSION     WP_128921484.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium nanningense
  ORGANISM  Bradyrhizobium nanningense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bradyrhizobium nanningense"
                     /db_xref="taxon:1325118"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34281
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msapvhakvv iigsgpagyt aaiyaaraml epiliqgiqp ggqltittdv enypgfadvi
       61 qgpwlmeqme kqavhvgtki vtdlvtklea aqrpfrlicd sgdvyladav ilatgaqarw
      121 lglpsetkfq gggvsacatc dgffyrnkdv vvigggntav eealyltnha sqvtivhrrd
      181 hfraerilqe rlfkhpkikv iwdcavdeic gtenpnkvth vrlknvktga lrdvktdgvf
      241 iaighapate lvkdqiklkp sgyvevapns tatsmpglfa agdvadetyr qavtaaglgc
      301 maaleaerfl alraseraaa e
//
LOCUS       WP_128923667             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bradyrhizobium guangxiense].
ACCESSION   WP_128923667
VERSION     WP_128923667.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium guangxiense
  ORGANISM  Bradyrhizobium guangxiense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bradyrhizobium guangxiense"
                     /db_xref="taxon:1325115"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34199
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msapvhakvv iigsgpagyt aaiyaaraml epiliqgmqa ggqltittdv enypgfadvi
       61 qgpwlmeqme kqavhvgtki vtdlvvklet aqrpfrltcd sgdvyladav ilatgaqarw
      121 lglpsevkfq gggvsacatc dgffyrnkdv vvvgggntav eealyltnha sqvtivhrrd
      181 hfraerilqe rlfrhpkikv iwdsavdeic gnenpnkvth vrlknvktga lsdlktdgvf
      241 iaighapate lvkdqvklkp sgyvetapns tatsvpglfa agdvadetyr qavtaaglgc
      301 maaleaerfl alraseraaa e
//
LOCUS       WP_128927824             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium guangxiense].
ACCESSION   WP_128927824
VERSION     WP_128927824.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium guangxiense
  ORGANISM  Bradyrhizobium guangxiense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium guangxiense"
                     /db_xref="taxon:1325115"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39154
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag iksglpdsef taagatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmpaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegakpge
      301 vvdvdgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpka
//
LOCUS       WP_128931483             321 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Bradyrhizobium].
ACCESSION   WP_128931483
VERSION     WP_128931483.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34152
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msapvhakvi iigsgpagyt aaiyaaraml epiliqgiqp ggqltittdv enypgfadvi
       61 qgpwlmeqme kqavhvgtti vtdlvtklet aqrpfrltcd sgdvyladtv ilatgaqarw
      121 lglpsegkfq gggvsacatc dgffyrnkev vvvgggnsav eealyltnha sqvtivhrrd
      181 hfraerilqe rlfkhpkikv vwdsavdeic gtenpnkvth vrlknvktga lrdlktdgif
      241 iaighapate lvkgqvklkp sgyvevapns tatsvpglfa agdvadetyr qavtaaglgc
      301 maaleaerfl alraseraaa e
//
LOCUS       WP_128936493             375 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit
            alpha [Bradyrhizobium].
ACCESSION   WP_128936493
VERSION     WP_128936493.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium
  ORGANISM  Bradyrhizobium
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium"
                     /db_xref="taxon:374"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39275
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pleprvaasp dtvkkfkalg aeiavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneas lktmadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa dmvksmkpgs vlvdlaverg gnvegakage
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_128949889             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium guangzhouense].
ACCESSION   WP_128949889
VERSION     WP_128949889.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium guangzhouense
  ORGANISM  Bradyrhizobium guangzhouense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium guangzhouense"
                     /db_xref="taxon:1325095"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39261
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag lksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsg emvksmkpgs vlvdlaverg gnvegarage
      301 vvetdgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 trdgavihpn fqpkv
//
LOCUS       WP_128953837             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bradyrhizobium guangzhouense].
ACCESSION   WP_128953837
VERSION     WP_128953837.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium guangzhouense
  ORGANISM  Bradyrhizobium guangzhouense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bradyrhizobium guangzhouense"
                     /db_xref="taxon:1325095"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34159
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msapvhakvv iigsgpagyt aaiyaaraml epiliqgmqa ggqltittdv enypgfadvi
       61 qgpwlmeqme kqavhvgtri vtdlvvkldt sqrpfrltcd sgdvyladtv ilatgaqarw
      121 lglpseakfq gggvsacatc dgffyrnkev vvvgggntav eealyltnha sqvtivhrrd
      181 hfraerilqe rlfkhpkirv iwdsavdeic gtenpnkvth vrlknvktga lsdvktdgvf
      241 iaighapate lvkdavklkp sgyvevapns tatsvpglfa agdvadetyr qavtaaglgc
      301 maaleaerfl alraseraaa e
//
LOCUS       WP_128956756             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium zhanjiangense].
ACCESSION   WP_128956756
VERSION     WP_128956756.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium zhanjiangense
  ORGANISM  Bradyrhizobium zhanjiangense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium zhanjiangense"
                     /db_xref="taxon:1325107"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39261
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pleprvaasp dtvkkfkalg aeiavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneas lktmadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa dmvksmkpgs vlvdlaverg gnvegakgge
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 tkdgavihpn fqpkv
//
LOCUS       WP_128964238             375 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Bradyrhizobium guangdongense].
ACCESSION   WP_128964238
VERSION     WP_128964238.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium guangdongense
  ORGANISM  Bradyrhizobium guangdongense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bradyrhizobium guangdongense"
                     /db_xref="taxon:1325090"
     Protein         1..375
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39217
     Region          1..364
                     /region_name="Rubrum_tdh"
                     /note="Rubrum transdehydrogenase NAD-binding and catalytic
                     domains; cd05304"
                     /db_xref="CDD:240629"
     Site            order(15,72,91,288,314,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(44,124..125,134..135,138..139,142..143,145..146,
                     148..153,155,157..159,162,185..186,278..279,321..322,326,
                     329..330)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(119..120,124,127,130,171..174,194..196,228,239,
                     256..258,265,267)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:240629"
     Site            order(121..122,124,134,177..178,185,201..202,204..207)
                     /site_type="other"
                     /note="trimer interface B [polypeptide binding]"
                     /db_xref="CDD:240629"
     Site            order(154..158,161,164,187,189)
                     /site_type="other"
                     /note="trimer interface A [polypeptide binding]"
                     /db_xref="CDD:240629"
ORIGIN      
        1 mkiavakeid pseprvaasp dtvkkfkalg aeiavepgag iksglpdsef tavgatvsad
       61 alkdadiiik vkrpeasels qykrgalvia imdpygneaa lkamadagvs afamelmpri
      121 traqvmdvls sqanlagyra viegaeafgr afpmmmtaag tvpaakvfvm gvgvaglqai
      181 atarrlgavv tatdvrpatk eqveslgakf lavedeefkn aqtaggyake mskeyqakqa
      241 altaehikkq divittalip grpapklvsa emvksmkpgs vlvdlaverg gnvegakage
      301 vvdldgikiv gytnvagrva asasslyarn lfsfietmvd kkekklavnw ddelvkatal
      361 trdgavihpn fqpka
//
LOCUS       WP_128968293             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Bradyrhizobium guangdongense].
ACCESSION   WP_128968293
VERSION     WP_128968293.1
KEYWORDS    RefSeq.
SOURCE      Bradyrhizobium guangdongense
  ORGANISM  Bradyrhizobium guangdongense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Bradyrhizobium guangdongense"
                     /db_xref="taxon:1325090"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34261
     Region          8..311
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msapvhakvv iigsgpagyt aaiyaaraml epiliqgmqa ggqltittdv enypgfadvi
       61 qgpwlmeqme kqavhvgtri vtdlvtklet sqrpfrltcd sgdvyladtv ilatgaqarw
      121 lglpsevkfq gggvsacatc dgffyrnkev vvvgggntav eealyltnha sevtivhrrd
      181 hfraerilqe rlfkhpkikv vwdsavdeic gtenpnkvth vrlknvktga ltdlktdgvf
      241 iaighapate lvkdqiklkp sgyvevapns tatsvpglfa agdvadetyr qavtaaglgc
      301 maaleaerfl alraseraaa e
//
LOCUS       WP_128977008             509 aa            linear   BCT 07-JUL-2024
DEFINITION  Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha
            [Streptomyces roseicoloratus].
ACCESSION   WP_128977008
VERSION     WP_128977008.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces roseicoloratus
  ORGANISM  Streptomyces roseicoloratus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ahmad,S., Glavas,N.A. and Bragg,P.D.
  TITLE     A mutation at Gly314 of the beta subunit of the Escherichia coli
            pyridine nucleotide transhydrogenase abolishes activity and affects
            the NADP(H)-induced conformational change
  JOURNAL   Eur J Biochem 207 (2), 733-739 (1992)
   PUBMED   1633824
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Tong,R.C., Glavas,N.A. and Bragg,P.D.
  TITLE     Topological analysis of the pyridine nucleotide transhydrogenase of
            Escherichia coli using proteolytic enzymes
  JOURNAL   Biochim Biophys Acta 1080 (1), 19-28 (1991)
   PUBMED   1932078
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Clarke,D.M., Loo,T.W., Gillam,S. and Bragg,P.D.
  TITLE     Nucleotide sequence of the pntA and pntB genes encoding the
            pyridine nucleotide transhydrogenase of Escherichia coli
  JOURNAL   Eur J Biochem 158 (3), 647-653 (1986)
   PUBMED   3525165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF006942.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09424
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Streptomyces roseicoloratus"
                     /db_xref="taxon:2508722"
     Protein         1..509
                     /product="Re/Si-specific NAD(P)(+) transhydrogenase
                     subunit alpha"
                     /EC_number="7.1.1.1"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51849
     Region          1..508
                     /region_name="pntA"
                     /note="Re/Si-specific NAD(P)(+) transhydrogenase subunit
                     alpha; PRK09424"
                     /db_xref="CDD:236507"
ORIGIN      
        1 mivgvlrear agehrvaatp atveqirglg yevvvdagag aaagftdgay eaagaavgea
       61 aaadvvlgve apsraqldav rpeatvialf apafdpvmve elgrrpftal smdavprisr
      121 aqsmdvlssm aniagyravv eaahefgrff tgqvtaagkv ppakvlvaga gvaglaaigt
      181 agslgavvra tdprpevadq vrslggeyls iespevevst tgyakemgdd ykareaelya
      241 aqcrdadivi ttalipgrpa pvlitadmva amkpgsvivd maaanggnvv gtvkgekavt
      301 angvtilgyt dlagrlpaqa sqlygtnlvn llklmtpgkd grlvldwddp vqrsitvvra
      361 gesawppppv rvsaapvpaa aaaapavesa vrkpvtagrk fgavsvaala lflaagfapa
      421 allphvtvfv laivigyyvi ghvhhalhtp lmsvtnaisg iivvgsllqi gqsstavtvl
      481 sfvaillasi nvfggfavtr rmlamfnrs
//
LOCUS       WP_128978900             335 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces roseicoloratus].
ACCESSION   WP_128978900
VERSION     WP_128978900.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces roseicoloratus
  ORGANISM  Streptomyces roseicoloratus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Streptomyces roseicoloratus"
                     /db_xref="taxon:2508722"
     gene            1..335
                     /gene="trxB"
     Protein         1..335
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35430
     Region          16..321
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mttattptga qddvreviii gsgpagytaa lytaraqlkp llfgssifvg gsltttteve
       61 nfpgfpqgid gpdlmenmra qavrfgaemi dddivsvdla gdiklltdsa gtvhraktvi
      121 iatgsgyrkl glpqedelsg rgvswcatcd gfffrdrdii vvgggdtame eatfltrfar
      181 svtvvhrrst lrasktmqnr afaedkisfa fdseiaeiks engmlsgvvl rdvltgdtre
      241 ldatglfiai ghdprtelfa dqleldddgy lktqspttrt slpgvfgagd vvdhiyrqai
      301 taagsgcaaa ldaerylaal rdaepaaetg lvsag
//
LOCUS       WP_128979754             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Halarcobacter ebronensis].
ACCESSION   WP_128979754
VERSION     WP_128979754.1
KEYWORDS    RefSeq.
SOURCE      Halarcobacter ebronensis (Arcobacter ebronensis)
  ORGANISM  Halarcobacter ebronensis
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Halarcobacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Halarcobacter ebronensis"
                     /db_xref="taxon:1462615"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32728
     Region          3..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldlaiiggg pagltaglya trgglknvtm femgmpggqi tgsseienyp gqgaivsgmd
       61 lmqswpeqcq rfglkhemnq vskvtksgdv ftvttadgkt qeaksvllat gsvprragfk
      121 gekeffgrgi stcatcdgff ykgkevalig ggdsaleeav ylskicskvy lvhrrdtyra
      181 apstiehmka cenieevtnv mveevygdas gvtglkvknr dsgeirdlav pgvfvfvgrd
      241 vlneplkqdd gtflcdvndq gevivdlrmr tsvpglyaag dvrieaakqv vcaagdgata
      301 avniieylg
//
LOCUS       WP_128983210             321 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Streptomyces roseicoloratus].
ACCESSION   WP_128983210
VERSION     WP_128983210.1
KEYWORDS    RefSeq.
SOURCE      Streptomyces roseicoloratus
  ORGANISM  Streptomyces roseicoloratus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Kitasatosporales; Streptomycetaceae; Streptomyces.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Streptomyces roseicoloratus"
                     /db_xref="taxon:2508722"
     gene            1..321
                     /gene="trxB"
     Protein         1..321
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33955
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdvrnviii gsgpagytaa lytaraslkp lvfegavtag galmntteve nfpgfrdgim
       61 gpdlmdnmra qaerfgaelv pddivavdlt geiktvtdta gtvyrakavi vttgsqhrkl
      121 glpnedtlsg rgvswcatcd gfffrdqdia vvgggdtame eatflsrfak svtivhrrds
      181 lraskamqer afadpkikfa wdsevaeihg dtklsgltlr ntktgetsel pvtglfiavg
      241 hdprtelfkg qleldaegyl kvdapstrtn lagvfgagdv vdhtyrqait aagtgcsaal
      301 daerflaals dseklaetpa v
//
LOCUS       WP_128986452             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arcobacter cloacae].
ACCESSION   WP_128986452
VERSION     WP_128986452.1
KEYWORDS    RefSeq.
SOURCE      Arcobacter cloacae (Pseudarcobacter cloacae)
  ORGANISM  Arcobacter cloacae
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Arcobacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Arcobacter cloacae"
                     /db_xref="taxon:1054034"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32960
     Region          3..308
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mldlaiiggg pagltaglya trgglknvvm femgmpggqi tgsseienyp gqaevvsgmd
       61 lmanwpeqcq rfglkhemaq vdnvtktgdi fklvtsdkke yearavliat gsvprragfk
      121 geneffgrgi stcatcdgff ykgkevavig ggdsaieeav ylaklckkvy lvhrrdtyra
      181 apstiehmkh tenieevtnv iveevfgdam gvtglkvkhk dtgeirdlpt pgvfvfvgrd
      241 vlnaplkqad gtflcdvnes gevivdlrmr tsvpglyaag diridapkqv vcaagdgata
      301 avniieylg
//
LOCUS       WP_129001861             317 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Filimonas effusa].
ACCESSION   WP_129001861
VERSION     WP_129001861.1
KEYWORDS    RefSeq.
SOURCE      Filimonas effusa
  ORGANISM  Filimonas effusa
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae; Filimonas.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Filimonas effusa"
                     /db_xref="taxon:2508721"
     gene            1..317
                     /gene="trxB"
     Protein         1..317
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33927
     Region          11..314
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 meqgtvervh cliigsgpag ytaaiyaara nmkpvlyqgi qpggqltitt evenypgype
       61 giqgpemmvn fekqavrmga diryglatkv dfsgpvhkvw iddekliead aviiatgasa
      121 kwlgieseqr lngygvsaca vcdgfffkgk evaivgagdt aceeaiylsk lasnvhmivr
      181 kgedgmkask vmqdrvkata nikvyyhset vevvgekkve avtirnnqdn ttqtvpvsaf
      241 fvaighqpns difkgwltmd dagylitvpg tsktnvpgvf asgdvqdkiy rqavtasgsg
      301 cmaaldaery lsehgiv
//
LOCUS       WP_129008716             309 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Arcobacter sp. CECT 8983].
ACCESSION   WP_129008716
VERSION     WP_129008716.1
KEYWORDS    RefSeq.
SOURCE      Arcobacter sp. CECT 8983
  ORGANISM  Arcobacter sp. CECT 8983
            Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
            Campylobacterales; Arcobacteraceae; Arcobacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Arcobacter sp. CECT 8983"
                     /db_xref="taxon:2044508"
     gene            1..309
                     /gene="trxB"
     Protein         1..309
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33026
     Region          3..308
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 mldlaiiggg pagltaglya trgglnnvtm femgmpggqi tgsseienyp gqekvvtgme
       61 lmeswptqam kfglkhemqq ilkvrkagdn fevelgdgtk qearsvllat gsvpkkggfk
      121 gedkffgrgi stcatcdgff yknkevavig ggdtaleeay ylskicskvy lvhrrdtyra
      181 apstiehmkk aenieevtnv tveevvgdnm gvtgiivksk engetreivv pgvfvfvgrn
      241 vlsdalkqdd gsylcdvneq tevivdlkmr tnvpglyaag dvrieaakqv vcaaadgata
      301 avdiieylg
//
LOCUS       WP_129018865             326 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Gelidibacter gilvus].
ACCESSION   WP_129018865
VERSION     WP_129018865.1
KEYWORDS    RefSeq.
SOURCE      Gelidibacter gilvus
  ORGANISM  Gelidibacter gilvus
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Gelidibacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Gelidibacter gilvus"
                     /db_xref="taxon:59602"
     gene            1..326
                     /gene="trxB"
     Protein         1..326
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35221
     Region          9..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msdaiekvkc liigsgpagy taaiyaaran mfpvlyqgeq pggqltttnd venfpgypdg
       61 itgpemmiel qkqaerfgte irdgwitkvd fsgdvhkvwv hdgkeihcet viistgatam
      121 ylgipseqky lklgggvsac avcdgffyrn qevvivgagd saceeahyls klckkvtmlv
      181 rrdefrasqi mqdrvkntkn ieiiyntnte evlgdgqlvt gvraknnitg evfdipatgf
      241 fvaighkpnt difkdfleld ptgyiinipg tsktsidgvf vsgdaadnvy rqavtaagtg
      301 cmaaldaery lasidssfev ntatny
//
LOCUS       WP_129021220             316 aa            linear   BCT 07-JUL-2024
DEFINITION  MULTISPECIES: thioredoxin-disulfide reductase [Edaphocola].
ACCESSION   WP_129021220
VERSION     WP_129021220.1
KEYWORDS    RefSeq.
SOURCE      Edaphocola
  ORGANISM  Edaphocola
            Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia;
            Chitinophagales; Chitinophagaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Edaphocola"
                     /db_xref="taxon:2601681"
     gene            1..316
                     /gene="trxB"
     Protein         1..316
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34483
     Region          11..312
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mstentteli dcliigsgpa gytaaiyasr anlkpvlysg lqpggqltit tdvenypgyp
       61 egimgpqmmk dfenqarrmg adlrwgmisk vdlsvrpfrv evdesswiea nsiiiatgas
      121 akwlgleseq rlngygvsac avcdgfffkd kevaivgagd taceealyls kicskvhmfi
      181 rkeemraskv mqdrvlktsn ievywntetd eilgekkvea vrvlnnktne kteiplsaff
      241 vaighqpnsd lfagvidmdd qgyimttpgt sktniqgvfa cgdvqdkmyr qavtaagsgc
      301 maaldaeryl gefvhn
//
LOCUS       WP_129023443             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Flavobacterium sp. YO12].
ACCESSION   WP_129023443
VERSION     WP_129023443.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium sp. YO12
  ORGANISM  Flavobacterium sp. YO12
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Flavobacterium sp. YO12"
                     /db_xref="taxon:1920029"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33926
     Region          7..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mmiekikcli igsgpagyta aiyaaranmn pvlyqgmqpg gqltttneve nfpgyvdgvt
       61 gpemmiqlqe qskrfgadir dgwatkvdfs gdihkvwind tielhcetvi istgasakyl
      121 glpseqhylq mgggvsacav cdgffyrnqe vvivgagdsa ceeahylskl ckkvtmlvrs
      181 ekfraskime ervrktenie ilmnhdtvev lgdenvvhai kaknkttsev fdipatgffv
      241 aighkpntdi fadyitldet gyivntpgts ktnvegvfva gdaadhvyrq aitaagtgcm
      301 aaldaeryla ske
//
LOCUS       WP_129027629             312 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Aquirufa rosea].
ACCESSION   WP_129027629
VERSION     WP_129027629.1
KEYWORDS    RefSeq.
SOURCE      Aquirufa rosea
  ORGANISM  Aquirufa rosea
            Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
            Flectobacillaceae; Aquirufa.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Aquirufa rosea"
                     /db_xref="taxon:2509241"
     gene            1..312
                     /gene="trxB"
     Protein         1..312
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=33440
     Region          6..306
                     /region_name="TRX_reduct"
                     /note="thioredoxin-disulfide reductase; TIGR01292"
                     /db_xref="CDD:273540"
ORIGIN      
        1 maekikclii gsgpagytaa iyasraglqp vmyqggqpgg qlttttevdn fpgypngveg
       61 pammqdlenq akrfgtdvrf gmatrvdfna qpkkvwiddq ieleadavii atgasakwlg
      121 legektfngl gvsacavcdg ffyknqvvav vgagdtaaee asylanlcte vhmivrrnem
      181 raslimqerv knnpkihihw nseteeilgd tngvtgirik nnvsgeteei altgffvaig
      241 hqpntsifkg qldmdaqeyl itekgssrtn ipgvfacgdv qdsiyrqavt aagsgcmaal
      301 daerwlaanh lh
//
LOCUS       WP_129029547             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium tetani].
ACCESSION   WP_129029547
VERSION     WP_129029547.1
KEYWORDS    RefSeq.
SOURCE      Clostridium tetani
  ORGANISM  Clostridium tetani
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Clostridium tetani"
                     /db_xref="taxon:1513"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35366
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnkeekildl viigsgpagl taaiyasrmk ldfivlenel vggqirssys venypgfrsi
       61 sgeelvnkiy dhavdlgski defdeiqyvk lteeekiiet yeyiykpkav iiaagakyrp
      121 lpipeekkyh gngihhcelc dgefyqdkni mvvgggnsal egaiflsrya knitmmhkld
      181 cfqgekslqd evfnnskiki iwntdiknaf genkleevlv edlktkeqyk idvdgifvyi
      241 gmvpntdlyk dyinlnergy iiadestktn iegvfaagdv rvkqfrqlvt anadgavaal
      301 saekyiskkr renng
//
LOCUS       WP_129031148             313 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Levilactobacillus suantsaii].
ACCESSION   WP_129031148
VERSION     WP_129031148.1
KEYWORDS    RefSeq.
SOURCE      Levilactobacillus suantsaii
  ORGANISM  Levilactobacillus suantsaii
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Levilactobacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Levilactobacillus suantsaii"
                     /db_xref="taxon:2292255"
     gene            1..313
                     /gene="trxB"
     Protein         1..313
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=32992
     Region          4..306
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mknydvivig agpggmtgal yasranlsvl mldrgiyggq mnntaaieny pgfksvlgpd
       61 lakdmydgat qfgaefaygs vdsiedhgdh kvvktddgdy sakavliatg seykklgvpg
      121 ednyggrgvs ycavcdgaff knrdvivvgg gdsaieegiy laglaskvti vvrrdqlraq
      181 kilqdrafan dkiefvwntn vteiqgdkmk vtgvathnnq tgetghldas gvfiyvgtlp
      241 mttaftdlgi tddagwiktd dhmatavpgi faigdvrqkd lrqittavge ggtagqaafn
      301 yletlkaqas sea
//
LOCUS       WP_129033806             315 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Clostridium tetani].
ACCESSION   WP_129033806
VERSION     WP_129033806.1
KEYWORDS    RefSeq.
SOURCE      Clostridium tetani
  ORGANISM  Clostridium tetani
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Clostridium tetani"
                     /db_xref="taxon:1513"
     gene            1..315
                     /gene="trxB"
     Protein         1..315
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=35409
     Region          9..310
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnkeekildl viigsgpagl taaiyasrmk ldfivlenel vggqirstys ienypgfrsi
       61 sgeelvnkiy dhavdlgaki defdeiqyik lteeekliet yeyiykpkav iiaagakyrp
      121 lpipeekkyh gngihhcelc dgefyqnksi mvvgggnsal egaiflsrya knitmvhqld
      181 yfqgekslqd evfnnskiki lwntdiknaf genkleevlv edlktkeqyk invdgifvyi
      241 gmvpntdlyk dyinlnergy iiadestktn iegvfaagdv rakqfrqlvt anadgavaal
      301 saekytskkr rennd
//
LOCUS       WP_129043577             337 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Micrococcus luteus].
ACCESSION   WP_129043577
VERSION     WP_129043577.1
KEYWORDS    RefSeq.
SOURCE      Micrococcus luteus
  ORGANISM  Micrococcus luteus
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Micrococcaceae; Micrococcus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lin,K., O'Brien,K.M., Trujillo,C., Wang,R., Wallach,J.B.,
            Schnappinger,D. and Ehrt,S.
  TITLE     Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for
            Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant
            Defense
  JOURNAL   PLoS Pathog 12 (6), e1005675 (2016)
   PUBMED   27249779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Kashima,Y. and Ishikawa,K.
  TITLE     A hyperthermostable novel protein-disulfide oxidoreductase is
            reduced by thioredoxin reductase from hyperthermophilic archaeon
            Pyrococcus horikoshii
  JOURNAL   Arch Biochem Biophys 418 (2), 179-185 (2003)
   PUBMED   14522589
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Prongay,A.J., Engelke,D.R. and Williams,C.H. Jr.
  TITLE     Characterization of two active site mutations of thioredoxin
            reductase from Escherichia coli
  JOURNAL   J Biol Chem 264 (5), 2656-2664 (1989)
   PUBMED   2644268
  REMARK    Erratum:[J Biol Chem 1989 Jul 15;264(20):12113]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01292.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Micrococcus luteus"
                     /db_xref="taxon:1270"
     gene            1..337
                     /gene="trxB"
     Protein         1..337
                     /product="thioredoxin-disulfide reductase"
                     /EC_number="1.8.1.9"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004791 - thioredoxin-disulfide reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0019430 - removal of superoxide radicals
                     [Evidence IEA]"
                     /calculated_mol_wt=34982
     Region          18..321
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msttstdtts teqatdqlii igsgpagyta aiyaaragla prviagsvth ggalmnttev
       61 enfpgfpggi qgpelmagla eqaarfgavi eyddaasvrl sghlkevttl agktyrapav
      121 ivatgsayrv lglpeekkls ghgvswcatc dgfffreqdi ivvgggdsam eealfltrfa
      181 ksvtvvvrrd alraskimaa rakdnekirf aynsavtaih gtdkvtgvtl adtitgdtre
      241 vaatgvfvai ghlprtelva gqldlddegy ivvdarttht nlsgvfacgd avdhryrqai
      301 taagtgcaaa ldaerylaal edadsiatal veepthg
//
LOCUS       WP_129046312             314 aa            linear   BCT 07-JUL-2024
DEFINITION  thioredoxin-disulfide reductase [Oleiharenicola lentus].
ACCE